data_8U5I
# 
_entry.id   8U5I 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8U5I         pdb_00008u5i 10.2210/pdb8u5i/pdb 
WWPDB D_1000277220 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        8U5I 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              harris.seth@gene.com 
_pdbx_contact_author.name_first         Seth 
_pdbx_contact_author.name_last          Harris 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1728-9771 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Steinbacher, S.' 1 ?                   
'Lammens, A.'     2 ?                   
'Harris, S.F.'    3 0000-0003-1728-9771 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Exploiting Stereo-Complexity to Identify  Spirocyclic Imidazoisoindoles as Potent and Orally Bioavailable Dual Inhibitors of Indoleamine-2,3-Dioxygenase and Tryptophan-2,3-Dioxygenase
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pastor, R.'   1 ? 
primary 'Harris, S.F.' 2 ? 
# 
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 'Indoleamine 2,3-dioxygenase 1'                                                                       44355.102 
2   1.13.11.52 ? 'N-TERMINAL TRUNCATED' ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                                     616.487   
2   ?          ? ?                      ? 
3 non-polymer nat '(1R,2S)-8-(ethanesulfonyl)-2-[(4R,5S,9aM)-5H-imidazo[5,1-a]isoindol-5-yl]-8-azaspiro[4.5]decan-1-ol' 401.522   
2   ?          ? ?                      ? 
4 water       nat water                                                                                                 18.015    
478 ?          ? ?                      ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IDO-1,Indoleamine-pyrrole 2,3-dioxygenase' 
# 
_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       
;MISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMA
YVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLL
VEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVY
EGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLR
EAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMA
YVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLL
VEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVY
EGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLR
EAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_strand_id                 A,B 
_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 '(1R,2S)-8-(ethanesulfonyl)-2-[(4R,5S,9aM)-5H-imidazo[5,1-a]isoindol-5-yl]-8-azaspiro[4.5]decan-1-ol' W2Z 
4 water                                                                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ILE n 
1 3   SER n 
1 4   LYS n 
1 5   GLU n 
1 6   TYR n 
1 7   HIS n 
1 8   ILE n 
1 9   ASP n 
1 10  GLU n 
1 11  GLU n 
1 12  VAL n 
1 13  GLY n 
1 14  PHE n 
1 15  ALA n 
1 16  LEU n 
1 17  PRO n 
1 18  ASN n 
1 19  PRO n 
1 20  GLN n 
1 21  GLU n 
1 22  ASN n 
1 23  LEU n 
1 24  PRO n 
1 25  ASP n 
1 26  PHE n 
1 27  TYR n 
1 28  ASN n 
1 29  ASP n 
1 30  TRP n 
1 31  MET n 
1 32  PHE n 
1 33  ILE n 
1 34  ALA n 
1 35  LYS n 
1 36  HIS n 
1 37  LEU n 
1 38  PRO n 
1 39  ASP n 
1 40  LEU n 
1 41  ILE n 
1 42  GLU n 
1 43  SER n 
1 44  GLY n 
1 45  GLN n 
1 46  LEU n 
1 47  ARG n 
1 48  GLU n 
1 49  ARG n 
1 50  VAL n 
1 51  GLU n 
1 52  LYS n 
1 53  LEU n 
1 54  ASN n 
1 55  MET n 
1 56  LEU n 
1 57  SER n 
1 58  ILE n 
1 59  ASP n 
1 60  HIS n 
1 61  LEU n 
1 62  THR n 
1 63  ASP n 
1 64  HIS n 
1 65  LYS n 
1 66  SER n 
1 67  GLN n 
1 68  ARG n 
1 69  LEU n 
1 70  ALA n 
1 71  ARG n 
1 72  LEU n 
1 73  VAL n 
1 74  LEU n 
1 75  GLY n 
1 76  CYS n 
1 77  ILE n 
1 78  THR n 
1 79  MET n 
1 80  ALA n 
1 81  TYR n 
1 82  VAL n 
1 83  TRP n 
1 84  GLY n 
1 85  LYS n 
1 86  GLY n 
1 87  HIS n 
1 88  GLY n 
1 89  ASP n 
1 90  VAL n 
1 91  ARG n 
1 92  LYS n 
1 93  VAL n 
1 94  LEU n 
1 95  PRO n 
1 96  ARG n 
1 97  ASN n 
1 98  ILE n 
1 99  ALA n 
1 100 VAL n 
1 101 PRO n 
1 102 TYR n 
1 103 CYS n 
1 104 GLN n 
1 105 LEU n 
1 106 SER n 
1 107 LYS n 
1 108 LYS n 
1 109 LEU n 
1 110 GLU n 
1 111 LEU n 
1 112 PRO n 
1 113 PRO n 
1 114 ILE n 
1 115 LEU n 
1 116 VAL n 
1 117 TYR n 
1 118 ALA n 
1 119 ASP n 
1 120 CYS n 
1 121 VAL n 
1 122 LEU n 
1 123 ALA n 
1 124 ASN n 
1 125 TRP n 
1 126 LYS n 
1 127 LYS n 
1 128 LYS n 
1 129 ASP n 
1 130 PRO n 
1 131 ASN n 
1 132 LYS n 
1 133 PRO n 
1 134 LEU n 
1 135 THR n 
1 136 TYR n 
1 137 GLU n 
1 138 ASN n 
1 139 MET n 
1 140 ASP n 
1 141 VAL n 
1 142 LEU n 
1 143 PHE n 
1 144 SER n 
1 145 PHE n 
1 146 ARG n 
1 147 ASP n 
1 148 GLY n 
1 149 ASP n 
1 150 CYS n 
1 151 SER n 
1 152 LYS n 
1 153 GLY n 
1 154 PHE n 
1 155 PHE n 
1 156 LEU n 
1 157 VAL n 
1 158 SER n 
1 159 LEU n 
1 160 LEU n 
1 161 VAL n 
1 162 GLU n 
1 163 ILE n 
1 164 ALA n 
1 165 ALA n 
1 166 ALA n 
1 167 SER n 
1 168 ALA n 
1 169 ILE n 
1 170 LYS n 
1 171 VAL n 
1 172 ILE n 
1 173 PRO n 
1 174 THR n 
1 175 VAL n 
1 176 PHE n 
1 177 LYS n 
1 178 ALA n 
1 179 MET n 
1 180 GLN n 
1 181 MET n 
1 182 GLN n 
1 183 GLU n 
1 184 ARG n 
1 185 ASP n 
1 186 THR n 
1 187 LEU n 
1 188 LEU n 
1 189 LYS n 
1 190 ALA n 
1 191 LEU n 
1 192 LEU n 
1 193 GLU n 
1 194 ILE n 
1 195 ALA n 
1 196 SER n 
1 197 CYS n 
1 198 LEU n 
1 199 GLU n 
1 200 LYS n 
1 201 ALA n 
1 202 LEU n 
1 203 GLN n 
1 204 VAL n 
1 205 PHE n 
1 206 HIS n 
1 207 GLN n 
1 208 ILE n 
1 209 HIS n 
1 210 ASP n 
1 211 HIS n 
1 212 VAL n 
1 213 ASN n 
1 214 PRO n 
1 215 LYS n 
1 216 ALA n 
1 217 PHE n 
1 218 PHE n 
1 219 SER n 
1 220 VAL n 
1 221 LEU n 
1 222 ARG n 
1 223 ILE n 
1 224 TYR n 
1 225 LEU n 
1 226 SER n 
1 227 GLY n 
1 228 TRP n 
1 229 LYS n 
1 230 GLY n 
1 231 ASN n 
1 232 PRO n 
1 233 GLN n 
1 234 LEU n 
1 235 SER n 
1 236 ASP n 
1 237 GLY n 
1 238 LEU n 
1 239 VAL n 
1 240 TYR n 
1 241 GLU n 
1 242 GLY n 
1 243 PHE n 
1 244 TRP n 
1 245 GLU n 
1 246 ASP n 
1 247 PRO n 
1 248 LYS n 
1 249 GLU n 
1 250 PHE n 
1 251 ALA n 
1 252 GLY n 
1 253 GLY n 
1 254 SER n 
1 255 ALA n 
1 256 GLY n 
1 257 GLN n 
1 258 SER n 
1 259 SER n 
1 260 VAL n 
1 261 PHE n 
1 262 GLN n 
1 263 CYS n 
1 264 PHE n 
1 265 ASP n 
1 266 VAL n 
1 267 LEU n 
1 268 LEU n 
1 269 GLY n 
1 270 ILE n 
1 271 GLN n 
1 272 GLN n 
1 273 THR n 
1 274 ALA n 
1 275 GLY n 
1 276 GLY n 
1 277 GLY n 
1 278 HIS n 
1 279 ALA n 
1 280 ALA n 
1 281 GLN n 
1 282 PHE n 
1 283 LEU n 
1 284 GLN n 
1 285 ASP n 
1 286 MET n 
1 287 ARG n 
1 288 ARG n 
1 289 TYR n 
1 290 MET n 
1 291 PRO n 
1 292 PRO n 
1 293 ALA n 
1 294 HIS n 
1 295 ARG n 
1 296 ASN n 
1 297 PHE n 
1 298 LEU n 
1 299 CYS n 
1 300 SER n 
1 301 LEU n 
1 302 GLU n 
1 303 SER n 
1 304 ASN n 
1 305 PRO n 
1 306 SER n 
1 307 VAL n 
1 308 ARG n 
1 309 GLU n 
1 310 PHE n 
1 311 VAL n 
1 312 LEU n 
1 313 SER n 
1 314 LYS n 
1 315 GLY n 
1 316 ASP n 
1 317 ALA n 
1 318 GLY n 
1 319 LEU n 
1 320 ARG n 
1 321 GLU n 
1 322 ALA n 
1 323 TYR n 
1 324 ASP n 
1 325 ALA n 
1 326 CYS n 
1 327 VAL n 
1 328 LYS n 
1 329 ALA n 
1 330 LEU n 
1 331 VAL n 
1 332 SER n 
1 333 LEU n 
1 334 ARG n 
1 335 SER n 
1 336 TYR n 
1 337 HIS n 
1 338 LEU n 
1 339 GLN n 
1 340 ILE n 
1 341 VAL n 
1 342 THR n 
1 343 LYS n 
1 344 TYR n 
1 345 ILE n 
1 346 LEU n 
1 347 ILE n 
1 348 PRO n 
1 349 ALA n 
1 350 SER n 
1 351 GLN n 
1 352 GLN n 
1 353 PRO n 
1 354 LYS n 
1 355 GLU n 
1 356 ASN n 
1 357 LYS n 
1 358 THR n 
1 359 SER n 
1 360 GLU n 
1 361 ASP n 
1 362 PRO n 
1 363 SER n 
1 364 LYS n 
1 365 LEU n 
1 366 GLU n 
1 367 ALA n 
1 368 LYS n 
1 369 GLY n 
1 370 THR n 
1 371 GLY n 
1 372 GLY n 
1 373 THR n 
1 374 ASP n 
1 375 LEU n 
1 376 MET n 
1 377 ASN n 
1 378 PHE n 
1 379 LEU n 
1 380 LYS n 
1 381 THR n 
1 382 VAL n 
1 383 ARG n 
1 384 SER n 
1 385 THR n 
1 386 THR n 
1 387 GLU n 
1 388 LYS n 
1 389 SER n 
1 390 LEU n 
1 391 LEU n 
1 392 LYS n 
1 393 GLU n 
1 394 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   394 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'IDO1, IDO, INDO' 
_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                ? 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_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 
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  
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 
W2Z non-polymer         . '(1R,2S)-8-(ethanesulfonyl)-2-[(4R,5S,9aM)-5H-imidazo[5,1-a]isoindol-5-yl]-8-azaspiro[4.5]decan-1-ol' ? 
'C21 H27 N3 O3 S'  401.522 
# 
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   MET 1   10  10  MET MET A . n 
A 1 2   ILE 2   11  11  ILE ILE A . n 
A 1 3   SER 3   12  12  SER SER A . n 
A 1 4   LYS 4   13  13  LYS LYS A . n 
A 1 5   GLU 5   14  14  GLU GLU A . n 
A 1 6   TYR 6   15  15  TYR TYR A . n 
A 1 7   HIS 7   16  16  HIS HIS A . n 
A 1 8   ILE 8   17  17  ILE ILE A . n 
A 1 9   ASP 9   18  18  ASP ASP A . n 
A 1 10  GLU 10  19  19  GLU GLU A . n 
A 1 11  GLU 11  20  20  GLU GLU A . n 
A 1 12  VAL 12  21  21  VAL VAL A . n 
A 1 13  GLY 13  22  22  GLY GLY A . n 
A 1 14  PHE 14  23  23  PHE PHE A . n 
A 1 15  ALA 15  24  24  ALA ALA A . n 
A 1 16  LEU 16  25  25  LEU LEU A . n 
A 1 17  PRO 17  26  26  PRO PRO A . n 
A 1 18  ASN 18  27  27  ASN ASN A . n 
A 1 19  PRO 19  28  28  PRO PRO A . n 
A 1 20  GLN 20  29  29  GLN GLN A . n 
A 1 21  GLU 21  30  30  GLU GLU A . n 
A 1 22  ASN 22  31  31  ASN ASN A . n 
A 1 23  LEU 23  32  32  LEU LEU A . n 
A 1 24  PRO 24  33  33  PRO PRO A . n 
A 1 25  ASP 25  34  34  ASP ASP A . n 
A 1 26  PHE 26  35  35  PHE PHE A . n 
A 1 27  TYR 27  36  36  TYR TYR A . n 
A 1 28  ASN 28  37  37  ASN ASN A . n 
A 1 29  ASP 29  38  38  ASP ASP A . n 
A 1 30  TRP 30  39  39  TRP TRP A . n 
A 1 31  MET 31  40  40  MET MET A . n 
A 1 32  PHE 32  41  41  PHE PHE A . n 
A 1 33  ILE 33  42  42  ILE ILE A . n 
A 1 34  ALA 34  43  43  ALA ALA A . n 
A 1 35  LYS 35  44  44  LYS LYS A . n 
A 1 36  HIS 36  45  45  HIS HIS A . n 
A 1 37  LEU 37  46  46  LEU LEU A . n 
A 1 38  PRO 38  47  47  PRO PRO A . n 
A 1 39  ASP 39  48  48  ASP ASP A . n 
A 1 40  LEU 40  49  49  LEU LEU A . n 
A 1 41  ILE 41  50  50  ILE ILE A . n 
A 1 42  GLU 42  51  51  GLU GLU A . n 
A 1 43  SER 43  52  52  SER SER A . n 
A 1 44  GLY 44  53  53  GLY GLY A . n 
A 1 45  GLN 45  54  54  GLN GLN A . n 
A 1 46  LEU 46  55  55  LEU LEU A . n 
A 1 47  ARG 47  56  56  ARG ARG A . n 
A 1 48  GLU 48  57  57  GLU GLU A . n 
A 1 49  ARG 49  58  58  ARG ARG A . n 
A 1 50  VAL 50  59  59  VAL VAL A . n 
A 1 51  GLU 51  60  60  GLU GLU A . n 
A 1 52  LYS 52  61  61  LYS LYS A . n 
A 1 53  LEU 53  62  62  LEU LEU A . n 
A 1 54  ASN 54  63  63  ASN ASN A . n 
A 1 55  MET 55  64  64  MET MET A . n 
A 1 56  LEU 56  65  65  LEU LEU A . n 
A 1 57  SER 57  66  66  SER SER A . n 
A 1 58  ILE 58  67  67  ILE ILE A . n 
A 1 59  ASP 59  68  68  ASP ASP A . n 
A 1 60  HIS 60  69  69  HIS HIS A . n 
A 1 61  LEU 61  70  70  LEU LEU A . n 
A 1 62  THR 62  71  71  THR THR A . n 
A 1 63  ASP 63  72  72  ASP ASP A . n 
A 1 64  HIS 64  73  73  HIS HIS A . n 
A 1 65  LYS 65  74  74  LYS LYS A . n 
A 1 66  SER 66  75  75  SER SER A . n 
A 1 67  GLN 67  76  76  GLN GLN A . n 
A 1 68  ARG 68  77  77  ARG ARG A . n 
A 1 69  LEU 69  78  78  LEU LEU A . n 
A 1 70  ALA 70  79  79  ALA ALA A . n 
A 1 71  ARG 71  80  80  ARG ARG A . n 
A 1 72  LEU 72  81  81  LEU LEU A . n 
A 1 73  VAL 73  82  82  VAL VAL A . n 
A 1 74  LEU 74  83  83  LEU LEU A . n 
A 1 75  GLY 75  84  84  GLY GLY A . n 
A 1 76  CYS 76  85  85  CYS CYS A . n 
A 1 77  ILE 77  86  86  ILE ILE A . n 
A 1 78  THR 78  87  87  THR THR A . n 
A 1 79  MET 79  88  88  MET MET A . n 
A 1 80  ALA 80  89  89  ALA ALA A . n 
A 1 81  TYR 81  90  90  TYR TYR A . n 
A 1 82  VAL 82  91  91  VAL VAL A . n 
A 1 83  TRP 83  92  92  TRP TRP A . n 
A 1 84  GLY 84  93  93  GLY GLY A . n 
A 1 85  LYS 85  94  94  LYS LYS A . n 
A 1 86  GLY 86  95  95  GLY GLY A . n 
A 1 87  HIS 87  96  96  HIS HIS A . n 
A 1 88  GLY 88  97  97  GLY GLY A . n 
A 1 89  ASP 89  98  98  ASP ASP A . n 
A 1 90  VAL 90  99  99  VAL VAL A . n 
A 1 91  ARG 91  100 100 ARG ARG A . n 
A 1 92  LYS 92  101 101 LYS LYS A . n 
A 1 93  VAL 93  102 102 VAL VAL A . n 
A 1 94  LEU 94  103 103 LEU LEU A . n 
A 1 95  PRO 95  104 104 PRO PRO A . n 
A 1 96  ARG 96  105 105 ARG ARG A . n 
A 1 97  ASN 97  106 106 ASN ASN A . n 
A 1 98  ILE 98  107 107 ILE ILE A . n 
A 1 99  ALA 99  108 108 ALA ALA A . n 
A 1 100 VAL 100 109 109 VAL VAL A . n 
A 1 101 PRO 101 110 110 PRO PRO A . n 
A 1 102 TYR 102 111 111 TYR TYR A . n 
A 1 103 CYS 103 112 112 CYS CYS A . n 
A 1 104 GLN 104 113 113 GLN GLN A . n 
A 1 105 LEU 105 114 114 LEU LEU A . n 
A 1 106 SER 106 115 115 SER SER A . n 
A 1 107 LYS 107 116 116 LYS LYS A . n 
A 1 108 LYS 108 117 117 LYS LYS A . n 
A 1 109 LEU 109 118 118 LEU LEU A . n 
A 1 110 GLU 110 119 119 GLU GLU A . n 
A 1 111 LEU 111 120 120 LEU LEU A . n 
A 1 112 PRO 112 121 121 PRO PRO A . n 
A 1 113 PRO 113 122 122 PRO PRO A . n 
A 1 114 ILE 114 123 123 ILE ILE A . n 
A 1 115 LEU 115 124 124 LEU LEU A . n 
A 1 116 VAL 116 125 125 VAL VAL A . n 
A 1 117 TYR 117 126 126 TYR TYR A . n 
A 1 118 ALA 118 127 127 ALA ALA A . n 
A 1 119 ASP 119 128 128 ASP ASP A . n 
A 1 120 CYS 120 129 129 CYS CYS A . n 
A 1 121 VAL 121 130 130 VAL VAL A . n 
A 1 122 LEU 122 131 131 LEU LEU A . n 
A 1 123 ALA 123 132 132 ALA ALA A . n 
A 1 124 ASN 124 133 133 ASN ASN A . n 
A 1 125 TRP 125 134 134 TRP TRP A . n 
A 1 126 LYS 126 135 135 LYS LYS A . n 
A 1 127 LYS 127 136 136 LYS LYS A . n 
A 1 128 LYS 128 137 137 LYS LYS A . n 
A 1 129 ASP 129 138 138 ASP ASP A . n 
A 1 130 PRO 130 139 139 PRO PRO A . n 
A 1 131 ASN 131 140 140 ASN ASN A . n 
A 1 132 LYS 132 141 141 LYS LYS A . n 
A 1 133 PRO 133 142 142 PRO PRO A . n 
A 1 134 LEU 134 143 143 LEU LEU A . n 
A 1 135 THR 135 144 144 THR THR A . n 
A 1 136 TYR 136 145 145 TYR TYR A . n 
A 1 137 GLU 137 146 146 GLU GLU A . n 
A 1 138 ASN 138 147 147 ASN ASN A . n 
A 1 139 MET 139 148 148 MET MET A . n 
A 1 140 ASP 140 149 149 ASP ASP A . n 
A 1 141 VAL 141 150 150 VAL VAL A . n 
A 1 142 LEU 142 151 151 LEU LEU A . n 
A 1 143 PHE 143 152 152 PHE PHE A . n 
A 1 144 SER 144 153 153 SER SER A . n 
A 1 145 PHE 145 154 154 PHE PHE A . n 
A 1 146 ARG 146 155 155 ARG ARG A . n 
A 1 147 ASP 147 156 156 ASP ASP A . n 
A 1 148 GLY 148 157 157 GLY GLY A . n 
A 1 149 ASP 149 158 158 ASP ASP A . n 
A 1 150 CYS 150 159 159 CYS CYS A . n 
A 1 151 SER 151 160 160 SER SER A . n 
A 1 152 LYS 152 161 161 LYS LYS A . n 
A 1 153 GLY 153 162 162 GLY GLY A . n 
A 1 154 PHE 154 163 163 PHE PHE A . n 
A 1 155 PHE 155 164 164 PHE PHE A . n 
A 1 156 LEU 156 165 165 LEU LEU A . n 
A 1 157 VAL 157 166 166 VAL VAL A . n 
A 1 158 SER 158 167 167 SER SER A . n 
A 1 159 LEU 159 168 168 LEU LEU A . n 
A 1 160 LEU 160 169 169 LEU LEU A . n 
A 1 161 VAL 161 170 170 VAL VAL A . n 
A 1 162 GLU 162 171 171 GLU GLU A . n 
A 1 163 ILE 163 172 172 ILE ILE A . n 
A 1 164 ALA 164 173 173 ALA ALA A . n 
A 1 165 ALA 165 174 174 ALA ALA A . n 
A 1 166 ALA 166 175 175 ALA ALA A . n 
A 1 167 SER 167 176 176 SER SER A . n 
A 1 168 ALA 168 177 177 ALA ALA A . n 
A 1 169 ILE 169 178 178 ILE ILE A . n 
A 1 170 LYS 170 179 179 LYS LYS A . n 
A 1 171 VAL 171 180 180 VAL VAL A . n 
A 1 172 ILE 172 181 181 ILE ILE A . n 
A 1 173 PRO 173 182 182 PRO PRO A . n 
A 1 174 THR 174 183 183 THR THR A . n 
A 1 175 VAL 175 184 184 VAL VAL A . n 
A 1 176 PHE 176 185 185 PHE PHE A . n 
A 1 177 LYS 177 186 186 LYS LYS A . n 
A 1 178 ALA 178 187 187 ALA ALA A . n 
A 1 179 MET 179 188 188 MET MET A . n 
A 1 180 GLN 180 189 189 GLN GLN A . n 
A 1 181 MET 181 190 190 MET MET A . n 
A 1 182 GLN 182 191 191 GLN GLN A . n 
A 1 183 GLU 183 192 192 GLU GLU A . n 
A 1 184 ARG 184 193 193 ARG ARG A . n 
A 1 185 ASP 185 194 194 ASP ASP A . n 
A 1 186 THR 186 195 195 THR THR A . n 
A 1 187 LEU 187 196 196 LEU LEU A . n 
A 1 188 LEU 188 197 197 LEU LEU A . n 
A 1 189 LYS 189 198 198 LYS LYS A . n 
A 1 190 ALA 190 199 199 ALA ALA A . n 
A 1 191 LEU 191 200 200 LEU LEU A . n 
A 1 192 LEU 192 201 201 LEU LEU A . n 
A 1 193 GLU 193 202 202 GLU GLU A . n 
A 1 194 ILE 194 203 203 ILE ILE A . n 
A 1 195 ALA 195 204 204 ALA ALA A . n 
A 1 196 SER 196 205 205 SER SER A . n 
A 1 197 CYS 197 206 206 CYS CYS A . n 
A 1 198 LEU 198 207 207 LEU LEU A . n 
A 1 199 GLU 199 208 208 GLU GLU A . n 
A 1 200 LYS 200 209 209 LYS LYS A . n 
A 1 201 ALA 201 210 210 ALA ALA A . n 
A 1 202 LEU 202 211 211 LEU LEU A . n 
A 1 203 GLN 203 212 212 GLN GLN A . n 
A 1 204 VAL 204 213 213 VAL VAL A . n 
A 1 205 PHE 205 214 214 PHE PHE A . n 
A 1 206 HIS 206 215 215 HIS HIS A . n 
A 1 207 GLN 207 216 216 GLN GLN A . n 
A 1 208 ILE 208 217 217 ILE ILE A . n 
A 1 209 HIS 209 218 218 HIS HIS A . n 
A 1 210 ASP 210 219 219 ASP ASP A . n 
A 1 211 HIS 211 220 220 HIS HIS A . n 
A 1 212 VAL 212 221 221 VAL VAL A . n 
A 1 213 ASN 213 222 222 ASN ASN A . n 
A 1 214 PRO 214 223 223 PRO PRO A . n 
A 1 215 LYS 215 224 224 LYS LYS A . n 
A 1 216 ALA 216 225 225 ALA ALA A . n 
A 1 217 PHE 217 226 226 PHE PHE A . n 
A 1 218 PHE 218 227 227 PHE PHE A . n 
A 1 219 SER 219 228 228 SER SER A . n 
A 1 220 VAL 220 229 229 VAL VAL A . n 
A 1 221 LEU 221 230 230 LEU LEU A . n 
A 1 222 ARG 222 231 231 ARG ARG A . n 
A 1 223 ILE 223 232 232 ILE ILE A . n 
A 1 224 TYR 224 233 233 TYR TYR A . n 
A 1 225 LEU 225 234 234 LEU LEU A . n 
A 1 226 SER 226 235 235 SER SER A . n 
A 1 227 GLY 227 236 236 GLY GLY A . n 
A 1 228 TRP 228 237 237 TRP TRP A . n 
A 1 229 LYS 229 238 238 LYS LYS A . n 
A 1 230 GLY 230 239 239 GLY GLY A . n 
A 1 231 ASN 231 240 240 ASN ASN A . n 
A 1 232 PRO 232 241 241 PRO PRO A . n 
A 1 233 GLN 233 242 242 GLN GLN A . n 
A 1 234 LEU 234 243 243 LEU LEU A . n 
A 1 235 SER 235 244 244 SER SER A . n 
A 1 236 ASP 236 245 245 ASP ASP A . n 
A 1 237 GLY 237 246 246 GLY GLY A . n 
A 1 238 LEU 238 247 247 LEU LEU A . n 
A 1 239 VAL 239 248 248 VAL VAL A . n 
A 1 240 TYR 240 249 249 TYR TYR A . n 
A 1 241 GLU 241 250 250 GLU GLU A . n 
A 1 242 GLY 242 251 251 GLY GLY A . n 
A 1 243 PHE 243 252 252 PHE PHE A . n 
A 1 244 TRP 244 253 253 TRP TRP A . n 
A 1 245 GLU 245 254 254 GLU GLU A . n 
A 1 246 ASP 246 255 255 ASP ASP A . n 
A 1 247 PRO 247 256 256 PRO PRO A . n 
A 1 248 LYS 248 257 257 LYS LYS A . n 
A 1 249 GLU 249 258 258 GLU GLU A . n 
A 1 250 PHE 250 259 259 PHE PHE A . n 
A 1 251 ALA 251 260 260 ALA ALA A . n 
A 1 252 GLY 252 261 261 GLY GLY A . n 
A 1 253 GLY 253 262 262 GLY GLY A . n 
A 1 254 SER 254 263 263 SER SER A . n 
A 1 255 ALA 255 264 264 ALA ALA A . n 
A 1 256 GLY 256 265 265 GLY GLY A . n 
A 1 257 GLN 257 266 266 GLN GLN A . n 
A 1 258 SER 258 267 267 SER SER A . n 
A 1 259 SER 259 268 268 SER SER A . n 
A 1 260 VAL 260 269 269 VAL VAL A . n 
A 1 261 PHE 261 270 270 PHE PHE A . n 
A 1 262 GLN 262 271 271 GLN GLN A . n 
A 1 263 CYS 263 272 272 CYS CYS A . n 
A 1 264 PHE 264 273 273 PHE PHE A . n 
A 1 265 ASP 265 274 274 ASP ASP A . n 
A 1 266 VAL 266 275 275 VAL VAL A . n 
A 1 267 LEU 267 276 276 LEU LEU A . n 
A 1 268 LEU 268 277 277 LEU LEU A . n 
A 1 269 GLY 269 278 278 GLY GLY A . n 
A 1 270 ILE 270 279 279 ILE ILE A . n 
A 1 271 GLN 271 280 280 GLN GLN A . n 
A 1 272 GLN 272 281 281 GLN GLN A . n 
A 1 273 THR 273 282 282 THR THR A . n 
A 1 274 ALA 274 283 283 ALA ALA A . n 
A 1 275 GLY 275 284 284 GLY GLY A . n 
A 1 276 GLY 276 285 285 GLY GLY A . n 
A 1 277 GLY 277 286 286 GLY GLY A . n 
A 1 278 HIS 278 287 287 HIS HIS A . n 
A 1 279 ALA 279 288 288 ALA ALA A . n 
A 1 280 ALA 280 289 289 ALA ALA A . n 
A 1 281 GLN 281 290 290 GLN GLN A . n 
A 1 282 PHE 282 291 291 PHE PHE A . n 
A 1 283 LEU 283 292 292 LEU LEU A . n 
A 1 284 GLN 284 293 293 GLN GLN A . n 
A 1 285 ASP 285 294 294 ASP ASP A . n 
A 1 286 MET 286 295 295 MET MET A . n 
A 1 287 ARG 287 296 296 ARG ARG A . n 
A 1 288 ARG 288 297 297 ARG ARG A . n 
A 1 289 TYR 289 298 298 TYR TYR A . n 
A 1 290 MET 290 299 299 MET MET A . n 
A 1 291 PRO 291 300 300 PRO PRO A . n 
A 1 292 PRO 292 301 301 PRO PRO A . n 
A 1 293 ALA 293 302 302 ALA ALA A . n 
A 1 294 HIS 294 303 303 HIS HIS A . n 
A 1 295 ARG 295 304 304 ARG ARG A . n 
A 1 296 ASN 296 305 305 ASN ASN A . n 
A 1 297 PHE 297 306 306 PHE PHE A . n 
A 1 298 LEU 298 307 307 LEU LEU A . n 
A 1 299 CYS 299 308 308 CYS CYS A . n 
A 1 300 SER 300 309 309 SER SER A . n 
A 1 301 LEU 301 310 310 LEU LEU A . n 
A 1 302 GLU 302 311 311 GLU GLU A . n 
A 1 303 SER 303 312 312 SER SER A . n 
A 1 304 ASN 304 313 313 ASN ASN A . n 
A 1 305 PRO 305 314 314 PRO PRO A . n 
A 1 306 SER 306 315 315 SER SER A . n 
A 1 307 VAL 307 316 316 VAL VAL A . n 
A 1 308 ARG 308 317 317 ARG ARG A . n 
A 1 309 GLU 309 318 318 GLU GLU A . n 
A 1 310 PHE 310 319 319 PHE PHE A . n 
A 1 311 VAL 311 320 320 VAL VAL A . n 
A 1 312 LEU 312 321 321 LEU LEU A . n 
A 1 313 SER 313 322 322 SER SER A . n 
A 1 314 LYS 314 323 323 LYS LYS A . n 
A 1 315 GLY 315 324 324 GLY GLY A . n 
A 1 316 ASP 316 325 325 ASP ASP A . n 
A 1 317 ALA 317 326 326 ALA ALA A . n 
A 1 318 GLY 318 327 327 GLY GLY A . n 
A 1 319 LEU 319 328 328 LEU LEU A . n 
A 1 320 ARG 320 329 329 ARG ARG A . n 
A 1 321 GLU 321 330 330 GLU GLU A . n 
A 1 322 ALA 322 331 331 ALA ALA A . n 
A 1 323 TYR 323 332 332 TYR TYR A . n 
A 1 324 ASP 324 333 333 ASP ASP A . n 
A 1 325 ALA 325 334 334 ALA ALA A . n 
A 1 326 CYS 326 335 335 CYS CYS A . n 
A 1 327 VAL 327 336 336 VAL VAL A . n 
A 1 328 LYS 328 337 337 LYS LYS A . n 
A 1 329 ALA 329 338 338 ALA ALA A . n 
A 1 330 LEU 330 339 339 LEU LEU A . n 
A 1 331 VAL 331 340 340 VAL VAL A . n 
A 1 332 SER 332 341 341 SER SER A . n 
A 1 333 LEU 333 342 342 LEU LEU A . n 
A 1 334 ARG 334 343 343 ARG ARG A . n 
A 1 335 SER 335 344 344 SER SER A . n 
A 1 336 TYR 336 345 345 TYR TYR A . n 
A 1 337 HIS 337 346 346 HIS HIS A . n 
A 1 338 LEU 338 347 347 LEU LEU A . n 
A 1 339 GLN 339 348 348 GLN GLN A . n 
A 1 340 ILE 340 349 349 ILE ILE A . n 
A 1 341 VAL 341 350 350 VAL VAL A . n 
A 1 342 THR 342 351 351 THR THR A . n 
A 1 343 LYS 343 352 352 LYS LYS A . n 
A 1 344 TYR 344 353 353 TYR TYR A . n 
A 1 345 ILE 345 354 354 ILE ILE A . n 
A 1 346 LEU 346 355 355 LEU LEU A . n 
A 1 347 ILE 347 356 356 ILE ILE A . n 
A 1 348 PRO 348 357 357 PRO PRO A . n 
A 1 349 ALA 349 358 358 ALA ALA A . n 
A 1 350 SER 350 359 359 SER SER A . n 
A 1 351 GLN 351 360 360 GLN GLN A . n 
A 1 352 GLN 352 361 361 GLN GLN A . n 
A 1 353 PRO 353 362 362 PRO PRO A . n 
A 1 354 LYS 354 363 ?   ?   ?   A . n 
A 1 355 GLU 355 364 ?   ?   ?   A . n 
A 1 356 ASN 356 365 ?   ?   ?   A . n 
A 1 357 LYS 357 366 ?   ?   ?   A . n 
A 1 358 THR 358 367 ?   ?   ?   A . n 
A 1 359 SER 359 368 ?   ?   ?   A . n 
A 1 360 GLU 360 369 ?   ?   ?   A . n 
A 1 361 ASP 361 370 ?   ?   ?   A . n 
A 1 362 PRO 362 371 ?   ?   ?   A . n 
A 1 363 SER 363 372 ?   ?   ?   A . n 
A 1 364 LYS 364 373 ?   ?   ?   A . n 
A 1 365 LEU 365 374 ?   ?   ?   A . n 
A 1 366 GLU 366 375 ?   ?   ?   A . n 
A 1 367 ALA 367 376 ?   ?   ?   A . n 
A 1 368 LYS 368 377 ?   ?   ?   A . n 
A 1 369 GLY 369 378 ?   ?   ?   A . n 
A 1 370 THR 370 379 ?   ?   ?   A . n 
A 1 371 GLY 371 380 380 GLY GLY A . n 
A 1 372 GLY 372 381 381 GLY GLY A . n 
A 1 373 THR 373 382 382 THR THR A . n 
A 1 374 ASP 374 383 383 ASP ASP A . n 
A 1 375 LEU 375 384 384 LEU LEU A . n 
A 1 376 MET 376 385 385 MET MET A . n 
A 1 377 ASN 377 386 386 ASN ASN A . n 
A 1 378 PHE 378 387 387 PHE PHE A . n 
A 1 379 LEU 379 388 388 LEU LEU A . n 
A 1 380 LYS 380 389 389 LYS LYS A . n 
A 1 381 THR 381 390 390 THR THR A . n 
A 1 382 VAL 382 391 391 VAL VAL A . n 
A 1 383 ARG 383 392 392 ARG ARG A . n 
A 1 384 SER 384 393 393 SER SER A . n 
A 1 385 THR 385 394 394 THR THR A . n 
A 1 386 THR 386 395 395 THR THR A . n 
A 1 387 GLU 387 396 396 GLU GLU A . n 
A 1 388 LYS 388 397 397 LYS LYS A . n 
A 1 389 SER 389 398 398 SER SER A . n 
A 1 390 LEU 390 399 399 LEU LEU A . n 
A 1 391 LEU 391 400 400 LEU LEU A . n 
A 1 392 LYS 392 401 401 LYS LYS A . n 
A 1 393 GLU 393 402 ?   ?   ?   A . n 
A 1 394 GLY 394 403 ?   ?   ?   A . n 
B 1 1   MET 1   10  ?   ?   ?   B . n 
B 1 2   ILE 2   11  11  ILE ILE B . n 
B 1 3   SER 3   12  12  SER SER B . n 
B 1 4   LYS 4   13  13  LYS LYS B . n 
B 1 5   GLU 5   14  14  GLU GLU B . n 
B 1 6   TYR 6   15  15  TYR TYR B . n 
B 1 7   HIS 7   16  16  HIS HIS B . n 
B 1 8   ILE 8   17  17  ILE ILE B . n 
B 1 9   ASP 9   18  18  ASP ASP B . n 
B 1 10  GLU 10  19  19  GLU GLU B . n 
B 1 11  GLU 11  20  20  GLU GLU B . n 
B 1 12  VAL 12  21  21  VAL VAL B . n 
B 1 13  GLY 13  22  22  GLY GLY B . n 
B 1 14  PHE 14  23  23  PHE PHE B . n 
B 1 15  ALA 15  24  24  ALA ALA B . n 
B 1 16  LEU 16  25  25  LEU LEU B . n 
B 1 17  PRO 17  26  26  PRO PRO B . n 
B 1 18  ASN 18  27  27  ASN ASN B . n 
B 1 19  PRO 19  28  28  PRO PRO B . n 
B 1 20  GLN 20  29  29  GLN GLN B . n 
B 1 21  GLU 21  30  30  GLU GLU B . n 
B 1 22  ASN 22  31  31  ASN ASN B . n 
B 1 23  LEU 23  32  32  LEU LEU B . n 
B 1 24  PRO 24  33  33  PRO PRO B . n 
B 1 25  ASP 25  34  34  ASP ASP B . n 
B 1 26  PHE 26  35  35  PHE PHE B . n 
B 1 27  TYR 27  36  36  TYR TYR B . n 
B 1 28  ASN 28  37  37  ASN ASN B . n 
B 1 29  ASP 29  38  38  ASP ASP B . n 
B 1 30  TRP 30  39  39  TRP TRP B . n 
B 1 31  MET 31  40  40  MET MET B . n 
B 1 32  PHE 32  41  41  PHE PHE B . n 
B 1 33  ILE 33  42  42  ILE ILE B . n 
B 1 34  ALA 34  43  43  ALA ALA B . n 
B 1 35  LYS 35  44  44  LYS LYS B . n 
B 1 36  HIS 36  45  45  HIS HIS B . n 
B 1 37  LEU 37  46  46  LEU LEU B . n 
B 1 38  PRO 38  47  47  PRO PRO B . n 
B 1 39  ASP 39  48  48  ASP ASP B . n 
B 1 40  LEU 40  49  49  LEU LEU B . n 
B 1 41  ILE 41  50  50  ILE ILE B . n 
B 1 42  GLU 42  51  51  GLU GLU B . n 
B 1 43  SER 43  52  52  SER SER B . n 
B 1 44  GLY 44  53  53  GLY GLY B . n 
B 1 45  GLN 45  54  54  GLN GLN B . n 
B 1 46  LEU 46  55  55  LEU LEU B . n 
B 1 47  ARG 47  56  56  ARG ARG B . n 
B 1 48  GLU 48  57  57  GLU GLU B . n 
B 1 49  ARG 49  58  58  ARG ARG B . n 
B 1 50  VAL 50  59  59  VAL VAL B . n 
B 1 51  GLU 51  60  60  GLU GLU B . n 
B 1 52  LYS 52  61  61  LYS LYS B . n 
B 1 53  LEU 53  62  62  LEU LEU B . n 
B 1 54  ASN 54  63  63  ASN ASN B . n 
B 1 55  MET 55  64  64  MET MET B . n 
B 1 56  LEU 56  65  65  LEU LEU B . n 
B 1 57  SER 57  66  66  SER SER B . n 
B 1 58  ILE 58  67  67  ILE ILE B . n 
B 1 59  ASP 59  68  68  ASP ASP B . n 
B 1 60  HIS 60  69  69  HIS HIS B . n 
B 1 61  LEU 61  70  70  LEU LEU B . n 
B 1 62  THR 62  71  71  THR THR B . n 
B 1 63  ASP 63  72  72  ASP ASP B . n 
B 1 64  HIS 64  73  73  HIS HIS B . n 
B 1 65  LYS 65  74  74  LYS LYS B . n 
B 1 66  SER 66  75  75  SER SER B . n 
B 1 67  GLN 67  76  76  GLN GLN B . n 
B 1 68  ARG 68  77  77  ARG ARG B . n 
B 1 69  LEU 69  78  78  LEU LEU B . n 
B 1 70  ALA 70  79  79  ALA ALA B . n 
B 1 71  ARG 71  80  80  ARG ARG B . n 
B 1 72  LEU 72  81  81  LEU LEU B . n 
B 1 73  VAL 73  82  82  VAL VAL B . n 
B 1 74  LEU 74  83  83  LEU LEU B . n 
B 1 75  GLY 75  84  84  GLY GLY B . n 
B 1 76  CYS 76  85  85  CYS CYS B . n 
B 1 77  ILE 77  86  86  ILE ILE B . n 
B 1 78  THR 78  87  87  THR THR B . n 
B 1 79  MET 79  88  88  MET MET B . n 
B 1 80  ALA 80  89  89  ALA ALA B . n 
B 1 81  TYR 81  90  90  TYR TYR B . n 
B 1 82  VAL 82  91  91  VAL VAL B . n 
B 1 83  TRP 83  92  92  TRP TRP B . n 
B 1 84  GLY 84  93  93  GLY GLY B . n 
B 1 85  LYS 85  94  94  LYS LYS B . n 
B 1 86  GLY 86  95  95  GLY GLY B . n 
B 1 87  HIS 87  96  96  HIS HIS B . n 
B 1 88  GLY 88  97  97  GLY GLY B . n 
B 1 89  ASP 89  98  98  ASP ASP B . n 
B 1 90  VAL 90  99  99  VAL VAL B . n 
B 1 91  ARG 91  100 100 ARG ARG B . n 
B 1 92  LYS 92  101 101 LYS LYS B . n 
B 1 93  VAL 93  102 102 VAL VAL B . n 
B 1 94  LEU 94  103 103 LEU LEU B . n 
B 1 95  PRO 95  104 104 PRO PRO B . n 
B 1 96  ARG 96  105 105 ARG ARG B . n 
B 1 97  ASN 97  106 106 ASN ASN B . n 
B 1 98  ILE 98  107 107 ILE ILE B . n 
B 1 99  ALA 99  108 108 ALA ALA B . n 
B 1 100 VAL 100 109 109 VAL VAL B . n 
B 1 101 PRO 101 110 110 PRO PRO B . n 
B 1 102 TYR 102 111 111 TYR TYR B . n 
B 1 103 CYS 103 112 112 CYS CYS B . n 
B 1 104 GLN 104 113 113 GLN GLN B . n 
B 1 105 LEU 105 114 114 LEU LEU B . n 
B 1 106 SER 106 115 115 SER SER B . n 
B 1 107 LYS 107 116 116 LYS LYS B . n 
B 1 108 LYS 108 117 117 LYS LYS B . n 
B 1 109 LEU 109 118 118 LEU LEU B . n 
B 1 110 GLU 110 119 119 GLU GLU B . n 
B 1 111 LEU 111 120 120 LEU LEU B . n 
B 1 112 PRO 112 121 121 PRO PRO B . n 
B 1 113 PRO 113 122 122 PRO PRO B . n 
B 1 114 ILE 114 123 123 ILE ILE B . n 
B 1 115 LEU 115 124 124 LEU LEU B . n 
B 1 116 VAL 116 125 125 VAL VAL B . n 
B 1 117 TYR 117 126 126 TYR TYR B . n 
B 1 118 ALA 118 127 127 ALA ALA B . n 
B 1 119 ASP 119 128 128 ASP ASP B . n 
B 1 120 CYS 120 129 129 CYS CYS B . n 
B 1 121 VAL 121 130 130 VAL VAL B . n 
B 1 122 LEU 122 131 131 LEU LEU B . n 
B 1 123 ALA 123 132 132 ALA ALA B . n 
B 1 124 ASN 124 133 133 ASN ASN B . n 
B 1 125 TRP 125 134 134 TRP TRP B . n 
B 1 126 LYS 126 135 135 LYS LYS B . n 
B 1 127 LYS 127 136 136 LYS LYS B . n 
B 1 128 LYS 128 137 137 LYS LYS B . n 
B 1 129 ASP 129 138 138 ASP ASP B . n 
B 1 130 PRO 130 139 139 PRO PRO B . n 
B 1 131 ASN 131 140 140 ASN ASN B . n 
B 1 132 LYS 132 141 141 LYS LYS B . n 
B 1 133 PRO 133 142 142 PRO PRO B . n 
B 1 134 LEU 134 143 143 LEU LEU B . n 
B 1 135 THR 135 144 144 THR THR B . n 
B 1 136 TYR 136 145 145 TYR TYR B . n 
B 1 137 GLU 137 146 146 GLU GLU B . n 
B 1 138 ASN 138 147 147 ASN ASN B . n 
B 1 139 MET 139 148 148 MET MET B . n 
B 1 140 ASP 140 149 149 ASP ASP B . n 
B 1 141 VAL 141 150 150 VAL VAL B . n 
B 1 142 LEU 142 151 151 LEU LEU B . n 
B 1 143 PHE 143 152 152 PHE PHE B . n 
B 1 144 SER 144 153 153 SER SER B . n 
B 1 145 PHE 145 154 154 PHE PHE B . n 
B 1 146 ARG 146 155 155 ARG ARG B . n 
B 1 147 ASP 147 156 156 ASP ASP B . n 
B 1 148 GLY 148 157 157 GLY GLY B . n 
B 1 149 ASP 149 158 158 ASP ASP B . n 
B 1 150 CYS 150 159 159 CYS CYS B . n 
B 1 151 SER 151 160 160 SER SER B . n 
B 1 152 LYS 152 161 161 LYS LYS B . n 
B 1 153 GLY 153 162 162 GLY GLY B . n 
B 1 154 PHE 154 163 163 PHE PHE B . n 
B 1 155 PHE 155 164 164 PHE PHE B . n 
B 1 156 LEU 156 165 165 LEU LEU B . n 
B 1 157 VAL 157 166 166 VAL VAL B . n 
B 1 158 SER 158 167 167 SER SER B . n 
B 1 159 LEU 159 168 168 LEU LEU B . n 
B 1 160 LEU 160 169 169 LEU LEU B . n 
B 1 161 VAL 161 170 170 VAL VAL B . n 
B 1 162 GLU 162 171 171 GLU GLU B . n 
B 1 163 ILE 163 172 172 ILE ILE B . n 
B 1 164 ALA 164 173 173 ALA ALA B . n 
B 1 165 ALA 165 174 174 ALA ALA B . n 
B 1 166 ALA 166 175 175 ALA ALA B . n 
B 1 167 SER 167 176 176 SER SER B . n 
B 1 168 ALA 168 177 177 ALA ALA B . n 
B 1 169 ILE 169 178 178 ILE ILE B . n 
B 1 170 LYS 170 179 179 LYS LYS B . n 
B 1 171 VAL 171 180 180 VAL VAL B . n 
B 1 172 ILE 172 181 181 ILE ILE B . n 
B 1 173 PRO 173 182 182 PRO PRO B . n 
B 1 174 THR 174 183 183 THR THR B . n 
B 1 175 VAL 175 184 184 VAL VAL B . n 
B 1 176 PHE 176 185 185 PHE PHE B . n 
B 1 177 LYS 177 186 186 LYS LYS B . n 
B 1 178 ALA 178 187 187 ALA ALA B . n 
B 1 179 MET 179 188 188 MET MET B . n 
B 1 180 GLN 180 189 189 GLN GLN B . n 
B 1 181 MET 181 190 190 MET MET B . n 
B 1 182 GLN 182 191 191 GLN GLN B . n 
B 1 183 GLU 183 192 192 GLU GLU B . n 
B 1 184 ARG 184 193 193 ARG ARG B . n 
B 1 185 ASP 185 194 194 ASP ASP B . n 
B 1 186 THR 186 195 195 THR THR B . n 
B 1 187 LEU 187 196 196 LEU LEU B . n 
B 1 188 LEU 188 197 197 LEU LEU B . n 
B 1 189 LYS 189 198 198 LYS LYS B . n 
B 1 190 ALA 190 199 199 ALA ALA B . n 
B 1 191 LEU 191 200 200 LEU LEU B . n 
B 1 192 LEU 192 201 201 LEU LEU B . n 
B 1 193 GLU 193 202 202 GLU GLU B . n 
B 1 194 ILE 194 203 203 ILE ILE B . n 
B 1 195 ALA 195 204 204 ALA ALA B . n 
B 1 196 SER 196 205 205 SER SER B . n 
B 1 197 CYS 197 206 206 CYS CYS B . n 
B 1 198 LEU 198 207 207 LEU LEU B . n 
B 1 199 GLU 199 208 208 GLU GLU B . n 
B 1 200 LYS 200 209 209 LYS LYS B . n 
B 1 201 ALA 201 210 210 ALA ALA B . n 
B 1 202 LEU 202 211 211 LEU LEU B . n 
B 1 203 GLN 203 212 212 GLN GLN B . n 
B 1 204 VAL 204 213 213 VAL VAL B . n 
B 1 205 PHE 205 214 214 PHE PHE B . n 
B 1 206 HIS 206 215 215 HIS HIS B . n 
B 1 207 GLN 207 216 216 GLN GLN B . n 
B 1 208 ILE 208 217 217 ILE ILE B . n 
B 1 209 HIS 209 218 218 HIS HIS B . n 
B 1 210 ASP 210 219 219 ASP ASP B . n 
B 1 211 HIS 211 220 220 HIS HIS B . n 
B 1 212 VAL 212 221 221 VAL VAL B . n 
B 1 213 ASN 213 222 222 ASN ASN B . n 
B 1 214 PRO 214 223 223 PRO PRO B . n 
B 1 215 LYS 215 224 224 LYS LYS B . n 
B 1 216 ALA 216 225 225 ALA ALA B . n 
B 1 217 PHE 217 226 226 PHE PHE B . n 
B 1 218 PHE 218 227 227 PHE PHE B . n 
B 1 219 SER 219 228 228 SER SER B . n 
B 1 220 VAL 220 229 229 VAL VAL B . n 
B 1 221 LEU 221 230 230 LEU LEU B . n 
B 1 222 ARG 222 231 231 ARG ARG B . n 
B 1 223 ILE 223 232 232 ILE ILE B . n 
B 1 224 TYR 224 233 233 TYR TYR B . n 
B 1 225 LEU 225 234 234 LEU LEU B . n 
B 1 226 SER 226 235 235 SER SER B . n 
B 1 227 GLY 227 236 236 GLY GLY B . n 
B 1 228 TRP 228 237 237 TRP TRP B . n 
B 1 229 LYS 229 238 238 LYS LYS B . n 
B 1 230 GLY 230 239 239 GLY GLY B . n 
B 1 231 ASN 231 240 240 ASN ASN B . n 
B 1 232 PRO 232 241 241 PRO PRO B . n 
B 1 233 GLN 233 242 242 GLN GLN B . n 
B 1 234 LEU 234 243 243 LEU LEU B . n 
B 1 235 SER 235 244 244 SER SER B . n 
B 1 236 ASP 236 245 245 ASP ASP B . n 
B 1 237 GLY 237 246 246 GLY GLY B . n 
B 1 238 LEU 238 247 247 LEU LEU B . n 
B 1 239 VAL 239 248 248 VAL VAL B . n 
B 1 240 TYR 240 249 249 TYR TYR B . n 
B 1 241 GLU 241 250 250 GLU GLU B . n 
B 1 242 GLY 242 251 251 GLY GLY B . n 
B 1 243 PHE 243 252 252 PHE PHE B . n 
B 1 244 TRP 244 253 253 TRP TRP B . n 
B 1 245 GLU 245 254 254 GLU GLU B . n 
B 1 246 ASP 246 255 255 ASP ASP B . n 
B 1 247 PRO 247 256 256 PRO PRO B . n 
B 1 248 LYS 248 257 257 LYS LYS B . n 
B 1 249 GLU 249 258 258 GLU GLU B . n 
B 1 250 PHE 250 259 259 PHE PHE B . n 
B 1 251 ALA 251 260 260 ALA ALA B . n 
B 1 252 GLY 252 261 261 GLY GLY B . n 
B 1 253 GLY 253 262 262 GLY GLY B . n 
B 1 254 SER 254 263 263 SER SER B . n 
B 1 255 ALA 255 264 264 ALA ALA B . n 
B 1 256 GLY 256 265 265 GLY GLY B . n 
B 1 257 GLN 257 266 266 GLN GLN B . n 
B 1 258 SER 258 267 267 SER SER B . n 
B 1 259 SER 259 268 268 SER SER B . n 
B 1 260 VAL 260 269 269 VAL VAL B . n 
B 1 261 PHE 261 270 270 PHE PHE B . n 
B 1 262 GLN 262 271 271 GLN GLN B . n 
B 1 263 CYS 263 272 272 CYS CYS B . n 
B 1 264 PHE 264 273 273 PHE PHE B . n 
B 1 265 ASP 265 274 274 ASP ASP B . n 
B 1 266 VAL 266 275 275 VAL VAL B . n 
B 1 267 LEU 267 276 276 LEU LEU B . n 
B 1 268 LEU 268 277 277 LEU LEU B . n 
B 1 269 GLY 269 278 278 GLY GLY B . n 
B 1 270 ILE 270 279 279 ILE ILE B . n 
B 1 271 GLN 271 280 280 GLN GLN B . n 
B 1 272 GLN 272 281 281 GLN GLN B . n 
B 1 273 THR 273 282 282 THR THR B . n 
B 1 274 ALA 274 283 283 ALA ALA B . n 
B 1 275 GLY 275 284 284 GLY GLY B . n 
B 1 276 GLY 276 285 285 GLY GLY B . n 
B 1 277 GLY 277 286 286 GLY GLY B . n 
B 1 278 HIS 278 287 287 HIS HIS B . n 
B 1 279 ALA 279 288 288 ALA ALA B . n 
B 1 280 ALA 280 289 289 ALA ALA B . n 
B 1 281 GLN 281 290 290 GLN GLN B . n 
B 1 282 PHE 282 291 291 PHE PHE B . n 
B 1 283 LEU 283 292 292 LEU LEU B . n 
B 1 284 GLN 284 293 293 GLN GLN B . n 
B 1 285 ASP 285 294 294 ASP ASP B . n 
B 1 286 MET 286 295 295 MET MET B . n 
B 1 287 ARG 287 296 296 ARG ARG B . n 
B 1 288 ARG 288 297 297 ARG ARG B . n 
B 1 289 TYR 289 298 298 TYR TYR B . n 
B 1 290 MET 290 299 299 MET MET B . n 
B 1 291 PRO 291 300 300 PRO PRO B . n 
B 1 292 PRO 292 301 301 PRO PRO B . n 
B 1 293 ALA 293 302 302 ALA ALA B . n 
B 1 294 HIS 294 303 303 HIS HIS B . n 
B 1 295 ARG 295 304 304 ARG ARG B . n 
B 1 296 ASN 296 305 305 ASN ASN B . n 
B 1 297 PHE 297 306 306 PHE PHE B . n 
B 1 298 LEU 298 307 307 LEU LEU B . n 
B 1 299 CYS 299 308 308 CYS CYS B . n 
B 1 300 SER 300 309 309 SER SER B . n 
B 1 301 LEU 301 310 310 LEU LEU B . n 
B 1 302 GLU 302 311 311 GLU GLU B . n 
B 1 303 SER 303 312 312 SER SER B . n 
B 1 304 ASN 304 313 313 ASN ASN B . n 
B 1 305 PRO 305 314 314 PRO PRO B . n 
B 1 306 SER 306 315 315 SER SER B . n 
B 1 307 VAL 307 316 316 VAL VAL B . n 
B 1 308 ARG 308 317 317 ARG ARG B . n 
B 1 309 GLU 309 318 318 GLU GLU B . n 
B 1 310 PHE 310 319 319 PHE PHE B . n 
B 1 311 VAL 311 320 320 VAL VAL B . n 
B 1 312 LEU 312 321 321 LEU LEU B . n 
B 1 313 SER 313 322 322 SER SER B . n 
B 1 314 LYS 314 323 323 LYS LYS B . n 
B 1 315 GLY 315 324 324 GLY GLY B . n 
B 1 316 ASP 316 325 325 ASP ASP B . n 
B 1 317 ALA 317 326 326 ALA ALA B . n 
B 1 318 GLY 318 327 327 GLY GLY B . n 
B 1 319 LEU 319 328 328 LEU LEU B . n 
B 1 320 ARG 320 329 329 ARG ARG B . n 
B 1 321 GLU 321 330 330 GLU GLU B . n 
B 1 322 ALA 322 331 331 ALA ALA B . n 
B 1 323 TYR 323 332 332 TYR TYR B . n 
B 1 324 ASP 324 333 333 ASP ASP B . n 
B 1 325 ALA 325 334 334 ALA ALA B . n 
B 1 326 CYS 326 335 335 CYS CYS B . n 
B 1 327 VAL 327 336 336 VAL VAL B . n 
B 1 328 LYS 328 337 337 LYS LYS B . n 
B 1 329 ALA 329 338 338 ALA ALA B . n 
B 1 330 LEU 330 339 339 LEU LEU B . n 
B 1 331 VAL 331 340 340 VAL VAL B . n 
B 1 332 SER 332 341 341 SER SER B . n 
B 1 333 LEU 333 342 342 LEU LEU B . n 
B 1 334 ARG 334 343 343 ARG ARG B . n 
B 1 335 SER 335 344 344 SER SER B . n 
B 1 336 TYR 336 345 345 TYR TYR B . n 
B 1 337 HIS 337 346 346 HIS HIS B . n 
B 1 338 LEU 338 347 347 LEU LEU B . n 
B 1 339 GLN 339 348 348 GLN GLN B . n 
B 1 340 ILE 340 349 349 ILE ILE B . n 
B 1 341 VAL 341 350 350 VAL VAL B . n 
B 1 342 THR 342 351 351 THR THR B . n 
B 1 343 LYS 343 352 352 LYS LYS B . n 
B 1 344 TYR 344 353 353 TYR TYR B . n 
B 1 345 ILE 345 354 354 ILE ILE B . n 
B 1 346 LEU 346 355 355 LEU LEU B . n 
B 1 347 ILE 347 356 356 ILE ILE B . n 
B 1 348 PRO 348 357 357 PRO PRO B . n 
B 1 349 ALA 349 358 358 ALA ALA B . n 
B 1 350 SER 350 359 359 SER SER B . n 
B 1 351 GLN 351 360 360 GLN GLN B . n 
B 1 352 GLN 352 361 361 GLN GLN B . n 
B 1 353 PRO 353 362 362 PRO PRO B . n 
B 1 354 LYS 354 363 ?   ?   ?   B . n 
B 1 355 GLU 355 364 ?   ?   ?   B . n 
B 1 356 ASN 356 365 ?   ?   ?   B . n 
B 1 357 LYS 357 366 ?   ?   ?   B . n 
B 1 358 THR 358 367 ?   ?   ?   B . n 
B 1 359 SER 359 368 ?   ?   ?   B . n 
B 1 360 GLU 360 369 ?   ?   ?   B . n 
B 1 361 ASP 361 370 ?   ?   ?   B . n 
B 1 362 PRO 362 371 ?   ?   ?   B . n 
B 1 363 SER 363 372 ?   ?   ?   B . n 
B 1 364 LYS 364 373 ?   ?   ?   B . n 
B 1 365 LEU 365 374 ?   ?   ?   B . n 
B 1 366 GLU 366 375 ?   ?   ?   B . n 
B 1 367 ALA 367 376 ?   ?   ?   B . n 
B 1 368 LYS 368 377 ?   ?   ?   B . n 
B 1 369 GLY 369 378 ?   ?   ?   B . n 
B 1 370 THR 370 379 ?   ?   ?   B . n 
B 1 371 GLY 371 380 380 GLY GLY B . n 
B 1 372 GLY 372 381 381 GLY GLY B . n 
B 1 373 THR 373 382 382 THR THR B . n 
B 1 374 ASP 374 383 383 ASP ASP B . n 
B 1 375 LEU 375 384 384 LEU LEU B . n 
B 1 376 MET 376 385 385 MET MET B . n 
B 1 377 ASN 377 386 386 ASN ASN B . n 
B 1 378 PHE 378 387 387 PHE PHE B . n 
B 1 379 LEU 379 388 388 LEU LEU B . n 
B 1 380 LYS 380 389 389 LYS LYS B . n 
B 1 381 THR 381 390 390 THR THR B . n 
B 1 382 VAL 382 391 391 VAL VAL B . n 
B 1 383 ARG 383 392 392 ARG ARG B . n 
B 1 384 SER 384 393 393 SER SER B . n 
B 1 385 THR 385 394 394 THR THR B . n 
B 1 386 THR 386 395 395 THR THR B . n 
B 1 387 GLU 387 396 396 GLU GLU B . n 
B 1 388 LYS 388 397 397 LYS LYS B . n 
B 1 389 SER 389 398 398 SER SER B . n 
B 1 390 LEU 390 399 399 LEU LEU B . n 
B 1 391 LEU 391 400 400 LEU LEU B . n 
B 1 392 LYS 392 401 401 LYS LYS B . n 
B 1 393 GLU 393 402 402 GLU GLU B . n 
B 1 394 GLY 394 403 403 GLY GLY B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        W2Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   W2Z 
_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 
C 2 HEM 1   501 500 HEM HEM A . 
D 3 W2Z 1   502 1   W2Z INX A . 
E 2 HEM 1   501 500 HEM HEM B . 
F 3 W2Z 1   502 2   W2Z INX B . 
G 4 HOH 1   601 328 HOH HOH A . 
G 4 HOH 2   602 423 HOH HOH A . 
G 4 HOH 3   603 246 HOH HOH A . 
G 4 HOH 4   604 600 HOH HOH A . 
G 4 HOH 5   605 414 HOH HOH A . 
G 4 HOH 6   606 356 HOH HOH A . 
G 4 HOH 7   607 279 HOH HOH A . 
G 4 HOH 8   608 267 HOH HOH A . 
G 4 HOH 9   609 26  HOH HOH A . 
G 4 HOH 10  610 143 HOH HOH A . 
G 4 HOH 11  611 71  HOH HOH A . 
G 4 HOH 12  612 463 HOH HOH A . 
G 4 HOH 13  613 121 HOH HOH A . 
G 4 HOH 14  614 165 HOH HOH A . 
G 4 HOH 15  615 195 HOH HOH A . 
G 4 HOH 16  616 271 HOH HOH A . 
G 4 HOH 17  617 63  HOH HOH A . 
G 4 HOH 18  618 326 HOH HOH A . 
G 4 HOH 19  619 123 HOH HOH A . 
G 4 HOH 20  620 633 HOH HOH A . 
G 4 HOH 21  621 66  HOH HOH A . 
G 4 HOH 22  622 4   HOH HOH A . 
G 4 HOH 23  623 346 HOH HOH A . 
G 4 HOH 24  624 196 HOH HOH A . 
G 4 HOH 25  625 45  HOH HOH A . 
G 4 HOH 26  626 363 HOH HOH A . 
G 4 HOH 27  627 102 HOH HOH A . 
G 4 HOH 28  628 270 HOH HOH A . 
G 4 HOH 29  629 412 HOH HOH A . 
G 4 HOH 30  630 28  HOH HOH A . 
G 4 HOH 31  631 198 HOH HOH A . 
G 4 HOH 32  632 80  HOH HOH A . 
G 4 HOH 33  633 259 HOH HOH A . 
G 4 HOH 34  634 197 HOH HOH A . 
G 4 HOH 35  635 200 HOH HOH A . 
G 4 HOH 36  636 125 HOH HOH A . 
G 4 HOH 37  637 375 HOH HOH A . 
G 4 HOH 38  638 218 HOH HOH A . 
G 4 HOH 39  639 337 HOH HOH A . 
G 4 HOH 40  640 297 HOH HOH A . 
G 4 HOH 41  641 36  HOH HOH A . 
G 4 HOH 42  642 642 HOH HOH A . 
G 4 HOH 43  643 492 HOH HOH A . 
G 4 HOH 44  644 323 HOH HOH A . 
G 4 HOH 45  645 331 HOH HOH A . 
G 4 HOH 46  646 219 HOH HOH A . 
G 4 HOH 47  647 10  HOH HOH A . 
G 4 HOH 48  648 68  HOH HOH A . 
G 4 HOH 49  649 171 HOH HOH A . 
G 4 HOH 50  650 38  HOH HOH A . 
G 4 HOH 51  651 253 HOH HOH A . 
G 4 HOH 52  652 51  HOH HOH A . 
G 4 HOH 53  653 107 HOH HOH A . 
G 4 HOH 54  654 451 HOH HOH A . 
G 4 HOH 55  655 417 HOH HOH A . 
G 4 HOH 56  656 75  HOH HOH A . 
G 4 HOH 57  657 366 HOH HOH A . 
G 4 HOH 58  658 163 HOH HOH A . 
G 4 HOH 59  659 124 HOH HOH A . 
G 4 HOH 60  660 120 HOH HOH A . 
G 4 HOH 61  661 211 HOH HOH A . 
G 4 HOH 62  662 73  HOH HOH A . 
G 4 HOH 63  663 64  HOH HOH A . 
G 4 HOH 64  664 357 HOH HOH A . 
G 4 HOH 65  665 631 HOH HOH A . 
G 4 HOH 66  666 176 HOH HOH A . 
G 4 HOH 67  667 273 HOH HOH A . 
G 4 HOH 68  668 53  HOH HOH A . 
G 4 HOH 69  669 546 HOH HOH A . 
G 4 HOH 70  670 191 HOH HOH A . 
G 4 HOH 71  671 50  HOH HOH A . 
G 4 HOH 72  672 597 HOH HOH A . 
G 4 HOH 73  673 95  HOH HOH A . 
G 4 HOH 74  674 110 HOH HOH A . 
G 4 HOH 75  675 54  HOH HOH A . 
G 4 HOH 76  676 158 HOH HOH A . 
G 4 HOH 77  677 192 HOH HOH A . 
G 4 HOH 78  678 330 HOH HOH A . 
G 4 HOH 79  679 275 HOH HOH A . 
G 4 HOH 80  680 316 HOH HOH A . 
G 4 HOH 81  681 162 HOH HOH A . 
G 4 HOH 82  682 482 HOH HOH A . 
G 4 HOH 83  683 405 HOH HOH A . 
G 4 HOH 84  684 432 HOH HOH A . 
G 4 HOH 85  685 148 HOH HOH A . 
G 4 HOH 86  686 130 HOH HOH A . 
G 4 HOH 87  687 177 HOH HOH A . 
G 4 HOH 88  688 530 HOH HOH A . 
G 4 HOH 89  689 353 HOH HOH A . 
G 4 HOH 90  690 416 HOH HOH A . 
G 4 HOH 91  691 47  HOH HOH A . 
G 4 HOH 92  692 169 HOH HOH A . 
G 4 HOH 93  693 518 HOH HOH A . 
G 4 HOH 94  694 61  HOH HOH A . 
G 4 HOH 95  695 65  HOH HOH A . 
G 4 HOH 96  696 81  HOH HOH A . 
G 4 HOH 97  697 35  HOH HOH A . 
G 4 HOH 98  698 588 HOH HOH A . 
G 4 HOH 99  699 59  HOH HOH A . 
G 4 HOH 100 700 339 HOH HOH A . 
G 4 HOH 101 701 295 HOH HOH A . 
G 4 HOH 102 702 128 HOH HOH A . 
G 4 HOH 103 703 138 HOH HOH A . 
G 4 HOH 104 704 49  HOH HOH A . 
G 4 HOH 105 705 106 HOH HOH A . 
G 4 HOH 106 706 239 HOH HOH A . 
G 4 HOH 107 707 159 HOH HOH A . 
G 4 HOH 108 708 434 HOH HOH A . 
G 4 HOH 109 709 126 HOH HOH A . 
G 4 HOH 110 710 132 HOH HOH A . 
G 4 HOH 111 711 79  HOH HOH A . 
G 4 HOH 112 712 205 HOH HOH A . 
G 4 HOH 113 713 260 HOH HOH A . 
G 4 HOH 114 714 193 HOH HOH A . 
G 4 HOH 115 715 329 HOH HOH A . 
G 4 HOH 116 716 27  HOH HOH A . 
G 4 HOH 117 717 151 HOH HOH A . 
G 4 HOH 118 718 5   HOH HOH A . 
G 4 HOH 119 719 127 HOH HOH A . 
G 4 HOH 120 720 296 HOH HOH A . 
G 4 HOH 121 721 25  HOH HOH A . 
G 4 HOH 122 722 635 HOH HOH A . 
G 4 HOH 123 723 113 HOH HOH A . 
G 4 HOH 124 724 76  HOH HOH A . 
G 4 HOH 125 725 213 HOH HOH A . 
G 4 HOH 126 726 6   HOH HOH A . 
G 4 HOH 127 727 214 HOH HOH A . 
G 4 HOH 128 728 436 HOH HOH A . 
G 4 HOH 129 729 118 HOH HOH A . 
G 4 HOH 130 730 114 HOH HOH A . 
G 4 HOH 131 731 306 HOH HOH A . 
G 4 HOH 132 732 409 HOH HOH A . 
G 4 HOH 133 733 315 HOH HOH A . 
G 4 HOH 134 734 40  HOH HOH A . 
G 4 HOH 135 735 72  HOH HOH A . 
G 4 HOH 136 736 251 HOH HOH A . 
G 4 HOH 137 737 108 HOH HOH A . 
G 4 HOH 138 738 475 HOH HOH A . 
G 4 HOH 139 739 77  HOH HOH A . 
G 4 HOH 140 740 474 HOH HOH A . 
G 4 HOH 141 741 188 HOH HOH A . 
G 4 HOH 142 742 304 HOH HOH A . 
G 4 HOH 143 743 224 HOH HOH A . 
G 4 HOH 144 744 142 HOH HOH A . 
G 4 HOH 145 745 93  HOH HOH A . 
G 4 HOH 146 746 7   HOH HOH A . 
G 4 HOH 147 747 348 HOH HOH A . 
G 4 HOH 148 748 452 HOH HOH A . 
G 4 HOH 149 749 310 HOH HOH A . 
G 4 HOH 150 750 255 HOH HOH A . 
G 4 HOH 151 751 335 HOH HOH A . 
G 4 HOH 152 752 444 HOH HOH A . 
G 4 HOH 153 753 359 HOH HOH A . 
G 4 HOH 154 754 94  HOH HOH A . 
G 4 HOH 155 755 470 HOH HOH A . 
G 4 HOH 156 756 439 HOH HOH A . 
G 4 HOH 157 757 428 HOH HOH A . 
G 4 HOH 158 758 526 HOH HOH A . 
G 4 HOH 159 759 468 HOH HOH A . 
G 4 HOH 160 760 478 HOH HOH A . 
G 4 HOH 161 761 321 HOH HOH A . 
G 4 HOH 162 762 290 HOH HOH A . 
G 4 HOH 163 763 223 HOH HOH A . 
G 4 HOH 164 764 52  HOH HOH A . 
G 4 HOH 165 765 314 HOH HOH A . 
G 4 HOH 166 766 261 HOH HOH A . 
G 4 HOH 167 767 289 HOH HOH A . 
G 4 HOH 168 768 115 HOH HOH A . 
G 4 HOH 169 769 212 HOH HOH A . 
G 4 HOH 170 770 570 HOH HOH A . 
G 4 HOH 171 771 401 HOH HOH A . 
G 4 HOH 172 772 352 HOH HOH A . 
G 4 HOH 173 773 266 HOH HOH A . 
G 4 HOH 174 774 528 HOH HOH A . 
G 4 HOH 175 775 111 HOH HOH A . 
G 4 HOH 176 776 361 HOH HOH A . 
G 4 HOH 177 777 17  HOH HOH A . 
G 4 HOH 178 778 140 HOH HOH A . 
G 4 HOH 179 779 447 HOH HOH A . 
G 4 HOH 180 780 264 HOH HOH A . 
G 4 HOH 181 781 90  HOH HOH A . 
G 4 HOH 182 782 421 HOH HOH A . 
G 4 HOH 183 783 584 HOH HOH A . 
G 4 HOH 184 784 202 HOH HOH A . 
G 4 HOH 185 785 605 HOH HOH A . 
G 4 HOH 186 786 226 HOH HOH A . 
G 4 HOH 187 787 648 HOH HOH A . 
G 4 HOH 188 788 131 HOH HOH A . 
G 4 HOH 189 789 645 HOH HOH A . 
G 4 HOH 190 790 469 HOH HOH A . 
G 4 HOH 191 791 269 HOH HOH A . 
G 4 HOH 192 792 332 HOH HOH A . 
G 4 HOH 193 793 578 HOH HOH A . 
G 4 HOH 194 794 201 HOH HOH A . 
G 4 HOH 195 795 221 HOH HOH A . 
G 4 HOH 196 796 8   HOH HOH A . 
G 4 HOH 197 797 394 HOH HOH A . 
G 4 HOH 198 798 254 HOH HOH A . 
G 4 HOH 199 799 586 HOH HOH A . 
G 4 HOH 200 800 117 HOH HOH A . 
G 4 HOH 201 801 364 HOH HOH A . 
G 4 HOH 202 802 598 HOH HOH A . 
G 4 HOH 203 803 349 HOH HOH A . 
G 4 HOH 204 804 587 HOH HOH A . 
G 4 HOH 205 805 590 HOH HOH A . 
G 4 HOH 206 806 367 HOH HOH A . 
G 4 HOH 207 807 173 HOH HOH A . 
G 4 HOH 208 808 601 HOH HOH A . 
G 4 HOH 209 809 362 HOH HOH A . 
G 4 HOH 210 810 319 HOH HOH A . 
G 4 HOH 211 811 325 HOH HOH A . 
G 4 HOH 212 812 458 HOH HOH A . 
G 4 HOH 213 813 610 HOH HOH A . 
G 4 HOH 214 814 322 HOH HOH A . 
G 4 HOH 215 815 276 HOH HOH A . 
G 4 HOH 216 816 155 HOH HOH A . 
G 4 HOH 217 817 634 HOH HOH A . 
G 4 HOH 218 818 243 HOH HOH A . 
G 4 HOH 219 819 583 HOH HOH A . 
G 4 HOH 220 820 249 HOH HOH A . 
G 4 HOH 221 821 248 HOH HOH A . 
G 4 HOH 222 822 234 HOH HOH A . 
G 4 HOH 223 823 373 HOH HOH A . 
G 4 HOH 224 824 589 HOH HOH A . 
G 4 HOH 225 825 647 HOH HOH A . 
G 4 HOH 226 826 299 HOH HOH A . 
G 4 HOH 227 827 602 HOH HOH A . 
G 4 HOH 228 828 609 HOH HOH A . 
G 4 HOH 229 829 594 HOH HOH A . 
G 4 HOH 230 830 579 HOH HOH A . 
G 4 HOH 231 831 643 HOH HOH A . 
G 4 HOH 232 832 637 HOH HOH A . 
G 4 HOH 233 833 455 HOH HOH A . 
G 4 HOH 234 834 236 HOH HOH A . 
G 4 HOH 235 835 374 HOH HOH A . 
G 4 HOH 236 836 607 HOH HOH A . 
G 4 HOH 237 837 636 HOH HOH A . 
G 4 HOH 238 838 592 HOH HOH A . 
G 4 HOH 239 839 591 HOH HOH A . 
G 4 HOH 240 840 459 HOH HOH A . 
G 4 HOH 241 841 596 HOH HOH A . 
G 4 HOH 242 842 376 HOH HOH A . 
G 4 HOH 243 843 606 HOH HOH A . 
H 4 HOH 1   601 483 HOH HOH B . 
H 4 HOH 2   602 450 HOH HOH B . 
H 4 HOH 3   603 388 HOH HOH B . 
H 4 HOH 4   604 13  HOH HOH B . 
H 4 HOH 5   605 55  HOH HOH B . 
H 4 HOH 6   606 621 HOH HOH B . 
H 4 HOH 7   607 479 HOH HOH B . 
H 4 HOH 8   608 187 HOH HOH B . 
H 4 HOH 9   609 340 HOH HOH B . 
H 4 HOH 10  610 268 HOH HOH B . 
H 4 HOH 11  611 334 HOH HOH B . 
H 4 HOH 12  612 485 HOH HOH B . 
H 4 HOH 13  613 62  HOH HOH B . 
H 4 HOH 14  614 179 HOH HOH B . 
H 4 HOH 15  615 393 HOH HOH B . 
H 4 HOH 16  616 43  HOH HOH B . 
H 4 HOH 17  617 33  HOH HOH B . 
H 4 HOH 18  618 639 HOH HOH B . 
H 4 HOH 19  619 229 HOH HOH B . 
H 4 HOH 20  620 342 HOH HOH B . 
H 4 HOH 21  621 386 HOH HOH B . 
H 4 HOH 22  622 83  HOH HOH B . 
H 4 HOH 23  623 265 HOH HOH B . 
H 4 HOH 24  624 97  HOH HOH B . 
H 4 HOH 25  625 141 HOH HOH B . 
H 4 HOH 26  626 462 HOH HOH B . 
H 4 HOH 27  627 87  HOH HOH B . 
H 4 HOH 28  628 390 HOH HOH B . 
H 4 HOH 29  629 70  HOH HOH B . 
H 4 HOH 30  630 39  HOH HOH B . 
H 4 HOH 31  631 446 HOH HOH B . 
H 4 HOH 32  632 247 HOH HOH B . 
H 4 HOH 33  633 186 HOH HOH B . 
H 4 HOH 34  634 85  HOH HOH B . 
H 4 HOH 35  635 42  HOH HOH B . 
H 4 HOH 36  636 217 HOH HOH B . 
H 4 HOH 37  637 134 HOH HOH B . 
H 4 HOH 38  638 377 HOH HOH B . 
H 4 HOH 39  639 88  HOH HOH B . 
H 4 HOH 40  640 347 HOH HOH B . 
H 4 HOH 41  641 11  HOH HOH B . 
H 4 HOH 42  642 619 HOH HOH B . 
H 4 HOH 43  643 208 HOH HOH B . 
H 4 HOH 44  644 18  HOH HOH B . 
H 4 HOH 45  645 2   HOH HOH B . 
H 4 HOH 46  646 406 HOH HOH B . 
H 4 HOH 47  647 287 HOH HOH B . 
H 4 HOH 48  648 302 HOH HOH B . 
H 4 HOH 49  649 96  HOH HOH B . 
H 4 HOH 50  650 399 HOH HOH B . 
H 4 HOH 51  651 154 HOH HOH B . 
H 4 HOH 52  652 48  HOH HOH B . 
H 4 HOH 53  653 116 HOH HOH B . 
H 4 HOH 54  654 164 HOH HOH B . 
H 4 HOH 55  655 225 HOH HOH B . 
H 4 HOH 56  656 274 HOH HOH B . 
H 4 HOH 57  657 82  HOH HOH B . 
H 4 HOH 58  658 112 HOH HOH B . 
H 4 HOH 59  659 194 HOH HOH B . 
H 4 HOH 60  660 9   HOH HOH B . 
H 4 HOH 61  661 383 HOH HOH B . 
H 4 HOH 62  662 189 HOH HOH B . 
H 4 HOH 63  663 31  HOH HOH B . 
H 4 HOH 64  664 41  HOH HOH B . 
H 4 HOH 65  665 69  HOH HOH B . 
H 4 HOH 66  666 78  HOH HOH B . 
H 4 HOH 67  667 442 HOH HOH B . 
H 4 HOH 68  668 220 HOH HOH B . 
H 4 HOH 69  669 181 HOH HOH B . 
H 4 HOH 70  670 429 HOH HOH B . 
H 4 HOH 71  671 29  HOH HOH B . 
H 4 HOH 72  672 385 HOH HOH B . 
H 4 HOH 73  673 56  HOH HOH B . 
H 4 HOH 74  674 241 HOH HOH B . 
H 4 HOH 75  675 122 HOH HOH B . 
H 4 HOH 76  676 152 HOH HOH B . 
H 4 HOH 77  677 101 HOH HOH B . 
H 4 HOH 78  678 146 HOH HOH B . 
H 4 HOH 79  679 34  HOH HOH B . 
H 4 HOH 80  680 257 HOH HOH B . 
H 4 HOH 81  681 19  HOH HOH B . 
H 4 HOH 82  682 60  HOH HOH B . 
H 4 HOH 83  683 156 HOH HOH B . 
H 4 HOH 84  684 30  HOH HOH B . 
H 4 HOH 85  685 210 HOH HOH B . 
H 4 HOH 86  686 391 HOH HOH B . 
H 4 HOH 87  687 206 HOH HOH B . 
H 4 HOH 88  688 392 HOH HOH B . 
H 4 HOH 89  689 431 HOH HOH B . 
H 4 HOH 90  690 491 HOH HOH B . 
H 4 HOH 91  691 403 HOH HOH B . 
H 4 HOH 92  692 147 HOH HOH B . 
H 4 HOH 93  693 183 HOH HOH B . 
H 4 HOH 94  694 473 HOH HOH B . 
H 4 HOH 95  695 166 HOH HOH B . 
H 4 HOH 96  696 23  HOH HOH B . 
H 4 HOH 97  697 22  HOH HOH B . 
H 4 HOH 98  698 84  HOH HOH B . 
H 4 HOH 99  699 277 HOH HOH B . 
H 4 HOH 100 700 309 HOH HOH B . 
H 4 HOH 101 701 149 HOH HOH B . 
H 4 HOH 102 702 1   HOH HOH B . 
H 4 HOH 103 703 44  HOH HOH B . 
H 4 HOH 104 704 410 HOH HOH B . 
H 4 HOH 105 705 222 HOH HOH B . 
H 4 HOH 106 706 46  HOH HOH B . 
H 4 HOH 107 707 174 HOH HOH B . 
H 4 HOH 108 708 282 HOH HOH B . 
H 4 HOH 109 709 327 HOH HOH B . 
H 4 HOH 110 710 144 HOH HOH B . 
H 4 HOH 111 711 3   HOH HOH B . 
H 4 HOH 112 712 32  HOH HOH B . 
H 4 HOH 113 713 105 HOH HOH B . 
H 4 HOH 114 714 99  HOH HOH B . 
H 4 HOH 115 715 24  HOH HOH B . 
H 4 HOH 116 716 230 HOH HOH B . 
H 4 HOH 117 717 109 HOH HOH B . 
H 4 HOH 118 718 430 HOH HOH B . 
H 4 HOH 119 719 167 HOH HOH B . 
H 4 HOH 120 720 20  HOH HOH B . 
H 4 HOH 121 721 12  HOH HOH B . 
H 4 HOH 122 722 285 HOH HOH B . 
H 4 HOH 123 723 170 HOH HOH B . 
H 4 HOH 124 724 172 HOH HOH B . 
H 4 HOH 125 725 630 HOH HOH B . 
H 4 HOH 126 726 445 HOH HOH B . 
H 4 HOH 127 727 301 HOH HOH B . 
H 4 HOH 128 728 160 HOH HOH B . 
H 4 HOH 129 729 145 HOH HOH B . 
H 4 HOH 130 730 184 HOH HOH B . 
H 4 HOH 131 731 58  HOH HOH B . 
H 4 HOH 132 732 617 HOH HOH B . 
H 4 HOH 133 733 227 HOH HOH B . 
H 4 HOH 134 734 100 HOH HOH B . 
H 4 HOH 135 735 98  HOH HOH B . 
H 4 HOH 136 736 157 HOH HOH B . 
H 4 HOH 137 737 139 HOH HOH B . 
H 4 HOH 138 738 168 HOH HOH B . 
H 4 HOH 139 739 620 HOH HOH B . 
H 4 HOH 140 740 400 HOH HOH B . 
H 4 HOH 141 741 379 HOH HOH B . 
H 4 HOH 142 742 199 HOH HOH B . 
H 4 HOH 143 743 252 HOH HOH B . 
H 4 HOH 144 744 209 HOH HOH B . 
H 4 HOH 145 745 153 HOH HOH B . 
H 4 HOH 146 746 175 HOH HOH B . 
H 4 HOH 147 747 91  HOH HOH B . 
H 4 HOH 148 748 216 HOH HOH B . 
H 4 HOH 149 749 500 HOH HOH B . 
H 4 HOH 150 750 318 HOH HOH B . 
H 4 HOH 151 751 203 HOH HOH B . 
H 4 HOH 152 752 150 HOH HOH B . 
H 4 HOH 153 753 533 HOH HOH B . 
H 4 HOH 154 754 92  HOH HOH B . 
H 4 HOH 155 755 235 HOH HOH B . 
H 4 HOH 156 756 284 HOH HOH B . 
H 4 HOH 157 757 129 HOH HOH B . 
H 4 HOH 158 758 308 HOH HOH B . 
H 4 HOH 159 759 298 HOH HOH B . 
H 4 HOH 160 760 424 HOH HOH B . 
H 4 HOH 161 761 294 HOH HOH B . 
H 4 HOH 162 762 16  HOH HOH B . 
H 4 HOH 163 763 190 HOH HOH B . 
H 4 HOH 164 764 638 HOH HOH B . 
H 4 HOH 165 765 272 HOH HOH B . 
H 4 HOH 166 766 395 HOH HOH B . 
H 4 HOH 167 767 398 HOH HOH B . 
H 4 HOH 168 768 37  HOH HOH B . 
H 4 HOH 169 769 313 HOH HOH B . 
H 4 HOH 170 770 136 HOH HOH B . 
H 4 HOH 171 771 258 HOH HOH B . 
H 4 HOH 172 772 293 HOH HOH B . 
H 4 HOH 173 773 135 HOH HOH B . 
H 4 HOH 174 774 103 HOH HOH B . 
H 4 HOH 175 775 378 HOH HOH B . 
H 4 HOH 176 776 627 HOH HOH B . 
H 4 HOH 177 777 104 HOH HOH B . 
H 4 HOH 178 778 300 HOH HOH B . 
H 4 HOH 179 779 476 HOH HOH B . 
H 4 HOH 180 780 182 HOH HOH B . 
H 4 HOH 181 781 133 HOH HOH B . 
H 4 HOH 182 782 233 HOH HOH B . 
H 4 HOH 183 783 178 HOH HOH B . 
H 4 HOH 184 784 333 HOH HOH B . 
H 4 HOH 185 785 618 HOH HOH B . 
H 4 HOH 186 786 57  HOH HOH B . 
H 4 HOH 187 787 161 HOH HOH B . 
H 4 HOH 188 788 15  HOH HOH B . 
H 4 HOH 189 789 611 HOH HOH B . 
H 4 HOH 190 790 336 HOH HOH B . 
H 4 HOH 191 791 343 HOH HOH B . 
H 4 HOH 192 792 625 HOH HOH B . 
H 4 HOH 193 793 464 HOH HOH B . 
H 4 HOH 194 794 422 HOH HOH B . 
H 4 HOH 195 795 288 HOH HOH B . 
H 4 HOH 196 796 305 HOH HOH B . 
H 4 HOH 197 797 245 HOH HOH B . 
H 4 HOH 198 798 486 HOH HOH B . 
H 4 HOH 199 799 415 HOH HOH B . 
H 4 HOH 200 800 616 HOH HOH B . 
H 4 HOH 201 801 291 HOH HOH B . 
H 4 HOH 202 802 426 HOH HOH B . 
H 4 HOH 203 803 644 HOH HOH B . 
H 4 HOH 204 804 641 HOH HOH B . 
H 4 HOH 205 805 14  HOH HOH B . 
H 4 HOH 206 806 612 HOH HOH B . 
H 4 HOH 207 807 387 HOH HOH B . 
H 4 HOH 208 808 615 HOH HOH B . 
H 4 HOH 209 809 360 HOH HOH B . 
H 4 HOH 210 810 137 HOH HOH B . 
H 4 HOH 211 811 461 HOH HOH B . 
H 4 HOH 212 812 622 HOH HOH B . 
H 4 HOH 213 813 341 HOH HOH B . 
H 4 HOH 214 814 215 HOH HOH B . 
H 4 HOH 215 815 256 HOH HOH B . 
H 4 HOH 216 816 454 HOH HOH B . 
H 4 HOH 217 817 382 HOH HOH B . 
H 4 HOH 218 818 320 HOH HOH B . 
H 4 HOH 219 819 250 HOH HOH B . 
H 4 HOH 220 820 180 HOH HOH B . 
H 4 HOH 221 821 628 HOH HOH B . 
H 4 HOH 222 822 204 HOH HOH B . 
H 4 HOH 223 823 608 HOH HOH B . 
H 4 HOH 224 824 623 HOH HOH B . 
H 4 HOH 225 825 460 HOH HOH B . 
H 4 HOH 226 826 312 HOH HOH B . 
H 4 HOH 227 827 244 HOH HOH B . 
H 4 HOH 228 828 629 HOH HOH B . 
H 4 HOH 229 829 384 HOH HOH B . 
H 4 HOH 230 830 185 HOH HOH B . 
H 4 HOH 231 831 624 HOH HOH B . 
H 4 HOH 232 832 457 HOH HOH B . 
H 4 HOH 233 833 380 HOH HOH B . 
H 4 HOH 234 834 381 HOH HOH B . 
H 4 HOH 235 835 646 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A MET 10  ? SD  ? A MET 1   SD  
2  1 Y 0 A MET 10  ? CE  ? A MET 1   CE  
3  1 Y 0 A LYS 13  ? CG  ? A LYS 4   CG  
4  1 Y 0 A LYS 13  ? CD  ? A LYS 4   CD  
5  1 Y 0 A LYS 13  ? CE  ? A LYS 4   CE  
6  1 Y 0 A LYS 13  ? NZ  ? A LYS 4   NZ  
7  1 Y 0 A GLU 14  ? CG  ? A GLU 5   CG  
8  1 Y 0 A GLU 14  ? CD  ? A GLU 5   CD  
9  1 Y 0 A GLU 14  ? OE1 ? A GLU 5   OE1 
10 1 Y 0 A GLU 14  ? OE2 ? A GLU 5   OE2 
11 1 Y 0 A GLU 19  ? CG  ? A GLU 10  CG  
12 1 Y 0 A GLU 19  ? CD  ? A GLU 10  CD  
13 1 Y 0 A GLU 19  ? OE1 ? A GLU 10  OE1 
14 1 Y 0 A GLU 19  ? OE2 ? A GLU 10  OE2 
15 1 Y 0 A LYS 44  ? CE  ? A LYS 35  CE  
16 1 Y 0 A LYS 44  ? NZ  ? A LYS 35  NZ  
17 1 Y 0 A LYS 101 ? CE  ? A LYS 92  CE  
18 1 Y 0 A LYS 101 ? NZ  ? A LYS 92  NZ  
19 1 Y 0 A LYS 116 ? NZ  ? A LYS 107 NZ  
20 1 Y 0 A LYS 117 ? NZ  ? A LYS 108 NZ  
21 1 Y 0 A LYS 141 ? CE  ? A LYS 132 CE  
22 1 Y 0 A LYS 141 ? NZ  ? A LYS 132 NZ  
23 1 Y 0 A GLU 146 ? CG  ? A GLU 137 CG  
24 1 Y 0 A GLU 146 ? CD  ? A GLU 137 CD  
25 1 Y 0 A GLU 146 ? OE1 ? A GLU 137 OE1 
26 1 Y 0 A GLU 146 ? OE2 ? A GLU 137 OE2 
27 1 Y 0 A ILE 178 ? CD1 ? A ILE 169 CD1 
28 1 Y 0 A LYS 186 ? CD  ? A LYS 177 CD  
29 1 Y 0 A LYS 186 ? CE  ? A LYS 177 CE  
30 1 Y 0 A LYS 186 ? NZ  ? A LYS 177 NZ  
31 1 Y 0 A GLN 189 ? CG  ? A GLN 180 CG  
32 1 Y 0 A GLN 189 ? CD  ? A GLN 180 CD  
33 1 Y 0 A GLN 189 ? OE1 ? A GLN 180 OE1 
34 1 Y 0 A GLN 189 ? NE2 ? A GLN 180 NE2 
35 1 Y 0 A MET 190 ? CE  ? A MET 181 CE  
36 1 Y 0 A LYS 198 ? CE  ? A LYS 189 CE  
37 1 Y 0 A LYS 198 ? NZ  ? A LYS 189 NZ  
38 1 Y 0 A LYS 209 ? CD  ? A LYS 200 CD  
39 1 Y 0 A LYS 209 ? CE  ? A LYS 200 CE  
40 1 Y 0 A LYS 209 ? NZ  ? A LYS 200 NZ  
41 1 Y 0 A LYS 224 ? CE  ? A LYS 215 CE  
42 1 Y 0 A LYS 224 ? NZ  ? A LYS 215 NZ  
43 1 Y 0 A GLU 254 ? CD  ? A GLU 245 CD  
44 1 Y 0 A GLU 254 ? OE1 ? A GLU 245 OE1 
45 1 Y 0 A GLU 254 ? OE2 ? A GLU 245 OE2 
46 1 Y 0 A GLU 318 ? CD  ? A GLU 309 CD  
47 1 Y 0 A GLU 318 ? OE1 ? A GLU 309 OE1 
48 1 Y 0 A GLU 318 ? OE2 ? A GLU 309 OE2 
49 1 Y 0 A LYS 323 ? NZ  ? A LYS 314 NZ  
50 1 Y 0 A LYS 337 ? NZ  ? A LYS 328 NZ  
51 1 Y 0 A GLU 396 ? CD  ? A GLU 387 CD  
52 1 Y 0 A GLU 396 ? OE1 ? A GLU 387 OE1 
53 1 Y 0 A GLU 396 ? OE2 ? A GLU 387 OE2 
54 1 Y 0 A LYS 397 ? NZ  ? A LYS 388 NZ  
55 1 Y 0 A LYS 401 ? NZ  ? A LYS 392 NZ  
56 1 Y 0 B SER 12  ? OG  ? B SER 3   OG  
57 1 Y 0 B LYS 13  ? CE  ? B LYS 4   CE  
58 1 Y 0 B LYS 13  ? NZ  ? B LYS 4   NZ  
59 1 Y 0 B GLU 14  ? CG  ? B GLU 5   CG  
60 1 Y 0 B GLU 14  ? CD  ? B GLU 5   CD  
61 1 Y 0 B GLU 14  ? OE1 ? B GLU 5   OE1 
62 1 Y 0 B GLU 14  ? OE2 ? B GLU 5   OE2 
63 1 Y 0 B LYS 44  ? CD  ? B LYS 35  CD  
64 1 Y 0 B LYS 44  ? CE  ? B LYS 35  CE  
65 1 Y 0 B LYS 44  ? NZ  ? B LYS 35  NZ  
66 1 Y 0 B LYS 101 ? CE  ? B LYS 92  CE  
67 1 Y 0 B LYS 101 ? NZ  ? B LYS 92  NZ  
68 1 Y 0 B LYS 116 ? CE  ? B LYS 107 CE  
69 1 Y 0 B LYS 116 ? NZ  ? B LYS 107 NZ  
70 1 Y 0 B LYS 141 ? NZ  ? B LYS 132 NZ  
71 1 Y 0 B ILE 178 ? CD1 ? B ILE 169 CD1 
72 1 Y 0 B LYS 186 ? CE  ? B LYS 177 CE  
73 1 Y 0 B LYS 186 ? NZ  ? B LYS 177 NZ  
74 1 Y 0 B GLN 189 ? CD  ? B GLN 180 CD  
75 1 Y 0 B GLN 189 ? OE1 ? B GLN 180 OE1 
76 1 Y 0 B GLN 189 ? NE2 ? B GLN 180 NE2 
77 1 Y 0 B LYS 198 ? NZ  ? B LYS 189 NZ  
78 1 Y 0 B LYS 224 ? CE  ? B LYS 215 CE  
79 1 Y 0 B LYS 224 ? NZ  ? B LYS 215 NZ  
80 1 Y 0 B LYS 337 ? CD  ? B LYS 328 CD  
81 1 Y 0 B LYS 337 ? CE  ? B LYS 328 CE  
82 1 Y 0 B LYS 337 ? NZ  ? B LYS 328 NZ  
83 1 Y 0 B LYS 401 ? NZ  ? B LYS 392 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.2.0005 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        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                     8U5I 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.862 
_cell.length_a_esd                 ? 
_cell.length_b                     89.888 
_cell.length_b_esd                 ? 
_cell.length_c                     133.520 
_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                         8U5I 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8U5I 
_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             2.87 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.15 
_exptl_crystal.description                  ? 
_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              8 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% (w/v) PEG 6K, 0.10M TRIS/HCl pH=8.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-04-07 
_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                    ? 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8U5I 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.17 
_reflns.d_resolution_low                               45.31 
_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                                     53451 
_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                           97.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.71 
_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                                0.078 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.071 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_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 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
_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 
2.17  2.42  ? ? ? ? ? ? 14886 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.48700000000000004  ? ? 1 1 0.9329999999999999 ? ? ? ? 
0.44299999999999995  ? ? ? ? ? ? ? ? ? 
2.42  2.67  ? ? ? ? ? ? 9832  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.266                ? ? 2 1 0.972              ? ? ? ? 0.242 ? ? ? ? 
? ? ? ? ? 
2.67  3.07  ? ? ? ? ? ? 9789  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.135                ? ? 3 1 0.991              ? ? ? ? 0.122 ? ? ? ? 
? ? ? ? ? 
3.07  3.74  ? ? ? ? ? ? 8521  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.063                ? ? 4 1 0.997              ? ? ? ? 0.057 ? ? ? ? 
? ? ? ? ? 
3.74  4.74  ? ? ? ? ? ? 5270  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.037000000000000005 ? ? 5 1 0.998              ? ? ? ? 0.033 ? ? ? ? 
? ? ? ? ? 
4.74  6.08  ? ? ? ? ? ? 2693  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.032                ? ? 6 1 0.9990000000000001 ? ? ? ? 
0.028999999999999998 ? ? ? ? ? ? ? ? ? 
6.08  8.88  ? ? ? ? ? ? 1644  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.027999999999999997 ? ? 7 1 0.9990000000000001 ? ? ? ? 
0.026000000000000002 ? ? ? ? ? ? ? ? ? 
8.88  14.21 ? ? ? ? ? ? 613   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.023                ? ? 8 1 0.9990000000000001 ? ? ? ? 0.021 ? ? ? ? 
? ? ? ? ? 
14.21 45.31 ? ? ? ? ? ? 203   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.027999999999999997 ? ? 9 1 0.998              ? ? ? ? 0.025 ? ? ? ? 
? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -2.04 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.54 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            1.50 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               38.619 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.929 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8U5I 
_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                            2.17 
_refine.ls_d_res_low                             45.31 
_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                     51992 
_refine.ls_number_reflns_R_free                  1459 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.67 
_refine.ls_percent_reflns_R_free                 2.7 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17795 
_refine.ls_R_factor_R_free                       0.21923 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17679 
_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                    'BABINET MODEL WITH MASK' 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.200 
_refine.pdbx_overall_ESU_R_Free                  0.173 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             8.722 
_refine.overall_SU_ML                            0.125 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.17 
_refine_hist.d_res_low                        45.31 
_refine_hist.number_atoms_solvent             478 
_refine_hist.number_atoms_total               6573 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5953 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         142 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.022  6364  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  5755  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.212  2.016  8706  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.973  3.000  13361 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.465  5.000  791   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.034 24.161 274   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.463 15.000 1044  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.098 15.000 33    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.071  0.200  940   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  7146  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1275  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? 0.187  0.200  1403  ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.141  0.200  5753  ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? 0.162  0.200  3103  ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.200  3198  ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? 0.112  0.200  429   ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? 0.192  0.200  16    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? 0.137  0.200  48    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? 0.102  0.200  16    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.621  2.000  5043  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.355  2.000  1559  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.984  3.000  6264  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.128  4.000  2939  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.164  6.000  2438  ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.170 
_refine_ls_shell.d_res_low                        2.226 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             110 
_refine_ls_shell.number_reflns_R_work             3819 
_refine_ls_shell.percent_reflns_obs               98.55 
_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                  0.221 
_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   20 
_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                  0.272 
# 
_struct.entry_id                     8U5I 
_struct.title                        'Crystal Structure of human IDO1 bound to Compound 23' 
_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        8U5I 
_struct_keywords.text            'IDO, TDO, complex, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    I23O1_HUMAN 
_struct_ref.pdbx_db_accession          P14902 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAY
VWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLV
EIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYE
GFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLRE
AYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
;
_struct_ref.pdbx_align_begin           11 
# 
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 8U5I A 2 ? 394 ? P14902 11 ? 403 ? 11 403 
2 1 8U5I B 2 ? 394 ? P14902 11 ? 403 ? 11 403 
# 
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 8U5I MET A 1 ? UNP P14902 ? ? 'initiating methionine' 10 1 
2 8U5I MET B 1 ? UNP P14902 ? ? 'initiating methionine' 10 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     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)' 4260  ? 
1 MORE         -47   ? 
1 'SSA (A^2)'  31090 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 SER A 3   ? HIS A 7   ? SER A 12  HIS A 16  5 ? 5  
HELX_P HELX_P2  AA2 PRO A 24  ? PHE A 26  ? PRO A 33  PHE A 35  5 ? 3  
HELX_P HELX_P3  AA3 TYR A 27  ? HIS A 36  ? TYR A 36  HIS A 45  1 ? 10 
HELX_P HELX_P4  AA4 HIS A 36  ? SER A 43  ? HIS A 45  SER A 52  1 ? 8  
HELX_P HELX_P5  AA5 GLN A 45  ? LYS A 52  ? GLN A 54  LYS A 61  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 63  ? GLY A 84  ? ASP A 72  GLY A 93  1 ? 22 
HELX_P HELX_P7  AA7 PRO A 95  ? GLU A 110 ? PRO A 104 GLU A 119 1 ? 16 
HELX_P HELX_P8  AA8 VAL A 116 ? VAL A 121 ? VAL A 125 VAL A 130 1 ? 6  
HELX_P HELX_P9  AA9 THR A 135 ? GLU A 137 ? THR A 144 GLU A 146 5 ? 3  
HELX_P HELX_P10 AB1 CYS A 150 ? SER A 167 ? CYS A 159 SER A 176 1 ? 18 
HELX_P HELX_P11 AB2 ALA A 168 ? LYS A 170 ? ALA A 177 LYS A 179 5 ? 3  
HELX_P HELX_P12 AB3 VAL A 171 ? MET A 181 ? VAL A 180 MET A 190 1 ? 11 
HELX_P HELX_P13 AB4 GLU A 183 ? HIS A 206 ? GLU A 192 HIS A 215 1 ? 24 
HELX_P HELX_P14 AB5 GLN A 207 ? VAL A 212 ? GLN A 216 VAL A 221 1 ? 6  
HELX_P HELX_P15 AB6 ASN A 213 ? VAL A 220 ? ASN A 222 VAL A 229 1 ? 8  
HELX_P HELX_P16 AB7 VAL A 220 ? SER A 226 ? VAL A 229 SER A 235 1 ? 7  
HELX_P HELX_P17 AB8 ASN A 231 ? SER A 235 ? ASN A 240 SER A 244 5 ? 5  
HELX_P HELX_P18 AB9 SER A 254 ? GLN A 257 ? SER A 263 GLN A 266 5 ? 4  
HELX_P HELX_P19 AC1 SER A 258 ? LEU A 268 ? SER A 267 LEU A 277 1 ? 11 
HELX_P HELX_P20 AC2 GLY A 277 ? ARG A 287 ? GLY A 286 ARG A 296 1 ? 11 
HELX_P HELX_P21 AC3 ARG A 288 ? MET A 290 ? ARG A 297 MET A 299 5 ? 3  
HELX_P HELX_P22 AC4 PRO A 291 ? ASN A 304 ? PRO A 300 ASN A 313 1 ? 14 
HELX_P HELX_P23 AC5 SER A 306 ? GLY A 315 ? SER A 315 GLY A 324 1 ? 10 
HELX_P HELX_P24 AC6 ASP A 316 ? ILE A 345 ? ASP A 325 ILE A 354 1 ? 30 
HELX_P HELX_P25 AC7 ILE A 345 ? GLN A 352 ? ILE A 354 GLN A 361 1 ? 8  
HELX_P HELX_P26 AC8 GLY A 372 ? LYS A 388 ? GLY A 381 LYS A 397 1 ? 17 
HELX_P HELX_P27 AC9 SER B 3   ? HIS B 7   ? SER B 12  HIS B 16  5 ? 5  
HELX_P HELX_P28 AD1 PRO B 24  ? PHE B 26  ? PRO B 33  PHE B 35  5 ? 3  
HELX_P HELX_P29 AD2 TYR B 27  ? HIS B 36  ? TYR B 36  HIS B 45  1 ? 10 
HELX_P HELX_P30 AD3 HIS B 36  ? SER B 43  ? HIS B 45  SER B 52  1 ? 8  
HELX_P HELX_P31 AD4 GLN B 45  ? LEU B 53  ? GLN B 54  LEU B 62  1 ? 9  
HELX_P HELX_P32 AD5 ASP B 63  ? GLY B 84  ? ASP B 72  GLY B 93  1 ? 22 
HELX_P HELX_P33 AD6 PRO B 95  ? LEU B 109 ? PRO B 104 LEU B 118 1 ? 15 
HELX_P HELX_P34 AD7 VAL B 116 ? VAL B 121 ? VAL B 125 VAL B 130 1 ? 6  
HELX_P HELX_P35 AD8 THR B 135 ? GLU B 137 ? THR B 144 GLU B 146 5 ? 3  
HELX_P HELX_P36 AD9 CYS B 150 ? SER B 167 ? CYS B 159 SER B 176 1 ? 18 
HELX_P HELX_P37 AE1 ALA B 168 ? LYS B 170 ? ALA B 177 LYS B 179 5 ? 3  
HELX_P HELX_P38 AE2 VAL B 171 ? MET B 181 ? VAL B 180 MET B 190 1 ? 11 
HELX_P HELX_P39 AE3 GLU B 183 ? HIS B 206 ? GLU B 192 HIS B 215 1 ? 24 
HELX_P HELX_P40 AE4 GLN B 207 ? VAL B 212 ? GLN B 216 VAL B 221 1 ? 6  
HELX_P HELX_P41 AE5 ASN B 213 ? VAL B 220 ? ASN B 222 VAL B 229 1 ? 8  
HELX_P HELX_P42 AE6 VAL B 220 ? SER B 226 ? VAL B 229 SER B 235 1 ? 7  
HELX_P HELX_P43 AE7 ASN B 231 ? SER B 235 ? ASN B 240 SER B 244 5 ? 5  
HELX_P HELX_P44 AE8 SER B 254 ? GLN B 257 ? SER B 263 GLN B 266 5 ? 4  
HELX_P HELX_P45 AE9 SER B 258 ? LEU B 268 ? SER B 267 LEU B 277 1 ? 11 
HELX_P HELX_P46 AF1 GLY B 277 ? ARG B 287 ? GLY B 286 ARG B 296 1 ? 11 
HELX_P HELX_P47 AF2 ARG B 288 ? MET B 290 ? ARG B 297 MET B 299 5 ? 3  
HELX_P HELX_P48 AF3 PRO B 291 ? SER B 303 ? PRO B 300 SER B 312 1 ? 13 
HELX_P HELX_P49 AF4 SER B 306 ? SER B 313 ? SER B 315 SER B 322 1 ? 8  
HELX_P HELX_P50 AF5 ASP B 316 ? ILE B 345 ? ASP B 325 ILE B 354 1 ? 30 
HELX_P HELX_P51 AF6 ILE B 345 ? GLN B 351 ? ILE B 354 GLN B 360 1 ? 7  
HELX_P HELX_P52 AF7 GLY B 372 ? LYS B 388 ? GLY B 381 LYS B 397 1 ? 17 
# 
_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 
disulf1 disulf ? ? A CYS 299 SG  ? ? ? 1_555 B CYS 299 SG  ? ? A CYS 308 B CYS 308 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc1 metalc ? ? A HIS 337 NE2 ? ? ? 1_555 C HEM .   FE  ? ? A HIS 346 A HEM 501 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 D W2Z .   N28 ? ? A HEM 501 A W2Z 502 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc3 metalc ? ? B HIS 337 NE2 ? ? ? 1_555 E HEM .   FE  ? ? B HIS 346 B HEM 501 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc4 metalc ? ? E HEM .   FE  ? ? ? 1_555 F W2Z .   N28 ? ? B HEM 501 B W2Z 502 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
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  NE2 ? A HIS 337 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NA  ? C HEM . ? A HEM 501 ? 1_555 86.4  ? 
2  NE2 ? A HIS 337 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB  ? C HEM . ? A HEM 501 ? 1_555 96.0  ? 
3  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB  ? C HEM . ? A HEM 501 ? 1_555 91.4  ? 
4  NE2 ? A HIS 337 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC  ? C HEM . ? A HEM 501 ? 1_555 91.5  ? 
5  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC  ? C HEM . ? A HEM 501 ? 1_555 177.2 ? 
6  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC  ? C HEM . ? A HEM 501 ? 1_555 90.7  ? 
7  NE2 ? A HIS 337 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND  ? C HEM . ? A HEM 501 ? 1_555 82.5  ? 
8  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND  ? C HEM . ? A HEM 501 ? 1_555 88.0  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND  ? C HEM . ? A HEM 501 ? 1_555 178.4 ? 
10 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND  ? C HEM . ? A HEM 501 ? 1_555 89.8  ? 
11 NE2 ? A HIS 337 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N28 ? D W2Z . ? A W2Z 502 ? 1_555 174.1 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N28 ? D W2Z . ? A W2Z 502 ? 1_555 89.6  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N28 ? D W2Z . ? A W2Z 502 ? 1_555 88.4  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N28 ? D W2Z . ? A W2Z 502 ? 1_555 92.3  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N28 ? D W2Z . ? A W2Z 502 ? 1_555 93.1  ? 
16 NE2 ? B HIS 337 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NA  ? E HEM . ? B HEM 501 ? 1_555 85.0  ? 
17 NE2 ? B HIS 337 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NB  ? E HEM . ? B HEM 501 ? 1_555 93.6  ? 
18 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NB  ? E HEM . ? B HEM 501 ? 1_555 88.2  ? 
19 NE2 ? B HIS 337 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC  ? E HEM . ? B HEM 501 ? 1_555 93.3  ? 
20 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC  ? E HEM . ? B HEM 501 ? 1_555 178.2 ? 
21 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC  ? E HEM . ? B HEM 501 ? 1_555 91.2  ? 
22 NE2 ? B HIS 337 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND  ? E HEM . ? B HEM 501 ? 1_555 85.3  ? 
23 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND  ? E HEM . ? B HEM 501 ? 1_555 91.3  ? 
24 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND  ? E HEM . ? B HEM 501 ? 1_555 178.8 ? 
25 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND  ? E HEM . ? B HEM 501 ? 1_555 89.3  ? 
26 NE2 ? B HIS 337 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N28 ? F W2Z . ? B W2Z 502 ? 1_555 173.8 ? 
27 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N28 ? F W2Z . ? B W2Z 502 ? 1_555 89.0  ? 
28 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N28 ? F W2Z . ? B W2Z 502 ? 1_555 87.9  ? 
29 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N28 ? F W2Z . ? B W2Z 502 ? 1_555 92.7  ? 
30 ND  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N28 ? F W2Z . ? B W2Z 502 ? 1_555 93.2  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       299 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      299 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        308 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       308 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 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 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? anti-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 VAL A 93  ? LEU A 94  ? VAL A 102 LEU A 103 
AA1 2 VAL A 239 ? TYR A 240 ? VAL A 248 TYR A 249 
AA2 1 LYS A 126 ? LYS A 127 ? LYS A 135 LYS A 136 
AA2 2 MET A 139 ? ASP A 140 ? MET A 148 ASP A 149 
AA3 1 VAL B 93  ? LEU B 94  ? VAL B 102 LEU B 103 
AA3 2 VAL B 239 ? TYR B 240 ? VAL B 248 TYR B 249 
AA4 1 LYS B 126 ? LYS B 127 ? LYS B 135 LYS B 136 
AA4 2 MET B 139 ? ASP B 140 ? MET B 148 ASP B 149 
# 
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 94  ? N LEU A 103 O VAL A 239 ? O VAL A 248 
AA2 1 2 N LYS A 126 ? N LYS A 135 O ASP A 140 ? O ASP A 149 
AA3 1 2 N LEU B 94  ? N LEU B 103 O VAL B 239 ? O VAL B 248 
AA4 1 2 N LYS B 126 ? N LYS B 135 O ASP B 140 ? O ASP B 149 
# 
_pdbx_entry_details.entry_id                   8U5I 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ASN A 27  ? ? 33.77   68.84  
2  1 VAL A 130 ? ? -108.33 -60.13 
3  1 ASN A 133 ? ? -109.18 54.41  
4  1 VAL A 229 ? ? -120.55 -68.37 
5  1 ILE A 354 ? ? -123.82 -58.18 
6  1 ASN B 27  ? A 38.41   68.71  
7  1 ASN B 27  ? B 39.49   68.24  
8  1 ASN B 133 ? ? -103.09 54.19  
9  1 VAL B 229 ? ? -122.47 -66.70 
10 1 ILE B 354 ? ? -121.70 -59.98 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     297 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.132 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 0.490   -0.542  -18.819 -0.1202 ? -0.0203 ? -0.0394 ? 0.0372  ? -0.0036 ? 0.0066  ? 3.5338 ? 
1.2484  ? -1.3593 ? 3.0714 ? -1.4416 ? 4.2486 ? 0.0163  ? -0.3532 ? -0.3028 ? 0.0750  ? -0.2206 ? -0.5275 ? 0.0676  ? 0.6912  ? 
0.2044  ? 
2 'X-RAY DIFFRACTION' ? refined -18.660 -0.485  -12.825 -0.0815 ? -0.0284 ? -0.0115 ? -0.0887 ? -0.0053 ? -0.1056 ? 2.7120 ? 
0.2867  ? -0.9255 ? 1.4236 ? -0.2368 ? 1.6139 ? -0.0144 ? -0.2559 ? -0.0608 ? 0.1948  ? -0.0627 ? 0.0899  ? 0.0335  ? 0.1206  ? 
0.0771  ? 
3 'X-RAY DIFFRACTION' ? refined -30.048 7.477   -20.288 -0.1278 ? 0.0293  ? -0.0223 ? -0.1569 ? -0.0277 ? -0.0778 ? 4.9399 ? 
2.7221  ? -0.5437 ? 6.5890 ? -3.2116 ? 5.0490 ? 0.0322  ? 0.0887  ? 0.2248  ? 0.0637  ? 0.0416  ? 0.4045  ? 0.0646  ? -0.2445 ? 
-0.0739 ? 
4 'X-RAY DIFFRACTION' ? refined -46.526 -22.891 -27.567 -0.1347 ? -0.0021 ? 0.0203  ? -0.1623 ? -0.0385 ? -0.0175 ? 4.1696 ? 
-0.3882 ? 1.3295  ? 2.4189 ? -0.0764 ? 2.1523 ? -0.0784 ? -0.3211 ? 0.1666  ? -0.0120 ? -0.0081 ? 0.2425  ? -0.0540 ? -0.1913 ? 
0.0866  ? 
5 'X-RAY DIFFRACTION' ? refined -27.525 -28.251 -24.020 -0.0897 ? -0.0005 ? 0.0253  ? -0.1342 ? -0.0151 ? -0.1097 ? 3.3114 ? 
-0.8889 ? 1.0015  ? 1.3019 ? -0.1309 ? 1.1047 ? -0.0570 ? -0.1042 ? 0.0793  ? 0.0848  ? -0.0188 ? -0.0563 ? 0.0539  ? 0.0665  ? 
0.0757  ? 
6 'X-RAY DIFFRACTION' ? refined -16.928 -31.000 -35.560 -0.1003 ? 0.0296  ? 0.0837  ? -0.0456 ? -0.0140 ? -0.0962 ? 4.7185 ? 
0.2630  ? 3.0093  ? 2.9007 ? 0.7202  ? 6.8055 ? 0.0419  ? 0.6028  ? -0.0056 ? -0.2665 ? -0.1282 ? -0.2336 ? -0.0277 ? 0.4989  ? 
0.0863  ? 
# 
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 ? ? A 1   ? ? ? A 107 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 108 ? ? ? A 335 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? A 336 ? ? ? A 403 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? B 1   ? ? ? B 107 ? ? ? 
5 'X-RAY DIFFRACTION' 5 ? ? B 108 ? ? ? B 335 ? ? ? 
6 'X-RAY DIFFRACTION' 6 ? ? B 336 ? ? ? B 403 ? ? ? 
# 
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 LYS 363 ? A LYS 354 
2  1 Y 1 A GLU 364 ? A GLU 355 
3  1 Y 1 A ASN 365 ? A ASN 356 
4  1 Y 1 A LYS 366 ? A LYS 357 
5  1 Y 1 A THR 367 ? A THR 358 
6  1 Y 1 A SER 368 ? A SER 359 
7  1 Y 1 A GLU 369 ? A GLU 360 
8  1 Y 1 A ASP 370 ? A ASP 361 
9  1 Y 1 A PRO 371 ? A PRO 362 
10 1 Y 1 A SER 372 ? A SER 363 
11 1 Y 1 A LYS 373 ? A LYS 364 
12 1 Y 1 A LEU 374 ? A LEU 365 
13 1 Y 1 A GLU 375 ? A GLU 366 
14 1 Y 1 A ALA 376 ? A ALA 367 
15 1 Y 1 A LYS 377 ? A LYS 368 
16 1 Y 1 A GLY 378 ? A GLY 369 
17 1 Y 1 A THR 379 ? A THR 370 
18 1 Y 1 A GLU 402 ? A GLU 393 
19 1 Y 1 A GLY 403 ? A GLY 394 
20 1 Y 1 B MET 10  ? B MET 1   
21 1 Y 1 B LYS 363 ? B LYS 354 
22 1 Y 1 B GLU 364 ? B GLU 355 
23 1 Y 1 B ASN 365 ? B ASN 356 
24 1 Y 1 B LYS 366 ? B LYS 357 
25 1 Y 1 B THR 367 ? B THR 358 
26 1 Y 1 B SER 368 ? B SER 359 
27 1 Y 1 B GLU 369 ? B GLU 360 
28 1 Y 1 B ASP 370 ? B ASP 361 
29 1 Y 1 B PRO 371 ? B PRO 362 
30 1 Y 1 B SER 372 ? B SER 363 
31 1 Y 1 B LYS 373 ? B LYS 364 
32 1 Y 1 B LEU 374 ? B LEU 365 
33 1 Y 1 B GLU 375 ? B GLU 366 
34 1 Y 1 B ALA 376 ? B ALA 367 
35 1 Y 1 B LYS 377 ? B LYS 368 
36 1 Y 1 B GLY 378 ? B GLY 369 
37 1 Y 1 B THR 379 ? B THR 370 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
HOH O    O  N N 233 
HOH H1   H  N N 234 
HOH H2   H  N N 235 
ILE N    N  N N 236 
ILE CA   C  N S 237 
ILE C    C  N N 238 
ILE O    O  N N 239 
ILE CB   C  N S 240 
ILE CG1  C  N N 241 
ILE CG2  C  N N 242 
ILE CD1  C  N N 243 
ILE OXT  O  N N 244 
ILE H    H  N N 245 
ILE H2   H  N N 246 
ILE HA   H  N N 247 
ILE HB   H  N N 248 
ILE HG12 H  N N 249 
ILE HG13 H  N N 250 
ILE HG21 H  N N 251 
ILE HG22 H  N N 252 
ILE HG23 H  N N 253 
ILE HD11 H  N N 254 
ILE HD12 H  N N 255 
ILE HD13 H  N N 256 
ILE HXT  H  N N 257 
LEU N    N  N N 258 
LEU CA   C  N S 259 
LEU C    C  N N 260 
LEU O    O  N N 261 
LEU CB   C  N N 262 
LEU CG   C  N N 263 
LEU CD1  C  N N 264 
LEU CD2  C  N N 265 
LEU OXT  O  N N 266 
LEU H    H  N N 267 
LEU H2   H  N N 268 
LEU HA   H  N N 269 
LEU HB2  H  N N 270 
LEU HB3  H  N N 271 
LEU HG   H  N N 272 
LEU HD11 H  N N 273 
LEU HD12 H  N N 274 
LEU HD13 H  N N 275 
LEU HD21 H  N N 276 
LEU HD22 H  N N 277 
LEU HD23 H  N N 278 
LEU HXT  H  N N 279 
LYS N    N  N N 280 
LYS CA   C  N S 281 
LYS C    C  N N 282 
LYS O    O  N N 283 
LYS CB   C  N N 284 
LYS CG   C  N N 285 
LYS CD   C  N N 286 
LYS CE   C  N N 287 
LYS NZ   N  N N 288 
LYS OXT  O  N N 289 
LYS H    H  N N 290 
LYS H2   H  N N 291 
LYS HA   H  N N 292 
LYS HB2  H  N N 293 
LYS HB3  H  N N 294 
LYS HG2  H  N N 295 
LYS HG3  H  N N 296 
LYS HD2  H  N N 297 
LYS HD3  H  N N 298 
LYS HE2  H  N N 299 
LYS HE3  H  N N 300 
LYS HZ1  H  N N 301 
LYS HZ2  H  N N 302 
LYS HZ3  H  N N 303 
LYS HXT  H  N N 304 
MET N    N  N N 305 
MET CA   C  N S 306 
MET C    C  N N 307 
MET O    O  N N 308 
MET CB   C  N N 309 
MET CG   C  N N 310 
MET SD   S  N N 311 
MET CE   C  N N 312 
MET OXT  O  N N 313 
MET H    H  N N 314 
MET H2   H  N N 315 
MET HA   H  N N 316 
MET HB2  H  N N 317 
MET HB3  H  N N 318 
MET HG2  H  N N 319 
MET HG3  H  N N 320 
MET HE1  H  N N 321 
MET HE2  H  N N 322 
MET HE3  H  N N 323 
MET HXT  H  N N 324 
PHE N    N  N N 325 
PHE CA   C  N S 326 
PHE C    C  N N 327 
PHE O    O  N N 328 
PHE CB   C  N N 329 
PHE CG   C  Y N 330 
PHE CD1  C  Y N 331 
PHE CD2  C  Y N 332 
PHE CE1  C  Y N 333 
PHE CE2  C  Y N 334 
PHE CZ   C  Y N 335 
PHE OXT  O  N N 336 
PHE H    H  N N 337 
PHE H2   H  N N 338 
PHE HA   H  N N 339 
PHE HB2  H  N N 340 
PHE HB3  H  N N 341 
PHE HD1  H  N N 342 
PHE HD2  H  N N 343 
PHE HE1  H  N N 344 
PHE HE2  H  N N 345 
PHE HZ   H  N N 346 
PHE HXT  H  N N 347 
PRO N    N  N N 348 
PRO CA   C  N S 349 
PRO C    C  N N 350 
PRO O    O  N N 351 
PRO CB   C  N N 352 
PRO CG   C  N N 353 
PRO CD   C  N N 354 
PRO OXT  O  N N 355 
PRO H    H  N N 356 
PRO HA   H  N N 357 
PRO HB2  H  N N 358 
PRO HB3  H  N N 359 
PRO HG2  H  N N 360 
PRO HG3  H  N N 361 
PRO HD2  H  N N 362 
PRO HD3  H  N N 363 
PRO HXT  H  N N 364 
SER N    N  N N 365 
SER CA   C  N S 366 
SER C    C  N N 367 
SER O    O  N N 368 
SER CB   C  N N 369 
SER OG   O  N N 370 
SER OXT  O  N N 371 
SER H    H  N N 372 
SER H2   H  N N 373 
SER HA   H  N N 374 
SER HB2  H  N N 375 
SER HB3  H  N N 376 
SER HG   H  N N 377 
SER HXT  H  N N 378 
THR N    N  N N 379 
THR CA   C  N S 380 
THR C    C  N N 381 
THR O    O  N N 382 
THR CB   C  N R 383 
THR OG1  O  N N 384 
THR CG2  C  N N 385 
THR OXT  O  N N 386 
THR H    H  N N 387 
THR H2   H  N N 388 
THR HA   H  N N 389 
THR HB   H  N N 390 
THR HG1  H  N N 391 
THR HG21 H  N N 392 
THR HG22 H  N N 393 
THR HG23 H  N N 394 
THR HXT  H  N N 395 
TRP N    N  N N 396 
TRP CA   C  N S 397 
TRP C    C  N N 398 
TRP O    O  N N 399 
TRP CB   C  N N 400 
TRP CG   C  Y N 401 
TRP CD1  C  Y N 402 
TRP CD2  C  Y N 403 
TRP NE1  N  Y N 404 
TRP CE2  C  Y N 405 
TRP CE3  C  Y N 406 
TRP CZ2  C  Y N 407 
TRP CZ3  C  Y N 408 
TRP CH2  C  Y N 409 
TRP OXT  O  N N 410 
TRP H    H  N N 411 
TRP H2   H  N N 412 
TRP HA   H  N N 413 
TRP HB2  H  N N 414 
TRP HB3  H  N N 415 
TRP HD1  H  N N 416 
TRP HE1  H  N N 417 
TRP HE3  H  N N 418 
TRP HZ2  H  N N 419 
TRP HZ3  H  N N 420 
TRP HH2  H  N N 421 
TRP HXT  H  N N 422 
TYR N    N  N N 423 
TYR CA   C  N S 424 
TYR C    C  N N 425 
TYR O    O  N N 426 
TYR CB   C  N N 427 
TYR CG   C  Y N 428 
TYR CD1  C  Y N 429 
TYR CD2  C  Y N 430 
TYR CE1  C  Y N 431 
TYR CE2  C  Y N 432 
TYR CZ   C  Y N 433 
TYR OH   O  N N 434 
TYR OXT  O  N N 435 
TYR H    H  N N 436 
TYR H2   H  N N 437 
TYR HA   H  N N 438 
TYR HB2  H  N N 439 
TYR HB3  H  N N 440 
TYR HD1  H  N N 441 
TYR HD2  H  N N 442 
TYR HE1  H  N N 443 
TYR HE2  H  N N 444 
TYR HH   H  N N 445 
TYR HXT  H  N N 446 
VAL N    N  N N 447 
VAL CA   C  N S 448 
VAL C    C  N N 449 
VAL O    O  N N 450 
VAL CB   C  N N 451 
VAL CG1  C  N N 452 
VAL CG2  C  N N 453 
VAL OXT  O  N N 454 
VAL H    H  N N 455 
VAL H2   H  N N 456 
VAL HA   H  N N 457 
VAL HB   H  N N 458 
VAL HG11 H  N N 459 
VAL HG12 H  N N 460 
VAL HG13 H  N N 461 
VAL HG21 H  N N 462 
VAL HG22 H  N N 463 
VAL HG23 H  N N 464 
VAL HXT  H  N N 465 
W2Z C1   C  N N 466 
W2Z C2   C  N N 467 
W2Z C7   C  N N 468 
W2Z C8   C  N N 469 
W2Z C11  C  N N 470 
W2Z C12  C  N S 471 
W2Z C17  C  N S 472 
W2Z C19  C  Y N 473 
W2Z C21  C  Y N 474 
W2Z C23  C  Y N 475 
W2Z C24  C  Y N 476 
W2Z C27  C  Y N 477 
W2Z C30  C  N N 478 
W2Z C31  C  N N 479 
W2Z S3   S  N N 480 
W2Z O4   O  N N 481 
W2Z O5   O  N N 482 
W2Z N6   N  N N 483 
W2Z C9   C  N N 484 
W2Z C10  C  N N 485 
W2Z C14  C  N R 486 
W2Z O16  O  N N 487 
W2Z C20  C  Y N 488 
W2Z C22  C  Y N 489 
W2Z C25  C  Y N 490 
W2Z N26  N  Y N 491 
W2Z N28  N  Y N 492 
W2Z C29  C  Y N 493 
W2Z H1   H  N N 494 
W2Z H2   H  N N 495 
W2Z H3   H  N N 496 
W2Z H4   H  N N 497 
W2Z H5   H  N N 498 
W2Z H6   H  N N 499 
W2Z H7   H  N N 500 
W2Z H8   H  N N 501 
W2Z H9   H  N N 502 
W2Z H10  H  N N 503 
W2Z H11  H  N N 504 
W2Z H12  H  N N 505 
W2Z H13  H  N N 506 
W2Z H14  H  N N 507 
W2Z H15  H  N N 508 
W2Z H16  H  N N 509 
W2Z H17  H  N N 510 
W2Z H18  H  N N 511 
W2Z H19  H  N N 512 
W2Z H20  H  N N 513 
W2Z H21  H  N N 514 
W2Z H22  H  N N 515 
W2Z H23  H  N N 516 
W2Z H24  H  N N 517 
W2Z H25  H  N N 518 
W2Z H26  H  N N 519 
W2Z H27  H  N N 520 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
ILE N   CA   sing N N 234 
ILE N   H    sing N N 235 
ILE N   H2   sing N N 236 
ILE CA  C    sing N N 237 
ILE CA  CB   sing N N 238 
ILE CA  HA   sing N N 239 
ILE C   O    doub N N 240 
ILE C   OXT  sing N N 241 
ILE CB  CG1  sing N N 242 
ILE CB  CG2  sing N N 243 
ILE CB  HB   sing N N 244 
ILE CG1 CD1  sing N N 245 
ILE CG1 HG12 sing N N 246 
ILE CG1 HG13 sing N N 247 
ILE CG2 HG21 sing N N 248 
ILE CG2 HG22 sing N N 249 
ILE CG2 HG23 sing N N 250 
ILE CD1 HD11 sing N N 251 
ILE CD1 HD12 sing N N 252 
ILE CD1 HD13 sing N N 253 
ILE OXT HXT  sing N N 254 
LEU N   CA   sing N N 255 
LEU N   H    sing N N 256 
LEU N   H2   sing N N 257 
LEU CA  C    sing N N 258 
LEU CA  CB   sing N N 259 
LEU CA  HA   sing N N 260 
LEU C   O    doub N N 261 
LEU C   OXT  sing N N 262 
LEU CB  CG   sing N N 263 
LEU CB  HB2  sing N N 264 
LEU CB  HB3  sing N N 265 
LEU CG  CD1  sing N N 266 
LEU CG  CD2  sing N N 267 
LEU CG  HG   sing N N 268 
LEU CD1 HD11 sing N N 269 
LEU CD1 HD12 sing N N 270 
LEU CD1 HD13 sing N N 271 
LEU CD2 HD21 sing N N 272 
LEU CD2 HD22 sing N N 273 
LEU CD2 HD23 sing N N 274 
LEU OXT HXT  sing N N 275 
LYS N   CA   sing N N 276 
LYS N   H    sing N N 277 
LYS N   H2   sing N N 278 
LYS CA  C    sing N N 279 
LYS CA  CB   sing N N 280 
LYS CA  HA   sing N N 281 
LYS C   O    doub N N 282 
LYS C   OXT  sing N N 283 
LYS CB  CG   sing N N 284 
LYS CB  HB2  sing N N 285 
LYS CB  HB3  sing N N 286 
LYS CG  CD   sing N N 287 
LYS CG  HG2  sing N N 288 
LYS CG  HG3  sing N N 289 
LYS CD  CE   sing N N 290 
LYS CD  HD2  sing N N 291 
LYS CD  HD3  sing N N 292 
LYS CE  NZ   sing N N 293 
LYS CE  HE2  sing N N 294 
LYS CE  HE3  sing N N 295 
LYS NZ  HZ1  sing N N 296 
LYS NZ  HZ2  sing N N 297 
LYS NZ  HZ3  sing N N 298 
LYS OXT HXT  sing N N 299 
MET N   CA   sing N N 300 
MET N   H    sing N N 301 
MET N   H2   sing N N 302 
MET CA  C    sing N N 303 
MET CA  CB   sing N N 304 
MET CA  HA   sing N N 305 
MET C   O    doub N N 306 
MET C   OXT  sing N N 307 
MET CB  CG   sing N N 308 
MET CB  HB2  sing N N 309 
MET CB  HB3  sing N N 310 
MET CG  SD   sing N N 311 
MET CG  HG2  sing N N 312 
MET CG  HG3  sing N N 313 
MET SD  CE   sing N N 314 
MET CE  HE1  sing N N 315 
MET CE  HE2  sing N N 316 
MET CE  HE3  sing N N 317 
MET OXT HXT  sing N N 318 
PHE N   CA   sing N N 319 
PHE N   H    sing N N 320 
PHE N   H2   sing N N 321 
PHE CA  C    sing N N 322 
PHE CA  CB   sing N N 323 
PHE CA  HA   sing N N 324 
PHE C   O    doub N N 325 
PHE C   OXT  sing N N 326 
PHE CB  CG   sing N N 327 
PHE CB  HB2  sing N N 328 
PHE CB  HB3  sing N N 329 
PHE CG  CD1  doub Y N 330 
PHE CG  CD2  sing Y N 331 
PHE CD1 CE1  sing Y N 332 
PHE CD1 HD1  sing N N 333 
PHE CD2 CE2  doub Y N 334 
PHE CD2 HD2  sing N N 335 
PHE CE1 CZ   doub Y N 336 
PHE CE1 HE1  sing N N 337 
PHE CE2 CZ   sing Y N 338 
PHE CE2 HE2  sing N N 339 
PHE CZ  HZ   sing N N 340 
PHE OXT HXT  sing N N 341 
PRO N   CA   sing N N 342 
PRO N   CD   sing N N 343 
PRO N   H    sing N N 344 
PRO CA  C    sing N N 345 
PRO CA  CB   sing N N 346 
PRO CA  HA   sing N N 347 
PRO C   O    doub N N 348 
PRO C   OXT  sing N N 349 
PRO CB  CG   sing N N 350 
PRO CB  HB2  sing N N 351 
PRO CB  HB3  sing N N 352 
PRO CG  CD   sing N N 353 
PRO CG  HG2  sing N N 354 
PRO CG  HG3  sing N N 355 
PRO CD  HD2  sing N N 356 
PRO CD  HD3  sing N N 357 
PRO OXT HXT  sing N N 358 
SER N   CA   sing N N 359 
SER N   H    sing N N 360 
SER N   H2   sing N N 361 
SER CA  C    sing N N 362 
SER CA  CB   sing N N 363 
SER CA  HA   sing N N 364 
SER C   O    doub N N 365 
SER C   OXT  sing N N 366 
SER CB  OG   sing N N 367 
SER CB  HB2  sing N N 368 
SER CB  HB3  sing N N 369 
SER OG  HG   sing N N 370 
SER OXT HXT  sing N N 371 
THR N   CA   sing N N 372 
THR N   H    sing N N 373 
THR N   H2   sing N N 374 
THR CA  C    sing N N 375 
THR CA  CB   sing N N 376 
THR CA  HA   sing N N 377 
THR C   O    doub N N 378 
THR C   OXT  sing N N 379 
THR CB  OG1  sing N N 380 
THR CB  CG2  sing N N 381 
THR CB  HB   sing N N 382 
THR OG1 HG1  sing N N 383 
THR CG2 HG21 sing N N 384 
THR CG2 HG22 sing N N 385 
THR CG2 HG23 sing N N 386 
THR OXT HXT  sing N N 387 
TRP N   CA   sing N N 388 
TRP N   H    sing N N 389 
TRP N   H2   sing N N 390 
TRP CA  C    sing N N 391 
TRP CA  CB   sing N N 392 
TRP CA  HA   sing N N 393 
TRP C   O    doub N N 394 
TRP C   OXT  sing N N 395 
TRP CB  CG   sing N N 396 
TRP CB  HB2  sing N N 397 
TRP CB  HB3  sing N N 398 
TRP CG  CD1  doub Y N 399 
TRP CG  CD2  sing Y N 400 
TRP CD1 NE1  sing Y N 401 
TRP CD1 HD1  sing N N 402 
TRP CD2 CE2  doub Y N 403 
TRP CD2 CE3  sing Y N 404 
TRP NE1 CE2  sing Y N 405 
TRP NE1 HE1  sing N N 406 
TRP CE2 CZ2  sing Y N 407 
TRP CE3 CZ3  doub Y N 408 
TRP CE3 HE3  sing N N 409 
TRP CZ2 CH2  doub Y N 410 
TRP CZ2 HZ2  sing N N 411 
TRP CZ3 CH2  sing Y N 412 
TRP CZ3 HZ3  sing N N 413 
TRP CH2 HH2  sing N N 414 
TRP OXT HXT  sing N N 415 
TYR N   CA   sing N N 416 
TYR N   H    sing N N 417 
TYR N   H2   sing N N 418 
TYR CA  C    sing N N 419 
TYR CA  CB   sing N N 420 
TYR CA  HA   sing N N 421 
TYR C   O    doub N N 422 
TYR C   OXT  sing N N 423 
TYR CB  CG   sing N N 424 
TYR CB  HB2  sing N N 425 
TYR CB  HB3  sing N N 426 
TYR CG  CD1  doub Y N 427 
TYR CG  CD2  sing Y N 428 
TYR CD1 CE1  sing Y N 429 
TYR CD1 HD1  sing N N 430 
TYR CD2 CE2  doub Y N 431 
TYR CD2 HD2  sing N N 432 
TYR CE1 CZ   doub Y N 433 
TYR CE1 HE1  sing N N 434 
TYR CE2 CZ   sing Y N 435 
TYR CE2 HE2  sing N N 436 
TYR CZ  OH   sing N N 437 
TYR OH  HH   sing N N 438 
TYR OXT HXT  sing N N 439 
VAL N   CA   sing N N 440 
VAL N   H    sing N N 441 
VAL N   H2   sing N N 442 
VAL CA  C    sing N N 443 
VAL CA  CB   sing N N 444 
VAL CA  HA   sing N N 445 
VAL C   O    doub N N 446 
VAL C   OXT  sing N N 447 
VAL CB  CG1  sing N N 448 
VAL CB  CG2  sing N N 449 
VAL CB  HB   sing N N 450 
VAL CG1 HG11 sing N N 451 
VAL CG1 HG12 sing N N 452 
VAL CG1 HG13 sing N N 453 
VAL CG2 HG21 sing N N 454 
VAL CG2 HG22 sing N N 455 
VAL CG2 HG23 sing N N 456 
VAL OXT HXT  sing N N 457 
W2Z C2  S3   sing N N 458 
W2Z C2  C1   sing N N 459 
W2Z O4  S3   doub N N 460 
W2Z O5  S3   doub N N 461 
W2Z S3  N6   sing N N 462 
W2Z N6  C31  sing N N 463 
W2Z N6  C7   sing N N 464 
W2Z C31 C30  sing N N 465 
W2Z C7  C8   sing N N 466 
W2Z C8  C9   sing N N 467 
W2Z C30 C9   sing N N 468 
W2Z C9  C14  sing N N 469 
W2Z C9  C10  sing N N 470 
W2Z C14 O16  sing N N 471 
W2Z C14 C12  sing N N 472 
W2Z C10 C11  sing N N 473 
W2Z C12 C11  sing N N 474 
W2Z C12 C17  sing N N 475 
W2Z C17 N26  sing N N 476 
W2Z C17 C19  sing N N 477 
W2Z C20 C19  doub Y N 478 
W2Z C20 C21  sing Y N 479 
W2Z C27 N26  sing Y N 480 
W2Z C27 N28  doub Y N 481 
W2Z N26 C25  sing Y N 482 
W2Z C19 C24  sing Y N 483 
W2Z C21 C22  doub Y N 484 
W2Z N28 C29  sing Y N 485 
W2Z C25 C24  sing N N 486 
W2Z C25 C29  doub Y N 487 
W2Z C24 C23  doub Y N 488 
W2Z C22 C23  sing Y N 489 
W2Z C1  H1   sing N N 490 
W2Z C1  H2   sing N N 491 
W2Z C1  H3   sing N N 492 
W2Z C2  H4   sing N N 493 
W2Z C2  H5   sing N N 494 
W2Z C7  H6   sing N N 495 
W2Z C7  H7   sing N N 496 
W2Z C8  H8   sing N N 497 
W2Z C8  H9   sing N N 498 
W2Z C11 H10  sing N N 499 
W2Z C11 H11  sing N N 500 
W2Z C12 H12  sing N N 501 
W2Z C17 H13  sing N N 502 
W2Z C21 H14  sing N N 503 
W2Z C23 H15  sing N N 504 
W2Z C27 H16  sing N N 505 
W2Z C30 H17  sing N N 506 
W2Z C30 H18  sing N N 507 
W2Z C31 H19  sing N N 508 
W2Z C31 H20  sing N N 509 
W2Z C10 H21  sing N N 510 
W2Z C10 H22  sing N N 511 
W2Z C14 H23  sing N N 512 
W2Z O16 H24  sing N N 513 
W2Z C20 H25  sing N N 514 
W2Z C22 H26  sing N N 515 
W2Z C29 H27  sing N N 516 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'internal model' 
# 
_atom_sites.entry_id                    8U5I 
_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]   0.011784 
_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]   0.011125 
_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]   0.007490 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
# 
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   . MET A 1 1   ? -20.036 -9.839  6.966   1.00 82.35 ? 10  MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? -19.176 -9.293  5.866   1.00 78.77 ? 10  MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? -19.238 -10.144 4.593   1.00 76.30 ? 10  MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? -19.529 -11.343 4.645   1.00 77.36 ? 10  MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? -17.711 -9.170  6.318   1.00 79.59 ? 10  MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? -17.457 -8.075  7.342   1.00 82.98 ? 10  MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? -15.728 -7.964  7.842   0.00 83.13 ? 10  MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? -15.544 -9.454  8.820   0.00 86.60 ? 10  MET A CE  1 
ATOM   9    N  N   . ILE A 1 2   ? -18.961 -9.501  3.457   1.00 72.62 ? 11  ILE A N   1 
ATOM   10   C  CA  . ILE A 1 2   ? -18.760 -10.189 2.175   1.00 69.44 ? 11  ILE A CA  1 
ATOM   11   C  C   . ILE A 1 2   ? -17.424 -10.936 2.222   1.00 69.13 ? 11  ILE A C   1 
ATOM   12   O  O   . ILE A 1 2   ? -16.447 -10.432 2.782   1.00 69.52 ? 11  ILE A O   1 
ATOM   13   C  CB  . ILE A 1 2   ? -18.773 -9.185  0.981   1.00 66.32 ? 11  ILE A CB  1 
ATOM   14   C  CG1 . ILE A 1 2   ? -20.180 -8.597  0.812   1.00 66.72 ? 11  ILE A CG1 1 
ATOM   15   C  CG2 . ILE A 1 2   ? -18.325 -9.858  -0.334  1.00 63.43 ? 11  ILE A CG2 1 
ATOM   16   C  CD1 . ILE A 1 2   ? -20.254 -7.374  -0.081  1.00 64.95 ? 11  ILE A CD1 1 
ATOM   17   N  N   . SER A 1 3   ? -17.392 -12.124 1.618   1.00 68.15 ? 12  SER A N   1 
ATOM   18   C  CA  . SER A 1 3   ? -16.200 -12.978 1.616   1.00 67.77 ? 12  SER A CA  1 
ATOM   19   C  C   . SER A 1 3   ? -15.006 -12.324 0.913   1.00 64.42 ? 12  SER A C   1 
ATOM   20   O  O   . SER A 1 3   ? -15.167 -11.578 -0.059  1.00 60.64 ? 12  SER A O   1 
ATOM   21   C  CB  . SER A 1 3   ? -16.505 -14.331 0.958   1.00 69.80 ? 12  SER A CB  1 
ATOM   22   O  OG  . SER A 1 3   ? -15.353 -15.159 0.919   1.00 73.50 ? 12  SER A OG  1 
ATOM   23   N  N   . LYS A 1 4   ? -13.811 -12.627 1.421   1.00 64.02 ? 13  LYS A N   1 
ATOM   24   C  CA  . LYS A 1 4   ? -12.559 -12.058 0.911   1.00 60.39 ? 13  LYS A CA  1 
ATOM   25   C  C   . LYS A 1 4   ? -12.210 -12.533 -0.500  1.00 55.62 ? 13  LYS A C   1 
ATOM   26   O  O   . LYS A 1 4   ? -11.442 -11.873 -1.191  1.00 54.43 ? 13  LYS A O   1 
ATOM   27   C  CB  . LYS A 1 4   ? -11.396 -12.372 1.871   1.00 63.15 ? 13  LYS A CB  1 
ATOM   28   C  CG  . LYS A 1 4   ? -11.457 -11.580 3.174   0.00 65.62 ? 13  LYS A CG  1 
ATOM   29   C  CD  . LYS A 1 4   ? -10.366 -12.022 4.135   0.00 68.75 ? 13  LYS A CD  1 
ATOM   30   C  CE  . LYS A 1 4   ? -10.453 -11.274 5.456   0.00 71.20 ? 13  LYS A CE  1 
ATOM   31   N  NZ  . LYS A 1 4   ? -9.393  -11.700 6.411   0.00 74.67 ? 13  LYS A NZ  1 
ATOM   32   N  N   . GLU A 1 5   ? -12.771 -13.667 -0.920  1.00 54.45 ? 14  GLU A N   1 
ATOM   33   C  CA  . GLU A 1 5   ? -12.584 -14.185 -2.280  1.00 52.68 ? 14  GLU A CA  1 
ATOM   34   C  C   . GLU A 1 5   ? -13.161 -13.298 -3.397  1.00 49.09 ? 14  GLU A C   1 
ATOM   35   O  O   . GLU A 1 5   ? -12.775 -13.460 -4.560  1.00 47.93 ? 14  GLU A O   1 
ATOM   36   C  CB  . GLU A 1 5   ? -13.192 -15.586 -2.393  1.00 55.76 ? 14  GLU A CB  1 
ATOM   37   C  CG  . GLU A 1 5   ? -14.701 -15.688 -2.373  0.00 55.56 ? 14  GLU A CG  1 
ATOM   38   C  CD  . GLU A 1 5   ? -15.215 -17.095 -2.103  0.00 58.02 ? 14  GLU A CD  1 
ATOM   39   O  OE1 . GLU A 1 5   ? -14.572 -18.070 -2.549  0.00 59.06 ? 14  GLU A OE1 1 
ATOM   40   O  OE2 . GLU A 1 5   ? -16.271 -17.225 -1.449  0.00 59.19 ? 14  GLU A OE2 1 
ATOM   41   N  N   . TYR A 1 6   ? -14.085 -12.391 -3.054  1.00 46.78 ? 15  TYR A N   1 
ATOM   42   C  CA  . TYR A 1 6   ? -14.665 -11.439 -4.020  1.00 44.10 ? 15  TYR A CA  1 
ATOM   43   C  C   . TYR A 1 6   ? -13.899 -10.121 -4.145  1.00 42.28 ? 15  TYR A C   1 
ATOM   44   O  O   . TYR A 1 6   ? -14.261 -9.303  -4.971  1.00 41.28 ? 15  TYR A O   1 
ATOM   45   C  CB  . TYR A 1 6   ? -16.127 -11.138 -3.679  1.00 43.20 ? 15  TYR A CB  1 
ATOM   46   C  CG  . TYR A 1 6   ? -17.020 -12.364 -3.677  1.00 46.62 ? 15  TYR A CG  1 
ATOM   47   C  CD1 . TYR A 1 6   ? -17.197 -13.124 -4.837  1.00 46.46 ? 15  TYR A CD1 1 
ATOM   48   C  CD2 . TYR A 1 6   ? -17.699 -12.757 -2.528  1.00 42.72 ? 15  TYR A CD2 1 
ATOM   49   C  CE1 . TYR A 1 6   ? -18.018 -14.246 -4.845  1.00 45.95 ? 15  TYR A CE1 1 
ATOM   50   C  CE2 . TYR A 1 6   ? -18.522 -13.881 -2.526  1.00 48.45 ? 15  TYR A CE2 1 
ATOM   51   C  CZ  . TYR A 1 6   ? -18.678 -14.617 -3.691  1.00 47.34 ? 15  TYR A CZ  1 
ATOM   52   O  OH  . TYR A 1 6   ? -19.493 -15.722 -3.704  1.00 47.65 ? 15  TYR A OH  1 
ATOM   53   N  N   . HIS A 1 7   ? -12.857 -9.912  -3.338  1.00 44.66 ? 16  HIS A N   1 
ATOM   54   C  CA  . HIS A 1 7   ? -11.980 -8.720  -3.451  1.00 43.45 ? 16  HIS A CA  1 
ATOM   55   C  C   . HIS A 1 7   ? -12.754 -7.391  -3.553  1.00 41.28 ? 16  HIS A C   1 
ATOM   56   O  O   . HIS A 1 7   ? -12.515 -6.557  -4.445  1.00 37.25 ? 16  HIS A O   1 
ATOM   57   C  CB  . HIS A 1 7   ? -10.976 -8.900  -4.601  1.00 42.93 ? 16  HIS A CB  1 
ATOM   58   C  CG  . HIS A 1 7   ? -10.096 -10.097 -4.428  1.00 49.62 ? 16  HIS A CG  1 
ATOM   59   N  ND1 . HIS A 1 7   ? -10.202 -11.220 -5.218  1.00 56.68 ? 16  HIS A ND1 1 
ATOM   60   C  CD2 . HIS A 1 7   ? -9.136  -10.371 -3.513  1.00 55.33 ? 16  HIS A CD2 1 
ATOM   61   C  CE1 . HIS A 1 7   ? -9.325  -12.123 -4.818  1.00 55.90 ? 16  HIS A CE1 1 
ATOM   62   N  NE2 . HIS A 1 7   ? -8.665  -11.633 -3.784  1.00 57.77 ? 16  HIS A NE2 1 
ATOM   63   N  N   . ILE A 1 8   ? -13.695 -7.239  -2.620  1.00 41.66 ? 17  ILE A N   1 
ATOM   64   C  CA  . ILE A 1 8   ? -14.494 -6.037  -2.460  1.00 40.99 ? 17  ILE A CA  1 
ATOM   65   C  C   . ILE A 1 8   ? -13.996 -5.356  -1.193  1.00 41.35 ? 17  ILE A C   1 
ATOM   66   O  O   . ILE A 1 8   ? -14.078 -5.930  -0.112  1.00 43.68 ? 17  ILE A O   1 
ATOM   67   C  CB  . ILE A 1 8   ? -16.000 -6.373  -2.353  1.00 41.41 ? 17  ILE A CB  1 
ATOM   68   C  CG1 . ILE A 1 8   ? -16.519 -6.854  -3.713  1.00 41.18 ? 17  ILE A CG1 1 
ATOM   69   C  CG2 . ILE A 1 8   ? -16.814 -5.143  -1.895  1.00 43.44 ? 17  ILE A CG2 1 
ATOM   70   C  CD1 . ILE A 1 8   ? -17.824 -7.626  -3.662  1.00 41.34 ? 17  ILE A CD1 1 
ATOM   71   N  N   . ASP A 1 9   ? -13.474 -4.141  -1.345  1.00 40.67 ? 18  ASP A N   1 
ATOM   72   C  CA  . ASP A 1 9   ? -12.974 -3.349  -0.227  1.00 42.89 ? 18  ASP A CA  1 
ATOM   73   C  C   . ASP A 1 9   ? -14.109 -2.654  0.539   1.00 43.78 ? 18  ASP A C   1 
ATOM   74   O  O   . ASP A 1 9   ? -15.116 -2.239  -0.041  1.00 42.57 ? 18  ASP A O   1 
ATOM   75   C  CB  . ASP A 1 9   ? -11.978 -2.303  -0.731  1.00 42.27 ? 18  ASP A CB  1 
ATOM   76   C  CG  . ASP A 1 9   ? -11.211 -1.644  0.395   1.00 44.90 ? 18  ASP A CG  1 
ATOM   77   O  OD1 . ASP A 1 9   ? -10.323 -2.309  0.972   1.00 51.81 ? 18  ASP A OD1 1 
ATOM   78   O  OD2 . ASP A 1 9   ? -11.516 -0.477  0.714   1.00 46.64 ? 18  ASP A OD2 1 
ATOM   79   N  N   . GLU A 1 10  ? -13.926 -2.513  1.844   1.00 48.11 ? 19  GLU A N   1 
ATOM   80   C  CA  . GLU A 1 10  ? -14.913 -1.858  2.701   1.00 50.77 ? 19  GLU A CA  1 
ATOM   81   C  C   . GLU A 1 10  ? -15.120 -0.373  2.343   1.00 51.12 ? 19  GLU A C   1 
ATOM   82   O  O   . GLU A 1 10  ? -16.241 0.129   2.435   1.00 52.29 ? 19  GLU A O   1 
ATOM   83   C  CB  . GLU A 1 10  ? -14.507 -1.993  4.170   1.00 54.42 ? 19  GLU A CB  1 
ATOM   84   C  CG  . GLU A 1 10  ? -15.578 -1.559  5.171   0.00 57.40 ? 19  GLU A CG  1 
ATOM   85   C  CD  . GLU A 1 10  ? -15.236 -1.921  6.608   0.00 61.04 ? 19  GLU A CD  1 
ATOM   86   O  OE1 . GLU A 1 10  ? -14.040 -1.894  6.972   0.00 61.87 ? 19  GLU A OE1 1 
ATOM   87   O  OE2 . GLU A 1 10  ? -16.169 -2.226  7.380   0.00 63.11 ? 19  GLU A OE2 1 
ATOM   88   N  N   . GLU A 1 11  ? -14.052 0.308   1.921   1.00 49.58 ? 20  GLU A N   1 
ATOM   89   C  CA  . GLU A 1 11  ? -14.098 1.750   1.646   1.00 49.99 ? 20  GLU A CA  1 
ATOM   90   C  C   . GLU A 1 11  ? -14.318 2.048   0.169   1.00 45.37 ? 20  GLU A C   1 
ATOM   91   O  O   . GLU A 1 11  ? -15.178 2.857   -0.170  1.00 46.69 ? 20  GLU A O   1 
ATOM   92   C  CB  . GLU A 1 11  ? -12.811 2.437   2.113   1.00 52.55 ? 20  GLU A CB  1 
ATOM   93   C  CG  . GLU A 1 11  ? -12.847 3.972   2.019   1.00 54.84 ? 20  GLU A CG  1 
ATOM   94   C  CD  . GLU A 1 11  ? -11.571 4.642   2.524   1.00 57.56 ? 20  GLU A CD  1 
ATOM   95   O  OE1 . GLU A 1 11  ? -10.464 4.148   2.206   1.00 57.18 ? 20  GLU A OE1 1 
ATOM   96   O  OE2 . GLU A 1 11  ? -11.682 5.675   3.225   1.00 62.34 ? 20  GLU A OE2 1 
ATOM   97   N  N   . VAL A 1 12  ? -13.529 1.417   -0.699  1.00 41.84 ? 21  VAL A N   1 
ATOM   98   C  CA  . VAL A 1 12  ? -13.563 1.724   -2.138  1.00 38.71 ? 21  VAL A CA  1 
ATOM   99   C  C   . VAL A 1 12  ? -14.340 0.693   -2.985  1.00 35.57 ? 21  VAL A C   1 
ATOM   100  O  O   . VAL A 1 12  ? -14.468 0.865   -4.193  1.00 33.46 ? 21  VAL A O   1 
ATOM   101  C  CB  . VAL A 1 12  ? -12.133 1.997   -2.698  1.00 36.85 ? 21  VAL A CB  1 
ATOM   102  C  CG1 . VAL A 1 12  ? -11.461 3.122   -1.911  1.00 42.02 ? 21  VAL A CG1 1 
ATOM   103  C  CG2 . VAL A 1 12  ? -11.260 0.748   -2.698  1.00 36.73 ? 21  VAL A CG2 1 
ATOM   104  N  N   . GLY A 1 13  ? -14.864 -0.358  -2.350  1.00 36.81 ? 22  GLY A N   1 
ATOM   105  C  CA  . GLY A 1 13  ? -15.690 -1.360  -3.041  1.00 35.26 ? 22  GLY A CA  1 
ATOM   106  C  C   . GLY A 1 13  ? -14.916 -2.188  -4.042  1.00 33.65 ? 22  GLY A C   1 
ATOM   107  O  O   . GLY A 1 13  ? -13.917 -2.821  -3.689  1.00 33.37 ? 22  GLY A O   1 
ATOM   108  N  N   . PHE A 1 14  ? -15.365 -2.170  -5.297  1.00 32.32 ? 23  PHE A N   1 
ATOM   109  C  CA  . PHE A 1 14  ? -14.664 -2.876  -6.385  1.00 31.28 ? 23  PHE A CA  1 
ATOM   110  C  C   . PHE A 1 14  ? -13.401 -2.163  -6.874  1.00 30.11 ? 23  PHE A C   1 
ATOM   111  O  O   . PHE A 1 14  ? -12.642 -2.732  -7.652  1.00 26.22 ? 23  PHE A O   1 
ATOM   112  C  CB  . PHE A 1 14  ? -15.584 -3.076  -7.591  1.00 31.49 ? 23  PHE A CB  1 
ATOM   113  C  CG  . PHE A 1 14  ? -16.814 -3.870  -7.293  1.00 32.10 ? 23  PHE A CG  1 
ATOM   114  C  CD1 . PHE A 1 14  ? -16.767 -5.251  -7.240  1.00 33.00 ? 23  PHE A CD1 1 
ATOM   115  C  CD2 . PHE A 1 14  ? -18.022 -3.237  -7.088  1.00 32.48 ? 23  PHE A CD2 1 
ATOM   116  C  CE1 . PHE A 1 14  ? -17.910 -5.996  -6.990  1.00 32.87 ? 23  PHE A CE1 1 
ATOM   117  C  CE2 . PHE A 1 14  ? -19.184 -3.970  -6.826  1.00 37.17 ? 23  PHE A CE2 1 
ATOM   118  C  CZ  . PHE A 1 14  ? -19.125 -5.352  -6.780  1.00 32.38 ? 23  PHE A CZ  1 
ATOM   119  N  N   . ALA A 1 15  ? -13.180 -0.925  -6.448  1.00 30.76 ? 24  ALA A N   1 
ATOM   120  C  CA  . ALA A 1 15  ? -11.938 -0.232  -6.769  1.00 31.78 ? 24  ALA A CA  1 
ATOM   121  C  C   . ALA A 1 15  ? -10.735 -0.892  -6.086  1.00 33.77 ? 24  ALA A C   1 
ATOM   122  O  O   . ALA A 1 15  ? -10.853 -1.463  -4.999  1.00 34.30 ? 24  ALA A O   1 
ATOM   123  C  CB  . ALA A 1 15  ? -12.034 1.224   -6.392  1.00 34.78 ? 24  ALA A CB  1 
ATOM   124  N  N   . LEU A 1 16  ? -9.581  -0.838  -6.743  1.00 33.62 ? 25  LEU A N   1 
ATOM   125  C  CA  . LEU A 1 16  ? -8.343  -1.328  -6.143  1.00 34.55 ? 25  LEU A CA  1 
ATOM   126  C  C   . LEU A 1 16  ? -7.918  -0.369  -5.020  1.00 37.20 ? 25  LEU A C   1 
ATOM   127  O  O   . LEU A 1 16  ? -7.661  0.805   -5.294  1.00 38.27 ? 25  LEU A O   1 
ATOM   128  C  CB  . LEU A 1 16  ? -7.239  -1.443  -7.200  1.00 32.59 ? 25  LEU A CB  1 
ATOM   129  C  CG  . LEU A 1 16  ? -5.958  -2.166  -6.767  1.00 34.83 ? 25  LEU A CG  1 
ATOM   130  C  CD1 . LEU A 1 16  ? -6.200  -3.672  -6.505  1.00 34.87 ? 25  LEU A CD1 1 
ATOM   131  C  CD2 . LEU A 1 16  ? -4.902  -1.976  -7.827  1.00 32.64 ? 25  LEU A CD2 1 
ATOM   132  N  N   . PRO A 1 17  ? -7.870  -0.849  -3.749  1.00 39.56 ? 26  PRO A N   1 
ATOM   133  C  CA  . PRO A 1 17  ? -7.421  0.055   -2.691  1.00 41.92 ? 26  PRO A CA  1 
ATOM   134  C  C   . PRO A 1 17  ? -5.949  0.400   -2.867  1.00 42.64 ? 26  PRO A C   1 
ATOM   135  O  O   . PRO A 1 17  ? -5.177  -0.448  -3.327  1.00 39.22 ? 26  PRO A O   1 
ATOM   136  C  CB  . PRO A 1 17  ? -7.648  -0.750  -1.405  1.00 44.89 ? 26  PRO A CB  1 
ATOM   137  C  CG  . PRO A 1 17  ? -7.649  -2.162  -1.833  1.00 44.13 ? 26  PRO A CG  1 
ATOM   138  C  CD  . PRO A 1 17  ? -8.197  -2.187  -3.216  1.00 39.61 ? 26  PRO A CD  1 
ATOM   139  N  N   . ASN A 1 18  ? -5.598  1.645   -2.539  1.00 45.63 ? 27  ASN A N   1 
ATOM   140  C  CA  . ASN A 1 18  ? -4.227  2.169   -2.617  1.00 45.86 ? 27  ASN A CA  1 
ATOM   141  C  C   . ASN A 1 18  ? -3.414  1.573   -3.785  1.00 44.20 ? 27  ASN A C   1 
ATOM   142  O  O   . ASN A 1 18  ? -2.493  0.785   -3.562  1.00 45.18 ? 27  ASN A O   1 
ATOM   143  C  CB  . ASN A 1 18  ? -3.529  1.956   -1.261  1.00 50.20 ? 27  ASN A CB  1 
ATOM   144  C  CG  . ASN A 1 18  ? -2.212  2.723   -1.130  1.00 53.38 ? 27  ASN A CG  1 
ATOM   145  O  OD1 . ASN A 1 18  ? -1.848  3.537   -1.979  1.00 55.77 ? 27  ASN A OD1 1 
ATOM   146  N  ND2 . ASN A 1 18  ? -1.495  2.457   -0.050  1.00 59.74 ? 27  ASN A ND2 1 
ATOM   147  N  N   . PRO A 1 19  ? -3.782  1.919   -5.039  1.00 41.81 ? 28  PRO A N   1 
ATOM   148  C  CA  . PRO A 1 19  ? -3.086  1.354   -6.189  1.00 40.93 ? 28  PRO A CA  1 
ATOM   149  C  C   . PRO A 1 19  ? -1.585  1.603   -6.165  1.00 42.56 ? 28  PRO A C   1 
ATOM   150  O  O   . PRO A 1 19  ? -1.125  2.627   -5.636  1.00 41.41 ? 28  PRO A O   1 
ATOM   151  C  CB  . PRO A 1 19  ? -3.728  2.073   -7.383  1.00 39.93 ? 28  PRO A CB  1 
ATOM   152  C  CG  . PRO A 1 19  ? -5.058  2.482   -6.906  1.00 39.49 ? 28  PRO A CG  1 
ATOM   153  C  CD  . PRO A 1 19  ? -4.877  2.811   -5.460  1.00 39.10 ? 28  PRO A CD  1 
ATOM   154  N  N   . GLN A 1 20  ? -0.839  0.664   -6.730  1.00 42.03 ? 29  GLN A N   1 
ATOM   155  C  CA  . GLN A 1 20  ? 0.608   0.789   -6.823  1.00 45.92 ? 29  GLN A CA  1 
ATOM   156  C  C   . GLN A 1 20  ? 0.930   1.819   -7.892  1.00 44.86 ? 29  GLN A C   1 
ATOM   157  O  O   . GLN A 1 20  ? 0.268   1.868   -8.945  1.00 41.26 ? 29  GLN A O   1 
ATOM   158  C  CB  . GLN A 1 20  ? 1.240   -0.557  -7.162  1.00 47.74 ? 29  GLN A CB  1 
ATOM   159  C  CG  . GLN A 1 20  ? 2.723   -0.646  -6.873  1.00 49.57 ? 29  GLN A CG  1 
ATOM   160  C  CD  . GLN A 1 20  ? 3.240   -2.073  -6.964  1.00 52.41 ? 29  GLN A CD  1 
ATOM   161  O  OE1 . GLN A 1 20  ? 2.679   -2.985  -6.354  1.00 51.73 ? 29  GLN A OE1 1 
ATOM   162  N  NE2 . GLN A 1 20  ? 4.322   -2.272  -7.726  1.00 54.59 ? 29  GLN A NE2 1 
ATOM   163  N  N   . GLU A 1 21  ? 1.940   2.638   -7.615  1.00 46.00 ? 30  GLU A N   1 
ATOM   164  C  CA  . GLU A 1 21  ? 2.312   3.752   -8.487  1.00 49.36 ? 30  GLU A CA  1 
ATOM   165  C  C   . GLU A 1 21  ? 3.555   3.465   -9.346  1.00 49.56 ? 30  GLU A C   1 
ATOM   166  O  O   . GLU A 1 21  ? 3.615   3.874   -10.505 1.00 47.61 ? 30  GLU A O   1 
ATOM   167  C  CB  . GLU A 1 21  ? 2.524   4.994   -7.629  1.00 52.39 ? 30  GLU A CB  1 
ATOM   168  C  CG  . GLU A 1 21  ? 2.406   6.286   -8.398  1.00 54.98 ? 30  GLU A CG  1 
ATOM   169  C  CD  . GLU A 1 21  ? 2.528   7.516   -7.520  1.00 59.16 ? 30  GLU A CD  1 
ATOM   170  O  OE1 . GLU A 1 21  ? 2.882   8.577   -8.077  1.00 69.68 ? 30  GLU A OE1 1 
ATOM   171  O  OE2 . GLU A 1 21  ? 2.271   7.431   -6.290  1.00 57.38 ? 30  GLU A OE2 1 
ATOM   172  N  N   . ASN A 1 22  ? 4.528   2.756   -8.770  1.00 52.37 ? 31  ASN A N   1 
ATOM   173  C  CA  . ASN A 1 22  ? 5.798   2.433   -9.427  1.00 53.19 ? 31  ASN A CA  1 
ATOM   174  C  C   . ASN A 1 22  ? 5.966   0.926   -9.588  1.00 52.14 ? 31  ASN A C   1 
ATOM   175  O  O   . ASN A 1 22  ? 5.621   0.156   -8.684  1.00 51.28 ? 31  ASN A O   1 
ATOM   176  C  CB  . ASN A 1 22  ? 6.960   2.973   -8.594  1.00 58.12 ? 31  ASN A CB  1 
ATOM   177  C  CG  . ASN A 1 22  ? 6.891   4.478   -8.400  1.00 60.81 ? 31  ASN A CG  1 
ATOM   178  O  OD1 . ASN A 1 22  ? 6.713   5.230   -9.359  1.00 64.76 ? 31  ASN A OD1 1 
ATOM   179  N  ND2 . ASN A 1 22  ? 7.032   4.923   -7.158  1.00 67.03 ? 31  ASN A ND2 1 
ATOM   180  N  N   . LEU A 1 23  ? 6.488   0.515   -10.740 1.00 50.54 ? 32  LEU A N   1 
ATOM   181  C  CA  . LEU A 1 23  ? 6.795   -0.892  -11.007 1.00 51.24 ? 32  LEU A CA  1 
ATOM   182  C  C   . LEU A 1 23  ? 8.218   -1.177  -10.556 1.00 54.57 ? 32  LEU A C   1 
ATOM   183  O  O   . LEU A 1 23  ? 8.976   -0.233  -10.294 1.00 56.95 ? 32  LEU A O   1 
ATOM   184  C  CB  . LEU A 1 23  ? 6.642   -1.214  -12.503 1.00 49.29 ? 32  LEU A CB  1 
ATOM   185  C  CG  . LEU A 1 23  ? 5.214   -1.375  -13.025 1.00 46.47 ? 32  LEU A CG  1 
ATOM   186  C  CD1 . LEU A 1 23  ? 5.198   -1.443  -14.541 1.00 44.17 ? 32  LEU A CD1 1 
ATOM   187  C  CD2 . LEU A 1 23  ? 4.546   -2.612  -12.436 1.00 46.85 ? 32  LEU A CD2 1 
ATOM   188  N  N   . PRO A 1 24  ? 8.592   -2.472  -10.442 1.00 55.14 ? 33  PRO A N   1 
ATOM   189  C  CA  . PRO A 1 24  ? 10.008  -2.810  -10.240 1.00 58.95 ? 33  PRO A CA  1 
ATOM   190  C  C   . PRO A 1 24  ? 10.911  -2.234  -11.336 1.00 59.13 ? 33  PRO A C   1 
ATOM   191  O  O   . PRO A 1 24  ? 10.462  -2.083  -12.480 1.00 56.10 ? 33  PRO A O   1 
ATOM   192  C  CB  . PRO A 1 24  ? 10.010  -4.345  -10.277 1.00 60.09 ? 33  PRO A CB  1 
ATOM   193  C  CG  . PRO A 1 24  ? 8.642   -4.731  -9.855  1.00 55.85 ? 33  PRO A CG  1 
ATOM   194  C  CD  . PRO A 1 24  ? 7.746   -3.682  -10.446 1.00 52.87 ? 33  PRO A CD  1 
ATOM   195  N  N   . ASP A 1 25  ? 12.155  -1.903  -10.971 1.00 61.88 ? 34  ASP A N   1 
ATOM   196  C  CA  . ASP A 1 25  ? 13.150  -1.308  -11.889 1.00 63.45 ? 34  ASP A CA  1 
ATOM   197  C  C   . ASP A 1 25  ? 13.266  -2.053  -13.222 1.00 62.38 ? 34  ASP A C   1 
ATOM   198  O  O   . ASP A 1 25  ? 13.474  -1.429  -14.265 1.00 61.12 ? 34  ASP A O   1 
ATOM   199  C  CB  . ASP A 1 25  ? 14.552  -1.257  -11.237 1.00 68.01 ? 34  ASP A CB  1 
ATOM   200  C  CG  . ASP A 1 25  ? 14.653  -0.251  -10.088 1.00 71.45 ? 34  ASP A CG  1 
ATOM   201  O  OD1 . ASP A 1 25  ? 13.679  0.480   -9.815  1.00 72.15 ? 34  ASP A OD1 1 
ATOM   202  O  OD2 . ASP A 1 25  ? 15.729  -0.194  -9.448  1.00 81.02 ? 34  ASP A OD2 1 
ATOM   203  N  N   . PHE A 1 26  ? 13.135  -3.382  -13.172 1.00 63.04 ? 35  PHE A N   1 
ATOM   204  C  CA  . PHE A 1 26  ? 13.109  -4.240  -14.371 1.00 62.13 ? 35  PHE A CA  1 
ATOM   205  C  C   . PHE A 1 26  ? 12.205  -3.695  -15.492 1.00 55.99 ? 35  PHE A C   1 
ATOM   206  O  O   . PHE A 1 26  ? 12.571  -3.756  -16.666 1.00 55.21 ? 35  PHE A O   1 
ATOM   207  C  CB  . PHE A 1 26  ? 12.679  -5.669  -13.994 1.00 63.08 ? 35  PHE A CB  1 
ATOM   208  C  CG  . PHE A 1 26  ? 12.909  -6.683  -15.081 1.00 63.87 ? 35  PHE A CG  1 
ATOM   209  C  CD1 . PHE A 1 26  ? 14.161  -7.275  -15.244 1.00 71.06 ? 35  PHE A CD1 1 
ATOM   210  C  CD2 . PHE A 1 26  ? 11.875  -7.052  -15.941 1.00 61.83 ? 35  PHE A CD2 1 
ATOM   211  C  CE1 . PHE A 1 26  ? 14.383  -8.218  -16.253 1.00 71.64 ? 35  PHE A CE1 1 
ATOM   212  C  CE2 . PHE A 1 26  ? 12.086  -7.990  -16.953 1.00 63.67 ? 35  PHE A CE2 1 
ATOM   213  C  CZ  . PHE A 1 26  ? 13.343  -8.575  -17.110 1.00 67.47 ? 35  PHE A CZ  1 
ATOM   214  N  N   . TYR A 1 27  ? 11.051  -3.143  -15.116 1.00 53.14 ? 36  TYR A N   1 
ATOM   215  C  CA  . TYR A 1 27  ? 10.068  -2.607  -16.071 1.00 49.88 ? 36  TYR A CA  1 
ATOM   216  C  C   . TYR A 1 27  ? 10.151  -1.089  -16.303 1.00 48.68 ? 36  TYR A C   1 
ATOM   217  O  O   . TYR A 1 27  ? 9.182   -0.489  -16.775 1.00 46.37 ? 36  TYR A O   1 
ATOM   218  C  CB  . TYR A 1 27  ? 8.657   -2.992  -15.607 1.00 47.77 ? 36  TYR A CB  1 
ATOM   219  C  CG  . TYR A 1 27  ? 8.500   -4.474  -15.418 1.00 48.41 ? 36  TYR A CG  1 
ATOM   220  C  CD1 . TYR A 1 27  ? 8.255   -5.306  -16.508 1.00 47.27 ? 36  TYR A CD1 1 
ATOM   221  C  CD2 . TYR A 1 27  ? 8.627   -5.055  -14.153 1.00 52.68 ? 36  TYR A CD2 1 
ATOM   222  C  CE1 . TYR A 1 27  ? 8.121   -6.682  -16.346 1.00 50.27 ? 36  TYR A CE1 1 
ATOM   223  C  CE2 . TYR A 1 27  ? 8.498   -6.437  -13.976 1.00 51.08 ? 36  TYR A CE2 1 
ATOM   224  C  CZ  . TYR A 1 27  ? 8.244   -7.241  -15.076 1.00 51.84 ? 36  TYR A CZ  1 
ATOM   225  O  OH  . TYR A 1 27  ? 8.115   -8.591  -14.908 1.00 53.11 ? 36  TYR A OH  1 
ATOM   226  N  N   . ASN A 1 28  ? 11.299  -0.473  -15.996 1.00 52.67 ? 37  ASN A N   1 
ATOM   227  C  CA  . ASN A 1 28  ? 11.506  0.971   -16.219 1.00 53.40 ? 37  ASN A CA  1 
ATOM   228  C  C   . ASN A 1 28  ? 11.197  1.421   -17.645 1.00 50.64 ? 37  ASN A C   1 
ATOM   229  O  O   . ASN A 1 28  ? 10.605  2.484   -17.832 1.00 48.96 ? 37  ASN A O   1 
ATOM   230  C  CB  . ASN A 1 28  ? 12.939  1.413   -15.847 1.00 57.35 ? 37  ASN A CB  1 
ATOM   231  C  CG  . ASN A 1 28  ? 13.130  1.633   -14.346 1.00 64.89 ? 37  ASN A CG  1 
ATOM   232  O  OD1 . ASN A 1 28  ? 12.187  1.949   -13.617 1.00 68.61 ? 37  ASN A OD1 1 
ATOM   233  N  ND2 . ASN A 1 28  ? 14.373  1.478   -13.883 1.00 68.43 ? 37  ASN A ND2 1 
ATOM   234  N  N   . ASP A 1 29  ? 11.581  0.608   -18.632 1.00 51.34 ? 38  ASP A N   1 
ATOM   235  C  CA  . ASP A 1 29  ? 11.308  0.907   -20.052 1.00 50.39 ? 38  ASP A CA  1 
ATOM   236  C  C   . ASP A 1 29  ? 9.817   1.051   -20.367 1.00 46.65 ? 38  ASP A C   1 
ATOM   237  O  O   . ASP A 1 29  ? 9.444   1.883   -21.195 1.00 47.25 ? 38  ASP A O   1 
ATOM   238  C  CB  . ASP A 1 29  ? 11.919  -0.155  -20.979 1.00 51.91 ? 38  ASP A CB  1 
ATOM   239  C  CG  . ASP A 1 29  ? 13.437  -0.182  -20.934 1.00 55.69 ? 38  ASP A CG  1 
ATOM   240  O  OD1 . ASP A 1 29  ? 14.063  0.820   -20.525 1.00 59.20 ? 38  ASP A OD1 1 
ATOM   241  O  OD2 . ASP A 1 29  ? 14.009  -1.220  -21.321 1.00 60.24 ? 38  ASP A OD2 1 
ATOM   242  N  N   . TRP A 1 30  ? 8.977   0.239   -19.724 1.00 45.78 ? 39  TRP A N   1 
ATOM   243  C  CA  . TRP A 1 30  ? 7.516   0.408   -19.815 1.00 41.28 ? 39  TRP A CA  1 
ATOM   244  C  C   . TRP A 1 30  ? 7.083   1.698   -19.142 1.00 38.85 ? 39  TRP A C   1 
ATOM   245  O  O   . TRP A 1 30  ? 6.341   2.482   -19.728 1.00 37.05 ? 39  TRP A O   1 
ATOM   246  C  CB  . TRP A 1 30  ? 6.757   -0.738  -19.148 1.00 40.89 ? 39  TRP A CB  1 
ATOM   247  C  CG  . TRP A 1 30  ? 6.940   -2.090  -19.752 1.00 42.81 ? 39  TRP A CG  1 
ATOM   248  C  CD1 . TRP A 1 30  ? 7.615   -2.405  -20.894 1.00 43.99 ? 39  TRP A CD1 1 
ATOM   249  C  CD2 . TRP A 1 30  ? 6.392   -3.318  -19.257 1.00 42.09 ? 39  TRP A CD2 1 
ATOM   250  N  NE1 . TRP A 1 30  ? 7.536   -3.755  -21.132 1.00 41.36 ? 39  TRP A NE1 1 
ATOM   251  C  CE2 . TRP A 1 30  ? 6.795   -4.342  -20.143 1.00 41.16 ? 39  TRP A CE2 1 
ATOM   252  C  CE3 . TRP A 1 30  ? 5.607   -3.654  -18.142 1.00 41.09 ? 39  TRP A CE3 1 
ATOM   253  C  CZ2 . TRP A 1 30  ? 6.443   -5.683  -19.949 1.00 43.79 ? 39  TRP A CZ2 1 
ATOM   254  C  CZ3 . TRP A 1 30  ? 5.246   -4.986  -17.954 1.00 39.71 ? 39  TRP A CZ3 1 
ATOM   255  C  CH2 . TRP A 1 30  ? 5.671   -5.985  -18.853 1.00 43.57 ? 39  TRP A CH2 1 
ATOM   256  N  N   . MET A 1 31  ? 7.545   1.889   -17.906 1.00 41.20 ? 40  MET A N   1 
ATOM   257  C  CA  . MET A 1 31  ? 7.193   3.051   -17.090 1.00 42.82 ? 40  MET A CA  1 
ATOM   258  C  C   . MET A 1 31  ? 7.545   4.378   -17.746 1.00 43.74 ? 40  MET A C   1 
ATOM   259  O  O   . MET A 1 31  ? 6.723   5.302   -17.719 1.00 42.05 ? 40  MET A O   1 
ATOM   260  C  CB  . MET A 1 31  ? 7.860   2.986   -15.707 1.00 48.09 ? 40  MET A CB  1 
ATOM   261  C  CG  . MET A 1 31  ? 7.169   2.070   -14.696 1.00 52.58 ? 40  MET A CG  1 
ATOM   262  S  SD  . MET A 1 31  ? 5.432   2.430   -14.337 1.00 55.79 ? 40  MET A SD  1 
ATOM   263  C  CE  . MET A 1 31  ? 5.406   4.208   -14.196 1.00 49.16 ? 40  MET A CE  1 
ATOM   264  N  N   . PHE A 1 32  ? 8.743   4.471   -18.333 1.00 44.39 ? 41  PHE A N   1 
ATOM   265  C  CA  . PHE A 1 32  ? 9.168   5.701   -19.022 1.00 45.18 ? 41  PHE A CA  1 
ATOM   266  C  C   . PHE A 1 32  ? 8.163   6.118   -20.086 1.00 42.12 ? 41  PHE A C   1 
ATOM   267  O  O   . PHE A 1 32  ? 7.797   7.288   -20.160 1.00 41.36 ? 41  PHE A O   1 
ATOM   268  C  CB  . PHE A 1 32  ? 10.557  5.579   -19.670 1.00 49.39 ? 41  PHE A CB  1 
ATOM   269  C  CG  . PHE A 1 32  ? 11.029  6.868   -20.322 1.00 50.97 ? 41  PHE A CG  1 
ATOM   270  C  CD1 . PHE A 1 32  ? 10.722  7.151   -21.659 1.00 52.74 ? 41  PHE A CD1 1 
ATOM   271  C  CD2 . PHE A 1 32  ? 11.739  7.816   -19.587 1.00 57.22 ? 41  PHE A CD2 1 
ATOM   272  C  CE1 . PHE A 1 32  ? 11.127  8.348   -22.256 1.00 52.75 ? 41  PHE A CE1 1 
ATOM   273  C  CE2 . PHE A 1 32  ? 12.159  9.017   -20.177 1.00 59.06 ? 41  PHE A CE2 1 
ATOM   274  C  CZ  . PHE A 1 32  ? 11.849  9.282   -21.515 1.00 56.88 ? 41  PHE A CZ  1 
ATOM   275  N  N   . ILE A 1 33  ? 7.722   5.153   -20.891 1.00 40.86 ? 42  ILE A N   1 
ATOM   276  C  CA  . ILE A 1 33  ? 6.792   5.421   -21.989 1.00 38.51 ? 42  ILE A CA  1 
ATOM   277  C  C   . ILE A 1 33  ? 5.419   5.855   -21.452 1.00 36.48 ? 42  ILE A C   1 
ATOM   278  O  O   . ILE A 1 33  ? 4.893   6.891   -21.862 1.00 37.42 ? 42  ILE A O   1 
ATOM   279  C  CB  . ILE A 1 33  ? 6.663   4.202   -22.942 1.00 37.91 ? 42  ILE A CB  1 
ATOM   280  C  CG1 . ILE A 1 33  ? 8.014   3.913   -23.618 1.00 39.37 ? 42  ILE A CG1 1 
ATOM   281  C  CG2 . ILE A 1 33  ? 5.601   4.457   -24.030 1.00 35.41 ? 42  ILE A CG2 1 
ATOM   282  C  CD1 . ILE A 1 33  ? 8.112   2.544   -24.242 1.00 40.34 ? 42  ILE A CD1 1 
ATOM   283  N  N   . ALA A 1 34  ? 4.854   5.070   -20.538 1.00 35.87 ? 43  ALA A N   1 
ATOM   284  C  CA  . ALA A 1 34  ? 3.534   5.376   -19.960 1.00 34.87 ? 43  ALA A CA  1 
ATOM   285  C  C   . ALA A 1 34  ? 3.492   6.720   -19.224 1.00 36.05 ? 43  ALA A C   1 
ATOM   286  O  O   . ALA A 1 34  ? 2.484   7.432   -19.284 1.00 37.18 ? 43  ALA A O   1 
ATOM   287  C  CB  . ALA A 1 34  ? 3.086   4.265   -19.041 1.00 35.55 ? 43  ALA A CB  1 
ATOM   288  N  N   . LYS A 1 35  ? 4.578   7.058   -18.537 1.00 35.90 ? 44  LYS A N   1 
ATOM   289  C  CA  . LYS A 1 35  ? 4.668   8.330   -17.807 1.00 39.45 ? 44  LYS A CA  1 
ATOM   290  C  C   . LYS A 1 35  ? 4.787   9.566   -18.699 1.00 39.06 ? 44  LYS A C   1 
ATOM   291  O  O   . LYS A 1 35  ? 4.468   10.664  -18.259 1.00 37.33 ? 44  LYS A O   1 
ATOM   292  C  CB  . LYS A 1 35  ? 5.831   8.295   -16.812 1.00 40.91 ? 44  LYS A CB  1 
ATOM   293  C  CG  . LYS A 1 35  ? 5.533   7.419   -15.598 1.00 44.12 ? 44  LYS A CG  1 
ATOM   294  C  CD  . LYS A 1 35  ? 6.763   7.239   -14.704 1.00 49.80 ? 44  LYS A CD  1 
ATOM   295  C  CE  . LYS A 1 35  ? 6.416   7.322   -13.215 0.00 49.37 ? 44  LYS A CE  1 
ATOM   296  N  NZ  . LYS A 1 35  ? 7.548   6.882   -12.354 0.00 52.45 ? 44  LYS A NZ  1 
ATOM   297  N  N   . HIS A 1 36  ? 5.254   9.390   -19.936 1.00 40.33 ? 45  HIS A N   1 
ATOM   298  C  CA  . HIS A 1 36  ? 5.478   10.511  -20.861 1.00 40.73 ? 45  HIS A CA  1 
ATOM   299  C  C   . HIS A 1 36  ? 4.654   10.395  -22.152 1.00 38.67 ? 45  HIS A C   1 
ATOM   300  O  O   . HIS A 1 36  ? 5.070   10.879  -23.213 1.00 38.57 ? 45  HIS A O   1 
ATOM   301  C  CB  . HIS A 1 36  ? 6.972   10.615  -21.166 1.00 43.00 ? 45  HIS A CB  1 
ATOM   302  C  CG  . HIS A 1 36  ? 7.822   10.775  -19.943 1.00 49.54 ? 45  HIS A CG  1 
ATOM   303  N  ND1 . HIS A 1 36  ? 8.167   9.716   -19.131 1.00 52.62 ? 45  HIS A ND1 1 
ATOM   304  C  CD2 . HIS A 1 36  ? 8.386   11.872  -19.388 1.00 51.81 ? 45  HIS A CD2 1 
ATOM   305  C  CE1 . HIS A 1 36  ? 8.912   10.153  -18.132 1.00 53.86 ? 45  HIS A CE1 1 
ATOM   306  N  NE2 . HIS A 1 36  ? 9.064   11.457  -18.268 1.00 55.49 ? 45  HIS A NE2 1 
ATOM   307  N  N   . LEU A 1 37  ? 3.469   9.787   -22.058 1.00 36.33 ? 46  LEU A N   1 
ATOM   308  C  CA  . LEU A 1 37  ? 2.616   9.623   -23.229 1.00 34.37 ? 46  LEU A CA  1 
ATOM   309  C  C   . LEU A 1 37  ? 2.265   10.938  -23.929 1.00 35.47 ? 46  LEU A C   1 
ATOM   310  O  O   . LEU A 1 37  ? 2.403   11.017  -25.152 1.00 35.98 ? 46  LEU A O   1 
ATOM   311  C  CB  . LEU A 1 37  ? 1.332   8.847   -22.902 1.00 33.96 ? 46  LEU A CB  1 
ATOM   312  C  CG  . LEU A 1 37  ? 1.418   7.336   -22.737 1.00 31.58 ? 46  LEU A CG  1 
ATOM   313  C  CD1 . LEU A 1 37  ? 0.028   6.799   -22.467 1.00 30.48 ? 46  LEU A CD1 1 
ATOM   314  C  CD2 . LEU A 1 37  ? 2.030   6.628   -23.955 1.00 33.10 ? 46  LEU A CD2 1 
ATOM   315  N  N   . PRO A 1 38  ? 1.814   11.968  -23.172 1.00 34.97 ? 47  PRO A N   1 
ATOM   316  C  CA  . PRO A 1 38  ? 1.456   13.231  -23.826 1.00 35.26 ? 47  PRO A CA  1 
ATOM   317  C  C   . PRO A 1 38  ? 2.527   13.757  -24.785 1.00 36.05 ? 47  PRO A C   1 
ATOM   318  O  O   . PRO A 1 38  ? 2.220   14.032  -25.942 1.00 33.72 ? 47  PRO A O   1 
ATOM   319  C  CB  . PRO A 1 38  ? 1.231   14.185  -22.649 1.00 35.69 ? 47  PRO A CB  1 
ATOM   320  C  CG  . PRO A 1 38  ? 0.779   13.299  -21.553 1.00 37.53 ? 47  PRO A CG  1 
ATOM   321  C  CD  . PRO A 1 38  ? 1.584   12.040  -21.716 1.00 35.49 ? 47  PRO A CD  1 
ATOM   322  N  N   A ASP A 1 39  ? 3.764   13.867  -24.303 0.50 37.94 ? 48  ASP A N   1 
ATOM   323  N  N   B ASP A 1 39  ? 3.761   13.864  -24.288 0.50 37.80 ? 48  ASP A N   1 
ATOM   324  C  CA  A ASP A 1 39  ? 4.883   14.370  -25.115 0.50 39.53 ? 48  ASP A CA  1 
ATOM   325  C  CA  B ASP A 1 39  ? 4.919   14.335  -25.067 0.50 39.10 ? 48  ASP A CA  1 
ATOM   326  C  C   A ASP A 1 39  ? 5.330   13.384  -26.202 0.50 37.63 ? 48  ASP A C   1 
ATOM   327  C  C   B ASP A 1 39  ? 5.285   13.377  -26.201 0.50 37.25 ? 48  ASP A C   1 
ATOM   328  O  O   A ASP A 1 39  ? 5.615   13.802  -27.323 0.50 38.79 ? 48  ASP A O   1 
ATOM   329  O  O   B ASP A 1 39  ? 5.472   13.802  -27.340 0.50 38.20 ? 48  ASP A O   1 
ATOM   330  C  CB  A ASP A 1 39  ? 6.079   14.760  -24.226 0.50 41.72 ? 48  ASP A CB  1 
ATOM   331  C  CB  B ASP A 1 39  ? 6.131   14.534  -24.139 0.50 40.45 ? 48  ASP A CB  1 
ATOM   332  C  CG  A ASP A 1 39  ? 5.837   16.044  -23.421 0.50 46.38 ? 48  ASP A CG  1 
ATOM   333  C  CG  B ASP A 1 39  ? 7.418   14.855  -24.894 0.50 44.44 ? 48  ASP A CG  1 
ATOM   334  O  OD1 A ASP A 1 39  ? 4.731   16.629  -23.482 0.50 47.85 ? 48  ASP A OD1 1 
ATOM   335  O  OD1 B ASP A 1 39  ? 7.403   15.749  -25.768 0.50 44.48 ? 48  ASP A OD1 1 
ATOM   336  O  OD2 A ASP A 1 39  ? 6.771   16.468  -22.708 0.50 53.65 ? 48  ASP A OD2 1 
ATOM   337  O  OD2 B ASP A 1 39  ? 8.446   14.207  -24.602 0.50 46.49 ? 48  ASP A OD2 1 
ATOM   338  N  N   . LEU A 1 40  ? 5.392   12.092  -25.880 1.00 36.20 ? 49  LEU A N   1 
ATOM   339  C  CA  . LEU A 1 40  ? 5.808   11.073  -26.867 1.00 36.06 ? 49  LEU A CA  1 
ATOM   340  C  C   . LEU A 1 40  ? 4.804   10.876  -28.015 1.00 33.84 ? 49  LEU A C   1 
ATOM   341  O  O   . LEU A 1 40  ? 5.209   10.658  -29.161 1.00 33.99 ? 49  LEU A O   1 
ATOM   342  C  CB  . LEU A 1 40  ? 6.087   9.732   -26.189 1.00 35.24 ? 49  LEU A CB  1 
ATOM   343  C  CG  . LEU A 1 40  ? 7.265   9.679   -25.215 1.00 37.20 ? 49  LEU A CG  1 
ATOM   344  C  CD1 . LEU A 1 40  ? 7.213   8.359   -24.431 1.00 39.14 ? 49  LEU A CD1 1 
ATOM   345  C  CD2 . LEU A 1 40  ? 8.591   9.831   -25.931 1.00 40.19 ? 49  LEU A CD2 1 
ATOM   346  N  N   . ILE A 1 41  ? 3.510   10.961  -27.713 1.00 32.15 ? 50  ILE A N   1 
ATOM   347  C  CA  . ILE A 1 41  ? 2.485   10.877  -28.752 1.00 33.69 ? 50  ILE A CA  1 
ATOM   348  C  C   . ILE A 1 41  ? 2.568   12.099  -29.652 1.00 34.70 ? 50  ILE A C   1 
ATOM   349  O  O   . ILE A 1 41  ? 2.636   11.961  -30.867 1.00 37.43 ? 50  ILE A O   1 
ATOM   350  C  CB  . ILE A 1 41  ? 1.054   10.757  -28.178 1.00 33.59 ? 50  ILE A CB  1 
ATOM   351  C  CG1 . ILE A 1 41  ? 0.862   9.392   -27.512 1.00 31.75 ? 50  ILE A CG1 1 
ATOM   352  C  CG2 . ILE A 1 41  ? 0.009   10.933  -29.295 1.00 31.04 ? 50  ILE A CG2 1 
ATOM   353  C  CD1 . ILE A 1 41  ? -0.349  9.326   -26.612 1.00 30.61 ? 50  ILE A CD1 1 
ATOM   354  N  N   . GLU A 1 42  ? 2.559   13.280  -29.037 1.00 36.74 ? 51  GLU A N   1 
ATOM   355  C  CA  . GLU A 1 42  ? 2.545   14.554  -29.759 1.00 37.11 ? 51  GLU A CA  1 
ATOM   356  C  C   . GLU A 1 42  ? 3.717   14.661  -30.726 1.00 38.79 ? 51  GLU A C   1 
ATOM   357  O  O   . GLU A 1 42  ? 3.538   15.037  -31.885 1.00 38.63 ? 51  GLU A O   1 
ATOM   358  C  CB  . GLU A 1 42  ? 2.566   15.732  -28.767 1.00 37.32 ? 51  GLU A CB  1 
ATOM   359  C  CG  . GLU A 1 42  ? 2.156   17.090  -29.359 1.00 42.43 ? 51  GLU A CG  1 
ATOM   360  C  CD  . GLU A 1 42  ? 3.205   17.731  -30.258 1.00 51.99 ? 51  GLU A CD  1 
ATOM   361  O  OE1 . GLU A 1 42  ? 4.420   17.613  -29.973 1.00 60.56 ? 51  GLU A OE1 1 
ATOM   362  O  OE2 . GLU A 1 42  ? 2.806   18.371  -31.256 1.00 60.92 ? 51  GLU A OE2 1 
ATOM   363  N  N   . SER A 1 43  ? 4.909   14.322  -30.241 1.00 38.25 ? 52  SER A N   1 
ATOM   364  C  CA  . SER A 1 43  ? 6.128   14.400  -31.045 1.00 40.70 ? 52  SER A CA  1 
ATOM   365  C  C   . SER A 1 43  ? 6.318   13.203  -31.996 1.00 39.45 ? 52  SER A C   1 
ATOM   366  O  O   . SER A 1 43  ? 7.321   13.126  -32.673 1.00 39.30 ? 52  SER A O   1 
ATOM   367  C  CB  . SER A 1 43  ? 7.348   14.535  -30.127 1.00 41.01 ? 52  SER A CB  1 
ATOM   368  O  OG  . SER A 1 43  ? 7.451   13.391  -29.306 1.00 40.56 ? 52  SER A OG  1 
ATOM   369  N  N   . GLY A 1 44  ? 5.371   12.271  -32.044 1.00 38.98 ? 53  GLY A N   1 
ATOM   370  C  CA  . GLY A 1 44  ? 5.503   11.091  -32.890 1.00 39.10 ? 53  GLY A CA  1 
ATOM   371  C  C   . GLY A 1 44  ? 6.670   10.193  -32.524 1.00 39.41 ? 53  GLY A C   1 
ATOM   372  O  O   . GLY A 1 44  ? 7.245   9.559   -33.397 1.00 40.40 ? 53  GLY A O   1 
ATOM   373  N  N   . GLN A 1 45  ? 7.021   10.153  -31.237 1.00 40.28 ? 54  GLN A N   1 
ATOM   374  C  CA  . GLN A 1 45  ? 8.071   9.267   -30.723 1.00 41.11 ? 54  GLN A CA  1 
ATOM   375  C  C   . GLN A 1 45  ? 7.515   7.970   -30.156 1.00 39.09 ? 54  GLN A C   1 
ATOM   376  O  O   . GLN A 1 45  ? 8.255   7.003   -30.012 1.00 40.58 ? 54  GLN A O   1 
ATOM   377  C  CB  . GLN A 1 45  ? 8.868   9.952   -29.611 1.00 42.79 ? 54  GLN A CB  1 
ATOM   378  C  CG  . GLN A 1 45  ? 9.695   11.132  -30.054 1.00 45.48 ? 54  GLN A CG  1 
ATOM   379  C  CD  . GLN A 1 45  ? 10.396  11.785  -28.889 1.00 48.95 ? 54  GLN A CD  1 
ATOM   380  O  OE1 . GLN A 1 45  ? 11.318  11.209  -28.314 1.00 55.88 ? 54  GLN A OE1 1 
ATOM   381  N  NE2 . GLN A 1 45  ? 9.953   12.981  -28.517 1.00 48.70 ? 54  GLN A NE2 1 
ATOM   382  N  N   . LEU A 1 46  ? 6.226   7.946   -29.826 1.00 36.62 ? 55  LEU A N   1 
ATOM   383  C  CA  . LEU A 1 46  ? 5.648   6.833   -29.087 1.00 35.77 ? 55  LEU A CA  1 
ATOM   384  C  C   . LEU A 1 46  ? 5.798   5.501   -29.821 1.00 36.74 ? 55  LEU A C   1 
ATOM   385  O  O   . LEU A 1 46  ? 6.259   4.523   -29.241 1.00 37.39 ? 55  LEU A O   1 
ATOM   386  C  CB  . LEU A 1 46  ? 4.168   7.110   -28.774 1.00 35.35 ? 55  LEU A CB  1 
ATOM   387  C  CG  . LEU A 1 46  ? 3.362   6.136   -27.904 1.00 33.11 ? 55  LEU A CG  1 
ATOM   388  C  CD1 . LEU A 1 46  ? 2.845   4.896   -28.665 1.00 36.59 ? 55  LEU A CD1 1 
ATOM   389  C  CD2 . LEU A 1 46  ? 4.143   5.713   -26.677 1.00 33.47 ? 55  LEU A CD2 1 
ATOM   390  N  N   . ARG A 1 47  ? 5.403   5.467   -31.088 1.00 36.74 ? 56  ARG A N   1 
ATOM   391  C  CA  . ARG A 1 47  ? 5.334   4.204   -31.827 1.00 37.60 ? 56  ARG A CA  1 
ATOM   392  C  C   . ARG A 1 47  ? 6.700   3.584   -32.041 1.00 39.52 ? 56  ARG A C   1 
ATOM   393  O  O   . ARG A 1 47  ? 6.849   2.384   -31.845 1.00 38.68 ? 56  ARG A O   1 
ATOM   394  C  CB  . ARG A 1 47  ? 4.604   4.378   -33.159 1.00 37.37 ? 56  ARG A CB  1 
ATOM   395  C  CG  . ARG A 1 47  ? 3.111   4.488   -32.967 1.00 36.48 ? 56  ARG A CG  1 
ATOM   396  C  CD  . ARG A 1 47  ? 2.421   4.982   -34.213 1.00 37.24 ? 56  ARG A CD  1 
ATOM   397  N  NE  . ARG A 1 47  ? 1.002   4.662   -34.197 1.00 34.13 ? 56  ARG A NE  1 
ATOM   398  C  CZ  . ARG A 1 47  ? 0.113   5.073   -35.105 1.00 36.27 ? 56  ARG A CZ  1 
ATOM   399  N  NH1 . ARG A 1 47  ? 0.474   5.829   -36.137 1.00 39.09 ? 56  ARG A NH1 1 
ATOM   400  N  NH2 . ARG A 1 47  ? -1.157  4.711   -34.985 1.00 34.81 ? 56  ARG A NH2 1 
ATOM   401  N  N   . GLU A 1 48  ? 7.687   4.404   -32.418 1.00 41.17 ? 57  GLU A N   1 
ATOM   402  C  CA  . GLU A 1 48  ? 9.058   3.915   -32.592 1.00 44.28 ? 57  GLU A CA  1 
ATOM   403  C  C   . GLU A 1 48  ? 9.632   3.407   -31.260 1.00 44.00 ? 57  GLU A C   1 
ATOM   404  O  O   . GLU A 1 48  ? 10.302  2.373   -31.243 1.00 43.30 ? 57  GLU A O   1 
ATOM   405  C  CB  . GLU A 1 48  ? 9.978   4.975   -33.223 1.00 44.49 ? 57  GLU A CB  1 
ATOM   406  C  CG  . GLU A 1 48  ? 11.393  4.455   -33.486 1.00 50.52 ? 57  GLU A CG  1 
ATOM   407  C  CD  . GLU A 1 48  ? 12.195  5.286   -34.492 1.00 53.76 ? 57  GLU A CD  1 
ATOM   408  O  OE1 . GLU A 1 48  ? 12.108  6.536   -34.480 1.00 61.51 ? 57  GLU A OE1 1 
ATOM   409  O  OE2 . GLU A 1 48  ? 12.932  4.673   -35.285 1.00 57.25 ? 57  GLU A OE2 1 
ATOM   410  N  N   . ARG A 1 49  ? 9.351   4.117   -30.164 1.00 41.66 ? 58  ARG A N   1 
ATOM   411  C  CA  . ARG A 1 49  ? 9.775   3.691   -28.811 1.00 43.37 ? 58  ARG A CA  1 
ATOM   412  C  C   . ARG A 1 49  ? 9.217   2.317   -28.417 1.00 41.87 ? 58  ARG A C   1 
ATOM   413  O  O   . ARG A 1 49  ? 9.954   1.465   -27.926 1.00 42.58 ? 58  ARG A O   1 
ATOM   414  C  CB  . ARG A 1 49  ? 9.355   4.717   -27.751 1.00 42.90 ? 58  ARG A CB  1 
ATOM   415  C  CG  . ARG A 1 49  ? 10.076  6.061   -27.848 1.00 48.40 ? 58  ARG A CG  1 
ATOM   416  C  CD  . ARG A 1 49  ? 11.214  6.197   -26.877 1.00 55.40 ? 58  ARG A CD  1 
ATOM   417  N  NE  . ARG A 1 49  ? 11.639  7.591   -26.736 1.00 56.84 ? 58  ARG A NE  1 
ATOM   418  C  CZ  . ARG A 1 49  ? 12.539  8.025   -25.855 1.00 58.06 ? 58  ARG A CZ  1 
ATOM   419  N  NH1 . ARG A 1 49  ? 13.135  7.182   -25.012 1.00 63.91 ? 58  ARG A NH1 1 
ATOM   420  N  NH2 . ARG A 1 49  ? 12.844  9.318   -25.810 1.00 58.70 ? 58  ARG A NH2 1 
ATOM   421  N  N   . VAL A 1 50  ? 7.918   2.118   -28.630 1.00 38.73 ? 59  VAL A N   1 
ATOM   422  C  CA  . VAL A 1 50  ? 7.278   0.820   -28.385 1.00 38.83 ? 59  VAL A CA  1 
ATOM   423  C  C   . VAL A 1 50  ? 7.873   -0.267  -29.303 1.00 41.13 ? 59  VAL A C   1 
ATOM   424  O  O   . VAL A 1 50  ? 8.116   -1.393  -28.858 1.00 42.10 ? 59  VAL A O   1 
ATOM   425  C  CB  . VAL A 1 50  ? 5.738   0.889   -28.571 1.00 36.32 ? 59  VAL A CB  1 
ATOM   426  C  CG1 . VAL A 1 50  ? 5.090   -0.507  -28.467 1.00 39.41 ? 59  VAL A CG1 1 
ATOM   427  C  CG2 . VAL A 1 50  ? 5.104   1.828   -27.543 1.00 35.79 ? 59  VAL A CG2 1 
ATOM   428  N  N   . GLU A 1 51  ? 8.097   0.078   -30.572 1.00 41.33 ? 60  GLU A N   1 
ATOM   429  C  CA  . GLU A 1 51  ? 8.701   -0.850  -31.543 1.00 44.11 ? 60  GLU A CA  1 
ATOM   430  C  C   . GLU A 1 51  ? 10.151  -1.220  -31.220 1.00 46.61 ? 60  GLU A C   1 
ATOM   431  O  O   . GLU A 1 51  ? 10.607  -2.301  -31.600 1.00 47.91 ? 60  GLU A O   1 
ATOM   432  C  CB  . GLU A 1 51  ? 8.611   -0.281  -32.960 1.00 44.89 ? 60  GLU A CB  1 
ATOM   433  C  CG  . GLU A 1 51  ? 7.187   -0.276  -33.504 1.00 42.92 ? 60  GLU A CG  1 
ATOM   434  C  CD  . GLU A 1 51  ? 6.931   0.778   -34.568 1.00 40.69 ? 60  GLU A CD  1 
ATOM   435  O  OE1 . GLU A 1 51  ? 7.885   1.378   -35.091 1.00 40.96 ? 60  GLU A OE1 1 
ATOM   436  O  OE2 . GLU A 1 51  ? 5.748   1.012   -34.874 1.00 39.13 ? 60  GLU A OE2 1 
ATOM   437  N  N   . LYS A 1 52  ? 10.859  -0.331  -30.522 1.00 47.28 ? 61  LYS A N   1 
ATOM   438  C  CA  . LYS A 1 52  ? 12.251  -0.567  -30.128 1.00 51.46 ? 61  LYS A CA  1 
ATOM   439  C  C   . LYS A 1 52  ? 12.400  -1.225  -28.742 1.00 52.01 ? 61  LYS A C   1 
ATOM   440  O  O   . LYS A 1 52  ? 13.521  -1.541  -28.333 1.00 54.83 ? 61  LYS A O   1 
ATOM   441  C  CB  . LYS A 1 52  ? 13.053  0.743   -30.191 1.00 53.23 ? 61  LYS A CB  1 
ATOM   442  C  CG  . LYS A 1 52  ? 13.123  1.389   -31.582 1.00 53.63 ? 61  LYS A CG  1 
ATOM   443  C  CD  . LYS A 1 52  ? 14.107  0.723   -32.512 1.00 59.20 ? 61  LYS A CD  1 
ATOM   444  C  CE  . LYS A 1 52  ? 14.099  1.419   -33.865 1.00 57.67 ? 61  LYS A CE  1 
ATOM   445  N  NZ  . LYS A 1 52  ? 15.009  0.768   -34.849 1.00 64.92 ? 61  LYS A NZ  1 
ATOM   446  N  N   . LEU A 1 53  ? 11.288  -1.441  -28.032 1.00 49.50 ? 62  LEU A N   1 
ATOM   447  C  CA  . LEU A 1 53  ? 11.299  -2.172  -26.754 1.00 49.67 ? 62  LEU A CA  1 
ATOM   448  C  C   . LEU A 1 53  ? 11.782  -3.611  -26.903 1.00 51.02 ? 62  LEU A C   1 
ATOM   449  O  O   . LEU A 1 53  ? 11.567  -4.244  -27.938 1.00 47.67 ? 62  LEU A O   1 
ATOM   450  C  CB  . LEU A 1 53  ? 9.902   -2.226  -26.120 1.00 47.87 ? 62  LEU A CB  1 
ATOM   451  C  CG  . LEU A 1 53  ? 9.346   -0.985  -25.424 1.00 50.00 ? 62  LEU A CG  1 
ATOM   452  C  CD1 . LEU A 1 53  ? 7.871   -1.164  -25.146 1.00 51.75 ? 62  LEU A CD1 1 
ATOM   453  C  CD2 . LEU A 1 53  ? 10.096  -0.711  -24.131 1.00 54.76 ? 62  LEU A CD2 1 
ATOM   454  N  N   . ASN A 1 54  ? 12.430  -4.108  -25.850 1.00 53.76 ? 63  ASN A N   1 
ATOM   455  C  CA  . ASN A 1 54  ? 12.728  -5.531  -25.705 1.00 56.80 ? 63  ASN A CA  1 
ATOM   456  C  C   . ASN A 1 54  ? 11.555  -6.222  -25.031 1.00 54.34 ? 63  ASN A C   1 
ATOM   457  O  O   . ASN A 1 54  ? 10.890  -5.619  -24.188 1.00 51.55 ? 63  ASN A O   1 
ATOM   458  C  CB  . ASN A 1 54  ? 13.984  -5.734  -24.863 1.00 60.64 ? 63  ASN A CB  1 
ATOM   459  C  CG  . ASN A 1 54  ? 15.235  -5.213  -25.545 1.00 66.72 ? 63  ASN A CG  1 
ATOM   460  O  OD1 . ASN A 1 54  ? 15.397  -5.337  -26.762 1.00 67.04 ? 63  ASN A OD1 1 
ATOM   461  N  ND2 . ASN A 1 54  ? 16.136  -4.638  -24.757 1.00 71.92 ? 63  ASN A ND2 1 
ATOM   462  N  N   . MET A 1 55  ? 11.307  -7.478  -25.404 1.00 56.66 ? 64  MET A N   1 
ATOM   463  C  CA  . MET A 1 55  ? 10.257  -8.286  -24.768 1.00 55.52 ? 64  MET A CA  1 
ATOM   464  C  C   . MET A 1 55  ? 10.676  -8.607  -23.340 1.00 55.17 ? 64  MET A C   1 
ATOM   465  O  O   . MET A 1 55  ? 11.708  -9.248  -23.122 1.00 56.48 ? 64  MET A O   1 
ATOM   466  C  CB  . MET A 1 55  ? 9.995   -9.588  -25.536 1.00 57.78 ? 64  MET A CB  1 
ATOM   467  C  CG  . MET A 1 55  ? 8.684   -10.279 -25.129 1.00 55.81 ? 64  MET A CG  1 
ATOM   468  S  SD  . MET A 1 55  ? 8.450   -11.882 -25.929 1.00 63.11 ? 64  MET A SD  1 
ATOM   469  C  CE  . MET A 1 55  ? 8.227   -11.408 -27.644 1.00 65.49 ? 64  MET A CE  1 
ATOM   470  N  N   . LEU A 1 56  ? 9.885   -8.137  -22.379 1.00 50.63 ? 65  LEU A N   1 
ATOM   471  C  CA  . LEU A 1 56  ? 10.181  -8.327  -20.962 1.00 52.03 ? 65  LEU A CA  1 
ATOM   472  C  C   . LEU A 1 56  ? 9.265   -9.392  -20.363 1.00 50.91 ? 65  LEU A C   1 
ATOM   473  O  O   . LEU A 1 56  ? 8.070   -9.434  -20.656 1.00 48.81 ? 65  LEU A O   1 
ATOM   474  C  CB  . LEU A 1 56  ? 10.049  -7.003  -20.205 1.00 50.08 ? 65  LEU A CB  1 
ATOM   475  C  CG  . LEU A 1 56  ? 11.014  -5.876  -20.603 1.00 50.74 ? 65  LEU A CG  1 
ATOM   476  C  CD1 . LEU A 1 56  ? 10.704  -4.628  -19.788 1.00 52.10 ? 65  LEU A CD1 1 
ATOM   477  C  CD2 . LEU A 1 56  ? 12.484  -6.263  -20.432 1.00 56.98 ? 65  LEU A CD2 1 
ATOM   478  N  N   . SER A 1 57  ? 9.849   -10.263 -19.544 1.00 53.58 ? 66  SER A N   1 
ATOM   479  C  CA  . SER A 1 57  ? 9.111   -11.310 -18.842 1.00 54.70 ? 66  SER A CA  1 
ATOM   480  C  C   . SER A 1 57  ? 8.189   -10.681 -17.799 1.00 53.21 ? 66  SER A C   1 
ATOM   481  O  O   . SER A 1 57  ? 8.575   -9.721  -17.130 1.00 52.65 ? 66  SER A O   1 
ATOM   482  C  CB  . SER A 1 57  ? 10.088  -12.277 -18.156 1.00 58.20 ? 66  SER A CB  1 
ATOM   483  O  OG  . SER A 1 57  ? 9.407   -13.327 -17.495 1.00 57.29 ? 66  SER A OG  1 
ATOM   484  N  N   . ILE A 1 58  ? 6.982   -11.231 -17.663 1.00 52.50 ? 67  ILE A N   1 
ATOM   485  C  CA  . ILE A 1 58  ? 6.019   -10.781 -16.643 1.00 49.68 ? 67  ILE A CA  1 
ATOM   486  C  C   . ILE A 1 58  ? 6.243   -11.406 -15.255 1.00 52.03 ? 67  ILE A C   1 
ATOM   487  O  O   . ILE A 1 58  ? 5.522   -11.082 -14.310 1.00 50.27 ? 67  ILE A O   1 
ATOM   488  C  CB  . ILE A 1 58  ? 4.546   -11.040 -17.082 1.00 47.66 ? 67  ILE A CB  1 
ATOM   489  C  CG1 . ILE A 1 58  ? 4.216   -12.542 -17.186 1.00 48.72 ? 67  ILE A CG1 1 
ATOM   490  C  CG2 . ILE A 1 58  ? 4.259   -10.338 -18.399 1.00 46.05 ? 67  ILE A CG2 1 
ATOM   491  C  CD1 . ILE A 1 58  ? 2.736   -12.838 -17.058 1.00 45.99 ? 67  ILE A CD1 1 
ATOM   492  N  N   . ASP A 1 59  ? 7.234   -12.289 -15.134 1.00 57.01 ? 68  ASP A N   1 
ATOM   493  C  CA  . ASP A 1 59  ? 7.427   -13.087 -13.916 1.00 60.30 ? 68  ASP A CA  1 
ATOM   494  C  C   . ASP A 1 59  ? 7.878   -12.285 -12.694 1.00 61.49 ? 68  ASP A C   1 
ATOM   495  O  O   . ASP A 1 59  ? 7.701   -12.745 -11.563 1.00 63.41 ? 68  ASP A O   1 
ATOM   496  C  CB  . ASP A 1 59  ? 8.423   -14.229 -14.171 1.00 64.90 ? 68  ASP A CB  1 
ATOM   497  C  CG  . ASP A 1 59  ? 7.947   -15.205 -15.242 1.00 65.96 ? 68  ASP A CG  1 
ATOM   498  O  OD1 . ASP A 1 59  ? 6.743   -15.208 -15.591 1.00 63.07 ? 68  ASP A OD1 1 
ATOM   499  O  OD2 . ASP A 1 59  ? 8.791   -15.978 -15.735 1.00 74.56 ? 68  ASP A OD2 1 
ATOM   500  N  N   . HIS A 1 60  ? 8.442   -11.095 -12.920 1.00 60.42 ? 69  HIS A N   1 
ATOM   501  C  CA  . HIS A 1 60  ? 8.878   -10.209 -11.827 1.00 61.65 ? 69  HIS A CA  1 
ATOM   502  C  C   . HIS A 1 60  ? 7.775   -9.240  -11.351 1.00 57.64 ? 69  HIS A C   1 
ATOM   503  O  O   . HIS A 1 60  ? 8.026   -8.372  -10.512 1.00 57.89 ? 69  HIS A O   1 
ATOM   504  C  CB  . HIS A 1 60  ? 10.147  -9.455  -12.232 1.00 62.95 ? 69  HIS A CB  1 
ATOM   505  C  CG  . HIS A 1 60  ? 11.206  -10.342 -12.812 1.00 66.62 ? 69  HIS A CG  1 
ATOM   506  N  ND1 . HIS A 1 60  ? 11.873  -11.290 -12.067 1.00 73.51 ? 69  HIS A ND1 1 
ATOM   507  C  CD2 . HIS A 1 60  ? 11.691  -10.445 -14.072 1.00 66.50 ? 69  HIS A CD2 1 
ATOM   508  C  CE1 . HIS A 1 60  ? 12.734  -11.928 -12.840 1.00 76.78 ? 69  HIS A CE1 1 
ATOM   509  N  NE2 . HIS A 1 60  ? 12.642  -11.435 -14.061 1.00 74.23 ? 69  HIS A NE2 1 
ATOM   510  N  N   . LEU A 1 61  ? 6.563   -9.389  -11.889 1.00 54.91 ? 70  LEU A N   1 
ATOM   511  C  CA  . LEU A 1 61  ? 5.370   -8.750  -11.331 1.00 53.01 ? 70  LEU A CA  1 
ATOM   512  C  C   . LEU A 1 61  ? 4.819   -9.714  -10.281 1.00 54.92 ? 70  LEU A C   1 
ATOM   513  O  O   . LEU A 1 61  ? 3.969   -10.555 -10.575 1.00 56.37 ? 70  LEU A O   1 
ATOM   514  C  CB  . LEU A 1 61  ? 4.344   -8.473  -12.431 1.00 49.32 ? 70  LEU A CB  1 
ATOM   515  C  CG  . LEU A 1 61  ? 4.840   -7.571  -13.565 1.00 46.37 ? 70  LEU A CG  1 
ATOM   516  C  CD1 . LEU A 1 61  ? 3.926   -7.670  -14.769 1.00 45.62 ? 70  LEU A CD1 1 
ATOM   517  C  CD2 . LEU A 1 61  ? 4.957   -6.140  -13.088 1.00 45.38 ? 70  LEU A CD2 1 
ATOM   518  N  N   . THR A 1 62  ? 5.319   -9.591  -9.055  1.00 56.94 ? 71  THR A N   1 
ATOM   519  C  CA  . THR A 1 62  ? 5.184   -10.671 -8.060  1.00 59.47 ? 71  THR A CA  1 
ATOM   520  C  C   . THR A 1 62  ? 3.874   -10.674 -7.270  1.00 56.93 ? 71  THR A C   1 
ATOM   521  O  O   . THR A 1 62  ? 3.569   -11.667 -6.617  1.00 58.77 ? 71  THR A O   1 
ATOM   522  C  CB  . THR A 1 62  ? 6.378   -10.704 -7.065  1.00 63.24 ? 71  THR A CB  1 
ATOM   523  O  OG1 . THR A 1 62  ? 6.360   -9.541  -6.230  1.00 66.72 ? 71  THR A OG1 1 
ATOM   524  C  CG2 . THR A 1 62  ? 7.715   -10.790 -7.809  1.00 65.01 ? 71  THR A CG2 1 
ATOM   525  N  N   . ASP A 1 63  ? 3.112   -9.579  -7.320  1.00 53.03 ? 72  ASP A N   1 
ATOM   526  C  CA  . ASP A 1 63  ? 1.808   -9.507  -6.645  1.00 51.28 ? 72  ASP A CA  1 
ATOM   527  C  C   . ASP A 1 63  ? 0.732   -8.864  -7.511  1.00 46.81 ? 72  ASP A C   1 
ATOM   528  O  O   . ASP A 1 63  ? 1.022   -8.327  -8.583  1.00 45.40 ? 72  ASP A O   1 
ATOM   529  C  CB  . ASP A 1 63  ? 1.922   -8.804  -5.277  1.00 52.74 ? 72  ASP A CB  1 
ATOM   530  C  CG  . ASP A 1 63  ? 2.508   -7.397  -5.358  1.00 52.80 ? 72  ASP A CG  1 
ATOM   531  O  OD1 . ASP A 1 63  ? 2.385   -6.707  -6.395  1.00 44.50 ? 72  ASP A OD1 1 
ATOM   532  O  OD2 . ASP A 1 63  ? 3.091   -6.970  -4.343  1.00 58.95 ? 72  ASP A OD2 1 
ATOM   533  N  N   . HIS A 1 64  ? -0.506  -8.937  -7.023  1.00 46.02 ? 73  HIS A N   1 
ATOM   534  C  CA  . HIS A 1 64  ? -1.686  -8.426  -7.714  1.00 42.78 ? 73  HIS A CA  1 
ATOM   535  C  C   . HIS A 1 64  ? -1.613  -6.938  -8.070  1.00 40.75 ? 73  HIS A C   1 
ATOM   536  O  O   . HIS A 1 64  ? -1.920  -6.567  -9.188  1.00 39.77 ? 73  HIS A O   1 
ATOM   537  C  CB  . HIS A 1 64  ? -2.949  -8.693  -6.881  1.00 40.99 ? 73  HIS A CB  1 
ATOM   538  C  CG  . HIS A 1 64  ? -4.215  -8.262  -7.553  1.00 40.33 ? 73  HIS A CG  1 
ATOM   539  N  ND1 . HIS A 1 64  ? -4.689  -8.859  -8.702  1.00 40.60 ? 73  HIS A ND1 1 
ATOM   540  C  CD2 . HIS A 1 64  ? -5.097  -7.278  -7.249  1.00 39.40 ? 73  HIS A CD2 1 
ATOM   541  C  CE1 . HIS A 1 64  ? -5.815  -8.271  -9.068  1.00 38.13 ? 73  HIS A CE1 1 
ATOM   542  N  NE2 . HIS A 1 64  ? -6.084  -7.310  -8.202  1.00 38.26 ? 73  HIS A NE2 1 
ATOM   543  N  N   . LYS A 1 65  ? -1.227  -6.100  -7.113  1.00 42.87 ? 74  LYS A N   1 
ATOM   544  C  CA  . LYS A 1 65  ? -1.132  -4.656  -7.345  1.00 41.26 ? 74  LYS A CA  1 
ATOM   545  C  C   . LYS A 1 65  ? -0.093  -4.297  -8.411  1.00 41.05 ? 74  LYS A C   1 
ATOM   546  O  O   . LYS A 1 65  ? -0.341  -3.432  -9.253  1.00 39.80 ? 74  LYS A O   1 
ATOM   547  C  CB  . LYS A 1 65  ? -0.829  -3.911  -6.043  1.00 43.16 ? 74  LYS A CB  1 
ATOM   548  C  CG  . LYS A 1 65  ? -2.007  -3.841  -5.075  1.00 42.70 ? 74  LYS A CG  1 
ATOM   549  C  CD  . LYS A 1 65  ? -1.738  -2.818  -3.987  1.00 45.17 ? 74  LYS A CD  1 
ATOM   550  C  CE  . LYS A 1 65  ? -2.905  -2.686  -3.040  1.00 47.49 ? 74  LYS A CE  1 
ATOM   551  N  NZ  . LYS A 1 65  ? -2.716  -1.532  -2.118  1.00 46.12 ? 74  LYS A NZ  1 
ATOM   552  N  N   . SER A 1 66  ? 1.061   -4.960  -8.381  1.00 43.28 ? 75  SER A N   1 
ATOM   553  C  CA  . SER A 1 66  ? 2.074   -4.766  -9.431  1.00 44.24 ? 75  SER A CA  1 
ATOM   554  C  C   . SER A 1 66  ? 1.578   -5.258  -10.806 1.00 41.34 ? 75  SER A C   1 
ATOM   555  O  O   . SER A 1 66  ? 1.870   -4.633  -11.830 1.00 40.15 ? 75  SER A O   1 
ATOM   556  C  CB  . SER A 1 66  ? 3.390   -5.446  -9.058  1.00 46.23 ? 75  SER A CB  1 
ATOM   557  O  OG  . SER A 1 66  ? 3.220   -6.848  -9.006  1.00 54.75 ? 75  SER A OG  1 
ATOM   558  N  N   . GLN A 1 67  ? 0.830   -6.366  -10.817 1.00 39.41 ? 76  GLN A N   1 
ATOM   559  C  CA  . GLN A 1 67  ? 0.221   -6.897  -12.048 1.00 38.19 ? 76  GLN A CA  1 
ATOM   560  C  C   . GLN A 1 67  ? -0.857  -5.965  -12.593 1.00 36.08 ? 76  GLN A C   1 
ATOM   561  O  O   . GLN A 1 67  ? -0.950  -5.751  -13.806 1.00 35.81 ? 76  GLN A O   1 
ATOM   562  C  CB  . GLN A 1 67  ? -0.368  -8.293  -11.809 1.00 39.71 ? 76  GLN A CB  1 
ATOM   563  C  CG  . GLN A 1 67  ? 0.684   -9.374  -11.635 1.00 40.96 ? 76  GLN A CG  1 
ATOM   564  C  CD  . GLN A 1 67  ? 0.151   -10.639 -10.972 1.00 44.27 ? 76  GLN A CD  1 
ATOM   565  O  OE1 . GLN A 1 67  ? -1.025  -10.979 -11.094 1.00 43.92 ? 76  GLN A OE1 1 
ATOM   566  N  NE2 . GLN A 1 67  ? 1.029   -11.345 -10.269 1.00 48.97 ? 76  GLN A NE2 1 
ATOM   567  N  N   . ARG A 1 68  ? -1.661  -5.406  -11.692 1.00 34.29 ? 77  ARG A N   1 
ATOM   568  C  CA  . ARG A 1 68  ? -2.678  -4.429  -12.068 1.00 33.43 ? 77  ARG A CA  1 
ATOM   569  C  C   . ARG A 1 68  ? -2.081  -3.098  -12.540 1.00 33.06 ? 77  ARG A C   1 
ATOM   570  O  O   . ARG A 1 68  ? -2.623  -2.486  -13.456 1.00 30.07 ? 77  ARG A O   1 
ATOM   571  C  CB  . ARG A 1 68  ? -3.661  -4.211  -10.912 1.00 33.95 ? 77  ARG A CB  1 
ATOM   572  C  CG  . ARG A 1 68  ? -4.546  -5.423  -10.642 1.00 33.27 ? 77  ARG A CG  1 
ATOM   573  C  CD  . ARG A 1 68  ? -5.645  -5.582  -11.677 1.00 34.03 ? 77  ARG A CD  1 
ATOM   574  N  NE  . ARG A 1 68  ? -6.541  -4.432  -11.634 1.00 32.57 ? 77  ARG A NE  1 
ATOM   575  C  CZ  . ARG A 1 68  ? -7.490  -4.235  -10.728 1.00 33.52 ? 77  ARG A CZ  1 
ATOM   576  N  NH1 . ARG A 1 68  ? -7.735  -5.122  -9.769  1.00 36.21 ? 77  ARG A NH1 1 
ATOM   577  N  NH2 . ARG A 1 68  ? -8.208  -3.127  -10.800 1.00 31.59 ? 77  ARG A NH2 1 
ATOM   578  N  N   . LEU A 1 69  ? -0.975  -2.659  -11.924 1.00 34.44 ? 78  LEU A N   1 
ATOM   579  C  CA  . LEU A 1 69  ? -0.253  -1.471  -12.404 1.00 34.51 ? 78  LEU A CA  1 
ATOM   580  C  C   . LEU A 1 69  ? 0.280   -1.713  -13.812 1.00 33.82 ? 78  LEU A C   1 
ATOM   581  O  O   . LEU A 1 69  ? 0.079   -0.889  -14.701 1.00 32.46 ? 78  LEU A O   1 
ATOM   582  C  CB  . LEU A 1 69  ? 0.905   -1.076  -11.472 1.00 35.60 ? 78  LEU A CB  1 
ATOM   583  C  CG  . LEU A 1 69  ? 1.771   0.124   -11.919 1.00 37.57 ? 78  LEU A CG  1 
ATOM   584  C  CD1 . LEU A 1 69  ? 0.926   1.364   -12.287 1.00 34.36 ? 78  LEU A CD1 1 
ATOM   585  C  CD2 . LEU A 1 69  ? 2.807   0.485   -10.870 1.00 39.58 ? 78  LEU A CD2 1 
ATOM   586  N  N   . ALA A 1 70  ? 0.955   -2.848  -13.998 1.00 35.84 ? 79  ALA A N   1 
ATOM   587  C  CA  . ALA A 1 70  ? 1.492   -3.240  -15.307 1.00 35.70 ? 79  ALA A CA  1 
ATOM   588  C  C   . ALA A 1 70  ? 0.419   -3.284  -16.398 1.00 33.48 ? 79  ALA A C   1 
ATOM   589  O  O   . ALA A 1 70  ? 0.663   -2.834  -17.524 1.00 33.29 ? 79  ALA A O   1 
ATOM   590  C  CB  . ALA A 1 70  ? 2.211   -4.584  -15.209 1.00 38.25 ? 79  ALA A CB  1 
ATOM   591  N  N   . ARG A 1 71  ? -0.761  -3.809  -16.066 1.00 31.88 ? 80  ARG A N   1 
ATOM   592  C  CA  . ARG A 1 71  ? -1.918  -3.777  -16.988 1.00 30.67 ? 80  ARG A CA  1 
ATOM   593  C  C   . ARG A 1 71  ? -2.329  -2.362  -17.362 1.00 29.38 ? 80  ARG A C   1 
ATOM   594  O  O   . ARG A 1 71  ? -2.674  -2.106  -18.513 1.00 28.93 ? 80  ARG A O   1 
ATOM   595  C  CB  . ARG A 1 71  ? -3.141  -4.480  -16.393 1.00 30.81 ? 80  ARG A CB  1 
ATOM   596  C  CG  . ARG A 1 71  ? -3.382  -5.881  -16.907 1.00 32.42 ? 80  ARG A CG  1 
ATOM   597  C  CD  . ARG A 1 71  ? -4.752  -6.335  -16.501 1.00 31.56 ? 80  ARG A CD  1 
ATOM   598  N  NE  . ARG A 1 71  ? -5.820  -5.683  -17.275 1.00 30.80 ? 80  ARG A NE  1 
ATOM   599  C  CZ  . ARG A 1 71  ? -6.224  -6.061  -18.484 1.00 28.85 ? 80  ARG A CZ  1 
ATOM   600  N  NH1 . ARG A 1 71  ? -5.654  -7.085  -19.110 1.00 33.53 ? 80  ARG A NH1 1 
ATOM   601  N  NH2 . ARG A 1 71  ? -7.208  -5.403  -19.078 1.00 31.00 ? 80  ARG A NH2 1 
ATOM   602  N  N   . LEU A 1 72  ? -2.326  -1.463  -16.380 1.00 31.32 ? 81  LEU A N   1 
ATOM   603  C  CA  . LEU A 1 72  ? -2.645  -0.047  -16.616 1.00 30.53 ? 81  LEU A CA  1 
ATOM   604  C  C   . LEU A 1 72  ? -1.587  0.604   -17.528 1.00 31.84 ? 81  LEU A C   1 
ATOM   605  O  O   . LEU A 1 72  ? -1.923  1.283   -18.501 1.00 30.74 ? 81  LEU A O   1 
ATOM   606  C  CB  . LEU A 1 72  ? -2.780  0.708   -15.287 1.00 30.51 ? 81  LEU A CB  1 
ATOM   607  C  CG  . LEU A 1 72  ? -3.022  2.218   -15.335 1.00 30.80 ? 81  LEU A CG  1 
ATOM   608  C  CD1 . LEU A 1 72  ? -4.239  2.569   -16.169 1.00 28.90 ? 81  LEU A CD1 1 
ATOM   609  C  CD2 . LEU A 1 72  ? -3.169  2.748   -13.929 1.00 34.44 ? 81  LEU A CD2 1 
ATOM   610  N  N   . VAL A 1 73  ? -0.316  0.357   -17.212 1.00 32.23 ? 82  VAL A N   1 
ATOM   611  C  CA  . VAL A 1 73  ? 0.811   0.815   -18.026 1.00 31.28 ? 82  VAL A CA  1 
ATOM   612  C  C   . VAL A 1 73  ? 0.676   0.316   -19.468 1.00 30.02 ? 82  VAL A C   1 
ATOM   613  O  O   . VAL A 1 73  ? 0.590   1.115   -20.406 1.00 27.51 ? 82  VAL A O   1 
ATOM   614  C  CB  . VAL A 1 73  ? 2.163   0.358   -17.389 1.00 33.52 ? 82  VAL A CB  1 
ATOM   615  C  CG1 . VAL A 1 73  ? 3.339   0.519   -18.345 1.00 35.60 ? 82  VAL A CG1 1 
ATOM   616  C  CG2 . VAL A 1 73  ? 2.429   1.154   -16.110 1.00 35.64 ? 82  VAL A CG2 1 
ATOM   617  N  N   . LEU A 1 74  ? 0.625   -1.004  -19.630 1.00 30.42 ? 83  LEU A N   1 
ATOM   618  C  CA  . LEU A 1 74  ? 0.609   -1.626  -20.957 1.00 31.05 ? 83  LEU A CA  1 
ATOM   619  C  C   . LEU A 1 74  ? -0.641  -1.302  -21.774 1.00 29.42 ? 83  LEU A C   1 
ATOM   620  O  O   . LEU A 1 74  ? -0.573  -1.219  -23.003 1.00 31.09 ? 83  LEU A O   1 
ATOM   621  C  CB  . LEU A 1 74  ? 0.792   -3.149  -20.839 1.00 32.85 ? 83  LEU A CB  1 
ATOM   622  C  CG  . LEU A 1 74  ? 2.157   -3.632  -20.320 1.00 32.59 ? 83  LEU A CG  1 
ATOM   623  C  CD1 . LEU A 1 74  ? 2.125   -5.138  -20.119 1.00 37.60 ? 83  LEU A CD1 1 
ATOM   624  C  CD2 . LEU A 1 74  ? 3.275   -3.250  -21.249 1.00 34.99 ? 83  LEU A CD2 1 
ATOM   625  N  N   . GLY A 1 75  ? -1.770  -1.135  -21.090 1.00 28.57 ? 84  GLY A N   1 
ATOM   626  C  CA  . GLY A 1 75  ? -3.030  -0.781  -21.722 1.00 27.40 ? 84  GLY A CA  1 
ATOM   627  C  C   . GLY A 1 75  ? -3.032  0.631   -22.261 1.00 25.68 ? 84  GLY A C   1 
ATOM   628  O  O   . GLY A 1 75  ? -3.530  0.871   -23.352 1.00 28.21 ? 84  GLY A O   1 
ATOM   629  N  N   . CYS A 1 76  ? -2.469  1.561   -21.496 1.00 29.03 ? 85  CYS A N   1 
ATOM   630  C  CA  . CYS A 1 76  ? -2.328  2.950   -21.935 1.00 28.02 ? 85  CYS A CA  1 
ATOM   631  C  C   . CYS A 1 76  ? -1.369  3.064   -23.114 1.00 28.55 ? 85  CYS A C   1 
ATOM   632  O  O   . CYS A 1 76  ? -1.648  3.790   -24.069 1.00 27.93 ? 85  CYS A O   1 
ATOM   633  C  CB  . CYS A 1 76  ? -1.880  3.848   -20.785 1.00 29.35 ? 85  CYS A CB  1 
ATOM   634  S  SG  . CYS A 1 76  ? -3.169  4.107   -19.545 1.00 29.38 ? 85  CYS A SG  1 
ATOM   635  N  N   . ILE A 1 77  ? -0.264  2.321   -23.051 1.00 29.67 ? 86  ILE A N   1 
ATOM   636  C  CA  . ILE A 1 77  ? 0.715   2.291   -24.130 1.00 30.53 ? 86  ILE A CA  1 
ATOM   637  C  C   . ILE A 1 77  ? 0.066   1.709   -25.369 1.00 30.16 ? 86  ILE A C   1 
ATOM   638  O  O   . ILE A 1 77  ? 0.283   2.216   -26.468 1.00 31.39 ? 86  ILE A O   1 
ATOM   639  C  CB  . ILE A 1 77  ? 1.996   1.498   -23.750 1.00 31.58 ? 86  ILE A CB  1 
ATOM   640  C  CG1 . ILE A 1 77  ? 2.776   2.265   -22.679 1.00 35.39 ? 86  ILE A CG1 1 
ATOM   641  C  CG2 . ILE A 1 77  ? 2.904   1.280   -24.985 1.00 31.70 ? 86  ILE A CG2 1 
ATOM   642  C  CD1 . ILE A 1 77  ? 3.900   1.482   -22.003 1.00 38.63 ? 86  ILE A CD1 1 
ATOM   643  N  N   . THR A 1 78  ? -0.730  0.656   -25.185 1.00 29.55 ? 87  THR A N   1 
ATOM   644  C  CA  . THR A 1 78  ? -1.404  -0.008  -26.307 1.00 29.30 ? 87  THR A CA  1 
ATOM   645  C  C   . THR A 1 78  ? -2.385  0.941   -27.032 1.00 28.85 ? 87  THR A C   1 
ATOM   646  O  O   . THR A 1 78  ? -2.395  0.976   -28.269 1.00 28.43 ? 87  THR A O   1 
ATOM   647  C  CB  . THR A 1 78  ? -2.070  -1.339  -25.852 1.00 30.63 ? 87  THR A CB  1 
ATOM   648  O  OG1 . THR A 1 78  ? -1.046  -2.245  -25.411 1.00 25.68 ? 87  THR A OG1 1 
ATOM   649  C  CG2 . THR A 1 78  ? -2.855  -1.997  -26.979 1.00 29.12 ? 87  THR A CG2 1 
ATOM   650  N  N   A MET A 1 79  ? -3.177  1.699   -26.273 0.50 26.22 ? 88  MET A N   1 
ATOM   651  N  N   B MET A 1 79  ? -3.171  1.709   -26.269 0.50 27.13 ? 88  MET A N   1 
ATOM   652  C  CA  A MET A 1 79  ? -4.079  2.693   -26.861 0.50 26.55 ? 88  MET A CA  1 
ATOM   653  C  CA  B MET A 1 79  ? -4.080  2.708   -26.849 0.50 27.90 ? 88  MET A CA  1 
ATOM   654  C  C   A MET A 1 79  ? -3.314  3.784   -27.610 0.50 26.94 ? 88  MET A C   1 
ATOM   655  C  C   B MET A 1 79  ? -3.306  3.773   -27.617 0.50 27.83 ? 88  MET A C   1 
ATOM   656  O  O   A MET A 1 79  ? -3.689  4.152   -28.723 0.50 27.27 ? 88  MET A O   1 
ATOM   657  O  O   B MET A 1 79  ? -3.670  4.117   -28.742 0.50 27.96 ? 88  MET A O   1 
ATOM   658  C  CB  A MET A 1 79  ? -4.993  3.318   -25.794 0.50 24.25 ? 88  MET A CB  1 
ATOM   659  C  CB  B MET A 1 79  ? -4.941  3.402   -25.776 0.50 27.44 ? 88  MET A CB  1 
ATOM   660  C  CG  A MET A 1 79  ? -6.030  2.357   -25.211 0.50 21.48 ? 88  MET A CG  1 
ATOM   661  C  CG  B MET A 1 79  ? -5.899  2.512   -24.974 0.50 28.20 ? 88  MET A CG  1 
ATOM   662  S  SD  A MET A 1 79  ? -7.134  1.649   -26.448 0.50 21.97 ? 88  MET A SD  1 
ATOM   663  S  SD  B MET A 1 79  ? -6.708  1.170   -25.872 0.50 34.11 ? 88  MET A SD  1 
ATOM   664  C  CE  A MET A 1 79  ? -8.533  1.173   -25.446 0.50 14.46 ? 88  MET A CE  1 
ATOM   665  C  CE  B MET A 1 79  ? -5.711  -0.208  -25.308 0.50 31.33 ? 88  MET A CE  1 
ATOM   666  N  N   . ALA A 1 80  ? -2.237  4.276   -27.002 1.00 29.24 ? 89  ALA A N   1 
ATOM   667  C  CA  . ALA A 1 80  ? -1.359  5.273   -27.630 1.00 29.88 ? 89  ALA A CA  1 
ATOM   668  C  C   . ALA A 1 80  ? -0.776  4.754   -28.944 1.00 30.44 ? 89  ALA A C   1 
ATOM   669  O  O   . ALA A 1 80  ? -0.747  5.471   -29.949 1.00 29.82 ? 89  ALA A O   1 
ATOM   670  C  CB  . ALA A 1 80  ? -0.247  5.675   -26.667 1.00 31.98 ? 89  ALA A CB  1 
ATOM   671  N  N   . TYR A 1 81  ? -0.369  3.485   -28.936 1.00 30.84 ? 90  TYR A N   1 
ATOM   672  C  CA  . TYR A 1 81  ? 0.203   2.851   -30.119 1.00 30.85 ? 90  TYR A CA  1 
ATOM   673  C  C   . TYR A 1 81  ? -0.827  2.647   -31.233 1.00 30.30 ? 90  TYR A C   1 
ATOM   674  O  O   . TYR A 1 81  ? -0.533  2.900   -32.388 1.00 29.41 ? 90  TYR A O   1 
ATOM   675  C  CB  . TYR A 1 81  ? 0.855   1.508   -29.770 1.00 32.05 ? 90  TYR A CB  1 
ATOM   676  C  CG  . TYR A 1 81  ? 1.648   0.949   -30.925 1.00 33.60 ? 90  TYR A CG  1 
ATOM   677  C  CD1 . TYR A 1 81  ? 2.974   1.323   -31.128 1.00 36.99 ? 90  TYR A CD1 1 
ATOM   678  C  CD2 . TYR A 1 81  ? 1.061   0.074   -31.839 1.00 33.87 ? 90  TYR A CD2 1 
ATOM   679  C  CE1 . TYR A 1 81  ? 3.714   0.824   -32.212 1.00 36.08 ? 90  TYR A CE1 1 
ATOM   680  C  CE2 . TYR A 1 81  ? 1.783   -0.428  -32.914 1.00 37.57 ? 90  TYR A CE2 1 
ATOM   681  C  CZ  . TYR A 1 81  ? 3.110   -0.047  -33.100 1.00 37.88 ? 90  TYR A CZ  1 
ATOM   682  O  OH  . TYR A 1 81  ? 3.813   -0.550  -34.169 1.00 39.16 ? 90  TYR A OH  1 
ATOM   683  N  N   . VAL A 1 82  ? -2.014  2.153   -30.892 1.00 29.70 ? 91  VAL A N   1 
ATOM   684  C  CA  . VAL A 1 82  ? -3.034  1.884   -31.897 1.00 29.42 ? 91  VAL A CA  1 
ATOM   685  C  C   . VAL A 1 82  ? -3.577  3.183   -32.496 1.00 30.21 ? 91  VAL A C   1 
ATOM   686  O  O   . VAL A 1 82  ? -3.672  3.301   -33.708 1.00 30.50 ? 91  VAL A O   1 
ATOM   687  C  CB  . VAL A 1 82  ? -4.180  1.004   -31.343 1.00 28.88 ? 91  VAL A CB  1 
ATOM   688  C  CG1 . VAL A 1 82  ? -5.312  0.859   -32.375 1.00 29.85 ? 91  VAL A CG1 1 
ATOM   689  C  CG2 . VAL A 1 82  ? -3.645  -0.395  -30.963 1.00 30.00 ? 91  VAL A CG2 1 
ATOM   690  N  N   . TRP A 1 83  ? -3.940  4.137   -31.646 1.00 29.29 ? 92  TRP A N   1 
ATOM   691  C  CA  . TRP A 1 83  ? -4.606  5.369   -32.096 1.00 29.07 ? 92  TRP A CA  1 
ATOM   692  C  C   . TRP A 1 83  ? -3.659  6.484   -32.499 1.00 28.93 ? 92  TRP A C   1 
ATOM   693  O  O   . TRP A 1 83  ? -4.079  7.428   -33.177 1.00 27.64 ? 92  TRP A O   1 
ATOM   694  C  CB  . TRP A 1 83  ? -5.566  5.878   -31.023 1.00 28.12 ? 92  TRP A CB  1 
ATOM   695  C  CG  . TRP A 1 83  ? -6.546  4.847   -30.610 1.00 27.30 ? 92  TRP A CG  1 
ATOM   696  C  CD1 . TRP A 1 83  ? -6.752  4.392   -29.353 1.00 24.69 ? 92  TRP A CD1 1 
ATOM   697  C  CD2 . TRP A 1 83  ? -7.430  4.096   -31.462 1.00 26.26 ? 92  TRP A CD2 1 
ATOM   698  N  NE1 . TRP A 1 83  ? -7.722  3.419   -29.352 1.00 22.95 ? 92  TRP A NE1 1 
ATOM   699  C  CE2 . TRP A 1 83  ? -8.158  3.218   -30.631 1.00 26.81 ? 92  TRP A CE2 1 
ATOM   700  C  CE3 . TRP A 1 83  ? -7.682  4.082   -32.841 1.00 27.70 ? 92  TRP A CE3 1 
ATOM   701  C  CZ2 . TRP A 1 83  ? -9.125  2.332   -31.132 1.00 26.77 ? 92  TRP A CZ2 1 
ATOM   702  C  CZ3 . TRP A 1 83  ? -8.650  3.202   -33.337 1.00 30.48 ? 92  TRP A CZ3 1 
ATOM   703  C  CH2 . TRP A 1 83  ? -9.356  2.343   -32.478 1.00 26.43 ? 92  TRP A CH2 1 
ATOM   704  N  N   . GLY A 1 84  ? -2.399  6.387   -32.078 1.00 29.90 ? 93  GLY A N   1 
ATOM   705  C  CA  . GLY A 1 84  ? -1.373  7.345   -32.480 1.00 31.02 ? 93  GLY A CA  1 
ATOM   706  C  C   . GLY A 1 84  ? -1.702  8.713   -31.918 1.00 31.74 ? 93  GLY A C   1 
ATOM   707  O  O   . GLY A 1 84  ? -2.025  8.839   -30.738 1.00 33.26 ? 93  GLY A O   1 
ATOM   708  N  N   . LYS A 1 85  ? -1.652  9.726   -32.776 1.00 32.51 ? 94  LYS A N   1 
ATOM   709  C  CA  . LYS A 1 85  ? -2.003  11.098  -32.404 1.00 33.73 ? 94  LYS A CA  1 
ATOM   710  C  C   . LYS A 1 85  ? -3.515  11.339  -32.298 1.00 33.36 ? 94  LYS A C   1 
ATOM   711  O  O   . LYS A 1 85  ? -3.934  12.441  -31.937 1.00 31.33 ? 94  LYS A O   1 
ATOM   712  C  CB  . LYS A 1 85  ? -1.386  12.085  -33.390 1.00 34.53 ? 94  LYS A CB  1 
ATOM   713  C  CG  . LYS A 1 85  ? 0.133   12.052  -33.410 1.00 38.16 ? 94  LYS A CG  1 
ATOM   714  C  CD  . LYS A 1 85  ? 0.693   12.988  -34.469 1.00 37.86 ? 94  LYS A CD  1 
ATOM   715  C  CE  . LYS A 1 85  ? 2.210   12.971  -34.460 1.00 40.11 ? 94  LYS A CE  1 
ATOM   716  N  NZ  . LYS A 1 85  ? 2.821   13.957  -35.394 1.00 42.54 ? 94  LYS A NZ  1 
ATOM   717  N  N   . GLY A 1 86  ? -4.322  10.325  -32.620 1.00 33.81 ? 95  GLY A N   1 
ATOM   718  C  CA  . GLY A 1 86  ? -5.771  10.381  -32.449 1.00 35.54 ? 95  GLY A CA  1 
ATOM   719  C  C   . GLY A 1 86  ? -6.481  11.090  -33.582 1.00 38.93 ? 95  GLY A C   1 
ATOM   720  O  O   . GLY A 1 86  ? -7.539  11.689  -33.365 1.00 42.24 ? 95  GLY A O   1 
ATOM   721  N  N   . HIS A 1 87  ? -5.910  11.005  -34.787 1.00 39.94 ? 96  HIS A N   1 
ATOM   722  C  CA  . HIS A 1 87  ? -6.412  11.702  -35.967 1.00 43.21 ? 96  HIS A CA  1 
ATOM   723  C  C   . HIS A 1 87  ? -6.902  10.723  -37.045 1.00 44.47 ? 96  HIS A C   1 
ATOM   724  O  O   . HIS A 1 87  ? -7.071  11.107  -38.196 1.00 47.65 ? 96  HIS A O   1 
ATOM   725  C  CB  . HIS A 1 87  ? -5.312  12.615  -36.530 1.00 46.21 ? 96  HIS A CB  1 
ATOM   726  C  CG  . HIS A 1 87  ? -4.811  13.630  -35.551 1.00 50.03 ? 96  HIS A CG  1 
ATOM   727  N  ND1 . HIS A 1 87  ? -5.644  14.293  -34.673 1.00 54.16 ? 96  HIS A ND1 1 
ATOM   728  C  CD2 . HIS A 1 87  ? -3.564  14.105  -35.315 1.00 53.05 ? 96  HIS A CD2 1 
ATOM   729  C  CE1 . HIS A 1 87  ? -4.931  15.124  -33.934 1.00 53.70 ? 96  HIS A CE1 1 
ATOM   730  N  NE2 . HIS A 1 87  ? -3.666  15.030  -34.304 1.00 51.87 ? 96  HIS A NE2 1 
ATOM   731  N  N   . GLY A 1 88  ? -7.139  9.469   -36.660 1.00 44.28 ? 97  GLY A N   1 
ATOM   732  C  CA  . GLY A 1 88  ? -7.643  8.440   -37.568 1.00 44.94 ? 97  GLY A CA  1 
ATOM   733  C  C   . GLY A 1 88  ? -6.584  7.553   -38.206 1.00 44.51 ? 97  GLY A C   1 
ATOM   734  O  O   . GLY A 1 88  ? -6.920  6.681   -39.005 1.00 44.66 ? 97  GLY A O   1 
ATOM   735  N  N   . ASP A 1 89  ? -5.312  7.769   -37.871 1.00 44.30 ? 98  ASP A N   1 
ATOM   736  C  CA  . ASP A 1 89  ? -4.248  6.897   -38.347 1.00 44.85 ? 98  ASP A CA  1 
ATOM   737  C  C   . ASP A 1 89  ? -4.044  5.777   -37.338 1.00 44.21 ? 98  ASP A C   1 
ATOM   738  O  O   . ASP A 1 89  ? -3.694  6.037   -36.195 1.00 47.92 ? 98  ASP A O   1 
ATOM   739  C  CB  . ASP A 1 89  ? -2.955  7.665   -38.555 1.00 45.61 ? 98  ASP A CB  1 
ATOM   740  C  CG  . ASP A 1 89  ? -1.992  6.915   -39.435 1.00 48.32 ? 98  ASP A CG  1 
ATOM   741  O  OD1 . ASP A 1 89  ? -1.354  5.955   -38.951 1.00 52.61 ? 98  ASP A OD1 1 
ATOM   742  O  OD2 . ASP A 1 89  ? -1.892  7.281   -40.618 1.00 56.62 ? 98  ASP A OD2 1 
ATOM   743  N  N   . VAL A 1 90  ? -4.241  4.540   -37.781 1.00 42.77 ? 99  VAL A N   1 
ATOM   744  C  CA  . VAL A 1 90  ? -4.385  3.395   -36.894 1.00 40.32 ? 99  VAL A CA  1 
ATOM   745  C  C   . VAL A 1 90  ? -3.318  2.334   -37.194 1.00 39.84 ? 99  VAL A C   1 
ATOM   746  O  O   . VAL A 1 90  ? -3.094  1.988   -38.355 1.00 43.22 ? 99  VAL A O   1 
ATOM   747  C  CB  . VAL A 1 90  ? -5.800  2.785   -37.054 1.00 41.57 ? 99  VAL A CB  1 
ATOM   748  C  CG1 . VAL A 1 90  ? -6.015  1.605   -36.119 1.00 43.25 ? 99  VAL A CG1 1 
ATOM   749  C  CG2 . VAL A 1 90  ? -6.877  3.850   -36.798 1.00 42.61 ? 99  VAL A CG2 1 
ATOM   750  N  N   . ARG A 1 91  ? -2.667  1.842   -36.140 1.00 36.83 ? 100 ARG A N   1 
ATOM   751  C  CA  . ARG A 1 91  ? -1.835  0.634   -36.202 1.00 37.43 ? 100 ARG A CA  1 
ATOM   752  C  C   . ARG A 1 91  ? -2.739  -0.594  -36.048 1.00 37.97 ? 100 ARG A C   1 
ATOM   753  O  O   . ARG A 1 91  ? -3.511  -0.677  -35.097 1.00 35.88 ? 100 ARG A O   1 
ATOM   754  C  CB  . ARG A 1 91  ? -0.757  0.641   -35.110 1.00 35.66 ? 100 ARG A CB  1 
ATOM   755  C  CG  . ARG A 1 91  ? 0.470   1.499   -35.448 1.00 41.02 ? 100 ARG A CG  1 
ATOM   756  C  CD  . ARG A 1 91  ? 1.404   0.786   -36.438 1.00 43.45 ? 100 ARG A CD  1 
ATOM   757  N  NE  . ARG A 1 91  ? 2.762   1.337   -36.448 1.00 45.17 ? 100 ARG A NE  1 
ATOM   758  C  CZ  . ARG A 1 91  ? 3.138   2.467   -37.048 1.00 47.11 ? 100 ARG A CZ  1 
ATOM   759  N  NH1 . ARG A 1 91  ? 2.265   3.224   -37.707 1.00 47.61 ? 100 ARG A NH1 1 
ATOM   760  N  NH2 . ARG A 1 91  ? 4.414   2.852   -36.986 1.00 46.22 ? 100 ARG A NH2 1 
ATOM   761  N  N   . LYS A 1 92  ? -2.646  -1.525  -36.998 1.00 40.25 ? 101 LYS A N   1 
ATOM   762  C  CA  . LYS A 1 92  ? -3.451  -2.755  -37.006 1.00 42.55 ? 101 LYS A CA  1 
ATOM   763  C  C   . LYS A 1 92  ? -2.735  -3.965  -36.366 1.00 44.40 ? 101 LYS A C   1 
ATOM   764  O  O   . LYS A 1 92  ? -3.362  -5.013  -36.126 1.00 44.29 ? 101 LYS A O   1 
ATOM   765  C  CB  . LYS A 1 92  ? -3.861  -3.092  -38.438 1.00 45.31 ? 101 LYS A CB  1 
ATOM   766  C  CG  . LYS A 1 92  ? -4.812  -2.068  -39.055 1.00 47.96 ? 101 LYS A CG  1 
ATOM   767  C  CD  . LYS A 1 92  ? -5.393  -2.561  -40.375 1.00 50.92 ? 101 LYS A CD  1 
ATOM   768  C  CE  . LYS A 1 92  ? -6.725  -1.931  -40.723 0.00 51.07 ? 101 LYS A CE  1 
ATOM   769  N  NZ  . LYS A 1 92  ? -7.290  -2.451  -41.999 0.00 54.67 ? 101 LYS A NZ  1 
ATOM   770  N  N   . VAL A 1 93  ? -1.438  -3.811  -36.090 1.00 43.70 ? 102 VAL A N   1 
ATOM   771  C  CA  . VAL A 1 93  ? -0.616  -4.852  -35.479 1.00 43.14 ? 102 VAL A CA  1 
ATOM   772  C  C   . VAL A 1 93  ? 0.093   -4.259  -34.268 1.00 39.94 ? 102 VAL A C   1 
ATOM   773  O  O   . VAL A 1 93  ? 0.759   -3.233  -34.379 1.00 39.23 ? 102 VAL A O   1 
ATOM   774  C  CB  . VAL A 1 93  ? 0.438   -5.391  -36.475 1.00 46.28 ? 102 VAL A CB  1 
ATOM   775  C  CG1 . VAL A 1 93  ? 1.336   -6.454  -35.818 1.00 48.92 ? 102 VAL A CG1 1 
ATOM   776  C  CG2 . VAL A 1 93  ? -0.238  -5.975  -37.724 1.00 48.36 ? 102 VAL A CG2 1 
ATOM   777  N  N   . LEU A 1 94  ? -0.047  -4.916  -33.124 1.00 38.13 ? 103 LEU A N   1 
ATOM   778  C  CA  . LEU A 1 94  ? 0.658   -4.536  -31.904 1.00 37.87 ? 103 LEU A CA  1 
ATOM   779  C  C   . LEU A 1 94  ? 1.923   -5.397  -31.827 1.00 39.82 ? 103 LEU A C   1 
ATOM   780  O  O   . LEU A 1 94  ? 1.817   -6.627  -31.788 1.00 40.16 ? 103 LEU A O   1 
ATOM   781  C  CB  . LEU A 1 94  ? -0.248  -4.781  -30.693 1.00 36.57 ? 103 LEU A CB  1 
ATOM   782  C  CG  . LEU A 1 94  ? 0.240   -4.334  -29.317 1.00 33.53 ? 103 LEU A CG  1 
ATOM   783  C  CD1 . LEU A 1 94  ? 0.340   -2.808  -29.229 1.00 29.65 ? 103 LEU A CD1 1 
ATOM   784  C  CD2 . LEU A 1 94  ? -0.676  -4.880  -28.238 1.00 33.62 ? 103 LEU A CD2 1 
ATOM   785  N  N   . PRO A 1 95  ? 3.120   -4.768  -31.821 1.00 41.86 ? 104 PRO A N   1 
ATOM   786  C  CA  . PRO A 1 95  ? 4.357   -5.560  -31.967 1.00 45.57 ? 104 PRO A CA  1 
ATOM   787  C  C   . PRO A 1 95  ? 4.613   -6.506  -30.786 1.00 46.03 ? 104 PRO A C   1 
ATOM   788  O  O   . PRO A 1 95  ? 4.270   -6.183  -29.645 1.00 41.37 ? 104 PRO A O   1 
ATOM   789  C  CB  . PRO A 1 95  ? 5.462   -4.498  -32.099 1.00 45.31 ? 104 PRO A CB  1 
ATOM   790  C  CG  . PRO A 1 95  ? 4.886   -3.247  -31.572 1.00 43.89 ? 104 PRO A CG  1 
ATOM   791  C  CD  . PRO A 1 95  ? 3.398   -3.327  -31.677 1.00 40.37 ? 104 PRO A CD  1 
ATOM   792  N  N   . ARG A 1 96  ? 5.205   -7.662  -31.085 1.00 49.90 ? 105 ARG A N   1 
ATOM   793  C  CA  . ARG A 1 96  ? 5.304   -8.778  -30.134 1.00 51.88 ? 105 ARG A CA  1 
ATOM   794  C  C   . ARG A 1 96  ? 5.946   -8.443  -28.778 1.00 51.66 ? 105 ARG A C   1 
ATOM   795  O  O   . ARG A 1 96  ? 5.520   -8.982  -27.750 1.00 50.22 ? 105 ARG A O   1 
ATOM   796  C  CB  . ARG A 1 96  ? 6.019   -9.977  -30.781 1.00 56.95 ? 105 ARG A CB  1 
ATOM   797  C  CG  . ARG A 1 96  ? 7.517   -9.774  -31.022 1.00 61.52 ? 105 ARG A CG  1 
ATOM   798  C  CD  . ARG A 1 96  ? 8.159   -10.930 -31.774 1.00 64.91 ? 105 ARG A CD  1 
ATOM   799  N  NE  . ARG A 1 96  ? 7.938   -10.819 -33.217 1.00 68.20 ? 105 ARG A NE  1 
ATOM   800  C  CZ  . ARG A 1 96  ? 7.133   -11.585 -33.964 1.00 73.88 ? 105 ARG A CZ  1 
ATOM   801  N  NH1 . ARG A 1 96  ? 6.418   -12.593 -33.448 1.00 74.13 ? 105 ARG A NH1 1 
ATOM   802  N  NH2 . ARG A 1 96  ? 7.047   -11.340 -35.273 1.00 76.08 ? 105 ARG A NH2 1 
ATOM   803  N  N   A ASN A 1 97  ? 6.943   -7.560  -28.773 0.50 51.47 ? 106 ASN A N   1 
ATOM   804  N  N   B ASN A 1 97  ? 6.952   -7.560  -28.805 0.50 51.91 ? 106 ASN A N   1 
ATOM   805  C  CA  A ASN A 1 97  ? 7.661   -7.221  -27.537 0.50 51.08 ? 106 ASN A CA  1 
ATOM   806  C  CA  B ASN A 1 97  ? 7.669   -7.104  -27.597 0.50 51.62 ? 106 ASN A CA  1 
ATOM   807  C  C   A ASN A 1 97  ? 6.797   -6.513  -26.477 0.50 49.11 ? 106 ASN A C   1 
ATOM   808  C  C   B ASN A 1 97  ? 6.758   -6.578  -26.489 0.50 49.53 ? 106 ASN A C   1 
ATOM   809  O  O   A ASN A 1 97  ? 7.149   -6.522  -25.299 0.50 49.66 ? 106 ASN A O   1 
ATOM   810  O  O   B ASN A 1 97  ? 7.028   -6.783  -25.304 0.50 50.24 ? 106 ASN A O   1 
ATOM   811  C  CB  A ASN A 1 97  ? 8.947   -6.430  -27.847 0.50 52.29 ? 106 ASN A CB  1 
ATOM   812  C  CB  B ASN A 1 97  ? 8.768   -6.065  -27.935 0.50 52.62 ? 106 ASN A CB  1 
ATOM   813  C  CG  A ASN A 1 97  ? 10.026  -7.290  -28.527 0.50 54.36 ? 106 ASN A CG  1 
ATOM   814  C  CG  B ASN A 1 97  ? 8.241   -4.813  -28.665 0.50 50.20 ? 106 ASN A CG  1 
ATOM   815  O  OD1 A ASN A 1 97  ? 9.769   -8.413  -28.964 0.50 51.13 ? 106 ASN A OD1 1 
ATOM   816  O  OD1 B ASN A 1 97  ? 7.052   -4.494  -28.640 0.50 45.22 ? 106 ASN A OD1 1 
ATOM   817  N  ND2 A ASN A 1 97  ? 11.238  -6.758  -28.612 0.50 55.72 ? 106 ASN A ND2 1 
ATOM   818  N  ND2 B ASN A 1 97  ? 9.153   -4.101  -29.324 0.50 49.46 ? 106 ASN A ND2 1 
ATOM   819  N  N   . ILE A 1 98  ? 5.676   -5.918  -26.895 1.00 47.44 ? 107 ILE A N   1 
ATOM   820  C  CA  . ILE A 1 98  ? 4.640   -5.427  -25.968 1.00 43.92 ? 107 ILE A CA  1 
ATOM   821  C  C   . ILE A 1 98  ? 3.421   -6.371  -25.927 1.00 41.61 ? 107 ILE A C   1 
ATOM   822  O  O   . ILE A 1 98  ? 2.905   -6.657  -24.850 1.00 39.33 ? 107 ILE A O   1 
ATOM   823  C  CB  . ILE A 1 98  ? 4.235   -3.941  -26.271 1.00 43.26 ? 107 ILE A CB  1 
ATOM   824  C  CG1 . ILE A 1 98  ? 3.183   -3.456  -25.273 1.00 44.53 ? 107 ILE A CG1 1 
ATOM   825  C  CG2 . ILE A 1 98  ? 3.725   -3.736  -27.701 1.00 42.75 ? 107 ILE A CG2 1 
ATOM   826  C  CD1 . ILE A 1 98  ? 3.240   -1.986  -25.031 1.00 43.90 ? 107 ILE A CD1 1 
ATOM   827  N  N   . ALA A 1 99  ? 2.989   -6.867  -27.089 1.00 38.45 ? 108 ALA A N   1 
ATOM   828  C  CA  . ALA A 1 99  ? 1.784   -7.710  -27.199 1.00 37.08 ? 108 ALA A CA  1 
ATOM   829  C  C   . ALA A 1 99  ? 1.867   -9.028  -26.414 1.00 36.76 ? 108 ALA A C   1 
ATOM   830  O  O   . ALA A 1 99  ? 0.899   -9.428  -25.772 1.00 34.37 ? 108 ALA A O   1 
ATOM   831  C  CB  . ALA A 1 99  ? 1.460   -7.993  -28.663 1.00 36.84 ? 108 ALA A CB  1 
ATOM   832  N  N   . VAL A 1 100 ? 3.025   -9.680  -26.448 1.00 38.46 ? 109 VAL A N   1 
ATOM   833  C  CA  . VAL A 1 100 ? 3.205   -10.964 -25.760 1.00 40.43 ? 109 VAL A CA  1 
ATOM   834  C  C   . VAL A 1 100 ? 3.064   -10.841 -24.223 1.00 39.31 ? 109 VAL A C   1 
ATOM   835  O  O   . VAL A 1 100 ? 2.183   -11.486 -23.648 1.00 40.10 ? 109 VAL A O   1 
ATOM   836  C  CB  . VAL A 1 100 ? 4.517   -11.680 -26.204 1.00 42.45 ? 109 VAL A CB  1 
ATOM   837  C  CG1 . VAL A 1 100 ? 4.786   -12.950 -25.386 1.00 44.39 ? 109 VAL A CG1 1 
ATOM   838  C  CG2 . VAL A 1 100 ? 4.429   -12.040 -27.685 1.00 44.72 ? 109 VAL A CG2 1 
ATOM   839  N  N   . PRO A 1 101 ? 3.901   -10.005 -23.564 1.00 39.74 ? 110 PRO A N   1 
ATOM   840  C  CA  . PRO A 1 101 ? 3.737   -9.851  -22.104 1.00 39.11 ? 110 PRO A CA  1 
ATOM   841  C  C   . PRO A 1 101 ? 2.376   -9.296  -21.660 1.00 36.83 ? 110 PRO A C   1 
ATOM   842  O  O   . PRO A 1 101 ? 1.893   -9.655  -20.585 1.00 36.88 ? 110 PRO A O   1 
ATOM   843  C  CB  . PRO A 1 101 ? 4.867   -8.887  -21.712 1.00 39.63 ? 110 PRO A CB  1 
ATOM   844  C  CG  . PRO A 1 101 ? 5.285   -8.222  -22.974 1.00 40.94 ? 110 PRO A CG  1 
ATOM   845  C  CD  . PRO A 1 101 ? 5.030   -9.199  -24.072 1.00 40.74 ? 110 PRO A CD  1 
ATOM   846  N  N   . TYR A 1 102 ? 1.770   -8.441  -22.478 1.00 34.62 ? 111 TYR A N   1 
ATOM   847  C  CA  . TYR A 1 102 ? 0.453   -7.881  -22.161 1.00 32.63 ? 111 TYR A CA  1 
ATOM   848  C  C   . TYR A 1 102 ? -0.618  -8.975  -22.198 1.00 32.09 ? 111 TYR A C   1 
ATOM   849  O  O   . TYR A 1 102 ? -1.423  -9.082  -21.278 1.00 29.77 ? 111 TYR A O   1 
ATOM   850  C  CB  . TYR A 1 102 ? 0.122   -6.744  -23.128 1.00 30.91 ? 111 TYR A CB  1 
ATOM   851  C  CG  . TYR A 1 102 ? -1.148  -5.963  -22.859 1.00 30.60 ? 111 TYR A CG  1 
ATOM   852  C  CD1 . TYR A 1 102 ? -1.682  -5.827  -21.571 1.00 31.87 ? 111 TYR A CD1 1 
ATOM   853  C  CD2 . TYR A 1 102 ? -1.791  -5.300  -23.903 1.00 30.42 ? 111 TYR A CD2 1 
ATOM   854  C  CE1 . TYR A 1 102 ? -2.832  -5.083  -21.352 1.00 31.32 ? 111 TYR A CE1 1 
ATOM   855  C  CE2 . TYR A 1 102 ? -2.936  -4.548  -23.683 1.00 29.36 ? 111 TYR A CE2 1 
ATOM   856  C  CZ  . TYR A 1 102 ? -3.453  -4.453  -22.418 1.00 26.73 ? 111 TYR A CZ  1 
ATOM   857  O  OH  . TYR A 1 102 ? -4.579  -3.708  -22.210 1.00 28.54 ? 111 TYR A OH  1 
ATOM   858  N  N   . CYS A 1 103 ? -0.600  -9.792  -23.251 1.00 32.38 ? 112 CYS A N   1 
ATOM   859  C  CA  . CYS A 1 103 ? -1.492  -10.947 -23.346 1.00 33.37 ? 112 CYS A CA  1 
ATOM   860  C  C   . CYS A 1 103 ? -1.218  -11.998 -22.266 1.00 35.76 ? 112 CYS A C   1 
ATOM   861  O  O   . CYS A 1 103 ? -2.156  -12.589 -21.735 1.00 33.64 ? 112 CYS A O   1 
ATOM   862  C  CB  . CYS A 1 103 ? -1.415  -11.579 -24.733 1.00 33.18 ? 112 CYS A CB  1 
ATOM   863  S  SG  . CYS A 1 103 ? -2.163  -10.567 -26.016 1.00 33.19 ? 112 CYS A SG  1 
ATOM   864  N  N   . GLN A 1 104 ? 0.058   -12.226 -21.945 1.00 38.46 ? 113 GLN A N   1 
ATOM   865  C  CA  . GLN A 1 104 ? 0.420   -13.148 -20.851 1.00 39.27 ? 113 GLN A CA  1 
ATOM   866  C  C   . GLN A 1 104 ? -0.114  -12.645 -19.512 1.00 38.03 ? 113 GLN A C   1 
ATOM   867  O  O   . GLN A 1 104 ? -0.727  -13.404 -18.757 1.00 36.68 ? 113 GLN A O   1 
ATOM   868  C  CB  . GLN A 1 104 ? 1.936   -13.345 -20.778 1.00 41.15 ? 113 GLN A CB  1 
ATOM   869  C  CG  . GLN A 1 104 ? 2.488   -14.225 -21.899 1.00 42.12 ? 113 GLN A CG  1 
ATOM   870  C  CD  . GLN A 1 104 ? 4.011   -14.252 -21.964 1.00 47.61 ? 113 GLN A CD  1 
ATOM   871  O  OE1 . GLN A 1 104 ? 4.688   -13.280 -21.616 1.00 46.46 ? 113 GLN A OE1 1 
ATOM   872  N  NE2 . GLN A 1 104 ? 4.555   -15.376 -22.430 1.00 48.24 ? 113 GLN A NE2 1 
ATOM   873  N  N   . LEU A 1 105 ? 0.111   -11.361 -19.235 1.00 36.74 ? 114 LEU A N   1 
ATOM   874  C  CA  . LEU A 1 105 ? -0.358  -10.728 -17.999 1.00 37.19 ? 114 LEU A CA  1 
ATOM   875  C  C   . LEU A 1 105 ? -1.886  -10.742 -17.913 1.00 36.37 ? 114 LEU A C   1 
ATOM   876  O  O   . LEU A 1 105 ? -2.452  -11.019 -16.860 1.00 31.86 ? 114 LEU A O   1 
ATOM   877  C  CB  . LEU A 1 105 ? 0.141   -9.276  -17.928 1.00 36.22 ? 114 LEU A CB  1 
ATOM   878  C  CG  . LEU A 1 105 ? -0.237  -8.450  -16.693 1.00 36.53 ? 114 LEU A CG  1 
ATOM   879  C  CD1 . LEU A 1 105 ? 0.300   -9.073  -15.417 1.00 40.17 ? 114 LEU A CD1 1 
ATOM   880  C  CD2 . LEU A 1 105 ? 0.280   -7.039  -16.858 1.00 38.75 ? 114 LEU A CD2 1 
ATOM   881  N  N   . SER A 1 106 ? -2.530  -10.415 -19.033 1.00 35.63 ? 115 SER A N   1 
ATOM   882  C  CA  . SER A 1 106 ? -3.985  -10.388 -19.127 1.00 35.32 ? 115 SER A CA  1 
ATOM   883  C  C   . SER A 1 106 ? -4.593  -11.773 -18.861 1.00 36.58 ? 115 SER A C   1 
ATOM   884  O  O   . SER A 1 106 ? -5.589  -11.898 -18.136 1.00 35.33 ? 115 SER A O   1 
ATOM   885  C  CB  . SER A 1 106 ? -4.392  -9.866  -20.507 1.00 32.66 ? 115 SER A CB  1 
ATOM   886  O  OG  . SER A 1 106 ? -3.852  -8.578  -20.729 1.00 31.71 ? 115 SER A OG  1 
ATOM   887  N  N   . LYS A 1 107 ? -3.970  -12.802 -19.431 1.00 37.85 ? 116 LYS A N   1 
ATOM   888  C  CA  . LYS A 1 107 ? -4.371  -14.192 -19.210 1.00 40.26 ? 116 LYS A CA  1 
ATOM   889  C  C   . LYS A 1 107 ? -4.221  -14.572 -17.736 1.00 41.59 ? 116 LYS A C   1 
ATOM   890  O  O   . LYS A 1 107 ? -5.124  -15.178 -17.158 1.00 43.02 ? 116 LYS A O   1 
ATOM   891  C  CB  . LYS A 1 107 ? -3.543  -15.129 -20.102 1.00 42.66 ? 116 LYS A CB  1 
ATOM   892  C  CG  . LYS A 1 107 ? -3.883  -16.622 -19.992 1.00 45.72 ? 116 LYS A CG  1 
ATOM   893  C  CD  . LYS A 1 107 ? -3.047  -17.433 -20.996 1.00 48.55 ? 116 LYS A CD  1 
ATOM   894  C  CE  . LYS A 1 107 ? -3.075  -18.927 -20.697 1.00 54.48 ? 116 LYS A CE  1 
ATOM   895  N  NZ  . LYS A 1 107 ? -2.272  -19.710 -21.670 0.00 53.72 ? 116 LYS A NZ  1 
ATOM   896  N  N   . LYS A 1 108 ? -3.096  -14.185 -17.135 1.00 43.19 ? 117 LYS A N   1 
ATOM   897  C  CA  . LYS A 1 108 ? -2.858  -14.382 -15.698 1.00 44.06 ? 117 LYS A CA  1 
ATOM   898  C  C   . LYS A 1 108 ? -3.958  -13.747 -14.834 1.00 41.96 ? 117 LYS A C   1 
ATOM   899  O  O   . LYS A 1 108 ? -4.497  -14.396 -13.929 1.00 41.20 ? 117 LYS A O   1 
ATOM   900  C  CB  . LYS A 1 108 ? -1.485  -13.831 -15.295 1.00 44.08 ? 117 LYS A CB  1 
ATOM   901  C  CG  . LYS A 1 108 ? -1.073  -14.164 -13.865 1.00 48.22 ? 117 LYS A CG  1 
ATOM   902  C  CD  . LYS A 1 108 ? 0.443   -14.174 -13.708 1.00 50.60 ? 117 LYS A CD  1 
ATOM   903  C  CE  . LYS A 1 108 ? 0.859   -14.607 -12.315 1.00 54.94 ? 117 LYS A CE  1 
ATOM   904  N  NZ  . LYS A 1 108 ? 2.344   -14.607 -12.155 0.00 55.16 ? 117 LYS A NZ  1 
ATOM   905  N  N   . LEU A 1 109 ? -4.295  -12.495 -15.133 1.00 39.65 ? 118 LEU A N   1 
ATOM   906  C  CA  . LEU A 1 109 ? -5.354  -11.772 -14.407 1.00 40.33 ? 118 LEU A CA  1 
ATOM   907  C  C   . LEU A 1 109 ? -6.787  -12.097 -14.881 1.00 39.23 ? 118 LEU A C   1 
ATOM   908  O  O   . LEU A 1 109 ? -7.753  -11.587 -14.308 1.00 40.18 ? 118 LEU A O   1 
ATOM   909  C  CB  . LEU A 1 109 ? -5.104  -10.255 -14.487 1.00 39.33 ? 118 LEU A CB  1 
ATOM   910  C  CG  . LEU A 1 109 ? -3.936  -9.702  -13.658 1.00 40.38 ? 118 LEU A CG  1 
ATOM   911  C  CD1 . LEU A 1 109 ? -3.634  -8.275  -14.070 1.00 37.63 ? 118 LEU A CD1 1 
ATOM   912  C  CD2 . LEU A 1 109 ? -4.210  -9.766  -12.157 1.00 43.06 ? 118 LEU A CD2 1 
ATOM   913  N  N   . GLU A 1 110 ? -6.917  -12.932 -15.916 1.00 40.21 ? 119 GLU A N   1 
ATOM   914  C  CA  . GLU A 1 110 ? -8.205  -13.296 -16.528 1.00 40.44 ? 119 GLU A CA  1 
ATOM   915  C  C   . GLU A 1 110 ? -8.994  -12.060 -16.969 1.00 37.86 ? 119 GLU A C   1 
ATOM   916  O  O   . GLU A 1 110 ? -10.176 -11.921 -16.680 1.00 39.99 ? 119 GLU A O   1 
ATOM   917  C  CB  . GLU A 1 110 ? -9.045  -14.177 -15.597 1.00 40.66 ? 119 GLU A CB  1 
ATOM   918  C  CG  . GLU A 1 110 ? -8.322  -15.394 -15.030 1.00 47.68 ? 119 GLU A CG  1 
ATOM   919  C  CD  . GLU A 1 110 ? -9.213  -16.207 -14.104 1.00 49.66 ? 119 GLU A CD  1 
ATOM   920  O  OE1 . GLU A 1 110 ? -10.337 -16.554 -14.521 1.00 57.67 ? 119 GLU A OE1 1 
ATOM   921  O  OE2 . GLU A 1 110 ? -8.791  -16.497 -12.961 1.00 59.29 ? 119 GLU A OE2 1 
ATOM   922  N  N   . LEU A 1 111 ? -8.305  -11.154 -17.647 1.00 36.12 ? 120 LEU A N   1 
ATOM   923  C  CA  . LEU A 1 111 ? -8.911  -9.970  -18.237 1.00 34.05 ? 120 LEU A CA  1 
ATOM   924  C  C   . LEU A 1 111 ? -8.477  -9.931  -19.690 1.00 33.36 ? 120 LEU A C   1 
ATOM   925  O  O   . LEU A 1 111 ? -7.442  -10.498 -20.018 1.00 34.57 ? 120 LEU A O   1 
ATOM   926  C  CB  . LEU A 1 111 ? -8.431  -8.719  -17.514 1.00 32.27 ? 120 LEU A CB  1 
ATOM   927  C  CG  . LEU A 1 111 ? -9.029  -8.471  -16.133 1.00 34.77 ? 120 LEU A CG  1 
ATOM   928  C  CD1 . LEU A 1 111 ? -8.169  -7.481  -15.344 1.00 34.78 ? 120 LEU A CD1 1 
ATOM   929  C  CD2 . LEU A 1 111 ? -10.466 -7.960  -16.257 1.00 31.12 ? 120 LEU A CD2 1 
ATOM   930  N  N   . PRO A 1 112 ? -9.250  -9.267  -20.569 1.00 31.82 ? 121 PRO A N   1 
ATOM   931  C  CA  . PRO A 1 112 ? -8.825  -9.217  -21.974 1.00 32.10 ? 121 PRO A CA  1 
ATOM   932  C  C   . PRO A 1 112 ? -7.665  -8.236  -22.191 1.00 30.22 ? 121 PRO A C   1 
ATOM   933  O  O   . PRO A 1 112 ? -7.540  -7.284  -21.428 1.00 28.51 ? 121 PRO A O   1 
ATOM   934  C  CB  . PRO A 1 112 ? -10.080 -8.725  -22.711 1.00 31.93 ? 121 PRO A CB  1 
ATOM   935  C  CG  . PRO A 1 112 ? -11.128 -8.573  -21.700 1.00 33.22 ? 121 PRO A CG  1 
ATOM   936  C  CD  . PRO A 1 112 ? -10.507 -8.537  -20.362 1.00 31.86 ? 121 PRO A CD  1 
ATOM   937  N  N   . PRO A 1 113 ? -6.850  -8.433  -23.246 1.00 31.00 ? 122 PRO A N   1 
ATOM   938  C  CA  . PRO A 1 113 ? -5.690  -7.563  -23.496 1.00 29.54 ? 122 PRO A CA  1 
ATOM   939  C  C   . PRO A 1 113 ? -6.085  -6.217  -24.132 1.00 28.21 ? 122 PRO A C   1 
ATOM   940  O  O   . PRO A 1 113 ? -5.738  -5.926  -25.275 1.00 27.75 ? 122 PRO A O   1 
ATOM   941  C  CB  . PRO A 1 113 ? -4.828  -8.411  -24.423 1.00 31.11 ? 122 PRO A CB  1 
ATOM   942  C  CG  . PRO A 1 113 ? -5.810  -9.196  -25.200 1.00 30.43 ? 122 PRO A CG  1 
ATOM   943  C  CD  . PRO A 1 113 ? -6.963  -9.484  -24.274 1.00 31.77 ? 122 PRO A CD  1 
ATOM   944  N  N   . ILE A 1 114 ? -6.810  -5.412  -23.363 1.00 26.31 ? 123 ILE A N   1 
ATOM   945  C  CA  . ILE A 1 114 ? -7.190  -4.063  -23.752 1.00 26.36 ? 123 ILE A CA  1 
ATOM   946  C  C   . ILE A 1 114 ? -7.461  -3.268  -22.472 1.00 28.03 ? 123 ILE A C   1 
ATOM   947  O  O   . ILE A 1 114 ? -7.794  -3.845  -21.430 1.00 29.96 ? 123 ILE A O   1 
ATOM   948  C  CB  . ILE A 1 114 ? -8.413  -4.067  -24.718 1.00 26.60 ? 123 ILE A CB  1 
ATOM   949  C  CG1 . ILE A 1 114 ? -8.669  -2.660  -25.276 1.00 25.73 ? 123 ILE A CG1 1 
ATOM   950  C  CG2 . ILE A 1 114 ? -9.670  -4.647  -24.027 1.00 25.36 ? 123 ILE A CG2 1 
ATOM   951  C  CD1 . ILE A 1 114 ? -9.611  -2.605  -26.466 1.00 28.14 ? 123 ILE A CD1 1 
ATOM   952  N  N   . LEU A 1 115 ? -7.299  -1.950  -22.538 1.00 26.43 ? 124 LEU A N   1 
ATOM   953  C  CA  . LEU A 1 115 ? -7.563  -1.105  -21.383 1.00 24.35 ? 124 LEU A CA  1 
ATOM   954  C  C   . LEU A 1 115 ? -9.032  -1.234  -20.992 1.00 22.84 ? 124 LEU A C   1 
ATOM   955  O  O   . LEU A 1 115 ? -9.912  -0.989  -21.815 1.00 24.33 ? 124 LEU A O   1 
ATOM   956  C  CB  . LEU A 1 115 ? -7.211  0.351   -21.680 1.00 23.41 ? 124 LEU A CB  1 
ATOM   957  C  CG  . LEU A 1 115 ? -7.096  1.307   -20.485 1.00 23.65 ? 124 LEU A CG  1 
ATOM   958  C  CD1 . LEU A 1 115 ? -5.857  1.017   -19.665 1.00 27.46 ? 124 LEU A CD1 1 
ATOM   959  C  CD2 . LEU A 1 115 ? -7.091  2.740   -20.979 1.00 25.81 ? 124 LEU A CD2 1 
ATOM   960  N  N   . VAL A 1 116 ? -9.284  -1.659  -19.751 1.00 23.86 ? 125 VAL A N   1 
ATOM   961  C  CA  . VAL A 1 116 ? -10.650 -1.769  -19.222 1.00 23.82 ? 125 VAL A CA  1 
ATOM   962  C  C   . VAL A 1 116 ? -10.896 -0.741  -18.118 1.00 24.38 ? 125 VAL A C   1 
ATOM   963  O  O   . VAL A 1 116 ? -9.973  -0.109  -17.611 1.00 23.07 ? 125 VAL A O   1 
ATOM   964  C  CB  . VAL A 1 116 ? -11.010 -3.225  -18.752 1.00 22.82 ? 125 VAL A CB  1 
ATOM   965  C  CG1 . VAL A 1 116 ? -10.747 -4.236  -19.868 1.00 23.16 ? 125 VAL A CG1 1 
ATOM   966  C  CG2 . VAL A 1 116 ? -10.264 -3.644  -17.486 1.00 27.69 ? 125 VAL A CG2 1 
ATOM   967  N  N   . TYR A 1 117 ? -12.164 -0.596  -17.756 1.00 24.07 ? 126 TYR A N   1 
ATOM   968  C  CA  . TYR A 1 117 ? -12.598 0.265   -16.650 1.00 23.43 ? 126 TYR A CA  1 
ATOM   969  C  C   . TYR A 1 117 ? -11.824 -0.010  -15.364 1.00 23.17 ? 126 TYR A C   1 
ATOM   970  O  O   . TYR A 1 117 ? -11.421 0.917   -14.647 1.00 23.63 ? 126 TYR A O   1 
ATOM   971  C  CB  . TYR A 1 117 ? -14.089 0.033   -16.432 1.00 23.50 ? 126 TYR A CB  1 
ATOM   972  C  CG  . TYR A 1 117 ? -14.759 0.836   -15.356 1.00 20.77 ? 126 TYR A CG  1 
ATOM   973  C  CD1 . TYR A 1 117 ? -15.218 2.129   -15.618 1.00 20.26 ? 126 TYR A CD1 1 
ATOM   974  C  CD2 . TYR A 1 117 ? -15.011 0.281   -14.100 1.00 21.69 ? 126 TYR A CD2 1 
ATOM   975  C  CE1 . TYR A 1 117 ? -15.881 2.864   -14.633 1.00 22.62 ? 126 TYR A CE1 1 
ATOM   976  C  CE2 . TYR A 1 117 ? -15.673 1.005   -13.106 1.00 25.12 ? 126 TYR A CE2 1 
ATOM   977  C  CZ  . TYR A 1 117 ? -16.108 2.306   -13.386 1.00 23.45 ? 126 TYR A CZ  1 
ATOM   978  O  OH  . TYR A 1 117 ? -16.771 3.046   -12.430 1.00 25.04 ? 126 TYR A OH  1 
ATOM   979  N  N   . ALA A 1 118 ? -11.622 -1.291  -15.080 1.00 25.60 ? 127 ALA A N   1 
ATOM   980  C  CA  . ALA A 1 118 ? -10.827 -1.728  -13.930 1.00 27.33 ? 127 ALA A CA  1 
ATOM   981  C  C   . ALA A 1 118 ? -9.355  -1.287  -13.945 1.00 27.73 ? 127 ALA A C   1 
ATOM   982  O  O   . ALA A 1 118 ? -8.729  -1.231  -12.890 1.00 30.32 ? 127 ALA A O   1 
ATOM   983  C  CB  . ALA A 1 118 ? -10.920 -3.251  -13.757 1.00 29.05 ? 127 ALA A CB  1 
ATOM   984  N  N   . ASP A 1 119 ? -8.813  -0.982  -15.122 1.00 27.98 ? 128 ASP A N   1 
ATOM   985  C  CA  . ASP A 1 119 ? -7.475  -0.420  -15.233 1.00 28.25 ? 128 ASP A CA  1 
ATOM   986  C  C   . ASP A 1 119 ? -7.523  1.086   -15.049 1.00 29.02 ? 128 ASP A C   1 
ATOM   987  O  O   . ASP A 1 119 ? -6.907  1.628   -14.126 1.00 30.70 ? 128 ASP A O   1 
ATOM   988  C  CB  . ASP A 1 119 ? -6.853  -0.729  -16.597 1.00 29.37 ? 128 ASP A CB  1 
ATOM   989  C  CG  . ASP A 1 119 ? -6.795  -2.215  -16.905 1.00 29.58 ? 128 ASP A CG  1 
ATOM   990  O  OD1 . ASP A 1 119 ? -6.469  -3.030  -16.010 1.00 26.79 ? 128 ASP A OD1 1 
ATOM   991  O  OD2 . ASP A 1 119 ? -7.052  -2.549  -18.071 1.00 23.31 ? 128 ASP A OD2 1 
ATOM   992  N  N   . CYS A 1 120 ? -8.257  1.762   -15.931 1.00 28.50 ? 129 CYS A N   1 
ATOM   993  C  CA  . CYS A 1 120 ? -8.128  3.222   -16.070 1.00 28.50 ? 129 CYS A CA  1 
ATOM   994  C  C   . CYS A 1 120 ? -8.968  4.051   -15.090 1.00 28.34 ? 129 CYS A C   1 
ATOM   995  O  O   . CYS A 1 120 ? -8.735  5.259   -14.958 1.00 27.09 ? 129 CYS A O   1 
ATOM   996  C  CB  . CYS A 1 120 ? -8.394  3.649   -17.511 1.00 27.06 ? 129 CYS A CB  1 
ATOM   997  S  SG  . CYS A 1 120 ? -10.057 3.381   -18.102 1.00 28.03 ? 129 CYS A SG  1 
ATOM   998  N  N   . VAL A 1 121 ? -9.928  3.418   -14.408 1.00 28.35 ? 130 VAL A N   1 
ATOM   999  C  CA  . VAL A 1 121 ? -10.661 4.062   -13.302 1.00 27.94 ? 130 VAL A CA  1 
ATOM   1000 C  C   . VAL A 1 121 ? -10.223 3.446   -11.975 1.00 28.09 ? 130 VAL A C   1 
ATOM   1001 O  O   . VAL A 1 121 ? -9.684  4.139   -11.114 1.00 29.13 ? 130 VAL A O   1 
ATOM   1002 C  CB  . VAL A 1 121 ? -12.193 3.970   -13.503 1.00 27.13 ? 130 VAL A CB  1 
ATOM   1003 C  CG1 . VAL A 1 121 ? -12.965 4.587   -12.329 1.00 28.76 ? 130 VAL A CG1 1 
ATOM   1004 C  CG2 . VAL A 1 121 ? -12.579 4.685   -14.796 1.00 28.07 ? 130 VAL A CG2 1 
ATOM   1005 N  N   . LEU A 1 122 ? -10.427 2.140   -11.832 1.00 26.47 ? 131 LEU A N   1 
ATOM   1006 C  CA  . LEU A 1 122 ? -10.299 1.484   -10.529 1.00 28.00 ? 131 LEU A CA  1 
ATOM   1007 C  C   . LEU A 1 122 ? -8.865  1.337   -10.009 1.00 28.10 ? 131 LEU A C   1 
ATOM   1008 O  O   . LEU A 1 122 ? -8.666  1.290   -8.805  1.00 28.21 ? 131 LEU A O   1 
ATOM   1009 C  CB  . LEU A 1 122 ? -10.983 0.110   -10.549 1.00 27.02 ? 131 LEU A CB  1 
ATOM   1010 C  CG  . LEU A 1 122 ? -12.444 0.069   -11.000 1.00 22.62 ? 131 LEU A CG  1 
ATOM   1011 C  CD1 . LEU A 1 122 ? -12.992 -1.332  -10.825 1.00 23.09 ? 131 LEU A CD1 1 
ATOM   1012 C  CD2 . LEU A 1 122 ? -13.300 1.086   -10.263 1.00 24.13 ? 131 LEU A CD2 1 
ATOM   1013 N  N   . ALA A 1 123 ? -7.884  1.260   -10.907 1.00 29.60 ? 132 ALA A N   1 
ATOM   1014 C  CA  . ALA A 1 123 ? -6.470  1.106   -10.520 1.00 31.53 ? 132 ALA A CA  1 
ATOM   1015 C  C   . ALA A 1 123 ? -5.599  2.337   -10.859 1.00 31.16 ? 132 ALA A C   1 
ATOM   1016 O  O   . ALA A 1 123 ? -4.391  2.331   -10.618 1.00 33.75 ? 132 ALA A O   1 
ATOM   1017 C  CB  . ALA A 1 123 ? -5.900  -0.149  -11.180 1.00 32.49 ? 132 ALA A CB  1 
ATOM   1018 N  N   . ASN A 1 124 ? -6.224  3.391   -11.377 1.00 30.54 ? 133 ASN A N   1 
ATOM   1019 C  CA  . ASN A 1 124 ? -5.526  4.535   -11.962 1.00 31.87 ? 133 ASN A CA  1 
ATOM   1020 C  C   . ASN A 1 124 ? -5.662  5.762   -11.066 1.00 30.75 ? 133 ASN A C   1 
ATOM   1021 O  O   . ASN A 1 124 ? -6.101  6.822   -11.504 1.00 29.72 ? 133 ASN A O   1 
ATOM   1022 C  CB  . ASN A 1 124 ? -6.111  4.812   -13.350 1.00 28.86 ? 133 ASN A CB  1 
ATOM   1023 C  CG  . ASN A 1 124 ? -5.322  5.859   -14.148 1.00 32.03 ? 133 ASN A CG  1 
ATOM   1024 O  OD1 . ASN A 1 124 ? -4.195  6.208   -13.804 1.00 35.55 ? 133 ASN A OD1 1 
ATOM   1025 N  ND2 . ASN A 1 124 ? -5.923  6.350   -15.225 1.00 25.89 ? 133 ASN A ND2 1 
ATOM   1026 N  N   . TRP A 1 125 ? -5.285  5.618   -9.804  1.00 32.51 ? 134 TRP A N   1 
ATOM   1027 C  CA  . TRP A 1 125 ? -5.486  6.710   -8.855  1.00 33.51 ? 134 TRP A CA  1 
ATOM   1028 C  C   . TRP A 1 125 ? -4.550  6.679   -7.674  1.00 36.17 ? 134 TRP A C   1 
ATOM   1029 O  O   . TRP A 1 125 ? -3.923  5.660   -7.385  1.00 37.88 ? 134 TRP A O   1 
ATOM   1030 C  CB  . TRP A 1 125 ? -6.949  6.748   -8.372  1.00 31.72 ? 134 TRP A CB  1 
ATOM   1031 C  CG  . TRP A 1 125 ? -7.388  5.589   -7.508  1.00 31.98 ? 134 TRP A CG  1 
ATOM   1032 C  CD1 . TRP A 1 125 ? -7.961  4.418   -7.928  1.00 32.56 ? 134 TRP A CD1 1 
ATOM   1033 C  CD2 . TRP A 1 125 ? -7.339  5.514   -6.071  1.00 36.54 ? 134 TRP A CD2 1 
ATOM   1034 N  NE1 . TRP A 1 125 ? -8.259  3.618   -6.846  1.00 35.08 ? 134 TRP A NE1 1 
ATOM   1035 C  CE2 . TRP A 1 125 ? -7.893  4.266   -5.697  1.00 35.47 ? 134 TRP A CE2 1 
ATOM   1036 C  CE3 . TRP A 1 125 ? -6.878  6.379   -5.066  1.00 37.74 ? 134 TRP A CE3 1 
ATOM   1037 C  CZ2 . TRP A 1 125 ? -7.990  3.854   -4.361  1.00 37.89 ? 134 TRP A CZ2 1 
ATOM   1038 C  CZ3 . TRP A 1 125 ? -6.972  5.969   -3.731  1.00 40.61 ? 134 TRP A CZ3 1 
ATOM   1039 C  CH2 . TRP A 1 125 ? -7.521  4.713   -3.394  1.00 40.18 ? 134 TRP A CH2 1 
ATOM   1040 N  N   . LYS A 1 126 ? -4.477  7.821   -6.999  1.00 38.62 ? 135 LYS A N   1 
ATOM   1041 C  CA  . LYS A 1 126 ? -3.740  7.960   -5.751  1.00 41.44 ? 135 LYS A CA  1 
ATOM   1042 C  C   . LYS A 1 126 ? -4.300  9.117   -4.930  1.00 42.28 ? 135 LYS A C   1 
ATOM   1043 O  O   . LYS A 1 126 ? -4.951  10.013  -5.471  1.00 40.36 ? 135 LYS A O   1 
ATOM   1044 C  CB  . LYS A 1 126 ? -2.249  8.195   -6.017  1.00 42.35 ? 135 LYS A CB  1 
ATOM   1045 C  CG  . LYS A 1 126 ? -1.934  9.479   -6.803  1.00 44.32 ? 135 LYS A CG  1 
ATOM   1046 C  CD  . LYS A 1 126 ? -0.450  9.675   -7.031  1.00 46.53 ? 135 LYS A CD  1 
ATOM   1047 C  CE  . LYS A 1 126 ? 0.301   9.976   -5.739  1.00 53.39 ? 135 LYS A CE  1 
ATOM   1048 N  NZ  . LYS A 1 126 ? 1.690   10.464  -5.998  1.00 55.45 ? 135 LYS A NZ  1 
ATOM   1049 N  N   . LYS A 1 127 ? -4.046  9.076   -3.626  1.00 44.62 ? 136 LYS A N   1 
ATOM   1050 C  CA  . LYS A 1 127 ? -4.215  10.247  -2.773  1.00 47.76 ? 136 LYS A CA  1 
ATOM   1051 C  C   . LYS A 1 127 ? -2.964  11.115  -2.888  1.00 50.00 ? 136 LYS A C   1 
ATOM   1052 O  O   . LYS A 1 127 ? -1.844  10.592  -2.896  1.00 51.53 ? 136 LYS A O   1 
ATOM   1053 C  CB  . LYS A 1 127 ? -4.428  9.846   -1.310  1.00 49.23 ? 136 LYS A CB  1 
ATOM   1054 C  CG  . LYS A 1 127 ? -5.804  9.283   -1.012  1.00 48.22 ? 136 LYS A CG  1 
ATOM   1055 C  CD  . LYS A 1 127 ? -5.965  9.044   0.481   1.00 51.38 ? 136 LYS A CD  1 
ATOM   1056 C  CE  . LYS A 1 127 ? -7.360  8.581   0.834   1.00 49.87 ? 136 LYS A CE  1 
ATOM   1057 N  NZ  . LYS A 1 127 ? -7.513  8.410   2.294   1.00 50.21 ? 136 LYS A NZ  1 
ATOM   1058 N  N   . LYS A 1 128 ? -3.155  12.430  -2.987  1.00 51.68 ? 137 LYS A N   1 
ATOM   1059 C  CA  . LYS A 1 128 ? -2.051  13.389  -2.850  1.00 53.65 ? 137 LYS A CA  1 
ATOM   1060 C  C   . LYS A 1 128 ? -1.512  13.333  -1.420  1.00 56.86 ? 137 LYS A C   1 
ATOM   1061 O  O   . LYS A 1 128 ? -0.311  13.165  -1.206  1.00 57.54 ? 137 LYS A O   1 
ATOM   1062 C  CB  . LYS A 1 128 ? -2.514  14.815  -3.164  1.00 54.16 ? 137 LYS A CB  1 
ATOM   1063 C  CG  . LYS A 1 128 ? -2.918  15.060  -4.615  1.00 51.46 ? 137 LYS A CG  1 
ATOM   1064 C  CD  . LYS A 1 128 ? -3.563  16.435  -4.747  1.00 53.62 ? 137 LYS A CD  1 
ATOM   1065 C  CE  . LYS A 1 128 ? -3.794  16.842  -6.196  1.00 52.93 ? 137 LYS A CE  1 
ATOM   1066 N  NZ  . LYS A 1 128 ? -4.552  18.127  -6.289  1.00 49.89 ? 137 LYS A NZ  1 
ATOM   1067 N  N   . ASP A 1 129 ? -2.424  13.482  -0.459  1.00 58.30 ? 138 ASP A N   1 
ATOM   1068 C  CA  . ASP A 1 129 ? -2.135  13.344  0.964   1.00 61.28 ? 138 ASP A CA  1 
ATOM   1069 C  C   . ASP A 1 129 ? -2.867  12.086  1.463   1.00 60.52 ? 138 ASP A C   1 
ATOM   1070 O  O   . ASP A 1 129 ? -4.096  12.089  1.537   1.00 58.85 ? 138 ASP A O   1 
ATOM   1071 C  CB  . ASP A 1 129 ? -2.611  14.595  1.718   1.00 63.17 ? 138 ASP A CB  1 
ATOM   1072 C  CG  . ASP A 1 129 ? -2.189  14.616  3.192   1.00 66.68 ? 138 ASP A CG  1 
ATOM   1073 O  OD1 . ASP A 1 129 ? -1.616  13.628  3.699   1.00 67.70 ? 138 ASP A OD1 1 
ATOM   1074 O  OD2 . ASP A 1 129 ? -2.445  15.646  3.854   1.00 72.10 ? 138 ASP A OD2 1 
ATOM   1075 N  N   . PRO A 1 130 ? -2.119  11.010  1.798   1.00 63.14 ? 139 PRO A N   1 
ATOM   1076 C  CA  . PRO A 1 130 ? -2.688  9.788   2.407   1.00 63.21 ? 139 PRO A CA  1 
ATOM   1077 C  C   . PRO A 1 130 ? -3.532  9.980   3.675   1.00 63.90 ? 139 PRO A C   1 
ATOM   1078 O  O   . PRO A 1 130 ? -4.407  9.159   3.945   1.00 63.48 ? 139 PRO A O   1 
ATOM   1079 C  CB  . PRO A 1 130 ? -1.446  8.959   2.753   1.00 65.51 ? 139 PRO A CB  1 
ATOM   1080 C  CG  . PRO A 1 130 ? -0.418  9.408   1.807   1.00 67.43 ? 139 PRO A CG  1 
ATOM   1081 C  CD  . PRO A 1 130 ? -0.665  10.869  1.589   1.00 65.83 ? 139 PRO A CD  1 
ATOM   1082 N  N   . ASN A 1 131 ? -3.258  11.036  4.439   1.00 66.56 ? 140 ASN A N   1 
ATOM   1083 C  CA  . ASN A 1 131 ? -4.000  11.342  5.672   1.00 69.36 ? 140 ASN A CA  1 
ATOM   1084 C  C   . ASN A 1 131 ? -5.274  12.183  5.480   1.00 68.06 ? 140 ASN A C   1 
ATOM   1085 O  O   . ASN A 1 131 ? -5.960  12.488  6.458   1.00 69.04 ? 140 ASN A O   1 
ATOM   1086 C  CB  . ASN A 1 131 ? -3.066  12.025  6.686   1.00 73.90 ? 140 ASN A CB  1 
ATOM   1087 C  CG  . ASN A 1 131 ? -1.938  11.114  7.147   1.00 77.71 ? 140 ASN A CG  1 
ATOM   1088 O  OD1 . ASN A 1 131 ? -0.764  11.473  7.060   1.00 82.23 ? 140 ASN A OD1 1 
ATOM   1089 N  ND2 . ASN A 1 131 ? -2.292  9.927   7.637   1.00 77.99 ? 140 ASN A ND2 1 
ATOM   1090 N  N   . LYS A 1 132 ? -5.588  12.548  4.235   1.00 65.57 ? 141 LYS A N   1 
ATOM   1091 C  CA  . LYS A 1 132 ? -6.827  13.261  3.907   1.00 64.28 ? 141 LYS A CA  1 
ATOM   1092 C  C   . LYS A 1 132 ? -7.791  12.341  3.128   1.00 60.43 ? 141 LYS A C   1 
ATOM   1093 O  O   . LYS A 1 132 ? -7.364  11.314  2.593   1.00 55.81 ? 141 LYS A O   1 
ATOM   1094 C  CB  . LYS A 1 132 ? -6.498  14.536  3.125   1.00 64.95 ? 141 LYS A CB  1 
ATOM   1095 C  CG  . LYS A 1 132 ? -5.925  15.642  4.000   1.00 68.34 ? 141 LYS A CG  1 
ATOM   1096 C  CD  . LYS A 1 132 ? -5.424  16.819  3.177   1.00 69.02 ? 141 LYS A CD  1 
ATOM   1097 C  CE  . LYS A 1 132 ? -4.906  17.931  4.058   0.00 72.22 ? 141 LYS A CE  1 
ATOM   1098 N  NZ  . LYS A 1 132 ? -4.406  19.086  3.263   0.00 72.63 ? 141 LYS A NZ  1 
ATOM   1099 N  N   . PRO A 1 133 ? -9.092  12.700  3.068   1.00 59.95 ? 142 PRO A N   1 
ATOM   1100 C  CA  . PRO A 1 133 ? -10.080 11.780  2.486   1.00 57.64 ? 142 PRO A CA  1 
ATOM   1101 C  C   . PRO A 1 133 ? -9.992  11.575  0.971   1.00 54.70 ? 142 PRO A C   1 
ATOM   1102 O  O   . PRO A 1 133 ? -9.274  12.300  0.274   1.00 54.92 ? 142 PRO A O   1 
ATOM   1103 C  CB  . PRO A 1 133 ? -11.430 12.433  2.839   1.00 58.85 ? 142 PRO A CB  1 
ATOM   1104 C  CG  . PRO A 1 133 ? -11.125 13.519  3.806   1.00 61.17 ? 142 PRO A CG  1 
ATOM   1105 C  CD  . PRO A 1 133 ? -9.736  13.944  3.531   1.00 61.92 ? 142 PRO A CD  1 
ATOM   1106 N  N   . LEU A 1 134 ? -10.740 10.587  0.489   1.00 51.93 ? 143 LEU A N   1 
ATOM   1107 C  CA  . LEU A 1 134 ? -10.924 10.354  -0.944  1.00 48.30 ? 143 LEU A CA  1 
ATOM   1108 C  C   . LEU A 1 134 ? -11.883 11.378  -1.547  1.00 46.66 ? 143 LEU A C   1 
ATOM   1109 O  O   . LEU A 1 134 ? -13.075 11.105  -1.735  1.00 45.70 ? 143 LEU A O   1 
ATOM   1110 C  CB  . LEU A 1 134 ? -11.449 8.935   -1.199  1.00 47.62 ? 143 LEU A CB  1 
ATOM   1111 C  CG  . LEU A 1 134 ? -10.499 7.789   -0.868  1.00 50.61 ? 143 LEU A CG  1 
ATOM   1112 C  CD1 . LEU A 1 134 ? -11.263 6.470   -0.836  1.00 50.79 ? 143 LEU A CD1 1 
ATOM   1113 C  CD2 . LEU A 1 134 ? -9.348  7.731   -1.873  1.00 53.56 ? 143 LEU A CD2 1 
ATOM   1114 N  N   . THR A 1 135 ? -11.346 12.562  -1.838  1.00 46.79 ? 144 THR A N   1 
ATOM   1115 C  CA  . THR A 1 135 ? -12.074 13.636  -2.522  1.00 45.19 ? 144 THR A CA  1 
ATOM   1116 C  C   . THR A 1 135 ? -11.261 14.067  -3.728  1.00 43.33 ? 144 THR A C   1 
ATOM   1117 O  O   . THR A 1 135 ? -10.057 13.828  -3.772  1.00 42.65 ? 144 THR A O   1 
ATOM   1118 C  CB  . THR A 1 135 ? -12.268 14.867  -1.616  1.00 47.93 ? 144 THR A CB  1 
ATOM   1119 O  OG1 . THR A 1 135 ? -10.988 15.378  -1.220  1.00 51.96 ? 144 THR A OG1 1 
ATOM   1120 C  CG2 . THR A 1 135 ? -13.086 14.515  -0.375  1.00 48.34 ? 144 THR A CG2 1 
ATOM   1121 N  N   . TYR A 1 136 ? -11.913 14.727  -4.682  1.00 41.51 ? 145 TYR A N   1 
ATOM   1122 C  CA  . TYR A 1 136 ? -11.253 15.155  -5.923  1.00 40.82 ? 145 TYR A CA  1 
ATOM   1123 C  C   . TYR A 1 136 ? -9.992  15.990  -5.668  1.00 41.23 ? 145 TYR A C   1 
ATOM   1124 O  O   . TYR A 1 136 ? -8.940  15.728  -6.266  1.00 37.25 ? 145 TYR A O   1 
ATOM   1125 C  CB  . TYR A 1 136 ? -12.221 15.936  -6.820  1.00 40.60 ? 145 TYR A CB  1 
ATOM   1126 C  CG  . TYR A 1 136 ? -11.671 16.173  -8.203  1.00 39.47 ? 145 TYR A CG  1 
ATOM   1127 C  CD1 . TYR A 1 136 ? -11.808 15.208  -9.189  1.00 39.67 ? 145 TYR A CD1 1 
ATOM   1128 C  CD2 . TYR A 1 136 ? -10.986 17.357  -8.521  1.00 42.15 ? 145 TYR A CD2 1 
ATOM   1129 C  CE1 . TYR A 1 136 ? -11.297 15.400  -10.455 1.00 37.36 ? 145 TYR A CE1 1 
ATOM   1130 C  CE2 . TYR A 1 136 ? -10.469 17.561  -9.793  1.00 42.95 ? 145 TYR A CE2 1 
ATOM   1131 C  CZ  . TYR A 1 136 ? -10.634 16.572  -10.758 1.00 37.37 ? 145 TYR A CZ  1 
ATOM   1132 O  OH  . TYR A 1 136 ? -10.142 16.732  -12.027 1.00 38.98 ? 145 TYR A OH  1 
ATOM   1133 N  N   . GLU A 1 137 ? -10.108 16.969  -4.766  1.00 43.12 ? 146 GLU A N   1 
ATOM   1134 C  CA  . GLU A 1 137 ? -8.998  17.870  -4.415  1.00 46.32 ? 146 GLU A CA  1 
ATOM   1135 C  C   . GLU A 1 137 ? -7.779  17.175  -3.803  1.00 46.91 ? 146 GLU A C   1 
ATOM   1136 O  O   . GLU A 1 137 ? -6.679  17.739  -3.817  1.00 47.67 ? 146 GLU A O   1 
ATOM   1137 C  CB  . GLU A 1 137 ? -9.473  18.964  -3.446  1.00 47.97 ? 146 GLU A CB  1 
ATOM   1138 C  CG  . GLU A 1 137 ? -8.518  20.140  -3.239  0.00 50.78 ? 146 GLU A CG  1 
ATOM   1139 C  CD  . GLU A 1 137 ? -9.156  21.323  -2.527  0.00 53.26 ? 146 GLU A CD  1 
ATOM   1140 O  OE1 . GLU A 1 137 ? -10.019 21.108  -1.648  0.00 53.32 ? 146 GLU A OE1 1 
ATOM   1141 O  OE2 . GLU A 1 137 ? -8.786  22.474  -2.842  0.00 54.52 ? 146 GLU A OE2 1 
ATOM   1142 N  N   . ASN A 1 138 ? -7.984  15.981  -3.242  1.00 46.68 ? 147 ASN A N   1 
ATOM   1143 C  CA  . ASN A 1 138 ? -6.910  15.179  -2.650  1.00 47.46 ? 147 ASN A CA  1 
ATOM   1144 C  C   . ASN A 1 138 ? -6.581  13.957  -3.513  1.00 44.10 ? 147 ASN A C   1 
ATOM   1145 O  O   . ASN A 1 138 ? -6.057  12.963  -3.012  1.00 43.91 ? 147 ASN A O   1 
ATOM   1146 C  CB  . ASN A 1 138 ? -7.310  14.751  -1.227  1.00 47.56 ? 147 ASN A CB  1 
ATOM   1147 C  CG  . ASN A 1 138 ? -6.209  13.978  -0.501  1.00 50.39 ? 147 ASN A CG  1 
ATOM   1148 O  OD1 . ASN A 1 138 ? -5.037  14.348  -0.543  1.00 50.62 ? 147 ASN A OD1 1 
ATOM   1149 N  ND2 . ASN A 1 138 ? -6.588  12.885  0.147   1.00 52.95 ? 147 ASN A ND2 1 
ATOM   1150 N  N   . MET A 1 139 ? -6.879  14.014  -4.806  1.00 41.81 ? 148 MET A N   1 
ATOM   1151 C  CA  . MET A 1 139 ? -6.609  12.869  -5.675  1.00 41.11 ? 148 MET A CA  1 
ATOM   1152 C  C   . MET A 1 139 ? -6.001  13.255  -7.015  1.00 39.75 ? 148 MET A C   1 
ATOM   1153 O  O   . MET A 1 139 ? -6.193  14.378  -7.493  1.00 40.24 ? 148 MET A O   1 
ATOM   1154 C  CB  . MET A 1 139 ? -7.887  12.059  -5.886  1.00 39.30 ? 148 MET A CB  1 
ATOM   1155 C  CG  . MET A 1 139 ? -8.378  11.346  -4.627  1.00 43.41 ? 148 MET A CG  1 
ATOM   1156 S  SD  . MET A 1 139 ? -10.049 10.718  -4.799  1.00 43.22 ? 148 MET A SD  1 
ATOM   1157 C  CE  . MET A 1 139 ? -9.672  9.138   -5.549  1.00 41.76 ? 148 MET A CE  1 
ATOM   1158 N  N   A ASP A 1 140 ? -5.255  12.320  -7.601  0.50 39.31 ? 149 ASP A N   1 
ATOM   1159 N  N   B ASP A 1 140 ? -5.244  12.313  -7.585  0.50 39.24 ? 149 ASP A N   1 
ATOM   1160 C  CA  A ASP A 1 140 ? -4.808  12.431  -8.989  0.50 38.31 ? 149 ASP A CA  1 
ATOM   1161 C  CA  B ASP A 1 140 ? -4.686  12.405  -8.940  0.50 38.34 ? 149 ASP A CA  1 
ATOM   1162 C  C   A ASP A 1 140 ? -4.826  11.062  -9.665  0.50 36.23 ? 149 ASP A C   1 
ATOM   1163 C  C   B ASP A 1 140 ? -4.847  11.055  -9.660  0.50 36.03 ? 149 ASP A C   1 
ATOM   1164 O  O   A ASP A 1 140 ? -4.879  10.023  -9.002  0.50 35.55 ? 149 ASP A O   1 
ATOM   1165 O  O   B ASP A 1 140 ? -5.033  10.020  -9.017  0.50 34.78 ? 149 ASP A O   1 
ATOM   1166 C  CB  A ASP A 1 140 ? -3.408  13.056  -9.073  0.50 39.83 ? 149 ASP A CB  1 
ATOM   1167 C  CB  B ASP A 1 140 ? -3.193  12.786  -8.881  0.50 39.67 ? 149 ASP A CB  1 
ATOM   1168 C  CG  A ASP A 1 140 ? -3.230  13.937  -10.311 0.50 38.71 ? 149 ASP A CG  1 
ATOM   1169 C  CG  B ASP A 1 140 ? -2.960  14.292  -8.764  0.50 41.44 ? 149 ASP A CG  1 
ATOM   1170 O  OD1 A ASP A 1 140 ? -3.691  13.549  -11.419 0.50 30.51 ? 149 ASP A OD1 1 
ATOM   1171 O  OD1 B ASP A 1 140 ? -3.553  15.064  -9.553  0.50 40.35 ? 149 ASP A OD1 1 
ATOM   1172 O  OD2 A ASP A 1 140 ? -2.627  15.024  -10.164 0.50 39.03 ? 149 ASP A OD2 1 
ATOM   1173 O  OD2 B ASP A 1 140 ? -2.161  14.706  -7.896  0.50 39.60 ? 149 ASP A OD2 1 
ATOM   1174 N  N   . VAL A 1 141 ? -4.795  11.076  -10.992 1.00 35.73 ? 150 VAL A N   1 
ATOM   1175 C  CA  . VAL A 1 141 ? -4.675  9.835   -11.778 1.00 34.30 ? 150 VAL A CA  1 
ATOM   1176 C  C   . VAL A 1 141 ? -3.197  9.487   -11.857 1.00 34.87 ? 150 VAL A C   1 
ATOM   1177 O  O   . VAL A 1 141 ? -2.337  10.315  -11.541 1.00 34.72 ? 150 VAL A O   1 
ATOM   1178 C  CB  . VAL A 1 141 ? -5.335  9.897   -13.187 1.00 32.33 ? 150 VAL A CB  1 
ATOM   1179 C  CG1 . VAL A 1 141 ? -6.825  10.091  -13.042 1.00 35.08 ? 150 VAL A CG1 1 
ATOM   1180 C  CG2 . VAL A 1 141 ? -4.716  10.983  -14.099 1.00 37.99 ? 150 VAL A CG2 1 
ATOM   1181 N  N   . LEU A 1 142 ? -2.907  8.254   -12.246 1.00 33.54 ? 151 LEU A N   1 
ATOM   1182 C  CA  . LEU A 1 142 ? -1.526  7.832   -12.450 1.00 34.23 ? 151 LEU A CA  1 
ATOM   1183 C  C   . LEU A 1 142 ? -1.112  8.093   -13.888 1.00 33.47 ? 151 LEU A C   1 
ATOM   1184 O  O   . LEU A 1 142 ? 0.014   8.512   -14.127 1.00 33.31 ? 151 LEU A O   1 
ATOM   1185 C  CB  . LEU A 1 142 ? -1.334  6.359   -12.072 1.00 33.85 ? 151 LEU A CB  1 
ATOM   1186 C  CG  . LEU A 1 142 ? -1.812  5.969   -10.667 1.00 33.12 ? 151 LEU A CG  1 
ATOM   1187 C  CD1 . LEU A 1 142 ? -1.406  4.539   -10.373 1.00 35.28 ? 151 LEU A CD1 1 
ATOM   1188 C  CD2 . LEU A 1 142 ? -1.272  6.910   -9.590  1.00 37.44 ? 151 LEU A CD2 1 
ATOM   1189 N  N   . PHE A 1 143 ? -2.020  7.860   -14.841 1.00 32.64 ? 152 PHE A N   1 
ATOM   1190 C  CA  . PHE A 1 143 ? -1.705  8.047   -16.254 1.00 32.47 ? 152 PHE A CA  1 
ATOM   1191 C  C   . PHE A 1 143 ? -2.772  8.828   -17.037 1.00 31.13 ? 152 PHE A C   1 
ATOM   1192 O  O   . PHE A 1 143 ? -3.960  8.743   -16.737 1.00 28.36 ? 152 PHE A O   1 
ATOM   1193 C  CB  . PHE A 1 143 ? -1.417  6.695   -16.919 1.00 32.41 ? 152 PHE A CB  1 
ATOM   1194 C  CG  . PHE A 1 143 ? -0.364  5.908   -16.212 1.00 31.97 ? 152 PHE A CG  1 
ATOM   1195 C  CD1 . PHE A 1 143 ? 0.986   6.154   -16.452 1.00 36.67 ? 152 PHE A CD1 1 
ATOM   1196 C  CD2 . PHE A 1 143 ? -0.717  4.970   -15.249 1.00 34.74 ? 152 PHE A CD2 1 
ATOM   1197 C  CE1 . PHE A 1 143 ? 1.977   5.441   -15.765 1.00 37.86 ? 152 PHE A CE1 1 
ATOM   1198 C  CE2 . PHE A 1 143 ? 0.257   4.253   -14.548 1.00 35.64 ? 152 PHE A CE2 1 
ATOM   1199 C  CZ  . PHE A 1 143 ? 1.607   4.486   -14.806 1.00 37.62 ? 152 PHE A CZ  1 
ATOM   1200 N  N   A SER A 1 144 ? -2.298  9.572   -18.036 0.50 31.04 ? 153 SER A N   1 
ATOM   1201 N  N   B SER A 1 144 ? -2.300  9.614   -18.006 0.50 31.09 ? 153 SER A N   1 
ATOM   1202 C  CA  A SER A 1 144 ? -3.119  10.317  -18.983 0.50 31.27 ? 153 SER A CA  1 
ATOM   1203 C  CA  B SER A 1 144 ? -3.128  10.316  -18.985 0.50 31.34 ? 153 SER A CA  1 
ATOM   1204 C  C   A SER A 1 144 ? -2.542  10.125  -20.388 0.50 31.12 ? 153 SER A C   1 
ATOM   1205 C  C   B SER A 1 144 ? -2.588  10.019  -20.387 0.50 31.11 ? 153 SER A C   1 
ATOM   1206 O  O   A SER A 1 144 ? -1.381  9.746   -20.531 0.50 32.54 ? 153 SER A O   1 
ATOM   1207 O  O   B SER A 1 144 ? -1.507  9.444   -20.525 0.50 32.34 ? 153 SER A O   1 
ATOM   1208 C  CB  A SER A 1 144 ? -3.098  11.798  -18.622 0.50 32.31 ? 153 SER A CB  1 
ATOM   1209 C  CB  B SER A 1 144 ? -3.084  11.824  -18.733 0.50 32.51 ? 153 SER A CB  1 
ATOM   1210 O  OG  A SER A 1 144 ? -3.621  12.007  -17.325 0.50 30.91 ? 153 SER A OG  1 
ATOM   1211 O  OG  B SER A 1 144 ? -1.794  12.355  -18.987 0.50 32.15 ? 153 SER A OG  1 
ATOM   1212 N  N   . PHE A 1 145 ? -3.345  10.404  -21.413 1.00 30.23 ? 154 PHE A N   1 
ATOM   1213 C  CA  . PHE A 1 145 ? -2.933  10.210  -22.819 1.00 30.40 ? 154 PHE A CA  1 
ATOM   1214 C  C   . PHE A 1 145 ? -2.295  11.451  -23.448 1.00 31.44 ? 154 PHE A C   1 
ATOM   1215 O  O   . PHE A 1 145 ? -1.199  11.367  -24.003 1.00 33.68 ? 154 PHE A O   1 
ATOM   1216 C  CB  . PHE A 1 145 ? -4.129  9.730   -23.657 1.00 29.83 ? 154 PHE A CB  1 
ATOM   1217 C  CG  . PHE A 1 145 ? -4.653  8.397   -23.214 1.00 27.16 ? 154 PHE A CG  1 
ATOM   1218 C  CD1 . PHE A 1 145 ? -3.945  7.235   -23.505 1.00 31.94 ? 154 PHE A CD1 1 
ATOM   1219 C  CD2 . PHE A 1 145 ? -5.805  8.304   -22.442 1.00 28.20 ? 154 PHE A CD2 1 
ATOM   1220 C  CE1 . PHE A 1 145 ? -4.395  5.992   -23.066 1.00 29.99 ? 154 PHE A CE1 1 
ATOM   1221 C  CE2 . PHE A 1 145 ? -6.268  7.060   -21.994 1.00 30.19 ? 154 PHE A CE2 1 
ATOM   1222 C  CZ  . PHE A 1 145 ? -5.554  5.905   -22.308 1.00 30.21 ? 154 PHE A CZ  1 
ATOM   1223 N  N   . ARG A 1 146 ? -2.996  12.578  -23.368 1.00 30.67 ? 155 ARG A N   1 
ATOM   1224 C  CA  . ARG A 1 146 ? -2.586  13.844  -23.973 1.00 33.10 ? 155 ARG A CA  1 
ATOM   1225 C  C   . ARG A 1 146 ? -2.811  14.989  -22.985 1.00 35.30 ? 155 ARG A C   1 
ATOM   1226 O  O   . ARG A 1 146 ? -3.665  14.895  -22.098 1.00 33.45 ? 155 ARG A O   1 
ATOM   1227 C  CB  . ARG A 1 146 ? -3.408  14.135  -25.237 1.00 33.52 ? 155 ARG A CB  1 
ATOM   1228 C  CG  . ARG A 1 146 ? -3.448  13.028  -26.296 1.00 34.17 ? 155 ARG A CG  1 
ATOM   1229 C  CD  . ARG A 1 146 ? -2.066  12.709  -26.862 1.00 33.14 ? 155 ARG A CD  1 
ATOM   1230 N  NE  . ARG A 1 146 ? -1.442  13.855  -27.511 1.00 36.26 ? 155 ARG A NE  1 
ATOM   1231 C  CZ  . ARG A 1 146 ? -1.673  14.252  -28.762 1.00 34.31 ? 155 ARG A CZ  1 
ATOM   1232 N  NH1 . ARG A 1 146 ? -2.526  13.608  -29.552 1.00 34.45 ? 155 ARG A NH1 1 
ATOM   1233 N  NH2 . ARG A 1 146 ? -1.029  15.309  -29.232 1.00 37.07 ? 155 ARG A NH2 1 
ATOM   1234 N  N   . ASP A 1 147 ? -2.064  16.076  -23.156 1.00 37.76 ? 156 ASP A N   1 
ATOM   1235 C  CA  . ASP A 1 147 ? -2.304  17.290  -22.382 1.00 39.44 ? 156 ASP A CA  1 
ATOM   1236 C  C   . ASP A 1 147 ? -3.654  17.879  -22.790 1.00 39.83 ? 156 ASP A C   1 
ATOM   1237 O  O   . ASP A 1 147 ? -3.989  17.934  -23.981 1.00 40.05 ? 156 ASP A O   1 
ATOM   1238 C  CB  . ASP A 1 147 ? -1.176  18.313  -22.583 1.00 42.58 ? 156 ASP A CB  1 
ATOM   1239 C  CG  . ASP A 1 147 ? 0.155   17.849  -21.989 1.00 46.08 ? 156 ASP A CG  1 
ATOM   1240 O  OD1 . ASP A 1 147 ? 0.159   16.998  -21.065 1.00 42.96 ? 156 ASP A OD1 1 
ATOM   1241 O  OD2 . ASP A 1 147 ? 1.204   18.340  -22.454 1.00 49.04 ? 156 ASP A OD2 1 
ATOM   1242 N  N   . GLY A 1 148 ? -4.437  18.279  -21.791 1.00 38.29 ? 157 GLY A N   1 
ATOM   1243 C  CA  . GLY A 1 148 ? -5.790  18.769  -22.017 1.00 38.31 ? 157 GLY A CA  1 
ATOM   1244 C  C   . GLY A 1 148 ? -6.846  17.726  -22.363 1.00 35.71 ? 157 GLY A C   1 
ATOM   1245 O  O   . GLY A 1 148 ? -7.970  18.102  -22.692 1.00 35.50 ? 157 GLY A O   1 
ATOM   1246 N  N   . ASP A 1 149 ? -6.515  16.432  -22.279 1.00 34.69 ? 158 ASP A N   1 
ATOM   1247 C  CA  . ASP A 1 149 ? -7.496  15.355  -22.538 1.00 33.07 ? 158 ASP A CA  1 
ATOM   1248 C  C   . ASP A 1 149 ? -8.603  15.193  -21.464 1.00 32.73 ? 158 ASP A C   1 
ATOM   1249 O  O   . ASP A 1 149 ? -9.563  14.440  -21.679 1.00 31.97 ? 158 ASP A O   1 
ATOM   1250 C  CB  . ASP A 1 149 ? -6.803  13.997  -22.833 1.00 31.86 ? 158 ASP A CB  1 
ATOM   1251 C  CG  . ASP A 1 149 ? -6.128  13.350  -21.609 1.00 30.81 ? 158 ASP A CG  1 
ATOM   1252 O  OD1 . ASP A 1 149 ? -6.124  13.914  -20.498 1.00 33.51 ? 158 ASP A OD1 1 
ATOM   1253 O  OD2 . ASP A 1 149 ? -5.559  12.247  -21.786 1.00 28.33 ? 158 ASP A OD2 1 
ATOM   1254 N  N   . CYS A 1 150 ? -8.457  15.882  -20.326 1.00 31.03 ? 159 CYS A N   1 
ATOM   1255 C  CA  . CYS A 1 150 ? -9.408  15.845  -19.210 1.00 32.11 ? 159 CYS A CA  1 
ATOM   1256 C  C   . CYS A 1 150 ? -9.566  14.449  -18.602 1.00 32.05 ? 159 CYS A C   1 
ATOM   1257 O  O   . CYS A 1 150 ? -10.614 14.124  -18.043 1.00 33.77 ? 159 CYS A O   1 
ATOM   1258 C  CB  . CYS A 1 150 ? -10.772 16.436  -19.608 1.00 31.91 ? 159 CYS A CB  1 
ATOM   1259 S  SG  . CYS A 1 150 ? -10.716 18.185  -19.891 1.00 37.25 ? 159 CYS A SG  1 
ATOM   1260 N  N   . SER A 1 151 ? -8.507  13.646  -18.679 1.00 31.44 ? 160 SER A N   1 
ATOM   1261 C  CA  . SER A 1 151 ? -8.528  12.281  -18.152 1.00 29.73 ? 160 SER A CA  1 
ATOM   1262 C  C   . SER A 1 151 ? -8.567  12.266  -16.626 1.00 28.21 ? 160 SER A C   1 
ATOM   1263 O  O   . SER A 1 151 ? -9.213  11.395  -16.054 1.00 26.07 ? 160 SER A O   1 
ATOM   1264 C  CB  . SER A 1 151 ? -7.325  11.478  -18.655 1.00 30.13 ? 160 SER A CB  1 
ATOM   1265 O  OG  . SER A 1 151 ? -6.132  12.173  -18.387 1.00 33.03 ? 160 SER A OG  1 
ATOM   1266 N  N   . LYS A 1 152 ? -7.882  13.212  -15.973 1.00 28.85 ? 161 LYS A N   1 
ATOM   1267 C  CA  . LYS A 1 152 ? -8.007  13.375  -14.520 1.00 30.94 ? 161 LYS A CA  1 
ATOM   1268 C  C   . LYS A 1 152 ? -9.478  13.541  -14.132 1.00 30.79 ? 161 LYS A C   1 
ATOM   1269 O  O   . LYS A 1 152 ? -9.999  12.768  -13.331 1.00 32.63 ? 161 LYS A O   1 
ATOM   1270 C  CB  . LYS A 1 152 ? -7.189  14.563  -13.992 1.00 33.26 ? 161 LYS A CB  1 
ATOM   1271 C  CG  . LYS A 1 152 ? -7.275  14.714  -12.469 1.00 35.80 ? 161 LYS A CG  1 
ATOM   1272 C  CD  . LYS A 1 152 ? -6.367  15.798  -11.895 1.00 38.93 ? 161 LYS A CD  1 
ATOM   1273 C  CE  . LYS A 1 152 ? -6.670  15.979  -10.422 1.00 40.81 ? 161 LYS A CE  1 
ATOM   1274 N  NZ  . LYS A 1 152 ? -5.662  16.788  -9.698  1.00 45.15 ? 161 LYS A NZ  1 
ATOM   1275 N  N   . GLY A 1 153 ? -10.138 14.540  -14.716 1.00 29.86 ? 162 GLY A N   1 
ATOM   1276 C  CA  . GLY A 1 153 ? -11.537 14.829  -14.413 1.00 29.85 ? 162 GLY A CA  1 
ATOM   1277 C  C   . GLY A 1 153 ? -12.464 13.667  -14.729 1.00 28.08 ? 162 GLY A C   1 
ATOM   1278 O  O   . GLY A 1 153 ? -13.343 13.323  -13.939 1.00 25.08 ? 162 GLY A O   1 
ATOM   1279 N  N   . PHE A 1 154 ? -12.259 13.039  -15.880 1.00 28.46 ? 163 PHE A N   1 
ATOM   1280 C  CA  . PHE A 1 154 ? -13.107 11.927  -16.274 1.00 26.68 ? 163 PHE A CA  1 
ATOM   1281 C  C   . PHE A 1 154 ? -12.890 10.682  -15.404 1.00 28.55 ? 163 PHE A C   1 
ATOM   1282 O  O   . PHE A 1 154 ? -13.859 10.104  -14.877 1.00 28.35 ? 163 PHE A O   1 
ATOM   1283 C  CB  . PHE A 1 154 ? -12.892 11.586  -17.743 1.00 27.09 ? 163 PHE A CB  1 
ATOM   1284 C  CG  . PHE A 1 154 ? -13.749 10.460  -18.211 1.00 25.68 ? 163 PHE A CG  1 
ATOM   1285 C  CD1 . PHE A 1 154 ? -15.134 10.617  -18.265 1.00 26.13 ? 163 PHE A CD1 1 
ATOM   1286 C  CD2 . PHE A 1 154 ? -13.189 9.227   -18.556 1.00 26.67 ? 163 PHE A CD2 1 
ATOM   1287 C  CE1 . PHE A 1 154 ? -15.950 9.573   -18.673 1.00 25.39 ? 163 PHE A CE1 1 
ATOM   1288 C  CE2 . PHE A 1 154 ? -14.001 8.178   -18.975 1.00 25.83 ? 163 PHE A CE2 1 
ATOM   1289 C  CZ  . PHE A 1 154 ? -15.377 8.350   -19.024 1.00 24.89 ? 163 PHE A CZ  1 
ATOM   1290 N  N   . PHE A 1 155 ? -11.633 10.262  -15.263 1.00 28.59 ? 164 PHE A N   1 
ATOM   1291 C  CA  . PHE A 1 155 ? -11.329 9.052   -14.502 1.00 26.64 ? 164 PHE A CA  1 
ATOM   1292 C  C   . PHE A 1 155 ? -11.637 9.180   -13.015 1.00 27.71 ? 164 PHE A C   1 
ATOM   1293 O  O   . PHE A 1 155 ? -12.190 8.247   -12.425 1.00 25.27 ? 164 PHE A O   1 
ATOM   1294 C  CB  . PHE A 1 155 ? -9.872  8.604   -14.688 1.00 28.32 ? 164 PHE A CB  1 
ATOM   1295 C  CG  . PHE A 1 155 ? -9.524  8.123   -16.088 1.00 27.08 ? 164 PHE A CG  1 
ATOM   1296 C  CD1 . PHE A 1 155 ? -10.433 7.398   -16.878 1.00 28.19 ? 164 PHE A CD1 1 
ATOM   1297 C  CD2 . PHE A 1 155 ? -8.244  8.344   -16.597 1.00 26.48 ? 164 PHE A CD2 1 
ATOM   1298 C  CE1 . PHE A 1 155 ? -10.080 6.959   -18.153 1.00 21.80 ? 164 PHE A CE1 1 
ATOM   1299 C  CE2 . PHE A 1 155 ? -7.885  7.886   -17.873 1.00 23.96 ? 164 PHE A CE2 1 
ATOM   1300 C  CZ  . PHE A 1 155 ? -8.804  7.203   -18.646 1.00 24.72 ? 164 PHE A CZ  1 
ATOM   1301 N  N   . LEU A 1 156 ? -11.301 10.325  -12.414 1.00 28.13 ? 165 LEU A N   1 
ATOM   1302 C  CA  . LEU A 1 156 ? -11.502 10.510  -10.972 1.00 29.48 ? 165 LEU A CA  1 
ATOM   1303 C  C   . LEU A 1 156 ? -12.955 10.706  -10.573 1.00 29.33 ? 165 LEU A C   1 
ATOM   1304 O  O   . LEU A 1 156 ? -13.387 10.167  -9.555  1.00 29.38 ? 165 LEU A O   1 
ATOM   1305 C  CB  . LEU A 1 156 ? -10.656 11.660  -10.406 1.00 32.49 ? 165 LEU A CB  1 
ATOM   1306 C  CG  . LEU A 1 156 ? -9.144  11.448  -10.300 1.00 34.07 ? 165 LEU A CG  1 
ATOM   1307 C  CD1 . LEU A 1 156 ? -8.531  12.632  -9.562  1.00 36.77 ? 165 LEU A CD1 1 
ATOM   1308 C  CD2 . LEU A 1 156 ? -8.773  10.135  -9.592  1.00 36.81 ? 165 LEU A CD2 1 
ATOM   1309 N  N   . VAL A 1 157 ? -13.703 11.483  -11.349 1.00 29.18 ? 166 VAL A N   1 
ATOM   1310 C  CA  . VAL A 1 157 ? -15.137 11.617  -11.106 1.00 29.18 ? 166 VAL A CA  1 
ATOM   1311 C  C   . VAL A 1 157 ? -15.818 10.255  -11.273 1.00 28.08 ? 166 VAL A C   1 
ATOM   1312 O  O   . VAL A 1 157 ? -16.657 9.909   -10.460 1.00 29.37 ? 166 VAL A O   1 
ATOM   1313 C  CB  . VAL A 1 157 ? -15.812 12.707  -11.983 1.00 29.77 ? 166 VAL A CB  1 
ATOM   1314 C  CG1 . VAL A 1 157 ? -17.330 12.734  -11.762 1.00 29.19 ? 166 VAL A CG1 1 
ATOM   1315 C  CG2 . VAL A 1 157 ? -15.237 14.078  -11.650 1.00 29.02 ? 166 VAL A CG2 1 
ATOM   1316 N  N   . SER A 1 158 ? -15.448 9.495   -12.306 1.00 28.43 ? 167 SER A N   1 
ATOM   1317 C  CA  . SER A 1 158 ? -15.939 8.120   -12.483 1.00 26.31 ? 167 SER A CA  1 
ATOM   1318 C  C   . SER A 1 158 ? -15.638 7.278   -11.247 1.00 27.58 ? 167 SER A C   1 
ATOM   1319 O  O   . SER A 1 158 ? -16.520 6.582   -10.723 1.00 25.80 ? 167 SER A O   1 
ATOM   1320 C  CB  . SER A 1 158 ? -15.307 7.458   -13.704 1.00 25.82 ? 167 SER A CB  1 
ATOM   1321 O  OG  . SER A 1 158 ? -15.748 8.048   -14.917 1.00 23.16 ? 167 SER A OG  1 
ATOM   1322 N  N   . LEU A 1 159 ? -14.396 7.362   -10.777 1.00 27.07 ? 168 LEU A N   1 
ATOM   1323 C  CA  . LEU A 1 159 ? -13.986 6.660   -9.566  1.00 28.64 ? 168 LEU A CA  1 
ATOM   1324 C  C   . LEU A 1 159 ? -14.805 7.054   -8.337  1.00 31.05 ? 168 LEU A C   1 
ATOM   1325 O  O   . LEU A 1 159 ? -15.219 6.190   -7.566  1.00 29.99 ? 168 LEU A O   1 
ATOM   1326 C  CB  . LEU A 1 159 ? -12.508 6.892   -9.275  1.00 29.21 ? 168 LEU A CB  1 
ATOM   1327 C  CG  . LEU A 1 159 ? -11.941 6.214   -8.028  1.00 30.70 ? 168 LEU A CG  1 
ATOM   1328 C  CD1 . LEU A 1 159 ? -12.056 4.693   -8.108  1.00 33.89 ? 168 LEU A CD1 1 
ATOM   1329 C  CD2 . LEU A 1 159 ? -10.509 6.639   -7.856  1.00 33.23 ? 168 LEU A CD2 1 
ATOM   1330 N  N   . LEU A 1 160 ? -15.021 8.353   -8.148  1.00 31.52 ? 169 LEU A N   1 
ATOM   1331 C  CA  . LEU A 1 160 ? -15.756 8.829   -6.973  1.00 31.95 ? 169 LEU A CA  1 
ATOM   1332 C  C   . LEU A 1 160 ? -17.223 8.405   -6.988  1.00 29.28 ? 169 LEU A C   1 
ATOM   1333 O  O   . LEU A 1 160 ? -17.783 8.114   -5.943  1.00 29.83 ? 169 LEU A O   1 
ATOM   1334 C  CB  . LEU A 1 160 ? -15.649 10.347  -6.839  1.00 33.49 ? 169 LEU A CB  1 
ATOM   1335 C  CG  . LEU A 1 160 ? -14.262 10.871  -6.473  1.00 34.64 ? 169 LEU A CG  1 
ATOM   1336 C  CD1 . LEU A 1 160 ? -14.158 12.361  -6.798  1.00 42.29 ? 169 LEU A CD1 1 
ATOM   1337 C  CD2 . LEU A 1 160 ? -13.944 10.598  -5.011  1.00 38.19 ? 169 LEU A CD2 1 
ATOM   1338 N  N   . VAL A 1 161 ? -17.832 8.394   -8.170  1.00 29.35 ? 170 VAL A N   1 
ATOM   1339 C  CA  . VAL A 1 161 ? -19.213 7.931   -8.338  1.00 30.83 ? 170 VAL A CA  1 
ATOM   1340 C  C   . VAL A 1 161 ? -19.297 6.443   -7.976  1.00 30.76 ? 170 VAL A C   1 
ATOM   1341 O  O   . VAL A 1 161 ? -20.190 6.013   -7.237  1.00 29.56 ? 170 VAL A O   1 
ATOM   1342 C  CB  . VAL A 1 161 ? -19.729 8.160   -9.781  1.00 26.59 ? 170 VAL A CB  1 
ATOM   1343 C  CG1 . VAL A 1 161 ? -21.117 7.563   -9.957  1.00 30.89 ? 170 VAL A CG1 1 
ATOM   1344 C  CG2 . VAL A 1 161 ? -19.788 9.646   -10.110 1.00 30.61 ? 170 VAL A CG2 1 
ATOM   1345 N  N   . GLU A 1 162 ? -18.353 5.673   -8.511  1.00 31.72 ? 171 GLU A N   1 
ATOM   1346 C  CA  . GLU A 1 162 ? -18.186 4.256   -8.171  1.00 31.43 ? 171 GLU A CA  1 
ATOM   1347 C  C   . GLU A 1 162 ? -18.045 4.048   -6.657  1.00 33.56 ? 171 GLU A C   1 
ATOM   1348 O  O   . GLU A 1 162 ? -18.711 3.180   -6.078  1.00 32.77 ? 171 GLU A O   1 
ATOM   1349 C  CB  . GLU A 1 162 ? -16.961 3.712   -8.912  1.00 29.90 ? 171 GLU A CB  1 
ATOM   1350 C  CG  . GLU A 1 162 ? -16.508 2.308   -8.556  1.00 31.73 ? 171 GLU A CG  1 
ATOM   1351 C  CD  . GLU A 1 162 ? -17.074 1.214   -9.433  1.00 28.82 ? 171 GLU A CD  1 
ATOM   1352 O  OE1 . GLU A 1 162 ? -17.675 1.506   -10.492 1.00 26.66 ? 171 GLU A OE1 1 
ATOM   1353 O  OE2 . GLU A 1 162 ? -16.882 0.039   -9.052  1.00 30.89 ? 171 GLU A OE2 1 
ATOM   1354 N  N   . ILE A 1 163 ? -17.174 4.837   -6.028  1.00 34.18 ? 172 ILE A N   1 
ATOM   1355 C  CA  . ILE A 1 163 ? -16.929 4.716   -4.589  1.00 35.35 ? 172 ILE A CA  1 
ATOM   1356 C  C   . ILE A 1 163 ? -18.179 5.051   -3.761  1.00 35.71 ? 172 ILE A C   1 
ATOM   1357 O  O   . ILE A 1 163 ? -18.447 4.377   -2.766  1.00 36.14 ? 172 ILE A O   1 
ATOM   1358 C  CB  . ILE A 1 163 ? -15.710 5.562   -4.129  1.00 37.10 ? 172 ILE A CB  1 
ATOM   1359 C  CG1 . ILE A 1 163 ? -14.414 4.922   -4.638  1.00 36.39 ? 172 ILE A CG1 1 
ATOM   1360 C  CG2 . ILE A 1 163 ? -15.650 5.681   -2.590  1.00 37.61 ? 172 ILE A CG2 1 
ATOM   1361 C  CD1 . ILE A 1 163 ? -13.208 5.838   -4.581  1.00 37.10 ? 172 ILE A CD1 1 
ATOM   1362 N  N   . ALA A 1 164 ? -18.929 6.074   -4.171  1.00 32.60 ? 173 ALA A N   1 
ATOM   1363 C  CA  . ALA A 1 164 ? -20.173 6.445   -3.474  1.00 34.21 ? 173 ALA A CA  1 
ATOM   1364 C  C   . ALA A 1 164 ? -21.265 5.382   -3.630  1.00 32.58 ? 173 ALA A C   1 
ATOM   1365 O  O   . ALA A 1 164 ? -21.977 5.078   -2.676  1.00 33.28 ? 173 ALA A O   1 
ATOM   1366 C  CB  . ALA A 1 164 ? -20.679 7.793   -3.961  1.00 33.61 ? 173 ALA A CB  1 
ATOM   1367 N  N   . ALA A 1 165 ? -21.412 4.837   -4.835  1.00 33.59 ? 174 ALA A N   1 
ATOM   1368 C  CA  . ALA A 1 165 ? -22.328 3.709   -5.066  1.00 34.49 ? 174 ALA A CA  1 
ATOM   1369 C  C   . ALA A 1 165 ? -21.913 2.480   -4.238  1.00 37.11 ? 174 ALA A C   1 
ATOM   1370 O  O   . ALA A 1 165 ? -22.761 1.778   -3.690  1.00 38.89 ? 174 ALA A O   1 
ATOM   1371 C  CB  . ALA A 1 165 ? -22.399 3.363   -6.548  1.00 33.55 ? 174 ALA A CB  1 
ATOM   1372 N  N   . ALA A 1 166 ? -20.604 2.266   -4.119  1.00 38.71 ? 175 ALA A N   1 
ATOM   1373 C  CA  . ALA A 1 166 ? -20.037 1.101   -3.429  1.00 38.58 ? 175 ALA A CA  1 
ATOM   1374 C  C   . ALA A 1 166 ? -20.255 1.056   -1.922  1.00 41.27 ? 175 ALA A C   1 
ATOM   1375 O  O   . ALA A 1 166 ? -20.093 -0.007  -1.308  1.00 40.36 ? 175 ALA A O   1 
ATOM   1376 C  CB  . ALA A 1 166 ? -18.554 1.014   -3.712  1.00 39.07 ? 175 ALA A CB  1 
ATOM   1377 N  N   . SER A 1 167 ? -20.591 2.193   -1.315  1.00 41.80 ? 176 SER A N   1 
ATOM   1378 C  CA  . SER A 1 167 ? -20.941 2.216   0.104   1.00 43.32 ? 176 SER A CA  1 
ATOM   1379 C  C   . SER A 1 167 ? -22.167 1.355   0.449   1.00 41.84 ? 176 SER A C   1 
ATOM   1380 O  O   . SER A 1 167 ? -22.277 0.876   1.572   1.00 43.98 ? 176 SER A O   1 
ATOM   1381 C  CB  . SER A 1 167 ? -21.123 3.660   0.601   1.00 46.47 ? 176 SER A CB  1 
ATOM   1382 O  OG  . SER A 1 167 ? -22.049 4.369   -0.207  1.00 51.79 ? 176 SER A OG  1 
ATOM   1383 N  N   . ALA A 1 168 ? -23.064 1.150   -0.514  1.00 40.55 ? 177 ALA A N   1 
ATOM   1384 C  CA  . ALA A 1 168 ? -24.217 0.243   -0.355  1.00 42.00 ? 177 ALA A CA  1 
ATOM   1385 C  C   . ALA A 1 168 ? -23.909 -1.259  -0.553  1.00 41.66 ? 177 ALA A C   1 
ATOM   1386 O  O   . ALA A 1 168 ? -24.719 -2.098  -0.137  1.00 39.65 ? 177 ALA A O   1 
ATOM   1387 C  CB  . ALA A 1 168 ? -25.351 0.663   -1.281  1.00 41.52 ? 177 ALA A CB  1 
ATOM   1388 N  N   . ILE A 1 169 ? -22.768 -1.598  -1.166  1.00 38.89 ? 178 ILE A N   1 
ATOM   1389 C  CA  . ILE A 1 169 ? -22.380 -3.007  -1.392  1.00 40.25 ? 178 ILE A CA  1 
ATOM   1390 C  C   . ILE A 1 169 ? -22.380 -3.831  -0.097  1.00 42.65 ? 178 ILE A C   1 
ATOM   1391 O  O   . ILE A 1 169 ? -22.858 -4.963  -0.085  1.00 43.37 ? 178 ILE A O   1 
ATOM   1392 C  CB  . ILE A 1 169 ? -20.990 -3.142  -2.095  1.00 39.92 ? 178 ILE A CB  1 
ATOM   1393 C  CG1 . ILE A 1 169 ? -21.049 -2.608  -3.529  1.00 35.38 ? 178 ILE A CG1 1 
ATOM   1394 C  CG2 . ILE A 1 169 ? -20.519 -4.605  -2.152  1.00 41.55 ? 178 ILE A CG2 1 
ATOM   1395 C  CD1 . ILE A 1 169 ? -19.664 -2.301  -4.082  0.00 37.34 ? 178 ILE A CD1 1 
ATOM   1396 N  N   . LYS A 1 170 ? -21.863 -3.252  0.984   1.00 43.84 ? 179 LYS A N   1 
ATOM   1397 C  CA  . LYS A 1 170 ? -21.829 -3.921  2.285   1.00 48.03 ? 179 LYS A CA  1 
ATOM   1398 C  C   . LYS A 1 170 ? -23.210 -4.200  2.915   1.00 48.94 ? 179 LYS A C   1 
ATOM   1399 O  O   . LYS A 1 170 ? -23.295 -4.956  3.877   1.00 49.43 ? 179 LYS A O   1 
ATOM   1400 C  CB  . LYS A 1 170 ? -20.940 -3.149  3.278   1.00 51.84 ? 179 LYS A CB  1 
ATOM   1401 C  CG  . LYS A 1 170 ? -21.373 -1.715  3.609   1.00 53.33 ? 179 LYS A CG  1 
ATOM   1402 C  CD  . LYS A 1 170 ? -20.263 -0.959  4.368   1.00 56.94 ? 179 LYS A CD  1 
ATOM   1403 C  CE  . LYS A 1 170 ? -20.064 0.481   3.877   1.00 58.69 ? 179 LYS A CE  1 
ATOM   1404 N  NZ  . LYS A 1 170 ? -21.158 1.400   4.312   1.00 59.12 ? 179 LYS A NZ  1 
ATOM   1405 N  N   . VAL A 1 171 ? -24.269 -3.601  2.368   1.00 47.74 ? 180 VAL A N   1 
ATOM   1406 C  CA  . VAL A 1 171 ? -25.648 -3.861  2.794   1.00 48.11 ? 180 VAL A CA  1 
ATOM   1407 C  C   . VAL A 1 171 ? -26.200 -5.153  2.154   1.00 47.47 ? 180 VAL A C   1 
ATOM   1408 O  O   . VAL A 1 171 ? -27.154 -5.738  2.662   1.00 48.26 ? 180 VAL A O   1 
ATOM   1409 C  CB  . VAL A 1 171 ? -26.576 -2.644  2.468   1.00 46.09 ? 180 VAL A CB  1 
ATOM   1410 C  CG1 . VAL A 1 171 ? -27.971 -2.840  3.032   1.00 48.49 ? 180 VAL A CG1 1 
ATOM   1411 C  CG2 . VAL A 1 171 ? -25.983 -1.342  3.022   1.00 45.85 ? 180 VAL A CG2 1 
ATOM   1412 N  N   . ILE A 1 172 ? -25.586 -5.610  1.065   1.00 47.08 ? 181 ILE A N   1 
ATOM   1413 C  CA  . ILE A 1 172 ? -26.086 -6.772  0.308   1.00 47.17 ? 181 ILE A CA  1 
ATOM   1414 C  C   . ILE A 1 172 ? -26.219 -8.076  1.117   1.00 49.12 ? 181 ILE A C   1 
ATOM   1415 O  O   . ILE A 1 172 ? -27.232 -8.763  0.982   1.00 50.04 ? 181 ILE A O   1 
ATOM   1416 C  CB  . ILE A 1 172 ? -25.271 -6.987  -1.006  1.00 46.76 ? 181 ILE A CB  1 
ATOM   1417 C  CG1 . ILE A 1 172 ? -25.602 -5.852  -1.979  1.00 42.86 ? 181 ILE A CG1 1 
ATOM   1418 C  CG2 . ILE A 1 172 ? -25.591 -8.349  -1.652  1.00 47.57 ? 181 ILE A CG2 1 
ATOM   1419 C  CD1 . ILE A 1 172 ? -24.704 -5.743  -3.173  1.00 43.01 ? 181 ILE A CD1 1 
ATOM   1420 N  N   . PRO A 1 173 ? -25.202 -8.438  1.930   1.00 50.10 ? 182 PRO A N   1 
ATOM   1421 C  CA  . PRO A 1 173 ? -25.368 -9.582  2.835   1.00 51.31 ? 182 PRO A CA  1 
ATOM   1422 C  C   . PRO A 1 173 ? -26.565 -9.456  3.783   1.00 52.61 ? 182 PRO A C   1 
ATOM   1423 O  O   . PRO A 1 173 ? -27.232 -10.454 4.049   1.00 53.73 ? 182 PRO A O   1 
ATOM   1424 C  CB  . PRO A 1 173 ? -24.060 -9.592  3.637   1.00 53.21 ? 182 PRO A CB  1 
ATOM   1425 C  CG  . PRO A 1 173 ? -23.082 -8.902  2.771   1.00 51.33 ? 182 PRO A CG  1 
ATOM   1426 C  CD  . PRO A 1 173 ? -23.850 -7.860  2.036   1.00 49.63 ? 182 PRO A CD  1 
ATOM   1427 N  N   . THR A 1 174 ? -26.803 -8.240  4.288   1.00 52.07 ? 183 THR A N   1 
ATOM   1428 C  CA  . THR A 1 174 ? -27.953 -7.927  5.147   1.00 51.13 ? 183 THR A CA  1 
ATOM   1429 C  C   . THR A 1 174 ? -29.278 -8.157  4.421   1.00 50.12 ? 183 THR A C   1 
ATOM   1430 O  O   . THR A 1 174 ? -30.225 -8.671  5.020   1.00 50.88 ? 183 THR A O   1 
ATOM   1431 C  CB  . THR A 1 174 ? -27.921 -6.458  5.628   1.00 51.12 ? 183 THR A CB  1 
ATOM   1432 O  OG1 . THR A 1 174 ? -26.614 -6.145  6.123   1.00 51.50 ? 183 THR A OG1 1 
ATOM   1433 C  CG2 . THR A 1 174 ? -28.963 -6.195  6.725   1.00 52.85 ? 183 THR A CG2 1 
ATOM   1434 N  N   . VAL A 1 175 ? -29.338 -7.770  3.145   1.00 46.05 ? 184 VAL A N   1 
ATOM   1435 C  CA  . VAL A 1 175 ? -30.552 -7.933  2.340   1.00 46.60 ? 184 VAL A CA  1 
ATOM   1436 C  C   . VAL A 1 175 ? -30.955 -9.405  2.272   1.00 47.49 ? 184 VAL A C   1 
ATOM   1437 O  O   . VAL A 1 175 ? -32.073 -9.764  2.661   1.00 45.59 ? 184 VAL A O   1 
ATOM   1438 C  CB  . VAL A 1 175 ? -30.381 -7.383  0.909   1.00 43.80 ? 184 VAL A CB  1 
ATOM   1439 C  CG1 . VAL A 1 175 ? -31.542 -7.819  -0.012  1.00 43.87 ? 184 VAL A CG1 1 
ATOM   1440 C  CG2 . VAL A 1 175 ? -30.267 -5.865  0.944   1.00 45.56 ? 184 VAL A CG2 1 
ATOM   1441 N  N   . PHE A 1 176 ? -30.035 -10.237 1.782   1.00 46.28 ? 185 PHE A N   1 
ATOM   1442 C  CA  . PHE A 1 176 ? -30.290 -11.674 1.629   1.00 48.33 ? 185 PHE A CA  1 
ATOM   1443 C  C   . PHE A 1 176 ? -30.508 -12.392 2.955   1.00 50.12 ? 185 PHE A C   1 
ATOM   1444 O  O   . PHE A 1 176 ? -31.318 -13.315 3.016   1.00 53.48 ? 185 PHE A O   1 
ATOM   1445 C  CB  . PHE A 1 176 ? -29.167 -12.357 0.838   1.00 48.75 ? 185 PHE A CB  1 
ATOM   1446 C  CG  . PHE A 1 176 ? -29.088 -11.910 -0.586  1.00 45.71 ? 185 PHE A CG  1 
ATOM   1447 C  CD1 . PHE A 1 176 ? -30.168 -12.099 -1.445  1.00 45.36 ? 185 PHE A CD1 1 
ATOM   1448 C  CD2 . PHE A 1 176 ? -27.943 -11.295 -1.075  1.00 47.68 ? 185 PHE A CD2 1 
ATOM   1449 C  CE1 . PHE A 1 176 ? -30.111 -11.674 -2.769  1.00 46.05 ? 185 PHE A CE1 1 
ATOM   1450 C  CE2 . PHE A 1 176 ? -27.872 -10.876 -2.401  1.00 45.83 ? 185 PHE A CE2 1 
ATOM   1451 C  CZ  . PHE A 1 176 ? -28.954 -11.057 -3.250  1.00 45.62 ? 185 PHE A CZ  1 
ATOM   1452 N  N   . LYS A 1 177 ? -29.780 -11.975 3.994   1.00 50.81 ? 186 LYS A N   1 
ATOM   1453 C  CA  . LYS A 1 177 ? -30.017 -12.447 5.363   1.00 54.27 ? 186 LYS A CA  1 
ATOM   1454 C  C   . LYS A 1 177 ? -31.447 -12.117 5.808   1.00 55.42 ? 186 LYS A C   1 
ATOM   1455 O  O   . LYS A 1 177 ? -32.162 -12.984 6.317   1.00 56.77 ? 186 LYS A O   1 
ATOM   1456 C  CB  . LYS A 1 177 ? -29.011 -11.819 6.341   1.00 56.02 ? 186 LYS A CB  1 
ATOM   1457 C  CG  . LYS A 1 177 ? -29.090 -12.352 7.773   1.00 57.07 ? 186 LYS A CG  1 
ATOM   1458 C  CD  . LYS A 1 177 ? -27.860 -11.962 8.581   0.00 59.18 ? 186 LYS A CD  1 
ATOM   1459 C  CE  . LYS A 1 177 ? -27.922 -12.523 9.992   0.00 62.10 ? 186 LYS A CE  1 
ATOM   1460 N  NZ  . LYS A 1 177 ? -26.730 -12.143 10.799  0.00 63.03 ? 186 LYS A NZ  1 
ATOM   1461 N  N   . ALA A 1 178 ? -31.852 -10.864 5.598   1.00 53.89 ? 187 ALA A N   1 
ATOM   1462 C  CA  . ALA A 1 178 ? -33.208 -10.409 5.930   1.00 54.24 ? 187 ALA A CA  1 
ATOM   1463 C  C   . ALA A 1 178 ? -34.320 -11.153 5.176   1.00 53.76 ? 187 ALA A C   1 
ATOM   1464 O  O   . ALA A 1 178 ? -35.388 -11.389 5.741   1.00 53.36 ? 187 ALA A O   1 
ATOM   1465 C  CB  . ALA A 1 178 ? -33.337 -8.907  5.721   1.00 52.40 ? 187 ALA A CB  1 
ATOM   1466 N  N   . MET A 1 179 ? -34.067 -11.534 3.925   1.00 52.35 ? 188 MET A N   1 
ATOM   1467 C  CA  . MET A 1 179 ? -35.043 -12.311 3.145   1.00 55.15 ? 188 MET A CA  1 
ATOM   1468 C  C   . MET A 1 179 ? -35.184 -13.745 3.648   1.00 58.01 ? 188 MET A C   1 
ATOM   1469 O  O   . MET A 1 179 ? -36.301 -14.209 3.889   1.00 57.54 ? 188 MET A O   1 
ATOM   1470 C  CB  . MET A 1 179 ? -34.679 -12.337 1.664   1.00 52.76 ? 188 MET A CB  1 
ATOM   1471 C  CG  . MET A 1 179 ? -35.091 -11.096 0.923   1.00 54.03 ? 188 MET A CG  1 
ATOM   1472 S  SD  . MET A 1 179 ? -34.390 -11.034 -0.726  1.00 54.75 ? 188 MET A SD  1 
ATOM   1473 C  CE  . MET A 1 179 ? -35.027 -12.522 -1.494  1.00 60.64 ? 188 MET A CE  1 
ATOM   1474 N  N   . GLN A 1 180 ? -34.051 -14.435 3.800   1.00 59.56 ? 189 GLN A N   1 
ATOM   1475 C  CA  . GLN A 1 180 ? -34.028 -15.825 4.292   1.00 61.77 ? 189 GLN A CA  1 
ATOM   1476 C  C   . GLN A 1 180 ? -34.597 -15.945 5.703   1.00 65.43 ? 189 GLN A C   1 
ATOM   1477 O  O   . GLN A 1 180 ? -35.370 -16.865 5.998   1.00 67.81 ? 189 GLN A O   1 
ATOM   1478 C  CB  . GLN A 1 180 ? -32.602 -16.393 4.264   1.00 62.69 ? 189 GLN A CB  1 
ATOM   1479 C  CG  . GLN A 1 180 ? -32.569 -17.941 4.323   0.00 64.24 ? 189 GLN A CG  1 
ATOM   1480 C  CD  . GLN A 1 180 ? -31.159 -18.508 4.229   0.00 64.43 ? 189 GLN A CD  1 
ATOM   1481 O  OE1 . GLN A 1 180 ? -30.278 -17.930 3.589   0.00 62.74 ? 189 GLN A OE1 1 
ATOM   1482 N  NE2 . GLN A 1 180 ? -30.944 -19.655 4.863   0.00 66.54 ? 189 GLN A NE2 1 
ATOM   1483 N  N   . MET A 1 181 ? -34.225 -14.999 6.564   1.00 65.01 ? 190 MET A N   1 
ATOM   1484 C  CA  . MET A 1 181 ? -34.735 -14.945 7.934   1.00 66.29 ? 190 MET A CA  1 
ATOM   1485 C  C   . MET A 1 181 ? -36.145 -14.351 8.048   1.00 65.56 ? 190 MET A C   1 
ATOM   1486 O  O   . MET A 1 181 ? -36.682 -14.295 9.157   1.00 68.47 ? 190 MET A O   1 
ATOM   1487 C  CB  . MET A 1 181 ? -33.775 -14.139 8.825   1.00 67.88 ? 190 MET A CB  1 
ATOM   1488 C  CG  . MET A 1 181 ? -32.365 -14.715 8.931   1.00 72.31 ? 190 MET A CG  1 
ATOM   1489 S  SD  . MET A 1 181 ? -32.317 -16.247 9.866   1.00 85.39 ? 190 MET A SD  1 
ATOM   1490 C  CE  . MET A 1 181 ? -32.342 -17.519 8.567   0.00 82.66 ? 190 MET A CE  1 
ATOM   1491 N  N   . GLN A 1 182 ? -36.739 -13.922 6.926   1.00 63.29 ? 191 GLN A N   1 
ATOM   1492 C  CA  . GLN A 1 182 ? -38.031 -13.225 6.907   1.00 62.72 ? 191 GLN A CA  1 
ATOM   1493 C  C   . GLN A 1 182 ? -37.998 -12.073 7.910   1.00 62.42 ? 191 GLN A C   1 
ATOM   1494 O  O   . GLN A 1 182 ? -38.744 -12.068 8.878   1.00 64.89 ? 191 GLN A O   1 
ATOM   1495 C  CB  . GLN A 1 182 ? -39.199 -14.196 7.202   1.00 64.97 ? 191 GLN A CB  1 
ATOM   1496 C  CG  . GLN A 1 182 ? -39.621 -15.100 6.036   1.00 66.16 ? 191 GLN A CG  1 
ATOM   1497 C  CD  . GLN A 1 182 ? -40.386 -14.379 4.922   1.00 67.28 ? 191 GLN A CD  1 
ATOM   1498 O  OE1 . GLN A 1 182 ? -40.415 -14.849 3.785   1.00 66.59 ? 191 GLN A OE1 1 
ATOM   1499 N  NE2 . GLN A 1 182 ? -41.013 -13.248 5.244   1.00 69.98 ? 191 GLN A NE2 1 
ATOM   1500 N  N   . GLU A 1 183 ? -37.075 -11.139 7.702   1.00 59.16 ? 192 GLU A N   1 
ATOM   1501 C  CA  . GLU A 1 183 ? -36.927 -9.964  8.561   1.00 58.36 ? 192 GLU A CA  1 
ATOM   1502 C  C   . GLU A 1 183 ? -37.335 -8.732  7.753   1.00 55.08 ? 192 GLU A C   1 
ATOM   1503 O  O   . GLU A 1 183 ? -36.507 -8.114  7.075   1.00 51.16 ? 192 GLU A O   1 
ATOM   1504 C  CB  . GLU A 1 183 ? -35.490 -9.843  9.082   1.00 59.46 ? 192 GLU A CB  1 
ATOM   1505 C  CG  . GLU A 1 183 ? -35.042 -10.982 10.016  1.00 64.17 ? 192 GLU A CG  1 
ATOM   1506 C  CD  . GLU A 1 183 ? -35.610 -10.889 11.430  1.00 69.77 ? 192 GLU A CD  1 
ATOM   1507 O  OE1 . GLU A 1 183 ? -35.647 -9.779  12.006  1.00 72.55 ? 192 GLU A OE1 1 
ATOM   1508 O  OE2 . GLU A 1 183 ? -36.002 -11.940 11.982  1.00 78.34 ? 192 GLU A OE2 1 
ATOM   1509 N  N   . ARG A 1 184 ? -38.627 -8.408  7.825   1.00 53.63 ? 193 ARG A N   1 
ATOM   1510 C  CA  . ARG A 1 184 ? -39.227 -7.267  7.116   1.00 51.10 ? 193 ARG A CA  1 
ATOM   1511 C  C   . ARG A 1 184 ? -38.568 -5.941  7.480   1.00 48.72 ? 193 ARG A C   1 
ATOM   1512 O  O   . ARG A 1 184 ? -38.281 -5.132  6.603   1.00 46.42 ? 193 ARG A O   1 
ATOM   1513 C  CB  . ARG A 1 184 ? -40.732 -7.192  7.433   1.00 53.51 ? 193 ARG A CB  1 
ATOM   1514 C  CG  . ARG A 1 184 ? -41.505 -6.064  6.740   1.00 50.59 ? 193 ARG A CG  1 
ATOM   1515 C  CD  . ARG A 1 184 ? -41.670 -4.807  7.610   1.00 50.68 ? 193 ARG A CD  1 
ATOM   1516 N  NE  . ARG A 1 184 ? -42.375 -3.741  6.894   1.00 49.84 ? 193 ARG A NE  1 
ATOM   1517 C  CZ  . ARG A 1 184 ? -42.545 -2.499  7.347   1.00 50.66 ? 193 ARG A CZ  1 
ATOM   1518 N  NH1 . ARG A 1 184 ? -42.034 -2.104  8.511   1.00 53.66 ? 193 ARG A NH1 1 
ATOM   1519 N  NH2 . ARG A 1 184 ? -43.210 -1.621  6.605   1.00 50.09 ? 193 ARG A NH2 1 
ATOM   1520 N  N   . ASP A 1 185 ? -38.355 -5.724  8.778   1.00 49.82 ? 194 ASP A N   1 
ATOM   1521 C  CA  . ASP A 1 185 ? -37.834 -4.446  9.276   1.00 49.79 ? 194 ASP A CA  1 
ATOM   1522 C  C   . ASP A 1 185 ? -36.372 -4.261  8.877   1.00 47.94 ? 194 ASP A C   1 
ATOM   1523 O  O   . ASP A 1 185 ? -35.991 -3.194  8.394   1.00 48.17 ? 194 ASP A O   1 
ATOM   1524 C  CB  . ASP A 1 185 ? -37.997 -4.333  10.799  1.00 50.95 ? 194 ASP A CB  1 
ATOM   1525 C  CG  . ASP A 1 185 ? -39.452 -4.489  11.261  1.00 52.37 ? 194 ASP A CG  1 
ATOM   1526 O  OD1 . ASP A 1 185 ? -40.375 -4.209  10.473  1.00 49.34 ? 194 ASP A OD1 1 
ATOM   1527 O  OD2 . ASP A 1 185 ? -39.672 -4.886  12.423  1.00 52.69 ? 194 ASP A OD2 1 
ATOM   1528 N  N   . THR A 1 186 ? -35.566 -5.306  9.061   1.00 47.35 ? 195 THR A N   1 
ATOM   1529 C  CA  . THR A 1 186 ? -34.161 -5.305  8.620   1.00 46.32 ? 195 THR A CA  1 
ATOM   1530 C  C   . THR A 1 186 ? -34.048 -5.026  7.122   1.00 42.50 ? 195 THR A C   1 
ATOM   1531 O  O   . THR A 1 186 ? -33.256 -4.179  6.704   1.00 40.68 ? 195 THR A O   1 
ATOM   1532 C  CB  . THR A 1 186 ? -33.469 -6.659  8.928   1.00 47.57 ? 195 THR A CB  1 
ATOM   1533 O  OG1 . THR A 1 186 ? -33.721 -7.028  10.290  1.00 50.05 ? 195 THR A OG1 1 
ATOM   1534 C  CG2 . THR A 1 186 ? -31.954 -6.581  8.685   1.00 45.73 ? 195 THR A CG2 1 
ATOM   1535 N  N   . LEU A 1 187 ? -34.846 -5.739  6.327   1.00 41.07 ? 196 LEU A N   1 
ATOM   1536 C  CA  . LEU A 1 187 ? -34.861 -5.552  4.872   1.00 39.94 ? 196 LEU A CA  1 
ATOM   1537 C  C   . LEU A 1 187 ? -35.264 -4.128  4.463   1.00 39.17 ? 196 LEU A C   1 
ATOM   1538 O  O   . LEU A 1 187 ? -34.644 -3.541  3.576   1.00 37.19 ? 196 LEU A O   1 
ATOM   1539 C  CB  . LEU A 1 187 ? -35.801 -6.562  4.200   1.00 38.56 ? 196 LEU A CB  1 
ATOM   1540 C  CG  . LEU A 1 187 ? -35.919 -6.487  2.675   1.00 36.85 ? 196 LEU A CG  1 
ATOM   1541 C  CD1 . LEU A 1 187 ? -34.580 -6.789  1.997   1.00 40.38 ? 196 LEU A CD1 1 
ATOM   1542 C  CD2 . LEU A 1 187 ? -36.993 -7.427  2.187   1.00 37.55 ? 196 LEU A CD2 1 
ATOM   1543 N  N   . LEU A 1 188 ? -36.314 -3.605  5.096   1.00 41.54 ? 197 LEU A N   1 
ATOM   1544 C  CA  . LEU A 1 188 ? -36.776 -2.236  4.851   1.00 41.46 ? 197 LEU A CA  1 
ATOM   1545 C  C   . LEU A 1 188 ? -35.638 -1.244  5.085   1.00 40.42 ? 197 LEU A C   1 
ATOM   1546 O  O   . LEU A 1 188 ? -35.313 -0.461  4.198   1.00 36.72 ? 197 LEU A O   1 
ATOM   1547 C  CB  . LEU A 1 188 ? -37.990 -1.907  5.733   1.00 41.89 ? 197 LEU A CB  1 
ATOM   1548 C  CG  . LEU A 1 188 ? -38.547 -0.478  5.792   1.00 45.24 ? 197 LEU A CG  1 
ATOM   1549 C  CD1 . LEU A 1 188 ? -38.739 0.127   4.437   1.00 45.43 ? 197 LEU A CD1 1 
ATOM   1550 C  CD2 . LEU A 1 188 ? -39.875 -0.469  6.541   1.00 49.41 ? 197 LEU A CD2 1 
ATOM   1551 N  N   . LYS A 1 189 ? -35.022 -1.308  6.267   1.00 43.60 ? 198 LYS A N   1 
ATOM   1552 C  CA  . LYS A 1 189 ? -33.851 -0.465  6.599   1.00 43.96 ? 198 LYS A CA  1 
ATOM   1553 C  C   . LYS A 1 189 ? -32.713 -0.609  5.562   1.00 40.95 ? 198 LYS A C   1 
ATOM   1554 O  O   . LYS A 1 189 ? -32.155 0.388   5.090   1.00 39.30 ? 198 LYS A O   1 
ATOM   1555 C  CB  . LYS A 1 189 ? -33.348 -0.795  8.021   1.00 46.72 ? 198 LYS A CB  1 
ATOM   1556 C  CG  . LYS A 1 189 ? -32.063 -0.071  8.445   1.00 47.57 ? 198 LYS A CG  1 
ATOM   1557 C  CD  . LYS A 1 189 ? -31.710 -0.357  9.892   1.00 50.55 ? 198 LYS A CD  1 
ATOM   1558 C  CE  . LYS A 1 189 ? -30.335 0.168   10.248  0.00 50.82 ? 198 LYS A CE  1 
ATOM   1559 N  NZ  . LYS A 1 189 ? -29.961 -0.146  11.655  0.00 53.27 ? 198 LYS A NZ  1 
ATOM   1560 N  N   . ALA A 1 190 ? -32.395 -1.852  5.203   1.00 40.61 ? 199 ALA A N   1 
ATOM   1561 C  CA  . ALA A 1 190 ? -31.343 -2.147  4.225   1.00 38.32 ? 199 ALA A CA  1 
ATOM   1562 C  C   . ALA A 1 190 ? -31.619 -1.503  2.863   1.00 38.27 ? 199 ALA A C   1 
ATOM   1563 O  O   . ALA A 1 190 ? -30.730 -0.868  2.272   1.00 36.01 ? 199 ALA A O   1 
ATOM   1564 C  CB  . ALA A 1 190 ? -31.164 -3.643  4.081   1.00 38.85 ? 199 ALA A CB  1 
ATOM   1565 N  N   . LEU A 1 191 ? -32.849 -1.647  2.373   1.00 39.43 ? 200 LEU A N   1 
ATOM   1566 C  CA  . LEU A 1 191 ? -33.235 -1.021  1.096   1.00 38.20 ? 200 LEU A CA  1 
ATOM   1567 C  C   . LEU A 1 191 ? -33.178 0.510   1.142   1.00 37.95 ? 200 LEU A C   1 
ATOM   1568 O  O   . LEU A 1 191 ? -32.772 1.130   0.175   1.00 37.06 ? 200 LEU A O   1 
ATOM   1569 C  CB  . LEU A 1 191 ? -34.625 -1.485  0.643   1.00 38.92 ? 200 LEU A CB  1 
ATOM   1570 C  CG  . LEU A 1 191 ? -34.788 -2.945  0.209   1.00 36.40 ? 200 LEU A CG  1 
ATOM   1571 C  CD1 . LEU A 1 191 ? -36.231 -3.187  -0.159  1.00 39.47 ? 200 LEU A CD1 1 
ATOM   1572 C  CD2 . LEU A 1 191 ? -33.891 -3.310  -0.950  1.00 37.59 ? 200 LEU A CD2 1 
ATOM   1573 N  N   . LEU A 1 192 ? -33.564 1.111   2.266   1.00 39.80 ? 201 LEU A N   1 
ATOM   1574 C  CA  . LEU A 1 192 ? -33.450 2.572   2.431   1.00 39.95 ? 201 LEU A CA  1 
ATOM   1575 C  C   . LEU A 1 192 ? -32.006 3.075   2.423   1.00 39.13 ? 201 LEU A C   1 
ATOM   1576 O  O   . LEU A 1 192 ? -31.736 4.152   1.898   1.00 38.34 ? 201 LEU A O   1 
ATOM   1577 C  CB  . LEU A 1 192 ? -34.174 3.043   3.696   1.00 40.36 ? 201 LEU A CB  1 
ATOM   1578 C  CG  . LEU A 1 192 ? -35.697 2.916   3.656   1.00 41.25 ? 201 LEU A CG  1 
ATOM   1579 C  CD1 . LEU A 1 192 ? -36.270 3.210   5.018   1.00 41.21 ? 201 LEU A CD1 1 
ATOM   1580 C  CD2 . LEU A 1 192 ? -36.330 3.837   2.610   1.00 39.39 ? 201 LEU A CD2 1 
ATOM   1581 N  N   . GLU A 1 193 ? -31.089 2.296   2.995   1.00 41.25 ? 202 GLU A N   1 
ATOM   1582 C  CA  . GLU A 1 193 ? -29.658 2.633   2.981   1.00 40.65 ? 202 GLU A CA  1 
ATOM   1583 C  C   . GLU A 1 193 ? -29.054 2.547   1.580   1.00 39.09 ? 202 GLU A C   1 
ATOM   1584 O  O   . GLU A 1 193 ? -28.188 3.351   1.227   1.00 37.24 ? 202 GLU A O   1 
ATOM   1585 C  CB  . GLU A 1 193 ? -28.881 1.735   3.956   1.00 43.65 ? 202 GLU A CB  1 
ATOM   1586 C  CG  . GLU A 1 193 ? -27.341 1.877   3.932   1.00 46.87 ? 202 GLU A CG  1 
ATOM   1587 C  CD  . GLU A 1 193 ? -26.821 3.272   4.275   1.00 52.80 ? 202 GLU A CD  1 
ATOM   1588 O  OE1 . GLU A 1 193 ? -27.539 4.065   4.922   1.00 57.20 ? 202 GLU A OE1 1 
ATOM   1589 O  OE2 . GLU A 1 193 ? -25.663 3.559   3.902   1.00 55.26 ? 202 GLU A OE2 1 
ATOM   1590 N  N   . ILE A 1 194 ? -29.499 1.567   0.796   1.00 38.72 ? 203 ILE A N   1 
ATOM   1591 C  CA  . ILE A 1 194 ? -29.066 1.427   -0.593  1.00 35.88 ? 203 ILE A CA  1 
ATOM   1592 C  C   . ILE A 1 194 ? -29.535 2.624   -1.429  1.00 36.67 ? 203 ILE A C   1 
ATOM   1593 O  O   . ILE A 1 194 ? -28.762 3.176   -2.211  1.00 33.95 ? 203 ILE A O   1 
ATOM   1594 C  CB  . ILE A 1 194 ? -29.572 0.086   -1.228  1.00 35.90 ? 203 ILE A CB  1 
ATOM   1595 C  CG1 . ILE A 1 194 ? -28.837 -1.103  -0.600  1.00 35.62 ? 203 ILE A CG1 1 
ATOM   1596 C  CG2 . ILE A 1 194 ? -29.372 0.079   -2.762  1.00 33.77 ? 203 ILE A CG2 1 
ATOM   1597 C  CD1 . ILE A 1 194 ? -29.514 -2.433  -0.794  1.00 36.30 ? 203 ILE A CD1 1 
ATOM   1598 N  N   . ALA A 1 195 ? -30.803 3.012   -1.279  1.00 38.07 ? 204 ALA A N   1 
ATOM   1599 C  CA  . ALA A 1 195 ? -31.319 4.180   -2.001  1.00 38.00 ? 204 ALA A CA  1 
ATOM   1600 C  C   . ALA A 1 195 ? -30.491 5.427   -1.655  1.00 38.69 ? 204 ALA A C   1 
ATOM   1601 O  O   . ALA A 1 195 ? -30.101 6.181   -2.551  1.00 38.31 ? 204 ALA A O   1 
ATOM   1602 C  CB  . ALA A 1 195 ? -32.785 4.398   -1.702  1.00 39.08 ? 204 ALA A CB  1 
ATOM   1603 N  N   . SER A 1 196 ? -30.182 5.598   -0.368  1.00 39.12 ? 205 SER A N   1 
ATOM   1604 C  CA  . SER A 1 196 ? -29.362 6.723   0.111   1.00 40.92 ? 205 SER A CA  1 
ATOM   1605 C  C   . SER A 1 196 ? -27.996 6.805   -0.591  1.00 39.39 ? 205 SER A C   1 
ATOM   1606 O  O   . SER A 1 196 ? -27.591 7.873   -1.026  1.00 39.33 ? 205 SER A O   1 
ATOM   1607 C  CB  . SER A 1 196 ? -29.184 6.642   1.632   1.00 42.57 ? 205 SER A CB  1 
ATOM   1608 O  OG  . SER A 1 196 ? -28.474 7.757   2.139   1.00 48.28 ? 205 SER A OG  1 
ATOM   1609 N  N   . CYS A 1 197 ? -27.313 5.671   -0.725  1.00 40.17 ? 206 CYS A N   1 
ATOM   1610 C  CA  . CYS A 1 197 ? -26.009 5.618   -1.402  1.00 39.36 ? 206 CYS A CA  1 
ATOM   1611 C  C   . CYS A 1 197 ? -26.077 5.865   -2.906  1.00 38.59 ? 206 CYS A C   1 
ATOM   1612 O  O   . CYS A 1 197 ? -25.174 6.481   -3.475  1.00 39.94 ? 206 CYS A O   1 
ATOM   1613 C  CB  . CYS A 1 197 ? -25.339 4.273   -1.159  1.00 39.91 ? 206 CYS A CB  1 
ATOM   1614 S  SG  . CYS A 1 197 ? -24.940 3.942   0.560   1.00 42.47 ? 206 CYS A SG  1 
ATOM   1615 N  N   . LEU A 1 198 ? -27.125 5.360   -3.552  1.00 38.51 ? 207 LEU A N   1 
ATOM   1616 C  CA  . LEU A 1 198 ? -27.333 5.599   -4.984  1.00 37.37 ? 207 LEU A CA  1 
ATOM   1617 C  C   . LEU A 1 198 ? -27.761 7.037   -5.286  1.00 38.56 ? 207 LEU A C   1 
ATOM   1618 O  O   . LEU A 1 198 ? -27.408 7.593   -6.338  1.00 36.89 ? 207 LEU A O   1 
ATOM   1619 C  CB  . LEU A 1 198 ? -28.346 4.610   -5.553  1.00 37.51 ? 207 LEU A CB  1 
ATOM   1620 C  CG  . LEU A 1 198 ? -27.898 3.143   -5.508  1.00 37.74 ? 207 LEU A CG  1 
ATOM   1621 C  CD1 . LEU A 1 198 ? -29.063 2.250   -5.898  1.00 39.58 ? 207 LEU A CD1 1 
ATOM   1622 C  CD2 . LEU A 1 198 ? -26.686 2.888   -6.409  1.00 34.82 ? 207 LEU A CD2 1 
ATOM   1623 N  N   . GLU A 1 199 ? -28.528 7.619   -4.370  1.00 39.17 ? 208 GLU A N   1 
ATOM   1624 C  CA  . GLU A 1 199 ? -28.865 9.041   -4.417  1.00 41.51 ? 208 GLU A CA  1 
ATOM   1625 C  C   . GLU A 1 199 ? -27.607 9.902   -4.228  1.00 42.56 ? 208 GLU A C   1 
ATOM   1626 O  O   . GLU A 1 199 ? -27.380 10.829  -5.001  1.00 41.58 ? 208 GLU A O   1 
ATOM   1627 C  CB  . GLU A 1 199 ? -29.936 9.377   -3.369  1.00 42.62 ? 208 GLU A CB  1 
ATOM   1628 C  CG  . GLU A 1 199 ? -31.337 8.836   -3.721  1.00 41.39 ? 208 GLU A CG  1 
ATOM   1629 C  CD  . GLU A 1 199 ? -32.310 8.796   -2.532  1.00 45.18 ? 208 GLU A CD  1 
ATOM   1630 O  OE1 . GLU A 1 199 ? -32.049 9.468   -1.514  1.00 45.07 ? 208 GLU A OE1 1 
ATOM   1631 O  OE2 . GLU A 1 199 ? -33.349 8.093   -2.620  1.00 40.31 ? 208 GLU A OE2 1 
ATOM   1632 N  N   . LYS A 1 200 ? -26.789 9.571   -3.224  1.00 42.22 ? 209 LYS A N   1 
ATOM   1633 C  CA  . LYS A 1 200 ? -25.500 10.250  -3.003  1.00 43.45 ? 209 LYS A CA  1 
ATOM   1634 C  C   . LYS A 1 200 ? -24.578 10.158  -4.217  1.00 42.17 ? 209 LYS A C   1 
ATOM   1635 O  O   . LYS A 1 200 ? -23.926 11.139  -4.567  1.00 44.46 ? 209 LYS A O   1 
ATOM   1636 C  CB  . LYS A 1 200 ? -24.769 9.694   -1.771  1.00 45.25 ? 209 LYS A CB  1 
ATOM   1637 C  CG  . LYS A 1 200 ? -25.274 10.246  -0.437  1.00 48.71 ? 209 LYS A CG  1 
ATOM   1638 C  CD  . LYS A 1 200 ? -24.542 9.615   0.736   0.00 48.52 ? 209 LYS A CD  1 
ATOM   1639 C  CE  . LYS A 1 200 ? -25.025 10.184  2.060   0.00 51.06 ? 209 LYS A CE  1 
ATOM   1640 N  NZ  . LYS A 1 200 ? -24.323 9.571   3.222   0.00 52.41 ? 209 LYS A NZ  1 
ATOM   1641 N  N   . ALA A 1 201 ? -24.534 8.987   -4.854  1.00 39.71 ? 210 ALA A N   1 
ATOM   1642 C  CA  . ALA A 1 201 ? -23.708 8.784   -6.047  1.00 38.10 ? 210 ALA A CA  1 
ATOM   1643 C  C   . ALA A 1 201 ? -24.061 9.749   -7.194  1.00 36.97 ? 210 ALA A C   1 
ATOM   1644 O  O   . ALA A 1 201 ? -23.169 10.175  -7.925  1.00 34.61 ? 210 ALA A O   1 
ATOM   1645 C  CB  . ALA A 1 201 ? -23.795 7.346   -6.516  1.00 38.23 ? 210 ALA A CB  1 
ATOM   1646 N  N   . LEU A 1 202 ? -25.345 10.096  -7.331  1.00 36.26 ? 211 LEU A N   1 
ATOM   1647 C  CA  . LEU A 1 202 ? -25.787 11.084  -8.325  1.00 36.91 ? 211 LEU A CA  1 
ATOM   1648 C  C   . LEU A 1 202 ? -25.207 12.470  -8.047  1.00 36.99 ? 211 LEU A C   1 
ATOM   1649 O  O   . LEU A 1 202 ? -24.734 13.141  -8.963  1.00 34.14 ? 211 LEU A O   1 
ATOM   1650 C  CB  . LEU A 1 202 ? -27.318 11.171  -8.397  1.00 37.47 ? 211 LEU A CB  1 
ATOM   1651 C  CG  . LEU A 1 202 ? -27.945 12.215  -9.345  1.00 38.32 ? 211 LEU A CG  1 
ATOM   1652 C  CD1 . LEU A 1 202 ? -27.417 12.079  -10.765 1.00 39.59 ? 211 LEU A CD1 1 
ATOM   1653 C  CD2 . LEU A 1 202 ? -29.469 12.107  -9.337  1.00 39.56 ? 211 LEU A CD2 1 
ATOM   1654 N  N   . GLN A 1 203 ? -25.240 12.890  -6.788  1.00 37.11 ? 212 GLN A N   1 
ATOM   1655 C  CA  . GLN A 1 203 ? -24.680 14.189  -6.413  1.00 40.30 ? 212 GLN A CA  1 
ATOM   1656 C  C   . GLN A 1 203 ? -23.176 14.243  -6.699  1.00 38.32 ? 212 GLN A C   1 
ATOM   1657 O  O   . GLN A 1 203 ? -22.674 15.262  -7.169  1.00 40.47 ? 212 GLN A O   1 
ATOM   1658 C  CB  . GLN A 1 203 ? -24.987 14.527  -4.948  1.00 43.51 ? 212 GLN A CB  1 
ATOM   1659 C  CG  . GLN A 1 203 ? -26.497 14.531  -4.595  1.00 48.98 ? 212 GLN A CG  1 
ATOM   1660 C  CD  . GLN A 1 203 ? -27.347 15.420  -5.515  1.00 51.97 ? 212 GLN A CD  1 
ATOM   1661 O  OE1 . GLN A 1 203 ? -27.029 16.590  -5.728  1.00 51.65 ? 212 GLN A OE1 1 
ATOM   1662 N  NE2 . GLN A 1 203 ? -28.434 14.861  -6.053  1.00 44.35 ? 212 GLN A NE2 1 
ATOM   1663 N  N   . VAL A 1 204 ? -22.476 13.132  -6.467  1.00 36.98 ? 213 VAL A N   1 
ATOM   1664 C  CA  . VAL A 1 204 ? -21.054 13.013  -6.827  1.00 37.51 ? 213 VAL A CA  1 
ATOM   1665 C  C   . VAL A 1 204 ? -20.831 13.247  -8.343  1.00 37.73 ? 213 VAL A C   1 
ATOM   1666 O  O   . VAL A 1 204 ? -19.864 13.910  -8.733  1.00 36.37 ? 213 VAL A O   1 
ATOM   1667 C  CB  . VAL A 1 204 ? -20.463 11.637  -6.373  1.00 36.13 ? 213 VAL A CB  1 
ATOM   1668 C  CG1 . VAL A 1 204 ? -19.026 11.431  -6.869  1.00 33.81 ? 213 VAL A CG1 1 
ATOM   1669 C  CG2 . VAL A 1 204 ? -20.494 11.512  -4.855  1.00 39.30 ? 213 VAL A CG2 1 
ATOM   1670 N  N   . PHE A 1 205 ? -21.741 12.725  -9.173  1.00 38.01 ? 214 PHE A N   1 
ATOM   1671 C  CA  . PHE A 1 205 ? -21.673 12.866  -10.647 1.00 37.76 ? 214 PHE A CA  1 
ATOM   1672 C  C   . PHE A 1 205 ? -21.617 14.340  -11.099 1.00 38.40 ? 214 PHE A C   1 
ATOM   1673 O  O   . PHE A 1 205 ? -20.916 14.673  -12.055 1.00 36.39 ? 214 PHE A O   1 
ATOM   1674 C  CB  . PHE A 1 205 ? -22.891 12.168  -11.297 1.00 40.54 ? 214 PHE A CB  1 
ATOM   1675 C  CG  . PHE A 1 205 ? -22.661 11.623  -12.698 1.00 35.46 ? 214 PHE A CG  1 
ATOM   1676 C  CD1 . PHE A 1 205 ? -21.852 12.272  -13.644 1.00 41.53 ? 214 PHE A CD1 1 
ATOM   1677 C  CD2 . PHE A 1 205 ? -23.334 10.474  -13.096 1.00 41.48 ? 214 PHE A CD2 1 
ATOM   1678 C  CE1 . PHE A 1 205 ? -21.690 11.764  -14.930 1.00 41.96 ? 214 PHE A CE1 1 
ATOM   1679 C  CE2 . PHE A 1 205 ? -23.175 9.958   -14.386 1.00 40.56 ? 214 PHE A CE2 1 
ATOM   1680 C  CZ  . PHE A 1 205 ? -22.357 10.606  -15.302 1.00 39.88 ? 214 PHE A CZ  1 
ATOM   1681 N  N   . HIS A 1 206 ? -22.329 15.217  -10.391 1.00 39.39 ? 215 HIS A N   1 
ATOM   1682 C  CA  . HIS A 1 206 ? -22.435 16.637  -10.756 1.00 40.76 ? 215 HIS A CA  1 
ATOM   1683 C  C   . HIS A 1 206 ? -21.073 17.317  -10.983 1.00 41.90 ? 215 HIS A C   1 
ATOM   1684 O  O   . HIS A 1 206 ? -20.976 18.251  -11.778 1.00 42.01 ? 215 HIS A O   1 
ATOM   1685 C  CB  . HIS A 1 206 ? -23.247 17.410  -9.697  1.00 42.20 ? 215 HIS A CB  1 
ATOM   1686 C  CG  . HIS A 1 206 ? -24.685 16.985  -9.599  1.00 41.48 ? 215 HIS A CG  1 
ATOM   1687 N  ND1 . HIS A 1 206 ? -25.619 17.688  -8.869  1.00 44.51 ? 215 HIS A ND1 1 
ATOM   1688 C  CD2 . HIS A 1 206 ? -25.352 15.944  -10.157 1.00 41.97 ? 215 HIS A CD2 1 
ATOM   1689 C  CE1 . HIS A 1 206 ? -26.793 17.088  -8.966  1.00 46.21 ? 215 HIS A CE1 1 
ATOM   1690 N  NE2 . HIS A 1 206 ? -26.658 16.025  -9.739  1.00 37.80 ? 215 HIS A NE2 1 
ATOM   1691 N  N   . GLN A 1 207 ? -20.039 16.838  -10.283 1.00 42.93 ? 216 GLN A N   1 
ATOM   1692 C  CA  . GLN A 1 207 ? -18.637 17.270  -10.475 1.00 43.91 ? 216 GLN A CA  1 
ATOM   1693 C  C   . GLN A 1 207 ? -18.081 17.184  -11.904 1.00 43.22 ? 216 GLN A C   1 
ATOM   1694 O  O   . GLN A 1 207 ? -17.161 17.939  -12.257 1.00 43.32 ? 216 GLN A O   1 
ATOM   1695 C  CB  . GLN A 1 207 ? -17.702 16.418  -9.613  1.00 44.77 ? 216 GLN A CB  1 
ATOM   1696 C  CG  . GLN A 1 207 ? -17.761 16.680  -8.145  1.00 47.78 ? 216 GLN A CG  1 
ATOM   1697 C  CD  . GLN A 1 207 ? -16.852 15.743  -7.391  1.00 47.67 ? 216 GLN A CD  1 
ATOM   1698 O  OE1 . GLN A 1 207 ? -15.781 16.138  -6.927  1.00 50.55 ? 216 GLN A OE1 1 
ATOM   1699 N  NE2 . GLN A 1 207 ? -17.260 14.482  -7.289  1.00 47.98 ? 216 GLN A NE2 1 
ATOM   1700 N  N   . ILE A 1 208 ? -18.596 16.247  -12.702 1.00 40.30 ? 217 ILE A N   1 
ATOM   1701 C  CA  . ILE A 1 208 ? -18.086 16.015  -14.065 1.00 38.36 ? 217 ILE A CA  1 
ATOM   1702 C  C   . ILE A 1 208 ? -17.974 17.326  -14.870 1.00 39.33 ? 217 ILE A C   1 
ATOM   1703 O  O   . ILE A 1 208 ? -16.989 17.528  -15.589 1.00 36.02 ? 217 ILE A O   1 
ATOM   1704 C  CB  . ILE A 1 208 ? -18.939 14.944  -14.820 1.00 36.90 ? 217 ILE A CB  1 
ATOM   1705 C  CG1 . ILE A 1 208 ? -18.161 14.314  -15.990 1.00 41.48 ? 217 ILE A CG1 1 
ATOM   1706 C  CG2 . ILE A 1 208 ? -20.279 15.498  -15.279 1.00 36.83 ? 217 ILE A CG2 1 
ATOM   1707 C  CD1 . ILE A 1 208 ? -17.533 12.963  -15.650 1.00 36.29 ? 217 ILE A CD1 1 
ATOM   1708 N  N   . HIS A 1 209 ? -18.967 18.207  -14.695 1.00 38.66 ? 218 HIS A N   1 
ATOM   1709 C  CA  . HIS A 1 209 ? -19.057 19.490  -15.403 1.00 40.34 ? 218 HIS A CA  1 
ATOM   1710 C  C   . HIS A 1 209 ? -17.906 20.439  -15.067 1.00 39.98 ? 218 HIS A C   1 
ATOM   1711 O  O   . HIS A 1 209 ? -17.474 21.206  -15.921 1.00 40.27 ? 218 HIS A O   1 
ATOM   1712 C  CB  . HIS A 1 209 ? -20.402 20.181  -15.116 1.00 41.01 ? 218 HIS A CB  1 
ATOM   1713 C  CG  . HIS A 1 209 ? -21.601 19.367  -15.509 1.00 42.93 ? 218 HIS A CG  1 
ATOM   1714 N  ND1 . HIS A 1 209 ? -22.067 19.299  -16.805 1.00 43.76 ? 218 HIS A ND1 1 
ATOM   1715 C  CD2 . HIS A 1 209 ? -22.430 18.588  -14.773 1.00 40.40 ? 218 HIS A CD2 1 
ATOM   1716 C  CE1 . HIS A 1 209 ? -23.132 18.518  -16.849 1.00 43.78 ? 218 HIS A CE1 1 
ATOM   1717 N  NE2 . HIS A 1 209 ? -23.372 18.071  -15.629 1.00 40.56 ? 218 HIS A NE2 1 
ATOM   1718 N  N   . ASP A 1 210 ? -17.413 20.367  -13.831 1.00 41.81 ? 219 ASP A N   1 
ATOM   1719 C  CA  . ASP A 1 210 ? -16.312 21.220  -13.361 1.00 42.97 ? 219 ASP A CA  1 
ATOM   1720 C  C   . ASP A 1 210 ? -14.948 20.832  -13.932 1.00 40.75 ? 219 ASP A C   1 
ATOM   1721 O  O   . ASP A 1 210 ? -14.102 21.699  -14.134 1.00 43.53 ? 219 ASP A O   1 
ATOM   1722 C  CB  . ASP A 1 210 ? -16.217 21.188  -11.829 1.00 44.90 ? 219 ASP A CB  1 
ATOM   1723 C  CG  . ASP A 1 210 ? -17.478 21.700  -11.141 1.00 49.38 ? 219 ASP A CG  1 
ATOM   1724 O  OD1 . ASP A 1 210 ? -18.048 22.723  -11.586 1.00 53.87 ? 219 ASP A OD1 1 
ATOM   1725 O  OD2 . ASP A 1 210 ? -17.886 21.078  -10.138 1.00 45.04 ? 219 ASP A OD2 1 
ATOM   1726 N  N   . HIS A 1 211 ? -14.730 19.541  -14.175 1.00 39.20 ? 220 HIS A N   1 
ATOM   1727 C  CA  . HIS A 1 211 ? -13.391 19.015  -14.490 1.00 38.12 ? 220 HIS A CA  1 
ATOM   1728 C  C   . HIS A 1 211 ? -13.228 18.402  -15.881 1.00 36.26 ? 220 HIS A C   1 
ATOM   1729 O  O   . HIS A 1 211 ? -12.125 17.982  -16.233 1.00 36.24 ? 220 HIS A O   1 
ATOM   1730 C  CB  . HIS A 1 211 ? -12.993 17.985  -13.431 1.00 38.79 ? 220 HIS A CB  1 
ATOM   1731 C  CG  . HIS A 1 211 ? -13.202 18.457  -12.024 1.00 39.40 ? 220 HIS A CG  1 
ATOM   1732 N  ND1 . HIS A 1 211 ? -12.583 19.578  -11.517 1.00 39.83 ? 220 HIS A ND1 1 
ATOM   1733 C  CD2 . HIS A 1 211 ? -13.970 17.965  -11.024 1.00 38.42 ? 220 HIS A CD2 1 
ATOM   1734 C  CE1 . HIS A 1 211 ? -12.959 19.756  -10.263 1.00 41.57 ? 220 HIS A CE1 1 
ATOM   1735 N  NE2 . HIS A 1 211 ? -13.798 18.790  -9.939  1.00 42.15 ? 220 HIS A NE2 1 
ATOM   1736 N  N   . VAL A 1 212 ? -14.306 18.325  -16.659 1.00 35.17 ? 221 VAL A N   1 
ATOM   1737 C  CA  . VAL A 1 212 ? -14.235 17.801  -18.024 1.00 34.36 ? 221 VAL A CA  1 
ATOM   1738 C  C   . VAL A 1 212 ? -14.893 18.789  -18.980 1.00 33.97 ? 221 VAL A C   1 
ATOM   1739 O  O   . VAL A 1 212 ? -16.021 19.236  -18.749 1.00 35.02 ? 221 VAL A O   1 
ATOM   1740 C  CB  . VAL A 1 212 ? -14.886 16.413  -18.159 1.00 32.04 ? 221 VAL A CB  1 
ATOM   1741 C  CG1 . VAL A 1 212 ? -14.588 15.809  -19.542 1.00 34.53 ? 221 VAL A CG1 1 
ATOM   1742 C  CG2 . VAL A 1 212 ? -14.377 15.474  -17.086 1.00 32.66 ? 221 VAL A CG2 1 
ATOM   1743 N  N   . ASN A 1 213 ? -14.150 19.124  -20.034 1.00 34.78 ? 222 ASN A N   1 
ATOM   1744 C  CA  . ASN A 1 213 ? -14.589 19.999  -21.115 1.00 35.02 ? 222 ASN A CA  1 
ATOM   1745 C  C   . ASN A 1 213 ? -15.135 19.103  -22.239 1.00 32.83 ? 222 ASN A C   1 
ATOM   1746 O  O   . ASN A 1 213 ? -14.442 18.166  -22.650 1.00 29.20 ? 222 ASN A O   1 
ATOM   1747 C  CB  . ASN A 1 213 ? -13.400 20.846  -21.607 1.00 37.92 ? 222 ASN A CB  1 
ATOM   1748 C  CG  . ASN A 1 213 ? -13.584 21.351  -23.017 1.00 40.44 ? 222 ASN A CG  1 
ATOM   1749 O  OD1 . ASN A 1 213 ? -12.910 20.889  -23.933 1.00 49.52 ? 222 ASN A OD1 1 
ATOM   1750 N  ND2 . ASN A 1 213 ? -14.513 22.289  -23.205 1.00 52.12 ? 222 ASN A ND2 1 
ATOM   1751 N  N   . PRO A 1 214 ? -16.376 19.362  -22.717 1.00 33.51 ? 223 PRO A N   1 
ATOM   1752 C  CA  . PRO A 1 214 ? -16.963 18.555  -23.808 1.00 32.58 ? 223 PRO A CA  1 
ATOM   1753 C  C   . PRO A 1 214 ? -16.098 18.390  -25.063 1.00 32.83 ? 223 PRO A C   1 
ATOM   1754 O  O   . PRO A 1 214 ? -15.934 17.270  -25.533 1.00 32.27 ? 223 PRO A O   1 
ATOM   1755 C  CB  . PRO A 1 214 ? -18.255 19.297  -24.143 1.00 33.74 ? 223 PRO A CB  1 
ATOM   1756 C  CG  . PRO A 1 214 ? -18.618 19.995  -22.887 1.00 38.08 ? 223 PRO A CG  1 
ATOM   1757 C  CD  . PRO A 1 214 ? -17.325 20.387  -22.236 1.00 35.22 ? 223 PRO A CD  1 
ATOM   1758 N  N   . LYS A 1 215 ? -15.548 19.488  -25.575 1.00 33.95 ? 224 LYS A N   1 
ATOM   1759 C  CA  . LYS A 1 215 ? -14.748 19.465  -26.797 1.00 35.87 ? 224 LYS A CA  1 
ATOM   1760 C  C   . LYS A 1 215 ? -13.549 18.526  -26.658 1.00 36.02 ? 224 LYS A C   1 
ATOM   1761 O  O   . LYS A 1 215 ? -13.366 17.630  -27.489 1.00 33.63 ? 224 LYS A O   1 
ATOM   1762 C  CB  . LYS A 1 215 ? -14.281 20.873  -27.185 1.00 37.99 ? 224 LYS A CB  1 
ATOM   1763 C  CG  . LYS A 1 215 ? -13.689 20.950  -28.598 1.00 41.07 ? 224 LYS A CG  1 
ATOM   1764 C  CD  . LYS A 1 215 ? -13.503 22.385  -29.075 1.00 44.58 ? 224 LYS A CD  1 
ATOM   1765 C  CE  . LYS A 1 215 ? -12.920 22.417  -30.490 0.00 44.46 ? 224 LYS A CE  1 
ATOM   1766 N  NZ  . LYS A 1 215 ? -12.732 23.811  -30.977 0.00 46.87 ? 224 LYS A NZ  1 
ATOM   1767 N  N   . ALA A 1 216 ? -12.769 18.720  -25.595 1.00 35.20 ? 225 ALA A N   1 
ATOM   1768 C  CA  . ALA A 1 216 ? -11.605 17.867  -25.293 1.00 33.65 ? 225 ALA A CA  1 
ATOM   1769 C  C   . ALA A 1 216 ? -11.985 16.413  -25.063 1.00 31.73 ? 225 ALA A C   1 
ATOM   1770 O  O   . ALA A 1 216 ? -11.303 15.500  -25.542 1.00 30.75 ? 225 ALA A O   1 
ATOM   1771 C  CB  . ALA A 1 216 ? -10.864 18.391  -24.079 1.00 35.03 ? 225 ALA A CB  1 
ATOM   1772 N  N   . PHE A 1 217 ? -13.068 16.192  -24.323 1.00 31.24 ? 226 PHE A N   1 
ATOM   1773 C  CA  . PHE A 1 217 ? -13.548 14.835  -24.101 1.00 28.60 ? 226 PHE A CA  1 
ATOM   1774 C  C   . PHE A 1 217 ? -13.866 14.128  -25.417 1.00 28.79 ? 226 PHE A C   1 
ATOM   1775 O  O   . PHE A 1 217 ? -13.417 13.003  -25.643 1.00 28.38 ? 226 PHE A O   1 
ATOM   1776 C  CB  . PHE A 1 217 ? -14.791 14.795  -23.222 1.00 28.36 ? 226 PHE A CB  1 
ATOM   1777 C  CG  . PHE A 1 217 ? -15.237 13.403  -22.930 1.00 27.59 ? 226 PHE A CG  1 
ATOM   1778 C  CD1 . PHE A 1 217 ? -14.586 12.664  -21.952 1.00 28.74 ? 226 PHE A CD1 1 
ATOM   1779 C  CD2 . PHE A 1 217 ? -16.237 12.789  -23.690 1.00 26.94 ? 226 PHE A CD2 1 
ATOM   1780 C  CE1 . PHE A 1 217 ? -14.951 11.344  -21.687 1.00 29.07 ? 226 PHE A CE1 1 
ATOM   1781 C  CE2 . PHE A 1 217 ? -16.619 11.465  -23.430 1.00 27.20 ? 226 PHE A CE2 1 
ATOM   1782 C  CZ  . PHE A 1 217 ? -15.969 10.746  -22.421 1.00 28.35 ? 226 PHE A CZ  1 
ATOM   1783 N  N   . PHE A 1 218 ? -14.658 14.793  -26.259 1.00 29.19 ? 227 PHE A N   1 
ATOM   1784 C  CA  . PHE A 1 218 ? -15.127 14.206  -27.500 1.00 29.13 ? 227 PHE A CA  1 
ATOM   1785 C  C   . PHE A 1 218 ? -14.014 14.035  -28.519 1.00 29.91 ? 227 PHE A C   1 
ATOM   1786 O  O   . PHE A 1 218 ? -13.936 13.004  -29.174 1.00 29.43 ? 227 PHE A O   1 
ATOM   1787 C  CB  . PHE A 1 218 ? -16.254 15.042  -28.121 1.00 30.50 ? 227 PHE A CB  1 
ATOM   1788 C  CG  . PHE A 1 218 ? -16.743 14.497  -29.431 1.00 29.82 ? 227 PHE A CG  1 
ATOM   1789 C  CD1 . PHE A 1 218 ? -17.609 13.411  -29.462 1.00 29.93 ? 227 PHE A CD1 1 
ATOM   1790 C  CD2 . PHE A 1 218 ? -16.303 15.042  -30.638 1.00 35.40 ? 227 PHE A CD2 1 
ATOM   1791 C  CE1 . PHE A 1 218 ? -18.034 12.879  -30.679 1.00 31.64 ? 227 PHE A CE1 1 
ATOM   1792 C  CE2 . PHE A 1 218 ? -16.733 14.523  -31.854 1.00 35.37 ? 227 PHE A CE2 1 
ATOM   1793 C  CZ  . PHE A 1 218 ? -17.606 13.440  -31.873 1.00 31.95 ? 227 PHE A CZ  1 
ATOM   1794 N  N   . SER A 1 219 ? -13.183 15.057  -28.687 1.00 31.58 ? 228 SER A N   1 
ATOM   1795 C  CA  . SER A 1 219 ? -12.202 15.049  -29.774 1.00 34.28 ? 228 SER A CA  1 
ATOM   1796 C  C   . SER A 1 219 ? -10.939 14.240  -29.448 1.00 33.00 ? 228 SER A C   1 
ATOM   1797 O  O   . SER A 1 219 ? -10.272 13.764  -30.366 1.00 35.80 ? 228 SER A O   1 
ATOM   1798 C  CB  . SER A 1 219 ? -11.848 16.483  -30.191 1.00 34.83 ? 228 SER A CB  1 
ATOM   1799 O  OG  . SER A 1 219 ? -11.408 17.227  -29.070 1.00 39.64 ? 228 SER A OG  1 
ATOM   1800 N  N   . VAL A 1 220 ? -10.620 14.088  -28.162 1.00 33.27 ? 229 VAL A N   1 
ATOM   1801 C  CA  . VAL A 1 220 ? -9.346  13.493  -27.712 1.00 33.78 ? 229 VAL A CA  1 
ATOM   1802 C  C   . VAL A 1 220 ? -9.550  12.236  -26.846 1.00 32.33 ? 229 VAL A C   1 
ATOM   1803 O  O   . VAL A 1 220 ? -9.209  11.133  -27.268 1.00 30.98 ? 229 VAL A O   1 
ATOM   1804 C  CB  . VAL A 1 220 ? -8.470  14.527  -26.932 1.00 36.11 ? 229 VAL A CB  1 
ATOM   1805 C  CG1 . VAL A 1 220 ? -7.094  13.934  -26.571 1.00 37.24 ? 229 VAL A CG1 1 
ATOM   1806 C  CG2 . VAL A 1 220 ? -8.286  15.825  -27.743 1.00 38.27 ? 229 VAL A CG2 1 
ATOM   1807 N  N   . LEU A 1 221 ? -10.089 12.401  -25.640 1.00 31.74 ? 230 LEU A N   1 
ATOM   1808 C  CA  . LEU A 1 221 ? -10.157 11.289  -24.683 1.00 31.43 ? 230 LEU A CA  1 
ATOM   1809 C  C   . LEU A 1 221 ? -10.995 10.118  -25.189 1.00 31.05 ? 230 LEU A C   1 
ATOM   1810 O  O   . LEU A 1 221 ? -10.597 8.963   -25.013 1.00 29.38 ? 230 LEU A O   1 
ATOM   1811 C  CB  . LEU A 1 221 ? -10.705 11.745  -23.328 1.00 32.00 ? 230 LEU A CB  1 
ATOM   1812 C  CG  . LEU A 1 221 ? -10.693 10.718  -22.184 1.00 30.00 ? 230 LEU A CG  1 
ATOM   1813 C  CD1 . LEU A 1 221 ? -9.304  10.127  -21.943 1.00 34.63 ? 230 LEU A CD1 1 
ATOM   1814 C  CD2 . LEU A 1 221 ? -11.199 11.368  -20.915 1.00 29.69 ? 230 LEU A CD2 1 
ATOM   1815 N  N   . ARG A 1 222 ? -12.145 10.425  -25.796 1.00 29.11 ? 231 ARG A N   1 
ATOM   1816 C  CA  . ARG A 1 222 ? -13.019 9.410   -26.418 1.00 29.86 ? 231 ARG A CA  1 
ATOM   1817 C  C   . ARG A 1 222 ? -12.223 8.494   -27.339 1.00 29.35 ? 231 ARG A C   1 
ATOM   1818 O  O   . ARG A 1 222 ? -12.440 7.290   -27.349 1.00 28.25 ? 231 ARG A O   1 
ATOM   1819 C  CB  . ARG A 1 222 ? -14.156 10.087  -27.220 1.00 29.70 ? 231 ARG A CB  1 
ATOM   1820 C  CG  . ARG A 1 222 ? -15.056 9.138   -28.043 1.00 31.16 ? 231 ARG A CG  1 
ATOM   1821 C  CD  . ARG A 1 222 ? -16.183 9.875   -28.734 1.00 37.69 ? 231 ARG A CD  1 
ATOM   1822 N  NE  . ARG A 1 222 ? -15.654 10.765  -29.763 1.00 42.55 ? 231 ARG A NE  1 
ATOM   1823 C  CZ  . ARG A 1 222 ? -15.427 10.450  -31.040 1.00 46.41 ? 231 ARG A CZ  1 
ATOM   1824 N  NH1 . ARG A 1 222 ? -15.699 9.241   -31.534 1.00 49.81 ? 231 ARG A NH1 1 
ATOM   1825 N  NH2 . ARG A 1 222 ? -14.933 11.375  -31.849 1.00 47.75 ? 231 ARG A NH2 1 
ATOM   1826 N  N   . ILE A 1 223 ? -11.294 9.087   -28.097 1.00 31.08 ? 232 ILE A N   1 
ATOM   1827 C  CA  . ILE A 1 223 ? -10.506 8.371   -29.100 1.00 30.28 ? 232 ILE A CA  1 
ATOM   1828 C  C   . ILE A 1 223 ? -9.619  7.334   -28.438 1.00 29.41 ? 232 ILE A C   1 
ATOM   1829 O  O   . ILE A 1 223 ? -9.599  6.179   -28.861 1.00 31.64 ? 232 ILE A O   1 
ATOM   1830 C  CB  . ILE A 1 223 ? -9.640  9.351   -29.955 1.00 32.82 ? 232 ILE A CB  1 
ATOM   1831 C  CG1 . ILE A 1 223 ? -10.525 10.372  -30.700 1.00 34.22 ? 232 ILE A CG1 1 
ATOM   1832 C  CG2 . ILE A 1 223 ? -8.742  8.617   -30.941 1.00 34.76 ? 232 ILE A CG2 1 
ATOM   1833 C  CD1 . ILE A 1 223 ? -11.563 9.785   -31.643 1.00 36.52 ? 232 ILE A CD1 1 
ATOM   1834 N  N   . TYR A 1 224 ? -8.881  7.757   -27.416 1.00 25.59 ? 233 TYR A N   1 
ATOM   1835 C  CA  . TYR A 1 224 ? -7.939  6.880   -26.726 1.00 26.96 ? 233 TYR A CA  1 
ATOM   1836 C  C   . TYR A 1 224 ? -8.613  5.801   -25.900 1.00 27.79 ? 233 TYR A C   1 
ATOM   1837 O  O   . TYR A 1 224 ? -8.016  4.764   -25.677 1.00 28.35 ? 233 TYR A O   1 
ATOM   1838 C  CB  . TYR A 1 224 ? -6.968  7.699   -25.869 1.00 26.97 ? 233 TYR A CB  1 
ATOM   1839 C  CG  . TYR A 1 224 ? -6.008  8.475   -26.731 1.00 25.86 ? 233 TYR A CG  1 
ATOM   1840 C  CD1 . TYR A 1 224 ? -4.949  7.829   -27.365 1.00 26.11 ? 233 TYR A CD1 1 
ATOM   1841 C  CD2 . TYR A 1 224 ? -6.175  9.838   -26.956 1.00 29.40 ? 233 TYR A CD2 1 
ATOM   1842 C  CE1 . TYR A 1 224 ? -4.063  8.525   -28.192 1.00 26.03 ? 233 TYR A CE1 1 
ATOM   1843 C  CE2 . TYR A 1 224 ? -5.284  10.549  -27.796 1.00 29.10 ? 233 TYR A CE2 1 
ATOM   1844 C  CZ  . TYR A 1 224 ? -4.236  9.876   -28.401 1.00 25.49 ? 233 TYR A CZ  1 
ATOM   1845 O  OH  . TYR A 1 224 ? -3.351  10.546  -29.217 1.00 28.81 ? 233 TYR A OH  1 
ATOM   1846 N  N   . LEU A 1 225 ? -9.846  6.045   -25.452 1.00 26.56 ? 234 LEU A N   1 
ATOM   1847 C  CA  . LEU A 1 225 ? -10.646 5.020   -24.758 1.00 27.53 ? 234 LEU A CA  1 
ATOM   1848 C  C   . LEU A 1 225 ? -11.332 3.981   -25.646 1.00 27.18 ? 234 LEU A C   1 
ATOM   1849 O  O   . LEU A 1 225 ? -11.731 2.920   -25.140 1.00 29.87 ? 234 LEU A O   1 
ATOM   1850 C  CB  . LEU A 1 225 ? -11.718 5.685   -23.885 1.00 26.47 ? 234 LEU A CB  1 
ATOM   1851 C  CG  . LEU A 1 225 ? -11.178 6.599   -22.799 1.00 27.61 ? 234 LEU A CG  1 
ATOM   1852 C  CD1 . LEU A 1 225 ? -12.324 7.314   -22.112 1.00 29.63 ? 234 LEU A CD1 1 
ATOM   1853 C  CD2 . LEU A 1 225 ? -10.330 5.826   -21.799 1.00 33.58 ? 234 LEU A CD2 1 
ATOM   1854 N  N   A SER A 1 226 ? -11.481 4.270   -26.937 0.50 27.38 ? 235 SER A N   1 
ATOM   1855 N  N   B SER A 1 226 ? -11.467 4.276   -26.940 0.50 26.88 ? 235 SER A N   1 
ATOM   1856 C  CA  A SER A 1 226 ? -12.188 3.366   -27.847 0.50 27.50 ? 235 SER A CA  1 
ATOM   1857 C  CA  B SER A 1 226 ? -12.154 3.386   -27.882 0.50 26.67 ? 235 SER A CA  1 
ATOM   1858 C  C   A SER A 1 226 ? -11.376 2.094   -28.116 0.50 28.66 ? 235 SER A C   1 
ATOM   1859 C  C   B SER A 1 226 ? -11.368 2.090   -28.110 0.50 28.20 ? 235 SER A C   1 
ATOM   1860 O  O   A SER A 1 226 ? -10.155 2.075   -27.946 0.50 28.83 ? 235 SER A O   1 
ATOM   1861 O  O   B SER A 1 226 ? -10.152 2.046   -27.903 0.50 28.33 ? 235 SER A O   1 
ATOM   1862 C  CB  A SER A 1 226 ? -12.518 4.073   -29.160 0.50 28.79 ? 235 SER A CB  1 
ATOM   1863 C  CB  B SER A 1 226 ? -12.376 4.094   -29.222 0.50 27.60 ? 235 SER A CB  1 
ATOM   1864 O  OG  A SER A 1 226 ? -11.340 4.451   -29.846 0.50 30.20 ? 235 SER A OG  1 
ATOM   1865 O  OG  B SER A 1 226 ? -13.146 5.277   -29.069 0.50 23.54 ? 235 SER A OG  1 
ATOM   1866 N  N   . GLY A 1 227 ? -12.074 1.040   -28.527 1.00 28.10 ? 236 GLY A N   1 
ATOM   1867 C  CA  . GLY A 1 227 ? -11.470 -0.261  -28.780 1.00 27.87 ? 236 GLY A CA  1 
ATOM   1868 C  C   . GLY A 1 227 ? -11.599 -0.717  -30.208 1.00 28.31 ? 236 GLY A C   1 
ATOM   1869 O  O   . GLY A 1 227 ? -11.721 0.089   -31.138 1.00 29.15 ? 236 GLY A O   1 
ATOM   1870 N  N   . TRP A 1 228 ? -11.573 -2.036  -30.373 1.00 28.67 ? 237 TRP A N   1 
ATOM   1871 C  CA  . TRP A 1 228 ? -11.619 -2.662  -31.687 1.00 29.48 ? 237 TRP A CA  1 
ATOM   1872 C  C   . TRP A 1 228 ? -12.553 -3.874  -31.673 1.00 31.26 ? 237 TRP A C   1 
ATOM   1873 O  O   . TRP A 1 228 ? -12.145 -4.988  -31.982 1.00 33.49 ? 237 TRP A O   1 
ATOM   1874 C  CB  . TRP A 1 228 ? -10.205 -3.016  -32.161 1.00 28.50 ? 237 TRP A CB  1 
ATOM   1875 C  CG  . TRP A 1 228 ? -9.267  -3.437  -31.075 1.00 29.20 ? 237 TRP A CG  1 
ATOM   1876 C  CD1 . TRP A 1 228 ? -9.025  -4.705  -30.644 1.00 29.07 ? 237 TRP A CD1 1 
ATOM   1877 C  CD2 . TRP A 1 228 ? -8.427  -2.578  -30.293 1.00 26.81 ? 237 TRP A CD2 1 
ATOM   1878 N  NE1 . TRP A 1 228 ? -8.089  -4.692  -29.640 1.00 28.36 ? 237 TRP A NE1 1 
ATOM   1879 C  CE2 . TRP A 1 228 ? -7.698  -3.400  -29.410 1.00 23.20 ? 237 TRP A CE2 1 
ATOM   1880 C  CE3 . TRP A 1 228 ? -8.219  -1.191  -30.255 1.00 27.71 ? 237 TRP A CE3 1 
ATOM   1881 C  CZ2 . TRP A 1 228 ? -6.788  -2.878  -28.477 1.00 28.03 ? 237 TRP A CZ2 1 
ATOM   1882 C  CZ3 . TRP A 1 228 ? -7.301  -0.673  -29.337 1.00 25.37 ? 237 TRP A CZ3 1 
ATOM   1883 C  CH2 . TRP A 1 228 ? -6.603  -1.520  -28.464 1.00 27.73 ? 237 TRP A CH2 1 
ATOM   1884 N  N   . LYS A 1 229 ? -13.806 -3.632  -31.291 1.00 31.85 ? 238 LYS A N   1 
ATOM   1885 C  CA  . LYS A 1 229 ? -14.903 -4.580  -31.504 1.00 32.14 ? 238 LYS A CA  1 
ATOM   1886 C  C   . LYS A 1 229 ? -16.032 -3.868  -32.243 1.00 34.61 ? 238 LYS A C   1 
ATOM   1887 O  O   . LYS A 1 229 ? -16.570 -2.886  -31.741 1.00 33.88 ? 238 LYS A O   1 
ATOM   1888 C  CB  . LYS A 1 229 ? -15.411 -5.145  -30.185 1.00 31.37 ? 238 LYS A CB  1 
ATOM   1889 C  CG  . LYS A 1 229 ? -16.506 -6.202  -30.367 1.00 31.79 ? 238 LYS A CG  1 
ATOM   1890 C  CD  . LYS A 1 229 ? -16.738 -7.002  -29.115 1.00 34.29 ? 238 LYS A CD  1 
ATOM   1891 C  CE  . LYS A 1 229 ? -17.761 -8.099  -29.358 1.00 38.05 ? 238 LYS A CE  1 
ATOM   1892 N  NZ  . LYS A 1 229 ? -19.079 -7.531  -29.726 1.00 36.67 ? 238 LYS A NZ  1 
ATOM   1893 N  N   . GLY A 1 230 ? -16.385 -4.367  -33.430 1.00 36.54 ? 239 GLY A N   1 
ATOM   1894 C  CA  . GLY A 1 230 ? -17.333 -3.683  -34.309 1.00 39.49 ? 239 GLY A CA  1 
ATOM   1895 C  C   . GLY A 1 230 ? -16.916 -2.260  -34.669 1.00 41.65 ? 239 GLY A C   1 
ATOM   1896 O  O   . GLY A 1 230 ? -17.767 -1.382  -34.825 1.00 42.83 ? 239 GLY A O   1 
ATOM   1897 N  N   . ASN A 1 231 ? -15.604 -2.041  -34.785 1.00 40.91 ? 240 ASN A N   1 
ATOM   1898 C  CA  . ASN A 1 231 ? -15.033 -0.738  -35.109 1.00 40.03 ? 240 ASN A CA  1 
ATOM   1899 C  C   . ASN A 1 231 ? -14.573 -0.792  -36.559 1.00 41.12 ? 240 ASN A C   1 
ATOM   1900 O  O   . ASN A 1 231 ? -13.648 -1.541  -36.860 1.00 41.53 ? 240 ASN A O   1 
ATOM   1901 C  CB  . ASN A 1 231 ? -13.849 -0.427  -34.183 1.00 39.38 ? 240 ASN A CB  1 
ATOM   1902 C  CG  . ASN A 1 231 ? -13.337 1.003   -34.334 1.00 39.72 ? 240 ASN A CG  1 
ATOM   1903 O  OD1 . ASN A 1 231 ? -13.538 1.649   -35.364 1.00 38.98 ? 240 ASN A OD1 1 
ATOM   1904 N  ND2 . ASN A 1 231 ? -12.683 1.504   -33.291 1.00 38.21 ? 240 ASN A ND2 1 
ATOM   1905 N  N   . PRO A 1 232 ? -15.216 -0.016  -37.466 1.00 42.22 ? 241 PRO A N   1 
ATOM   1906 C  CA  . PRO A 1 232 ? -14.807 0.006   -38.887 1.00 44.21 ? 241 PRO A CA  1 
ATOM   1907 C  C   . PRO A 1 232 ? -13.325 0.320   -39.156 1.00 43.90 ? 241 PRO A C   1 
ATOM   1908 O  O   . PRO A 1 232 ? -12.781 -0.110  -40.181 1.00 42.70 ? 241 PRO A O   1 
ATOM   1909 C  CB  . PRO A 1 232 ? -15.705 1.098   -39.498 1.00 45.24 ? 241 PRO A CB  1 
ATOM   1910 C  CG  . PRO A 1 232 ? -16.894 1.134   -38.641 1.00 45.31 ? 241 PRO A CG  1 
ATOM   1911 C  CD  . PRO A 1 232 ? -16.375 0.870   -37.239 1.00 42.32 ? 241 PRO A CD  1 
ATOM   1912 N  N   . GLN A 1 233 ? -12.694 1.057   -38.243 1.00 43.37 ? 242 GLN A N   1 
ATOM   1913 C  CA  . GLN A 1 233 ? -11.255 1.355   -38.320 1.00 46.15 ? 242 GLN A CA  1 
ATOM   1914 C  C   . GLN A 1 233 ? -10.390 0.099   -38.212 1.00 46.78 ? 242 GLN A C   1 
ATOM   1915 O  O   . GLN A 1 233 ? -9.374  -0.008  -38.899 1.00 49.00 ? 242 GLN A O   1 
ATOM   1916 C  CB  . GLN A 1 233 ? -10.847 2.321   -37.209 1.00 43.88 ? 242 GLN A CB  1 
ATOM   1917 C  CG  . GLN A 1 233 ? -11.503 3.684   -37.271 1.00 44.33 ? 242 GLN A CG  1 
ATOM   1918 C  CD  . GLN A 1 233 ? -11.086 4.561   -36.109 1.00 46.37 ? 242 GLN A CD  1 
ATOM   1919 O  OE1 . GLN A 1 233 ? -10.540 5.646   -36.305 1.00 43.55 ? 242 GLN A OE1 1 
ATOM   1920 N  NE2 . GLN A 1 233 ? -11.325 4.083   -34.886 1.00 49.87 ? 242 GLN A NE2 1 
ATOM   1921 N  N   . LEU A 1 234 ? -10.788 -0.821  -37.328 1.00 46.82 ? 243 LEU A N   1 
ATOM   1922 C  CA  . LEU A 1 234 ? -10.140 -2.126  -37.163 1.00 47.16 ? 243 LEU A CA  1 
ATOM   1923 C  C   . LEU A 1 234 ? -11.196 -3.220  -37.300 1.00 46.88 ? 243 LEU A C   1 
ATOM   1924 O  O   . LEU A 1 234 ? -11.569 -3.878  -36.323 1.00 43.83 ? 243 LEU A O   1 
ATOM   1925 C  CB  . LEU A 1 234 ? -9.442  -2.232  -35.804 1.00 46.59 ? 243 LEU A CB  1 
ATOM   1926 C  CG  . LEU A 1 234 ? -8.332  -1.222  -35.517 1.00 47.76 ? 243 LEU A CG  1 
ATOM   1927 C  CD1 . LEU A 1 234 ? -8.896  0.013   -34.823 1.00 50.96 ? 243 LEU A CD1 1 
ATOM   1928 C  CD2 . LEU A 1 234 ? -7.246  -1.849  -34.651 1.00 48.32 ? 243 LEU A CD2 1 
ATOM   1929 N  N   . SER A 1 235 ? -11.667 -3.377  -38.535 1.00 47.86 ? 244 SER A N   1 
ATOM   1930 C  CA  . SER A 1 235 ? -12.744 -4.295  -38.932 1.00 49.39 ? 244 SER A CA  1 
ATOM   1931 C  C   . SER A 1 235 ? -12.671 -5.697  -38.320 1.00 48.06 ? 244 SER A C   1 
ATOM   1932 O  O   . SER A 1 235 ? -13.678 -6.215  -37.839 1.00 50.64 ? 244 SER A O   1 
ATOM   1933 C  CB  . SER A 1 235 ? -12.752 -4.400  -40.476 1.00 51.43 ? 244 SER A CB  1 
ATOM   1934 O  OG  . SER A 1 235 ? -13.587 -5.439  -40.963 1.00 57.91 ? 244 SER A OG  1 
ATOM   1935 N  N   . ASP A 1 236 ? -11.481 -6.294  -38.348 1.00 48.22 ? 245 ASP A N   1 
ATOM   1936 C  CA  . ASP A 1 236 ? -11.266 -7.678  -37.897 1.00 48.42 ? 245 ASP A CA  1 
ATOM   1937 C  C   . ASP A 1 236 ? -10.638 -7.769  -36.509 1.00 46.98 ? 245 ASP A C   1 
ATOM   1938 O  O   . ASP A 1 236 ? -10.414 -8.876  -36.010 1.00 48.47 ? 245 ASP A O   1 
ATOM   1939 C  CB  . ASP A 1 236 ? -10.370 -8.422  -38.901 1.00 51.67 ? 245 ASP A CB  1 
ATOM   1940 C  CG  . ASP A 1 236 ? -10.977 -8.490  -40.293 1.00 54.83 ? 245 ASP A CG  1 
ATOM   1941 O  OD1 . ASP A 1 236 ? -12.176 -8.813  -40.404 1.00 56.82 ? 245 ASP A OD1 1 
ATOM   1942 O  OD2 . ASP A 1 236 ? -10.247 -8.231  -41.277 1.00 61.17 ? 245 ASP A OD2 1 
ATOM   1943 N  N   . GLY A 1 237 ? -10.373 -6.613  -35.892 1.00 43.35 ? 246 GLY A N   1 
ATOM   1944 C  CA  . GLY A 1 237 ? -9.716  -6.524  -34.593 1.00 39.83 ? 246 GLY A CA  1 
ATOM   1945 C  C   . GLY A 1 237 ? -8.255  -6.129  -34.735 1.00 38.89 ? 246 GLY A C   1 
ATOM   1946 O  O   . GLY A 1 237 ? -7.833  -5.626  -35.786 1.00 35.84 ? 246 GLY A O   1 
ATOM   1947 N  N   . LEU A 1 238 ? -7.494  -6.372  -33.668 1.00 35.30 ? 247 LEU A N   1 
ATOM   1948 C  CA  . LEU A 1 238 ? -6.073  -6.048  -33.601 1.00 35.64 ? 247 LEU A CA  1 
ATOM   1949 C  C   . LEU A 1 238 ? -5.253  -7.335  -33.611 1.00 37.02 ? 247 LEU A C   1 
ATOM   1950 O  O   . LEU A 1 238 ? -5.624  -8.315  -32.960 1.00 36.84 ? 247 LEU A O   1 
ATOM   1951 C  CB  . LEU A 1 238 ? -5.788  -5.259  -32.321 1.00 33.86 ? 247 LEU A CB  1 
ATOM   1952 C  CG  . LEU A 1 238 ? -4.381  -4.711  -32.065 1.00 34.54 ? 247 LEU A CG  1 
ATOM   1953 C  CD1 . LEU A 1 238 ? -4.095  -3.522  -32.977 1.00 35.94 ? 247 LEU A CD1 1 
ATOM   1954 C  CD2 . LEU A 1 238 ? -4.245  -4.296  -30.622 1.00 30.93 ? 247 LEU A CD2 1 
ATOM   1955 N  N   . VAL A 1 239 ? -4.146  -7.332  -34.356 1.00 38.20 ? 248 VAL A N   1 
ATOM   1956 C  CA  . VAL A 1 239 ? -3.187  -8.438  -34.322 1.00 37.80 ? 248 VAL A CA  1 
ATOM   1957 C  C   . VAL A 1 239 ? -2.271  -8.218  -33.112 1.00 35.91 ? 248 VAL A C   1 
ATOM   1958 O  O   . VAL A 1 239 ? -1.540  -7.231  -33.043 1.00 31.49 ? 248 VAL A O   1 
ATOM   1959 C  CB  . VAL A 1 239 ? -2.375  -8.548  -35.623 1.00 39.67 ? 248 VAL A CB  1 
ATOM   1960 C  CG1 . VAL A 1 239 ? -1.340  -9.689  -35.557 1.00 40.85 ? 248 VAL A CG1 1 
ATOM   1961 C  CG2 . VAL A 1 239 ? -3.308  -8.776  -36.814 1.00 44.10 ? 248 VAL A CG2 1 
ATOM   1962 N  N   . TYR A 1 240 ? -2.372  -9.123  -32.140 1.00 36.65 ? 249 TYR A N   1 
ATOM   1963 C  CA  . TYR A 1 240 ? -1.438  -9.202  -31.029 1.00 36.21 ? 249 TYR A CA  1 
ATOM   1964 C  C   . TYR A 1 240 ? -0.341  -10.120 -31.520 1.00 39.01 ? 249 TYR A C   1 
ATOM   1965 O  O   . TYR A 1 240 ? -0.437  -11.345 -31.393 1.00 35.59 ? 249 TYR A O   1 
ATOM   1966 C  CB  . TYR A 1 240 ? -2.106  -9.765  -29.778 1.00 37.09 ? 249 TYR A CB  1 
ATOM   1967 C  CG  . TYR A 1 240 ? -3.182  -8.872  -29.237 1.00 34.29 ? 249 TYR A CG  1 
ATOM   1968 C  CD1 . TYR A 1 240 ? -4.471  -8.929  -29.750 1.00 33.73 ? 249 TYR A CD1 1 
ATOM   1969 C  CD2 . TYR A 1 240 ? -2.912  -7.949  -28.228 1.00 35.94 ? 249 TYR A CD2 1 
ATOM   1970 C  CE1 . TYR A 1 240 ? -5.469  -8.104  -29.267 1.00 34.61 ? 249 TYR A CE1 1 
ATOM   1971 C  CE2 . TYR A 1 240 ? -3.907  -7.115  -27.740 1.00 34.68 ? 249 TYR A CE2 1 
ATOM   1972 C  CZ  . TYR A 1 240 ? -5.185  -7.203  -28.267 1.00 32.40 ? 249 TYR A CZ  1 
ATOM   1973 O  OH  . TYR A 1 240 ? -6.186  -6.401  -27.803 1.00 31.22 ? 249 TYR A OH  1 
ATOM   1974 N  N   . GLU A 1 241 ? 0.680   -9.510  -32.116 1.00 40.89 ? 250 GLU A N   1 
ATOM   1975 C  CA  . GLU A 1 241 ? 1.743   -10.241 -32.816 1.00 43.96 ? 250 GLU A CA  1 
ATOM   1976 C  C   . GLU A 1 241 ? 2.491   -11.167 -31.861 1.00 44.44 ? 250 GLU A C   1 
ATOM   1977 O  O   . GLU A 1 241 ? 2.876   -10.752 -30.771 1.00 43.32 ? 250 GLU A O   1 
ATOM   1978 C  CB  . GLU A 1 241 ? 2.719   -9.252  -33.460 1.00 43.21 ? 250 GLU A CB  1 
ATOM   1979 C  CG  . GLU A 1 241 ? 3.683   -9.867  -34.454 1.00 47.79 ? 250 GLU A CG  1 
ATOM   1980 C  CD  . GLU A 1 241 ? 4.713   -8.869  -34.933 1.00 49.51 ? 250 GLU A CD  1 
ATOM   1981 O  OE1 . GLU A 1 241 ? 5.448   -8.329  -34.076 1.00 52.19 ? 250 GLU A OE1 1 
ATOM   1982 O  OE2 . GLU A 1 241 ? 4.786   -8.625  -36.160 1.00 54.89 ? 250 GLU A OE2 1 
ATOM   1983 N  N   . GLY A 1 242 ? 2.662   -12.427 -32.266 1.00 47.45 ? 251 GLY A N   1 
ATOM   1984 C  CA  . GLY A 1 242 ? 3.362   -13.423 -31.453 1.00 48.10 ? 251 GLY A CA  1 
ATOM   1985 C  C   . GLY A 1 242 ? 2.512   -14.203 -30.463 1.00 47.64 ? 251 GLY A C   1 
ATOM   1986 O  O   . GLY A 1 242 ? 2.954   -15.242 -29.986 1.00 49.69 ? 251 GLY A O   1 
ATOM   1987 N  N   . PHE A 1 243 ? 1.304   -13.725 -30.148 1.00 46.80 ? 252 PHE A N   1 
ATOM   1988 C  CA  . PHE A 1 243 ? 0.415   -14.414 -29.200 1.00 46.05 ? 252 PHE A CA  1 
ATOM   1989 C  C   . PHE A 1 243 ? -0.707  -15.144 -29.944 1.00 46.71 ? 252 PHE A C   1 
ATOM   1990 O  O   . PHE A 1 243 ? -0.885  -16.351 -29.765 1.00 47.61 ? 252 PHE A O   1 
ATOM   1991 C  CB  . PHE A 1 243 ? -0.150  -13.440 -28.159 1.00 42.04 ? 252 PHE A CB  1 
ATOM   1992 C  CG  . PHE A 1 243 ? -0.653  -14.123 -26.914 1.00 42.59 ? 252 PHE A CG  1 
ATOM   1993 C  CD1 . PHE A 1 243 ? 0.229   -14.467 -25.886 1.00 42.77 ? 252 PHE A CD1 1 
ATOM   1994 C  CD2 . PHE A 1 243 ? -1.998  -14.445 -26.776 1.00 39.24 ? 252 PHE A CD2 1 
ATOM   1995 C  CE1 . PHE A 1 243 ? -0.229  -15.110 -24.733 1.00 42.82 ? 252 PHE A CE1 1 
ATOM   1996 C  CE2 . PHE A 1 243 ? -2.473  -15.089 -25.628 1.00 41.74 ? 252 PHE A CE2 1 
ATOM   1997 C  CZ  . PHE A 1 243 ? -1.585  -15.424 -24.603 1.00 43.12 ? 252 PHE A CZ  1 
ATOM   1998 N  N   . TRP A 1 244 ? -1.454  -14.404 -30.763 1.00 45.06 ? 253 TRP A N   1 
ATOM   1999 C  CA  . TRP A 1 244 ? -2.414  -14.979 -31.712 1.00 47.27 ? 253 TRP A CA  1 
ATOM   2000 C  C   . TRP A 1 244 ? -2.040  -14.567 -33.129 1.00 48.82 ? 253 TRP A C   1 
ATOM   2001 O  O   . TRP A 1 244 ? -1.594  -13.440 -33.354 1.00 48.75 ? 253 TRP A O   1 
ATOM   2002 C  CB  . TRP A 1 244 ? -3.830  -14.488 -31.433 1.00 44.96 ? 253 TRP A CB  1 
ATOM   2003 C  CG  . TRP A 1 244 ? -4.412  -14.950 -30.162 1.00 43.60 ? 253 TRP A CG  1 
ATOM   2004 C  CD1 . TRP A 1 244 ? -4.724  -16.231 -29.821 1.00 46.64 ? 253 TRP A CD1 1 
ATOM   2005 C  CD2 . TRP A 1 244 ? -4.798  -14.131 -29.060 1.00 43.51 ? 253 TRP A CD2 1 
ATOM   2006 N  NE1 . TRP A 1 244 ? -5.263  -16.265 -28.561 1.00 45.14 ? 253 TRP A NE1 1 
ATOM   2007 C  CE2 . TRP A 1 244 ? -5.325  -14.987 -28.070 1.00 45.84 ? 253 TRP A CE2 1 
ATOM   2008 C  CE3 . TRP A 1 244 ? -4.732  -12.752 -28.800 1.00 41.46 ? 253 TRP A CE3 1 
ATOM   2009 C  CZ2 . TRP A 1 244 ? -5.796  -14.510 -26.840 1.00 37.58 ? 253 TRP A CZ2 1 
ATOM   2010 C  CZ3 . TRP A 1 244 ? -5.201  -12.281 -27.582 1.00 40.73 ? 253 TRP A CZ3 1 
ATOM   2011 C  CH2 . TRP A 1 244 ? -5.724  -13.159 -26.617 1.00 39.96 ? 253 TRP A CH2 1 
ATOM   2012 N  N   . GLU A 1 245 ? -2.246  -15.480 -34.076 1.00 52.03 ? 254 GLU A N   1 
ATOM   2013 C  CA  . GLU A 1 245 ? -2.005  -15.219 -35.500 1.00 53.18 ? 254 GLU A CA  1 
ATOM   2014 C  C   . GLU A 1 245 ? -3.105  -14.343 -36.105 1.00 52.09 ? 254 GLU A C   1 
ATOM   2015 O  O   . GLU A 1 245 ? -2.813  -13.431 -36.881 1.00 50.96 ? 254 GLU A O   1 
ATOM   2016 C  CB  . GLU A 1 245 ? -1.927  -16.534 -36.283 1.00 56.04 ? 254 GLU A CB  1 
ATOM   2017 C  CG  . GLU A 1 245 ? -0.783  -17.444 -35.861 1.00 62.10 ? 254 GLU A CG  1 
ATOM   2018 C  CD  . GLU A 1 245 ? -0.658  -18.706 -36.710 0.00 61.42 ? 254 GLU A CD  1 
ATOM   2019 O  OE1 . GLU A 1 245 ? -1.585  -19.015 -37.490 0.00 62.62 ? 254 GLU A OE1 1 
ATOM   2020 O  OE2 . GLU A 1 245 ? 0.379   -19.392 -36.593 0.00 63.65 ? 254 GLU A OE2 1 
ATOM   2021 N  N   . ASP A 1 246 ? -4.359  -14.648 -35.764 1.00 50.62 ? 255 ASP A N   1 
ATOM   2022 C  CA  . ASP A 1 246 ? -5.519  -13.925 -36.285 1.00 50.07 ? 255 ASP A CA  1 
ATOM   2023 C  C   . ASP A 1 246 ? -5.783  -12.660 -35.473 1.00 47.91 ? 255 ASP A C   1 
ATOM   2024 O  O   . ASP A 1 246 ? -5.510  -12.635 -34.271 1.00 46.06 ? 255 ASP A O   1 
ATOM   2025 C  CB  . ASP A 1 246 ? -6.778  -14.803 -36.247 1.00 50.65 ? 255 ASP A CB  1 
ATOM   2026 C  CG  . ASP A 1 246 ? -6.784  -15.892 -37.317 1.00 56.63 ? 255 ASP A CG  1 
ATOM   2027 O  OD1 . ASP A 1 246 ? -5.895  -15.915 -38.200 1.00 58.52 ? 255 ASP A OD1 1 
ATOM   2028 O  OD2 . ASP A 1 246 ? -7.707  -16.733 -37.272 1.00 63.65 ? 255 ASP A OD2 1 
ATOM   2029 N  N   . PRO A 1 247 ? -6.338  -11.613 -36.120 1.00 46.33 ? 256 PRO A N   1 
ATOM   2030 C  CA  . PRO A 1 247 ? -6.713  -10.431 -35.351 1.00 43.18 ? 256 PRO A CA  1 
ATOM   2031 C  C   . PRO A 1 247 ? -7.880  -10.748 -34.411 1.00 40.49 ? 256 PRO A C   1 
ATOM   2032 O  O   . PRO A 1 247 ? -8.745  -11.573 -34.740 1.00 38.05 ? 256 PRO A O   1 
ATOM   2033 C  CB  . PRO A 1 247 ? -7.109  -9.415  -36.426 1.00 44.72 ? 256 PRO A CB  1 
ATOM   2034 C  CG  . PRO A 1 247 ? -7.545  -10.250 -37.582 1.00 46.92 ? 256 PRO A CG  1 
ATOM   2035 C  CD  . PRO A 1 247 ? -6.654  -11.454 -37.555 1.00 47.98 ? 256 PRO A CD  1 
ATOM   2036 N  N   . LYS A 1 248 ? -7.855  -10.113 -33.243 1.00 35.93 ? 257 LYS A N   1 
ATOM   2037 C  CA  . LYS A 1 248 ? -8.819  -10.354 -32.181 1.00 36.30 ? 257 LYS A CA  1 
ATOM   2038 C  C   . LYS A 1 248 ? -9.515  -9.056  -31.811 1.00 35.86 ? 257 LYS A C   1 
ATOM   2039 O  O   . LYS A 1 248 ? -8.867  -8.003  -31.693 1.00 34.22 ? 257 LYS A O   1 
ATOM   2040 C  CB  . LYS A 1 248 ? -8.117  -10.940 -30.949 1.00 34.80 ? 257 LYS A CB  1 
ATOM   2041 C  CG  . LYS A 1 248 ? -7.391  -12.271 -31.188 1.00 36.17 ? 257 LYS A CG  1 
ATOM   2042 C  CD  . LYS A 1 248 ? -8.338  -13.376 -31.617 1.00 36.83 ? 257 LYS A CD  1 
ATOM   2043 C  CE  . LYS A 1 248 ? -7.616  -14.703 -31.801 1.00 41.08 ? 257 LYS A CE  1 
ATOM   2044 N  NZ  . LYS A 1 248 ? -8.587  -15.779 -32.175 1.00 44.30 ? 257 LYS A NZ  1 
ATOM   2045 N  N   . GLU A 1 249 ? -10.834 -9.148  -31.624 1.00 34.65 ? 258 GLU A N   1 
ATOM   2046 C  CA  . GLU A 1 249 ? -11.662 -8.000  -31.303 1.00 33.48 ? 258 GLU A CA  1 
ATOM   2047 C  C   . GLU A 1 249 ? -11.909 -7.935  -29.806 1.00 31.92 ? 258 GLU A C   1 
ATOM   2048 O  O   . GLU A 1 249 ? -12.330 -8.916  -29.190 1.00 36.06 ? 258 GLU A O   1 
ATOM   2049 C  CB  . GLU A 1 249 ? -13.012 -8.072  -32.022 1.00 32.63 ? 258 GLU A CB  1 
ATOM   2050 C  CG  . GLU A 1 249 ? -12.966 -7.799  -33.515 1.00 35.87 ? 258 GLU A CG  1 
ATOM   2051 C  CD  . GLU A 1 249 ? -14.359 -7.824  -34.114 1.00 38.45 ? 258 GLU A CD  1 
ATOM   2052 O  OE1 . GLU A 1 249 ? -14.959 -8.913  -34.160 1.00 46.69 ? 258 GLU A OE1 1 
ATOM   2053 O  OE2 . GLU A 1 249 ? -14.872 -6.758  -34.509 1.00 43.04 ? 258 GLU A OE2 1 
ATOM   2054 N  N   . PHE A 1 250 ? -11.643 -6.773  -29.228 1.00 30.44 ? 259 PHE A N   1 
ATOM   2055 C  CA  . PHE A 1 250 ? -11.970 -6.491  -27.841 1.00 29.65 ? 259 PHE A CA  1 
ATOM   2056 C  C   . PHE A 1 250 ? -12.535 -5.091  -27.754 1.00 28.47 ? 259 PHE A C   1 
ATOM   2057 O  O   . PHE A 1 250 ? -12.020 -4.165  -28.386 1.00 28.45 ? 259 PHE A O   1 
ATOM   2058 C  CB  . PHE A 1 250 ? -10.737 -6.641  -26.948 1.00 30.17 ? 259 PHE A CB  1 
ATOM   2059 C  CG  . PHE A 1 250 ? -10.196 -8.045  -26.910 1.00 29.99 ? 259 PHE A CG  1 
ATOM   2060 C  CD1 . PHE A 1 250 ? -10.849 -9.032  -26.171 1.00 35.13 ? 259 PHE A CD1 1 
ATOM   2061 C  CD2 . PHE A 1 250 ? -9.054  -8.389  -27.627 1.00 30.30 ? 259 PHE A CD2 1 
ATOM   2062 C  CE1 . PHE A 1 250 ? -10.369 -10.354 -26.146 1.00 28.88 ? 259 PHE A CE1 1 
ATOM   2063 C  CE2 . PHE A 1 250 ? -8.558  -9.696  -27.598 1.00 31.51 ? 259 PHE A CE2 1 
ATOM   2064 C  CZ  . PHE A 1 250 ? -9.218  -10.680 -26.857 1.00 33.07 ? 259 PHE A CZ  1 
ATOM   2065 N  N   . ALA A 1 251 ? -13.604 -4.963  -26.973 1.00 28.95 ? 260 ALA A N   1 
ATOM   2066 C  CA  . ALA A 1 251 ? -14.298 -3.711  -26.764 1.00 27.17 ? 260 ALA A CA  1 
ATOM   2067 C  C   . ALA A 1 251 ? -13.460 -2.752  -25.942 1.00 26.03 ? 260 ALA A C   1 
ATOM   2068 O  O   . ALA A 1 251 ? -12.744 -3.165  -25.016 1.00 26.47 ? 260 ALA A O   1 
ATOM   2069 C  CB  . ALA A 1 251 ? -15.641 -3.955  -26.051 1.00 27.08 ? 260 ALA A CB  1 
ATOM   2070 N  N   . GLY A 1 252 ? -13.591 -1.468  -26.267 1.00 25.60 ? 261 GLY A N   1 
ATOM   2071 C  CA  . GLY A 1 252 ? -13.028 -0.397  -25.473 1.00 26.59 ? 261 GLY A CA  1 
ATOM   2072 C  C   . GLY A 1 252 ? -13.771 -0.247  -24.164 1.00 26.61 ? 261 GLY A C   1 
ATOM   2073 O  O   . GLY A 1 252 ? -14.806 -0.888  -23.943 1.00 27.95 ? 261 GLY A O   1 
ATOM   2074 N  N   . GLY A 1 253 ? -13.245 0.604   -23.296 1.00 24.07 ? 262 GLY A N   1 
ATOM   2075 C  CA  . GLY A 1 253 ? -13.784 0.778   -21.958 1.00 26.19 ? 262 GLY A CA  1 
ATOM   2076 C  C   . GLY A 1 253 ? -15.248 1.201   -21.932 1.00 26.19 ? 262 GLY A C   1 
ATOM   2077 O  O   . GLY A 1 253 ? -15.743 1.838   -22.866 1.00 23.66 ? 262 GLY A O   1 
ATOM   2078 N  N   . SER A 1 254 ? -15.927 0.817   -20.857 1.00 26.83 ? 263 SER A N   1 
ATOM   2079 C  CA  . SER A 1 254 ? -17.332 1.148   -20.638 1.00 26.54 ? 263 SER A CA  1 
ATOM   2080 C  C   . SER A 1 254 ? -17.590 1.049   -19.152 1.00 27.51 ? 263 SER A C   1 
ATOM   2081 O  O   . SER A 1 254 ? -17.042 0.166   -18.492 1.00 26.87 ? 263 SER A O   1 
ATOM   2082 C  CB  . SER A 1 254 ? -18.237 0.198   -21.433 1.00 30.15 ? 263 SER A CB  1 
ATOM   2083 O  OG  . SER A 1 254 ? -19.602 0.337   -21.076 1.00 28.69 ? 263 SER A OG  1 
ATOM   2084 N  N   . ALA A 1 255 ? -18.400 1.962   -18.605 1.00 26.81 ? 264 ALA A N   1 
ATOM   2085 C  CA  . ALA A 1 255 ? -18.869 1.794   -17.230 1.00 26.66 ? 264 ALA A CA  1 
ATOM   2086 C  C   . ALA A 1 255 ? -19.959 0.717   -17.154 1.00 24.90 ? 264 ALA A C   1 
ATOM   2087 O  O   . ALA A 1 255 ? -20.438 0.402   -16.073 1.00 28.33 ? 264 ALA A O   1 
ATOM   2088 C  CB  . ALA A 1 255 ? -19.337 3.117   -16.642 1.00 28.27 ? 264 ALA A CB  1 
ATOM   2089 N  N   . GLY A 1 256 ? -20.350 0.154   -18.297 1.00 24.49 ? 265 GLY A N   1 
ATOM   2090 C  CA  . GLY A 1 256 ? -20.951 -1.178  -18.351 1.00 25.82 ? 265 GLY A CA  1 
ATOM   2091 C  C   . GLY A 1 256 ? -20.086 -2.258  -17.703 1.00 24.49 ? 265 GLY A C   1 
ATOM   2092 O  O   . GLY A 1 256 ? -20.602 -3.247  -17.200 1.00 21.77 ? 265 GLY A O   1 
ATOM   2093 N  N   . GLN A 1 257 ? -18.769 -2.051  -17.711 1.00 24.98 ? 266 GLN A N   1 
ATOM   2094 C  CA  . GLN A 1 257 ? -17.822 -2.927  -17.024 1.00 25.60 ? 266 GLN A CA  1 
ATOM   2095 C  C   . GLN A 1 257 ? -17.727 -2.640  -15.522 1.00 26.50 ? 266 GLN A C   1 
ATOM   2096 O  O   . GLN A 1 257 ? -17.020 -3.352  -14.806 1.00 25.60 ? 266 GLN A O   1 
ATOM   2097 C  CB  . GLN A 1 257 ? -16.433 -2.800  -17.652 1.00 26.03 ? 266 GLN A CB  1 
ATOM   2098 C  CG  . GLN A 1 257 ? -16.402 -3.050  -19.162 1.00 22.02 ? 266 GLN A CG  1 
ATOM   2099 C  CD  . GLN A 1 257 ? -15.132 -2.573  -19.827 1.00 22.15 ? 266 GLN A CD  1 
ATOM   2100 O  OE1 . GLN A 1 257 ? -14.395 -1.748  -19.280 1.00 23.62 ? 266 GLN A OE1 1 
ATOM   2101 N  NE2 . GLN A 1 257 ? -14.891 -3.053  -21.040 1.00 23.82 ? 266 GLN A NE2 1 
ATOM   2102 N  N   . SER A 1 258 ? -18.421 -1.606  -15.041 1.00 25.02 ? 267 SER A N   1 
ATOM   2103 C  CA  . SER A 1 258 ? -18.503 -1.358  -13.612 1.00 25.32 ? 267 SER A CA  1 
ATOM   2104 C  C   . SER A 1 258 ? -19.354 -2.421  -12.958 1.00 25.75 ? 267 SER A C   1 
ATOM   2105 O  O   . SER A 1 258 ? -20.496 -2.645  -13.359 1.00 25.40 ? 267 SER A O   1 
ATOM   2106 C  CB  . SER A 1 258 ? -19.110 0.004   -13.292 1.00 25.74 ? 267 SER A CB  1 
ATOM   2107 O  OG  . SER A 1 258 ? -19.298 0.095   -11.896 1.00 23.42 ? 267 SER A OG  1 
ATOM   2108 N  N   . SER A 1 259 ? -18.793 -3.065  -11.944 1.00 25.61 ? 268 SER A N   1 
ATOM   2109 C  CA  . SER A 1 259 ? -19.507 -4.080  -11.215 1.00 27.68 ? 268 SER A CA  1 
ATOM   2110 C  C   . SER A 1 259 ? -20.582 -3.517  -10.271 1.00 28.89 ? 268 SER A C   1 
ATOM   2111 O  O   . SER A 1 259 ? -21.547 -4.220  -10.023 1.00 29.28 ? 268 SER A O   1 
ATOM   2112 C  CB  . SER A 1 259 ? -18.530 -4.967  -10.442 1.00 29.41 ? 268 SER A CB  1 
ATOM   2113 O  OG  . SER A 1 259 ? -17.589 -5.565  -11.315 1.00 30.77 ? 268 SER A OG  1 
ATOM   2114 N  N   A VAL A 1 260 ? -20.416 -2.287  -9.749  0.50 29.65 ? 269 VAL A N   1 
ATOM   2115 N  N   B VAL A 1 260 ? -20.431 -2.287  -9.775  0.50 29.38 ? 269 VAL A N   1 
ATOM   2116 C  CA  A VAL A 1 260 ? -21.392 -1.710  -8.786  0.50 30.76 ? 269 VAL A CA  1 
ATOM   2117 C  CA  B VAL A 1 260 ? -21.368 -1.761  -8.773  0.50 30.07 ? 269 VAL A CA  1 
ATOM   2118 C  C   A VAL A 1 260 ? -22.788 -1.562  -9.370  0.50 30.02 ? 269 VAL A C   1 
ATOM   2119 C  C   B VAL A 1 260 ? -22.777 -1.510  -9.343  0.50 29.61 ? 269 VAL A C   1 
ATOM   2120 O  O   A VAL A 1 260 ? -23.770 -1.956  -8.736  0.50 30.77 ? 269 VAL A O   1 
ATOM   2121 O  O   B VAL A 1 260 ? -23.764 -1.804  -8.669  0.50 30.54 ? 269 VAL A O   1 
ATOM   2122 C  CB  A VAL A 1 260 ? -20.992 -0.314  -8.142  0.50 32.03 ? 269 VAL A CB  1 
ATOM   2123 C  CB  B VAL A 1 260 ? -20.798 -0.519  -7.998  0.50 30.63 ? 269 VAL A CB  1 
ATOM   2124 C  CG1 A VAL A 1 260 ? -19.830 -0.448  -7.223  0.50 34.73 ? 269 VAL A CG1 1 
ATOM   2125 C  CG1 B VAL A 1 260 ? -20.844 0.764   -8.823  0.50 29.37 ? 269 VAL A CG1 1 
ATOM   2126 C  CG2 A VAL A 1 260 ? -20.711 0.774   -9.159  0.50 32.41 ? 269 VAL A CG2 1 
ATOM   2127 C  CG2 B VAL A 1 260 ? -21.544 -0.325  -6.669  0.50 32.31 ? 269 VAL A CG2 1 
ATOM   2128 N  N   . PHE A 1 261 ? -22.868 -1.016  -10.578 1.00 28.19 ? 270 PHE A N   1 
ATOM   2129 C  CA  . PHE A 1 261 ? -24.169 -0.747  -11.215 1.00 29.84 ? 270 PHE A CA  1 
ATOM   2130 C  C   . PHE A 1 261 ? -24.823 -2.005  -11.751 1.00 30.79 ? 270 PHE A C   1 
ATOM   2131 O  O   . PHE A 1 261 ? -26.045 -2.154  -11.649 1.00 29.48 ? 270 PHE A O   1 
ATOM   2132 C  CB  . PHE A 1 261 ? -24.048 0.332   -12.274 1.00 32.62 ? 270 PHE A CB  1 
ATOM   2133 C  CG  . PHE A 1 261 ? -23.472 1.598   -11.730 1.00 36.19 ? 270 PHE A CG  1 
ATOM   2134 C  CD1 . PHE A 1 261 ? -24.131 2.277   -10.702 1.00 36.98 ? 270 PHE A CD1 1 
ATOM   2135 C  CD2 . PHE A 1 261 ? -22.242 2.072   -12.171 1.00 36.74 ? 270 PHE A CD2 1 
ATOM   2136 C  CE1 . PHE A 1 261 ? -23.592 3.431   -10.151 1.00 38.27 ? 270 PHE A CE1 1 
ATOM   2137 C  CE2 . PHE A 1 261 ? -21.693 3.232   -11.622 1.00 40.23 ? 270 PHE A CE2 1 
ATOM   2138 C  CZ  . PHE A 1 261 ? -22.375 3.905   -10.610 1.00 38.67 ? 270 PHE A CZ  1 
ATOM   2139 N  N   . GLN A 1 262 ? -24.013 -2.918  -12.281 1.00 27.81 ? 271 GLN A N   1 
ATOM   2140 C  CA  . GLN A 1 262 ? -24.501 -4.251  -12.606 1.00 28.80 ? 271 GLN A CA  1 
ATOM   2141 C  C   . GLN A 1 262 ? -25.014 -4.994  -11.357 1.00 28.55 ? 271 GLN A C   1 
ATOM   2142 O  O   . GLN A 1 262 ? -25.997 -5.707  -11.432 1.00 29.89 ? 271 GLN A O   1 
ATOM   2143 C  CB  . GLN A 1 262 ? -23.413 -5.064  -13.316 1.00 29.97 ? 271 GLN A CB  1 
ATOM   2144 C  CG  . GLN A 1 262 ? -23.075 -4.560  -14.730 1.00 27.22 ? 271 GLN A CG  1 
ATOM   2145 C  CD  . GLN A 1 262 ? -23.124 -5.653  -15.805 1.00 31.06 ? 271 GLN A CD  1 
ATOM   2146 O  OE1 . GLN A 1 262 ? -23.770 -6.678  -15.629 1.00 26.42 ? 271 GLN A OE1 1 
ATOM   2147 N  NE2 . GLN A 1 262 ? -22.462 -5.413  -16.935 1.00 21.55 ? 271 GLN A NE2 1 
ATOM   2148 N  N   A CYS A 1 263 ? -24.307 -4.800  -10.247 0.50 30.51 ? 272 CYS A N   1 
ATOM   2149 N  N   B CYS A 1 263 ? -24.337 -4.814  -10.222 0.50 28.46 ? 272 CYS A N   1 
ATOM   2150 C  CA  A CYS A 1 263 ? -24.619 -5.366  -8.935  0.50 31.39 ? 272 CYS A CA  1 
ATOM   2151 C  CA  B CYS A 1 263 ? -24.723 -5.465  -8.960  0.50 30.30 ? 272 CYS A CA  1 
ATOM   2152 C  C   A CYS A 1 263 ? -26.017 -4.999  -8.426  0.50 31.82 ? 272 CYS A C   1 
ATOM   2153 C  C   B CYS A 1 263 ? -26.080 -5.016  -8.440  0.50 30.98 ? 272 CYS A C   1 
ATOM   2154 O  O   A CYS A 1 263 ? -26.769 -5.868  -7.984  0.50 30.58 ? 272 CYS A O   1 
ATOM   2155 O  O   B CYS A 1 263 ? -26.867 -5.847  -7.987  0.50 29.72 ? 272 CYS A O   1 
ATOM   2156 C  CB  A CYS A 1 263 ? -23.550 -4.872  -7.949  0.50 32.36 ? 272 CYS A CB  1 
ATOM   2157 C  CB  B CYS A 1 263 ? -23.674 -5.247  -7.861  0.50 30.83 ? 272 CYS A CB  1 
ATOM   2158 S  SG  A CYS A 1 263 ? -23.753 -5.272  -6.260  0.50 39.22 ? 272 CYS A SG  1 
ATOM   2159 S  SG  B CYS A 1 263 ? -22.390 -6.491  -7.867  0.50 35.42 ? 272 CYS A SG  1 
ATOM   2160 N  N   . PHE A 1 264 ? -26.352 -3.713  -8.494  1.00 30.92 ? 273 PHE A N   1 
ATOM   2161 C  CA  . PHE A 1 264 ? -27.654 -3.217  -8.036  1.00 34.10 ? 273 PHE A CA  1 
ATOM   2162 C  C   . PHE A 1 264 ? -28.786 -3.507  -9.006  1.00 33.43 ? 273 PHE A C   1 
ATOM   2163 O  O   . PHE A 1 264 ? -29.911 -3.713  -8.560  1.00 32.98 ? 273 PHE A O   1 
ATOM   2164 C  CB  . PHE A 1 264 ? -27.568 -1.748  -7.606  1.00 38.34 ? 273 PHE A CB  1 
ATOM   2165 C  CG  . PHE A 1 264 ? -26.732 -1.562  -6.367  1.00 41.45 ? 273 PHE A CG  1 
ATOM   2166 C  CD1 . PHE A 1 264 ? -27.052 -2.255  -5.188  1.00 44.69 ? 273 PHE A CD1 1 
ATOM   2167 C  CD2 . PHE A 1 264 ? -25.601 -0.747  -6.376  1.00 44.36 ? 273 PHE A CD2 1 
ATOM   2168 C  CE1 . PHE A 1 264 ? -26.272 -2.122  -4.040  1.00 44.79 ? 273 PHE A CE1 1 
ATOM   2169 C  CE2 . PHE A 1 264 ? -24.820 -0.607  -5.229  1.00 46.40 ? 273 PHE A CE2 1 
ATOM   2170 C  CZ  . PHE A 1 264 ? -25.155 -1.298  -4.063  1.00 46.93 ? 273 PHE A CZ  1 
ATOM   2171 N  N   . ASP A 1 265 ? -28.493 -3.593  -10.307 1.00 31.47 ? 274 ASP A N   1 
ATOM   2172 C  CA  . ASP A 1 265 ? -29.478 -4.121  -11.261 1.00 31.64 ? 274 ASP A CA  1 
ATOM   2173 C  C   . ASP A 1 265 ? -29.856 -5.553  -10.905 1.00 29.36 ? 274 ASP A C   1 
ATOM   2174 O  O   . ASP A 1 265 ? -31.044 -5.876  -10.804 1.00 25.87 ? 274 ASP A O   1 
ATOM   2175 C  CB  . ASP A 1 265 ? -28.991 -4.030  -12.716 1.00 30.34 ? 274 ASP A CB  1 
ATOM   2176 C  CG  . ASP A 1 265 ? -29.005 -2.602  -13.250 1.00 37.90 ? 274 ASP A CG  1 
ATOM   2177 O  OD1 . ASP A 1 265 ? -29.848 -1.789  -12.814 1.00 35.00 ? 274 ASP A OD1 1 
ATOM   2178 O  OD2 . ASP A 1 265 ? -28.167 -2.296  -14.118 1.00 39.87 ? 274 ASP A OD2 1 
ATOM   2179 N  N   . VAL A 1 266 ? -28.843 -6.390  -10.681 1.00 30.02 ? 275 VAL A N   1 
ATOM   2180 C  CA  . VAL A 1 266 ? -29.063 -7.778  -10.248 1.00 31.60 ? 275 VAL A CA  1 
ATOM   2181 C  C   . VAL A 1 266 ? -29.793 -7.836  -8.907  1.00 31.46 ? 275 VAL A C   1 
ATOM   2182 O  O   . VAL A 1 266 ? -30.787 -8.559  -8.766  1.00 31.41 ? 275 VAL A O   1 
ATOM   2183 C  CB  . VAL A 1 266 ? -27.726 -8.571  -10.138 1.00 32.50 ? 275 VAL A CB  1 
ATOM   2184 C  CG1 . VAL A 1 266 ? -27.936 -9.942  -9.468  1.00 34.13 ? 275 VAL A CG1 1 
ATOM   2185 C  CG2 . VAL A 1 266 ? -27.112 -8.770  -11.510 1.00 29.67 ? 275 VAL A CG2 1 
ATOM   2186 N  N   . LEU A 1 267 ? -29.290 -7.088  -7.926  1.00 30.78 ? 276 LEU A N   1 
ATOM   2187 C  CA  . LEU A 1 267 ? -29.871 -7.099  -6.579  1.00 34.09 ? 276 LEU A CA  1 
ATOM   2188 C  C   . LEU A 1 267 ? -31.357 -6.757  -6.618  1.00 33.37 ? 276 LEU A C   1 
ATOM   2189 O  O   . LEU A 1 267 ? -32.162 -7.425  -5.983  1.00 36.02 ? 276 LEU A O   1 
ATOM   2190 C  CB  . LEU A 1 267 ? -29.141 -6.125  -5.638  1.00 33.63 ? 276 LEU A CB  1 
ATOM   2191 C  CG  . LEU A 1 267 ? -29.592 -6.189  -4.169  1.00 36.59 ? 276 LEU A CG  1 
ATOM   2192 C  CD1 . LEU A 1 267 ? -29.089 -7.462  -3.490  1.00 40.31 ? 276 LEU A CD1 1 
ATOM   2193 C  CD2 . LEU A 1 267 ? -29.128 -4.965  -3.410  1.00 39.87 ? 276 LEU A CD2 1 
ATOM   2194 N  N   . LEU A 1 268 ? -31.705 -5.736  -7.397  1.00 30.99 ? 277 LEU A N   1 
ATOM   2195 C  CA  . LEU A 1 268 ? -33.079 -5.240  -7.482  1.00 31.62 ? 277 LEU A CA  1 
ATOM   2196 C  C   . LEU A 1 268 ? -33.951 -5.971  -8.519  1.00 31.12 ? 277 LEU A C   1 
ATOM   2197 O  O   . LEU A 1 268 ? -35.082 -5.564  -8.757  1.00 32.23 ? 277 LEU A O   1 
ATOM   2198 C  CB  . LEU A 1 268 ? -33.046 -3.734  -7.749  1.00 30.31 ? 277 LEU A CB  1 
ATOM   2199 C  CG  . LEU A 1 268 ? -32.330 -2.934  -6.643  1.00 30.99 ? 277 LEU A CG  1 
ATOM   2200 C  CD1 . LEU A 1 268 ? -31.985 -1.544  -7.111  1.00 30.99 ? 277 LEU A CD1 1 
ATOM   2201 C  CD2 . LEU A 1 268 ? -33.185 -2.867  -5.345  1.00 31.44 ? 277 LEU A CD2 1 
ATOM   2202 N  N   . GLY A 1 269 ? -33.432 -7.046  -9.120  1.00 29.27 ? 278 GLY A N   1 
ATOM   2203 C  CA  . GLY A 1 269 ? -34.179 -7.857  -10.078 1.00 31.11 ? 278 GLY A CA  1 
ATOM   2204 C  C   . GLY A 1 269 ? -34.569 -7.122  -11.346 1.00 31.20 ? 278 GLY A C   1 
ATOM   2205 O  O   . GLY A 1 269 ? -35.597 -7.422  -11.948 1.00 31.37 ? 278 GLY A O   1 
ATOM   2206 N  N   . ILE A 1 270 ? -33.747 -6.157  -11.752 1.00 33.18 ? 279 ILE A N   1 
ATOM   2207 C  CA  . ILE A 1 270 ? -33.994 -5.377  -12.975 1.00 33.76 ? 279 ILE A CA  1 
ATOM   2208 C  C   . ILE A 1 270 ? -33.779 -6.200  -14.284 1.00 34.19 ? 279 ILE A C   1 
ATOM   2209 O  O   . ILE A 1 270 ? -34.350 -5.872  -15.322 1.00 35.25 ? 279 ILE A O   1 
ATOM   2210 C  CB  . ILE A 1 270 ? -33.200 -4.034  -12.919 1.00 32.69 ? 279 ILE A CB  1 
ATOM   2211 C  CG1 . ILE A 1 270 ? -33.809 -3.145  -11.818 1.00 35.20 ? 279 ILE A CG1 1 
ATOM   2212 C  CG2 . ILE A 1 270 ? -33.250 -3.293  -14.251 1.00 33.42 ? 279 ILE A CG2 1 
ATOM   2213 C  CD1 . ILE A 1 270 ? -32.942 -2.037  -11.308 1.00 35.50 ? 279 ILE A CD1 1 
ATOM   2214 N  N   A GLN A 1 271 ? -32.974 -7.259  -14.218 0.50 35.41 ? 280 GLN A N   1 
ATOM   2215 N  N   B GLN A 1 271 ? -32.952 -7.241  -14.204 0.50 35.64 ? 280 GLN A N   1 
ATOM   2216 C  CA  A GLN A 1 271 ? -32.782 -8.196  -15.343 0.50 35.49 ? 280 GLN A CA  1 
ATOM   2217 C  CA  B GLN A 1 271 ? -32.732 -8.197  -15.302 0.50 35.86 ? 280 GLN A CA  1 
ATOM   2218 C  C   A GLN A 1 271 ? -32.266 -7.519  -16.628 0.50 33.95 ? 280 GLN A C   1 
ATOM   2219 C  C   B GLN A 1 271 ? -32.265 -7.525  -16.608 0.50 34.22 ? 280 GLN A C   1 
ATOM   2220 O  O   A GLN A 1 271 ? -32.838 -7.693  -17.715 0.50 35.01 ? 280 GLN A O   1 
ATOM   2221 O  O   B GLN A 1 271 ? -32.863 -7.705  -17.679 0.50 35.32 ? 280 GLN A O   1 
ATOM   2222 C  CB  A GLN A 1 271 ? -34.071 -8.979  -15.635 0.50 36.16 ? 280 GLN A CB  1 
ATOM   2223 C  CB  B GLN A 1 271 ? -33.979 -9.072  -15.524 0.50 36.99 ? 280 GLN A CB  1 
ATOM   2224 C  CG  A GLN A 1 271 ? -34.608 -9.811  -14.479 0.50 37.25 ? 280 GLN A CG  1 
ATOM   2225 C  CG  B GLN A 1 271 ? -34.430 -9.896  -14.299 0.50 39.59 ? 280 GLN A CG  1 
ATOM   2226 C  CD  A GLN A 1 271 ? -35.902 -10.530 -14.832 0.50 39.70 ? 280 GLN A CD  1 
ATOM   2227 C  CD  B GLN A 1 271 ? -33.447 -10.989 -13.854 0.50 42.71 ? 280 GLN A CD  1 
ATOM   2228 O  OE1 A GLN A 1 271 ? -36.458 -10.342 -15.918 0.50 42.49 ? 280 GLN A OE1 1 
ATOM   2229 O  OE1 B GLN A 1 271 ? -33.542 -11.493 -12.737 0.50 44.46 ? 280 GLN A OE1 1 
ATOM   2230 N  NE2 A GLN A 1 271 ? -36.395 -11.350 -13.909 0.50 40.05 ? 280 GLN A NE2 1 
ATOM   2231 N  NE2 B GLN A 1 271 ? -32.519 -11.366 -14.725 0.50 46.67 ? 280 GLN A NE2 1 
ATOM   2232 N  N   . GLN A 1 272 ? -31.188 -6.753  -16.493 1.00 32.25 ? 281 GLN A N   1 
ATOM   2233 C  CA  . GLN A 1 272 ? -30.595 -6.030  -17.634 1.00 33.06 ? 281 GLN A CA  1 
ATOM   2234 C  C   . GLN A 1 272 ? -29.970 -6.964  -18.655 1.00 32.29 ? 281 GLN A C   1 
ATOM   2235 O  O   . GLN A 1 272 ? -29.922 -6.633  -19.837 1.00 32.63 ? 281 GLN A O   1 
ATOM   2236 C  CB  . GLN A 1 272 ? -29.496 -5.054  -17.179 1.00 31.67 ? 281 GLN A CB  1 
ATOM   2237 C  CG  . GLN A 1 272 ? -29.948 -3.898  -16.344 1.00 37.01 ? 281 GLN A CG  1 
ATOM   2238 C  CD  . GLN A 1 272 ? -30.738 -2.831  -17.088 1.00 30.23 ? 281 GLN A CD  1 
ATOM   2239 O  OE1 . GLN A 1 272 ? -31.052 -2.956  -18.269 1.00 34.01 ? 281 GLN A OE1 1 
ATOM   2240 N  NE2 . GLN A 1 272 ? -31.072 -1.767  -16.375 1.00 33.26 ? 281 GLN A NE2 1 
ATOM   2241 N  N   . THR A 1 273 ? -29.476 -8.109  -18.180 1.00 32.13 ? 282 THR A N   1 
ATOM   2242 C  CA  . THR A 1 273 ? -28.823 -9.113  -19.020 1.00 32.01 ? 282 THR A CA  1 
ATOM   2243 C  C   . THR A 1 273 ? -29.773 -10.201 -19.524 1.00 34.18 ? 282 THR A C   1 
ATOM   2244 O  O   . THR A 1 273 ? -29.352 -11.075 -20.274 1.00 35.47 ? 282 THR A O   1 
ATOM   2245 C  CB  . THR A 1 273 ? -27.650 -9.770  -18.265 1.00 30.54 ? 282 THR A CB  1 
ATOM   2246 O  OG1 . THR A 1 273 ? -28.122 -10.318 -17.030 1.00 32.09 ? 282 THR A OG1 1 
ATOM   2247 C  CG2 . THR A 1 273 ? -26.569 -8.735  -17.971 1.00 31.02 ? 282 THR A CG2 1 
ATOM   2248 N  N   . ALA A 1 274 ? -31.044 -10.144 -19.130 1.00 33.95 ? 283 ALA A N   1 
ATOM   2249 C  CA  . ALA A 1 274 ? -32.034 -11.123 -19.566 1.00 35.25 ? 283 ALA A CA  1 
ATOM   2250 C  C   . ALA A 1 274 ? -32.649 -10.756 -20.917 1.00 34.78 ? 283 ALA A C   1 
ATOM   2251 O  O   . ALA A 1 274 ? -32.779 -9.573  -21.256 1.00 32.06 ? 283 ALA A O   1 
ATOM   2252 C  CB  . ALA A 1 274 ? -33.135 -11.246 -18.524 1.00 39.02 ? 283 ALA A CB  1 
ATOM   2253 N  N   . GLY A 1 275 ? -33.006 -11.784 -21.690 1.00 33.01 ? 284 GLY A N   1 
ATOM   2254 C  CA  . GLY A 1 275 ? -33.948 -11.647 -22.802 1.00 36.28 ? 284 GLY A CA  1 
ATOM   2255 C  C   . GLY A 1 275 ? -33.451 -11.839 -24.220 1.00 36.10 ? 284 GLY A C   1 
ATOM   2256 O  O   . GLY A 1 275 ? -34.269 -11.945 -25.132 1.00 40.49 ? 284 GLY A O   1 
ATOM   2257 N  N   . GLY A 1 276 ? -32.139 -11.872 -24.425 1.00 34.08 ? 285 GLY A N   1 
ATOM   2258 C  CA  . GLY A 1 276 ? -31.575 -12.104 -25.760 1.00 37.40 ? 285 GLY A CA  1 
ATOM   2259 C  C   . GLY A 1 276 ? -31.377 -10.874 -26.649 1.00 36.96 ? 285 GLY A C   1 
ATOM   2260 O  O   . GLY A 1 276 ? -30.952 -11.010 -27.798 1.00 37.23 ? 285 GLY A O   1 
ATOM   2261 N  N   . GLY A 1 277 ? -31.664 -9.682  -26.123 1.00 35.91 ? 286 GLY A N   1 
ATOM   2262 C  CA  . GLY A 1 277 ? -31.530 -8.445  -26.886 1.00 35.08 ? 286 GLY A CA  1 
ATOM   2263 C  C   . GLY A 1 277 ? -30.122 -7.881  -26.959 1.00 32.91 ? 286 GLY A C   1 
ATOM   2264 O  O   . GLY A 1 277 ? -29.196 -8.355  -26.291 1.00 30.15 ? 286 GLY A O   1 
ATOM   2265 N  N   . HIS A 1 278 ? -29.994 -6.818  -27.747 1.00 35.01 ? 287 HIS A N   1 
ATOM   2266 C  CA  . HIS A 1 278 ? -28.715 -6.152  -28.019 1.00 34.37 ? 287 HIS A CA  1 
ATOM   2267 C  C   . HIS A 1 278 ? -28.051 -5.568  -26.770 1.00 31.75 ? 287 HIS A C   1 
ATOM   2268 O  O   . HIS A 1 278 ? -26.856 -5.770  -26.557 1.00 27.49 ? 287 HIS A O   1 
ATOM   2269 C  CB  . HIS A 1 278 ? -28.917 -5.035  -29.060 1.00 37.84 ? 287 HIS A CB  1 
ATOM   2270 C  CG  . HIS A 1 278 ? -27.642 -4.451  -29.582 1.00 39.50 ? 287 HIS A CG  1 
ATOM   2271 N  ND1 . HIS A 1 278 ? -26.935 -3.477  -28.907 1.00 51.81 ? 287 HIS A ND1 1 
ATOM   2272 C  CD2 . HIS A 1 278 ? -26.950 -4.697  -30.721 1.00 50.11 ? 287 HIS A CD2 1 
ATOM   2273 C  CE1 . HIS A 1 278 ? -25.857 -3.154  -29.602 1.00 45.55 ? 287 HIS A CE1 1 
ATOM   2274 N  NE2 . HIS A 1 278 ? -25.843 -3.878  -30.707 1.00 50.80 ? 287 HIS A NE2 1 
ATOM   2275 N  N   . ALA A 1 279 ? -28.831 -4.840  -25.967 1.00 30.14 ? 288 ALA A N   1 
ATOM   2276 C  CA  . ALA A 1 279 ? -28.312 -4.158  -24.783 1.00 28.05 ? 288 ALA A CA  1 
ATOM   2277 C  C   . ALA A 1 279 ? -27.908 -5.170  -23.711 1.00 27.77 ? 288 ALA A C   1 
ATOM   2278 O  O   . ALA A 1 279 ? -26.853 -5.027  -23.092 1.00 22.12 ? 288 ALA A O   1 
ATOM   2279 C  CB  . ALA A 1 279 ? -29.339 -3.176  -24.225 1.00 28.87 ? 288 ALA A CB  1 
ATOM   2280 N  N   . ALA A 1 280 ? -28.755 -6.182  -23.509 1.00 26.79 ? 289 ALA A N   1 
ATOM   2281 C  CA  . ALA A 1 280 ? -28.460 -7.298  -22.607 1.00 27.73 ? 289 ALA A CA  1 
ATOM   2282 C  C   . ALA A 1 280 ? -27.161 -8.012  -22.971 1.00 27.94 ? 289 ALA A C   1 
ATOM   2283 O  O   . ALA A 1 280 ? -26.365 -8.325  -22.091 1.00 28.85 ? 289 ALA A O   1 
ATOM   2284 C  CB  . ALA A 1 280 ? -29.622 -8.306  -22.604 1.00 28.87 ? 289 ALA A CB  1 
ATOM   2285 N  N   . GLN A 1 281 ? -26.979 -8.268  -24.267 1.00 29.79 ? 290 GLN A N   1 
ATOM   2286 C  CA  . GLN A 1 281 ? -25.795 -8.949  -24.802 1.00 30.39 ? 290 GLN A CA  1 
ATOM   2287 C  C   . GLN A 1 281 ? -24.530 -8.170  -24.463 1.00 28.23 ? 290 GLN A C   1 
ATOM   2288 O  O   . GLN A 1 281 ? -23.530 -8.753  -24.029 1.00 26.40 ? 290 GLN A O   1 
ATOM   2289 C  CB  . GLN A 1 281 ? -25.910 -9.122  -26.330 1.00 31.92 ? 290 GLN A CB  1 
ATOM   2290 C  CG  . GLN A 1 281 ? -24.854 -10.039 -26.951 1.00 35.29 ? 290 GLN A CG  1 
ATOM   2291 C  CD  . GLN A 1 281 ? -25.097 -10.369 -28.427 1.00 42.10 ? 290 GLN A CD  1 
ATOM   2292 O  OE1 . GLN A 1 281 ? -26.238 -10.412 -28.904 1.00 50.50 ? 290 GLN A OE1 1 
ATOM   2293 N  NE2 . GLN A 1 281 ? -24.011 -10.637 -29.150 1.00 55.26 ? 290 GLN A NE2 1 
ATOM   2294 N  N   . PHE A 1 282 ? -24.598 -6.852  -24.637 1.00 26.21 ? 291 PHE A N   1 
ATOM   2295 C  CA  . PHE A 1 282 ? -23.458 -5.974  -24.378 1.00 26.32 ? 291 PHE A CA  1 
ATOM   2296 C  C   . PHE A 1 282 ? -23.060 -5.989  -22.909 1.00 25.26 ? 291 PHE A C   1 
ATOM   2297 O  O   . PHE A 1 282 ? -21.902 -6.189  -22.586 1.00 25.78 ? 291 PHE A O   1 
ATOM   2298 C  CB  . PHE A 1 282 ? -23.762 -4.546  -24.835 1.00 26.58 ? 291 PHE A CB  1 
ATOM   2299 C  CG  . PHE A 1 282 ? -22.666 -3.567  -24.518 1.00 26.52 ? 291 PHE A CG  1 
ATOM   2300 C  CD1 . PHE A 1 282 ? -21.494 -3.543  -25.276 1.00 27.27 ? 291 PHE A CD1 1 
ATOM   2301 C  CD2 . PHE A 1 282 ? -22.800 -2.677  -23.459 1.00 24.04 ? 291 PHE A CD2 1 
ATOM   2302 C  CE1 . PHE A 1 282 ? -20.478 -2.641  -24.980 1.00 27.93 ? 291 PHE A CE1 1 
ATOM   2303 C  CE2 . PHE A 1 282 ? -21.793 -1.772  -23.160 1.00 26.56 ? 291 PHE A CE2 1 
ATOM   2304 C  CZ  . PHE A 1 282 ? -20.624 -1.761  -23.928 1.00 24.95 ? 291 PHE A CZ  1 
ATOM   2305 N  N   . LEU A 1 283 ? -24.038 -5.784  -22.032 1.00 24.60 ? 292 LEU A N   1 
ATOM   2306 C  CA  . LEU A 1 283 ? -23.796 -5.758  -20.594 1.00 23.76 ? 292 LEU A CA  1 
ATOM   2307 C  C   . LEU A 1 283 ? -23.337 -7.104  -20.038 1.00 22.28 ? 292 LEU A C   1 
ATOM   2308 O  O   . LEU A 1 283 ? -22.516 -7.133  -19.133 1.00 20.51 ? 292 LEU A O   1 
ATOM   2309 C  CB  . LEU A 1 283 ? -25.034 -5.236  -19.846 1.00 24.35 ? 292 LEU A CB  1 
ATOM   2310 C  CG  . LEU A 1 283 ? -25.350 -3.733  -20.046 1.00 22.03 ? 292 LEU A CG  1 
ATOM   2311 C  CD1 . LEU A 1 283 ? -26.688 -3.372  -19.385 1.00 23.78 ? 292 LEU A CD1 1 
ATOM   2312 C  CD2 . LEU A 1 283 ? -24.273 -2.832  -19.514 1.00 19.79 ? 292 LEU A CD2 1 
ATOM   2313 N  N   . GLN A 1 284 ? -23.854 -8.205  -20.577 1.00 24.25 ? 293 GLN A N   1 
ATOM   2314 C  CA  . GLN A 1 284 ? -23.329 -9.529  -20.241 1.00 26.32 ? 293 GLN A CA  1 
ATOM   2315 C  C   . GLN A 1 284 ? -21.886 -9.691  -20.710 1.00 24.50 ? 293 GLN A C   1 
ATOM   2316 O  O   . GLN A 1 284 ? -21.045 -10.126 -19.937 1.00 25.79 ? 293 GLN A O   1 
ATOM   2317 C  CB  . GLN A 1 284 ? -24.193 -10.642 -20.827 1.00 28.21 ? 293 GLN A CB  1 
ATOM   2318 C  CG  . GLN A 1 284 ? -23.813 -12.058 -20.348 1.00 32.91 ? 293 GLN A CG  1 
ATOM   2319 C  CD  . GLN A 1 284 ? -23.960 -12.279 -18.834 1.00 37.65 ? 293 GLN A CD  1 
ATOM   2320 O  OE1 . GLN A 1 284 ? -24.894 -11.778 -18.206 1.00 38.07 ? 293 GLN A OE1 1 
ATOM   2321 N  NE2 . GLN A 1 284 ? -23.043 -13.054 -18.256 1.00 41.08 ? 293 GLN A NE2 1 
ATOM   2322 N  N   . ASP A 1 285 ? -21.607 -9.335  -21.965 1.00 26.69 ? 294 ASP A N   1 
ATOM   2323 C  CA  . ASP A 1 285 ? -20.234 -9.365  -22.509 1.00 25.14 ? 294 ASP A CA  1 
ATOM   2324 C  C   . ASP A 1 285 ? -19.269 -8.548  -21.648 1.00 23.76 ? 294 ASP A C   1 
ATOM   2325 O  O   . ASP A 1 285 ? -18.168 -9.006  -21.355 1.00 20.75 ? 294 ASP A O   1 
ATOM   2326 C  CB  . ASP A 1 285 ? -20.200 -8.853  -23.952 1.00 27.21 ? 294 ASP A CB  1 
ATOM   2327 C  CG  . ASP A 1 285 ? -18.869 -9.157  -24.674 1.00 34.40 ? 294 ASP A CG  1 
ATOM   2328 O  OD1 . ASP A 1 285 ? -18.333 -10.283 -24.541 1.00 35.59 ? 294 ASP A OD1 1 
ATOM   2329 O  OD2 . ASP A 1 285 ? -18.378 -8.268  -25.407 1.00 36.28 ? 294 ASP A OD2 1 
ATOM   2330 N  N   . MET A 1 286 ? -19.707 -7.366  -21.215 1.00 23.92 ? 295 MET A N   1 
ATOM   2331 C  CA  . MET A 1 286 ? -18.881 -6.481  -20.376 1.00 23.38 ? 295 MET A CA  1 
ATOM   2332 C  C   . MET A 1 286 ? -18.437 -7.106  -19.062 1.00 23.03 ? 295 MET A C   1 
ATOM   2333 O  O   . MET A 1 286 ? -17.406 -6.718  -18.527 1.00 25.38 ? 295 MET A O   1 
ATOM   2334 C  CB  . MET A 1 286 ? -19.582 -5.136  -20.118 1.00 24.15 ? 295 MET A CB  1 
ATOM   2335 C  CG  . MET A 1 286 ? -19.574 -4.148  -21.299 1.00 25.32 ? 295 MET A CG  1 
ATOM   2336 S  SD  . MET A 1 286 ? -18.017 -4.077  -22.228 1.00 24.77 ? 295 MET A SD  1 
ATOM   2337 C  CE  . MET A 1 286 ? -18.317 -5.260  -23.532 1.00 24.97 ? 295 MET A CE  1 
ATOM   2338 N  N   . ARG A 1 287 ? -19.135 -8.134  -18.598 1.00 23.48 ? 296 ARG A N   1 
ATOM   2339 C  CA  . ARG A 1 287 ? -18.716 -8.861  -17.365 1.00 24.18 ? 296 ARG A CA  1 
ATOM   2340 C  C   . ARG A 1 287 ? -17.376 -9.591  -17.577 1.00 25.53 ? 296 ARG A C   1 
ATOM   2341 O  O   . ARG A 1 287 ? -16.659 -9.738  -16.608 1.00 25.41 ? 296 ARG A O   1 
ATOM   2342 C  CB  . ARG A 1 287 ? -19.842 -9.785  -16.890 1.00 24.43 ? 296 ARG A CB  1 
ATOM   2343 C  CG  . ARG A 1 287 ? -21.137 -9.062  -16.561 1.00 23.33 ? 296 ARG A CG  1 
ATOM   2344 C  CD  . ARG A 1 287 ? -22.228 -10.033 -16.163 1.00 26.33 ? 296 ARG A CD  1 
ATOM   2345 N  NE  . ARG A 1 287 ? -23.375 -9.357  -15.585 1.00 30.32 ? 296 ARG A NE  1 
ATOM   2346 C  CZ  . ARG A 1 287 ? -24.343 -9.959  -14.909 1.00 32.98 ? 296 ARG A CZ  1 
ATOM   2347 N  NH1 . ARG A 1 287 ? -24.217 -11.226 -14.563 1.00 35.77 ? 296 ARG A NH1 1 
ATOM   2348 N  NH2 . ARG A 1 287 ? -25.431 -9.289  -14.579 1.00 31.16 ? 296 ARG A NH2 1 
ATOM   2349 N  N   . ARG A 1 288 ? -17.021 -9.929  -18.813 1.00 25.74 ? 297 ARG A N   1 
ATOM   2350 C  CA  . ARG A 1 288 ? -15.726 -10.590 -19.122 1.00 29.69 ? 297 ARG A CA  1 
ATOM   2351 C  C   . ARG A 1 288 ? -14.581 -9.579  -19.012 1.00 27.18 ? 297 ARG A C   1 
ATOM   2352 O  O   . ARG A 1 288 ? -13.434 -10.002 -18.941 1.00 27.84 ? 297 ARG A O   1 
ATOM   2353 C  CB  . ARG A 1 288 ? -15.740 -11.170 -20.532 1.00 31.52 ? 297 ARG A CB  1 
ATOM   2354 C  CG  . ARG A 1 288 ? -16.853 -12.158 -20.833 1.00 37.20 ? 297 ARG A CG  1 
ATOM   2355 C  CD  . ARG A 1 288 ? -16.994 -12.150 -22.341 1.00 45.83 ? 297 ARG A CD  1 
ATOM   2356 N  NE  . ARG A 1 288 ? -15.904 -12.795 -23.055 1.00 57.88 ? 297 ARG A NE  1 
ATOM   2357 C  CZ  . ARG A 1 288 ? -15.098 -12.185 -23.915 1.00 56.94 ? 297 ARG A CZ  1 
ATOM   2358 N  NH1 . ARG A 1 288 ? -15.520 -11.132 -24.590 1.00 56.25 ? 297 ARG A NH1 1 
ATOM   2359 N  NH2 . ARG A 1 288 ? -13.868 -12.631 -24.093 1.00 61.28 ? 297 ARG A NH2 1 
ATOM   2360 N  N   . TYR A 1 289 ? -14.918 -8.292  -18.984 1.00 25.64 ? 298 TYR A N   1 
ATOM   2361 C  CA  . TYR A 1 289 ? -13.905 -7.212  -18.872 1.00 24.24 ? 298 TYR A CA  1 
ATOM   2362 C  C   . TYR A 1 289 ? -13.740 -6.841  -17.394 1.00 25.59 ? 298 TYR A C   1 
ATOM   2363 O  O   . TYR A 1 289 ? -12.894 -5.995  -17.095 1.00 26.27 ? 298 TYR A O   1 
ATOM   2364 C  CB  . TYR A 1 289 ? -14.344 -6.103  -19.833 1.00 22.54 ? 298 TYR A CB  1 
ATOM   2365 C  CG  . TYR A 1 289 ? -14.305 -6.430  -21.318 1.00 23.76 ? 298 TYR A CG  1 
ATOM   2366 C  CD1 . TYR A 1 289 ? -15.223 -7.301  -21.891 1.00 22.38 ? 298 TYR A CD1 1 
ATOM   2367 C  CD2 . TYR A 1 289 ? -13.359 -5.846  -22.151 1.00 24.10 ? 298 TYR A CD2 1 
ATOM   2368 C  CE1 . TYR A 1 289 ? -15.184 -7.602  -23.240 1.00 22.53 ? 298 TYR A CE1 1 
ATOM   2369 C  CE2 . TYR A 1 289 ? -13.314 -6.136  -23.502 1.00 22.54 ? 298 TYR A CE2 1 
ATOM   2370 C  CZ  . TYR A 1 289 ? -14.230 -7.014  -24.048 1.00 22.15 ? 298 TYR A CZ  1 
ATOM   2371 O  OH  . TYR A 1 289 ? -14.188 -7.300  -25.377 1.00 24.60 ? 298 TYR A OH  1 
ATOM   2372 N  N   . MET A 1 290 ? -14.536 -7.440  -16.508 1.00 25.47 ? 299 MET A N   1 
ATOM   2373 C  CA  . MET A 1 290 ? -14.406 -7.232  -15.066 1.00 24.70 ? 299 MET A CA  1 
ATOM   2374 C  C   . MET A 1 290 ? -13.393 -8.208  -14.471 1.00 28.10 ? 299 MET A C   1 
ATOM   2375 O  O   . MET A 1 290 ? -13.241 -9.309  -14.987 1.00 27.73 ? 299 MET A O   1 
ATOM   2376 C  CB  . MET A 1 290 ? -15.735 -7.484  -14.363 1.00 22.90 ? 299 MET A CB  1 
ATOM   2377 C  CG  . MET A 1 290 ? -16.846 -6.551  -14.770 1.00 21.61 ? 299 MET A CG  1 
ATOM   2378 S  SD  . MET A 1 290 ? -18.399 -7.044  -13.996 1.00 23.35 ? 299 MET A SD  1 
ATOM   2379 C  CE  . MET A 1 290 ? -19.495 -5.884  -14.799 1.00 18.39 ? 299 MET A CE  1 
ATOM   2380 N  N   . PRO A 1 291 ? -12.725 -7.827  -13.363 1.00 27.50 ? 300 PRO A N   1 
ATOM   2381 C  CA  . PRO A 1 291 ? -11.894 -8.813  -12.665 1.00 29.84 ? 300 PRO A CA  1 
ATOM   2382 C  C   . PRO A 1 291 ? -12.693 -10.049 -12.262 1.00 31.01 ? 300 PRO A C   1 
ATOM   2383 O  O   . PRO A 1 291 ? -13.848 -9.905  -11.858 1.00 32.67 ? 300 PRO A O   1 
ATOM   2384 C  CB  . PRO A 1 291 ? -11.418 -8.056  -11.426 1.00 29.32 ? 300 PRO A CB  1 
ATOM   2385 C  CG  . PRO A 1 291 ? -11.436 -6.626  -11.846 1.00 29.49 ? 300 PRO A CG  1 
ATOM   2386 C  CD  . PRO A 1 291 ? -12.660 -6.508  -12.704 1.00 27.37 ? 300 PRO A CD  1 
ATOM   2387 N  N   . PRO A 1 292 ? -12.093 -11.253 -12.374 1.00 33.13 ? 301 PRO A N   1 
ATOM   2388 C  CA  . PRO A 1 292 ? -12.839 -12.510 -12.186 1.00 33.49 ? 301 PRO A CA  1 
ATOM   2389 C  C   . PRO A 1 292 ? -13.569 -12.637 -10.843 1.00 34.47 ? 301 PRO A C   1 
ATOM   2390 O  O   . PRO A 1 292 ? -14.671 -13.176 -10.799 1.00 34.24 ? 301 PRO A O   1 
ATOM   2391 C  CB  . PRO A 1 292 ? -11.752 -13.590 -12.331 1.00 34.24 ? 301 PRO A CB  1 
ATOM   2392 C  CG  . PRO A 1 292 ? -10.456 -12.866 -12.112 1.00 34.05 ? 301 PRO A CG  1 
ATOM   2393 C  CD  . PRO A 1 292 ? -10.670 -11.515 -12.668 1.00 34.59 ? 301 PRO A CD  1 
ATOM   2394 N  N   . ALA A 1 293 ? -12.964 -12.132 -9.771  1.00 34.81 ? 302 ALA A N   1 
ATOM   2395 C  CA  . ALA A 1 293 ? -13.595 -12.127 -8.449  1.00 33.96 ? 302 ALA A CA  1 
ATOM   2396 C  C   . ALA A 1 293 ? -14.897 -11.312 -8.435  1.00 31.66 ? 302 ALA A C   1 
ATOM   2397 O  O   . ALA A 1 293 ? -15.844 -11.665 -7.746  1.00 30.16 ? 302 ALA A O   1 
ATOM   2398 C  CB  . ALA A 1 293 ? -12.618 -11.597 -7.401  1.00 36.48 ? 302 ALA A CB  1 
ATOM   2399 N  N   . HIS A 1 294 ? -14.947 -10.251 -9.232  1.00 30.64 ? 303 HIS A N   1 
ATOM   2400 C  CA  . HIS A 1 294 ? -16.121 -9.371  -9.309  1.00 29.39 ? 303 HIS A CA  1 
ATOM   2401 C  C   . HIS A 1 294 ? -17.220 -9.954  -10.199 1.00 29.93 ? 303 HIS A C   1 
ATOM   2402 O  O   . HIS A 1 294 ? -18.409 -9.843  -9.898  1.00 29.76 ? 303 HIS A O   1 
ATOM   2403 C  CB  . HIS A 1 294 ? -15.693 -7.995  -9.808  1.00 28.18 ? 303 HIS A CB  1 
ATOM   2404 C  CG  . HIS A 1 294 ? -14.658 -7.345  -8.943  1.00 28.52 ? 303 HIS A CG  1 
ATOM   2405 N  ND1 . HIS A 1 294 ? -13.963 -6.222  -9.325  1.00 27.31 ? 303 HIS A ND1 1 
ATOM   2406 C  CD2 . HIS A 1 294 ? -14.194 -7.675  -7.717  1.00 27.29 ? 303 HIS A CD2 1 
ATOM   2407 C  CE1 . HIS A 1 294 ? -13.117 -5.886  -8.369  1.00 30.50 ? 303 HIS A CE1 1 
ATOM   2408 N  NE2 . HIS A 1 294 ? -13.237 -6.753  -7.382  1.00 34.11 ? 303 HIS A NE2 1 
ATOM   2409 N  N   . ARG A 1 295 ? -16.788 -10.540 -11.310 1.00 32.61 ? 304 ARG A N   1 
ATOM   2410 C  CA  . ARG A 1 295 ? -17.582 -11.447 -12.160 1.00 32.68 ? 304 ARG A CA  1 
ATOM   2411 C  C   . ARG A 1 295 ? -18.300 -12.500 -11.313 1.00 33.57 ? 304 ARG A C   1 
ATOM   2412 O  O   . ARG A 1 295 ? -19.520 -12.686 -11.419 1.00 33.74 ? 304 ARG A O   1 
ATOM   2413 C  CB  . ARG A 1 295 ? -16.625 -12.155 -13.136 1.00 35.07 ? 304 ARG A CB  1 
ATOM   2414 C  CG  . ARG A 1 295 ? -17.158 -12.532 -14.493 1.00 39.16 ? 304 ARG A CG  1 
ATOM   2415 C  CD  . ARG A 1 295 ? -16.051 -12.396 -15.540 1.00 38.58 ? 304 ARG A CD  1 
ATOM   2416 N  NE  . ARG A 1 295 ? -15.003 -13.402 -15.428 1.00 46.15 ? 304 ARG A NE  1 
ATOM   2417 C  CZ  . ARG A 1 295 ? -13.704 -13.214 -15.690 1.00 41.72 ? 304 ARG A CZ  1 
ATOM   2418 N  NH1 . ARG A 1 295 ? -13.221 -12.027 -16.043 1.00 38.66 ? 304 ARG A NH1 1 
ATOM   2419 N  NH2 . ARG A 1 295 ? -12.864 -14.235 -15.561 1.00 49.75 ? 304 ARG A NH2 1 
ATOM   2420 N  N   . ASN A 1 296 ? -17.521 -13.169 -10.463 1.00 32.89 ? 305 ASN A N   1 
ATOM   2421 C  CA  . ASN A 1 296 ? -18.027 -14.209 -9.578  1.00 34.17 ? 305 ASN A CA  1 
ATOM   2422 C  C   . ASN A 1 296 ? -19.034 -13.672 -8.577  1.00 32.00 ? 305 ASN A C   1 
ATOM   2423 O  O   . ASN A 1 296 ? -20.013 -14.343 -8.264  1.00 30.78 ? 305 ASN A O   1 
ATOM   2424 C  CB  . ASN A 1 296 ? -16.875 -14.885 -8.820  1.00 35.72 ? 305 ASN A CB  1 
ATOM   2425 C  CG  . ASN A 1 296 ? -15.936 -15.655 -9.735  1.00 37.11 ? 305 ASN A CG  1 
ATOM   2426 O  OD1 . ASN A 1 296 ? -16.252 -15.924 -10.895 1.00 31.35 ? 305 ASN A OD1 1 
ATOM   2427 N  ND2 . ASN A 1 296 ? -14.774 -16.020 -9.208  1.00 37.39 ? 305 ASN A ND2 1 
ATOM   2428 N  N   . PHE A 1 297 ? -18.774 -12.471 -8.070  1.00 30.61 ? 306 PHE A N   1 
ATOM   2429 C  CA  . PHE A 1 297 ? -19.682 -11.824 -7.134  1.00 31.68 ? 306 PHE A CA  1 
ATOM   2430 C  C   . PHE A 1 297 ? -21.039 -11.518 -7.788  1.00 30.39 ? 306 PHE A C   1 
ATOM   2431 O  O   . PHE A 1 297 ? -22.071 -11.678 -7.145  1.00 29.57 ? 306 PHE A O   1 
ATOM   2432 C  CB  . PHE A 1 297 ? -19.055 -10.546 -6.567  1.00 31.16 ? 306 PHE A CB  1 
ATOM   2433 C  CG  . PHE A 1 297 ? -19.912 -9.864  -5.545  1.00 30.07 ? 306 PHE A CG  1 
ATOM   2434 C  CD1 . PHE A 1 297 ? -20.103 -10.438 -4.295  1.00 35.12 ? 306 PHE A CD1 1 
ATOM   2435 C  CD2 . PHE A 1 297 ? -20.555 -8.670  -5.841  1.00 28.36 ? 306 PHE A CD2 1 
ATOM   2436 C  CE1 . PHE A 1 297 ? -20.911 -9.828  -3.353  1.00 34.40 ? 306 PHE A CE1 1 
ATOM   2437 C  CE2 . PHE A 1 297 ? -21.362 -8.050  -4.907  1.00 30.55 ? 306 PHE A CE2 1 
ATOM   2438 C  CZ  . PHE A 1 297 ? -21.535 -8.618  -3.658  1.00 30.46 ? 306 PHE A CZ  1 
ATOM   2439 N  N   . LEU A 1 298 ? -21.033 -11.078 -9.051  1.00 28.53 ? 307 LEU A N   1 
ATOM   2440 C  CA  . LEU A 1 298 ? -22.288 -10.852 -9.798  1.00 28.31 ? 307 LEU A CA  1 
ATOM   2441 C  C   . LEU A 1 298 ? -23.074 -12.138 -10.018 1.00 27.43 ? 307 LEU A C   1 
ATOM   2442 O  O   . LEU A 1 298 ? -24.278 -12.177 -9.815  1.00 26.53 ? 307 LEU A O   1 
ATOM   2443 C  CB  . LEU A 1 298 ? -22.024 -10.198 -11.152 1.00 29.50 ? 307 LEU A CB  1 
ATOM   2444 C  CG  . LEU A 1 298 ? -21.853 -8.689  -11.148 1.00 32.78 ? 307 LEU A CG  1 
ATOM   2445 C  CD1 . LEU A 1 298 ? -21.350 -8.242  -12.501 1.00 34.26 ? 307 LEU A CD1 1 
ATOM   2446 C  CD2 . LEU A 1 298 ? -23.174 -8.008  -10.835 1.00 37.22 ? 307 LEU A CD2 1 
ATOM   2447 N  N   . CYS A 1 299 ? -22.367 -13.182 -10.432 1.00 29.97 ? 308 CYS A N   1 
ATOM   2448 C  CA  . CYS A 1 299 ? -22.937 -14.519 -10.591 1.00 31.07 ? 308 CYS A CA  1 
ATOM   2449 C  C   . CYS A 1 299 ? -23.592 -15.016 -9.307  1.00 33.74 ? 308 CYS A C   1 
ATOM   2450 O  O   . CYS A 1 299 ? -24.687 -15.581 -9.330  1.00 32.03 ? 308 CYS A O   1 
ATOM   2451 C  CB  . CYS A 1 299 ? -21.830 -15.486 -11.008 1.00 31.58 ? 308 CYS A CB  1 
ATOM   2452 S  SG  . CYS A 1 299 ? -22.341 -17.176 -11.076 1.00 36.92 ? 308 CYS A SG  1 
ATOM   2453 N  N   . SER A 1 300 ? -22.889 -14.816 -8.195  1.00 35.93 ? 309 SER A N   1 
ATOM   2454 C  CA  . SER A 1 300 ? -23.383 -15.163 -6.872  1.00 37.27 ? 309 SER A CA  1 
ATOM   2455 C  C   . SER A 1 300 ? -24.703 -14.461 -6.557  1.00 35.27 ? 309 SER A C   1 
ATOM   2456 O  O   . SER A 1 300 ? -25.642 -15.099 -6.067  1.00 34.91 ? 309 SER A O   1 
ATOM   2457 C  CB  . SER A 1 300 ? -22.338 -14.807 -5.809  1.00 39.64 ? 309 SER A CB  1 
ATOM   2458 O  OG  . SER A 1 300 ? -22.750 -15.260 -4.528  1.00 53.33 ? 309 SER A OG  1 
ATOM   2459 N  N   . LEU A 1 301 ? -24.770 -13.158 -6.837  1.00 32.81 ? 310 LEU A N   1 
ATOM   2460 C  CA  . LEU A 1 301 ? -25.999 -12.387 -6.619  1.00 34.57 ? 310 LEU A CA  1 
ATOM   2461 C  C   . LEU A 1 301 ? -27.162 -12.906 -7.456  1.00 34.10 ? 310 LEU A C   1 
ATOM   2462 O  O   . LEU A 1 301 ? -28.284 -12.956 -6.981  1.00 32.79 ? 310 LEU A O   1 
ATOM   2463 C  CB  . LEU A 1 301 ? -25.805 -10.893 -6.915  1.00 31.09 ? 310 LEU A CB  1 
ATOM   2464 C  CG  . LEU A 1 301 ? -24.795 -10.085 -6.095  1.00 32.95 ? 310 LEU A CG  1 
ATOM   2465 C  CD1 . LEU A 1 301 ? -25.019 -8.602  -6.306  1.00 31.35 ? 310 LEU A CD1 1 
ATOM   2466 C  CD2 . LEU A 1 301 ? -24.839 -10.416 -4.606  1.00 35.20 ? 310 LEU A CD2 1 
ATOM   2467 N  N   . GLU A 1 302 ? -26.884 -13.286 -8.698  1.00 36.04 ? 311 GLU A N   1 
ATOM   2468 C  CA  . GLU A 1 302 ? -27.928 -13.799 -9.592  1.00 38.45 ? 311 GLU A CA  1 
ATOM   2469 C  C   . GLU A 1 302 ? -28.474 -15.150 -9.160  1.00 37.89 ? 311 GLU A C   1 
ATOM   2470 O  O   . GLU A 1 302 ? -29.614 -15.456 -9.457  1.00 38.54 ? 311 GLU A O   1 
ATOM   2471 C  CB  . GLU A 1 302 ? -27.421 -13.870 -11.033 1.00 37.86 ? 311 GLU A CB  1 
ATOM   2472 C  CG  . GLU A 1 302 ? -27.328 -12.501 -11.654 1.00 41.04 ? 311 GLU A CG  1 
ATOM   2473 C  CD  . GLU A 1 302 ? -26.870 -12.517 -13.084 1.00 39.76 ? 311 GLU A CD  1 
ATOM   2474 O  OE1 . GLU A 1 302 ? -27.251 -11.594 -13.834 1.00 39.37 ? 311 GLU A OE1 1 
ATOM   2475 O  OE2 . GLU A 1 302 ? -26.101 -13.425 -13.457 1.00 47.64 ? 311 GLU A OE2 1 
ATOM   2476 N  N   . SER A 1 303 ? -27.656 -15.940 -8.466  1.00 38.85 ? 312 SER A N   1 
ATOM   2477 C  CA  . SER A 1 303 ? -28.061 -17.245 -7.957  1.00 43.44 ? 312 SER A CA  1 
ATOM   2478 C  C   . SER A 1 303 ? -28.933 -17.149 -6.704  1.00 43.84 ? 312 SER A C   1 
ATOM   2479 O  O   . SER A 1 303 ? -29.646 -18.088 -6.396  1.00 43.61 ? 312 SER A O   1 
ATOM   2480 C  CB  . SER A 1 303 ? -26.829 -18.117 -7.666  1.00 45.47 ? 312 SER A CB  1 
ATOM   2481 O  OG  . SER A 1 303 ? -26.094 -18.392 -8.856  1.00 51.48 ? 312 SER A OG  1 
ATOM   2482 N  N   . ASN A 1 304 ? -28.857 -16.032 -5.981  1.00 44.80 ? 313 ASN A N   1 
ATOM   2483 C  CA  . ASN A 1 304 ? -29.684 -15.806 -4.781  1.00 47.82 ? 313 ASN A CA  1 
ATOM   2484 C  C   . ASN A 1 304 ? -31.126 -15.476 -5.172  1.00 46.12 ? 313 ASN A C   1 
ATOM   2485 O  O   . ASN A 1 304 ? -31.369 -15.015 -6.285  1.00 44.29 ? 313 ASN A O   1 
ATOM   2486 C  CB  . ASN A 1 304 ? -29.108 -14.662 -3.923  1.00 47.80 ? 313 ASN A CB  1 
ATOM   2487 C  CG  . ASN A 1 304 ? -27.692 -14.941 -3.434  1.00 54.36 ? 313 ASN A CG  1 
ATOM   2488 O  OD1 . ASN A 1 304 ? -27.369 -16.053 -3.021  1.00 60.46 ? 313 ASN A OD1 1 
ATOM   2489 N  ND2 . ASN A 1 304 ? -26.840 -13.918 -3.481  1.00 64.64 ? 313 ASN A ND2 1 
ATOM   2490 N  N   . PRO A 1 305 ? -32.093 -15.702 -4.262  1.00 51.05 ? 314 PRO A N   1 
ATOM   2491 C  CA  . PRO A 1 305 ? -33.486 -15.356 -4.605  1.00 51.05 ? 314 PRO A CA  1 
ATOM   2492 C  C   . PRO A 1 305 ? -33.718 -13.860 -4.897  1.00 49.35 ? 314 PRO A C   1 
ATOM   2493 O  O   . PRO A 1 305 ? -32.953 -13.003 -4.445  1.00 48.29 ? 314 PRO A O   1 
ATOM   2494 C  CB  . PRO A 1 305 ? -34.286 -15.829 -3.382  1.00 54.90 ? 314 PRO A CB  1 
ATOM   2495 C  CG  . PRO A 1 305 ? -33.289 -15.958 -2.276  1.00 56.21 ? 314 PRO A CG  1 
ATOM   2496 C  CD  . PRO A 1 305 ? -31.988 -16.308 -2.920  1.00 53.49 ? 314 PRO A CD  1 
ATOM   2497 N  N   . SER A 1 306 ? -34.754 -13.576 -5.681  1.00 48.35 ? 315 SER A N   1 
ATOM   2498 C  CA  . SER A 1 306 ? -35.040 -12.219 -6.145  1.00 46.32 ? 315 SER A CA  1 
ATOM   2499 C  C   . SER A 1 306 ? -35.581 -11.339 -5.012  1.00 44.88 ? 315 SER A C   1 
ATOM   2500 O  O   . SER A 1 306 ? -36.507 -11.730 -4.304  1.00 46.16 ? 315 SER A O   1 
ATOM   2501 C  CB  . SER A 1 306 ? -36.043 -12.252 -7.304  1.00 47.09 ? 315 SER A CB  1 
ATOM   2502 O  OG  . SER A 1 306 ? -36.388 -10.943 -7.734  1.00 48.42 ? 315 SER A OG  1 
ATOM   2503 N  N   . VAL A 1 307 ? -34.976 -10.166 -4.843  1.00 40.88 ? 316 VAL A N   1 
ATOM   2504 C  CA  . VAL A 1 307 ? -35.480 -9.132  -3.937  1.00 42.06 ? 316 VAL A CA  1 
ATOM   2505 C  C   . VAL A 1 307 ? -36.810 -8.572  -4.472  1.00 41.29 ? 316 VAL A C   1 
ATOM   2506 O  O   . VAL A 1 307 ? -37.750 -8.382  -3.701  1.00 39.95 ? 316 VAL A O   1 
ATOM   2507 C  CB  . VAL A 1 307 ? -34.455 -7.973  -3.747  1.00 40.33 ? 316 VAL A CB  1 
ATOM   2508 C  CG1 . VAL A 1 307 ? -35.006 -6.866  -2.841  1.00 43.71 ? 316 VAL A CG1 1 
ATOM   2509 C  CG2 . VAL A 1 307 ? -33.138 -8.498  -3.168  1.00 42.40 ? 316 VAL A CG2 1 
ATOM   2510 N  N   . ARG A 1 308 ? -36.868 -8.307  -5.780  1.00 37.91 ? 317 ARG A N   1 
ATOM   2511 C  CA  . ARG A 1 308 ? -38.076 -7.798  -6.427  1.00 39.64 ? 317 ARG A CA  1 
ATOM   2512 C  C   . ARG A 1 308 ? -39.292 -8.697  -6.182  1.00 41.34 ? 317 ARG A C   1 
ATOM   2513 O  O   . ARG A 1 308 ? -40.353 -8.204  -5.833  1.00 40.10 ? 317 ARG A O   1 
ATOM   2514 C  CB  . ARG A 1 308 ? -37.864 -7.622  -7.933  1.00 37.42 ? 317 ARG A CB  1 
ATOM   2515 C  CG  . ARG A 1 308 ? -39.098 -7.101  -8.680  1.00 38.75 ? 317 ARG A CG  1 
ATOM   2516 C  CD  . ARG A 1 308 ? -38.787 -6.507  -10.057 1.00 39.17 ? 317 ARG A CD  1 
ATOM   2517 N  NE  . ARG A 1 308 ? -39.792 -5.507  -10.436 1.00 38.45 ? 317 ARG A NE  1 
ATOM   2518 C  CZ  . ARG A 1 308 ? -40.941 -5.761  -11.074 1.00 41.49 ? 317 ARG A CZ  1 
ATOM   2519 N  NH1 . ARG A 1 308 ? -41.277 -6.996  -11.446 1.00 50.59 ? 317 ARG A NH1 1 
ATOM   2520 N  NH2 . ARG A 1 308 ? -41.780 -4.762  -11.349 1.00 43.14 ? 317 ARG A NH2 1 
ATOM   2521 N  N   . GLU A 1 309 ? -39.123 -10.004 -6.376  1.00 43.84 ? 318 GLU A N   1 
ATOM   2522 C  CA  . GLU A 1 309 ? -40.207 -10.969 -6.170  1.00 45.89 ? 318 GLU A CA  1 
ATOM   2523 C  C   . GLU A 1 309 ? -40.612 -11.088 -4.706  1.00 45.69 ? 318 GLU A C   1 
ATOM   2524 O  O   . GLU A 1 309 ? -41.796 -11.237 -4.414  1.00 46.44 ? 318 GLU A O   1 
ATOM   2525 C  CB  . GLU A 1 309 ? -39.840 -12.349 -6.720  1.00 48.71 ? 318 GLU A CB  1 
ATOM   2526 C  CG  . GLU A 1 309 ? -39.803 -12.410 -8.239  1.00 54.04 ? 318 GLU A CG  1 
ATOM   2527 C  CD  . GLU A 1 309 ? -41.141 -12.310 -8.926  0.00 53.76 ? 318 GLU A CD  1 
ATOM   2528 O  OE1 . GLU A 1 309 ? -41.261 -11.533 -9.897  0.00 53.35 ? 318 GLU A OE1 1 
ATOM   2529 O  OE2 . GLU A 1 309 ? -42.091 -12.997 -8.491  0.00 55.61 ? 318 GLU A OE2 1 
ATOM   2530 N  N   . PHE A 1 310 ? -39.630 -11.032 -3.803  1.00 44.42 ? 319 PHE A N   1 
ATOM   2531 C  CA  . PHE A 1 310 ? -39.893 -10.991 -2.357  1.00 45.39 ? 319 PHE A CA  1 
ATOM   2532 C  C   . PHE A 1 310 ? -40.753 -9.781  -2.001  1.00 44.44 ? 319 PHE A C   1 
ATOM   2533 O  O   . PHE A 1 310 ? -41.772 -9.930  -1.352  1.00 47.39 ? 319 PHE A O   1 
ATOM   2534 C  CB  . PHE A 1 310 ? -38.588 -10.949 -1.552  1.00 44.63 ? 319 PHE A CB  1 
ATOM   2535 C  CG  . PHE A 1 310 ? -38.782 -11.086 -0.061  1.00 47.41 ? 319 PHE A CG  1 
ATOM   2536 C  CD1 . PHE A 1 310 ? -39.092 -9.971  0.729   1.00 48.18 ? 319 PHE A CD1 1 
ATOM   2537 C  CD2 . PHE A 1 310 ? -38.644 -12.324 0.560   1.00 46.70 ? 319 PHE A CD2 1 
ATOM   2538 C  CE1 . PHE A 1 310 ? -39.277 -10.095 2.112   1.00 48.55 ? 319 PHE A CE1 1 
ATOM   2539 C  CE2 . PHE A 1 310 ? -38.825 -12.458 1.945   1.00 52.22 ? 319 PHE A CE2 1 
ATOM   2540 C  CZ  . PHE A 1 310 ? -39.141 -11.338 2.722   1.00 48.88 ? 319 PHE A CZ  1 
ATOM   2541 N  N   . VAL A 1 311 ? -40.341 -8.593  -2.431  1.00 42.72 ? 320 VAL A N   1 
ATOM   2542 C  CA  . VAL A 1 311 ? -41.100 -7.372  -2.146  1.00 44.35 ? 320 VAL A CA  1 
ATOM   2543 C  C   . VAL A 1 311 ? -42.461 -7.397  -2.844  1.00 45.39 ? 320 VAL A C   1 
ATOM   2544 O  O   . VAL A 1 311 ? -43.469 -7.050  -2.225  1.00 45.86 ? 320 VAL A O   1 
ATOM   2545 C  CB  . VAL A 1 311 ? -40.314 -6.082  -2.510  1.00 41.30 ? 320 VAL A CB  1 
ATOM   2546 C  CG1 . VAL A 1 311 ? -41.181 -4.837  -2.300  1.00 44.96 ? 320 VAL A CG1 1 
ATOM   2547 C  CG2 . VAL A 1 311 ? -39.062 -5.967  -1.650  1.00 38.63 ? 320 VAL A CG2 1 
ATOM   2548 N  N   . LEU A 1 312 ? -42.484 -7.801  -4.115  1.00 45.51 ? 321 LEU A N   1 
ATOM   2549 C  CA  . LEU A 1 312 ? -43.747 -7.928  -4.877  1.00 48.78 ? 321 LEU A CA  1 
ATOM   2550 C  C   . LEU A 1 312 ? -44.793 -8.819  -4.210  1.00 50.68 ? 321 LEU A C   1 
ATOM   2551 O  O   . LEU A 1 312 ? -45.991 -8.540  -4.299  1.00 52.04 ? 321 LEU A O   1 
ATOM   2552 C  CB  . LEU A 1 312 ? -43.508 -8.485  -6.291  1.00 50.28 ? 321 LEU A CB  1 
ATOM   2553 C  CG  . LEU A 1 312 ? -43.362 -7.497  -7.445  1.00 54.00 ? 321 LEU A CG  1 
ATOM   2554 C  CD1 . LEU A 1 312 ? -42.903 -8.235  -8.692  1.00 55.39 ? 321 LEU A CD1 1 
ATOM   2555 C  CD2 . LEU A 1 312 ? -44.677 -6.765  -7.716  1.00 57.91 ? 321 LEU A CD2 1 
ATOM   2556 N  N   . SER A 1 313 ? -44.334 -9.895  -3.573  1.00 50.65 ? 322 SER A N   1 
ATOM   2557 C  CA  . SER A 1 313 ? -45.229 -10.881 -2.975  1.00 52.26 ? 322 SER A CA  1 
ATOM   2558 C  C   . SER A 1 313 ? -45.890 -10.424 -1.667  1.00 53.87 ? 322 SER A C   1 
ATOM   2559 O  O   . SER A 1 313 ? -46.938 -10.958 -1.303  1.00 56.01 ? 322 SER A O   1 
ATOM   2560 C  CB  . SER A 1 313 ? -44.467 -12.186 -2.720  1.00 53.09 ? 322 SER A CB  1 
ATOM   2561 O  OG  . SER A 1 313 ? -43.461 -12.016 -1.732  1.00 52.92 ? 322 SER A OG  1 
ATOM   2562 N  N   . LYS A 1 314 ? -45.302 -9.436  -0.981  1.00 51.41 ? 323 LYS A N   1 
ATOM   2563 C  CA  . LYS A 1 314 ? -45.554 -9.234  0.461   1.00 51.83 ? 323 LYS A CA  1 
ATOM   2564 C  C   . LYS A 1 314 ? -46.722 -8.319  0.857   1.00 51.16 ? 323 LYS A C   1 
ATOM   2565 O  O   . LYS A 1 314 ? -47.196 -8.406  2.002   1.00 53.34 ? 323 LYS A O   1 
ATOM   2566 C  CB  . LYS A 1 314 ? -44.263 -8.803  1.170   1.00 52.66 ? 323 LYS A CB  1 
ATOM   2567 C  CG  . LYS A 1 314 ? -43.234 -9.932  1.262   1.00 54.98 ? 323 LYS A CG  1 
ATOM   2568 C  CD  . LYS A 1 314 ? -43.502 -10.900 2.402   1.00 60.19 ? 323 LYS A CD  1 
ATOM   2569 C  CE  . LYS A 1 314 ? -42.708 -12.193 2.223   1.00 59.82 ? 323 LYS A CE  1 
ATOM   2570 N  NZ  . LYS A 1 314 ? -43.290 -13.068 1.168   0.00 60.52 ? 323 LYS A NZ  1 
ATOM   2571 N  N   . GLY A 1 315 ? -47.196 -7.471  -0.059  1.00 46.70 ? 324 GLY A N   1 
ATOM   2572 C  CA  . GLY A 1 315 ? -48.363 -6.606  0.214   1.00 45.42 ? 324 GLY A CA  1 
ATOM   2573 C  C   . GLY A 1 315 ? -48.067 -5.570  1.289   1.00 42.97 ? 324 GLY A C   1 
ATOM   2574 O  O   . GLY A 1 315 ? -48.889 -5.296  2.158   1.00 43.62 ? 324 GLY A O   1 
ATOM   2575 N  N   . ASP A 1 316 ? -46.880 -4.985  1.180   1.00 41.08 ? 325 ASP A N   1 
ATOM   2576 C  CA  . ASP A 1 316 ? -46.247 -4.199  2.221   1.00 39.98 ? 325 ASP A CA  1 
ATOM   2577 C  C   . ASP A 1 316 ? -45.817 -2.870  1.592   1.00 37.07 ? 325 ASP A C   1 
ATOM   2578 O  O   . ASP A 1 316 ? -44.762 -2.788  0.954   1.00 33.85 ? 325 ASP A O   1 
ATOM   2579 C  CB  . ASP A 1 316 ? -45.028 -4.978  2.746   1.00 38.53 ? 325 ASP A CB  1 
ATOM   2580 C  CG  . ASP A 1 316 ? -44.396 -4.345  3.982   1.00 40.87 ? 325 ASP A CG  1 
ATOM   2581 O  OD1 . ASP A 1 316 ? -44.428 -3.106  4.144   1.00 42.04 ? 325 ASP A OD1 1 
ATOM   2582 O  OD2 . ASP A 1 316 ? -43.864 -5.107  4.806   1.00 43.26 ? 325 ASP A OD2 1 
ATOM   2583 N  N   . ALA A 1 317 ? -46.650 -1.851  1.771   1.00 39.83 ? 326 ALA A N   1 
ATOM   2584 C  CA  . ALA A 1 317 ? -46.426 -0.531  1.189   1.00 39.88 ? 326 ALA A CA  1 
ATOM   2585 C  C   . ALA A 1 317 ? -45.063 0.051   1.576   1.00 39.84 ? 326 ALA A C   1 
ATOM   2586 O  O   . ALA A 1 317 ? -44.392 0.629   0.735   1.00 37.54 ? 326 ALA A O   1 
ATOM   2587 C  CB  . ALA A 1 317 ? -47.555 0.416   1.580   1.00 41.32 ? 326 ALA A CB  1 
ATOM   2588 N  N   . GLY A 1 318 ? -44.647 -0.144  2.833   1.00 41.90 ? 327 GLY A N   1 
ATOM   2589 C  CA  . GLY A 1 318 ? -43.336 0.322   3.316   1.00 40.02 ? 327 GLY A CA  1 
ATOM   2590 C  C   . GLY A 1 318 ? -42.163 -0.261  2.538   1.00 38.25 ? 327 GLY A C   1 
ATOM   2591 O  O   . GLY A 1 318 ? -41.286 0.477   2.081   1.00 36.56 ? 327 GLY A O   1 
ATOM   2592 N  N   . LEU A 1 319 ? -42.160 -1.585  2.380   1.00 37.83 ? 328 LEU A N   1 
ATOM   2593 C  CA  . LEU A 1 319 ? -41.135 -2.280  1.589   1.00 38.14 ? 328 LEU A CA  1 
ATOM   2594 C  C   . LEU A 1 319 ? -41.150 -1.893  0.113   1.00 35.90 ? 328 LEU A C   1 
ATOM   2595 O  O   . LEU A 1 319 ? -40.088 -1.740  -0.491  1.00 32.38 ? 328 LEU A O   1 
ATOM   2596 C  CB  . LEU A 1 319 ? -41.264 -3.813  1.692   1.00 39.48 ? 328 LEU A CB  1 
ATOM   2597 C  CG  . LEU A 1 319 ? -40.505 -4.584  2.770   1.00 46.47 ? 328 LEU A CG  1 
ATOM   2598 C  CD1 . LEU A 1 319 ? -40.822 -6.074  2.621   1.00 50.53 ? 328 LEU A CD1 1 
ATOM   2599 C  CD2 . LEU A 1 319 ? -39.014 -4.379  2.695   1.00 44.84 ? 328 LEU A CD2 1 
ATOM   2600 N  N   . ARG A 1 320 ? -42.345 -1.773  -0.467  1.00 37.52 ? 329 ARG A N   1 
ATOM   2601 C  CA  . ARG A 1 320 ? -42.474 -1.380  -1.880  1.00 38.86 ? 329 ARG A CA  1 
ATOM   2602 C  C   . ARG A 1 320 ? -41.881 0.001   -2.145  1.00 37.01 ? 329 ARG A C   1 
ATOM   2603 O  O   . ARG A 1 320 ? -41.157 0.173   -3.128  1.00 37.82 ? 329 ARG A O   1 
ATOM   2604 C  CB  . ARG A 1 320 ? -43.933 -1.436  -2.363  1.00 39.48 ? 329 ARG A CB  1 
ATOM   2605 C  CG  . ARG A 1 320 ? -44.457 -2.856  -2.585  1.00 44.17 ? 329 ARG A CG  1 
ATOM   2606 C  CD  . ARG A 1 320 ? -45.688 -2.872  -3.499  1.00 47.85 ? 329 ARG A CD  1 
ATOM   2607 N  NE  . ARG A 1 320 ? -46.769 -2.048  -2.961  1.00 50.11 ? 329 ARG A NE  1 
ATOM   2608 C  CZ  . ARG A 1 320 ? -47.676 -2.442  -2.070  1.00 55.13 ? 329 ARG A CZ  1 
ATOM   2609 N  NH1 . ARG A 1 320 ? -47.680 -3.680  -1.575  1.00 60.55 ? 329 ARG A NH1 1 
ATOM   2610 N  NH2 . ARG A 1 320 ? -48.603 -1.576  -1.663  1.00 53.22 ? 329 ARG A NH2 1 
ATOM   2611 N  N   . GLU A 1 321 ? -42.172 0.967   -1.273  1.00 38.28 ? 330 GLU A N   1 
ATOM   2612 C  CA  . GLU A 1 321 ? -41.600 2.322   -1.397  1.00 41.45 ? 330 GLU A CA  1 
ATOM   2613 C  C   . GLU A 1 321 ? -40.083 2.339   -1.274  1.00 39.44 ? 330 GLU A C   1 
ATOM   2614 O  O   . GLU A 1 321 ? -39.414 3.055   -2.009  1.00 38.09 ? 330 GLU A O   1 
ATOM   2615 C  CB  . GLU A 1 321 ? -42.171 3.270   -0.347  1.00 43.09 ? 330 GLU A CB  1 
ATOM   2616 C  CG  . GLU A 1 321 ? -43.635 3.603   -0.525  1.00 48.71 ? 330 GLU A CG  1 
ATOM   2617 C  CD  . GLU A 1 321 ? -44.199 4.344   0.681   1.00 54.52 ? 330 GLU A CD  1 
ATOM   2618 O  OE1 . GLU A 1 321 ? -43.465 5.192   1.247   1.00 63.95 ? 330 GLU A OE1 1 
ATOM   2619 O  OE2 . GLU A 1 321 ? -45.365 4.079   1.062   1.00 61.01 ? 330 GLU A OE2 1 
ATOM   2620 N  N   . ALA A 1 322 ? -39.555 1.576   -0.318  1.00 41.23 ? 331 ALA A N   1 
ATOM   2621 C  CA  . ALA A 1 322 ? -38.107 1.451   -0.127  1.00 38.79 ? 331 ALA A CA  1 
ATOM   2622 C  C   . ALA A 1 322 ? -37.451 0.795   -1.332  1.00 38.78 ? 331 ALA A C   1 
ATOM   2623 O  O   . ALA A 1 322 ? -36.403 1.254   -1.812  1.00 37.37 ? 331 ALA A O   1 
ATOM   2624 C  CB  . ALA A 1 322 ? -37.804 0.660   1.129   1.00 41.00 ? 331 ALA A CB  1 
ATOM   2625 N  N   . TYR A 1 323 ? -38.067 -0.281  -1.818  1.00 37.71 ? 332 TYR A N   1 
ATOM   2626 C  CA  . TYR A 1 323 ? -37.626 -0.913  -3.053  1.00 35.59 ? 332 TYR A CA  1 
ATOM   2627 C  C   . TYR A 1 323 ? -37.642 0.090   -4.209  1.00 34.64 ? 332 TYR A C   1 
ATOM   2628 O  O   . TYR A 1 323 ? -36.652 0.240   -4.911  1.00 33.84 ? 332 TYR A O   1 
ATOM   2629 C  CB  . TYR A 1 323 ? -38.492 -2.132  -3.400  1.00 35.95 ? 332 TYR A CB  1 
ATOM   2630 C  CG  . TYR A 1 323 ? -38.167 -2.690  -4.757  1.00 35.29 ? 332 TYR A CG  1 
ATOM   2631 C  CD1 . TYR A 1 323 ? -37.123 -3.595  -4.933  1.00 37.11 ? 332 TYR A CD1 1 
ATOM   2632 C  CD2 . TYR A 1 323 ? -38.876 -2.274  -5.882  1.00 34.73 ? 332 TYR A CD2 1 
ATOM   2633 C  CE1 . TYR A 1 323 ? -36.808 -4.089  -6.207  1.00 35.96 ? 332 TYR A CE1 1 
ATOM   2634 C  CE2 . TYR A 1 323 ? -38.573 -2.753  -7.147  1.00 31.72 ? 332 TYR A CE2 1 
ATOM   2635 C  CZ  . TYR A 1 323 ? -37.542 -3.654  -7.307  1.00 33.72 ? 332 TYR A CZ  1 
ATOM   2636 O  OH  . TYR A 1 323 ? -37.256 -4.112  -8.558  1.00 32.82 ? 332 TYR A OH  1 
ATOM   2637 N  N   . ASP A 1 324 ? -38.781 0.750   -4.406  1.00 36.37 ? 333 ASP A N   1 
ATOM   2638 C  CA  . ASP A 1 324 ? -38.941 1.742   -5.478  1.00 36.67 ? 333 ASP A CA  1 
ATOM   2639 C  C   . ASP A 1 324 ? -37.955 2.906   -5.373  1.00 35.19 ? 333 ASP A C   1 
ATOM   2640 O  O   . ASP A 1 324 ? -37.522 3.430   -6.393  1.00 33.54 ? 333 ASP A O   1 
ATOM   2641 C  CB  . ASP A 1 324 ? -40.384 2.283   -5.519  1.00 38.05 ? 333 ASP A CB  1 
ATOM   2642 C  CG  . ASP A 1 324 ? -41.353 1.351   -6.255  1.00 39.98 ? 333 ASP A CG  1 
ATOM   2643 O  OD1 . ASP A 1 324 ? -40.938 0.279   -6.742  1.00 37.47 ? 333 ASP A OD1 1 
ATOM   2644 O  OD2 . ASP A 1 324 ? -42.545 1.709   -6.363  1.00 39.38 ? 333 ASP A OD2 1 
ATOM   2645 N  N   . ALA A 1 325 ? -37.603 3.294   -4.148  1.00 36.06 ? 334 ALA A N   1 
ATOM   2646 C  CA  . ALA A 1 325 ? -36.589 4.329   -3.918  1.00 36.43 ? 334 ALA A CA  1 
ATOM   2647 C  C   . ALA A 1 325 ? -35.227 3.923   -4.467  1.00 35.51 ? 334 ALA A C   1 
ATOM   2648 O  O   . ALA A 1 325 ? -34.483 4.773   -4.951  1.00 36.45 ? 334 ALA A O   1 
ATOM   2649 C  CB  . ALA A 1 325 ? -36.479 4.659   -2.437  1.00 37.07 ? 334 ALA A CB  1 
ATOM   2650 N  N   . CYS A 1 326 ? -34.904 2.628   -4.392  1.00 35.41 ? 335 CYS A N   1 
ATOM   2651 C  CA  . CYS A 1 326 ? -33.671 2.106   -4.984  1.00 33.36 ? 335 CYS A CA  1 
ATOM   2652 C  C   . CYS A 1 326 ? -33.719 2.177   -6.507  1.00 31.74 ? 335 CYS A C   1 
ATOM   2653 O  O   . CYS A 1 326 ? -32.753 2.627   -7.136  1.00 30.07 ? 335 CYS A O   1 
ATOM   2654 C  CB  . CYS A 1 326 ? -33.396 0.677   -4.529  1.00 34.15 ? 335 CYS A CB  1 
ATOM   2655 S  SG  . CYS A 1 326 ? -33.090 0.563   -2.779  1.00 34.02 ? 335 CYS A SG  1 
ATOM   2656 N  N   . VAL A 1 327 ? -34.848 1.755   -7.080  1.00 35.33 ? 336 VAL A N   1 
ATOM   2657 C  CA  . VAL A 1 327 ? -35.049 1.790   -8.525  1.00 32.47 ? 336 VAL A CA  1 
ATOM   2658 C  C   . VAL A 1 327 ? -35.057 3.229   -9.050  1.00 30.50 ? 336 VAL A C   1 
ATOM   2659 O  O   . VAL A 1 327 ? -34.410 3.510   -10.050 1.00 27.95 ? 336 VAL A O   1 
ATOM   2660 C  CB  . VAL A 1 327 ? -36.338 1.041   -8.959  1.00 32.18 ? 336 VAL A CB  1 
ATOM   2661 C  CG1 . VAL A 1 327 ? -36.650 1.260   -10.446 1.00 34.05 ? 336 VAL A CG1 1 
ATOM   2662 C  CG2 . VAL A 1 327 ? -36.204 -0.448  -8.673  1.00 35.55 ? 336 VAL A CG2 1 
ATOM   2663 N  N   . LYS A 1 328 ? -35.803 4.117   -8.393  1.00 34.31 ? 337 LYS A N   1 
ATOM   2664 C  CA  . LYS A 1 328 ? -35.837 5.537   -8.769  1.00 36.34 ? 337 LYS A CA  1 
ATOM   2665 C  C   . LYS A 1 328 ? -34.440 6.153   -8.786  1.00 34.29 ? 337 LYS A C   1 
ATOM   2666 O  O   . LYS A 1 328 ? -34.120 6.945   -9.674  1.00 33.54 ? 337 LYS A O   1 
ATOM   2667 C  CB  . LYS A 1 328 ? -36.720 6.348   -7.820  1.00 38.83 ? 337 LYS A CB  1 
ATOM   2668 C  CG  . LYS A 1 328 ? -38.203 6.175   -8.052  1.00 48.23 ? 337 LYS A CG  1 
ATOM   2669 C  CD  . LYS A 1 328 ? -39.029 6.637   -6.851  1.00 52.12 ? 337 LYS A CD  1 
ATOM   2670 C  CE  . LYS A 1 328 ? -40.512 6.399   -7.074  1.00 56.88 ? 337 LYS A CE  1 
ATOM   2671 N  NZ  . LYS A 1 328 ? -41.310 6.617   -5.841  0.00 61.44 ? 337 LYS A NZ  1 
ATOM   2672 N  N   . ALA A 1 329 ? -33.624 5.802   -7.796  1.00 36.49 ? 338 ALA A N   1 
ATOM   2673 C  CA  . ALA A 1 329 ? -32.247 6.303   -7.718  1.00 36.33 ? 338 ALA A CA  1 
ATOM   2674 C  C   . ALA A 1 329 ? -31.418 5.860   -8.932  1.00 33.71 ? 338 ALA A C   1 
ATOM   2675 O  O   . ALA A 1 329 ? -30.643 6.650   -9.481  1.00 33.36 ? 338 ALA A O   1 
ATOM   2676 C  CB  . ALA A 1 329 ? -31.587 5.880   -6.405  1.00 38.48 ? 338 ALA A CB  1 
ATOM   2677 N  N   . LEU A 1 330 ? -31.627 4.624   -9.385  1.00 33.15 ? 339 LEU A N   1 
ATOM   2678 C  CA  . LEU A 1 330 ? -30.949 4.125   -10.583 1.00 30.38 ? 339 LEU A CA  1 
ATOM   2679 C  C   . LEU A 1 330 ? -31.449 4.810   -11.866 1.00 30.64 ? 339 LEU A C   1 
ATOM   2680 O  O   . LEU A 1 330 ? -30.642 5.159   -12.741 1.00 26.90 ? 339 LEU A O   1 
ATOM   2681 C  CB  . LEU A 1 330 ? -31.049 2.594   -10.693 1.00 29.94 ? 339 LEU A CB  1 
ATOM   2682 C  CG  . LEU A 1 330 ? -30.160 1.766   -9.752  1.00 32.14 ? 339 LEU A CG  1 
ATOM   2683 C  CD1 . LEU A 1 330 ? -30.445 0.282   -9.957  1.00 35.73 ? 339 LEU A CD1 1 
ATOM   2684 C  CD2 . LEU A 1 330 ? -28.656 2.033   -9.942  1.00 35.54 ? 339 LEU A CD2 1 
ATOM   2685 N  N   . VAL A 1 331 ? -32.762 5.008   -11.969 1.00 29.80 ? 340 VAL A N   1 
ATOM   2686 C  CA  . VAL A 1 331 ? -33.352 5.765   -13.086 1.00 30.71 ? 340 VAL A CA  1 
ATOM   2687 C  C   . VAL A 1 331 ? -32.804 7.207   -13.136 1.00 30.18 ? 340 VAL A C   1 
ATOM   2688 O  O   . VAL A 1 331 ? -32.407 7.690   -14.190 1.00 28.77 ? 340 VAL A O   1 
ATOM   2689 C  CB  . VAL A 1 331 ? -34.906 5.791   -12.994 1.00 32.85 ? 340 VAL A CB  1 
ATOM   2690 C  CG1 . VAL A 1 331 ? -35.524 6.778   -13.992 1.00 34.62 ? 340 VAL A CG1 1 
ATOM   2691 C  CG2 . VAL A 1 331 ? -35.462 4.404   -13.236 1.00 34.22 ? 340 VAL A CG2 1 
ATOM   2692 N  N   . SER A 1 332 ? -32.801 7.879   -11.994 1.00 33.58 ? 341 SER A N   1 
ATOM   2693 C  CA  . SER A 1 332 ? -32.335 9.270   -11.915 1.00 34.84 ? 341 SER A CA  1 
ATOM   2694 C  C   . SER A 1 332 ? -30.870 9.409   -12.324 1.00 33.95 ? 341 SER A C   1 
ATOM   2695 O  O   . SER A 1 332 ? -30.503 10.347  -13.039 1.00 30.17 ? 341 SER A O   1 
ATOM   2696 C  CB  . SER A 1 332 ? -32.530 9.810   -10.508 1.00 34.70 ? 341 SER A CB  1 
ATOM   2697 O  OG  . SER A 1 332 ? -33.892 9.722   -10.132 1.00 43.04 ? 341 SER A OG  1 
ATOM   2698 N  N   . LEU A 1 333 ? -30.046 8.467   -11.860 1.00 36.18 ? 342 LEU A N   1 
ATOM   2699 C  CA  . LEU A 1 333 ? -28.643 8.375   -12.270 1.00 33.78 ? 342 LEU A CA  1 
ATOM   2700 C  C   . LEU A 1 333 ? -28.530 8.228   -13.778 1.00 29.65 ? 342 LEU A C   1 
ATOM   2701 O  O   . LEU A 1 333 ? -27.823 8.997   -14.435 1.00 28.07 ? 342 LEU A O   1 
ATOM   2702 C  CB  . LEU A 1 333 ? -27.945 7.201   -11.572 1.00 36.51 ? 342 LEU A CB  1 
ATOM   2703 C  CG  . LEU A 1 333 ? -26.419 7.148   -11.726 1.00 39.49 ? 342 LEU A CG  1 
ATOM   2704 C  CD1 . LEU A 1 333 ? -25.749 8.238   -10.879 1.00 39.95 ? 342 LEU A CD1 1 
ATOM   2705 C  CD2 . LEU A 1 333 ? -25.889 5.772   -11.352 1.00 41.79 ? 342 LEU A CD2 1 
ATOM   2706 N  N   . ARG A 1 334 ? -29.253 7.255   -14.323 1.00 27.49 ? 343 ARG A N   1 
ATOM   2707 C  CA  . ARG A 1 334 ? -29.278 7.017   -15.775 1.00 25.37 ? 343 ARG A CA  1 
ATOM   2708 C  C   . ARG A 1 334 ? -29.855 8.161   -16.612 1.00 25.72 ? 343 ARG A C   1 
ATOM   2709 O  O   . ARG A 1 334 ? -29.412 8.388   -17.741 1.00 25.12 ? 343 ARG A O   1 
ATOM   2710 C  CB  . ARG A 1 334 ? -29.973 5.688   -16.092 1.00 25.31 ? 343 ARG A CB  1 
ATOM   2711 C  CG  . ARG A 1 334 ? -29.110 4.532   -15.670 1.00 24.19 ? 343 ARG A CG  1 
ATOM   2712 C  CD  . ARG A 1 334 ? -29.668 3.177   -15.996 1.00 23.52 ? 343 ARG A CD  1 
ATOM   2713 N  NE  . ARG A 1 334 ? -28.618 2.191   -15.730 1.00 26.52 ? 343 ARG A NE  1 
ATOM   2714 C  CZ  . ARG A 1 334 ? -28.671 1.170   -14.878 1.00 26.94 ? 343 ARG A CZ  1 
ATOM   2715 N  NH1 . ARG A 1 334 ? -29.758 0.892   -14.165 1.00 26.83 ? 343 ARG A NH1 1 
ATOM   2716 N  NH2 . ARG A 1 334 ? -27.602 0.391   -14.766 1.00 26.54 ? 343 ARG A NH2 1 
ATOM   2717 N  N   . SER A 1 335 ? -30.816 8.887   -16.054 1.00 26.76 ? 344 SER A N   1 
ATOM   2718 C  CA  . SER A 1 335 ? -31.398 10.050  -16.722 1.00 27.93 ? 344 SER A CA  1 
ATOM   2719 C  C   . SER A 1 335 ? -30.403 11.202  -16.790 1.00 27.66 ? 344 SER A C   1 
ATOM   2720 O  O   . SER A 1 335 ? -30.239 11.823  -17.837 1.00 28.16 ? 344 SER A O   1 
ATOM   2721 C  CB  . SER A 1 335 ? -32.669 10.501  -15.999 1.00 28.60 ? 344 SER A CB  1 
ATOM   2722 O  OG  . SER A 1 335 ? -33.610 9.449   -15.996 1.00 33.36 ? 344 SER A OG  1 
ATOM   2723 N  N   . TYR A 1 336 ? -29.751 11.477  -15.666 1.00 26.54 ? 345 TYR A N   1 
ATOM   2724 C  CA  . TYR A 1 336 ? -28.686 12.463  -15.614 1.00 28.56 ? 345 TYR A CA  1 
ATOM   2725 C  C   . TYR A 1 336 ? -27.529 12.107  -16.552 1.00 27.89 ? 345 TYR A C   1 
ATOM   2726 O  O   . TYR A 1 336 ? -26.980 12.965  -17.245 1.00 26.49 ? 345 TYR A O   1 
ATOM   2727 C  CB  . TYR A 1 336 ? -28.166 12.585  -14.192 1.00 30.64 ? 345 TYR A CB  1 
ATOM   2728 C  CG  . TYR A 1 336 ? -27.245 13.749  -14.021 1.00 33.34 ? 345 TYR A CG  1 
ATOM   2729 C  CD1 . TYR A 1 336 ? -27.749 15.037  -13.846 1.00 34.08 ? 345 TYR A CD1 1 
ATOM   2730 C  CD2 . TYR A 1 336 ? -25.861 13.574  -14.047 1.00 36.47 ? 345 TYR A CD2 1 
ATOM   2731 C  CE1 . TYR A 1 336 ? -26.900 16.114  -13.694 1.00 36.88 ? 345 TYR A CE1 1 
ATOM   2732 C  CE2 . TYR A 1 336 ? -25.001 14.653  -13.891 1.00 35.03 ? 345 TYR A CE2 1 
ATOM   2733 C  CZ  . TYR A 1 336 ? -25.522 15.910  -13.723 1.00 34.27 ? 345 TYR A CZ  1 
ATOM   2734 O  OH  . TYR A 1 336 ? -24.669 16.965  -13.573 1.00 42.25 ? 345 TYR A OH  1 
ATOM   2735 N  N   . HIS A 1 337 ? -27.173 10.830  -16.560 1.00 27.63 ? 346 HIS A N   1 
ATOM   2736 C  CA  . HIS A 1 337 ? -26.149 10.294  -17.446 1.00 26.10 ? 346 HIS A CA  1 
ATOM   2737 C  C   . HIS A 1 337 ? -26.474 10.510  -18.930 1.00 26.57 ? 346 HIS A C   1 
ATOM   2738 O  O   . HIS A 1 337 ? -25.593 10.888  -19.699 1.00 25.65 ? 346 HIS A O   1 
ATOM   2739 C  CB  . HIS A 1 337 ? -25.946 8.813   -17.118 1.00 27.95 ? 346 HIS A CB  1 
ATOM   2740 C  CG  . HIS A 1 337 ? -24.937 8.131   -17.970 1.00 23.50 ? 346 HIS A CG  1 
ATOM   2741 N  ND1 . HIS A 1 337 ? -25.279 7.466   -19.120 1.00 25.17 ? 346 HIS A ND1 1 
ATOM   2742 C  CD2 . HIS A 1 337 ? -23.596 8.012   -17.846 1.00 27.84 ? 346 HIS A CD2 1 
ATOM   2743 C  CE1 . HIS A 1 337 ? -24.193 6.955   -19.668 1.00 24.84 ? 346 HIS A CE1 1 
ATOM   2744 N  NE2 . HIS A 1 337 ? -23.156 7.265   -18.910 1.00 20.57 ? 346 HIS A NE2 1 
ATOM   2745 N  N   . LEU A 1 338 ? -27.727 10.302  -19.330 1.00 25.73 ? 347 LEU A N   1 
ATOM   2746 C  CA  . LEU A 1 338 ? -28.164 10.639  -20.691 1.00 27.10 ? 347 LEU A CA  1 
ATOM   2747 C  C   . LEU A 1 338 ? -27.917 12.108  -21.043 1.00 28.69 ? 347 LEU A C   1 
ATOM   2748 O  O   . LEU A 1 338 ? -27.456 12.416  -22.139 1.00 25.91 ? 347 LEU A O   1 
ATOM   2749 C  CB  . LEU A 1 338 ? -29.651 10.299  -20.914 1.00 28.56 ? 347 LEU A CB  1 
ATOM   2750 C  CG  . LEU A 1 338 ? -29.877 8.818   -21.265 1.00 32.19 ? 347 LEU A CG  1 
ATOM   2751 C  CD1 . LEU A 1 338 ? -31.304 8.384   -20.968 1.00 36.45 ? 347 LEU A CD1 1 
ATOM   2752 C  CD2 . LEU A 1 338 ? -29.536 8.538   -22.712 1.00 28.40 ? 347 LEU A CD2 1 
ATOM   2753 N  N   . GLN A 1 339 ? -28.216 13.001  -20.100 1.00 29.43 ? 348 GLN A N   1 
ATOM   2754 C  CA  . GLN A 1 339 ? -28.016 14.439  -20.314 1.00 30.89 ? 348 GLN A CA  1 
ATOM   2755 C  C   . GLN A 1 339 ? -26.520 14.774  -20.460 1.00 30.23 ? 348 GLN A C   1 
ATOM   2756 O  O   . GLN A 1 339 ? -26.160 15.662  -21.227 1.00 30.94 ? 348 GLN A O   1 
ATOM   2757 C  CB  . GLN A 1 339 ? -28.666 15.243  -19.189 1.00 31.51 ? 348 GLN A CB  1 
ATOM   2758 C  CG  . GLN A 1 339 ? -30.174 15.027  -19.100 1.00 34.85 ? 348 GLN A CG  1 
ATOM   2759 C  CD  . GLN A 1 339 ? -30.784 15.718  -17.914 1.00 38.03 ? 348 GLN A CD  1 
ATOM   2760 O  OE1 . GLN A 1 339 ? -30.560 16.906  -17.698 1.00 48.44 ? 348 GLN A OE1 1 
ATOM   2761 N  NE2 . GLN A 1 339 ? -31.567 14.984  -17.138 1.00 41.23 ? 348 GLN A NE2 1 
ATOM   2762 N  N   . ILE A 1 340 ? -25.675 14.042  -19.731 1.00 29.01 ? 349 ILE A N   1 
ATOM   2763 C  CA  . ILE A 1 340 ? -24.215 14.080  -19.895 1.00 30.05 ? 349 ILE A CA  1 
ATOM   2764 C  C   . ILE A 1 340 ? -23.798 13.699  -21.317 1.00 28.72 ? 349 ILE A C   1 
ATOM   2765 O  O   . ILE A 1 340 ? -23.017 14.419  -21.943 1.00 26.20 ? 349 ILE A O   1 
ATOM   2766 C  CB  . ILE A 1 340 ? -23.485 13.185  -18.829 1.00 30.37 ? 349 ILE A CB  1 
ATOM   2767 C  CG1 . ILE A 1 340 ? -23.693 13.747  -17.417 1.00 33.64 ? 349 ILE A CG1 1 
ATOM   2768 C  CG2 . ILE A 1 340 ? -21.965 13.016  -19.117 1.00 32.55 ? 349 ILE A CG2 1 
ATOM   2769 C  CD1 . ILE A 1 340 ? -23.109 15.129  -17.155 1.00 39.09 ? 349 ILE A CD1 1 
ATOM   2770 N  N   . VAL A 1 341 ? -24.355 12.607  -21.839 1.00 28.24 ? 350 VAL A N   1 
ATOM   2771 C  CA  . VAL A 1 341 ? -24.031 12.141  -23.193 1.00 26.02 ? 350 VAL A CA  1 
ATOM   2772 C  C   . VAL A 1 341 ? -24.441 13.172  -24.258 1.00 25.88 ? 350 VAL A C   1 
ATOM   2773 O  O   . VAL A 1 341 ? -23.734 13.358  -25.254 1.00 25.38 ? 350 VAL A O   1 
ATOM   2774 C  CB  . VAL A 1 341 ? -24.638 10.735  -23.491 1.00 25.87 ? 350 VAL A CB  1 
ATOM   2775 C  CG1 . VAL A 1 341 ? -24.279 10.265  -24.915 1.00 27.08 ? 350 VAL A CG1 1 
ATOM   2776 C  CG2 . VAL A 1 341 ? -24.118 9.725   -22.491 1.00 25.54 ? 350 VAL A CG2 1 
ATOM   2777 N  N   . THR A 1 342 ? -25.569 13.838  -24.049 1.00 25.27 ? 351 THR A N   1 
ATOM   2778 C  CA  . THR A 1 342 ? -25.986 14.928  -24.932 1.00 27.06 ? 351 THR A CA  1 
ATOM   2779 C  C   . THR A 1 342 ? -24.946 16.069  -24.953 1.00 29.02 ? 351 THR A C   1 
ATOM   2780 O  O   . THR A 1 342 ? -24.581 16.559  -26.020 1.00 29.47 ? 351 THR A O   1 
ATOM   2781 C  CB  . THR A 1 342 ? -27.376 15.461  -24.538 1.00 28.25 ? 351 THR A CB  1 
ATOM   2782 O  OG1 . THR A 1 342 ? -28.311 14.377  -24.554 1.00 28.58 ? 351 THR A OG1 1 
ATOM   2783 C  CG2 . THR A 1 342 ? -27.861 16.550  -25.506 1.00 29.68 ? 351 THR A CG2 1 
ATOM   2784 N  N   . LYS A 1 343 ? -24.489 16.471  -23.773 1.00 27.41 ? 352 LYS A N   1 
ATOM   2785 C  CA  . LYS A 1 343 ? -23.513 17.547  -23.628 1.00 28.73 ? 352 LYS A CA  1 
ATOM   2786 C  C   . LYS A 1 343 ? -22.112 17.147  -24.113 1.00 28.67 ? 352 LYS A C   1 
ATOM   2787 O  O   . LYS A 1 343 ? -21.457 17.925  -24.804 1.00 30.50 ? 352 LYS A O   1 
ATOM   2788 C  CB  . LYS A 1 343 ? -23.442 18.009  -22.166 1.00 28.14 ? 352 LYS A CB  1 
ATOM   2789 C  CG  . LYS A 1 343 ? -22.310 18.998  -21.869 1.00 33.90 ? 352 LYS A CG  1 
ATOM   2790 C  CD  . LYS A 1 343 ? -22.381 19.551  -20.473 1.00 33.84 ? 352 LYS A CD  1 
ATOM   2791 C  CE  . LYS A 1 343 ? -21.222 20.497  -20.242 1.00 32.24 ? 352 LYS A CE  1 
ATOM   2792 N  NZ  . LYS A 1 343 ? -21.296 21.158  -18.919 1.00 40.97 ? 352 LYS A NZ  1 
ATOM   2793 N  N   . TYR A 1 344 ? -21.667 15.946  -23.743 1.00 26.77 ? 353 TYR A N   1 
ATOM   2794 C  CA  . TYR A 1 344 ? -20.276 15.515  -23.961 1.00 26.68 ? 353 TYR A CA  1 
ATOM   2795 C  C   . TYR A 1 344 ? -20.007 14.737  -25.253 1.00 26.21 ? 353 TYR A C   1 
ATOM   2796 O  O   . TYR A 1 344 ? -18.844 14.615  -25.666 1.00 26.07 ? 353 TYR A O   1 
ATOM   2797 C  CB  . TYR A 1 344 ? -19.784 14.739  -22.736 1.00 26.84 ? 353 TYR A CB  1 
ATOM   2798 C  CG  . TYR A 1 344 ? -19.456 15.661  -21.591 1.00 27.83 ? 353 TYR A CG  1 
ATOM   2799 C  CD1 . TYR A 1 344 ? -20.432 16.058  -20.680 1.00 28.91 ? 353 TYR A CD1 1 
ATOM   2800 C  CD2 . TYR A 1 344 ? -18.174 16.178  -21.445 1.00 30.56 ? 353 TYR A CD2 1 
ATOM   2801 C  CE1 . TYR A 1 344 ? -20.129 16.923  -19.635 1.00 32.53 ? 353 TYR A CE1 1 
ATOM   2802 C  CE2 . TYR A 1 344 ? -17.865 17.044  -20.415 1.00 32.12 ? 353 TYR A CE2 1 
ATOM   2803 C  CZ  . TYR A 1 344 ? -18.843 17.418  -19.515 1.00 31.91 ? 353 TYR A CZ  1 
ATOM   2804 O  OH  . TYR A 1 344 ? -18.531 18.263  -18.486 1.00 34.37 ? 353 TYR A OH  1 
ATOM   2805 N  N   . ILE A 1 345 ? -21.057 14.223  -25.893 1.00 27.31 ? 354 ILE A N   1 
ATOM   2806 C  CA  . ILE A 1 345 ? -20.916 13.496  -27.162 1.00 28.06 ? 354 ILE A CA  1 
ATOM   2807 C  C   . ILE A 1 345 ? -21.767 14.097  -28.272 1.00 27.97 ? 354 ILE A C   1 
ATOM   2808 O  O   . ILE A 1 345 ? -21.219 14.473  -29.310 1.00 31.56 ? 354 ILE A O   1 
ATOM   2809 C  CB  . ILE A 1 345 ? -21.187 11.975  -26.994 1.00 27.82 ? 354 ILE A CB  1 
ATOM   2810 C  CG1 . ILE A 1 345 ? -20.070 11.371  -26.131 1.00 30.20 ? 354 ILE A CG1 1 
ATOM   2811 C  CG2 . ILE A 1 345 ? -21.279 11.266  -28.382 1.00 30.03 ? 354 ILE A CG2 1 
ATOM   2812 C  CD1 . ILE A 1 345 ? -20.192 9.894   -25.824 1.00 34.60 ? 354 ILE A CD1 1 
ATOM   2813 N  N   . LEU A 1 346 ? -23.084 14.178  -28.074 1.00 27.15 ? 355 LEU A N   1 
ATOM   2814 C  CA  . LEU A 1 346 ? -23.987 14.585  -29.165 1.00 28.99 ? 355 LEU A CA  1 
ATOM   2815 C  C   . LEU A 1 346 ? -23.700 15.992  -29.675 1.00 30.82 ? 355 LEU A C   1 
ATOM   2816 O  O   . LEU A 1 346 ? -23.593 16.202  -30.895 1.00 29.88 ? 355 LEU A O   1 
ATOM   2817 C  CB  . LEU A 1 346 ? -25.460 14.494  -28.765 1.00 29.33 ? 355 LEU A CB  1 
ATOM   2818 C  CG  . LEU A 1 346 ? -26.034 13.142  -28.328 1.00 30.80 ? 355 LEU A CG  1 
ATOM   2819 C  CD1 . LEU A 1 346 ? -27.530 13.284  -28.153 1.00 30.83 ? 355 LEU A CD1 1 
ATOM   2820 C  CD2 . LEU A 1 346 ? -25.724 12.007  -29.302 1.00 34.57 ? 355 LEU A CD2 1 
ATOM   2821 N  N   . ILE A 1 347 ? -23.558 16.940  -28.746 1.00 28.23 ? 356 ILE A N   1 
ATOM   2822 C  CA  . ILE A 1 347 ? -23.386 18.346  -29.111 1.00 31.46 ? 356 ILE A CA  1 
ATOM   2823 C  C   . ILE A 1 347 ? -22.019 18.574  -29.793 1.00 31.03 ? 356 ILE A C   1 
ATOM   2824 O  O   . ILE A 1 347 ? -21.982 19.131  -30.893 1.00 33.62 ? 356 ILE A O   1 
ATOM   2825 C  CB  . ILE A 1 347 ? -23.721 19.314  -27.913 1.00 30.98 ? 356 ILE A CB  1 
ATOM   2826 C  CG1 . ILE A 1 347 ? -25.248 19.371  -27.727 1.00 33.84 ? 356 ILE A CG1 1 
ATOM   2827 C  CG2 . ILE A 1 347 ? -23.195 20.738  -28.161 1.00 32.59 ? 356 ILE A CG2 1 
ATOM   2828 C  CD1 . ILE A 1 347 ? -25.735 20.018  -26.433 1.00 35.32 ? 356 ILE A CD1 1 
ATOM   2829 N  N   . PRO A 1 348 ? -20.906 18.130  -29.166 1.00 32.08 ? 357 PRO A N   1 
ATOM   2830 C  CA  . PRO A 1 348 ? -19.600 18.174  -29.838 1.00 32.18 ? 357 PRO A CA  1 
ATOM   2831 C  C   . PRO A 1 348 ? -19.576 17.479  -31.194 1.00 30.77 ? 357 PRO A C   1 
ATOM   2832 O  O   . PRO A 1 348 ? -19.004 18.027  -32.126 1.00 31.10 ? 357 PRO A O   1 
ATOM   2833 C  CB  . PRO A 1 348 ? -18.676 17.469  -28.847 1.00 31.77 ? 357 PRO A CB  1 
ATOM   2834 C  CG  . PRO A 1 348 ? -19.300 17.706  -27.537 1.00 32.71 ? 357 PRO A CG  1 
ATOM   2835 C  CD  . PRO A 1 348 ? -20.770 17.633  -27.786 1.00 29.78 ? 357 PRO A CD  1 
ATOM   2836 N  N   . ALA A 1 349 ? -20.221 16.314  -31.315 1.00 30.81 ? 358 ALA A N   1 
ATOM   2837 C  CA  . ALA A 1 349 ? -20.292 15.608  -32.612 1.00 34.70 ? 358 ALA A CA  1 
ATOM   2838 C  C   . ALA A 1 349 ? -20.979 16.443  -33.686 1.00 38.43 ? 358 ALA A C   1 
ATOM   2839 O  O   . ALA A 1 349 ? -20.562 16.416  -34.847 1.00 41.55 ? 358 ALA A O   1 
ATOM   2840 C  CB  . ALA A 1 349 ? -20.980 14.268  -32.479 1.00 33.28 ? 358 ALA A CB  1 
ATOM   2841 N  N   . SER A 1 350 ? -22.017 17.186  -33.297 1.00 37.33 ? 359 SER A N   1 
ATOM   2842 C  CA  . SER A 1 350 ? -22.714 18.088  -34.226 1.00 40.54 ? 359 SER A CA  1 
ATOM   2843 C  C   . SER A 1 350 ? -21.870 19.297  -34.644 1.00 43.39 ? 359 SER A C   1 
ATOM   2844 O  O   . SER A 1 350 ? -22.069 19.822  -35.732 1.00 46.30 ? 359 SER A O   1 
ATOM   2845 C  CB  . SER A 1 350 ? -24.022 18.586  -33.609 1.00 37.30 ? 359 SER A CB  1 
ATOM   2846 O  OG  . SER A 1 350 ? -23.771 19.521  -32.579 1.00 33.04 ? 359 SER A OG  1 
ATOM   2847 N  N   . GLN A 1 351 ? -20.966 19.736  -33.765 1.00 46.45 ? 360 GLN A N   1 
ATOM   2848 C  CA  . GLN A 1 351 ? -20.129 20.928  -33.982 1.00 51.77 ? 360 GLN A CA  1 
ATOM   2849 C  C   . GLN A 1 351 ? -18.823 20.654  -34.741 1.00 55.52 ? 360 GLN A C   1 
ATOM   2850 O  O   . GLN A 1 351 ? -18.120 21.603  -35.069 1.00 60.42 ? 360 GLN A O   1 
ATOM   2851 C  CB  . GLN A 1 351 ? -19.765 21.592  -32.640 1.00 50.25 ? 360 GLN A CB  1 
ATOM   2852 C  CG  . GLN A 1 351 ? -20.922 22.240  -31.861 1.00 52.33 ? 360 GLN A CG  1 
ATOM   2853 C  CD  . GLN A 1 351 ? -20.525 22.633  -30.418 1.00 53.55 ? 360 GLN A CD  1 
ATOM   2854 O  OE1 . GLN A 1 351 ? -20.749 23.765  -29.987 1.00 61.72 ? 360 GLN A OE1 1 
ATOM   2855 N  NE2 . GLN A 1 351 ? -19.932 21.697  -29.683 1.00 53.44 ? 360 GLN A NE2 1 
ATOM   2856 N  N   . GLN A 1 352 ? -18.480 19.391  -35.005 1.00 58.14 ? 361 GLN A N   1 
ATOM   2857 C  CA  . GLN A 1 352 ? -17.212 19.068  -35.683 1.00 62.93 ? 361 GLN A CA  1 
ATOM   2858 C  C   . GLN A 1 352 ? -17.321 19.297  -37.207 1.00 68.84 ? 361 GLN A C   1 
ATOM   2859 O  O   . GLN A 1 352 ? -18.391 19.078  -37.787 1.00 71.05 ? 361 GLN A O   1 
ATOM   2860 C  CB  . GLN A 1 352 ? -16.749 17.637  -35.347 1.00 62.65 ? 361 GLN A CB  1 
ATOM   2861 C  CG  . GLN A 1 352 ? -17.429 16.509  -36.123 1.00 63.27 ? 361 GLN A CG  1 
ATOM   2862 C  CD  . GLN A 1 352 ? -17.112 15.138  -35.551 1.00 62.66 ? 361 GLN A CD  1 
ATOM   2863 O  OE1 . GLN A 1 352 ? -15.960 14.841  -35.228 1.00 64.82 ? 361 GLN A OE1 1 
ATOM   2864 N  NE2 . GLN A 1 352 ? -18.131 14.291  -35.433 1.00 57.41 ? 361 GLN A NE2 1 
ATOM   2865 N  N   . PRO A 1 353 ? -16.221 19.743  -37.857 1.00 73.94 ? 362 PRO A N   1 
ATOM   2866 C  CA  . PRO A 1 353 ? -16.270 20.048  -39.295 1.00 77.70 ? 362 PRO A CA  1 
ATOM   2867 C  C   . PRO A 1 353 ? -16.273 18.800  -40.184 1.00 80.51 ? 362 PRO A C   1 
ATOM   2868 O  O   . PRO A 1 353 ? -15.864 17.722  -39.747 1.00 80.42 ? 362 PRO A O   1 
ATOM   2869 C  CB  . PRO A 1 353 ? -14.994 20.866  -39.517 1.00 81.23 ? 362 PRO A CB  1 
ATOM   2870 C  CG  . PRO A 1 353 ? -14.046 20.343  -38.513 1.00 79.70 ? 362 PRO A CG  1 
ATOM   2871 C  CD  . PRO A 1 353 ? -14.873 19.982  -37.303 1.00 75.03 ? 362 PRO A CD  1 
ATOM   2872 N  N   . GLY A 1 371 ? -23.302 5.419   -34.180 1.00 57.55 ? 380 GLY A N   1 
ATOM   2873 C  CA  . GLY A 1 371 ? -23.140 6.829   -33.836 1.00 53.20 ? 380 GLY A CA  1 
ATOM   2874 C  C   . GLY A 1 371 ? -23.936 7.260   -32.615 1.00 49.39 ? 380 GLY A C   1 
ATOM   2875 O  O   . GLY A 1 371 ? -24.284 6.436   -31.770 1.00 45.24 ? 380 GLY A O   1 
ATOM   2876 N  N   . GLY A 1 372 ? -24.239 8.556   -32.543 1.00 47.77 ? 381 GLY A N   1 
ATOM   2877 C  CA  . GLY A 1 372 ? -24.872 9.160   -31.370 1.00 43.37 ? 381 GLY A CA  1 
ATOM   2878 C  C   . GLY A 1 372 ? -26.228 8.568   -31.032 1.00 42.09 ? 381 GLY A C   1 
ATOM   2879 O  O   . GLY A 1 372 ? -26.493 8.253   -29.876 1.00 38.98 ? 381 GLY A O   1 
ATOM   2880 N  N   . THR A 1 373 ? -27.075 8.400   -32.045 1.00 42.19 ? 382 THR A N   1 
ATOM   2881 C  CA  . THR A 1 373 ? -28.407 7.812   -31.861 1.00 41.76 ? 382 THR A CA  1 
ATOM   2882 C  C   . THR A 1 373 ? -28.349 6.379   -31.310 1.00 39.05 ? 382 THR A C   1 
ATOM   2883 O  O   . THR A 1 373 ? -29.142 6.029   -30.446 1.00 37.42 ? 382 THR A O   1 
ATOM   2884 C  CB  . THR A 1 373 ? -29.221 7.854   -33.172 1.00 45.55 ? 382 THR A CB  1 
ATOM   2885 O  OG1 . THR A 1 373 ? -29.399 9.222   -33.564 1.00 46.74 ? 382 THR A OG1 1 
ATOM   2886 C  CG2 . THR A 1 373 ? -30.605 7.196   -33.015 1.00 47.17 ? 382 THR A CG2 1 
ATOM   2887 N  N   . ASP A 1 374 ? -27.424 5.568   -31.816 1.00 39.26 ? 383 ASP A N   1 
ATOM   2888 C  CA  . ASP A 1 374 ? -27.279 4.185   -31.362 1.00 40.46 ? 383 ASP A CA  1 
ATOM   2889 C  C   . ASP A 1 374 ? -26.783 4.120   -29.933 1.00 37.24 ? 383 ASP A C   1 
ATOM   2890 O  O   . ASP A 1 374 ? -27.235 3.261   -29.174 1.00 35.91 ? 383 ASP A O   1 
ATOM   2891 C  CB  . ASP A 1 374 ? -26.367 3.365   -32.292 1.00 44.73 ? 383 ASP A CB  1 
ATOM   2892 C  CG  . ASP A 1 374 ? -27.048 2.993   -33.606 1.00 53.23 ? 383 ASP A CG  1 
ATOM   2893 O  OD1 . ASP A 1 374 ? -28.281 3.174   -33.731 1.00 55.46 ? 383 ASP A OD1 1 
ATOM   2894 O  OD2 . ASP A 1 374 ? -26.345 2.516   -34.524 1.00 59.99 ? 383 ASP A OD2 1 
ATOM   2895 N  N   . LEU A 1 375 ? -25.890 5.041   -29.560 1.00 34.32 ? 384 LEU A N   1 
ATOM   2896 C  CA  . LEU A 1 375 ? -25.434 5.148   -28.175 1.00 33.13 ? 384 LEU A CA  1 
ATOM   2897 C  C   . LEU A 1 375 ? -26.567 5.552   -27.238 1.00 30.15 ? 384 LEU A C   1 
ATOM   2898 O  O   . LEU A 1 375 ? -26.754 4.916   -26.203 1.00 28.37 ? 384 LEU A O   1 
ATOM   2899 C  CB  . LEU A 1 375 ? -24.255 6.126   -28.049 1.00 35.66 ? 384 LEU A CB  1 
ATOM   2900 C  CG  . LEU A 1 375 ? -22.951 5.676   -28.731 1.00 37.93 ? 384 LEU A CG  1 
ATOM   2901 C  CD1 . LEU A 1 375 ? -21.928 6.788   -28.656 1.00 41.74 ? 384 LEU A CD1 1 
ATOM   2902 C  CD2 . LEU A 1 375 ? -22.384 4.378   -28.141 1.00 35.46 ? 384 LEU A CD2 1 
ATOM   2903 N  N   . MET A 1 376 ? -27.321 6.586   -27.614 1.00 29.38 ? 385 MET A N   1 
ATOM   2904 C  CA  . MET A 1 376 ? -28.462 7.061   -26.818 1.00 28.31 ? 385 MET A CA  1 
ATOM   2905 C  C   . MET A 1 376 ? -29.554 5.997   -26.672 1.00 28.29 ? 385 MET A C   1 
ATOM   2906 O  O   . MET A 1 376 ? -30.113 5.834   -25.587 1.00 27.10 ? 385 MET A O   1 
ATOM   2907 C  CB  . MET A 1 376 ? -29.091 8.314   -27.437 1.00 29.61 ? 385 MET A CB  1 
ATOM   2908 C  CG  . MET A 1 376 ? -28.198 9.545   -27.493 1.00 34.12 ? 385 MET A CG  1 
ATOM   2909 S  SD  . MET A 1 376 ? -27.523 10.026  -25.911 1.00 32.77 ? 385 MET A SD  1 
ATOM   2910 C  CE  . MET A 1 376 ? -28.871 10.929  -25.181 1.00 28.21 ? 385 MET A CE  1 
ATOM   2911 N  N   . ASN A 1 377 ? -29.849 5.292   -27.763 1.00 29.15 ? 386 ASN A N   1 
ATOM   2912 C  CA  . ASN A 1 377 ? -30.853 4.231   -27.753 1.00 32.01 ? 386 ASN A CA  1 
ATOM   2913 C  C   . ASN A 1 377 ? -30.479 3.072   -26.842 1.00 33.05 ? 386 ASN A C   1 
ATOM   2914 O  O   . ASN A 1 377 ? -31.355 2.504   -26.176 1.00 33.79 ? 386 ASN A O   1 
ATOM   2915 C  CB  . ASN A 1 377 ? -31.115 3.703   -29.167 1.00 33.51 ? 386 ASN A CB  1 
ATOM   2916 C  CG  . ASN A 1 377 ? -32.003 4.628   -30.001 1.00 38.36 ? 386 ASN A CG  1 
ATOM   2917 O  OD1 . ASN A 1 377 ? -32.184 4.397   -31.198 1.00 39.50 ? 386 ASN A OD1 1 
ATOM   2918 N  ND2 . ASN A 1 377 ? -32.574 5.654   -29.375 1.00 28.59 ? 386 ASN A ND2 1 
ATOM   2919 N  N   . PHE A 1 378 ? -29.193 2.711   -26.827 1.00 32.37 ? 387 PHE A N   1 
ATOM   2920 C  CA  . PHE A 1 378 ? -28.707 1.696   -25.889 1.00 31.18 ? 387 PHE A CA  1 
ATOM   2921 C  C   . PHE A 1 378 ? -28.955 2.146   -24.444 1.00 29.30 ? 387 PHE A C   1 
ATOM   2922 O  O   . PHE A 1 378 ? -29.524 1.410   -23.650 1.00 27.43 ? 387 PHE A O   1 
ATOM   2923 C  CB  . PHE A 1 378 ? -27.223 1.372   -26.115 1.00 31.50 ? 387 PHE A CB  1 
ATOM   2924 C  CG  . PHE A 1 378 ? -26.576 0.685   -24.945 1.00 32.25 ? 387 PHE A CG  1 
ATOM   2925 C  CD1 . PHE A 1 378 ? -26.906 -0.635  -24.625 1.00 27.85 ? 387 PHE A CD1 1 
ATOM   2926 C  CD2 . PHE A 1 378 ? -25.670 1.361   -24.136 1.00 25.01 ? 387 PHE A CD2 1 
ATOM   2927 C  CE1 . PHE A 1 378 ? -26.329 -1.264  -23.536 1.00 31.42 ? 387 PHE A CE1 1 
ATOM   2928 C  CE2 . PHE A 1 378 ? -25.078 0.727   -23.050 1.00 26.41 ? 387 PHE A CE2 1 
ATOM   2929 C  CZ  . PHE A 1 378 ? -25.410 -0.578  -22.745 1.00 29.10 ? 387 PHE A CZ  1 
ATOM   2930 N  N   . LEU A 1 379 ? -28.541 3.367   -24.122 1.00 26.59 ? 388 LEU A N   1 
ATOM   2931 C  CA  . LEU A 1 379 ? -28.715 3.909   -22.788 1.00 25.46 ? 388 LEU A CA  1 
ATOM   2932 C  C   . LEU A 1 379 ? -30.178 4.067   -22.371 1.00 24.89 ? 388 LEU A C   1 
ATOM   2933 O  O   . LEU A 1 379 ? -30.510 3.891   -21.193 1.00 24.26 ? 388 LEU A O   1 
ATOM   2934 C  CB  . LEU A 1 379 ? -28.001 5.261   -22.669 1.00 25.66 ? 388 LEU A CB  1 
ATOM   2935 C  CG  . LEU A 1 379 ? -26.477 5.226   -22.768 1.00 27.96 ? 388 LEU A CG  1 
ATOM   2936 C  CD1 . LEU A 1 379 ? -25.937 6.645   -22.718 1.00 27.52 ? 388 LEU A CD1 1 
ATOM   2937 C  CD2 . LEU A 1 379 ? -25.850 4.394   -21.664 1.00 27.83 ? 388 LEU A CD2 1 
ATOM   2938 N  N   . LYS A 1 380 ? -31.028 4.426   -23.328 1.00 24.62 ? 389 LYS A N   1 
ATOM   2939 C  CA  . LYS A 1 380 ? -32.468 4.560   -23.102 1.00 26.14 ? 389 LYS A CA  1 
ATOM   2940 C  C   . LYS A 1 380 ? -33.130 3.186   -22.860 1.00 25.65 ? 389 LYS A C   1 
ATOM   2941 O  O   . LYS A 1 380 ? -34.004 3.067   -22.005 1.00 25.39 ? 389 LYS A O   1 
ATOM   2942 C  CB  . LYS A 1 380 ? -33.127 5.319   -24.266 1.00 28.39 ? 389 LYS A CB  1 
ATOM   2943 C  CG  . LYS A 1 380 ? -32.820 6.826   -24.253 1.00 26.66 ? 389 LYS A CG  1 
ATOM   2944 C  CD  . LYS A 1 380 ? -33.287 7.515   -25.536 1.00 31.25 ? 389 LYS A CD  1 
ATOM   2945 C  CE  . LYS A 1 380 ? -32.807 8.960   -25.638 1.00 26.27 ? 389 LYS A CE  1 
ATOM   2946 N  NZ  . LYS A 1 380 ? -33.428 9.699   -26.801 1.00 31.44 ? 389 LYS A NZ  1 
ATOM   2947 N  N   . THR A 1 381 ? -32.683 2.161   -23.584 1.00 25.02 ? 390 THR A N   1 
ATOM   2948 C  CA  . THR A 1 381 ? -33.111 0.770   -23.330 1.00 27.18 ? 390 THR A CA  1 
ATOM   2949 C  C   . THR A 1 381 ? -32.814 0.355   -21.887 1.00 26.75 ? 390 THR A C   1 
ATOM   2950 O  O   . THR A 1 381 ? -33.698 -0.145  -21.188 1.00 26.61 ? 390 THR A O   1 
ATOM   2951 C  CB  . THR A 1 381 ? -32.460 -0.208  -24.321 1.00 27.89 ? 390 THR A CB  1 
ATOM   2952 O  OG1 . THR A 1 381 ? -32.867 0.149   -25.638 1.00 25.67 ? 390 THR A OG1 1 
ATOM   2953 C  CG2 . THR A 1 381 ? -32.877 -1.696  -24.060 1.00 31.15 ? 390 THR A CG2 1 
ATOM   2954 N  N   . VAL A 1 382 ? -31.590 0.620   -21.438 1.00 24.55 ? 391 VAL A N   1 
ATOM   2955 C  CA  . VAL A 1 382 ? -31.164 0.287   -20.077 1.00 24.97 ? 391 VAL A CA  1 
ATOM   2956 C  C   . VAL A 1 382 ? -31.933 1.100   -19.005 1.00 26.70 ? 391 VAL A C   1 
ATOM   2957 O  O   . VAL A 1 382 ? -32.304 0.571   -17.930 1.00 26.33 ? 391 VAL A O   1 
ATOM   2958 C  CB  . VAL A 1 382 ? -29.621 0.447   -19.932 1.00 22.93 ? 391 VAL A CB  1 
ATOM   2959 C  CG1 . VAL A 1 382 ? -29.165 0.179   -18.529 1.00 25.20 ? 391 VAL A CG1 1 
ATOM   2960 C  CG2 . VAL A 1 382 ? -28.882 -0.517  -20.895 1.00 24.71 ? 391 VAL A CG2 1 
ATOM   2961 N  N   . ARG A 1 383 ? -32.151 2.382   -19.279 1.00 26.66 ? 392 ARG A N   1 
ATOM   2962 C  CA  . ARG A 1 383 ? -32.974 3.211   -18.396 1.00 26.77 ? 392 ARG A CA  1 
ATOM   2963 C  C   . ARG A 1 383 ? -34.405 2.710   -18.321 1.00 27.22 ? 392 ARG A C   1 
ATOM   2964 O  O   . ARG A 1 383 ? -34.982 2.624   -17.234 1.00 30.20 ? 392 ARG A O   1 
ATOM   2965 C  CB  . ARG A 1 383 ? -33.000 4.673   -18.839 1.00 26.74 ? 392 ARG A CB  1 
ATOM   2966 C  CG  . ARG A 1 383 ? -33.752 5.553   -17.834 1.00 29.46 ? 392 ARG A CG  1 
ATOM   2967 C  CD  . ARG A 1 383 ? -33.670 6.990   -18.163 1.00 31.86 ? 392 ARG A CD  1 
ATOM   2968 N  NE  . ARG A 1 383 ? -34.315 7.288   -19.433 1.00 37.77 ? 392 ARG A NE  1 
ATOM   2969 C  CZ  . ARG A 1 383 ? -34.508 8.513   -19.919 1.00 38.23 ? 392 ARG A CZ  1 
ATOM   2970 N  NH1 . ARG A 1 383 ? -34.134 9.589   -19.241 1.00 40.31 ? 392 ARG A NH1 1 
ATOM   2971 N  NH2 . ARG A 1 383 ? -35.093 8.661   -21.097 1.00 44.12 ? 392 ARG A NH2 1 
ATOM   2972 N  N   . SER A 1 384 ? -34.979 2.409   -19.478 1.00 29.85 ? 393 SER A N   1 
ATOM   2973 C  CA  . SER A 1 384 ? -36.370 1.954   -19.553 1.00 31.82 ? 393 SER A CA  1 
ATOM   2974 C  C   . SER A 1 384 ? -36.576 0.641   -18.807 1.00 32.13 ? 393 SER A C   1 
ATOM   2975 O  O   . SER A 1 384 ? -37.584 0.473   -18.115 1.00 32.41 ? 393 SER A O   1 
ATOM   2976 C  CB  . SER A 1 384 ? -36.820 1.833   -21.011 1.00 34.36 ? 393 SER A CB  1 
ATOM   2977 O  OG  . SER A 1 384 ? -38.119 1.277   -21.098 1.00 42.36 ? 393 SER A OG  1 
ATOM   2978 N  N   . THR A 1 385 ? -35.618 -0.277  -18.936 1.00 30.70 ? 394 THR A N   1 
ATOM   2979 C  CA  . THR A 1 385 ? -35.649 -1.546  -18.198 1.00 32.28 ? 394 THR A CA  1 
ATOM   2980 C  C   . THR A 1 385 ? -35.629 -1.294  -16.688 1.00 30.90 ? 394 THR A C   1 
ATOM   2981 O  O   . THR A 1 385 ? -36.333 -1.967  -15.937 1.00 30.18 ? 394 THR A O   1 
ATOM   2982 C  CB  . THR A 1 385 ? -34.493 -2.481  -18.627 1.00 32.14 ? 394 THR A CB  1 
ATOM   2983 O  OG1 . THR A 1 385 ? -34.623 -2.758  -20.026 1.00 32.39 ? 394 THR A OG1 1 
ATOM   2984 C  CG2 . THR A 1 385 ? -34.513 -3.803  -17.865 1.00 31.56 ? 394 THR A CG2 1 
ATOM   2985 N  N   . THR A 1 386 ? -34.857 -0.292  -16.272 1.00 28.44 ? 395 THR A N   1 
ATOM   2986 C  CA  . THR A 1 386 ? -34.828 0.157   -14.885 1.00 30.12 ? 395 THR A CA  1 
ATOM   2987 C  C   . THR A 1 386 ? -36.182 0.732   -14.436 1.00 31.00 ? 395 THR A C   1 
ATOM   2988 O  O   . THR A 1 386 ? -36.746 0.258   -13.454 1.00 32.30 ? 395 THR A O   1 
ATOM   2989 C  CB  . THR A 1 386 ? -33.702 1.197   -14.669 1.00 28.61 ? 395 THR A CB  1 
ATOM   2990 O  OG1 . THR A 1 386 ? -32.515 0.731   -15.314 1.00 27.80 ? 395 THR A OG1 1 
ATOM   2991 C  CG2 . THR A 1 386 ? -33.423 1.424   -13.192 1.00 27.28 ? 395 THR A CG2 1 
ATOM   2992 N  N   . GLU A 1 387 ? -36.697 1.725   -15.166 1.00 32.90 ? 396 GLU A N   1 
ATOM   2993 C  CA  . GLU A 1 387 ? -38.022 2.338   -14.876 1.00 35.18 ? 396 GLU A CA  1 
ATOM   2994 C  C   . GLU A 1 387 ? -39.156 1.312   -14.823 1.00 36.02 ? 396 GLU A C   1 
ATOM   2995 O  O   . GLU A 1 387 ? -40.025 1.380   -13.960 1.00 36.53 ? 396 GLU A O   1 
ATOM   2996 C  CB  . GLU A 1 387 ? -38.385 3.387   -15.931 1.00 36.03 ? 396 GLU A CB  1 
ATOM   2997 C  CG  . GLU A 1 387 ? -37.521 4.630   -15.925 1.00 43.23 ? 396 GLU A CG  1 
ATOM   2998 C  CD  . GLU A 1 387 ? -37.869 5.606   -17.041 0.00 37.28 ? 396 GLU A CD  1 
ATOM   2999 O  OE1 . GLU A 1 387 ? -38.045 5.165   -18.198 0.00 38.56 ? 396 GLU A OE1 1 
ATOM   3000 O  OE2 . GLU A 1 387 ? -37.950 6.822   -16.765 0.00 39.54 ? 396 GLU A OE2 1 
ATOM   3001 N  N   . LYS A 1 388 ? -39.127 0.363   -15.753 1.00 36.57 ? 397 LYS A N   1 
ATOM   3002 C  CA  . LYS A 1 388 ? -40.127 -0.711  -15.830 1.00 40.75 ? 397 LYS A CA  1 
ATOM   3003 C  C   . LYS A 1 388 ? -40.091 -1.711  -14.656 1.00 39.13 ? 397 LYS A C   1 
ATOM   3004 O  O   . LYS A 1 388 ? -40.982 -2.547  -14.542 1.00 37.55 ? 397 LYS A O   1 
ATOM   3005 C  CB  . LYS A 1 388 ? -39.995 -1.467  -17.164 1.00 41.66 ? 397 LYS A CB  1 
ATOM   3006 C  CG  . LYS A 1 388 ? -40.551 -0.719  -18.369 1.00 45.17 ? 397 LYS A CG  1 
ATOM   3007 C  CD  . LYS A 1 388 ? -40.081 -1.382  -19.670 1.00 48.47 ? 397 LYS A CD  1 
ATOM   3008 C  CE  . LYS A 1 388 ? -40.865 -0.889  -20.884 1.00 55.42 ? 397 LYS A CE  1 
ATOM   3009 N  NZ  . LYS A 1 388 ? -40.405 -1.552  -22.147 0.00 52.59 ? 397 LYS A NZ  1 
ATOM   3010 N  N   . SER A 1 389 ? -39.063 -1.636  -13.809 1.00 37.60 ? 398 SER A N   1 
ATOM   3011 C  CA  . SER A 1 389 ? -39.016 -2.408  -12.565 1.00 38.13 ? 398 SER A CA  1 
ATOM   3012 C  C   . SER A 1 389 ? -39.701 -1.717  -11.384 1.00 38.59 ? 398 SER A C   1 
ATOM   3013 O  O   . SER A 1 389 ? -39.802 -2.309  -10.313 1.00 39.56 ? 398 SER A O   1 
ATOM   3014 C  CB  . SER A 1 389 ? -37.567 -2.734  -12.197 1.00 35.67 ? 398 SER A CB  1 
ATOM   3015 O  OG  . SER A 1 389 ? -36.928 -3.374  -13.279 1.00 36.51 ? 398 SER A OG  1 
ATOM   3016 N  N   . LEU A 1 390 ? -40.158 -0.475  -11.555 1.00 40.68 ? 399 LEU A N   1 
ATOM   3017 C  CA  . LEU A 1 390 ? -40.941 0.191   -10.503 1.00 45.14 ? 399 LEU A CA  1 
ATOM   3018 C  C   . LEU A 1 390 ? -42.214 -0.602  -10.236 1.00 48.93 ? 399 LEU A C   1 
ATOM   3019 O  O   . LEU A 1 390 ? -42.874 -1.044  -11.173 1.00 49.80 ? 399 LEU A O   1 
ATOM   3020 C  CB  . LEU A 1 390 ? -41.288 1.632   -10.879 1.00 44.57 ? 399 LEU A CB  1 
ATOM   3021 C  CG  . LEU A 1 390 ? -40.130 2.634   -10.869 1.00 44.62 ? 399 LEU A CG  1 
ATOM   3022 C  CD1 . LEU A 1 390 ? -40.568 3.945   -11.510 1.00 48.63 ? 399 LEU A CD1 1 
ATOM   3023 C  CD2 . LEU A 1 390 ? -39.597 2.893   -9.462  1.00 45.52 ? 399 LEU A CD2 1 
ATOM   3024 N  N   . LEU A 1 391 ? -42.516 -0.807  -8.955  1.00 53.64 ? 400 LEU A N   1 
ATOM   3025 C  CA  . LEU A 1 391 ? -43.715 -1.529  -8.526  1.00 60.17 ? 400 LEU A CA  1 
ATOM   3026 C  C   . LEU A 1 391 ? -44.926 -0.602  -8.577  1.00 66.08 ? 400 LEU A C   1 
ATOM   3027 O  O   . LEU A 1 391 ? -46.004 -1.024  -9.003  1.00 70.01 ? 400 LEU A O   1 
ATOM   3028 C  CB  . LEU A 1 391 ? -43.542 -2.094  -7.110  1.00 61.92 ? 400 LEU A CB  1 
ATOM   3029 C  CG  . LEU A 1 391 ? -42.262 -2.895  -6.841  1.00 57.55 ? 400 LEU A CG  1 
ATOM   3030 C  CD1 . LEU A 1 391 ? -42.207 -3.324  -5.393  1.00 61.63 ? 400 LEU A CD1 1 
ATOM   3031 C  CD2 . LEU A 1 391 ? -42.164 -4.099  -7.753  1.00 55.38 ? 400 LEU A CD2 1 
ATOM   3032 N  N   . LYS A 1 392 ? -44.738 0.648   -8.138  1.00 68.68 ? 401 LYS A N   1 
ATOM   3033 C  CA  . LYS A 1 392 ? -45.781 1.683   -8.177  1.00 72.80 ? 401 LYS A CA  1 
ATOM   3034 C  C   . LYS A 1 392 ? -45.661 2.500   -9.458  1.00 71.80 ? 401 LYS A C   1 
ATOM   3035 O  O   . LYS A 1 392 ? -44.600 3.061   -9.749  1.00 70.66 ? 401 LYS A O   1 
ATOM   3036 C  CB  . LYS A 1 392 ? -45.663 2.609   -6.960  1.00 76.35 ? 401 LYS A CB  1 
ATOM   3037 C  CG  . LYS A 1 392 ? -46.900 3.457   -6.671  1.00 81.80 ? 401 LYS A CG  1 
ATOM   3038 C  CD  . LYS A 1 392 ? -46.793 4.158   -5.316  1.00 83.95 ? 401 LYS A CD  1 
ATOM   3039 C  CE  . LYS A 1 392 ? -47.998 5.043   -5.050  1.00 89.99 ? 401 LYS A CE  1 
ATOM   3040 N  NZ  . LYS A 1 392 ? -47.929 5.699   -3.711  0.00 94.78 ? 401 LYS A NZ  1 
ATOM   3041 N  N   . ILE B 1 2   ? -26.107 -31.143 -5.571  1.00 62.33 ? 11  ILE B N   1 
ATOM   3042 C  CA  . ILE B 1 2   ? -26.407 -29.853 -6.286  1.00 59.94 ? 11  ILE B CA  1 
ATOM   3043 C  C   . ILE B 1 2   ? -27.689 -29.233 -5.723  1.00 60.39 ? 11  ILE B C   1 
ATOM   3044 O  O   . ILE B 1 2   ? -28.723 -29.906 -5.663  1.00 59.53 ? 11  ILE B O   1 
ATOM   3045 C  CB  . ILE B 1 2   ? -26.555 -30.044 -7.832  1.00 57.02 ? 11  ILE B CB  1 
ATOM   3046 C  CG1 . ILE B 1 2   ? -25.241 -30.550 -8.446  1.00 56.09 ? 11  ILE B CG1 1 
ATOM   3047 C  CG2 . ILE B 1 2   ? -26.952 -28.716 -8.521  1.00 55.41 ? 11  ILE B CG2 1 
ATOM   3048 C  CD1 . ILE B 1 2   ? -25.391 -31.209 -9.779  1.00 53.12 ? 11  ILE B CD1 1 
ATOM   3049 N  N   . SER B 1 3   ? -27.613 -27.956 -5.339  1.00 60.98 ? 12  SER B N   1 
ATOM   3050 C  CA  . SER B 1 3   ? -28.759 -27.228 -4.773  1.00 61.51 ? 12  SER B CA  1 
ATOM   3051 C  C   . SER B 1 3   ? -29.965 -27.224 -5.716  1.00 58.85 ? 12  SER B C   1 
ATOM   3052 O  O   . SER B 1 3   ? -29.819 -27.035 -6.926  1.00 56.36 ? 12  SER B O   1 
ATOM   3053 C  CB  . SER B 1 3   ? -28.380 -25.782 -4.432  1.00 62.56 ? 12  SER B CB  1 
ATOM   3054 O  OG  . SER B 1 3   ? -29.429 -25.127 -3.732  0.00 64.08 ? 12  SER B OG  1 
ATOM   3055 N  N   . LYS B 1 4   ? -31.150 -27.413 -5.134  1.00 59.10 ? 13  LYS B N   1 
ATOM   3056 C  CA  . LYS B 1 4   ? -32.412 -27.519 -5.881  1.00 56.73 ? 13  LYS B CA  1 
ATOM   3057 C  C   . LYS B 1 4   ? -32.771 -26.237 -6.647  1.00 52.80 ? 13  LYS B C   1 
ATOM   3058 O  O   . LYS B 1 4   ? -33.549 -26.287 -7.597  1.00 47.52 ? 13  LYS B O   1 
ATOM   3059 C  CB  . LYS B 1 4   ? -33.559 -27.902 -4.933  1.00 59.99 ? 13  LYS B CB  1 
ATOM   3060 C  CG  . LYS B 1 4   ? -33.400 -29.273 -4.268  1.00 63.52 ? 13  LYS B CG  1 
ATOM   3061 C  CD  . LYS B 1 4   ? -34.388 -29.466 -3.124  1.00 66.39 ? 13  LYS B CD  1 
ATOM   3062 C  CE  . LYS B 1 4   ? -34.345 -30.902 -2.602  0.00 68.51 ? 13  LYS B CE  1 
ATOM   3063 N  NZ  . LYS B 1 4   ? -35.331 -31.124 -1.509  0.00 71.88 ? 13  LYS B NZ  1 
ATOM   3064 N  N   . GLU B 1 5   ? -32.203 -25.104 -6.219  1.00 53.70 ? 14  GLU B N   1 
ATOM   3065 C  CA  . GLU B 1 5   ? -32.325 -23.815 -6.916  1.00 51.68 ? 14  GLU B CA  1 
ATOM   3066 C  C   . GLU B 1 5   ? -31.744 -23.787 -8.338  1.00 47.80 ? 14  GLU B C   1 
ATOM   3067 O  O   . GLU B 1 5   ? -32.145 -22.937 -9.136  1.00 47.03 ? 14  GLU B O   1 
ATOM   3068 C  CB  . GLU B 1 5   ? -31.670 -22.697 -6.089  1.00 54.44 ? 14  GLU B CB  1 
ATOM   3069 C  CG  . GLU B 1 5   ? -30.190 -22.730 -5.904  0.00 55.40 ? 14  GLU B CG  1 
ATOM   3070 C  CD  . GLU B 1 5   ? -29.681 -21.733 -4.874  0.00 58.23 ? 14  GLU B CD  1 
ATOM   3071 O  OE1 . GLU B 1 5   ? -30.232 -20.614 -4.791  0.00 58.93 ? 14  GLU B OE1 1 
ATOM   3072 O  OE2 . GLU B 1 5   ? -28.720 -22.067 -4.150  0.00 60.00 ? 14  GLU B OE2 1 
ATOM   3073 N  N   . TYR B 1 6   ? -30.804 -24.684 -8.649  1.00 44.95 ? 15  TYR B N   1 
ATOM   3074 C  CA  . TYR B 1 6   ? -30.297 -24.820 -10.029 1.00 42.39 ? 15  TYR B CA  1 
ATOM   3075 C  C   . TYR B 1 6   ? -31.224 -25.624 -10.955 1.00 40.74 ? 15  TYR B C   1 
ATOM   3076 O  O   . TYR B 1 6   ? -31.026 -25.612 -12.161 1.00 40.71 ? 15  TYR B O   1 
ATOM   3077 C  CB  . TYR B 1 6   ? -28.873 -25.391 -10.049 1.00 39.67 ? 15  TYR B CB  1 
ATOM   3078 C  CG  . TYR B 1 6   ? -27.851 -24.489 -9.380  1.00 36.97 ? 15  TYR B CG  1 
ATOM   3079 C  CD1 . TYR B 1 6   ? -27.581 -23.210 -9.877  1.00 36.80 ? 15  TYR B CD1 1 
ATOM   3080 C  CD2 . TYR B 1 6   ? -27.167 -24.901 -8.247  1.00 36.23 ? 15  TYR B CD2 1 
ATOM   3081 C  CE1 . TYR B 1 6   ? -26.647 -22.369 -9.255  1.00 36.82 ? 15  TYR B CE1 1 
ATOM   3082 C  CE2 . TYR B 1 6   ? -26.228 -24.077 -7.629  1.00 44.18 ? 15  TYR B CE2 1 
ATOM   3083 C  CZ  . TYR B 1 6   ? -25.972 -22.815 -8.138  1.00 39.60 ? 15  TYR B CZ  1 
ATOM   3084 O  OH  . TYR B 1 6   ? -25.045 -22.018 -7.511  1.00 44.30 ? 15  TYR B OH  1 
ATOM   3085 N  N   . HIS B 1 7   ? -32.227 -26.311 -10.400 1.00 42.42 ? 16  HIS B N   1 
ATOM   3086 C  CA  . HIS B 1 7   ? -33.247 -27.034 -11.193 1.00 40.43 ? 16  HIS B CA  1 
ATOM   3087 C  C   . HIS B 1 7   ? -32.629 -28.059 -12.163 1.00 39.50 ? 16  HIS B C   1 
ATOM   3088 O  O   . HIS B 1 7   ? -32.937 -28.108 -13.368 1.00 37.74 ? 16  HIS B O   1 
ATOM   3089 C  CB  . HIS B 1 7   ? -34.199 -26.047 -11.887 1.00 41.51 ? 16  HIS B CB  1 
ATOM   3090 C  CG  . HIS B 1 7   ? -34.983 -25.206 -10.921 1.00 46.79 ? 16  HIS B CG  1 
ATOM   3091 N  ND1 . HIS B 1 7   ? -35.947 -25.736 -10.090 1.00 55.25 ? 16  HIS B ND1 1 
ATOM   3092 C  CD2 . HIS B 1 7   ? -34.925 -23.886 -10.630 1.00 48.93 ? 16  HIS B CD2 1 
ATOM   3093 C  CE1 . HIS B 1 7   ? -36.458 -24.776 -9.340  1.00 54.08 ? 16  HIS B CE1 1 
ATOM   3094 N  NE2 . HIS B 1 7   ? -35.854 -23.643 -9.648  1.00 51.07 ? 16  HIS B NE2 1 
ATOM   3095 N  N   . ILE B 1 8   ? -31.727 -28.851 -11.592 1.00 38.19 ? 17  ILE B N   1 
ATOM   3096 C  CA  . ILE B 1 8   ? -31.053 -29.940 -12.267 1.00 37.64 ? 17  ILE B CA  1 
ATOM   3097 C  C   . ILE B 1 8   ? -31.587 -31.219 -11.607 1.00 37.68 ? 17  ILE B C   1 
ATOM   3098 O  O   . ILE B 1 8   ? -31.470 -31.399 -10.394 1.00 36.07 ? 17  ILE B O   1 
ATOM   3099 C  CB  . ILE B 1 8   ? -29.509 -29.843 -12.124 1.00 37.00 ? 17  ILE B CB  1 
ATOM   3100 C  CG1 . ILE B 1 8   ? -28.982 -28.585 -12.834 1.00 38.15 ? 17  ILE B CG1 1 
ATOM   3101 C  CG2 . ILE B 1 8   ? -28.823 -31.090 -12.700 1.00 38.72 ? 17  ILE B CG2 1 
ATOM   3102 C  CD1 . ILE B 1 8   ? -27.578 -28.182 -12.439 1.00 35.94 ? 17  ILE B CD1 1 
ATOM   3103 N  N   . ASP B 1 9   ? -32.181 -32.076 -12.426 1.00 37.89 ? 18  ASP B N   1 
ATOM   3104 C  CA  . ASP B 1 9   ? -32.776 -33.318 -11.985 1.00 39.42 ? 18  ASP B CA  1 
ATOM   3105 C  C   . ASP B 1 9   ? -31.718 -34.411 -11.910 1.00 41.30 ? 18  ASP B C   1 
ATOM   3106 O  O   . ASP B 1 9   ? -30.770 -34.419 -12.690 1.00 41.04 ? 18  ASP B O   1 
ATOM   3107 C  CB  . ASP B 1 9   ? -33.869 -33.723 -12.970 1.00 40.27 ? 18  ASP B CB  1 
ATOM   3108 C  CG  . ASP B 1 9   ? -34.637 -34.928 -12.504 1.00 40.95 ? 18  ASP B CG  1 
ATOM   3109 O  OD1 . ASP B 1 9   ? -35.464 -34.757 -11.588 1.00 45.20 ? 18  ASP B OD1 1 
ATOM   3110 O  OD2 . ASP B 1 9   ? -34.386 -36.034 -13.031 1.00 40.63 ? 18  ASP B OD2 1 
ATOM   3111 N  N   . GLU B 1 10  ? -31.891 -35.343 -10.979 1.00 44.94 ? 19  GLU B N   1 
ATOM   3112 C  CA  . GLU B 1 10  ? -30.940 -36.441 -10.813 1.00 47.31 ? 19  GLU B CA  1 
ATOM   3113 C  C   . GLU B 1 10  ? -30.938 -37.394 -12.018 1.00 45.18 ? 19  GLU B C   1 
ATOM   3114 O  O   . GLU B 1 10  ? -29.879 -37.896 -12.407 1.00 46.32 ? 19  GLU B O   1 
ATOM   3115 C  CB  . GLU B 1 10  ? -31.219 -37.224 -9.519  1.00 51.09 ? 19  GLU B CB  1 
ATOM   3116 C  CG  . GLU B 1 10  ? -29.989 -37.966 -8.999  1.00 55.59 ? 19  GLU B CG  1 
ATOM   3117 C  CD  . GLU B 1 10  ? -30.284 -38.972 -7.902  1.00 61.99 ? 19  GLU B CD  1 
ATOM   3118 O  OE1 . GLU B 1 10  ? -31.463 -39.107 -7.489  1.00 71.77 ? 19  GLU B OE1 1 
ATOM   3119 O  OE2 . GLU B 1 10  ? -29.318 -39.639 -7.459  1.00 66.98 ? 19  GLU B OE2 1 
ATOM   3120 N  N   . GLU B 1 11  ? -32.114 -37.635 -12.598 1.00 43.69 ? 20  GLU B N   1 
ATOM   3121 C  CA  . GLU B 1 11  ? -32.253 -38.574 -13.713 1.00 43.86 ? 20  GLU B CA  1 
ATOM   3122 C  C   . GLU B 1 11  ? -31.959 -37.898 -15.047 1.00 39.73 ? 20  GLU B C   1 
ATOM   3123 O  O   . GLU B 1 11  ? -31.131 -38.386 -15.810 1.00 40.97 ? 20  GLU B O   1 
ATOM   3124 C  CB  . GLU B 1 11  ? -33.658 -39.198 -13.747 1.00 45.01 ? 20  GLU B CB  1 
ATOM   3125 C  CG  . GLU B 1 11  ? -33.785 -40.384 -14.720 1.00 47.74 ? 20  GLU B CG  1 
ATOM   3126 C  CD  . GLU B 1 11  ? -35.167 -41.025 -14.732 1.00 49.71 ? 20  GLU B CD  1 
ATOM   3127 O  OE1 . GLU B 1 11  ? -36.168 -40.288 -14.821 1.00 57.62 ? 20  GLU B OE1 1 
ATOM   3128 O  OE2 . GLU B 1 11  ? -35.249 -42.270 -14.682 1.00 52.16 ? 20  GLU B OE2 1 
ATOM   3129 N  N   . VAL B 1 12  ? -32.640 -36.784 -15.315 1.00 36.03 ? 21  VAL B N   1 
ATOM   3130 C  CA  . VAL B 1 12  ? -32.602 -36.135 -16.633 1.00 33.14 ? 21  VAL B CA  1 
ATOM   3131 C  C   . VAL B 1 12  ? -31.786 -34.828 -16.702 1.00 30.42 ? 21  VAL B C   1 
ATOM   3132 O  O   . VAL B 1 12  ? -31.824 -34.143 -17.713 1.00 30.15 ? 21  VAL B O   1 
ATOM   3133 C  CB  . VAL B 1 12  ? -34.035 -35.932 -17.212 1.00 31.40 ? 21  VAL B CB  1 
ATOM   3134 C  CG1 . VAL B 1 12  ? -34.790 -37.267 -17.258 1.00 34.44 ? 21  VAL B CG1 1 
ATOM   3135 C  CG2 . VAL B 1 12  ? -34.834 -34.866 -16.439 1.00 34.30 ? 21  VAL B CG2 1 
ATOM   3136 N  N   . GLY B 1 13  ? -31.038 -34.502 -15.650 1.00 32.98 ? 22  GLY B N   1 
ATOM   3137 C  CA  . GLY B 1 13  ? -30.207 -33.296 -15.622 1.00 32.75 ? 22  GLY B CA  1 
ATOM   3138 C  C   . GLY B 1 13  ? -30.956 -31.999 -15.899 1.00 31.41 ? 22  GLY B C   1 
ATOM   3139 O  O   . GLY B 1 13  ? -31.865 -31.621 -15.156 1.00 29.87 ? 22  GLY B O   1 
ATOM   3140 N  N   . PHE B 1 14  ? -30.560 -31.322 -16.977 1.00 30.03 ? 23  PHE B N   1 
ATOM   3141 C  CA  . PHE B 1 14  ? -31.144 -30.036 -17.360 1.00 27.11 ? 23  PHE B CA  1 
ATOM   3142 C  C   . PHE B 1 14  ? -32.485 -30.169 -18.054 1.00 25.63 ? 23  PHE B C   1 
ATOM   3143 O  O   . PHE B 1 14  ? -33.195 -29.180 -18.180 1.00 24.38 ? 23  PHE B O   1 
ATOM   3144 C  CB  . PHE B 1 14  ? -30.199 -29.260 -18.275 1.00 26.38 ? 23  PHE B CB  1 
ATOM   3145 C  CG  . PHE B 1 14  ? -28.921 -28.864 -17.621 1.00 26.33 ? 23  PHE B CG  1 
ATOM   3146 C  CD1 . PHE B 1 14  ? -28.891 -27.813 -16.722 1.00 29.00 ? 23  PHE B CD1 1 
ATOM   3147 C  CD2 . PHE B 1 14  ? -27.743 -29.529 -17.908 1.00 27.38 ? 23  PHE B CD2 1 
ATOM   3148 C  CE1 . PHE B 1 14  ? -27.712 -27.436 -16.095 1.00 29.98 ? 23  PHE B CE1 1 
ATOM   3149 C  CE2 . PHE B 1 14  ? -26.541 -29.159 -17.293 1.00 30.27 ? 23  PHE B CE2 1 
ATOM   3150 C  CZ  . PHE B 1 14  ? -26.528 -28.108 -16.389 1.00 31.57 ? 23  PHE B CZ  1 
ATOM   3151 N  N   . ALA B 1 15  ? -32.841 -31.361 -18.530 1.00 27.23 ? 24  ALA B N   1 
ATOM   3152 C  CA  . ALA B 1 15  ? -34.193 -31.573 -19.048 1.00 26.96 ? 24  ALA B CA  1 
ATOM   3153 C  C   . ALA B 1 15  ? -35.258 -31.316 -17.973 1.00 29.11 ? 24  ALA B C   1 
ATOM   3154 O  O   . ALA B 1 15  ? -35.002 -31.461 -16.757 1.00 30.34 ? 24  ALA B O   1 
ATOM   3155 C  CB  . ALA B 1 15  ? -34.349 -32.963 -19.619 1.00 28.55 ? 24  ALA B CB  1 
ATOM   3156 N  N   . LEU B 1 16  ? -36.436 -30.907 -18.431 1.00 27.40 ? 25  LEU B N   1 
ATOM   3157 C  CA  . LEU B 1 16  ? -37.589 -30.734 -17.556 1.00 29.59 ? 25  LEU B CA  1 
ATOM   3158 C  C   . LEU B 1 16  ? -38.130 -32.132 -17.240 1.00 31.70 ? 25  LEU B C   1 
ATOM   3159 O  O   . LEU B 1 16  ? -38.519 -32.844 -18.161 1.00 32.08 ? 25  LEU B O   1 
ATOM   3160 C  CB  . LEU B 1 16  ? -38.661 -29.885 -18.242 1.00 26.35 ? 25  LEU B CB  1 
ATOM   3161 C  CG  . LEU B 1 16  ? -39.906 -29.520 -17.435 1.00 27.72 ? 25  LEU B CG  1 
ATOM   3162 C  CD1 . LEU B 1 16  ? -39.569 -28.577 -16.294 1.00 31.58 ? 25  LEU B CD1 1 
ATOM   3163 C  CD2 . LEU B 1 16  ? -40.931 -28.896 -18.333 1.00 26.63 ? 25  LEU B CD2 1 
ATOM   3164 N  N   . PRO B 1 17  ? -38.133 -32.536 -15.949 1.00 34.37 ? 26  PRO B N   1 
ATOM   3165 C  CA  . PRO B 1 17  ? -38.639 -33.877 -15.654 1.00 35.29 ? 26  PRO B CA  1 
ATOM   3166 C  C   . PRO B 1 17  ? -40.149 -33.942 -15.878 1.00 35.70 ? 26  PRO B C   1 
ATOM   3167 O  O   . PRO B 1 17  ? -40.856 -32.983 -15.547 1.00 33.36 ? 26  PRO B O   1 
ATOM   3168 C  CB  . PRO B 1 17  ? -38.288 -34.102 -14.181 1.00 37.57 ? 26  PRO B CB  1 
ATOM   3169 C  CG  . PRO B 1 17  ? -37.765 -32.823 -13.665 1.00 40.21 ? 26  PRO B CG  1 
ATOM   3170 C  CD  . PRO B 1 17  ? -37.714 -31.808 -14.741 1.00 35.23 ? 26  PRO B CD  1 
ATOM   3171 N  N   A ASN B 1 18  ? -40.592 -35.049 -16.475 0.50 36.06 ? 27  ASN B N   1 
ATOM   3172 N  N   B ASN B 1 18  ? -40.629 -35.055 -16.436 0.50 35.39 ? 27  ASN B N   1 
ATOM   3173 C  CA  A ASN B 1 18  ? -41.998 -35.334 -16.752 0.50 35.82 ? 27  ASN B CA  1 
ATOM   3174 C  CA  B ASN B 1 18  ? -42.059 -35.292 -16.683 0.50 35.07 ? 27  ASN B CA  1 
ATOM   3175 C  C   A ASN B 1 18  ? -42.795 -34.100 -17.191 0.50 34.30 ? 27  ASN B C   1 
ATOM   3176 C  C   B ASN B 1 18  ? -42.805 -34.037 -17.173 0.50 33.64 ? 27  ASN B C   1 
ATOM   3177 O  O   A ASN B 1 18  ? -43.640 -33.604 -16.443 0.50 34.87 ? 27  ASN B O   1 
ATOM   3178 O  O   B ASN B 1 18  ? -43.617 -33.461 -16.441 0.50 33.72 ? 27  ASN B O   1 
ATOM   3179 C  CB  A ASN B 1 18  ? -42.624 -36.027 -15.541 0.50 39.10 ? 27  ASN B CB  1 
ATOM   3180 C  CB  B ASN B 1 18  ? -42.710 -35.880 -15.420 0.50 37.78 ? 27  ASN B CB  1 
ATOM   3181 C  CG  A ASN B 1 18  ? -41.901 -37.321 -15.170 0.50 42.81 ? 27  ASN B CG  1 
ATOM   3182 C  CG  B ASN B 1 18  ? -44.141 -36.382 -15.652 0.50 38.35 ? 27  ASN B CG  1 
ATOM   3183 O  OD1 A ASN B 1 18  ? -41.494 -37.513 -14.021 0.50 46.09 ? 27  ASN B OD1 1 
ATOM   3184 O  OD1 B ASN B 1 18  ? -44.552 -36.664 -16.778 0.50 36.69 ? 27  ASN B OD1 1 
ATOM   3185 N  ND2 A ASN B 1 18  ? -41.723 -38.207 -16.151 0.50 42.95 ? 27  ASN B ND2 1 
ATOM   3186 N  ND2 B ASN B 1 18  ? -44.897 -36.500 -14.568 0.50 38.16 ? 27  ASN B ND2 1 
ATOM   3187 N  N   . PRO B 1 19  ? -42.495 -33.581 -18.403 1.00 32.75 ? 28  PRO B N   1 
ATOM   3188 C  CA  . PRO B 1 19  ? -43.165 -32.396 -18.951 1.00 30.66 ? 28  PRO B CA  1 
ATOM   3189 C  C   . PRO B 1 19  ? -44.695 -32.494 -18.995 1.00 31.80 ? 28  PRO B C   1 
ATOM   3190 O  O   . PRO B 1 19  ? -45.251 -33.581 -19.175 1.00 30.09 ? 28  PRO B O   1 
ATOM   3191 C  CB  . PRO B 1 19  ? -42.603 -32.308 -20.371 1.00 27.77 ? 28  PRO B CB  1 
ATOM   3192 C  CG  . PRO B 1 19  ? -41.309 -32.955 -20.291 1.00 28.68 ? 28  PRO B CG  1 
ATOM   3193 C  CD  . PRO B 1 19  ? -41.485 -34.088 -19.354 1.00 29.55 ? 28  PRO B CD  1 
ATOM   3194 N  N   . GLN B 1 20  ? -45.351 -31.356 -18.797 1.00 31.91 ? 29  GLN B N   1 
ATOM   3195 C  CA  . GLN B 1 20  ? -46.805 -31.269 -18.946 1.00 33.80 ? 29  GLN B CA  1 
ATOM   3196 C  C   . GLN B 1 20  ? -47.183 -31.432 -20.421 1.00 30.87 ? 29  GLN B C   1 
ATOM   3197 O  O   . GLN B 1 20  ? -46.474 -30.942 -21.299 1.00 28.67 ? 29  GLN B O   1 
ATOM   3198 C  CB  . GLN B 1 20  ? -47.292 -29.925 -18.417 1.00 34.89 ? 29  GLN B CB  1 
ATOM   3199 C  CG  . GLN B 1 20  ? -48.793 -29.813 -18.248 1.00 35.99 ? 29  GLN B CG  1 
ATOM   3200 C  CD  . GLN B 1 20  ? -49.175 -28.685 -17.302 1.00 39.02 ? 29  GLN B CD  1 
ATOM   3201 O  OE1 . GLN B 1 20  ? -48.532 -28.492 -16.262 1.00 33.99 ? 29  GLN B OE1 1 
ATOM   3202 N  NE2 . GLN B 1 20  ? -50.225 -27.935 -17.655 1.00 35.72 ? 29  GLN B NE2 1 
ATOM   3203 N  N   . GLU B 1 21  ? -48.280 -32.140 -20.674 1.00 31.03 ? 30  GLU B N   1 
ATOM   3204 C  CA  . GLU B 1 21  ? -48.782 -32.398 -22.024 1.00 33.63 ? 30  GLU B CA  1 
ATOM   3205 C  C   . GLU B 1 21  ? -49.982 -31.541 -22.401 1.00 32.20 ? 30  GLU B C   1 
ATOM   3206 O  O   . GLU B 1 21  ? -50.156 -31.217 -23.569 1.00 31.06 ? 30  GLU B O   1 
ATOM   3207 C  CB  . GLU B 1 21  ? -49.219 -33.853 -22.163 1.00 34.56 ? 30  GLU B CB  1 
ATOM   3208 C  CG  . GLU B 1 21  ? -48.129 -34.875 -21.995 1.00 40.14 ? 30  GLU B CG  1 
ATOM   3209 C  CD  . GLU B 1 21  ? -48.660 -36.288 -22.142 1.00 41.19 ? 30  GLU B CD  1 
ATOM   3210 O  OE1 . GLU B 1 21  ? -49.471 -36.529 -23.060 1.00 43.61 ? 30  GLU B OE1 1 
ATOM   3211 O  OE2 . GLU B 1 21  ? -48.261 -37.153 -21.344 1.00 47.67 ? 30  GLU B OE2 1 
ATOM   3212 N  N   . ASN B 1 22  ? -50.825 -31.222 -21.423 1.00 35.05 ? 31  ASN B N   1 
ATOM   3213 C  CA  . ASN B 1 22  ? -52.057 -30.470 -21.651 1.00 35.85 ? 31  ASN B CA  1 
ATOM   3214 C  C   . ASN B 1 22  ? -52.061 -29.190 -20.839 1.00 33.90 ? 31  ASN B C   1 
ATOM   3215 O  O   . ASN B 1 22  ? -51.701 -29.205 -19.665 1.00 31.63 ? 31  ASN B O   1 
ATOM   3216 C  CB  . ASN B 1 22  ? -53.258 -31.323 -21.249 1.00 38.88 ? 31  ASN B CB  1 
ATOM   3217 C  CG  . ASN B 1 22  ? -53.347 -32.617 -22.048 1.00 46.42 ? 31  ASN B CG  1 
ATOM   3218 O  OD1 . ASN B 1 22  ? -53.467 -32.592 -23.276 1.00 52.47 ? 31  ASN B OD1 1 
ATOM   3219 N  ND2 . ASN B 1 22  ? -53.280 -33.750 -21.356 1.00 46.92 ? 31  ASN B ND2 1 
ATOM   3220 N  N   . LEU B 1 23  ? -52.478 -28.094 -21.469 1.00 33.59 ? 32  LEU B N   1 
ATOM   3221 C  CA  . LEU B 1 23  ? -52.676 -26.814 -20.785 1.00 34.36 ? 32  LEU B CA  1 
ATOM   3222 C  C   . LEU B 1 23  ? -54.068 -26.789 -20.170 1.00 37.47 ? 32  LEU B C   1 
ATOM   3223 O  O   . LEU B 1 23  ? -54.909 -27.611 -20.523 1.00 36.83 ? 32  LEU B O   1 
ATOM   3224 C  CB  . LEU B 1 23  ? -52.543 -25.650 -21.773 1.00 32.61 ? 32  LEU B CB  1 
ATOM   3225 C  CG  . LEU B 1 23  ? -51.146 -25.381 -22.318 1.00 31.38 ? 32  LEU B CG  1 
ATOM   3226 C  CD1 . LEU B 1 23  ? -51.201 -24.364 -23.442 1.00 35.43 ? 32  LEU B CD1 1 
ATOM   3227 C  CD2 . LEU B 1 23  ? -50.203 -24.897 -21.221 1.00 37.23 ? 32  LEU B CD2 1 
ATOM   3228 N  N   . PRO B 1 24  ? -54.329 -25.837 -19.256 1.00 39.11 ? 33  PRO B N   1 
ATOM   3229 C  CA  . PRO B 1 24  ? -55.707 -25.594 -18.827 1.00 41.44 ? 33  PRO B CA  1 
ATOM   3230 C  C   . PRO B 1 24  ? -56.666 -25.393 -20.011 1.00 40.35 ? 33  PRO B C   1 
ATOM   3231 O  O   . PRO B 1 24  ? -56.233 -24.944 -21.076 1.00 38.51 ? 33  PRO B O   1 
ATOM   3232 C  CB  . PRO B 1 24  ? -55.591 -24.305 -17.998 1.00 42.03 ? 33  PRO B CB  1 
ATOM   3233 C  CG  . PRO B 1 24  ? -54.216 -24.309 -17.485 1.00 38.81 ? 33  PRO B CG  1 
ATOM   3234 C  CD  . PRO B 1 24  ? -53.374 -24.961 -18.548 1.00 41.22 ? 33  PRO B CD  1 
ATOM   3235 N  N   . ASP B 1 25  ? -57.947 -25.716 -19.810 1.00 42.32 ? 34  ASP B N   1 
ATOM   3236 C  CA  . ASP B 1 25  ? -58.979 -25.594 -20.857 1.00 43.28 ? 34  ASP B CA  1 
ATOM   3237 C  C   . ASP B 1 25  ? -59.063 -24.187 -21.455 1.00 41.91 ? 34  ASP B C   1 
ATOM   3238 O  O   . ASP B 1 25  ? -59.383 -24.032 -22.630 1.00 38.67 ? 34  ASP B O   1 
ATOM   3239 C  CB  . ASP B 1 25  ? -60.372 -25.971 -20.324 1.00 47.45 ? 34  ASP B CB  1 
ATOM   3240 C  CG  . ASP B 1 25  ? -60.494 -27.445 -19.930 1.00 52.39 ? 34  ASP B CG  1 
ATOM   3241 O  OD1 . ASP B 1 25  ? -59.652 -28.273 -20.338 1.00 54.88 ? 34  ASP B OD1 1 
ATOM   3242 O  OD2 . ASP B 1 25  ? -61.460 -27.770 -19.206 1.00 58.98 ? 34  ASP B OD2 1 
ATOM   3243 N  N   . PHE B 1 26  ? -58.788 -23.175 -20.630 1.00 43.09 ? 35  PHE B N   1 
ATOM   3244 C  CA  . PHE B 1 26  ? -58.684 -21.770 -21.063 1.00 42.71 ? 35  PHE B CA  1 
ATOM   3245 C  C   . PHE B 1 26  ? -57.851 -21.599 -22.343 1.00 38.66 ? 35  PHE B C   1 
ATOM   3246 O  O   . PHE B 1 26  ? -58.203 -20.802 -23.214 1.00 38.20 ? 35  PHE B O   1 
ATOM   3247 C  CB  . PHE B 1 26  ? -58.087 -20.922 -19.920 1.00 44.44 ? 35  PHE B CB  1 
ATOM   3248 C  CG  . PHE B 1 26  ? -58.233 -19.445 -20.108 1.00 42.12 ? 35  PHE B CG  1 
ATOM   3249 C  CD1 . PHE B 1 26  ? -59.437 -18.815 -19.817 1.00 48.60 ? 35  PHE B CD1 1 
ATOM   3250 C  CD2 . PHE B 1 26  ? -57.161 -18.676 -20.555 1.00 41.43 ? 35  PHE B CD2 1 
ATOM   3251 C  CE1 . PHE B 1 26  ? -59.582 -17.433 -19.983 1.00 50.30 ? 35  PHE B CE1 1 
ATOM   3252 C  CE2 . PHE B 1 26  ? -57.288 -17.297 -20.729 1.00 43.02 ? 35  PHE B CE2 1 
ATOM   3253 C  CZ  . PHE B 1 26  ? -58.503 -16.672 -20.439 1.00 46.92 ? 35  PHE B CZ  1 
ATOM   3254 N  N   . TYR B 1 27  ? -56.783 -22.388 -22.469 1.00 36.28 ? 36  TYR B N   1 
ATOM   3255 C  CA  . TYR B 1 27  ? -55.858 -22.312 -23.608 1.00 33.40 ? 36  TYR B CA  1 
ATOM   3256 C  C   . TYR B 1 27  ? -56.112 -23.302 -24.756 1.00 33.41 ? 36  TYR B C   1 
ATOM   3257 O  O   . TYR B 1 27  ? -55.247 -23.467 -25.618 1.00 30.98 ? 36  TYR B O   1 
ATOM   3258 C  CB  . TYR B 1 27  ? -54.424 -22.454 -23.087 1.00 30.87 ? 36  TYR B CB  1 
ATOM   3259 C  CG  . TYR B 1 27  ? -54.107 -21.414 -22.055 1.00 28.45 ? 36  TYR B CG  1 
ATOM   3260 C  CD1 . TYR B 1 27  ? -53.808 -20.113 -22.436 1.00 33.29 ? 36  TYR B CD1 1 
ATOM   3261 C  CD2 . TYR B 1 27  ? -54.163 -21.705 -20.694 1.00 35.50 ? 36  TYR B CD2 1 
ATOM   3262 C  CE1 . TYR B 1 27  ? -53.528 -19.133 -21.496 1.00 31.60 ? 36  TYR B CE1 1 
ATOM   3263 C  CE2 . TYR B 1 27  ? -53.880 -20.731 -19.738 1.00 35.90 ? 36  TYR B CE2 1 
ATOM   3264 C  CZ  . TYR B 1 27  ? -53.561 -19.440 -20.150 1.00 32.14 ? 36  TYR B CZ  1 
ATOM   3265 O  OH  . TYR B 1 27  ? -53.290 -18.464 -19.217 1.00 32.94 ? 36  TYR B OH  1 
ATOM   3266 N  N   . ASN B 1 28  ? -57.293 -23.928 -24.792 1.00 35.45 ? 37  ASN B N   1 
ATOM   3267 C  CA  . ASN B 1 28  ? -57.652 -24.879 -25.862 1.00 35.21 ? 37  ASN B CA  1 
ATOM   3268 C  C   . ASN B 1 28  ? -57.379 -24.378 -27.279 1.00 33.86 ? 37  ASN B C   1 
ATOM   3269 O  O   . ASN B 1 28  ? -56.949 -25.160 -28.127 1.00 34.12 ? 37  ASN B O   1 
ATOM   3270 C  CB  . ASN B 1 28  ? -59.135 -25.289 -25.769 1.00 37.65 ? 37  ASN B CB  1 
ATOM   3271 C  CG  . ASN B 1 28  ? -59.410 -26.297 -24.658 1.00 39.73 ? 37  ASN B CG  1 
ATOM   3272 O  OD1 . ASN B 1 28  ? -58.497 -26.864 -24.069 1.00 41.05 ? 37  ASN B OD1 1 
ATOM   3273 N  ND2 . ASN B 1 28  ? -60.687 -26.507 -24.363 1.00 40.13 ? 37  ASN B ND2 1 
ATOM   3274 N  N   . ASP B 1 29  ? -57.636 -23.093 -27.535 1.00 32.60 ? 38  ASP B N   1 
ATOM   3275 C  CA  . ASP B 1 29  ? -57.373 -22.510 -28.859 1.00 34.05 ? 38  ASP B CA  1 
ATOM   3276 C  C   . ASP B 1 29  ? -55.890 -22.549 -29.241 1.00 33.41 ? 38  ASP B C   1 
ATOM   3277 O  O   . ASP B 1 29  ? -55.571 -22.746 -30.418 1.00 33.60 ? 38  ASP B O   1 
ATOM   3278 C  CB  . ASP B 1 29  ? -57.919 -21.079 -28.969 1.00 36.38 ? 38  ASP B CB  1 
ATOM   3279 C  CG  . ASP B 1 29  ? -59.449 -21.020 -28.929 1.00 40.28 ? 38  ASP B CG  1 
ATOM   3280 O  OD1 . ASP B 1 29  ? -60.123 -22.016 -29.277 1.00 43.55 ? 38  ASP B OD1 1 
ATOM   3281 O  OD2 . ASP B 1 29  ? -59.981 -19.959 -28.551 1.00 48.19 ? 38  ASP B OD2 1 
ATOM   3282 N  N   . TRP B 1 30  ? -54.996 -22.364 -28.265 1.00 31.98 ? 39  TRP B N   1 
ATOM   3283 C  CA  . TRP B 1 30  ? -53.558 -22.504 -28.511 1.00 31.12 ? 39  TRP B CA  1 
ATOM   3284 C  C   . TRP B 1 30  ? -53.207 -23.961 -28.784 1.00 29.87 ? 39  TRP B C   1 
ATOM   3285 O  O   . TRP B 1 30  ? -52.516 -24.269 -29.752 1.00 29.96 ? 39  TRP B O   1 
ATOM   3286 C  CB  . TRP B 1 30  ? -52.725 -22.067 -27.308 1.00 31.15 ? 39  TRP B CB  1 
ATOM   3287 C  CG  . TRP B 1 30  ? -52.756 -20.628 -26.969 1.00 30.37 ? 39  TRP B CG  1 
ATOM   3288 C  CD1 . TRP B 1 30  ? -53.345 -19.623 -27.668 1.00 29.19 ? 39  TRP B CD1 1 
ATOM   3289 C  CD2 . TRP B 1 30  ? -52.102 -20.017 -25.854 1.00 27.80 ? 39  TRP B CD2 1 
ATOM   3290 N  NE1 . TRP B 1 30  ? -53.118 -18.429 -27.053 1.00 31.94 ? 39  TRP B NE1 1 
ATOM   3291 C  CE2 . TRP B 1 30  ? -52.365 -18.635 -25.928 1.00 30.01 ? 39  TRP B CE2 1 
ATOM   3292 C  CE3 . TRP B 1 30  ? -51.323 -20.507 -24.795 1.00 27.64 ? 39  TRP B CE3 1 
ATOM   3293 C  CZ2 . TRP B 1 30  ? -51.876 -17.725 -24.984 1.00 30.43 ? 39  TRP B CZ2 1 
ATOM   3294 C  CZ3 . TRP B 1 30  ? -50.836 -19.604 -23.846 1.00 30.10 ? 39  TRP B CZ3 1 
ATOM   3295 C  CH2 . TRP B 1 30  ? -51.117 -18.225 -23.950 1.00 32.47 ? 39  TRP B CH2 1 
ATOM   3296 N  N   . MET B 1 31  ? -53.684 -24.841 -27.909 1.00 30.16 ? 40  MET B N   1 
ATOM   3297 C  CA  . MET B 1 31  ? -53.414 -26.271 -28.017 1.00 31.43 ? 40  MET B CA  1 
ATOM   3298 C  C   . MET B 1 31  ? -53.866 -26.862 -29.340 1.00 31.63 ? 40  MET B C   1 
ATOM   3299 O  O   . MET B 1 31  ? -53.122 -27.646 -29.930 1.00 30.85 ? 40  MET B O   1 
ATOM   3300 C  CB  . MET B 1 31  ? -54.059 -27.041 -26.868 1.00 33.16 ? 40  MET B CB  1 
ATOM   3301 C  CG  . MET B 1 31  ? -53.367 -26.800 -25.532 1.00 43.05 ? 40  MET B CG  1 
ATOM   3302 S  SD  . MET B 1 31  ? -51.669 -27.440 -25.315 1.00 49.70 ? 40  MET B SD  1 
ATOM   3303 C  CE  . MET B 1 31  ? -51.551 -28.780 -26.490 1.00 27.13 ? 40  MET B CE  1 
ATOM   3304 N  N   . PHE B 1 32  ? -55.058 -26.484 -29.812 1.00 30.44 ? 41  PHE B N   1 
ATOM   3305 C  CA  . PHE B 1 32  ? -55.548 -26.992 -31.103 1.00 31.84 ? 41  PHE B CA  1 
ATOM   3306 C  C   . PHE B 1 32  ? -54.576 -26.683 -32.245 1.00 30.29 ? 41  PHE B C   1 
ATOM   3307 O  O   . PHE B 1 32  ? -54.258 -27.556 -33.046 1.00 30.78 ? 41  PHE B O   1 
ATOM   3308 C  CB  . PHE B 1 32  ? -56.948 -26.462 -31.454 1.00 33.55 ? 41  PHE B CB  1 
ATOM   3309 C  CG  . PHE B 1 32  ? -57.352 -26.757 -32.875 1.00 31.46 ? 41  PHE B CG  1 
ATOM   3310 C  CD1 . PHE B 1 32  ? -57.677 -28.054 -33.256 1.00 33.49 ? 41  PHE B CD1 1 
ATOM   3311 C  CD2 . PHE B 1 32  ? -57.352 -25.753 -33.839 1.00 28.87 ? 41  PHE B CD2 1 
ATOM   3312 C  CE1 . PHE B 1 32  ? -58.031 -28.346 -34.583 1.00 34.88 ? 41  PHE B CE1 1 
ATOM   3313 C  CE2 . PHE B 1 32  ? -57.693 -26.032 -35.157 1.00 34.75 ? 41  PHE B CE2 1 
ATOM   3314 C  CZ  . PHE B 1 32  ? -58.035 -27.331 -35.532 1.00 33.21 ? 41  PHE B CZ  1 
ATOM   3315 N  N   . ILE B 1 33  ? -54.106 -25.441 -32.304 1.00 30.63 ? 42  ILE B N   1 
ATOM   3316 C  CA  . ILE B 1 33  ? -53.186 -25.021 -33.361 1.00 29.52 ? 42  ILE B CA  1 
ATOM   3317 C  C   . ILE B 1 33  ? -51.863 -25.800 -33.256 1.00 28.69 ? 42  ILE B C   1 
ATOM   3318 O  O   . ILE B 1 33  ? -51.394 -26.340 -34.251 1.00 26.38 ? 42  ILE B O   1 
ATOM   3319 C  CB  . ILE B 1 33  ? -52.944 -23.481 -33.358 1.00 29.32 ? 42  ILE B CB  1 
ATOM   3320 C  CG1 . ILE B 1 33  ? -54.261 -22.730 -33.640 1.00 28.25 ? 42  ILE B CG1 1 
ATOM   3321 C  CG2 . ILE B 1 33  ? -51.917 -23.093 -34.422 1.00 29.12 ? 42  ILE B CG2 1 
ATOM   3322 C  CD1 . ILE B 1 33  ? -54.193 -21.214 -33.464 1.00 29.58 ? 42  ILE B CD1 1 
ATOM   3323 N  N   . ALA B 1 34  ? -51.295 -25.865 -32.050 1.00 29.10 ? 43  ALA B N   1 
ATOM   3324 C  CA  . ALA B 1 34  ? -50.022 -26.564 -31.808 1.00 29.09 ? 43  ALA B CA  1 
ATOM   3325 C  C   . ALA B 1 34  ? -50.102 -28.061 -32.107 1.00 30.98 ? 43  ALA B C   1 
ATOM   3326 O  O   . ALA B 1 34  ? -49.189 -28.630 -32.732 1.00 30.95 ? 43  ALA B O   1 
ATOM   3327 C  CB  . ALA B 1 34  ? -49.565 -26.344 -30.379 1.00 29.83 ? 43  ALA B CB  1 
ATOM   3328 N  N   . LYS B 1 35  ? -51.203 -28.681 -31.677 1.00 30.54 ? 44  LYS B N   1 
ATOM   3329 C  CA  . LYS B 1 35  ? -51.439 -30.106 -31.892 1.00 32.15 ? 44  LYS B CA  1 
ATOM   3330 C  C   . LYS B 1 35  ? -51.694 -30.480 -33.355 1.00 33.08 ? 44  LYS B C   1 
ATOM   3331 O  O   . LYS B 1 35  ? -51.526 -31.638 -33.718 1.00 30.60 ? 44  LYS B O   1 
ATOM   3332 C  CB  . LYS B 1 35  ? -52.622 -30.601 -31.041 1.00 34.58 ? 44  LYS B CB  1 
ATOM   3333 C  CG  . LYS B 1 35  ? -52.290 -30.746 -29.557 1.00 39.72 ? 44  LYS B CG  1 
ATOM   3334 C  CD  . LYS B 1 35  ? -53.501 -31.236 -28.762 0.00 37.32 ? 44  LYS B CD  1 
ATOM   3335 C  CE  . LYS B 1 35  ? -53.103 -32.062 -27.547 0.00 38.58 ? 44  LYS B CE  1 
ATOM   3336 N  NZ  . LYS B 1 35  ? -54.268 -32.361 -26.669 0.00 40.94 ? 44  LYS B NZ  1 
ATOM   3337 N  N   . HIS B 1 36  ? -52.133 -29.512 -34.166 1.00 31.48 ? 45  HIS B N   1 
ATOM   3338 C  CA  . HIS B 1 36  ? -52.468 -29.746 -35.560 1.00 29.05 ? 45  HIS B CA  1 
ATOM   3339 C  C   . HIS B 1 36  ? -51.648 -28.903 -36.532 1.00 27.23 ? 45  HIS B C   1 
ATOM   3340 O  O   . HIS B 1 36  ? -52.105 -28.637 -37.650 1.00 25.96 ? 45  HIS B O   1 
ATOM   3341 C  CB  . HIS B 1 36  ? -53.961 -29.522 -35.764 1.00 29.32 ? 45  HIS B CB  1 
ATOM   3342 C  CG  . HIS B 1 36  ? -54.810 -30.557 -35.104 1.00 35.37 ? 45  HIS B CG  1 
ATOM   3343 N  ND1 . HIS B 1 36  ? -55.137 -31.745 -35.721 1.00 36.65 ? 45  HIS B ND1 1 
ATOM   3344 C  CD2 . HIS B 1 36  ? -55.390 -30.593 -33.881 1.00 33.95 ? 45  HIS B CD2 1 
ATOM   3345 C  CE1 . HIS B 1 36  ? -55.894 -32.464 -34.911 1.00 38.02 ? 45  HIS B CE1 1 
ATOM   3346 N  NE2 . HIS B 1 36  ? -56.056 -31.791 -33.787 1.00 34.56 ? 45  HIS B NE2 1 
ATOM   3347 N  N   . LEU B 1 37  ? -50.434 -28.510 -36.130 1.00 25.85 ? 46  LEU B N   1 
ATOM   3348 C  CA  . LEU B 1 37  ? -49.553 -27.732 -37.008 1.00 26.99 ? 46  LEU B CA  1 
ATOM   3349 C  C   . LEU B 1 37  ? -49.336 -28.365 -38.384 1.00 26.31 ? 46  LEU B C   1 
ATOM   3350 O  O   . LEU B 1 37  ? -49.511 -27.686 -39.395 1.00 27.58 ? 46  LEU B O   1 
ATOM   3351 C  CB  . LEU B 1 37  ? -48.190 -27.430 -36.360 1.00 27.78 ? 46  LEU B CB  1 
ATOM   3352 C  CG  . LEU B 1 37  ? -48.101 -26.344 -35.292 1.00 28.47 ? 46  LEU B CG  1 
ATOM   3353 C  CD1 . LEU B 1 37  ? -46.639 -26.169 -34.906 1.00 26.02 ? 46  LEU B CD1 1 
ATOM   3354 C  CD2 . LEU B 1 37  ? -48.691 -25.002 -35.713 1.00 33.96 ? 46  LEU B CD2 1 
ATOM   3355 N  N   . PRO B 1 38  ? -48.975 -29.663 -38.439 1.00 26.96 ? 47  PRO B N   1 
ATOM   3356 C  CA  . PRO B 1 38  ? -48.819 -30.281 -39.750 1.00 27.89 ? 47  PRO B CA  1 
ATOM   3357 C  C   . PRO B 1 38  ? -50.052 -30.128 -40.650 1.00 29.94 ? 47  PRO B C   1 
ATOM   3358 O  O   . PRO B 1 38  ? -49.909 -29.813 -41.840 1.00 31.41 ? 47  PRO B O   1 
ATOM   3359 C  CB  . PRO B 1 38  ? -48.563 -31.755 -39.409 1.00 26.91 ? 47  PRO B CB  1 
ATOM   3360 C  CG  . PRO B 1 38  ? -47.997 -31.730 -38.097 1.00 27.24 ? 47  PRO B CG  1 
ATOM   3361 C  CD  . PRO B 1 38  ? -48.663 -30.621 -37.366 1.00 26.66 ? 47  PRO B CD  1 
ATOM   3362 N  N   . ASP B 1 39  ? -51.238 -30.334 -40.077 1.00 28.78 ? 48  ASP B N   1 
ATOM   3363 C  CA  . ASP B 1 39  ? -52.489 -30.271 -40.842 1.00 30.75 ? 48  ASP B CA  1 
ATOM   3364 C  C   . ASP B 1 39  ? -52.824 -28.836 -41.246 1.00 28.50 ? 48  ASP B C   1 
ATOM   3365 O  O   . ASP B 1 39  ? -53.255 -28.586 -42.371 1.00 29.53 ? 48  ASP B O   1 
ATOM   3366 C  CB  . ASP B 1 39  ? -53.650 -30.856 -40.033 1.00 31.56 ? 48  ASP B CB  1 
ATOM   3367 C  CG  . ASP B 1 39  ? -53.434 -32.315 -39.662 1.00 34.33 ? 48  ASP B CG  1 
ATOM   3368 O  OD1 . ASP B 1 39  ? -52.917 -33.095 -40.495 1.00 34.43 ? 48  ASP B OD1 1 
ATOM   3369 O  OD2 . ASP B 1 39  ? -53.793 -32.675 -38.526 1.00 33.64 ? 48  ASP B OD2 1 
ATOM   3370 N  N   . LEU B 1 40  ? -52.624 -27.907 -40.323 1.00 27.52 ? 49  LEU B N   1 
ATOM   3371 C  CA  . LEU B 1 40  ? -52.940 -26.502 -40.562 1.00 28.74 ? 49  LEU B CA  1 
ATOM   3372 C  C   . LEU B 1 40  ? -51.966 -25.854 -41.541 1.00 28.53 ? 49  LEU B C   1 
ATOM   3373 O  O   . LEU B 1 40  ? -52.388 -25.072 -42.393 1.00 28.39 ? 49  LEU B O   1 
ATOM   3374 C  CB  . LEU B 1 40  ? -53.002 -25.723 -39.245 1.00 23.55 ? 49  LEU B CB  1 
ATOM   3375 C  CG  . LEU B 1 40  ? -54.163 -26.114 -38.326 1.00 28.55 ? 49  LEU B CG  1 
ATOM   3376 C  CD1 . LEU B 1 40  ? -53.991 -25.458 -36.973 1.00 26.06 ? 49  LEU B CD1 1 
ATOM   3377 C  CD2 . LEU B 1 40  ? -55.555 -25.771 -38.937 1.00 27.13 ? 49  LEU B CD2 1 
ATOM   3378 N  N   . ILE B 1 41  ? -50.685 -26.212 -41.451 1.00 28.33 ? 50  ILE B N   1 
ATOM   3379 C  CA  . ILE B 1 41  ? -49.684 -25.721 -42.408 1.00 29.48 ? 50  ILE B CA  1 
ATOM   3380 C  C   . ILE B 1 41  ? -49.961 -26.254 -43.805 1.00 31.64 ? 50  ILE B C   1 
ATOM   3381 O  O   . ILE B 1 41  ? -50.013 -25.468 -44.748 1.00 34.71 ? 50  ILE B O   1 
ATOM   3382 C  CB  . ILE B 1 41  ? -48.224 -26.032 -41.977 1.00 28.87 ? 50  ILE B CB  1 
ATOM   3383 C  CG1 . ILE B 1 41  ? -47.887 -25.288 -40.680 1.00 29.28 ? 50  ILE B CG1 1 
ATOM   3384 C  CG2 . ILE B 1 41  ? -47.221 -25.619 -43.080 1.00 30.62 ? 50  ILE B CG2 1 
ATOM   3385 C  CD1 . ILE B 1 41  ? -46.689 -25.862 -39.952 1.00 30.82 ? 50  ILE B CD1 1 
ATOM   3386 N  N   A GLU B 1 42  ? -50.155 -27.567 -43.924 0.50 32.63 ? 51  GLU B N   1 
ATOM   3387 N  N   B GLU B 1 42  ? -50.141 -27.575 -43.930 0.50 32.22 ? 51  GLU B N   1 
ATOM   3388 C  CA  A GLU B 1 42  ? -50.384 -28.207 -45.221 0.50 33.95 ? 51  GLU B CA  1 
ATOM   3389 C  CA  B GLU B 1 42  ? -50.402 -28.223 -45.230 0.50 34.00 ? 51  GLU B CA  1 
ATOM   3390 C  C   A GLU B 1 42  ? -51.652 -27.702 -45.936 0.50 34.57 ? 51  GLU B C   1 
ATOM   3391 C  C   B GLU B 1 42  ? -51.644 -27.664 -45.937 0.50 34.44 ? 51  GLU B C   1 
ATOM   3392 O  O   A GLU B 1 42  ? -51.673 -27.633 -47.169 0.50 35.13 ? 51  GLU B O   1 
ATOM   3393 O  O   B GLU B 1 42  ? -51.642 -27.519 -47.164 0.50 35.13 ? 51  GLU B O   1 
ATOM   3394 C  CB  A GLU B 1 42  ? -50.429 -29.736 -45.071 0.50 35.46 ? 51  GLU B CB  1 
ATOM   3395 C  CB  B GLU B 1 42  ? -50.534 -29.754 -45.091 0.50 34.99 ? 51  GLU B CB  1 
ATOM   3396 C  CG  A GLU B 1 42  ? -50.202 -30.506 -46.366 0.50 40.43 ? 51  GLU B CG  1 
ATOM   3397 C  CG  B GLU B 1 42  ? -50.471 -30.519 -46.436 0.50 38.77 ? 51  GLU B CG  1 
ATOM   3398 C  CD  A GLU B 1 42  ? -48.742 -30.542 -46.778 0.50 45.58 ? 51  GLU B CD  1 
ATOM   3399 C  CD  B GLU B 1 42  ? -51.043 -31.938 -46.379 0.50 40.76 ? 51  GLU B CD  1 
ATOM   3400 O  OE1 A GLU B 1 42  ? -47.976 -31.322 -46.170 0.50 49.60 ? 51  GLU B OE1 1 
ATOM   3401 O  OE1 B GLU B 1 42  ? -50.779 -32.659 -45.395 0.50 41.40 ? 51  GLU B OE1 1 
ATOM   3402 O  OE2 A GLU B 1 42  ? -48.358 -29.795 -47.706 0.50 46.96 ? 51  GLU B OE2 1 
ATOM   3403 O  OE2 B GLU B 1 42  ? -51.747 -32.337 -47.337 0.50 42.28 ? 51  GLU B OE2 1 
ATOM   3404 N  N   . SER B 1 43  ? -52.689 -27.358 -45.166 1.00 32.61 ? 52  SER B N   1 
ATOM   3405 C  CA  . SER B 1 43  ? -53.942 -26.797 -45.718 1.00 34.74 ? 52  SER B CA  1 
ATOM   3406 C  C   . SER B 1 43  ? -53.928 -25.278 -45.918 1.00 33.32 ? 52  SER B C   1 
ATOM   3407 O  O   . SER B 1 43  ? -54.875 -24.733 -46.464 1.00 34.28 ? 52  SER B O   1 
ATOM   3408 C  CB  . SER B 1 43  ? -55.142 -27.163 -44.838 1.00 33.74 ? 52  SER B CB  1 
ATOM   3409 O  OG  . SER B 1 43  ? -55.004 -26.615 -43.546 1.00 30.37 ? 52  SER B OG  1 
ATOM   3410 N  N   . GLY B 1 44  ? -52.869 -24.603 -45.487 1.00 32.98 ? 53  GLY B N   1 
ATOM   3411 C  CA  . GLY B 1 44  ? -52.789 -23.149 -45.582 1.00 34.48 ? 53  GLY B CA  1 
ATOM   3412 C  C   . GLY B 1 44  ? -53.755 -22.458 -44.632 1.00 34.48 ? 53  GLY B C   1 
ATOM   3413 O  O   . GLY B 1 44  ? -54.190 -21.344 -44.905 1.00 31.83 ? 53  GLY B O   1 
ATOM   3414 N  N   . GLN B 1 45  ? -54.072 -23.120 -43.515 1.00 33.75 ? 54  GLN B N   1 
ATOM   3415 C  CA  . GLN B 1 45  ? -55.040 -22.615 -42.539 1.00 33.85 ? 54  GLN B CA  1 
ATOM   3416 C  C   . GLN B 1 45  ? -54.378 -22.114 -41.259 1.00 30.19 ? 54  GLN B C   1 
ATOM   3417 O  O   . GLN B 1 45  ? -55.041 -21.495 -40.438 1.00 27.78 ? 54  GLN B O   1 
ATOM   3418 C  CB  . GLN B 1 45  ? -56.046 -23.713 -42.189 1.00 35.73 ? 54  GLN B CB  1 
ATOM   3419 C  CG  . GLN B 1 45  ? -56.930 -24.166 -43.357 1.00 42.20 ? 54  GLN B CG  1 
ATOM   3420 C  CD  . GLN B 1 45  ? -58.160 -23.296 -43.602 1.00 49.34 ? 54  GLN B CD  1 
ATOM   3421 O  OE1 . GLN B 1 45  ? -59.044 -23.683 -44.366 1.00 53.42 ? 54  GLN B OE1 1 
ATOM   3422 N  NE2 . GLN B 1 45  ? -58.228 -22.130 -42.959 1.00 53.69 ? 54  GLN B NE2 1 
ATOM   3423 N  N   . LEU B 1 46  ? -53.081 -22.365 -41.092 1.00 29.51 ? 55  LEU B N   1 
ATOM   3424 C  CA  . LEU B 1 46  ? -52.381 -22.023 -39.850 1.00 29.70 ? 55  LEU B CA  1 
ATOM   3425 C  C   . LEU B 1 46  ? -52.409 -20.519 -39.567 1.00 30.00 ? 55  LEU B C   1 
ATOM   3426 O  O   . LEU B 1 46  ? -52.734 -20.088 -38.457 1.00 26.31 ? 55  LEU B O   1 
ATOM   3427 C  CB  . LEU B 1 46  ? -50.927 -22.524 -39.903 1.00 28.32 ? 55  LEU B CB  1 
ATOM   3428 C  CG  . LEU B 1 46  ? -49.967 -22.325 -38.721 1.00 30.19 ? 55  LEU B CG  1 
ATOM   3429 C  CD1 . LEU B 1 46  ? -49.244 -20.957 -38.737 1.00 34.04 ? 55  LEU B CD1 1 
ATOM   3430 C  CD2 . LEU B 1 46  ? -50.649 -22.542 -37.392 1.00 29.57 ? 55  LEU B CD2 1 
ATOM   3431 N  N   . ARG B 1 47  ? -52.043 -19.727 -40.564 1.00 31.79 ? 56  ARG B N   1 
ATOM   3432 C  CA  . ARG B 1 47  ? -51.972 -18.275 -40.369 1.00 34.82 ? 56  ARG B CA  1 
ATOM   3433 C  C   . ARG B 1 47  ? -53.329 -17.674 -40.016 1.00 34.32 ? 56  ARG B C   1 
ATOM   3434 O  O   . ARG B 1 47  ? -53.418 -16.883 -39.081 1.00 36.13 ? 56  ARG B O   1 
ATOM   3435 C  CB  . ARG B 1 47  ? -51.324 -17.602 -41.577 1.00 36.48 ? 56  ARG B CB  1 
ATOM   3436 C  CG  . ARG B 1 47  ? -49.822 -17.850 -41.559 1.00 38.62 ? 56  ARG B CG  1 
ATOM   3437 C  CD  . ARG B 1 47  ? -49.172 -17.672 -42.887 1.00 40.13 ? 56  ARG B CD  1 
ATOM   3438 N  NE  . ARG B 1 47  ? -47.719 -17.636 -42.735 1.00 38.61 ? 56  ARG B NE  1 
ATOM   3439 C  CZ  . ARG B 1 47  ? -46.854 -17.544 -43.746 1.00 35.99 ? 56  ARG B CZ  1 
ATOM   3440 N  NH1 . ARG B 1 47  ? -47.263 -17.518 -45.014 1.00 29.74 ? 56  ARG B NH1 1 
ATOM   3441 N  NH2 . ARG B 1 47  ? -45.553 -17.495 -43.480 1.00 35.28 ? 56  ARG B NH2 1 
ATOM   3442 N  N   . GLU B 1 48  ? -54.373 -18.111 -40.719 1.00 35.81 ? 57  GLU B N   1 
ATOM   3443 C  CA  . GLU B 1 48  ? -55.757 -17.693 -40.447 1.00 37.54 ? 57  GLU B CA  1 
ATOM   3444 C  C   . GLU B 1 48  ? -56.170 -18.045 -39.024 1.00 34.63 ? 57  GLU B C   1 
ATOM   3445 O  O   . GLU B 1 48  ? -56.761 -17.219 -38.328 1.00 34.50 ? 57  GLU B O   1 
ATOM   3446 C  CB  . GLU B 1 48  ? -56.739 -18.334 -41.452 1.00 37.67 ? 57  GLU B CB  1 
ATOM   3447 C  CG  . GLU B 1 48  ? -58.215 -17.959 -41.246 1.00 43.73 ? 57  GLU B CG  1 
ATOM   3448 C  CD  . GLU B 1 48  ? -59.111 -18.359 -42.417 1.00 51.92 ? 57  GLU B CD  1 
ATOM   3449 O  OE1 . GLU B 1 48  ? -58.910 -19.453 -42.995 1.00 67.65 ? 57  GLU B OE1 1 
ATOM   3450 O  OE2 . GLU B 1 48  ? -60.031 -17.584 -42.754 1.00 66.76 ? 57  GLU B OE2 1 
ATOM   3451 N  N   . ARG B 1 49  ? -55.858 -19.266 -38.593 1.00 31.94 ? 58  ARG B N   1 
ATOM   3452 C  CA  . ARG B 1 49  ? -56.210 -19.710 -37.240 1.00 31.35 ? 58  ARG B CA  1 
ATOM   3453 C  C   . ARG B 1 49  ? -55.533 -18.841 -36.173 1.00 30.73 ? 58  ARG B C   1 
ATOM   3454 O  O   . ARG B 1 49  ? -56.172 -18.438 -35.195 1.00 30.97 ? 58  ARG B O   1 
ATOM   3455 C  CB  . ARG B 1 49  ? -55.852 -21.186 -37.031 1.00 29.16 ? 58  ARG B CB  1 
ATOM   3456 C  CG  . ARG B 1 49  ? -56.779 -22.173 -37.709 1.00 33.30 ? 58  ARG B CG  1 
ATOM   3457 C  CD  . ARG B 1 49  ? -58.182 -22.170 -37.092 1.00 36.65 ? 58  ARG B CD  1 
ATOM   3458 N  NE  . ARG B 1 49  ? -59.068 -21.247 -37.782 1.00 33.00 ? 58  ARG B NE  1 
ATOM   3459 C  CZ  . ARG B 1 49  ? -60.175 -20.688 -37.281 1.00 41.39 ? 58  ARG B CZ  1 
ATOM   3460 N  NH1 . ARG B 1 49  ? -60.601 -20.932 -36.037 1.00 36.95 ? 58  ARG B NH1 1 
ATOM   3461 N  NH2 . ARG B 1 49  ? -60.877 -19.862 -38.053 1.00 43.07 ? 58  ARG B NH2 1 
ATOM   3462 N  N   . VAL B 1 50  ? -54.250 -18.551 -36.385 1.00 29.92 ? 59  VAL B N   1 
ATOM   3463 C  CA  . VAL B 1 50  ? -53.483 -17.692 -35.484 1.00 29.98 ? 59  VAL B CA  1 
ATOM   3464 C  C   . VAL B 1 50  ? -54.079 -16.285 -35.471 1.00 31.19 ? 59  VAL B C   1 
ATOM   3465 O  O   . VAL B 1 50  ? -54.256 -15.703 -34.412 1.00 30.17 ? 59  VAL B O   1 
ATOM   3466 C  CB  . VAL B 1 50  ? -51.963 -17.660 -35.856 1.00 26.88 ? 59  VAL B CB  1 
ATOM   3467 C  CG1 . VAL B 1 50  ? -51.211 -16.563 -35.100 1.00 28.61 ? 59  VAL B CG1 1 
ATOM   3468 C  CG2 . VAL B 1 50  ? -51.328 -19.012 -35.556 1.00 27.77 ? 59  VAL B CG2 1 
ATOM   3469 N  N   . GLU B 1 51  ? -54.392 -15.760 -36.651 1.00 34.76 ? 60  GLU B N   1 
ATOM   3470 C  CA  . GLU B 1 51  ? -54.989 -14.424 -36.777 1.00 36.73 ? 60  GLU B CA  1 
ATOM   3471 C  C   . GLU B 1 51  ? -56.379 -14.318 -36.133 1.00 36.84 ? 60  GLU B C   1 
ATOM   3472 O  O   . GLU B 1 51  ? -56.756 -13.246 -35.671 1.00 36.02 ? 60  GLU B O   1 
ATOM   3473 C  CB  . GLU B 1 51  ? -55.012 -13.995 -38.248 1.00 37.50 ? 60  GLU B CB  1 
ATOM   3474 C  CG  . GLU B 1 51  ? -53.595 -13.711 -38.787 1.00 37.73 ? 60  GLU B CG  1 
ATOM   3475 C  CD  . GLU B 1 51  ? -53.443 -13.896 -40.293 1.00 39.45 ? 60  GLU B CD  1 
ATOM   3476 O  OE1 . GLU B 1 51  ? -52.286 -14.043 -40.734 1.00 41.99 ? 60  GLU B OE1 1 
ATOM   3477 O  OE2 . GLU B 1 51  ? -54.452 -13.894 -41.035 1.00 43.39 ? 60  GLU B OE2 1 
ATOM   3478 N  N   . LYS B 1 52  ? -57.107 -15.434 -36.084 1.00 37.59 ? 61  LYS B N   1 
ATOM   3479 C  CA  . LYS B 1 52  ? -58.439 -15.498 -35.450 1.00 39.65 ? 61  LYS B CA  1 
ATOM   3480 C  C   . LYS B 1 52  ? -58.411 -15.626 -33.928 1.00 37.40 ? 61  LYS B C   1 
ATOM   3481 O  O   . LYS B 1 52  ? -59.450 -15.459 -33.284 1.00 40.09 ? 61  LYS B O   1 
ATOM   3482 C  CB  . LYS B 1 52  ? -59.286 -16.647 -36.049 1.00 40.73 ? 61  LYS B CB  1 
ATOM   3483 C  CG  . LYS B 1 52  ? -60.263 -16.205 -37.120 1.00 48.53 ? 61  LYS B CG  1 
ATOM   3484 C  CD  . LYS B 1 52  ? -59.575 -15.654 -38.360 1.00 54.67 ? 61  LYS B CD  1 
ATOM   3485 C  CE  . LYS B 1 52  ? -60.592 -15.116 -39.359 1.00 56.37 ? 61  LYS B CE  1 
ATOM   3486 N  NZ  . LYS B 1 52  ? -61.239 -16.236 -40.098 1.00 58.91 ? 61  LYS B NZ  1 
ATOM   3487 N  N   . LEU B 1 53  ? -57.250 -15.938 -33.354 1.00 35.37 ? 62  LEU B N   1 
ATOM   3488 C  CA  . LEU B 1 53  ? -57.103 -16.017 -31.899 1.00 34.02 ? 62  LEU B CA  1 
ATOM   3489 C  C   . LEU B 1 53  ? -57.480 -14.714 -31.216 1.00 36.03 ? 62  LEU B C   1 
ATOM   3490 O  O   . LEU B 1 53  ? -57.136 -13.642 -31.705 1.00 34.53 ? 62  LEU B O   1 
ATOM   3491 C  CB  . LEU B 1 53  ? -55.654 -16.336 -31.503 1.00 34.03 ? 62  LEU B CB  1 
ATOM   3492 C  CG  . LEU B 1 53  ? -55.103 -17.731 -31.761 1.00 33.34 ? 62  LEU B CG  1 
ATOM   3493 C  CD1 . LEU B 1 53  ? -53.647 -17.774 -31.336 1.00 33.24 ? 62  LEU B CD1 1 
ATOM   3494 C  CD2 . LEU B 1 53  ? -55.904 -18.786 -31.008 1.00 38.32 ? 62  LEU B CD2 1 
ATOM   3495 N  N   . ASN B 1 54  ? -58.195 -14.832 -30.099 1.00 36.60 ? 63  ASN B N   1 
ATOM   3496 C  CA  . ASN B 1 54  ? -58.313 -13.761 -29.124 1.00 39.10 ? 63  ASN B CA  1 
ATOM   3497 C  C   . ASN B 1 54  ? -57.045 -13.754 -28.277 1.00 38.31 ? 63  ASN B C   1 
ATOM   3498 O  O   . ASN B 1 54  ? -56.420 -14.811 -28.080 1.00 35.30 ? 63  ASN B O   1 
ATOM   3499 C  CB  . ASN B 1 54  ? -59.515 -13.983 -28.203 1.00 43.12 ? 63  ASN B CB  1 
ATOM   3500 C  CG  . ASN B 1 54  ? -60.845 -14.029 -28.948 1.00 47.11 ? 63  ASN B CG  1 
ATOM   3501 O  OD1 . ASN B 1 54  ? -61.629 -14.958 -28.764 1.00 51.26 ? 63  ASN B OD1 1 
ATOM   3502 N  ND2 . ASN B 1 54  ? -61.105 -13.026 -29.780 1.00 45.83 ? 63  ASN B ND2 1 
ATOM   3503 N  N   . MET B 1 55  ? -56.665 -12.572 -27.787 1.00 38.44 ? 64  MET B N   1 
ATOM   3504 C  CA  . MET B 1 55  ? -55.543 -12.434 -26.853 1.00 38.80 ? 64  MET B CA  1 
ATOM   3505 C  C   . MET B 1 55  ? -55.900 -13.065 -25.508 1.00 38.39 ? 64  MET B C   1 
ATOM   3506 O  O   . MET B 1 55  ? -56.802 -12.588 -24.822 1.00 39.93 ? 64  MET B O   1 
ATOM   3507 C  CB  . MET B 1 55  ? -55.167 -10.962 -26.636 1.00 40.41 ? 64  MET B CB  1 
ATOM   3508 C  CG  . MET B 1 55  ? -53.761 -10.770 -26.037 1.00 38.27 ? 64  MET B CG  1 
ATOM   3509 S  SD  . MET B 1 55  ? -53.339 -9.028  -25.782 1.00 47.94 ? 64  MET B SD  1 
ATOM   3510 C  CE  . MET B 1 55  ? -53.262 -8.391  -27.456 1.00 45.73 ? 64  MET B CE  1 
ATOM   3511 N  N   . LEU B 1 56  ? -55.197 -14.136 -25.144 1.00 35.59 ? 65  LEU B N   1 
ATOM   3512 C  CA  . LEU B 1 56  ? -55.437 -14.837 -23.881 1.00 36.66 ? 65  LEU B CA  1 
ATOM   3513 C  C   . LEU B 1 56  ? -54.406 -14.432 -22.834 1.00 37.77 ? 65  LEU B C   1 
ATOM   3514 O  O   . LEU B 1 56  ? -53.209 -14.358 -23.125 1.00 36.17 ? 65  LEU B O   1 
ATOM   3515 C  CB  . LEU B 1 56  ? -55.421 -16.356 -24.084 1.00 34.81 ? 65  LEU B CB  1 
ATOM   3516 C  CG  . LEU B 1 56  ? -56.468 -16.914 -25.058 1.00 32.42 ? 65  LEU B CG  1 
ATOM   3517 C  CD1 . LEU B 1 56  ? -56.251 -18.408 -25.270 1.00 36.31 ? 65  LEU B CD1 1 
ATOM   3518 C  CD2 . LEU B 1 56  ? -57.891 -16.646 -24.594 1.00 39.63 ? 65  LEU B CD2 1 
ATOM   3519 N  N   . SER B 1 57  ? -54.891 -14.159 -21.620 1.00 39.59 ? 66  SER B N   1 
ATOM   3520 C  CA  . SER B 1 57  ? -54.041 -13.849 -20.480 1.00 40.67 ? 66  SER B CA  1 
ATOM   3521 C  C   . SER B 1 57  ? -53.180 -15.061 -20.124 1.00 39.99 ? 66  SER B C   1 
ATOM   3522 O  O   . SER B 1 57  ? -53.647 -16.197 -20.217 1.00 38.92 ? 66  SER B O   1 
ATOM   3523 C  CB  . SER B 1 57  ? -54.897 -13.443 -19.272 1.00 43.25 ? 66  SER B CB  1 
ATOM   3524 O  OG  . SER B 1 57  ? -54.123 -13.386 -18.089 1.00 43.90 ? 66  SER B OG  1 
ATOM   3525 N  N   . ILE B 1 58  ? -51.931 -14.813 -19.726 1.00 38.76 ? 67  ILE B N   1 
ATOM   3526 C  CA  . ILE B 1 58  ? -51.045 -15.880 -19.240 1.00 38.09 ? 67  ILE B CA  1 
ATOM   3527 C  C   . ILE B 1 58  ? -51.188 -16.148 -17.735 1.00 39.63 ? 67  ILE B C   1 
ATOM   3528 O  O   . ILE B 1 58  ? -50.481 -17.004 -17.193 1.00 37.08 ? 67  ILE B O   1 
ATOM   3529 C  CB  . ILE B 1 58  ? -49.543 -15.613 -19.574 1.00 37.91 ? 67  ILE B CB  1 
ATOM   3530 C  CG1 . ILE B 1 58  ? -48.995 -14.367 -18.854 1.00 39.93 ? 67  ILE B CG1 1 
ATOM   3531 C  CG2 . ILE B 1 58  ? -49.350 -15.489 -21.078 1.00 36.03 ? 67  ILE B CG2 1 
ATOM   3532 C  CD1 . ILE B 1 58  ? -47.511 -14.435 -18.600 1.00 39.44 ? 67  ILE B CD1 1 
ATOM   3533 N  N   . ASP B 1 59  ? -52.081 -15.414 -17.066 1.00 43.33 ? 68  ASP B N   1 
ATOM   3534 C  CA  . ASP B 1 59  ? -52.227 -15.483 -15.604 1.00 46.63 ? 68  ASP B CA  1 
ATOM   3535 C  C   . ASP B 1 59  ? -52.797 -16.815 -15.100 1.00 46.44 ? 68  ASP B C   1 
ATOM   3536 O  O   . ASP B 1 59  ? -52.640 -17.148 -13.926 1.00 46.62 ? 68  ASP B O   1 
ATOM   3537 C  CB  . ASP B 1 59  ? -53.100 -14.319 -15.089 1.00 50.35 ? 68  ASP B CB  1 
ATOM   3538 C  CG  . ASP B 1 59  ? -52.438 -12.940 -15.265 1.00 53.09 ? 68  ASP B CG  1 
ATOM   3539 O  OD1 . ASP B 1 59  ? -51.258 -12.854 -15.674 1.00 55.77 ? 68  ASP B OD1 1 
ATOM   3540 O  OD2 . ASP B 1 59  ? -53.118 -11.927 -14.992 1.00 59.48 ? 68  ASP B OD2 1 
ATOM   3541 N  N   . HIS B 1 60  ? -53.435 -17.578 -15.988 1.00 45.49 ? 69  HIS B N   1 
ATOM   3542 C  CA  . HIS B 1 60  ? -53.958 -18.913 -15.649 1.00 46.35 ? 69  HIS B CA  1 
ATOM   3543 C  C   . HIS B 1 60  ? -52.939 -20.044 -15.873 1.00 44.15 ? 69  HIS B C   1 
ATOM   3544 O  O   . HIS B 1 60  ? -53.283 -21.217 -15.721 1.00 44.65 ? 69  HIS B O   1 
ATOM   3545 C  CB  . HIS B 1 60  ? -55.251 -19.174 -16.426 1.00 48.41 ? 69  HIS B CB  1 
ATOM   3546 C  CG  . HIS B 1 60  ? -56.228 -18.045 -16.332 1.00 50.02 ? 69  HIS B CG  1 
ATOM   3547 N  ND1 . HIS B 1 60  ? -56.939 -17.773 -15.185 1.00 56.87 ? 69  HIS B ND1 1 
ATOM   3548 C  CD2 . HIS B 1 60  ? -56.564 -17.080 -17.221 1.00 52.88 ? 69  HIS B CD2 1 
ATOM   3549 C  CE1 . HIS B 1 60  ? -57.699 -16.710 -15.382 1.00 59.55 ? 69  HIS B CE1 1 
ATOM   3550 N  NE2 . HIS B 1 60  ? -57.487 -16.268 -16.609 1.00 59.45 ? 69  HIS B NE2 1 
ATOM   3551 N  N   . LEU B 1 61  ? -51.701 -19.690 -16.230 1.00 39.99 ? 70  LEU B N   1 
ATOM   3552 C  CA  . LEU B 1 61  ? -50.572 -20.629 -16.243 1.00 39.29 ? 70  LEU B CA  1 
ATOM   3553 C  C   . LEU B 1 61  ? -49.846 -20.487 -14.905 1.00 41.64 ? 70  LEU B C   1 
ATOM   3554 O  O   . LEU B 1 61  ? -48.949 -19.648 -14.753 1.00 41.66 ? 70  LEU B O   1 
ATOM   3555 C  CB  . LEU B 1 61  ? -49.632 -20.330 -17.411 1.00 35.84 ? 70  LEU B CB  1 
ATOM   3556 C  CG  . LEU B 1 61  ? -50.253 -20.422 -18.799 1.00 36.16 ? 70  LEU B CG  1 
ATOM   3557 C  CD1 . LEU B 1 61  ? -49.363 -19.734 -19.839 1.00 36.38 ? 70  LEU B CD1 1 
ATOM   3558 C  CD2 . LEU B 1 61  ? -50.524 -21.879 -19.172 1.00 31.72 ? 70  LEU B CD2 1 
ATOM   3559 N  N   . THR B 1 62  ? -50.234 -21.333 -13.951 1.00 43.21 ? 71  THR B N   1 
ATOM   3560 C  CA  . THR B 1 62  ? -49.986 -21.106 -12.521 1.00 46.80 ? 71  THR B CA  1 
ATOM   3561 C  C   . THR B 1 62  ? -48.730 -21.769 -11.957 1.00 46.71 ? 71  THR B C   1 
ATOM   3562 O  O   . THR B 1 62  ? -48.388 -21.528 -10.791 1.00 49.05 ? 71  THR B O   1 
ATOM   3563 C  CB  . THR B 1 62  ? -51.189 -21.599 -11.674 1.00 49.39 ? 71  THR B CB  1 
ATOM   3564 O  OG1 . THR B 1 62  ? -51.304 -23.024 -11.784 1.00 51.22 ? 71  THR B OG1 1 
ATOM   3565 C  CG2 . THR B 1 62  ? -52.497 -20.950 -12.142 1.00 50.43 ? 71  THR B CG2 1 
ATOM   3566 N  N   . ASP B 1 63  ? -48.071 -22.616 -12.753 1.00 44.00 ? 72  ASP B N   1 
ATOM   3567 C  CA  . ASP B 1 63  ? -46.821 -23.266 -12.338 1.00 43.13 ? 72  ASP B CA  1 
ATOM   3568 C  C   . ASP B 1 63  ? -45.811 -23.325 -13.475 1.00 39.91 ? 72  ASP B C   1 
ATOM   3569 O  O   . ASP B 1 63  ? -46.145 -23.058 -14.630 1.00 37.57 ? 72  ASP B O   1 
ATOM   3570 C  CB  . ASP B 1 63  ? -47.082 -24.665 -11.744 1.00 44.89 ? 72  ASP B CB  1 
ATOM   3571 C  CG  . ASP B 1 63  ? -47.806 -25.608 -12.704 1.00 45.94 ? 72  ASP B CG  1 
ATOM   3572 O  OD1 . ASP B 1 63  ? -47.568 -25.566 -13.927 1.00 42.94 ? 72  ASP B OD1 1 
ATOM   3573 O  OD2 . ASP B 1 63  ? -48.610 -26.423 -12.216 1.00 52.25 ? 72  ASP B OD2 1 
ATOM   3574 N  N   . HIS B 1 64  ? -44.577 -23.680 -13.126 1.00 38.33 ? 73  HIS B N   1 
ATOM   3575 C  CA  . HIS B 1 64  ? -43.467 -23.702 -14.077 1.00 35.65 ? 73  HIS B CA  1 
ATOM   3576 C  C   . HIS B 1 64  ? -43.696 -24.627 -15.273 1.00 32.60 ? 73  HIS B C   1 
ATOM   3577 O  O   . HIS B 1 64  ? -43.386 -24.257 -16.409 1.00 31.22 ? 73  HIS B O   1 
ATOM   3578 C  CB  . HIS B 1 64  ? -42.169 -24.091 -13.357 1.00 37.36 ? 73  HIS B CB  1 
ATOM   3579 C  CG  . HIS B 1 64  ? -40.966 -24.059 -14.240 1.00 34.63 ? 73  HIS B CG  1 
ATOM   3580 N  ND1 . HIS B 1 64  ? -40.352 -22.883 -14.617 1.00 39.08 ? 73  HIS B ND1 1 
ATOM   3581 C  CD2 . HIS B 1 64  ? -40.277 -25.055 -14.840 1.00 36.37 ? 73  HIS B CD2 1 
ATOM   3582 C  CE1 . HIS B 1 64  ? -39.331 -23.160 -15.408 1.00 40.01 ? 73  HIS B CE1 1 
ATOM   3583 N  NE2 . HIS B 1 64  ? -39.265 -24.470 -15.560 1.00 35.62 ? 73  HIS B NE2 1 
ATOM   3584 N  N   . LYS B 1 65  ? -44.241 -25.816 -15.027 1.00 32.21 ? 74  LYS B N   1 
ATOM   3585 C  CA  . LYS B 1 65  ? -44.498 -26.779 -16.115 1.00 32.80 ? 74  LYS B CA  1 
ATOM   3586 C  C   . LYS B 1 65  ? -45.591 -26.319 -17.082 1.00 30.62 ? 74  LYS B C   1 
ATOM   3587 O  O   . LYS B 1 65  ? -45.454 -26.513 -18.289 1.00 28.17 ? 74  LYS B O   1 
ATOM   3588 C  CB  . LYS B 1 65  ? -44.818 -28.175 -15.564 1.00 33.77 ? 74  LYS B CB  1 
ATOM   3589 C  CG  . LYS B 1 65  ? -43.606 -28.864 -14.943 1.00 36.61 ? 74  LYS B CG  1 
ATOM   3590 C  CD  . LYS B 1 65  ? -43.839 -30.354 -14.769 1.00 37.93 ? 74  LYS B CD  1 
ATOM   3591 C  CE  . LYS B 1 65  ? -42.709 -30.988 -13.980 1.00 38.72 ? 74  LYS B CE  1 
ATOM   3592 N  NZ  . LYS B 1 65  ? -42.908 -32.452 -13.854 1.00 38.35 ? 74  LYS B NZ  1 
ATOM   3593 N  N   . SER B 1 66  ? -46.663 -25.711 -16.569 1.00 32.57 ? 75  SER B N   1 
ATOM   3594 C  CA  . SER B 1 66  ? -47.706 -25.159 -17.451 1.00 34.80 ? 75  SER B CA  1 
ATOM   3595 C  C   . SER B 1 66  ? -47.146 -24.016 -18.305 1.00 32.77 ? 75  SER B C   1 
ATOM   3596 O  O   . SER B 1 66  ? -47.465 -23.917 -19.492 1.00 33.19 ? 75  SER B O   1 
ATOM   3597 C  CB  . SER B 1 66  ? -48.952 -24.710 -16.669 1.00 36.48 ? 75  SER B CB  1 
ATOM   3598 O  OG  . SER B 1 66  ? -48.629 -23.756 -15.670 1.00 47.94 ? 75  SER B OG  1 
ATOM   3599 N  N   . GLN B 1 67  ? -46.292 -23.187 -17.702 1.00 32.86 ? 76  GLN B N   1 
ATOM   3600 C  CA  . GLN B 1 67  ? -45.601 -22.098 -18.411 1.00 32.18 ? 76  GLN B CA  1 
ATOM   3601 C  C   . GLN B 1 67  ? -44.597 -22.594 -19.464 1.00 29.01 ? 76  GLN B C   1 
ATOM   3602 O  O   . GLN B 1 67  ? -44.503 -22.025 -20.553 1.00 28.36 ? 76  GLN B O   1 
ATOM   3603 C  CB  . GLN B 1 67  ? -44.891 -21.172 -17.404 1.00 35.03 ? 76  GLN B CB  1 
ATOM   3604 C  CG  . GLN B 1 67  ? -45.843 -20.340 -16.527 1.00 34.36 ? 76  GLN B CG  1 
ATOM   3605 C  CD  . GLN B 1 67  ? -45.164 -19.705 -15.315 1.00 38.85 ? 76  GLN B CD  1 
ATOM   3606 O  OE1 . GLN B 1 67  ? -43.958 -19.837 -15.104 1.00 41.27 ? 76  GLN B OE1 1 
ATOM   3607 N  NE2 . GLN B 1 67  ? -45.950 -19.015 -14.509 1.00 42.86 ? 76  GLN B NE2 1 
ATOM   3608 N  N   . ARG B 1 68  ? -43.853 -23.649 -19.138 1.00 28.58 ? 77  ARG B N   1 
ATOM   3609 C  CA  . ARG B 1 68  ? -42.894 -24.243 -20.077 1.00 27.29 ? 77  ARG B CA  1 
ATOM   3610 C  C   . ARG B 1 68  ? -43.611 -24.913 -21.254 1.00 26.93 ? 77  ARG B C   1 
ATOM   3611 O  O   . ARG B 1 68  ? -43.129 -24.839 -22.382 1.00 23.69 ? 77  ARG B O   1 
ATOM   3612 C  CB  . ARG B 1 68  ? -41.965 -25.234 -19.366 1.00 28.25 ? 77  ARG B CB  1 
ATOM   3613 C  CG  . ARG B 1 68  ? -40.968 -24.585 -18.408 1.00 27.43 ? 77  ARG B CG  1 
ATOM   3614 C  CD  . ARG B 1 68  ? -39.829 -23.892 -19.124 1.00 28.24 ? 77  ARG B CD  1 
ATOM   3615 N  NE  . ARG B 1 68  ? -39.027 -24.851 -19.879 1.00 28.47 ? 77  ARG B NE  1 
ATOM   3616 C  CZ  . ARG B 1 68  ? -38.046 -25.596 -19.374 1.00 27.59 ? 77  ARG B CZ  1 
ATOM   3617 N  NH1 . ARG B 1 68  ? -37.682 -25.506 -18.100 1.00 26.02 ? 77  ARG B NH1 1 
ATOM   3618 N  NH2 . ARG B 1 68  ? -37.411 -26.438 -20.170 1.00 29.11 ? 77  ARG B NH2 1 
ATOM   3619 N  N   . LEU B 1 69  ? -44.759 -25.543 -20.983 1.00 26.63 ? 78  LEU B N   1 
ATOM   3620 C  CA  . LEU B 1 69  ? -45.606 -26.100 -22.036 1.00 26.83 ? 78  LEU B CA  1 
ATOM   3621 C  C   . LEU B 1 69  ? -46.168 -25.011 -22.959 1.00 26.36 ? 78  LEU B C   1 
ATOM   3622 O  O   . LEU B 1 69  ? -46.177 -25.173 -24.183 1.00 25.46 ? 78  LEU B O   1 
ATOM   3623 C  CB  . LEU B 1 69  ? -46.760 -26.942 -21.448 1.00 27.13 ? 78  LEU B CB  1 
ATOM   3624 C  CG  . LEU B 1 69  ? -47.744 -27.545 -22.464 1.00 27.82 ? 78  LEU B CG  1 
ATOM   3625 C  CD1 . LEU B 1 69  ? -47.039 -28.384 -23.546 1.00 27.95 ? 78  LEU B CD1 1 
ATOM   3626 C  CD2 . LEU B 1 69  ? -48.803 -28.358 -21.782 1.00 27.43 ? 78  LEU B CD2 1 
ATOM   3627 N  N   . ALA B 1 70  ? -46.653 -23.925 -22.364 1.00 26.78 ? 79  ALA B N   1 
ATOM   3628 C  CA  . ALA B 1 70  ? -47.184 -22.788 -23.124 1.00 27.25 ? 79  ALA B CA  1 
ATOM   3629 C  C   . ALA B 1 70  ? -46.101 -22.175 -24.005 1.00 27.04 ? 79  ALA B C   1 
ATOM   3630 O  O   . ALA B 1 70  ? -46.353 -21.842 -25.163 1.00 26.55 ? 79  ALA B O   1 
ATOM   3631 C  CB  . ALA B 1 70  ? -47.775 -21.736 -22.184 1.00 27.27 ? 79  ALA B CB  1 
ATOM   3632 N  N   . ARG B 1 71  ? -44.893 -22.058 -23.457 1.00 28.17 ? 80  ARG B N   1 
ATOM   3633 C  CA  . ARG B 1 71  ? -43.728 -21.609 -24.234 1.00 27.56 ? 80  ARG B CA  1 
ATOM   3634 C  C   . ARG B 1 71  ? -43.451 -22.478 -25.440 1.00 25.68 ? 80  ARG B C   1 
ATOM   3635 O  O   . ARG B 1 71  ? -43.237 -21.962 -26.536 1.00 25.87 ? 80  ARG B O   1 
ATOM   3636 C  CB  . ARG B 1 71  ? -42.460 -21.511 -23.365 1.00 29.02 ? 80  ARG B CB  1 
ATOM   3637 C  CG  . ARG B 1 71  ? -42.069 -20.082 -23.034 1.00 29.50 ? 80  ARG B CG  1 
ATOM   3638 C  CD  . ARG B 1 71  ? -40.633 -20.015 -22.557 1.00 29.84 ? 80  ARG B CD  1 
ATOM   3639 N  NE  . ARG B 1 71  ? -39.654 -20.211 -23.631 1.00 25.77 ? 80  ARG B NE  1 
ATOM   3640 C  CZ  . ARG B 1 71  ? -39.186 -19.259 -24.443 1.00 25.44 ? 80  ARG B CZ  1 
ATOM   3641 N  NH1 . ARG B 1 71  ? -39.591 -17.999 -24.348 1.00 25.61 ? 80  ARG B NH1 1 
ATOM   3642 N  NH2 . ARG B 1 71  ? -38.292 -19.577 -25.370 1.00 23.59 ? 80  ARG B NH2 1 
ATOM   3643 N  N   . LEU B 1 72  ? -43.447 -23.792 -25.229 1.00 25.98 ? 81  LEU B N   1 
ATOM   3644 C  CA  . LEU B 1 72  ? -43.282 -24.757 -26.309 1.00 24.47 ? 81  LEU B CA  1 
ATOM   3645 C  C   . LEU B 1 72  ? -44.399 -24.624 -27.373 1.00 23.67 ? 81  LEU B C   1 
ATOM   3646 O  O   . LEU B 1 72  ? -44.120 -24.569 -28.570 1.00 26.20 ? 81  LEU B O   1 
ATOM   3647 C  CB  . LEU B 1 72  ? -43.226 -26.186 -25.734 1.00 25.07 ? 81  LEU B CB  1 
ATOM   3648 C  CG  . LEU B 1 72  ? -43.207 -27.374 -26.700 1.00 24.15 ? 81  LEU B CG  1 
ATOM   3649 C  CD1 . LEU B 1 72  ? -42.075 -27.272 -27.693 1.00 28.15 ? 81  LEU B CD1 1 
ATOM   3650 C  CD2 . LEU B 1 72  ? -43.118 -28.666 -25.921 1.00 25.78 ? 81  LEU B CD2 1 
ATOM   3651 N  N   . VAL B 1 73  ? -45.644 -24.558 -26.917 1.00 24.91 ? 82  VAL B N   1 
ATOM   3652 C  CA  . VAL B 1 73  ? -46.825 -24.377 -27.787 1.00 25.05 ? 82  VAL B CA  1 
ATOM   3653 C  C   . VAL B 1 73  ? -46.725 -23.100 -28.624 1.00 25.23 ? 82  VAL B C   1 
ATOM   3654 O  O   . VAL B 1 73  ? -46.834 -23.147 -29.854 1.00 24.03 ? 82  VAL B O   1 
ATOM   3655 C  CB  . VAL B 1 73  ? -48.138 -24.357 -26.933 1.00 26.59 ? 82  VAL B CB  1 
ATOM   3656 C  CG1 . VAL B 1 73  ? -49.332 -23.727 -27.684 1.00 29.40 ? 82  VAL B CG1 1 
ATOM   3657 C  CG2 . VAL B 1 73  ? -48.507 -25.776 -26.475 1.00 26.68 ? 82  VAL B CG2 1 
ATOM   3658 N  N   . LEU B 1 74  ? -46.529 -21.971 -27.943 1.00 25.77 ? 83  LEU B N   1 
ATOM   3659 C  CA  . LEU B 1 74  ? -46.455 -20.647 -28.596 1.00 26.68 ? 83  LEU B CA  1 
ATOM   3660 C  C   . LEU B 1 74  ? -45.230 -20.508 -29.484 1.00 25.46 ? 83  LEU B C   1 
ATOM   3661 O  O   . LEU B 1 74  ? -45.297 -19.901 -30.560 1.00 27.34 ? 83  LEU B O   1 
ATOM   3662 C  CB  . LEU B 1 74  ? -46.483 -19.519 -27.552 1.00 26.52 ? 83  LEU B CB  1 
ATOM   3663 C  CG  . LEU B 1 74  ? -47.770 -19.358 -26.729 1.00 27.35 ? 83  LEU B CG  1 
ATOM   3664 C  CD1 . LEU B 1 74  ? -47.618 -18.274 -25.690 1.00 28.57 ? 83  LEU B CD1 1 
ATOM   3665 C  CD2 . LEU B 1 74  ? -48.969 -19.050 -27.607 1.00 26.85 ? 83  LEU B CD2 1 
ATOM   3666 N  N   . GLY B 1 75  ? -44.117 -21.082 -29.031 1.00 25.45 ? 84  GLY B N   1 
ATOM   3667 C  CA  . GLY B 1 75  ? -42.889 -21.161 -29.817 1.00 24.59 ? 84  GLY B CA  1 
ATOM   3668 C  C   . GLY B 1 75  ? -43.057 -21.907 -31.125 1.00 23.84 ? 84  GLY B C   1 
ATOM   3669 O  O   . GLY B 1 75  ? -42.656 -21.416 -32.164 1.00 25.64 ? 84  GLY B O   1 
ATOM   3670 N  N   . CYS B 1 76  ? -43.659 -23.090 -31.075 1.00 24.89 ? 85  CYS B N   1 
ATOM   3671 C  CA  . CYS B 1 76  ? -43.910 -23.874 -32.287 1.00 24.88 ? 85  CYS B CA  1 
ATOM   3672 C  C   . CYS B 1 76  ? -44.886 -23.167 -33.224 1.00 24.18 ? 85  CYS B C   1 
ATOM   3673 O  O   . CYS B 1 76  ? -44.662 -23.142 -34.430 1.00 25.97 ? 85  CYS B O   1 
ATOM   3674 C  CB  . CYS B 1 76  ? -44.431 -25.273 -31.938 1.00 26.09 ? 85  CYS B CB  1 
ATOM   3675 S  SG  . CYS B 1 76  ? -43.171 -26.307 -31.173 1.00 25.65 ? 85  CYS B SG  1 
ATOM   3676 N  N   . ILE B 1 77  ? -45.949 -22.586 -32.665 1.00 24.11 ? 86  ILE B N   1 
ATOM   3677 C  CA  . ILE B 1 77  ? -46.925 -21.813 -33.449 1.00 24.60 ? 86  ILE B CA  1 
ATOM   3678 C  C   . ILE B 1 77  ? -46.240 -20.627 -34.142 1.00 23.98 ? 86  ILE B C   1 
ATOM   3679 O  O   . ILE B 1 77  ? -46.530 -20.335 -35.290 1.00 26.15 ? 86  ILE B O   1 
ATOM   3680 C  CB  . ILE B 1 77  ? -48.120 -21.320 -32.586 1.00 24.38 ? 86  ILE B CB  1 
ATOM   3681 C  CG1 . ILE B 1 77  ? -49.005 -22.501 -32.164 1.00 27.48 ? 86  ILE B CG1 1 
ATOM   3682 C  CG2 . ILE B 1 77  ? -48.985 -20.310 -33.360 1.00 28.29 ? 86  ILE B CG2 1 
ATOM   3683 C  CD1 . ILE B 1 77  ? -50.053 -22.149 -31.057 1.00 28.53 ? 86  ILE B CD1 1 
ATOM   3684 N  N   . THR B 1 78  ? -45.333 -19.963 -33.431 1.00 23.11 ? 87  THR B N   1 
ATOM   3685 C  CA  . THR B 1 78  ? -44.596 -18.816 -33.966 1.00 23.27 ? 87  THR B CA  1 
ATOM   3686 C  C   . THR B 1 78  ? -43.695 -19.202 -35.152 1.00 24.31 ? 87  THR B C   1 
ATOM   3687 O  O   . THR B 1 78  ? -43.659 -18.479 -36.164 1.00 24.93 ? 87  THR B O   1 
ATOM   3688 C  CB  . THR B 1 78  ? -43.822 -18.104 -32.834 1.00 23.76 ? 87  THR B CB  1 
ATOM   3689 O  OG1 . THR B 1 78  ? -44.768 -17.583 -31.892 1.00 22.39 ? 87  THR B OG1 1 
ATOM   3690 C  CG2 . THR B 1 78  ? -42.976 -16.957 -33.345 1.00 27.56 ? 87  THR B CG2 1 
ATOM   3691 N  N   A MET B 1 79  ? -42.989 -20.329 -35.038 0.50 22.71 ? 88  MET B N   1 
ATOM   3692 N  N   B MET B 1 79  ? -42.982 -20.321 -35.037 0.50 22.32 ? 88  MET B N   1 
ATOM   3693 C  CA  A MET B 1 79  ? -42.143 -20.813 -36.133 0.50 24.28 ? 88  MET B CA  1 
ATOM   3694 C  CA  B MET B 1 79  ? -42.153 -20.806 -36.142 0.50 23.69 ? 88  MET B CA  1 
ATOM   3695 C  C   A MET B 1 79  ? -43.005 -21.130 -37.357 0.50 25.32 ? 88  MET B C   1 
ATOM   3696 C  C   B MET B 1 79  ? -43.008 -21.132 -37.362 0.50 24.92 ? 88  MET B C   1 
ATOM   3697 O  O   A MET B 1 79  ? -42.667 -20.737 -38.468 0.50 26.94 ? 88  MET B O   1 
ATOM   3698 O  O   B MET B 1 79  ? -42.669 -20.748 -38.476 0.50 26.60 ? 88  MET B O   1 
ATOM   3699 C  CB  A MET B 1 79  ? -41.334 -22.055 -35.729 0.50 24.64 ? 88  MET B CB  1 
ATOM   3700 C  CB  B MET B 1 79  ? -41.330 -22.028 -35.723 0.50 23.28 ? 88  MET B CB  1 
ATOM   3701 C  CG  A MET B 1 79  ? -40.338 -21.888 -34.561 0.50 23.18 ? 88  MET B CG  1 
ATOM   3702 C  CG  B MET B 1 79  ? -40.227 -21.715 -34.723 0.50 20.37 ? 88  MET B CG  1 
ATOM   3703 S  SD  A MET B 1 79  ? -39.448 -20.318 -34.416 0.50 28.96 ? 88  MET B SD  1 
ATOM   3704 S  SD  B MET B 1 79  ? -39.031 -20.503 -35.326 0.50 24.82 ? 88  MET B SD  1 
ATOM   3705 C  CE  A MET B 1 79  ? -40.381 -19.539 -33.104 0.50 27.99 ? 88  MET B CE  1 
ATOM   3706 C  CE  B MET B 1 79  ? -37.621 -20.930 -34.310 0.50 19.60 ? 88  MET B CE  1 
ATOM   3707 N  N   . ALA B 1 80  ? -44.132 -21.803 -37.134 1.00 25.70 ? 89  ALA B N   1 
ATOM   3708 C  CA  . ALA B 1 80  ? -45.087 -22.122 -38.201 1.00 26.35 ? 89  ALA B CA  1 
ATOM   3709 C  C   . ALA B 1 80  ? -45.670 -20.873 -38.860 1.00 27.33 ? 89  ALA B C   1 
ATOM   3710 O  O   . ALA B 1 80  ? -45.800 -20.818 -40.082 1.00 31.68 ? 89  ALA B O   1 
ATOM   3711 C  CB  . ALA B 1 80  ? -46.212 -22.984 -37.646 1.00 27.29 ? 89  ALA B CB  1 
ATOM   3712 N  N   . TYR B 1 81  ? -45.994 -19.876 -38.044 1.00 26.10 ? 90  TYR B N   1 
ATOM   3713 C  CA  . TYR B 1 81  ? -46.582 -18.631 -38.532 1.00 27.06 ? 90  TYR B CA  1 
ATOM   3714 C  C   . TYR B 1 81  ? -45.582 -17.830 -39.365 1.00 27.79 ? 90  TYR B C   1 
ATOM   3715 O  O   . TYR B 1 81  ? -45.918 -17.324 -40.435 1.00 28.54 ? 90  TYR B O   1 
ATOM   3716 C  CB  . TYR B 1 81  ? -47.082 -17.769 -37.364 1.00 25.99 ? 90  TYR B CB  1 
ATOM   3717 C  CG  . TYR B 1 81  ? -47.879 -16.587 -37.858 1.00 28.54 ? 90  TYR B CG  1 
ATOM   3718 C  CD1 . TYR B 1 81  ? -49.241 -16.703 -38.119 1.00 27.25 ? 90  TYR B CD1 1 
ATOM   3719 C  CD2 . TYR B 1 81  ? -47.265 -15.372 -38.120 1.00 26.41 ? 90  TYR B CD2 1 
ATOM   3720 C  CE1 . TYR B 1 81  ? -49.966 -15.637 -38.603 1.00 26.41 ? 90  TYR B CE1 1 
ATOM   3721 C  CE2 . TYR B 1 81  ? -47.988 -14.300 -38.616 1.00 29.22 ? 90  TYR B CE2 1 
ATOM   3722 C  CZ  . TYR B 1 81  ? -49.340 -14.439 -38.849 1.00 29.08 ? 90  TYR B CZ  1 
ATOM   3723 O  OH  . TYR B 1 81  ? -50.067 -13.382 -39.336 1.00 32.34 ? 90  TYR B OH  1 
ATOM   3724 N  N   . VAL B 1 82  ? -44.370 -17.686 -38.842 1.00 26.53 ? 91  VAL B N   1 
ATOM   3725 C  CA  . VAL B 1 82  ? -43.314 -16.955 -39.532 1.00 27.27 ? 91  VAL B CA  1 
ATOM   3726 C  C   . VAL B 1 82  ? -42.931 -17.687 -40.818 1.00 26.60 ? 91  VAL B C   1 
ATOM   3727 O  O   . VAL B 1 82  ? -42.929 -17.101 -41.882 1.00 29.09 ? 91  VAL B O   1 
ATOM   3728 C  CB  . VAL B 1 82  ? -42.082 -16.733 -38.602 1.00 26.07 ? 91  VAL B CB  1 
ATOM   3729 C  CG1 . VAL B 1 82  ? -40.877 -16.181 -39.367 1.00 30.17 ? 91  VAL B CG1 1 
ATOM   3730 C  CG2 . VAL B 1 82  ? -42.463 -15.786 -37.455 1.00 28.34 ? 91  VAL B CG2 1 
ATOM   3731 N  N   . TRP B 1 83  ? -42.626 -18.971 -40.722 1.00 28.40 ? 92  TRP B N   1 
ATOM   3732 C  CA  . TRP B 1 83  ? -42.117 -19.706 -41.889 1.00 29.85 ? 92  TRP B CA  1 
ATOM   3733 C  C   . TRP B 1 83  ? -43.179 -20.234 -42.847 1.00 30.85 ? 92  TRP B C   1 
ATOM   3734 O  O   . TRP B 1 83  ? -42.865 -20.496 -44.007 1.00 31.92 ? 92  TRP B O   1 
ATOM   3735 C  CB  . TRP B 1 83  ? -41.170 -20.824 -41.451 1.00 28.73 ? 92  TRP B CB  1 
ATOM   3736 C  CG  . TRP B 1 83  ? -40.043 -20.315 -40.631 1.00 29.02 ? 92  TRP B CG  1 
ATOM   3737 C  CD1 . TRP B 1 83  ? -39.713 -20.723 -39.386 1.00 28.14 ? 92  TRP B CD1 1 
ATOM   3738 C  CD2 . TRP B 1 83  ? -39.110 -19.269 -40.973 1.00 28.58 ? 92  TRP B CD2 1 
ATOM   3739 N  NE1 . TRP B 1 83  ? -38.635 -20.025 -38.928 1.00 30.29 ? 92  TRP B NE1 1 
ATOM   3740 C  CE2 . TRP B 1 83  ? -38.243 -19.120 -39.876 1.00 30.65 ? 92  TRP B CE2 1 
ATOM   3741 C  CE3 . TRP B 1 83  ? -38.929 -18.445 -42.096 1.00 31.75 ? 92  TRP B CE3 1 
ATOM   3742 C  CZ2 . TRP B 1 83  ? -37.201 -18.183 -39.859 1.00 34.05 ? 92  TRP B CZ2 1 
ATOM   3743 C  CZ3 . TRP B 1 83  ? -37.890 -17.513 -42.082 1.00 35.96 ? 92  TRP B CZ3 1 
ATOM   3744 C  CH2 . TRP B 1 83  ? -37.036 -17.398 -40.966 1.00 34.67 ? 92  TRP B CH2 1 
ATOM   3745 N  N   . GLY B 1 84  ? -44.415 -20.401 -42.377 1.00 32.62 ? 93  GLY B N   1 
ATOM   3746 C  CA  . GLY B 1 84  ? -45.496 -20.932 -43.216 1.00 35.30 ? 93  GLY B CA  1 
ATOM   3747 C  C   . GLY B 1 84  ? -45.215 -22.358 -43.673 1.00 36.13 ? 93  GLY B C   1 
ATOM   3748 O  O   . GLY B 1 84  ? -44.857 -23.211 -42.859 1.00 35.79 ? 93  GLY B O   1 
ATOM   3749 N  N   . LYS B 1 85  ? -45.351 -22.603 -44.978 1.00 39.40 ? 94  LYS B N   1 
ATOM   3750 C  CA  . LYS B 1 85  ? -45.016 -23.906 -45.583 1.00 42.37 ? 94  LYS B CA  1 
ATOM   3751 C  C   . LYS B 1 85  ? -43.500 -24.109 -45.817 1.00 44.09 ? 94  LYS B C   1 
ATOM   3752 O  O   . LYS B 1 85  ? -43.084 -25.171 -46.282 1.00 45.25 ? 94  LYS B O   1 
ATOM   3753 C  CB  . LYS B 1 85  ? -45.786 -24.108 -46.898 1.00 43.65 ? 94  LYS B CB  1 
ATOM   3754 C  CG  . LYS B 1 85  ? -47.281 -24.356 -46.724 1.00 43.78 ? 94  LYS B CG  1 
ATOM   3755 C  CD  . LYS B 1 85  ? -47.957 -24.733 -48.049 1.00 47.82 ? 94  LYS B CD  1 
ATOM   3756 C  CE  . LYS B 1 85  ? -49.441 -25.042 -47.854 1.00 48.82 ? 94  LYS B CE  1 
ATOM   3757 N  NZ  . LYS B 1 85  ? -50.189 -25.239 -49.134 1.00 51.72 ? 94  LYS B NZ  1 
ATOM   3758 N  N   . GLY B 1 86  ? -42.681 -23.105 -45.503 1.00 45.02 ? 95  GLY B N   1 
ATOM   3759 C  CA  . GLY B 1 86  ? -41.232 -23.216 -45.657 1.00 48.35 ? 95  GLY B CA  1 
ATOM   3760 C  C   . GLY B 1 86  ? -40.765 -23.209 -47.099 1.00 53.47 ? 95  GLY B C   1 
ATOM   3761 O  O   . GLY B 1 86  ? -39.848 -23.956 -47.449 1.00 54.93 ? 95  GLY B O   1 
ATOM   3762 N  N   . HIS B 1 87  ? -41.409 -22.377 -47.925 1.00 57.15 ? 96  HIS B N   1 
ATOM   3763 C  CA  . HIS B 1 87  ? -41.045 -22.189 -49.336 1.00 61.94 ? 96  HIS B CA  1 
ATOM   3764 C  C   . HIS B 1 87  ? -40.574 -20.756 -49.631 1.00 63.78 ? 96  HIS B C   1 
ATOM   3765 O  O   . HIS B 1 87  ? -40.382 -20.406 -50.798 1.00 67.74 ? 96  HIS B O   1 
ATOM   3766 C  CB  . HIS B 1 87  ? -42.241 -22.514 -50.252 1.00 65.82 ? 96  HIS B CB  1 
ATOM   3767 C  CG  . HIS B 1 87  ? -42.842 -23.868 -50.022 1.00 70.32 ? 96  HIS B CG  1 
ATOM   3768 N  ND1 . HIS B 1 87  ? -42.085 -25.018 -49.940 1.00 74.73 ? 96  HIS B ND1 1 
ATOM   3769 C  CD2 . HIS B 1 87  ? -44.132 -24.256 -49.876 1.00 71.63 ? 96  HIS B CD2 1 
ATOM   3770 C  CE1 . HIS B 1 87  ? -42.881 -26.054 -49.737 1.00 74.77 ? 96  HIS B CE1 1 
ATOM   3771 N  NE2 . HIS B 1 87  ? -44.128 -25.619 -49.696 1.00 73.49 ? 96  HIS B NE2 1 
ATOM   3772 N  N   . GLY B 1 88  ? -40.386 -19.938 -48.590 1.00 62.21 ? 97  GLY B N   1 
ATOM   3773 C  CA  . GLY B 1 88  ? -40.021 -18.520 -48.747 1.00 63.32 ? 97  GLY B CA  1 
ATOM   3774 C  C   . GLY B 1 88  ? -41.147 -17.507 -48.556 1.00 63.25 ? 97  GLY B C   1 
ATOM   3775 O  O   . GLY B 1 88  ? -40.881 -16.306 -48.507 1.00 65.02 ? 97  GLY B O   1 
ATOM   3776 N  N   . ASP B 1 89  ? -42.397 -17.968 -48.471 1.00 61.14 ? 98  ASP B N   1 
ATOM   3777 C  CA  . ASP B 1 89  ? -43.521 -17.100 -48.096 1.00 58.99 ? 98  ASP B CA  1 
ATOM   3778 C  C   . ASP B 1 89  ? -43.419 -16.909 -46.584 1.00 54.96 ? 98  ASP B C   1 
ATOM   3779 O  O   . ASP B 1 89  ? -43.585 -17.871 -45.828 1.00 54.41 ? 98  ASP B O   1 
ATOM   3780 C  CB  . ASP B 1 89  ? -44.871 -17.726 -48.497 1.00 59.53 ? 98  ASP B CB  1 
ATOM   3781 C  CG  . ASP B 1 89  ? -46.000 -16.695 -48.607 1.00 61.59 ? 98  ASP B CG  1 
ATOM   3782 O  OD1 . ASP B 1 89  ? -46.140 -15.834 -47.715 1.00 57.27 ? 98  ASP B OD1 1 
ATOM   3783 O  OD2 . ASP B 1 89  ? -46.763 -16.755 -49.594 1.00 70.32 ? 98  ASP B OD2 1 
ATOM   3784 N  N   . VAL B 1 90  ? -43.140 -15.675 -46.165 1.00 52.32 ? 99  VAL B N   1 
ATOM   3785 C  CA  . VAL B 1 90  ? -42.670 -15.361 -44.808 1.00 49.47 ? 99  VAL B CA  1 
ATOM   3786 C  C   . VAL B 1 90  ? -43.511 -14.240 -44.180 1.00 46.75 ? 99  VAL B C   1 
ATOM   3787 O  O   . VAL B 1 90  ? -43.934 -13.323 -44.878 1.00 49.84 ? 99  VAL B O   1 
ATOM   3788 C  CB  . VAL B 1 90  ? -41.145 -14.974 -44.863 1.00 51.89 ? 99  VAL B CB  1 
ATOM   3789 C  CG1 . VAL B 1 90  ? -40.684 -14.122 -43.664 1.00 52.24 ? 99  VAL B CG1 1 
ATOM   3790 C  CG2 . VAL B 1 90  ? -40.285 -16.235 -44.984 1.00 52.00 ? 99  VAL B CG2 1 
ATOM   3791 N  N   . ARG B 1 91  ? -43.743 -14.320 -42.868 1.00 42.99 ? 100 ARG B N   1 
ATOM   3792 C  CA  . ARG B 1 91  ? -44.408 -13.243 -42.115 1.00 42.13 ? 100 ARG B CA  1 
ATOM   3793 C  C   . ARG B 1 91  ? -43.417 -12.528 -41.202 1.00 40.64 ? 100 ARG B C   1 
ATOM   3794 O  O   . ARG B 1 91  ? -42.769 -13.166 -40.366 1.00 35.25 ? 100 ARG B O   1 
ATOM   3795 C  CB  . ARG B 1 91  ? -45.574 -13.787 -41.285 1.00 41.39 ? 100 ARG B CB  1 
ATOM   3796 C  CG  . ARG B 1 91  ? -46.736 -14.329 -42.112 1.00 40.17 ? 100 ARG B CG  1 
ATOM   3797 C  CD  . ARG B 1 91  ? -47.562 -13.236 -42.783 1.00 47.99 ? 100 ARG B CD  1 
ATOM   3798 N  NE  . ARG B 1 91  ? -48.244 -13.755 -43.977 1.00 48.87 ? 100 ARG B NE  1 
ATOM   3799 C  CZ  . ARG B 1 91  ? -49.544 -14.041 -44.098 1.00 52.05 ? 100 ARG B CZ  1 
ATOM   3800 N  NH1 . ARG B 1 91  ? -50.418 -13.866 -43.099 1.00 51.70 ? 100 ARG B NH1 1 
ATOM   3801 N  NH2 . ARG B 1 91  ? -49.987 -14.517 -45.261 1.00 57.38 ? 100 ARG B NH2 1 
ATOM   3802 N  N   . LYS B 1 92  ? -43.309 -11.207 -41.373 1.00 40.99 ? 101 LYS B N   1 
ATOM   3803 C  CA  . LYS B 1 92  ? -42.419 -10.359 -40.559 1.00 41.84 ? 101 LYS B CA  1 
ATOM   3804 C  C   . LYS B 1 92  ? -43.108 -9.759  -39.319 1.00 38.14 ? 101 LYS B C   1 
ATOM   3805 O  O   . LYS B 1 92  ? -42.440 -9.195  -38.461 1.00 34.65 ? 101 LYS B O   1 
ATOM   3806 C  CB  . LYS B 1 92  ? -41.816 -9.247  -41.422 1.00 46.15 ? 101 LYS B CB  1 
ATOM   3807 C  CG  . LYS B 1 92  ? -41.102 -9.767  -42.679 1.00 52.17 ? 101 LYS B CG  1 
ATOM   3808 C  CD  . LYS B 1 92  ? -40.147 -8.738  -43.275 1.00 53.50 ? 101 LYS B CD  1 
ATOM   3809 C  CE  . LYS B 1 92  ? -39.540 -9.241  -44.575 0.00 55.09 ? 101 LYS B CE  1 
ATOM   3810 N  NZ  . LYS B 1 92  ? -38.570 -8.268  -45.148 0.00 58.78 ? 101 LYS B NZ  1 
ATOM   3811 N  N   . VAL B 1 93  ? -44.432 -9.892  -39.228 1.00 37.29 ? 102 VAL B N   1 
ATOM   3812 C  CA  . VAL B 1 93  ? -45.211 -9.390  -38.087 1.00 36.24 ? 102 VAL B CA  1 
ATOM   3813 C  C   . VAL B 1 93  ? -45.930 -10.563 -37.423 1.00 34.11 ? 102 VAL B C   1 
ATOM   3814 O  O   . VAL B 1 93  ? -46.739 -11.231 -38.064 1.00 34.57 ? 102 VAL B O   1 
ATOM   3815 C  CB  . VAL B 1 93  ? -46.257 -8.324  -38.528 1.00 35.53 ? 102 VAL B CB  1 
ATOM   3816 C  CG1 . VAL B 1 93  ? -46.999 -7.742  -37.326 1.00 35.29 ? 102 VAL B CG1 1 
ATOM   3817 C  CG2 . VAL B 1 93  ? -45.587 -7.188  -39.313 1.00 39.22 ? 102 VAL B CG2 1 
ATOM   3818 N  N   . LEU B 1 94  ? -45.632 -10.803 -36.145 1.00 33.06 ? 103 LEU B N   1 
ATOM   3819 C  CA  . LEU B 1 94  ? -46.353 -11.784 -35.342 1.00 30.91 ? 103 LEU B CA  1 
ATOM   3820 C  C   . LEU B 1 94  ? -47.555 -11.065 -34.720 1.00 31.91 ? 103 LEU B C   1 
ATOM   3821 O  O   . LEU B 1 94  ? -47.357 -10.111 -33.967 1.00 30.03 ? 103 LEU B O   1 
ATOM   3822 C  CB  . LEU B 1 94  ? -45.449 -12.365 -34.255 1.00 29.67 ? 103 LEU B CB  1 
ATOM   3823 C  CG  . LEU B 1 94  ? -45.987 -13.551 -33.449 1.00 28.54 ? 103 LEU B CG  1 
ATOM   3824 C  CD1 . LEU B 1 94  ? -46.223 -14.778 -34.324 1.00 28.70 ? 103 LEU B CD1 1 
ATOM   3825 C  CD2 . LEU B 1 94  ? -45.050 -13.905 -32.291 1.00 28.42 ? 103 LEU B CD2 1 
ATOM   3826 N  N   . PRO B 1 95  ? -48.801 -11.503 -35.039 1.00 34.02 ? 104 PRO B N   1 
ATOM   3827 C  CA  . PRO B 1 95  ? -50.007 -10.834 -34.537 1.00 35.45 ? 104 PRO B CA  1 
ATOM   3828 C  C   . PRO B 1 95  ? -50.002 -10.656 -33.025 1.00 33.82 ? 104 PRO B C   1 
ATOM   3829 O  O   . PRO B 1 95  ? -49.550 -11.547 -32.307 1.00 32.12 ? 104 PRO B O   1 
ATOM   3830 C  CB  . PRO B 1 95  ? -51.134 -11.795 -34.943 1.00 37.08 ? 104 PRO B CB  1 
ATOM   3831 C  CG  . PRO B 1 95  ? -50.626 -12.522 -36.100 1.00 34.75 ? 104 PRO B CG  1 
ATOM   3832 C  CD  . PRO B 1 95  ? -49.150 -12.643 -35.910 1.00 31.01 ? 104 PRO B CD  1 
ATOM   3833 N  N   . ARG B 1 96  ? -50.509 -9.521  -32.560 1.00 35.79 ? 105 ARG B N   1 
ATOM   3834 C  CA  . ARG B 1 96  ? -50.493 -9.184  -31.125 1.00 38.38 ? 105 ARG B CA  1 
ATOM   3835 C  C   . ARG B 1 96  ? -51.184 -10.203 -30.213 1.00 38.10 ? 105 ARG B C   1 
ATOM   3836 O  O   . ARG B 1 96  ? -50.735 -10.414 -29.079 1.00 38.67 ? 105 ARG B O   1 
ATOM   3837 C  CB  . ARG B 1 96  ? -51.067 -7.776  -30.878 1.00 40.20 ? 105 ARG B CB  1 
ATOM   3838 C  CG  . ARG B 1 96  ? -52.561 -7.634  -31.177 1.00 42.56 ? 105 ARG B CG  1 
ATOM   3839 C  CD  . ARG B 1 96  ? -53.093 -6.265  -30.820 1.00 44.33 ? 105 ARG B CD  1 
ATOM   3840 N  NE  . ARG B 1 96  ? -52.445 -5.214  -31.606 1.00 45.66 ? 105 ARG B NE  1 
ATOM   3841 C  CZ  . ARG B 1 96  ? -51.660 -4.241  -31.133 1.00 54.61 ? 105 ARG B CZ  1 
ATOM   3842 N  NH1 . ARG B 1 96  ? -51.397 -4.122  -29.826 1.00 54.76 ? 105 ARG B NH1 1 
ATOM   3843 N  NH2 . ARG B 1 96  ? -51.145 -3.350  -31.986 1.00 54.36 ? 105 ARG B NH2 1 
ATOM   3844 N  N   A ASN B 1 97  ? -52.251 -10.836 -30.693 0.50 38.48 ? 106 ASN B N   1 
ATOM   3845 N  N   B ASN B 1 97  ? -52.258 -10.816 -30.728 0.50 37.71 ? 106 ASN B N   1 
ATOM   3846 C  CA  A ASN B 1 97  ? -52.996 -11.792 -29.866 0.50 38.04 ? 106 ASN B CA  1 
ATOM   3847 C  CA  B ASN B 1 97  ? -53.024 -11.846 -30.005 0.50 36.26 ? 106 ASN B CA  1 
ATOM   3848 C  C   A ASN B 1 97  ? -52.197 -13.053 -29.502 0.50 36.06 ? 106 ASN B C   1 
ATOM   3849 C  C   B ASN B 1 97  ? -52.156 -12.990 -29.484 0.50 35.21 ? 106 ASN B C   1 
ATOM   3850 O  O   A ASN B 1 97  ? -52.527 -13.714 -28.523 0.50 37.62 ? 106 ASN B O   1 
ATOM   3851 O  O   B ASN B 1 97  ? -52.376 -13.484 -28.382 0.50 36.51 ? 106 ASN B O   1 
ATOM   3852 C  CB  A ASN B 1 97  ? -54.352 -12.131 -30.505 0.50 38.51 ? 106 ASN B CB  1 
ATOM   3853 C  CB  B ASN B 1 97  ? -54.223 -12.375 -30.836 0.50 36.66 ? 106 ASN B CB  1 
ATOM   3854 C  CG  A ASN B 1 97  ? -55.336 -10.951 -30.471 0.50 40.88 ? 106 ASN B CG  1 
ATOM   3855 C  CG  B ASN B 1 97  ? -53.823 -13.002 -32.190 0.50 34.41 ? 106 ASN B CG  1 
ATOM   3856 O  OD1 A ASN B 1 97  ? -55.024 -9.864  -29.978 0.50 40.70 ? 106 ASN B OD1 1 
ATOM   3857 O  OD1 B ASN B 1 97  ? -52.663 -13.315 -32.440 0.50 35.46 ? 106 ASN B OD1 1 
ATOM   3858 N  ND2 A ASN B 1 97  ? -56.533 -11.172 -30.995 0.50 41.45 ? 106 ASN B ND2 1 
ATOM   3859 N  ND2 B ASN B 1 97  ? -54.813 -13.186 -33.065 0.50 28.64 ? 106 ASN B ND2 1 
ATOM   3860 N  N   . ILE B 1 98  ? -51.157 -13.373 -30.278 1.00 34.30 ? 107 ILE B N   1 
ATOM   3861 C  CA  . ILE B 1 98  ? -50.154 -14.373 -29.884 1.00 33.82 ? 107 ILE B CA  1 
ATOM   3862 C  C   . ILE B 1 98  ? -48.851 -13.724 -29.372 1.00 32.18 ? 107 ILE B C   1 
ATOM   3863 O  O   . ILE B 1 98  ? -48.266 -14.214 -28.405 1.00 30.72 ? 107 ILE B O   1 
ATOM   3864 C  CB  . ILE B 1 98  ? -49.863 -15.426 -31.023 1.00 35.46 ? 107 ILE B CB  1 
ATOM   3865 C  CG1 . ILE B 1 98  ? -48.912 -16.508 -30.517 1.00 38.65 ? 107 ILE B CG1 1 
ATOM   3866 C  CG2 . ILE B 1 98  ? -49.280 -14.794 -32.284 1.00 35.85 ? 107 ILE B CG2 1 
ATOM   3867 C  CD1 . ILE B 1 98  ? -49.113 -17.829 -31.195 1.00 37.45 ? 107 ILE B CD1 1 
ATOM   3868 N  N   . ALA B 1 99  ? -48.410 -12.632 -30.003 1.00 31.79 ? 108 ALA B N   1 
ATOM   3869 C  CA  . ALA B 1 99  ? -47.135 -11.991 -29.641 1.00 33.01 ? 108 ALA B CA  1 
ATOM   3870 C  C   . ALA B 1 99  ? -47.096 -11.482 -28.194 1.00 32.85 ? 108 ALA B C   1 
ATOM   3871 O  O   . ALA B 1 99  ? -46.114 -11.719 -27.476 1.00 33.48 ? 108 ALA B O   1 
ATOM   3872 C  CB  . ALA B 1 99  ? -46.797 -10.867 -30.609 1.00 34.19 ? 108 ALA B CB  1 
ATOM   3873 N  N   . VAL B 1 100 ? -48.166 -10.820 -27.759 1.00 32.62 ? 109 VAL B N   1 
ATOM   3874 C  CA  . VAL B 1 100 ? -48.237 -10.300 -26.385 1.00 33.84 ? 109 VAL B CA  1 
ATOM   3875 C  C   . VAL B 1 100 ? -48.067 -11.401 -25.314 1.00 32.20 ? 109 VAL B C   1 
ATOM   3876 O  O   . VAL B 1 100 ? -47.118 -11.333 -24.533 1.00 33.16 ? 109 VAL B O   1 
ATOM   3877 C  CB  . VAL B 1 100 ? -49.508 -9.408  -26.148 1.00 35.75 ? 109 VAL B CB  1 
ATOM   3878 C  CG1 . VAL B 1 100 ? -49.739 -9.103  -24.657 1.00 38.38 ? 109 VAL B CG1 1 
ATOM   3879 C  CG2 . VAL B 1 100 ? -49.378 -8.092  -26.919 1.00 38.87 ? 109 VAL B CG2 1 
ATOM   3880 N  N   . PRO B 1 101 ? -48.975 -12.404 -25.267 1.00 32.45 ? 110 PRO B N   1 
ATOM   3881 C  CA  . PRO B 1 101 ? -48.817 -13.474 -24.272 1.00 30.93 ? 110 PRO B CA  1 
ATOM   3882 C  C   . PRO B 1 101 ? -47.494 -14.220 -24.341 1.00 29.30 ? 110 PRO B C   1 
ATOM   3883 O  O   . PRO B 1 101 ? -46.938 -14.554 -23.298 1.00 30.69 ? 110 PRO B O   1 
ATOM   3884 C  CB  . PRO B 1 101 ? -49.990 -14.426 -24.562 1.00 29.43 ? 110 PRO B CB  1 
ATOM   3885 C  CG  . PRO B 1 101 ? -50.522 -14.031 -25.862 1.00 34.43 ? 110 PRO B CG  1 
ATOM   3886 C  CD  . PRO B 1 101 ? -50.211 -12.581 -26.049 1.00 32.95 ? 110 PRO B CD  1 
ATOM   3887 N  N   . TYR B 1 102 ? -47.004 -14.465 -25.555 1.00 28.68 ? 111 TYR B N   1 
ATOM   3888 C  CA  . TYR B 1 102 ? -45.718 -15.122 -25.760 1.00 27.95 ? 111 TYR B CA  1 
ATOM   3889 C  C   . TYR B 1 102 ? -44.569 -14.308 -25.195 1.00 27.36 ? 111 TYR B C   1 
ATOM   3890 O  O   . TYR B 1 102 ? -43.705 -14.850 -24.511 1.00 26.44 ? 111 TYR B O   1 
ATOM   3891 C  CB  . TYR B 1 102 ? -45.481 -15.395 -27.253 1.00 27.40 ? 111 TYR B CB  1 
ATOM   3892 C  CG  . TYR B 1 102 ? -44.272 -16.259 -27.601 1.00 26.97 ? 111 TYR B CG  1 
ATOM   3893 C  CD1 . TYR B 1 102 ? -43.813 -17.271 -26.748 1.00 28.23 ? 111 TYR B CD1 1 
ATOM   3894 C  CD2 . TYR B 1 102 ? -43.621 -16.100 -28.827 1.00 26.82 ? 111 TYR B CD2 1 
ATOM   3895 C  CE1 . TYR B 1 102 ? -42.724 -18.077 -27.101 1.00 25.23 ? 111 TYR B CE1 1 
ATOM   3896 C  CE2 . TYR B 1 102 ? -42.536 -16.899 -29.184 1.00 24.62 ? 111 TYR B CE2 1 
ATOM   3897 C  CZ  . TYR B 1 102 ? -42.095 -17.882 -28.319 1.00 26.06 ? 111 TYR B CZ  1 
ATOM   3898 O  OH  . TYR B 1 102 ? -41.025 -18.666 -28.672 1.00 22.86 ? 111 TYR B OH  1 
ATOM   3899 N  N   . CYS B 1 103 ? -44.560 -13.008 -25.475 1.00 29.44 ? 112 CYS B N   1 
ATOM   3900 C  CA  . CYS B 1 103 ? -43.516 -12.136 -24.937 1.00 29.79 ? 112 CYS B CA  1 
ATOM   3901 C  C   . CYS B 1 103 ? -43.639 -11.969 -23.422 1.00 30.82 ? 112 CYS B C   1 
ATOM   3902 O  O   . CYS B 1 103 ? -42.623 -11.951 -22.723 1.00 29.63 ? 112 CYS B O   1 
ATOM   3903 C  CB  . CYS B 1 103 ? -43.513 -10.778 -25.627 1.00 30.30 ? 112 CYS B CB  1 
ATOM   3904 S  SG  . CYS B 1 103 ? -42.891 -10.821 -27.302 1.00 34.85 ? 112 CYS B SG  1 
ATOM   3905 N  N   . GLN B 1 104 ? -44.875 -11.831 -22.934 1.00 31.19 ? 113 GLN B N   1 
ATOM   3906 C  CA  . GLN B 1 104 ? -45.155 -11.773 -21.486 1.00 33.29 ? 113 GLN B CA  1 
ATOM   3907 C  C   . GLN B 1 104 ? -44.659 -13.031 -20.773 1.00 31.77 ? 113 GLN B C   1 
ATOM   3908 O  O   . GLN B 1 104 ? -43.975 -12.956 -19.761 1.00 32.15 ? 113 GLN B O   1 
ATOM   3909 C  CB  . GLN B 1 104 ? -46.663 -11.612 -21.235 1.00 34.20 ? 113 GLN B CB  1 
ATOM   3910 C  CG  . GLN B 1 104 ? -47.195 -10.205 -21.482 1.00 34.64 ? 113 GLN B CG  1 
ATOM   3911 C  CD  . GLN B 1 104 ? -48.698 -10.094 -21.267 1.00 38.90 ? 113 GLN B CD  1 
ATOM   3912 O  OE1 . GLN B 1 104 ? -49.446 -11.049 -21.480 1.00 40.85 ? 113 GLN B OE1 1 
ATOM   3913 N  NE2 . GLN B 1 104 ? -49.147 -8.915  -20.838 1.00 38.21 ? 113 GLN B NE2 1 
ATOM   3914 N  N   . LEU B 1 105 ? -45.011 -14.184 -21.319 1.00 31.76 ? 114 LEU B N   1 
ATOM   3915 C  CA  . LEU B 1 105 ? -44.570 -15.462 -20.776 1.00 32.65 ? 114 LEU B CA  1 
ATOM   3916 C  C   . LEU B 1 105 ? -43.042 -15.618 -20.851 1.00 30.26 ? 114 LEU B C   1 
ATOM   3917 O  O   . LEU B 1 105 ? -42.407 -16.061 -19.894 1.00 26.35 ? 114 LEU B O   1 
ATOM   3918 C  CB  . LEU B 1 105 ? -45.254 -16.604 -21.526 1.00 31.12 ? 114 LEU B CB  1 
ATOM   3919 C  CG  . LEU B 1 105 ? -45.034 -18.018 -21.001 1.00 34.82 ? 114 LEU B CG  1 
ATOM   3920 C  CD1 . LEU B 1 105 ? -45.585 -18.167 -19.589 1.00 37.61 ? 114 LEU B CD1 1 
ATOM   3921 C  CD2 . LEU B 1 105 ? -45.695 -19.006 -21.954 1.00 35.75 ? 114 LEU B CD2 1 
ATOM   3922 N  N   . SER B 1 106 ? -42.470 -15.252 -21.992 1.00 30.23 ? 115 SER B N   1 
ATOM   3923 C  CA  . SER B 1 106 ? -41.011 -15.287 -22.184 1.00 30.05 ? 115 SER B CA  1 
ATOM   3924 C  C   . SER B 1 106 ? -40.282 -14.402 -21.154 1.00 30.03 ? 115 SER B C   1 
ATOM   3925 O  O   . SER B 1 106 ? -39.255 -14.799 -20.591 1.00 23.29 ? 115 SER B O   1 
ATOM   3926 C  CB  . SER B 1 106 ? -40.662 -14.858 -23.613 1.00 29.14 ? 115 SER B CB  1 
ATOM   3927 O  OG  . SER B 1 106 ? -41.238 -15.737 -24.577 1.00 23.02 ? 115 SER B OG  1 
ATOM   3928 N  N   . LYS B 1 107 ? -40.829 -13.215 -20.897 1.00 33.28 ? 116 LYS B N   1 
ATOM   3929 C  CA  . LYS B 1 107 ? -40.292 -12.313 -19.865 1.00 35.96 ? 116 LYS B CA  1 
ATOM   3930 C  C   . LYS B 1 107 ? -40.326 -12.958 -18.472 1.00 36.96 ? 116 LYS B C   1 
ATOM   3931 O  O   . LYS B 1 107 ? -39.338 -12.905 -17.730 1.00 38.31 ? 116 LYS B O   1 
ATOM   3932 C  CB  . LYS B 1 107 ? -41.060 -10.977 -19.844 1.00 38.17 ? 116 LYS B CB  1 
ATOM   3933 C  CG  . LYS B 1 107 ? -40.326 -9.863  -19.116 1.00 40.50 ? 116 LYS B CG  1 
ATOM   3934 C  CD  . LYS B 1 107 ? -41.160 -8.578  -18.990 1.00 46.59 ? 116 LYS B CD  1 
ATOM   3935 C  CE  . LYS B 1 107 ? -40.405 -7.491  -18.247 0.00 46.54 ? 116 LYS B CE  1 
ATOM   3936 N  NZ  . LYS B 1 107 ? -41.206 -6.243  -18.113 0.00 48.44 ? 116 LYS B NZ  1 
ATOM   3937 N  N   . LYS B 1 108 ? -41.456 -13.579 -18.134 1.00 37.59 ? 117 LYS B N   1 
ATOM   3938 C  CA  . LYS B 1 108 ? -41.631 -14.265 -16.846 1.00 38.61 ? 117 LYS B CA  1 
ATOM   3939 C  C   . LYS B 1 108 ? -40.578 -15.368 -16.609 1.00 36.81 ? 117 LYS B C   1 
ATOM   3940 O  O   . LYS B 1 108 ? -40.046 -15.493 -15.503 1.00 37.92 ? 117 LYS B O   1 
ATOM   3941 C  CB  . LYS B 1 108 ? -43.047 -14.843 -16.749 1.00 39.93 ? 117 LYS B CB  1 
ATOM   3942 C  CG  . LYS B 1 108 ? -43.424 -15.367 -15.375 1.00 42.99 ? 117 LYS B CG  1 
ATOM   3943 C  CD  . LYS B 1 108 ? -44.934 -15.617 -15.251 1.00 45.29 ? 117 LYS B CD  1 
ATOM   3944 C  CE  . LYS B 1 108 ? -45.352 -15.792 -13.778 1.00 52.83 ? 117 LYS B CE  1 
ATOM   3945 N  NZ  . LYS B 1 108 ? -46.831 -15.663 -13.582 1.00 54.27 ? 117 LYS B NZ  1 
ATOM   3946 N  N   . LEU B 1 109 ? -40.274 -16.132 -17.656 1.00 33.68 ? 118 LEU B N   1 
ATOM   3947 C  CA  . LEU B 1 109 ? -39.283 -17.217 -17.609 1.00 34.24 ? 118 LEU B CA  1 
ATOM   3948 C  C   . LEU B 1 109 ? -37.860 -16.790 -18.006 1.00 32.14 ? 118 LEU B C   1 
ATOM   3949 O  O   . LEU B 1 109 ? -36.958 -17.624 -18.036 1.00 31.99 ? 118 LEU B O   1 
ATOM   3950 C  CB  . LEU B 1 109 ? -39.740 -18.377 -18.507 1.00 30.63 ? 118 LEU B CB  1 
ATOM   3951 C  CG  . LEU B 1 109 ? -41.057 -19.060 -18.115 1.00 35.62 ? 118 LEU B CG  1 
ATOM   3952 C  CD1 . LEU B 1 109 ? -41.513 -19.982 -19.235 1.00 33.99 ? 118 LEU B CD1 1 
ATOM   3953 C  CD2 . LEU B 1 109 ? -40.932 -19.830 -16.805 1.00 37.22 ? 118 LEU B CD2 1 
ATOM   3954 N  N   . GLU B 1 110 ? -37.674 -15.501 -18.299 1.00 33.44 ? 119 GLU B N   1 
ATOM   3955 C  CA  . GLU B 1 110 ? -36.377 -14.915 -18.679 1.00 34.24 ? 119 GLU B CA  1 
ATOM   3956 C  C   . GLU B 1 110 ? -35.753 -15.592 -19.889 1.00 31.63 ? 119 GLU B C   1 
ATOM   3957 O  O   . GLU B 1 110 ? -34.562 -15.885 -19.889 1.00 31.47 ? 119 GLU B O   1 
ATOM   3958 C  CB  . GLU B 1 110 ? -35.394 -14.915 -17.497 1.00 34.97 ? 119 GLU B CB  1 
ATOM   3959 C  CG  . GLU B 1 110 ? -35.918 -14.239 -16.239 1.00 43.44 ? 119 GLU B CG  1 
ATOM   3960 C  CD  . GLU B 1 110 ? -34.902 -14.216 -15.105 1.00 46.63 ? 119 GLU B CD  1 
ATOM   3961 O  OE1 . GLU B 1 110 ? -35.275 -14.589 -13.971 1.00 59.50 ? 119 GLU B OE1 1 
ATOM   3962 O  OE2 . GLU B 1 110 ? -33.734 -13.827 -15.339 1.00 53.24 ? 119 GLU B OE2 1 
ATOM   3963 N  N   . LEU B 1 111 ? -36.570 -15.857 -20.913 1.00 29.02 ? 120 LEU B N   1 
ATOM   3964 C  CA  . LEU B 1 111 ? -36.087 -16.453 -22.153 1.00 28.05 ? 120 LEU B CA  1 
ATOM   3965 C  C   . LEU B 1 111 ? -36.487 -15.543 -23.302 1.00 27.55 ? 120 LEU B C   1 
ATOM   3966 O  O   . LEU B 1 111 ? -37.487 -14.836 -23.189 1.00 28.35 ? 120 LEU B O   1 
ATOM   3967 C  CB  . LEU B 1 111 ? -36.669 -17.858 -22.348 1.00 26.04 ? 120 LEU B CB  1 
ATOM   3968 C  CG  . LEU B 1 111 ? -36.173 -18.944 -21.391 1.00 27.09 ? 120 LEU B CG  1 
ATOM   3969 C  CD1 . LEU B 1 111 ? -37.084 -20.151 -21.417 1.00 27.00 ? 120 LEU B CD1 1 
ATOM   3970 C  CD2 . LEU B 1 111 ? -34.752 -19.373 -21.714 1.00 26.08 ? 120 LEU B CD2 1 
ATOM   3971 N  N   . PRO B 1 112 ? -35.712 -15.544 -24.409 1.00 27.66 ? 121 PRO B N   1 
ATOM   3972 C  CA  . PRO B 1 112 ? -36.118 -14.761 -25.590 1.00 28.66 ? 121 PRO B CA  1 
ATOM   3973 C  C   . PRO B 1 112 ? -37.398 -15.316 -26.210 1.00 28.50 ? 121 PRO B C   1 
ATOM   3974 O  O   . PRO B 1 112 ? -37.606 -16.523 -26.144 1.00 30.02 ? 121 PRO B O   1 
ATOM   3975 C  CB  . PRO B 1 112 ? -34.934 -14.950 -26.550 1.00 28.62 ? 121 PRO B CB  1 
ATOM   3976 C  CG  . PRO B 1 112 ? -33.786 -15.315 -25.652 1.00 29.50 ? 121 PRO B CG  1 
ATOM   3977 C  CD  . PRO B 1 112 ? -34.425 -16.218 -24.659 1.00 29.02 ? 121 PRO B CD  1 
ATOM   3978 N  N   . PRO B 1 113 ? -38.256 -14.461 -26.802 1.00 28.57 ? 122 PRO B N   1 
ATOM   3979 C  CA  . PRO B 1 113 ? -39.491 -14.954 -27.411 1.00 27.28 ? 122 PRO B CA  1 
ATOM   3980 C  C   . PRO B 1 113 ? -39.257 -15.649 -28.756 1.00 26.69 ? 122 PRO B C   1 
ATOM   3981 O  O   . PRO B 1 113 ? -39.678 -15.166 -29.822 1.00 25.47 ? 122 PRO B O   1 
ATOM   3982 C  CB  . PRO B 1 113 ? -40.336 -13.677 -27.539 1.00 29.69 ? 122 PRO B CB  1 
ATOM   3983 C  CG  . PRO B 1 113 ? -39.323 -12.608 -27.755 1.00 30.26 ? 122 PRO B CG  1 
ATOM   3984 C  CD  . PRO B 1 113 ? -38.147 -12.993 -26.914 1.00 29.26 ? 122 PRO B CD  1 
ATOM   3985 N  N   . ILE B 1 114 ? -38.588 -16.797 -28.686 1.00 24.83 ? 123 ILE B N   1 
ATOM   3986 C  CA  . ILE B 1 114 ? -38.350 -17.652 -29.849 1.00 23.19 ? 123 ILE B CA  1 
ATOM   3987 C  C   . ILE B 1 114 ? -38.183 -19.073 -29.332 1.00 22.87 ? 123 ILE B C   1 
ATOM   3988 O  O   . ILE B 1 114 ? -37.826 -19.266 -28.182 1.00 21.69 ? 123 ILE B O   1 
ATOM   3989 C  CB  . ILE B 1 114 ? -37.106 -17.190 -30.668 1.00 22.70 ? 123 ILE B CB  1 
ATOM   3990 C  CG1 . ILE B 1 114 ? -36.991 -17.978 -31.979 1.00 23.14 ? 123 ILE B CG1 1 
ATOM   3991 C  CG2 . ILE B 1 114 ? -35.824 -17.285 -29.830 1.00 22.78 ? 123 ILE B CG2 1 
ATOM   3992 C  CD1 . ILE B 1 114 ? -36.130 -17.340 -33.029 1.00 22.57 ? 123 ILE B CD1 1 
ATOM   3993 N  N   . LEU B 1 115 ? -38.458 -20.058 -30.176 1.00 22.94 ? 124 LEU B N   1 
ATOM   3994 C  CA  . LEU B 1 115 ? -38.314 -21.448 -29.789 1.00 21.99 ? 124 LEU B CA  1 
ATOM   3995 C  C   . LEU B 1 115 ? -36.840 -21.719 -29.502 1.00 22.56 ? 124 LEU B C   1 
ATOM   3996 O  O   . LEU B 1 115 ? -35.994 -21.470 -30.360 1.00 26.27 ? 124 LEU B O   1 
ATOM   3997 C  CB  . LEU B 1 115 ? -38.805 -22.368 -30.895 1.00 20.87 ? 124 LEU B CB  1 
ATOM   3998 C  CG  . LEU B 1 115 ? -38.916 -23.850 -30.568 1.00 19.13 ? 124 LEU B CG  1 
ATOM   3999 C  CD1 . LEU B 1 115 ? -40.095 -24.102 -29.633 1.00 26.15 ? 124 LEU B CD1 1 
ATOM   4000 C  CD2 . LEU B 1 115 ? -39.090 -24.650 -31.859 1.00 23.08 ? 124 LEU B CD2 1 
ATOM   4001 N  N   . VAL B 1 116 ? -36.556 -22.193 -28.288 1.00 21.30 ? 125 VAL B N   1 
ATOM   4002 C  CA  . VAL B 1 116 ? -35.196 -22.524 -27.864 1.00 23.38 ? 125 VAL B CA  1 
ATOM   4003 C  C   . VAL B 1 116 ? -35.073 -24.030 -27.594 1.00 24.46 ? 125 VAL B C   1 
ATOM   4004 O  O   . VAL B 1 116 ? -36.071 -24.748 -27.491 1.00 20.92 ? 125 VAL B O   1 
ATOM   4005 C  CB  . VAL B 1 116 ? -34.734 -21.703 -26.616 1.00 21.82 ? 125 VAL B CB  1 
ATOM   4006 C  CG1 . VAL B 1 116 ? -34.864 -20.202 -26.865 1.00 19.24 ? 125 VAL B CG1 1 
ATOM   4007 C  CG2 . VAL B 1 116 ? -35.483 -22.093 -25.343 1.00 20.46 ? 125 VAL B CG2 1 
ATOM   4008 N  N   . TYR B 1 117 ? -33.827 -24.477 -27.491 1.00 24.87 ? 126 TYR B N   1 
ATOM   4009 C  CA  . TYR B 1 117 ? -33.478 -25.866 -27.140 1.00 23.38 ? 126 TYR B CA  1 
ATOM   4010 C  C   . TYR B 1 117 ? -34.221 -26.374 -25.896 1.00 23.96 ? 126 TYR B C   1 
ATOM   4011 O  O   . TYR B 1 117 ? -34.716 -27.506 -25.856 1.00 23.21 ? 126 TYR B O   1 
ATOM   4012 C  CB  . TYR B 1 117 ? -31.973 -25.920 -26.919 1.00 24.58 ? 126 TYR B CB  1 
ATOM   4013 C  CG  . TYR B 1 117 ? -31.398 -27.268 -26.609 1.00 23.60 ? 126 TYR B CG  1 
ATOM   4014 C  CD1 . TYR B 1 117 ? -31.026 -28.139 -27.635 1.00 24.15 ? 126 TYR B CD1 1 
ATOM   4015 C  CD2 . TYR B 1 117 ? -31.180 -27.663 -25.299 1.00 23.01 ? 126 TYR B CD2 1 
ATOM   4016 C  CE1 . TYR B 1 117 ? -30.478 -29.383 -27.354 1.00 24.32 ? 126 TYR B CE1 1 
ATOM   4017 C  CE2 . TYR B 1 117 ? -30.625 -28.910 -25.006 1.00 27.82 ? 126 TYR B CE2 1 
ATOM   4018 C  CZ  . TYR B 1 117 ? -30.281 -29.768 -26.037 1.00 27.11 ? 126 TYR B CZ  1 
ATOM   4019 O  OH  . TYR B 1 117 ? -29.724 -31.000 -25.753 1.00 29.29 ? 126 TYR B OH  1 
ATOM   4020 N  N   . ALA B 1 118 ? -34.299 -25.520 -24.885 1.00 21.78 ? 127 ALA B N   1 
ATOM   4021 C  CA  . ALA B 1 118 ? -35.044 -25.824 -23.673 1.00 21.34 ? 127 ALA B CA  1 
ATOM   4022 C  C   . ALA B 1 118 ? -36.535 -26.078 -23.884 1.00 23.30 ? 127 ALA B C   1 
ATOM   4023 O  O   . ALA B 1 118 ? -37.141 -26.803 -23.089 1.00 25.60 ? 127 ALA B O   1 
ATOM   4024 C  CB  . ALA B 1 118 ? -34.835 -24.730 -22.642 1.00 23.58 ? 127 ALA B CB  1 
ATOM   4025 N  N   . ASP B 1 119 ? -37.124 -25.493 -24.932 1.00 24.27 ? 128 ASP B N   1 
ATOM   4026 C  CA  . ASP B 1 119 ? -38.523 -25.762 -25.288 1.00 22.59 ? 128 ASP B CA  1 
ATOM   4027 C  C   . ASP B 1 119 ? -38.620 -27.067 -26.061 1.00 21.99 ? 128 ASP B C   1 
ATOM   4028 O  O   . ASP B 1 119 ? -39.245 -28.030 -25.609 1.00 23.35 ? 128 ASP B O   1 
ATOM   4029 C  CB  . ASP B 1 119 ? -39.135 -24.648 -26.147 1.00 23.23 ? 128 ASP B CB  1 
ATOM   4030 C  CG  . ASP B 1 119 ? -39.023 -23.269 -25.522 1.00 25.36 ? 128 ASP B CG  1 
ATOM   4031 O  OD1 . ASP B 1 119 ? -39.281 -23.102 -24.310 1.00 23.37 ? 128 ASP B OD1 1 
ATOM   4032 O  OD2 . ASP B 1 119 ? -38.697 -22.344 -26.285 1.00 22.35 ? 128 ASP B OD2 1 
ATOM   4033 N  N   . CYS B 1 120 ? -37.988 -27.091 -27.226 1.00 21.54 ? 129 CYS B N   1 
ATOM   4034 C  CA  . CYS B 1 120 ? -38.236 -28.138 -28.216 1.00 24.19 ? 129 CYS B CA  1 
ATOM   4035 C  C   . CYS B 1 120 ? -37.480 -29.445 -27.966 1.00 23.20 ? 129 CYS B C   1 
ATOM   4036 O  O   . CYS B 1 120 ? -37.804 -30.444 -28.585 1.00 22.81 ? 129 CYS B O   1 
ATOM   4037 C  CB  . CYS B 1 120 ? -37.978 -27.614 -29.630 1.00 23.19 ? 129 CYS B CB  1 
ATOM   4038 S  SG  . CYS B 1 120 ? -36.295 -27.163 -30.016 1.00 23.89 ? 129 CYS B SG  1 
ATOM   4039 N  N   . VAL B 1 121 ? -36.486 -29.439 -27.072 1.00 24.39 ? 130 VAL B N   1 
ATOM   4040 C  CA  . VAL B 1 121 ? -35.831 -30.683 -26.632 1.00 24.31 ? 130 VAL B CA  1 
ATOM   4041 C  C   . VAL B 1 121 ? -36.198 -30.973 -25.184 1.00 24.42 ? 130 VAL B C   1 
ATOM   4042 O  O   . VAL B 1 121 ? -36.860 -31.965 -24.882 1.00 23.55 ? 130 VAL B O   1 
ATOM   4043 C  CB  . VAL B 1 121 ? -34.289 -30.633 -26.823 1.00 24.35 ? 130 VAL B CB  1 
ATOM   4044 C  CG1 . VAL B 1 121 ? -33.625 -31.939 -26.383 1.00 27.01 ? 130 VAL B CG1 1 
ATOM   4045 C  CG2 . VAL B 1 121 ? -33.964 -30.375 -28.278 1.00 24.18 ? 130 VAL B CG2 1 
ATOM   4046 N  N   . LEU B 1 122 ? -35.807 -30.076 -24.295 1.00 24.07 ? 131 LEU B N   1 
ATOM   4047 C  CA  . LEU B 1 122 ? -35.866 -30.356 -22.869 1.00 24.65 ? 131 LEU B CA  1 
ATOM   4048 C  C   . LEU B 1 122 ? -37.284 -30.465 -22.301 1.00 26.82 ? 131 LEU B C   1 
ATOM   4049 O  O   . LEU B 1 122 ? -37.474 -31.158 -21.310 1.00 26.24 ? 131 LEU B O   1 
ATOM   4050 C  CB  . LEU B 1 122 ? -35.036 -29.325 -22.089 1.00 25.39 ? 131 LEU B CB  1 
ATOM   4051 C  CG  . LEU B 1 122 ? -33.564 -29.184 -22.513 1.00 24.26 ? 131 LEU B CG  1 
ATOM   4052 C  CD1 . LEU B 1 122 ? -32.828 -28.189 -21.629 1.00 24.42 ? 131 LEU B CD1 1 
ATOM   4053 C  CD2 . LEU B 1 122 ? -32.844 -30.528 -22.515 1.00 24.28 ? 131 LEU B CD2 1 
ATOM   4054 N  N   . ALA B 1 123 ? -38.259 -29.797 -22.928 1.00 27.06 ? 132 ALA B N   1 
ATOM   4055 C  CA  . ALA B 1 123 ? -39.665 -29.780 -22.463 1.00 26.41 ? 132 ALA B CA  1 
ATOM   4056 C  C   . ALA B 1 123 ? -40.666 -30.478 -23.404 1.00 25.64 ? 132 ALA B C   1 
ATOM   4057 O  O   . ALA B 1 123 ? -41.849 -30.580 -23.068 1.00 25.43 ? 132 ALA B O   1 
ATOM   4058 C  CB  . ALA B 1 123 ? -40.103 -28.332 -22.224 1.00 25.83 ? 132 ALA B CB  1 
ATOM   4059 N  N   . ASN B 1 124 ? -40.181 -30.970 -24.548 1.00 24.03 ? 133 ASN B N   1 
ATOM   4060 C  CA  . ASN B 1 124 ? -41.011 -31.482 -25.646 1.00 25.72 ? 133 ASN B CA  1 
ATOM   4061 C  C   . ASN B 1 124 ? -41.016 -33.017 -25.664 1.00 24.87 ? 133 ASN B C   1 
ATOM   4062 O  O   . ASN B 1 124 ? -40.713 -33.653 -26.676 1.00 24.90 ? 133 ASN B O   1 
ATOM   4063 C  CB  . ASN B 1 124 ? -40.475 -30.918 -26.973 1.00 22.74 ? 133 ASN B CB  1 
ATOM   4064 C  CG  . ASN B 1 124 ? -41.367 -31.212 -28.177 1.00 26.33 ? 133 ASN B CG  1 
ATOM   4065 O  OD1 . ASN B 1 124 ? -42.543 -31.550 -28.041 1.00 26.55 ? 133 ASN B OD1 1 
ATOM   4066 N  ND2 . ASN B 1 124 ? -40.790 -31.079 -29.375 1.00 22.29 ? 133 ASN B ND2 1 
ATOM   4067 N  N   . TRP B 1 125 ? -41.365 -33.618 -24.536 1.00 26.17 ? 134 TRP B N   1 
ATOM   4068 C  CA  . TRP B 1 125 ? -41.285 -35.061 -24.436 1.00 26.48 ? 134 TRP B CA  1 
ATOM   4069 C  C   . TRP B 1 125 ? -42.203 -35.664 -23.396 1.00 28.99 ? 134 TRP B C   1 
ATOM   4070 O  O   . TRP B 1 125 ? -42.719 -34.981 -22.520 1.00 29.66 ? 134 TRP B O   1 
ATOM   4071 C  CB  . TRP B 1 125 ? -39.825 -35.513 -24.223 1.00 26.00 ? 134 TRP B CB  1 
ATOM   4072 C  CG  . TRP B 1 125 ? -39.252 -35.207 -22.876 1.00 24.72 ? 134 TRP B CG  1 
ATOM   4073 C  CD1 . TRP B 1 125 ? -38.609 -34.059 -22.490 1.00 24.49 ? 134 TRP B CD1 1 
ATOM   4074 C  CD2 . TRP B 1 125 ? -39.257 -36.069 -21.731 1.00 28.21 ? 134 TRP B CD2 1 
ATOM   4075 N  NE1 . TRP B 1 125 ? -38.226 -34.154 -21.169 1.00 25.76 ? 134 TRP B NE1 1 
ATOM   4076 C  CE2 . TRP B 1 125 ? -38.613 -35.375 -20.681 1.00 27.14 ? 134 TRP B CE2 1 
ATOM   4077 C  CE3 . TRP B 1 125 ? -39.754 -37.358 -21.487 1.00 28.42 ? 134 TRP B CE3 1 
ATOM   4078 C  CZ2 . TRP B 1 125 ? -38.443 -35.932 -19.412 1.00 28.07 ? 134 TRP B CZ2 1 
ATOM   4079 C  CZ3 . TRP B 1 125 ? -39.590 -37.911 -20.224 1.00 30.17 ? 134 TRP B CZ3 1 
ATOM   4080 C  CH2 . TRP B 1 125 ? -38.937 -37.198 -19.200 1.00 32.11 ? 134 TRP B CH2 1 
ATOM   4081 N  N   . LYS B 1 126 ? -42.402 -36.968 -23.541 1.00 31.57 ? 135 LYS B N   1 
ATOM   4082 C  CA  . LYS B 1 126 ? -43.132 -37.786 -22.587 1.00 32.36 ? 135 LYS B CA  1 
ATOM   4083 C  C   . LYS B 1 126 ? -42.640 -39.226 -22.663 1.00 33.40 ? 135 LYS B C   1 
ATOM   4084 O  O   . LYS B 1 126 ? -42.072 -39.644 -23.675 1.00 34.63 ? 135 LYS B O   1 
ATOM   4085 C  CB  . LYS B 1 126 ? -44.638 -37.751 -22.875 1.00 32.66 ? 135 LYS B CB  1 
ATOM   4086 C  CG  . LYS B 1 126 ? -45.054 -38.291 -24.247 1.00 34.69 ? 135 LYS B CG  1 
ATOM   4087 C  CD  . LYS B 1 126 ? -46.566 -38.217 -24.456 1.00 37.50 ? 135 LYS B CD  1 
ATOM   4088 C  CE  . LYS B 1 126 ? -47.300 -39.336 -23.703 1.00 43.33 ? 135 LYS B CE  1 
ATOM   4089 N  NZ  . LYS B 1 126 ? -48.781 -39.176 -23.710 1.00 46.29 ? 135 LYS B NZ  1 
ATOM   4090 N  N   . LYS B 1 127 ? -42.849 -39.956 -21.575 1.00 36.52 ? 136 LYS B N   1 
ATOM   4091 C  CA  . LYS B 1 127 ? -42.746 -41.413 -21.556 1.00 39.21 ? 136 LYS B CA  1 
ATOM   4092 C  C   . LYS B 1 127 ? -44.083 -41.987 -22.000 1.00 42.81 ? 136 LYS B C   1 
ATOM   4093 O  O   . LYS B 1 127 ? -45.141 -41.462 -21.631 1.00 42.69 ? 136 LYS B O   1 
ATOM   4094 C  CB  . LYS B 1 127 ? -42.448 -41.932 -20.147 1.00 40.66 ? 136 LYS B CB  1 
ATOM   4095 C  CG  . LYS B 1 127 ? -40.983 -42.027 -19.787 1.00 41.13 ? 136 LYS B CG  1 
ATOM   4096 C  CD  . LYS B 1 127 ? -40.826 -42.679 -18.406 1.00 42.17 ? 136 LYS B CD  1 
ATOM   4097 C  CE  . LYS B 1 127 ? -39.372 -42.905 -18.027 1.00 45.65 ? 136 LYS B CE  1 
ATOM   4098 N  NZ  . LYS B 1 127 ? -39.225 -43.854 -16.875 1.00 42.79 ? 136 LYS B NZ  1 
ATOM   4099 N  N   . LYS B 1 128 ? -44.040 -43.068 -22.774 1.00 45.45 ? 137 LYS B N   1 
ATOM   4100 C  CA  . LYS B 1 128 ? -45.257 -43.803 -23.124 1.00 48.17 ? 137 LYS B CA  1 
ATOM   4101 C  C   . LYS B 1 128 ? -45.695 -44.622 -21.914 1.00 50.31 ? 137 LYS B C   1 
ATOM   4102 O  O   . LYS B 1 128 ? -46.827 -44.496 -21.449 1.00 52.17 ? 137 LYS B O   1 
ATOM   4103 C  CB  . LYS B 1 128 ? -45.027 -44.697 -24.342 1.00 48.50 ? 137 LYS B CB  1 
ATOM   4104 C  CG  . LYS B 1 128 ? -44.754 -43.919 -25.624 1.00 48.38 ? 137 LYS B CG  1 
ATOM   4105 C  CD  . LYS B 1 128 ? -44.324 -44.849 -26.752 1.00 49.60 ? 137 LYS B CD  1 
ATOM   4106 C  CE  . LYS B 1 128 ? -44.451 -44.184 -28.112 1.00 50.99 ? 137 LYS B CE  1 
ATOM   4107 N  NZ  . LYS B 1 128 ? -43.967 -45.058 -29.217 1.00 54.04 ? 137 LYS B NZ  1 
ATOM   4108 N  N   . ASP B 1 129 ? -44.779 -45.443 -21.409 1.00 53.27 ? 138 ASP B N   1 
ATOM   4109 C  CA  . ASP B 1 129 ? -44.982 -46.220 -20.192 1.00 57.45 ? 138 ASP B CA  1 
ATOM   4110 C  C   . ASP B 1 129 ? -44.117 -45.619 -19.073 1.00 58.80 ? 138 ASP B C   1 
ATOM   4111 O  O   . ASP B 1 129 ? -42.888 -45.723 -19.131 1.00 56.92 ? 138 ASP B O   1 
ATOM   4112 C  CB  . ASP B 1 129 ? -44.615 -47.691 -20.432 1.00 59.53 ? 138 ASP B CB  1 
ATOM   4113 C  CG  . ASP B 1 129 ? -45.039 -48.608 -19.287 1.00 60.87 ? 138 ASP B CG  1 
ATOM   4114 O  OD1 . ASP B 1 129 ? -45.317 -48.114 -18.174 1.00 60.82 ? 138 ASP B OD1 1 
ATOM   4115 O  OD2 . ASP B 1 129 ? -45.086 -49.838 -19.503 1.00 64.53 ? 138 ASP B OD2 1 
ATOM   4116 N  N   . PRO B 1 130 ? -44.755 -44.994 -18.052 1.00 62.13 ? 139 PRO B N   1 
ATOM   4117 C  CA  . PRO B 1 130 ? -44.051 -44.517 -16.843 1.00 62.05 ? 139 PRO B CA  1 
ATOM   4118 C  C   . PRO B 1 130 ? -43.187 -45.566 -16.112 1.00 63.70 ? 139 PRO B C   1 
ATOM   4119 O  O   . PRO B 1 130 ? -42.185 -45.202 -15.498 1.00 64.04 ? 139 PRO B O   1 
ATOM   4120 C  CB  . PRO B 1 130 ? -45.196 -44.057 -15.929 1.00 65.26 ? 139 PRO B CB  1 
ATOM   4121 C  CG  . PRO B 1 130 ? -46.306 -43.718 -16.845 1.00 64.51 ? 139 PRO B CG  1 
ATOM   4122 C  CD  . PRO B 1 130 ? -46.197 -44.676 -17.991 1.00 63.90 ? 139 PRO B CD  1 
ATOM   4123 N  N   . ASN B 1 131 ? -43.571 -46.842 -16.188 1.00 64.99 ? 140 ASN B N   1 
ATOM   4124 C  CA  . ASN B 1 131 ? -42.812 -47.936 -15.562 1.00 66.12 ? 140 ASN B CA  1 
ATOM   4125 C  C   . ASN B 1 131 ? -41.586 -48.433 -16.344 1.00 64.61 ? 140 ASN B C   1 
ATOM   4126 O  O   . ASN B 1 131 ? -40.844 -49.281 -15.834 1.00 64.95 ? 140 ASN B O   1 
ATOM   4127 C  CB  . ASN B 1 131 ? -43.735 -49.134 -15.288 1.00 70.50 ? 140 ASN B CB  1 
ATOM   4128 C  CG  . ASN B 1 131 ? -44.889 -48.793 -14.362 1.00 72.99 ? 140 ASN B CG  1 
ATOM   4129 O  OD1 . ASN B 1 131 ? -45.055 -47.644 -13.935 1.00 69.93 ? 140 ASN B OD1 1 
ATOM   4130 N  ND2 . ASN B 1 131 ? -45.702 -49.797 -14.053 1.00 81.24 ? 140 ASN B ND2 1 
ATOM   4131 N  N   . LYS B 1 132 ? -41.382 -47.936 -17.568 1.00 61.41 ? 141 LYS B N   1 
ATOM   4132 C  CA  . LYS B 1 132 ? -40.215 -48.317 -18.387 1.00 59.22 ? 141 LYS B CA  1 
ATOM   4133 C  C   . LYS B 1 132 ? -39.199 -47.165 -18.484 1.00 55.60 ? 141 LYS B C   1 
ATOM   4134 O  O   . LYS B 1 132 ? -39.572 -45.998 -18.329 1.00 52.88 ? 141 LYS B O   1 
ATOM   4135 C  CB  . LYS B 1 132 ? -40.659 -48.776 -19.784 1.00 58.77 ? 141 LYS B CB  1 
ATOM   4136 C  CG  . LYS B 1 132 ? -41.194 -50.207 -19.818 1.00 62.52 ? 141 LYS B CG  1 
ATOM   4137 C  CD  . LYS B 1 132 ? -41.299 -50.744 -21.241 1.00 63.05 ? 141 LYS B CD  1 
ATOM   4138 C  CE  . LYS B 1 132 ? -41.766 -52.198 -21.258 1.00 66.89 ? 141 LYS B CE  1 
ATOM   4139 N  NZ  . LYS B 1 132 ? -41.577 -52.815 -22.593 0.00 66.64 ? 141 LYS B NZ  1 
ATOM   4140 N  N   . PRO B 1 133 ? -37.912 -47.491 -18.736 1.00 53.25 ? 142 PRO B N   1 
ATOM   4141 C  CA  . PRO B 1 133 ? -36.885 -46.449 -18.793 1.00 50.14 ? 142 PRO B CA  1 
ATOM   4142 C  C   . PRO B 1 133 ? -37.016 -45.437 -19.941 1.00 45.92 ? 142 PRO B C   1 
ATOM   4143 O  O   . PRO B 1 133 ? -37.894 -45.546 -20.808 1.00 46.54 ? 142 PRO B O   1 
ATOM   4144 C  CB  . PRO B 1 133 ? -35.572 -47.243 -18.913 1.00 50.05 ? 142 PRO B CB  1 
ATOM   4145 C  CG  . PRO B 1 133 ? -35.954 -48.564 -19.421 1.00 54.95 ? 142 PRO B CG  1 
ATOM   4146 C  CD  . PRO B 1 133 ? -37.339 -48.837 -18.942 1.00 55.03 ? 142 PRO B CD  1 
ATOM   4147 N  N   . LEU B 1 134 ? -36.139 -44.444 -19.897 1.00 42.01 ? 143 LEU B N   1 
ATOM   4148 C  CA  . LEU B 1 134 ? -36.049 -43.415 -20.921 1.00 39.23 ? 143 LEU B CA  1 
ATOM   4149 C  C   . LEU B 1 134 ? -35.246 -43.924 -22.114 1.00 37.80 ? 143 LEU B C   1 
ATOM   4150 O  O   . LEU B 1 134 ? -34.034 -43.713 -22.206 1.00 35.83 ? 143 LEU B O   1 
ATOM   4151 C  CB  . LEU B 1 134 ? -35.426 -42.142 -20.341 1.00 37.99 ? 143 LEU B CB  1 
ATOM   4152 C  CG  . LEU B 1 134 ? -36.273 -41.440 -19.274 1.00 41.58 ? 143 LEU B CG  1 
ATOM   4153 C  CD1 . LEU B 1 134 ? -35.442 -40.389 -18.545 1.00 44.36 ? 143 LEU B CD1 1 
ATOM   4154 C  CD2 . LEU B 1 134 ? -37.526 -40.809 -19.871 1.00 40.17 ? 143 LEU B CD2 1 
ATOM   4155 N  N   . THR B 1 135 ? -35.948 -44.624 -23.004 1.00 38.10 ? 144 THR B N   1 
ATOM   4156 C  CA  . THR B 1 135 ? -35.421 -45.066 -24.296 1.00 37.61 ? 144 THR B CA  1 
ATOM   4157 C  C   . THR B 1 135 ? -36.305 -44.514 -25.404 1.00 35.49 ? 144 THR B C   1 
ATOM   4158 O  O   . THR B 1 135 ? -37.471 -44.192 -25.171 1.00 33.39 ? 144 THR B O   1 
ATOM   4159 C  CB  . THR B 1 135 ? -35.443 -46.605 -24.426 1.00 41.71 ? 144 THR B CB  1 
ATOM   4160 O  OG1 . THR B 1 135 ? -36.792 -47.074 -24.309 1.00 38.68 ? 144 THR B OG1 1 
ATOM   4161 C  CG2 . THR B 1 135 ? -34.580 -47.269 -23.354 1.00 44.37 ? 144 THR B CG2 1 
ATOM   4162 N  N   . TYR B 1 136 ? -35.761 -44.454 -26.614 1.00 33.95 ? 145 TYR B N   1 
ATOM   4163 C  CA  . TYR B 1 136 ? -36.491 -43.925 -27.779 1.00 34.48 ? 145 TYR B CA  1 
ATOM   4164 C  C   . TYR B 1 136 ? -37.886 -44.550 -27.960 1.00 36.82 ? 145 TYR B C   1 
ATOM   4165 O  O   . TYR B 1 136 ? -38.876 -43.841 -28.204 1.00 35.38 ? 145 TYR B O   1 
ATOM   4166 C  CB  . TYR B 1 136 ? -35.669 -44.119 -29.062 1.00 32.52 ? 145 TYR B CB  1 
ATOM   4167 C  CG  . TYR B 1 136 ? -36.230 -43.365 -30.235 1.00 32.00 ? 145 TYR B CG  1 
ATOM   4168 C  CD1 . TYR B 1 136 ? -35.917 -42.023 -30.432 1.00 29.32 ? 145 TYR B CD1 1 
ATOM   4169 C  CD2 . TYR B 1 136 ? -37.089 -43.985 -31.150 1.00 36.22 ? 145 TYR B CD2 1 
ATOM   4170 C  CE1 . TYR B 1 136 ? -36.444 -41.306 -31.507 1.00 30.32 ? 145 TYR B CE1 1 
ATOM   4171 C  CE2 . TYR B 1 136 ? -37.617 -43.275 -32.241 1.00 34.03 ? 145 TYR B CE2 1 
ATOM   4172 C  CZ  . TYR B 1 136 ? -37.286 -41.933 -32.403 1.00 31.13 ? 145 TYR B CZ  1 
ATOM   4173 O  OH  . TYR B 1 136 ? -37.789 -41.216 -33.457 1.00 33.04 ? 145 TYR B OH  1 
ATOM   4174 N  N   . GLU B 1 137 ? -37.947 -45.869 -27.800 1.00 37.17 ? 146 GLU B N   1 
ATOM   4175 C  CA  . GLU B 1 137 ? -39.149 -46.655 -28.094 1.00 40.49 ? 146 GLU B CA  1 
ATOM   4176 C  C   . GLU B 1 137 ? -40.229 -46.478 -27.031 1.00 39.27 ? 146 GLU B C   1 
ATOM   4177 O  O   . GLU B 1 137 ? -41.395 -46.768 -27.286 1.00 40.75 ? 146 GLU B O   1 
ATOM   4178 C  CB  . GLU B 1 137 ? -38.808 -48.150 -28.221 1.00 44.19 ? 146 GLU B CB  1 
ATOM   4179 C  CG  . GLU B 1 137 ? -37.771 -48.486 -29.313 1.00 51.78 ? 146 GLU B CG  1 
ATOM   4180 C  CD  . GLU B 1 137 ? -36.316 -48.203 -28.917 1.00 58.73 ? 146 GLU B CD  1 
ATOM   4181 O  OE1 . GLU B 1 137 ? -36.002 -48.107 -27.704 1.00 61.46 ? 146 GLU B OE1 1 
ATOM   4182 O  OE2 . GLU B 1 137 ? -35.483 -48.053 -29.832 1.00 60.26 ? 146 GLU B OE2 1 
ATOM   4183 N  N   . ASN B 1 138 ? -39.830 -46.035 -25.838 1.00 37.64 ? 147 ASN B N   1 
ATOM   4184 C  CA  . ASN B 1 138 ? -40.760 -45.707 -24.758 1.00 38.50 ? 147 ASN B CA  1 
ATOM   4185 C  C   . ASN B 1 138 ? -40.974 -44.198 -24.619 1.00 35.80 ? 147 ASN B C   1 
ATOM   4186 O  O   . ASN B 1 138 ? -41.435 -43.735 -23.584 1.00 37.33 ? 147 ASN B O   1 
ATOM   4187 C  CB  . ASN B 1 138 ? -40.248 -46.293 -23.429 1.00 38.62 ? 147 ASN B CB  1 
ATOM   4188 C  CG  . ASN B 1 138 ? -41.260 -46.159 -22.298 1.00 40.44 ? 147 ASN B CG  1 
ATOM   4189 O  OD1 . ASN B 1 138 ? -42.458 -46.379 -22.489 1.00 43.29 ? 147 ASN B OD1 1 
ATOM   4190 N  ND2 . ASN B 1 138 ? -40.783 -45.776 -21.122 1.00 41.83 ? 147 ASN B ND2 1 
ATOM   4191 N  N   . MET B 1 139 ? -40.657 -43.429 -25.656 1.00 35.15 ? 148 MET B N   1 
ATOM   4192 C  CA  . MET B 1 139 ? -40.801 -41.978 -25.602 1.00 34.83 ? 148 MET B CA  1 
ATOM   4193 C  C   . MET B 1 139 ? -41.494 -41.429 -26.847 1.00 33.18 ? 148 MET B C   1 
ATOM   4194 O  O   . MET B 1 139 ? -41.507 -42.072 -27.894 1.00 33.01 ? 148 MET B O   1 
ATOM   4195 C  CB  . MET B 1 139 ? -39.424 -41.329 -25.410 1.00 31.43 ? 148 MET B CB  1 
ATOM   4196 C  CG  . MET B 1 139 ? -38.834 -41.573 -24.027 1.00 34.87 ? 148 MET B CG  1 
ATOM   4197 S  SD  . MET B 1 139 ? -37.099 -41.150 -23.879 1.00 35.63 ? 148 MET B SD  1 
ATOM   4198 C  CE  . MET B 1 139 ? -37.242 -39.366 -23.799 1.00 33.31 ? 148 MET B CE  1 
ATOM   4199 N  N   A ASP B 1 140 ? -42.077 -40.243 -26.718 0.50 33.19 ? 149 ASP B N   1 
ATOM   4200 N  N   B ASP B 1 140 ? -42.109 -40.256 -26.688 0.50 32.93 ? 149 ASP B N   1 
ATOM   4201 C  CA  A ASP B 1 140 ? -42.547 -39.490 -27.881 0.50 32.96 ? 149 ASP B CA  1 
ATOM   4202 C  CA  B ASP B 1 140 ? -42.672 -39.467 -27.794 0.50 32.71 ? 149 ASP B CA  1 
ATOM   4203 C  C   A ASP B 1 140 ? -42.381 -37.993 -27.638 0.50 31.19 ? 149 ASP B C   1 
ATOM   4204 C  C   B ASP B 1 140 ? -42.268 -37.997 -27.636 0.50 30.66 ? 149 ASP B C   1 
ATOM   4205 O  O   A ASP B 1 140 ? -42.276 -37.544 -26.497 0.50 30.04 ? 149 ASP B O   1 
ATOM   4206 O  O   B ASP B 1 140 ? -41.860 -37.582 -26.555 0.50 28.44 ? 149 ASP B O   1 
ATOM   4207 C  CB  A ASP B 1 140 ? -44.012 -39.833 -28.197 0.50 34.30 ? 149 ASP B CB  1 
ATOM   4208 C  CB  B ASP B 1 140 ? -44.212 -39.567 -27.802 0.50 34.11 ? 149 ASP B CB  1 
ATOM   4209 C  CG  A ASP B 1 140 ? -44.383 -39.607 -29.672 0.50 34.09 ? 149 ASP B CG  1 
ATOM   4210 C  CG  B ASP B 1 140 ? -44.746 -40.621 -28.769 0.50 34.72 ? 149 ASP B CG  1 
ATOM   4211 O  OD1 A ASP B 1 140 ? -43.676 -38.872 -30.405 0.50 27.34 ? 149 ASP B OD1 1 
ATOM   4212 O  OD1 B ASP B 1 140 ? -44.218 -40.741 -29.895 0.50 38.27 ? 149 ASP B OD1 1 
ATOM   4213 O  OD2 A ASP B 1 140 ? -45.411 -40.172 -30.097 0.50 34.40 ? 149 ASP B OD2 1 
ATOM   4214 O  OD2 B ASP B 1 140 ? -45.724 -41.310 -28.408 0.50 33.57 ? 149 ASP B OD2 1 
ATOM   4215 N  N   . VAL B 1 141 ? -42.353 -37.235 -28.728 1.00 31.47 ? 150 VAL B N   1 
ATOM   4216 C  CA  . VAL B 1 141 ? -42.378 -35.761 -28.660 1.00 30.54 ? 150 VAL B CA  1 
ATOM   4217 C  C   . VAL B 1 141 ? -43.821 -35.302 -28.516 1.00 31.18 ? 150 VAL B C   1 
ATOM   4218 O  O   . VAL B 1 141 ? -44.752 -36.034 -28.854 1.00 31.13 ? 150 VAL B O   1 
ATOM   4219 C  CB  . VAL B 1 141 ? -41.734 -35.043 -29.878 1.00 29.54 ? 150 VAL B CB  1 
ATOM   4220 C  CG1 . VAL B 1 141 ? -40.265 -35.280 -29.883 1.00 36.53 ? 150 VAL B CG1 1 
ATOM   4221 C  CG2 . VAL B 1 141 ? -42.376 -35.445 -31.223 1.00 35.52 ? 150 VAL B CG2 1 
ATOM   4222 N  N   . LEU B 1 142 ? -43.994 -34.093 -27.996 1.00 29.68 ? 151 LEU B N   1 
ATOM   4223 C  CA  . LEU B 1 142 ? -45.318 -33.493 -27.884 1.00 30.75 ? 151 LEU B CA  1 
ATOM   4224 C  C   . LEU B 1 142 ? -45.755 -32.784 -29.172 1.00 31.43 ? 151 LEU B C   1 
ATOM   4225 O  O   . LEU B 1 142 ? -46.932 -32.842 -29.526 1.00 32.55 ? 151 LEU B O   1 
ATOM   4226 C  CB  . LEU B 1 142 ? -45.378 -32.540 -26.684 1.00 29.64 ? 151 LEU B CB  1 
ATOM   4227 C  CG  . LEU B 1 142 ? -44.957 -33.142 -25.334 1.00 27.77 ? 151 LEU B CG  1 
ATOM   4228 C  CD1 . LEU B 1 142 ? -45.067 -32.103 -24.245 1.00 29.07 ? 151 LEU B CD1 1 
ATOM   4229 C  CD2 . LEU B 1 142 ? -45.773 -34.377 -24.965 1.00 29.10 ? 151 LEU B CD2 1 
ATOM   4230 N  N   . PHE B 1 143 ? -44.824 -32.113 -29.859 1.00 30.58 ? 152 PHE B N   1 
ATOM   4231 C  CA  . PHE B 1 143 ? -45.153 -31.329 -31.063 1.00 29.28 ? 152 PHE B CA  1 
ATOM   4232 C  C   . PHE B 1 143 ? -44.129 -31.493 -32.197 1.00 28.83 ? 152 PHE B C   1 
ATOM   4233 O  O   . PHE B 1 143 ? -42.914 -31.596 -31.978 1.00 26.81 ? 152 PHE B O   1 
ATOM   4234 C  CB  . PHE B 1 143 ? -45.337 -29.839 -30.725 1.00 28.06 ? 152 PHE B CB  1 
ATOM   4235 C  CG  . PHE B 1 143 ? -46.247 -29.594 -29.558 1.00 26.79 ? 152 PHE B CG  1 
ATOM   4236 C  CD1 . PHE B 1 143 ? -47.634 -29.617 -29.715 1.00 30.57 ? 152 PHE B CD1 1 
ATOM   4237 C  CD2 . PHE B 1 143 ? -45.714 -29.384 -28.285 1.00 28.25 ? 152 PHE B CD2 1 
ATOM   4238 C  CE1 . PHE B 1 143 ? -48.482 -29.423 -28.619 1.00 28.49 ? 152 PHE B CE1 1 
ATOM   4239 C  CE2 . PHE B 1 143 ? -46.538 -29.185 -27.184 1.00 29.63 ? 152 PHE B CE2 1 
ATOM   4240 C  CZ  . PHE B 1 143 ? -47.931 -29.200 -27.346 1.00 33.20 ? 152 PHE B CZ  1 
ATOM   4241 N  N   . SER B 1 144 ? -44.669 -31.540 -33.408 1.00 28.82 ? 153 SER B N   1 
ATOM   4242 C  CA  . SER B 1 144 ? -43.919 -31.573 -34.650 1.00 28.03 ? 153 SER B CA  1 
ATOM   4243 C  C   . SER B 1 144 ? -44.438 -30.425 -35.512 1.00 27.06 ? 153 SER B C   1 
ATOM   4244 O  O   . SER B 1 144 ? -45.443 -29.803 -35.164 1.00 26.57 ? 153 SER B O   1 
ATOM   4245 C  CB  . SER B 1 144 ? -44.174 -32.908 -35.352 1.00 28.91 ? 153 SER B CB  1 
ATOM   4246 O  OG  . SER B 1 144 ? -45.544 -33.034 -35.692 1.00 34.36 ? 153 SER B OG  1 
ATOM   4247 N  N   . PHE B 1 145 ? -43.763 -30.160 -36.629 1.00 26.99 ? 154 PHE B N   1 
ATOM   4248 C  CA  . PHE B 1 145 ? -44.140 -29.079 -37.552 1.00 26.15 ? 154 PHE B CA  1 
ATOM   4249 C  C   . PHE B 1 145 ? -44.909 -29.600 -38.750 1.00 26.79 ? 154 PHE B C   1 
ATOM   4250 O  O   . PHE B 1 145 ? -46.015 -29.148 -39.023 1.00 26.60 ? 154 PHE B O   1 
ATOM   4251 C  CB  . PHE B 1 145 ? -42.895 -28.312 -38.001 1.00 28.24 ? 154 PHE B CB  1 
ATOM   4252 C  CG  . PHE B 1 145 ? -42.219 -27.605 -36.876 1.00 26.03 ? 154 PHE B CG  1 
ATOM   4253 C  CD1 . PHE B 1 145 ? -42.767 -26.431 -36.362 1.00 28.15 ? 154 PHE B CD1 1 
ATOM   4254 C  CD2 . PHE B 1 145 ? -41.072 -28.130 -36.286 1.00 27.64 ? 154 PHE B CD2 1 
ATOM   4255 C  CE1 . PHE B 1 145 ? -42.171 -25.778 -35.299 1.00 26.19 ? 154 PHE B CE1 1 
ATOM   4256 C  CE2 . PHE B 1 145 ? -40.471 -27.480 -35.225 1.00 28.94 ? 154 PHE B CE2 1 
ATOM   4257 C  CZ  . PHE B 1 145 ? -41.027 -26.302 -34.726 1.00 29.39 ? 154 PHE B CZ  1 
ATOM   4258 N  N   . ARG B 1 146 ? -44.313 -30.564 -39.441 1.00 26.02 ? 155 ARG B N   1 
ATOM   4259 C  CA  . ARG B 1 146 ? -44.881 -31.188 -40.631 1.00 27.81 ? 155 ARG B CA  1 
ATOM   4260 C  C   . ARG B 1 146 ? -44.786 -32.692 -40.493 1.00 29.30 ? 155 ARG B C   1 
ATOM   4261 O  O   . ARG B 1 146 ? -43.931 -33.201 -39.774 1.00 27.22 ? 155 ARG B O   1 
ATOM   4262 C  CB  . ARG B 1 146 ? -44.096 -30.779 -41.883 1.00 27.67 ? 155 ARG B CB  1 
ATOM   4263 C  CG  . ARG B 1 146 ? -43.878 -29.290 -42.055 1.00 31.98 ? 155 ARG B CG  1 
ATOM   4264 C  CD  . ARG B 1 146 ? -45.184 -28.538 -42.244 1.00 32.06 ? 155 ARG B CD  1 
ATOM   4265 N  NE  . ARG B 1 146 ? -45.809 -28.845 -43.523 1.00 31.71 ? 155 ARG B NE  1 
ATOM   4266 C  CZ  . ARG B 1 146 ? -45.405 -28.378 -44.705 1.00 40.56 ? 155 ARG B CZ  1 
ATOM   4267 N  NH1 . ARG B 1 146 ? -44.357 -27.567 -44.821 1.00 42.32 ? 155 ARG B NH1 1 
ATOM   4268 N  NH2 . ARG B 1 146 ? -46.058 -28.737 -45.799 1.00 44.08 ? 155 ARG B NH2 1 
ATOM   4269 N  N   . ASP B 1 147 ? -45.635 -33.412 -41.213 1.00 32.86 ? 156 ASP B N   1 
ATOM   4270 C  CA  . ASP B 1 147 ? -45.532 -34.868 -41.214 1.00 34.90 ? 156 ASP B CA  1 
ATOM   4271 C  C   . ASP B 1 147 ? -44.328 -35.278 -42.058 1.00 35.93 ? 156 ASP B C   1 
ATOM   4272 O  O   . ASP B 1 147 ? -44.071 -34.692 -43.108 1.00 34.95 ? 156 ASP B O   1 
ATOM   4273 C  CB  . ASP B 1 147 ? -46.818 -35.510 -41.714 1.00 37.52 ? 156 ASP B CB  1 
ATOM   4274 C  CG  . ASP B 1 147 ? -47.988 -35.293 -40.765 1.00 38.73 ? 156 ASP B CG  1 
ATOM   4275 O  OD1 . ASP B 1 147 ? -47.800 -35.311 -39.518 1.00 37.73 ? 156 ASP B OD1 1 
ATOM   4276 O  OD2 . ASP B 1 147 ? -49.109 -35.116 -41.282 1.00 41.13 ? 156 ASP B OD2 1 
ATOM   4277 N  N   . GLY B 1 148 ? -43.577 -36.262 -41.565 1.00 37.70 ? 157 GLY B N   1 
ATOM   4278 C  CA  . GLY B 1 148 ? -42.304 -36.652 -42.174 1.00 37.23 ? 157 GLY B CA  1 
ATOM   4279 C  C   . GLY B 1 148 ? -41.138 -35.690 -41.961 1.00 35.76 ? 157 GLY B C   1 
ATOM   4280 O  O   . GLY B 1 148 ? -40.107 -35.840 -42.622 1.00 36.14 ? 157 GLY B O   1 
ATOM   4281 N  N   . ASP B 1 149 ? -41.263 -34.719 -41.045 1.00 33.25 ? 158 ASP B N   1 
ATOM   4282 C  CA  . ASP B 1 149 ? -40.133 -33.803 -40.733 1.00 31.93 ? 158 ASP B CA  1 
ATOM   4283 C  C   . ASP B 1 149 ? -39.067 -34.410 -39.801 1.00 30.70 ? 158 ASP B C   1 
ATOM   4284 O  O   . ASP B 1 149 ? -38.071 -33.754 -39.510 1.00 29.03 ? 158 ASP B O   1 
ATOM   4285 C  CB  . ASP B 1 149 ? -40.614 -32.443 -40.187 1.00 31.24 ? 158 ASP B CB  1 
ATOM   4286 C  CG  . ASP B 1 149 ? -41.268 -32.530 -38.806 1.00 31.81 ? 158 ASP B CG  1 
ATOM   4287 O  OD1 . ASP B 1 149 ? -41.329 -33.621 -38.207 1.00 32.64 ? 158 ASP B OD1 1 
ATOM   4288 O  OD2 . ASP B 1 149 ? -41.754 -31.483 -38.330 1.00 30.39 ? 158 ASP B OD2 1 
ATOM   4289 N  N   . CYS B 1 150 ? -39.299 -35.636 -39.320 1.00 32.14 ? 159 CYS B N   1 
ATOM   4290 C  CA  . CYS B 1 150 ? -38.390 -36.349 -38.408 1.00 32.58 ? 159 CYS B CA  1 
ATOM   4291 C  C   . CYS B 1 150 ? -38.083 -35.584 -37.123 1.00 31.22 ? 159 CYS B C   1 
ATOM   4292 O  O   . CYS B 1 150 ? -36.967 -35.677 -36.579 1.00 29.15 ? 159 CYS B O   1 
ATOM   4293 C  CB  . CYS B 1 150 ? -37.078 -36.728 -39.122 1.00 33.56 ? 159 CYS B CB  1 
ATOM   4294 S  SG  . CYS B 1 150 ? -37.308 -37.815 -40.484 1.00 35.93 ? 159 CYS B SG  1 
ATOM   4295 N  N   . SER B 1 151 ? -39.066 -34.831 -36.632 1.00 30.79 ? 160 SER B N   1 
ATOM   4296 C  CA  . SER B 1 151 ? -38.864 -34.034 -35.426 1.00 29.95 ? 160 SER B CA  1 
ATOM   4297 C  C   . SER B 1 151 ? -38.791 -34.936 -34.191 1.00 28.97 ? 160 SER B C   1 
ATOM   4298 O  O   . SER B 1 151 ? -38.026 -34.652 -33.280 1.00 27.21 ? 160 SER B O   1 
ATOM   4299 C  CB  . SER B 1 151 ? -39.919 -32.914 -35.290 1.00 31.86 ? 160 SER B CB  1 
ATOM   4300 O  OG  . SER B 1 151 ? -41.228 -33.409 -35.237 1.00 37.20 ? 160 SER B OG  1 
ATOM   4301 N  N   . LYS B 1 152 ? -39.520 -36.058 -34.185 1.00 28.92 ? 161 LYS B N   1 
ATOM   4302 C  CA  . LYS B 1 152 ? -39.386 -37.030 -33.096 1.00 29.43 ? 161 LYS B CA  1 
ATOM   4303 C  C   . LYS B 1 152 ? -37.945 -37.559 -33.018 1.00 27.65 ? 161 LYS B C   1 
ATOM   4304 O  O   . LYS B 1 152 ? -37.306 -37.473 -31.969 1.00 23.02 ? 161 LYS B O   1 
ATOM   4305 C  CB  . LYS B 1 152 ? -40.382 -38.181 -33.247 1.00 31.41 ? 161 LYS B CB  1 
ATOM   4306 C  CG  . LYS B 1 152 ? -40.324 -39.226 -32.133 1.00 35.27 ? 161 LYS B CG  1 
ATOM   4307 C  CD  . LYS B 1 152 ? -41.309 -40.346 -32.412 1.00 36.68 ? 161 LYS B CD  1 
ATOM   4308 C  CE  . LYS B 1 152 ? -41.164 -41.488 -31.439 1.00 42.32 ? 161 LYS B CE  1 
ATOM   4309 N  NZ  . LYS B 1 152 ? -42.210 -42.553 -31.717 1.00 48.47 ? 161 LYS B NZ  1 
ATOM   4310 N  N   . GLY B 1 153 ? -37.451 -38.087 -34.134 1.00 26.92 ? 162 GLY B N   1 
ATOM   4311 C  CA  . GLY B 1 153 ? -36.062 -38.534 -34.248 1.00 27.77 ? 162 GLY B CA  1 
ATOM   4312 C  C   . GLY B 1 153 ? -35.050 -37.477 -33.817 1.00 26.76 ? 162 GLY B C   1 
ATOM   4313 O  O   . GLY B 1 153 ? -34.174 -37.750 -32.998 1.00 28.40 ? 162 GLY B O   1 
ATOM   4314 N  N   . PHE B 1 154 ? -35.181 -36.261 -34.338 1.00 25.81 ? 163 PHE B N   1 
ATOM   4315 C  CA  . PHE B 1 154 ? -34.213 -35.208 -34.041 1.00 24.99 ? 163 PHE B CA  1 
ATOM   4316 C  C   . PHE B 1 154 ? -34.290 -34.738 -32.582 1.00 25.68 ? 163 PHE B C   1 
ATOM   4317 O  O   . PHE B 1 154 ? -33.269 -34.702 -31.869 1.00 25.57 ? 163 PHE B O   1 
ATOM   4318 C  CB  . PHE B 1 154 ? -34.365 -34.018 -34.996 1.00 26.26 ? 163 PHE B CB  1 
ATOM   4319 C  CG  . PHE B 1 154 ? -33.402 -32.902 -34.702 1.00 26.10 ? 163 PHE B CG  1 
ATOM   4320 C  CD1 . PHE B 1 154 ? -32.030 -33.102 -34.867 1.00 27.78 ? 163 PHE B CD1 1 
ATOM   4321 C  CD2 . PHE B 1 154 ? -33.847 -31.685 -34.197 1.00 26.13 ? 163 PHE B CD2 1 
ATOM   4322 C  CE1 . PHE B 1 154 ? -31.117 -32.093 -34.551 1.00 27.02 ? 163 PHE B CE1 1 
ATOM   4323 C  CE2 . PHE B 1 154 ? -32.939 -30.664 -33.889 1.00 26.91 ? 163 PHE B CE2 1 
ATOM   4324 C  CZ  . PHE B 1 154 ? -31.567 -30.883 -34.068 1.00 26.55 ? 163 PHE B CZ  1 
ATOM   4325 N  N   . PHE B 1 155 ? -35.490 -34.383 -32.132 1.00 25.96 ? 164 PHE B N   1 
ATOM   4326 C  CA  . PHE B 1 155 ? -35.659 -33.876 -30.773 1.00 24.86 ? 164 PHE B CA  1 
ATOM   4327 C  C   . PHE B 1 155 ? -35.384 -34.945 -29.707 1.00 26.37 ? 164 PHE B C   1 
ATOM   4328 O  O   . PHE B 1 155 ? -34.772 -34.639 -28.677 1.00 22.11 ? 164 PHE B O   1 
ATOM   4329 C  CB  . PHE B 1 155 ? -37.059 -33.277 -30.551 1.00 25.60 ? 164 PHE B CB  1 
ATOM   4330 C  CG  . PHE B 1 155 ? -37.354 -32.035 -31.364 1.00 24.87 ? 164 PHE B CG  1 
ATOM   4331 C  CD1 . PHE B 1 155 ? -36.408 -31.009 -31.519 1.00 24.51 ? 164 PHE B CD1 1 
ATOM   4332 C  CD2 . PHE B 1 155 ? -38.613 -31.857 -31.937 1.00 27.82 ? 164 PHE B CD2 1 
ATOM   4333 C  CE1 . PHE B 1 155 ? -36.704 -29.855 -32.275 1.00 26.60 ? 164 PHE B CE1 1 
ATOM   4334 C  CE2 . PHE B 1 155 ? -38.914 -30.696 -32.680 1.00 26.75 ? 164 PHE B CE2 1 
ATOM   4335 C  CZ  . PHE B 1 155 ? -37.956 -29.696 -32.841 1.00 19.85 ? 164 PHE B CZ  1 
ATOM   4336 N  N   . LEU B 1 156 ? -35.824 -36.184 -29.938 1.00 25.07 ? 165 LEU B N   1 
ATOM   4337 C  CA  . LEU B 1 156 ? -35.623 -37.229 -28.924 1.00 27.66 ? 165 LEU B CA  1 
ATOM   4338 C  C   . LEU B 1 156 ? -34.207 -37.759 -28.882 1.00 25.64 ? 165 LEU B C   1 
ATOM   4339 O  O   . LEU B 1 156 ? -33.697 -38.001 -27.806 1.00 26.44 ? 165 LEU B O   1 
ATOM   4340 C  CB  . LEU B 1 156 ? -36.616 -38.378 -29.048 1.00 30.81 ? 165 LEU B CB  1 
ATOM   4341 C  CG  . LEU B 1 156 ? -38.090 -38.071 -28.761 1.00 35.50 ? 165 LEU B CG  1 
ATOM   4342 C  CD1 . LEU B 1 156 ? -38.851 -39.382 -28.729 1.00 39.44 ? 165 LEU B CD1 1 
ATOM   4343 C  CD2 . LEU B 1 156 ? -38.321 -37.298 -27.457 1.00 35.35 ? 165 LEU B CD2 1 
ATOM   4344 N  N   . VAL B 1 157 ? -33.557 -37.934 -30.024 1.00 26.53 ? 166 VAL B N   1 
ATOM   4345 C  CA  . VAL B 1 157 ? -32.143 -38.318 -29.988 1.00 26.84 ? 166 VAL B CA  1 
ATOM   4346 C  C   . VAL B 1 157 ? -31.338 -37.223 -29.285 1.00 25.42 ? 166 VAL B C   1 
ATOM   4347 O  O   . VAL B 1 157 ? -30.488 -37.534 -28.445 1.00 26.68 ? 166 VAL B O   1 
ATOM   4348 C  CB  . VAL B 1 157 ? -31.570 -38.673 -31.377 1.00 27.52 ? 166 VAL B CB  1 
ATOM   4349 C  CG1 . VAL B 1 157 ? -30.066 -38.893 -31.312 1.00 29.95 ? 166 VAL B CG1 1 
ATOM   4350 C  CG2 . VAL B 1 157 ? -32.247 -39.944 -31.915 1.00 30.71 ? 166 VAL B CG2 1 
ATOM   4351 N  N   . SER B 1 158 ? -31.621 -35.956 -29.603 1.00 24.47 ? 167 SER B N   1 
ATOM   4352 C  CA  . SER B 1 158 ? -30.985 -34.812 -28.916 1.00 22.67 ? 167 SER B CA  1 
ATOM   4353 C  C   . SER B 1 158 ? -31.185 -34.913 -27.415 1.00 23.13 ? 167 SER B C   1 
ATOM   4354 O  O   . SER B 1 158 ? -30.240 -34.761 -26.643 1.00 23.22 ? 167 SER B O   1 
ATOM   4355 C  CB  . SER B 1 158 ? -31.528 -33.470 -29.421 1.00 21.69 ? 167 SER B CB  1 
ATOM   4356 O  OG  . SER B 1 158 ? -31.179 -33.243 -30.776 1.00 20.52 ? 167 SER B OG  1 
ATOM   4357 N  N   . LEU B 1 159 ? -32.419 -35.199 -27.008 1.00 22.08 ? 168 LEU B N   1 
ATOM   4358 C  CA  . LEU B 1 159 ? -32.736 -35.361 -25.599 1.00 22.77 ? 168 LEU B CA  1 
ATOM   4359 C  C   . LEU B 1 159 ? -32.019 -36.567 -24.950 1.00 23.33 ? 168 LEU B C   1 
ATOM   4360 O  O   . LEU B 1 159 ? -31.508 -36.464 -23.835 1.00 22.50 ? 168 LEU B O   1 
ATOM   4361 C  CB  . LEU B 1 159 ? -34.244 -35.467 -25.407 1.00 21.80 ? 168 LEU B CB  1 
ATOM   4362 C  CG  . LEU B 1 159 ? -34.751 -35.754 -23.999 1.00 25.71 ? 168 LEU B CG  1 
ATOM   4363 C  CD1 . LEU B 1 159 ? -34.373 -34.654 -23.006 1.00 25.29 ? 168 LEU B CD1 1 
ATOM   4364 C  CD2 . LEU B 1 159 ? -36.247 -35.947 -24.068 1.00 27.04 ? 168 LEU B CD2 1 
ATOM   4365 N  N   . LEU B 1 160 ? -31.990 -37.702 -25.635 1.00 23.35 ? 169 LEU B N   1 
ATOM   4366 C  CA  . LEU B 1 160 ? -31.280 -38.885 -25.122 1.00 23.64 ? 169 LEU B CA  1 
ATOM   4367 C  C   . LEU B 1 160 ? -29.771 -38.619 -24.938 1.00 23.81 ? 169 LEU B C   1 
ATOM   4368 O  O   . LEU B 1 160 ? -29.181 -39.027 -23.930 1.00 25.95 ? 169 LEU B O   1 
ATOM   4369 C  CB  . LEU B 1 160 ? -31.546 -40.098 -26.025 1.00 26.48 ? 169 LEU B CB  1 
ATOM   4370 C  CG  . LEU B 1 160 ? -33.005 -40.605 -25.966 1.00 27.95 ? 169 LEU B CG  1 
ATOM   4371 C  CD1 . LEU B 1 160 ? -33.330 -41.541 -27.125 1.00 32.15 ? 169 LEU B CD1 1 
ATOM   4372 C  CD2 . LEU B 1 160 ? -33.269 -41.303 -24.639 1.00 32.91 ? 169 LEU B CD2 1 
ATOM   4373 N  N   . VAL B 1 161 ? -29.166 -37.909 -25.885 1.00 23.31 ? 170 VAL B N   1 
ATOM   4374 C  CA  . VAL B 1 161 ? -27.748 -37.510 -25.785 1.00 25.55 ? 170 VAL B CA  1 
ATOM   4375 C  C   . VAL B 1 161 ? -27.559 -36.571 -24.597 1.00 27.77 ? 170 VAL B C   1 
ATOM   4376 O  O   . VAL B 1 161 ? -26.645 -36.756 -23.787 1.00 25.42 ? 170 VAL B O   1 
ATOM   4377 C  CB  . VAL B 1 161 ? -27.235 -36.844 -27.086 1.00 25.89 ? 170 VAL B CB  1 
ATOM   4378 C  CG1 . VAL B 1 161 ? -25.807 -36.302 -26.924 1.00 31.46 ? 170 VAL B CG1 1 
ATOM   4379 C  CG2 . VAL B 1 161 ? -27.253 -37.828 -28.211 1.00 22.64 ? 170 VAL B CG2 1 
ATOM   4380 N  N   . GLU B 1 162 ? -28.455 -35.594 -24.486 1.00 27.69 ? 171 GLU B N   1 
ATOM   4381 C  CA  . GLU B 1 162 ? -28.487 -34.671 -23.354 1.00 28.58 ? 171 GLU B CA  1 
ATOM   4382 C  C   . GLU B 1 162 ? -28.512 -35.423 -22.010 1.00 30.70 ? 171 GLU B C   1 
ATOM   4383 O  O   . GLU B 1 162 ? -27.732 -35.113 -21.105 1.00 30.77 ? 171 GLU B O   1 
ATOM   4384 C  CB  . GLU B 1 162 ? -29.704 -33.741 -23.494 1.00 28.69 ? 171 GLU B CB  1 
ATOM   4385 C  CG  . GLU B 1 162 ? -29.967 -32.785 -22.341 1.00 27.58 ? 171 GLU B CG  1 
ATOM   4386 C  CD  . GLU B 1 162 ? -29.163 -31.497 -22.393 1.00 25.68 ? 171 GLU B CD  1 
ATOM   4387 O  OE1 . GLU B 1 162 ? -28.644 -31.127 -23.470 1.00 23.50 ? 171 GLU B OE1 1 
ATOM   4388 O  OE2 . GLU B 1 162 ? -29.056 -30.846 -21.337 1.00 27.23 ? 171 GLU B OE2 1 
ATOM   4389 N  N   . ILE B 1 163 ? -29.410 -36.397 -21.898 1.00 28.80 ? 172 ILE B N   1 
ATOM   4390 C  CA  . ILE B 1 163 ? -29.589 -37.181 -20.674 1.00 29.41 ? 172 ILE B CA  1 
ATOM   4391 C  C   . ILE B 1 163 ? -28.392 -38.092 -20.375 1.00 28.20 ? 172 ILE B C   1 
ATOM   4392 O  O   . ILE B 1 163 ? -28.003 -38.229 -19.221 1.00 26.92 ? 172 ILE B O   1 
ATOM   4393 C  CB  . ILE B 1 163 ? -30.901 -38.015 -20.728 1.00 30.95 ? 172 ILE B CB  1 
ATOM   4394 C  CG1 . ILE B 1 163 ? -32.120 -37.073 -20.704 1.00 32.34 ? 172 ILE B CG1 1 
ATOM   4395 C  CG2 . ILE B 1 163 ? -30.996 -39.016 -19.552 1.00 33.37 ? 172 ILE B CG2 1 
ATOM   4396 C  CD1 . ILE B 1 163 ? -33.422 -37.729 -21.187 1.00 33.43 ? 172 ILE B CD1 1 
ATOM   4397 N  N   . ALA B 1 164 ? -27.814 -38.702 -21.408 1.00 27.93 ? 173 ALA B N   1 
ATOM   4398 C  CA  . ALA B 1 164 ? -26.642 -39.559 -21.228 1.00 30.81 ? 173 ALA B CA  1 
ATOM   4399 C  C   . ALA B 1 164 ? -25.488 -38.737 -20.661 1.00 29.58 ? 173 ALA B C   1 
ATOM   4400 O  O   . ALA B 1 164 ? -24.885 -39.113 -19.655 1.00 28.58 ? 173 ALA B O   1 
ATOM   4401 C  CB  . ALA B 1 164 ? -26.248 -40.199 -22.539 1.00 29.82 ? 173 ALA B CB  1 
ATOM   4402 N  N   . ALA B 1 165 ? -25.221 -37.598 -21.298 1.00 30.23 ? 174 ALA B N   1 
ATOM   4403 C  CA  . ALA B 1 165 ? -24.187 -36.661 -20.850 1.00 31.45 ? 174 ALA B CA  1 
ATOM   4404 C  C   . ALA B 1 165 ? -24.468 -36.117 -19.448 1.00 33.12 ? 174 ALA B C   1 
ATOM   4405 O  O   . ALA B 1 165 ? -23.549 -35.956 -18.648 1.00 35.76 ? 174 ALA B O   1 
ATOM   4406 C  CB  . ALA B 1 165 ? -24.066 -35.512 -21.842 1.00 32.95 ? 174 ALA B CB  1 
ATOM   4407 N  N   . ALA B 1 166 ? -25.742 -35.863 -19.153 1.00 34.29 ? 175 ALA B N   1 
ATOM   4408 C  CA  . ALA B 1 166 ? -26.158 -35.266 -17.878 1.00 36.03 ? 175 ALA B CA  1 
ATOM   4409 C  C   . ALA B 1 166 ? -26.022 -36.162 -16.653 1.00 37.92 ? 175 ALA B C   1 
ATOM   4410 O  O   . ALA B 1 166 ? -26.076 -35.661 -15.520 1.00 37.10 ? 175 ALA B O   1 
ATOM   4411 C  CB  . ALA B 1 166 ? -27.579 -34.790 -17.972 1.00 39.16 ? 175 ALA B CB  1 
ATOM   4412 N  N   . SER B 1 167 ? -25.870 -37.469 -16.867 1.00 35.67 ? 176 SER B N   1 
ATOM   4413 C  CA  . SER B 1 167 ? -25.542 -38.402 -15.785 1.00 36.63 ? 176 SER B CA  1 
ATOM   4414 C  C   . SER B 1 167 ? -24.241 -38.043 -15.048 1.00 34.77 ? 176 SER B C   1 
ATOM   4415 O  O   . SER B 1 167 ? -24.100 -38.339 -13.863 1.00 34.53 ? 176 SER B O   1 
ATOM   4416 C  CB  . SER B 1 167 ? -25.448 -39.833 -16.327 1.00 39.52 ? 176 SER B CB  1 
ATOM   4417 O  OG  . SER B 1 167 ? -26.689 -40.232 -16.895 1.00 47.05 ? 176 SER B OG  1 
ATOM   4418 N  N   . ALA B 1 168 ? -23.312 -37.402 -15.752 1.00 31.98 ? 177 ALA B N   1 
ATOM   4419 C  CA  . ALA B 1 168 ? -22.062 -36.908 -15.159 1.00 33.95 ? 177 ALA B CA  1 
ATOM   4420 C  C   . ALA B 1 168 ? -22.204 -35.628 -14.315 1.00 34.16 ? 177 ALA B C   1 
ATOM   4421 O  O   . ALA B 1 168 ? -21.306 -35.330 -13.522 1.00 30.67 ? 177 ALA B O   1 
ATOM   4422 C  CB  . ALA B 1 168 ? -21.019 -36.700 -16.245 1.00 32.29 ? 177 ALA B CB  1 
ATOM   4423 N  N   . ILE B 1 169 ? -23.302 -34.879 -14.487 1.00 33.24 ? 178 ILE B N   1 
ATOM   4424 C  CA  . ILE B 1 169 ? -23.499 -33.582 -13.793 1.00 34.24 ? 178 ILE B CA  1 
ATOM   4425 C  C   . ILE B 1 169 ? -23.468 -33.727 -12.278 1.00 37.16 ? 178 ILE B C   1 
ATOM   4426 O  O   . ILE B 1 169 ? -22.885 -32.886 -11.585 1.00 37.77 ? 178 ILE B O   1 
ATOM   4427 C  CB  . ILE B 1 169 ? -24.840 -32.888 -14.199 1.00 34.68 ? 178 ILE B CB  1 
ATOM   4428 C  CG1 . ILE B 1 169 ? -24.793 -32.438 -15.659 1.00 31.61 ? 178 ILE B CG1 1 
ATOM   4429 C  CG2 . ILE B 1 169 ? -25.147 -31.664 -13.315 1.00 38.17 ? 178 ILE B CG2 1 
ATOM   4430 C  CD1 . ILE B 1 169 ? -26.188 -32.216 -16.220 0.00 32.30 ? 178 ILE B CD1 1 
ATOM   4431 N  N   . LYS B 1 170 ? -24.094 -34.791 -11.769 1.00 35.90 ? 179 LYS B N   1 
ATOM   4432 C  CA  . LYS B 1 170 ? -24.104 -35.056 -10.330 1.00 38.35 ? 179 LYS B CA  1 
ATOM   4433 C  C   . LYS B 1 170 ? -22.723 -35.311 -9.716  1.00 38.32 ? 179 LYS B C   1 
ATOM   4434 O  O   . LYS B 1 170 ? -22.586 -35.260 -8.499  1.00 41.61 ? 179 LYS B O   1 
ATOM   4435 C  CB  . LYS B 1 170 ? -25.020 -36.239 -10.000 1.00 39.98 ? 179 LYS B CB  1 
ATOM   4436 C  CG  . LYS B 1 170 ? -24.555 -37.593 -10.557 1.00 39.67 ? 179 LYS B CG  1 
ATOM   4437 C  CD  . LYS B 1 170 ? -25.418 -38.754 -10.058 1.00 43.63 ? 179 LYS B CD  1 
ATOM   4438 C  CE  . LYS B 1 170 ? -26.870 -38.651 -10.520 1.00 43.76 ? 179 LYS B CE  1 
ATOM   4439 N  NZ  . LYS B 1 170 ? -27.001 -38.467 -11.990 1.00 44.26 ? 179 LYS B NZ  1 
ATOM   4440 N  N   . VAL B 1 171 ? -21.731 -35.605 -10.554 1.00 36.42 ? 180 VAL B N   1 
ATOM   4441 C  CA  . VAL B 1 171 ? -20.351 -35.838 -10.123 1.00 38.77 ? 180 VAL B CA  1 
ATOM   4442 C  C   . VAL B 1 171 ? -19.616 -34.512 -9.882  1.00 37.88 ? 180 VAL B C   1 
ATOM   4443 O  O   . VAL B 1 171 ? -18.603 -34.482 -9.186  1.00 38.97 ? 180 VAL B O   1 
ATOM   4444 C  CB  . VAL B 1 171 ? -19.574 -36.712 -11.174 1.00 38.25 ? 180 VAL B CB  1 
ATOM   4445 C  CG1 . VAL B 1 171 ? -18.189 -37.064 -10.696 1.00 41.43 ? 180 VAL B CG1 1 
ATOM   4446 C  CG2 . VAL B 1 171 ? -20.340 -38.005 -11.489 1.00 39.91 ? 180 VAL B CG2 1 
ATOM   4447 N  N   . ILE B 1 172 ? -20.126 -33.417 -10.438 1.00 38.34 ? 181 ILE B N   1 
ATOM   4448 C  CA  . ILE B 1 172 ? -19.428 -32.122 -10.384 1.00 39.11 ? 181 ILE B CA  1 
ATOM   4449 C  C   . ILE B 1 172 ? -19.105 -31.638 -8.956  1.00 40.47 ? 181 ILE B C   1 
ATOM   4450 O  O   . ILE B 1 172 ? -17.994 -31.179 -8.724  1.00 41.66 ? 181 ILE B O   1 
ATOM   4451 C  CB  . ILE B 1 172 ? -20.184 -31.028 -11.208 1.00 38.53 ? 181 ILE B CB  1 
ATOM   4452 C  CG1 . ILE B 1 172 ? -20.083 -31.352 -12.701 1.00 37.21 ? 181 ILE B CG1 1 
ATOM   4453 C  CG2 . ILE B 1 172 ? -19.620 -29.612 -10.939 1.00 37.67 ? 181 ILE B CG2 1 
ATOM   4454 C  CD1 . ILE B 1 172 ? -21.039 -30.582 -13.592 1.00 37.93 ? 181 ILE B CD1 1 
ATOM   4455 N  N   . PRO B 1 173 ? -20.071 -31.716 -8.011  1.00 42.84 ? 182 PRO B N   1 
ATOM   4456 C  CA  . PRO B 1 173 ? -19.769 -31.351 -6.623  1.00 44.47 ? 182 PRO B CA  1 
ATOM   4457 C  C   . PRO B 1 173 ? -18.728 -32.251 -5.946  1.00 45.31 ? 182 PRO B C   1 
ATOM   4458 O  O   . PRO B 1 173 ? -18.007 -31.784 -5.070  1.00 45.72 ? 182 PRO B O   1 
ATOM   4459 C  CB  . PRO B 1 173 ? -21.126 -31.485 -5.919  1.00 45.76 ? 182 PRO B CB  1 
ATOM   4460 C  CG  . PRO B 1 173 ? -22.121 -31.435 -6.994  1.00 44.94 ? 182 PRO B CG  1 
ATOM   4461 C  CD  . PRO B 1 173 ? -21.487 -32.098 -8.151  1.00 43.33 ? 182 PRO B CD  1 
ATOM   4462 N  N   . THR B 1 174 ? -18.674 -33.526 -6.342  1.00 44.40 ? 183 THR B N   1 
ATOM   4463 C  CA  . THR B 1 174 ? -17.591 -34.423 -5.936  1.00 44.20 ? 183 THR B CA  1 
ATOM   4464 C  C   . THR B 1 174 ? -16.243 -33.905 -6.445  1.00 41.23 ? 183 THR B C   1 
ATOM   4465 O  O   . THR B 1 174 ? -15.266 -33.918 -5.707  1.00 43.08 ? 183 THR B O   1 
ATOM   4466 C  CB  . THR B 1 174 ? -17.800 -35.878 -6.448  1.00 44.26 ? 183 THR B CB  1 
ATOM   4467 O  OG1 . THR B 1 174 ? -19.123 -36.316 -6.125  1.00 47.42 ? 183 THR B OG1 1 
ATOM   4468 C  CG2 . THR B 1 174 ? -16.796 -36.834 -5.813  1.00 45.28 ? 183 THR B CG2 1 
ATOM   4469 N  N   . VAL B 1 175 ? -16.202 -33.448 -7.693  1.00 38.86 ? 184 VAL B N   1 
ATOM   4470 C  CA  . VAL B 1 175 ? -14.960 -32.934 -8.281  1.00 39.35 ? 184 VAL B CA  1 
ATOM   4471 C  C   . VAL B 1 175 ? -14.406 -31.781 -7.439  1.00 40.02 ? 184 VAL B C   1 
ATOM   4472 O  O   . VAL B 1 175 ? -13.250 -31.840 -6.998  1.00 34.01 ? 184 VAL B O   1 
ATOM   4473 C  CB  . VAL B 1 175 ? -15.142 -32.540 -9.771  1.00 36.67 ? 184 VAL B CB  1 
ATOM   4474 C  CG1 . VAL B 1 175 ? -13.941 -31.739 -10.313 1.00 37.70 ? 184 VAL B CG1 1 
ATOM   4475 C  CG2 . VAL B 1 175 ? -15.359 -33.793 -10.613 1.00 33.92 ? 184 VAL B CG2 1 
ATOM   4476 N  N   . PHE B 1 176 ? -15.241 -30.770 -7.183  1.00 39.46 ? 185 PHE B N   1 
ATOM   4477 C  CA  . PHE B 1 176 ? -14.809 -29.595 -6.414  1.00 42.00 ? 185 PHE B CA  1 
ATOM   4478 C  C   . PHE B 1 176 ? -14.538 -29.883 -4.944  1.00 43.53 ? 185 PHE B C   1 
ATOM   4479 O  O   . PHE B 1 176 ? -13.604 -29.323 -4.375  1.00 46.17 ? 185 PHE B O   1 
ATOM   4480 C  CB  . PHE B 1 176 ? -15.818 -28.441 -6.541  1.00 44.07 ? 185 PHE B CB  1 
ATOM   4481 C  CG  . PHE B 1 176 ? -15.942 -27.905 -7.935  1.00 43.15 ? 185 PHE B CG  1 
ATOM   4482 C  CD1 . PHE B 1 176 ? -14.818 -27.483 -8.640  1.00 41.43 ? 185 PHE B CD1 1 
ATOM   4483 C  CD2 . PHE B 1 176 ? -17.189 -27.814 -8.550  1.00 47.96 ? 185 PHE B CD2 1 
ATOM   4484 C  CE1 . PHE B 1 176 ? -14.930 -26.992 -9.938  1.00 44.11 ? 185 PHE B CE1 1 
ATOM   4485 C  CE2 . PHE B 1 176 ? -17.309 -27.313 -9.839  1.00 44.59 ? 185 PHE B CE2 1 
ATOM   4486 C  CZ  . PHE B 1 176 ? -16.179 -26.905 -10.539 1.00 44.11 ? 185 PHE B CZ  1 
ATOM   4487 N  N   . LYS B 1 177 ? -15.354 -30.740 -4.332  1.00 44.39 ? 186 LYS B N   1 
ATOM   4488 C  CA  . LYS B 1 177 ? -15.109 -31.193 -2.959  1.00 46.94 ? 186 LYS B CA  1 
ATOM   4489 C  C   . LYS B 1 177 ? -13.802 -31.985 -2.867  1.00 46.17 ? 186 LYS B C   1 
ATOM   4490 O  O   . LYS B 1 177 ? -13.043 -31.809 -1.922  1.00 46.81 ? 186 LYS B O   1 
ATOM   4491 C  CB  . LYS B 1 177 ? -16.276 -32.044 -2.448  1.00 48.48 ? 186 LYS B CB  1 
ATOM   4492 C  CG  . LYS B 1 177 ? -16.138 -32.498 -1.004  1.00 52.87 ? 186 LYS B CG  1 
ATOM   4493 C  CD  . LYS B 1 177 ? -17.456 -33.025 -0.456  1.00 55.40 ? 186 LYS B CD  1 
ATOM   4494 C  CE  . LYS B 1 177 ? -17.334 -33.397 1.009   0.00 57.37 ? 186 LYS B CE  1 
ATOM   4495 N  NZ  . LYS B 1 177 ? -18.617 -33.909 1.565   0.00 58.66 ? 186 LYS B NZ  1 
ATOM   4496 N  N   . ALA B 1 178 ? -13.562 -32.856 -3.851  1.00 44.56 ? 187 ALA B N   1 
ATOM   4497 C  CA  . ALA B 1 178 ? -12.319 -33.630 -3.937  1.00 44.19 ? 187 ALA B CA  1 
ATOM   4498 C  C   . ALA B 1 178 ? -11.110 -32.715 -4.059  1.00 43.56 ? 187 ALA B C   1 
ATOM   4499 O  O   . ALA B 1 178 ? -10.110 -32.908 -3.361  1.00 43.72 ? 187 ALA B O   1 
ATOM   4500 C  CB  . ALA B 1 178 ? -12.363 -34.612 -5.110  1.00 42.64 ? 187 ALA B CB  1 
ATOM   4501 N  N   . MET B 1 179 ? -11.214 -31.708 -4.924  1.00 41.86 ? 188 MET B N   1 
ATOM   4502 C  CA  . MET B 1 179 ? -10.149 -30.715 -5.073  1.00 45.25 ? 188 MET B CA  1 
ATOM   4503 C  C   . MET B 1 179 ? -9.892  -29.911 -3.801  1.00 47.39 ? 188 MET B C   1 
ATOM   4504 O  O   . MET B 1 179 ? -8.759  -29.862 -3.321  1.00 47.96 ? 188 MET B O   1 
ATOM   4505 C  CB  . MET B 1 179 ? -10.459 -29.760 -6.211  1.00 44.01 ? 188 MET B CB  1 
ATOM   4506 C  CG  . MET B 1 179 ? -10.113 -30.317 -7.559  1.00 44.46 ? 188 MET B CG  1 
ATOM   4507 S  SD  . MET B 1 179 ? -10.624 -29.223 -8.880  1.00 47.98 ? 188 MET B SD  1 
ATOM   4508 C  CE  . MET B 1 179 ? -9.853  -27.674 -8.435  1.00 50.96 ? 188 MET B CE  1 
ATOM   4509 N  N   . GLN B 1 180 ? -10.946 -29.291 -3.268  1.00 49.42 ? 189 GLN B N   1 
ATOM   4510 C  CA  . GLN B 1 180 ? -10.854 -28.474 -2.050  1.00 51.41 ? 189 GLN B CA  1 
ATOM   4511 C  C   . GLN B 1 180 ? -10.257 -29.267 -0.880  1.00 53.88 ? 189 GLN B C   1 
ATOM   4512 O  O   . GLN B 1 180 ? -9.407  -28.750 -0.148  1.00 55.48 ? 189 GLN B O   1 
ATOM   4513 C  CB  . GLN B 1 180 ? -12.234 -27.920 -1.664  1.00 52.36 ? 189 GLN B CB  1 
ATOM   4514 C  CG  . GLN B 1 180 ? -12.207 -26.829 -0.589  1.00 56.44 ? 189 GLN B CG  1 
ATOM   4515 C  CD  . GLN B 1 180 ? -13.588 -26.341 -0.180  0.00 55.45 ? 189 GLN B CD  1 
ATOM   4516 O  OE1 . GLN B 1 180 ? -13.924 -26.283 1.003   0.00 57.88 ? 189 GLN B OE1 1 
ATOM   4517 N  NE2 . GLN B 1 180 ? -14.399 -25.987 -1.172  0.00 54.05 ? 189 GLN B NE2 1 
ATOM   4518 N  N   . MET B 1 181 ? -10.697 -30.519 -0.732  1.00 53.03 ? 190 MET B N   1 
ATOM   4519 C  CA  . MET B 1 181 ? -10.208 -31.423 0.310   1.00 55.58 ? 190 MET B CA  1 
ATOM   4520 C  C   . MET B 1 181 ? -8.924  -32.182 -0.047  1.00 54.95 ? 190 MET B C   1 
ATOM   4521 O  O   . MET B 1 181 ? -8.450  -32.969 0.775   1.00 55.48 ? 190 MET B O   1 
ATOM   4522 C  CB  . MET B 1 181 ? -11.300 -32.443 0.678   1.00 57.72 ? 190 MET B CB  1 
ATOM   4523 C  CG  . MET B 1 181 ? -12.573 -31.845 1.265   1.00 63.39 ? 190 MET B CG  1 
ATOM   4524 S  SD  . MET B 1 181 ? -12.280 -30.934 2.790   1.00 78.35 ? 190 MET B SD  1 
ATOM   4525 C  CE  . MET B 1 181 ? -12.263 -29.246 2.182   1.00 79.20 ? 190 MET B CE  1 
ATOM   4526 N  N   . GLN B 1 182 ? -8.363  -31.953 -1.241  1.00 53.04 ? 191 GLN B N   1 
ATOM   4527 C  CA  . GLN B 1 182 ? -7.185  -32.688 -1.732  1.00 52.58 ? 191 GLN B CA  1 
ATOM   4528 C  C   . GLN B 1 182 ? -7.418  -34.197 -1.601  1.00 51.73 ? 191 GLN B C   1 
ATOM   4529 O  O   . GLN B 1 182 ? -6.741  -34.870 -0.828  1.00 54.98 ? 191 GLN B O   1 
ATOM   4530 C  CB  . GLN B 1 182 ? -5.902  -32.258 -0.986  1.00 55.68 ? 191 GLN B CB  1 
ATOM   4531 C  CG  . GLN B 1 182 ? -5.454  -30.804 -1.230  1.00 60.30 ? 191 GLN B CG  1 
ATOM   4532 C  CD  . GLN B 1 182 ? -4.620  -30.606 -2.502  1.00 63.71 ? 191 GLN B CD  1 
ATOM   4533 O  OE1 . GLN B 1 182 ? -3.881  -31.498 -2.935  1.00 69.71 ? 191 GLN B OE1 1 
ATOM   4534 N  NE2 . GLN B 1 182 ? -4.720  -29.416 -3.089  1.00 60.97 ? 191 GLN B NE2 1 
ATOM   4535 N  N   . GLU B 1 183 ? -8.428  -34.690 -2.315  1.00 48.63 ? 192 GLU B N   1 
ATOM   4536 C  CA  . GLU B 1 183 ? -8.773  -36.111 -2.361  1.00 47.93 ? 192 GLU B CA  1 
ATOM   4537 C  C   . GLU B 1 183 ? -8.508  -36.618 -3.775  1.00 44.51 ? 192 GLU B C   1 
ATOM   4538 O  O   . GLU B 1 183 ? -9.397  -36.621 -4.628  1.00 42.09 ? 192 GLU B O   1 
ATOM   4539 C  CB  . GLU B 1 183 ? -10.233 -36.326 -1.958  1.00 48.62 ? 192 GLU B CB  1 
ATOM   4540 C  CG  . GLU B 1 183 ? -10.507 -36.090 -0.472  1.00 57.05 ? 192 GLU B CG  1 
ATOM   4541 C  CD  . GLU B 1 183 ? -9.949  -37.189 0.434   1.00 64.22 ? 192 GLU B CD  1 
ATOM   4542 O  OE1 . GLU B 1 183 ? -9.957  -38.373 0.032   1.00 69.38 ? 192 GLU B OE1 1 
ATOM   4543 O  OE2 . GLU B 1 183 ? -9.505  -36.867 1.558   1.00 69.05 ? 192 GLU B OE2 1 
ATOM   4544 N  N   . ARG B 1 184 ? -7.265  -37.041 -4.002  1.00 44.04 ? 193 ARG B N   1 
ATOM   4545 C  CA  . ARG B 1 184 ? -6.784  -37.442 -5.322  1.00 41.73 ? 193 ARG B CA  1 
ATOM   4546 C  C   . ARG B 1 184 ? -7.548  -38.628 -5.903  1.00 39.33 ? 193 ARG B C   1 
ATOM   4547 O  O   . ARG B 1 184 ? -7.939  -38.592 -7.068  1.00 35.37 ? 193 ARG B O   1 
ATOM   4548 C  CB  . ARG B 1 184 ? -5.283  -37.760 -5.258  1.00 43.86 ? 193 ARG B CB  1 
ATOM   4549 C  CG  . ARG B 1 184 ? -4.653  -38.239 -6.574  1.00 41.92 ? 193 ARG B CG  1 
ATOM   4550 C  CD  . ARG B 1 184 ? -4.699  -39.764 -6.734  1.00 40.41 ? 193 ARG B CD  1 
ATOM   4551 N  NE  . ARG B 1 184 ? -3.884  -40.209 -7.853  1.00 42.24 ? 193 ARG B NE  1 
ATOM   4552 C  CZ  . ARG B 1 184 ? -3.868  -41.441 -8.356  1.00 42.46 ? 193 ARG B CZ  1 
ATOM   4553 N  NH1 . ARG B 1 184 ? -4.644  -42.408 -7.869  1.00 47.56 ? 193 ARG B NH1 1 
ATOM   4554 N  NH2 . ARG B 1 184 ? -3.072  -41.708 -9.380  1.00 42.01 ? 193 ARG B NH2 1 
ATOM   4555 N  N   . ASP B 1 185 ? -7.717  -39.683 -5.102  1.00 40.52 ? 194 ASP B N   1 
ATOM   4556 C  CA  . ASP B 1 185 ? -8.405  -40.909 -5.549  1.00 39.93 ? 194 ASP B CA  1 
ATOM   4557 C  C   . ASP B 1 185 ? -9.872  -40.638 -5.873  1.00 38.89 ? 194 ASP B C   1 
ATOM   4558 O  O   . ASP B 1 185 ? -10.382 -41.122 -6.881  1.00 35.85 ? 194 ASP B O   1 
ATOM   4559 C  CB  . ASP B 1 185 ? -8.295  -42.037 -4.505  1.00 42.90 ? 194 ASP B CB  1 
ATOM   4560 C  CG  . ASP B 1 185 ? -6.853  -42.423 -4.201  1.00 41.84 ? 194 ASP B CG  1 
ATOM   4561 O  OD1 . ASP B 1 185 ? -5.962  -42.129 -5.015  1.00 44.20 ? 194 ASP B OD1 1 
ATOM   4562 O  OD2 . ASP B 1 185 ? -6.605  -43.019 -3.140  1.00 43.44 ? 194 ASP B OD2 1 
ATOM   4563 N  N   . THR B 1 186 ? -10.532 -39.852 -5.022  1.00 39.30 ? 195 THR B N   1 
ATOM   4564 C  CA  . THR B 1 186 ? -11.910 -39.417 -5.268  1.00 37.86 ? 195 THR B CA  1 
ATOM   4565 C  C   . THR B 1 186 ? -12.032 -38.597 -6.560  1.00 34.48 ? 195 THR B C   1 
ATOM   4566 O  O   . THR B 1 186 ? -12.909 -38.872 -7.386  1.00 33.08 ? 195 THR B O   1 
ATOM   4567 C  CB  . THR B 1 186 ? -12.457 -38.610 -4.071  1.00 38.47 ? 195 THR B CB  1 
ATOM   4568 O  OG1 . THR B 1 186 ? -12.342 -39.402 -2.882  1.00 44.71 ? 195 THR B OG1 1 
ATOM   4569 C  CG2 . THR B 1 186 ? -13.928 -38.213 -4.286  1.00 40.50 ? 195 THR B CG2 1 
ATOM   4570 N  N   . LEU B 1 187 ? -11.158 -37.604 -6.730  1.00 33.51 ? 196 LEU B N   1 
ATOM   4571 C  CA  . LEU B 1 187 ? -11.140 -36.781 -7.954  1.00 33.00 ? 196 LEU B CA  1 
ATOM   4572 C  C   . LEU B 1 187 ? -10.917 -37.625 -9.208  1.00 33.13 ? 196 LEU B C   1 
ATOM   4573 O  O   . LEU B 1 187 ? -11.603 -37.440 -10.215 1.00 32.19 ? 196 LEU B O   1 
ATOM   4574 C  CB  . LEU B 1 187 ? -10.064 -35.682 -7.887  1.00 32.42 ? 196 LEU B CB  1 
ATOM   4575 C  CG  . LEU B 1 187 ? -9.857  -34.815 -9.145  1.00 27.25 ? 196 LEU B CG  1 
ATOM   4576 C  CD1 . LEU B 1 187 ? -11.124 -34.108 -9.581  1.00 30.01 ? 196 LEU B CD1 1 
ATOM   4577 C  CD2 . LEU B 1 187 ? -8.763  -33.795 -8.918  1.00 32.25 ? 196 LEU B CD2 1 
ATOM   4578 N  N   . LEU B 1 188 ? -9.937  -38.519 -9.141  1.00 34.16 ? 197 LEU B N   1 
ATOM   4579 C  CA  . LEU B 1 188 ? -9.650  -39.458 -10.230 1.00 35.47 ? 197 LEU B CA  1 
ATOM   4580 C  C   . LEU B 1 188 ? -10.892 -40.263 -10.612 1.00 34.08 ? 197 LEU B C   1 
ATOM   4581 O  O   . LEU B 1 188 ? -11.251 -40.328 -11.781 1.00 32.80 ? 197 LEU B O   1 
ATOM   4582 C  CB  . LEU B 1 188 ? -8.508  -40.403 -9.829  1.00 36.11 ? 197 LEU B CB  1 
ATOM   4583 C  CG  . LEU B 1 188 ? -8.182  -41.605 -10.716 1.00 37.30 ? 197 LEU B CG  1 
ATOM   4584 C  CD1 . LEU B 1 188 ? -7.941  -41.193 -12.135 1.00 38.99 ? 197 LEU B CD1 1 
ATOM   4585 C  CD2 . LEU B 1 188 ? -6.966  -42.345 -10.168 1.00 42.27 ? 197 LEU B CD2 1 
ATOM   4586 N  N   . LYS B 1 189 ? -11.545 -40.855 -9.614  1.00 37.27 ? 198 LYS B N   1 
ATOM   4587 C  CA  . LYS B 1 189 ? -12.780 -41.634 -9.825  1.00 38.57 ? 198 LYS B CA  1 
ATOM   4588 C  C   . LYS B 1 189 ? -13.886 -40.779 -10.463 1.00 36.75 ? 198 LYS B C   1 
ATOM   4589 O  O   . LYS B 1 189 ? -14.577 -41.232 -11.377 1.00 36.78 ? 198 LYS B O   1 
ATOM   4590 C  CB  . LYS B 1 189 ? -13.264 -42.244 -8.497  1.00 41.09 ? 198 LYS B CB  1 
ATOM   4591 C  CG  . LYS B 1 189 ? -14.405 -43.260 -8.627  1.00 41.04 ? 198 LYS B CG  1 
ATOM   4592 C  CD  . LYS B 1 189 ? -14.820 -43.785 -7.263  1.00 47.26 ? 198 LYS B CD  1 
ATOM   4593 C  CE  . LYS B 1 189 ? -16.015 -44.728 -7.355  1.00 51.87 ? 198 LYS B CE  1 
ATOM   4594 N  NZ  . LYS B 1 189 ? -16.428 -45.244 -6.024  0.00 50.53 ? 198 LYS B NZ  1 
ATOM   4595 N  N   . ALA B 1 190 ? -14.029 -39.545 -9.981  1.00 36.00 ? 199 ALA B N   1 
ATOM   4596 C  CA  . ALA B 1 190 ? -15.011 -38.592 -10.508 1.00 33.56 ? 199 ALA B CA  1 
ATOM   4597 C  C   . ALA B 1 190 ? -14.774 -38.270 -11.978 1.00 32.26 ? 199 ALA B C   1 
ATOM   4598 O  O   . ALA B 1 190 ? -15.708 -38.302 -12.786 1.00 33.34 ? 199 ALA B O   1 
ATOM   4599 C  CB  . ALA B 1 190 ? -14.998 -37.301 -9.681  1.00 32.98 ? 199 ALA B CB  1 
ATOM   4600 N  N   . LEU B 1 191 ? -13.526 -37.956 -12.320 1.00 30.54 ? 200 LEU B N   1 
ATOM   4601 C  CA  . LEU B 1 191 ? -13.172 -37.637 -13.705 1.00 29.16 ? 200 LEU B CA  1 
ATOM   4602 C  C   . LEU B 1 191 ? -13.358 -38.843 -14.618 1.00 27.87 ? 200 LEU B C   1 
ATOM   4603 O  O   . LEU B 1 191 ? -13.815 -38.691 -15.739 1.00 29.99 ? 200 LEU B O   1 
ATOM   4604 C  CB  . LEU B 1 191 ? -11.743 -37.108 -13.812 1.00 26.37 ? 200 LEU B CB  1 
ATOM   4605 C  CG  . LEU B 1 191 ? -11.464 -35.746 -13.182 1.00 27.34 ? 200 LEU B CG  1 
ATOM   4606 C  CD1 . LEU B 1 191 ? -9.964  -35.476 -13.146 1.00 26.56 ? 200 LEU B CD1 1 
ATOM   4607 C  CD2 . LEU B 1 191 ? -12.190 -34.637 -13.932 1.00 27.95 ? 200 LEU B CD2 1 
ATOM   4608 N  N   . LEU B 1 192 ? -13.021 -40.036 -14.148 1.00 29.62 ? 201 LEU B N   1 
ATOM   4609 C  CA  . LEU B 1 192 ? -13.298 -41.245 -14.942 1.00 33.22 ? 201 LEU B CA  1 
ATOM   4610 C  C   . LEU B 1 192 ? -14.798 -41.474 -15.189 1.00 32.48 ? 201 LEU B C   1 
ATOM   4611 O  O   . LEU B 1 192 ? -15.163 -41.967 -16.248 1.00 32.90 ? 201 LEU B O   1 
ATOM   4612 C  CB  . LEU B 1 192 ? -12.656 -42.489 -14.323 1.00 34.89 ? 201 LEU B CB  1 
ATOM   4613 C  CG  . LEU B 1 192 ? -11.118 -42.527 -14.299 1.00 36.74 ? 201 LEU B CG  1 
ATOM   4614 C  CD1 . LEU B 1 192 ? -10.659 -43.784 -13.594 1.00 37.94 ? 201 LEU B CD1 1 
ATOM   4615 C  CD2 . LEU B 1 192 ? -10.492 -42.441 -15.693 1.00 39.65 ? 201 LEU B CD2 1 
ATOM   4616 N  N   . GLU B 1 193 ? -15.647 -41.114 -14.227 1.00 34.52 ? 202 GLU B N   1 
ATOM   4617 C  CA  . GLU B 1 193 ? -17.101 -41.263 -14.379 1.00 35.61 ? 202 GLU B CA  1 
ATOM   4618 C  C   . GLU B 1 193 ? -17.637 -40.278 -15.405 1.00 34.31 ? 202 GLU B C   1 
ATOM   4619 O  O   . GLU B 1 193 ? -18.470 -40.645 -16.236 1.00 34.09 ? 202 GLU B O   1 
ATOM   4620 C  CB  . GLU B 1 193 ? -17.825 -41.082 -13.037 1.00 38.11 ? 202 GLU B CB  1 
ATOM   4621 C  CG  . GLU B 1 193 ? -19.374 -41.116 -13.106 1.00 42.13 ? 202 GLU B CG  1 
ATOM   4622 C  CD  . GLU B 1 193 ? -19.955 -42.425 -13.657 1.00 47.99 ? 202 GLU B CD  1 
ATOM   4623 O  OE1 . GLU B 1 193 ? -19.296 -43.486 -13.568 1.00 48.52 ? 202 GLU B OE1 1 
ATOM   4624 O  OE2 . GLU B 1 193 ? -21.093 -42.386 -14.165 1.00 47.15 ? 202 GLU B OE2 1 
ATOM   4625 N  N   . ILE B 1 194 ? -17.152 -39.036 -15.340 1.00 33.69 ? 203 ILE B N   1 
ATOM   4626 C  CA  . ILE B 1 194 ? -17.496 -38.006 -16.322 1.00 30.66 ? 203 ILE B CA  1 
ATOM   4627 C  C   . ILE B 1 194 ? -17.154 -38.492 -17.726 1.00 29.69 ? 203 ILE B C   1 
ATOM   4628 O  O   . ILE B 1 194 ? -17.998 -38.427 -18.628 1.00 27.75 ? 203 ILE B O   1 
ATOM   4629 C  CB  . ILE B 1 194 ? -16.811 -36.631 -15.994 1.00 29.53 ? 203 ILE B CB  1 
ATOM   4630 C  CG1 . ILE B 1 194 ? -17.421 -36.034 -14.718 1.00 33.67 ? 203 ILE B CG1 1 
ATOM   4631 C  CG2 . ILE B 1 194 ? -16.953 -35.627 -17.146 1.00 29.76 ? 203 ILE B CG2 1 
ATOM   4632 C  CD1 . ILE B 1 194 ? -16.612 -34.912 -14.084 1.00 33.65 ? 203 ILE B CD1 1 
ATOM   4633 N  N   . ALA B 1 195 ? -15.929 -38.992 -17.898 1.00 29.97 ? 204 ALA B N   1 
ATOM   4634 C  CA  . ALA B 1 195 ? -15.471 -39.517 -19.189 1.00 29.39 ? 204 ALA B CA  1 
ATOM   4635 C  C   . ALA B 1 195 ? -16.377 -40.640 -19.696 1.00 30.67 ? 204 ALA B C   1 
ATOM   4636 O  O   . ALA B 1 195 ? -16.794 -40.626 -20.852 1.00 30.38 ? 204 ALA B O   1 
ATOM   4637 C  CB  . ALA B 1 195 ? -14.024 -39.995 -19.090 1.00 30.37 ? 204 ALA B CB  1 
ATOM   4638 N  N   . SER B 1 196 ? -16.704 -41.581 -18.809 1.00 32.26 ? 205 SER B N   1 
ATOM   4639 C  CA  . SER B 1 196 ? -17.619 -42.684 -19.131 1.00 34.03 ? 205 SER B CA  1 
ATOM   4640 C  C   . SER B 1 196 ? -18.972 -42.195 -19.668 1.00 31.34 ? 205 SER B C   1 
ATOM   4641 O  O   . SER B 1 196 ? -19.447 -42.688 -20.683 1.00 29.70 ? 205 SER B O   1 
ATOM   4642 C  CB  . SER B 1 196 ? -17.839 -43.563 -17.900 1.00 34.05 ? 205 SER B CB  1 
ATOM   4643 O  OG  . SER B 1 196 ? -18.696 -44.633 -18.200 1.00 42.69 ? 205 SER B OG  1 
ATOM   4644 N  N   . CYS B 1 197 ? -19.564 -41.215 -18.988 1.00 32.44 ? 206 CYS B N   1 
ATOM   4645 C  CA  . CYS B 1 197 ? -20.858 -40.651 -19.397 1.00 31.42 ? 206 CYS B CA  1 
ATOM   4646 C  C   . CYS B 1 197 ? -20.808 -39.916 -20.727 1.00 30.29 ? 206 CYS B C   1 
ATOM   4647 O  O   . CYS B 1 197 ? -21.710 -40.064 -21.545 1.00 33.33 ? 206 CYS B O   1 
ATOM   4648 C  CB  . CYS B 1 197 ? -21.394 -39.711 -18.323 1.00 32.02 ? 206 CYS B CB  1 
ATOM   4649 S  SG  . CYS B 1 197 ? -21.812 -40.574 -16.798 1.00 39.31 ? 206 CYS B SG  1 
ATOM   4650 N  N   . LEU B 1 198 ? -19.770 -39.109 -20.933 1.00 29.24 ? 207 LEU B N   1 
ATOM   4651 C  CA  . LEU B 1 198 ? -19.589 -38.406 -22.206 1.00 28.64 ? 207 LEU B CA  1 
ATOM   4652 C  C   . LEU B 1 198 ? -19.325 -39.364 -23.358 1.00 28.15 ? 207 LEU B C   1 
ATOM   4653 O  O   . LEU B 1 198 ? -19.757 -39.104 -24.473 1.00 26.60 ? 207 LEU B O   1 
ATOM   4654 C  CB  . LEU B 1 198 ? -18.471 -37.372 -22.105 1.00 29.00 ? 207 LEU B CB  1 
ATOM   4655 C  CG  . LEU B 1 198 ? -18.692 -36.238 -21.093 1.00 27.04 ? 207 LEU B CG  1 
ATOM   4656 C  CD1 . LEU B 1 198 ? -17.479 -35.350 -21.101 1.00 28.03 ? 207 LEU B CD1 1 
ATOM   4657 C  CD2 . LEU B 1 198 ? -19.942 -35.430 -21.398 1.00 27.14 ? 207 LEU B CD2 1 
ATOM   4658 N  N   . GLU B 1 199 ? -18.617 -40.461 -23.078 1.00 28.31 ? 208 GLU B N   1 
ATOM   4659 C  CA  . GLU B 1 199 ? -18.449 -41.550 -24.039 1.00 31.84 ? 208 GLU B CA  1 
ATOM   4660 C  C   . GLU B 1 199 ? -19.784 -42.255 -24.329 1.00 31.53 ? 208 GLU B C   1 
ATOM   4661 O  O   . GLU B 1 199 ? -20.057 -42.609 -25.471 1.00 33.46 ? 208 GLU B O   1 
ATOM   4662 C  CB  . GLU B 1 199 ? -17.402 -42.566 -23.542 1.00 32.09 ? 208 GLU B CB  1 
ATOM   4663 C  CG  . GLU B 1 199 ? -15.967 -42.021 -23.546 1.00 35.19 ? 208 GLU B CG  1 
ATOM   4664 C  CD  . GLU B 1 199 ? -14.993 -42.808 -22.659 1.00 37.41 ? 208 GLU B CD  1 
ATOM   4665 O  OE1 . GLU B 1 199 ? -15.295 -43.961 -22.273 1.00 37.06 ? 208 GLU B OE1 1 
ATOM   4666 O  OE2 . GLU B 1 199 ? -13.902 -42.269 -22.368 1.00 35.16 ? 208 GLU B OE2 1 
ATOM   4667 N  N   . LYS B 1 200 ? -20.601 -42.464 -23.300 1.00 32.03 ? 209 LYS B N   1 
ATOM   4668 C  CA  . LYS B 1 200 ? -21.943 -43.029 -23.494 1.00 34.66 ? 209 LYS B CA  1 
ATOM   4669 C  C   . LYS B 1 200 ? -22.830 -42.123 -24.350 1.00 31.93 ? 209 LYS B C   1 
ATOM   4670 O  O   . LYS B 1 200 ? -23.504 -42.607 -25.242 1.00 33.36 ? 209 LYS B O   1 
ATOM   4671 C  CB  . LYS B 1 200 ? -22.617 -43.343 -22.156 1.00 35.37 ? 209 LYS B CB  1 
ATOM   4672 C  CG  . LYS B 1 200 ? -22.072 -44.620 -21.544 1.00 43.53 ? 209 LYS B CG  1 
ATOM   4673 C  CD  . LYS B 1 200 ? -22.551 -44.857 -20.125 1.00 44.42 ? 209 LYS B CD  1 
ATOM   4674 C  CE  . LYS B 1 200 ? -21.905 -46.120 -19.556 1.00 49.17 ? 209 LYS B CE  1 
ATOM   4675 N  NZ  . LYS B 1 200 ? -22.255 -46.334 -18.126 1.00 53.96 ? 209 LYS B NZ  1 
ATOM   4676 N  N   . ALA B 1 201 ? -22.791 -40.816 -24.090 1.00 31.19 ? 210 ALA B N   1 
ATOM   4677 C  CA  . ALA B 1 201 ? -23.500 -39.815 -24.900 1.00 31.01 ? 210 ALA B CA  1 
ATOM   4678 C  C   . ALA B 1 201 ? -23.224 -39.937 -26.400 1.00 31.53 ? 210 ALA B C   1 
ATOM   4679 O  O   . ALA B 1 201 ? -24.141 -39.784 -27.210 1.00 33.62 ? 210 ALA B O   1 
ATOM   4680 C  CB  . ALA B 1 201 ? -23.161 -38.396 -24.421 1.00 30.58 ? 210 ALA B CB  1 
ATOM   4681 N  N   . LEU B 1 202 ? -21.971 -40.220 -26.759 1.00 31.96 ? 211 LEU B N   1 
ATOM   4682 C  CA  . LEU B 1 202 ? -21.582 -40.393 -28.163 1.00 31.98 ? 211 LEU B CA  1 
ATOM   4683 C  C   . LEU B 1 202 ? -22.225 -41.640 -28.766 1.00 31.62 ? 211 LEU B C   1 
ATOM   4684 O  O   . LEU B 1 202 ? -22.733 -41.597 -29.886 1.00 29.49 ? 211 LEU B O   1 
ATOM   4685 C  CB  . LEU B 1 202 ? -20.054 -40.443 -28.323 1.00 33.17 ? 211 LEU B CB  1 
ATOM   4686 C  CG  . LEU B 1 202 ? -19.500 -40.853 -29.699 1.00 34.29 ? 211 LEU B CG  1 
ATOM   4687 C  CD1 . LEU B 1 202 ? -20.014 -39.934 -30.811 1.00 32.64 ? 211 LEU B CD1 1 
ATOM   4688 C  CD2 . LEU B 1 202 ? -17.987 -40.874 -29.697 1.00 35.67 ? 211 LEU B CD2 1 
ATOM   4689 N  N   . GLN B 1 203 ? -22.195 -42.747 -28.034 1.00 31.90 ? 212 GLN B N   1 
ATOM   4690 C  CA  . GLN B 1 203 ? -22.862 -43.970 -28.491 1.00 34.05 ? 212 GLN B CA  1 
ATOM   4691 C  C   . GLN B 1 203 ? -24.355 -43.762 -28.736 1.00 31.90 ? 212 GLN B C   1 
ATOM   4692 O  O   . GLN B 1 203 ? -24.880 -44.233 -29.742 1.00 35.01 ? 212 GLN B O   1 
ATOM   4693 C  CB  . GLN B 1 203 ? -22.627 -45.127 -27.509 1.00 38.02 ? 212 GLN B CB  1 
ATOM   4694 C  CG  . GLN B 1 203 ? -21.153 -45.516 -27.371 1.00 41.51 ? 212 GLN B CG  1 
ATOM   4695 C  CD  . GLN B 1 203 ? -20.509 -45.851 -28.708 1.00 46.32 ? 212 GLN B CD  1 
ATOM   4696 O  OE1 . GLN B 1 203 ? -21.088 -46.582 -29.517 1.00 46.86 ? 212 GLN B OE1 1 
ATOM   4697 N  NE2 . GLN B 1 203 ? -19.320 -45.297 -28.958 1.00 44.56 ? 212 GLN B NE2 1 
ATOM   4698 N  N   . VAL B 1 204 ? -25.011 -43.036 -27.831 1.00 31.07 ? 213 VAL B N   1 
ATOM   4699 C  CA  . VAL B 1 204 ? -26.427 -42.647 -27.964 1.00 31.89 ? 213 VAL B CA  1 
ATOM   4700 C  C   . VAL B 1 204 ? -26.662 -41.794 -29.229 1.00 31.15 ? 213 VAL B C   1 
ATOM   4701 O  O   . VAL B 1 204 ? -27.654 -41.986 -29.943 1.00 31.10 ? 213 VAL B O   1 
ATOM   4702 C  CB  . VAL B 1 204 ? -26.920 -41.881 -26.689 1.00 30.86 ? 213 VAL B CB  1 
ATOM   4703 C  CG1 . VAL B 1 204 ? -28.312 -41.280 -26.882 1.00 30.73 ? 213 VAL B CG1 1 
ATOM   4704 C  CG2 . VAL B 1 204 ? -26.918 -42.814 -25.453 1.00 32.29 ? 213 VAL B CG2 1 
ATOM   4705 N  N   . PHE B 1 205 ? -25.738 -40.872 -29.496 1.00 29.17 ? 214 PHE B N   1 
ATOM   4706 C  CA  . PHE B 1 205 ? -25.780 -40.019 -30.694 1.00 30.22 ? 214 PHE B CA  1 
ATOM   4707 C  C   . PHE B 1 205 ? -25.865 -40.870 -31.975 1.00 29.67 ? 214 PHE B C   1 
ATOM   4708 O  O   . PHE B 1 205 ? -26.565 -40.485 -32.909 1.00 27.80 ? 214 PHE B O   1 
ATOM   4709 C  CB  . PHE B 1 205 ? -24.548 -39.078 -30.720 1.00 30.90 ? 214 PHE B CB  1 
ATOM   4710 C  CG  . PHE B 1 205 ? -24.698 -37.800 -31.552 1.00 28.89 ? 214 PHE B CG  1 
ATOM   4711 C  CD1 . PHE B 1 205 ? -25.655 -37.641 -32.572 1.00 31.96 ? 214 PHE B CD1 1 
ATOM   4712 C  CD2 . PHE B 1 205 ? -23.792 -36.761 -31.341 1.00 28.70 ? 214 PHE B CD2 1 
ATOM   4713 C  CE1 . PHE B 1 205 ? -25.715 -36.476 -33.330 1.00 31.78 ? 214 PHE B CE1 1 
ATOM   4714 C  CE2 . PHE B 1 205 ? -23.844 -35.591 -32.097 1.00 30.95 ? 214 PHE B CE2 1 
ATOM   4715 C  CZ  . PHE B 1 205 ? -24.813 -35.444 -33.090 1.00 31.90 ? 214 PHE B CZ  1 
ATOM   4716 N  N   . HIS B 1 206 ? -25.198 -42.033 -32.005 1.00 32.89 ? 215 HIS B N   1 
ATOM   4717 C  CA  . HIS B 1 206 ? -25.246 -42.949 -33.170 1.00 36.29 ? 215 HIS B CA  1 
ATOM   4718 C  C   . HIS B 1 206 ? -26.669 -43.292 -33.637 1.00 35.60 ? 215 HIS B C   1 
ATOM   4719 O  O   . HIS B 1 206 ? -26.868 -43.569 -34.816 1.00 34.93 ? 215 HIS B O   1 
ATOM   4720 C  CB  . HIS B 1 206 ? -24.485 -44.270 -32.922 1.00 39.56 ? 215 HIS B CB  1 
ATOM   4721 C  CG  . HIS B 1 206 ? -23.011 -44.103 -32.713 1.00 40.84 ? 215 HIS B CG  1 
ATOM   4722 N  ND1 . HIS B 1 206 ? -22.149 -45.175 -32.636 1.00 44.30 ? 215 HIS B ND1 1 
ATOM   4723 C  CD2 . HIS B 1 206 ? -22.245 -42.996 -32.571 1.00 45.02 ? 215 HIS B CD2 1 
ATOM   4724 C  CE1 . HIS B 1 206 ? -20.917 -44.736 -32.448 1.00 48.93 ? 215 HIS B CE1 1 
ATOM   4725 N  NE2 . HIS B 1 206 ? -20.948 -43.416 -32.405 1.00 47.78 ? 215 HIS B NE2 1 
ATOM   4726 N  N   . GLN B 1 207 ? -27.639 -43.265 -32.721 1.00 34.16 ? 216 GLN B N   1 
ATOM   4727 C  CA  . GLN B 1 207 ? -29.059 -43.468 -33.063 1.00 36.30 ? 216 GLN B CA  1 
ATOM   4728 C  C   . GLN B 1 207 ? -29.660 -42.457 -34.041 1.00 33.84 ? 216 GLN B C   1 
ATOM   4729 O  O   . GLN B 1 207 ? -30.719 -42.733 -34.602 1.00 35.13 ? 216 GLN B O   1 
ATOM   4730 C  CB  . GLN B 1 207 ? -29.939 -43.442 -31.808 1.00 36.54 ? 216 GLN B CB  1 
ATOM   4731 C  CG  . GLN B 1 207 ? -29.705 -44.557 -30.827 1.00 40.54 ? 216 GLN B CG  1 
ATOM   4732 C  CD  . GLN B 1 207 ? -30.536 -44.362 -29.576 1.00 42.28 ? 216 GLN B CD  1 
ATOM   4733 O  OE1 . GLN B 1 207 ? -31.767 -44.392 -29.629 1.00 43.11 ? 216 GLN B OE1 1 
ATOM   4734 N  NE2 . GLN B 1 207 ? -29.869 -44.156 -28.443 1.00 47.86 ? 216 GLN B NE2 1 
ATOM   4735 N  N   . ILE B 1 208 ? -29.025 -41.294 -34.234 1.00 33.12 ? 217 ILE B N   1 
ATOM   4736 C  CA  . ILE B 1 208 ? -29.567 -40.251 -35.131 1.00 30.16 ? 217 ILE B CA  1 
ATOM   4737 C  C   . ILE B 1 208 ? -29.834 -40.792 -36.547 1.00 31.60 ? 217 ILE B C   1 
ATOM   4738 O  O   . ILE B 1 208 ? -30.853 -40.460 -37.170 1.00 29.62 ? 217 ILE B O   1 
ATOM   4739 C  CB  . ILE B 1 208 ? -28.658 -38.973 -35.155 1.00 30.91 ? 217 ILE B CB  1 
ATOM   4740 C  CG1 . ILE B 1 208 ? -29.397 -37.752 -35.737 1.00 32.52 ? 217 ILE B CG1 1 
ATOM   4741 C  CG2 . ILE B 1 208 ? -27.337 -39.218 -35.898 1.00 27.83 ? 217 ILE B CG2 1 
ATOM   4742 C  CD1 . ILE B 1 208 ? -30.302 -37.053 -34.753 1.00 36.38 ? 217 ILE B CD1 1 
ATOM   4743 N  N   . HIS B 1 209 ? -28.944 -41.670 -37.009 1.00 30.63 ? 218 HIS B N   1 
ATOM   4744 C  CA  . HIS B 1 209 ? -29.030 -42.263 -38.334 1.00 33.34 ? 218 HIS B CA  1 
ATOM   4745 C  C   . HIS B 1 209 ? -30.280 -43.127 -38.530 1.00 35.10 ? 218 HIS B C   1 
ATOM   4746 O  O   . HIS B 1 209 ? -30.776 -43.253 -39.650 1.00 34.98 ? 218 HIS B O   1 
ATOM   4747 C  CB  . HIS B 1 209 ? -27.766 -43.077 -38.629 1.00 35.01 ? 218 HIS B CB  1 
ATOM   4748 C  CG  . HIS B 1 209 ? -26.503 -42.274 -38.545 1.00 36.78 ? 218 HIS B CG  1 
ATOM   4749 N  ND1 . HIS B 1 209 ? -26.114 -41.393 -39.532 1.00 38.95 ? 218 HIS B ND1 1 
ATOM   4750 C  CD2 . HIS B 1 209 ? -25.550 -42.207 -37.586 1.00 37.24 ? 218 HIS B CD2 1 
ATOM   4751 C  CE1 . HIS B 1 209 ? -24.972 -40.827 -39.188 1.00 41.18 ? 218 HIS B CE1 1 
ATOM   4752 N  NE2 . HIS B 1 209 ? -24.610 -41.299 -38.009 1.00 37.76 ? 218 HIS B NE2 1 
ATOM   4753 N  N   . ASP B 1 210 ? -30.782 -43.705 -37.441 1.00 35.54 ? 219 ASP B N   1 
ATOM   4754 C  CA  . ASP B 1 210 ? -31.937 -44.607 -37.482 1.00 36.74 ? 219 ASP B CA  1 
ATOM   4755 C  C   . ASP B 1 210 ? -33.271 -43.870 -37.488 1.00 34.32 ? 219 ASP B C   1 
ATOM   4756 O  O   . ASP B 1 210 ? -34.270 -44.450 -37.877 1.00 36.09 ? 219 ASP B O   1 
ATOM   4757 C  CB  . ASP B 1 210 ? -31.924 -45.557 -36.274 1.00 38.37 ? 219 ASP B CB  1 
ATOM   4758 C  CG  . ASP B 1 210 ? -30.679 -46.439 -36.220 1.00 41.18 ? 219 ASP B CG  1 
ATOM   4759 O  OD1 . ASP B 1 210 ? -30.294 -47.012 -37.265 1.00 49.97 ? 219 ASP B OD1 1 
ATOM   4760 O  OD2 . ASP B 1 210 ? -30.099 -46.565 -35.114 1.00 45.33 ? 219 ASP B OD2 1 
ATOM   4761 N  N   . HIS B 1 211 ? -33.299 -42.617 -37.035 1.00 32.00 ? 220 HIS B N   1 
ATOM   4762 C  CA  . HIS B 1 211 ? -34.570 -41.898 -36.835 1.00 31.31 ? 220 HIS B CA  1 
ATOM   4763 C  C   . HIS B 1 211 ? -34.708 -40.563 -37.581 1.00 31.67 ? 220 HIS B C   1 
ATOM   4764 O  O   . HIS B 1 211 ? -35.787 -39.968 -37.554 1.00 30.64 ? 220 HIS B O   1 
ATOM   4765 C  CB  . HIS B 1 211 ? -34.810 -41.686 -35.336 1.00 29.28 ? 220 HIS B CB  1 
ATOM   4766 C  CG  . HIS B 1 211 ? -34.709 -42.938 -34.528 1.00 27.17 ? 220 HIS B CG  1 
ATOM   4767 N  ND1 . HIS B 1 211 ? -35.523 -44.027 -34.747 1.00 32.72 ? 220 HIS B ND1 1 
ATOM   4768 C  CD2 . HIS B 1 211 ? -33.881 -43.285 -33.512 1.00 28.67 ? 220 HIS B CD2 1 
ATOM   4769 C  CE1 . HIS B 1 211 ? -35.200 -44.992 -33.905 1.00 33.51 ? 220 HIS B CE1 1 
ATOM   4770 N  NE2 . HIS B 1 211 ? -34.213 -44.565 -33.139 1.00 30.37 ? 220 HIS B NE2 1 
ATOM   4771 N  N   . VAL B 1 212 ? -33.642 -40.107 -38.247 1.00 32.06 ? 221 VAL B N   1 
ATOM   4772 C  CA  . VAL B 1 212 ? -33.670 -38.869 -39.032 1.00 32.71 ? 221 VAL B CA  1 
ATOM   4773 C  C   . VAL B 1 212 ? -33.140 -39.147 -40.437 1.00 32.90 ? 221 VAL B C   1 
ATOM   4774 O  O   . VAL B 1 212 ? -32.067 -39.725 -40.590 1.00 31.07 ? 221 VAL B O   1 
ATOM   4775 C  CB  . VAL B 1 212 ? -32.824 -37.739 -38.388 1.00 31.77 ? 221 VAL B CB  1 
ATOM   4776 C  CG1 . VAL B 1 212 ? -33.161 -36.382 -39.021 1.00 34.05 ? 221 VAL B CG1 1 
ATOM   4777 C  CG2 . VAL B 1 212 ? -33.043 -37.674 -36.878 1.00 33.79 ? 221 VAL B CG2 1 
ATOM   4778 N  N   . ASN B 1 213 ? -33.910 -38.723 -41.444 1.00 34.00 ? 222 ASN B N   1 
ATOM   4779 C  CA  . ASN B 1 213 ? -33.538 -38.816 -42.861 1.00 35.84 ? 222 ASN B CA  1 
ATOM   4780 C  C   . ASN B 1 213 ? -32.948 -37.456 -43.278 1.00 34.07 ? 222 ASN B C   1 
ATOM   4781 O  O   . ASN B 1 213 ? -33.547 -36.420 -42.957 1.00 32.59 ? 222 ASN B O   1 
ATOM   4782 C  CB  . ASN B 1 213 ? -34.780 -39.177 -43.703 1.00 40.34 ? 222 ASN B CB  1 
ATOM   4783 C  CG  . ASN B 1 213 ? -34.661 -38.758 -45.164 1.00 44.09 ? 222 ASN B CG  1 
ATOM   4784 O  OD1 . ASN B 1 213 ? -35.250 -37.758 -45.578 1.00 54.53 ? 222 ASN B OD1 1 
ATOM   4785 N  ND2 . ASN B 1 213 ? -33.898 -39.514 -45.944 1.00 51.65 ? 222 ASN B ND2 1 
ATOM   4786 N  N   . PRO B 1 214 ? -31.770 -37.444 -43.947 1.00 33.96 ? 223 PRO B N   1 
ATOM   4787 C  CA  . PRO B 1 214 ? -31.130 -36.175 -44.345 1.00 35.08 ? 223 PRO B CA  1 
ATOM   4788 C  C   . PRO B 1 214 ? -31.996 -35.186 -45.123 1.00 34.98 ? 223 PRO B C   1 
ATOM   4789 O  O   . PRO B 1 214 ? -32.040 -34.008 -44.757 1.00 33.35 ? 223 PRO B O   1 
ATOM   4790 C  CB  . PRO B 1 214 ? -29.937 -36.631 -45.180 1.00 36.07 ? 223 PRO B CB  1 
ATOM   4791 C  CG  . PRO B 1 214 ? -29.599 -37.965 -44.630 1.00 36.84 ? 223 PRO B CG  1 
ATOM   4792 C  CD  . PRO B 1 214 ? -30.915 -38.595 -44.307 1.00 37.24 ? 223 PRO B CD  1 
ATOM   4793 N  N   . LYS B 1 215 ? -32.684 -35.668 -46.156 1.00 37.73 ? 224 LYS B N   1 
ATOM   4794 C  CA  . LYS B 1 215 ? -33.553 -34.829 -46.985 1.00 39.49 ? 224 LYS B CA  1 
ATOM   4795 C  C   . LYS B 1 215 ? -34.674 -34.158 -46.176 1.00 38.20 ? 224 LYS B C   1 
ATOM   4796 O  O   . LYS B 1 215 ? -34.858 -32.942 -46.269 1.00 38.77 ? 224 LYS B O   1 
ATOM   4797 C  CB  . LYS B 1 215 ? -34.144 -35.649 -48.140 1.00 42.85 ? 224 LYS B CB  1 
ATOM   4798 C  CG  . LYS B 1 215 ? -34.985 -34.852 -49.140 1.00 44.17 ? 224 LYS B CG  1 
ATOM   4799 C  CD  . LYS B 1 215 ? -35.435 -35.733 -50.312 1.00 50.84 ? 224 LYS B CD  1 
ATOM   4800 C  CE  . LYS B 1 215 ? -36.231 -34.934 -51.333 0.00 50.33 ? 224 LYS B CE  1 
ATOM   4801 N  NZ  . LYS B 1 215 ? -36.681 -35.776 -52.475 0.00 52.54 ? 224 LYS B NZ  1 
ATOM   4802 N  N   . ALA B 1 216 ? -35.409 -34.947 -45.388 1.00 35.12 ? 225 ALA B N   1 
ATOM   4803 C  CA  . ALA B 1 216 ? -36.478 -34.407 -44.525 1.00 34.05 ? 225 ALA B CA  1 
ATOM   4804 C  C   . ALA B 1 216 ? -35.947 -33.398 -43.527 1.00 32.95 ? 225 ALA B C   1 
ATOM   4805 O  O   . ALA B 1 216 ? -36.573 -32.355 -43.283 1.00 29.81 ? 225 ALA B O   1 
ATOM   4806 C  CB  . ALA B 1 216 ? -37.187 -35.517 -43.781 1.00 33.84 ? 225 ALA B CB  1 
ATOM   4807 N  N   . PHE B 1 217 ? -34.798 -33.712 -42.934 1.00 31.55 ? 226 PHE B N   1 
ATOM   4808 C  CA  . PHE B 1 217 ? -34.190 -32.809 -41.987 1.00 31.44 ? 226 PHE B CA  1 
ATOM   4809 C  C   . PHE B 1 217 ? -33.835 -31.464 -42.624 1.00 32.23 ? 226 PHE B C   1 
ATOM   4810 O  O   . PHE B 1 217 ? -34.224 -30.411 -42.111 1.00 31.68 ? 226 PHE B O   1 
ATOM   4811 C  CB  . PHE B 1 217 ? -32.935 -33.405 -41.367 1.00 31.83 ? 226 PHE B CB  1 
ATOM   4812 C  CG  . PHE B 1 217 ? -32.302 -32.498 -40.374 1.00 28.72 ? 226 PHE B CG  1 
ATOM   4813 C  CD1 . PHE B 1 217 ? -32.822 -32.410 -39.098 1.00 31.20 ? 226 PHE B CD1 1 
ATOM   4814 C  CD2 . PHE B 1 217 ? -31.228 -31.679 -40.727 1.00 31.59 ? 226 PHE B CD2 1 
ATOM   4815 C  CE1 . PHE B 1 217 ? -32.279 -31.551 -38.166 1.00 32.28 ? 226 PHE B CE1 1 
ATOM   4816 C  CE2 . PHE B 1 217 ? -30.676 -30.810 -39.794 1.00 32.81 ? 226 PHE B CE2 1 
ATOM   4817 C  CZ  . PHE B 1 217 ? -31.212 -30.751 -38.508 1.00 31.64 ? 226 PHE B CZ  1 
ATOM   4818 N  N   . PHE B 1 218 ? -33.078 -31.524 -43.715 1.00 34.76 ? 227 PHE B N   1 
ATOM   4819 C  CA  . PHE B 1 218 ? -32.585 -30.332 -44.408 1.00 37.77 ? 227 PHE B CA  1 
ATOM   4820 C  C   . PHE B 1 218 ? -33.708 -29.510 -45.034 1.00 39.25 ? 227 PHE B C   1 
ATOM   4821 O  O   . PHE B 1 218 ? -33.767 -28.300 -44.845 1.00 36.58 ? 227 PHE B O   1 
ATOM   4822 C  CB  . PHE B 1 218 ? -31.579 -30.725 -45.498 1.00 39.37 ? 227 PHE B CB  1 
ATOM   4823 C  CG  . PHE B 1 218 ? -30.977 -29.555 -46.224 1.00 40.42 ? 227 PHE B CG  1 
ATOM   4824 C  CD1 . PHE B 1 218 ? -29.890 -28.877 -45.683 1.00 39.97 ? 227 PHE B CD1 1 
ATOM   4825 C  CD2 . PHE B 1 218 ? -31.487 -29.141 -47.455 1.00 41.62 ? 227 PHE B CD2 1 
ATOM   4826 C  CE1 . PHE B 1 218 ? -29.319 -27.796 -46.350 1.00 42.46 ? 227 PHE B CE1 1 
ATOM   4827 C  CE2 . PHE B 1 218 ? -30.924 -28.063 -48.132 1.00 43.46 ? 227 PHE B CE2 1 
ATOM   4828 C  CZ  . PHE B 1 218 ? -29.836 -27.388 -47.577 1.00 43.68 ? 227 PHE B CZ  1 
ATOM   4829 N  N   . SER B 1 219 ? -34.579 -30.173 -45.790 1.00 41.54 ? 228 SER B N   1 
ATOM   4830 C  CA  . SER B 1 219 ? -35.625 -29.478 -46.553 1.00 43.05 ? 228 SER B CA  1 
ATOM   4831 C  C   . SER B 1 219 ? -36.843 -29.043 -45.722 1.00 41.83 ? 228 SER B C   1 
ATOM   4832 O  O   . SER B 1 219 ? -37.581 -28.154 -46.150 1.00 42.60 ? 228 SER B O   1 
ATOM   4833 C  CB  . SER B 1 219 ? -36.073 -30.331 -47.755 1.00 46.17 ? 228 SER B CB  1 
ATOM   4834 O  OG  . SER B 1 219 ? -36.736 -31.512 -47.337 1.00 50.31 ? 228 SER B OG  1 
ATOM   4835 N  N   . VAL B 1 220 ? -37.057 -29.637 -44.546 1.00 40.57 ? 229 VAL B N   1 
ATOM   4836 C  CA  . VAL B 1 220 ? -38.270 -29.354 -43.762 1.00 39.85 ? 229 VAL B CA  1 
ATOM   4837 C  C   . VAL B 1 220 ? -37.938 -28.835 -42.369 1.00 39.19 ? 229 VAL B C   1 
ATOM   4838 O  O   . VAL B 1 220 ? -38.219 -27.672 -42.061 1.00 38.48 ? 229 VAL B O   1 
ATOM   4839 C  CB  . VAL B 1 220 ? -39.219 -30.595 -43.688 1.00 41.63 ? 229 VAL B CB  1 
ATOM   4840 C  CG1 . VAL B 1 220 ? -40.563 -30.223 -43.071 1.00 41.80 ? 229 VAL B CG1 1 
ATOM   4841 C  CG2 . VAL B 1 220 ? -39.437 -31.177 -45.074 1.00 43.81 ? 229 VAL B CG2 1 
ATOM   4842 N  N   . LEU B 1 221 ? -37.341 -29.679 -41.528 1.00 36.90 ? 230 LEU B N   1 
ATOM   4843 C  CA  . LEU B 1 221 ? -37.142 -29.331 -40.117 1.00 35.47 ? 230 LEU B CA  1 
ATOM   4844 C  C   . LEU B 1 221 ? -36.170 -28.163 -39.896 1.00 35.33 ? 230 LEU B C   1 
ATOM   4845 O  O   . LEU B 1 221 ? -36.417 -27.301 -39.045 1.00 35.00 ? 230 LEU B O   1 
ATOM   4846 C  CB  . LEU B 1 221 ? -36.687 -30.557 -39.308 1.00 35.77 ? 230 LEU B CB  1 
ATOM   4847 C  CG  . LEU B 1 221 ? -36.652 -30.440 -37.775 1.00 32.78 ? 230 LEU B CG  1 
ATOM   4848 C  CD1 . LEU B 1 221 ? -37.990 -30.007 -37.183 1.00 33.64 ? 230 LEU B CD1 1 
ATOM   4849 C  CD2 . LEU B 1 221 ? -36.227 -31.763 -37.160 1.00 35.77 ? 230 LEU B CD2 1 
ATOM   4850 N  N   . ARG B 1 222 ? -35.077 -28.142 -40.654 1.00 34.81 ? 231 ARG B N   1 
ATOM   4851 C  CA  . ARG B 1 222 ? -34.115 -27.029 -40.626 1.00 35.39 ? 231 ARG B CA  1 
ATOM   4852 C  C   . ARG B 1 222 ? -34.802 -25.653 -40.727 1.00 34.53 ? 231 ARG B C   1 
ATOM   4853 O  O   . ARG B 1 222 ? -34.452 -24.730 -39.997 1.00 34.36 ? 231 ARG B O   1 
ATOM   4854 C  CB  . ARG B 1 222 ? -33.099 -27.196 -41.764 1.00 36.83 ? 231 ARG B CB  1 
ATOM   4855 C  CG  . ARG B 1 222 ? -32.030 -26.103 -41.862 1.00 38.70 ? 231 ARG B CG  1 
ATOM   4856 C  CD  . ARG B 1 222 ? -31.074 -26.361 -42.998 1.00 38.98 ? 231 ARG B CD  1 
ATOM   4857 N  NE  . ARG B 1 222 ? -31.757 -26.255 -44.289 1.00 45.76 ? 231 ARG B NE  1 
ATOM   4858 C  CZ  . ARG B 1 222 ? -32.035 -25.123 -44.938 1.00 46.75 ? 231 ARG B CZ  1 
ATOM   4859 N  NH1 . ARG B 1 222 ? -31.688 -23.932 -44.456 1.00 49.43 ? 231 ARG B NH1 1 
ATOM   4860 N  NH2 . ARG B 1 222 ? -32.679 -25.187 -46.095 1.00 47.50 ? 231 ARG B NH2 1 
ATOM   4861 N  N   . ILE B 1 223 ? -35.781 -25.543 -41.626 1.00 36.26 ? 232 ILE B N   1 
ATOM   4862 C  CA  . ILE B 1 223 ? -36.551 -24.306 -41.826 1.00 35.15 ? 232 ILE B CA  1 
ATOM   4863 C  C   . ILE B 1 223 ? -37.233 -23.864 -40.531 1.00 32.39 ? 232 ILE B C   1 
ATOM   4864 O  O   . ILE B 1 223 ? -37.032 -22.733 -40.068 1.00 30.96 ? 232 ILE B O   1 
ATOM   4865 C  CB  . ILE B 1 223 ? -37.602 -24.462 -42.989 1.00 38.19 ? 232 ILE B CB  1 
ATOM   4866 C  CG1 . ILE B 1 223 ? -36.916 -24.322 -44.361 1.00 44.75 ? 232 ILE B CG1 1 
ATOM   4867 C  CG2 . ILE B 1 223 ? -38.744 -23.444 -42.885 1.00 40.60 ? 232 ILE B CG2 1 
ATOM   4868 C  CD1 . ILE B 1 223 ? -36.186 -25.541 -44.824 1.00 47.53 ? 232 ILE B CD1 1 
ATOM   4869 N  N   . TYR B 1 224 ? -38.024 -24.758 -39.940 1.00 28.41 ? 233 TYR B N   1 
ATOM   4870 C  CA  . TYR B 1 224 ? -38.798 -24.411 -38.736 1.00 28.11 ? 233 TYR B CA  1 
ATOM   4871 C  C   . TYR B 1 224 ? -37.959 -24.132 -37.498 1.00 27.42 ? 233 TYR B C   1 
ATOM   4872 O  O   . TYR B 1 224 ? -38.385 -23.386 -36.625 1.00 30.99 ? 233 TYR B O   1 
ATOM   4873 C  CB  . TYR B 1 224 ? -39.872 -25.466 -38.446 1.00 27.32 ? 233 TYR B CB  1 
ATOM   4874 C  CG  . TYR B 1 224 ? -40.868 -25.492 -39.568 1.00 28.94 ? 233 TYR B CG  1 
ATOM   4875 C  CD1 . TYR B 1 224 ? -41.824 -24.487 -39.686 1.00 29.19 ? 233 TYR B CD1 1 
ATOM   4876 C  CD2 . TYR B 1 224 ? -40.805 -26.466 -40.558 1.00 21.93 ? 233 TYR B CD2 1 
ATOM   4877 C  CE1 . TYR B 1 224 ? -42.712 -24.468 -40.746 1.00 26.90 ? 233 TYR B CE1 1 
ATOM   4878 C  CE2 . TYR B 1 224 ? -41.698 -26.459 -41.631 1.00 29.50 ? 233 TYR B CE2 1 
ATOM   4879 C  CZ  . TYR B 1 224 ? -42.646 -25.459 -41.711 1.00 25.68 ? 233 TYR B CZ  1 
ATOM   4880 O  OH  . TYR B 1 224 ? -43.519 -25.438 -42.751 1.00 27.26 ? 233 TYR B OH  1 
ATOM   4881 N  N   . LEU B 1 225 ? -36.766 -24.705 -37.429 1.00 28.58 ? 234 LEU B N   1 
ATOM   4882 C  CA  . LEU B 1 225 ? -35.815 -24.380 -36.356 1.00 28.29 ? 234 LEU B CA  1 
ATOM   4883 C  C   . LEU B 1 225 ? -35.034 -23.069 -36.532 1.00 28.18 ? 234 LEU B C   1 
ATOM   4884 O  O   . LEU B 1 225 ? -34.421 -22.606 -35.578 1.00 30.73 ? 234 LEU B O   1 
ATOM   4885 C  CB  . LEU B 1 225 ? -34.817 -25.535 -36.181 1.00 27.72 ? 234 LEU B CB  1 
ATOM   4886 C  CG  . LEU B 1 225 ? -35.428 -26.909 -35.878 1.00 28.93 ? 234 LEU B CG  1 
ATOM   4887 C  CD1 . LEU B 1 225 ? -34.325 -27.953 -35.841 1.00 29.82 ? 234 LEU B CD1 1 
ATOM   4888 C  CD2 . LEU B 1 225 ? -36.243 -26.886 -34.566 1.00 31.29 ? 234 LEU B CD2 1 
ATOM   4889 N  N   A SER B 1 226 ? -35.038 -22.485 -37.728 0.50 30.53 ? 235 SER B N   1 
ATOM   4890 N  N   B SER B 1 226 ? -35.066 -22.485 -37.729 0.50 30.22 ? 235 SER B N   1 
ATOM   4891 C  CA  A SER B 1 226 ? -34.234 -21.278 -37.985 0.50 31.66 ? 235 SER B CA  1 
ATOM   4892 C  CA  B SER B 1 226 ? -34.307 -21.258 -38.025 0.50 31.28 ? 235 SER B CA  1 
ATOM   4893 C  C   A SER B 1 226 ? -34.883 -20.033 -37.371 0.50 32.56 ? 235 SER B C   1 
ATOM   4894 C  C   B SER B 1 226 ? -34.900 -20.044 -37.311 0.50 32.26 ? 235 SER B C   1 
ATOM   4895 O  O   A SER B 1 226 ? -36.104 -19.955 -37.244 0.50 32.72 ? 235 SER B O   1 
ATOM   4896 O  O   B SER B 1 226 ? -36.102 -20.004 -37.040 0.50 32.19 ? 235 SER B O   1 
ATOM   4897 C  CB  A SER B 1 226 ? -33.998 -21.085 -39.482 0.50 32.36 ? 235 SER B CB  1 
ATOM   4898 C  CB  B SER B 1 226 ? -34.262 -21.002 -39.531 0.50 31.49 ? 235 SER B CB  1 
ATOM   4899 O  OG  A SER B 1 226 ? -35.205 -20.821 -40.156 0.50 33.42 ? 235 SER B OG  1 
ATOM   4900 O  OG  B SER B 1 226 ? -33.685 -22.102 -40.208 0.50 31.38 ? 235 SER B OG  1 
ATOM   4901 N  N   . GLY B 1 227 ? -34.046 -19.072 -36.992 1.00 32.20 ? 236 GLY B N   1 
ATOM   4902 C  CA  . GLY B 1 227 ? -34.473 -17.858 -36.302 1.00 31.46 ? 236 GLY B CA  1 
ATOM   4903 C  C   . GLY B 1 227 ? -34.401 -16.621 -37.167 1.00 31.48 ? 236 GLY B C   1 
ATOM   4904 O  O   . GLY B 1 227 ? -34.416 -16.696 -38.401 1.00 32.42 ? 236 GLY B O   1 
ATOM   4905 N  N   . TRP B 1 228 ? -34.330 -15.474 -36.496 1.00 31.67 ? 237 TRP B N   1 
ATOM   4906 C  CA  . TRP B 1 228 ? -34.255 -14.176 -37.160 1.00 33.11 ? 237 TRP B CA  1 
ATOM   4907 C  C   . TRP B 1 228 ? -33.220 -13.269 -36.484 1.00 34.48 ? 237 TRP B C   1 
ATOM   4908 O  O   . TRP B 1 228 ? -33.528 -12.171 -36.048 1.00 34.66 ? 237 TRP B O   1 
ATOM   4909 C  CB  . TRP B 1 228 ? -35.644 -13.532 -37.256 1.00 31.45 ? 237 TRP B CB  1 
ATOM   4910 C  CG  . TRP B 1 228 ? -36.535 -13.795 -36.093 1.00 28.06 ? 237 TRP B CG  1 
ATOM   4911 C  CD1 . TRP B 1 228 ? -36.665 -13.032 -34.963 1.00 27.98 ? 237 TRP B CD1 1 
ATOM   4912 C  CD2 . TRP B 1 228 ? -37.441 -14.892 -35.944 1.00 26.16 ? 237 TRP B CD2 1 
ATOM   4913 N  NE1 . TRP B 1 228 ? -37.593 -13.593 -34.123 1.00 27.49 ? 237 TRP B NE1 1 
ATOM   4914 C  CE2 . TRP B 1 228 ? -38.087 -14.735 -34.700 1.00 23.92 ? 237 TRP B CE2 1 
ATOM   4915 C  CE3 . TRP B 1 228 ? -37.763 -16.003 -36.739 1.00 29.68 ? 237 TRP B CE3 1 
ATOM   4916 C  CZ2 . TRP B 1 228 ? -39.034 -15.654 -34.229 1.00 28.11 ? 237 TRP B CZ2 1 
ATOM   4917 C  CZ3 . TRP B 1 228 ? -38.715 -16.910 -36.271 1.00 25.21 ? 237 TRP B CZ3 1 
ATOM   4918 C  CH2 . TRP B 1 228 ? -39.339 -16.724 -35.034 1.00 22.58 ? 237 TRP B CH2 1 
ATOM   4919 N  N   . LYS B 1 229 ? -31.987 -13.765 -36.418 1.00 36.91 ? 238 LYS B N   1 
ATOM   4920 C  CA  . LYS B 1 229 ? -30.807 -12.971 -36.060 1.00 39.67 ? 238 LYS B CA  1 
ATOM   4921 C  C   . LYS B 1 229 ? -29.728 -13.257 -37.094 1.00 42.39 ? 238 LYS B C   1 
ATOM   4922 O  O   . LYS B 1 229 ? -29.209 -14.375 -37.153 1.00 44.49 ? 238 LYS B O   1 
ATOM   4923 C  CB  . LYS B 1 229 ? -30.321 -13.313 -34.654 1.00 37.83 ? 238 LYS B CB  1 
ATOM   4924 C  CG  . LYS B 1 229 ? -29.007 -12.627 -34.261 1.00 40.59 ? 238 LYS B CG  1 
ATOM   4925 C  CD  . LYS B 1 229 ? -28.904 -12.473 -32.763 1.00 42.57 ? 238 LYS B CD  1 
ATOM   4926 C  CE  . LYS B 1 229 ? -27.559 -11.938 -32.328 1.00 46.54 ? 238 LYS B CE  1 
ATOM   4927 N  NZ  . LYS B 1 229 ? -27.439 -12.028 -30.837 1.00 48.57 ? 238 LYS B NZ  1 
ATOM   4928 N  N   . GLY B 1 230 ? -29.405 -12.253 -37.906 1.00 47.30 ? 239 GLY B N   1 
ATOM   4929 C  CA  . GLY B 1 230 ? -28.525 -12.426 -39.069 1.00 49.52 ? 239 GLY B CA  1 
ATOM   4930 C  C   . GLY B 1 230 ? -29.136 -13.236 -40.212 1.00 51.12 ? 239 GLY B C   1 
ATOM   4931 O  O   . GLY B 1 230 ? -28.399 -13.839 -41.000 1.00 52.30 ? 239 GLY B O   1 
ATOM   4932 N  N   . ASN B 1 231 ? -30.472 -13.250 -40.303 1.00 49.78 ? 240 ASN B N   1 
ATOM   4933 C  CA  . ASN B 1 231 ? -31.200 -13.989 -41.340 1.00 50.25 ? 240 ASN B CA  1 
ATOM   4934 C  C   . ASN B 1 231 ? -31.695 -13.006 -42.402 1.00 52.67 ? 240 ASN B C   1 
ATOM   4935 O  O   . ASN B 1 231 ? -32.515 -12.151 -42.087 1.00 53.33 ? 240 ASN B O   1 
ATOM   4936 C  CB  . ASN B 1 231 ? -32.390 -14.744 -40.725 1.00 49.93 ? 240 ASN B CB  1 
ATOM   4937 C  CG  . ASN B 1 231 ? -33.000 -15.788 -41.675 1.00 49.14 ? 240 ASN B CG  1 
ATOM   4938 O  OD1 . ASN B 1 231 ? -32.920 -15.677 -42.905 1.00 46.11 ? 240 ASN B OD1 1 
ATOM   4939 N  ND2 . ASN B 1 231 ? -33.612 -16.813 -41.090 1.00 47.65 ? 240 ASN B ND2 1 
ATOM   4940 N  N   . PRO B 1 232 ? -31.196 -13.110 -43.657 1.00 55.15 ? 241 PRO B N   1 
ATOM   4941 C  CA  . PRO B 1 232 ? -31.661 -12.232 -44.753 1.00 57.10 ? 241 PRO B CA  1 
ATOM   4942 C  C   . PRO B 1 232 ? -33.178 -12.214 -45.018 1.00 57.09 ? 241 PRO B C   1 
ATOM   4943 O  O   . PRO B 1 232 ? -33.707 -11.191 -45.455 1.00 56.97 ? 241 PRO B O   1 
ATOM   4944 C  CB  . PRO B 1 232 ? -30.922 -12.782 -45.978 1.00 58.29 ? 241 PRO B CB  1 
ATOM   4945 C  CG  . PRO B 1 232 ? -29.723 -13.428 -45.437 1.00 58.11 ? 241 PRO B CG  1 
ATOM   4946 C  CD  . PRO B 1 232 ? -30.136 -14.023 -44.125 1.00 54.80 ? 241 PRO B CD  1 
ATOM   4947 N  N   . GLN B 1 233 ? -33.855 -13.334 -44.756 1.00 57.40 ? 242 GLN B N   1 
ATOM   4948 C  CA  . GLN B 1 233 ? -35.321 -13.426 -44.887 1.00 57.22 ? 242 GLN B CA  1 
ATOM   4949 C  C   . GLN B 1 233 ? -36.071 -12.471 -43.958 1.00 56.22 ? 242 GLN B C   1 
ATOM   4950 O  O   . GLN B 1 233 ? -37.128 -11.947 -44.331 1.00 55.61 ? 242 GLN B O   1 
ATOM   4951 C  CB  . GLN B 1 233 ? -35.796 -14.855 -44.628 1.00 55.65 ? 242 GLN B CB  1 
ATOM   4952 C  CG  . GLN B 1 233 ? -35.345 -15.841 -45.683 1.00 60.39 ? 242 GLN B CG  1 
ATOM   4953 C  CD  . GLN B 1 233 ? -36.038 -17.177 -45.556 1.00 59.41 ? 242 GLN B CD  1 
ATOM   4954 O  OE1 . GLN B 1 233 ? -36.838 -17.556 -46.412 1.00 69.15 ? 242 GLN B OE1 1 
ATOM   4955 N  NE2 . GLN B 1 233 ? -35.750 -17.892 -44.477 1.00 63.56 ? 242 GLN B NE2 1 
ATOM   4956 N  N   . LEU B 1 234 ? -35.535 -12.277 -42.750 1.00 54.38 ? 243 LEU B N   1 
ATOM   4957 C  CA  . LEU B 1 234 ? -36.024 -11.261 -41.815 1.00 55.16 ? 243 LEU B CA  1 
ATOM   4958 C  C   . LEU B 1 234 ? -34.837 -10.416 -41.348 1.00 54.99 ? 243 LEU B C   1 
ATOM   4959 O  O   . LEU B 1 234 ? -34.415 -10.509 -40.194 1.00 53.48 ? 243 LEU B O   1 
ATOM   4960 C  CB  . LEU B 1 234 ? -36.732 -11.910 -40.612 1.00 54.76 ? 243 LEU B CB  1 
ATOM   4961 C  CG  . LEU B 1 234 ? -37.978 -12.767 -40.870 1.00 53.88 ? 243 LEU B CG  1 
ATOM   4962 C  CD1 . LEU B 1 234 ? -37.606 -14.193 -41.187 1.00 55.87 ? 243 LEU B CD1 1 
ATOM   4963 C  CD2 . LEU B 1 234 ? -38.894 -12.760 -39.663 1.00 53.47 ? 243 LEU B CD2 1 
ATOM   4964 N  N   . SER B 1 235 ? -34.307 -9.601  -42.263 1.00 56.34 ? 244 SER B N   1 
ATOM   4965 C  CA  . SER B 1 235 ? -33.080 -8.804  -42.042 1.00 56.48 ? 244 SER B CA  1 
ATOM   4966 C  C   . SER B 1 235 ? -33.065 -7.994  -40.743 1.00 54.10 ? 244 SER B C   1 
ATOM   4967 O  O   . SER B 1 235 ? -32.036 -7.916  -40.076 1.00 54.10 ? 244 SER B O   1 
ATOM   4968 C  CB  . SER B 1 235 ? -32.850 -7.836  -43.217 1.00 61.03 ? 244 SER B CB  1 
ATOM   4969 O  OG  . SER B 1 235 ? -32.558 -8.535  -44.415 1.00 66.42 ? 244 SER B OG  1 
ATOM   4970 N  N   . ASP B 1 236 ? -34.201 -7.385  -40.406 1.00 52.08 ? 245 ASP B N   1 
ATOM   4971 C  CA  . ASP B 1 236 ? -34.320 -6.552  -39.205 1.00 50.79 ? 245 ASP B CA  1 
ATOM   4972 C  C   . ASP B 1 236 ? -34.980 -7.266  -38.018 1.00 46.40 ? 245 ASP B C   1 
ATOM   4973 O  O   . ASP B 1 236 ? -35.262 -6.631  -37.003 1.00 44.40 ? 245 ASP B O   1 
ATOM   4974 C  CB  . ASP B 1 236 ? -35.091 -5.279  -39.543 1.00 55.80 ? 245 ASP B CB  1 
ATOM   4975 C  CG  . ASP B 1 236 ? -34.442 -4.492  -40.670 1.00 63.72 ? 245 ASP B CG  1 
ATOM   4976 O  OD1 . ASP B 1 236 ? -33.362 -3.908  -40.436 1.00 66.62 ? 245 ASP B OD1 1 
ATOM   4977 O  OD2 . ASP B 1 236 ? -35.013 -4.465  -41.785 1.00 68.59 ? 245 ASP B OD2 1 
ATOM   4978 N  N   . GLY B 1 237 ? -35.196 -8.580  -38.130 1.00 40.68 ? 246 GLY B N   1 
ATOM   4979 C  CA  . GLY B 1 237 ? -35.856 -9.349  -37.090 1.00 38.18 ? 246 GLY B CA  1 
ATOM   4980 C  C   . GLY B 1 237 ? -37.364 -9.410  -37.256 1.00 37.09 ? 246 GLY B C   1 
ATOM   4981 O  O   . GLY B 1 237 ? -37.887 -9.104  -38.325 1.00 37.62 ? 246 GLY B O   1 
ATOM   4982 N  N   . LEU B 1 238 ? -38.051 -9.804  -36.182 1.00 36.12 ? 247 LEU B N   1 
ATOM   4983 C  CA  . LEU B 1 238 ? -39.506 -10.002 -36.169 1.00 34.35 ? 247 LEU B CA  1 
ATOM   4984 C  C   . LEU B 1 238 ? -40.191 -8.907  -35.362 1.00 33.68 ? 247 LEU B C   1 
ATOM   4985 O  O   . LEU B 1 238 ? -39.741 -8.566  -34.262 1.00 32.56 ? 247 LEU B O   1 
ATOM   4986 C  CB  . LEU B 1 238 ? -39.842 -11.365 -35.533 1.00 34.14 ? 247 LEU B CB  1 
ATOM   4987 C  CG  . LEU B 1 238 ? -41.279 -11.880 -35.651 1.00 31.67 ? 247 LEU B CG  1 
ATOM   4988 C  CD1 . LEU B 1 238 ? -41.593 -12.256 -37.081 1.00 34.15 ? 247 LEU B CD1 1 
ATOM   4989 C  CD2 . LEU B 1 238 ? -41.512 -13.083 -34.761 1.00 32.02 ? 247 LEU B CD2 1 
ATOM   4990 N  N   . VAL B 1 239 ? -41.277 -8.365  -35.906 1.00 34.30 ? 248 VAL B N   1 
ATOM   4991 C  CA  . VAL B 1 239 ? -42.144 -7.460  -35.160 1.00 35.83 ? 248 VAL B CA  1 
ATOM   4992 C  C   . VAL B 1 239 ? -43.062 -8.324  -34.279 1.00 33.92 ? 248 VAL B C   1 
ATOM   4993 O  O   . VAL B 1 239 ? -43.861 -9.112  -34.790 1.00 32.91 ? 248 VAL B O   1 
ATOM   4994 C  CB  . VAL B 1 239 ? -42.974 -6.526  -36.092 1.00 37.45 ? 248 VAL B CB  1 
ATOM   4995 C  CG1 . VAL B 1 239 ? -43.969 -5.667  -35.293 1.00 39.46 ? 248 VAL B CG1 1 
ATOM   4996 C  CG2 . VAL B 1 239 ? -42.052 -5.614  -36.884 1.00 37.93 ? 248 VAL B CG2 1 
ATOM   4997 N  N   . TYR B 1 240 ? -42.907 -8.183  -32.964 1.00 32.82 ? 249 TYR B N   1 
ATOM   4998 C  CA  . TYR B 1 240 ? -43.806 -8.770  -31.977 1.00 32.57 ? 249 TYR B CA  1 
ATOM   4999 C  C   . TYR B 1 240 ? -44.874 -7.740  -31.672 1.00 33.99 ? 249 TYR B C   1 
ATOM   5000 O  O   . TYR B 1 240 ? -44.723 -6.922  -30.761 1.00 35.07 ? 249 TYR B O   1 
ATOM   5001 C  CB  . TYR B 1 240 ? -43.044 -9.153  -30.709 1.00 34.55 ? 249 TYR B CB  1 
ATOM   5002 C  CG  . TYR B 1 240 ? -42.060 -10.283 -30.933 1.00 31.64 ? 249 TYR B CG  1 
ATOM   5003 C  CD1 . TYR B 1 240 ? -40.819 -10.041 -31.514 1.00 28.28 ? 249 TYR B CD1 1 
ATOM   5004 C  CD2 . TYR B 1 240 ? -42.376 -11.591 -30.570 1.00 31.37 ? 249 TYR B CD2 1 
ATOM   5005 C  CE1 . TYR B 1 240 ? -39.911 -11.069 -31.729 1.00 33.97 ? 249 TYR B CE1 1 
ATOM   5006 C  CE2 . TYR B 1 240 ? -41.475 -12.629 -30.776 1.00 32.18 ? 249 TYR B CE2 1 
ATOM   5007 C  CZ  . TYR B 1 240 ? -40.241 -12.358 -31.357 1.00 29.71 ? 249 TYR B CZ  1 
ATOM   5008 O  OH  . TYR B 1 240 ? -39.347 -13.363 -31.568 1.00 30.76 ? 249 TYR B OH  1 
ATOM   5009 N  N   . GLU B 1 241 ? -45.946 -7.780  -32.463 1.00 34.20 ? 250 GLU B N   1 
ATOM   5010 C  CA  . GLU B 1 241 ? -46.961 -6.727  -32.476 1.00 35.34 ? 250 GLU B CA  1 
ATOM   5011 C  C   . GLU B 1 241 ? -47.597 -6.554  -31.099 1.00 35.85 ? 250 GLU B C   1 
ATOM   5012 O  O   . GLU B 1 241 ? -47.907 -7.537  -30.430 1.00 36.13 ? 250 GLU B O   1 
ATOM   5013 C  CB  . GLU B 1 241 ? -48.044 -7.055  -33.505 1.00 35.80 ? 250 GLU B CB  1 
ATOM   5014 C  CG  . GLU B 1 241 ? -49.022 -5.896  -33.776 1.00 39.38 ? 250 GLU B CG  1 
ATOM   5015 C  CD  . GLU B 1 241 ? -50.163 -6.308  -34.680 1.00 40.15 ? 250 GLU B CD  1 
ATOM   5016 O  OE1 . GLU B 1 241 ? -50.714 -7.410  -34.475 1.00 44.52 ? 250 GLU B OE1 1 
ATOM   5017 O  OE2 . GLU B 1 241 ? -50.511 -5.532  -35.590 1.00 46.61 ? 250 GLU B OE2 1 
ATOM   5018 N  N   . GLY B 1 242 ? -47.744 -5.304  -30.663 1.00 37.92 ? 251 GLY B N   1 
ATOM   5019 C  CA  . GLY B 1 242 ? -48.302 -4.998  -29.348 1.00 38.33 ? 251 GLY B CA  1 
ATOM   5020 C  C   . GLY B 1 242 ? -47.363 -5.107  -28.156 1.00 38.16 ? 251 GLY B C   1 
ATOM   5021 O  O   . GLY B 1 242 ? -47.734 -4.698  -27.052 1.00 39.54 ? 251 GLY B O   1 
ATOM   5022 N  N   . PHE B 1 243 ? -46.156 -5.639  -28.354 1.00 37.82 ? 252 PHE B N   1 
ATOM   5023 C  CA  . PHE B 1 243 ? -45.187 -5.772  -27.268 1.00 38.77 ? 252 PHE B CA  1 
ATOM   5024 C  C   . PHE B 1 243 ? -44.015 -4.813  -27.477 1.00 39.25 ? 252 PHE B C   1 
ATOM   5025 O  O   . PHE B 1 243 ? -43.719 -4.020  -26.589 1.00 40.23 ? 252 PHE B O   1 
ATOM   5026 C  CB  . PHE B 1 243 ? -44.716 -7.223  -27.090 1.00 37.07 ? 252 PHE B CB  1 
ATOM   5027 C  CG  . PHE B 1 243 ? -44.114 -7.474  -25.739 1.00 37.64 ? 252 PHE B CG  1 
ATOM   5028 C  CD1 . PHE B 1 243 ? -44.929 -7.690  -24.632 1.00 40.12 ? 252 PHE B CD1 1 
ATOM   5029 C  CD2 . PHE B 1 243 ? -42.745 -7.417  -25.554 1.00 37.82 ? 252 PHE B CD2 1 
ATOM   5030 C  CE1 . PHE B 1 243 ? -44.380 -7.881  -23.366 1.00 36.99 ? 252 PHE B CE1 1 
ATOM   5031 C  CE2 . PHE B 1 243 ? -42.188 -7.601  -24.287 1.00 37.09 ? 252 PHE B CE2 1 
ATOM   5032 C  CZ  . PHE B 1 243 ? -43.009 -7.839  -23.198 1.00 36.34 ? 252 PHE B CZ  1 
ATOM   5033 N  N   . TRP B 1 244 ? -43.372 -4.884  -28.646 1.00 39.64 ? 253 TRP B N   1 
ATOM   5034 C  CA  . TRP B 1 244 ? -42.387 -3.878  -29.094 1.00 43.44 ? 253 TRP B CA  1 
ATOM   5035 C  C   . TRP B 1 244 ? -42.781 -3.292  -30.453 1.00 45.00 ? 253 TRP B C   1 
ATOM   5036 O  O   . TRP B 1 244 ? -43.306 -4.002  -31.318 1.00 43.72 ? 253 TRP B O   1 
ATOM   5037 C  CB  . TRP B 1 244 ? -40.988 -4.483  -29.247 1.00 42.90 ? 253 TRP B CB  1 
ATOM   5038 C  CG  . TRP B 1 244 ? -40.404 -5.068  -28.023 1.00 43.57 ? 253 TRP B CG  1 
ATOM   5039 C  CD1 . TRP B 1 244 ? -40.017 -4.402  -26.899 1.00 44.06 ? 253 TRP B CD1 1 
ATOM   5040 C  CD2 . TRP B 1 244 ? -40.068 -6.448  -27.812 1.00 37.91 ? 253 TRP B CD2 1 
ATOM   5041 N  NE1 . TRP B 1 244 ? -39.489 -5.287  -25.986 1.00 43.48 ? 253 TRP B NE1 1 
ATOM   5042 C  CE2 . TRP B 1 244 ? -39.512 -6.548  -26.518 1.00 38.22 ? 253 TRP B CE2 1 
ATOM   5043 C  CE3 . TRP B 1 244 ? -40.214 -7.615  -28.579 1.00 38.83 ? 253 TRP B CE3 1 
ATOM   5044 C  CZ2 . TRP B 1 244 ? -39.082 -7.770  -25.977 1.00 38.57 ? 253 TRP B CZ2 1 
ATOM   5045 C  CZ3 . TRP B 1 244 ? -39.787 -8.830  -28.043 1.00 34.00 ? 253 TRP B CZ3 1 
ATOM   5046 C  CH2 . TRP B 1 244 ? -39.232 -8.896  -26.751 1.00 37.88 ? 253 TRP B CH2 1 
ATOM   5047 N  N   . GLU B 1 245 ? -42.480 -2.010  -30.646 1.00 49.11 ? 254 GLU B N   1 
ATOM   5048 C  CA  . GLU B 1 245 ? -42.794 -1.304  -31.896 1.00 51.17 ? 254 GLU B CA  1 
ATOM   5049 C  C   . GLU B 1 245 ? -41.877 -1.667  -33.065 1.00 51.78 ? 254 GLU B C   1 
ATOM   5050 O  O   . GLU B 1 245 ? -42.347 -1.764  -34.207 1.00 53.59 ? 254 GLU B O   1 
ATOM   5051 C  CB  . GLU B 1 245 ? -42.784 0.207   -31.680 1.00 55.90 ? 254 GLU B CB  1 
ATOM   5052 C  CG  . GLU B 1 245 ? -43.974 0.698   -30.874 1.00 58.92 ? 254 GLU B CG  1 
ATOM   5053 C  CD  . GLU B 1 245 ? -44.360 2.112   -31.214 1.00 61.17 ? 254 GLU B CD  1 
ATOM   5054 O  OE1 . GLU B 1 245 ? -45.501 2.316   -31.687 1.00 57.18 ? 254 GLU B OE1 1 
ATOM   5055 O  OE2 . GLU B 1 245 ? -43.515 3.012   -31.013 1.00 70.62 ? 254 GLU B OE2 1 
ATOM   5056 N  N   . ASP B 1 246 ? -40.589 -1.870  -32.781 1.00 48.92 ? 255 ASP B N   1 
ATOM   5057 C  CA  . ASP B 1 246 ? -39.598 -2.188  -33.812 1.00 47.10 ? 255 ASP B CA  1 
ATOM   5058 C  C   . ASP B 1 246 ? -39.292 -3.674  -33.849 1.00 43.89 ? 255 ASP B C   1 
ATOM   5059 O  O   . ASP B 1 246 ? -39.441 -4.361  -32.834 1.00 41.28 ? 255 ASP B O   1 
ATOM   5060 C  CB  . ASP B 1 246 ? -38.308 -1.394  -33.574 1.00 47.83 ? 255 ASP B CB  1 
ATOM   5061 C  CG  . ASP B 1 246 ? -38.473 0.093   -33.875 1.00 53.96 ? 255 ASP B CG  1 
ATOM   5062 O  OD1 . ASP B 1 246 ? -39.353 0.463   -34.689 1.00 51.74 ? 255 ASP B OD1 1 
ATOM   5063 O  OD2 . ASP B 1 246 ? -37.720 0.892   -33.292 1.00 56.89 ? 255 ASP B OD2 1 
ATOM   5064 N  N   . PRO B 1 247 ? -38.834 -4.174  -35.011 1.00 42.72 ? 256 PRO B N   1 
ATOM   5065 C  CA  . PRO B 1 247 ? -38.542 -5.602  -35.086 1.00 40.78 ? 256 PRO B CA  1 
ATOM   5066 C  C   . PRO B 1 247 ? -37.324 -5.967  -34.236 1.00 38.52 ? 256 PRO B C   1 
ATOM   5067 O  O   . PRO B 1 247 ? -36.401 -5.169  -34.111 1.00 37.90 ? 256 PRO B O   1 
ATOM   5068 C  CB  . PRO B 1 247 ? -38.285 -5.830  -36.577 1.00 41.36 ? 256 PRO B CB  1 
ATOM   5069 C  CG  . PRO B 1 247 ? -37.764 -4.510  -37.066 1.00 44.22 ? 256 PRO B CG  1 
ATOM   5070 C  CD  . PRO B 1 247 ? -38.540 -3.485  -36.285 1.00 44.65 ? 256 PRO B CD  1 
ATOM   5071 N  N   . LYS B 1 248 ? -37.366 -7.148  -33.630 1.00 36.02 ? 257 LYS B N   1 
ATOM   5072 C  CA  . LYS B 1 248 ? -36.317 -7.621  -32.734 1.00 36.39 ? 257 LYS B CA  1 
ATOM   5073 C  C   . LYS B 1 248 ? -35.732 -8.897  -33.314 1.00 36.87 ? 257 LYS B C   1 
ATOM   5074 O  O   . LYS B 1 248 ? -36.473 -9.760  -33.806 1.00 34.17 ? 257 LYS B O   1 
ATOM   5075 C  CB  . LYS B 1 248 ? -36.878 -7.892  -31.336 1.00 35.87 ? 257 LYS B CB  1 
ATOM   5076 C  CG  . LYS B 1 248 ? -37.553 -6.685  -30.677 1.00 38.98 ? 257 LYS B CG  1 
ATOM   5077 C  CD  . LYS B 1 248 ? -36.558 -5.691  -30.110 1.00 41.11 ? 257 LYS B CD  1 
ATOM   5078 C  CE  . LYS B 1 248 ? -37.142 -4.304  -30.037 1.00 46.35 ? 257 LYS B CE  1 
ATOM   5079 N  NZ  . LYS B 1 248 ? -36.355 -3.418  -29.147 1.00 50.42 ? 257 LYS B NZ  1 
ATOM   5080 N  N   . GLU B 1 249 ? -34.406 -8.993  -33.267 1.00 36.59 ? 258 GLU B N   1 
ATOM   5081 C  CA  . GLU B 1 249 ? -33.673 -10.146 -33.771 1.00 36.73 ? 258 GLU B CA  1 
ATOM   5082 C  C   . GLU B 1 249 ? -33.411 -11.118 -32.636 1.00 34.61 ? 258 GLU B C   1 
ATOM   5083 O  O   . GLU B 1 249 ? -32.917 -10.718 -31.591 1.00 32.27 ? 258 GLU B O   1 
ATOM   5084 C  CB  . GLU B 1 249 ? -32.330 -9.725  -34.389 1.00 38.97 ? 258 GLU B CB  1 
ATOM   5085 C  CG  . GLU B 1 249 ? -32.432 -9.132  -35.786 1.00 42.64 ? 258 GLU B CG  1 
ATOM   5086 C  CD  . GLU B 1 249 ? -31.074 -9.036  -36.465 1.00 46.75 ? 258 GLU B CD  1 
ATOM   5087 O  OE1 . GLU B 1 249 ? -30.243 -8.227  -36.002 1.00 53.10 ? 258 GLU B OE1 1 
ATOM   5088 O  OE2 . GLU B 1 249 ? -30.838 -9.770  -37.454 1.00 51.00 ? 258 GLU B OE2 1 
ATOM   5089 N  N   . PHE B 1 250 ? -33.770 -12.387 -32.834 1.00 33.86 ? 259 PHE B N   1 
ATOM   5090 C  CA  . PHE B 1 250 ? -33.458 -13.456 -31.873 1.00 31.44 ? 259 PHE B CA  1 
ATOM   5091 C  C   . PHE B 1 250 ? -32.953 -14.668 -32.627 1.00 30.06 ? 259 PHE B C   1 
ATOM   5092 O  O   . PHE B 1 250 ? -33.447 -14.971 -33.714 1.00 28.85 ? 259 PHE B O   1 
ATOM   5093 C  CB  . PHE B 1 250 ? -34.686 -13.824 -31.037 1.00 31.60 ? 259 PHE B CB  1 
ATOM   5094 C  CG  . PHE B 1 250 ? -35.180 -12.704 -30.166 1.00 30.24 ? 259 PHE B CG  1 
ATOM   5095 C  CD1 . PHE B 1 250 ? -34.401 -12.237 -29.108 1.00 33.96 ? 259 PHE B CD1 1 
ATOM   5096 C  CD2 . PHE B 1 250 ? -36.415 -12.115 -30.397 1.00 29.35 ? 259 PHE B CD2 1 
ATOM   5097 C  CE1 . PHE B 1 250 ? -34.841 -11.200 -28.293 1.00 35.57 ? 259 PHE B CE1 1 
ATOM   5098 C  CE2 . PHE B 1 250 ? -36.873 -11.068 -29.588 1.00 33.75 ? 259 PHE B CE2 1 
ATOM   5099 C  CZ  . PHE B 1 250 ? -36.085 -10.606 -28.537 1.00 39.02 ? 259 PHE B CZ  1 
ATOM   5100 N  N   . ALA B 1 251 ? -31.958 -15.346 -32.057 1.00 29.95 ? 260 ALA B N   1 
ATOM   5101 C  CA  . ALA B 1 251 ? -31.343 -16.502 -32.711 1.00 31.38 ? 260 ALA B CA  1 
ATOM   5102 C  C   . ALA B 1 251 ? -32.244 -17.727 -32.646 1.00 28.93 ? 260 ALA B C   1 
ATOM   5103 O  O   . ALA B 1 251 ? -32.968 -17.944 -31.664 1.00 27.70 ? 260 ALA B O   1 
ATOM   5104 C  CB  . ALA B 1 251 ? -29.983 -16.824 -32.086 1.00 32.15 ? 260 ALA B CB  1 
ATOM   5105 N  N   . GLY B 1 252 ? -32.183 -18.527 -33.705 1.00 28.41 ? 261 GLY B N   1 
ATOM   5106 C  CA  . GLY B 1 252 ? -32.856 -19.811 -33.749 1.00 28.41 ? 261 GLY B CA  1 
ATOM   5107 C  C   . GLY B 1 252 ? -32.169 -20.811 -32.846 1.00 27.92 ? 261 GLY B C   1 
ATOM   5108 O  O   . GLY B 1 252 ? -31.094 -20.545 -32.308 1.00 27.49 ? 261 GLY B O   1 
ATOM   5109 N  N   . GLY B 1 253 ? -32.794 -21.969 -32.675 1.00 26.51 ? 262 GLY B N   1 
ATOM   5110 C  CA  . GLY B 1 253 ? -32.286 -22.991 -31.768 1.00 26.36 ? 262 GLY B CA  1 
ATOM   5111 C  C   . GLY B 1 253 ? -30.878 -23.457 -32.108 1.00 24.94 ? 262 GLY B C   1 
ATOM   5112 O  O   . GLY B 1 253 ? -30.475 -23.464 -33.269 1.00 24.80 ? 262 GLY B O   1 
ATOM   5113 N  N   . SER B 1 254 ? -30.130 -23.808 -31.070 1.00 26.64 ? 263 SER B N   1 
ATOM   5114 C  CA  . SER B 1 254 ? -28.774 -24.339 -31.195 1.00 25.82 ? 263 SER B CA  1 
ATOM   5115 C  C   . SER B 1 254 ? -28.549 -25.215 -29.998 1.00 25.97 ? 263 SER B C   1 
ATOM   5116 O  O   . SER B 1 254 ? -29.000 -24.863 -28.913 1.00 24.00 ? 263 SER B O   1 
ATOM   5117 C  CB  . SER B 1 254 ? -27.755 -23.208 -31.194 1.00 26.64 ? 263 SER B CB  1 
ATOM   5118 O  OG  . SER B 1 254 ? -26.441 -23.716 -31.046 1.00 28.76 ? 263 SER B OG  1 
ATOM   5119 N  N   . ALA B 1 255 ? -27.851 -26.340 -30.170 1.00 23.78 ? 264 ALA B N   1 
ATOM   5120 C  CA  . ALA B 1 255 ? -27.397 -27.109 -29.014 1.00 24.01 ? 264 ALA B CA  1 
ATOM   5121 C  C   . ALA B 1 255 ? -26.192 -26.435 -28.317 1.00 22.44 ? 264 ALA B C   1 
ATOM   5122 O  O   . ALA B 1 255 ? -25.744 -26.903 -27.290 1.00 21.56 ? 264 ALA B O   1 
ATOM   5123 C  CB  . ALA B 1 255 ? -27.097 -28.542 -29.382 1.00 23.81 ? 264 ALA B CB  1 
ATOM   5124 N  N   . GLY B 1 256 ? -25.695 -25.319 -28.850 1.00 22.96 ? 265 GLY B N   1 
ATOM   5125 C  CA  . GLY B 1 256 ? -24.951 -24.347 -28.044 1.00 22.68 ? 265 GLY B CA  1 
ATOM   5126 C  C   . GLY B 1 256 ? -25.755 -23.815 -26.860 1.00 22.63 ? 265 GLY B C   1 
ATOM   5127 O  O   . GLY B 1 256 ? -25.181 -23.320 -25.870 1.00 21.96 ? 265 GLY B O   1 
ATOM   5128 N  N   . GLN B 1 257 ? -27.084 -23.917 -26.958 1.00 21.23 ? 266 GLN B N   1 
ATOM   5129 C  CA  . GLN B 1 257 ? -27.985 -23.602 -25.846 1.00 22.36 ? 266 GLN B CA  1 
ATOM   5130 C  C   . GLN B 1 257 ? -28.097 -24.751 -24.836 1.00 22.82 ? 266 GLN B C   1 
ATOM   5131 O  O   . GLN B 1 257 ? -28.726 -24.592 -23.804 1.00 24.14 ? 266 GLN B O   1 
ATOM   5132 C  CB  . GLN B 1 257 ? -29.378 -23.225 -26.356 1.00 21.30 ? 266 GLN B CB  1 
ATOM   5133 C  CG  . GLN B 1 257 ? -29.392 -22.105 -27.389 1.00 23.60 ? 266 GLN B CG  1 
ATOM   5134 C  CD  . GLN B 1 257 ? -30.737 -21.926 -28.078 1.00 24.94 ? 266 GLN B CD  1 
ATOM   5135 O  OE1 . GLN B 1 257 ? -31.542 -22.852 -28.138 1.00 26.24 ? 266 GLN B OE1 1 
ATOM   5136 N  NE2 . GLN B 1 257 ? -30.967 -20.735 -28.636 1.00 21.52 ? 266 GLN B NE2 1 
ATOM   5137 N  N   . SER B 1 258 ? -27.497 -25.906 -25.119 1.00 23.42 ? 267 SER B N   1 
ATOM   5138 C  CA  . SER B 1 258 ? -27.485 -27.007 -24.164 1.00 23.13 ? 267 SER B CA  1 
ATOM   5139 C  C   . SER B 1 258 ? -26.536 -26.652 -23.040 1.00 24.09 ? 267 SER B C   1 
ATOM   5140 O  O   . SER B 1 258 ? -25.388 -26.286 -23.281 1.00 24.03 ? 267 SER B O   1 
ATOM   5141 C  CB  . SER B 1 258 ? -27.034 -28.310 -24.817 1.00 24.80 ? 267 SER B CB  1 
ATOM   5142 O  OG  . SER B 1 258 ? -26.777 -29.269 -23.830 1.00 25.63 ? 267 SER B OG  1 
ATOM   5143 N  N   . SER B 1 259 ? -27.026 -26.747 -21.815 1.00 25.56 ? 268 SER B N   1 
ATOM   5144 C  CA  . SER B 1 259 ? -26.215 -26.471 -20.654 1.00 27.06 ? 268 SER B CA  1 
ATOM   5145 C  C   . SER B 1 259 ? -25.191 -27.568 -20.314 1.00 28.75 ? 268 SER B C   1 
ATOM   5146 O  O   . SER B 1 259 ? -24.212 -27.247 -19.659 1.00 28.80 ? 268 SER B O   1 
ATOM   5147 C  CB  . SER B 1 259 ? -27.094 -26.151 -19.438 1.00 26.29 ? 268 SER B CB  1 
ATOM   5148 O  OG  . SER B 1 259 ? -27.883 -24.988 -19.675 1.00 25.62 ? 268 SER B OG  1 
ATOM   5149 N  N   A VAL B 1 260 ? -25.413 -28.827 -20.735 0.50 29.19 ? 269 VAL B N   1 
ATOM   5150 N  N   B VAL B 1 260 ? -25.395 -28.811 -20.761 0.50 29.34 ? 269 VAL B N   1 
ATOM   5151 C  CA  A VAL B 1 260 ? -24.494 -29.946 -20.377 0.50 29.24 ? 269 VAL B CA  1 
ATOM   5152 C  CA  B VAL B 1 260 ? -24.517 -29.919 -20.348 0.50 29.11 ? 269 VAL B CA  1 
ATOM   5153 C  C   A VAL B 1 260 ? -23.112 -29.779 -20.990 0.50 28.95 ? 269 VAL B C   1 
ATOM   5154 C  C   B VAL B 1 260 ? -23.125 -29.823 -20.995 0.50 28.93 ? 269 VAL B C   1 
ATOM   5155 O  O   A VAL B 1 260 ? -22.103 -29.841 -20.286 0.50 30.42 ? 269 VAL B O   1 
ATOM   5156 O  O   B VAL B 1 260 ? -22.117 -29.951 -20.305 0.50 30.70 ? 269 VAL B O   1 
ATOM   5157 C  CB  A VAL B 1 260 ? -25.014 -31.425 -20.705 0.50 30.00 ? 269 VAL B CB  1 
ATOM   5158 C  CB  B VAL B 1 260 ? -25.200 -31.337 -20.510 0.50 29.79 ? 269 VAL B CB  1 
ATOM   5159 C  CG1 A VAL B 1 260 ? -26.048 -31.877 -19.727 0.50 32.72 ? 269 VAL B CG1 1 
ATOM   5160 C  CG1 B VAL B 1 260 ? -25.339 -31.774 -21.957 0.50 28.12 ? 269 VAL B CG1 1 
ATOM   5161 C  CG2 A VAL B 1 260 ? -25.556 -31.598 -22.103 0.50 29.27 ? 269 VAL B CG2 1 
ATOM   5162 C  CG2 B VAL B 1 260 ? -24.442 -32.394 -19.707 0.50 31.53 ? 269 VAL B CG2 1 
ATOM   5163 N  N   . PHE B 1 261 ? -23.067 -29.534 -22.290 1.00 28.88 ? 270 PHE B N   1 
ATOM   5164 C  CA  . PHE B 1 261 ? -21.782 -29.403 -22.995 1.00 29.13 ? 270 PHE B CA  1 
ATOM   5165 C  C   . PHE B 1 261 ? -21.039 -28.120 -22.642 1.00 29.10 ? 270 PHE B C   1 
ATOM   5166 O  O   . PHE B 1 261 ? -19.814 -28.133 -22.456 1.00 29.73 ? 270 PHE B O   1 
ATOM   5167 C  CB  . PHE B 1 261 ? -21.997 -29.588 -24.482 1.00 32.40 ? 270 PHE B CB  1 
ATOM   5168 C  CG  . PHE B 1 261 ? -22.701 -30.873 -24.788 1.00 36.04 ? 270 PHE B CG  1 
ATOM   5169 C  CD1 . PHE B 1 261 ? -22.095 -32.091 -24.461 1.00 38.95 ? 270 PHE B CD1 1 
ATOM   5170 C  CD2 . PHE B 1 261 ? -23.993 -30.879 -25.296 1.00 36.27 ? 270 PHE B CD2 1 
ATOM   5171 C  CE1 . PHE B 1 261 ? -22.751 -33.293 -24.679 1.00 38.88 ? 270 PHE B CE1 1 
ATOM   5172 C  CE2 . PHE B 1 261 ? -24.660 -32.084 -25.517 1.00 35.49 ? 270 PHE B CE2 1 
ATOM   5173 C  CZ  . PHE B 1 261 ? -24.032 -33.290 -25.211 1.00 35.33 ? 270 PHE B CZ  1 
ATOM   5174 N  N   . GLN B 1 262 ? -21.786 -27.033 -22.480 1.00 26.69 ? 271 GLN B N   1 
ATOM   5175 C  CA  . GLN B 1 262 ? -21.232 -25.815 -21.927 1.00 27.10 ? 271 GLN B CA  1 
ATOM   5176 C  C   . GLN B 1 262 ? -20.660 -26.015 -20.519 1.00 27.05 ? 271 GLN B C   1 
ATOM   5177 O  O   . GLN B 1 262 ? -19.583 -25.497 -20.228 1.00 28.07 ? 271 GLN B O   1 
ATOM   5178 C  CB  . GLN B 1 262 ? -22.266 -24.681 -21.940 1.00 27.40 ? 271 GLN B CB  1 
ATOM   5179 C  CG  . GLN B 1 262 ? -22.602 -24.174 -23.357 1.00 26.72 ? 271 GLN B CG  1 
ATOM   5180 C  CD  . GLN B 1 262 ? -22.467 -22.664 -23.514 1.00 24.43 ? 271 GLN B CD  1 
ATOM   5181 O  OE1 . GLN B 1 262 ? -21.701 -22.017 -22.796 1.00 22.60 ? 271 GLN B OE1 1 
ATOM   5182 N  NE2 . GLN B 1 262 ? -23.214 -22.100 -24.454 1.00 21.80 ? 271 GLN B NE2 1 
ATOM   5183 N  N   A CYS B 1 263 ? -21.355 -26.770 -19.664 0.50 27.17 ? 272 CYS B N   1 
ATOM   5184 N  N   B CYS B 1 263 ? -21.365 -26.762 -19.670 0.50 26.62 ? 272 CYS B N   1 
ATOM   5185 C  CA  A CYS B 1 263 ? -20.895 -26.975 -18.282 0.50 28.75 ? 272 CYS B CA  1 
ATOM   5186 C  CA  B CYS B 1 263 ? -20.908 -27.009 -18.294 0.50 27.80 ? 272 CYS B CA  1 
ATOM   5187 C  C   A CYS B 1 263 ? -19.617 -27.822 -18.200 0.50 28.34 ? 272 CYS B C   1 
ATOM   5188 C  C   B CYS B 1 263 ? -19.608 -27.807 -18.227 0.50 27.78 ? 272 CYS B C   1 
ATOM   5189 O  O   A CYS B 1 263 ? -18.743 -27.529 -17.384 0.50 28.57 ? 272 CYS B O   1 
ATOM   5190 O  O   B CYS B 1 263 ? -18.718 -27.474 -17.446 0.50 28.00 ? 272 CYS B O   1 
ATOM   5191 C  CB  A CYS B 1 263 ? -21.998 -27.544 -17.373 0.50 29.67 ? 272 CYS B CB  1 
ATOM   5192 C  CB  B CYS B 1 263 ? -21.987 -27.693 -17.449 0.50 28.11 ? 272 CYS B CB  1 
ATOM   5193 S  SG  A CYS B 1 263 ? -22.201 -29.340 -17.357 0.50 34.49 ? 272 CYS B SG  1 
ATOM   5194 S  SG  B CYS B 1 263 ? -23.101 -26.515 -16.677 0.50 29.00 ? 272 CYS B SG  1 
ATOM   5195 N  N   . PHE B 1 264 ? -19.503 -28.852 -19.039 1.00 27.04 ? 273 PHE B N   1 
ATOM   5196 C  CA  . PHE B 1 264 ? -18.260 -29.657 -19.083 1.00 29.07 ? 273 PHE B CA  1 
ATOM   5197 C  C   . PHE B 1 264 ? -17.092 -28.920 -19.712 1.00 27.34 ? 273 PHE B C   1 
ATOM   5198 O  O   . PHE B 1 264 ? -15.960 -29.104 -19.276 1.00 28.92 ? 273 PHE B O   1 
ATOM   5199 C  CB  . PHE B 1 264 ? -18.506 -31.043 -19.680 1.00 29.40 ? 273 PHE B CB  1 
ATOM   5200 C  CG  . PHE B 1 264 ? -19.313 -31.907 -18.767 1.00 28.95 ? 273 PHE B CG  1 
ATOM   5201 C  CD1 . PHE B 1 264 ? -18.833 -32.207 -17.491 1.00 31.88 ? 273 PHE B CD1 1 
ATOM   5202 C  CD2 . PHE B 1 264 ? -20.566 -32.365 -19.129 1.00 31.21 ? 273 PHE B CD2 1 
ATOM   5203 C  CE1 . PHE B 1 264 ? -19.583 -32.965 -16.607 1.00 35.51 ? 273 PHE B CE1 1 
ATOM   5204 C  CE2 . PHE B 1 264 ? -21.320 -33.124 -18.249 1.00 33.08 ? 273 PHE B CE2 1 
ATOM   5205 C  CZ  . PHE B 1 264 ? -20.827 -33.423 -16.989 1.00 35.43 ? 273 PHE B CZ  1 
ATOM   5206 N  N   . ASP B 1 265 ? -17.360 -28.050 -20.684 1.00 27.34 ? 274 ASP B N   1 
ATOM   5207 C  CA  . ASP B 1 265 ? -16.323 -27.126 -21.156 1.00 29.72 ? 274 ASP B CA  1 
ATOM   5208 C  C   . ASP B 1 265 ? -15.817 -26.241 -20.032 1.00 29.38 ? 274 ASP B C   1 
ATOM   5209 O  O   . ASP B 1 265 ? -14.610 -26.096 -19.864 1.00 31.52 ? 274 ASP B O   1 
ATOM   5210 C  CB  . ASP B 1 265 ? -16.815 -26.258 -22.316 1.00 31.64 ? 274 ASP B CB  1 
ATOM   5211 C  CG  . ASP B 1 265 ? -16.877 -27.015 -23.625 1.00 35.22 ? 274 ASP B CG  1 
ATOM   5212 O  OD1 . ASP B 1 265 ? -16.150 -28.016 -23.791 1.00 40.84 ? 274 ASP B OD1 1 
ATOM   5213 O  OD2 . ASP B 1 265 ? -17.652 -26.595 -24.495 1.00 41.89 ? 274 ASP B OD2 1 
ATOM   5214 N  N   . VAL B 1 266 ? -16.742 -25.668 -19.261 1.00 29.45 ? 275 VAL B N   1 
ATOM   5215 C  CA  . VAL B 1 266 ? -16.389 -24.848 -18.101 1.00 29.96 ? 275 VAL B CA  1 
ATOM   5216 C  C   . VAL B 1 266 ? -15.618 -25.678 -17.068 1.00 30.32 ? 275 VAL B C   1 
ATOM   5217 O  O   . VAL B 1 266 ? -14.530 -25.291 -16.659 1.00 31.29 ? 275 VAL B O   1 
ATOM   5218 C  CB  . VAL B 1 266 ? -17.633 -24.187 -17.444 1.00 30.08 ? 275 VAL B CB  1 
ATOM   5219 C  CG1 . VAL B 1 266 ? -17.264 -23.530 -16.092 1.00 32.46 ? 275 VAL B CG1 1 
ATOM   5220 C  CG2 . VAL B 1 266 ? -18.238 -23.138 -18.382 1.00 25.84 ? 275 VAL B CG2 1 
ATOM   5221 N  N   . LEU B 1 267 ? -16.173 -26.823 -16.679 1.00 30.14 ? 276 LEU B N   1 
ATOM   5222 C  CA  . LEU B 1 267 ? -15.549 -27.689 -15.661 1.00 31.74 ? 276 LEU B CA  1 
ATOM   5223 C  C   . LEU B 1 267 ? -14.106 -28.051 -16.027 1.00 30.70 ? 276 LEU B C   1 
ATOM   5224 O  O   . LEU B 1 267 ? -13.213 -27.963 -15.195 1.00 34.56 ? 276 LEU B O   1 
ATOM   5225 C  CB  . LEU B 1 267 ? -16.362 -28.970 -15.465 1.00 30.65 ? 276 LEU B CB  1 
ATOM   5226 C  CG  . LEU B 1 267 ? -15.916 -29.948 -14.364 1.00 34.33 ? 276 LEU B CG  1 
ATOM   5227 C  CD1 . LEU B 1 267 ? -16.242 -29.398 -12.989 1.00 39.47 ? 276 LEU B CD1 1 
ATOM   5228 C  CD2 . LEU B 1 267 ? -16.595 -31.283 -14.566 1.00 36.56 ? 276 LEU B CD2 1 
ATOM   5229 N  N   . LEU B 1 268 ? -13.881 -28.415 -17.281 1.00 29.74 ? 277 LEU B N   1 
ATOM   5230 C  CA  . LEU B 1 268 ? -12.550 -28.835 -17.734 1.00 31.65 ? 277 LEU B CA  1 
ATOM   5231 C  C   . LEU B 1 268 ? -11.640 -27.663 -18.152 1.00 33.09 ? 277 LEU B C   1 
ATOM   5232 O  O   . LEU B 1 268 ? -10.542 -27.894 -18.655 1.00 33.59 ? 277 LEU B O   1 
ATOM   5233 C  CB  . LEU B 1 268 ? -12.692 -29.855 -18.872 1.00 29.76 ? 277 LEU B CB  1 
ATOM   5234 C  CG  . LEU B 1 268 ? -13.533 -31.092 -18.513 1.00 30.92 ? 277 LEU B CG  1 
ATOM   5235 C  CD1 . LEU B 1 268 ? -13.978 -31.838 -19.755 1.00 31.23 ? 277 LEU B CD1 1 
ATOM   5236 C  CD2 . LEU B 1 268 ? -12.766 -32.016 -17.569 1.00 34.26 ? 277 LEU B CD2 1 
ATOM   5237 N  N   . GLY B 1 269 ? -12.087 -26.420 -17.945 1.00 33.46 ? 278 GLY B N   1 
ATOM   5238 C  CA  . GLY B 1 269 ? -11.274 -25.237 -18.236 1.00 35.21 ? 278 GLY B CA  1 
ATOM   5239 C  C   . GLY B 1 269 ? -10.979 -25.042 -19.712 1.00 33.90 ? 278 GLY B C   1 
ATOM   5240 O  O   . GLY B 1 269 ? -9.949  -24.485 -20.070 1.00 35.84 ? 278 GLY B O   1 
ATOM   5241 N  N   . ILE B 1 270 ? -11.882 -25.511 -20.566 1.00 35.38 ? 279 ILE B N   1 
ATOM   5242 C  CA  . ILE B 1 270 ? -11.736 -25.374 -22.022 1.00 37.06 ? 279 ILE B CA  1 
ATOM   5243 C  C   . ILE B 1 270 ? -11.871 -23.891 -22.450 1.00 40.66 ? 279 ILE B C   1 
ATOM   5244 O  O   . ILE B 1 270 ? -11.202 -23.450 -23.390 1.00 44.80 ? 279 ILE B O   1 
ATOM   5245 C  CB  . ILE B 1 270 ? -12.698 -26.350 -22.762 1.00 35.07 ? 279 ILE B CB  1 
ATOM   5246 C  CG1 . ILE B 1 270 ? -12.242 -27.798 -22.477 1.00 38.66 ? 279 ILE B CG1 1 
ATOM   5247 C  CG2 . ILE B 1 270 ? -12.736 -26.075 -24.281 1.00 36.38 ? 279 ILE B CG2 1 
ATOM   5248 C  CD1 . ILE B 1 270 ? -13.222 -28.900 -22.851 1.00 33.29 ? 279 ILE B CD1 1 
ATOM   5249 N  N   . GLN B 1 271 ? -12.686 -23.125 -21.722 1.00 43.35 ? 280 GLN B N   1 
ATOM   5250 C  CA  . GLN B 1 271 ? -12.821 -21.666 -21.906 1.00 44.14 ? 280 GLN B CA  1 
ATOM   5251 C  C   . GLN B 1 271 ? -13.280 -21.329 -23.323 1.00 42.17 ? 280 GLN B C   1 
ATOM   5252 O  O   . GLN B 1 271 ? -12.590 -20.647 -24.084 1.00 40.50 ? 280 GLN B O   1 
ATOM   5253 C  CB  . GLN B 1 271 ? -11.532 -20.918 -21.537 1.00 46.67 ? 280 GLN B CB  1 
ATOM   5254 C  CG  . GLN B 1 271 ? -11.210 -20.943 -20.061 1.00 51.43 ? 280 GLN B CG  1 
ATOM   5255 C  CD  . GLN B 1 271 ? -9.883  -20.271 -19.753 1.00 54.52 ? 280 GLN B CD  1 
ATOM   5256 O  OE1 . GLN B 1 271 ? -8.830  -20.701 -20.230 1.00 64.51 ? 280 GLN B OE1 1 
ATOM   5257 N  NE2 . GLN B 1 271 ? -9.926  -19.216 -18.949 1.00 60.81 ? 280 GLN B NE2 1 
ATOM   5258 N  N   . GLN B 1 272 ? -14.459 -21.838 -23.658 1.00 41.25 ? 281 GLN B N   1 
ATOM   5259 C  CA  . GLN B 1 272 ? -15.054 -21.626 -24.976 1.00 41.74 ? 281 GLN B CA  1 
ATOM   5260 C  C   . GLN B 1 272 ? -15.504 -20.191 -25.209 1.00 42.90 ? 281 GLN B C   1 
ATOM   5261 O  O   . GLN B 1 272 ? -15.622 -19.784 -26.356 1.00 44.39 ? 281 GLN B O   1 
ATOM   5262 C  CB  . GLN B 1 272 ? -16.258 -22.548 -25.184 1.00 40.88 ? 281 GLN B CB  1 
ATOM   5263 C  CG  . GLN B 1 272 ? -15.915 -24.018 -25.226 1.00 41.06 ? 281 GLN B CG  1 
ATOM   5264 C  CD  . GLN B 1 272 ? -15.277 -24.476 -26.528 1.00 40.38 ? 281 GLN B CD  1 
ATOM   5265 O  OE1 . GLN B 1 272 ? -14.869 -23.670 -27.362 1.00 40.18 ? 281 GLN B OE1 1 
ATOM   5266 N  NE2 . GLN B 1 272 ? -15.200 -25.791 -26.708 1.00 38.31 ? 281 GLN B NE2 1 
ATOM   5267 N  N   . THR B 1 273 ? -15.761 -19.448 -24.128 1.00 42.64 ? 282 THR B N   1 
ATOM   5268 C  CA  . THR B 1 273 ? -16.280 -18.084 -24.205 1.00 42.24 ? 282 THR B CA  1 
ATOM   5269 C  C   . THR B 1 273 ? -15.207 -17.026 -23.946 1.00 42.45 ? 282 THR B C   1 
ATOM   5270 O  O   . THR B 1 273 ? -15.539 -15.849 -23.796 1.00 42.10 ? 282 THR B O   1 
ATOM   5271 C  CB  . THR B 1 273 ? -17.467 -17.886 -23.215 1.00 41.97 ? 282 THR B CB  1 
ATOM   5272 O  OG1 . THR B 1 273 ? -17.003 -18.007 -21.865 1.00 42.95 ? 282 THR B OG1 1 
ATOM   5273 C  CG2 . THR B 1 273 ? -18.571 -18.914 -23.476 1.00 38.80 ? 282 THR B CG2 1 
ATOM   5274 N  N   . ALA B 1 274 ? -13.935 -17.437 -23.920 1.00 42.61 ? 283 ALA B N   1 
ATOM   5275 C  CA  . ALA B 1 274 ? -12.811 -16.522 -23.724 1.00 44.92 ? 283 ALA B CA  1 
ATOM   5276 C  C   . ALA B 1 274 ? -12.326 -15.921 -25.047 1.00 45.95 ? 283 ALA B C   1 
ATOM   5277 O  O   . ALA B 1 274 ? -12.643 -16.423 -26.124 1.00 45.74 ? 283 ALA B O   1 
ATOM   5278 C  CB  . ALA B 1 274 ? -11.648 -17.243 -23.019 1.00 45.04 ? 283 ALA B CB  1 
ATOM   5279 N  N   . GLY B 1 275 ? -11.539 -14.852 -24.942 1.00 47.29 ? 284 GLY B N   1 
ATOM   5280 C  CA  . GLY B 1 275 ? -10.873 -14.234 -26.092 1.00 49.17 ? 284 GLY B CA  1 
ATOM   5281 C  C   . GLY B 1 275 ? -11.758 -13.401 -27.004 1.00 47.81 ? 284 GLY B C   1 
ATOM   5282 O  O   . GLY B 1 275 ? -12.945 -13.217 -26.735 1.00 45.79 ? 284 GLY B O   1 
ATOM   5283 N  N   . GLY B 1 276 ? -11.167 -12.928 -28.102 1.00 48.21 ? 285 GLY B N   1 
ATOM   5284 C  CA  . GLY B 1 276 ? -11.808 -11.980 -29.013 1.00 50.36 ? 285 GLY B CA  1 
ATOM   5285 C  C   . GLY B 1 276 ? -12.277 -12.551 -30.341 1.00 50.97 ? 285 GLY B C   1 
ATOM   5286 O  O   . GLY B 1 276 ? -12.130 -11.890 -31.377 1.00 50.86 ? 285 GLY B O   1 
ATOM   5287 N  N   . GLY B 1 277 ? -12.861 -13.758 -30.303 1.00 49.10 ? 286 GLY B N   1 
ATOM   5288 C  CA  . GLY B 1 277 ? -13.373 -14.449 -31.500 1.00 47.53 ? 286 GLY B CA  1 
ATOM   5289 C  C   . GLY B 1 277 ? -14.885 -14.621 -31.533 1.00 45.49 ? 286 GLY B C   1 
ATOM   5290 O  O   . GLY B 1 277 ? -15.565 -14.490 -30.512 1.00 44.52 ? 286 GLY B O   1 
ATOM   5291 N  N   . HIS B 1 278 ? -15.410 -14.939 -32.714 1.00 44.51 ? 287 HIS B N   1 
ATOM   5292 C  CA  . HIS B 1 278 ? -16.863 -15.037 -32.923 1.00 42.46 ? 287 HIS B CA  1 
ATOM   5293 C  C   . HIS B 1 278 ? -17.511 -16.276 -32.287 1.00 36.84 ? 287 HIS B C   1 
ATOM   5294 O  O   . HIS B 1 278 ? -18.643 -16.199 -31.816 1.00 32.30 ? 287 HIS B O   1 
ATOM   5295 C  CB  . HIS B 1 278 ? -17.212 -14.973 -34.418 1.00 45.49 ? 287 HIS B CB  1 
ATOM   5296 C  CG  . HIS B 1 278 ? -16.783 -13.700 -35.084 1.00 52.49 ? 287 HIS B CG  1 
ATOM   5297 N  ND1 . HIS B 1 278 ? -17.224 -12.460 -34.674 1.00 60.24 ? 287 HIS B ND1 1 
ATOM   5298 C  CD2 . HIS B 1 278 ? -15.956 -13.476 -36.134 1.00 61.49 ? 287 HIS B CD2 1 
ATOM   5299 C  CE1 . HIS B 1 278 ? -16.687 -11.527 -35.442 1.00 62.46 ? 287 HIS B CE1 1 
ATOM   5300 N  NE2 . HIS B 1 278 ? -15.913 -12.117 -36.335 1.00 63.18 ? 287 HIS B NE2 1 
ATOM   5301 N  N   . ALA B 1 279 ? -16.814 -17.410 -32.278 1.00 34.48 ? 288 ALA B N   1 
ATOM   5302 C  CA  . ALA B 1 279 ? -17.367 -18.634 -31.672 1.00 33.66 ? 288 ALA B CA  1 
ATOM   5303 C  C   . ALA B 1 279 ? -17.647 -18.428 -30.185 1.00 30.91 ? 288 ALA B C   1 
ATOM   5304 O  O   . ALA B 1 279 ? -18.700 -18.811 -29.693 1.00 30.04 ? 288 ALA B O   1 
ATOM   5305 C  CB  . ALA B 1 279 ? -16.435 -19.828 -31.880 1.00 33.76 ? 288 ALA B CB  1 
ATOM   5306 N  N   . ALA B 1 280 ? -16.699 -17.801 -29.493 1.00 32.70 ? 289 ALA B N   1 
ATOM   5307 C  CA  . ALA B 1 280 ? -16.846 -17.416 -28.083 1.00 32.58 ? 289 ALA B CA  1 
ATOM   5308 C  C   . ALA B 1 280 ? -18.057 -16.528 -27.824 1.00 32.14 ? 289 ALA B C   1 
ATOM   5309 O  O   . ALA B 1 280 ? -18.826 -16.753 -26.877 1.00 30.46 ? 289 ALA B O   1 
ATOM   5310 C  CB  . ALA B 1 280 ? -15.587 -16.705 -27.607 1.00 36.20 ? 289 ALA B CB  1 
ATOM   5311 N  N   . GLN B 1 281 ? -18.222 -15.525 -28.673 1.00 30.46 ? 290 GLN B N   1 
ATOM   5312 C  CA  . GLN B 1 281 ? -19.334 -14.597 -28.548 1.00 33.00 ? 290 GLN B CA  1 
ATOM   5313 C  C   . GLN B 1 281 ? -20.651 -15.339 -28.728 1.00 30.76 ? 290 GLN B C   1 
ATOM   5314 O  O   . GLN B 1 281 ? -21.604 -15.147 -27.963 1.00 30.16 ? 290 GLN B O   1 
ATOM   5315 C  CB  . GLN B 1 281 ? -19.210 -13.484 -29.590 1.00 34.81 ? 290 GLN B CB  1 
ATOM   5316 C  CG  . GLN B 1 281 ? -19.828 -12.190 -29.178 1.00 46.83 ? 290 GLN B CG  1 
ATOM   5317 C  CD  . GLN B 1 281 ? -19.113 -11.502 -28.025 1.00 44.02 ? 290 GLN B CD  1 
ATOM   5318 O  OE1 . GLN B 1 281 ? -17.934 -11.743 -27.750 1.00 52.47 ? 290 GLN B OE1 1 
ATOM   5319 N  NE2 . GLN B 1 281 ? -19.835 -10.635 -27.346 1.00 51.83 ? 290 GLN B NE2 1 
ATOM   5320 N  N   . PHE B 1 282 ? -20.688 -16.202 -29.737 1.00 29.99 ? 291 PHE B N   1 
ATOM   5321 C  CA  . PHE B 1 282 ? -21.884 -16.967 -30.044 1.00 29.27 ? 291 PHE B CA  1 
ATOM   5322 C  C   . PHE B 1 282 ? -22.267 -17.908 -28.912 1.00 26.34 ? 291 PHE B C   1 
ATOM   5323 O  O   . PHE B 1 282 ? -23.430 -17.948 -28.499 1.00 23.53 ? 291 PHE B O   1 
ATOM   5324 C  CB  . PHE B 1 282 ? -21.718 -17.772 -31.334 1.00 30.11 ? 291 PHE B CB  1 
ATOM   5325 C  CG  . PHE B 1 282 ? -22.900 -18.634 -31.639 1.00 31.62 ? 291 PHE B CG  1 
ATOM   5326 C  CD1 . PHE B 1 282 ? -24.069 -18.068 -32.147 1.00 31.82 ? 291 PHE B CD1 1 
ATOM   5327 C  CD2 . PHE B 1 282 ? -22.873 -20.003 -31.372 1.00 33.91 ? 291 PHE B CD2 1 
ATOM   5328 C  CE1 . PHE B 1 282 ? -25.185 -18.863 -32.411 1.00 32.30 ? 291 PHE B CE1 1 
ATOM   5329 C  CE2 . PHE B 1 282 ? -23.980 -20.797 -31.633 1.00 31.58 ? 291 PHE B CE2 1 
ATOM   5330 C  CZ  . PHE B 1 282 ? -25.136 -20.223 -32.159 1.00 33.25 ? 291 PHE B CZ  1 
ATOM   5331 N  N   . LEU B 1 283 ? -21.304 -18.675 -28.419 1.00 24.75 ? 292 LEU B N   1 
ATOM   5332 C  CA  . LEU B 1 283 ? -21.589 -19.590 -27.306 1.00 23.79 ? 292 LEU B CA  1 
ATOM   5333 C  C   . LEU B 1 283 ? -21.965 -18.820 -26.036 1.00 24.57 ? 292 LEU B C   1 
ATOM   5334 O  O   . LEU B 1 283 ? -22.838 -19.262 -25.286 1.00 26.18 ? 292 LEU B O   1 
ATOM   5335 C  CB  . LEU B 1 283 ? -20.422 -20.556 -27.056 1.00 22.43 ? 292 LEU B CB  1 
ATOM   5336 C  CG  . LEU B 1 283 ? -20.181 -21.580 -28.178 1.00 25.13 ? 292 LEU B CG  1 
ATOM   5337 C  CD1 . LEU B 1 283 ? -18.900 -22.359 -27.920 1.00 28.23 ? 292 LEU B CD1 1 
ATOM   5338 C  CD2 . LEU B 1 283 ? -21.340 -22.544 -28.344 1.00 20.92 ? 292 LEU B CD2 1 
ATOM   5339 N  N   . GLN B 1 284 ? -21.317 -17.676 -25.806 1.00 25.82 ? 293 GLN B N   1 
ATOM   5340 C  CA  . GLN B 1 284 ? -21.725 -16.765 -24.725 1.00 28.74 ? 293 GLN B CA  1 
ATOM   5341 C  C   . GLN B 1 284 ? -23.179 -16.305 -24.880 1.00 28.35 ? 293 GLN B C   1 
ATOM   5342 O  O   . GLN B 1 284 ? -23.936 -16.369 -23.916 1.00 29.40 ? 293 GLN B O   1 
ATOM   5343 C  CB  . GLN B 1 284 ? -20.773 -15.554 -24.603 1.00 28.54 ? 293 GLN B CB  1 
ATOM   5344 C  CG  . GLN B 1 284 ? -21.311 -14.417 -23.715 1.00 35.12 ? 293 GLN B CG  1 
ATOM   5345 C  CD  . GLN B 1 284 ? -20.249 -13.407 -23.319 1.00 37.76 ? 293 GLN B CD  1 
ATOM   5346 O  OE1 . GLN B 1 284 ? -19.700 -13.476 -22.226 1.00 46.68 ? 293 GLN B OE1 1 
ATOM   5347 N  NE2 . GLN B 1 284 ? -19.958 -12.472 -24.208 1.00 36.87 ? 293 GLN B NE2 1 
ATOM   5348 N  N   A ASP B 1 285 ? -23.557 -15.858 -26.080 0.50 28.82 ? 294 ASP B N   1 
ATOM   5349 N  N   B ASP B 1 285 ? -23.551 -15.859 -26.081 0.50 28.05 ? 294 ASP B N   1 
ATOM   5350 C  CA  A ASP B 1 285 ? -24.936 -15.404 -26.359 0.50 28.53 ? 294 ASP B CA  1 
ATOM   5351 C  CA  B ASP B 1 285 ? -24.930 -15.418 -26.361 0.50 28.31 ? 294 ASP B CA  1 
ATOM   5352 C  C   A ASP B 1 285 ? -25.977 -16.502 -26.102 0.50 27.76 ? 294 ASP B C   1 
ATOM   5353 C  C   B ASP B 1 285 ? -25.966 -16.508 -26.079 0.50 27.53 ? 294 ASP B C   1 
ATOM   5354 O  O   A ASP B 1 285 ? -27.049 -16.221 -25.564 0.50 26.47 ? 294 ASP B O   1 
ATOM   5355 O  O   B ASP B 1 285 ? -27.021 -16.231 -25.504 0.50 26.11 ? 294 ASP B O   1 
ATOM   5356 C  CB  A ASP B 1 285 ? -25.057 -14.887 -27.809 0.50 29.66 ? 294 ASP B CB  1 
ATOM   5357 C  CB  B ASP B 1 285 ? -25.082 -14.955 -27.819 0.50 29.21 ? 294 ASP B CB  1 
ATOM   5358 C  CG  A ASP B 1 285 ? -26.391 -14.163 -28.097 0.50 32.28 ? 294 ASP B CG  1 
ATOM   5359 C  CG  B ASP B 1 285 ? -24.275 -13.699 -28.140 0.50 34.43 ? 294 ASP B CG  1 
ATOM   5360 O  OD1 A ASP B 1 285 ? -27.025 -13.598 -27.173 0.50 31.89 ? 294 ASP B OD1 1 
ATOM   5361 O  OD1 B ASP B 1 285 ? -23.694 -13.078 -27.219 0.50 35.02 ? 294 ASP B OD1 1 
ATOM   5362 O  OD2 A ASP B 1 285 ? -26.792 -14.143 -29.284 0.50 37.69 ? 294 ASP B OD2 1 
ATOM   5363 O  OD2 B ASP B 1 285 ? -24.216 -13.341 -29.337 0.50 35.74 ? 294 ASP B OD2 1 
ATOM   5364 N  N   . MET B 1 286 ? -25.651 -17.745 -26.461 1.00 25.90 ? 295 MET B N   1 
ATOM   5365 C  CA  . MET B 1 286 ? -26.589 -18.876 -26.297 1.00 24.92 ? 295 MET B CA  1 
ATOM   5366 C  C   . MET B 1 286 ? -26.926 -19.230 -24.842 1.00 24.63 ? 295 MET B C   1 
ATOM   5367 O  O   . MET B 1 286 ? -27.971 -19.823 -24.573 1.00 26.80 ? 295 MET B O   1 
ATOM   5368 C  CB  . MET B 1 286 ? -26.100 -20.108 -27.067 1.00 25.02 ? 295 MET B CB  1 
ATOM   5369 C  CG  . MET B 1 286 ? -26.136 -19.961 -28.590 1.00 25.60 ? 295 MET B CG  1 
ATOM   5370 S  SD  . MET B 1 286 ? -27.722 -19.431 -29.271 1.00 27.33 ? 295 MET B SD  1 
ATOM   5371 C  CE  . MET B 1 286 ? -27.463 -17.666 -29.468 1.00 32.11 ? 295 MET B CE  1 
ATOM   5372 N  N   . ARG B 1 287 ? -26.070 -18.826 -23.911 1.00 25.98 ? 296 ARG B N   1 
ATOM   5373 C  CA  . ARG B 1 287 ? -26.371 -18.916 -22.484 1.00 26.66 ? 296 ARG B CA  1 
ATOM   5374 C  C   . ARG B 1 287 ? -27.610 -18.133 -22.074 1.00 28.16 ? 296 ARG B C   1 
ATOM   5375 O  O   . ARG B 1 287 ? -28.320 -18.552 -21.174 1.00 27.88 ? 296 ARG B O   1 
ATOM   5376 C  CB  . ARG B 1 287 ? -25.186 -18.451 -21.646 1.00 25.61 ? 296 ARG B CB  1 
ATOM   5377 C  CG  . ARG B 1 287 ? -23.996 -19.328 -21.827 1.00 27.81 ? 296 ARG B CG  1 
ATOM   5378 C  CD  . ARG B 1 287 ? -22.936 -18.985 -20.844 1.00 30.21 ? 296 ARG B CD  1 
ATOM   5379 N  NE  . ARG B 1 287 ? -21.767 -19.821 -21.033 1.00 30.87 ? 296 ARG B NE  1 
ATOM   5380 C  CZ  . ARG B 1 287 ? -20.701 -19.797 -20.240 1.00 32.47 ? 296 ARG B CZ  1 
ATOM   5381 N  NH1 . ARG B 1 287 ? -20.644 -18.965 -19.212 1.00 32.54 ? 296 ARG B NH1 1 
ATOM   5382 N  NH2 . ARG B 1 287 ? -19.683 -20.614 -20.487 1.00 33.01 ? 296 ARG B NH2 1 
ATOM   5383 N  N   A ARG B 1 288 ? -27.842 -17.006 -22.752 0.50 27.81 ? 297 ARG B N   1 
ATOM   5384 N  N   B ARG B 1 288 ? -27.857 -17.007 -22.734 0.50 28.67 ? 297 ARG B N   1 
ATOM   5385 C  CA  A ARG B 1 288 ? -29.052 -16.186 -22.597 0.50 27.41 ? 297 ARG B CA  1 
ATOM   5386 C  CA  B ARG B 1 288 ? -29.063 -16.217 -22.495 0.50 29.01 ? 297 ARG B CA  1 
ATOM   5387 C  C   A ARG B 1 288 ? -30.325 -16.918 -23.006 0.50 25.17 ? 297 ARG B C   1 
ATOM   5388 C  C   B ARG B 1 288 ? -30.328 -16.836 -23.110 0.50 26.18 ? 297 ARG B C   1 
ATOM   5389 O  O   A ARG B 1 288 ? -31.420 -16.551 -22.574 0.50 23.09 ? 297 ARG B O   1 
ATOM   5390 O  O   B ARG B 1 288 ? -31.422 -16.317 -22.909 0.50 24.84 ? 297 ARG B O   1 
ATOM   5391 C  CB  A ARG B 1 288 ? -28.946 -14.912 -23.446 0.50 27.04 ? 297 ARG B CB  1 
ATOM   5392 C  CB  B ARG B 1 288 ? -28.832 -14.765 -22.936 0.50 29.77 ? 297 ARG B CB  1 
ATOM   5393 C  CG  A ARG B 1 288 ? -27.805 -13.974 -23.082 0.50 28.51 ? 297 ARG B CG  1 
ATOM   5394 C  CG  B ARG B 1 288 ? -27.992 -13.999 -21.903 0.50 34.69 ? 297 ARG B CG  1 
ATOM   5395 C  CD  A ARG B 1 288 ? -27.875 -13.506 -21.617 0.50 32.84 ? 297 ARG B CD  1 
ATOM   5396 C  CD  B ARG B 1 288 ? -27.149 -12.872 -22.490 0.50 35.82 ? 297 ARG B CD  1 
ATOM   5397 N  NE  A ARG B 1 288 ? -27.026 -14.298 -20.721 0.50 32.04 ? 297 ARG B NE  1 
ATOM   5398 N  NE  B ARG B 1 288 ? -27.929 -12.016 -23.383 0.50 36.58 ? 297 ARG B NE  1 
ATOM   5399 C  CZ  A ARG B 1 288 ? -27.118 -14.343 -19.390 0.50 28.74 ? 297 ARG B CZ  1 
ATOM   5400 C  CZ  B ARG B 1 288 ? -27.742 -11.858 -24.697 0.50 35.39 ? 297 ARG B CZ  1 
ATOM   5401 N  NH1 A ARG B 1 288 ? -28.047 -13.662 -18.731 0.50 17.29 ? 297 ARG B NH1 1 
ATOM   5402 N  NH1 B ARG B 1 288 ? -26.756 -12.471 -25.369 0.50 29.99 ? 297 ARG B NH1 1 
ATOM   5403 N  NH2 A ARG B 1 288 ? -26.272 -15.114 -18.704 0.50 34.49 ? 297 ARG B NH2 1 
ATOM   5404 N  NH2 B ARG B 1 288 ? -28.554 -11.038 -25.351 0.50 28.44 ? 297 ARG B NH2 1 
ATOM   5405 N  N   . TYR B 1 289 ? -30.174 -17.949 -23.833 1.00 25.55 ? 298 TYR B N   1 
ATOM   5406 C  CA  . TYR B 1 289 ? -31.300 -18.756 -24.326 1.00 24.82 ? 298 TYR B CA  1 
ATOM   5407 C  C   . TYR B 1 289 ? -31.511 -20.013 -23.478 1.00 25.78 ? 298 TYR B C   1 
ATOM   5408 O  O   . TYR B 1 289 ? -32.366 -20.838 -23.806 1.00 26.16 ? 298 TYR B O   1 
ATOM   5409 C  CB  . TYR B 1 289 ? -31.071 -19.124 -25.789 1.00 24.98 ? 298 TYR B CB  1 
ATOM   5410 C  CG  . TYR B 1 289 ? -31.102 -17.936 -26.728 1.00 22.47 ? 298 TYR B CG  1 
ATOM   5411 C  CD1 . TYR B 1 289 ? -30.107 -16.956 -26.691 1.00 22.15 ? 298 TYR B CD1 1 
ATOM   5412 C  CD2 . TYR B 1 289 ? -32.104 -17.815 -27.689 1.00 24.10 ? 298 TYR B CD2 1 
ATOM   5413 C  CE1 . TYR B 1 289 ? -30.131 -15.861 -27.566 1.00 24.06 ? 298 TYR B CE1 1 
ATOM   5414 C  CE2 . TYR B 1 289 ? -32.148 -16.735 -28.553 1.00 25.88 ? 298 TYR B CE2 1 
ATOM   5415 C  CZ  . TYR B 1 289 ? -31.156 -15.768 -28.499 1.00 26.05 ? 298 TYR B CZ  1 
ATOM   5416 O  OH  . TYR B 1 289 ? -31.227 -14.725 -29.385 1.00 23.88 ? 298 TYR B OH  1 
ATOM   5417 N  N   . MET B 1 290 ? -30.740 -20.155 -22.392 1.00 25.60 ? 299 MET B N   1 
ATOM   5418 C  CA  . MET B 1 290 ? -30.926 -21.241 -21.433 1.00 26.22 ? 299 MET B CA  1 
ATOM   5419 C  C   . MET B 1 290 ? -31.831 -20.760 -20.324 1.00 29.21 ? 299 MET B C   1 
ATOM   5420 O  O   . MET B 1 290 ? -31.830 -19.567 -20.024 1.00 31.67 ? 299 MET B O   1 
ATOM   5421 C  CB  . MET B 1 290 ? -29.597 -21.624 -20.796 1.00 26.38 ? 299 MET B CB  1 
ATOM   5422 C  CG  . MET B 1 290 ? -28.548 -22.070 -21.766 1.00 27.66 ? 299 MET B CG  1 
ATOM   5423 S  SD  . MET B 1 290 ? -26.989 -22.352 -20.906 1.00 25.39 ? 299 MET B SD  1 
ATOM   5424 C  CE  . MET B 1 290 ? -25.998 -22.925 -22.280 1.00 19.95 ? 299 MET B CE  1 
ATOM   5425 N  N   . PRO B 1 291 ? -32.554 -21.683 -19.656 1.00 28.09 ? 300 PRO B N   1 
ATOM   5426 C  CA  . PRO B 1 291 ? -33.303 -21.261 -18.467 1.00 29.35 ? 300 PRO B CA  1 
ATOM   5427 C  C   . PRO B 1 291 ? -32.380 -20.598 -17.416 1.00 30.23 ? 300 PRO B C   1 
ATOM   5428 O  O   . PRO B 1 291 ? -31.227 -21.023 -17.278 1.00 28.85 ? 300 PRO B O   1 
ATOM   5429 C  CB  . PRO B 1 291 ? -33.884 -22.572 -17.923 1.00 28.94 ? 300 PRO B CB  1 
ATOM   5430 C  CG  . PRO B 1 291 ? -33.857 -23.525 -19.057 1.00 29.37 ? 300 PRO B CG  1 
ATOM   5431 C  CD  . PRO B 1 291 ? -32.701 -23.126 -19.923 1.00 27.91 ? 300 PRO B CD  1 
ATOM   5432 N  N   . PRO B 1 292 ? -32.873 -19.568 -16.699 1.00 29.12 ? 301 PRO B N   1 
ATOM   5433 C  CA  . PRO B 1 292 ? -32.028 -18.747 -15.817 1.00 31.78 ? 301 PRO B CA  1 
ATOM   5434 C  C   . PRO B 1 292 ? -31.241 -19.499 -14.742 1.00 32.77 ? 301 PRO B C   1 
ATOM   5435 O  O   . PRO B 1 292 ? -30.078 -19.161 -14.485 1.00 31.55 ? 301 PRO B O   1 
ATOM   5436 C  CB  . PRO B 1 292 ? -33.026 -17.759 -15.177 1.00 34.16 ? 301 PRO B CB  1 
ATOM   5437 C  CG  . PRO B 1 292 ? -34.364 -18.339 -15.405 1.00 33.35 ? 301 PRO B CG  1 
ATOM   5438 C  CD  . PRO B 1 292 ? -34.268 -19.098 -16.688 1.00 30.33 ? 301 PRO B CD  1 
ATOM   5439 N  N   . ALA B 1 293 ? -31.867 -20.502 -14.130 1.00 33.56 ? 302 ALA B N   1 
ATOM   5440 C  CA  . ALA B 1 293 ? -31.190 -21.354 -13.143 1.00 34.10 ? 302 ALA B CA  1 
ATOM   5441 C  C   . ALA B 1 293 ? -30.028 -22.134 -13.767 1.00 30.15 ? 302 ALA B C   1 
ATOM   5442 O  O   . ALA B 1 293 ? -29.035 -22.408 -13.109 1.00 32.96 ? 302 ALA B O   1 
ATOM   5443 C  CB  . ALA B 1 293 ? -32.188 -22.306 -12.485 1.00 34.51 ? 302 ALA B CB  1 
ATOM   5444 N  N   . HIS B 1 294 ? -30.149 -22.466 -15.044 1.00 32.91 ? 303 HIS B N   1 
ATOM   5445 C  CA  . HIS B 1 294 ? -29.100 -23.193 -15.759 1.00 31.28 ? 303 HIS B CA  1 
ATOM   5446 C  C   . HIS B 1 294 ? -27.954 -22.268 -16.169 1.00 32.45 ? 303 HIS B C   1 
ATOM   5447 O  O   . HIS B 1 294 ? -26.795 -22.666 -16.077 1.00 31.63 ? 303 HIS B O   1 
ATOM   5448 C  CB  . HIS B 1 294 ? -29.681 -23.934 -16.953 1.00 29.25 ? 303 HIS B CB  1 
ATOM   5449 C  CG  . HIS B 1 294 ? -30.730 -24.938 -16.581 1.00 31.50 ? 303 HIS B CG  1 
ATOM   5450 N  ND1 . HIS B 1 294 ? -31.525 -25.568 -17.514 1.00 31.51 ? 303 HIS B ND1 1 
ATOM   5451 C  CD2 . HIS B 1 294 ? -31.106 -25.425 -15.377 1.00 29.62 ? 303 HIS B CD2 1 
ATOM   5452 C  CE1 . HIS B 1 294 ? -32.350 -26.392 -16.896 1.00 31.39 ? 303 HIS B CE1 1 
ATOM   5453 N  NE2 . HIS B 1 294 ? -32.110 -26.332 -15.600 1.00 30.15 ? 303 HIS B NE2 1 
ATOM   5454 N  N   . ARG B 1 295 ? -28.288 -21.047 -16.602 1.00 33.93 ? 304 ARG B N   1 
ATOM   5455 C  CA  . ARG B 1 295 ? -27.303 -19.945 -16.747 1.00 35.34 ? 304 ARG B CA  1 
ATOM   5456 C  C   . ARG B 1 295 ? -26.514 -19.764 -15.463 1.00 33.97 ? 304 ARG B C   1 
ATOM   5457 O  O   . ARG B 1 295 ? -25.286 -19.749 -15.499 1.00 35.74 ? 304 ARG B O   1 
ATOM   5458 C  CB  . ARG B 1 295 ? -27.951 -18.584 -17.078 1.00 35.92 ? 304 ARG B CB  1 
ATOM   5459 C  CG  . ARG B 1 295 ? -28.982 -18.603 -18.179 1.00 42.53 ? 304 ARG B CG  1 
ATOM   5460 C  CD  . ARG B 1 295 ? -29.155 -17.246 -18.869 1.00 38.75 ? 304 ARG B CD  1 
ATOM   5461 N  NE  . ARG B 1 295 ? -29.849 -16.243 -18.079 1.00 44.46 ? 304 ARG B NE  1 
ATOM   5462 C  CZ  . ARG B 1 295 ? -31.175 -16.087 -18.012 1.00 49.53 ? 304 ARG B CZ  1 
ATOM   5463 N  NH1 . ARG B 1 295 ? -32.016 -16.905 -18.655 1.00 38.45 ? 304 ARG B NH1 1 
ATOM   5464 N  NH2 . ARG B 1 295 ? -31.675 -15.110 -17.258 1.00 48.14 ? 304 ARG B NH2 1 
ATOM   5465 N  N   . ASN B 1 296 ? -27.235 -19.623 -14.344 1.00 36.62 ? 305 ASN B N   1 
ATOM   5466 C  CA  . ASN B 1 296 ? -26.642 -19.413 -13.012 1.00 38.89 ? 305 ASN B CA  1 
ATOM   5467 C  C   . ASN B 1 296 ? -25.653 -20.506 -12.639 1.00 36.21 ? 305 ASN B C   1 
ATOM   5468 O  O   . ASN B 1 296 ? -24.607 -20.222 -12.067 1.00 37.13 ? 305 ASN B O   1 
ATOM   5469 C  CB  . ASN B 1 296 ? -27.721 -19.379 -11.906 1.00 42.46 ? 305 ASN B CB  1 
ATOM   5470 C  CG  . ASN B 1 296 ? -28.547 -18.102 -11.898 1.00 48.97 ? 305 ASN B CG  1 
ATOM   5471 O  OD1 . ASN B 1 296 ? -28.235 -17.137 -12.591 1.00 57.10 ? 305 ASN B OD1 1 
ATOM   5472 N  ND2 . ASN B 1 296 ? -29.623 -18.098 -11.098 1.00 46.81 ? 305 ASN B ND2 1 
ATOM   5473 N  N   . PHE B 1 297 ? -26.027 -21.751 -12.936 1.00 34.30 ? 306 PHE B N   1 
ATOM   5474 C  CA  . PHE B 1 297 ? -25.209 -22.919 -12.647 1.00 32.72 ? 306 PHE B CA  1 
ATOM   5475 C  C   . PHE B 1 297 ? -23.888 -22.856 -13.409 1.00 31.14 ? 306 PHE B C   1 
ATOM   5476 O  O   . PHE B 1 297 ? -22.841 -23.091 -12.827 1.00 31.11 ? 306 PHE B O   1 
ATOM   5477 C  CB  . PHE B 1 297 ? -25.968 -24.209 -12.978 1.00 31.41 ? 306 PHE B CB  1 
ATOM   5478 C  CG  . PHE B 1 297 ? -25.206 -25.454 -12.652 1.00 30.69 ? 306 PHE B CG  1 
ATOM   5479 C  CD1 . PHE B 1 297 ? -25.036 -25.854 -11.329 1.00 36.23 ? 306 PHE B CD1 1 
ATOM   5480 C  CD2 . PHE B 1 297 ? -24.631 -26.214 -13.658 1.00 31.66 ? 306 PHE B CD2 1 
ATOM   5481 C  CE1 . PHE B 1 297 ? -24.315 -26.997 -11.026 1.00 37.23 ? 306 PHE B CE1 1 
ATOM   5482 C  CE2 . PHE B 1 297 ? -23.905 -27.371 -13.363 1.00 29.95 ? 306 PHE B CE2 1 
ATOM   5483 C  CZ  . PHE B 1 297 ? -23.749 -27.761 -12.060 1.00 35.65 ? 306 PHE B CZ  1 
ATOM   5484 N  N   . LEU B 1 298 ? -23.947 -22.529 -14.698 1.00 31.35 ? 307 LEU B N   1 
ATOM   5485 C  CA  . LEU B 1 298 ? -22.739 -22.333 -15.521 1.00 31.01 ? 307 LEU B CA  1 
ATOM   5486 C  C   . LEU B 1 298 ? -21.770 -21.316 -14.938 1.00 31.65 ? 307 LEU B C   1 
ATOM   5487 O  O   . LEU B 1 298 ? -20.567 -21.587 -14.844 1.00 28.21 ? 307 LEU B O   1 
ATOM   5488 C  CB  . LEU B 1 298 ? -23.097 -21.878 -16.941 1.00 32.21 ? 307 LEU B CB  1 
ATOM   5489 C  CG  . LEU B 1 298 ? -23.382 -22.946 -17.980 1.00 37.29 ? 307 LEU B CG  1 
ATOM   5490 C  CD1 . LEU B 1 298 ? -23.961 -22.324 -19.217 1.00 34.96 ? 307 LEU B CD1 1 
ATOM   5491 C  CD2 . LEU B 1 298 ? -22.105 -23.674 -18.332 1.00 45.39 ? 307 LEU B CD2 1 
ATOM   5492 N  N   . CYS B 1 299 ? -22.284 -20.142 -14.561 1.00 32.67 ? 308 CYS B N   1 
ATOM   5493 C  CA  . CYS B 1 299 ? -21.413 -19.101 -14.018 1.00 33.83 ? 308 CYS B CA  1 
ATOM   5494 C  C   . CYS B 1 299 ? -20.884 -19.462 -12.621 1.00 34.83 ? 308 CYS B C   1 
ATOM   5495 O  O   . CYS B 1 299 ? -19.772 -19.050 -12.254 1.00 33.20 ? 308 CYS B O   1 
ATOM   5496 C  CB  . CYS B 1 299 ? -22.056 -17.704 -14.080 1.00 36.80 ? 308 CYS B CB  1 
ATOM   5497 S  SG  . CYS B 1 299 ? -23.328 -17.297 -12.856 1.00 44.19 ? 308 CYS B SG  1 
ATOM   5498 N  N   A SER B 1 300 ? -21.666 -20.226 -11.860 0.50 34.36 ? 309 SER B N   1 
ATOM   5499 N  N   B SER B 1 300 ? -21.671 -20.231 -11.861 0.50 34.66 ? 309 SER B N   1 
ATOM   5500 C  CA  A SER B 1 300 ? -21.218 -20.738 -10.566 0.50 35.84 ? 309 SER B CA  1 
ATOM   5501 C  CA  B SER B 1 300 ? -21.230 -20.770 -10.569 0.50 36.35 ? 309 SER B CA  1 
ATOM   5502 C  C   A SER B 1 300 ? -20.040 -21.720 -10.704 0.50 34.71 ? 309 SER B C   1 
ATOM   5503 C  C   B SER B 1 300 ? -20.025 -21.704 -10.719 0.50 34.99 ? 309 SER B C   1 
ATOM   5504 O  O   A SER B 1 300 ? -19.153 -21.723 -9.855  0.50 34.48 ? 309 SER B O   1 
ATOM   5505 O  O   B SER B 1 300 ? -19.115 -21.667 -9.897  0.50 34.62 ? 309 SER B O   1 
ATOM   5506 C  CB  A SER B 1 300 ? -22.386 -21.370 -9.797  0.50 36.76 ? 309 SER B CB  1 
ATOM   5507 C  CB  B SER B 1 300 ? -22.373 -21.498 -9.838  0.50 37.55 ? 309 SER B CB  1 
ATOM   5508 O  OG  A SER B 1 300 ? -23.438 -20.430 -9.621  0.50 33.45 ? 309 SER B OG  1 
ATOM   5509 O  OG  B SER B 1 300 ? -22.643 -22.773 -10.404 0.50 35.17 ? 309 SER B OG  1 
ATOM   5510 N  N   . LEU B 1 301 ? -20.025 -22.526 -11.769 1.00 34.12 ? 310 LEU B N   1 
ATOM   5511 C  CA  . LEU B 1 301 ? -18.872 -23.404 -12.078 1.00 34.02 ? 310 LEU B CA  1 
ATOM   5512 C  C   . LEU B 1 301 ? -17.624 -22.595 -12.413 1.00 35.17 ? 310 LEU B C   1 
ATOM   5513 O  O   . LEU B 1 301 ? -16.512 -22.956 -12.013 1.00 35.71 ? 310 LEU B O   1 
ATOM   5514 C  CB  . LEU B 1 301 ? -19.168 -24.348 -13.245 1.00 31.39 ? 310 LEU B CB  1 
ATOM   5515 C  CG  . LEU B 1 301 ? -20.304 -25.370 -13.142 1.00 34.78 ? 310 LEU B CG  1 
ATOM   5516 C  CD1 . LEU B 1 301 ? -20.256 -26.304 -14.317 1.00 32.84 ? 310 LEU B CD1 1 
ATOM   5517 C  CD2 . LEU B 1 301 ? -20.260 -26.174 -11.858 1.00 38.24 ? 310 LEU B CD2 1 
ATOM   5518 N  N   . GLU B 1 302 ? -17.826 -21.486 -13.122 1.00 36.66 ? 311 GLU B N   1 
ATOM   5519 C  CA  . GLU B 1 302 ? -16.743 -20.554 -13.457 1.00 37.31 ? 311 GLU B CA  1 
ATOM   5520 C  C   . GLU B 1 302 ? -16.108 -19.923 -12.222 1.00 37.07 ? 311 GLU B C   1 
ATOM   5521 O  O   . GLU B 1 302 ? -14.932 -19.603 -12.249 1.00 38.39 ? 311 GLU B O   1 
ATOM   5522 C  CB  . GLU B 1 302 ? -17.237 -19.467 -14.429 1.00 36.38 ? 311 GLU B CB  1 
ATOM   5523 C  CG  . GLU B 1 302 ? -17.635 -20.027 -15.793 1.00 38.29 ? 311 GLU B CG  1 
ATOM   5524 C  CD  . GLU B 1 302 ? -18.175 -18.976 -16.754 1.00 40.09 ? 311 GLU B CD  1 
ATOM   5525 O  OE1 . GLU B 1 302 ? -19.007 -18.127 -16.353 1.00 44.90 ? 311 GLU B OE1 1 
ATOM   5526 O  OE2 . GLU B 1 302 ? -17.779 -19.019 -17.935 1.00 47.01 ? 311 GLU B OE2 1 
ATOM   5527 N  N   . SER B 1 303 ? -16.880 -19.757 -11.148 1.00 39.26 ? 312 SER B N   1 
ATOM   5528 C  CA  . SER B 1 303 ? -16.370 -19.166 -9.900  1.00 42.52 ? 312 SER B CA  1 
ATOM   5529 C  C   . SER B 1 303 ? -15.575 -20.117 -9.000  1.00 43.33 ? 312 SER B C   1 
ATOM   5530 O  O   . SER B 1 303 ? -14.897 -19.658 -8.078  1.00 44.97 ? 312 SER B O   1 
ATOM   5531 C  CB  . SER B 1 303 ? -17.516 -18.559 -9.096  1.00 44.14 ? 312 SER B CB  1 
ATOM   5532 O  OG  . SER B 1 303 ? -18.295 -19.568 -8.487  1.00 51.77 ? 312 SER B OG  1 
ATOM   5533 N  N   . ASN B 1 304 ? -15.667 -21.426 -9.246  1.00 42.84 ? 313 ASN B N   1 
ATOM   5534 C  CA  . ASN B 1 304 ? -14.883 -22.414 -8.489  1.00 43.14 ? 313 ASN B CA  1 
ATOM   5535 C  C   . ASN B 1 304 ? -13.481 -22.537 -9.079  1.00 42.58 ? 313 ASN B C   1 
ATOM   5536 O  O   . ASN B 1 304 ? -13.268 -22.121 -10.220 1.00 42.36 ? 313 ASN B O   1 
ATOM   5537 C  CB  . ASN B 1 304 ? -15.588 -23.776 -8.467  1.00 42.98 ? 313 ASN B CB  1 
ATOM   5538 C  CG  . ASN B 1 304 ? -16.763 -23.803 -7.516  1.00 46.19 ? 313 ASN B CG  1 
ATOM   5539 O  OD1 . ASN B 1 304 ? -16.617 -24.126 -6.339  1.00 57.46 ? 313 ASN B OD1 1 
ATOM   5540 N  ND2 . ASN B 1 304 ? -17.936 -23.464 -8.019  1.00 52.51 ? 313 ASN B ND2 1 
ATOM   5541 N  N   . PRO B 1 305 ? -12.514 -23.090 -8.305  1.00 44.09 ? 314 PRO B N   1 
ATOM   5542 C  CA  . PRO B 1 305 ? -11.157 -23.293 -8.837  1.00 43.58 ? 314 PRO B CA  1 
ATOM   5543 C  C   . PRO B 1 305 ? -11.087 -24.181 -10.088 1.00 40.46 ? 314 PRO B C   1 
ATOM   5544 O  O   . PRO B 1 305 ? -11.972 -24.999 -10.329 1.00 38.79 ? 314 PRO B O   1 
ATOM   5545 C  CB  . PRO B 1 305 ? -10.412 -23.953 -7.665  1.00 45.05 ? 314 PRO B CB  1 
ATOM   5546 C  CG  . PRO B 1 305 ? -11.173 -23.564 -6.456  1.00 45.29 ? 314 PRO B CG  1 
ATOM   5547 C  CD  . PRO B 1 305 ? -12.601 -23.519 -6.893  1.00 45.32 ? 314 PRO B CD  1 
ATOM   5548 N  N   . SER B 1 306 ? -10.024 -24.006 -10.865 1.00 40.67 ? 315 SER B N   1 
ATOM   5549 C  CA  . SER B 1 306 ? -9.859  -24.713 -12.130 1.00 39.72 ? 315 SER B CA  1 
ATOM   5550 C  C   . SER B 1 306 ? -9.429  -26.171 -11.897 1.00 38.58 ? 315 SER B C   1 
ATOM   5551 O  O   . SER B 1 306 ? -8.454  -26.428 -11.193 1.00 38.44 ? 315 SER B O   1 
ATOM   5552 C  CB  . SER B 1 306 ? -8.854  -23.971 -13.025 1.00 39.40 ? 315 SER B CB  1 
ATOM   5553 O  OG  . SER B 1 306 ? -8.486  -24.734 -14.159 1.00 39.94 ? 315 SER B OG  1 
ATOM   5554 N  N   . VAL B 1 307 ? -10.177 -27.109 -12.486 1.00 37.51 ? 316 VAL B N   1 
ATOM   5555 C  CA  . VAL B 1 307 ? -9.824  -28.531 -12.486 1.00 38.18 ? 316 VAL B CA  1 
ATOM   5556 C  C   . VAL B 1 307 ? -8.563  -28.752 -13.316 1.00 37.36 ? 316 VAL B C   1 
ATOM   5557 O  O   . VAL B 1 307 ? -7.672  -29.522 -12.924 1.00 36.99 ? 316 VAL B O   1 
ATOM   5558 C  CB  . VAL B 1 307 ? -10.958 -29.422 -13.083 1.00 39.18 ? 316 VAL B CB  1 
ATOM   5559 C  CG1 . VAL B 1 307 ? -10.544 -30.901 -13.118 1.00 44.08 ? 316 VAL B CG1 1 
ATOM   5560 C  CG2 . VAL B 1 307 ? -12.258 -29.272 -12.292 1.00 44.76 ? 316 VAL B CG2 1 
ATOM   5561 N  N   . ARG B 1 308 ? -8.518  -28.102 -14.477 1.00 35.40 ? 317 ARG B N   1 
ATOM   5562 C  CA  . ARG B 1 308 ? -7.360  -28.152 -15.361 1.00 36.48 ? 317 ARG B CA  1 
ATOM   5563 C  C   . ARG B 1 308 ? -6.069  -27.725 -14.665 1.00 37.46 ? 317 ARG B C   1 
ATOM   5564 O  O   . ARG B 1 308 ? -5.073  -28.441 -14.739 1.00 35.46 ? 317 ARG B O   1 
ATOM   5565 C  CB  . ARG B 1 308 ? -7.582  -27.269 -16.585 1.00 36.55 ? 317 ARG B CB  1 
ATOM   5566 C  CG  . ARG B 1 308 ? -6.442  -27.340 -17.581 1.00 36.27 ? 317 ARG B CG  1 
ATOM   5567 C  CD  . ARG B 1 308 ? -6.788  -26.721 -18.888 1.00 37.60 ? 317 ARG B CD  1 
ATOM   5568 N  NE  . ARG B 1 308 ? -5.973  -27.291 -19.953 1.00 39.13 ? 317 ARG B NE  1 
ATOM   5569 C  CZ  . ARG B 1 308 ? -4.770  -26.854 -20.318 1.00 42.48 ? 317 ARG B CZ  1 
ATOM   5570 N  NH1 . ARG B 1 308 ? -4.186  -25.821 -19.711 1.00 50.65 ? 317 ARG B NH1 1 
ATOM   5571 N  NH2 . ARG B 1 308 ? -4.138  -27.457 -21.314 1.00 42.53 ? 317 ARG B NH2 1 
ATOM   5572 N  N   A GLU B 1 309 ? -6.085  -26.566 -14.008 0.50 39.54 ? 318 GLU B N   1 
ATOM   5573 N  N   B GLU B 1 309 ? -6.106  -26.568 -13.995 0.50 39.49 ? 318 GLU B N   1 
ATOM   5574 C  CA  A GLU B 1 309 ? -4.890  -26.068 -13.315 0.50 41.62 ? 318 GLU B CA  1 
ATOM   5575 C  CA  B GLU B 1 309 ? -4.926  -26.037 -13.290 0.50 41.72 ? 318 GLU B CA  1 
ATOM   5576 C  C   A GLU B 1 309 ? -4.539  -26.898 -12.074 0.50 41.80 ? 318 GLU B C   1 
ATOM   5577 C  C   B GLU B 1 309 ? -4.542  -26.926 -12.102 0.50 41.66 ? 318 GLU B C   1 
ATOM   5578 O  O   A GLU B 1 309 ? -3.362  -27.006 -11.726 0.50 44.61 ? 318 GLU B O   1 
ATOM   5579 O  O   B GLU B 1 309 ? -3.354  -27.103 -11.823 0.50 44.03 ? 318 GLU B O   1 
ATOM   5580 C  CB  A GLU B 1 309 ? -5.019  -24.577 -12.973 0.50 43.51 ? 318 GLU B CB  1 
ATOM   5581 C  CB  B GLU B 1 309 ? -5.098  -24.552 -12.879 0.50 43.14 ? 318 GLU B CB  1 
ATOM   5582 C  CG  A GLU B 1 309 ? -5.146  -23.647 -14.199 0.50 46.59 ? 318 GLU B CG  1 
ATOM   5583 C  CG  B GLU B 1 309 ? -5.523  -24.249 -11.429 0.50 46.39 ? 318 GLU B CG  1 
ATOM   5584 C  CD  A GLU B 1 309 ? -4.024  -23.826 -15.225 0.50 49.96 ? 318 GLU B CD  1 
ATOM   5585 C  CD  B GLU B 1 309 ? -5.590  -22.752 -11.147 0.50 47.36 ? 318 GLU B CD  1 
ATOM   5586 O  OE1 A GLU B 1 309 ? -2.838  -23.878 -14.823 0.50 46.75 ? 318 GLU B OE1 1 
ATOM   5587 O  OE1 B GLU B 1 309 ? -4.522  -22.101 -11.169 0.50 51.69 ? 318 GLU B OE1 1 
ATOM   5588 O  OE2 A GLU B 1 309 ? -4.335  -23.924 -16.435 0.50 51.95 ? 318 GLU B OE2 1 
ATOM   5589 O  OE2 B GLU B 1 309 ? -6.697  -22.227 -10.893 0.50 48.88 ? 318 GLU B OE2 1 
ATOM   5590 N  N   . PHE B 1 310 ? -5.544  -27.491 -11.427 1.00 40.39 ? 319 PHE B N   1 
ATOM   5591 C  CA  . PHE B 1 310 ? -5.313  -28.481 -10.363 1.00 41.72 ? 319 PHE B CA  1 
ATOM   5592 C  C   . PHE B 1 310 ? -4.564  -29.713 -10.899 1.00 41.03 ? 319 PHE B C   1 
ATOM   5593 O  O   . PHE B 1 310 ? -3.570  -30.132 -10.312 1.00 40.66 ? 319 PHE B O   1 
ATOM   5594 C  CB  . PHE B 1 310 ? -6.634  -28.920 -9.720  1.00 40.55 ? 319 PHE B CB  1 
ATOM   5595 C  CG  . PHE B 1 310 ? -6.464  -29.806 -8.513  1.00 39.86 ? 319 PHE B CG  1 
ATOM   5596 C  CD1 . PHE B 1 310 ? -6.316  -31.188 -8.655  1.00 43.53 ? 319 PHE B CD1 1 
ATOM   5597 C  CD2 . PHE B 1 310 ? -6.455  -29.263 -7.229  1.00 45.79 ? 319 PHE B CD2 1 
ATOM   5598 C  CE1 . PHE B 1 310 ? -6.150  -32.019 -7.543  1.00 42.46 ? 319 PHE B CE1 1 
ATOM   5599 C  CE2 . PHE B 1 310 ? -6.292  -30.082 -6.101  1.00 44.49 ? 319 PHE B CE2 1 
ATOM   5600 C  CZ  . PHE B 1 310 ? -6.142  -31.465 -6.257  1.00 46.82 ? 319 PHE B CZ  1 
ATOM   5601 N  N   . VAL B 1 311 ? -5.044  -30.266 -12.012 1.00 40.27 ? 320 VAL B N   1 
ATOM   5602 C  CA  . VAL B 1 311 ? -4.428  -31.444 -12.635 1.00 41.75 ? 320 VAL B CA  1 
ATOM   5603 C  C   . VAL B 1 311 ? -3.043  -31.113 -13.210 1.00 43.39 ? 320 VAL B C   1 
ATOM   5604 O  O   . VAL B 1 311 ? -2.099  -31.878 -13.012 1.00 41.15 ? 320 VAL B O   1 
ATOM   5605 C  CB  . VAL B 1 311 ? -5.351  -32.077 -13.711 1.00 40.53 ? 320 VAL B CB  1 
ATOM   5606 C  CG1 . VAL B 1 311 ? -4.614  -33.131 -14.537 1.00 41.90 ? 320 VAL B CG1 1 
ATOM   5607 C  CG2 . VAL B 1 311 ? -6.564  -32.721 -13.045 1.00 40.12 ? 320 VAL B CG2 1 
ATOM   5608 N  N   . LEU B 1 312 ? -2.927  -29.980 -13.904 1.00 45.26 ? 321 LEU B N   1 
ATOM   5609 C  CA  . LEU B 1 312 ? -1.625  -29.508 -14.416 1.00 47.96 ? 321 LEU B CA  1 
ATOM   5610 C  C   . LEU B 1 312 ? -0.549  -29.359 -13.334 1.00 50.42 ? 321 LEU B C   1 
ATOM   5611 O  O   . LEU B 1 312 ? 0.636   -29.542 -13.617 1.00 51.87 ? 321 LEU B O   1 
ATOM   5612 C  CB  . LEU B 1 312 ? -1.771  -28.177 -15.165 1.00 50.28 ? 321 LEU B CB  1 
ATOM   5613 C  CG  . LEU B 1 312 ? -2.011  -28.273 -16.672 1.00 52.57 ? 321 LEU B CG  1 
ATOM   5614 C  CD1 . LEU B 1 312 ? -2.554  -26.970 -17.198 1.00 56.47 ? 321 LEU B CD1 1 
ATOM   5615 C  CD2 . LEU B 1 312 ? -0.731  -28.633 -17.413 1.00 57.57 ? 321 LEU B CD2 1 
ATOM   5616 N  N   . SER B 1 313 ? -0.966  -29.038 -12.108 1.00 50.88 ? 322 SER B N   1 
ATOM   5617 C  CA  . SER B 1 313 ? -0.037  -28.811 -11.001 1.00 52.68 ? 322 SER B CA  1 
ATOM   5618 C  C   . SER B 1 313 ? 0.548   -30.061 -10.305 1.00 53.25 ? 322 SER B C   1 
ATOM   5619 O  O   . SER B 1 313 ? 1.530   -29.917 -9.588  1.00 53.21 ? 322 SER B O   1 
ATOM   5620 C  CB  . SER B 1 313 ? -0.705  -27.927 -9.936  1.00 53.85 ? 322 SER B CB  1 
ATOM   5621 O  OG  . SER B 1 313 ? -1.744  -28.620 -9.254  1.00 54.30 ? 322 SER B OG  1 
ATOM   5622 N  N   . LYS B 1 314 ? -0.025  -31.258 -10.511 1.00 51.72 ? 323 LYS B N   1 
ATOM   5623 C  CA  . LYS B 1 314 ? 0.139   -32.385 -9.550  1.00 50.79 ? 323 LYS B CA  1 
ATOM   5624 C  C   . LYS B 1 314 ? 1.157   -33.497 -9.865  1.00 52.02 ? 323 LYS B C   1 
ATOM   5625 O  O   . LYS B 1 314 ? 1.425   -34.338 -8.981  1.00 54.47 ? 323 LYS B O   1 
ATOM   5626 C  CB  . LYS B 1 314 ? -1.224  -33.026 -9.267  1.00 51.40 ? 323 LYS B CB  1 
ATOM   5627 C  CG  . LYS B 1 314 ? -2.152  -32.128 -8.465  1.00 52.18 ? 323 LYS B CG  1 
ATOM   5628 C  CD  . LYS B 1 314 ? -1.934  -32.231 -6.974  1.00 56.59 ? 323 LYS B CD  1 
ATOM   5629 C  CE  . LYS B 1 314 ? -2.515  -31.024 -6.254  1.00 58.55 ? 323 LYS B CE  1 
ATOM   5630 N  NZ  . LYS B 1 314 ? -1.658  -29.812 -6.428  1.00 66.05 ? 323 LYS B NZ  1 
ATOM   5631 N  N   . GLY B 1 315 ? 1.739   -33.496 -11.072 1.00 48.49 ? 324 GLY B N   1 
ATOM   5632 C  CA  . GLY B 1 315 ? 2.718   -34.525 -11.499 1.00 45.91 ? 324 GLY B CA  1 
ATOM   5633 C  C   . GLY B 1 315 ? 2.200   -35.946 -11.326 1.00 43.60 ? 324 GLY B C   1 
ATOM   5634 O  O   . GLY B 1 315 ? 2.886   -36.821 -10.794 1.00 44.83 ? 324 GLY B O   1 
ATOM   5635 N  N   . ASP B 1 316 ? 0.967   -36.150 -11.773 1.00 41.22 ? 325 ASP B N   1 
ATOM   5636 C  CA  . ASP B 1 316 ? 0.196   -37.348 -11.491 1.00 38.42 ? 325 ASP B CA  1 
ATOM   5637 C  C   . ASP B 1 316 ? -0.388  -37.870 -12.810 1.00 34.80 ? 325 ASP B C   1 
ATOM   5638 O  O   . ASP B 1 316 ? -1.377  -37.341 -13.300 1.00 36.15 ? 325 ASP B O   1 
ATOM   5639 C  CB  . ASP B 1 316 ? -0.890  -36.949 -10.488 1.00 37.74 ? 325 ASP B CB  1 
ATOM   5640 C  CG  . ASP B 1 316 ? -1.698  -38.119 -9.977  1.00 39.42 ? 325 ASP B CG  1 
ATOM   5641 O  OD1 . ASP B 1 316 ? -1.994  -39.065 -10.738 1.00 42.71 ? 325 ASP B OD1 1 
ATOM   5642 O  OD2 . ASP B 1 316 ? -2.060  -38.069 -8.793  1.00 40.56 ? 325 ASP B OD2 1 
ATOM   5643 N  N   . ALA B 1 317 ? 0.246   -38.890 -13.384 1.00 34.55 ? 326 ALA B N   1 
ATOM   5644 C  CA  . ALA B 1 317 ? -0.157  -39.453 -14.689 1.00 34.11 ? 326 ALA B CA  1 
ATOM   5645 C  C   . ALA B 1 317 ? -1.602  -39.948 -14.682 1.00 33.08 ? 326 ALA B C   1 
ATOM   5646 O  O   . ALA B 1 317 ? -2.367  -39.661 -15.602 1.00 33.11 ? 326 ALA B O   1 
ATOM   5647 C  CB  . ALA B 1 317 ? 0.793   -40.587 -15.096 1.00 34.10 ? 326 ALA B CB  1 
ATOM   5648 N  N   . GLY B 1 318 ? -1.967  -40.676 -13.630 1.00 34.78 ? 327 GLY B N   1 
ATOM   5649 C  CA  . GLY B 1 318 ? -3.346  -41.091 -13.385 1.00 34.84 ? 327 GLY B CA  1 
ATOM   5650 C  C   . GLY B 1 318 ? -4.367  -39.977 -13.541 1.00 33.54 ? 327 GLY B C   1 
ATOM   5651 O  O   . GLY B 1 318 ? -5.290  -40.098 -14.351 1.00 31.78 ? 327 GLY B O   1 
ATOM   5652 N  N   . LEU B 1 319 ? -4.188  -38.889 -12.786 1.00 33.36 ? 328 LEU B N   1 
ATOM   5653 C  CA  . LEU B 1 319 ? -5.090  -37.731 -12.866 1.00 33.67 ? 328 LEU B CA  1 
ATOM   5654 C  C   . LEU B 1 319 ? -5.105  -37.065 -14.230 1.00 31.29 ? 328 LEU B C   1 
ATOM   5655 O  O   . LEU B 1 319 ? -6.168  -36.675 -14.712 1.00 28.81 ? 328 LEU B O   1 
ATOM   5656 C  CB  . LEU B 1 319 ? -4.743  -36.645 -11.835 1.00 36.82 ? 328 LEU B CB  1 
ATOM   5657 C  CG  . LEU B 1 319 ? -5.349  -36.700 -10.437 1.00 41.07 ? 328 LEU B CG  1 
ATOM   5658 C  CD1 . LEU B 1 319 ? -4.852  -35.481 -9.670  1.00 47.18 ? 328 LEU B CD1 1 
ATOM   5659 C  CD2 . LEU B 1 319 ? -6.869  -36.738 -10.450 1.00 40.46 ? 328 LEU B CD2 1 
ATOM   5660 N  N   . ARG B 1 320 ? -3.922  -36.891 -14.817 1.00 32.15 ? 329 ARG B N   1 
ATOM   5661 C  CA  . ARG B 1 320 ? -3.808  -36.299 -16.153 1.00 33.51 ? 329 ARG B CA  1 
ATOM   5662 C  C   . ARG B 1 320 ? -4.546  -37.118 -17.212 1.00 31.45 ? 329 ARG B C   1 
ATOM   5663 O  O   . ARG B 1 320 ? -5.242  -36.554 -18.049 1.00 30.31 ? 329 ARG B O   1 
ATOM   5664 C  CB  . ARG B 1 320 ? -2.339  -36.121 -16.552 1.00 34.34 ? 329 ARG B CB  1 
ATOM   5665 C  CG  . ARG B 1 320 ? -1.621  -34.995 -15.796 1.00 38.68 ? 329 ARG B CG  1 
ATOM   5666 C  CD  . ARG B 1 320 ? -0.360  -34.537 -16.522 1.00 43.17 ? 329 ARG B CD  1 
ATOM   5667 N  NE  . ARG B 1 320 ? 0.503   -35.662 -16.889 1.00 49.33 ? 329 ARG B NE  1 
ATOM   5668 C  CZ  . ARG B 1 320 ? 1.340   -36.304 -16.069 1.00 54.84 ? 329 ARG B CZ  1 
ATOM   5669 N  NH1 . ARG B 1 320 ? 1.456   -35.956 -14.792 1.00 59.86 ? 329 ARG B NH1 1 
ATOM   5670 N  NH2 . ARG B 1 320 ? 2.071   -37.317 -16.533 1.00 55.73 ? 329 ARG B NH2 1 
ATOM   5671 N  N   . GLU B 1 321 ? -4.388  -38.439 -17.164 1.00 31.38 ? 330 GLU B N   1 
ATOM   5672 C  CA  . GLU B 1 321 ? -5.076  -39.341 -18.097 1.00 33.34 ? 330 GLU B CA  1 
ATOM   5673 C  C   . GLU B 1 321 ? -6.585  -39.295 -17.917 1.00 30.77 ? 330 GLU B C   1 
ATOM   5674 O  O   . GLU B 1 321 ? -7.325  -39.324 -18.897 1.00 29.72 ? 330 GLU B O   1 
ATOM   5675 C  CB  . GLU B 1 321 ? -4.598  -40.786 -17.931 1.00 32.75 ? 330 GLU B CB  1 
ATOM   5676 C  CG  . GLU B 1 321 ? -3.169  -41.023 -18.405 1.00 42.70 ? 330 GLU B CG  1 
ATOM   5677 C  CD  . GLU B 1 321 ? -2.593  -42.333 -17.890 1.00 47.01 ? 330 GLU B CD  1 
ATOM   5678 O  OE1 . GLU B 1 321 ? -3.389  -43.275 -17.644 1.00 60.90 ? 330 GLU B OE1 1 
ATOM   5679 O  OE2 . GLU B 1 321 ? -1.350  -42.420 -17.733 1.00 57.34 ? 330 GLU B OE2 1 
ATOM   5680 N  N   . ALA B 1 322 ? -7.033  -39.238 -16.667 1.00 29.56 ? 331 ALA B N   1 
ATOM   5681 C  CA  . ALA B 1 322 ? -8.466  -39.129 -16.375 1.00 29.44 ? 331 ALA B CA  1 
ATOM   5682 C  C   . ALA B 1 322 ? -9.030  -37.809 -16.880 1.00 29.21 ? 331 ALA B C   1 
ATOM   5683 O  O   . ALA B 1 322 ? -10.094 -37.784 -17.502 1.00 28.88 ? 331 ALA B O   1 
ATOM   5684 C  CB  . ALA B 1 322 ? -8.719  -39.283 -14.897 1.00 28.52 ? 331 ALA B CB  1 
ATOM   5685 N  N   . TYR B 1 323 ? -8.302  -36.722 -16.619 1.00 30.10 ? 332 TYR B N   1 
ATOM   5686 C  CA  . TYR B 1 323 ? -8.648  -35.402 -17.155 1.00 28.70 ? 332 TYR B CA  1 
ATOM   5687 C  C   . TYR B 1 323 ? -8.744  -35.429 -18.686 1.00 28.53 ? 332 TYR B C   1 
ATOM   5688 O  O   . TYR B 1 323 ? -9.746  -34.977 -19.242 1.00 25.50 ? 332 TYR B O   1 
ATOM   5689 C  CB  . TYR B 1 323 ? -7.631  -34.335 -16.723 1.00 29.41 ? 332 TYR B CB  1 
ATOM   5690 C  CG  . TYR B 1 323 ? -7.870  -33.001 -17.388 1.00 31.36 ? 332 TYR B CG  1 
ATOM   5691 C  CD1 . TYR B 1 323 ? -8.781  -32.099 -16.864 1.00 31.03 ? 332 TYR B CD1 1 
ATOM   5692 C  CD2 . TYR B 1 323 ? -7.214  -32.662 -18.573 1.00 31.26 ? 332 TYR B CD2 1 
ATOM   5693 C  CE1 . TYR B 1 323 ? -9.023  -30.879 -17.486 1.00 28.85 ? 332 TYR B CE1 1 
ATOM   5694 C  CE2 . TYR B 1 323 ? -7.452  -31.454 -19.204 1.00 29.63 ? 332 TYR B CE2 1 
ATOM   5695 C  CZ  . TYR B 1 323 ? -8.355  -30.566 -18.657 1.00 30.24 ? 332 TYR B CZ  1 
ATOM   5696 O  OH  . TYR B 1 323 ? -8.583  -29.367 -19.280 1.00 30.17 ? 332 TYR B OH  1 
ATOM   5697 N  N   . ASP B 1 324 ? -7.703  -35.948 -19.349 1.00 28.20 ? 333 ASP B N   1 
ATOM   5698 C  CA  . ASP B 1 324 ? -7.674  -36.003 -20.831 1.00 28.48 ? 333 ASP B CA  1 
ATOM   5699 C  C   . ASP B 1 324 ? -8.747  -36.896 -21.427 1.00 29.15 ? 333 ASP B C   1 
ATOM   5700 O  O   . ASP B 1 324 ? -9.239  -36.610 -22.525 1.00 30.03 ? 333 ASP B O   1 
ATOM   5701 C  CB  . ASP B 1 324 ? -6.312  -36.450 -21.371 1.00 26.98 ? 333 ASP B CB  1 
ATOM   5702 C  CG  . ASP B 1 324 ? -5.333  -35.302 -21.564 1.00 30.80 ? 333 ASP B CG  1 
ATOM   5703 O  OD1 . ASP B 1 324 ? -5.672  -34.130 -21.293 1.00 29.91 ? 333 ASP B OD1 1 
ATOM   5704 O  OD2 . ASP B 1 324 ? -4.205  -35.576 -22.024 1.00 32.05 ? 333 ASP B OD2 1 
ATOM   5705 N  N   . ALA B 1 325 ? -9.101  -37.974 -20.729 1.00 29.78 ? 334 ALA B N   1 
ATOM   5706 C  CA  . ALA B 1 325 ? -10.207 -38.831 -21.177 1.00 30.08 ? 334 ALA B CA  1 
ATOM   5707 C  C   . ALA B 1 325 ? -11.532 -38.058 -21.232 1.00 30.54 ? 334 ALA B C   1 
ATOM   5708 O  O   . ALA B 1 325 ? -12.328 -38.279 -22.141 1.00 33.10 ? 334 ALA B O   1 
ATOM   5709 C  CB  . ALA B 1 325 ? -10.328 -40.062 -20.305 1.00 30.29 ? 334 ALA B CB  1 
ATOM   5710 N  N   . CYS B 1 326 ? -11.750 -37.130 -20.292 1.00 30.61 ? 335 CYS B N   1 
ATOM   5711 C  CA  . CYS B 1 326 ? -12.926 -36.251 -20.330 1.00 27.97 ? 335 CYS B CA  1 
ATOM   5712 C  C   . CYS B 1 326 ? -12.870 -35.309 -21.530 1.00 27.54 ? 335 CYS B C   1 
ATOM   5713 O  O   . CYS B 1 326 ? -13.859 -35.182 -22.265 1.00 27.20 ? 335 CYS B O   1 
ATOM   5714 C  CB  . CYS B 1 326 ? -13.079 -35.427 -19.044 1.00 28.75 ? 335 CYS B CB  1 
ATOM   5715 S  SG  . CYS B 1 326 ? -13.404 -36.384 -17.572 1.00 26.78 ? 335 CYS B SG  1 
ATOM   5716 N  N   . VAL B 1 327 ? -11.726 -34.654 -21.723 1.00 25.95 ? 336 VAL B N   1 
ATOM   5717 C  CA  . VAL B 1 327 ? -11.544 -33.729 -22.854 1.00 26.01 ? 336 VAL B CA  1 
ATOM   5718 C  C   . VAL B 1 327 ? -11.687 -34.472 -24.190 1.00 27.69 ? 336 VAL B C   1 
ATOM   5719 O  O   . VAL B 1 327 ? -12.380 -33.999 -25.099 1.00 25.85 ? 336 VAL B O   1 
ATOM   5720 C  CB  . VAL B 1 327 ? -10.192 -32.963 -22.792 1.00 25.49 ? 336 VAL B CB  1 
ATOM   5721 C  CG1 . VAL B 1 327 ? -9.986  -32.097 -24.035 1.00 27.25 ? 336 VAL B CG1 1 
ATOM   5722 C  CG2 . VAL B 1 327 ? -10.134 -32.085 -21.559 1.00 29.25 ? 336 VAL B CG2 1 
ATOM   5723 N  N   . LYS B 1 328 ? -11.034 -35.626 -24.288 1.00 29.68 ? 337 LYS B N   1 
ATOM   5724 C  CA  . LYS B 1 328 ? -11.084 -36.473 -25.478 1.00 29.34 ? 337 LYS B CA  1 
ATOM   5725 C  C   . LYS B 1 328 ? -12.512 -36.906 -25.817 1.00 28.77 ? 337 LYS B C   1 
ATOM   5726 O  O   . LYS B 1 328 ? -12.883 -36.966 -26.995 1.00 27.04 ? 337 LYS B O   1 
ATOM   5727 C  CB  . LYS B 1 328 ? -10.195 -37.705 -25.284 1.00 31.75 ? 337 LYS B CB  1 
ATOM   5728 C  CG  . LYS B 1 328 ? -10.103 -38.621 -26.487 1.00 38.98 ? 337 LYS B CG  1 
ATOM   5729 C  CD  . LYS B 1 328 ? -9.007  -39.655 -26.298 0.00 38.70 ? 337 LYS B CD  1 
ATOM   5730 C  CE  . LYS B 1 328 ? -9.079  -40.726 -27.371 0.00 40.91 ? 337 LYS B CE  1 
ATOM   5731 N  NZ  . LYS B 1 328 ? -7.915  -41.652 -27.321 0.00 45.46 ? 337 LYS B NZ  1 
ATOM   5732 N  N   . ALA B 1 329 ? -13.300 -37.209 -24.786 1.00 28.50 ? 338 ALA B N   1 
ATOM   5733 C  CA  . ALA B 1 329 ? -14.723 -37.518 -24.966 1.00 30.01 ? 338 ALA B CA  1 
ATOM   5734 C  C   . ALA B 1 329 ? -15.493 -36.359 -25.621 1.00 27.52 ? 338 ALA B C   1 
ATOM   5735 O  O   . ALA B 1 329 ? -16.301 -36.587 -26.526 1.00 29.43 ? 338 ALA B O   1 
ATOM   5736 C  CB  . ALA B 1 329 ? -15.365 -37.938 -23.636 1.00 29.83 ? 338 ALA B CB  1 
ATOM   5737 N  N   . LEU B 1 330 ? -15.211 -35.124 -25.206 1.00 28.32 ? 339 LEU B N   1 
ATOM   5738 C  CA  . LEU B 1 330 ? -15.793 -33.936 -25.877 1.00 27.87 ? 339 LEU B CA  1 
ATOM   5739 C  C   . LEU B 1 330 ? -15.277 -33.745 -27.309 1.00 28.23 ? 339 LEU B C   1 
ATOM   5740 O  O   . LEU B 1 330 ? -16.050 -33.401 -28.212 1.00 26.22 ? 339 LEU B O   1 
ATOM   5741 C  CB  . LEU B 1 330 ? -15.581 -32.662 -25.056 1.00 26.57 ? 339 LEU B CB  1 
ATOM   5742 C  CG  . LEU B 1 330 ? -16.328 -32.602 -23.723 1.00 29.05 ? 339 LEU B CG  1 
ATOM   5743 C  CD1 . LEU B 1 330 ? -15.849 -31.405 -22.922 1.00 29.17 ? 339 LEU B CD1 1 
ATOM   5744 C  CD2 . LEU B 1 330 ? -17.831 -32.533 -23.918 1.00 28.93 ? 339 LEU B CD2 1 
ATOM   5745 N  N   . VAL B 1 331 ? -13.990 -34.004 -27.521 1.00 28.29 ? 340 VAL B N   1 
ATOM   5746 C  CA  . VAL B 1 331 ? -13.407 -33.969 -28.867 1.00 29.00 ? 340 VAL B CA  1 
ATOM   5747 C  C   . VAL B 1 331 ? -14.084 -35.014 -29.757 1.00 28.76 ? 340 VAL B C   1 
ATOM   5748 O  O   . VAL B 1 331 ? -14.486 -34.691 -30.877 1.00 28.00 ? 340 VAL B O   1 
ATOM   5749 C  CB  . VAL B 1 331 ? -11.863 -34.189 -28.855 1.00 29.25 ? 340 VAL B CB  1 
ATOM   5750 C  CG1 . VAL B 1 331 ? -11.300 -34.373 -30.273 1.00 30.89 ? 340 VAL B CG1 1 
ATOM   5751 C  CG2 . VAL B 1 331 ? -11.159 -33.027 -28.153 1.00 26.58 ? 340 VAL B CG2 1 
ATOM   5752 N  N   . SER B 1 332 ? -14.209 -36.247 -29.258 1.00 28.61 ? 341 SER B N   1 
ATOM   5753 C  CA  . SER B 1 332 ? -14.850 -37.324 -30.031 1.00 31.43 ? 341 SER B CA  1 
ATOM   5754 C  C   . SER B 1 332 ? -16.296 -36.983 -30.408 1.00 27.60 ? 341 SER B C   1 
ATOM   5755 O  O   . SER B 1 332 ? -16.716 -37.231 -31.530 1.00 26.83 ? 341 SER B O   1 
ATOM   5756 C  CB  . SER B 1 332 ? -14.821 -38.654 -29.273 1.00 31.35 ? 341 SER B CB  1 
ATOM   5757 O  OG  . SER B 1 332 ? -13.494 -39.087 -29.083 1.00 39.13 ? 341 SER B OG  1 
ATOM   5758 N  N   . LEU B 1 333 ? -17.043 -36.409 -29.470 1.00 29.39 ? 342 LEU B N   1 
ATOM   5759 C  CA  . LEU B 1 333 ? -18.440 -35.996 -29.761 1.00 29.23 ? 342 LEU B CA  1 
ATOM   5760 C  C   . LEU B 1 333 ? -18.464 -34.959 -30.887 1.00 27.92 ? 342 LEU B C   1 
ATOM   5761 O  O   . LEU B 1 333 ? -19.228 -35.141 -31.827 1.00 27.41 ? 342 LEU B O   1 
ATOM   5762 C  CB  . LEU B 1 333 ? -19.079 -35.430 -28.491 1.00 30.49 ? 342 LEU B CB  1 
ATOM   5763 C  CG  . LEU B 1 333 ? -20.589 -35.224 -28.563 1.00 33.14 ? 342 LEU B CG  1 
ATOM   5764 C  CD1 . LEU B 1 333 ? -21.326 -36.540 -28.381 1.00 37.61 ? 342 LEU B CD1 1 
ATOM   5765 C  CD2 . LEU B 1 333 ? -21.038 -34.211 -27.529 1.00 37.95 ? 342 LEU B CD2 1 
ATOM   5766 N  N   . ARG B 1 334 ? -17.634 -33.933 -30.781 1.00 26.33 ? 343 ARG B N   1 
ATOM   5767 C  CA  . ARG B 1 334 ? -17.650 -32.832 -31.771 1.00 24.92 ? 343 ARG B CA  1 
ATOM   5768 C  C   . ARG B 1 334 ? -17.131 -33.324 -33.127 1.00 25.35 ? 343 ARG B C   1 
ATOM   5769 O  O   . ARG B 1 334 ? -17.652 -32.867 -34.137 1.00 22.91 ? 343 ARG B O   1 
ATOM   5770 C  CB  . ARG B 1 334 ? -16.885 -31.645 -31.183 1.00 25.92 ? 343 ARG B CB  1 
ATOM   5771 C  CG  . ARG B 1 334 ? -17.625 -30.946 -30.052 1.00 24.89 ? 343 ARG B CG  1 
ATOM   5772 C  CD  . ARG B 1 334 ? -16.788 -29.917 -29.322 1.00 27.26 ? 343 ARG B CD  1 
ATOM   5773 N  NE  . ARG B 1 334 ? -17.617 -28.927 -28.655 1.00 26.71 ? 343 ARG B NE  1 
ATOM   5774 C  CZ  . ARG B 1 334 ? -17.611 -28.684 -27.352 1.00 29.40 ? 343 ARG B CZ  1 
ATOM   5775 N  NH1 . ARG B 1 334 ? -16.623 -29.121 -26.595 1.00 29.00 ? 343 ARG B NH1 1 
ATOM   5776 N  NH2 . ARG B 1 334 ? -18.595 -27.990 -26.811 1.00 32.60 ? 343 ARG B NH2 1 
ATOM   5777 N  N   . SER B 1 335 ? -16.156 -34.229 -33.124 1.00 24.58 ? 344 SER B N   1 
ATOM   5778 C  CA  . SER B 1 335 ? -15.638 -34.814 -34.383 1.00 26.36 ? 344 SER B CA  1 
ATOM   5779 C  C   . SER B 1 335 ? -16.766 -35.624 -35.035 1.00 26.84 ? 344 SER B C   1 
ATOM   5780 O  O   . SER B 1 335 ? -17.001 -35.433 -36.223 1.00 27.45 ? 344 SER B O   1 
ATOM   5781 C  CB  . SER B 1 335 ? -14.366 -35.604 -34.129 1.00 29.65 ? 344 SER B CB  1 
ATOM   5782 O  OG  . SER B 1 335 ? -13.430 -34.850 -33.381 1.00 28.92 ? 344 SER B OG  1 
ATOM   5783 N  N   . TYR B 1 336 ? -17.453 -36.459 -34.258 1.00 26.74 ? 345 TYR B N   1 
ATOM   5784 C  CA  . TYR B 1 336 ? -18.622 -37.197 -34.762 1.00 27.56 ? 345 TYR B CA  1 
ATOM   5785 C  C   . TYR B 1 336 ? -19.716 -36.247 -35.282 1.00 25.27 ? 345 TYR B C   1 
ATOM   5786 O  O   . TYR B 1 336 ? -20.317 -36.476 -36.324 1.00 24.88 ? 345 TYR B O   1 
ATOM   5787 C  CB  . TYR B 1 336 ? -19.206 -38.084 -33.667 1.00 27.05 ? 345 TYR B CB  1 
ATOM   5788 C  CG  . TYR B 1 336 ? -20.266 -39.024 -34.180 1.00 32.25 ? 345 TYR B CG  1 
ATOM   5789 C  CD1 . TYR B 1 336 ? -19.915 -40.204 -34.846 1.00 32.50 ? 345 TYR B CD1 1 
ATOM   5790 C  CD2 . TYR B 1 336 ? -21.623 -38.740 -34.006 1.00 31.53 ? 345 TYR B CD2 1 
ATOM   5791 C  CE1 . TYR B 1 336 ? -20.892 -41.076 -35.321 1.00 37.68 ? 345 TYR B CE1 1 
ATOM   5792 C  CE2 . TYR B 1 336 ? -22.609 -39.607 -34.477 1.00 34.22 ? 345 TYR B CE2 1 
ATOM   5793 C  CZ  . TYR B 1 336 ? -22.240 -40.766 -35.129 1.00 34.97 ? 345 TYR B CZ  1 
ATOM   5794 O  OH  . TYR B 1 336 ? -23.207 -41.601 -35.600 1.00 40.14 ? 345 TYR B OH  1 
ATOM   5795 N  N   . HIS B 1 337 ? -19.945 -35.180 -34.537 1.00 25.61 ? 346 HIS B N   1 
ATOM   5796 C  CA  . HIS B 1 337 ? -20.932 -34.156 -34.875 1.00 25.32 ? 346 HIS B CA  1 
ATOM   5797 C  C   . HIS B 1 337 ? -20.618 -33.469 -36.213 1.00 26.49 ? 346 HIS B C   1 
ATOM   5798 O  O   . HIS B 1 337 ? -21.537 -33.184 -36.982 1.00 27.22 ? 346 HIS B O   1 
ATOM   5799 C  CB  . HIS B 1 337 ? -21.016 -33.167 -33.708 1.00 24.24 ? 346 HIS B CB  1 
ATOM   5800 C  CG  . HIS B 1 337 ? -21.964 -32.034 -33.912 1.00 24.86 ? 346 HIS B CG  1 
ATOM   5801 N  ND1 . HIS B 1 337 ? -21.541 -30.793 -34.332 1.00 25.12 ? 346 HIS B ND1 1 
ATOM   5802 C  CD2 . HIS B 1 337 ? -23.301 -31.937 -33.725 1.00 25.16 ? 346 HIS B CD2 1 
ATOM   5803 C  CE1 . HIS B 1 337 ? -22.575 -29.977 -34.388 1.00 23.48 ? 346 HIS B CE1 1 
ATOM   5804 N  NE2 . HIS B 1 337 ? -23.658 -30.645 -34.031 1.00 22.34 ? 346 HIS B NE2 1 
ATOM   5805 N  N   . LEU B 1 338 ? -19.333 -33.244 -36.511 1.00 28.96 ? 347 LEU B N   1 
ATOM   5806 C  CA  . LEU B 1 338 ? -18.916 -32.750 -37.835 1.00 29.07 ? 347 LEU B CA  1 
ATOM   5807 C  C   . LEU B 1 338 ? -19.370 -33.663 -38.983 1.00 29.98 ? 347 LEU B C   1 
ATOM   5808 O  O   . LEU B 1 338 ? -19.823 -33.169 -40.022 1.00 31.44 ? 347 LEU B O   1 
ATOM   5809 C  CB  . LEU B 1 338 ? -17.391 -32.569 -37.924 1.00 30.81 ? 347 LEU B CB  1 
ATOM   5810 C  CG  . LEU B 1 338 ? -16.728 -31.434 -37.136 1.00 35.00 ? 347 LEU B CG  1 
ATOM   5811 C  CD1 . LEU B 1 338 ? -15.209 -31.532 -37.290 1.00 36.21 ? 347 LEU B CD1 1 
ATOM   5812 C  CD2 . LEU B 1 338 ? -17.225 -30.069 -37.574 1.00 33.09 ? 347 LEU B CD2 1 
ATOM   5813 N  N   . GLN B 1 339 ? -19.232 -34.977 -38.799 1.00 28.19 ? 348 GLN B N   1 
ATOM   5814 C  CA  . GLN B 1 339 ? -19.722 -35.956 -39.780 1.00 31.88 ? 348 GLN B CA  1 
ATOM   5815 C  C   . GLN B 1 339 ? -21.240 -35.863 -39.934 1.00 29.42 ? 348 GLN B C   1 
ATOM   5816 O  O   . GLN B 1 339 ? -21.776 -35.995 -41.031 1.00 34.31 ? 348 GLN B O   1 
ATOM   5817 C  CB  . GLN B 1 339 ? -19.391 -37.402 -39.369 1.00 34.75 ? 348 GLN B CB  1 
ATOM   5818 C  CG  . GLN B 1 339 ? -17.920 -37.749 -39.126 1.00 38.65 ? 348 GLN B CG  1 
ATOM   5819 C  CD  . GLN B 1 339 ? -17.758 -39.181 -38.599 1.00 42.83 ? 348 GLN B CD  1 
ATOM   5820 O  OE1 . GLN B 1 339 ? -17.110 -39.415 -37.578 1.00 49.32 ? 348 GLN B OE1 1 
ATOM   5821 N  NE2 . GLN B 1 339 ? -18.378 -40.139 -39.285 1.00 48.75 ? 348 GLN B NE2 1 
ATOM   5822 N  N   . ILE B 1 340 ? -21.925 -35.656 -38.817 1.00 27.71 ? 349 ILE B N   1 
ATOM   5823 C  CA  . ILE B 1 340 ? -23.382 -35.487 -38.806 1.00 30.32 ? 349 ILE B CA  1 
ATOM   5824 C  C   . ILE B 1 340 ? -23.795 -34.260 -39.618 1.00 30.43 ? 349 ILE B C   1 
ATOM   5825 O  O   . ILE B 1 340 ? -24.715 -34.343 -40.433 1.00 32.76 ? 349 ILE B O   1 
ATOM   5826 C  CB  . ILE B 1 340 ? -23.926 -35.442 -37.342 1.00 29.16 ? 349 ILE B CB  1 
ATOM   5827 C  CG1 . ILE B 1 340 ? -23.765 -36.822 -36.677 1.00 30.95 ? 349 ILE B CG1 1 
ATOM   5828 C  CG2 . ILE B 1 340 ? -25.386 -34.938 -37.265 1.00 29.45 ? 349 ILE B CG2 1 
ATOM   5829 C  CD1 . ILE B 1 340 ? -24.527 -37.969 -37.331 1.00 34.86 ? 349 ILE B CD1 1 
ATOM   5830 N  N   . VAL B 1 341 ? -23.086 -33.146 -39.432 1.00 30.47 ? 350 VAL B N   1 
ATOM   5831 C  CA  . VAL B 1 341 ? -23.347 -31.933 -40.219 1.00 30.06 ? 350 VAL B CA  1 
ATOM   5832 C  C   . VAL B 1 341 ? -23.091 -32.189 -41.698 1.00 29.78 ? 350 VAL B C   1 
ATOM   5833 O  O   . VAL B 1 341 ? -23.858 -31.742 -42.547 1.00 31.63 ? 350 VAL B O   1 
ATOM   5834 C  CB  . VAL B 1 341 ? -22.545 -30.699 -39.715 1.00 29.24 ? 350 VAL B CB  1 
ATOM   5835 C  CG1 . VAL B 1 341 ? -22.797 -29.464 -40.608 1.00 32.49 ? 350 VAL B CG1 1 
ATOM   5836 C  CG2 . VAL B 1 341 ? -22.948 -30.378 -38.307 1.00 26.36 ? 350 VAL B CG2 1 
ATOM   5837 N  N   . THR B 1 342 ? -22.029 -32.920 -42.014 1.00 31.44 ? 351 THR B N   1 
ATOM   5838 C  CA  . THR B 1 342 ? -21.763 -33.277 -43.413 1.00 31.95 ? 351 THR B CA  1 
ATOM   5839 C  C   . THR B 1 342 ? -22.931 -34.070 -44.031 1.00 33.26 ? 351 THR B C   1 
ATOM   5840 O  O   . THR B 1 342 ? -23.362 -33.772 -45.148 1.00 38.09 ? 351 THR B O   1 
ATOM   5841 C  CB  . THR B 1 342 ? -20.437 -34.045 -43.557 1.00 32.72 ? 351 THR B CB  1 
ATOM   5842 O  OG1 . THR B 1 342 ? -19.377 -33.230 -43.039 1.00 33.24 ? 351 THR B OG1 1 
ATOM   5843 C  CG2 . THR B 1 342 ? -20.141 -34.410 -45.039 1.00 36.19 ? 351 THR B CG2 1 
ATOM   5844 N  N   . LYS B 1 343 ? -23.444 -35.058 -43.297 1.00 33.10 ? 352 LYS B N   1 
ATOM   5845 C  CA  . LYS B 1 343 ? -24.530 -35.915 -43.796 1.00 33.18 ? 352 LYS B CA  1 
ATOM   5846 C  C   . LYS B 1 343 ? -25.868 -35.181 -43.861 1.00 32.94 ? 352 LYS B C   1 
ATOM   5847 O  O   . LYS B 1 343 ? -26.589 -35.315 -44.845 1.00 34.05 ? 352 LYS B O   1 
ATOM   5848 C  CB  . LYS B 1 343 ? -24.677 -37.182 -42.940 1.00 33.78 ? 352 LYS B CB  1 
ATOM   5849 C  CG  . LYS B 1 343 ? -25.770 -38.153 -43.426 1.00 34.00 ? 352 LYS B CG  1 
ATOM   5850 C  CD  . LYS B 1 343 ? -25.902 -39.370 -42.533 1.00 34.64 ? 352 LYS B CD  1 
ATOM   5851 C  CE  . LYS B 1 343 ? -27.215 -40.101 -42.801 1.00 36.23 ? 352 LYS B CE  1 
ATOM   5852 N  NZ  . LYS B 1 343 ? -27.284 -41.419 -42.125 1.00 33.74 ? 352 LYS B NZ  1 
ATOM   5853 N  N   . TYR B 1 344 ? -26.193 -34.414 -42.823 1.00 31.54 ? 353 TYR B N   1 
ATOM   5854 C  CA  . TYR B 1 344 ? -27.536 -33.835 -42.669 1.00 31.59 ? 353 TYR B CA  1 
ATOM   5855 C  C   . TYR B 1 344 ? -27.712 -32.410 -43.223 1.00 34.04 ? 353 TYR B C   1 
ATOM   5856 O  O   . TYR B 1 344 ? -28.854 -31.995 -43.477 1.00 33.27 ? 353 TYR B O   1 
ATOM   5857 C  CB  . TYR B 1 344 ? -27.975 -33.923 -41.205 1.00 30.69 ? 353 TYR B CB  1 
ATOM   5858 C  CG  . TYR B 1 344 ? -28.379 -35.329 -40.822 1.00 28.56 ? 353 TYR B CG  1 
ATOM   5859 C  CD1 . TYR B 1 344 ? -27.435 -36.248 -40.345 1.00 31.00 ? 353 TYR B CD1 1 
ATOM   5860 C  CD2 . TYR B 1 344 ? -29.693 -35.754 -40.973 1.00 32.15 ? 353 TYR B CD2 1 
ATOM   5861 C  CE1 . TYR B 1 344 ? -27.803 -37.552 -40.009 1.00 32.50 ? 353 TYR B CE1 1 
ATOM   5862 C  CE2 . TYR B 1 344 ? -30.073 -37.056 -40.650 1.00 33.45 ? 353 TYR B CE2 1 
ATOM   5863 C  CZ  . TYR B 1 344 ? -29.125 -37.947 -40.167 1.00 30.28 ? 353 TYR B CZ  1 
ATOM   5864 O  OH  . TYR B 1 344 ? -29.486 -39.224 -39.851 1.00 33.22 ? 353 TYR B OH  1 
ATOM   5865 N  N   . ILE B 1 345 ? -26.603 -31.692 -43.437 1.00 33.40 ? 354 ILE B N   1 
ATOM   5866 C  CA  . ILE B 1 345 ? -26.636 -30.328 -43.988 1.00 35.76 ? 354 ILE B CA  1 
ATOM   5867 C  C   . ILE B 1 345 ? -25.839 -30.186 -45.281 1.00 37.02 ? 354 ILE B C   1 
ATOM   5868 O  O   . ILE B 1 345 ? -26.408 -29.822 -46.314 1.00 40.33 ? 354 ILE B O   1 
ATOM   5869 C  CB  . ILE B 1 345 ? -26.181 -29.286 -42.936 1.00 34.97 ? 354 ILE B CB  1 
ATOM   5870 C  CG1 . ILE B 1 345 ? -27.232 -29.218 -41.820 1.00 35.17 ? 354 ILE B CG1 1 
ATOM   5871 C  CG2 . ILE B 1 345 ? -25.996 -27.883 -43.585 1.00 39.13 ? 354 ILE B CG2 1 
ATOM   5872 C  CD1 . ILE B 1 345 ? -26.854 -28.406 -40.630 1.00 36.76 ? 354 ILE B CD1 1 
ATOM   5873 N  N   . LEU B 1 346 ? -24.537 -30.462 -45.235 1.00 37.76 ? 355 LEU B N   1 
ATOM   5874 C  CA  . LEU B 1 346 ? -23.658 -30.180 -46.390 1.00 39.67 ? 355 LEU B CA  1 
ATOM   5875 C  C   . LEU B 1 346 ? -24.007 -30.972 -47.645 1.00 41.27 ? 355 LEU B C   1 
ATOM   5876 O  O   . LEU B 1 346 ? -23.971 -30.425 -48.747 1.00 42.90 ? 355 LEU B O   1 
ATOM   5877 C  CB  . LEU B 1 346 ? -22.184 -30.416 -46.051 1.00 40.49 ? 355 LEU B CB  1 
ATOM   5878 C  CG  . LEU B 1 346 ? -21.582 -29.686 -44.849 1.00 40.84 ? 355 LEU B CG  1 
ATOM   5879 C  CD1 . LEU B 1 346 ? -20.100 -30.005 -44.785 1.00 41.10 ? 355 LEU B CD1 1 
ATOM   5880 C  CD2 . LEU B 1 346 ? -21.805 -28.178 -44.923 1.00 42.38 ? 355 LEU B CD2 1 
ATOM   5881 N  N   . ILE B 1 347 ? -24.345 -32.250 -47.476 1.00 41.27 ? 356 ILE B N   1 
ATOM   5882 C  CA  . ILE B 1 347 ? -24.647 -33.124 -48.619 1.00 42.94 ? 356 ILE B CA  1 
ATOM   5883 C  C   . ILE B 1 347 ? -26.011 -32.780 -49.254 1.00 42.48 ? 356 ILE B C   1 
ATOM   5884 O  O   . ILE B 1 347 ? -26.062 -32.540 -50.456 1.00 45.87 ? 356 ILE B O   1 
ATOM   5885 C  CB  . ILE B 1 347 ? -24.461 -34.639 -48.275 1.00 42.10 ? 356 ILE B CB  1 
ATOM   5886 C  CG1 . ILE B 1 347 ? -22.963 -34.950 -48.171 1.00 46.71 ? 356 ILE B CG1 1 
ATOM   5887 C  CG2 . ILE B 1 347 ? -25.100 -35.540 -49.346 1.00 47.65 ? 356 ILE B CG2 1 
ATOM   5888 C  CD1 . ILE B 1 347 ? -22.620 -36.291 -47.533 1.00 47.95 ? 356 ILE B CD1 1 
ATOM   5889 N  N   . PRO B 1 348 ? -27.111 -32.765 -48.469 1.00 40.61 ? 357 PRO B N   1 
ATOM   5890 C  CA  . PRO B 1 348 ? -28.398 -32.271 -48.985 1.00 41.89 ? 357 PRO B CA  1 
ATOM   5891 C  C   . PRO B 1 348 ? -28.323 -30.907 -49.694 1.00 43.36 ? 357 PRO B C   1 
ATOM   5892 O  O   . PRO B 1 348 ? -28.916 -30.738 -50.768 1.00 44.75 ? 357 PRO B O   1 
ATOM   5893 C  CB  . PRO B 1 348 ? -29.258 -32.181 -47.725 1.00 39.32 ? 357 PRO B CB  1 
ATOM   5894 C  CG  . PRO B 1 348 ? -28.751 -33.248 -46.868 1.00 38.26 ? 357 PRO B CG  1 
ATOM   5895 C  CD  . PRO B 1 348 ? -27.259 -33.261 -47.090 1.00 39.28 ? 357 PRO B CD  1 
ATOM   5896 N  N   . ALA B 1 349 ? -27.580 -29.971 -49.101 1.00 41.07 ? 358 ALA B N   1 
ATOM   5897 C  CA  . ALA B 1 349 ? -27.315 -28.666 -49.711 1.00 45.14 ? 358 ALA B CA  1 
ATOM   5898 C  C   . ALA B 1 349 ? -26.668 -28.777 -51.093 1.00 49.80 ? 358 ALA B C   1 
ATOM   5899 O  O   . ALA B 1 349 ? -27.041 -28.046 -52.000 1.00 54.69 ? 358 ALA B O   1 
ATOM   5900 C  CB  . ALA B 1 349 ? -26.445 -27.813 -48.792 1.00 42.05 ? 358 ALA B CB  1 
ATOM   5901 N  N   . SER B 1 350 ? -25.711 -29.694 -51.243 1.00 51.60 ? 359 SER B N   1 
ATOM   5902 C  CA  . SER B 1 350 ? -25.051 -29.938 -52.533 1.00 56.77 ? 359 SER B CA  1 
ATOM   5903 C  C   . SER B 1 350 ? -25.997 -30.523 -53.586 1.00 61.29 ? 359 SER B C   1 
ATOM   5904 O  O   . SER B 1 350 ? -25.861 -30.228 -54.775 1.00 64.79 ? 359 SER B O   1 
ATOM   5905 C  CB  . SER B 1 350 ? -23.853 -30.879 -52.362 1.00 55.64 ? 359 SER B CB  1 
ATOM   5906 O  OG  . SER B 1 350 ? -24.279 -32.222 -52.188 1.00 52.14 ? 359 SER B OG  1 
ATOM   5907 N  N   . GLN B 1 351 ? -26.944 -31.347 -53.135 1.00 62.65 ? 360 GLN B N   1 
ATOM   5908 C  CA  . GLN B 1 351 ? -27.936 -32.003 -54.007 1.00 66.73 ? 360 GLN B CA  1 
ATOM   5909 C  C   . GLN B 1 351 ? -29.141 -31.127 -54.425 1.00 70.53 ? 360 GLN B C   1 
ATOM   5910 O  O   . GLN B 1 351 ? -29.985 -31.591 -55.195 1.00 73.55 ? 360 GLN B O   1 
ATOM   5911 C  CB  . GLN B 1 351 ? -28.457 -33.284 -53.325 1.00 64.45 ? 360 GLN B CB  1 
ATOM   5912 C  CG  . GLN B 1 351 ? -27.367 -34.343 -53.047 1.00 65.08 ? 360 GLN B CG  1 
ATOM   5913 C  CD  . GLN B 1 351 ? -27.766 -35.395 -52.010 1.00 62.86 ? 360 GLN B CD  1 
ATOM   5914 O  OE1 . GLN B 1 351 ? -28.569 -35.136 -51.110 1.00 65.75 ? 360 GLN B OE1 1 
ATOM   5915 N  NE2 . GLN B 1 351 ? -27.177 -36.583 -52.120 1.00 55.39 ? 360 GLN B NE2 1 
ATOM   5916 N  N   A GLN B 1 352 ? -29.236 -29.899 -53.910 0.50 71.16 ? 361 GLN B N   1 
ATOM   5917 N  N   B GLN B 1 352 ? -29.176 -29.876 -53.959 0.50 71.19 ? 361 GLN B N   1 
ATOM   5918 C  CA  A GLN B 1 352 ? -30.390 -29.036 -54.194 0.50 73.58 ? 361 GLN B CA  1 
ATOM   5919 C  CA  B GLN B 1 352 ? -30.297 -28.952 -54.184 0.50 73.49 ? 361 GLN B CA  1 
ATOM   5920 C  C   A GLN B 1 352 ? -30.235 -28.350 -55.562 0.50 78.67 ? 361 GLN B C   1 
ATOM   5921 C  C   B GLN B 1 352 ? -30.204 -28.333 -55.592 0.50 78.67 ? 361 GLN B C   1 
ATOM   5922 O  O   A GLN B 1 352 ? -29.120 -27.981 -55.944 0.50 80.50 ? 361 GLN B O   1 
ATOM   5923 O  O   B GLN B 1 352 ? -29.102 -27.988 -56.030 0.50 80.59 ? 361 GLN B O   1 
ATOM   5924 C  CB  A GLN B 1 352 ? -30.609 -28.011 -53.066 0.50 72.25 ? 361 GLN B CB  1 
ATOM   5925 C  CB  B GLN B 1 352 ? -30.272 -27.836 -53.115 0.50 72.08 ? 361 GLN B CB  1 
ATOM   5926 C  CG  A GLN B 1 352 ? -29.741 -26.751 -53.115 0.50 72.82 ? 361 GLN B CG  1 
ATOM   5927 C  CG  B GLN B 1 352 ? -31.637 -27.382 -52.595 0.50 71.79 ? 361 GLN B CG  1 
ATOM   5928 C  CD  A GLN B 1 352 ? -29.662 -26.046 -51.770 0.50 69.87 ? 361 GLN B CD  1 
ATOM   5929 C  CD  B GLN B 1 352 ? -32.287 -28.377 -51.638 0.50 67.45 ? 361 GLN B CD  1 
ATOM   5930 O  OE1 A GLN B 1 352 ? -30.681 -25.824 -51.115 0.50 68.48 ? 361 GLN B OE1 1 
ATOM   5931 O  OE1 B GLN B 1 352 ? -31.837 -29.516 -51.491 0.50 66.22 ? 361 GLN B OE1 1 
ATOM   5932 N  NE2 A GLN B 1 352 ? -28.452 -25.688 -51.355 0.50 66.91 ? 361 GLN B NE2 1 
ATOM   5933 N  NE2 B GLN B 1 352 ? -33.355 -27.943 -50.980 0.50 63.53 ? 361 GLN B NE2 1 
ATOM   5934 N  N   . PRO B 1 353 ? -31.348 -28.188 -56.307 1.00 81.74 ? 362 PRO B N   1 
ATOM   5935 C  CA  . PRO B 1 353 ? -31.303 -27.508 -57.614 1.00 86.38 ? 362 PRO B CA  1 
ATOM   5936 C  C   . PRO B 1 353 ? -31.179 -25.988 -57.483 1.00 88.63 ? 362 PRO B C   1 
ATOM   5937 O  O   . PRO B 1 353 ? -30.067 -25.462 -57.424 1.00 89.22 ? 362 PRO B O   1 
ATOM   5938 C  CB  . PRO B 1 353 ? -32.643 -27.888 -58.252 1.00 89.29 ? 362 PRO B CB  1 
ATOM   5939 C  CG  . PRO B 1 353 ? -33.557 -28.061 -57.100 1.00 86.04 ? 362 PRO B CG  1 
ATOM   5940 C  CD  . PRO B 1 353 ? -32.722 -28.638 -55.992 1.00 81.40 ? 362 PRO B CD  1 
ATOM   5941 N  N   . GLY B 1 371 ? -22.716 -20.116 -45.914 1.00 58.64 ? 380 GLY B N   1 
ATOM   5942 C  CA  . GLY B 1 371 ? -23.493 -20.775 -44.863 1.00 53.86 ? 380 GLY B CA  1 
ATOM   5943 C  C   . GLY B 1 371 ? -22.852 -22.058 -44.359 1.00 50.10 ? 380 GLY B C   1 
ATOM   5944 O  O   . GLY B 1 371 ? -22.438 -22.130 -43.209 1.00 45.26 ? 380 GLY B O   1 
ATOM   5945 N  N   . GLY B 1 372 ? -22.764 -23.063 -45.230 1.00 50.41 ? 381 GLY B N   1 
ATOM   5946 C  CA  . GLY B 1 372 ? -22.205 -24.376 -44.882 1.00 47.84 ? 381 GLY B CA  1 
ATOM   5947 C  C   . GLY B 1 372 ? -20.765 -24.305 -44.403 1.00 48.01 ? 381 GLY B C   1 
ATOM   5948 O  O   . GLY B 1 372 ? -20.414 -24.917 -43.398 1.00 45.59 ? 381 GLY B O   1 
ATOM   5949 N  N   . THR B 1 373 ? -19.947 -23.540 -45.128 1.00 50.89 ? 382 THR B N   1 
ATOM   5950 C  CA  . THR B 1 373 ? -18.558 -23.254 -44.742 1.00 51.13 ? 382 THR B CA  1 
ATOM   5951 C  C   . THR B 1 373 ? -18.496 -22.538 -43.391 1.00 47.73 ? 382 THR B C   1 
ATOM   5952 O  O   . THR B 1 373 ? -17.723 -22.930 -42.526 1.00 46.26 ? 382 THR B O   1 
ATOM   5953 C  CB  . THR B 1 373 ? -17.824 -22.424 -45.852 1.00 55.91 ? 382 THR B CB  1 
ATOM   5954 O  OG1 . THR B 1 373 ? -17.624 -23.256 -46.997 1.00 61.30 ? 382 THR B OG1 1 
ATOM   5955 C  CG2 . THR B 1 373 ? -16.454 -21.884 -45.396 1.00 57.50 ? 382 THR B CG2 1 
ATOM   5956 N  N   . ASP B 1 374 ? -19.313 -21.499 -43.224 1.00 46.97 ? 383 ASP B N   1 
ATOM   5957 C  CA  . ASP B 1 374 ? -19.379 -20.750 -41.964 1.00 46.47 ? 383 ASP B CA  1 
ATOM   5958 C  C   . ASP B 1 374 ? -19.757 -21.635 -40.780 1.00 40.55 ? 383 ASP B C   1 
ATOM   5959 O  O   . ASP B 1 374 ? -19.132 -21.549 -39.720 1.00 37.11 ? 383 ASP B O   1 
ATOM   5960 C  CB  . ASP B 1 374 ? -20.373 -19.584 -42.066 1.00 47.93 ? 383 ASP B CB  1 
ATOM   5961 C  CG  . ASP B 1 374 ? -19.873 -18.452 -42.947 1.00 58.62 ? 383 ASP B CG  1 
ATOM   5962 O  OD1 . ASP B 1 374 ? -18.652 -18.359 -43.214 1.00 65.32 ? 383 ASP B OD1 1 
ATOM   5963 O  OD2 . ASP B 1 374 ? -20.718 -17.637 -43.369 1.00 66.11 ? 383 ASP B OD2 1 
ATOM   5964 N  N   . LEU B 1 375 ? -20.768 -22.484 -40.971 1.00 38.11 ? 384 LEU B N   1 
ATOM   5965 C  CA  . LEU B 1 375 ? -21.226 -23.399 -39.922 1.00 37.08 ? 384 LEU B CA  1 
ATOM   5966 C  C   . LEU B 1 375 ? -20.135 -24.396 -39.528 1.00 35.52 ? 384 LEU B C   1 
ATOM   5967 O  O   . LEU B 1 375 ? -19.907 -24.617 -38.343 1.00 34.58 ? 384 LEU B O   1 
ATOM   5968 C  CB  . LEU B 1 375 ? -22.488 -24.159 -40.364 1.00 37.12 ? 384 LEU B CB  1 
ATOM   5969 C  CG  . LEU B 1 375 ? -23.786 -23.359 -40.548 1.00 40.36 ? 384 LEU B CG  1 
ATOM   5970 C  CD1 . LEU B 1 375 ? -24.868 -24.269 -41.136 1.00 42.16 ? 384 LEU B CD1 1 
ATOM   5971 C  CD2 . LEU B 1 375 ? -24.260 -22.722 -39.262 1.00 38.78 ? 384 LEU B CD2 1 
ATOM   5972 N  N   . MET B 1 376 ? -19.469 -24.988 -40.522 1.00 35.79 ? 385 MET B N   1 
ATOM   5973 C  CA  . MET B 1 376 ? -18.377 -25.933 -40.270 1.00 35.63 ? 385 MET B CA  1 
ATOM   5974 C  C   . MET B 1 376 ? -17.150 -25.260 -39.671 1.00 34.21 ? 385 MET B C   1 
ATOM   5975 O  O   . MET B 1 376 ? -16.506 -25.829 -38.803 1.00 32.83 ? 385 MET B O   1 
ATOM   5976 C  CB  . MET B 1 376 ? -17.978 -26.669 -41.550 1.00 38.65 ? 385 MET B CB  1 
ATOM   5977 C  CG  . MET B 1 376 ? -19.040 -27.619 -42.053 1.00 39.79 ? 385 MET B CG  1 
ATOM   5978 S  SD  . MET B 1 376 ? -19.298 -29.030 -40.956 1.00 39.59 ? 385 MET B SD  1 
ATOM   5979 C  CE  . MET B 1 376 ? -17.980 -30.123 -41.476 1.00 39.47 ? 385 MET B CE  1 
ATOM   5980 N  N   . ASN B 1 377 ? -16.829 -24.055 -40.130 1.00 36.02 ? 386 ASN B N   1 
ATOM   5981 C  CA  . ASN B 1 377 ? -15.718 -23.300 -39.538 1.00 37.49 ? 386 ASN B CA  1 
ATOM   5982 C  C   . ASN B 1 377 ? -15.953 -22.999 -38.063 1.00 34.92 ? 386 ASN B C   1 
ATOM   5983 O  O   . ASN B 1 377 ? -15.040 -23.166 -37.245 1.00 31.17 ? 386 ASN B O   1 
ATOM   5984 C  CB  . ASN B 1 377 ? -15.426 -22.020 -40.329 1.00 39.74 ? 386 ASN B CB  1 
ATOM   5985 C  CG  . ASN B 1 377 ? -14.770 -22.302 -41.682 1.00 44.84 ? 386 ASN B CG  1 
ATOM   5986 O  OD1 . ASN B 1 377 ? -14.604 -21.397 -42.505 1.00 43.43 ? 386 ASN B OD1 1 
ATOM   5987 N  ND2 . ASN B 1 377 ? -14.410 -23.559 -41.920 1.00 39.99 ? 386 ASN B ND2 1 
ATOM   5988 N  N   . PHE B 1 378 ? -17.183 -22.595 -37.729 1.00 33.96 ? 387 PHE B N   1 
ATOM   5989 C  CA  . PHE B 1 378 ? -17.576 -22.395 -36.330 1.00 31.93 ? 387 PHE B CA  1 
ATOM   5990 C  C   . PHE B 1 378 ? -17.388 -23.672 -35.514 1.00 29.32 ? 387 PHE B C   1 
ATOM   5991 O  O   . PHE B 1 378 ? -16.762 -23.655 -34.463 1.00 27.84 ? 387 PHE B O   1 
ATOM   5992 C  CB  . PHE B 1 378 ? -19.031 -21.928 -36.214 1.00 31.87 ? 387 PHE B CB  1 
ATOM   5993 C  CG  . PHE B 1 378 ? -19.595 -22.083 -34.835 1.00 30.73 ? 387 PHE B CG  1 
ATOM   5994 C  CD1 . PHE B 1 378 ? -19.116 -21.297 -33.789 1.00 31.01 ? 387 PHE B CD1 1 
ATOM   5995 C  CD2 . PHE B 1 378 ? -20.565 -23.046 -34.565 1.00 26.71 ? 387 PHE B CD2 1 
ATOM   5996 C  CE1 . PHE B 1 378 ? -19.619 -21.443 -32.508 1.00 30.74 ? 387 PHE B CE1 1 
ATOM   5997 C  CE2 . PHE B 1 378 ? -21.076 -23.196 -33.292 1.00 26.80 ? 387 PHE B CE2 1 
ATOM   5998 C  CZ  . PHE B 1 378 ? -20.604 -22.407 -32.257 1.00 26.23 ? 387 PHE B CZ  1 
ATOM   5999 N  N   . LEU B 1 379 ? -17.928 -24.778 -36.011 1.00 28.63 ? 388 LEU B N   1 
ATOM   6000 C  CA  . LEU B 1 379 ? -17.829 -26.052 -35.303 1.00 25.73 ? 388 LEU B CA  1 
ATOM   6001 C  C   . LEU B 1 379 ? -16.378 -26.531 -35.147 1.00 25.29 ? 388 LEU B C   1 
ATOM   6002 O  O   . LEU B 1 379 ? -16.012 -27.054 -34.097 1.00 25.07 ? 388 LEU B O   1 
ATOM   6003 C  CB  . LEU B 1 379 ? -18.683 -27.125 -35.992 1.00 25.96 ? 388 LEU B CB  1 
ATOM   6004 C  CG  . LEU B 1 379 ? -20.197 -26.875 -35.994 1.00 25.49 ? 388 LEU B CG  1 
ATOM   6005 C  CD1 . LEU B 1 379 ? -20.886 -27.879 -36.906 1.00 25.27 ? 388 LEU B CD1 1 
ATOM   6006 C  CD2 . LEU B 1 379 ? -20.784 -26.950 -34.600 1.00 23.71 ? 388 LEU B CD2 1 
ATOM   6007 N  N   . LYS B 1 380 ? -15.566 -26.336 -36.181 1.00 28.61 ? 389 LYS B N   1 
ATOM   6008 C  CA  . LYS B 1 380 ? -14.144 -26.691 -36.129 1.00 30.08 ? 389 LYS B CA  1 
ATOM   6009 C  C   . LYS B 1 380 ? -13.358 -25.843 -35.131 1.00 30.90 ? 389 LYS B C   1 
ATOM   6010 O  O   . LYS B 1 380 ? -12.463 -26.361 -34.450 1.00 28.89 ? 389 LYS B O   1 
ATOM   6011 C  CB  . LYS B 1 380 ? -13.514 -26.600 -37.517 1.00 33.98 ? 389 LYS B CB  1 
ATOM   6012 C  CG  . LYS B 1 380 ? -13.908 -27.760 -38.441 1.00 35.58 ? 389 LYS B CG  1 
ATOM   6013 C  CD  . LYS B 1 380 ? -13.364 -27.531 -39.846 1.00 39.87 ? 389 LYS B CD  1 
ATOM   6014 C  CE  . LYS B 1 380 ? -13.817 -28.607 -40.827 1.00 45.51 ? 389 LYS B CE  1 
ATOM   6015 N  NZ  . LYS B 1 380 ? -13.393 -28.261 -42.228 1.00 47.84 ? 389 LYS B NZ  1 
ATOM   6016 N  N   . THR B 1 381 ? -13.694 -24.554 -35.037 1.00 29.32 ? 390 THR B N   1 
ATOM   6017 C  CA  . THR B 1 381 ? -13.080 -23.673 -34.039 1.00 31.48 ? 390 THR B CA  1 
ATOM   6018 C  C   . THR B 1 381 ? -13.372 -24.177 -32.628 1.00 30.05 ? 390 THR B C   1 
ATOM   6019 O  O   . THR B 1 381 ? -12.480 -24.212 -31.775 1.00 29.13 ? 390 THR B O   1 
ATOM   6020 C  CB  . THR B 1 381 ? -13.566 -22.204 -34.194 1.00 32.83 ? 390 THR B CB  1 
ATOM   6021 O  OG1 . THR B 1 381 ? -13.183 -21.720 -35.480 1.00 33.88 ? 390 THR B OG1 1 
ATOM   6022 C  CG2 . THR B 1 381 ? -12.968 -21.281 -33.120 1.00 32.26 ? 390 THR B CG2 1 
ATOM   6023 N  N   . VAL B 1 382 ? -14.623 -24.570 -32.390 1.00 29.59 ? 391 VAL B N   1 
ATOM   6024 C  CA  . VAL B 1 382 ? -15.043 -25.050 -31.077 1.00 27.35 ? 391 VAL B CA  1 
ATOM   6025 C  C   . VAL B 1 382 ? -14.400 -26.412 -30.780 1.00 28.28 ? 391 VAL B C   1 
ATOM   6026 O  O   . VAL B 1 382 ? -13.930 -26.652 -29.658 1.00 25.83 ? 391 VAL B O   1 
ATOM   6027 C  CB  . VAL B 1 382 ? -16.584 -25.096 -30.956 1.00 27.92 ? 391 VAL B CB  1 
ATOM   6028 C  CG1 . VAL B 1 382 ? -17.025 -25.728 -29.638 1.00 27.47 ? 391 VAL B CG1 1 
ATOM   6029 C  CG2 . VAL B 1 382 ? -17.172 -23.674 -31.058 1.00 27.52 ? 391 VAL B CG2 1 
ATOM   6030 N  N   . ARG B 1 383 ? -14.369 -27.288 -31.783 1.00 28.22 ? 392 ARG B N   1 
ATOM   6031 C  CA  . ARG B 1 383 ? -13.655 -28.554 -31.659 1.00 29.60 ? 392 ARG B CA  1 
ATOM   6032 C  C   . ARG B 1 383 ? -12.169 -28.316 -31.344 1.00 31.57 ? 392 ARG B C   1 
ATOM   6033 O  O   . ARG B 1 383 ? -11.621 -28.938 -30.437 1.00 30.15 ? 392 ARG B O   1 
ATOM   6034 C  CB  . ARG B 1 383 ? -13.776 -29.385 -32.933 1.00 28.50 ? 392 ARG B CB  1 
ATOM   6035 C  CG  . ARG B 1 383 ? -13.265 -30.804 -32.758 1.00 27.12 ? 392 ARG B CG  1 
ATOM   6036 C  CD  . ARG B 1 383 ? -12.969 -31.482 -34.072 1.00 31.97 ? 392 ARG B CD  1 
ATOM   6037 N  NE  . ARG B 1 383 ? -12.003 -32.571 -33.907 1.00 32.50 ? 392 ARG B NE  1 
ATOM   6038 C  CZ  . ARG B 1 383 ? -10.701 -32.403 -33.679 1.00 37.50 ? 392 ARG B CZ  1 
ATOM   6039 N  NH1 . ARG B 1 383 ? -10.158 -31.183 -33.609 1.00 41.32 ? 392 ARG B NH1 1 
ATOM   6040 N  NH2 . ARG B 1 383 ? -9.927  -33.482 -33.541 1.00 39.67 ? 392 ARG B NH2 1 
ATOM   6041 N  N   . SER B 1 384 ? -11.537 -27.430 -32.110 1.00 34.12 ? 393 SER B N   1 
ATOM   6042 C  CA  . SER B 1 384 ? -10.120 -27.094 -31.928 1.00 36.24 ? 393 SER B CA  1 
ATOM   6043 C  C   . SER B 1 384 ? -9.797  -26.575 -30.527 1.00 37.27 ? 393 SER B C   1 
ATOM   6044 O  O   . SER B 1 384 ? -8.773  -26.952 -29.947 1.00 36.92 ? 393 SER B O   1 
ATOM   6045 C  CB  . SER B 1 384 ? -9.681  -26.049 -32.953 1.00 38.03 ? 393 SER B CB  1 
ATOM   6046 O  OG  . SER B 1 384 ? -8.325  -25.691 -32.761 1.00 42.82 ? 393 SER B OG  1 
ATOM   6047 N  N   . THR B 1 385 ? -10.658 -25.697 -30.008 1.00 34.92 ? 394 THR B N   1 
ATOM   6048 C  CA  . THR B 1 385 ? -10.510 -25.172 -28.650 1.00 36.44 ? 394 THR B CA  1 
ATOM   6049 C  C   . THR B 1 385 ? -10.516 -26.322 -27.628 1.00 33.87 ? 394 THR B C   1 
ATOM   6050 O  O   . THR B 1 385 ? -9.780  -26.284 -26.637 1.00 32.23 ? 394 THR B O   1 
ATOM   6051 C  CB  . THR B 1 385 ? -11.636 -24.159 -28.309 1.00 34.01 ? 394 THR B CB  1 
ATOM   6052 O  OG1 . THR B 1 385 ? -11.641 -23.113 -29.282 1.00 37.46 ? 394 THR B OG1 1 
ATOM   6053 C  CG2 . THR B 1 385 ? -11.436 -23.540 -26.931 1.00 38.02 ? 394 THR B CG2 1 
ATOM   6054 N  N   . THR B 1 386 ? -11.355 -27.322 -27.883 1.00 31.38 ? 395 THR B N   1 
ATOM   6055 C  CA  . THR B 1 386 ? -11.441 -28.515 -27.047 1.00 31.11 ? 395 THR B CA  1 
ATOM   6056 C  C   . THR B 1 386 ? -10.172 -29.357 -27.162 1.00 31.20 ? 395 THR B C   1 
ATOM   6057 O  O   . THR B 1 386 ? -9.577  -29.715 -26.155 1.00 30.80 ? 395 THR B O   1 
ATOM   6058 C  CB  . THR B 1 386 ? -12.661 -29.370 -27.440 1.00 30.35 ? 395 THR B CB  1 
ATOM   6059 O  OG1 . THR B 1 386 ? -13.792 -28.514 -27.629 1.00 28.99 ? 395 THR B OG1 1 
ATOM   6060 C  CG2 . THR B 1 386 ? -12.989 -30.403 -26.371 1.00 30.94 ? 395 THR B CG2 1 
ATOM   6061 N  N   . GLU B 1 387 ? -9.773  -29.660 -28.395 1.00 33.11 ? 396 GLU B N   1 
ATOM   6062 C  CA  . GLU B 1 387 ? -8.567  -30.457 -28.678 1.00 35.59 ? 396 GLU B CA  1 
ATOM   6063 C  C   . GLU B 1 387 ? -7.304  -29.833 -28.083 1.00 38.03 ? 396 GLU B C   1 
ATOM   6064 O  O   . GLU B 1 387 ? -6.403  -30.547 -27.644 1.00 38.26 ? 396 GLU B O   1 
ATOM   6065 C  CB  . GLU B 1 387 ? -8.394  -30.657 -30.195 1.00 35.91 ? 396 GLU B CB  1 
ATOM   6066 C  CG  . GLU B 1 387 ? -7.498  -31.851 -30.615 1.00 41.13 ? 396 GLU B CG  1 
ATOM   6067 C  CD  . GLU B 1 387 ? -6.002  -31.520 -30.736 1.00 50.01 ? 396 GLU B CD  1 
ATOM   6068 O  OE1 . GLU B 1 387 ? -5.648  -30.355 -31.019 1.00 53.00 ? 396 GLU B OE1 1 
ATOM   6069 O  OE2 . GLU B 1 387 ? -5.172  -32.444 -30.555 1.00 58.71 ? 396 GLU B OE2 1 
ATOM   6070 N  N   . LYS B 1 388 ? -7.252  -28.501 -28.063 1.00 39.84 ? 397 LYS B N   1 
ATOM   6071 C  CA  . LYS B 1 388 ? -6.087  -27.771 -27.560 1.00 43.32 ? 397 LYS B CA  1 
ATOM   6072 C  C   . LYS B 1 388 ? -6.027  -27.693 -26.025 1.00 42.19 ? 397 LYS B C   1 
ATOM   6073 O  O   . LYS B 1 388 ? -5.016  -27.255 -25.472 1.00 42.90 ? 397 LYS B O   1 
ATOM   6074 C  CB  . LYS B 1 388 ? -6.004  -26.384 -28.225 1.00 45.63 ? 397 LYS B CB  1 
ATOM   6075 C  CG  . LYS B 1 388 ? -5.508  -26.477 -29.678 1.00 49.24 ? 397 LYS B CG  1 
ATOM   6076 C  CD  . LYS B 1 388 ? -5.336  -25.117 -30.340 1.00 53.14 ? 397 LYS B CD  1 
ATOM   6077 C  CE  . LYS B 1 388 ? -4.258  -25.154 -31.441 1.00 57.91 ? 397 LYS B CE  1 
ATOM   6078 N  NZ  . LYS B 1 388 ? -4.513  -26.172 -32.507 1.00 56.49 ? 397 LYS B NZ  1 
ATOM   6079 N  N   . SER B 1 389 ? -7.095  -28.135 -25.351 1.00 38.62 ? 398 SER B N   1 
ATOM   6080 C  CA  . SER B 1 389 ? -7.093  -28.326 -23.900 1.00 38.00 ? 398 SER B CA  1 
ATOM   6081 C  C   . SER B 1 389 ? -6.534  -29.683 -23.448 1.00 37.25 ? 398 SER B C   1 
ATOM   6082 O  O   . SER B 1 389 ? -6.331  -29.891 -22.254 1.00 36.58 ? 398 SER B O   1 
ATOM   6083 C  CB  . SER B 1 389 ? -8.500  -28.143 -23.344 1.00 36.82 ? 398 SER B CB  1 
ATOM   6084 O  OG  . SER B 1 389 ? -8.968  -26.846 -23.654 1.00 38.66 ? 398 SER B OG  1 
ATOM   6085 N  N   . LEU B 1 390 ? -6.292  -30.604 -24.382 1.00 37.02 ? 399 LEU B N   1 
ATOM   6086 C  CA  . LEU B 1 390 ? -5.631  -31.877 -24.053 1.00 37.58 ? 399 LEU B CA  1 
ATOM   6087 C  C   . LEU B 1 390 ? -4.231  -31.627 -23.504 1.00 39.51 ? 399 LEU B C   1 
ATOM   6088 O  O   . LEU B 1 390 ? -3.463  -30.848 -24.068 1.00 41.30 ? 399 LEU B O   1 
ATOM   6089 C  CB  . LEU B 1 390 ? -5.542  -32.793 -25.279 1.00 37.16 ? 399 LEU B CB  1 
ATOM   6090 C  CG  . LEU B 1 390 ? -6.828  -33.447 -25.790 1.00 34.23 ? 399 LEU B CG  1 
ATOM   6091 C  CD1 . LEU B 1 390 ? -6.569  -34.093 -27.137 1.00 36.96 ? 399 LEU B CD1 1 
ATOM   6092 C  CD2 . LEU B 1 390 ? -7.349  -34.481 -24.813 1.00 33.29 ? 399 LEU B CD2 1 
ATOM   6093 N  N   . LEU B 1 391 ? -3.907  -32.283 -22.397 1.00 40.83 ? 400 LEU B N   1 
ATOM   6094 C  CA  . LEU B 1 391 ? -2.593  -32.124 -21.769 1.00 44.78 ? 400 LEU B CA  1 
ATOM   6095 C  C   . LEU B 1 391 ? -1.538  -32.888 -22.561 1.00 47.95 ? 400 LEU B C   1 
ATOM   6096 O  O   . LEU B 1 391 ? -0.429  -32.394 -22.774 1.00 50.46 ? 400 LEU B O   1 
ATOM   6097 C  CB  . LEU B 1 391 ? -2.632  -32.595 -20.314 1.00 44.72 ? 400 LEU B CB  1 
ATOM   6098 C  CG  . LEU B 1 391 ? -3.694  -31.922 -19.432 1.00 41.49 ? 400 LEU B CG  1 
ATOM   6099 C  CD1 . LEU B 1 391 ? -3.734  -32.588 -18.074 1.00 45.85 ? 400 LEU B CD1 1 
ATOM   6100 C  CD2 . LEU B 1 391 ? -3.448  -30.422 -19.289 1.00 41.79 ? 400 LEU B CD2 1 
ATOM   6101 N  N   . LYS B 1 392 ? -1.914  -34.093 -22.986 1.00 49.76 ? 401 LYS B N   1 
ATOM   6102 C  CA  . LYS B 1 392 ? -1.108  -34.962 -23.835 1.00 53.83 ? 401 LYS B CA  1 
ATOM   6103 C  C   . LYS B 1 392 ? -1.845  -35.133 -25.154 1.00 53.18 ? 401 LYS B C   1 
ATOM   6104 O  O   . LYS B 1 392 ? -3.073  -35.113 -25.173 1.00 48.19 ? 401 LYS B O   1 
ATOM   6105 C  CB  . LYS B 1 392 ? -0.956  -36.322 -23.148 1.00 56.05 ? 401 LYS B CB  1 
ATOM   6106 C  CG  . LYS B 1 392 ? -0.033  -37.293 -23.826 1.00 58.63 ? 401 LYS B CG  1 
ATOM   6107 C  CD  . LYS B 1 392 ? 0.004   -38.621 -23.093 1.00 61.93 ? 401 LYS B CD  1 
ATOM   6108 C  CE  . LYS B 1 392 ? 1.061   -39.549 -23.679 1.00 67.56 ? 401 LYS B CE  1 
ATOM   6109 N  NZ  . LYS B 1 392 ? 1.105   -40.860 -22.969 0.00 69.57 ? 401 LYS B NZ  1 
ATOM   6110 N  N   . GLU B 1 393 ? -1.098  -35.318 -26.244 1.00 56.97 ? 402 GLU B N   1 
ATOM   6111 C  CA  . GLU B 1 393 ? -1.693  -35.547 -27.573 1.00 56.70 ? 402 GLU B CA  1 
ATOM   6112 C  C   . GLU B 1 393 ? -2.649  -36.734 -27.574 1.00 56.28 ? 402 GLU B C   1 
ATOM   6113 O  O   . GLU B 1 393 ? -2.276  -37.834 -27.151 1.00 59.51 ? 402 GLU B O   1 
ATOM   6114 C  CB  . GLU B 1 393 ? -0.616  -35.801 -28.635 1.00 59.71 ? 402 GLU B CB  1 
ATOM   6115 C  CG  . GLU B 1 393 ? -0.012  -34.564 -29.232 1.00 57.44 ? 402 GLU B CG  1 
ATOM   6116 C  CD  . GLU B 1 393 ? 1.029   -34.900 -30.270 1.00 63.76 ? 402 GLU B CD  1 
ATOM   6117 O  OE1 . GLU B 1 393 ? 0.708   -35.669 -31.202 1.00 53.45 ? 402 GLU B OE1 1 
ATOM   6118 O  OE2 . GLU B 1 393 ? 2.172   -34.407 -30.151 1.00 65.56 ? 402 GLU B OE2 1 
ATOM   6119 N  N   . GLY B 1 394 ? -3.862  -36.507 -28.075 1.00 54.20 ? 403 GLY B N   1 
ATOM   6120 C  CA  . GLY B 1 394 ? -4.915  -37.524 -28.078 1.00 54.42 ? 403 GLY B CA  1 
ATOM   6121 C  C   . GLY B 1 394 ? -4.708  -38.656 -29.076 1.00 57.63 ? 403 GLY B C   1 
ATOM   6122 O  O   . GLY B 1 394 ? -3.631  -38.819 -29.656 1.00 58.82 ? 403 GLY B O   1 
HETATM 6123 C  CHA . HEM C 2 .   ? -22.388 3.774   -20.725 1.00 23.81 ? 501 HEM A CHA 1 
HETATM 6124 C  CHB . HEM C 2 .   ? -21.113 8.256   -22.093 1.00 23.78 ? 501 HEM A CHB 1 
HETATM 6125 C  CHC . HEM C 2 .   ? -19.491 9.098   -17.608 1.00 30.62 ? 501 HEM A CHC 1 
HETATM 6126 C  CHD . HEM C 2 .   ? -21.930 5.183   -16.102 1.00 28.40 ? 501 HEM A CHD 1 
HETATM 6127 C  C1A . HEM C 2 .   ? -22.120 4.866   -21.506 1.00 26.17 ? 501 HEM A C1A 1 
HETATM 6128 C  C2A . HEM C 2 .   ? -22.235 4.935   -22.946 1.00 26.83 ? 501 HEM A C2A 1 
HETATM 6129 C  C3A . HEM C 2 .   ? -21.887 6.170   -23.321 1.00 23.28 ? 501 HEM A C3A 1 
HETATM 6130 C  C4A . HEM C 2 .   ? -21.533 6.938   -22.146 1.00 24.97 ? 501 HEM A C4A 1 
HETATM 6131 C  CMA . HEM C 2 .   ? -21.894 6.674   -24.776 1.00 24.59 ? 501 HEM A CMA 1 
HETATM 6132 C  CAA . HEM C 2 .   ? -22.686 3.788   -23.895 1.00 29.18 ? 501 HEM A CAA 1 
HETATM 6133 C  CBA . HEM C 2 .   ? -21.470 3.099   -24.522 1.00 33.65 ? 501 HEM A CBA 1 
HETATM 6134 C  CGA . HEM C 2 .   ? -20.633 2.346   -23.505 1.00 33.33 ? 501 HEM A CGA 1 
HETATM 6135 O  O1A . HEM C 2 .   ? -19.405 2.582   -23.430 1.00 33.64 ? 501 HEM A O1A 1 
HETATM 6136 O  O2A . HEM C 2 .   ? -21.185 1.506   -22.761 1.00 33.04 ? 501 HEM A O2A 1 
HETATM 6137 C  C1B . HEM C 2 .   ? -20.543 8.901   -21.004 1.00 26.58 ? 501 HEM A C1B 1 
HETATM 6138 C  C2B . HEM C 2 .   ? -19.969 10.241  -20.979 1.00 24.57 ? 501 HEM A C2B 1 
HETATM 6139 C  C3B . HEM C 2 .   ? -19.510 10.490  -19.735 1.00 23.90 ? 501 HEM A C3B 1 
HETATM 6140 C  C4B . HEM C 2 .   ? -19.801 9.307   -18.933 1.00 26.71 ? 501 HEM A C4B 1 
HETATM 6141 C  CMB . HEM C 2 .   ? -19.955 11.142  -22.226 1.00 29.67 ? 501 HEM A CMB 1 
HETATM 6142 C  CAB . HEM C 2 .   ? -18.825 11.759  -19.157 1.00 23.77 ? 501 HEM A CAB 1 
HETATM 6143 C  CBB . HEM C 2 .   ? -18.065 12.587  -19.889 1.00 29.29 ? 501 HEM A CBB 1 
HETATM 6144 C  C1C . HEM C 2 .   ? -20.056 8.145   -16.792 1.00 28.11 ? 501 HEM A C1C 1 
HETATM 6145 C  C2C . HEM C 2 .   ? -20.040 8.133   -15.352 1.00 28.60 ? 501 HEM A C2C 1 
HETATM 6146 C  C3C . HEM C 2 .   ? -20.720 7.062   -14.945 1.00 29.38 ? 501 HEM A C3C 1 
HETATM 6147 C  C4C . HEM C 2 .   ? -21.188 6.345   -16.108 1.00 30.28 ? 501 HEM A C4C 1 
HETATM 6148 C  CMC . HEM C 2 .   ? -19.343 9.175   -14.445 1.00 32.69 ? 501 HEM A CMC 1 
HETATM 6149 C  CAC . HEM C 2 .   ? -20.967 6.634   -13.489 1.00 28.32 ? 501 HEM A CAC 1 
HETATM 6150 C  CBC . HEM C 2 .   ? -22.239 6.461   -13.100 1.00 35.18 ? 501 HEM A CBC 1 
HETATM 6151 C  C1D . HEM C 2 .   ? -22.261 4.416   -17.186 1.00 23.99 ? 501 HEM A C1D 1 
HETATM 6152 C  C2D . HEM C 2 .   ? -22.858 3.106   -17.110 1.00 27.20 ? 501 HEM A C2D 1 
HETATM 6153 C  C3D . HEM C 2 .   ? -22.988 2.652   -18.561 1.00 27.83 ? 501 HEM A C3D 1 
HETATM 6154 C  C4D . HEM C 2 .   ? -22.464 3.746   -19.354 1.00 23.61 ? 501 HEM A C4D 1 
HETATM 6155 C  CMD . HEM C 2 .   ? -23.250 2.347   -15.833 1.00 28.37 ? 501 HEM A CMD 1 
HETATM 6156 C  CAD . HEM C 2 .   ? -23.589 1.330   -19.064 1.00 26.17 ? 501 HEM A CAD 1 
HETATM 6157 C  CBD . HEM C 2 .   ? -25.076 1.539   -19.346 1.00 24.54 ? 501 HEM A CBD 1 
HETATM 6158 C  CGD . HEM C 2 .   ? -25.903 1.648   -18.087 1.00 27.91 ? 501 HEM A CGD 1 
HETATM 6159 O  O1D . HEM C 2 .   ? -26.751 2.574   -17.980 1.00 25.94 ? 501 HEM A O1D 1 
HETATM 6160 O  O2D . HEM C 2 .   ? -25.732 0.806   -17.177 1.00 26.47 ? 501 HEM A O2D 1 
HETATM 6161 N  NA  . HEM C 2 .   ? -21.698 6.104   -21.049 1.00 21.68 ? 501 HEM A NA  1 
HETATM 6162 N  NB  . HEM C 2 .   ? -20.418 8.380   -19.737 1.00 27.00 ? 501 HEM A NB  1 
HETATM 6163 N  NC  . HEM C 2 .   ? -20.762 7.037   -17.221 1.00 28.74 ? 501 HEM A NC  1 
HETATM 6164 N  ND  . HEM C 2 .   ? -22.038 4.741   -18.504 1.00 26.35 ? 501 HEM A ND  1 
HETATM 6165 FE FE  . HEM C 2 .   ? -21.181 6.595   -19.129 1.00 24.61 ? 501 HEM A FE  1 
HETATM 6166 C  C1  . W2Z D 3 .   ? -18.056 3.313   -29.025 1.00 50.18 ? 502 W2Z A C1  1 
HETATM 6167 C  C2  . W2Z D 3 .   ? -16.923 4.137   -29.648 1.00 45.66 ? 502 W2Z A C2  1 
HETATM 6168 C  C7  . W2Z D 3 .   ? -18.268 5.819   -26.740 1.00 35.60 ? 502 W2Z A C7  1 
HETATM 6169 C  C8  . W2Z D 3 .   ? -18.148 6.885   -25.656 1.00 35.79 ? 502 W2Z A C8  1 
HETATM 6170 C  C11 . W2Z D 3 .   ? -16.408 7.019   -22.326 1.00 28.02 ? 502 W2Z A C11 1 
HETATM 6171 C  C12 . W2Z D 3 .   ? -16.224 5.514   -22.657 1.00 23.19 ? 502 W2Z A C12 1 
HETATM 6172 C  C17 . W2Z D 3 .   ? -16.559 4.588   -21.475 1.00 19.64 ? 502 W2Z A C17 1 
HETATM 6173 C  C19 . W2Z D 3 .   ? -15.384 4.445   -20.545 1.00 23.51 ? 502 W2Z A C19 1 
HETATM 6174 C  C21 . W2Z D 3 .   ? -13.202 4.022   -19.707 1.00 20.61 ? 502 W2Z A C21 1 
HETATM 6175 C  C23 . W2Z D 3 .   ? -14.904 4.809   -18.199 1.00 21.92 ? 502 W2Z A C23 1 
HETATM 6176 C  C24 . W2Z D 3 .   ? -15.805 4.826   -19.254 1.00 21.62 ? 502 W2Z A C24 1 
HETATM 6177 C  C27 . W2Z D 3 .   ? -18.911 5.408   -20.632 1.00 20.14 ? 502 W2Z A C27 1 
HETATM 6178 C  C30 . W2Z D 3 .   ? -15.673 6.542   -25.492 1.00 35.38 ? 502 W2Z A C30 1 
HETATM 6179 C  C31 . W2Z D 3 .   ? -15.736 5.706   -26.784 1.00 32.92 ? 502 W2Z A C31 1 
HETATM 6180 S  S3  . W2Z D 3 .   ? -17.045 5.889   -29.175 1.00 42.92 ? 502 W2Z A S3  1 
HETATM 6181 O  O4  . W2Z D 3 .   ? -15.844 6.539   -29.560 1.00 39.20 ? 502 W2Z A O4  1 
HETATM 6182 O  O5  . W2Z D 3 .   ? -18.295 6.434   -29.545 1.00 42.73 ? 502 W2Z A O5  1 
HETATM 6183 N  N6  . W2Z D 3 .   ? -17.018 5.825   -27.518 1.00 37.08 ? 502 W2Z A N6  1 
HETATM 6184 C  C9  . W2Z D 3 .   ? -16.988 6.556   -24.706 1.00 32.07 ? 502 W2Z A C9  1 
HETATM 6185 C  C10 . W2Z D 3 .   ? -16.986 7.645   -23.617 1.00 33.69 ? 502 W2Z A C10 1 
HETATM 6186 C  C14 . W2Z D 3 .   ? -17.113 5.255   -23.910 1.00 28.01 ? 502 W2Z A C14 1 
HETATM 6187 O  O16 . W2Z D 3 .   ? -18.483 5.022   -23.610 1.00 26.19 ? 502 W2Z A O16 1 
HETATM 6188 C  C20 . W2Z D 3 .   ? -14.084 4.051   -20.762 1.00 22.00 ? 502 W2Z A C20 1 
HETATM 6189 C  C22 . W2Z D 3 .   ? -13.612 4.390   -18.443 1.00 19.50 ? 502 W2Z A C22 1 
HETATM 6190 C  C25 . W2Z D 3 .   ? -17.212 5.197   -19.321 1.00 20.07 ? 502 W2Z A C25 1 
HETATM 6191 N  N26 . W2Z D 3 .   ? -17.637 5.063   -20.615 1.00 19.58 ? 502 W2Z A N26 1 
HETATM 6192 N  N28 . W2Z D 3 .   ? -19.296 5.752   -19.437 1.00 19.91 ? 502 W2Z A N28 1 
HETATM 6193 C  C29 . W2Z D 3 .   ? -18.267 5.647   -18.607 1.00 21.82 ? 502 W2Z A C29 1 
HETATM 6194 C  CHA . HEM E 2 .   ? -24.141 -26.791 -33.119 1.00 21.88 ? 501 HEM B CHA 1 
HETATM 6195 C  CHB . HEM E 2 .   ? -25.830 -29.301 -36.920 1.00 22.67 ? 501 HEM B CHB 1 
HETATM 6196 C  CHC . HEM E 2 .   ? -27.480 -32.578 -33.775 1.00 26.48 ? 501 HEM B CHC 1 
HETATM 6197 C  CHD . HEM E 2 .   ? -24.629 -30.747 -30.369 1.00 23.01 ? 501 HEM B CHD 1 
HETATM 6198 C  C1A . HEM E 2 .   ? -24.506 -27.137 -34.403 1.00 22.11 ? 501 HEM B C1A 1 
HETATM 6199 C  C2A . HEM E 2 .   ? -24.393 -26.297 -35.579 1.00 23.59 ? 501 HEM B C2A 1 
HETATM 6200 C  C3A . HEM E 2 .   ? -24.849 -26.981 -36.632 1.00 22.82 ? 501 HEM B C3A 1 
HETATM 6201 C  C4A . HEM E 2 .   ? -25.276 -28.286 -36.173 1.00 19.73 ? 501 HEM B C4A 1 
HETATM 6202 C  CMA . HEM E 2 .   ? -24.878 -26.473 -38.086 1.00 26.95 ? 501 HEM B CMA 1 
HETATM 6203 C  CAA . HEM E 2 .   ? -23.825 -24.865 -35.591 1.00 26.10 ? 501 HEM B CAA 1 
HETATM 6204 C  CBA . HEM E 2 .   ? -24.959 -23.838 -35.567 1.00 26.45 ? 501 HEM B CBA 1 
HETATM 6205 C  CGA . HEM E 2 .   ? -25.712 -23.823 -34.266 1.00 23.50 ? 501 HEM B CGA 1 
HETATM 6206 O  O1A . HEM E 2 .   ? -26.970 -23.929 -34.305 1.00 34.73 ? 501 HEM B O1A 1 
HETATM 6207 O  O2A . HEM E 2 .   ? -25.080 -23.702 -33.193 1.00 30.27 ? 501 HEM B O2A 1 
HETATM 6208 C  C1B . HEM E 2 .   ? -26.470 -30.412 -36.412 1.00 22.51 ? 501 HEM B C1B 1 
HETATM 6209 C  C2B . HEM E 2 .   ? -27.196 -31.421 -37.160 1.00 24.25 ? 501 HEM B C2B 1 
HETATM 6210 C  C3B . HEM E 2 .   ? -27.651 -32.342 -36.280 1.00 23.29 ? 501 HEM B C3B 1 
HETATM 6211 C  C4B . HEM E 2 .   ? -27.203 -31.934 -34.958 1.00 21.18 ? 501 HEM B C4B 1 
HETATM 6212 C  CMB . HEM E 2 .   ? -27.365 -31.351 -38.694 1.00 26.53 ? 501 HEM B CMB 1 
HETATM 6213 C  CAB . HEM E 2 .   ? -28.481 -33.636 -36.490 1.00 21.39 ? 501 HEM B CAB 1 
HETATM 6214 C  CBB . HEM E 2 .   ? -29.315 -33.823 -37.517 1.00 26.08 ? 501 HEM B CBB 1 
HETATM 6215 C  C1C . HEM E 2 .   ? -26.834 -32.409 -32.586 1.00 20.72 ? 501 HEM B C1C 1 
HETATM 6216 C  C2C . HEM E 2 .   ? -26.894 -33.294 -31.439 1.00 23.22 ? 501 HEM B C2C 1 
HETATM 6217 C  C3C . HEM E 2 .   ? -26.094 -32.783 -30.503 1.00 25.45 ? 501 HEM B C3C 1 
HETATM 6218 C  C4C . HEM E 2 .   ? -25.513 -31.566 -31.020 1.00 22.43 ? 501 HEM B C4C 1 
HETATM 6219 C  CMC . HEM E 2 .   ? -27.742 -34.577 -31.331 1.00 23.68 ? 501 HEM B CMC 1 
HETATM 6220 C  CAC . HEM E 2 .   ? -25.792 -33.362 -29.110 1.00 29.00 ? 501 HEM B CAC 1 
HETATM 6221 C  CBC . HEM E 2 .   ? -24.503 -33.628 -28.860 1.00 26.11 ? 501 HEM B CBC 1 
HETATM 6222 C  C1D . HEM E 2 .   ? -24.254 -29.498 -30.761 1.00 25.03 ? 501 HEM B C1D 1 
HETATM 6223 C  C2D . HEM E 2 .   ? -23.530 -28.571 -29.935 1.00 25.62 ? 501 HEM B C2D 1 
HETATM 6224 C  C3D . HEM E 2 .   ? -23.379 -27.320 -30.787 1.00 22.99 ? 501 HEM B C3D 1 
HETATM 6225 C  C4D . HEM E 2 .   ? -24.033 -27.628 -32.038 1.00 25.02 ? 501 HEM B C4D 1 
HETATM 6226 C  CMD . HEM E 2 .   ? -23.036 -28.832 -28.501 1.00 25.79 ? 501 HEM B CMD 1 
HETATM 6227 C  CAD . HEM E 2 .   ? -22.663 -26.021 -30.381 1.00 24.42 ? 501 HEM B CAD 1 
HETATM 6228 C  CBD . HEM E 2 .   ? -21.194 -26.111 -30.785 1.00 25.72 ? 501 HEM B CBD 1 
HETATM 6229 C  CGD . HEM E 2 .   ? -20.395 -27.033 -29.901 1.00 28.04 ? 501 HEM B CGD 1 
HETATM 6230 O  O1D . HEM E 2 .   ? -19.578 -27.829 -30.445 1.00 24.34 ? 501 HEM B O1D 1 
HETATM 6231 O  O2D . HEM E 2 .   ? -20.550 -26.955 -28.657 1.00 25.66 ? 501 HEM B O2D 1 
HETATM 6232 N  NA  . HEM E 2 .   ? -25.046 -28.340 -34.817 1.00 19.86 ? 501 HEM B NA  1 
HETATM 6233 N  NB  . HEM E 2 .   ? -26.484 -30.770 -35.078 1.00 22.73 ? 501 HEM B NB  1 
HETATM 6234 N  NC  . HEM E 2 .   ? -25.988 -31.372 -32.296 1.00 21.31 ? 501 HEM B NC  1 
HETATM 6235 N  ND  . HEM E 2 .   ? -24.544 -28.914 -31.976 1.00 24.82 ? 501 HEM B ND  1 
HETATM 6236 FE FE  . HEM E 2 .   ? -25.542 -29.849 -33.531 1.00 24.61 ? 501 HEM B FE  1 
HETATM 6237 C  C1  . W2Z F 3 .   ? -28.405 -20.904 -39.415 1.00 49.78 ? 502 W2Z B C1  1 
HETATM 6238 C  C2  . W2Z F 3 .   ? -29.726 -21.261 -40.100 1.00 45.56 ? 502 W2Z B C2  1 
HETATM 6239 C  C7  . W2Z F 3 .   ? -28.413 -24.409 -38.835 1.00 38.94 ? 502 W2Z B C7  1 
HETATM 6240 C  C8  . W2Z F 3 .   ? -28.518 -25.912 -38.578 1.00 37.51 ? 502 W2Z B C8  1 
HETATM 6241 C  C11 . W2Z F 3 .   ? -30.381 -27.924 -35.994 1.00 30.88 ? 502 W2Z B C11 1 
HETATM 6242 C  C12 . W2Z F 3 .   ? -30.425 -26.517 -35.327 1.00 30.36 ? 502 W2Z B C12 1 
HETATM 6243 C  C17 . W2Z F 3 .   ? -30.012 -26.526 -33.841 1.00 25.48 ? 502 W2Z B C17 1 
HETATM 6244 C  C19 . W2Z F 3 .   ? -31.171 -26.915 -32.960 1.00 27.47 ? 502 W2Z B C19 1 
HETATM 6245 C  C21 . W2Z F 3 .   ? -33.310 -26.966 -31.911 1.00 25.49 ? 502 W2Z B C21 1 
HETATM 6246 C  C23 . W2Z F 3 .   ? -31.655 -28.584 -31.260 1.00 28.23 ? 502 W2Z B C23 1 
HETATM 6247 C  C24 . W2Z F 3 .   ? -30.769 -28.012 -32.180 1.00 25.00 ? 502 W2Z B C24 1 
HETATM 6248 C  C27 . W2Z F 3 .   ? -27.724 -27.815 -33.822 1.00 20.70 ? 502 W2Z B C27 1 
HETATM 6249 C  C30 . W2Z F 3 .   ? -30.983 -25.770 -38.273 1.00 35.48 ? 502 W2Z B C30 1 
HETATM 6250 C  C31 . W2Z F 3 .   ? -30.956 -24.292 -38.746 1.00 33.31 ? 502 W2Z B C31 1 
HETATM 6251 S  S3  . W2Z F 3 .   ? -29.675 -22.945 -40.774 1.00 45.79 ? 502 W2Z B S3  1 
HETATM 6252 O  O4  . W2Z F 3 .   ? -30.899 -23.197 -41.432 1.00 38.51 ? 502 W2Z B O4  1 
HETATM 6253 O  O5  . W2Z F 3 .   ? -28.443 -23.189 -41.438 1.00 43.56 ? 502 W2Z B O5  1 
HETATM 6254 N  N6  . W2Z F 3 .   ? -29.683 -23.925 -39.422 1.00 40.23 ? 502 W2Z B N6  1 
HETATM 6255 C  C9  . W2Z F 3 .   ? -29.666 -26.208 -37.614 1.00 35.91 ? 502 W2Z B C9  1 
HETATM 6256 C  C10 . W2Z F 3 .   ? -29.664 -27.723 -37.354 1.00 36.59 ? 502 W2Z B C10 1 
HETATM 6257 C  C14 . W2Z F 3 .   ? -29.516 -25.608 -36.206 1.00 28.65 ? 502 W2Z B C14 1 
HETATM 6258 O  O16 . W2Z F 3 .   ? -28.151 -25.606 -35.803 1.00 27.64 ? 502 W2Z B O16 1 
HETATM 6259 C  C20 . W2Z F 3 .   ? -32.432 -26.397 -32.815 1.00 26.36 ? 502 W2Z B C20 1 
HETATM 6260 C  C22 . W2Z F 3 .   ? -32.926 -28.054 -31.136 1.00 26.50 ? 502 W2Z B C22 1 
HETATM 6261 C  C25 . W2Z F 3 .   ? -29.395 -28.349 -32.545 1.00 24.92 ? 502 W2Z B C25 1 
HETATM 6262 N  N26 . W2Z F 3 .   ? -28.968 -27.479 -33.515 1.00 24.38 ? 502 W2Z B N26 1 
HETATM 6263 N  N28 . W2Z F 3 .   ? -27.363 -28.850 -33.118 1.00 25.13 ? 502 W2Z B N28 1 
HETATM 6264 C  C29 . W2Z F 3 .   ? -28.369 -29.219 -32.329 1.00 23.49 ? 502 W2Z B C29 1 
HETATM 6265 O  O   . HOH G 4 .   ? 8.376   -5.908  -23.244 1.00 38.82 ? 601 HOH A O   1 
HETATM 6266 O  O   . HOH G 4 .   ? -30.324 -10.423 -15.853 1.00 43.49 ? 602 HOH A O   1 
HETATM 6267 O  O   . HOH G 4 .   ? -26.440 -3.526  -15.462 1.00 24.80 ? 603 HOH A O   1 
HETATM 6268 O  O   . HOH G 4 .   ? -36.599 -6.297  -16.398 1.00 49.30 ? 604 HOH A O   1 
HETATM 6269 O  O   . HOH G 4 .   ? -26.196 -15.954 -13.556 1.00 40.46 ? 605 HOH A O   1 
HETATM 6270 O  O   . HOH G 4 .   ? -14.223 -9.210  -0.207  1.00 49.10 ? 606 HOH A O   1 
HETATM 6271 O  O   . HOH G 4 .   ? 7.361   7.024   -33.749 1.00 38.24 ? 607 HOH A O   1 
HETATM 6272 O  O   . HOH G 4 .   ? -37.823 -4.004  -16.386 1.00 42.68 ? 608 HOH A O   1 
HETATM 6273 O  O   . HOH G 4 .   ? -16.452 -1.886  -10.691 1.00 21.65 ? 609 HOH A O   1 
HETATM 6274 O  O   . HOH G 4 .   ? -16.055 -8.895  -26.306 1.00 30.86 ? 610 HOH A O   1 
HETATM 6275 O  O   . HOH G 4 .   ? -12.672 4.995   -32.890 1.00 44.38 ? 611 HOH A O   1 
HETATM 6276 O  O   . HOH G 4 .   ? -32.597 8.202   -28.991 1.00 34.17 ? 612 HOH A O   1 
HETATM 6277 O  O   . HOH G 4 .   ? -10.382 5.551   -31.975 1.00 40.58 ? 613 HOH A O   1 
HETATM 6278 O  O   . HOH G 4 .   ? -8.868  20.374  -21.860 1.00 39.97 ? 614 HOH A O   1 
HETATM 6279 O  O   . HOH G 4 .   ? -36.559 -10.762 -25.001 1.00 41.47 ? 615 HOH A O   1 
HETATM 6280 O  O   . HOH G 4 .   ? -43.707 -7.674  4.568   1.00 44.23 ? 616 HOH A O   1 
HETATM 6281 O  O   . HOH G 4 .   ? -3.749  -11.481 -32.763 1.00 34.30 ? 617 HOH A O   1 
HETATM 6282 O  O   . HOH G 4 .   ? -30.666 11.595  -0.969  1.00 55.44 ? 618 HOH A O   1 
HETATM 6283 O  O   . HOH G 4 .   ? -20.299 -12.608 -19.729 1.00 33.58 ? 619 HOH A O   1 
HETATM 6284 O  O   . HOH G 4 .   ? 12.282  2.236   -27.060 1.00 41.47 ? 620 HOH A O   1 
HETATM 6285 O  O   . HOH G 4 .   ? 0.749   9.360   -19.071 1.00 36.61 ? 621 HOH A O   1 
HETATM 6286 O  O   . HOH G 4 .   ? -4.824  -3.094  -19.686 1.00 23.57 ? 622 HOH A O   1 
HETATM 6287 O  O   . HOH G 4 .   ? 7.683   3.498   -36.599 1.00 36.94 ? 623 HOH A O   1 
HETATM 6288 O  O   . HOH G 4 .   ? -31.615 2.634   6.309   1.00 46.27 ? 624 HOH A O   1 
HETATM 6289 O  O   . HOH G 4 .   ? -30.339 14.518  -22.910 1.00 27.86 ? 625 HOH A O   1 
HETATM 6290 O  O   . HOH G 4 .   ? -10.467 -3.532  -8.865  1.00 32.18 ? 626 HOH A O   1 
HETATM 6291 O  O   . HOH G 4 .   ? -34.733 7.509   -4.762  1.00 33.19 ? 627 HOH A O   1 
HETATM 6292 O  O   . HOH G 4 .   ? 6.459   -13.566 -19.710 1.00 48.51 ? 628 HOH A O   1 
HETATM 6293 O  O   . HOH G 4 .   ? -26.510 -3.650  6.919   1.00 47.95 ? 629 HOH A O   1 
HETATM 6294 O  O   . HOH G 4 .   ? -14.961 -4.409  -10.937 1.00 32.46 ? 630 HOH A O   1 
HETATM 6295 O  O   . HOH G 4 .   ? -8.703  18.878  -12.483 1.00 45.95 ? 631 HOH A O   1 
HETATM 6296 O  O   . HOH G 4 .   ? -13.664 -3.997  -34.746 1.00 37.76 ? 632 HOH A O   1 
HETATM 6297 O  O   . HOH G 4 .   ? -11.083 21.879  -25.541 1.00 46.26 ? 633 HOH A O   1 
HETATM 6298 O  O   . HOH G 4 .   ? -11.104 13.595  -32.853 1.00 36.08 ? 634 HOH A O   1 
HETATM 6299 O  O   . HOH G 4 .   ? -31.766 12.606  -12.557 1.00 38.81 ? 635 HOH A O   1 
HETATM 6300 O  O   . HOH G 4 .   ? -42.690 -3.324  11.363  1.00 31.24 ? 636 HOH A O   1 
HETATM 6301 O  O   . HOH G 4 .   ? -30.484 2.667   -32.380 1.00 46.02 ? 637 HOH A O   1 
HETATM 6302 O  O   . HOH G 4 .   ? -17.360 -1.370  -24.405 1.00 37.07 ? 638 HOH A O   1 
HETATM 6303 O  O   . HOH G 4 .   ? -25.859 19.190  -12.793 1.00 46.35 ? 639 HOH A O   1 
HETATM 6304 O  O   . HOH G 4 .   ? -38.530 -6.906  13.686  1.00 52.04 ? 640 HOH A O   1 
HETATM 6305 O  O   . HOH G 4 .   ? -5.322  -2.779  -13.638 1.00 28.30 ? 641 HOH A O   1 
HETATM 6306 O  O   . HOH G 4 .   ? -14.502 2.984   -24.905 1.00 35.18 ? 642 HOH A O   1 
HETATM 6307 O  O   . HOH G 4 .   ? -12.203 9.299   2.282   1.00 54.02 ? 643 HOH A O   1 
HETATM 6308 O  O   . HOH G 4 .   ? -11.839 -11.097 -36.236 1.00 52.38 ? 644 HOH A O   1 
HETATM 6309 O  O   . HOH G 4 .   ? -36.833 -9.739  -11.594 1.00 46.37 ? 645 HOH A O   1 
HETATM 6310 O  O   . HOH G 4 .   ? 3.058   -2.705  -35.601 1.00 45.93 ? 646 HOH A O   1 
HETATM 6311 O  O   . HOH G 4 .   ? -27.887 6.739   -19.160 1.00 23.06 ? 647 HOH A O   1 
HETATM 6312 O  O   . HOH G 4 .   ? 0.469   3.246   -3.247  1.00 35.89 ? 648 HOH A O   1 
HETATM 6313 O  O   . HOH G 4 .   ? -40.511 2.804   3.112   1.00 36.23 ? 649 HOH A O   1 
HETATM 6314 O  O   . HOH G 4 .   ? -2.337  5.008   -5.349  1.00 36.54 ? 650 HOH A O   1 
HETATM 6315 O  O   . HOH G 4 .   ? -40.633 5.093   -3.214  1.00 36.11 ? 651 HOH A O   1 
HETATM 6316 O  O   . HOH G 4 .   ? -42.798 4.360   -6.407  1.00 56.58 ? 652 HOH A O   1 
HETATM 6317 O  O   . HOH G 4 .   ? -28.171 0.834   -29.757 1.00 36.02 ? 653 HOH A O   1 
HETATM 6318 O  O   . HOH G 4 .   ? -18.999 -17.388 -5.730  1.00 41.38 ? 654 HOH A O   1 
HETATM 6319 O  O   . HOH G 4 .   ? -24.446 14.511  -32.776 1.00 43.10 ? 655 HOH A O   1 
HETATM 6320 O  O   . HOH G 4 .   ? -6.494  7.636   -34.302 1.00 29.04 ? 656 HOH A O   1 
HETATM 6321 O  O   . HOH G 4 .   ? -14.723 15.322  -4.612  1.00 40.28 ? 657 HOH A O   1 
HETATM 6322 O  O   . HOH G 4 .   ? -5.621  -5.950  -37.268 1.00 43.72 ? 658 HOH A O   1 
HETATM 6323 O  O   . HOH G 4 .   ? -9.565  17.191  -16.110 1.00 33.86 ? 659 HOH A O   1 
HETATM 6324 O  O   . HOH G 4 .   ? -18.129 5.348   -12.696 1.00 31.10 ? 660 HOH A O   1 
HETATM 6325 O  O   . HOH G 4 .   ? 4.686   18.217  -25.649 1.00 55.81 ? 661 HOH A O   1 
HETATM 6326 O  O   . HOH G 4 .   ? -1.799  -1.372  -8.327  1.00 32.25 ? 662 HOH A O   1 
HETATM 6327 O  O   . HOH G 4 .   ? -49.343 -10.468 -2.402  1.00 52.35 ? 663 HOH A O   1 
HETATM 6328 O  O   . HOH G 4 .   ? -1.414  15.000  -19.293 1.00 48.37 ? 664 HOH A O   1 
HETATM 6329 O  O   . HOH G 4 .   ? 7.317   9.801   -36.076 1.00 43.94 ? 665 HOH A O   1 
HETATM 6330 O  O   . HOH G 4 .   ? -36.961 -11.511 -18.291 1.00 44.08 ? 666 HOH A O   1 
HETATM 6331 O  O   . HOH G 4 .   ? -17.073 9.081   -3.532  1.00 38.84 ? 667 HOH A O   1 
HETATM 6332 O  O   . HOH G 4 .   ? 9.847   0.675   -13.222 1.00 47.71 ? 668 HOH A O   1 
HETATM 6333 O  O   . HOH G 4 .   ? -36.640 -7.393  11.245  1.00 45.37 ? 669 HOH A O   1 
HETATM 6334 O  O   . HOH G 4 .   ? -22.815 6.997   -0.979  1.00 50.79 ? 670 HOH A O   1 
HETATM 6335 O  O   . HOH G 4 .   ? -29.541 8.459   -7.813  1.00 36.83 ? 671 HOH A O   1 
HETATM 6336 O  O   . HOH G 4 .   ? -17.439 -7.856  -34.095 1.00 48.12 ? 672 HOH A O   1 
HETATM 6337 O  O   . HOH G 4 .   ? -19.979 -6.557  -26.743 1.00 42.04 ? 673 HOH A O   1 
HETATM 6338 O  O   . HOH G 4 .   ? -14.585 -3.730  -13.703 1.00 31.53 ? 674 HOH A O   1 
HETATM 6339 O  O   . HOH G 4 .   ? -17.313 5.913   -15.449 1.00 28.69 ? 675 HOH A O   1 
HETATM 6340 O  O   . HOH G 4 .   ? -5.396  13.699  -30.043 1.00 37.63 ? 676 HOH A O   1 
HETATM 6341 O  O   . HOH G 4 .   ? -26.546 -12.689 -16.267 1.00 35.41 ? 677 HOH A O   1 
HETATM 6342 O  O   . HOH G 4 .   ? -18.516 -16.538 -12.243 1.00 36.70 ? 678 HOH A O   1 
HETATM 6343 O  O   . HOH G 4 .   ? -33.764 -7.171  -20.485 1.00 39.88 ? 679 HOH A O   1 
HETATM 6344 O  O   . HOH G 4 .   ? -35.692 10.119  -14.398 1.00 48.01 ? 680 HOH A O   1 
HETATM 6345 O  O   . HOH G 4 .   ? -25.533 17.723  -19.582 1.00 38.50 ? 681 HOH A O   1 
HETATM 6346 O  O   . HOH G 4 .   ? -28.436 -1.426  -27.958 1.00 51.51 ? 682 HOH A O   1 
HETATM 6347 O  O   . HOH G 4 .   ? -35.380 8.177   -0.823  1.00 48.18 ? 683 HOH A O   1 
HETATM 6348 O  O   . HOH G 4 .   ? -19.344 -1.637  -37.020 1.00 52.75 ? 684 HOH A O   1 
HETATM 6349 O  O   . HOH G 4 .   ? -9.528  1.301   1.222   1.00 40.48 ? 685 HOH A O   1 
HETATM 6350 O  O   . HOH G 4 .   ? -11.229 -4.052  -4.271  1.00 36.41 ? 686 HOH A O   1 
HETATM 6351 O  O   . HOH G 4 .   ? -20.807 -12.480 -13.802 1.00 35.96 ? 687 HOH A O   1 
HETATM 6352 O  O   . HOH G 4 .   ? -32.619 -14.981 -8.699  1.00 60.56 ? 688 HOH A O   1 
HETATM 6353 O  O   . HOH G 4 .   ? -14.716 8.969   -2.114  1.00 39.31 ? 689 HOH A O   1 
HETATM 6354 O  O   . HOH G 4 .   ? 12.129  2.748   -37.033 1.00 47.24 ? 690 HOH A O   1 
HETATM 6355 O  O   . HOH G 4 .   ? -22.272 -1.236  -14.906 1.00 25.81 ? 691 HOH A O   1 
HETATM 6356 O  O   . HOH G 4 .   ? -29.564 12.426  -5.598  1.00 50.26 ? 692 HOH A O   1 
HETATM 6357 O  O   . HOH G 4 .   ? -6.476  19.149  -10.784 1.00 53.65 ? 693 HOH A O   1 
HETATM 6358 O  O   . HOH G 4 .   ? -4.553  -12.940 -22.983 1.00 40.61 ? 694 HOH A O   1 
HETATM 6359 O  O   . HOH G 4 .   ? -32.578 -14.432 -21.207 1.00 23.73 ? 695 HOH A O   1 
HETATM 6360 O  O   . HOH G 4 .   ? -8.843  -5.272  -38.294 1.00 43.33 ? 696 HOH A O   1 
HETATM 6361 O  O   . HOH G 4 .   ? -28.726 4.109   -19.066 1.00 22.95 ? 697 HOH A O   1 
HETATM 6362 O  O   . HOH G 4 .   ? -12.447 17.839  -3.659  1.00 45.03 ? 698 HOH A O   1 
HETATM 6363 O  O   . HOH G 4 .   ? -7.127  17.501  -7.498  1.00 41.40 ? 699 HOH A O   1 
HETATM 6364 O  O   . HOH G 4 .   ? -23.013 -13.460 -2.482  1.00 56.39 ? 700 HOH A O   1 
HETATM 6365 O  O   . HOH G 4 .   ? -12.132 -12.346 -19.494 1.00 39.62 ? 701 HOH A O   1 
HETATM 6366 O  O   . HOH G 4 .   ? 13.147  -8.884  -26.865 1.00 45.87 ? 702 HOH A O   1 
HETATM 6367 O  O   . HOH G 4 .   ? -18.778 22.027  -18.186 1.00 36.46 ? 703 HOH A O   1 
HETATM 6368 O  O   . HOH G 4 .   ? 2.198   9.453   -31.880 1.00 33.76 ? 704 HOH A O   1 
HETATM 6369 O  O   . HOH G 4 .   ? -14.841 18.720  -7.396  1.00 44.23 ? 705 HOH A O   1 
HETATM 6370 O  O   . HOH G 4 .   ? 1.444   13.418  -37.717 1.00 49.17 ? 706 HOH A O   1 
HETATM 6371 O  O   . HOH G 4 .   ? -6.864  -12.672 -21.609 1.00 33.28 ? 707 HOH A O   1 
HETATM 6372 O  O   . HOH G 4 .   ? -8.207  2.067   -40.288 1.00 52.06 ? 708 HOH A O   1 
HETATM 6373 O  O   . HOH G 4 .   ? -10.404 20.758  -12.727 1.00 34.41 ? 709 HOH A O   1 
HETATM 6374 O  O   . HOH G 4 .   ? -21.742 20.900  -11.866 1.00 49.34 ? 710 HOH A O   1 
HETATM 6375 O  O   . HOH G 4 .   ? -1.954  0.818   -10.215 1.00 32.43 ? 711 HOH A O   1 
HETATM 6376 O  O   . HOH G 4 .   ? -4.150  15.308  -19.145 1.00 38.86 ? 712 HOH A O   1 
HETATM 6377 O  O   . HOH G 4 .   ? 3.149   -11.791 -13.064 1.00 50.19 ? 713 HOH A O   1 
HETATM 6378 O  O   . HOH G 4 .   ? -24.601 20.223  -36.789 1.00 43.65 ? 714 HOH A O   1 
HETATM 6379 O  O   . HOH G 4 .   ? -5.323  -1.138  -24.311 0.50 19.27 ? 715 HOH A O   1 
HETATM 6380 O  O   . HOH G 4 .   ? -10.713 1.603   -22.727 1.00 30.71 ? 716 HOH A O   1 
HETATM 6381 O  O   . HOH G 4 .   ? -21.482 20.652  -25.349 1.00 31.87 ? 717 HOH A O   1 
HETATM 6382 O  O   . HOH G 4 .   ? -13.227 -3.446  -16.032 1.00 21.83 ? 718 HOH A O   1 
HETATM 6383 O  O   . HOH G 4 .   ? -14.327 -15.034 -6.250  1.00 42.62 ? 719 HOH A O   1 
HETATM 6384 O  O   . HOH G 4 .   ? -24.689 -6.294  -28.235 1.00 42.82 ? 720 HOH A O   1 
HETATM 6385 O  O   . HOH G 4 .   ? -51.665 -5.407  2.444   1.00 38.13 ? 721 HOH A O   1 
HETATM 6386 O  O   . HOH G 4 .   ? -31.918 -14.613 0.613   1.00 54.88 ? 722 HOH A O   1 
HETATM 6387 O  O   . HOH G 4 .   ? -35.478 5.343   -21.319 1.00 27.55 ? 723 HOH A O   1 
HETATM 6388 O  O   . HOH G 4 .   ? -16.890 -0.028  -6.252  1.00 34.98 ? 724 HOH A O   1 
HETATM 6389 O  O   . HOH G 4 .   ? -9.605  -16.149 -29.592 1.00 45.20 ? 725 HOH A O   1 
HETATM 6390 O  O   . HOH G 4 .   ? -12.321 -2.423  -22.348 1.00 23.10 ? 726 HOH A O   1 
HETATM 6391 O  O   . HOH G 4 .   ? -19.485 21.591  -26.917 1.00 36.39 ? 727 HOH A O   1 
HETATM 6392 O  O   . HOH G 4 .   ? -35.992 -1.542  -22.161 1.00 49.98 ? 728 HOH A O   1 
HETATM 6393 O  O   . HOH G 4 .   ? -20.117 -17.159 -8.184  1.00 36.39 ? 729 HOH A O   1 
HETATM 6394 O  O   . HOH G 4 .   ? -44.104 1.784   -4.015  1.00 43.40 ? 730 HOH A O   1 
HETATM 6395 O  O   . HOH G 4 .   ? -16.489 20.736  -7.712  1.00 43.69 ? 731 HOH A O   1 
HETATM 6396 O  O   . HOH G 4 .   ? -18.131 2.160   1.925   1.00 53.95 ? 732 HOH A O   1 
HETATM 6397 O  O   . HOH G 4 .   ? 10.542  0.807   -35.854 1.00 47.36 ? 733 HOH A O   1 
HETATM 6398 O  O   . HOH G 4 .   ? -33.565 6.311   1.903   1.00 38.65 ? 734 HOH A O   1 
HETATM 6399 O  O   . HOH G 4 .   ? -24.644 -1.671  -16.329 1.00 28.68 ? 735 HOH A O   1 
HETATM 6400 O  O   . HOH G 4 .   ? -32.993 -8.506  -23.908 1.00 33.14 ? 736 HOH A O   1 
HETATM 6401 O  O   . HOH G 4 .   ? -9.235  6.985   -34.167 1.00 29.76 ? 737 HOH A O   1 
HETATM 6402 O  O   . HOH G 4 .   ? -40.051 2.778   -19.650 1.00 52.41 ? 738 HOH A O   1 
HETATM 6403 O  O   . HOH G 4 .   ? -16.673 22.524  -25.045 1.00 51.20 ? 739 HOH A O   1 
HETATM 6404 O  O   . HOH G 4 .   ? -30.779 -1.188  -27.043 1.00 52.73 ? 740 HOH A O   1 
HETATM 6405 O  O   . HOH G 4 .   ? -29.297 -7.213  -14.405 1.00 36.21 ? 741 HOH A O   1 
HETATM 6406 O  O   . HOH G 4 .   ? -0.494  2.928   -39.132 1.00 41.87 ? 742 HOH A O   1 
HETATM 6407 O  O   . HOH G 4 .   ? -30.837 -3.233  7.941   1.00 44.95 ? 743 HOH A O   1 
HETATM 6408 O  O   . HOH G 4 .   ? -5.173  4.143   -40.476 1.00 43.75 ? 744 HOH A O   1 
HETATM 6409 O  O   . HOH G 4 .   ? -22.250 3.828   -32.022 1.00 49.69 ? 745 HOH A O   1 
HETATM 6410 O  O   . HOH G 4 .   ? -31.555 -6.135  -24.219 1.00 24.12 ? 746 HOH A O   1 
HETATM 6411 O  O   . HOH G 4 .   ? -14.600 -15.930 -13.272 1.00 45.65 ? 747 HOH A O   1 
HETATM 6412 O  O   . HOH G 4 .   ? -7.394  2.617   -0.487  1.00 47.77 ? 748 HOH A O   1 
HETATM 6413 O  O   . HOH G 4 .   ? -10.604 -2.111  -40.913 1.00 44.61 ? 749 HOH A O   1 
HETATM 6414 O  O   . HOH G 4 .   ? -34.128 2.831   -26.951 1.00 38.81 ? 750 HOH A O   1 
HETATM 6415 O  O   . HOH G 4 .   ? -8.995  6.916   -11.620 1.00 35.74 ? 751 HOH A O   1 
HETATM 6416 O  O   . HOH G 4 .   ? -10.591 -15.288 -34.216 1.00 51.05 ? 752 HOH A O   1 
HETATM 6417 O  O   . HOH G 4 .   ? -4.296  -1.481  0.341   1.00 54.59 ? 753 HOH A O   1 
HETATM 6418 O  O   . HOH G 4 .   ? 4.365   7.844   -32.469 1.00 35.52 ? 754 HOH A O   1 
HETATM 6419 O  O   . HOH G 4 .   ? -36.787 -4.707  -20.445 1.00 48.92 ? 755 HOH A O   1 
HETATM 6420 O  O   . HOH G 4 .   ? -33.878 6.414   -32.513 1.00 46.59 ? 756 HOH A O   1 
HETATM 6421 O  O   . HOH G 4 .   ? -17.811 -3.137  0.742   1.00 48.73 ? 757 HOH A O   1 
HETATM 6422 O  O   . HOH G 4 .   ? 2.813   -17.468 -23.559 1.00 59.92 ? 758 HOH A O   1 
HETATM 6423 O  O   . HOH G 4 .   ? 2.432   7.713   -12.637 1.00 43.30 ? 759 HOH A O   1 
HETATM 6424 O  O   . HOH G 4 .   ? -23.446 -11.666 -24.528 0.50 19.20 ? 760 HOH A O   1 
HETATM 6425 O  O   . HOH G 4 .   ? -0.310  15.846  -25.526 1.00 37.42 ? 761 HOH A O   1 
HETATM 6426 O  O   . HOH G 4 .   ? 7.133   -11.755 -22.323 1.00 48.59 ? 762 HOH A O   1 
HETATM 6427 O  O   . HOH G 4 .   ? -2.917  6.124   -2.973  1.00 45.12 ? 763 HOH A O   1 
HETATM 6428 O  O   . HOH G 4 .   ? -3.754  18.164  -18.896 1.00 45.47 ? 764 HOH A O   1 
HETATM 6429 O  O   . HOH G 4 .   ? 6.370   -6.972  -8.056  1.00 55.50 ? 765 HOH A O   1 
HETATM 6430 O  O   . HOH G 4 .   ? 0.468   0.686   -3.071  1.00 47.21 ? 766 HOH A O   1 
HETATM 6431 O  O   . HOH G 4 .   ? -15.099 -10.022 -28.702 1.00 37.62 ? 767 HOH A O   1 
HETATM 6432 O  O   . HOH G 4 .   ? -26.790 -6.250  -14.297 1.00 35.44 ? 768 HOH A O   1 
HETATM 6433 O  O   . HOH G 4 .   ? -6.524  17.797  -18.992 1.00 35.35 ? 769 HOH A O   1 
HETATM 6434 O  O   . HOH G 4 .   ? -26.208 6.198   -34.559 1.00 53.79 ? 770 HOH A O   1 
HETATM 6435 O  O   . HOH G 4 .   ? -36.275 7.260   -23.513 1.00 52.57 ? 771 HOH A O   1 
HETATM 6436 O  O   . HOH G 4 .   ? 11.011  7.909   -30.972 1.00 41.49 ? 772 HOH A O   1 
HETATM 6437 O  O   . HOH G 4 .   ? -23.520 22.592  -17.379 1.00 54.99 ? 773 HOH A O   1 
HETATM 6438 O  O   . HOH G 4 .   ? -1.583  16.238  -32.404 1.00 49.97 ? 774 HOH A O   1 
HETATM 6439 O  O   . HOH G 4 .   ? -25.722 5.205   -16.763 1.00 43.53 ? 775 HOH A O   1 
HETATM 6440 O  O   . HOH G 4 .   ? -31.676 -4.046  -26.832 1.00 39.23 ? 776 HOH A O   1 
HETATM 6441 O  O   . HOH G 4 .   ? 4.532   14.018  -21.311 1.00 38.39 ? 777 HOH A O   1 
HETATM 6442 O  O   . HOH G 4 .   ? -5.874  15.343  -16.954 1.00 36.64 ? 778 HOH A O   1 
HETATM 6443 O  O   . HOH G 4 .   ? 12.800  -2.746  -8.067  1.00 50.02 ? 779 HOH A O   1 
HETATM 6444 O  O   . HOH G 4 .   ? -13.343 -14.097 4.101   1.00 51.04 ? 780 HOH A O   1 
HETATM 6445 O  O   . HOH G 4 .   ? 13.285  -4.699  -10.265 1.00 52.17 ? 781 HOH A O   1 
HETATM 6446 O  O   . HOH G 4 .   ? -20.107 -13.273 0.648   1.00 59.74 ? 782 HOH A O   1 
HETATM 6447 O  O   . HOH G 4 .   ? 2.122   17.136  -25.885 1.00 61.81 ? 783 HOH A O   1 
HETATM 6448 O  O   . HOH G 4 .   ? -0.853  -10.846 -4.596  1.00 49.87 ? 784 HOH A O   1 
HETATM 6449 O  O   . HOH G 4 .   ? -46.744 0.105   -5.215  1.00 55.41 ? 785 HOH A O   1 
HETATM 6450 O  O   . HOH G 4 .   ? -16.620 -2.689  -38.242 1.00 43.45 ? 786 HOH A O   1 
HETATM 6451 O  O   . HOH G 4 .   ? -22.816 -14.013 -14.868 1.00 54.63 ? 787 HOH A O   1 
HETATM 6452 O  O   . HOH G 4 .   ? 8.355   -6.325  -31.423 1.00 41.74 ? 788 HOH A O   1 
HETATM 6453 O  O   . HOH G 4 .   ? -15.375 -1.143  -28.860 1.00 45.83 ? 789 HOH A O   1 
HETATM 6454 O  O   . HOH G 4 .   ? -39.422 -11.343 -14.854 1.00 50.49 ? 790 HOH A O   1 
HETATM 6455 O  O   . HOH G 4 .   ? -9.549  -6.107  -7.354  1.00 47.65 ? 791 HOH A O   1 
HETATM 6456 O  O   . HOH G 4 .   ? -23.600 23.096  -19.979 1.00 52.32 ? 792 HOH A O   1 
HETATM 6457 O  O   . HOH G 4 .   ? 6.593   -4.469  -7.099  1.00 49.94 ? 793 HOH A O   1 
HETATM 6458 O  O   . HOH G 4 .   ? -29.930 -9.881  -13.257 1.00 48.32 ? 794 HOH A O   1 
HETATM 6459 O  O   . HOH G 4 .   ? 14.878  2.857   -37.312 1.00 48.88 ? 795 HOH A O   1 
HETATM 6460 O  O   . HOH G 4 .   ? -10.033 -10.813 -9.407  1.00 34.74 ? 796 HOH A O   1 
HETATM 6461 O  O   . HOH G 4 .   ? -5.051  1.038   -40.774 1.00 56.01 ? 797 HOH A O   1 
HETATM 6462 O  O   . HOH G 4 .   ? -40.553 -5.763  -14.893 1.00 53.06 ? 798 HOH A O   1 
HETATM 6463 O  O   . HOH G 4 .   ? 13.069  -10.740 -19.972 1.00 49.18 ? 799 HOH A O   1 
HETATM 6464 O  O   . HOH G 4 .   ? -33.852 9.361   -6.860  1.00 40.29 ? 800 HOH A O   1 
HETATM 6465 O  O   . HOH G 4 .   ? 1.530   -1.808  -3.498  1.00 53.61 ? 801 HOH A O   1 
HETATM 6466 O  O   . HOH G 4 .   ? -19.284 -6.404  -32.838 1.00 49.10 ? 802 HOH A O   1 
HETATM 6467 O  O   . HOH G 4 .   ? -4.643  15.973  -28.551 1.00 39.77 ? 803 HOH A O   1 
HETATM 6468 O  O   . HOH G 4 .   ? -0.864  -6.895  -3.896  1.00 45.16 ? 804 HOH A O   1 
HETATM 6469 O  O   . HOH G 4 .   ? -7.931  19.245  -25.853 1.00 57.60 ? 805 HOH A O   1 
HETATM 6470 O  O   . HOH G 4 .   ? -16.981 13.583  -4.050  1.00 44.16 ? 806 HOH A O   1 
HETATM 6471 O  O   . HOH G 4 .   ? -0.022  -1.489  -39.185 1.00 34.11 ? 807 HOH A O   1 
HETATM 6472 O  O   . HOH G 4 .   ? -32.407 -5.149  -21.698 1.00 49.28 ? 808 HOH A O   1 
HETATM 6473 O  O   . HOH G 4 .   ? -10.345 -5.779  -1.853  1.00 42.47 ? 809 HOH A O   1 
HETATM 6474 O  O   . HOH G 4 .   ? -19.393 15.600  -4.784  1.00 59.27 ? 810 HOH A O   1 
HETATM 6475 O  O   . HOH G 4 .   ? -42.925 -7.339  -14.546 1.00 56.81 ? 811 HOH A O   1 
HETATM 6476 O  O   . HOH G 4 .   ? -11.629 -17.604 -32.381 1.00 56.02 ? 812 HOH A O   1 
HETATM 6477 O  O   . HOH G 4 .   ? -36.071 2.476   -24.854 1.00 54.25 ? 813 HOH A O   1 
HETATM 6478 O  O   . HOH G 4 .   ? -29.722 13.315  -3.070  1.00 49.38 ? 814 HOH A O   1 
HETATM 6479 O  O   . HOH G 4 .   ? -25.028 21.262  -15.442 1.00 60.20 ? 815 HOH A O   1 
HETATM 6480 O  O   . HOH G 4 .   ? -36.449 -11.204 -20.780 1.00 35.92 ? 816 HOH A O   1 
HETATM 6481 O  O   . HOH G 4 .   ? -10.405 9.251   -35.093 1.00 49.47 ? 817 HOH A O   1 
HETATM 6482 O  O   . HOH G 4 .   ? -47.658 -3.113  -6.326  1.00 52.97 ? 818 HOH A O   1 
HETATM 6483 O  O   . HOH G 4 .   ? -16.263 -14.979 -18.465 1.00 50.29 ? 819 HOH A O   1 
HETATM 6484 O  O   . HOH G 4 .   ? -10.234 -20.169 -13.921 1.00 56.51 ? 820 HOH A O   1 
HETATM 6485 O  O   . HOH G 4 .   ? -35.370 -8.445  -25.142 1.00 34.60 ? 821 HOH A O   1 
HETATM 6486 O  O   . HOH G 4 .   ? -19.079 -4.235  -28.038 1.00 49.40 ? 822 HOH A O   1 
HETATM 6487 O  O   . HOH G 4 .   ? -22.292 -7.722  -27.498 1.00 48.98 ? 823 HOH A O   1 
HETATM 6488 O  O   . HOH G 4 .   ? -12.944 19.347  -5.522  1.00 45.69 ? 824 HOH A O   1 
HETATM 6489 O  O   . HOH G 4 .   ? -19.372 23.415  -21.297 1.00 60.13 ? 825 HOH A O   1 
HETATM 6490 O  O   . HOH G 4 .   ? -9.940  -8.560  -8.031  1.00 40.57 ? 826 HOH A O   1 
HETATM 6491 O  O   . HOH G 4 .   ? -35.365 -4.225  -23.496 1.00 47.96 ? 827 HOH A O   1 
HETATM 6492 O  O   . HOH G 4 .   ? -33.747 1.274   -29.510 1.00 53.49 ? 828 HOH A O   1 
HETATM 6493 O  O   . HOH G 4 .   ? -28.757 -2.127  6.587   1.00 46.02 ? 829 HOH A O   1 
HETATM 6494 O  O   . HOH G 4 .   ? -8.857  -13.192 -8.369  1.00 48.88 ? 830 HOH A O   1 
HETATM 6495 O  O   . HOH G 4 .   ? -15.793 1.921   -26.863 1.00 35.97 ? 831 HOH A O   1 
HETATM 6496 O  O   . HOH G 4 .   ? -25.194 0.363   6.315   1.00 49.56 ? 832 HOH A O   1 
HETATM 6497 O  O   . HOH G 4 .   ? -5.688  0.654   1.374   1.00 54.16 ? 833 HOH A O   1 
HETATM 6498 O  O   . HOH G 4 .   ? -31.373 10.461  -6.949  1.00 43.08 ? 834 HOH A O   1 
HETATM 6499 O  O   . HOH G 4 .   ? -19.695 -13.845 -15.904 1.00 39.86 ? 835 HOH A O   1 
HETATM 6500 O  O   . HOH G 4 .   ? -37.235 8.233   -4.149  1.00 43.75 ? 836 HOH A O   1 
HETATM 6501 O  O   . HOH G 4 .   ? -27.877 0.268   6.854   1.00 52.71 ? 837 HOH A O   1 
HETATM 6502 O  O   . HOH G 4 .   ? -7.411  18.628  -14.727 1.00 42.53 ? 838 HOH A O   1 
HETATM 6503 O  O   . HOH G 4 .   ? -7.889  20.265  -18.915 1.00 57.61 ? 839 HOH A O   1 
HETATM 6504 O  O   . HOH G 4 .   ? -17.755 -5.230  2.349   1.00 47.72 ? 840 HOH A O   1 
HETATM 6505 O  O   . HOH G 4 .   ? -33.912 6.663   5.011   1.00 52.72 ? 841 HOH A O   1 
HETATM 6506 O  O   . HOH G 4 .   ? -36.853 5.317   -24.825 1.00 53.41 ? 842 HOH A O   1 
HETATM 6507 O  O   . HOH G 4 .   ? -49.274 0.850   -5.910  1.00 57.72 ? 843 HOH A O   1 
HETATM 6508 O  O   . HOH H 4 .   ? -22.004 -12.480 -26.651 0.50 19.88 ? 601 HOH B O   1 
HETATM 6509 O  O   . HOH H 4 .   ? -35.872 -47.567 -32.059 1.00 51.85 ? 602 HOH B O   1 
HETATM 6510 O  O   . HOH H 4 .   ? -3.216  -28.456 -23.677 1.00 40.91 ? 603 HOH B O   1 
HETATM 6511 O  O   . HOH H 4 .   ? -26.417 -36.059 -13.118 1.00 32.86 ? 604 HOH B O   1 
HETATM 6512 O  O   . HOH H 4 .   ? -24.241 -14.793 -22.001 0.50 16.61 ? 605 HOH B O   1 
HETATM 6513 O  O   . HOH H 4 .   ? -9.819  -43.467 -7.542  1.00 47.71 ? 606 HOH B O   1 
HETATM 6514 O  O   . HOH H 4 .   ? 3.868   -35.825 -31.338 1.00 30.38 ? 607 HOH B O   1 
HETATM 6515 O  O   . HOH H 4 .   ? -1.427  -36.197 -32.465 1.00 36.79 ? 608 HOH B O   1 
HETATM 6516 O  O   . HOH H 4 .   ? -53.026 -8.319  -34.998 1.00 39.02 ? 609 HOH B O   1 
HETATM 6517 O  O   . HOH H 4 .   ? -29.445 -12.971 -28.919 1.00 38.90 ? 610 HOH B O   1 
HETATM 6518 O  O   . HOH H 4 .   ? -35.341 -27.804 -18.282 1.00 36.02 ? 611 HOH B O   1 
HETATM 6519 O  O   . HOH H 4 .   ? -29.818 -16.234 -14.377 1.00 46.70 ? 612 HOH B O   1 
HETATM 6520 O  O   . HOH H 4 .   ? -31.801 -22.973 -35.396 1.00 34.10 ? 613 HOH B O   1 
HETATM 6521 O  O   . HOH H 4 .   ? -35.450 -46.589 -37.099 1.00 36.25 ? 614 HOH B O   1 
HETATM 6522 O  O   . HOH H 4 .   ? -46.449 -36.805 -19.558 1.00 44.42 ? 615 HOH B O   1 
HETATM 6523 O  O   . HOH H 4 .   ? -12.621 -40.357 -23.623 1.00 27.68 ? 616 HOH B O   1 
HETATM 6524 O  O   . HOH H 4 .   ? -36.506 -20.787 -42.372 1.00 44.65 ? 617 HOH B O   1 
HETATM 6525 O  O   . HOH H 4 .   ? -57.010 -13.602 -40.831 1.00 51.03 ? 618 HOH B O   1 
HETATM 6526 O  O   . HOH H 4 .   ? -48.793 -13.000 -14.914 1.00 50.66 ? 619 HOH B O   1 
HETATM 6527 O  O   . HOH H 4 .   ? -45.624 -34.868 -37.512 1.00 40.72 ? 620 HOH B O   1 
HETATM 6528 O  O   . HOH H 4 .   ? -39.440 -38.238 -43.341 1.00 41.86 ? 621 HOH B O   1 
HETATM 6529 O  O   . HOH H 4 .   ? -6.448  -40.342 -21.114 1.00 33.12 ? 622 HOH B O   1 
HETATM 6530 O  O   . HOH H 4 .   ? -44.481 -11.197 -17.920 1.00 39.37 ? 623 HOH B O   1 
HETATM 6531 O  O   . HOH H 4 .   ? -15.799 -39.223 -32.935 1.00 34.94 ? 624 HOH B O   1 
HETATM 6532 O  O   . HOH H 4 .   ? -23.086 -14.107 -31.555 1.00 45.23 ? 625 HOH B O   1 
HETATM 6533 O  O   . HOH H 4 .   ? -15.019 -12.640 -28.201 1.00 49.95 ? 626 HOH B O   1 
HETATM 6534 O  O   . HOH H 4 .   ? -19.351 -24.626 -24.725 1.00 29.91 ? 627 HOH B O   1 
HETATM 6535 O  O   . HOH H 4 .   ? -41.518 -5.844  -32.275 1.00 38.01 ? 628 HOH B O   1 
HETATM 6536 O  O   . HOH H 4 .   ? -56.048 -26.613 -23.175 1.00 42.21 ? 629 HOH B O   1 
HETATM 6537 O  O   . HOH H 4 .   ? -51.442 -32.278 -37.437 1.00 41.02 ? 630 HOH B O   1 
HETATM 6538 O  O   . HOH H 4 .   ? -48.910 -10.843 -39.481 1.00 44.15 ? 631 HOH B O   1 
HETATM 6539 O  O   . HOH H 4 .   ? -54.016 -34.935 -37.213 1.00 35.83 ? 632 HOH B O   1 
HETATM 6540 O  O   . HOH H 4 .   ? -12.812 -26.027 -13.469 1.00 48.66 ? 633 HOH B O   1 
HETATM 6541 O  O   . HOH H 4 .   ? -44.307 -35.669 -20.460 1.00 27.32 ? 634 HOH B O   1 
HETATM 6542 O  O   . HOH H 4 .   ? -53.825 -15.545 -27.149 1.00 26.51 ? 635 HOH B O   1 
HETATM 6543 O  O   . HOH H 4 .   ? -50.099 -33.309 -42.936 1.00 45.18 ? 636 HOH B O   1 
HETATM 6544 O  O   . HOH H 4 .   ? -19.751 -38.659 -7.151  1.00 38.31 ? 637 HOH B O   1 
HETATM 6545 O  O   . HOH H 4 .   ? -30.810 -28.779 -8.633  1.00 48.62 ? 638 HOH B O   1 
HETATM 6546 O  O   . HOH H 4 .   ? -58.806 -21.219 -25.745 1.00 34.02 ? 639 HOH B O   1 
HETATM 6547 O  O   . HOH H 4 .   ? 0.509   -33.212 -13.385 1.00 52.81 ? 640 HOH B O   1 
HETATM 6548 O  O   . HOH H 4 .   ? -40.808 -20.750 -27.074 1.00 18.81 ? 641 HOH B O   1 
HETATM 6549 O  O   . HOH H 4 .   ? -41.021 -44.028 -29.877 1.00 41.04 ? 642 HOH B O   1 
HETATM 6550 O  O   . HOH H 4 .   ? -47.981 -17.301 -16.389 1.00 41.45 ? 643 HOH B O   1 
HETATM 6551 O  O   . HOH H 4 .   ? -47.540 -30.468 -33.699 1.00 26.04 ? 644 HOH B O   1 
HETATM 6552 O  O   . HOH H 4 .   ? -43.130 -35.510 -37.764 1.00 33.64 ? 645 HOH B O   1 
HETATM 6553 O  O   . HOH H 4 .   ? -42.120 -33.161 -44.037 1.00 54.19 ? 646 HOH B O   1 
HETATM 6554 O  O   . HOH H 4 .   ? -24.373 -41.707 -19.438 1.00 33.74 ? 647 HOH B O   1 
HETATM 6555 O  O   . HOH H 4 .   ? -31.399 -4.005  -38.654 1.00 55.51 ? 648 HOH B O   1 
HETATM 6556 O  O   . HOH H 4 .   ? -11.143 -28.523 -35.249 1.00 34.64 ? 649 HOH B O   1 
HETATM 6557 O  O   . HOH H 4 .   ? -44.730 -1.058  -35.148 1.00 39.91 ? 650 HOH B O   1 
HETATM 6558 O  O   . HOH H 4 .   ? -22.261 -43.864 -36.623 1.00 53.57 ? 651 HOH B O   1 
HETATM 6559 O  O   . HOH H 4 .   ? -40.472 -24.820 -22.496 1.00 22.82 ? 652 HOH B O   1 
HETATM 6560 O  O   . HOH H 4 .   ? -15.036 -43.733 -12.169 1.00 39.90 ? 653 HOH B O   1 
HETATM 6561 O  O   . HOH H 4 .   ? -28.637 -20.079 -33.228 1.00 37.28 ? 654 HOH B O   1 
HETATM 6562 O  O   . HOH H 4 .   ? -20.740 -37.716 -42.783 1.00 39.16 ? 655 HOH B O   1 
HETATM 6563 O  O   . HOH H 4 .   ? -22.774 -18.726 -7.679  1.00 40.09 ? 656 HOH B O   1 
HETATM 6564 O  O   . HOH H 4 .   ? -22.665 -40.611 -12.939 1.00 40.96 ? 657 HOH B O   1 
HETATM 6565 O  O   . HOH H 4 .   ? -53.963 -19.214 -43.310 1.00 36.04 ? 658 HOH B O   1 
HETATM 6566 O  O   . HOH H 4 .   ? -15.093 -35.725 -38.072 1.00 33.37 ? 659 HOH B O   1 
HETATM 6567 O  O   . HOH H 4 .   ? -23.762 -26.640 -25.376 1.00 26.39 ? 660 HOH B O   1 
HETATM 6568 O  O   . HOH H 4 .   ? -29.864 -41.278 -22.651 1.00 36.77 ? 661 HOH B O   1 
HETATM 6569 O  O   . HOH H 4 .   ? -4.028  -43.971 -4.823  1.00 34.37 ? 662 HOH B O   1 
HETATM 6570 O  O   . HOH H 4 .   ? -30.543 -26.025 -19.964 1.00 23.17 ? 663 HOH B O   1 
HETATM 6571 O  O   . HOH H 4 .   ? -31.042 -24.840 -22.479 1.00 23.10 ? 664 HOH B O   1 
HETATM 6572 O  O   . HOH H 4 .   ? -40.602 -19.856 -45.293 1.00 42.93 ? 665 HOH B O   1 
HETATM 6573 O  O   . HOH H 4 .   ? -21.285 -25.542 -26.499 1.00 21.89 ? 666 HOH B O   1 
HETATM 6574 O  O   . HOH H 4 .   ? -26.729 -45.798 -36.303 1.00 47.21 ? 667 HOH B O   1 
HETATM 6575 O  O   . HOH H 4 .   ? -41.741 -20.472 -13.728 1.00 50.00 ? 668 HOH B O   1 
HETATM 6576 O  O   . HOH H 4 .   ? -4.563  -37.234 -24.106 1.00 43.49 ? 669 HOH B O   1 
HETATM 6577 O  O   . HOH H 4 .   ? -30.897 -41.010 -16.336 1.00 42.24 ? 670 HOH B O   1 
HETATM 6578 O  O   . HOH H 4 .   ? -17.954 -28.526 -32.470 1.00 27.48 ? 671 HOH B O   1 
HETATM 6579 O  O   . HOH H 4 .   ? -30.588 -44.503 -25.872 1.00 36.33 ? 672 HOH B O   1 
HETATM 6580 O  O   . HOH H 4 .   ? -17.586 -38.955 -26.504 1.00 29.77 ? 673 HOH B O   1 
HETATM 6581 O  O   . HOH H 4 .   ? -17.984 -43.319 -27.040 1.00 39.73 ? 674 HOH B O   1 
HETATM 6582 O  O   . HOH H 4 .   ? -37.735 -12.154 -23.064 1.00 35.36 ? 675 HOH B O   1 
HETATM 6583 O  O   . HOH H 4 .   ? -21.198 -9.421  -29.331 1.00 47.99 ? 676 HOH B O   1 
HETATM 6584 O  O   . HOH H 4 .   ? -35.859 -32.381 -10.375 1.00 42.76 ? 677 HOH B O   1 
HETATM 6585 O  O   . HOH H 4 .   ? -49.638 -34.814 -37.608 1.00 50.67 ? 678 HOH B O   1 
HETATM 6586 O  O   . HOH H 4 .   ? -6.387  -42.487 -14.964 1.00 32.15 ? 679 HOH B O   1 
HETATM 6587 O  O   . HOH H 4 .   ? -29.869 -42.228 -41.978 1.00 33.11 ? 680 HOH B O   1 
HETATM 6588 O  O   . HOH H 4 .   ? -32.436 -23.474 -24.389 1.00 21.57 ? 681 HOH B O   1 
HETATM 6589 O  O   . HOH H 4 .   ? -34.395 -30.084 -14.514 1.00 32.81 ? 682 HOH B O   1 
HETATM 6590 O  O   . HOH H 4 .   ? -51.274 -12.034 -19.747 1.00 37.59 ? 683 HOH B O   1 
HETATM 6591 O  O   . HOH H 4 .   ? -29.415 -28.162 -21.274 1.00 23.08 ? 684 HOH B O   1 
HETATM 6592 O  O   . HOH H 4 .   ? -47.278 1.099   -30.042 1.00 42.41 ? 685 HOH B O   1 
HETATM 6593 O  O   . HOH H 4 .   ? -12.177 -16.092 -28.774 1.00 37.11 ? 686 HOH B O   1 
HETATM 6594 O  O   . HOH H 4 .   ? -13.965 -23.764 -12.476 1.00 44.62 ? 687 HOH B O   1 
HETATM 6595 O  O   . HOH H 4 .   ? -8.656  -13.937 -28.300 1.00 36.76 ? 688 HOH B O   1 
HETATM 6596 O  O   . HOH H 4 .   ? -55.346 -10.933 -35.510 1.00 48.83 ? 689 HOH B O   1 
HETATM 6597 O  O   . HOH H 4 .   ? -14.057 -21.875 -29.270 1.00 50.08 ? 690 HOH B O   1 
HETATM 6598 O  O   . HOH H 4 .   ? -20.177 -15.863 -21.024 1.00 56.01 ? 691 HOH B O   1 
HETATM 6599 O  O   . HOH H 4 .   ? -40.273 -11.022 -23.719 1.00 35.10 ? 692 HOH B O   1 
HETATM 6600 O  O   . HOH H 4 .   ? -28.243 -21.721 -35.245 1.00 46.49 ? 693 HOH B O   1 
HETATM 6601 O  O   . HOH H 4 .   ? -49.693 -28.031 -49.283 1.00 52.20 ? 694 HOH B O   1 
HETATM 6602 O  O   . HOH H 4 .   ? -8.468  -23.141 -18.231 1.00 40.62 ? 695 HOH B O   1 
HETATM 6603 O  O   . HOH H 4 .   ? -18.766 -30.392 -34.284 1.00 20.92 ? 696 HOH B O   1 
HETATM 6604 O  O   . HOH H 4 .   ? -32.291 -11.588 -38.885 1.00 40.39 ? 697 HOH B O   1 
HETATM 6605 O  O   . HOH H 4 .   ? -28.162 -34.351 -11.918 1.00 40.45 ? 698 HOH B O   1 
HETATM 6606 O  O   . HOH H 4 .   ? -34.310 -19.609 -42.931 1.00 42.14 ? 699 HOH B O   1 
HETATM 6607 O  O   . HOH H 4 .   ? -18.544 -15.994 -14.717 1.00 38.75 ? 700 HOH B O   1 
HETATM 6608 O  O   . HOH H 4 .   ? -13.700 -43.666 -17.809 1.00 38.73 ? 701 HOH B O   1 
HETATM 6609 O  O   . HOH H 4 .   ? -33.407 -20.139 -30.084 1.00 24.37 ? 702 HOH B O   1 
HETATM 6610 O  O   . HOH H 4 .   ? -43.966 -29.355 -21.833 1.00 24.86 ? 703 HOH B O   1 
HETATM 6611 O  O   . HOH H 4 .   ? -42.777 2.672   -28.396 1.00 58.35 ? 704 HOH B O   1 
HETATM 6612 O  O   . HOH H 4 .   ? -45.965 -3.328  -31.594 1.00 34.09 ? 705 HOH B O   1 
HETATM 6613 O  O   . HOH H 4 .   ? -29.439 -32.619 -19.139 1.00 33.17 ? 706 HOH B O   1 
HETATM 6614 O  O   . HOH H 4 .   ? -31.978 -38.482 -47.647 1.00 52.47 ? 707 HOH B O   1 
HETATM 6615 O  O   . HOH H 4 .   ? -23.852 -18.348 -17.412 1.00 48.76 ? 708 HOH B O   1 
HETATM 6616 O  O   . HOH H 4 .   ? -28.714 -36.819 -48.911 1.00 44.52 ? 709 HOH B O   1 
HETATM 6617 O  O   . HOH H 4 .   ? -15.908 -22.847 -21.518 1.00 40.58 ? 710 HOH B O   1 
HETATM 6618 O  O   . HOH H 4 .   ? -29.333 -31.275 -30.094 1.00 27.48 ? 711 HOH B O   1 
HETATM 6619 O  O   . HOH H 4 .   ? -58.051 -19.930 -33.782 1.00 31.53 ? 712 HOH B O   1 
HETATM 6620 O  O   . HOH H 4 .   ? -15.469 -39.884 -6.961  1.00 34.10 ? 713 HOH B O   1 
HETATM 6621 O  O   . HOH H 4 .   ? -35.460 -22.777 -32.879 1.00 36.84 ? 714 HOH B O   1 
HETATM 6622 O  O   . HOH H 4 .   ? -46.878 -35.181 -17.556 1.00 27.97 ? 715 HOH B O   1 
HETATM 6623 O  O   . HOH H 4 .   ? -35.487 -4.244  -26.618 1.00 57.43 ? 716 HOH B O   1 
HETATM 6624 O  O   . HOH H 4 .   ? -43.442 -20.511 -47.422 1.00 46.49 ? 717 HOH B O   1 
HETATM 6625 O  O   . HOH H 4 .   ? -17.966 -16.568 -19.656 1.00 44.88 ? 718 HOH B O   1 
HETATM 6626 O  O   . HOH H 4 .   ? -14.789 -45.123 -19.764 1.00 41.32 ? 719 HOH B O   1 
HETATM 6627 O  O   . HOH H 4 .   ? -44.065 -28.867 -19.074 1.00 22.72 ? 720 HOH B O   1 
HETATM 6628 O  O   . HOH H 4 .   ? -26.742 -37.062 -47.057 1.00 34.92 ? 721 HOH B O   1 
HETATM 6629 O  O   . HOH H 4 .   ? -46.555 -40.055 -19.626 1.00 53.43 ? 722 HOH B O   1 
HETATM 6630 O  O   . HOH H 4 .   ? -57.617 -13.457 -21.343 1.00 45.08 ? 723 HOH B O   1 
HETATM 6631 O  O   . HOH H 4 .   ? -52.717 -34.132 -34.362 1.00 37.92 ? 724 HOH B O   1 
HETATM 6632 O  O   . HOH H 4 .   ? -7.048  -28.224 -32.844 1.00 49.27 ? 725 HOH B O   1 
HETATM 6633 O  O   . HOH H 4 .   ? -59.613 -12.362 -25.162 1.00 51.36 ? 726 HOH B O   1 
HETATM 6634 O  O   . HOH H 4 .   ? -51.890 -11.848 -22.932 1.00 44.64 ? 727 HOH B O   1 
HETATM 6635 O  O   . HOH H 4 .   ? -41.433 -37.511 -39.213 1.00 38.46 ? 728 HOH B O   1 
HETATM 6636 O  O   . HOH H 4 .   ? -4.001  -36.842 -31.671 1.00 37.14 ? 729 HOH B O   1 
HETATM 6637 O  O   . HOH H 4 .   ? -11.987 -20.204 -11.891 1.00 44.54 ? 730 HOH B O   1 
HETATM 6638 O  O   . HOH H 4 .   ? -28.448 -32.778 -27.626 1.00 25.81 ? 731 HOH B O   1 
HETATM 6639 O  O   . HOH H 4 .   ? -60.176 -21.162 -41.098 1.00 55.63 ? 732 HOH B O   1 
HETATM 6640 O  O   . HOH H 4 .   ? -3.034  -37.492 -20.266 1.00 54.39 ? 733 HOH B O   1 
HETATM 6641 O  O   . HOH H 4 .   ? -44.683 -38.003 -39.585 1.00 42.58 ? 734 HOH B O   1 
HETATM 6642 O  O   . HOH H 4 .   ? -32.240 -41.734 -21.173 1.00 36.90 ? 735 HOH B O   1 
HETATM 6643 O  O   . HOH H 4 .   ? -33.044 -45.294 -26.991 1.00 34.12 ? 736 HOH B O   1 
HETATM 6644 O  O   . HOH H 4 .   ? -38.406 -39.250 -36.624 1.00 36.79 ? 737 HOH B O   1 
HETATM 6645 O  O   . HOH H 4 .   ? -32.838 -6.729  -32.457 1.00 42.59 ? 738 HOH B O   1 
HETATM 6646 O  O   . HOH H 4 .   ? -25.850 -41.069 -12.374 1.00 55.64 ? 739 HOH B O   1 
HETATM 6647 O  O   . HOH H 4 .   ? -13.200 -38.033 -0.506  1.00 55.81 ? 740 HOH B O   1 
HETATM 6648 O  O   . HOH H 4 .   ? -40.404 -19.538 -32.226 0.50 23.61 ? 741 HOH B O   1 
HETATM 6649 O  O   . HOH H 4 .   ? -54.418 -29.022 -23.381 1.00 41.79 ? 742 HOH B O   1 
HETATM 6650 O  O   . HOH H 4 .   ? -36.738 -37.520 -13.788 1.00 40.43 ? 743 HOH B O   1 
HETATM 6651 O  O   . HOH H 4 .   ? -47.644 -30.682 -14.603 1.00 45.27 ? 744 HOH B O   1 
HETATM 6652 O  O   . HOH H 4 .   ? -59.030 -23.409 -17.762 1.00 43.97 ? 745 HOH B O   1 
HETATM 6653 O  O   . HOH H 4 .   ? -49.425 -22.702 -44.148 1.00 38.12 ? 746 HOH B O   1 
HETATM 6654 O  O   . HOH H 4 .   ? -10.757 -26.307 -15.204 1.00 38.74 ? 747 HOH B O   1 
HETATM 6655 O  O   . HOH H 4 .   ? -57.618 -22.271 -32.437 1.00 28.94 ? 748 HOH B O   1 
HETATM 6656 O  O   . HOH H 4 .   ? -14.934 -19.651 -36.562 1.00 41.45 ? 749 HOH B O   1 
HETATM 6657 O  O   . HOH H 4 .   ? -39.265 -39.746 -16.500 1.00 49.64 ? 750 HOH B O   1 
HETATM 6658 O  O   . HOH H 4 .   ? -33.621 -8.579  -29.728 1.00 43.14 ? 751 HOH B O   1 
HETATM 6659 O  O   . HOH H 4 .   ? -31.145 -19.381 -37.174 1.00 50.60 ? 752 HOH B O   1 
HETATM 6660 O  O   . HOH H 4 .   ? -22.572 -38.740 -40.373 1.00 52.30 ? 753 HOH B O   1 
HETATM 6661 O  O   . HOH H 4 .   ? -20.965 -30.265 -31.323 1.00 38.75 ? 754 HOH B O   1 
HETATM 6662 O  O   . HOH H 4 .   ? -53.066 -32.820 -43.558 1.00 36.94 ? 755 HOH B O   1 
HETATM 6663 O  O   . HOH H 4 .   ? -46.507 -33.373 -15.822 1.00 42.71 ? 756 HOH B O   1 
HETATM 6664 O  O   . HOH H 4 .   ? -18.704 -23.369 -22.065 1.00 39.14 ? 757 HOH B O   1 
HETATM 6665 O  O   . HOH H 4 .   ? -57.786 -27.976 -27.869 1.00 42.98 ? 758 HOH B O   1 
HETATM 6666 O  O   . HOH H 4 .   ? -37.524 -20.038 -16.424 1.00 46.42 ? 759 HOH B O   1 
HETATM 6667 O  O   . HOH H 4 .   ? -60.519 -18.971 -23.438 1.00 41.85 ? 760 HOH B O   1 
HETATM 6668 O  O   . HOH H 4 .   ? -35.025 -28.717 -8.444  1.00 53.41 ? 761 HOH B O   1 
HETATM 6669 O  O   . HOH H 4 .   ? -47.591 -31.496 -42.709 1.00 28.55 ? 762 HOH B O   1 
HETATM 6670 O  O   . HOH H 4 .   ? -13.283 -14.950 -34.834 1.00 41.04 ? 763 HOH B O   1 
HETATM 6671 O  O   . HOH H 4 .   ? -24.623 -13.006 -23.307 0.50 20.53 ? 764 HOH B O   1 
HETATM 6672 O  O   . HOH H 4 .   ? -58.340 -27.020 -17.115 1.00 58.03 ? 765 HOH B O   1 
HETATM 6673 O  O   . HOH H 4 .   ? -18.853 -45.598 -21.260 1.00 55.45 ? 766 HOH B O   1 
HETATM 6674 O  O   . HOH H 4 .   ? -13.630 -22.569 -18.900 1.00 52.28 ? 767 HOH B O   1 
HETATM 6675 O  O   . HOH H 4 .   ? -51.186 -20.902 -43.221 1.00 31.54 ? 768 HOH B O   1 
HETATM 6676 O  O   . HOH H 4 .   ? -46.219 -34.580 -33.153 1.00 49.84 ? 769 HOH B O   1 
HETATM 6677 O  O   . HOH H 4 .   ? -41.870 -36.999 -35.889 1.00 34.03 ? 770 HOH B O   1 
HETATM 6678 O  O   . HOH H 4 .   ? -41.760 -3.951  -24.245 1.00 57.01 ? 771 HOH B O   1 
HETATM 6679 O  O   . HOH H 4 .   ? -42.995 -48.687 -24.426 1.00 48.03 ? 772 HOH B O   1 
HETATM 6680 O  O   . HOH H 4 .   ? -51.606 -23.948 -14.759 1.00 39.36 ? 773 HOH B O   1 
HETATM 6681 O  O   . HOH H 4 .   ? -34.391 -44.242 -17.384 1.00 44.73 ? 774 HOH B O   1 
HETATM 6682 O  O   . HOH H 4 .   ? -30.195 -20.568 -9.322  1.00 51.64 ? 775 HOH B O   1 
HETATM 6683 O  O   . HOH H 4 .   ? -30.690 -4.631  -41.785 1.00 58.67 ? 776 HOH B O   1 
HETATM 6684 O  O   . HOH H 4 .   ? -53.756 -10.032 -33.304 1.00 35.23 ? 777 HOH B O   1 
HETATM 6685 O  O   . HOH H 4 .   ? -12.133 -23.277 -38.273 1.00 50.07 ? 778 HOH B O   1 
HETATM 6686 O  O   . HOH H 4 .   ? -11.169 -12.931 -22.534 1.00 46.18 ? 779 HOH B O   1 
HETATM 6687 O  O   . HOH H 4 .   ? -33.346 -34.434 -8.393  1.00 56.04 ? 780 HOH B O   1 
HETATM 6688 O  O   . HOH H 4 .   ? -14.123 -17.473 -33.978 1.00 42.86 ? 781 HOH B O   1 
HETATM 6689 O  O   . HOH H 4 .   ? -14.107 -18.771 -20.958 1.00 43.64 ? 782 HOH B O   1 
HETATM 6690 O  O   . HOH H 4 .   ? -13.536 -40.527 -26.293 1.00 31.91 ? 783 HOH B O   1 
HETATM 6691 O  O   . HOH H 4 .   ? -46.494 -20.497 -47.017 1.00 49.06 ? 784 HOH B O   1 
HETATM 6692 O  O   . HOH H 4 .   ? -59.719 -19.154 -15.750 1.00 65.01 ? 785 HOH B O   1 
HETATM 6693 O  O   . HOH H 4 .   ? -13.655 -17.535 -30.298 1.00 33.97 ? 786 HOH B O   1 
HETATM 6694 O  O   . HOH H 4 .   ? -58.738 -10.208 -28.136 1.00 46.45 ? 787 HOH B O   1 
HETATM 6695 O  O   . HOH H 4 .   ? -38.689 -37.405 -15.545 1.00 38.60 ? 788 HOH B O   1 
HETATM 6696 O  O   . HOH H 4 .   ? -24.763 -26.574 -5.428  1.00 47.65 ? 789 HOH B O   1 
HETATM 6697 O  O   . HOH H 4 .   ? -48.495 -32.820 -34.530 1.00 48.08 ? 790 HOH B O   1 
HETATM 6698 O  O   A HOH H 4 .   ? -30.786 -16.946 -36.119 0.50 36.98 ? 791 HOH B O   1 
HETATM 6699 O  O   B HOH H 4 .   ? -30.877 -16.597 -37.735 0.50 28.50 ? 791 HOH B O   1 
HETATM 6700 O  O   . HOH H 4 .   ? -34.822 -45.396 -40.911 1.00 53.62 ? 792 HOH B O   1 
HETATM 6701 O  O   . HOH H 4 .   ? -5.307  -26.578 -4.513  1.00 51.04 ? 793 HOH B O   1 
HETATM 6702 O  O   . HOH H 4 .   ? -1.907  -44.099 -11.248 1.00 56.46 ? 794 HOH B O   1 
HETATM 6703 O  O   . HOH H 4 .   ? -37.775 -20.402 -44.998 1.00 44.15 ? 795 HOH B O   1 
HETATM 6704 O  O   . HOH H 4 .   ? -44.055 -3.816  -23.335 1.00 51.12 ? 796 HOH B O   1 
HETATM 6705 O  O   . HOH H 4 .   ? -16.819 -18.913 -35.214 1.00 56.85 ? 797 HOH B O   1 
HETATM 6706 O  O   . HOH H 4 .   ? -38.307 -47.200 -15.358 1.00 64.66 ? 798 HOH B O   1 
HETATM 6707 O  O   . HOH H 4 .   ? -24.865 -15.609 -15.741 1.00 42.30 ? 799 HOH B O   1 
HETATM 6708 O  O   . HOH H 4 .   ? -46.745 -29.161 -11.996 1.00 59.51 ? 800 HOH B O   1 
HETATM 6709 O  O   . HOH H 4 .   ? -58.937 -12.352 -38.014 1.00 56.77 ? 801 HOH B O   1 
HETATM 6710 O  O   . HOH H 4 .   ? -29.151 -16.692 -42.532 1.00 48.59 ? 802 HOH B O   1 
HETATM 6711 O  O   . HOH H 4 .   ? -32.601 -15.732 -12.298 1.00 53.60 ? 803 HOH B O   1 
HETATM 6712 O  O   . HOH H 4 .   ? -33.564 -43.032 -41.524 1.00 58.77 ? 804 HOH B O   1 
HETATM 6713 O  O   . HOH H 4 .   ? -35.019 -21.664 -14.436 1.00 29.06 ? 805 HOH B O   1 
HETATM 6714 O  O   . HOH H 4 .   ? -35.268 -30.106 -11.915 1.00 47.45 ? 806 HOH B O   1 
HETATM 6715 O  O   . HOH H 4 .   ? -18.334 -45.866 -25.715 1.00 50.35 ? 807 HOH B O   1 
HETATM 6716 O  O   . HOH H 4 .   ? -44.309 -27.247 -11.893 1.00 42.82 ? 808 HOH B O   1 
HETATM 6717 O  O   . HOH H 4 .   ? -35.910 -42.906 -40.578 1.00 44.16 ? 809 HOH B O   1 
HETATM 6718 O  O   . HOH H 4 .   ? -56.414 -29.691 -29.288 1.00 41.58 ? 810 HOH B O   1 
HETATM 6719 O  O   . HOH H 4 .   ? -52.334 -7.753  -21.849 1.00 50.65 ? 811 HOH B O   1 
HETATM 6720 O  O   . HOH H 4 .   ? -10.789 -44.307 -9.855  1.00 46.80 ? 812 HOH B O   1 
HETATM 6721 O  O   . HOH H 4 .   ? -15.953 -44.917 -14.366 1.00 52.70 ? 813 HOH B O   1 
HETATM 6722 O  O   . HOH H 4 .   ? -60.086 -18.897 -32.326 1.00 43.00 ? 814 HOH B O   1 
HETATM 6723 O  O   . HOH H 4 .   ? -32.289 -42.208 -43.974 1.00 50.37 ? 815 HOH B O   1 
HETATM 6724 O  O   . HOH H 4 .   ? -48.370 -37.397 -15.858 1.00 60.94 ? 816 HOH B O   1 
HETATM 6725 O  O   . HOH H 4 .   ? -28.425 -42.373 -20.530 1.00 39.30 ? 817 HOH B O   1 
HETATM 6726 O  O   . HOH H 4 .   ? -43.615 -31.728 -45.687 1.00 44.85 ? 818 HOH B O   1 
HETATM 6727 O  O   . HOH H 4 .   ? -46.774 -1.654  -29.677 1.00 41.69 ? 819 HOH B O   1 
HETATM 6728 O  O   . HOH H 4 .   ? -15.976 -41.197 -26.890 1.00 38.54 ? 820 HOH B O   1 
HETATM 6729 O  O   . HOH H 4 .   ? -35.306 -24.091 -15.131 1.00 49.99 ? 821 HOH B O   1 
HETATM 6730 O  O   . HOH H 4 .   ? -8.521  -12.661 -23.694 1.00 45.26 ? 822 HOH B O   1 
HETATM 6731 O  O   . HOH H 4 .   ? -60.013 -27.350 -29.287 1.00 46.00 ? 823 HOH B O   1 
HETATM 6732 O  O   . HOH H 4 .   ? -17.740 -39.822 -8.659  1.00 42.06 ? 824 HOH B O   1 
HETATM 6733 O  O   . HOH H 4 .   ? -59.829 -14.085 -22.654 1.00 49.82 ? 825 HOH B O   1 
HETATM 6734 O  O   . HOH H 4 .   ? -12.127 -20.828 -39.387 1.00 46.06 ? 826 HOH B O   1 
HETATM 6735 O  O   . HOH H 4 .   ? -50.954 -18.941 -45.771 1.00 41.92 ? 827 HOH B O   1 
HETATM 6736 O  O   . HOH H 4 .   ? -21.827 -38.399 -45.154 1.00 45.44 ? 828 HOH B O   1 
HETATM 6737 O  O   . HOH H 4 .   ? -30.059 -43.563 -23.726 1.00 41.12 ? 829 HOH B O   1 
HETATM 6738 O  O   . HOH H 4 .   ? -49.306 -20.925 -46.571 1.00 41.09 ? 830 HOH B O   1 
HETATM 6739 O  O   . HOH H 4 .   ? -18.635 -42.150 -9.526  1.00 42.64 ? 831 HOH B O   1 
HETATM 6740 O  O   . HOH H 4 .   ? -53.752 -9.991  -21.841 1.00 46.05 ? 832 HOH B O   1 
HETATM 6741 O  O   . HOH H 4 .   ? -32.104 -42.205 -18.454 1.00 47.15 ? 833 HOH B O   1 
HETATM 6742 O  O   . HOH H 4 .   ? -26.051 -43.470 -20.512 1.00 34.47 ? 834 HOH B O   1 
HETATM 6743 O  O   . HOH H 4 .   ? -39.174 -8.492  -22.649 1.00 46.13 ? 835 HOH B 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   . MET A 1   ? 1.1209 1.3108 0.6973 -0.2071 0.1366  0.2005  10  MET A N   
2    C CA  . MET A 1   ? 1.0701 1.2470 0.6759 -0.1918 0.1160  0.1814  10  MET A CA  
3    C C   . MET A 1   ? 1.0236 1.1862 0.6893 -0.1822 0.1040  0.1918  10  MET A C   
4    O O   . MET A 1   ? 1.0352 1.1908 0.7133 -0.1886 0.1027  0.2191  10  MET A O   
5    C CB  . MET A 1   ? 1.0930 1.2680 0.6633 -0.1944 0.0888  0.1874  10  MET A CB  
6    C CG  . MET A 1   ? 1.1532 1.3379 0.6618 -0.2062 0.0964  0.1670  10  MET A CG  
7    S SD  . MET A 1   ? 1.1652 1.3576 0.6358 -0.2144 0.0600  0.1770  10  MET A SD  
8    C CE  . MET A 1   ? 1.2123 1.4171 0.6609 -0.2248 0.0475  0.2288  10  MET A CE  
9    N N   . ILE A 2   ? 0.9683 1.1237 0.6671 -0.1686 0.0966  0.1691  11  ILE A N   
10   C CA  . ILE A 2   ? 0.9176 1.0561 0.6649 -0.1601 0.0823  0.1742  11  ILE A CA  
11   C C   . ILE A 2   ? 0.9212 1.0440 0.6614 -0.1563 0.0569  0.1947  11  ILE A C   
12   O O   . ILE A 2   ? 0.9336 1.0639 0.6440 -0.1554 0.0444  0.1933  11  ILE A O   
13   C CB  . ILE A 2   ? 0.8677 1.0054 0.6467 -0.1468 0.0815  0.1446  11  ILE A CB  
14   C CG1 . ILE A 2   ? 0.8601 1.0165 0.6583 -0.1470 0.1066  0.1311  11  ILE A CG1 
15   C CG2 . ILE A 2   ? 0.8243 0.9425 0.6433 -0.1393 0.0645  0.1479  11  ILE A CG2 
16   C CD1 . ILE A 2   ? 0.8294 0.9886 0.6498 -0.1331 0.1097  0.1039  11  ILE A CD1 
17   N N   . SER A 3   ? 0.9064 1.0078 0.6751 -0.1546 0.0504  0.2136  12  SER A N   
18   C CA  . SER A 3   ? 0.9072 0.9909 0.6769 -0.1469 0.0305  0.2375  12  SER A CA  
19   C C   . SER A 3   ? 0.8605 0.9447 0.6425 -0.1318 0.0129  0.2222  12  SER A C   
20   O O   . SER A 3   ? 0.8055 0.8891 0.6095 -0.1260 0.0152  0.1947  12  SER A O   
21   C CB  . SER A 3   ? 0.9339 0.9848 0.7334 -0.1473 0.0326  0.2554  12  SER A CB  
22   O OG  . SER A 3   ? 0.9861 1.0161 0.7906 -0.1353 0.0172  0.2793  12  SER A OG  
23   N N   . LYS A 4   ? 0.8581 0.9469 0.6274 -0.1261 -0.0050 0.2433  13  LYS A N   
24   C CA  . LYS A 4   ? 0.8056 0.9025 0.5865 -0.1137 -0.0228 0.2341  13  LYS A CA  
25   C C   . LYS A 4   ? 0.7388 0.8095 0.5649 -0.0980 -0.0253 0.2287  13  LYS A C   
26   O O   . LYS A 4   ? 0.7167 0.7938 0.5578 -0.0886 -0.0343 0.2125  13  LYS A O   
27   C CB  . LYS A 4   ? 0.8407 0.9577 0.6008 -0.1126 -0.0423 0.2643  13  LYS A CB  
28   C CG  . LYS A 4   ? 0.8795 1.0269 0.5867 -0.1309 -0.0440 0.2615  13  LYS A CG  
29   C CD  . LYS A 4   ? 0.9178 1.0904 0.6042 -0.1326 -0.0661 0.2970  13  LYS A CD  
30   C CE  . LYS A 4   ? 0.9595 1.1611 0.5845 -0.1557 -0.0678 0.2931  13  LYS A CE  
31   N NZ  . LYS A 4   ? 1.0004 1.2337 0.6029 -0.1604 -0.0928 0.3307  13  LYS A NZ  
32   N N   . GLU A 5   ? 0.7280 0.7679 0.5728 -0.0972 -0.0161 0.2413  14  GLU A N   
33   C CA  . GLU A 5   ? 0.7042 0.7125 0.5849 -0.0860 -0.0145 0.2328  14  GLU A CA  
34   C C   . GLU A 5   ? 0.6529 0.6631 0.5494 -0.0882 -0.0086 0.1967  14  GLU A C   
35   O O   . GLU A 5   ? 0.6365 0.6273 0.5572 -0.0788 -0.0101 0.1857  14  GLU A O   
36   C CB  . GLU A 5   ? 0.7532 0.7228 0.6425 -0.0909 -0.0037 0.2520  14  GLU A CB  
37   C CG  . GLU A 5   ? 0.7532 0.7198 0.6382 -0.1113 0.0118  0.2432  14  GLU A CG  
38   C CD  . GLU A 5   ? 0.7962 0.7275 0.6809 -0.1211 0.0213  0.2690  14  GLU A CD  
39   O OE1 . GLU A 5   ? 0.8182 0.7096 0.7163 -0.1105 0.0202  0.2828  14  GLU A OE1 
40   O OE2 . GLU A 5   ? 0.8120 0.7536 0.6834 -0.1394 0.0320  0.2755  14  GLU A OE2 
41   N N   . TYR A 6   ? 0.6206 0.6535 0.5034 -0.0995 -0.0003 0.1801  15  TYR A N   
42   C CA  . TYR A 6   ? 0.5790 0.6191 0.4777 -0.0997 0.0051  0.1502  15  TYR A CA  
43   C C   . TYR A 6   ? 0.5517 0.6100 0.4447 -0.0917 -0.0027 0.1311  15  TYR A C   
44   O O   . TYR A 6   ? 0.5333 0.5953 0.4399 -0.0895 0.0012  0.1091  15  TYR A O   
45   C CB  . TYR A 6   ? 0.5638 0.6192 0.4584 -0.1128 0.0213  0.1438  15  TYR A CB  
46   C CG  . TYR A 6   ? 0.6093 0.6492 0.5128 -0.1255 0.0299  0.1602  15  TYR A CG  
47   C CD1 . TYR A 6   ? 0.6076 0.6216 0.5360 -0.1281 0.0286  0.1572  15  TYR A CD1 
48   C CD2 . TYR A 6   ? 0.5632 0.6129 0.4472 -0.1377 0.0403  0.1777  15  TYR A CD2 
49   C CE1 . TYR A 6   ? 0.6052 0.6012 0.5393 -0.1442 0.0367  0.1706  15  TYR A CE1 
50   C CE2 . TYR A 6   ? 0.6379 0.6726 0.5305 -0.1523 0.0488  0.1936  15  TYR A CE2 
51   C CZ  . TYR A 6   ? 0.6246 0.6314 0.5427 -0.1564 0.0465  0.1895  15  TYR A CZ  
52   O OH  . TYR A 6   ? 0.6326 0.6209 0.5569 -0.1751 0.0550  0.2035  15  TYR A OH  
53   N N   . HIS A 7   ? 0.5844 0.6550 0.4574 -0.0892 -0.0141 0.1410  16  HIS A N   
54   C CA  . HIS A 7   ? 0.5659 0.6521 0.4328 -0.0855 -0.0233 0.1240  16  HIS A CA  
55   C C   . HIS A 7   ? 0.5390 0.6325 0.3969 -0.0904 -0.0111 0.0962  16  HIS A C   
56   O O   . HIS A 7   ? 0.4838 0.5751 0.3563 -0.0844 -0.0123 0.0768  16  HIS A O   
57   C CB  . HIS A 7   ? 0.5524 0.6291 0.4496 -0.0719 -0.0337 0.1220  16  HIS A CB  
58   C CG  . HIS A 7   ? 0.6359 0.7057 0.5436 -0.0629 -0.0430 0.1502  16  HIS A CG  
59   N ND1 . HIS A 7   ? 0.7273 0.7672 0.6591 -0.0544 -0.0377 0.1588  16  HIS A ND1 
60   C CD2 . HIS A 7   ? 0.7056 0.7942 0.6024 -0.0609 -0.0564 0.1739  16  HIS A CD2 
61   C CE1 . HIS A 7   ? 0.7165 0.7531 0.6545 -0.0442 -0.0449 0.1865  16  HIS A CE1 
62   N NE2 . HIS A 7   ? 0.7353 0.8052 0.6546 -0.0473 -0.0577 0.1982  16  HIS A NE2 
63   N N   . ILE A 8   ? 0.5493 0.6503 0.3835 -0.1001 0.0026  0.0965  17  ILE A N   
64   C CA  . ILE A 8   ? 0.5427 0.6496 0.3653 -0.1028 0.0191  0.0736  17  ILE A CA  
65   C C   . ILE A 8   ? 0.5599 0.6760 0.3354 -0.1133 0.0187  0.0693  17  ILE A C   
66   O O   . ILE A 8   ? 0.5960 0.7201 0.3435 -0.1231 0.0193  0.0860  17  ILE A O   
67   C CB  . ILE A 8   ? 0.5433 0.6545 0.3757 -0.1060 0.0391  0.0767  17  ILE A CB  
68   C CG1 . ILE A 8   ? 0.5278 0.6326 0.4043 -0.1001 0.0380  0.0765  17  ILE A CG1 
69   C CG2 . ILE A 8   ? 0.5713 0.6910 0.3883 -0.1063 0.0607  0.0568  17  ILE A CG2 
70   C CD1 . ILE A 8   ? 0.5224 0.6343 0.4140 -0.1080 0.0510  0.0879  17  ILE A CD1 
71   N N   . ASP A 9   ? 0.5558 0.6692 0.3202 -0.1136 0.0175  0.0471  18  ASP A N   
72   C CA  . ASP A 9   ? 0.5989 0.7170 0.3137 -0.1280 0.0173  0.0370  18  ASP A CA  
73   C C   . ASP A 9   ? 0.6218 0.7347 0.3068 -0.1335 0.0456  0.0208  18  ASP A C   
74   O O   . ASP A 9   ? 0.6008 0.7065 0.3102 -0.1224 0.0653  0.0092  18  ASP A O   
75   C CB  . ASP A 9   ? 0.5930 0.7056 0.3073 -0.1292 0.0067  0.0181  18  ASP A CB  
76   C CG  . ASP A 9   ? 0.6419 0.7610 0.3032 -0.1498 -0.0002 0.0100  18  ASP A CG  
77   O OD1 . ASP A 9   ? 0.7264 0.8669 0.3753 -0.1588 -0.0218 0.0314  18  ASP A OD1 
78   O OD2 . ASP A 9   ? 0.6793 0.7819 0.3108 -0.1576 0.0165  -0.0168 18  ASP A OD2 
79   N N   . GLU A 10  ? 0.6925 0.8113 0.3243 -0.1504 0.0480  0.0209  19  GLU A N   
80   C CA  . GLU A 10  ? 0.7405 0.8525 0.3359 -0.1566 0.0781  0.0042  19  GLU A CA  
81   C C   . GLU A 10  ? 0.7545 0.8429 0.3450 -0.1516 0.0972  -0.0300 19  GLU A C   
82   O O   . GLU A 10  ? 0.7713 0.8514 0.3641 -0.1430 0.1279  -0.0425 19  GLU A O   
83   C CB  . GLU A 10  ? 0.8051 0.9270 0.3357 -0.1795 0.0745  0.0101  19  GLU A CB  
84   C CG  . GLU A 10  ? 0.8588 0.9751 0.3471 -0.1868 0.1087  -0.0034 19  GLU A CG  
85   C CD  . GLU A 10  ? 0.9224 1.0523 0.3447 -0.2112 0.1037  0.0079  19  GLU A CD  
86   O OE1 . GLU A 10  ? 0.9395 1.0784 0.3328 -0.2271 0.0761  0.0129  19  GLU A OE1 
87   O OE2 . GLU A 10  ? 0.9544 1.0898 0.3539 -0.2154 0.1272  0.0134  19  GLU A OE2 
88   N N   . GLU A 11  ? 0.7396 0.8177 0.3266 -0.1559 0.0805  -0.0428 20  GLU A N   
89   C CA  . GLU A 11  ? 0.7581 0.8069 0.3343 -0.1541 0.0978  -0.0745 20  GLU A CA  
90   C C   . GLU A 11  ? 0.6827 0.7231 0.3182 -0.1319 0.0981  -0.0767 20  GLU A C   
91   O O   . GLU A 11  ? 0.7011 0.7237 0.3493 -0.1182 0.1239  -0.0917 20  GLU A O   
92   C CB  . GLU A 11  ? 0.8082 0.8488 0.3398 -0.1774 0.0808  -0.0889 20  GLU A CB  
93   C CG  . GLU A 11  ? 0.8582 0.8590 0.3667 -0.1808 0.1021  -0.1241 20  GLU A CG  
94   C CD  . GLU A 11  ? 0.9111 0.9043 0.3718 -0.2104 0.0844  -0.1395 20  GLU A CD  
95   O OE1 . GLU A 11  ? 0.8915 0.9116 0.3694 -0.2180 0.0506  -0.1224 20  GLU A OE1 
96   O OE2 . GLU A 11  ? 1.0007 0.9607 0.4073 -0.2266 0.1056  -0.1689 20  GLU A OE2 
97   N N   . VAL A 12  ? 0.6217 0.6755 0.2924 -0.1279 0.0705  -0.0610 21  VAL A N   
98   C CA  . VAL A 12  ? 0.5681 0.6146 0.2882 -0.1105 0.0678  -0.0636 21  VAL A CA  
99   C C   . VAL A 12  ? 0.5064 0.5690 0.2762 -0.0948 0.0660  -0.0437 21  VAL A C   
100  O O   . VAL A 12  ? 0.4678 0.5275 0.2760 -0.0820 0.0635  -0.0443 21  VAL A O   
101  C CB  . VAL A 12  ? 0.5435 0.5889 0.2678 -0.1174 0.0431  -0.0659 21  VAL A CB  
102  C CG1 . VAL A 12  ? 0.6313 0.6592 0.3059 -0.1375 0.0460  -0.0882 21  VAL A CG1 
103  C CG2 . VAL A 12  ? 0.5292 0.6007 0.2657 -0.1210 0.0158  -0.0410 21  VAL A CG2 
104  N N   . GLY A 13  ? 0.5181 0.5966 0.2839 -0.0984 0.0675  -0.0263 22  GLY A N   
105  C CA  . GLY A 13  ? 0.4803 0.5716 0.2878 -0.0891 0.0676  -0.0089 22  GLY A CA  
106  C C   . GLY A 13  ? 0.4496 0.5422 0.2868 -0.0855 0.0439  0.0037  22  GLY A C   
107  O O   . GLY A 13  ? 0.4493 0.5445 0.2741 -0.0919 0.0262  0.0153  22  GLY A O   
108  N N   . PHE A 14  ? 0.4201 0.5119 0.2962 -0.0750 0.0442  0.0022  23  PHE A N   
109  C CA  . PHE A 14  ? 0.3993 0.4877 0.3013 -0.0712 0.0256  0.0099  23  PHE A CA  
110  C C   . PHE A 14  ? 0.3880 0.4685 0.2874 -0.0690 0.0132  -0.0004 23  PHE A C   
111  O O   . PHE A 14  ? 0.3336 0.4120 0.2506 -0.0657 -0.0006 0.0059  23  PHE A O   
112  C CB  . PHE A 14  ? 0.3887 0.4807 0.3273 -0.0647 0.0294  0.0107  23  PHE A CB  
113  C CG  . PHE A 14  ? 0.3889 0.4933 0.3376 -0.0698 0.0394  0.0226  23  PHE A CG  
114  C CD1 . PHE A 14  ? 0.4006 0.5010 0.3524 -0.0776 0.0318  0.0385  23  PHE A CD1 
115  C CD2 . PHE A 14  ? 0.3857 0.5054 0.3431 -0.0666 0.0579  0.0190  23  PHE A CD2 
116  C CE1 . PHE A 14  ? 0.3920 0.5033 0.3535 -0.0859 0.0410  0.0498  23  PHE A CE1 
117  C CE2 . PHE A 14  ? 0.4344 0.5722 0.4056 -0.0731 0.0676  0.0316  23  PHE A CE2 
118  C CZ  . PHE A 14  ? 0.3750 0.5084 0.3470 -0.0847 0.0583  0.0466  23  PHE A CZ  
119  N N   . ALA A 15  ? 0.4057 0.4798 0.2833 -0.0717 0.0200  -0.0166 24  ALA A N   
120  C CA  . ALA A 15  ? 0.4224 0.4906 0.2945 -0.0745 0.0082  -0.0256 24  ALA A CA  
121  C C   . ALA A 15  ? 0.4486 0.5293 0.3053 -0.0841 -0.0104 -0.0133 24  ALA A C   
122  O O   . ALA A 15  ? 0.4599 0.5493 0.2939 -0.0918 -0.0112 -0.0028 24  ALA A O   
123  C CB  . ALA A 15  ? 0.4735 0.5261 0.3218 -0.0786 0.0217  -0.0465 24  ALA A CB  
124  N N   . LEU A 16  ? 0.4403 0.5254 0.3118 -0.0830 -0.0253 -0.0118 25  LEU A N   
125  C CA  . LEU A 16  ? 0.4483 0.5527 0.3117 -0.0904 -0.0438 0.0022  25  LEU A CA  
126  C C   . LEU A 16  ? 0.4944 0.6034 0.3158 -0.1099 -0.0459 -0.0092 25  LEU A C   
127  O O   . LEU A 16  ? 0.5145 0.6119 0.3278 -0.1166 -0.0420 -0.0287 25  LEU A O   
128  C CB  . LEU A 16  ? 0.4106 0.5223 0.3054 -0.0832 -0.0560 0.0065  25  LEU A CB  
129  C CG  . LEU A 16  ? 0.4278 0.5665 0.3293 -0.0847 -0.0748 0.0277  25  LEU A CG  
130  C CD1 . LEU A 16  ? 0.4239 0.5643 0.3367 -0.0740 -0.0765 0.0523  25  LEU A CD1 
131  C CD2 . LEU A 16  ? 0.3868 0.5342 0.3190 -0.0782 -0.0819 0.0273  25  LEU A CD2 
132  N N   . PRO A 17  ? 0.5296 0.6530 0.3206 -0.1212 -0.0512 0.0026  26  PRO A N   
133  C CA  . PRO A 17  ? 0.5736 0.7012 0.3179 -0.1443 -0.0542 -0.0102 26  PRO A CA  
134  C C   . PRO A 17  ? 0.5734 0.7226 0.3241 -0.1553 -0.0761 -0.0074 26  PRO A C   
135  O O   . PRO A 17  ? 0.5106 0.6833 0.2963 -0.1448 -0.0920 0.0150  26  PRO A O   
136  C CB  . PRO A 17  ? 0.6162 0.7601 0.3294 -0.1532 -0.0579 0.0077  26  PRO A CB  
137  C CG  . PRO A 17  ? 0.5901 0.7450 0.3415 -0.1353 -0.0656 0.0365  26  PRO A CG  
138  C CD  . PRO A 17  ? 0.5258 0.6600 0.3192 -0.1161 -0.0544 0.0279  26  PRO A CD  
139  N N   . ASN A 18  ? 0.6252 0.7647 0.3438 -0.1760 -0.0744 -0.0304 27  ASN A N   
140  C CA  . ASN A 18  ? 0.6202 0.7820 0.3403 -0.1935 -0.0944 -0.0310 27  ASN A CA  
141  C C   . ASN A 18  ? 0.5725 0.7559 0.3509 -0.1752 -0.1072 -0.0126 27  ASN A C   
142  O O   . ASN A 18  ? 0.5657 0.7890 0.3621 -0.1747 -0.1276 0.0132  27  ASN A O   
143  C CB  . ASN A 18  ? 0.6768 0.8729 0.3575 -0.2192 -0.1143 -0.0188 27  ASN A CB  
144  C CG  . ASN A 18  ? 0.7119 0.9330 0.3835 -0.2465 -0.1345 -0.0238 27  ASN A CG  
145  O OD1 . ASN A 18  ? 0.7409 0.9476 0.4302 -0.2485 -0.1307 -0.0397 27  ASN A OD1 
146  N ND2 . ASN A 18  ? 0.7881 1.0497 0.4318 -0.2696 -0.1568 -0.0082 27  ASN A ND2 
147  N N   . PRO A 19  ? 0.5408 0.6987 0.3489 -0.1588 -0.0937 -0.0242 28  PRO A N   
148  C CA  . PRO A 19  ? 0.5075 0.6817 0.3659 -0.1416 -0.1014 -0.0096 28  PRO A CA  
149  C C   . PRO A 19  ? 0.5115 0.7234 0.3821 -0.1558 -0.1215 -0.0008 28  PRO A C   
150  O O   . PRO A 19  ? 0.5058 0.7203 0.3472 -0.1824 -0.1268 -0.0152 28  PRO A O   
151  C CB  . PRO A 19  ? 0.5018 0.6410 0.3744 -0.1308 -0.0836 -0.0287 28  PRO A CB  
152  C CG  . PRO A 19  ? 0.5162 0.6241 0.3599 -0.1307 -0.0651 -0.0439 28  PRO A CG  
153  C CD  . PRO A 19  ? 0.5245 0.6392 0.3219 -0.1540 -0.0697 -0.0489 28  PRO A CD  
154  N N   . GLN A 20  ? 0.4809 0.7213 0.3947 -0.1389 -0.1310 0.0226  29  GLN A N   
155  C CA  . GLN A 20  ? 0.5074 0.7924 0.4449 -0.1480 -0.1490 0.0358  29  GLN A CA  
156  C C   . GLN A 20  ? 0.4943 0.7652 0.4450 -0.1530 -0.1412 0.0166  29  GLN A C   
157  O O   . GLN A 20  ? 0.4554 0.6926 0.4196 -0.1357 -0.1242 0.0059  29  GLN A O   
158  C CB  . GLN A 20  ? 0.5047 0.8206 0.4884 -0.1229 -0.1559 0.0674  29  GLN A CB  
159  C CG  . GLN A 20  ? 0.4989 0.8757 0.5089 -0.1310 -0.1773 0.0905  29  GLN A CG  
160  C CD  . GLN A 20  ? 0.5111 0.9159 0.5643 -0.1024 -0.1817 0.1259  29  GLN A CD  
161  O OE1 . GLN A 20  ? 0.5091 0.9043 0.5523 -0.0913 -0.1813 0.1410  29  GLN A OE1 
162  N NE2 . GLN A 20  ? 0.5113 0.9493 0.6137 -0.0897 -0.1838 0.1401  29  GLN A NE2 
163  N N   . GLU A 21  ? 0.5013 0.7995 0.4469 -0.1789 -0.1544 0.0136  30  GLU A N   
164  C CA  . GLU A 21  ? 0.5464 0.8303 0.4987 -0.1900 -0.1475 -0.0043 30  GLU A CA  
165  C C   . GLU A 21  ? 0.5172 0.8447 0.5214 -0.1827 -0.1553 0.0137  30  GLU A C   
166  O O   . GLU A 21  ? 0.4917 0.8020 0.5155 -0.1750 -0.1429 0.0052  30  GLU A O   
167  C CB  . GLU A 21  ? 0.6027 0.8787 0.5093 -0.2288 -0.1533 -0.0244 30  GLU A CB  
168  C CG  . GLU A 21  ? 0.6522 0.8868 0.5501 -0.2400 -0.1383 -0.0492 30  GLU A CG  
169  C CD  . GLU A 21  ? 0.7292 0.9429 0.5756 -0.2794 -0.1398 -0.0727 30  GLU A CD  
170  O OE1 . GLU A 21  ? 0.8703 1.0625 0.7148 -0.2959 -0.1333 -0.0875 30  GLU A OE1 
171  O OE2 . GLU A 21  ? 0.7198 0.9353 0.5249 -0.2954 -0.1461 -0.0769 30  GLU A OE2 
172  N N   . ASN A 22  ? 0.5256 0.9116 0.5526 -0.1841 -0.1747 0.0405  31  ASN A N   
173  C CA  . ASN A 22  ? 0.5007 0.9386 0.5816 -0.1762 -0.1819 0.0618  31  ASN A CA  
174  C C   . ASN A 22  ? 0.4664 0.9271 0.5877 -0.1403 -0.1812 0.0912  31  ASN A C   
175  O O   . ASN A 22  ? 0.4580 0.9240 0.5665 -0.1340 -0.1891 0.1060  31  ASN A O   
176  C CB  . ASN A 22  ? 0.5437 1.0409 0.6238 -0.2105 -0.2066 0.0722  31  ASN A CB  
177  C CG  . ASN A 22  ? 0.6012 1.0711 0.6383 -0.2502 -0.2064 0.0417  31  ASN A CG  
178  O OD1 . ASN A 22  ? 0.6627 1.0961 0.7019 -0.2507 -0.1899 0.0227  31  ASN A OD1 
179  N ND2 . ASN A 22  ? 0.6891 1.1736 0.6841 -0.2846 -0.2237 0.0373  31  ASN A ND2 
180  N N   . LEU A 23  ? 0.4276 0.8976 0.5950 -0.1172 -0.1695 0.0995  32  LEU A N   
181  C CA  . LEU A 23  ? 0.4166 0.9042 0.6260 -0.0818 -0.1645 0.1267  32  LEU A CA  
182  C C   . LEU A 23  ? 0.4180 0.9845 0.6710 -0.0832 -0.1829 0.1595  32  LEU A C   
183  O O   . LEU A 23  ? 0.4347 1.0413 0.6880 -0.1132 -0.1978 0.1577  32  LEU A O   
184  C CB  . LEU A 23  ? 0.3945 0.8500 0.6284 -0.0562 -0.1394 0.1172  32  LEU A CB  
185  C CG  . LEU A 23  ? 0.3927 0.7780 0.5947 -0.0463 -0.1216 0.0942  32  LEU A CG  
186  C CD1 . LEU A 23  ? 0.3659 0.7266 0.5856 -0.0303 -0.1001 0.0828  32  LEU A CD1 
187  C CD2 . LEU A 23  ? 0.4057 0.7726 0.6018 -0.0275 -0.1205 0.1077  32  LEU A CD2 
188  N N   . PRO A 24  ? 0.4047 0.9948 0.6956 -0.0517 -0.1820 0.1912  33  PRO A N   
189  C CA  . PRO A 24  ? 0.4075 1.0782 0.7540 -0.0450 -0.1956 0.2270  33  PRO A CA  
190  C C   . PRO A 24  ? 0.3876 1.0855 0.7737 -0.0460 -0.1852 0.2220  33  PRO A C   
191  O O   . PRO A 24  ? 0.3673 1.0154 0.7490 -0.0353 -0.1609 0.1980  33  PRO A O   
192  C CB  . PRO A 24  ? 0.4124 1.0782 0.7928 -0.0017 -0.1846 0.2563  33  PRO A CB  
193  C CG  . PRO A 24  ? 0.3975 0.9969 0.7275 -0.0001 -0.1792 0.2416  33  PRO A CG  
194  C CD  . PRO A 24  ? 0.3925 0.9375 0.6787 -0.0214 -0.1684 0.1978  33  PRO A CD  
195  N N   . ASP A 25  ? 0.3829 1.1623 0.8059 -0.0612 -0.2044 0.2454  34  ASP A N   
196  C CA  . ASP A 25  ? 0.3756 1.1947 0.8406 -0.0668 -0.1969 0.2451  34  ASP A CA  
197  C C   . ASP A 25  ? 0.3565 1.1523 0.8613 -0.0250 -0.1634 0.2460  34  ASP A C   
198  O O   . ASP A 25  ? 0.3417 1.1271 0.8534 -0.0304 -0.1469 0.2279  34  ASP A O   
199  C CB  . ASP A 25  ? 0.3813 1.3063 0.8965 -0.0799 -0.2225 0.2826  34  ASP A CB  
200  C CG  . ASP A 25  ? 0.4288 1.3838 0.9021 -0.1329 -0.2558 0.2765  34  ASP A CG  
201  O OD1 . ASP A 25  ? 0.4815 1.3724 0.8875 -0.1585 -0.2560 0.2416  34  ASP A OD1 
202  O OD2 . ASP A 25  ? 0.5083 1.5534 1.0165 -0.1496 -0.2814 0.3074  34  ASP A OD2 
203  N N   . PHE A 26  ? 0.3610 1.1458 0.8886 0.0152  -0.1524 0.2671  35  PHE A N   
204  C CA  . PHE A 26  ? 0.3523 1.1007 0.9076 0.0558  -0.1173 0.2646  35  PHE A CA  
205  C C   . PHE A 26  ? 0.3140 0.9867 0.8269 0.0486  -0.0951 0.2220  35  PHE A C   
206  O O   . PHE A 26  ? 0.2987 0.9647 0.8342 0.0638  -0.0701 0.2147  35  PHE A O   
207  C CB  . PHE A 26  ? 0.3724 1.0906 0.9338 0.0924  -0.1091 0.2840  35  PHE A CB  
208  C CG  . PHE A 26  ? 0.3797 1.0699 0.9770 0.1355  -0.0730 0.2878  35  PHE A CG  
209  C CD1 . PHE A 26  ? 0.4262 1.1789 1.0948 0.1650  -0.0638 0.3229  35  PHE A CD1 
210  C CD2 . PHE A 26  ? 0.3958 0.9981 0.9553 0.1459  -0.0471 0.2564  35  PHE A CD2 
211  C CE1 . PHE A 26  ? 0.4342 1.1549 1.1331 0.2061  -0.0256 0.3240  35  PHE A CE1 
212  C CE2 . PHE A 26  ? 0.4212 0.9918 1.0061 0.1822  -0.0119 0.2562  35  PHE A CE2 
213  C CZ  . PHE A 26  ? 0.4280 1.0541 1.0813 0.2133  0.0007  0.2887  35  PHE A CZ  
214  N N   . TYR A 27  ? 0.3154 0.9358 0.7678 0.0254  -0.1042 0.1959  36  TYR A N   
215  C CA  . TYR A 27  ? 0.3111 0.8624 0.7219 0.0181  -0.0868 0.1593  36  TYR A CA  
216  C C   . TYR A 27  ? 0.3014 0.8576 0.6905 -0.0184 -0.0942 0.1386  36  TYR A C   
217  O O   . TYR A 27  ? 0.3048 0.8049 0.6522 -0.0292 -0.0866 0.1110  36  TYR A O   
218  C CB  . TYR A 27  ? 0.3213 0.8098 0.6838 0.0193  -0.0879 0.1451  36  TYR A CB  
219  C CG  . TYR A 27  ? 0.3289 0.8023 0.7081 0.0525  -0.0786 0.1640  36  TYR A CG  
220  C CD1 . TYR A 27  ? 0.3263 0.7562 0.7134 0.0793  -0.0505 0.1560  36  TYR A CD1 
221  C CD2 . TYR A 27  ? 0.3719 0.8726 0.7569 0.0557  -0.0972 0.1906  36  TYR A CD2 
222  C CE1 . TYR A 27  ? 0.3672 0.7747 0.7680 0.1089  -0.0392 0.1724  36  TYR A CE1 
223  C CE2 . TYR A 27  ? 0.3524 0.8346 0.7538 0.0872  -0.0871 0.2109  36  TYR A CE2 
224  C CZ  . TYR A 27  ? 0.3757 0.8085 0.7854 0.1137  -0.0573 0.2009  36  TYR A CZ  
225  O OH  . TYR A 27  ? 0.3961 0.8024 0.8194 0.1432  -0.0451 0.2194  36  TYR A OH  
226  N N   . ASN A 28  ? 0.3197 0.9429 0.7387 -0.0375 -0.1086 0.1535  37  ASN A N   
227  C CA  . ASN A 28  ? 0.3335 0.9608 0.7345 -0.0747 -0.1144 0.1356  37  ASN A CA  
228  C C   . ASN A 28  ? 0.3161 0.8999 0.7080 -0.0704 -0.0892 0.1139  37  ASN A C   
229  O O   . ASN A 28  ? 0.3211 0.8656 0.6737 -0.0946 -0.0895 0.0908  37  ASN A O   
230  C CB  . ASN A 28  ? 0.3403 1.0539 0.7847 -0.0950 -0.1310 0.1582  37  ASN A CB  
231  C CG  . ASN A 28  ? 0.4275 1.1802 0.8578 -0.1222 -0.1636 0.1702  37  ASN A CG  
232  O OD1 . ASN A 28  ? 0.5076 1.2155 0.8836 -0.1381 -0.1730 0.1525  37  ASN A OD1 
233  N ND2 . ASN A 28  ? 0.4266 1.2672 0.9061 -0.1285 -0.1806 0.2014  37  ASN A ND2 
234  N N   . ASP A 29  ? 0.3120 0.9006 0.7380 -0.0394 -0.0663 0.1219  38  ASP A N   
235  C CA  . ASP A 29  ? 0.3169 0.8662 0.7314 -0.0342 -0.0412 0.1029  38  ASP A CA  
236  C C   . ASP A 29  ? 0.3142 0.7852 0.6732 -0.0349 -0.0355 0.0768  38  ASP A C   
237  O O   . ASP A 29  ? 0.3400 0.7805 0.6750 -0.0477 -0.0266 0.0596  38  ASP A O   
238  C CB  . ASP A 29  ? 0.3182 0.8811 0.7731 0.0011  -0.0148 0.1144  38  ASP A CB  
239  C CG  . ASP A 29  ? 0.3177 0.9632 0.8352 0.0040  -0.0147 0.1411  38  ASP A CG  
240  O OD1 . ASP A 29  ? 0.3438 1.0346 0.8710 -0.0276 -0.0325 0.1466  38  ASP A OD1 
241  O OD2 . ASP A 29  ? 0.3552 1.0202 0.9136 0.0378  0.0047  0.1570  38  ASP A OD2 
242  N N   . TRP A 30  ? 0.3188 0.7608 0.6599 -0.0212 -0.0405 0.0765  39  TRP A N   
243  C CA  . TRP A 30  ? 0.2997 0.6771 0.5915 -0.0249 -0.0389 0.0547  39  TRP A CA  
244  C C   . TRP A 30  ? 0.2831 0.6504 0.5427 -0.0561 -0.0551 0.0427  39  TRP A C   
245  O O   . TRP A 30  ? 0.2834 0.6108 0.5137 -0.0659 -0.0487 0.0250  39  TRP A O   
246  C CB  . TRP A 30  ? 0.3058 0.6598 0.5880 -0.0068 -0.0414 0.0593  39  TRP A CB  
247  C CG  . TRP A 30  ? 0.3257 0.6706 0.6303 0.0245  -0.0226 0.0674  39  TRP A CG  
248  C CD1 . TRP A 30  ? 0.3308 0.6817 0.6589 0.0396  -0.0009 0.0678  39  TRP A CD1 
249  C CD2 . TRP A 30  ? 0.3256 0.6466 0.6272 0.0437  -0.0207 0.0748  39  TRP A CD2 
250  N NE1 . TRP A 30  ? 0.3012 0.6302 0.6401 0.0677  0.0155  0.0732  39  TRP A NE1 
251  C CE2 . TRP A 30  ? 0.3103 0.6196 0.6340 0.0704  0.0032  0.0784  39  TRP A CE2 
252  C CE3 . TRP A 30  ? 0.3248 0.6310 0.6055 0.0403  -0.0352 0.0788  39  TRP A CE3 
253  C CZ2 . TRP A 30  ? 0.3529 0.6320 0.6788 0.0931  0.0130  0.0857  39  TRP A CZ2 
254  C CZ3 . TRP A 30  ? 0.3146 0.5953 0.5988 0.0622  -0.0269 0.0880  39  TRP A CZ3 
255  C CH2 . TRP A 30  ? 0.3610 0.6264 0.6680 0.0881  -0.0031 0.0914  39  TRP A CH2 
256  N N   . MET A 31  ? 0.2997 0.7022 0.5636 -0.0713 -0.0753 0.0534  40  MET A N   
257  C CA  . MET A 31  ? 0.3359 0.7263 0.5647 -0.1029 -0.0896 0.0406  40  MET A CA  
258  C C   . MET A 31  ? 0.3516 0.7361 0.5743 -0.1266 -0.0850 0.0288  40  MET A C   
259  O O   . MET A 31  ? 0.3580 0.6965 0.5431 -0.1413 -0.0827 0.0101  40  MET A O   
260  C CB  . MET A 31  ? 0.3846 0.8232 0.6196 -0.1190 -0.1128 0.0558  40  MET A CB  
261  C CG  . MET A 31  ? 0.4498 0.8792 0.6690 -0.1066 -0.1212 0.0629  40  MET A CG  
262  S SD  . MET A 31  ? 0.5340 0.8908 0.6949 -0.1107 -0.1153 0.0372  40  MET A SD  
263  C CE  . MET A 31  ? 0.4681 0.8048 0.5949 -0.1483 -0.1178 0.0140  40  MET A CE  
264  N N   . PHE A 32  ? 0.3320 0.7619 0.5927 -0.1295 -0.0817 0.0410  41  PHE A N   
265  C CA  . PHE A 32  ? 0.3443 0.7705 0.6020 -0.1534 -0.0759 0.0325  41  PHE A CA  
266  C C   . PHE A 32  ? 0.3357 0.7000 0.5648 -0.1453 -0.0578 0.0156  41  PHE A C   
267  O O   . PHE A 32  ? 0.3467 0.6770 0.5479 -0.1667 -0.0569 0.0026  41  PHE A O   
268  C CB  . PHE A 32  ? 0.3606 0.8473 0.6685 -0.1529 -0.0703 0.0502  41  PHE A CB  
269  C CG  . PHE A 32  ? 0.3828 0.8670 0.6870 -0.1814 -0.0647 0.0434  41  PHE A CG  
270  C CD1 . PHE A 32  ? 0.4192 0.8692 0.7155 -0.1724 -0.0431 0.0357  41  PHE A CD1 
271  C CD2 . PHE A 32  ? 0.4524 0.9654 0.7565 -0.2201 -0.0812 0.0445  41  PHE A CD2 
272  C CE1 . PHE A 32  ? 0.4230 0.8671 0.7142 -0.1990 -0.0371 0.0319  41  PHE A CE1 
273  C CE2 . PHE A 32  ? 0.4800 0.9848 0.7791 -0.2490 -0.0748 0.0384  41  PHE A CE2 
274  C CZ  . PHE A 32  ? 0.4660 0.9355 0.7597 -0.2370 -0.0522 0.0332  41  PHE A CZ  
275  N N   . ILE A 33  ? 0.3225 0.6720 0.5580 -0.1154 -0.0436 0.0169  42  ILE A N   
276  C CA  . ILE A 33  ? 0.3177 0.6173 0.5280 -0.1075 -0.0283 0.0043  42  ILE A CA  
277  C C   . ILE A 33  ? 0.3222 0.5715 0.4923 -0.1115 -0.0338 -0.0096 42  ILE A C   
278  O O   . ILE A 33  ? 0.3531 0.5683 0.5003 -0.1228 -0.0291 -0.0186 42  ILE A O   
279  C CB  . ILE A 33  ? 0.3074 0.6036 0.5295 -0.0783 -0.0123 0.0071  42  ILE A CB  
280  C CG1 . ILE A 33  ? 0.2972 0.6397 0.5589 -0.0728 -0.0005 0.0196  42  ILE A CG1 
281  C CG2 . ILE A 33  ? 0.3022 0.5503 0.4928 -0.0739 -0.0004 -0.0052 42  ILE A CG2 
282  C CD1 . ILE A 33  ? 0.3039 0.6473 0.5815 -0.0427 0.0163  0.0233  42  ILE A CD1 
283  N N   . ALA A 34  ? 0.3178 0.5637 0.4815 -0.1013 -0.0421 -0.0092 43  ALA A N   
284  C CA  . ALA A 34  ? 0.3307 0.5343 0.4600 -0.1029 -0.0450 -0.0210 43  ALA A CA  
285  C C   . ALA A 34  ? 0.3584 0.5465 0.4647 -0.1292 -0.0512 -0.0306 43  ALA A C   
286  O O   . ALA A 34  ? 0.3958 0.5410 0.4759 -0.1309 -0.0451 -0.0416 43  ALA A O   
287  C CB  . ALA A 34  ? 0.3379 0.5464 0.4663 -0.0898 -0.0523 -0.0164 43  ALA A CB  
288  N N   . LYS A 35  ? 0.3417 0.5644 0.4581 -0.1500 -0.0623 -0.0260 44  LYS A N   
289  C CA  . LYS A 35  ? 0.4011 0.6065 0.4915 -0.1805 -0.0675 -0.0377 44  LYS A CA  
290  C C   . LYS A 35  ? 0.4078 0.5849 0.4913 -0.1946 -0.0561 -0.0444 44  LYS A C   
291  O O   . LYS A 35  ? 0.4082 0.5478 0.4625 -0.2145 -0.0538 -0.0576 44  LYS A O   
292  C CB  . LYS A 35  ? 0.3988 0.6551 0.5005 -0.2036 -0.0856 -0.0299 44  LYS A CB  
293  C CG  . LYS A 35  ? 0.4370 0.7094 0.5301 -0.1974 -0.0986 -0.0251 44  LYS A CG  
294  C CD  . LYS A 35  ? 0.4823 0.8176 0.5925 -0.2180 -0.1194 -0.0109 44  LYS A CD  
295  C CE  . LYS A 35  ? 0.4905 0.8225 0.5630 -0.2364 -0.1337 -0.0172 44  LYS A CE  
296  N NZ  . LYS A 35  ? 0.4993 0.9019 0.5916 -0.2519 -0.1572 0.0030  44  LYS A NZ  
297  N N   . HIS A 36  ? 0.4106 0.6028 0.5189 -0.1847 -0.0471 -0.0351 45  HIS A N   
298  C CA  . HIS A 36  ? 0.4245 0.5945 0.5284 -0.1984 -0.0361 -0.0370 45  HIS A CA  
299  C C   . HIS A 36  ? 0.4096 0.5506 0.5091 -0.1755 -0.0214 -0.0350 45  HIS A C   
300  O O   . HIS A 36  ? 0.4062 0.5468 0.5125 -0.1799 -0.0117 -0.0293 45  HIS A O   
301  C CB  . HIS A 36  ? 0.4254 0.6472 0.5611 -0.2157 -0.0388 -0.0258 45  HIS A CB  
302  C CG  . HIS A 36  ? 0.4943 0.7527 0.6354 -0.2425 -0.0563 -0.0251 45  HIS A CG  
303  N ND1 . HIS A 36  ? 0.5116 0.8163 0.6714 -0.2333 -0.0702 -0.0157 45  HIS A ND1 
304  C CD2 . HIS A 36  ? 0.5284 0.7838 0.6563 -0.2805 -0.0630 -0.0319 45  HIS A CD2 
305  C CE1 . HIS A 36  ? 0.5178 0.8524 0.6761 -0.2646 -0.0867 -0.0153 45  HIS A CE1 
306  N NE2 . HIS A 36  ? 0.5553 0.8601 0.6931 -0.2953 -0.0826 -0.0267 45  HIS A NE2 
307  N N   . LEU A 37  ? 0.3918 0.5102 0.4783 -0.1537 -0.0204 -0.0388 46  LEU A N   
308  C CA  . LEU A 37  ? 0.3764 0.4727 0.4569 -0.1349 -0.0099 -0.0361 46  LEU A CA  
309  C C   . LEU A 37  ? 0.4081 0.4670 0.4726 -0.1436 -0.0006 -0.0356 46  LEU A C   
310  O O   . LEU A 37  ? 0.4127 0.4738 0.4807 -0.1395 0.0076  -0.0275 46  LEU A O   
311  C CB  . LEU A 37  ? 0.3802 0.4604 0.4496 -0.1149 -0.0121 -0.0398 46  LEU A CB  
312  C CG  . LEU A 37  ? 0.3362 0.4436 0.4202 -0.0990 -0.0163 -0.0368 46  LEU A CG  
313  C CD1 . LEU A 37  ? 0.3344 0.4198 0.4041 -0.0846 -0.0173 -0.0406 46  LEU A CD1 
314  C CD2 . LEU A 37  ? 0.3434 0.4710 0.4434 -0.0893 -0.0078 -0.0304 46  LEU A CD2 
315  N N   . PRO A 38  ? 0.4205 0.4426 0.4655 -0.1552 0.0001  -0.0436 47  PRO A N   
316  C CA  . PRO A 38  ? 0.4427 0.4231 0.4739 -0.1607 0.0112  -0.0405 47  PRO A CA  
317  C C   . PRO A 38  ? 0.4452 0.4381 0.4865 -0.1763 0.0167  -0.0312 47  PRO A C   
318  O O   . PRO A 38  ? 0.4203 0.4018 0.4590 -0.1682 0.0250  -0.0203 47  PRO A O   
319  C CB  . PRO A 38  ? 0.4678 0.4099 0.4782 -0.1764 0.0128  -0.0538 47  PRO A CB  
320  C CG  . PRO A 38  ? 0.4875 0.4438 0.4947 -0.1676 0.0039  -0.0624 47  PRO A CG  
321  C CD  . PRO A 38  ? 0.4347 0.4473 0.4663 -0.1633 -0.0069 -0.0555 47  PRO A CD  
322  N N   A ASP A 39  ? 0.4557 0.4768 0.5090 -0.1995 0.0115  -0.0337 48  ASP A N   
323  N N   B ASP A 39  ? 0.4540 0.4751 0.5073 -0.1995 0.0114  -0.0339 48  ASP A N   
324  C CA  A ASP A 39  ? 0.4651 0.5048 0.5320 -0.2178 0.0173  -0.0243 48  ASP A CA  
325  C CA  B ASP A 39  ? 0.4587 0.5006 0.5265 -0.2182 0.0167  -0.0246 48  ASP A CA  
326  C C   A ASP A 39  ? 0.4194 0.5024 0.5080 -0.2018 0.0216  -0.0131 48  ASP A C   
327  C C   B ASP A 39  ? 0.4151 0.4970 0.5031 -0.2010 0.0215  -0.0132 48  ASP A C   
328  O O   A ASP A 39  ? 0.4345 0.5158 0.5235 -0.2051 0.0324  -0.0031 48  ASP A O   
329  O O   B ASP A 39  ? 0.4293 0.5063 0.5159 -0.2031 0.0325  -0.0034 48  ASP A O   
330  C CB  A ASP A 39  ? 0.4811 0.5461 0.5579 -0.2502 0.0090  -0.0292 48  ASP A CB  
331  C CB  B ASP A 39  ? 0.4608 0.5348 0.5412 -0.2480 0.0070  -0.0291 48  ASP A CB  
332  C CG  A ASP A 39  ? 0.5677 0.5791 0.6154 -0.2755 0.0105  -0.0419 48  ASP A CG  
333  C CG  B ASP A 39  ? 0.4918 0.6015 0.5954 -0.2676 0.0120  -0.0176 48  ASP A CG  
334  O OD1 A ASP A 39  ? 0.6137 0.5674 0.6371 -0.2638 0.0198  -0.0462 48  ASP A OD1 
335  O OD1 B ASP A 39  ? 0.5054 0.5854 0.5994 -0.2761 0.0244  -0.0115 48  ASP A OD1 
336  O OD2 A ASP A 39  ? 0.6537 0.6816 0.7033 -0.3079 0.0029  -0.0474 48  ASP A OD2 
337  O OD2 B ASP A 39  ? 0.4876 0.6575 0.6212 -0.2740 0.0042  -0.0125 48  ASP A OD2 
338  N N   . LEU A 40  ? 0.3844 0.5026 0.4886 -0.1847 0.0151  -0.0147 49  LEU A N   
339  C CA  . LEU A 40  ? 0.3651 0.5179 0.4872 -0.1679 0.0228  -0.0071 49  LEU A CA  
340  C C   . LEU A 40  ? 0.3530 0.4787 0.4542 -0.1499 0.0317  -0.0049 49  LEU A C   
341  O O   . LEU A 40  ? 0.3492 0.4893 0.4530 -0.1468 0.0432  0.0017  49  LEU A O   
342  C CB  . LEU A 40  ? 0.3356 0.5247 0.4787 -0.1528 0.0157  -0.0086 49  LEU A CB  
343  C CG  . LEU A 40  ? 0.3360 0.5703 0.5070 -0.1682 0.0056  -0.0048 49  LEU A CG  
344  C CD1 . LEU A 40  ? 0.3473 0.6064 0.5334 -0.1487 -0.0029 -0.0038 49  LEU A CD1 
345  C CD2 . LEU A 40  ? 0.3493 0.6275 0.5503 -0.1786 0.0149  0.0065  49  LEU A CD2 
346  N N   . ILE A 41  ? 0.3503 0.4406 0.4307 -0.1396 0.0265  -0.0096 50  ILE A N   
347  C CA  . ILE A 41  ? 0.3832 0.4527 0.4443 -0.1260 0.0313  -0.0048 50  ILE A CA  
348  C C   . ILE A 41  ? 0.4066 0.4557 0.4560 -0.1376 0.0397  0.0065  50  ILE A C   
349  O O   . ILE A 41  ? 0.4413 0.4979 0.4828 -0.1350 0.0475  0.0148  50  ILE A O   
350  C CB  . ILE A 41  ? 0.3953 0.4381 0.4428 -0.1127 0.0237  -0.0092 50  ILE A CB  
351  C CG1 . ILE A 41  ? 0.3630 0.4247 0.4188 -0.1001 0.0170  -0.0178 50  ILE A CG1 
352  C CG2 . ILE A 41  ? 0.3744 0.4006 0.4042 -0.1030 0.0265  0.0004  50  ILE A CG2 
353  C CD1 . ILE A 41  ? 0.3582 0.3994 0.4054 -0.0915 0.0096  -0.0228 50  ILE A CD1 
354  N N   . GLU A 42  ? 0.4436 0.4638 0.4888 -0.1513 0.0392  0.0066  51  GLU A N   
355  C CA  . GLU A 42  ? 0.4622 0.4524 0.4953 -0.1622 0.0480  0.0190  51  GLU A CA  
356  C C   . GLU A 42  ? 0.4720 0.4889 0.5130 -0.1762 0.0574  0.0282  51  GLU A C   
357  O O   . GLU A 42  ? 0.4770 0.4856 0.5050 -0.1752 0.0653  0.0423  51  GLU A O   
358  C CB  . GLU A 42  ? 0.4797 0.4309 0.5075 -0.1783 0.0486  0.0132  51  GLU A CB  
359  C CG  . GLU A 42  ? 0.5659 0.4683 0.5781 -0.1831 0.0592  0.0268  51  GLU A CG  
360  C CD  . GLU A 42  ? 0.6842 0.5928 0.6985 -0.2040 0.0684  0.0393  51  GLU A CD  
361  O OE1 . GLU A 42  ? 0.7775 0.7167 0.8067 -0.2251 0.0677  0.0332  51  GLU A OE1 
362  O OE2 . GLU A 42  ? 0.8088 0.6945 0.8112 -0.1998 0.0764  0.0577  51  GLU A OE2 
363  N N   . SER A 43  ? 0.4456 0.4988 0.5089 -0.1893 0.0565  0.0221  52  SER A N   
364  C CA  . SER A 43  ? 0.4607 0.5473 0.5383 -0.2033 0.0672  0.0310  52  SER A CA  
365  C C   . SER A 43  ? 0.4316 0.5535 0.5137 -0.1857 0.0752  0.0328  52  SER A C   
366  O O   . SER A 43  ? 0.4147 0.5683 0.5101 -0.1937 0.0872  0.0393  52  SER A O   
367  C CB  . SER A 43  ? 0.4449 0.5637 0.5497 -0.2251 0.0627  0.0264  52  SER A CB  
368  O OG  . SER A 43  ? 0.4223 0.5735 0.5451 -0.2116 0.0528  0.0174  52  SER A OG  
369  N N   . GLY A 44  ? 0.4318 0.5471 0.5021 -0.1634 0.0704  0.0262  53  GLY A N   
370  C CA  . GLY A 44  ? 0.4258 0.5655 0.4944 -0.1486 0.0796  0.0238  53  GLY A CA  
371  C C   . GLY A 44  ? 0.4036 0.5881 0.5056 -0.1450 0.0853  0.0191  53  GLY A C   
372  O O   . GLY A 44  ? 0.4074 0.6148 0.5129 -0.1388 0.1012  0.0200  53  GLY A O   
373  N N   . GLN A 45  ? 0.4021 0.6001 0.5281 -0.1487 0.0733  0.0152  54  GLN A N   
374  C CA  . GLN A 45  ? 0.3844 0.6299 0.5477 -0.1426 0.0753  0.0151  54  GLN A CA  
375  C C   . GLN A 45  ? 0.3586 0.6025 0.5240 -0.1192 0.0694  0.0066  54  GLN A C   
376  O O   . GLN A 45  ? 0.3567 0.6348 0.5503 -0.1062 0.0758  0.0084  54  GLN A O   
377  C CB  . GLN A 45  ? 0.3895 0.6584 0.5780 -0.1639 0.0631  0.0188  54  GLN A CB  
378  C CG  . GLN A 45  ? 0.4182 0.6967 0.6130 -0.1912 0.0698  0.0279  54  GLN A CG  
379  C CD  . GLN A 45  ? 0.4489 0.7476 0.6632 -0.2171 0.0553  0.0289  54  GLN A CD  
380  O OE1 . GLN A 45  ? 0.5065 0.8592 0.7575 -0.2176 0.0503  0.0339  54  GLN A OE1 
381  N NE2 . GLN A 45  ? 0.4687 0.7238 0.6579 -0.2390 0.0486  0.0246  54  GLN A NE2 
382  N N   . LEU A 46  ? 0.3494 0.5545 0.4877 -0.1131 0.0586  -0.0007 55  LEU A N   
383  C CA  . LEU A 46  ? 0.3393 0.5404 0.4794 -0.0954 0.0507  -0.0078 55  LEU A CA  
384  C C   . LEU A 46  ? 0.3479 0.5571 0.4908 -0.0758 0.0655  -0.0112 55  LEU A C   
385  O O   . LEU A 46  ? 0.3415 0.5706 0.5083 -0.0624 0.0663  -0.0106 55  LEU A O   
386  C CB  . LEU A 46  ? 0.3576 0.5174 0.4681 -0.0936 0.0395  -0.0137 55  LEU A CB  
387  C CG  . LEU A 46  ? 0.3331 0.4836 0.4413 -0.0795 0.0299  -0.0204 55  LEU A CG  
388  C CD1 . LEU A 46  ? 0.3839 0.5257 0.4805 -0.0635 0.0383  -0.0257 55  LEU A CD1 
389  C CD2 . LEU A 46  ? 0.3193 0.4980 0.4546 -0.0791 0.0220  -0.0182 55  LEU A CD2 
390  N N   . ARG A 47  ? 0.3627 0.5543 0.4790 -0.0747 0.0777  -0.0142 56  ARG A N   
391  C CA  . ARG A 47  ? 0.3786 0.5649 0.4852 -0.0589 0.0931  -0.0224 56  ARG A CA  
392  C C   . ARG A 47  ? 0.3804 0.6014 0.5196 -0.0491 0.1125  -0.0190 56  ARG A C   
393  O O   . ARG A 47  ? 0.3660 0.5873 0.5165 -0.0307 0.1210  -0.0237 56  ARG A O   
394  C CB  . ARG A 47  ? 0.3979 0.5596 0.4624 -0.0648 0.1006  -0.0266 56  ARG A CB  
395  C CG  . ARG A 47  ? 0.4060 0.5372 0.4429 -0.0668 0.0832  -0.0299 56  ARG A CG  
396  C CD  . ARG A 47  ? 0.4332 0.5495 0.4322 -0.0767 0.0851  -0.0272 56  ARG A CD  
397  N NE  . ARG A 47  ? 0.4088 0.5039 0.3839 -0.0757 0.0714  -0.0310 56  ARG A NE  
398  C CZ  . ARG A 47  ? 0.4497 0.5353 0.3932 -0.0841 0.0661  -0.0254 56  ARG A CZ  
399  N NH1 . ARG A 47  ? 0.4892 0.5799 0.4163 -0.0939 0.0738  -0.0156 56  ARG A NH1 
400  N NH2 . ARG A 47  ? 0.4398 0.5141 0.3687 -0.0835 0.0524  -0.0273 56  ARG A NH2 
401  N N   . GLU A 48  ? 0.3860 0.6361 0.5424 -0.0608 0.1206  -0.0094 57  GLU A N   
402  C CA  . GLU A 48  ? 0.3979 0.6910 0.5937 -0.0513 0.1401  -0.0027 57  GLU A CA  
403  C C   . GLU A 48  ? 0.3686 0.6938 0.6095 -0.0410 0.1285  0.0055  57  GLU A C   
404  O O   . GLU A 48  ? 0.3429 0.6895 0.6129 -0.0197 0.1438  0.0086  57  GLU A O   
405  C CB  . GLU A 48  ? 0.3869 0.7093 0.5943 -0.0698 0.1499  0.0081  57  GLU A CB  
406  C CG  . GLU A 48  ? 0.4312 0.8048 0.6836 -0.0588 0.1731  0.0167  57  GLU A CG  
407  C CD  . GLU A 48  ? 0.4634 0.8610 0.7182 -0.0753 0.1915  0.0249  57  GLU A CD  
408  O OE1 . GLU A 48  ? 0.5664 0.9598 0.8108 -0.1011 0.1791  0.0315  57  GLU A OE1 
409  O OE2 . GLU A 48  ? 0.4962 0.9153 0.7637 -0.0620 0.2206  0.0252  57  GLU A OE2 
410  N N   . ARG A 49  ? 0.3371 0.6639 0.5819 -0.0555 0.1030  0.0095  58  ARG A N   
411  C CA  . ARG A 49  ? 0.3370 0.6941 0.6168 -0.0497 0.0874  0.0182  58  ARG A CA  
412  C C   . ARG A 49  ? 0.3254 0.6626 0.6029 -0.0240 0.0885  0.0136  58  ARG A C   
413  O O   . ARG A 49  ? 0.3111 0.6802 0.6265 -0.0064 0.0925  0.0245  58  ARG A O   
414  C CB  . ARG A 49  ? 0.3371 0.6869 0.6060 -0.0728 0.0612  0.0182  58  ARG A CB  
415  C CG  . ARG A 49  ? 0.3969 0.7681 0.6740 -0.1015 0.0581  0.0245  58  ARG A CG  
416  C CD  . ARG A 49  ? 0.4520 0.8811 0.7717 -0.1134 0.0459  0.0380  58  ARG A CD  
417  N NE  . ARG A 49  ? 0.4689 0.9051 0.7858 -0.1483 0.0379  0.0399  58  ARG A NE  
418  C CZ  . ARG A 49  ? 0.4596 0.9422 0.8043 -0.1706 0.0229  0.0494  58  ARG A CZ  
419  N NH1 . ARG A 49  ? 0.5049 1.0377 0.8858 -0.1597 0.0126  0.0613  58  ARG A NH1 
420  N NH2 . ARG A 49  ? 0.4722 0.9506 0.8076 -0.2055 0.0178  0.0483  58  ARG A NH2 
421  N N   . VAL A 50  ? 0.3168 0.6027 0.5521 -0.0224 0.0850  -0.0003 59  VAL A N   
422  C CA  . VAL A 50  ? 0.3296 0.5889 0.5568 -0.0020 0.0878  -0.0065 59  VAL A CA  
423  C C   . VAL A 50  ? 0.3556 0.6143 0.5927 0.0192  0.1170  -0.0092 59  VAL A C   
424  O O   . VAL A 50  ? 0.3608 0.6203 0.6186 0.0406  0.1239  -0.0049 59  VAL A O   
425  C CB  . VAL A 50  ? 0.3304 0.5393 0.5105 -0.0087 0.0789  -0.0205 59  VAL A CB  
426  C CG1 . VAL A 50  ? 0.3830 0.5618 0.5524 0.0086  0.0846  -0.0280 59  VAL A CG1 
427  C CG2 . VAL A 50  ? 0.3274 0.5328 0.4998 -0.0242 0.0544  -0.0183 59  VAL A CG2 
428  N N   . GLU A 51  ? 0.3652 0.6196 0.5853 0.0134  0.1358  -0.0158 60  GLU A N   
429  C CA  . GLU A 51  ? 0.4003 0.6515 0.6242 0.0317  0.1684  -0.0213 60  GLU A CA  
430  C C   . GLU A 51  ? 0.3946 0.6983 0.6782 0.0497  0.1827  -0.0042 60  GLU A C   
431  O O   . GLU A 51  ? 0.4085 0.7064 0.7056 0.0741  0.2094  -0.0063 60  GLU A O   
432  C CB  . GLU A 51  ? 0.4267 0.6649 0.6141 0.0178  0.1844  -0.0313 60  GLU A CB  
433  C CG  . GLU A 51  ? 0.4382 0.6255 0.5669 0.0056  0.1759  -0.0474 60  GLU A CG  
434  C CD  . GLU A 51  ? 0.4229 0.6065 0.5168 -0.0157 0.1768  -0.0487 60  GLU A CD  
435  O OE1 . GLU A 51  ? 0.4112 0.6246 0.5203 -0.0207 0.1904  -0.0406 60  GLU A OE1 
436  O OE2 . GLU A 51  ? 0.4271 0.5800 0.4798 -0.0277 0.1633  -0.0555 60  GLU A OE2 
437  N N   . LYS A 52  ? 0.3742 0.7286 0.6937 0.0372  0.1657  0.0130  61  LYS A N   
438  C CA  . LYS A 52  ? 0.3848 0.8027 0.7677 0.0507  0.1741  0.0340  61  LYS A CA  
439  C C   . LYS A 52  ? 0.3727 0.8125 0.7911 0.0652  0.1555  0.0499  61  LYS A C   
440  O O   . LYS A 52  ? 0.3702 0.8674 0.8455 0.0794  0.1602  0.0715  61  LYS A O   
441  C CB  . LYS A 52  ? 0.3835 0.8514 0.7877 0.0248  0.1663  0.0456  61  LYS A CB  
442  C CG  . LYS A 52  ? 0.4020 0.8576 0.7781 0.0116  0.1875  0.0359  61  LYS A CG  
443  C CD  . LYS A 52  ? 0.4551 0.9362 0.8580 0.0326  0.2256  0.0393  61  LYS A CD  
444  C CE  . LYS A 52  ? 0.4523 0.9195 0.8193 0.0158  0.2451  0.0299  61  LYS A CE  
445  N NZ  . LYS A 52  ? 0.5311 1.0187 0.9169 0.0359  0.2870  0.0301  61  LYS A NZ  
446  N N   . LEU A 53  ? 0.3651 0.7636 0.7519 0.0619  0.1351  0.0418  62  LEU A N   
447  C CA  . LEU A 53  ? 0.3547 0.7662 0.7665 0.0761  0.1189  0.0568  62  LEU A CA  
448  C C   . LEU A 53  ? 0.3626 0.7714 0.8044 0.1133  0.1443  0.0653  62  LEU A C   
449  O O   . LEU A 53  ? 0.3413 0.7082 0.7619 0.1270  0.1732  0.0493  62  LEU A O   
450  C CB  . LEU A 53  ? 0.3639 0.7243 0.7306 0.0666  0.0981  0.0441  62  LEU A CB  
451  C CG  . LEU A 53  ? 0.3980 0.7602 0.7417 0.0358  0.0689  0.0406  62  LEU A CG  
452  C CD1 . LEU A 53  ? 0.4541 0.7602 0.7520 0.0317  0.0586  0.0254  62  LEU A CD1 
453  C CD2 . LEU A 53  ? 0.4280 0.8455 0.8073 0.0284  0.0463  0.0614  62  LEU A CD2 
454  N N   . ASN A 54  ? 0.3672 0.8194 0.8562 0.1287  0.1335  0.0911  63  ASN A N   
455  C CA  . ASN A 54  ? 0.3994 0.8417 0.9171 0.1666  0.1534  0.1036  63  ASN A CA  
456  C C   . ASN A 54  ? 0.3994 0.7843 0.8811 0.1692  0.1406  0.0963  63  ASN A C   
457  O O   . ASN A 54  ? 0.3717 0.7564 0.8306 0.1460  0.1096  0.0952  63  ASN A O   
458  C CB  . ASN A 54  ? 0.3971 0.9200 0.9869 0.1828  0.1458  0.1407  63  ASN A CB  
459  C CG  . ASN A 54  ? 0.4377 1.0243 1.0731 0.1837  0.1626  0.1515  63  ASN A CG  
460  O OD1 . ASN A 54  ? 0.4524 1.0163 1.0787 0.1927  0.1961  0.1357  63  ASN A OD1 
461  N ND2 . ASN A 54  ? 0.4598 1.1291 1.1436 0.1724  0.1395  0.1788  63  ASN A ND2 
462  N N   . MET A 55  ? 0.4477 0.7819 0.9232 0.1963  0.1667  0.0908  64  MET A N   
463  C CA  . MET A 55  ? 0.4614 0.7406 0.9073 0.2001  0.1579  0.0867  64  MET A CA  
464  C C   . MET A 55  ? 0.4289 0.7519 0.9155 0.2114  0.1353  0.1206  64  MET A C   
465  O O   . MET A 55  ? 0.4148 0.7751 0.9562 0.2408  0.1478  0.1476  64  MET A O   
466  C CB  . MET A 55  ? 0.5179 0.7292 0.9481 0.2248  0.1942  0.0728  64  MET A CB  
467  C CG  . MET A 55  ? 0.5303 0.6741 0.9161 0.2183  0.1860  0.0606  64  MET A CG  
468  S SD  . MET A 55  ? 0.6574 0.7161 1.0243 0.2444  0.2294  0.0447  64  MET A SD  
469  C CE  . MET A 55  ? 0.7140 0.7416 1.0328 0.2259  0.2535  0.0060  64  MET A CE  
470  N N   . LEU A 56  ? 0.3806 0.7021 0.8408 0.1881  0.1028  0.1206  65  LEU A N   
471  C CA  . LEU A 56  ? 0.3751 0.7390 0.8630 0.1920  0.0772  0.1516  65  LEU A CA  
472  C C   . LEU A 56  ? 0.3869 0.6955 0.8518 0.2031  0.0768  0.1540  65  LEU A C   
473  O O   . LEU A 56  ? 0.3973 0.6454 0.8118 0.1888  0.0784  0.1280  65  LEU A O   
474  C CB  . LEU A 56  ? 0.3415 0.7465 0.8147 0.1560  0.0423  0.1508  65  LEU A CB  
475  C CG  . LEU A 56  ? 0.3219 0.7864 0.8197 0.1396  0.0384  0.1524  65  LEU A CG  
476  C CD1 . LEU A 56  ? 0.3402 0.8268 0.8125 0.1014  0.0056  0.1473  65  LEU A CD1 
477  C CD2 . LEU A 56  ? 0.3531 0.8908 0.9210 0.1620  0.0438  0.1864  65  LEU A CD2 
478  N N   . SER A 57  ? 0.3995 0.7321 0.9042 0.2286  0.0750  0.1879  66  SER A N   
479  C CA  . SER A 57  ? 0.4348 0.7203 0.9234 0.2400  0.0739  0.1973  66  SER A CA  
480  C C   . SER A 57  ? 0.4279 0.7164 0.8776 0.2083  0.0400  0.1939  66  SER A C   
481  O O   . SER A 57  ? 0.3985 0.7466 0.8553 0.1884  0.0134  0.2032  66  SER A O   
482  C CB  . SER A 57  ? 0.4481 0.7690 0.9945 0.2759  0.0780  0.2413  66  SER A CB  
483  O OG  . SER A 57  ? 0.4580 0.7295 0.9892 0.2877  0.0790  0.2532  66  SER A OG  
484  N N   . ILE A 58  ? 0.4543 0.6782 0.8623 0.2026  0.0426  0.1800  67  ILE A N   
485  C CA  . ILE A 58  ? 0.4316 0.6534 0.8025 0.1762  0.0155  0.1775  67  ILE A CA  
486  C C   . ILE A 58  ? 0.4471 0.6952 0.8347 0.1859  -0.0017 0.2148  67  ILE A C   
487  O O   . ILE A 58  ? 0.4343 0.6844 0.7911 0.1648  -0.0229 0.2154  67  ILE A O   
488  C CB  . ILE A 58  ? 0.4475 0.5958 0.7676 0.1624  0.0246  0.1475  67  ILE A CB  
489  C CG1 . ILE A 58  ? 0.4807 0.5698 0.8007 0.1844  0.0462  0.1547  67  ILE A CG1 
490  C CG2 . ILE A 58  ? 0.4406 0.5690 0.7400 0.1493  0.0369  0.1135  67  ILE A CG2 
491  C CD1 . ILE A 58  ? 0.4803 0.5135 0.7537 0.1652  0.0446  0.1366  67  ILE A CD1 
492  N N   . ASP A 59  ? 0.4871 0.7561 0.9230 0.2185  0.0086  0.2471  68  ASP A N   
493  C CA  . ASP A 59  ? 0.5170 0.8040 0.9702 0.2330  -0.0043 0.2874  68  ASP A CA  
494  C C   . ASP A 59  ? 0.5042 0.8697 0.9625 0.2127  -0.0414 0.3105  68  ASP A C   
495  O O   . ASP A 59  ? 0.5269 0.9030 0.9793 0.2130  -0.0579 0.3379  68  ASP A O   
496  C CB  . ASP A 59  ? 0.5555 0.8456 1.0649 0.2774  0.0189  0.3193  68  ASP A CB  
497  C CG  . ASP A 59  ? 0.6025 0.8036 1.1001 0.2972  0.0582  0.2973  68  ASP A CG  
498  O OD1 . ASP A 59  ? 0.6047 0.7417 1.0499 0.2761  0.0633  0.2640  68  ASP A OD1 
499  O OD2 . ASP A 59  ? 0.6984 0.8947 1.2396 0.3336  0.0849  0.3137  68  ASP A OD2 
500  N N   . HIS A 60  ? 0.4709 0.8886 0.9361 0.1925  -0.0541 0.2990  69  HIS A N   
501  C CA  . HIS A 60  ? 0.4632 0.9530 0.9262 0.1659  -0.0893 0.3147  69  HIS A CA  
502  C C   . HIS A 60  ? 0.4418 0.9077 0.8408 0.1262  -0.1056 0.2837  69  HIS A C   
503  O O   . HIS A 60  ? 0.4334 0.9476 0.8187 0.0983  -0.1320 0.2877  69  HIS A O   
504  C CB  . HIS A 60  ? 0.4410 1.0026 0.9480 0.1627  -0.0946 0.3218  69  HIS A CB  
505  C CG  . HIS A 60  ? 0.4575 1.0431 1.0307 0.2040  -0.0733 0.3498  69  HIS A CG  
506  N ND1 . HIS A 60  ? 0.5172 1.1415 1.1344 0.2322  -0.0791 0.3977  69  HIS A ND1 
507  C CD2 . HIS A 60  ? 0.4499 1.0242 1.0524 0.2239  -0.0436 0.3375  69  HIS A CD2 
508  C CE1 . HIS A 60  ? 0.5357 1.1714 1.2101 0.2697  -0.0526 0.4137  69  HIS A CE1 
509  N NE2 . HIS A 60  ? 0.5168 1.1220 1.1817 0.2646  -0.0299 0.3763  69  HIS A NE2 
510  N N   . LEU A 61  ? 0.4446 0.8368 0.8050 0.1231  -0.0888 0.2531  70  LEU A N   
511  C CA  . LEU A 61  ? 0.4486 0.8129 0.7526 0.0934  -0.0999 0.2299  70  LEU A CA  
512  C C   . LEU A 61  ? 0.4830 0.8311 0.7724 0.1000  -0.1057 0.2532  70  LEU A C   
513  O O   . LEU A 61  ? 0.5254 0.8149 0.8017 0.1113  -0.0884 0.2470  70  LEU A O   
514  C CB  . LEU A 61  ? 0.4320 0.7341 0.7079 0.0877  -0.0801 0.1907  70  LEU A CB  
515  C CG  . LEU A 61  ? 0.3872 0.6998 0.6749 0.0822  -0.0719 0.1692  70  LEU A CG  
516  C CD1 . LEU A 61  ? 0.4051 0.6566 0.6717 0.0843  -0.0500 0.1389  70  LEU A CD1 
517  C CD2 . LEU A 61  ? 0.3697 0.7166 0.6380 0.0507  -0.0918 0.1577  70  LEU A CD2 
518  N N   . THR A 62  ? 0.4906 0.8923 0.7807 0.0904  -0.1305 0.2810  71  THR A N   
519  C CA  . THR A 62  ? 0.5229 0.9237 0.8130 0.1034  -0.1367 0.3164  71  THR A CA  
520  C C   . THR A 62  ? 0.5218 0.8850 0.7563 0.0831  -0.1404 0.3050  71  THR A C   
521  O O   . THR A 62  ? 0.5517 0.8990 0.7824 0.0945  -0.1397 0.3311  71  THR A O   
522  C CB  . THR A 62  ? 0.5338 1.0163 0.8528 0.1046  -0.1631 0.3597  71  THR A CB  
523  O OG1 . THR A 62  ? 0.5768 1.0997 0.8586 0.0657  -0.1889 0.3490  71  THR A OG1 
524  C CG2 . THR A 62  ? 0.5196 1.0478 0.9027 0.1278  -0.1579 0.3766  71  THR A CG2 
525  N N   . ASP A 63  ? 0.4909 0.8399 0.6843 0.0544  -0.1425 0.2685  72  ASP A N   
526  C CA  . ASP A 63  ? 0.4970 0.8115 0.6401 0.0361  -0.1418 0.2550  72  ASP A CA  
527  C C   . ASP A 63  ? 0.4641 0.7309 0.5836 0.0254  -0.1253 0.2125  72  ASP A C   
528  O O   . ASP A 63  ? 0.4422 0.7046 0.5781 0.0280  -0.1173 0.1921  72  ASP A O   
529  C CB  . ASP A 63  ? 0.5123 0.8708 0.6206 0.0085  -0.1661 0.2631  72  ASP A CB  
530  C CG  . ASP A 63  ? 0.5038 0.8979 0.6044 -0.0156 -0.1784 0.2419  72  ASP A CG  
531  O OD1 . ASP A 63  ? 0.4037 0.7768 0.5103 -0.0173 -0.1663 0.2119  72  ASP A OD1 
532  O OD2 . ASP A 63  ? 0.5704 1.0137 0.6557 -0.0356 -0.2011 0.2562  72  ASP A OD2 
533  N N   . HIS A 64  ? 0.4770 0.7121 0.5596 0.0135  -0.1203 0.2022  73  HIS A N   
534  C CA  . HIS A 64  ? 0.4565 0.6506 0.5183 0.0041  -0.1054 0.1676  73  HIS A CA  
535  C C   . HIS A 64  ? 0.4306 0.6373 0.4804 -0.0130 -0.1086 0.1388  73  HIS A C   
536  O O   . HIS A 64  ? 0.4233 0.6072 0.4806 -0.0101 -0.0968 0.1167  73  HIS A O   
537  C CB  . HIS A 64  ? 0.4530 0.6249 0.4795 -0.0075 -0.1014 0.1669  73  HIS A CB  
538  C CG  . HIS A 64  ? 0.4612 0.5981 0.4730 -0.0153 -0.0864 0.1368  73  HIS A CG  
539  N ND1 . HIS A 64  ? 0.4710 0.5721 0.4996 -0.0047 -0.0717 0.1273  73  HIS A ND1 
540  C CD2 . HIS A 64  ? 0.4598 0.5943 0.4427 -0.0324 -0.0834 0.1151  73  HIS A CD2 
541  C CE1 . HIS A 64  ? 0.4505 0.5350 0.4634 -0.0158 -0.0634 0.1038  73  HIS A CE1 
542  N NE2 . HIS A 64  ? 0.4540 0.5578 0.4418 -0.0304 -0.0689 0.0968  73  HIS A NE2 
543  N N   . LYS A 65  ? 0.4536 0.6937 0.4814 -0.0324 -0.1240 0.1395  74  LYS A N   
544  C CA  . LYS A 65  ? 0.4363 0.6824 0.4490 -0.0510 -0.1259 0.1125  74  LYS A CA  
545  C C   . LYS A 65  ? 0.4163 0.6786 0.4645 -0.0439 -0.1264 0.1092  74  LYS A C   
546  O O   . LYS A 65  ? 0.4075 0.6516 0.4533 -0.0489 -0.1176 0.0847  74  LYS A O   
547  C CB  . LYS A 65  ? 0.4620 0.7381 0.4396 -0.0766 -0.1421 0.1138  74  LYS A CB  
548  C CG  . LYS A 65  ? 0.4785 0.7333 0.4107 -0.0889 -0.1361 0.1059  74  LYS A CG  
549  C CD  . LYS A 65  ? 0.5172 0.7925 0.4063 -0.1185 -0.1476 0.0961  74  LYS A CD  
550  C CE  . LYS A 65  ? 0.5699 0.8229 0.4115 -0.1303 -0.1372 0.0859  74  LYS A CE  
551  N NZ  . LYS A 65  ? 0.5661 0.8275 0.3588 -0.1610 -0.1429 0.0676  74  LYS A NZ  
552  N N   . SER A 66  ? 0.4212 0.7192 0.5040 -0.0312 -0.1357 0.1361  75  SER A N   
553  C CA  . SER A 66  ? 0.4142 0.7307 0.5362 -0.0213 -0.1327 0.1360  75  SER A CA  
554  C C   . SER A 66  ? 0.3868 0.6593 0.5246 -0.0012 -0.1102 0.1225  75  SER A C   
555  O O   . SER A 66  ? 0.3688 0.6385 0.5182 -0.0019 -0.1026 0.1064  75  SER A O   
556  C CB  . SER A 66  ? 0.4087 0.7779 0.5699 -0.0085 -0.1454 0.1716  75  SER A CB  
557  O OG  . SER A 66  ? 0.5165 0.8684 0.6953 0.0179  -0.1372 0.1946  75  SER A OG  
558  N N   . GLN A 67  ? 0.3747 0.6127 0.5099 0.0136  -0.0998 0.1292  76  GLN A N   
559  C CA  . GLN A 67  ? 0.3725 0.5648 0.5137 0.0270  -0.0792 0.1143  76  GLN A CA  
560  C C   . GLN A 67  ? 0.3642 0.5292 0.4775 0.0113  -0.0732 0.0837  76  GLN A C   
561  O O   . GLN A 67  ? 0.3646 0.5117 0.4842 0.0148  -0.0618 0.0675  76  GLN A O   
562  C CB  . GLN A 67  ? 0.4029 0.5623 0.5435 0.0411  -0.0704 0.1286  76  GLN A CB  
563  C CG  . GLN A 67  ? 0.4020 0.5763 0.5779 0.0650  -0.0692 0.1598  76  GLN A CG  
564  C CD  . GLN A 67  ? 0.4554 0.6012 0.6256 0.0748  -0.0650 0.1805  76  GLN A CD  
565  O OE1 . GLN A 67  ? 0.4734 0.5762 0.6192 0.0672  -0.0558 0.1671  76  GLN A OE1 
566  N NE2 . GLN A 67  ? 0.4977 0.6703 0.6928 0.0913  -0.0719 0.2159  76  GLN A NE2 
567  N N   . ARG A 68  ? 0.3523 0.5158 0.4349 -0.0054 -0.0799 0.0773  77  ARG A N   
568  C CA  . ARG A 68  ? 0.3559 0.4984 0.4157 -0.0181 -0.0738 0.0520  77  ARG A CA  
569  C C   . ARG A 68  ? 0.3461 0.5028 0.4071 -0.0282 -0.0766 0.0376  77  ARG A C   
570  O O   . ARG A 68  ? 0.3161 0.4529 0.3734 -0.0298 -0.0678 0.0203  77  ARG A O   
571  C CB  . ARG A 68  ? 0.3748 0.5121 0.4031 -0.0307 -0.0762 0.0500  77  ARG A CB  
572  C CG  . ARG A 68  ? 0.3743 0.4905 0.3994 -0.0238 -0.0696 0.0606  77  ARG A CG  
573  C CD  . ARG A 68  ? 0.3938 0.4790 0.4204 -0.0215 -0.0563 0.0455  77  ARG A CD  
574  N NE  . ARG A 68  ? 0.3820 0.4647 0.3909 -0.0326 -0.0527 0.0275  77  ARG A NE  
575  C CZ  . ARG A 68  ? 0.4013 0.4828 0.3895 -0.0409 -0.0496 0.0261  77  ARG A CZ  
576  N NH1 . ARG A 68  ? 0.4380 0.5207 0.4171 -0.0422 -0.0509 0.0419  77  ARG A NH1 
577  N NH2 . ARG A 68  ? 0.3817 0.4597 0.3588 -0.0469 -0.0431 0.0099  77  ARG A NH2 
578  N N   . LEU A 69  ? 0.3500 0.5422 0.4162 -0.0366 -0.0896 0.0466  78  LEU A N   
579  C CA  . LEU A 69  ? 0.3448 0.5510 0.4153 -0.0485 -0.0922 0.0351  78  LEU A CA  
580  C C   . LEU A 69  ? 0.3267 0.5310 0.4274 -0.0341 -0.0822 0.0344  78  LEU A C   
581  O O   . LEU A 69  ? 0.3159 0.5048 0.4126 -0.0389 -0.0746 0.0182  78  LEU A O   
582  C CB  . LEU A 69  ? 0.3430 0.5939 0.4158 -0.0637 -0.1100 0.0471  78  LEU A CB  
583  C CG  . LEU A 69  ? 0.3600 0.6284 0.4390 -0.0803 -0.1135 0.0370  78  LEU A CG  
584  C CD1 . LEU A 69  ? 0.3422 0.5711 0.3922 -0.0935 -0.1032 0.0098  78  LEU A CD1 
585  C CD2 . LEU A 69  ? 0.3705 0.6860 0.4474 -0.1014 -0.1337 0.0489  78  LEU A CD2 
586  N N   . ALA A 70  ? 0.3380 0.5563 0.4675 -0.0157 -0.0805 0.0529  79  ALA A N   
587  C CA  . ALA A 70  ? 0.3286 0.5428 0.4850 0.0001  -0.0669 0.0521  79  ALA A CA  
588  C C   . ALA A 70  ? 0.3208 0.4903 0.4611 0.0030  -0.0519 0.0326  79  ALA A C   
589  O O   . ALA A 70  ? 0.3181 0.4831 0.4638 0.0032  -0.0430 0.0221  79  ALA A O   
590  C CB  . ALA A 70  ? 0.3464 0.5733 0.5337 0.0229  -0.0632 0.0754  79  ALA A CB  
591  N N   . ARG A 71  ? 0.3168 0.4574 0.4370 0.0033  -0.0500 0.0292  80  ARG A N   
592  C CA  . ARG A 71  ? 0.3187 0.4242 0.4223 0.0013  -0.0397 0.0122  80  ARG A CA  
593  C C   . ARG A 71  ? 0.3075 0.4120 0.3967 -0.0122 -0.0412 -0.0029 80  ARG A C   
594  O O   . ARG A 71  ? 0.3079 0.3976 0.3938 -0.0122 -0.0334 -0.0133 80  ARG A O   
595  C CB  . ARG A 71  ? 0.3336 0.4166 0.4205 0.0000  -0.0393 0.0134  80  ARG A CB  
596  C CG  . ARG A 71  ? 0.3614 0.4172 0.4534 0.0110  -0.0286 0.0169  80  ARG A CG  
597  C CD  . ARG A 71  ? 0.3637 0.3980 0.4375 0.0034  -0.0280 0.0148  80  ARG A CD  
598  N NE  . ARG A 71  ? 0.3618 0.3863 0.4221 -0.0074 -0.0257 -0.0017 80  ARG A NE  
599  C CZ  . ARG A 71  ? 0.3451 0.3495 0.4016 -0.0093 -0.0178 -0.0120 80  ARG A CZ  
600  N NH1 . ARG A 71  ? 0.4094 0.3935 0.4712 -0.0010 -0.0081 -0.0118 80  ARG A NH1 
601  N NH2 . ARG A 71  ? 0.3758 0.3801 0.4221 -0.0195 -0.0190 -0.0222 80  ARG A NH2 
602  N N   . LEU A 72  ? 0.3316 0.4489 0.4094 -0.0243 -0.0504 -0.0037 81  LEU A N   
603  C CA  . LEU A 72  ? 0.3284 0.4392 0.3925 -0.0363 -0.0495 -0.0171 81  LEU A CA  
604  C C   . LEU A 72  ? 0.3360 0.4592 0.4145 -0.0389 -0.0477 -0.0190 81  LEU A C   
605  O O   . LEU A 72  ? 0.3284 0.4371 0.4025 -0.0407 -0.0409 -0.0276 81  LEU A O   
606  C CB  . LEU A 72  ? 0.3330 0.4489 0.3773 -0.0501 -0.0568 -0.0197 81  LEU A CB  
607  C CG  . LEU A 72  ? 0.3467 0.4490 0.3745 -0.0628 -0.0534 -0.0338 81  LEU A CG  
608  C CD1 . LEU A 72  ? 0.3328 0.4090 0.3562 -0.0559 -0.0425 -0.0416 81  LEU A CD1 
609  C CD2 . LEU A 72  ? 0.4013 0.5034 0.4037 -0.0768 -0.0578 -0.0384 81  LEU A CD2 
610  N N   . VAL A 73  ? 0.3245 0.4779 0.4221 -0.0388 -0.0537 -0.0081 82  VAL A N   
611  C CA  . VAL A 73  ? 0.2994 0.4726 0.4167 -0.0409 -0.0508 -0.0066 82  VAL A CA  
612  C C   . VAL A 73  ? 0.2863 0.4434 0.4110 -0.0278 -0.0363 -0.0104 82  VAL A C   
613  O O   . VAL A 73  ? 0.2598 0.4072 0.3783 -0.0336 -0.0301 -0.0188 82  VAL A O   
614  C CB  . VAL A 73  ? 0.3038 0.5213 0.4486 -0.0394 -0.0598 0.0109  82  VAL A CB  
615  C CG1 . VAL A 73  ? 0.3120 0.5550 0.4857 -0.0365 -0.0529 0.0158  82  VAL A CG1 
616  C CG2 . VAL A 73  ? 0.3288 0.5657 0.4597 -0.0609 -0.0759 0.0120  82  VAL A CG2 
617  N N   . LEU A 74  ? 0.2901 0.4412 0.4244 -0.0115 -0.0302 -0.0044 83  LEU A N   
618  C CA  . LEU A 74  ? 0.3029 0.4368 0.4400 -0.0007 -0.0147 -0.0099 83  LEU A CA  
619  C C   . LEU A 74  ? 0.3017 0.4042 0.4119 -0.0071 -0.0106 -0.0239 83  LEU A C   
620  O O   . LEU A 74  ? 0.3274 0.4214 0.4326 -0.0068 -0.0005 -0.0306 83  LEU A O   
621  C CB  . LEU A 74  ? 0.3242 0.4499 0.4740 0.0174  -0.0069 -0.0015 83  LEU A CB  
622  C CG  . LEU A 74  ? 0.2974 0.4585 0.4824 0.0301  -0.0073 0.0173  83  LEU A CG  
623  C CD1 . LEU A 74  ? 0.3637 0.5064 0.5585 0.0500  0.0018  0.0270  83  LEU A CD1 
624  C CD2 . LEU A 74  ? 0.3127 0.4973 0.5195 0.0335  0.0034  0.0178  83  LEU A CD2 
625  N N   . GLY A 75  ? 0.3008 0.3902 0.3945 -0.0129 -0.0183 -0.0265 84  GLY A N   
626  C CA  . GLY A 75  ? 0.2994 0.3681 0.3734 -0.0186 -0.0169 -0.0353 84  GLY A CA  
627  C C   . GLY A 75  ? 0.2787 0.3500 0.3469 -0.0272 -0.0174 -0.0390 84  GLY A C   
628  O O   . GLY A 75  ? 0.3172 0.3789 0.3757 -0.0292 -0.0132 -0.0428 84  GLY A O   
629  N N   . CYS A 76  ? 0.3159 0.3990 0.3882 -0.0339 -0.0228 -0.0372 85  CYS A N   
630  C CA  . CYS A 76  ? 0.3058 0.3859 0.3729 -0.0432 -0.0215 -0.0399 85  CYS A CA  
631  C C   . CYS A 76  ? 0.3063 0.3961 0.3824 -0.0437 -0.0143 -0.0383 85  CYS A C   
632  O O   . CYS A 76  ? 0.3048 0.3846 0.3718 -0.0474 -0.0098 -0.0393 85  CYS A O   
633  C CB  . CYS A 76  ? 0.3213 0.4071 0.3865 -0.0544 -0.0277 -0.0408 85  CYS A CB  
634  S SG  . CYS A 76  ? 0.3341 0.4017 0.3805 -0.0557 -0.0305 -0.0457 85  CYS A SG  
635  N N   . ILE A 77  ? 0.3073 0.4181 0.4020 -0.0386 -0.0121 -0.0338 86  ILE A N   
636  C CA  . ILE A 77  ? 0.3100 0.4338 0.4162 -0.0370 -0.0017 -0.0320 86  ILE A CA  
637  C C   . ILE A 77  ? 0.3173 0.4211 0.4075 -0.0311 0.0084  -0.0378 86  ILE A C   
638  O O   . ILE A 77  ? 0.3356 0.4386 0.4186 -0.0357 0.0161  -0.0390 86  ILE A O   
639  C CB  . ILE A 77  ? 0.3033 0.4576 0.4389 -0.0285 0.0008  -0.0233 86  ILE A CB  
640  C CG1 . ILE A 77  ? 0.3374 0.5200 0.4873 -0.0411 -0.0115 -0.0164 86  ILE A CG1 
641  C CG2 . ILE A 77  ? 0.2967 0.4629 0.4448 -0.0229 0.0173  -0.0223 86  ILE A CG2 
642  C CD1 . ILE A 77  ? 0.3547 0.5761 0.5369 -0.0329 -0.0148 -0.0026 86  ILE A CD1 
643  N N   . THR A 78  ? 0.3175 0.4054 0.3997 -0.0236 0.0079  -0.0413 87  THR A N   
644  C CA  . THR A 78  ? 0.3277 0.3954 0.3900 -0.0226 0.0160  -0.0488 87  THR A CA  
645  C C   . THR A 78  ? 0.3318 0.3912 0.3731 -0.0331 0.0112  -0.0500 87  THR A C   
646  O O   . THR A 78  ? 0.3331 0.3883 0.3587 -0.0373 0.0183  -0.0530 87  THR A O   
647  C CB  . THR A 78  ? 0.3520 0.4021 0.4098 -0.0163 0.0160  -0.0520 87  THR A CB  
648  O OG1 . THR A 78  ? 0.2803 0.3365 0.3591 -0.0033 0.0237  -0.0476 87  THR A OG1 
649  C CG2 . THR A 78  ? 0.3490 0.3763 0.3810 -0.0215 0.0226  -0.0621 87  THR A CG2 
650  N N   A MET A 79  ? 0.2992 0.3570 0.3400 -0.0364 0.0004  -0.0463 88  MET A N   
651  N N   B MET A 79  ? 0.3106 0.3686 0.3515 -0.0364 0.0004  -0.0463 88  MET A N   
652  C CA  A MET A 79  ? 0.3094 0.3619 0.3374 -0.0423 -0.0034 -0.0427 88  MET A CA  
653  C CA  B MET A 79  ? 0.3265 0.3790 0.3546 -0.0423 -0.0035 -0.0426 88  MET A CA  
654  C C   A MET A 79  ? 0.3131 0.3700 0.3404 -0.0477 0.0015  -0.0381 88  MET A C   
655  C C   B MET A 79  ? 0.3244 0.3814 0.3517 -0.0476 0.0016  -0.0382 88  MET A C   
656  O O   A MET A 79  ? 0.3230 0.3775 0.3357 -0.0517 0.0032  -0.0343 88  MET A O   
657  O O   B MET A 79  ? 0.3317 0.3863 0.3443 -0.0517 0.0034  -0.0345 88  MET A O   
658  C CB  A MET A 79  ? 0.2805 0.3288 0.3120 -0.0413 -0.0112 -0.0394 88  MET A CB  
659  C CB  B MET A 79  ? 0.3208 0.3691 0.3527 -0.0414 -0.0111 -0.0392 88  MET A CB  
660  C CG  A MET A 79  ? 0.2468 0.2924 0.2769 -0.0382 -0.0158 -0.0413 88  MET A CG  
661  C CG  B MET A 79  ? 0.3311 0.3770 0.3634 -0.0379 -0.0159 -0.0412 88  MET A CG  
662  S SD  A MET A 79  ? 0.2586 0.3032 0.2732 -0.0433 -0.0178 -0.0414 88  MET A SD  
663  S SD  B MET A 79  ? 0.4114 0.4536 0.4313 -0.0405 -0.0161 -0.0447 88  MET A SD  
664  C CE  A MET A 79  ? 0.1609 0.2076 0.1811 -0.0425 -0.0245 -0.0390 88  MET A CE  
665  C CE  B MET A 79  ? 0.3757 0.4121 0.4026 -0.0349 -0.0102 -0.0506 88  MET A CE  
666  N N   . ALA A 80  ? 0.3343 0.3999 0.3766 -0.0497 0.0032  -0.0371 89  ALA A N   
667  C CA  . ALA A 80  ? 0.3400 0.4110 0.3844 -0.0577 0.0090  -0.0324 89  ALA A CA  
668  C C   . ALA A 80  ? 0.3465 0.4255 0.3847 -0.0576 0.0203  -0.0331 89  ALA A C   
669  O O   . ALA A 80  ? 0.3435 0.4200 0.3694 -0.0641 0.0249  -0.0276 89  ALA A O   
670  C CB  . ALA A 80  ? 0.3554 0.4405 0.4190 -0.0636 0.0075  -0.0320 89  ALA A CB  
671  N N   . TYR A 81  ? 0.3474 0.4327 0.3916 -0.0495 0.0263  -0.0393 90  TYR A N   
672  C CA  . TYR A 81  ? 0.3493 0.4376 0.3851 -0.0477 0.0415  -0.0434 90  TYR A CA  
673  C C   . TYR A 81  ? 0.3591 0.4308 0.3612 -0.0530 0.0418  -0.0473 90  TYR A C   
674  O O   . TYR A 81  ? 0.3529 0.4265 0.3380 -0.0591 0.0513  -0.0466 90  TYR A O   
675  C CB  . TYR A 81  ? 0.3579 0.4506 0.4094 -0.0348 0.0508  -0.0490 90  TYR A CB  
676  C CG  . TYR A 81  ? 0.3786 0.4736 0.4243 -0.0312 0.0721  -0.0542 90  TYR A CG  
677  C CD1 . TYR A 81  ? 0.4047 0.5266 0.4740 -0.0297 0.0838  -0.0478 90  TYR A CD1 
678  C CD2 . TYR A 81  ? 0.4005 0.4713 0.4152 -0.0316 0.0816  -0.0662 90  TYR A CD2 
679  C CE1 . TYR A 81  ? 0.3939 0.5188 0.4581 -0.0250 0.1075  -0.0529 90  TYR A CE1 
680  C CE2 . TYR A 81  ? 0.4518 0.5202 0.4553 -0.0289 0.1047  -0.0737 90  TYR A CE2 
681  C CZ  . TYR A 81  ? 0.4382 0.5338 0.4673 -0.0240 0.1189  -0.0668 90  TYR A CZ  
682  O OH  . TYR A 81  ? 0.4588 0.5524 0.4768 -0.0200 0.1454  -0.0747 90  TYR A OH  
683  N N   . VAL A 82  ? 0.3592 0.4182 0.3510 -0.0523 0.0315  -0.0505 91  VAL A N   
684  C CA  . VAL A 82  ? 0.3691 0.4187 0.3300 -0.0607 0.0287  -0.0531 91  VAL A CA  
685  C C   . VAL A 82  ? 0.3804 0.4362 0.3312 -0.0683 0.0206  -0.0395 91  VAL A C   
686  O O   . VAL A 82  ? 0.3919 0.4495 0.3175 -0.0771 0.0239  -0.0375 91  VAL A O   
687  C CB  . VAL A 82  ? 0.3672 0.4066 0.3237 -0.0606 0.0190  -0.0583 91  VAL A CB  
688  C CG1 . VAL A 82  ? 0.3901 0.4280 0.3161 -0.0740 0.0120  -0.0584 91  VAL A CG1 
689  C CG2 . VAL A 82  ? 0.3842 0.4103 0.3455 -0.0533 0.0300  -0.0706 91  VAL A CG2 
690  N N   . TRP A 83  ? 0.3624 0.4194 0.3310 -0.0648 0.0113  -0.0297 92  TRP A N   
691  C CA  . TRP A 83  ? 0.3614 0.4190 0.3242 -0.0680 0.0046  -0.0139 92  TRP A CA  
692  C C   . TRP A 83  ? 0.3589 0.4161 0.3243 -0.0720 0.0125  -0.0053 92  TRP A C   
693  O O   . TRP A 83  ? 0.3464 0.4016 0.3023 -0.0752 0.0100  0.0099  92  TRP A O   
694  C CB  . TRP A 83  ? 0.3455 0.3986 0.3244 -0.0608 -0.0050 -0.0079 92  TRP A CB  
695  C CG  . TRP A 83  ? 0.3341 0.3905 0.3125 -0.0588 -0.0124 -0.0139 92  TRP A CG  
696  C CD1 . TRP A 83  ? 0.2973 0.3501 0.2906 -0.0527 -0.0145 -0.0206 92  TRP A CD1 
697  C CD2 . TRP A 83  ? 0.3244 0.3891 0.2843 -0.0663 -0.0188 -0.0138 92  TRP A CD2 
698  N NE1 . TRP A 83  ? 0.2756 0.3328 0.2635 -0.0550 -0.0207 -0.0237 92  TRP A NE1 
699  C CE2 . TRP A 83  ? 0.3288 0.3934 0.2965 -0.0645 -0.0240 -0.0204 92  TRP A CE2 
700  C CE3 . TRP A 83  ? 0.3482 0.4215 0.2828 -0.0771 -0.0212 -0.0085 92  TRP A CE3 
701  C CZ2 . TRP A 83  ? 0.3305 0.4026 0.2839 -0.0746 -0.0316 -0.0226 92  TRP A CZ2 
702  C CZ3 . TRP A 83  ? 0.3862 0.4682 0.3037 -0.0879 -0.0301 -0.0114 92  TRP A CZ3 
703  C CH2 . TRP A 83  ? 0.3317 0.4126 0.2598 -0.0872 -0.0351 -0.0187 92  TRP A CH2 
704  N N   . GLY A 84  ? 0.3649 0.4260 0.3451 -0.0722 0.0216  -0.0124 93  GLY A N   
705  C CA  . GLY A 84  ? 0.3766 0.4410 0.3610 -0.0797 0.0303  -0.0050 93  GLY A CA  
706  C C   . GLY A 84  ? 0.3884 0.4374 0.3804 -0.0818 0.0251  0.0058  93  GLY A C   
707  O O   . GLY A 84  ? 0.4062 0.4466 0.4109 -0.0775 0.0191  0.0012  93  GLY A O   
708  N N   . LYS A 85  ? 0.4040 0.4459 0.3853 -0.0884 0.0290  0.0202  94  LYS A N   
709  C CA  . LYS A 85  ? 0.4259 0.4443 0.4114 -0.0895 0.0277  0.0322  94  LYS A CA  
710  C C   . LYS A 85  ? 0.4262 0.4331 0.4081 -0.0775 0.0189  0.0419  94  LYS A C   
711  O O   . LYS A 85  ? 0.4069 0.3898 0.3938 -0.0740 0.0205  0.0520  94  LYS A O   
712  C CB  . LYS A 85  ? 0.4410 0.4538 0.4173 -0.1005 0.0366  0.0474  94  LYS A CB  
713  C CG  . LYS A 85  ? 0.4787 0.5061 0.4650 -0.1137 0.0470  0.0407  94  LYS A CG  
714  C CD  . LYS A 85  ? 0.4800 0.5032 0.4553 -0.1262 0.0570  0.0574  94  LYS A CD  
715  C CE  . LYS A 85  ? 0.4964 0.5406 0.4869 -0.1404 0.0682  0.0522  94  LYS A CE  
716  N NZ  . LYS A 85  ? 0.5317 0.5714 0.5134 -0.1557 0.0795  0.0691  94  LYS A NZ  
717  N N   . GLY A 86  ? 0.4288 0.4524 0.4032 -0.0718 0.0110  0.0393  95  GLY A N   
718  C CA  . GLY A 86  ? 0.4498 0.4735 0.4270 -0.0611 0.0014  0.0488  95  GLY A CA  
719  C C   . GLY A 86  ? 0.4951 0.5229 0.4612 -0.0598 -0.0025 0.0739  95  GLY A C   
720  O O   . GLY A 86  ? 0.5345 0.5584 0.5119 -0.0482 -0.0070 0.0895  95  GLY A O   
721  N N   . HIS A 87  ? 0.5116 0.5497 0.4564 -0.0710 0.0000  0.0793  96  HIS A N   
722  C CA  . HIS A 87  ? 0.5558 0.6005 0.4854 -0.0727 -0.0041 0.1060  96  HIS A CA  
723  C C   . HIS A 87  ? 0.5712 0.6450 0.4735 -0.0823 -0.0139 0.1065  96  HIS A C   
724  O O   . HIS A 87  ? 0.6149 0.7001 0.4955 -0.0893 -0.0174 0.1264  96  HIS A O   
725  C CB  . HIS A 87  ? 0.6015 0.6314 0.5228 -0.0818 0.0085  0.1150  96  HIS A CB  
726  C CG  . HIS A 87  ? 0.6534 0.6515 0.5961 -0.0783 0.0181  0.1137  96  HIS A CG  
727  N ND1 . HIS A 87  ? 0.7065 0.6834 0.6680 -0.0641 0.0165  0.1200  96  HIS A ND1 
728  C CD2 . HIS A 87  ? 0.6952 0.6787 0.6417 -0.0895 0.0301  0.1062  96  HIS A CD2 
729  C CE1 . HIS A 87  ? 0.7081 0.6533 0.6789 -0.0681 0.0276  0.1139  96  HIS A CE1 
730  N NE2 . HIS A 87  ? 0.6857 0.6365 0.6487 -0.0849 0.0344  0.1062  96  HIS A NE2 
731  N N   . GLY A 88  ? 0.5661 0.6498 0.4667 -0.0843 -0.0183 0.0850  97  GLY A N   
732  C CA  . GLY A 88  ? 0.5771 0.6823 0.4484 -0.0971 -0.0268 0.0802  97  GLY A CA  
733  C C   . GLY A 88  ? 0.5821 0.6840 0.4252 -0.1102 -0.0139 0.0583  97  GLY A C   
734  O O   . GLY A 88  ? 0.5910 0.7035 0.4024 -0.1237 -0.0179 0.0503  97  GLY A O   
735  N N   . ASP A 89  ? 0.5804 0.6683 0.4346 -0.1072 0.0025  0.0487  98  ASP A N   
736  C CA  . ASP A 89  ? 0.5938 0.6802 0.4300 -0.1148 0.0187  0.0282  98  ASP A CA  
737  C C   . ASP A 89  ? 0.5824 0.6610 0.4366 -0.1071 0.0223  0.0047  98  ASP A C   
738  O O   . ASP A 89  ? 0.6202 0.6932 0.5073 -0.0965 0.0230  0.0028  98  ASP A O   
739  C CB  . ASP A 89  ? 0.6020 0.6856 0.4455 -0.1161 0.0350  0.0331  98  ASP A CB  
740  C CG  . ASP A 89  ? 0.6430 0.7312 0.4619 -0.1244 0.0540  0.0184  98  ASP A CG  
741  O OD1 . ASP A 89  ? 0.6942 0.7794 0.5252 -0.1184 0.0653  -0.0024 98  ASP A OD1 
742  O OD2 . ASP A 89  ? 0.7566 0.8511 0.5437 -0.1361 0.0588  0.0288  98  ASP A OD2 
743  N N   . VAL A 90  ? 0.5731 0.6493 0.4026 -0.1139 0.0254  -0.0126 99  VAL A N   
744  C CA  . VAL A 90  ? 0.5413 0.6071 0.3837 -0.1074 0.0258  -0.0311 99  VAL A CA  
745  C C   . VAL A 90  ? 0.5427 0.5965 0.3745 -0.1066 0.0480  -0.0523 99  VAL A C   
746  O O   . VAL A 90  ? 0.5988 0.6495 0.3938 -0.1180 0.0592  -0.0598 99  VAL A O   
747  C CB  . VAL A 90  ? 0.5623 0.6307 0.3864 -0.1171 0.0092  -0.0322 99  VAL A CB  
748  C CG1 . VAL A 90  ? 0.5842 0.6385 0.4207 -0.1121 0.0100  -0.0494 99  VAL A CG1 
749  C CG2 . VAL A 90  ? 0.5645 0.6497 0.4047 -0.1142 -0.0104 -0.0077 99  VAL A CG2 
750  N N   . ARG A 91  ? 0.4959 0.5439 0.3597 -0.0924 0.0552  -0.0605 100 ARG A N   
751  C CA  . ARG A 91  ? 0.5085 0.5430 0.3705 -0.0860 0.0760  -0.0791 100 ARG A CA  
752  C C   . ARG A 91  ? 0.5286 0.5413 0.3726 -0.0901 0.0718  -0.0936 100 ARG A C   
753  O O   . ARG A 91  ? 0.4965 0.5089 0.3580 -0.0871 0.0558  -0.0893 100 ARG A O   
754  C CB  . ARG A 91  ? 0.4680 0.5113 0.3757 -0.0686 0.0832  -0.0765 100 ARG A CB  
755  C CG  . ARG A 91  ? 0.5237 0.5876 0.4471 -0.0674 0.0955  -0.0675 100 ARG A CG  
756  C CD  . ARG A 91  ? 0.5604 0.6217 0.4689 -0.0653 0.1236  -0.0792 100 ARG A CD  
757  N NE  . ARG A 91  ? 0.5634 0.6507 0.5019 -0.0598 0.1382  -0.0706 100 ARG A NE  
758  C CZ  . ARG A 91  ? 0.5840 0.6877 0.5184 -0.0709 0.1396  -0.0584 100 ARG A CZ  
759  N NH1 . ARG A 91  ? 0.6037 0.7001 0.5052 -0.0857 0.1271  -0.0510 100 ARG A NH1 
760  N NH2 . ARG A 91  ? 0.5533 0.6836 0.5191 -0.0674 0.1537  -0.0509 100 ARG A NH2 
761  N N   . LYS A 92  ? 0.5768 0.5693 0.3833 -0.0991 0.0878  -0.1114 101 LYS A N   
762  C CA  . LYS A 92  ? 0.6232 0.5881 0.4053 -0.1083 0.0869  -0.1282 101 LYS A CA  
763  C C   . LYS A 92  ? 0.6502 0.5871 0.4496 -0.0914 0.1075  -0.1423 101 LYS A C   
764  O O   . LYS A 92  ? 0.6626 0.5713 0.4488 -0.0969 0.1074  -0.1546 101 LYS A O   
765  C CB  . LYS A 92  ? 0.6820 0.6349 0.4048 -0.1325 0.0923  -0.1415 101 LYS A CB  
766  C CG  . LYS A 92  ? 0.7120 0.6942 0.4161 -0.1506 0.0676  -0.1239 101 LYS A CG  
767  C CD  . LYS A 92  ? 0.7736 0.7467 0.4146 -0.1795 0.0678  -0.1371 101 LYS A CD  
768  C CE  . LYS A 92  ? 0.7695 0.7735 0.3973 -0.1989 0.0364  -0.1183 101 LYS A CE  
769  N NZ  . LYS A 92  ? 0.8381 0.8380 0.4010 -0.2317 0.0335  -0.1307 101 LYS A NZ  
770  N N   . VAL A 93  ? 0.6277 0.5741 0.4587 -0.0713 0.1248  -0.1381 102 VAL A N   
771  C CA  . VAL A 93  ? 0.6184 0.5460 0.4746 -0.0503 0.1452  -0.1450 102 VAL A CA  
772  C C   . VAL A 93  ? 0.5484 0.5081 0.4612 -0.0312 0.1367  -0.1253 102 VAL A C   
773  O O   . VAL A 93  ? 0.5231 0.5141 0.4534 -0.0298 0.1355  -0.1136 102 VAL A O   
774  C CB  . VAL A 93  ? 0.6689 0.5812 0.5086 -0.0436 0.1805  -0.1593 102 VAL A CB  
775  C CG1 . VAL A 93  ? 0.6966 0.5916 0.5703 -0.0164 0.2037  -0.1620 102 VAL A CG1 
776  C CG2 . VAL A 93  ? 0.7287 0.6061 0.5026 -0.0671 0.1901  -0.1822 102 VAL A CG2 
777  N N   . LEU A 94  ? 0.5199 0.4709 0.4581 -0.0192 0.1309  -0.1215 103 LEU A N   
778  C CA  . LEU A 94  ? 0.4900 0.4708 0.4779 -0.0027 0.1228  -0.1037 103 LEU A CA  
779  C C   . LEU A 94  ? 0.5061 0.4854 0.5215 0.0204  0.1487  -0.1031 103 LEU A C   
780  O O   . LEU A 94  ? 0.5248 0.4684 0.5330 0.0297  0.1632  -0.1122 103 LEU A O   
781  C CB  . LEU A 94  ? 0.4725 0.4471 0.4697 -0.0033 0.1018  -0.0976 103 LEU A CB  
782  C CG  . LEU A 94  ? 0.4101 0.4147 0.4490 0.0078  0.0882  -0.0798 103 LEU A CG  
783  C CD1 . LEU A 94  ? 0.3479 0.3844 0.3943 -0.0022 0.0736  -0.0707 103 LEU A CD1 
784  C CD2 . LEU A 94  ? 0.4156 0.4062 0.4556 0.0076  0.0739  -0.0766 103 LEU A CD2 
785  N N   . PRO A 95  ? 0.5080 0.5257 0.5566 0.0299  0.1559  -0.0913 104 PRO A N   
786  C CA  . PRO A 95  ? 0.5440 0.5663 0.6212 0.0535  0.1847  -0.0892 104 PRO A CA  
787  C C   . PRO A 95  ? 0.5389 0.5581 0.6521 0.0755  0.1838  -0.0774 104 PRO A C   
788  O O   . PRO A 95  ? 0.4683 0.5048 0.5987 0.0727  0.1579  -0.0642 104 PRO A O   
789  C CB  . PRO A 95  ? 0.5126 0.5874 0.6217 0.0538  0.1862  -0.0752 104 PRO A CB  
790  C CG  . PRO A 95  ? 0.4888 0.5837 0.5952 0.0341  0.1550  -0.0668 104 PRO A CG  
791  C CD  . PRO A 95  ? 0.4710 0.5289 0.5341 0.0191  0.1397  -0.0785 104 PRO A CD  
792  N N   . ARG A 96  ? 0.5930 0.5880 0.7150 0.0973  0.2138  -0.0819 105 ARG A N   
793  C CA  . ARG A 96  ? 0.6152 0.5927 0.7633 0.1195  0.2174  -0.0714 105 ARG A CA  
794  C C   . ARG A 96  ? 0.5761 0.6074 0.7794 0.1320  0.1966  -0.0415 105 ARG A C   
795  O O   . ARG A 96  ? 0.5586 0.5791 0.7703 0.1375  0.1828  -0.0310 105 ARG A O   
796  C CB  . ARG A 96  ? 0.6892 0.6322 0.8425 0.1449  0.2590  -0.0793 105 ARG A CB  
797  C CG  . ARG A 96  ? 0.7146 0.7058 0.9172 0.1682  0.2809  -0.0644 105 ARG A CG  
798  C CD  . ARG A 96  ? 0.7701 0.7218 0.9742 0.1948  0.3277  -0.0750 105 ARG A CD  
799  N NE  . ARG A 96  ? 0.8412 0.7597 0.9904 0.1780  0.3511  -0.1051 105 ARG A NE  
800  C CZ  . ARG A 96  ? 0.9576 0.8035 1.0461 0.1660  0.3680  -0.1348 105 ARG A CZ  
801  N NH1 . ARG A 96  ? 0.9840 0.7750 1.0577 0.1687  0.3668  -0.1404 105 ARG A NH1 
802  N NH2 . ARG A 96  ? 1.0081 0.8359 1.0467 0.1482  0.3868  -0.1594 105 ARG A NH2 
803  N N   A ASN A 97  ? 0.5428 0.6322 0.7807 0.1333  0.1938  -0.0277 106 ASN A N   
804  N N   B ASN A 97  ? 0.5486 0.6377 0.7861 0.1334  0.1945  -0.0280 106 ASN A N   
805  C CA  A ASN A 97  ? 0.5017 0.6483 0.7908 0.1412  0.1735  0.0007  106 ASN A CA  
806  C CA  B ASN A 97  ? 0.5082 0.6571 0.7960 0.1391  0.1729  -0.0001 106 ASN A CA  
807  C C   A ASN A 97  ? 0.4788 0.6334 0.7539 0.1195  0.1363  0.0050  106 ASN A C   
808  C C   B ASN A 97  ? 0.4856 0.6370 0.7593 0.1202  0.1371  0.0044  106 ASN A C   
809  O O   A ASN A 97  ? 0.4641 0.6524 0.7703 0.1250  0.1186  0.0263  106 ASN A O   
810  O O   B ASN A 97  ? 0.4760 0.6536 0.7791 0.1282  0.1213  0.0251  106 ASN A O   
811  C CB  A ASN A 97  ? 0.4829 0.6921 0.8117 0.1430  0.1798  0.0135  106 ASN A CB  
812  C CB  B ASN A 97  ? 0.4903 0.7001 0.8090 0.1336  0.1743  0.0098  106 ASN A CB  
813  C CG  A ASN A 97  ? 0.4962 0.7113 0.8578 0.1735  0.2183  0.0183  106 ASN A CG  
814  C CG  B ASN A 97  ? 0.4736 0.6800 0.7537 0.1032  0.1646  -0.0060 106 ASN A CG  
815  O OD1 A ASN A 97  ? 0.4786 0.6405 0.8236 0.1912  0.2439  0.0064  106 ASN A OD1 
816  O OD1 B ASN A 97  ? 0.4358 0.6085 0.6739 0.0848  0.1483  -0.0191 106 ASN A OD1 
817  N ND2 A ASN A 97  ? 0.4764 0.7558 0.8851 0.1789  0.2241  0.0355  106 ASN A ND2 
818  N ND2 B ASN A 97  ? 0.4458 0.6899 0.7437 0.0987  0.1758  -0.0020 106 ASN A ND2 
819  N N   . ILE A 98  ? 0.4830 0.6082 0.7115 0.0958  0.1257  -0.0140 107 ILE A N   
820  C CA  . ILE A 98  ? 0.4463 0.5662 0.6562 0.0785  0.0968  -0.0134 107 ILE A CA  
821  C C   . ILE A 98  ? 0.4460 0.5119 0.6232 0.0778  0.0982  -0.0252 107 ILE A C   
822  O O   . ILE A 98  ? 0.4175 0.4800 0.5969 0.0777  0.0827  -0.0164 107 ILE A O   
823  C CB  . ILE A 98  ? 0.4405 0.5735 0.6298 0.0531  0.0816  -0.0207 107 ILE A CB  
824  C CG1 . ILE A 98  ? 0.4644 0.5906 0.6370 0.0389  0.0564  -0.0202 107 ILE A CG1 
825  C CG2 . ILE A 98  ? 0.4558 0.5602 0.6083 0.0430  0.0951  -0.0394 107 ILE A CG2 
826  C CD1 . ILE A 98  ? 0.4487 0.5992 0.6199 0.0203  0.0409  -0.0183 107 ILE A CD1 
827  N N   . ALA A 99  ? 0.3871 0.5361 0.5377 0.0565  0.0660  0.0315  108 ALA A N   
828  C CA  . ALA A 99  ? 0.3842 0.5042 0.5205 0.0574  0.0699  0.0219  108 ALA A CA  
829  C C   . ALA A 99  ? 0.3779 0.4878 0.5308 0.0705  0.0754  0.0281  108 ALA A C   
830  O O   . ALA A 99  ? 0.3563 0.4484 0.5012 0.0698  0.0711  0.0278  108 ALA A O   
831  C CB  . ALA A 99  ? 0.3898 0.4976 0.5123 0.0543  0.0826  0.0062  108 ALA A CB  
832  N N   . VAL A 100 ? 0.3872 0.5093 0.5649 0.0829  0.0853  0.0351  109 VAL A N   
833  C CA  . VAL A 100 ? 0.4087 0.5214 0.6059 0.0976  0.0926  0.0435  109 VAL A CA  
834  C C   . VAL A 100 ? 0.3902 0.5116 0.5917 0.0995  0.0774  0.0602  109 VAL A C   
835  O O   . VAL A 100 ? 0.4093 0.5095 0.6048 0.1013  0.0771  0.0611  109 VAL A O   
836  C CB  . VAL A 100 ? 0.4207 0.5457 0.6464 0.1121  0.1082  0.0481  109 VAL A CB  
837  C CG1 . VAL A 100 ? 0.4397 0.5570 0.6897 0.1291  0.1153  0.0612  109 VAL A CG1 
838  C CG2 . VAL A 100 ? 0.4574 0.5671 0.6748 0.1102  0.1258  0.0287  109 VAL A CG2 
839  N N   . PRO A 101 ? 0.3818 0.5352 0.5928 0.0981  0.0652  0.0725  110 PRO A N   
840  C CA  . PRO A 101 ? 0.3702 0.5341 0.5815 0.0983  0.0503  0.0867  110 PRO A CA  
841  C C   . PRO A 101 ? 0.3565 0.5027 0.5400 0.0857  0.0398  0.0796  110 PRO A C   
842  O O   . PRO A 101 ? 0.3596 0.5014 0.5403 0.0883  0.0338  0.0885  110 PRO A O   
843  C CB  . PRO A 101 ? 0.3597 0.5626 0.5834 0.0948  0.0393  0.0959  110 PRO A CB  
844  C CG  . PRO A 101 ? 0.3753 0.5828 0.5975 0.0879  0.0460  0.0844  110 PRO A CG  
845  C CD  . PRO A 101 ? 0.3812 0.5634 0.6033 0.0953  0.0646  0.0739  110 PRO A CD  
846  N N   . TYR A 102 ? 0.3380 0.4753 0.5021 0.0728  0.0384  0.0651  111 TYR A N   
847  C CA  . TYR A 102 ? 0.3263 0.4473 0.4663 0.0615  0.0297  0.0580  111 TYR A CA  
848  C C   . TYR A 102 ? 0.3316 0.4226 0.4651 0.0653  0.0377  0.0529  111 TYR A C   
849  O O   . TYR A 102 ? 0.3078 0.3902 0.4333 0.0635  0.0314  0.0566  111 TYR A O   
850  C CB  . TYR A 102 ? 0.3101 0.4300 0.4343 0.0487  0.0275  0.0460  111 TYR A CB  
851  C CG  . TYR A 102 ? 0.3177 0.4249 0.4203 0.0374  0.0183  0.0397  111 TYR A CG  
852  C CD1 . TYR A 102 ? 0.3355 0.4421 0.4332 0.0356  0.0086  0.0455  111 TYR A CD1 
853  C CD2 . TYR A 102 ? 0.3235 0.4216 0.4108 0.0286  0.0195  0.0286  111 TYR A CD2 
854  C CE1 . TYR A 102 ? 0.3383 0.4337 0.4181 0.0258  0.0018  0.0392  111 TYR A CE1 
855  C CE2 . TYR A 102 ? 0.3189 0.4071 0.3896 0.0195  0.0116  0.0242  111 TYR A CE2 
856  C CZ  . TYR A 102 ? 0.2872 0.3732 0.3551 0.0183  0.0035  0.0289  111 TYR A CZ  
857  O OH  . TYR A 102 ? 0.3182 0.3946 0.3717 0.0102  -0.0028 0.0241  111 TYR A OH  
858  N N   . CYS A 103 ? 0.3389 0.4148 0.4765 0.0699  0.0523  0.0436  112 CYS A N   
859  C CA  . CYS A 103 ? 0.3618 0.4090 0.4972 0.0732  0.0621  0.0373  112 CYS A CA  
860  C C   . CYS A 103 ? 0.3874 0.4308 0.5407 0.0862  0.0655  0.0530  112 CYS A C   
861  O O   . CYS A 103 ? 0.3687 0.3924 0.5170 0.0857  0.0666  0.0536  112 CYS A O   
862  C CB  . CYS A 103 ? 0.3637 0.3972 0.5000 0.0743  0.0780  0.0220  112 CYS A CB  
863  S SG  . CYS A 103 ? 0.3729 0.4054 0.4828 0.0584  0.0745  0.0036  112 CYS A SG  
864  N N   . GLN A 104 ? 0.4075 0.4713 0.5827 0.0979  0.0674  0.0670  113 GLN A N   
865  C CA  . GLN A 104 ? 0.4109 0.4765 0.6047 0.1117  0.0692  0.0863  113 GLN A CA  
866  C C   . GLN A 104 ? 0.3962 0.4709 0.5779 0.1067  0.0532  0.0975  113 GLN A C   
867  O O   . GLN A 104 ? 0.3843 0.4436 0.5660 0.1112  0.0554  0.1058  113 GLN A O   
868  C CB  . GLN A 104 ? 0.4167 0.5092 0.6377 0.1251  0.0722  0.1004  113 GLN A CB  
869  C CG  . GLN A 104 ? 0.4274 0.5070 0.6659 0.1349  0.0926  0.0925  113 GLN A CG  
870  C CD  . GLN A 104 ? 0.4775 0.5874 0.7439 0.1472  0.0959  0.1048  113 GLN A CD  
871  O OE1 . GLN A 104 ? 0.4512 0.5945 0.7194 0.1428  0.0823  0.1122  113 GLN A OE1 
872  N NE2 . GLN A 104 ? 0.4814 0.5798 0.7716 0.1623  0.1149  0.1064  113 GLN A NE2 
873  N N   . LEU A 105 ? 0.3754 0.4741 0.5465 0.0967  0.0383  0.0971  114 LEU A N   
874  C CA  . LEU A 105 ? 0.3822 0.4916 0.5394 0.0899  0.0233  0.1046  114 LEU A CA  
875  C C   . LEU A 105 ? 0.3880 0.4697 0.5241 0.0811  0.0235  0.0943  114 LEU A C   
876  O O   . LEU A 105 ? 0.3341 0.4122 0.4643 0.0819  0.0196  0.1033  114 LEU A O   
877  C CB  . LEU A 105 ? 0.3632 0.4994 0.5134 0.0787  0.0098  0.1011  114 LEU A CB  
878  C CG  . LEU A 105 ? 0.3678 0.5175 0.5029 0.0697  -0.0054 0.1053  114 LEU A CG  
879  C CD1 . LEU A 105 ? 0.4039 0.5732 0.5490 0.0797  -0.0105 0.1257  114 LEU A CD1 
880  C CD2 . LEU A 105 ? 0.3901 0.5611 0.5210 0.0575  -0.0153 0.0983  114 LEU A CD2 
881  N N   . SER A 106 ? 0.3879 0.4530 0.5130 0.0724  0.0279  0.0761  115 SER A N   
882  C CA  . SER A 106 ? 0.3976 0.4393 0.5051 0.0634  0.0282  0.0649  115 SER A CA  
883  C C   . SER A 106 ? 0.4195 0.4367 0.5336 0.0705  0.0394  0.0684  115 SER A C   
884  O O   . SER A 106 ? 0.4105 0.4168 0.5151 0.0665  0.0368  0.0702  115 SER A O   
885  C CB  . SER A 106 ? 0.3701 0.4034 0.4675 0.0544  0.0312  0.0466  115 SER A CB  
886  O OG  . SER A 106 ? 0.3528 0.4065 0.4453 0.0478  0.0221  0.0451  115 SER A OG  
887  N N   . LYS A 107 ? 0.4327 0.4410 0.5644 0.0809  0.0529  0.0694  116 LYS A N   
888  C CA  . LYS A 107 ? 0.4678 0.4511 0.6107 0.0888  0.0661  0.0737  116 LYS A CA  
889  C C   . LYS A 107 ? 0.4800 0.4710 0.6292 0.0973  0.0616  0.0967  116 LYS A C   
890  O O   . LYS A 107 ? 0.5054 0.4778 0.6513 0.0965  0.0653  0.1003  116 LYS A O   
891  C CB  . LYS A 107 ? 0.4946 0.4687 0.6577 0.0995  0.0825  0.0705  116 LYS A CB  
892  C CG  . LYS A 107 ? 0.5384 0.4824 0.7165 0.1080  0.0994  0.0734  116 LYS A CG  
893  C CD  . LYS A 107 ? 0.5709 0.5051 0.7686 0.1177  0.1171  0.0665  116 LYS A CD  
894  C CE  . LYS A 107 ? 0.6479 0.5544 0.8675 0.1300  0.1351  0.0746  116 LYS A CE  
895  N NZ  . LYS A 107 ? 0.6355 0.5307 0.8751 0.1397  0.1542  0.0662  116 LYS A NZ  
896  N N   . LYS A 108 ? 0.4874 0.5082 0.6453 0.1046  0.0532  0.1122  117 LYS A N   
897  C CA  . LYS A 108 ? 0.4922 0.5288 0.6532 0.1118  0.0459  0.1352  117 LYS A CA  
898  C C   . LYS A 108 ? 0.4738 0.5096 0.6109 0.0999  0.0353  0.1336  117 LYS A C   
899  O O   . LYS A 108 ? 0.4677 0.4944 0.6033 0.1036  0.0377  0.1462  117 LYS A O   
900  C CB  . LYS A 108 ? 0.4759 0.5513 0.6476 0.1177  0.0356  0.1486  117 LYS A CB  
901  C CG  . LYS A 108 ? 0.5194 0.6162 0.6965 0.1270  0.0282  0.1744  117 LYS A CG  
902  C CD  . LYS A 108 ? 0.5305 0.6621 0.7300 0.1386  0.0241  0.1901  117 LYS A CD  
903  C CE  . LYS A 108 ? 0.5754 0.7309 0.7810 0.1491  0.0167  0.2180  117 LYS A CE  
904  N NZ  . LYS A 108 ? 0.5571 0.7516 0.7870 0.1605  0.0114  0.2342  117 LYS A NZ  
905  N N   . LEU A 109 ? 0.4476 0.4918 0.5671 0.0862  0.0251  0.1187  118 LEU A N   
906  C CA  . LEU A 109 ? 0.4638 0.5070 0.5614 0.0746  0.0162  0.1144  118 LEU A CA  
907  C C   . LEU A 109 ? 0.4632 0.4755 0.5519 0.0672  0.0241  0.1005  118 LEU A C   
908  O O   . LEU A 109 ? 0.4813 0.4911 0.5543 0.0585  0.0188  0.0970  118 LEU A O   
909  C CB  . LEU A 109 ? 0.4482 0.5126 0.5334 0.0634  0.0031  0.1049  118 LEU A CB  
910  C CG  . LEU A 109 ? 0.4487 0.5480 0.5376 0.0657  -0.0084 0.1174  118 LEU A CG  
911  C CD1 . LEU A 109 ? 0.4114 0.5255 0.4926 0.0539  -0.0176 0.1045  118 LEU A CD1 
912  C CD2 . LEU A 109 ? 0.4823 0.5933 0.5606 0.0660  -0.0155 0.1310  118 LEU A CD2 
913  N N   . GLU A 110 ? 0.4793 0.4697 0.5787 0.0701  0.0369  0.0919  119 GLU A N   
914  C CA  . GLU A 110 ? 0.4932 0.4569 0.5866 0.0619  0.0445  0.0766  119 GLU A CA  
915  C C   . GLU A 110 ? 0.4650 0.4334 0.5403 0.0480  0.0350  0.0607  119 GLU A C   
916  O O   . GLU A 110 ? 0.4984 0.4574 0.5638 0.0402  0.0338  0.0557  119 GLU A O   
917  C CB  . GLU A 110 ? 0.5011 0.4482 0.5957 0.0637  0.0505  0.0865  119 GLU A CB  
918  C CG  . GLU A 110 ? 0.5855 0.5272 0.6989 0.0786  0.0602  0.1062  119 GLU A CG  
919  C CD  . GLU A 110 ? 0.6162 0.5409 0.7298 0.0794  0.0669  0.1173  119 GLU A CD  
920  O OE1 . GLU A 110 ? 0.7261 0.6279 0.8373 0.0706  0.0741  0.1039  119 GLU A OE1 
921  O OE2 . GLU A 110 ? 0.7334 0.6695 0.8498 0.0884  0.0648  0.1398  119 GLU A OE2 
922  N N   . LEU A 111 ? 0.4386 0.4226 0.5113 0.0456  0.0290  0.0545  120 LEU A N   
923  C CA  . LEU A 111 ? 0.4157 0.4038 0.4742 0.0341  0.0214  0.0410  120 LEU A CA  
924  C C   . LEU A 111 ? 0.4064 0.3932 0.4678 0.0332  0.0263  0.0294  120 LEU A C   
925  O O   . LEU A 111 ? 0.4164 0.4064 0.4905 0.0415  0.0327  0.0334  120 LEU A O   
926  C CB  . LEU A 111 ? 0.3882 0.3986 0.4394 0.0309  0.0089  0.0467  120 LEU A CB  
927  C CG  . LEU A 111 ? 0.4217 0.4354 0.4639 0.0285  0.0030  0.0541  120 LEU A CG  
928  C CD1 . LEU A 111 ? 0.4149 0.4534 0.4533 0.0270  -0.0079 0.0606  120 LEU A CD1 
929  C CD2 . LEU A 111 ? 0.3835 0.3853 0.4138 0.0189  0.0018  0.0429  120 LEU A CD2 
930  N N   . PRO A 112 ? 0.3916 0.3755 0.4418 0.0236  0.0236  0.0158  121 PRO A N   
931  C CA  . PRO A 112 ? 0.3948 0.3800 0.4450 0.0223  0.0283  0.0053  121 PRO A CA  
932  C C   . PRO A 112 ? 0.3637 0.3695 0.4150 0.0234  0.0229  0.0100  121 PRO A C   
933  O O   . PRO A 112 ? 0.3392 0.3572 0.3869 0.0208  0.0131  0.0166  121 PRO A O   
934  C CB  . PRO A 112 ? 0.3988 0.3786 0.4357 0.0117  0.0251  -0.0075 121 PRO A CB  
935  C CG  . PRO A 112 ? 0.4182 0.3929 0.4511 0.0082  0.0200  -0.0041 121 PRO A CG  
936  C CD  . PRO A 112 ? 0.3971 0.3784 0.4349 0.0143  0.0168  0.0104  121 PRO A CD  
937  N N   . PRO A 113 ? 0.3706 0.3803 0.4268 0.0262  0.0299  0.0053  122 PRO A N   
938  C CA  . PRO A 113 ? 0.3440 0.3742 0.4040 0.0270  0.0263  0.0102  122 PRO A CA  
939  C C   . PRO A 113 ? 0.3295 0.3666 0.3756 0.0168  0.0189  0.0048  122 PRO A C   
940  O O   . PRO A 113 ? 0.3231 0.3653 0.3659 0.0146  0.0228  -0.0008 122 PRO A O   
941  C CB  . PRO A 113 ? 0.3607 0.3900 0.4312 0.0340  0.0391  0.0063  122 PRO A CB  
942  C CG  . PRO A 113 ? 0.3615 0.3706 0.4241 0.0306  0.0471  -0.0076 122 PRO A CG  
943  C CD  . PRO A 113 ? 0.3843 0.3799 0.4430 0.0279  0.0426  -0.0060 122 PRO A CD  
944  N N   . ILE A 114 ? 0.3080 0.3452 0.3466 0.0112  0.0093  0.0072  123 ILE A N   
945  C CA  . ILE A 114 ? 0.3102 0.3527 0.3389 0.0028  0.0024  0.0049  123 ILE A CA  
946  C C   . ILE A 114 ? 0.3308 0.3765 0.3580 -0.0004 -0.0066 0.0104  123 ILE A C   
947  O O   . ILE A 114 ? 0.3562 0.3972 0.3848 0.0024  -0.0077 0.0138  123 ILE A O   
948  C CB  . ILE A 114 ? 0.3205 0.3529 0.3373 -0.0024 0.0036  -0.0048 123 ILE A CB  
949  C CG1 . ILE A 114 ? 0.3098 0.3491 0.3186 -0.0090 -0.0023 -0.0043 123 ILE A CG1 
950  C CG2 . ILE A 114 ? 0.3102 0.3291 0.3243 -0.0034 0.0023  -0.0076 123 ILE A CG2 
951  C CD1 . ILE A 114 ? 0.3449 0.3815 0.3427 -0.0132 -0.0016 -0.0116 123 ILE A CD1 
952  N N   . LEU A 115 ? 0.3088 0.3621 0.3331 -0.0066 -0.0121 0.0113  124 LEU A N   
953  C CA  . LEU A 115 ? 0.2826 0.3379 0.3046 -0.0111 -0.0194 0.0136  124 LEU A CA  
954  C C   . LEU A 115 ? 0.2710 0.3123 0.2847 -0.0126 -0.0205 0.0097  124 LEU A C   
955  O O   . LEU A 115 ? 0.2940 0.3281 0.3024 -0.0151 -0.0197 0.0049  124 LEU A O   
956  C CB  . LEU A 115 ? 0.2686 0.3305 0.2905 -0.0182 -0.0228 0.0135  124 LEU A CB  
957  C CG  . LEU A 115 ? 0.2701 0.3365 0.2920 -0.0240 -0.0291 0.0142  124 LEU A CG  
958  C CD1 . LEU A 115 ? 0.3097 0.3936 0.3402 -0.0226 -0.0318 0.0192  124 LEU A CD1 
959  C CD2 . LEU A 115 ? 0.2978 0.3630 0.3197 -0.0315 -0.0299 0.0125  124 LEU A CD2 
960  N N   . VAL A 116 ? 0.2845 0.3242 0.2977 -0.0110 -0.0223 0.0125  125 VAL A N   
961  C CA  . VAL A 116 ? 0.2901 0.3182 0.2969 -0.0128 -0.0226 0.0095  125 VAL A CA  
962  C C   . VAL A 116 ? 0.2978 0.3289 0.2997 -0.0177 -0.0277 0.0094  125 VAL A C   
963  O O   . VAL A 116 ? 0.2769 0.3193 0.2802 -0.0202 -0.0315 0.0115  125 VAL A O   
964  C CB  . VAL A 116 ? 0.2793 0.2994 0.2881 -0.0072 -0.0177 0.0121  125 VAL A CB  
965  C CG1 . VAL A 116 ? 0.2836 0.2984 0.2979 -0.0031 -0.0109 0.0095  125 VAL A CG1 
966  C CG2 . VAL A 116 ? 0.3374 0.3660 0.3487 -0.0031 -0.0193 0.0213  125 VAL A CG2 
967  N N   . TYR A 117 ? 0.2986 0.3202 0.2956 -0.0198 -0.0272 0.0058  126 TYR A N   
968  C CA  . TYR A 117 ? 0.2922 0.3141 0.2838 -0.0242 -0.0297 0.0038  126 TYR A CA  
969  C C   . TYR A 117 ? 0.2865 0.3190 0.2749 -0.0238 -0.0322 0.0085  126 TYR A C   
970  O O   . TYR A 117 ? 0.2910 0.3311 0.2758 -0.0292 -0.0359 0.0060  126 TYR A O   
971  C CB  . TYR A 117 ? 0.2976 0.3087 0.2865 -0.0244 -0.0266 0.0007  126 TYR A CB  
972  C CG  . TYR A 117 ? 0.2654 0.2748 0.2490 -0.0282 -0.0267 -0.0028 126 TYR A CG  
973  C CD1 . TYR A 117 ? 0.2597 0.2652 0.2448 -0.0319 -0.0270 -0.0080 126 TYR A CD1 
974  C CD2 . TYR A 117 ? 0.2787 0.2895 0.2560 -0.0277 -0.0252 -0.0006 126 TYR A CD2 
975  C CE1 . TYR A 117 ? 0.2920 0.2941 0.2732 -0.0351 -0.0250 -0.0129 126 TYR A CE1 
976  C CE2 . TYR A 117 ? 0.3247 0.3342 0.2956 -0.0316 -0.0238 -0.0053 126 TYR A CE2 
977  C CZ  . TYR A 117 ? 0.3044 0.3089 0.2777 -0.0353 -0.0233 -0.0125 126 TYR A CZ  
978  O OH  . TYR A 117 ? 0.3272 0.3288 0.2954 -0.0388 -0.0201 -0.0188 126 TYR A OH  
979  N N   . ALA A 118 ? 0.3164 0.3499 0.3065 -0.0177 -0.0300 0.0154  127 ALA A N   
980  C CA  . ALA A 118 ? 0.3345 0.3813 0.3227 -0.0154 -0.0329 0.0235  127 ALA A CA  
981  C C   . ALA A 118 ? 0.3316 0.3970 0.3251 -0.0163 -0.0383 0.0265  127 ALA A C   
982  O O   . ALA A 118 ? 0.3602 0.4417 0.3503 -0.0173 -0.0432 0.0313  127 ALA A O   
983  C CB  . ALA A 118 ? 0.3566 0.3984 0.3487 -0.0070 -0.0278 0.0325  127 ALA A CB  
984  N N   . ASP A 119 ? 0.3320 0.3974 0.3336 -0.0164 -0.0375 0.0240  128 ASP A N   
985  C CA  . ASP A 119 ? 0.3271 0.4105 0.3358 -0.0188 -0.0418 0.0257  128 ASP A CA  
986  C C   . ASP A 119 ? 0.3377 0.4227 0.3422 -0.0296 -0.0455 0.0172  128 ASP A C   
987  O O   . ASP A 119 ? 0.3546 0.4548 0.3572 -0.0354 -0.0510 0.0165  128 ASP A O   
988  C CB  . ASP A 119 ? 0.3378 0.4208 0.3572 -0.0147 -0.0376 0.0268  128 ASP A CB  
989  C CG  . ASP A 119 ? 0.3402 0.4182 0.3657 -0.0042 -0.0315 0.0329  128 ASP A CG  
990  O OD1 . ASP A 119 ? 0.3016 0.3867 0.3298 0.0017  -0.0323 0.0418  128 ASP A OD1 
991  O OD2 . ASP A 119 ? 0.2637 0.3308 0.2913 -0.0021 -0.0256 0.0289  128 ASP A OD2 
992  N N   . CYS A 120 ? 0.3365 0.4064 0.3401 -0.0325 -0.0422 0.0109  129 CYS A N   
993  C CA  . CYS A 120 ? 0.3365 0.4054 0.3409 -0.0416 -0.0435 0.0043  129 CYS A CA  
994  C C   . CYS A 120 ? 0.3399 0.4012 0.3357 -0.0480 -0.0440 -0.0034 129 CYS A C   
995  O O   . CYS A 120 ? 0.3238 0.3844 0.3212 -0.0563 -0.0445 -0.0097 129 CYS A O   
996  C CB  . CYS A 120 ? 0.3202 0.3788 0.3291 -0.0410 -0.0394 0.0038  129 CYS A CB  
997  S SG  . CYS A 120 ? 0.3408 0.3804 0.3440 -0.0368 -0.0355 0.0017  129 CYS A SG  
998  N N   . VAL A 121 ? 0.3449 0.3997 0.3324 -0.0444 -0.0426 -0.0033 130 VAL A N   
999  C CA  . VAL A 121 ? 0.3443 0.3946 0.3225 -0.0499 -0.0420 -0.0108 130 VAL A CA  
1000 C C   . VAL A 121 ? 0.3440 0.4100 0.3133 -0.0503 -0.0460 -0.0077 130 VAL A C   
1001 O O   . VAL A 121 ? 0.3551 0.4325 0.3192 -0.0583 -0.0497 -0.0133 130 VAL A O   
1002 C CB  . VAL A 121 ? 0.3407 0.3734 0.3167 -0.0465 -0.0365 -0.0131 130 VAL A CB  
1003 C CG1 . VAL A 121 ? 0.3658 0.3941 0.3327 -0.0513 -0.0340 -0.0212 130 VAL A CG1 
1004 C CG2 . VAL A 121 ? 0.3535 0.3751 0.3381 -0.0461 -0.0339 -0.0145 130 VAL A CG2 
1005 N N   . LEU A 122 ? 0.3236 0.3908 0.2915 -0.0420 -0.0451 0.0015  131 LEU A N   
1006 C CA  . LEU A 122 ? 0.3419 0.4218 0.2999 -0.0408 -0.0475 0.0071  131 LEU A CA  
1007 C C   . LEU A 122 ? 0.3341 0.4397 0.2938 -0.0418 -0.0552 0.0135  131 LEU A C   
1008 O O   . LEU A 122 ? 0.3341 0.4551 0.2828 -0.0447 -0.0592 0.0152  131 LEU A O   
1009 C CB  . LEU A 122 ? 0.3324 0.4036 0.2906 -0.0314 -0.0427 0.0166  131 LEU A CB  
1010 C CG  . LEU A 122 ? 0.2838 0.3338 0.2420 -0.0306 -0.0356 0.0113  131 LEU A CG  
1011 C CD1 . LEU A 122 ? 0.2916 0.3352 0.2504 -0.0233 -0.0308 0.0205  131 LEU A CD1 
1012 C CD2 . LEU A 122 ? 0.3077 0.3530 0.2562 -0.0376 -0.0337 0.0011  131 LEU A CD2 
1013 N N   . ALA A 123 ? 0.3462 0.4587 0.3196 -0.0394 -0.0571 0.0173  132 ALA A N   
1014 C CA  . ALA A 123 ? 0.3594 0.4995 0.3389 -0.0396 -0.0644 0.0245  132 ALA A CA  
1015 C C   . ALA A 123 ? 0.3490 0.4994 0.3356 -0.0502 -0.0684 0.0156  132 ALA A C   
1016 O O   . ALA A 123 ? 0.3708 0.5466 0.3651 -0.0520 -0.0748 0.0203  132 ALA A O   
1017 C CB  . ALA A 123 ? 0.3660 0.5093 0.3590 -0.0270 -0.0622 0.0380  132 ALA A CB  
1018 N N   . ASN A 124 ? 0.3478 0.4794 0.3331 -0.0573 -0.0643 0.0038  133 ASN A N   
1019 C CA  . ASN A 124 ? 0.3606 0.4948 0.3554 -0.0665 -0.0650 -0.0035 133 ASN A CA  
1020 C C   . ASN A 124 ? 0.3490 0.4840 0.3354 -0.0804 -0.0667 -0.0174 133 ASN A C   
1021 O O   . ASN A 124 ? 0.3412 0.4582 0.3298 -0.0867 -0.0617 -0.0269 133 ASN A O   
1022 C CB  . ASN A 124 ? 0.3280 0.4392 0.3294 -0.0632 -0.0577 -0.0046 133 ASN A CB  
1023 C CG  . ASN A 124 ? 0.3636 0.4767 0.3768 -0.0710 -0.0569 -0.0081 133 ASN A CG  
1024 O OD1 . ASN A 124 ? 0.3991 0.5327 0.4192 -0.0780 -0.0617 -0.0090 133 ASN A OD1 
1025 N ND2 . ASN A 124 ? 0.2913 0.3848 0.3077 -0.0698 -0.0508 -0.0093 133 ASN A ND2 
1026 N N   . TRP A 125 ? 0.3674 0.5235 0.3442 -0.0850 -0.0733 -0.0185 134 TRP A N   
1027 C CA  . TRP A 125 ? 0.3836 0.5402 0.3494 -0.0990 -0.0740 -0.0343 134 TRP A CA  
1028 C C   . TRP A 125 ? 0.4085 0.5987 0.3672 -0.1072 -0.0839 -0.0357 134 TRP A C   
1029 O O   . TRP A 125 ? 0.4217 0.6356 0.3819 -0.0996 -0.0906 -0.0215 134 TRP A O   
1030 C CB  . TRP A 125 ? 0.3733 0.5076 0.3242 -0.0967 -0.0670 -0.0403 134 TRP A CB  
1031 C CG  . TRP A 125 ? 0.3783 0.5215 0.3154 -0.0886 -0.0689 -0.0309 134 TRP A CG  
1032 C CD1 . TRP A 125 ? 0.3881 0.5220 0.3271 -0.0750 -0.0657 -0.0177 134 TRP A CD1 
1033 C CD2 . TRP A 125 ? 0.4357 0.5980 0.3545 -0.0944 -0.0733 -0.0340 134 TRP A CD2 
1034 N NE1 . TRP A 125 ? 0.4212 0.5658 0.3459 -0.0715 -0.0672 -0.0110 134 TRP A NE1 
1035 C CE2 . TRP A 125 ? 0.4245 0.5876 0.3356 -0.0828 -0.0722 -0.0200 134 TRP A CE2 
1036 C CE3 . TRP A 125 ? 0.4489 0.6284 0.3566 -0.1091 -0.0779 -0.0478 134 TRP A CE3 
1037 C CZ2 . TRP A 125 ? 0.4554 0.6367 0.3474 -0.0843 -0.0754 -0.0170 134 TRP A CZ2 
1038 C CZ3 . TRP A 125 ? 0.4856 0.6851 0.3725 -0.1113 -0.0819 -0.0466 134 TRP A CZ3 
1039 C CH2 . TRP A 125 ? 0.4823 0.6830 0.3613 -0.0984 -0.0807 -0.0300 134 TRP A CH2 
1040 N N   . LYS A 126 ? 0.4410 0.6335 0.3929 -0.1230 -0.0845 -0.0531 135 LYS A N   
1041 C CA  . LYS A 126 ? 0.4693 0.6948 0.4103 -0.1342 -0.0941 -0.0587 135 LYS A CA  
1042 C C   . LYS A 126 ? 0.4884 0.7032 0.4146 -0.1497 -0.0898 -0.0815 135 LYS A C   
1043 O O   . LYS A 126 ? 0.4728 0.6564 0.4043 -0.1532 -0.0796 -0.0929 135 LYS A O   
1044 C CB  . LYS A 126 ? 0.4654 0.7199 0.4237 -0.1416 -0.1028 -0.0566 135 LYS A CB  
1045 C CG  . LYS A 126 ? 0.4904 0.7292 0.4644 -0.1540 -0.0973 -0.0702 135 LYS A CG  
1046 C CD  . LYS A 126 ? 0.5017 0.7719 0.4944 -0.1621 -0.1054 -0.0678 135 LYS A CD  
1047 C CE  . LYS A 126 ? 0.5791 0.8868 0.5628 -0.1778 -0.1168 -0.0777 135 LYS A CE  
1048 N NZ  . LYS A 126 ? 0.5886 0.9249 0.5935 -0.1900 -0.1235 -0.0799 135 LYS A NZ  
1049 N N   . LYS A 127 ? 0.5153 0.7568 0.4231 -0.1583 -0.0969 -0.0875 136 LYS A N   
1050 C CA  . LYS A 127 ? 0.5602 0.7997 0.4547 -0.1769 -0.0942 -0.1124 136 LYS A CA  
1051 C C   . LYS A 127 ? 0.5775 0.8362 0.4861 -0.1939 -0.1006 -0.1234 136 LYS A C   
1052 O O   . LYS A 127 ? 0.5823 0.8757 0.4998 -0.1935 -0.1124 -0.1116 136 LYS A O   
1053 C CB  . LYS A 127 ? 0.5802 0.8440 0.4465 -0.1808 -0.0995 -0.1153 136 LYS A CB  
1054 C CG  . LYS A 127 ? 0.5801 0.8217 0.4305 -0.1688 -0.0902 -0.1106 136 LYS A CG  
1055 C CD  . LYS A 127 ? 0.6216 0.8884 0.4422 -0.1751 -0.0943 -0.1152 136 LYS A CD  
1056 C CE  . LYS A 127 ? 0.6149 0.8598 0.4200 -0.1651 -0.0833 -0.1122 136 LYS A CE  
1057 N NZ  . LYS A 127 ? 0.6212 0.8911 0.3954 -0.1721 -0.0861 -0.1172 136 LYS A NZ  
1058 N N   . LYS A 128 ? 0.6049 0.8409 0.5177 -0.2085 -0.0919 -0.1455 137 LYS A N   
1059 C CA  . LYS A 128 ? 0.6204 0.8741 0.5438 -0.2292 -0.0966 -0.1611 137 LYS A CA  
1060 C C   . LYS A 128 ? 0.6544 0.9492 0.5567 -0.2435 -0.1083 -0.1718 137 LYS A C   
1061 O O   . LYS A 128 ? 0.6472 0.9823 0.5567 -0.2512 -0.1216 -0.1679 137 LYS A O   
1062 C CB  . LYS A 128 ? 0.6370 0.8526 0.5684 -0.2418 -0.0822 -0.1833 137 LYS A CB  
1063 C CG  . LYS A 128 ? 0.6075 0.7862 0.5613 -0.2303 -0.0714 -0.1729 137 LYS A CG  
1064 C CD  . LYS A 128 ? 0.6462 0.7856 0.6057 -0.2406 -0.0558 -0.1933 137 LYS A CD  
1065 C CE  . LYS A 128 ? 0.6402 0.7473 0.6235 -0.2317 -0.0460 -0.1823 137 LYS A CE  
1066 N NZ  . LYS A 128 ? 0.6131 0.6798 0.6028 -0.2386 -0.0296 -0.1992 137 LYS A NZ  
1067 N N   . ASP A 129 ? 0.6843 0.9702 0.5606 -0.2467 -0.1029 -0.1850 138 ASP A N   
1068 C CA  . ASP A 129 ? 0.7183 1.0421 0.5679 -0.2586 -0.1129 -0.1945 138 ASP A CA  
1069 C C   . ASP A 129 ? 0.7132 1.0441 0.5424 -0.2400 -0.1148 -0.1744 138 ASP A C   
1070 O O   . ASP A 129 ? 0.7065 1.0053 0.5244 -0.2325 -0.1021 -0.1779 138 ASP A O   
1071 C CB  . ASP A 129 ? 0.7530 1.0599 0.5875 -0.2791 -0.1027 -0.2285 138 ASP A CB  
1072 C CG  . ASP A 129 ? 0.7929 1.1426 0.5981 -0.2960 -0.1134 -0.2429 138 ASP A CG  
1073 O OD1 . ASP A 129 ? 0.7945 1.1880 0.5896 -0.2902 -0.1290 -0.2241 138 ASP A OD1 
1074 O OD2 . ASP A 129 ? 0.8692 1.2089 0.6614 -0.3152 -0.1055 -0.2735 138 ASP A OD2 
1075 N N   . PRO A 130 ? 0.7333 1.1060 0.5596 -0.2322 -0.1298 -0.1524 139 PRO A N   
1076 C CA  . PRO A 130 ? 0.7372 1.1209 0.5437 -0.2161 -0.1322 -0.1319 139 PRO A CA  
1077 C C   . PRO A 130 ? 0.7571 1.1424 0.5286 -0.2238 -0.1275 -0.1466 139 PRO A C   
1078 O O   . PRO A 130 ? 0.7594 1.1352 0.5173 -0.2095 -0.1223 -0.1326 139 PRO A O   
1079 C CB  . PRO A 130 ? 0.7474 1.1840 0.5578 -0.2133 -0.1507 -0.1115 139 PRO A CB  
1080 C CG  . PRO A 130 ? 0.7597 1.2012 0.6013 -0.2184 -0.1549 -0.1126 139 PRO A CG  
1081 C CD  . PRO A 130 ? 0.7480 1.1605 0.5927 -0.2374 -0.1448 -0.1436 139 PRO A CD  
1082 N N   . ASN A 131 ? 0.7914 1.1889 0.5489 -0.2467 -0.1285 -0.1749 140 ASN A N   
1083 C CA  . ASN A 131 ? 0.8374 1.2377 0.5600 -0.2567 -0.1228 -0.1931 140 ASN A CA  
1084 C C   . ASN A 131 ? 0.8390 1.1874 0.5594 -0.2583 -0.1015 -0.2148 140 ASN A C   
1085 O O   . ASN A 131 ? 0.8612 1.2082 0.5538 -0.2662 -0.0939 -0.2319 140 ASN A O   
1086 C CB  . ASN A 131 ? 0.8864 1.3294 0.5922 -0.2820 -0.1345 -0.2149 140 ASN A CB  
1087 C CG  . ASN A 131 ? 0.9160 1.4181 0.6186 -0.2795 -0.1562 -0.1918 140 ASN A CG  
1088 O OD1 . ASN A 131 ? 0.9582 1.4914 0.6749 -0.2923 -0.1689 -0.1965 140 ASN A OD1 
1089 N ND2 . ASN A 131 ? 0.9196 1.4380 0.6055 -0.2626 -0.1600 -0.1656 140 ASN A ND2 
1090 N N   . LYS A 132 ? 0.8114 1.1192 0.5607 -0.2505 -0.0917 -0.2134 141 LYS A N   
1091 C CA  . LYS A 132 ? 0.8103 1.0690 0.5631 -0.2481 -0.0717 -0.2285 141 LYS A CA  
1092 C C   . LYS A 132 ? 0.7667 0.9996 0.5298 -0.2234 -0.0649 -0.2038 141 LYS A C   
1093 O O   . LYS A 132 ? 0.7001 0.9467 0.4738 -0.2098 -0.0746 -0.1775 141 LYS A O   
1094 C CB  . LYS A 132 ? 0.8193 1.0513 0.5971 -0.2599 -0.0646 -0.2476 141 LYS A CB  
1095 C CG  . LYS A 132 ? 0.8617 1.1075 0.6274 -0.2867 -0.0649 -0.2800 141 LYS A CG  
1096 C CD  . LYS A 132 ? 0.8689 1.0907 0.6631 -0.2989 -0.0588 -0.2955 141 LYS A CD  
1097 C CE  . LYS A 132 ? 0.9094 1.1419 0.6926 -0.3272 -0.0574 -0.3304 141 LYS A CE  
1098 N NZ  . LYS A 132 ? 0.9132 1.1202 0.7261 -0.3399 -0.0501 -0.3449 141 LYS A NZ  
1099 N N   . PRO A 133 ? 0.7733 0.9698 0.5345 -0.2181 -0.0479 -0.2128 142 PRO A N   
1100 C CA  . PRO A 133 ? 0.7482 0.9254 0.5165 -0.1967 -0.0420 -0.1909 142 PRO A CA  
1101 C C   . PRO A 133 ? 0.7074 0.8638 0.5073 -0.1839 -0.0424 -0.1744 142 PRO A C   
1102 O O   . PRO A 133 ? 0.7059 0.8565 0.5244 -0.1909 -0.0445 -0.1807 142 PRO A O   
1103 C CB  . PRO A 133 ? 0.7762 0.9226 0.5372 -0.1971 -0.0233 -0.2086 142 PRO A CB  
1104 C CG  . PRO A 133 ? 0.8089 0.9624 0.5530 -0.2182 -0.0197 -0.2389 142 PRO A CG  
1105 C CD  . PRO A 133 ? 0.8086 0.9808 0.5631 -0.2311 -0.0325 -0.2434 142 PRO A CD  
1106 N N   . LEU A 134 ? 0.6741 0.8200 0.4789 -0.1661 -0.0398 -0.1541 143 LEU A N   
1107 C CA  . LEU A 134 ? 0.6267 0.7504 0.4580 -0.1532 -0.0380 -0.1399 143 LEU A CA  
1108 C C   . LEU A 134 ? 0.6138 0.7002 0.4590 -0.1528 -0.0234 -0.1530 143 LEU A C   
1109 O O   . LEU A 134 ? 0.6073 0.6747 0.4545 -0.1421 -0.0140 -0.1484 143 LEU A O   
1110 C CB  . LEU A 134 ? 0.6175 0.7429 0.4487 -0.1359 -0.0395 -0.1160 143 LEU A CB  
1111 C CG  . LEU A 134 ? 0.6466 0.8048 0.4714 -0.1317 -0.0529 -0.0971 143 LEU A CG  
1112 C CD1 . LEU A 134 ? 0.6512 0.8064 0.4723 -0.1166 -0.0502 -0.0773 143 LEU A CD1 
1113 C CD2 . LEU A 134 ? 0.6743 0.8403 0.5205 -0.1303 -0.0620 -0.0884 143 LEU A CD2 
1114 N N   . THR A 135 ? 0.6149 0.6918 0.4712 -0.1645 -0.0212 -0.1685 144 THR A N   
1115 C CA  . THR A 135 ? 0.6006 0.6419 0.4746 -0.1639 -0.0075 -0.1787 144 THR A CA  
1116 C C   . THR A 135 ? 0.5714 0.6059 0.4692 -0.1647 -0.0113 -0.1725 144 THR A C   
1117 O O   . THR A 135 ? 0.5546 0.6127 0.4532 -0.1710 -0.0230 -0.1682 144 THR A O   
1118 C CB  . THR A 135 ? 0.6418 0.6725 0.5069 -0.1793 0.0032  -0.2070 144 THR A CB  
1119 O OG1 . THR A 135 ? 0.6876 0.7377 0.5488 -0.1970 -0.0051 -0.2195 144 THR A OG1 
1120 C CG2 . THR A 135 ? 0.6530 0.6911 0.4925 -0.1795 0.0087  -0.2150 144 THR A CG2 
1121 N N   . TYR A 136 ? 0.5519 0.5560 0.4694 -0.1585 -0.0011 -0.1713 145 TYR A N   
1122 C CA  . TYR A 136 ? 0.5384 0.5341 0.4784 -0.1580 -0.0030 -0.1632 145 TYR A CA  
1123 C C   . TYR A 136 ? 0.5391 0.5445 0.4827 -0.1764 -0.0064 -0.1770 145 TYR A C   
1124 O O   . TYR A 136 ? 0.4804 0.5017 0.4331 -0.1782 -0.0158 -0.1669 145 TYR A O   
1125 C CB  . TYR A 136 ? 0.5406 0.5021 0.4997 -0.1500 0.0100  -0.1615 145 TYR A CB  
1126 C CG  . TYR A 136 ? 0.5217 0.4763 0.5016 -0.1464 0.0079  -0.1478 145 TYR A CG  
1127 C CD1 . TYR A 136 ? 0.5205 0.4813 0.5053 -0.1324 0.0017  -0.1267 145 TYR A CD1 
1128 C CD2 . TYR A 136 ? 0.5548 0.4972 0.5493 -0.1581 0.0129  -0.1566 145 TYR A CD2 
1129 C CE1 . TYR A 136 ? 0.4872 0.4438 0.4883 -0.1294 0.0002  -0.1144 145 TYR A CE1 
1130 C CE2 . TYR A 136 ? 0.5606 0.4981 0.5733 -0.1548 0.0117  -0.1426 145 TYR A CE2 
1131 C CZ  . TYR A 136 ? 0.4865 0.4320 0.5013 -0.1402 0.0052  -0.1213 145 TYR A CZ  
1132 O OH  . TYR A 136 ? 0.5028 0.4453 0.5329 -0.1368 0.0045  -0.1074 145 TYR A OH  
1133 N N   . GLU A 137 ? 0.5683 0.5650 0.5050 -0.1906 0.0017  -0.2008 146 GLU A N   
1134 C CA  . GLU A 137 ? 0.6051 0.6095 0.5452 -0.2112 0.0000  -0.2185 146 GLU A CA  
1135 C C   . GLU A 137 ? 0.6024 0.6501 0.5298 -0.2204 -0.0171 -0.2167 146 GLU A C   
1136 O O   . GLU A 137 ? 0.6050 0.6651 0.5410 -0.2358 -0.0218 -0.2253 146 GLU A O   
1137 C CB  . GLU A 137 ? 0.6346 0.6212 0.5668 -0.2250 0.0132  -0.2473 146 GLU A CB  
1138 C CG  . GLU A 137 ? 0.6681 0.6519 0.6093 -0.2476 0.0161  -0.2689 146 GLU A CG  
1139 C CD  . GLU A 137 ? 0.7098 0.6650 0.6487 -0.2590 0.0338  -0.2975 146 GLU A CD  
1140 O OE1 . GLU A 137 ? 0.7176 0.6720 0.6365 -0.2559 0.0394  -0.3070 146 GLU A OE1 
1141 O OE2 . GLU A 137 ? 0.7270 0.6599 0.6848 -0.2712 0.0435  -0.3108 146 GLU A OE2 
1142 N N   . ASN A 138 ? 0.5980 0.6691 0.5064 -0.2112 -0.0259 -0.2054 147 ASN A N   
1143 C CA  . ASN A 138 ? 0.5972 0.7118 0.4941 -0.2162 -0.0425 -0.1989 147 ASN A CA  
1144 C C   . ASN A 138 ? 0.5471 0.6748 0.4536 -0.1989 -0.0518 -0.1704 147 ASN A C   
1145 O O   . ASN A 138 ? 0.5375 0.6977 0.4333 -0.1955 -0.0638 -0.1587 147 ASN A O   
1146 C CB  . ASN A 138 ? 0.6023 0.7361 0.4687 -0.2197 -0.0449 -0.2073 147 ASN A CB  
1147 C CG  . ASN A 138 ? 0.6264 0.8086 0.4798 -0.2251 -0.0626 -0.1999 147 ASN A CG  
1148 O OD1 . ASN A 138 ? 0.6189 0.8230 0.4815 -0.2380 -0.0714 -0.2047 147 ASN A OD1 
1149 N ND2 . ASN A 138 ? 0.6594 0.8594 0.4932 -0.2147 -0.0676 -0.1864 147 ASN A ND2 
1150 N N   . MET A 139 ? 0.5196 0.6227 0.4462 -0.1880 -0.0460 -0.1587 148 MET A N   
1151 C CA  . MET A 139 ? 0.5046 0.6176 0.4399 -0.1722 -0.0529 -0.1342 148 MET A CA  
1152 C C   . MET A 139 ? 0.4823 0.5860 0.4420 -0.1711 -0.0516 -0.1266 148 MET A C   
1153 O O   . MET A 139 ? 0.4928 0.5718 0.4643 -0.1776 -0.0422 -0.1363 148 MET A O   
1154 C CB  . MET A 139 ? 0.4895 0.5853 0.4184 -0.1549 -0.0475 -0.1228 148 MET A CB  
1155 C CG  . MET A 139 ? 0.5446 0.6551 0.4495 -0.1533 -0.0499 -0.1238 148 MET A CG  
1156 S SD  . MET A 139 ? 0.5523 0.6376 0.4524 -0.1371 -0.0398 -0.1159 148 MET A SD  
1157 C CE  . MET A 139 ? 0.5268 0.6260 0.4337 -0.1211 -0.0484 -0.0893 148 MET A CE  
1158 N N   A ASP A 140 ? 0.4676 0.5912 0.4350 -0.1626 -0.0600 -0.1088 149 ASP A N   
1159 N N   B ASP A 140 ? 0.4666 0.5907 0.4338 -0.1627 -0.0602 -0.1088 149 ASP A N   
1160 C CA  A ASP A 140 ? 0.4507 0.5660 0.4390 -0.1578 -0.0578 -0.0980 149 ASP A CA  
1161 C CA  B ASP A 140 ? 0.4500 0.5686 0.4383 -0.1585 -0.0588 -0.0980 149 ASP A CA  
1162 C C   A ASP A 140 ? 0.4211 0.5442 0.4112 -0.1401 -0.0617 -0.0773 149 ASP A C   
1163 C C   B ASP A 140 ? 0.4188 0.5416 0.4087 -0.1400 -0.0616 -0.0773 149 ASP A C   
1164 O O   A ASP A 140 ? 0.4107 0.5507 0.3893 -0.1333 -0.0678 -0.0703 149 ASP A O   
1165 O O   B ASP A 140 ? 0.4023 0.5391 0.3799 -0.1324 -0.0669 -0.0704 149 ASP A O   
1166 C CB  A ASP A 140 ? 0.4584 0.5940 0.4608 -0.1724 -0.0627 -0.1030 149 ASP A CB  
1167 C CB  B ASP A 140 ? 0.4537 0.5995 0.4541 -0.1720 -0.0661 -0.1012 149 ASP A CB  
1168 C CG  A ASP A 140 ? 0.4448 0.5587 0.4674 -0.1748 -0.0541 -0.1015 149 ASP A CG  
1169 C CG  B ASP A 140 ? 0.4778 0.6102 0.4863 -0.1908 -0.0597 -0.1203 149 ASP A CG  
1170 O OD1 A ASP A 140 ? 0.3441 0.4425 0.3728 -0.1609 -0.0496 -0.0875 149 ASP A OD1 
1171 O OD1 B ASP A 140 ? 0.4717 0.5714 0.4900 -0.1894 -0.0483 -0.1219 149 ASP A OD1 
1172 O OD2 A ASP A 140 ? 0.4458 0.5589 0.4780 -0.1915 -0.0516 -0.1146 149 ASP A OD2 
1173 O OD2 B ASP A 140 ? 0.4476 0.6031 0.4539 -0.2072 -0.0659 -0.1334 149 ASP A OD2 
1174 N N   . VAL A 141 ? 0.4144 0.5243 0.4188 -0.1331 -0.0573 -0.0678 150 VAL A N   
1175 C CA  . VAL A 141 ? 0.3927 0.5096 0.4010 -0.1180 -0.0597 -0.0504 150 VAL A CA  
1176 C C   . VAL A 141 ? 0.3859 0.5336 0.4054 -0.1209 -0.0672 -0.0440 150 VAL A C   
1177 O O   . VAL A 141 ? 0.3772 0.5382 0.4039 -0.1349 -0.0699 -0.0525 150 VAL A O   
1178 C CB  . VAL A 141 ? 0.3733 0.4658 0.3894 -0.1088 -0.0518 -0.0431 150 VAL A CB  
1179 C CG1 . VAL A 141 ? 0.4196 0.4869 0.4263 -0.1043 -0.0455 -0.0474 150 VAL A CG1 
1180 C CG2 . VAL A 141 ? 0.4420 0.5278 0.4736 -0.1167 -0.0473 -0.0444 150 VAL A CG2 
1181 N N   . LEU A 142 ? 0.3642 0.5237 0.3866 -0.1079 -0.0700 -0.0296 151 LEU A N   
1182 C CA  . LEU A 142 ? 0.3583 0.5473 0.3950 -0.1076 -0.0757 -0.0213 151 LEU A CA  
1183 C C   . LEU A 142 ? 0.3461 0.5269 0.3986 -0.1055 -0.0693 -0.0162 151 LEU A C   
1184 O O   . LEU A 142 ? 0.3329 0.5323 0.4004 -0.1130 -0.0712 -0.0160 151 LEU A O   
1185 C CB  . LEU A 142 ? 0.3485 0.5552 0.3825 -0.0940 -0.0807 -0.0077 151 LEU A CB  
1186 C CG  . LEU A 142 ? 0.3424 0.5576 0.3586 -0.0944 -0.0864 -0.0092 151 LEU A CG  
1187 C CD1 . LEU A 142 ? 0.3624 0.5973 0.3807 -0.0806 -0.0907 0.0075  151 LEU A CD1 
1188 C CD2 . LEU A 142 ? 0.3919 0.6276 0.4031 -0.1115 -0.0935 -0.0218 151 LEU A CD2 
1189 N N   . PHE A 143 ? 0.3452 0.5005 0.3944 -0.0960 -0.0619 -0.0123 152 PHE A N   
1190 C CA  . PHE A 143 ? 0.3415 0.4899 0.4022 -0.0933 -0.0554 -0.0066 152 PHE A CA  
1191 C C   . PHE A 143 ? 0.3361 0.4541 0.3926 -0.0936 -0.0476 -0.0095 152 PHE A C   
1192 O O   . PHE A 143 ? 0.3108 0.4111 0.3555 -0.0896 -0.0463 -0.0127 152 PHE A O   
1193 C CB  . PHE A 143 ? 0.3367 0.4936 0.4010 -0.0789 -0.0544 0.0050  152 PHE A CB  
1194 C CG  . PHE A 143 ? 0.3185 0.5057 0.3905 -0.0762 -0.0612 0.0108  152 PHE A CG  
1195 C CD1 . PHE A 143 ? 0.3639 0.5760 0.4536 -0.0812 -0.0628 0.0139  152 PHE A CD1 
1196 C CD2 . PHE A 143 ? 0.3548 0.5477 0.4175 -0.0691 -0.0660 0.0143  152 PHE A CD2 
1197 C CE1 . PHE A 143 ? 0.3650 0.6092 0.4643 -0.0779 -0.0699 0.0208  152 PHE A CE1 
1198 C CE2 . PHE A 143 ? 0.3534 0.5765 0.4241 -0.0655 -0.0728 0.0223  152 PHE A CE2 
1199 C CZ  . PHE A 143 ? 0.3633 0.6131 0.4528 -0.0695 -0.0752 0.0257  152 PHE A CZ  
1200 N N   A SER A 144 ? 0.3326 0.4469 0.3999 -0.0980 -0.0423 -0.0071 153 SER A N   
1201 N N   B SER A 144 ? 0.3333 0.4474 0.4007 -0.0984 -0.0424 -0.0074 153 SER A N   
1202 C CA  A SER A 144 ? 0.3440 0.4336 0.4103 -0.0970 -0.0348 -0.0055 153 SER A CA  
1203 C CA  B SER A 144 ? 0.3450 0.4345 0.4112 -0.0970 -0.0348 -0.0055 153 SER A CA  
1204 C C   A SER A 144 ? 0.3380 0.4326 0.4119 -0.0926 -0.0299 0.0048  153 SER A C   
1205 C C   B SER A 144 ? 0.3380 0.4328 0.4110 -0.0916 -0.0301 0.0050  153 SER A C   
1206 O O   A SER A 144 ? 0.3456 0.4616 0.4292 -0.0936 -0.0311 0.0082  153 SER A O   
1207 O O   B SER A 144 ? 0.3439 0.4601 0.4250 -0.0906 -0.0316 0.0089  153 SER A O   
1208 C CB  A SER A 144 ? 0.3591 0.4369 0.4317 -0.1106 -0.0315 -0.0138 153 SER A CB  
1209 C CB  B SER A 144 ? 0.3616 0.4389 0.4349 -0.1104 -0.0309 -0.0131 153 SER A CB  
1210 O OG  A SER A 144 ? 0.3456 0.4191 0.4098 -0.1155 -0.0348 -0.0253 153 SER A OG  
1211 O OG  B SER A 144 ? 0.3470 0.4392 0.4353 -0.1203 -0.0300 -0.0123 153 SER A OG  
1212 N N   . PHE A 145 ? 0.3340 0.4110 0.4036 -0.0877 -0.0242 0.0100  154 PHE A N   
1213 C CA  . PHE A 145 ? 0.3337 0.4152 0.4062 -0.0832 -0.0188 0.0197  154 PHE A CA  
1214 C C   . PHE A 145 ? 0.3436 0.4228 0.4280 -0.0926 -0.0125 0.0239  154 PHE A C   
1215 O O   . PHE A 145 ? 0.3635 0.4588 0.4573 -0.0949 -0.0096 0.0286  154 PHE A O   
1216 C CB  . PHE A 145 ? 0.3350 0.4036 0.3949 -0.0729 -0.0169 0.0241  154 PHE A CB  
1217 C CG  . PHE A 145 ? 0.3034 0.3747 0.3538 -0.0642 -0.0213 0.0208  154 PHE A CG  
1218 C CD1 . PHE A 145 ? 0.3587 0.4448 0.4101 -0.0583 -0.0211 0.0228  154 PHE A CD1 
1219 C CD2 . PHE A 145 ? 0.3234 0.3821 0.3658 -0.0622 -0.0245 0.0157  154 PHE A CD2 
1220 C CE1 . PHE A 145 ? 0.3360 0.4224 0.3809 -0.0504 -0.0237 0.0204  154 PHE A CE1 
1221 C CE2 . PHE A 145 ? 0.3505 0.4112 0.3855 -0.0549 -0.0275 0.0135  154 PHE A CE2 
1222 C CZ  . PHE A 145 ? 0.3460 0.4195 0.3824 -0.0492 -0.0271 0.0161  154 PHE A CZ  
1223 N N   . ARG A 146 ? 0.3404 0.3991 0.4258 -0.0974 -0.0092 0.0228  155 ARG A N   
1224 C CA  . ARG A 146 ? 0.3700 0.4203 0.4672 -0.1059 -0.0015 0.0281  155 ARG A CA  
1225 C C   . ARG A 146 ? 0.4008 0.4350 0.5055 -0.1168 -0.0001 0.0183  155 ARG A C   
1226 O O   . ARG A 146 ? 0.3832 0.4075 0.4801 -0.1148 -0.0037 0.0096  155 ARG A O   
1227 C CB  . ARG A 146 ? 0.3818 0.4186 0.4731 -0.0981 0.0042  0.0407  155 ARG A CB  
1228 C CG  . ARG A 146 ? 0.3895 0.4393 0.4695 -0.0874 0.0037  0.0484  155 ARG A CG  
1229 C CD  . ARG A 146 ? 0.3671 0.4377 0.4545 -0.0905 0.0071  0.0522  155 ARG A CD  
1230 N NE  . ARG A 146 ? 0.4036 0.4714 0.5027 -0.0987 0.0154  0.0608  155 ARG A NE  
1231 C CZ  . ARG A 146 ? 0.3817 0.4453 0.4764 -0.0956 0.0223  0.0740  155 ARG A CZ  
1232 N NH1 . ARG A 146 ? 0.3892 0.4527 0.4670 -0.0848 0.0209  0.0792  155 ARG A NH1 
1233 N NH2 . ARG A 146 ? 0.4135 0.4741 0.5208 -0.1040 0.0306  0.0825  155 ARG A NH2 
1234 N N   . ASP A 147 ? 0.4281 0.4586 0.5480 -0.1287 0.0063  0.0190  156 ASP A N   
1235 C CA  . ASP A 147 ? 0.4533 0.4637 0.5817 -0.1399 0.0106  0.0091  156 ASP A CA  
1236 C C   . ASP A 147 ? 0.4688 0.4510 0.5935 -0.1317 0.0166  0.0154  156 ASP A C   
1237 O O   . ASP A 147 ? 0.4736 0.4511 0.5971 -0.1232 0.0209  0.0312  156 ASP A O   
1238 C CB  . ASP A 147 ? 0.4861 0.4978 0.6341 -0.1554 0.0176  0.0091  156 ASP A CB  
1239 C CG  . ASP A 147 ? 0.5176 0.5603 0.6729 -0.1654 0.0109  0.0010  156 ASP A CG  
1240 O OD1 . ASP A 147 ? 0.4759 0.5346 0.6218 -0.1631 0.0008  -0.0080 156 ASP A OD1 
1241 O OD2 . ASP A 147 ? 0.5465 0.5989 0.7179 -0.1753 0.0158  0.0050  156 ASP A OD2 
1242 N N   . GLY A 148 ? 0.4555 0.4212 0.5781 -0.1336 0.0167  0.0033  157 GLY A N   
1243 C CA  . GLY A 148 ? 0.4644 0.4055 0.5855 -0.1244 0.0221  0.0083  157 GLY A CA  
1244 C C   . GLY A 148 ? 0.4350 0.3812 0.5408 -0.1084 0.0160  0.0151  157 GLY A C   
1245 O O   . GLY A 148 ? 0.4375 0.3676 0.5439 -0.0998 0.0198  0.0218  157 GLY A O   
1246 N N   . ASP A 149 ? 0.4184 0.3872 0.5125 -0.1044 0.0070  0.0136  158 ASP A N   
1247 C CA  . ASP A 149 ? 0.4009 0.3745 0.4811 -0.0910 0.0016  0.0177  158 ASP A CA  
1248 C C   . ASP A 149 ? 0.4020 0.3658 0.4759 -0.0878 -0.0005 0.0072  158 ASP A C   
1249 O O   . ASP A 149 ? 0.3948 0.3600 0.4598 -0.0776 -0.0038 0.0107  158 ASP A O   
1250 C CB  . ASP A 149 ? 0.3805 0.3781 0.4521 -0.0873 -0.0051 0.0194  158 ASP A CB  
1251 C CG  . ASP A 149 ? 0.3632 0.3751 0.4323 -0.0926 -0.0114 0.0074  158 ASP A CG  
1252 O OD1 . ASP A 149 ? 0.3986 0.4048 0.4700 -0.1007 -0.0117 -0.0038 158 ASP A OD1 
1253 O OD2 . ASP A 149 ? 0.3271 0.3573 0.3919 -0.0884 -0.0158 0.0096  158 ASP A OD2 
1254 N N   . CYS A 150 ? 0.3819 0.3369 0.4601 -0.0974 0.0018  -0.0063 159 CYS A N   
1255 C CA  . CYS A 150 ? 0.4007 0.3467 0.4727 -0.0962 0.0017  -0.0179 159 CYS A CA  
1256 C C   . CYS A 150 ? 0.3991 0.3623 0.4562 -0.0912 -0.0070 -0.0216 159 CYS A C   
1257 O O   . CYS A 150 ? 0.4251 0.3826 0.4754 -0.0857 -0.0071 -0.0256 159 CYS A O   
1258 C CB  . CYS A 150 ? 0.4032 0.3288 0.4804 -0.0871 0.0083  -0.0118 159 CYS A CB  
1259 S SG  . CYS A 150 ? 0.4730 0.3726 0.5696 -0.0931 0.0210  -0.0100 159 CYS A SG  
1260 N N   . SER A 151 ? 0.3855 0.3695 0.4394 -0.0932 -0.0133 -0.0197 160 SER A N   
1261 C CA  . SER A 151 ? 0.3626 0.3625 0.4047 -0.0879 -0.0206 -0.0208 160 SER A CA  
1262 C C   . SER A 151 ? 0.3446 0.3479 0.3794 -0.0942 -0.0232 -0.0339 160 SER A C   
1263 O O   . SER A 151 ? 0.3200 0.3265 0.3442 -0.0882 -0.0261 -0.0349 160 SER A O   
1264 C CB  . SER A 151 ? 0.3600 0.3810 0.4038 -0.0872 -0.0252 -0.0144 160 SER A CB  
1265 O OG  . SER A 151 ? 0.3907 0.4206 0.4437 -0.0988 -0.0252 -0.0185 160 SER A OG  
1266 N N   . LYS A 152 ? 0.3511 0.3544 0.3908 -0.1071 -0.0218 -0.0441 161 LYS A N   
1267 C CA  . LYS A 152 ? 0.3797 0.3857 0.4103 -0.1148 -0.0232 -0.0586 161 LYS A CA  
1268 C C   . LYS A 152 ? 0.3863 0.3727 0.4107 -0.1089 -0.0174 -0.0631 161 LYS A C   
1269 O O   . LYS A 152 ? 0.4117 0.4045 0.4234 -0.1051 -0.0204 -0.0657 161 LYS A O   
1270 C CB  . LYS A 152 ? 0.4069 0.4120 0.4450 -0.1314 -0.0207 -0.0716 161 LYS A CB  
1271 C CG  . LYS A 152 ? 0.4412 0.4522 0.4669 -0.1409 -0.0226 -0.0886 161 LYS A CG  
1272 C CD  . LYS A 152 ? 0.4777 0.4918 0.5098 -0.1598 -0.0212 -0.1041 161 LYS A CD  
1273 C CE  . LYS A 152 ? 0.5054 0.5233 0.5220 -0.1689 -0.0216 -0.1225 161 LYS A CE  
1274 N NZ  . LYS A 152 ? 0.5555 0.5852 0.5747 -0.1892 -0.0234 -0.1396 161 LYS A NZ  
1275 N N   . GLY A 153 ? 0.3787 0.3421 0.4136 -0.1075 -0.0085 -0.0624 162 GLY A N   
1276 C CA  . GLY A 153 ? 0.3852 0.3302 0.4187 -0.1013 -0.0016 -0.0660 162 GLY A CA  
1277 C C   . GLY A 153 ? 0.3633 0.3138 0.3899 -0.0879 -0.0053 -0.0561 162 GLY A C   
1278 O O   . GLY A 153 ? 0.3287 0.2771 0.3472 -0.0849 -0.0037 -0.0616 162 GLY A O   
1279 N N   . PHE A 154 ? 0.3647 0.3226 0.3941 -0.0809 -0.0095 -0.0424 163 PHE A N   
1280 C CA  . PHE A 154 ? 0.3423 0.3051 0.3663 -0.0698 -0.0126 -0.0344 163 PHE A CA  
1281 C C   . PHE A 154 ? 0.3653 0.3433 0.3761 -0.0694 -0.0186 -0.0371 163 PHE A C   
1282 O O   . PHE A 154 ? 0.3653 0.3418 0.3700 -0.0647 -0.0176 -0.0386 163 PHE A O   
1283 C CB  . PHE A 154 ? 0.3443 0.3118 0.3732 -0.0638 -0.0149 -0.0210 163 PHE A CB  
1284 C CG  . PHE A 154 ? 0.3264 0.2992 0.3502 -0.0545 -0.0179 -0.0149 163 PHE A CG  
1285 C CD1 . PHE A 154 ? 0.3340 0.2980 0.3609 -0.0485 -0.0148 -0.0140 163 PHE A CD1 
1286 C CD2 . PHE A 154 ? 0.3364 0.3230 0.3539 -0.0518 -0.0231 -0.0110 163 PHE A CD2 
1287 C CE1 . PHE A 154 ? 0.3237 0.2940 0.3471 -0.0417 -0.0177 -0.0098 163 PHE A CE1 
1288 C CE2 . PHE A 154 ? 0.3261 0.3156 0.3397 -0.0448 -0.0248 -0.0075 163 PHE A CE2 
1289 C CZ  . PHE A 154 ? 0.3158 0.2979 0.3321 -0.0406 -0.0225 -0.0073 163 PHE A CZ  
1290 N N   . PHE A 155 ? 0.3615 0.3552 0.3697 -0.0739 -0.0241 -0.0363 164 PHE A N   
1291 C CA  . PHE A 155 ? 0.3350 0.3444 0.3328 -0.0720 -0.0298 -0.0355 164 PHE A CA  
1292 C C   . PHE A 155 ? 0.3515 0.3627 0.3385 -0.0772 -0.0293 -0.0457 164 PHE A C   
1293 O O   . PHE A 155 ? 0.3224 0.3376 0.3002 -0.0723 -0.0302 -0.0437 164 PHE A O   
1294 C CB  . PHE A 155 ? 0.3490 0.3774 0.3495 -0.0744 -0.0357 -0.0308 164 PHE A CB  
1295 C CG  . PHE A 155 ? 0.3302 0.3606 0.3381 -0.0679 -0.0357 -0.0205 164 PHE A CG  
1296 C CD1 . PHE A 155 ? 0.3472 0.3702 0.3536 -0.0587 -0.0339 -0.0147 164 PHE A CD1 
1297 C CD2 . PHE A 155 ? 0.3160 0.3582 0.3321 -0.0719 -0.0375 -0.0173 164 PHE A CD2 
1298 C CE1 . PHE A 155 ? 0.2637 0.2900 0.2745 -0.0540 -0.0335 -0.0072 164 PHE A CE1 
1299 C CE2 . PHE A 155 ? 0.2812 0.3264 0.3027 -0.0662 -0.0363 -0.0086 164 PHE A CE2 
1300 C CZ  . PHE A 155 ? 0.2949 0.3319 0.3126 -0.0574 -0.0343 -0.0042 164 PHE A CZ  
1301 N N   . LEU A 156 ? 0.3578 0.3654 0.3455 -0.0878 -0.0269 -0.0571 165 LEU A N   
1302 C CA  . LEU A 156 ? 0.3780 0.3894 0.3529 -0.0946 -0.0261 -0.0691 165 LEU A CA  
1303 C C   . LEU A 156 ? 0.3829 0.3776 0.3539 -0.0904 -0.0179 -0.0743 165 LEU A C   
1304 O O   . LEU A 156 ? 0.3858 0.3870 0.3433 -0.0901 -0.0178 -0.0776 165 LEU A O   
1305 C CB  . LEU A 156 ? 0.4148 0.4286 0.3909 -0.1093 -0.0256 -0.0828 165 LEU A CB  
1306 C CG  . LEU A 156 ? 0.4262 0.4646 0.4036 -0.1167 -0.0348 -0.0810 165 LEU A CG  
1307 C CD1 . LEU A 156 ? 0.4598 0.5001 0.4373 -0.1335 -0.0334 -0.0982 165 LEU A CD1 
1308 C CD2 . LEU A 156 ? 0.4567 0.5202 0.4217 -0.1122 -0.0436 -0.0733 165 LEU A CD2 
1309 N N   . VAL A 157 ? 0.3834 0.3583 0.3670 -0.0868 -0.0107 -0.0740 166 VAL A N   
1310 C CA  . VAL A 157 ? 0.3877 0.3488 0.3720 -0.0808 -0.0027 -0.0767 166 VAL A CA  
1311 C C   . VAL A 157 ? 0.3728 0.3417 0.3523 -0.0709 -0.0060 -0.0661 166 VAL A C   
1312 O O   . VAL A 157 ? 0.3919 0.3605 0.3638 -0.0691 -0.0021 -0.0698 166 VAL A O   
1313 C CB  . VAL A 157 ? 0.3962 0.3367 0.3982 -0.0770 0.0054  -0.0754 166 VAL A CB  
1314 C CG1 . VAL A 157 ? 0.3911 0.3214 0.3966 -0.0691 0.0131  -0.0763 166 VAL A CG1 
1315 C CG2 . VAL A 157 ? 0.3889 0.3175 0.3964 -0.0878 0.0114  -0.0877 166 VAL A CG2 
1316 N N   . SER A 158 ? 0.3736 0.3491 0.3577 -0.0653 -0.0120 -0.0539 167 SER A N   
1317 C CA  . SER A 158 ? 0.3457 0.3281 0.3260 -0.0576 -0.0149 -0.0451 167 SER A CA  
1318 C C   . SER A 158 ? 0.3626 0.3573 0.3281 -0.0599 -0.0174 -0.0466 167 SER A C   
1319 O O   . SER A 158 ? 0.3420 0.3363 0.3021 -0.0561 -0.0144 -0.0452 167 SER A O   
1320 C CB  . SER A 158 ? 0.3356 0.3241 0.3214 -0.0534 -0.0204 -0.0347 167 SER A CB  
1321 O OG  . SER A 158 ? 0.3010 0.2808 0.2982 -0.0500 -0.0185 -0.0307 167 SER A OG  
1322 N N   . LEU A 159 ? 0.3540 0.3612 0.3136 -0.0661 -0.0228 -0.0484 168 LEU A N   
1323 C CA  . LEU A 159 ? 0.3734 0.3963 0.3185 -0.0685 -0.0263 -0.0481 168 LEU A CA  
1324 C C   . LEU A 159 ? 0.4091 0.4286 0.3419 -0.0726 -0.0202 -0.0584 168 LEU A C   
1325 O O   . LEU A 159 ? 0.3972 0.4234 0.3191 -0.0698 -0.0195 -0.0542 168 LEU A O   
1326 C CB  . LEU A 159 ? 0.3755 0.4158 0.3184 -0.0757 -0.0337 -0.0493 168 LEU A CB  
1327 C CG  . LEU A 159 ? 0.3922 0.4541 0.3201 -0.0781 -0.0393 -0.0469 168 LEU A CG  
1328 C CD1 . LEU A 159 ? 0.4310 0.4987 0.3579 -0.0673 -0.0411 -0.0313 168 LEU A CD1 
1329 C CD2 . LEU A 159 ? 0.4172 0.4984 0.3468 -0.0864 -0.0471 -0.0492 168 LEU A CD2 
1330 N N   . LEU A 160 ? 0.4180 0.4267 0.3530 -0.0794 -0.0147 -0.0717 169 LEU A N   
1331 C CA  . LEU A 160 ? 0.4286 0.4336 0.3519 -0.0841 -0.0072 -0.0842 169 LEU A CA  
1332 C C   . LEU A 160 ? 0.3973 0.3918 0.3234 -0.0757 0.0008  -0.0809 169 LEU A C   
1333 O O   . LEU A 160 ? 0.4073 0.4060 0.3202 -0.0768 0.0054  -0.0847 169 LEU A O   
1334 C CB  . LEU A 160 ? 0.4506 0.4432 0.3786 -0.0932 -0.0011 -0.1005 169 LEU A CB  
1335 C CG  . LEU A 160 ? 0.4626 0.4680 0.3856 -0.1055 -0.0077 -0.1084 169 LEU A CG  
1336 C CD1 . LEU A 160 ? 0.5615 0.5484 0.4970 -0.1133 -0.0005 -0.1217 169 LEU A CD1 
1337 C CD2 . LEU A 160 ? 0.5087 0.5337 0.4087 -0.1137 -0.0105 -0.1165 169 LEU A CD2 
1338 N N   . VAL A 161 ? 0.3964 0.3793 0.3396 -0.0680 0.0024  -0.0738 170 VAL A N   
1339 C CA  . VAL A 161 ? 0.4152 0.3915 0.3648 -0.0602 0.0087  -0.0696 170 VAL A CA  
1340 C C   . VAL A 161 ? 0.4135 0.4013 0.3538 -0.0566 0.0053  -0.0594 170 VAL A C   
1341 O O   . VAL A 161 ? 0.4001 0.3885 0.3347 -0.0551 0.0116  -0.0599 170 VAL A O   
1342 C CB  . VAL A 161 ? 0.3580 0.3248 0.3276 -0.0532 0.0086  -0.0626 170 VAL A CB  
1343 C CG1 . VAL A 161 ? 0.4105 0.3755 0.3878 -0.0462 0.0133  -0.0579 170 VAL A CG1 
1344 C CG2 . VAL A 161 ? 0.4097 0.3627 0.3907 -0.0552 0.0139  -0.0701 170 VAL A CG2 
1345 N N   . GLU A 162 ? 0.4229 0.4191 0.3632 -0.0550 -0.0033 -0.0498 171 GLU A N   
1346 C CA  . GLU A 162 ? 0.4185 0.4244 0.3514 -0.0514 -0.0062 -0.0390 171 GLU A CA  
1347 C C   . GLU A 162 ? 0.4482 0.4651 0.3619 -0.0556 -0.0048 -0.0410 171 GLU A C   
1348 O O   . GLU A 162 ? 0.4395 0.4583 0.3474 -0.0527 -0.0005 -0.0350 171 GLU A O   
1349 C CB  . GLU A 162 ? 0.3953 0.4087 0.3322 -0.0495 -0.0148 -0.0305 171 GLU A CB  
1350 C CG  . GLU A 162 ? 0.4170 0.4402 0.3484 -0.0452 -0.0178 -0.0184 171 GLU A CG  
1351 C CD  . GLU A 162 ? 0.3792 0.3944 0.3212 -0.0383 -0.0155 -0.0103 171 GLU A CD  
1352 O OE1 . GLU A 162 ? 0.3513 0.3568 0.3047 -0.0369 -0.0140 -0.0134 171 GLU A OE1 
1353 O OE2 . GLU A 162 ? 0.4051 0.4245 0.3441 -0.0344 -0.0152 -0.0004 171 GLU A OE2 
1354 N N   . ILE A 163 ? 0.4564 0.4819 0.3601 -0.0633 -0.0082 -0.0493 172 ILE A N   
1355 C CA  . ILE A 163 ? 0.4734 0.5138 0.3561 -0.0687 -0.0082 -0.0520 172 ILE A CA  
1356 C C   . ILE A 163 ? 0.4831 0.5162 0.3576 -0.0704 0.0032  -0.0610 172 ILE A C   
1357 O O   . ILE A 163 ? 0.4903 0.5334 0.3494 -0.0703 0.0057  -0.0563 172 ILE A O   
1358 C CB  . ILE A 163 ? 0.4939 0.5475 0.3681 -0.0788 -0.0151 -0.0615 172 ILE A CB  
1359 C CG1 . ILE A 163 ? 0.4781 0.5465 0.3579 -0.0763 -0.0263 -0.0491 172 ILE A CG1 
1360 C CG2 . ILE A 163 ? 0.5032 0.5729 0.3531 -0.0865 -0.0140 -0.0687 172 ILE A CG2 
1361 C CD1 . ILE A 163 ? 0.4832 0.5634 0.3631 -0.0863 -0.0334 -0.0582 172 ILE A CD1 
1362 N N   . ALA A 164 ? 0.4455 0.4621 0.3312 -0.0712 0.0107  -0.0727 173 ALA A N   
1363 C CA  . ALA A 164 ? 0.4696 0.4786 0.3517 -0.0715 0.0233  -0.0817 173 ALA A CA  
1364 C C   . ALA A 164 ? 0.4475 0.4541 0.3362 -0.0634 0.0283  -0.0700 173 ALA A C   
1365 O O   . ALA A 164 ? 0.4589 0.4694 0.3364 -0.0640 0.0364  -0.0711 173 ALA A O   
1366 C CB  . ALA A 164 ? 0.4629 0.4542 0.3599 -0.0725 0.0307  -0.0950 173 ALA A CB  
1367 N N   . ALA A 165 ? 0.4562 0.4570 0.3629 -0.0567 0.0242  -0.0597 174 ALA A N   
1368 C CA  . ALA A 165 ? 0.4655 0.4652 0.3798 -0.0507 0.0277  -0.0488 174 ALA A CA  
1369 C C   . ALA A 165 ? 0.5001 0.5114 0.3986 -0.0506 0.0258  -0.0374 174 ALA A C   
1370 O O   . ALA A 165 ? 0.5232 0.5353 0.4192 -0.0491 0.0333  -0.0322 174 ALA A O   
1371 C CB  . ALA A 165 ? 0.4491 0.4424 0.3833 -0.0455 0.0224  -0.0419 174 ALA A CB  
1372 N N   . ALA A 166 ? 0.5202 0.5415 0.4092 -0.0522 0.0163  -0.0326 175 ALA A N   
1373 C CA  . ALA A 166 ? 0.5186 0.5524 0.3950 -0.0504 0.0132  -0.0185 175 ALA A CA  
1374 C C   . ALA A 166 ? 0.5563 0.6019 0.4099 -0.0544 0.0184  -0.0190 175 ALA A C   
1375 O O   . ALA A 166 ? 0.5448 0.5996 0.3892 -0.0516 0.0184  -0.0044 175 ALA A O   
1376 C CB  . ALA A 166 ? 0.5217 0.5663 0.3967 -0.0504 0.0014  -0.0133 175 ALA A CB  
1377 N N   . SER A 167 ? 0.5662 0.6118 0.4103 -0.0610 0.0236  -0.0354 176 SER A N   
1378 C CA  . SER A 167 ? 0.5895 0.6463 0.4103 -0.0656 0.0306  -0.0385 176 SER A CA  
1379 C C   . SER A 167 ? 0.5716 0.6239 0.3942 -0.0613 0.0421  -0.0295 176 SER A C   
1380 O O   . SER A 167 ? 0.6014 0.6659 0.4039 -0.0630 0.0464  -0.0233 176 SER A O   
1381 C CB  . SER A 167 ? 0.6329 0.6874 0.4453 -0.0739 0.0361  -0.0611 176 SER A CB  
1382 O OG  . SER A 167 ? 0.6997 0.7344 0.5337 -0.0712 0.0438  -0.0707 176 SER A OG  
1383 N N   . ALA A 168 ? 0.5525 0.5892 0.3989 -0.0563 0.0467  -0.0282 177 ALA A N   
1384 C CA  . ALA A 168 ? 0.5699 0.6024 0.4233 -0.0528 0.0571  -0.0191 177 ALA A CA  
1385 C C   . ALA A 168 ? 0.5641 0.5974 0.4212 -0.0480 0.0538  0.0014  177 ALA A C   
1386 O O   . ALA A 168 ? 0.5387 0.5707 0.3971 -0.0468 0.0632  0.0107  177 ALA A O   
1387 C CB  . ALA A 168 ? 0.5600 0.5787 0.4388 -0.0505 0.0631  -0.0268 177 ALA A CB  
1388 N N   . ILE A 169 ? 0.5274 0.5624 0.3878 -0.0453 0.0422  0.0085  178 ILE A N   
1389 C CA  . ILE A 169 ? 0.5431 0.5768 0.4093 -0.0397 0.0402  0.0275  178 ILE A CA  
1390 C C   . ILE A 169 ? 0.5761 0.6208 0.4237 -0.0391 0.0455  0.0426  178 ILE A C   
1391 O O   . ILE A 169 ? 0.5848 0.6224 0.4404 -0.0356 0.0524  0.0564  178 ILE A O   
1392 C CB  . ILE A 169 ? 0.5363 0.5734 0.4069 -0.0365 0.0274  0.0323  178 ILE A CB  
1393 C CG1 . ILE A 169 ? 0.4762 0.5011 0.3669 -0.0360 0.0234  0.0216  178 ILE A CG1 
1394 C CG2 . ILE A 169 ? 0.5555 0.5917 0.4314 -0.0297 0.0271  0.0526  178 ILE A CG2 
1395 C CD1 . ILE A 169 ? 0.4986 0.5300 0.3903 -0.0350 0.0118  0.0215  178 ILE A CD1 
1396 N N   . LYS A 170 ? 0.5936 0.6558 0.4165 -0.0431 0.0428  0.0398  179 LYS A N   
1397 C CA  . LYS A 170 ? 0.6489 0.7258 0.4502 -0.0430 0.0472  0.0547  179 LYS A CA  
1398 C C   . LYS A 170 ? 0.6632 0.7347 0.4615 -0.0448 0.0632  0.0557  179 LYS A C   
1399 O O   . LYS A 170 ? 0.6713 0.7523 0.4546 -0.0437 0.0688  0.0717  179 LYS A O   
1400 C CB  . LYS A 170 ? 0.6985 0.7993 0.4719 -0.0486 0.0395  0.0490  179 LYS A CB  
1401 C CG  . LYS A 170 ? 0.7206 0.8223 0.4834 -0.0576 0.0432  0.0234  179 LYS A CG  
1402 C CD  . LYS A 170 ? 0.7667 0.8917 0.5052 -0.0647 0.0329  0.0154  179 LYS A CD  
1403 C CE  . LYS A 170 ? 0.7893 0.9074 0.5333 -0.0719 0.0299  -0.0102 179 LYS A CE  
1404 N NZ  . LYS A 170 ? 0.7998 0.9087 0.5380 -0.0776 0.0436  -0.0303 179 LYS A NZ  
1405 N N   . VAL A 171 ? 0.6473 0.7053 0.4611 -0.0472 0.0707  0.0401  180 VAL A N   
1406 C CA  . VAL A 171 ? 0.6525 0.7054 0.4700 -0.0487 0.0864  0.0402  180 VAL A CA  
1407 C C   . VAL A 171 ? 0.6412 0.6805 0.4820 -0.0446 0.0916  0.0551  180 VAL A C   
1408 O O   . VAL A 171 ? 0.6511 0.6887 0.4938 -0.0458 0.1046  0.0622  180 VAL A O   
1409 C CB  . VAL A 171 ? 0.6256 0.6720 0.4535 -0.0522 0.0926  0.0177  180 VAL A CB  
1410 C CG1 . VAL A 171 ? 0.6551 0.7005 0.4866 -0.0538 0.1095  0.0174  180 VAL A CG1 
1411 C CG2 . VAL A 171 ? 0.6262 0.6821 0.4336 -0.0571 0.0885  0.0007  180 VAL A CG2 
1412 N N   . ILE A 172 ? 0.6336 0.6633 0.4917 -0.0407 0.0824  0.0593  181 ILE A N   
1413 C CA  . ILE A 172 ? 0.6319 0.6464 0.5139 -0.0383 0.0873  0.0691  181 ILE A CA  
1414 C C   . ILE A 172 ? 0.6586 0.6723 0.5356 -0.0363 0.0968  0.0911  181 ILE A C   
1415 O O   . ILE A 172 ? 0.6683 0.6718 0.5613 -0.0384 0.1081  0.0948  181 ILE A O   
1416 C CB  . ILE A 172 ? 0.6244 0.6295 0.5230 -0.0346 0.0759  0.0678  181 ILE A CB  
1417 C CG1 . ILE A 172 ? 0.5720 0.5741 0.4825 -0.0371 0.0707  0.0477  181 ILE A CG1 
1418 C CG2 . ILE A 172 ? 0.6328 0.6223 0.5525 -0.0327 0.0816  0.0787  181 ILE A CG2 
1419 C CD1 . ILE A 172 ? 0.5721 0.5692 0.4928 -0.0342 0.0590  0.0442  181 ILE A CD1 
1420 N N   . PRO A 173 ? 0.6738 0.6992 0.5307 -0.0325 0.0923  0.1068  182 PRO A N   
1421 C CA  . PRO A 173 ? 0.6911 0.7175 0.5410 -0.0301 0.1024  0.1301  182 PRO A CA  
1422 C C   . PRO A 173 ? 0.7093 0.7406 0.5491 -0.0356 0.1173  0.1292  182 PRO A C   
1423 O O   . PRO A 173 ? 0.7234 0.7461 0.5719 -0.0357 0.1299  0.1438  182 PRO A O   
1424 C CB  . PRO A 173 ? 0.7168 0.7627 0.5423 -0.0254 0.0925  0.1440  182 PRO A CB  
1425 C CG  . PRO A 173 ? 0.6905 0.7384 0.5214 -0.0240 0.0772  0.1314  182 PRO A CG  
1426 C CD  . PRO A 173 ? 0.6682 0.7077 0.5096 -0.0301 0.0777  0.1057  182 PRO A CD  
1427 N N   . THR A 174 ? 0.7038 0.7483 0.5263 -0.0404 0.1167  0.1121  183 THR A N   
1428 C CA  . THR A 174 ? 0.6931 0.7435 0.5062 -0.0458 0.1315  0.1070  183 THR A CA  
1429 C C   . THR A 174 ? 0.6752 0.7102 0.5190 -0.0485 0.1425  0.0998  183 THR A C   
1430 O O   . THR A 174 ? 0.6842 0.7193 0.5297 -0.0513 0.1577  0.1076  183 THR A O   
1431 C CB  . THR A 174 ? 0.6951 0.7591 0.4880 -0.0503 0.1290  0.0851  183 THR A CB  
1432 O OG1 . THR A 174 ? 0.7031 0.7830 0.4706 -0.0495 0.1161  0.0880  183 THR A OG1 
1433 C CG2 . THR A 174 ? 0.7191 0.7923 0.4969 -0.0552 0.1459  0.0815  183 THR A CG2 
1434 N N   . VAL A 175 ? 0.6193 0.6434 0.4869 -0.0482 0.1346  0.0856  184 VAL A N   
1435 C CA  . VAL A 175 ? 0.6197 0.6331 0.5178 -0.0512 0.1422  0.0778  184 VAL A CA  
1436 C C   . VAL A 175 ? 0.6294 0.6316 0.5433 -0.0520 0.1515  0.0956  184 VAL A C   
1437 O O   . VAL A 175 ? 0.6021 0.6045 0.5255 -0.0564 0.1660  0.0983  184 VAL A O   
1438 C CB  . VAL A 175 ? 0.5798 0.5856 0.4989 -0.0502 0.1300  0.0628  184 VAL A CB  
1439 C CG1 . VAL A 175 ? 0.5725 0.5698 0.5245 -0.0537 0.1358  0.0582  184 VAL A CG1 
1440 C CG2 . VAL A 175 ? 0.6025 0.6165 0.5120 -0.0503 0.1246  0.0444  184 VAL A CG2 
1441 N N   . PHE A 176 ? 0.6161 0.6082 0.5342 -0.0479 0.1441  0.1072  185 PHE A N   
1442 C CA  . PHE A 176 ? 0.6414 0.6184 0.5767 -0.0483 0.1533  0.1236  185 PHE A CA  
1443 C C   . PHE A 176 ? 0.6677 0.6490 0.5876 -0.0482 0.1670  0.1450  185 PHE A C   
1444 O O   . PHE A 176 ? 0.7081 0.6790 0.6449 -0.0521 0.1808  0.1541  185 PHE A O   
1445 C CB  . PHE A 176 ? 0.6482 0.6128 0.5912 -0.0426 0.1434  0.1308  185 PHE A CB  
1446 C CG  . PHE A 176 ? 0.6058 0.5638 0.5673 -0.0438 0.1327  0.1119  185 PHE A CG  
1447 C CD1 . PHE A 176 ? 0.5953 0.5452 0.5831 -0.0506 0.1377  0.1002  185 PHE A CD1 
1448 C CD2 . PHE A 176 ? 0.6322 0.5943 0.5850 -0.0387 0.1177  0.1061  185 PHE A CD2 
1449 C CE1 . PHE A 176 ? 0.6000 0.5469 0.6029 -0.0518 0.1272  0.0836  185 PHE A CE1 
1450 C CE2 . PHE A 176 ? 0.6053 0.5621 0.5738 -0.0398 0.1085  0.0899  185 PHE A CE2 
1451 C CZ  . PHE A 176 ? 0.5971 0.5468 0.5895 -0.0461 0.1130  0.0789  185 PHE A CZ  
1452 N N   . LYS A 177 ? 0.6816 0.6793 0.5696 -0.0444 0.1633  0.1529  186 LYS A N   
1453 C CA  . LYS A 177 ? 0.7291 0.7367 0.5964 -0.0446 0.1759  0.1724  186 LYS A CA  
1454 C C   . LYS A 177 ? 0.7407 0.7529 0.6120 -0.0523 0.1916  0.1633  186 LYS A C   
1455 O O   . LYS A 177 ? 0.7573 0.7648 0.6347 -0.0550 0.2075  0.1785  186 LYS A O   
1456 C CB  . LYS A 177 ? 0.7562 0.7863 0.5861 -0.0410 0.1667  0.1772  186 LYS A CB  
1457 C CG  . LYS A 177 ? 0.7736 0.8174 0.5774 -0.0404 0.1778  0.2002  186 LYS A CG  
1458 C CD  . LYS A 177 ? 0.8040 0.8714 0.5732 -0.0361 0.1652  0.2083  186 LYS A CD  
1459 C CE  . LYS A 177 ? 0.8446 0.9287 0.5860 -0.0353 0.1755  0.2333  186 LYS A CE  
1460 N NZ  . LYS A 177 ? 0.8587 0.9708 0.5654 -0.0321 0.1618  0.2412  186 LYS A NZ  
1461 N N   . ALA A 178 ? 0.7190 0.7398 0.5889 -0.0553 0.1880  0.1391  187 ALA A N   
1462 C CA  . ALA A 178 ? 0.7190 0.7456 0.5963 -0.0614 0.2027  0.1279  187 ALA A CA  
1463 C C   . ALA A 178 ? 0.7047 0.7180 0.6199 -0.0662 0.2125  0.1279  187 ALA A C   
1464 O O   . ALA A 178 ? 0.6961 0.7138 0.6176 -0.0712 0.2293  0.1312  187 ALA A O   
1465 C CB  . ALA A 178 ? 0.6941 0.7299 0.5669 -0.0620 0.1964  0.1021  187 ALA A CB  
1466 N N   . MET A 179 ? 0.6835 0.6822 0.6234 -0.0657 0.2027  0.1237  188 MET A N   
1467 C CA  . MET A 179 ? 0.7108 0.6979 0.6868 -0.0720 0.2106  0.1224  188 MET A CA  
1468 C C   . MET A 179 ? 0.7493 0.7245 0.7305 -0.0742 0.2244  0.1457  188 MET A C   
1469 O O   . MET A 179 ? 0.7376 0.7126 0.7359 -0.0814 0.2401  0.1486  188 MET A O   
1470 C CB  . MET A 179 ? 0.6770 0.6528 0.6748 -0.0716 0.1962  0.1105  188 MET A CB  
1471 C CG  . MET A 179 ? 0.6865 0.6723 0.6940 -0.0721 0.1873  0.0877  188 MET A CG  
1472 S SD  . MET A 179 ? 0.6937 0.6692 0.7172 -0.0702 0.1686  0.0762  188 MET A SD  
1473 C CE  . MET A 179 ? 0.7628 0.7227 0.8187 -0.0784 0.1763  0.0808  188 MET A CE  
1474 N N   . GLN A 180 ? 0.7763 0.7419 0.7447 -0.0679 0.2193  0.1629  189 GLN A N   
1475 C CA  . GLN A 180 ? 0.8074 0.7590 0.7805 -0.0680 0.2326  0.1884  189 GLN A CA  
1476 C C   . GLN A 180 ? 0.8559 0.8200 0.8101 -0.0699 0.2491  0.2042  189 GLN A C   
1477 O O   . GLN A 180 ? 0.8839 0.8389 0.8537 -0.0755 0.2664  0.2173  189 GLN A O   
1478 C CB  . GLN A 180 ? 0.8260 0.7685 0.7873 -0.0582 0.2230  0.2051  189 GLN A CB  
1479 C CG  . GLN A 180 ? 0.8474 0.7672 0.8261 -0.0577 0.2363  0.2289  189 GLN A CG  
1480 C CD  . GLN A 180 ? 0.8552 0.7661 0.8268 -0.0463 0.2275  0.2459  189 GLN A CD  
1481 O OE1 . GLN A 180 ? 0.8341 0.7488 0.8008 -0.0410 0.2105  0.2342  189 GLN A OE1 
1482 N NE2 . GLN A 180 ? 0.8854 0.7845 0.8583 -0.0420 0.2399  0.2748  189 GLN A NE2 
1483 N N   . MET A 181 ? 0.8549 0.8401 0.7752 -0.0661 0.2444  0.2020  190 MET A N   
1484 C CA  . MET A 181 ? 0.8736 0.8746 0.7704 -0.0681 0.2595  0.2140  190 MET A CA  
1485 C C   . MET A 181 ? 0.8571 0.8674 0.7665 -0.0764 0.2725  0.1970  190 MET A C   
1486 O O   . MET A 181 ? 0.8955 0.9191 0.7870 -0.0788 0.2874  0.2052  190 MET A O   
1487 C CB  . MET A 181 ? 0.9010 0.9231 0.7549 -0.0622 0.2494  0.2157  190 MET A CB  
1488 C CG  . MET A 181 ? 0.9628 0.9828 0.8019 -0.0532 0.2372  0.2362  190 MET A CG  
1489 S SD  . MET A 181 ? 1.1322 1.1459 0.9664 -0.0499 0.2534  0.2770  190 MET A SD  
1490 C CE  . MET A 181 ? 1.0941 1.0715 0.9753 -0.0493 0.2559  0.2834  190 MET A CE  
1491 N N   . GLN A 182 ? 0.8198 0.8249 0.7598 -0.0803 0.2675  0.1747  191 GLN A N   
1492 C CA  . GLN A 182 ? 0.8035 0.8202 0.7595 -0.0864 0.2774  0.1571  191 GLN A CA  
1493 C C   . GLN A 182 ? 0.8039 0.8411 0.7267 -0.0838 0.2799  0.1486  191 GLN A C   
1494 O O   . GLN A 182 ? 0.8344 0.8831 0.7479 -0.0872 0.2974  0.1536  191 GLN A O   
1495 C CB  . GLN A 182 ? 0.8253 0.8384 0.8049 -0.0948 0.2987  0.1690  191 GLN A CB  
1496 C CG  . GLN A 182 ? 0.8324 0.8275 0.8537 -0.1012 0.2982  0.1674  191 GLN A CG  
1497 C CD  . GLN A 182 ? 0.8341 0.8359 0.8862 -0.1054 0.2907  0.1416  191 GLN A CD  
1498 O OE1 . GLN A 182 ? 0.8203 0.8103 0.8996 -0.1093 0.2830  0.1350  191 GLN A OE1 
1499 N NE2 . GLN A 182 ? 0.8630 0.8845 0.9114 -0.1045 0.2936  0.1272  191 GLN A NE2 
1500 N N   . GLU A 183 ? 0.7675 0.8088 0.6714 -0.0784 0.2630  0.1359  192 GLU A N   
1501 C CA  . GLU A 183 ? 0.7621 0.8208 0.6343 -0.0769 0.2638  0.1238  192 GLU A CA  
1502 C C   . GLU A 183 ? 0.7139 0.7744 0.6043 -0.0764 0.2573  0.0962  192 GLU A C   
1503 O O   . GLU A 183 ? 0.6666 0.7228 0.5544 -0.0727 0.2399  0.0853  192 GLU A O   
1504 C CB  . GLU A 183 ? 0.7868 0.8508 0.6216 -0.0720 0.2503  0.1319  192 GLU A CB  
1505 C CG  . GLU A 183 ? 0.8527 0.9191 0.6662 -0.0707 0.2568  0.1621  192 GLU A CG  
1506 C CD  . GLU A 183 ? 0.9271 1.0116 0.7124 -0.0741 0.2748  0.1691  192 GLU A CD  
1507 O OE1 . GLU A 183 ? 0.9650 1.0652 0.7265 -0.0757 0.2758  0.1512  192 GLU A OE1 
1508 O OE2 . GLU A 183 ? 1.0359 1.1185 0.8222 -0.0756 0.2891  0.1927  192 GLU A OE2 
1509 N N   . ARG A 184 ? 0.6867 0.7538 0.5973 -0.0800 0.2722  0.0866  193 ARG A N   
1510 C CA  . ARG A 184 ? 0.6460 0.7165 0.5789 -0.0786 0.2695  0.0631  193 ARG A CA  
1511 C C   . ARG A 184 ? 0.6231 0.6991 0.5287 -0.0747 0.2629  0.0462  193 ARG A C   
1512 O O   . ARG A 184 ? 0.5918 0.6629 0.5092 -0.0713 0.2500  0.0316  193 ARG A O   
1513 C CB  . ARG A 184 ? 0.6653 0.7465 0.6212 -0.0823 0.2901  0.0589  193 ARG A CB  
1514 C CG  . ARG A 184 ? 0.6170 0.7041 0.6011 -0.0796 0.2897  0.0375  193 ARG A CG  
1515 C CD  . ARG A 184 ? 0.6218 0.7188 0.5852 -0.0765 0.3000  0.0216  193 ARG A CD  
1516 N NE  . ARG A 184 ? 0.5997 0.7003 0.5936 -0.0721 0.2999  0.0033  193 ARG A NE  
1517 C CZ  . ARG A 184 ? 0.6115 0.7167 0.5968 -0.0681 0.3076  -0.0141 193 ARG A CZ  
1518 N NH1 . ARG A 184 ? 0.6622 0.7700 0.6067 -0.0693 0.3153  -0.0187 193 ARG A NH1 
1519 N NH2 . ARG A 184 ? 0.5924 0.7001 0.6107 -0.0628 0.3075  -0.0273 193 ARG A NH2 
1520 N N   . ASP A 185 ? 0.6457 0.7323 0.5148 -0.0760 0.2726  0.0482  194 ASP A N   
1521 C CA  . ASP A 185 ? 0.6523 0.7453 0.4941 -0.0747 0.2698  0.0295  194 ASP A CA  
1522 C C   . ASP A 185 ? 0.6367 0.7240 0.4609 -0.0723 0.2475  0.0293  194 ASP A C   
1523 O O   . ASP A 185 ? 0.6401 0.7238 0.4663 -0.0704 0.2382  0.0108  194 ASP A O   
1524 C CB  . ASP A 185 ? 0.6742 0.7826 0.4790 -0.0783 0.2864  0.0310  194 ASP A CB  
1525 C CG  . ASP A 185 ? 0.6841 0.7999 0.5059 -0.0807 0.3106  0.0311  194 ASP A CG  
1526 O OD1 . ASP A 185 ? 0.6338 0.7458 0.4951 -0.0791 0.3147  0.0218  194 ASP A OD1 
1527 O OD2 . ASP A 185 ? 0.6929 0.8206 0.4886 -0.0842 0.3257  0.0411  194 ASP A OD2 
1528 N N   . THR A 186 ? 0.6343 0.7206 0.4440 -0.0721 0.2399  0.0507  195 THR A N   
1529 C CA  . THR A 186 ? 0.6266 0.7089 0.4243 -0.0692 0.2188  0.0538  195 THR A CA  
1530 C C   . THR A 186 ? 0.5722 0.6398 0.4029 -0.0661 0.2053  0.0440  195 THR A C   
1531 O O   . THR A 186 ? 0.5515 0.6176 0.3765 -0.0645 0.1919  0.0312  195 THR A O   
1532 C CB  . THR A 186 ? 0.6463 0.7284 0.4326 -0.0676 0.2150  0.0821  195 THR A CB  
1533 O OG1 . THR A 186 ? 0.6824 0.7792 0.4402 -0.0703 0.2291  0.0948  195 THR A OG1 
1534 C CG2 . THR A 186 ? 0.6279 0.7114 0.3983 -0.0641 0.1944  0.0856  195 THR A CG2 
1535 N N   . LEU A 187 ? 0.5457 0.6040 0.4106 -0.0661 0.2093  0.0500  196 LEU A N   
1536 C CA  . LEU A 187 ? 0.5248 0.5718 0.4212 -0.0639 0.1973  0.0414  196 LEU A CA  
1537 C C   . LEU A 187 ? 0.5108 0.5599 0.4177 -0.0624 0.1963  0.0186  196 LEU A C   
1538 O O   . LEU A 187 ? 0.4855 0.5284 0.3989 -0.0596 0.1819  0.0099  196 LEU A O   
1539 C CB  . LEU A 187 ? 0.4981 0.5383 0.4286 -0.0663 0.2036  0.0499  196 LEU A CB  
1540 C CG  . LEU A 187 ? 0.4686 0.5003 0.4313 -0.0653 0.1917  0.0416  196 LEU A CG  
1541 C CD1 . LEU A 187 ? 0.5192 0.5409 0.4742 -0.0621 0.1741  0.0463  196 LEU A CD1 
1542 C CD2 . LEU A 187 ? 0.4675 0.4969 0.4625 -0.0702 0.2001  0.0473  196 LEU A CD2 
1543 N N   . LEU A 188 ? 0.5370 0.5942 0.4470 -0.0638 0.2127  0.0101  197 LEU A N   
1544 C CA  . LEU A 188 ? 0.5320 0.5905 0.4530 -0.0613 0.2154  -0.0106 197 LEU A CA  
1545 C C   . LEU A 188 ? 0.5284 0.5849 0.4223 -0.0604 0.2054  -0.0225 197 LEU A C   
1546 O O   . LEU A 188 ? 0.4796 0.5288 0.3866 -0.0573 0.1948  -0.0330 197 LEU A O   
1547 C CB  . LEU A 188 ? 0.5329 0.6017 0.4570 -0.0626 0.2375  -0.0167 197 LEU A CB  
1548 C CG  . LEU A 188 ? 0.5718 0.6423 0.5047 -0.0593 0.2459  -0.0380 197 LEU A CG  
1549 C CD1 . LEU A 188 ? 0.5650 0.6289 0.5324 -0.0539 0.2351  -0.0452 197 LEU A CD1 
1550 C CD2 . LEU A 188 ? 0.6175 0.6991 0.5608 -0.0602 0.2692  -0.0402 197 LEU A CD2 
1551 N N   . LYS A 189 ? 0.5787 0.6428 0.4350 -0.0638 0.2087  -0.0201 198 LYS A N   
1552 C CA  . LYS A 189 ? 0.5923 0.6577 0.4202 -0.0653 0.1986  -0.0312 198 LYS A CA  
1553 C C   . LYS A 189 ? 0.5548 0.6120 0.3890 -0.0630 0.1771  -0.0265 198 LYS A C   
1554 O O   . LYS A 189 ? 0.5354 0.5871 0.3708 -0.0624 0.1684  -0.0407 198 LYS A O   
1555 C CB  . LYS A 189 ? 0.6365 0.7164 0.4223 -0.0702 0.2036  -0.0248 198 LYS A CB  
1556 C CG  . LYS A 189 ? 0.6557 0.7417 0.4101 -0.0737 0.1916  -0.0349 198 LYS A CG  
1557 C CD  . LYS A 189 ? 0.7011 0.8062 0.4133 -0.0791 0.1972  -0.0291 198 LYS A CD  
1558 C CE  . LYS A 189 ? 0.7110 0.8263 0.3936 -0.0836 0.1822  -0.0362 198 LYS A CE  
1559 N NZ  . LYS A 189 ? 0.7486 0.8871 0.3882 -0.0892 0.1858  -0.0291 198 LYS A NZ  
1560 N N   . ALA A 190 ? 0.5494 0.6046 0.3889 -0.0616 0.1701  -0.0065 199 ALA A N   
1561 C CA  . ALA A 190 ? 0.5205 0.5683 0.3669 -0.0589 0.1516  -0.0005 199 ALA A CA  
1562 C C   . ALA A 190 ? 0.5133 0.5501 0.3906 -0.0559 0.1449  -0.0119 199 ALA A C   
1563 O O   . ALA A 190 ? 0.4865 0.5193 0.3624 -0.0548 0.1321  -0.0190 199 ALA A O   
1564 C CB  . ALA A 190 ? 0.5266 0.5718 0.3778 -0.0574 0.1496  0.0220  199 ALA A CB  
1565 N N   . LEU A 191 ? 0.5195 0.5536 0.4250 -0.0548 0.1536  -0.0130 200 LEU A N   
1566 C CA  . LEU A 191 ? 0.4962 0.5238 0.4316 -0.0516 0.1476  -0.0221 200 LEU A CA  
1567 C C   . LEU A 191 ? 0.4943 0.5203 0.4275 -0.0500 0.1487  -0.0403 200 LEU A C   
1568 O O   . LEU A 191 ? 0.4812 0.5007 0.4263 -0.0472 0.1381  -0.0457 200 LEU A O   
1569 C CB  . LEU A 191 ? 0.4941 0.5240 0.4609 -0.0514 0.1567  -0.0193 200 LEU A CB  
1570 C CG  . LEU A 191 ? 0.4588 0.4863 0.4379 -0.0538 0.1549  -0.0041 200 LEU A CG  
1571 C CD1 . LEU A 191 ? 0.4852 0.5185 0.4961 -0.0553 0.1646  -0.0049 200 LEU A CD1 
1572 C CD2 . LEU A 191 ? 0.4747 0.4937 0.4597 -0.0523 0.1381  -0.0007 200 LEU A CD2 
1573 N N   . LEU A 192 ? 0.5212 0.5523 0.4388 -0.0520 0.1624  -0.0496 201 LEU A N   
1574 C CA  . LEU A 192 ? 0.5257 0.5527 0.4396 -0.0513 0.1657  -0.0686 201 LEU A CA  
1575 C C   . LEU A 192 ? 0.5239 0.5472 0.4157 -0.0541 0.1521  -0.0740 201 LEU A C   
1576 O O   . LEU A 192 ? 0.5139 0.5286 0.4144 -0.0527 0.1485  -0.0861 201 LEU A O   
1577 C CB  . LEU A 192 ? 0.5334 0.5666 0.4336 -0.0537 0.1852  -0.0791 201 LEU A CB  
1578 C CG  . LEU A 192 ? 0.5339 0.5713 0.4620 -0.0502 0.2010  -0.0781 201 LEU A CG  
1579 C CD1 . LEU A 192 ? 0.5372 0.5823 0.4464 -0.0533 0.2210  -0.0870 201 LEU A CD1 
1580 C CD2 . LEU A 192 ? 0.5005 0.5313 0.4648 -0.0432 0.2008  -0.0862 201 LEU A CD2 
1581 N N   . GLU A 193 ? 0.5570 0.5877 0.4225 -0.0579 0.1449  -0.0639 202 GLU A N   
1582 C CA  . GLU A 193 ? 0.5556 0.5870 0.4018 -0.0610 0.1306  -0.0668 202 GLU A CA  
1583 C C   . GLU A 193 ? 0.5319 0.5545 0.3987 -0.0571 0.1152  -0.0614 202 GLU A C   
1584 O O   . GLU A 193 ? 0.5108 0.5296 0.3747 -0.0587 0.1064  -0.0701 202 GLU A O   
1585 C CB  . GLU A 193 ? 0.5993 0.6448 0.4145 -0.0648 0.1267  -0.0542 202 GLU A CB  
1586 C CG  . GLU A 193 ? 0.6440 0.6955 0.4416 -0.0677 0.1101  -0.0534 202 GLU A CG  
1587 C CD  . GLU A 193 ? 0.7232 0.7751 0.5077 -0.0740 0.1094  -0.0757 202 GLU A CD  
1588 O OE1 . GLU A 193 ? 0.7814 0.8317 0.5601 -0.0772 0.1234  -0.0918 202 GLU A OE1 
1589 O OE2 . GLU A 193 ? 0.7549 0.8087 0.5358 -0.0762 0.0955  -0.0773 202 GLU A OE2 
1590 N N   . ILE A 194 ? 0.5215 0.5413 0.4086 -0.0530 0.1127  -0.0477 203 ILE A N   
1591 C CA  . ILE A 194 ? 0.4814 0.4937 0.3883 -0.0495 0.0997  -0.0433 203 ILE A CA  
1592 C C   . ILE A 194 ? 0.4867 0.4911 0.4153 -0.0467 0.1004  -0.0557 203 ILE A C   
1593 O O   . ILE A 194 ? 0.4527 0.4517 0.3854 -0.0458 0.0900  -0.0587 203 ILE A O   
1594 C CB  . ILE A 194 ? 0.4762 0.4873 0.4005 -0.0472 0.0989  -0.0283 203 ILE A CB  
1595 C CG1 . ILE A 194 ? 0.4774 0.4930 0.3829 -0.0484 0.0962  -0.0133 203 ILE A CG1 
1596 C CG2 . ILE A 194 ? 0.4440 0.4483 0.3908 -0.0440 0.0876  -0.0274 203 ILE A CG2 
1597 C CD1 . ILE A 194 ? 0.4823 0.4954 0.4016 -0.0478 0.1015  0.0002  203 ILE A CD1 
1598 N N   . ALA A 195 ? 0.4994 0.5037 0.4434 -0.0446 0.1132  -0.0613 204 ALA A N   
1599 C CA  . ALA A 195 ? 0.4933 0.4908 0.4598 -0.0403 0.1153  -0.0710 204 ALA A CA  
1600 C C   . ALA A 195 ? 0.5091 0.4994 0.4615 -0.0428 0.1148  -0.0850 204 ALA A C   
1601 O O   . ALA A 195 ? 0.5029 0.4850 0.4677 -0.0403 0.1079  -0.0880 204 ALA A O   
1602 C CB  . ALA A 195 ? 0.4996 0.5009 0.4846 -0.0372 0.1308  -0.0745 204 ALA A CB  
1603 N N   . SER A 196 ? 0.5222 0.5163 0.4478 -0.0485 0.1219  -0.0932 205 SER A N   
1604 C CA  . SER A 196 ? 0.5524 0.5411 0.4615 -0.0537 0.1221  -0.1090 205 SER A CA  
1605 C C   . SER A 196 ? 0.5352 0.5215 0.4399 -0.0560 0.1050  -0.1058 205 SER A C   
1606 O O   . SER A 196 ? 0.5354 0.5114 0.4475 -0.0568 0.1034  -0.1158 205 SER A O   
1607 C CB  . SER A 196 ? 0.5808 0.5793 0.4573 -0.0612 0.1303  -0.1167 205 SER A CB  
1608 O OG  . SER A 196 ? 0.6598 0.6541 0.5206 -0.0681 0.1316  -0.1351 205 SER A OG  
1609 N N   . CYS A 197 ? 0.5453 0.5405 0.4404 -0.0567 0.0935  -0.0913 206 CYS A N   
1610 C CA  . CYS A 197 ? 0.5359 0.5313 0.4284 -0.0581 0.0779  -0.0868 206 CYS A CA  
1611 C C   . CYS A 197 ? 0.5205 0.5059 0.4400 -0.0524 0.0713  -0.0824 206 CYS A C   
1612 O O   . CYS A 197 ? 0.5384 0.5194 0.4598 -0.0540 0.0632  -0.0857 206 CYS A O   
1613 C CB  . CYS A 197 ? 0.5435 0.5509 0.4219 -0.0584 0.0692  -0.0710 206 CYS A CB  
1614 S SG  . CYS A 197 ? 0.5823 0.6065 0.4249 -0.0653 0.0729  -0.0718 206 CYS A SG  
1615 N N   . LEU A 198 ? 0.5132 0.4971 0.4531 -0.0463 0.0745  -0.0747 207 LEU A N   
1616 C CA  . LEU A 198 ? 0.4925 0.4703 0.4572 -0.0409 0.0685  -0.0704 207 LEU A CA  
1617 C C   . LEU A 198 ? 0.5058 0.4735 0.4858 -0.0383 0.0749  -0.0807 207 LEU A C   
1618 O O   . LEU A 198 ? 0.4823 0.4441 0.4754 -0.0356 0.0682  -0.0786 207 LEU A O   
1619 C CB  . LEU A 198 ? 0.4870 0.4695 0.4687 -0.0366 0.0694  -0.0601 207 LEU A CB  
1620 C CG  . LEU A 198 ? 0.4912 0.4795 0.4631 -0.0384 0.0634  -0.0485 207 LEU A CG  
1621 C CD1 . LEU A 198 ? 0.5074 0.4993 0.4971 -0.0364 0.0674  -0.0417 207 LEU A CD1 
1622 C CD2 . LEU A 198 ? 0.4555 0.4422 0.4253 -0.0383 0.0498  -0.0432 207 LEU A CD2 
1623 N N   . GLU A 199 ? 0.5146 0.4801 0.4936 -0.0386 0.0888  -0.0909 208 GLU A N   
1624 C CA  . GLU A 199 ? 0.5440 0.4973 0.5360 -0.0363 0.0980  -0.1026 208 GLU A CA  
1625 C C   . GLU A 199 ? 0.5648 0.5095 0.5426 -0.0431 0.0941  -0.1129 208 GLU A C   
1626 O O   . GLU A 199 ? 0.5512 0.4845 0.5442 -0.0408 0.0929  -0.1146 208 GLU A O   
1627 C CB  . GLU A 199 ? 0.5579 0.5111 0.5504 -0.0355 0.1157  -0.1127 208 GLU A CB  
1628 C CG  . GLU A 199 ? 0.5318 0.4931 0.5479 -0.0279 0.1215  -0.1035 208 GLU A CG  
1629 C CD  . GLU A 199 ? 0.5796 0.5456 0.5915 -0.0284 0.1389  -0.1112 208 GLU A CD  
1630 O OE1 . GLU A 199 ? 0.5861 0.5463 0.5801 -0.0332 0.1489  -0.1261 208 GLU A OE1 
1631 O OE2 . GLU A 199 ? 0.5094 0.4858 0.5362 -0.0247 0.1432  -0.1029 208 GLU A OE2 
1632 N N   . LYS A 200 ? 0.5677 0.5195 0.5171 -0.0519 0.0918  -0.1186 209 LYS A N   
1633 C CA  . LYS A 200 ? 0.5891 0.5377 0.5241 -0.0605 0.0862  -0.1284 209 LYS A CA  
1634 C C   . LYS A 200 ? 0.5701 0.5174 0.5146 -0.0592 0.0717  -0.1180 209 LYS A C   
1635 O O   . LYS A 200 ? 0.6007 0.5381 0.5504 -0.0627 0.0705  -0.1251 209 LYS A O   
1636 C CB  . LYS A 200 ? 0.6176 0.5813 0.5203 -0.0697 0.0832  -0.1326 209 LYS A CB  
1637 C CG  . LYS A 200 ? 0.6669 0.6305 0.5532 -0.0754 0.0980  -0.1500 209 LYS A CG  
1638 C CD  . LYS A 200 ? 0.6694 0.6524 0.5219 -0.0842 0.0932  -0.1512 209 LYS A CD  
1639 C CE  . LYS A 200 ? 0.7074 0.6922 0.5404 -0.0910 0.1084  -0.1701 209 LYS A CE  
1640 N NZ  . LYS A 200 ? 0.7287 0.7362 0.5264 -0.0998 0.1030  -0.1699 209 LYS A NZ  
1641 N N   . ALA A 201 ? 0.5350 0.4916 0.4823 -0.0546 0.0621  -0.1018 210 ALA A N   
1642 C CA  . ALA A 201 ? 0.5117 0.4685 0.4675 -0.0528 0.0494  -0.0917 210 ALA A CA  
1643 C C   . ALA A 201 ? 0.4936 0.4374 0.4737 -0.0475 0.0511  -0.0908 210 ALA A C   
1644 O O   . ALA A 201 ? 0.4637 0.4040 0.4475 -0.0492 0.0441  -0.0888 210 ALA A O   
1645 C CB  . ALA A 201 ? 0.5098 0.4767 0.4661 -0.0485 0.0419  -0.0765 210 ALA A CB  
1646 N N   . LEU A 202 ? 0.4808 0.4192 0.4779 -0.0408 0.0606  -0.0911 211 LEU A N   
1647 C CA  . LEU A 202 ? 0.4845 0.4119 0.5060 -0.0343 0.0635  -0.0885 211 LEU A CA  
1648 C C   . LEU A 202 ? 0.4906 0.4021 0.5129 -0.0390 0.0700  -0.1009 211 LEU A C   
1649 O O   . LEU A 202 ? 0.4533 0.3566 0.4875 -0.0376 0.0665  -0.0964 211 LEU A O   
1650 C CB  . LEU A 202 ? 0.4847 0.4128 0.5262 -0.0256 0.0730  -0.0859 211 LEU A CB  
1651 C CG  . LEU A 202 ? 0.4890 0.4082 0.5586 -0.0167 0.0771  -0.0809 211 LEU A CG  
1652 C CD1 . LEU A 202 ? 0.5014 0.4243 0.5785 -0.0140 0.0640  -0.0670 211 LEU A CD1 
1653 C CD2 . LEU A 202 ? 0.4957 0.4218 0.5856 -0.0080 0.0853  -0.0770 211 LEU A CD2 
1654 N N   . GLN A 203 ? 0.4978 0.4050 0.5071 -0.0453 0.0800  -0.1169 212 GLN A N   
1655 C CA  . GLN A 203 ? 0.5437 0.4348 0.5527 -0.0521 0.0876  -0.1323 212 GLN A CA  
1656 C C   . GLN A 203 ? 0.5214 0.4150 0.5195 -0.0612 0.0758  -0.1323 212 GLN A C   
1657 O O   . GLN A 203 ? 0.5497 0.4290 0.5590 -0.0639 0.0780  -0.1360 212 GLN A O   
1658 C CB  . GLN A 203 ? 0.5904 0.4790 0.5837 -0.0588 0.1007  -0.1518 212 GLN A CB  
1659 C CG  . GLN A 203 ? 0.6563 0.5429 0.6619 -0.0498 0.1149  -0.1529 212 GLN A CG  
1660 C CD  . GLN A 203 ? 0.6878 0.5593 0.7276 -0.0381 0.1231  -0.1470 212 GLN A CD  
1661 O OE1 . GLN A 203 ? 0.6862 0.5388 0.7374 -0.0392 0.1297  -0.1544 212 GLN A OE1 
1662 N NE2 . GLN A 203 ? 0.5822 0.4631 0.6396 -0.0269 0.1228  -0.1330 212 GLN A NE2 
1663 N N   . VAL A 204 ? 0.5047 0.4166 0.4838 -0.0653 0.0638  -0.1266 213 VAL A N   
1664 C CA  . VAL A 204 ? 0.5116 0.4305 0.4832 -0.0723 0.0515  -0.1237 213 VAL A CA  
1665 C C   . VAL A 204 ? 0.5098 0.4222 0.5017 -0.0661 0.0459  -0.1101 213 VAL A C   
1666 O O   . VAL A 204 ? 0.4931 0.4005 0.4884 -0.0720 0.0430  -0.1123 213 VAL A O   
1667 C CB  . VAL A 204 ? 0.4936 0.4346 0.4447 -0.0745 0.0403  -0.1162 213 VAL A CB  
1668 C CG1 . VAL A 204 ? 0.4620 0.4126 0.4099 -0.0795 0.0275  -0.1107 213 VAL A CG1 
1669 C CG2 . VAL A 204 ? 0.5384 0.4883 0.4665 -0.0821 0.0449  -0.1287 213 VAL A CG2 
1670 N N   . PHE A 205 ? 0.5085 0.4223 0.5135 -0.0550 0.0448  -0.0966 214 PHE A N   
1671 C CA  . PHE A 205 ? 0.5005 0.4116 0.5226 -0.0485 0.0394  -0.0826 214 PHE A CA  
1672 C C   . PHE A 205 ? 0.5091 0.4013 0.5484 -0.0483 0.0472  -0.0855 214 PHE A C   
1673 O O   . PHE A 205 ? 0.4822 0.3720 0.5286 -0.0487 0.0422  -0.0775 214 PHE A O   
1674 C CB  . PHE A 205 ? 0.5297 0.4473 0.5633 -0.0377 0.0386  -0.0707 214 PHE A CB  
1675 C CG  . PHE A 205 ? 0.4604 0.3861 0.5007 -0.0329 0.0281  -0.0555 214 PHE A CG  
1676 C CD1 . PHE A 205 ? 0.5369 0.4576 0.5834 -0.0337 0.0245  -0.0499 214 PHE A CD1 
1677 C CD2 . PHE A 205 ? 0.5323 0.4705 0.5733 -0.0281 0.0232  -0.0474 214 PHE A CD2 
1678 C CE1 . PHE A 205 ? 0.5381 0.4678 0.5886 -0.0295 0.0159  -0.0367 214 PHE A CE1 
1679 C CE2 . PHE A 205 ? 0.5164 0.4628 0.5620 -0.0247 0.0144  -0.0358 214 PHE A CE2 
1680 C CZ  . PHE A 205 ? 0.5078 0.4505 0.5571 -0.0251 0.0107  -0.0304 214 PHE A CZ  
1681 N N   . HIS A 206 ? 0.5241 0.4022 0.5703 -0.0480 0.0606  -0.0969 215 HIS A N   
1682 C CA  . HIS A 206 ? 0.5421 0.3985 0.6081 -0.0464 0.0710  -0.0995 215 HIS A CA  
1683 C C   . HIS A 206 ? 0.5599 0.4085 0.6238 -0.0569 0.0684  -0.1037 215 HIS A C   
1684 O O   . HIS A 206 ? 0.5601 0.3936 0.6423 -0.0542 0.0730  -0.0973 215 HIS A O   
1685 C CB  . HIS A 206 ? 0.5638 0.4055 0.6340 -0.0466 0.0877  -0.1159 215 HIS A CB  
1686 C CG  . HIS A 206 ? 0.5495 0.3971 0.6293 -0.0351 0.0931  -0.1106 215 HIS A CG  
1687 N ND1 . HIS A 206 ? 0.5887 0.4236 0.6787 -0.0315 0.1098  -0.1219 215 HIS A ND1 
1688 C CD2 . HIS A 206 ? 0.5489 0.4142 0.6315 -0.0268 0.0848  -0.0957 215 HIS A CD2 
1689 C CE1 . HIS A 206 ? 0.6034 0.4498 0.7026 -0.0213 0.1110  -0.1132 215 HIS A CE1 
1690 N NE2 . HIS A 206 ? 0.4922 0.3572 0.5870 -0.0189 0.0957  -0.0977 215 HIS A NE2 
1691 N N   . GLN A 207 ? 0.5760 0.4363 0.6187 -0.0688 0.0612  -0.1131 216 GLN A N   
1692 C CA  . GLN A 207 ? 0.5895 0.4494 0.6294 -0.0802 0.0562  -0.1166 216 GLN A CA  
1693 C C   . GLN A 207 ? 0.5761 0.4390 0.6272 -0.0758 0.0482  -0.0981 216 GLN A C   
1694 O O   . GLN A 207 ? 0.5776 0.4328 0.6354 -0.0834 0.0491  -0.0995 216 GLN A O   
1695 C CB  . GLN A 207 ? 0.6014 0.4827 0.6171 -0.0905 0.0461  -0.1241 216 GLN A CB  
1696 C CG  . GLN A 207 ? 0.6446 0.5262 0.6446 -0.1004 0.0525  -0.1451 216 GLN A CG  
1697 C CD  . GLN A 207 ? 0.6424 0.5499 0.6191 -0.1087 0.0405  -0.1476 216 GLN A CD  
1698 O OE1 . GLN A 207 ? 0.6790 0.5932 0.6483 -0.1221 0.0371  -0.1587 216 GLN A OE1 
1699 N NE2 . GLN A 207 ? 0.6445 0.5677 0.6109 -0.1006 0.0340  -0.1364 216 GLN A NE2 
1700 N N   . ILE A 208 ? 0.5347 0.4097 0.5868 -0.0648 0.0408  -0.0817 217 ILE A N   
1701 C CA  . ILE A 208 ? 0.5059 0.3872 0.5645 -0.0607 0.0328  -0.0647 217 ILE A CA  
1702 C C   . ILE A 208 ? 0.5178 0.3803 0.5961 -0.0598 0.0405  -0.0588 217 ILE A C   
1703 O O   . ILE A 208 ? 0.4745 0.3390 0.5552 -0.0641 0.0367  -0.0522 217 ILE A O   
1704 C CB  . ILE A 208 ? 0.4829 0.3776 0.5416 -0.0490 0.0262  -0.0503 217 ILE A CB  
1705 C CG1 . ILE A 208 ? 0.5374 0.4451 0.5936 -0.0478 0.0160  -0.0370 217 ILE A CG1 
1706 C CG2 . ILE A 208 ? 0.4791 0.3645 0.5557 -0.0380 0.0334  -0.0430 217 ILE A CG2 
1707 C CD1 . ILE A 208 ? 0.4714 0.3971 0.5105 -0.0509 0.0067  -0.0387 217 ILE A CD1 
1708 N N   . HIS A 209 ? 0.5104 0.3548 0.6036 -0.0540 0.0524  -0.0610 218 HIS A N   
1709 C CA  . HIS A 209 ? 0.5314 0.3549 0.6465 -0.0507 0.0620  -0.0533 218 HIS A CA  
1710 C C   . HIS A 209 ? 0.5311 0.3396 0.6484 -0.0650 0.0679  -0.0651 218 HIS A C   
1711 O O   . HIS A 209 ? 0.5337 0.3310 0.6653 -0.0650 0.0715  -0.0546 218 HIS A O   
1712 C CB  . HIS A 209 ? 0.5395 0.3469 0.6717 -0.0407 0.0750  -0.0545 218 HIS A CB  
1713 C CG  . HIS A 209 ? 0.5576 0.3810 0.6924 -0.0271 0.0698  -0.0422 218 HIS A CG  
1714 N ND1 . HIS A 209 ? 0.5613 0.3929 0.7083 -0.0157 0.0647  -0.0201 218 HIS A ND1 
1715 C CD2 . HIS A 209 ? 0.5247 0.3589 0.6516 -0.0241 0.0691  -0.0491 218 HIS A CD2 
1716 C CE1 . HIS A 209 ? 0.5561 0.4036 0.7036 -0.0070 0.0605  -0.0152 218 HIS A CE1 
1717 N NE2 . HIS A 209 ? 0.5189 0.3672 0.6551 -0.0118 0.0636  -0.0323 218 HIS A NE2 
1718 N N   . ASP A 210 ? 0.5584 0.3685 0.6616 -0.0776 0.0688  -0.0865 219 ASP A N   
1719 C CA  . ASP A 210 ? 0.5765 0.3756 0.6806 -0.0940 0.0737  -0.1015 219 ASP A CA  
1720 C C   . ASP A 210 ? 0.5447 0.3606 0.6432 -0.1022 0.0622  -0.0948 219 ASP A C   
1721 O O   . ASP A 210 ? 0.5801 0.3850 0.6889 -0.1126 0.0670  -0.0982 219 ASP A O   
1722 C CB  . ASP A 210 ? 0.6057 0.4069 0.6934 -0.1058 0.0766  -0.1272 219 ASP A CB  
1723 C CG  . ASP A 210 ? 0.6665 0.4494 0.7602 -0.0996 0.0910  -0.1377 219 ASP A CG  
1724 O OD1 . ASP A 210 ? 0.7243 0.4817 0.8407 -0.0932 0.1043  -0.1338 219 ASP A OD1 
1725 O OD2 . ASP A 210 ? 0.6137 0.4080 0.6897 -0.1009 0.0897  -0.1492 219 ASP A OD2 
1726 N N   . HIS A 211 ? 0.5212 0.3631 0.6051 -0.0980 0.0484  -0.0858 220 HIS A N   
1727 C CA  . HIS A 211 ? 0.5033 0.3650 0.5801 -0.1059 0.0376  -0.0822 220 HIS A CA  
1728 C C   . HIS A 211 ? 0.4748 0.3478 0.5549 -0.0962 0.0304  -0.0602 220 HIS A C   
1729 O O   . HIS A 211 ? 0.4705 0.3595 0.5470 -0.1016 0.0230  -0.0563 220 HIS A O   
1730 C CB  . HIS A 211 ? 0.5111 0.3959 0.5669 -0.1115 0.0279  -0.0929 220 HIS A CB  
1731 C CG  . HIS A 211 ? 0.5237 0.4021 0.5714 -0.1212 0.0341  -0.1149 220 HIS A CG  
1732 N ND1 . HIS A 211 ? 0.5311 0.3974 0.5848 -0.1362 0.0414  -0.1314 220 HIS A ND1 
1733 C CD2 . HIS A 211 ? 0.5146 0.3973 0.5480 -0.1188 0.0349  -0.1239 220 HIS A CD2 
1734 C CE1 . HIS A 211 ? 0.5579 0.4217 0.5999 -0.1428 0.0462  -0.1508 220 HIS A CE1 
1735 N NE2 . HIS A 211 ? 0.5661 0.4402 0.5952 -0.1321 0.0425  -0.1459 220 HIS A NE2 
1736 N N   . VAL A 212 ? 0.4608 0.3279 0.5475 -0.0822 0.0324  -0.0464 221 VAL A N   
1737 C CA  . VAL A 212 ? 0.4464 0.3247 0.5346 -0.0736 0.0262  -0.0266 221 VAL A CA  
1738 C C   . VAL A 212 ? 0.4411 0.3024 0.5471 -0.0655 0.0344  -0.0122 221 VAL A C   
1739 O O   . VAL A 212 ? 0.4558 0.3042 0.5706 -0.0580 0.0412  -0.0122 221 VAL A O   
1740 C CB  . VAL A 212 ? 0.4152 0.3117 0.4906 -0.0642 0.0171  -0.0215 221 VAL A CB  
1741 C CG1 . VAL A 212 ? 0.4426 0.3530 0.5165 -0.0584 0.0105  -0.0047 221 VAL A CG1 
1742 C CG2 . VAL A 212 ? 0.4236 0.3345 0.4830 -0.0706 0.0106  -0.0340 221 VAL A CG2 
1743 N N   . ASN A 213 ? 0.4490 0.3117 0.5609 -0.0668 0.0343  0.0010  222 ASN A N   
1744 C CA  . ASN A 213 ? 0.4509 0.3014 0.5785 -0.0588 0.0410  0.0194  222 ASN A CA  
1745 C C   . ASN A 213 ? 0.4190 0.2896 0.5390 -0.0469 0.0319  0.0367  222 ASN A C   
1746 O O   . ASN A 213 ? 0.3709 0.2610 0.4776 -0.0494 0.0233  0.0381  222 ASN A O   
1747 C CB  . ASN A 213 ? 0.4872 0.3295 0.6242 -0.0686 0.0466  0.0240  222 ASN A CB  
1748 C CG  . ASN A 213 ? 0.5166 0.3565 0.6634 -0.0599 0.0498  0.0487  222 ASN A CG  
1749 O OD1 . ASN A 213 ? 0.6285 0.4851 0.7679 -0.0603 0.0443  0.0598  222 ASN A OD1 
1750 N ND2 . ASN A 213 ? 0.6654 0.4857 0.8290 -0.0513 0.0592  0.0582  222 ASN A ND2 
1751 N N   . PRO A 214 ? 0.4256 0.2930 0.5547 -0.0344 0.0340  0.0489  223 PRO A N   
1752 C CA  . PRO A 214 ? 0.4090 0.2979 0.5308 -0.0243 0.0248  0.0644  223 PRO A CA  
1753 C C   . PRO A 214 ? 0.4101 0.3121 0.5251 -0.0258 0.0208  0.0786  223 PRO A C   
1754 O O   . PRO A 214 ? 0.4012 0.3242 0.5008 -0.0253 0.0116  0.0788  223 PRO A O   
1755 C CB  . PRO A 214 ? 0.4206 0.3018 0.5596 -0.0119 0.0300  0.0776  223 PRO A CB  
1756 C CG  . PRO A 214 ? 0.4793 0.3378 0.6299 -0.0141 0.0402  0.0626  223 PRO A CG  
1757 C CD  . PRO A 214 ? 0.4485 0.2940 0.5959 -0.0288 0.0450  0.0482  223 PRO A CD  
1758 N N   . LYS A 215 ? 0.4247 0.3136 0.5516 -0.0280 0.0290  0.0896  224 LYS A N   
1759 C CA  . LYS A 215 ? 0.4470 0.3476 0.5683 -0.0292 0.0274  0.1049  224 LYS A CA  
1760 C C   . LYS A 215 ? 0.4491 0.3645 0.5551 -0.0390 0.0216  0.0932  224 LYS A C   
1761 O O   . LYS A 215 ? 0.4165 0.3529 0.5085 -0.0365 0.0146  0.0988  224 LYS A O   
1762 C CB  . LYS A 215 ? 0.4747 0.3551 0.6135 -0.0317 0.0393  0.1177  224 LYS A CB  
1763 C CG  . LYS A 215 ? 0.5110 0.4047 0.6448 -0.0305 0.0389  0.1386  224 LYS A CG  
1764 C CD  . LYS A 215 ? 0.5560 0.4285 0.7094 -0.0301 0.0518  0.1563  224 LYS A CD  
1765 C CE  . LYS A 215 ? 0.5517 0.4398 0.6977 -0.0289 0.0517  0.1784  224 LYS A CE  
1766 N NZ  . LYS A 215 ? 0.5827 0.4495 0.7485 -0.0283 0.0652  0.1983  224 LYS A NZ  
1767 N N   . ALA A 216 ? 0.4409 0.3464 0.5502 -0.0499 0.0248  0.0764  225 ALA A N   
1768 C CA  . ALA A 216 ? 0.4198 0.3405 0.5181 -0.0588 0.0194  0.0652  225 ALA A CA  
1769 C C   . ALA A 216 ? 0.3949 0.3335 0.4770 -0.0541 0.0093  0.0576  225 ALA A C   
1770 O O   . ALA A 216 ? 0.3801 0.3365 0.4518 -0.0549 0.0044  0.0583  225 ALA A O   
1771 C CB  . ALA A 216 ? 0.4387 0.3480 0.5442 -0.0713 0.0235  0.0482  225 ALA A CB  
1772 N N   . PHE A 217 ? 0.3909 0.3241 0.4721 -0.0492 0.0076  0.0504  226 PHE A N   
1773 C CA  . PHE A 217 ? 0.3569 0.3049 0.4248 -0.0449 -0.0006 0.0443  226 PHE A CA  
1774 C C   . PHE A 217 ? 0.3567 0.3210 0.4162 -0.0378 -0.0056 0.0564  226 PHE A C   
1775 O O   . PHE A 217 ? 0.3505 0.3294 0.3984 -0.0384 -0.0107 0.0527  226 PHE A O   
1776 C CB  . PHE A 217 ? 0.3557 0.2957 0.4259 -0.0404 -0.0002 0.0370  226 PHE A CB  
1777 C CG  . PHE A 217 ? 0.3455 0.2992 0.4034 -0.0373 -0.0075 0.0307  226 PHE A CG  
1778 C CD1 . PHE A 217 ? 0.3614 0.3195 0.4109 -0.0431 -0.0101 0.0182  226 PHE A CD1 
1779 C CD2 . PHE A 217 ? 0.3349 0.2988 0.3899 -0.0293 -0.0118 0.0380  226 PHE A CD2 
1780 C CE1 . PHE A 217 ? 0.3654 0.3341 0.4048 -0.0402 -0.0155 0.0139  226 PHE A CE1 
1781 C CE2 . PHE A 217 ? 0.3379 0.3127 0.3829 -0.0279 -0.0173 0.0313  226 PHE A CE2 
1782 C CZ  . PHE A 217 ? 0.3547 0.3302 0.3924 -0.0330 -0.0185 0.0197  226 PHE A CZ  
1783 N N   . PHE A 218 ? 0.3604 0.3225 0.4262 -0.0310 -0.0038 0.0708  227 PHE A N   
1784 C CA  . PHE A 218 ? 0.3567 0.3367 0.4136 -0.0247 -0.0092 0.0820  227 PHE A CA  
1785 C C   . PHE A 218 ? 0.3656 0.3569 0.4140 -0.0282 -0.0088 0.0890  227 PHE A C   
1786 O O   . PHE A 218 ? 0.3584 0.3666 0.3931 -0.0272 -0.0138 0.0877  227 PHE A O   
1787 C CB  . PHE A 218 ? 0.3713 0.3494 0.4382 -0.0160 -0.0080 0.0979  227 PHE A CB  
1788 C CG  . PHE A 218 ? 0.3586 0.3592 0.4151 -0.0106 -0.0147 0.1098  227 PHE A CG  
1789 C CD1 . PHE A 218 ? 0.3578 0.3735 0.4061 -0.0079 -0.0226 0.1030  227 PHE A CD1 
1790 C CD2 . PHE A 218 ? 0.4278 0.4357 0.4816 -0.0094 -0.0129 0.1271  227 PHE A CD2 
1791 C CE1 . PHE A 218 ? 0.3755 0.4141 0.4127 -0.0050 -0.0292 0.1114  227 PHE A CE1 
1792 C CE2 . PHE A 218 ? 0.4238 0.4554 0.4648 -0.0055 -0.0195 0.1370  227 PHE A CE2 
1793 C CZ  . PHE A 218 ? 0.3779 0.4254 0.4105 -0.0037 -0.0281 0.1282  227 PHE A CZ  
1794 N N   . SER A 219 ? 0.3871 0.3687 0.4443 -0.0326 -0.0017 0.0961  228 SER A N   
1795 C CA  . SER A 219 ? 0.4197 0.4125 0.4704 -0.0353 0.0004  0.1058  228 SER A CA  
1796 C C   . SER A 219 ? 0.4026 0.4038 0.4473 -0.0426 -0.0001 0.0934  228 SER A C   
1797 O O   . SER A 219 ? 0.4362 0.4522 0.4717 -0.0433 0.0003  0.0979  228 SER A O   
1798 C CB  . SER A 219 ? 0.4264 0.4062 0.4908 -0.0370 0.0094  0.1210  228 SER A CB  
1799 O OG  . SER A 219 ? 0.4892 0.4489 0.5683 -0.0443 0.0152  0.1110  228 SER A OG  
1800 N N   . VAL A 220 ? 0.4069 0.4003 0.4568 -0.0477 -0.0008 0.0785  229 VAL A N   
1801 C CA  . VAL A 220 ? 0.4109 0.4129 0.4596 -0.0545 -0.0012 0.0686  229 VAL A CA  
1802 C C   . VAL A 220 ? 0.3930 0.4013 0.4339 -0.0527 -0.0077 0.0547  229 VAL A C   
1803 O O   . VAL A 220 ? 0.3744 0.3964 0.4062 -0.0502 -0.0102 0.0527  229 VAL A O   
1804 C CB  . VAL A 220 ? 0.4392 0.4302 0.5026 -0.0647 0.0041  0.0643  229 VAL A CB  
1805 C CG1 . VAL A 220 ? 0.4483 0.4540 0.5127 -0.0715 0.0028  0.0564  229 VAL A CG1 
1806 C CG2 . VAL A 220 ? 0.4664 0.4474 0.5403 -0.0669 0.0124  0.0789  229 VAL A CG2 
1807 N N   . LEU A 221 ? 0.3880 0.3854 0.4325 -0.0539 -0.0093 0.0455  230 LEU A N   
1808 C CA  . LEU A 221 ? 0.3843 0.3873 0.4224 -0.0531 -0.0144 0.0338  230 LEU A CA  
1809 C C   . LEU A 221 ? 0.3807 0.3909 0.4081 -0.0453 -0.0184 0.0343  230 LEU A C   
1810 O O   . LEU A 221 ? 0.3585 0.3779 0.3799 -0.0442 -0.0209 0.0290  230 LEU A O   
1811 C CB  . LEU A 221 ? 0.3945 0.3850 0.4364 -0.0559 -0.0144 0.0243  230 LEU A CB  
1812 C CG  . LEU A 221 ? 0.3695 0.3659 0.4044 -0.0560 -0.0190 0.0137  230 LEU A CG  
1813 C CD1 . LEU A 221 ? 0.4233 0.4346 0.4580 -0.0602 -0.0214 0.0113  230 LEU A CD1 
1814 C CD2 . LEU A 221 ? 0.3687 0.3533 0.4060 -0.0600 -0.0175 0.0044  230 LEU A CD2 
1815 N N   . ARG A 222 ? 0.3577 0.3642 0.3842 -0.0403 -0.0187 0.0407  231 ARG A N   
1816 C CA  . ARG A 222 ? 0.3673 0.3826 0.3845 -0.0346 -0.0227 0.0408  231 ARG A CA  
1817 C C   . ARG A 222 ? 0.3593 0.3883 0.3675 -0.0346 -0.0228 0.0411  231 ARG A C   
1818 O O   . ARG A 222 ? 0.3459 0.3805 0.3470 -0.0327 -0.0250 0.0343  231 ARG A O   
1819 C CB  . ARG A 222 ? 0.3646 0.3798 0.3842 -0.0298 -0.0234 0.0513  231 ARG A CB  
1820 C CG  . ARG A 222 ? 0.3816 0.4103 0.3918 -0.0258 -0.0284 0.0517  231 ARG A CG  
1821 C CD  . ARG A 222 ? 0.4617 0.4942 0.4762 -0.0208 -0.0303 0.0635  231 ARG A CD  
1822 N NE  . ARG A 222 ? 0.5220 0.5581 0.5364 -0.0203 -0.0276 0.0779  231 ARG A NE  
1823 C CZ  . ARG A 222 ? 0.5695 0.6220 0.5719 -0.0201 -0.0292 0.0846  231 ARG A CZ  
1824 N NH1 . ARG A 222 ? 0.6121 0.6790 0.6015 -0.0208 -0.0337 0.0766  231 ARG A NH1 
1825 N NH2 . ARG A 222 ? 0.5856 0.6397 0.5888 -0.0198 -0.0255 0.0994  231 ARG A NH2 
1826 N N   . ILE A 223 ? 0.3794 0.4127 0.3888 -0.0371 -0.0190 0.0487  232 ILE A N   
1827 C CA  . ILE A 223 ? 0.3676 0.4144 0.3685 -0.0370 -0.0170 0.0497  232 ILE A CA  
1828 C C   . ILE A 223 ? 0.3551 0.4057 0.3568 -0.0379 -0.0165 0.0398  232 ILE A C   
1829 O O   . ILE A 223 ? 0.3835 0.4410 0.3775 -0.0351 -0.0163 0.0345  232 ILE A O   
1830 C CB  . ILE A 223 ? 0.3975 0.4480 0.4014 -0.0400 -0.0116 0.0612  232 ILE A CB  
1831 C CG1 . ILE A 223 ? 0.4163 0.4639 0.4200 -0.0376 -0.0116 0.0746  232 ILE A CG1 
1832 C CG2 . ILE A 223 ? 0.4200 0.4855 0.4154 -0.0401 -0.0078 0.0612  232 ILE A CG2 
1833 C CD1 . ILE A 223 ? 0.4461 0.5051 0.4366 -0.0326 -0.0160 0.0773  232 ILE A CD1 
1834 N N   . TYR A 224 ? 0.3047 0.3512 0.3164 -0.0418 -0.0161 0.0373  233 TYR A N   
1835 C CA  . TYR A 224 ? 0.3187 0.3721 0.3337 -0.0420 -0.0162 0.0308  233 TYR A CA  
1836 C C   . TYR A 224 ? 0.3318 0.3814 0.3427 -0.0381 -0.0198 0.0232  233 TYR A C   
1837 O O   . TYR A 224 ? 0.3366 0.3925 0.3482 -0.0354 -0.0191 0.0198  233 TYR A O   
1838 C CB  . TYR A 224 ? 0.3145 0.3688 0.3412 -0.0486 -0.0160 0.0306  233 TYR A CB  
1839 C CG  . TYR A 224 ? 0.2964 0.3571 0.3292 -0.0529 -0.0108 0.0380  233 TYR A CG  
1840 C CD1 . TYR A 224 ? 0.2940 0.3697 0.3283 -0.0517 -0.0070 0.0395  233 TYR A CD1 
1841 C CD2 . TYR A 224 ? 0.3424 0.3939 0.3806 -0.0579 -0.0081 0.0441  233 TYR A CD2 
1842 C CE1 . TYR A 224 ? 0.2887 0.3717 0.3288 -0.0559 -0.0010 0.0469  233 TYR A CE1 
1843 C CE2 . TYR A 224 ? 0.3347 0.3918 0.3791 -0.0623 -0.0020 0.0524  233 TYR A CE2 
1844 C CZ  . TYR A 224 ? 0.2833 0.3571 0.3281 -0.0616 0.0013  0.0537  233 TYR A CZ  
1845 O OH  . TYR A 224 ? 0.3209 0.4016 0.3721 -0.0663 0.0083  0.0622  233 TYR A OH  
1846 N N   . LEU A 225 ? 0.3204 0.3600 0.3289 -0.0373 -0.0228 0.0214  234 LEU A N   
1847 C CA  . LEU A 225 ? 0.3353 0.3709 0.3399 -0.0339 -0.0252 0.0151  234 LEU A CA  
1848 C C   . LEU A 225 ? 0.3326 0.3705 0.3296 -0.0302 -0.0247 0.0128  234 LEU A C   
1849 O O   . LEU A 225 ? 0.3681 0.4031 0.3636 -0.0280 -0.0249 0.0073  234 LEU A O   
1850 C CB  . LEU A 225 ? 0.3247 0.3499 0.3311 -0.0350 -0.0273 0.0134  234 LEU A CB  
1851 C CG  . LEU A 225 ? 0.3385 0.3598 0.3508 -0.0400 -0.0274 0.0117  234 LEU A CG  
1852 C CD1 . LEU A 225 ? 0.3674 0.3771 0.3813 -0.0404 -0.0273 0.0091  234 LEU A CD1 
1853 C CD2 . LEU A 225 ? 0.4118 0.4400 0.4240 -0.0408 -0.0291 0.0078  234 LEU A CD2 
1854 N N   A SER A 226 ? 0.3349 0.3783 0.3270 -0.0303 -0.0237 0.0167  235 SER A N   
1855 N N   B SER A 226 ? 0.3286 0.3721 0.3207 -0.0303 -0.0236 0.0167  235 SER A N   
1856 C CA  A SER A 226 ? 0.3379 0.3858 0.3212 -0.0287 -0.0237 0.0126  235 SER A CA  
1857 C CA  B SER A 226 ? 0.3273 0.3755 0.3106 -0.0287 -0.0236 0.0129  235 SER A CA  
1858 C C   A SER A 226 ? 0.3522 0.4036 0.3331 -0.0272 -0.0190 0.0061  235 SER A C   
1859 C C   B SER A 226 ? 0.3464 0.3977 0.3272 -0.0272 -0.0190 0.0061  235 SER A C   
1860 O O   A SER A 226 ? 0.3517 0.4062 0.3375 -0.0266 -0.0156 0.0078  235 SER A O   
1861 O O   B SER A 226 ? 0.3454 0.3997 0.3314 -0.0265 -0.0156 0.0076  235 SER A O   
1862 C CB  A SER A 226 ? 0.3536 0.4100 0.3304 -0.0295 -0.0244 0.0196  235 SER A CB  
1863 C CB  B SER A 226 ? 0.3383 0.3953 0.3150 -0.0296 -0.0239 0.0199  235 SER A CB  
1864 O OG  A SER A 226 ? 0.3697 0.4327 0.3452 -0.0306 -0.0200 0.0247  235 SER A OG  
1865 O OG  B SER A 226 ? 0.2866 0.3399 0.2680 -0.0294 -0.0272 0.0279  235 SER A OG  
1866 N N   . GLY A 227 ? 0.3473 0.3982 0.3222 -0.0268 -0.0183 -0.0017 236 GLY A N   
1867 C CA  . GLY A 227 ? 0.3448 0.3952 0.3187 -0.0250 -0.0120 -0.0095 236 GLY A CA  
1868 C C   . GLY A 227 ? 0.3516 0.4100 0.3140 -0.0270 -0.0087 -0.0155 236 GLY A C   
1869 O O   . GLY A 227 ? 0.3615 0.4302 0.3160 -0.0292 -0.0107 -0.0104 236 GLY A O   
1870 N N   . TRP A 228 ? 0.3581 0.4118 0.3196 -0.0264 -0.0029 -0.0263 237 TRP A N   
1871 C CA  . TRP A 228 ? 0.3700 0.4305 0.3197 -0.0293 0.0021  -0.0360 237 TRP A CA  
1872 C C   . TRP A 228 ? 0.3956 0.4479 0.3441 -0.0324 0.0038  -0.0496 237 TRP A C   
1873 O O   . TRP A 228 ? 0.4258 0.4720 0.3745 -0.0319 0.0130  -0.0605 237 TRP A O   
1874 C CB  . TRP A 228 ? 0.3561 0.4198 0.3070 -0.0260 0.0120  -0.0374 237 TRP A CB  
1875 C CG  . TRP A 228 ? 0.3623 0.4176 0.3294 -0.0196 0.0161  -0.0339 237 TRP A CG  
1876 C CD1 . TRP A 228 ? 0.3616 0.4058 0.3372 -0.0154 0.0235  -0.0408 237 TRP A CD1 
1877 C CD2 . TRP A 228 ? 0.3273 0.3865 0.3049 -0.0168 0.0131  -0.0217 237 TRP A CD2 
1878 N NE1 . TRP A 228 ? 0.3479 0.3912 0.3383 -0.0091 0.0244  -0.0319 237 TRP A NE1 
1879 C CE2 . TRP A 228 ? 0.2789 0.3324 0.2702 -0.0107 0.0176  -0.0213 237 TRP A CE2 
1880 C CE3 . TRP A 228 ? 0.3362 0.4031 0.3137 -0.0194 0.0074  -0.0113 237 TRP A CE3 
1881 C CZ2 . TRP A 228 ? 0.3341 0.3931 0.3378 -0.0078 0.0149  -0.0112 237 TRP A CZ2 
1882 C CZ3 . TRP A 228 ? 0.3014 0.3708 0.2918 -0.0176 0.0060  -0.0033 237 TRP A CZ3 
1883 C CH2 . TRP A 228 ? 0.3280 0.3952 0.3305 -0.0122 0.0090  -0.0037 237 TRP A CH2 
1884 N N   . LYS A 229 ? 0.4030 0.4548 0.3522 -0.0356 -0.0041 -0.0488 238 LYS A N   
1885 C CA  . LYS A 229 ? 0.4084 0.4574 0.3555 -0.0412 -0.0041 -0.0616 238 LYS A CA  
1886 C C   . LYS A 229 ? 0.4369 0.5029 0.3752 -0.0468 -0.0138 -0.0601 238 LYS A C   
1887 O O   . LYS A 229 ? 0.4250 0.4943 0.3682 -0.0449 -0.0214 -0.0488 238 LYS A O   
1888 C CB  . LYS A 229 ? 0.3994 0.4328 0.3598 -0.0397 -0.0036 -0.0617 238 LYS A CB  
1889 C CG  . LYS A 229 ? 0.4059 0.4349 0.3670 -0.0467 -0.0020 -0.0755 238 LYS A CG  
1890 C CD  . LYS A 229 ? 0.4393 0.4499 0.4137 -0.0445 0.0025  -0.0754 238 LYS A CD  
1891 C CE  . LYS A 229 ? 0.4879 0.4930 0.4649 -0.0528 0.0059  -0.0899 238 LYS A CE  
1892 N NZ  . LYS A 229 ? 0.4660 0.4874 0.4400 -0.0600 -0.0042 -0.0914 238 LYS A NZ  
1893 N N   . GLY A 230 ? 0.4617 0.5394 0.3874 -0.0534 -0.0132 -0.0716 239 GLY A N   
1894 C CA  . GLY A 230 ? 0.4949 0.5948 0.4107 -0.0583 -0.0231 -0.0685 239 GLY A CA  
1895 C C   . GLY A 230 ? 0.5199 0.6316 0.4310 -0.0536 -0.0279 -0.0506 239 GLY A C   
1896 O O   . GLY A 230 ? 0.5303 0.6550 0.4419 -0.0535 -0.0371 -0.0402 239 GLY A O   
1897 N N   . ASN A 231 ? 0.5129 0.6198 0.4216 -0.0494 -0.0207 -0.0463 240 ASN A N   
1898 C CA  . ASN A 231 ? 0.4999 0.6151 0.4060 -0.0456 -0.0228 -0.0295 240 ASN A CA  
1899 C C   . ASN A 231 ? 0.5143 0.6468 0.4012 -0.0490 -0.0193 -0.0321 240 ASN A C   
1900 O O   . ASN A 231 ? 0.5223 0.6507 0.4049 -0.0493 -0.0094 -0.0420 240 ASN A O   
1901 C CB  . ASN A 231 ? 0.4925 0.5927 0.4108 -0.0399 -0.0170 -0.0228 240 ASN A CB  
1902 C CG  . ASN A 231 ? 0.4946 0.6001 0.4143 -0.0373 -0.0188 -0.0055 240 ASN A CG  
1903 O OD1 . ASN A 231 ? 0.4839 0.6046 0.3926 -0.0387 -0.0213 0.0022  240 ASN A OD1 
1904 N ND2 . ASN A 231 ? 0.4750 0.5685 0.4084 -0.0340 -0.0174 0.0009  240 ASN A ND2 
1905 N N   . PRO A 232 ? 0.5252 0.6783 0.4007 -0.0510 -0.0269 -0.0226 241 PRO A N   
1906 C CA  . PRO A 232 ? 0.5509 0.7239 0.4049 -0.0546 -0.0239 -0.0234 241 PRO A CA  
1907 C C   . PRO A 232 ? 0.5489 0.7185 0.4005 -0.0513 -0.0133 -0.0177 241 PRO A C   
1908 O O   . PRO A 232 ? 0.5355 0.7166 0.3703 -0.0546 -0.0063 -0.0254 241 PRO A O   
1909 C CB  . PRO A 232 ? 0.5590 0.7531 0.4068 -0.0544 -0.0351 -0.0062 241 PRO A CB  
1910 C CG  . PRO A 232 ? 0.5564 0.7456 0.4195 -0.0536 -0.0439 -0.0057 241 PRO A CG  
1911 C CD  . PRO A 232 ? 0.5217 0.6826 0.4038 -0.0496 -0.0381 -0.0097 241 PRO A CD  
1912 N N   . GLN A 233 ? 0.5412 0.6968 0.4099 -0.0457 -0.0118 -0.0055 242 GLN A N   
1913 C CA  . GLN A 233 ? 0.5764 0.7289 0.4481 -0.0431 -0.0019 -0.0001 242 GLN A CA  
1914 C C   . GLN A 233 ? 0.5866 0.7309 0.4602 -0.0427 0.0091  -0.0172 242 GLN A C   
1915 O O   . GLN A 233 ? 0.6145 0.7657 0.4818 -0.0426 0.0189  -0.0183 242 GLN A O   
1916 C CB  . GLN A 233 ? 0.5455 0.6844 0.4373 -0.0389 -0.0035 0.0135  242 GLN A CB  
1917 C CG  . GLN A 233 ? 0.5492 0.6921 0.4432 -0.0379 -0.0111 0.0318  242 GLN A CG  
1918 C CD  . GLN A 233 ? 0.5736 0.7005 0.4878 -0.0353 -0.0112 0.0410  242 GLN A CD  
1919 O OE1 . GLN A 233 ? 0.5362 0.6639 0.4546 -0.0350 -0.0086 0.0552  242 GLN A OE1 
1920 N NE2 . GLN A 233 ? 0.6186 0.7311 0.5451 -0.0340 -0.0135 0.0323  242 GLN A NE2 
1921 N N   . LEU A 234 ? 0.5885 0.7179 0.4725 -0.0420 0.0084  -0.0290 243 LEU A N   
1922 C CA  . LEU A 234 ? 0.5948 0.7138 0.4832 -0.0406 0.0191  -0.0449 243 LEU A CA  
1923 C C   . LEU A 234 ? 0.5946 0.7096 0.4769 -0.0456 0.0177  -0.0623 243 LEU A C   
1924 O O   . LEU A 234 ? 0.5569 0.6558 0.4525 -0.0442 0.0171  -0.0678 243 LEU A O   
1925 C CB  . LEU A 234 ? 0.5856 0.6884 0.4964 -0.0342 0.0213  -0.0404 243 LEU A CB  
1926 C CG  . LEU A 234 ? 0.5958 0.7025 0.5163 -0.0307 0.0228  -0.0253 243 LEU A CG  
1927 C CD1 . LEU A 234 ? 0.6349 0.7396 0.5616 -0.0313 0.0119  -0.0112 243 LEU A CD1 
1928 C CD2 . LEU A 234 ? 0.5998 0.6978 0.5385 -0.0248 0.0299  -0.0271 243 LEU A CD2 
1929 N N   . SER A 235 ? 0.6085 0.7397 0.4702 -0.0523 0.0173  -0.0705 244 SER A N   
1930 C CA  . SER A 235 ? 0.6301 0.7638 0.4827 -0.0603 0.0149  -0.0883 244 SER A CA  
1931 C C   . SER A 235 ? 0.6167 0.7284 0.4812 -0.0603 0.0242  -0.1062 244 SER A C   
1932 O O   . SER A 235 ? 0.6497 0.7541 0.5202 -0.0644 0.0193  -0.1135 244 SER A O   
1933 C CB  . SER A 235 ? 0.6573 0.8134 0.4835 -0.0675 0.0176  -0.0974 244 SER A CB  
1934 O OG  . SER A 235 ? 0.7416 0.9007 0.5579 -0.0771 0.0178  -0.1193 244 SER A OG  
1935 N N   . ASP A 236 ? 0.6204 0.7219 0.4899 -0.0554 0.0383  -0.1119 245 ASP A N   
1936 C CA  . ASP A 236 ? 0.6261 0.7057 0.5078 -0.0540 0.0501  -0.1280 245 ASP A CA  
1937 C C   . ASP A 236 ? 0.6058 0.6670 0.5122 -0.0436 0.0523  -0.1163 245 ASP A C   
1938 O O   . ASP A 236 ? 0.6266 0.6688 0.5463 -0.0404 0.0622  -0.1253 245 ASP A O   
1939 C CB  . ASP A 236 ? 0.6700 0.7508 0.5424 -0.0547 0.0664  -0.1436 245 ASP A CB  
1940 C CG  . ASP A 236 ? 0.7127 0.8128 0.5578 -0.0663 0.0653  -0.1584 245 ASP A CG  
1941 O OD1 . ASP A 236 ? 0.7391 0.8418 0.5780 -0.0756 0.0575  -0.1687 245 ASP A OD1 
1942 O OD2 . ASP A 236 ? 0.7932 0.9080 0.6229 -0.0667 0.0723  -0.1599 245 ASP A OD2 
1943 N N   . GLY A 237 ? 0.5558 0.6231 0.4684 -0.0388 0.0434  -0.0964 246 GLY A N   
1944 C CA  . GLY A 237 ? 0.5080 0.5636 0.4415 -0.0300 0.0437  -0.0842 246 GLY A CA  
1945 C C   . GLY A 237 ? 0.4917 0.5546 0.4312 -0.0234 0.0506  -0.0757 246 GLY A C   
1946 O O   . GLY A 237 ? 0.4525 0.5302 0.3791 -0.0259 0.0535  -0.0754 246 GLY A O   
1947 N N   . LEU A 238 ? 0.4426 0.4969 0.4018 -0.0153 0.0534  -0.0680 247 LEU A N   
1948 C CA  . LEU A 238 ? 0.4403 0.5032 0.4107 -0.0088 0.0593  -0.0589 247 LEU A CA  
1949 C C   . LEU A 238 ? 0.4564 0.5105 0.4399 -0.0012 0.0744  -0.0672 247 LEU A C   
1950 O O   . LEU A 238 ? 0.4565 0.4939 0.4494 0.0019  0.0773  -0.0720 247 LEU A O   
1951 C CB  . LEU A 238 ? 0.4126 0.4769 0.3972 -0.0055 0.0496  -0.0428 247 LEU A CB  
1952 C CG  . LEU A 238 ? 0.4122 0.4893 0.4109 -0.0007 0.0521  -0.0314 247 LEU A CG  
1953 C CD1 . LEU A 238 ? 0.4284 0.5208 0.4164 -0.0063 0.0506  -0.0260 247 LEU A CD1 
1954 C CD2 . LEU A 238 ? 0.3621 0.4381 0.3749 0.0018  0.0429  -0.0200 247 LEU A CD2 
1955 N N   . VAL A 239 ? 0.4671 0.5320 0.4525 0.0020  0.0851  -0.0680 248 VAL A N   
1956 C CA  . VAL A 239 ? 0.4584 0.5169 0.4609 0.0114  0.1007  -0.0732 248 VAL A CA  
1957 C C   . VAL A 239 ? 0.4245 0.4881 0.4518 0.0207  0.0972  -0.0558 248 VAL A C   
1958 O O   . VAL A 239 ? 0.3612 0.4424 0.3928 0.0204  0.0925  -0.0441 248 VAL A O   
1959 C CB  . VAL A 239 ? 0.4807 0.5505 0.4760 0.0114  0.1151  -0.0819 248 VAL A CB  
1960 C CG1 . VAL A 239 ? 0.4907 0.5536 0.5076 0.0229  0.1330  -0.0867 248 VAL A CG1 
1961 C CG2 . VAL A 239 ? 0.5465 0.6146 0.5144 0.0011  0.1175  -0.0999 248 VAL A CG2 
1962 N N   . TYR A 240 ? 0.4336 0.4823 0.4767 0.0278  0.0988  -0.0540 249 TYR A N   
1963 C CA  . TYR A 240 ? 0.4177 0.4728 0.4853 0.0381  0.0974  -0.0384 249 TYR A CA  
1964 C C   . TYR A 240 ? 0.4472 0.5034 0.5318 0.0485  0.1154  -0.0422 249 TYR A C   
1965 O O   . TYR A 240 ? 0.4065 0.4445 0.5013 0.0555  0.1266  -0.0484 249 TYR A O   
1966 C CB  . TYR A 240 ? 0.4314 0.4712 0.5067 0.0414  0.0912  -0.0329 249 TYR A CB  
1967 C CG  . TYR A 240 ? 0.4012 0.4402 0.4616 0.0320  0.0749  -0.0295 249 TYR A CG  
1968 C CD1 . TYR A 240 ? 0.4043 0.4312 0.4460 0.0229  0.0726  -0.0417 249 TYR A CD1 
1969 C CD2 . TYR A 240 ? 0.4161 0.4679 0.4816 0.0317  0.0621  -0.0150 249 TYR A CD2 
1970 C CE1 . TYR A 240 ? 0.4191 0.4462 0.4497 0.0153  0.0586  -0.0381 249 TYR A CE1 
1971 C CE2 . TYR A 240 ? 0.4050 0.4547 0.4578 0.0234  0.0490  -0.0132 249 TYR A CE2 
1972 C CZ  . TYR A 240 ? 0.3859 0.4231 0.4222 0.0161  0.0477  -0.0241 249 TYR A CZ  
1973 O OH  . TYR A 240 ? 0.3747 0.4104 0.4010 0.0092  0.0360  -0.0218 249 TYR A OH  
1974 N N   . GLU A 241 ? 0.4628 0.5397 0.5512 0.0493  0.1194  -0.0385 250 GLU A N   
1975 C CA  . GLU A 241 ? 0.4954 0.5766 0.5982 0.0583  0.1384  -0.0438 250 GLU A CA  
1976 C C   . GLU A 241 ? 0.4920 0.5704 0.6263 0.0736  0.1446  -0.0334 250 GLU A C   
1977 O O   . GLU A 241 ? 0.4686 0.5598 0.6175 0.0774  0.1329  -0.0161 250 GLU A O   
1978 C CB  . GLU A 241 ? 0.4768 0.5846 0.5802 0.0557  0.1397  -0.0380 250 GLU A CB  
1979 C CG  . GLU A 241 ? 0.5300 0.6437 0.6422 0.0625  0.1608  -0.0466 250 GLU A CG  
1980 C CD  . GLU A 241 ? 0.5407 0.6827 0.6576 0.0602  0.1620  -0.0379 250 GLU A CD  
1981 O OE1 . GLU A 241 ? 0.5618 0.7214 0.6998 0.0636  0.1534  -0.0212 250 GLU A OE1 
1982 O OE2 . GLU A 241 ? 0.6130 0.7607 0.7121 0.0543  0.1715  -0.0477 250 GLU A OE2 
1983 N N   . GLY A 242 ? 0.5322 0.5938 0.6767 0.0822  0.1632  -0.0440 251 GLY A N   
1984 C CA  . GLY A 242 ? 0.5313 0.5882 0.7079 0.0988  0.1717  -0.0332 251 GLY A CA  
1985 C C   . GLY A 242 ? 0.5322 0.5650 0.7130 0.1021  0.1678  -0.0294 251 GLY A C   
1986 O O   . GLY A 242 ? 0.5533 0.5757 0.7590 0.1162  0.1790  -0.0228 251 GLY A O   
1987 N N   . PHE A 243 ? 0.5320 0.5559 0.6901 0.0898  0.1531  -0.0322 252 PHE A N   
1988 C CA  . PHE A 243 ? 0.5291 0.5307 0.6897 0.0913  0.1494  -0.0285 252 PHE A CA  
1989 C C   . PHE A 243 ? 0.5525 0.5255 0.6967 0.0826  0.1588  -0.0509 252 PHE A C   
1990 O O   . PHE A 243 ? 0.5676 0.5162 0.7253 0.0892  0.1722  -0.0551 252 PHE A O   
1991 C CB  . PHE A 243 ? 0.4782 0.4906 0.6286 0.0844  0.1272  -0.0151 252 PHE A CB  
1992 C CG  . PHE A 243 ? 0.4868 0.4845 0.6469 0.0902  0.1239  -0.0037 252 PHE A CG  
1993 C CD1 . PHE A 243 ? 0.4771 0.4860 0.6618 0.1043  0.1232  0.0172  252 PHE A CD1 
1994 C CD2 . PHE A 243 ? 0.4568 0.4316 0.6023 0.0817  0.1218  -0.0127 252 PHE A CD2 
1995 C CE1 . PHE A 243 ? 0.4794 0.4759 0.6717 0.1101  0.1206  0.0298  252 PHE A CE1 
1996 C CE2 . PHE A 243 ? 0.4901 0.4512 0.6444 0.0867  0.1201  -0.0012 252 PHE A CE2 
1997 C CZ  . PHE A 243 ? 0.4967 0.4681 0.6734 0.1011  0.1197  0.0206  252 PHE A CZ  
1998 N N   . TRP A 244 ? 0.5394 0.5167 0.6560 0.0676  0.1516  -0.0645 253 TRP A N   
1999 C CA  . TRP A 244 ? 0.5798 0.5377 0.6786 0.0571  0.1600  -0.0885 253 TRP A CA  
2000 C C   . TRP A 244 ? 0.6004 0.5720 0.6826 0.0509  0.1667  -0.1032 253 TRP A C   
2001 O O   . TRP A 244 ? 0.5940 0.5899 0.6683 0.0483  0.1574  -0.0946 253 TRP A O   
2002 C CB  . TRP A 244 ? 0.5587 0.5123 0.6374 0.0437  0.1439  -0.0913 253 TRP A CB  
2003 C CG  . TRP A 244 ? 0.5426 0.4809 0.6330 0.0472  0.1388  -0.0803 253 TRP A CG  
2004 C CD1 . TRP A 244 ? 0.5853 0.4969 0.6897 0.0515  0.1514  -0.0849 253 TRP A CD1 
2005 C CD2 . TRP A 244 ? 0.5390 0.4871 0.6272 0.0459  0.1208  -0.0632 253 TRP A CD2 
2006 N NE1 . TRP A 244 ? 0.5663 0.4718 0.6771 0.0534  0.1420  -0.0698 253 TRP A NE1 
2007 C CE2 . TRP A 244 ? 0.5712 0.4994 0.6713 0.0499  0.1231  -0.0572 253 TRP A CE2 
2008 C CE3 . TRP A 244 ? 0.5089 0.4798 0.5868 0.0415  0.1040  -0.0526 253 TRP A CE3 
2009 C CZ2 . TRP A 244 ? 0.4653 0.3976 0.5650 0.0496  0.1090  -0.0415 253 TRP A CZ2 
2010 C CZ3 . TRP A 244 ? 0.4986 0.4719 0.5772 0.0410  0.0904  -0.0388 253 TRP A CZ3 
2011 C CH2 . TRP A 244 ? 0.4915 0.4467 0.5799 0.0450  0.0929  -0.0335 253 TRP A CH2 
2012 N N   . GLU A 245 ? 0.6483 0.6039 0.7247 0.0476  0.1835  -0.1257 254 GLU A N   
2013 C CA  . GLU A 245 ? 0.6655 0.6332 0.7220 0.0403  0.1917  -0.1427 254 GLU A CA  
2014 C C   . GLU A 245 ? 0.6587 0.6377 0.6826 0.0233  0.1761  -0.1501 254 GLU A C   
2015 O O   . GLU A 245 ? 0.6427 0.6440 0.6497 0.0184  0.1721  -0.1490 254 GLU A O   
2016 C CB  . GLU A 245 ? 0.7079 0.6537 0.7676 0.0411  0.2155  -0.1671 254 GLU A CB  
2017 C CG  . GLU A 245 ? 0.7771 0.7116 0.8710 0.0594  0.2343  -0.1606 254 GLU A CG  
2018 C CD  . GLU A 245 ? 0.7749 0.6860 0.8728 0.0604  0.2606  -0.1866 254 GLU A CD  
2019 O OE1 . GLU A 245 ? 0.8016 0.7019 0.8760 0.0453  0.2635  -0.2112 254 GLU A OE1 
2020 O OE2 . GLU A 245 ? 0.7961 0.7004 0.9217 0.0761  0.2789  -0.1828 254 GLU A OE2 
2021 N N   . ASP A 246 ? 0.6476 0.6117 0.6642 0.0148  0.1683  -0.1567 255 ASP A N   
2022 C CA  . ASP A 246 ? 0.6462 0.6213 0.6351 -0.0005 0.1534  -0.1633 255 ASP A CA  
2023 C C   . ASP A 246 ? 0.6141 0.6043 0.6019 -0.0006 0.1323  -0.1406 255 ASP A C   
2024 O O   . ASP A 246 ? 0.5861 0.5707 0.5934 0.0082  0.1277  -0.1241 255 ASP A O   
2025 C CB  . ASP A 246 ? 0.6617 0.6164 0.6464 -0.0103 0.1543  -0.1804 255 ASP A CB  
2026 C CG  . ASP A 246 ? 0.7439 0.6861 0.7218 -0.0162 0.1735  -0.2089 255 ASP A CG  
2027 O OD1 . ASP A 246 ? 0.7668 0.7178 0.7389 -0.0135 0.1859  -0.2166 255 ASP A OD1 
2028 O OD2 . ASP A 246 ? 0.8390 0.7622 0.8172 -0.0246 0.1769  -0.2247 255 ASP A OD2 
2029 N N   . PRO A 247 ? 0.5953 0.6048 0.5601 -0.0105 0.1197  -0.1399 256 PRO A N   
2030 C CA  . PRO A 247 ? 0.5520 0.5721 0.5164 -0.0111 0.1012  -0.1204 256 PRO A CA  
2031 C C   . PRO A 247 ? 0.5212 0.5264 0.4907 -0.0143 0.0923  -0.1198 256 PRO A C   
2032 O O   . PRO A 247 ? 0.4961 0.4897 0.4601 -0.0215 0.0962  -0.1365 256 PRO A O   
2033 C CB  . PRO A 247 ? 0.5728 0.6143 0.5120 -0.0206 0.0930  -0.1215 256 PRO A CB  
2034 C CG  . PRO A 247 ? 0.6069 0.6466 0.5293 -0.0290 0.1026  -0.1451 256 PRO A CG  
2035 C CD  . PRO A 247 ? 0.6206 0.6436 0.5589 -0.0212 0.1223  -0.1558 256 PRO A CD  
2036 N N   . LYS A 248 ? 0.4594 0.4656 0.4401 -0.0094 0.0816  -0.1015 257 LYS A N   
2037 C CA  . LYS A 248 ? 0.4662 0.4594 0.4537 -0.0106 0.0742  -0.0978 257 LYS A CA  
2038 C C   . LYS A 248 ? 0.4591 0.4650 0.4383 -0.0153 0.0572  -0.0863 257 LYS A C   
2039 O O   . LYS A 248 ? 0.4339 0.4533 0.4130 -0.0125 0.0514  -0.0735 257 LYS A O   
2040 C CB  . LYS A 248 ? 0.4436 0.4247 0.4539 0.0009  0.0791  -0.0862 257 LYS A CB  
2041 C CG  . LYS A 248 ? 0.4615 0.4274 0.4854 0.0082  0.0976  -0.0949 257 LYS A CG  
2042 C CD  . LYS A 248 ? 0.4776 0.4236 0.4981 0.0009  0.1062  -0.1143 257 LYS A CD  
2043 C CE  . LYS A 248 ? 0.5324 0.4594 0.5691 0.0088  0.1266  -0.1231 257 LYS A CE  
2044 N NZ  . LYS A 248 ? 0.5811 0.4864 0.6156 -0.0003 0.1357  -0.1437 257 LYS A NZ  
2045 N N   . GLU A 249 ? 0.4471 0.4481 0.4213 -0.0226 0.0503  -0.0913 258 GLU A N   
2046 C CA  . GLU A 249 ? 0.4309 0.4423 0.3989 -0.0267 0.0356  -0.0819 258 GLU A CA  
2047 C C   . GLU A 249 ? 0.4100 0.4117 0.3911 -0.0223 0.0308  -0.0706 258 GLU A C   
2048 O O   . GLU A 249 ? 0.4647 0.4509 0.4544 -0.0217 0.0356  -0.0747 258 GLU A O   
2049 C CB  . GLU A 249 ? 0.4225 0.4391 0.3782 -0.0373 0.0304  -0.0934 258 GLU A CB  
2050 C CG  . GLU A 249 ? 0.4640 0.4975 0.4015 -0.0433 0.0307  -0.1019 258 GLU A CG  
2051 C CD  . GLU A 249 ? 0.4970 0.5402 0.4236 -0.0540 0.0230  -0.1115 258 GLU A CD  
2052 O OE1 . GLU A 249 ? 0.6039 0.6369 0.5331 -0.0599 0.0281  -0.1269 258 GLU A OE1 
2053 O OE2 . GLU A 249 ? 0.5522 0.6137 0.4696 -0.0565 0.0119  -0.1029 258 GLU A OE2 
2054 N N   . PHE A 250 ? 0.3879 0.3985 0.3701 -0.0198 0.0222  -0.0568 259 PHE A N   
2055 C CA  . PHE A 250 ? 0.3770 0.3820 0.3674 -0.0173 0.0163  -0.0468 259 PHE A CA  
2056 C C   . PHE A 250 ? 0.3607 0.3761 0.3450 -0.0209 0.0053  -0.0398 259 PHE A C   
2057 O O   . PHE A 250 ? 0.3584 0.3852 0.3374 -0.0215 0.0028  -0.0354 259 PHE A O   
2058 C CB  . PHE A 250 ? 0.3801 0.3838 0.3824 -0.0088 0.0196  -0.0368 259 PHE A CB  
2059 C CG  . PHE A 250 ? 0.3784 0.3703 0.3907 -0.0030 0.0314  -0.0410 259 PHE A CG  
2060 C CD1 . PHE A 250 ? 0.4466 0.4226 0.4657 -0.0020 0.0352  -0.0423 259 PHE A CD1 
2061 C CD2 . PHE A 250 ? 0.3797 0.3757 0.3959 0.0018  0.0402  -0.0433 259 PHE A CD2 
2062 C CE1 . PHE A 250 ? 0.3682 0.3302 0.3988 0.0041  0.0479  -0.0454 259 PHE A CE1 
2063 C CE2 . PHE A 250 ? 0.3953 0.3787 0.4233 0.0084  0.0529  -0.0470 259 PHE A CE2 
2064 C CZ  . PHE A 250 ? 0.4186 0.3839 0.4542 0.0098  0.0569  -0.0478 259 PHE A CZ  
2065 N N   . ALA A 251 ? 0.3677 0.3782 0.3541 -0.0231 0.0001  -0.0383 260 ALA A N   
2066 C CA  . ALA A 251 ? 0.3438 0.3612 0.3273 -0.0257 -0.0088 -0.0322 260 ALA A CA  
2067 C C   . ALA A 251 ? 0.3273 0.3469 0.3148 -0.0222 -0.0117 -0.0217 260 ALA A C   
2068 O O   . ALA A 251 ? 0.3322 0.3474 0.3261 -0.0182 -0.0092 -0.0181 260 ALA A O   
2069 C CB  . ALA A 251 ? 0.3435 0.3549 0.3305 -0.0284 -0.0115 -0.0343 260 ALA A CB  
2070 N N   . GLY A 252 ? 0.3203 0.3474 0.3048 -0.0242 -0.0169 -0.0164 261 GLY A N   
2071 C CA  . GLY A 252 ? 0.3312 0.3592 0.3198 -0.0234 -0.0199 -0.0085 261 GLY A CA  
2072 C C   . GLY A 252 ? 0.3327 0.3535 0.3249 -0.0235 -0.0226 -0.0077 261 GLY A C   
2073 O O   . GLY A 252 ? 0.3512 0.3670 0.3435 -0.0241 -0.0223 -0.0118 261 GLY A O   
2074 N N   . GLY A 253 ? 0.2994 0.3205 0.2947 -0.0239 -0.0246 -0.0031 262 GLY A N   
2075 C CA  . GLY A 253 ? 0.3277 0.3432 0.3244 -0.0244 -0.0261 -0.0031 262 GLY A CA  
2076 C C   . GLY A 253 ? 0.3290 0.3403 0.3257 -0.0258 -0.0276 -0.0050 262 GLY A C   
2077 O O   . GLY A 253 ? 0.2959 0.3103 0.2927 -0.0266 -0.0292 -0.0038 262 GLY A O   
2078 N N   . SER A 254 ? 0.3386 0.3446 0.3361 -0.0256 -0.0266 -0.0067 263 SER A N   
2079 C CA  . SER A 254 ? 0.3351 0.3382 0.3350 -0.0265 -0.0269 -0.0085 263 SER A CA  
2080 C C   . SER A 254 ? 0.3493 0.3476 0.3484 -0.0267 -0.0249 -0.0092 263 SER A C   
2081 O O   . SER A 254 ? 0.3424 0.3398 0.3389 -0.0257 -0.0232 -0.0081 263 SER A O   
2082 C CB  . SER A 254 ? 0.3798 0.3846 0.3812 -0.0270 -0.0264 -0.0120 263 SER A CB  
2083 O OG  . SER A 254 ? 0.3598 0.3642 0.3662 -0.0279 -0.0263 -0.0135 263 SER A OG  
2084 N N   . ALA A 255 ? 0.3405 0.3363 0.3420 -0.0277 -0.0243 -0.0103 264 ALA A N   
2085 C CA  . ALA A 255 ? 0.3405 0.3327 0.3397 -0.0283 -0.0211 -0.0122 264 ALA A CA  
2086 C C   . ALA A 255 ? 0.3176 0.3085 0.3200 -0.0278 -0.0182 -0.0131 264 ALA A C   
2087 O O   . ALA A 255 ? 0.3625 0.3509 0.3629 -0.0283 -0.0144 -0.0135 264 ALA A O   
2088 C CB  . ALA A 255 ? 0.3613 0.3504 0.3625 -0.0295 -0.0194 -0.0148 264 ALA A CB  
2089 N N   . GLY A 256 ? 0.3100 0.3035 0.3169 -0.0279 -0.0195 -0.0139 265 GLY A N   
2090 C CA  . GLY A 256 ? 0.3266 0.3181 0.3363 -0.0291 -0.0164 -0.0158 265 GLY A CA  
2091 C C   . GLY A 256 ? 0.3131 0.2989 0.3183 -0.0277 -0.0130 -0.0131 265 GLY A C   
2092 O O   . GLY A 256 ? 0.2796 0.2604 0.2872 -0.0284 -0.0082 -0.0128 265 GLY A O   
2093 N N   . GLN A 257 ? 0.3205 0.3080 0.3208 -0.0254 -0.0152 -0.0101 266 GLN A N   
2094 C CA  . GLN A 257 ? 0.3299 0.3153 0.3276 -0.0224 -0.0128 -0.0050 266 GLN A CA  
2095 C C   . GLN A 257 ? 0.3427 0.3299 0.3344 -0.0221 -0.0124 -0.0007 266 GLN A C   
2096 O O   . GLN A 257 ? 0.3318 0.3201 0.3209 -0.0191 -0.0110 0.0059  266 GLN A O   
2097 C CB  . GLN A 257 ? 0.3339 0.3243 0.3309 -0.0200 -0.0154 -0.0030 266 GLN A CB  
2098 C CG  . GLN A 257 ? 0.2821 0.2725 0.2821 -0.0205 -0.0151 -0.0077 266 GLN A CG  
2099 C CD  . GLN A 257 ? 0.2816 0.2790 0.2808 -0.0190 -0.0174 -0.0061 266 GLN A CD  
2100 O OE1 . GLN A 257 ? 0.2987 0.3021 0.2965 -0.0191 -0.0206 -0.0024 266 GLN A OE1 
2101 N NE2 . GLN A 257 ? 0.3023 0.3002 0.3024 -0.0187 -0.0153 -0.0097 266 GLN A NE2 
2102 N N   . SER A 258 ? 0.3243 0.3127 0.3136 -0.0250 -0.0132 -0.0041 267 SER A N   
2103 C CA  . SER A 258 ? 0.3301 0.3205 0.3116 -0.0260 -0.0115 -0.0024 267 SER A CA  
2104 C C   . SER A 258 ? 0.3369 0.3227 0.3189 -0.0254 -0.0053 0.0010  267 SER A C   
2105 O O   . SER A 258 ? 0.3315 0.3127 0.3209 -0.0268 -0.0019 -0.0024 267 SER A O   
2106 C CB  . SER A 258 ? 0.3357 0.3264 0.3158 -0.0292 -0.0115 -0.0088 267 SER A CB  
2107 O OG  . SER A 258 ? 0.3088 0.3015 0.2797 -0.0308 -0.0084 -0.0088 267 SER A OG  
2108 N N   . SER A 259 ? 0.3366 0.3250 0.3115 -0.0234 -0.0038 0.0086  268 SER A N   
2109 C CA  . SER A 259 ? 0.3645 0.3480 0.3393 -0.0227 0.0032  0.0143  268 SER A CA  
2110 C C   . SER A 259 ? 0.3812 0.3660 0.3506 -0.0262 0.0075  0.0109  268 SER A C   
2111 O O   . SER A 259 ? 0.3864 0.3659 0.3603 -0.0270 0.0144  0.0128  268 SER A O   
2112 C CB  . SER A 259 ? 0.3869 0.3742 0.3564 -0.0181 0.0036  0.0266  268 SER A CB  
2113 O OG  . SER A 259 ? 0.4021 0.3875 0.3794 -0.0138 0.0016  0.0297  268 SER A OG  
2114 N N   A VAL A 260 ? 0.3915 0.3827 0.3523 -0.0287 0.0047  0.0052  269 VAL A N   
2115 N N   B VAL A 260 ? 0.3881 0.3792 0.3492 -0.0287 0.0047  0.0051  269 VAL A N   
2116 C CA  A VAL A 260 ? 0.4071 0.3995 0.3621 -0.0317 0.0106  0.0005  269 VAL A CA  
2117 C CA  B VAL A 260 ? 0.3985 0.3909 0.3533 -0.0316 0.0106  0.0010  269 VAL A CA  
2118 C C   A VAL A 260 ? 0.3952 0.3817 0.3639 -0.0326 0.0155  -0.0051 269 VAL A C   
2119 C C   B VAL A 260 ? 0.3900 0.3767 0.3584 -0.0327 0.0155  -0.0053 269 VAL A C   
2120 O O   A VAL A 260 ? 0.4045 0.3902 0.3743 -0.0337 0.0232  -0.0040 269 VAL A O   
2121 O O   B VAL A 260 ? 0.4018 0.3880 0.3707 -0.0339 0.0232  -0.0048 269 VAL A O   
2122 C CB  A VAL A 260 ? 0.4250 0.4231 0.3690 -0.0352 0.0083  -0.0079 269 VAL A CB  
2123 C CB  B VAL A 260 ? 0.4075 0.4072 0.3492 -0.0349 0.0079  -0.0057 269 VAL A CB  
2124 C CG1 A VAL A 260 ? 0.4607 0.4698 0.3891 -0.0362 0.0041  -0.0030 269 VAL A CG1 
2125 C CG1 B VAL A 260 ? 0.3901 0.3860 0.3399 -0.0365 0.0051  -0.0157 269 VAL A CG1 
2126 C CG2 A VAL A 260 ? 0.4280 0.4231 0.3805 -0.0360 0.0035  -0.0155 269 VAL A CG2 
2127 C CG2 B VAL A 260 ? 0.4316 0.4343 0.3616 -0.0377 0.0155  -0.0082 269 VAL A CG2 
2128 N N   . PHE A 261 ? 0.3689 0.3536 0.3486 -0.0322 0.0111  -0.0100 270 PHE A N   
2129 C CA  . PHE A 261 ? 0.3853 0.3690 0.3796 -0.0326 0.0139  -0.0145 270 PHE A CA  
2130 C C   . PHE A 261 ? 0.3944 0.3763 0.3992 -0.0335 0.0163  -0.0115 270 PHE A C   
2131 O O   . PHE A 261 ? 0.3739 0.3576 0.3887 -0.0352 0.0216  -0.0133 270 PHE A O   
2132 C CB  . PHE A 261 ? 0.4178 0.4024 0.4195 -0.0315 0.0082  -0.0188 270 PHE A CB  
2133 C CG  . PHE A 261 ? 0.4658 0.4495 0.4597 -0.0320 0.0077  -0.0230 270 PHE A CG  
2134 C CD1 . PHE A 261 ? 0.4769 0.4598 0.4683 -0.0330 0.0148  -0.0282 270 PHE A CD1 
2135 C CD2 . PHE A 261 ? 0.4743 0.4581 0.4635 -0.0323 0.0013  -0.0228 270 PHE A CD2 
2136 C CE1 . PHE A 261 ? 0.4966 0.4772 0.4805 -0.0349 0.0156  -0.0346 270 PHE A CE1 
2137 C CE2 . PHE A 261 ? 0.5210 0.5035 0.5040 -0.0346 0.0014  -0.0282 270 PHE A CE2 
2138 C CZ  . PHE A 261 ? 0.5030 0.4832 0.4831 -0.0362 0.0086  -0.0348 270 PHE A CZ  
2139 N N   . GLN A 262 ? 0.3583 0.3367 0.3618 -0.0327 0.0133  -0.0077 271 GLN A N   
2140 C CA  . GLN A 262 ? 0.3696 0.3431 0.3817 -0.0346 0.0176  -0.0057 271 GLN A CA  
2141 C C   . GLN A 262 ? 0.3684 0.3387 0.3779 -0.0356 0.0267  0.0004  271 GLN A C   
2142 O O   . GLN A 262 ? 0.3825 0.3503 0.4029 -0.0391 0.0327  -0.0002 271 GLN A O   
2143 C CB  . GLN A 262 ? 0.3864 0.3547 0.3975 -0.0326 0.0147  -0.0031 271 GLN A CB  
2144 C CG  . GLN A 262 ? 0.3493 0.3211 0.3640 -0.0328 0.0074  -0.0092 271 GLN A CG  
2145 C CD  . GLN A 262 ? 0.3969 0.3639 0.4195 -0.0350 0.0087  -0.0129 271 GLN A CD  
2146 O OE1 . GLN A 262 ? 0.3379 0.2986 0.3675 -0.0382 0.0152  -0.0132 271 GLN A OE1 
2147 N NE2 . GLN A 262 ? 0.2758 0.2457 0.2971 -0.0343 0.0033  -0.0165 271 GLN A NE2 
2148 N N   A CYS A 263 ? 0.3974 0.3695 0.3922 -0.0332 0.0275  0.0063  272 CYS A N   
2149 N N   B CYS A 263 ? 0.3715 0.3435 0.3663 -0.0332 0.0277  0.0064  272 CYS A N   
2150 C CA  A CYS A 263 ? 0.4112 0.3829 0.3985 -0.0335 0.0357  0.0141  272 CYS A CA  
2151 C CA  B CYS A 263 ? 0.3972 0.3682 0.3859 -0.0338 0.0364  0.0142  272 CYS A CA  
2152 C C   A CYS A 263 ? 0.4140 0.3888 0.4064 -0.0370 0.0433  0.0097  272 CYS A C   
2153 C C   B CYS A 263 ? 0.4031 0.3777 0.3962 -0.0372 0.0436  0.0096  272 CYS A C   
2154 O O   A CYS A 263 ? 0.3976 0.3692 0.3953 -0.0392 0.0520  0.0146  272 CYS A O   
2155 O O   B CYS A 263 ? 0.3863 0.3581 0.3849 -0.0395 0.0524  0.0142  272 CYS A O   
2156 C CB  A CYS A 263 ? 0.4275 0.4063 0.3956 -0.0310 0.0321  0.0188  272 CYS A CB  
2157 C CB  B CYS A 263 ? 0.4084 0.3854 0.3778 -0.0309 0.0343  0.0214  272 CYS A CB  
2158 S SG  A CYS A 263 ? 0.5180 0.5018 0.4703 -0.0313 0.0402  0.0287  272 CYS A SG  
2159 S SG  B CYS A 263 ? 0.4684 0.4417 0.4358 -0.0255 0.0325  0.0354  272 CYS A SG  
2160 N N   . PHE A 264 ? 0.4007 0.3811 0.3930 -0.0373 0.0410  0.0009  273 PHE A N   
2161 C CA  . PHE A 264 ? 0.4373 0.4219 0.4366 -0.0392 0.0488  -0.0040 273 PHE A CA  
2162 C C   . PHE A 264 ? 0.4206 0.4069 0.4427 -0.0415 0.0499  -0.0075 273 PHE A C   
2163 O O   . PHE A 264 ? 0.4105 0.4005 0.4419 -0.0439 0.0585  -0.0077 273 PHE A O   
2164 C CB  . PHE A 264 ? 0.4922 0.4808 0.4839 -0.0380 0.0482  -0.0119 273 PHE A CB  
2165 C CG  . PHE A 264 ? 0.5386 0.5294 0.5070 -0.0385 0.0495  -0.0099 273 PHE A CG  
2166 C CD1 . PHE A 264 ? 0.5823 0.5757 0.5399 -0.0400 0.0583  -0.0033 273 PHE A CD1 
2167 C CD2 . PHE A 264 ? 0.5789 0.5709 0.5358 -0.0382 0.0418  -0.0138 273 PHE A CD2 
2168 C CE1 . PHE A 264 ? 0.5895 0.5889 0.5236 -0.0408 0.0584  -0.0005 273 PHE A CE1 
2169 C CE2 . PHE A 264 ? 0.6100 0.6079 0.5451 -0.0399 0.0417  -0.0125 273 PHE A CE2 
2170 C CZ  . PHE A 264 ? 0.6192 0.6218 0.5420 -0.0411 0.0495  -0.0057 273 PHE A CZ  
2171 N N   . ASP A 265 ? 0.3931 0.3787 0.4239 -0.0413 0.0414  -0.0101 274 ASP A N   
2172 C CA  . ASP A 265 ? 0.3873 0.3770 0.4381 -0.0451 0.0413  -0.0132 274 ASP A CA  
2173 C C   . ASP A 265 ? 0.3588 0.3423 0.4144 -0.0498 0.0493  -0.0087 274 ASP A C   
2174 O O   . ASP A 265 ? 0.3079 0.2968 0.3784 -0.0543 0.0557  -0.0102 274 ASP A O   
2175 C CB  . ASP A 265 ? 0.3689 0.3600 0.4240 -0.0449 0.0308  -0.0170 274 ASP A CB  
2176 C CG  . ASP A 265 ? 0.4614 0.4601 0.5186 -0.0410 0.0242  -0.0204 274 ASP A CG  
2177 O OD1 . ASP A 265 ? 0.4202 0.4250 0.4847 -0.0394 0.0281  -0.0218 274 ASP A OD1 
2178 O OD2 . ASP A 265 ? 0.4881 0.4861 0.5406 -0.0392 0.0162  -0.0210 274 ASP A OD2 
2179 N N   . VAL A 266 ? 0.3744 0.3471 0.4192 -0.0486 0.0498  -0.0024 275 VAL A N   
2180 C CA  . VAL A 266 ? 0.3960 0.3593 0.4453 -0.0520 0.0591  0.0042  275 VAL A CA  
2181 C C   . VAL A 266 ? 0.3945 0.3602 0.4408 -0.0530 0.0700  0.0104  275 VAL A C   
2182 O O   . VAL A 266 ? 0.3896 0.3542 0.4497 -0.0587 0.0788  0.0113  275 VAL A O   
2183 C CB  . VAL A 266 ? 0.4149 0.3663 0.4534 -0.0477 0.0583  0.0126  275 VAL A CB  
2184 C CG1 . VAL A 266 ? 0.4382 0.3778 0.4810 -0.0497 0.0700  0.0228  275 VAL A CG1 
2185 C CG2 . VAL A 266 ? 0.3786 0.3263 0.4225 -0.0477 0.0507  0.0059  275 VAL A CG2 
2186 N N   . LEU A 267 ? 0.3907 0.3603 0.4186 -0.0486 0.0699  0.0140  276 LEU A N   
2187 C CA  . LEU A 267 ? 0.4339 0.4072 0.4541 -0.0495 0.0807  0.0197  276 LEU A CA  
2188 C C   . LEU A 267 ? 0.4163 0.3978 0.4539 -0.0537 0.0875  0.0128  276 LEU A C   
2189 O O   . LEU A 267 ? 0.4478 0.4294 0.4916 -0.0576 0.0990  0.0179  276 LEU A O   
2190 C CB  . LEU A 267 ? 0.4339 0.4133 0.4306 -0.0454 0.0782  0.0201  276 LEU A CB  
2191 C CG  . LEU A 267 ? 0.4741 0.4586 0.4573 -0.0465 0.0898  0.0263  276 LEU A CG  
2192 C CD1 . LEU A 267 ? 0.5261 0.5050 0.5003 -0.0457 0.0948  0.0430  276 LEU A CD1 
2193 C CD2 . LEU A 267 ? 0.5197 0.5126 0.4824 -0.0448 0.0873  0.0201  276 LEU A CD2 
2194 N N   . LEU A 268 ? 0.3803 0.3695 0.4276 -0.0527 0.0808  0.0024  277 LEU A N   
2195 C CA  . LEU A 268 ? 0.3782 0.3786 0.4445 -0.0548 0.0861  -0.0036 277 LEU A CA  
2196 C C   . LEU A 268 ? 0.3618 0.3667 0.4538 -0.0609 0.0849  -0.0066 277 LEU A C   
2197 O O   . LEU A 268 ? 0.3650 0.3831 0.4764 -0.0625 0.0872  -0.0112 277 LEU A O   
2198 C CB  . LEU A 268 ? 0.3595 0.3666 0.4254 -0.0496 0.0804  -0.0115 277 LEU A CB  
2199 C CG  . LEU A 268 ? 0.3772 0.3812 0.4191 -0.0459 0.0832  -0.0120 277 LEU A CG  
2200 C CD1 . LEU A 268 ? 0.3770 0.3821 0.4184 -0.0414 0.0762  -0.0198 277 LEU A CD1 
2201 C CD2 . LEU A 268 ? 0.3823 0.3913 0.4208 -0.0472 0.0981  -0.0115 277 LEU A CD2 
2202 N N   . GLY A 269 ? 0.3414 0.3364 0.4343 -0.0644 0.0818  -0.0044 278 GLY A N   
2203 C CA  . GLY A 269 ? 0.3562 0.3545 0.4715 -0.0724 0.0811  -0.0092 278 GLY A CA  
2204 C C   . GLY A 269 ? 0.3480 0.3610 0.4766 -0.0726 0.0697  -0.0184 278 GLY A C   
2205 O O   . GLY A 269 ? 0.3388 0.3642 0.4890 -0.0795 0.0695  -0.0234 278 GLY A O   
2206 N N   . ILE A 270 ? 0.3771 0.3903 0.4933 -0.0655 0.0599  -0.0197 279 ILE A N   
2207 C CA  . ILE A 270 ? 0.3763 0.4036 0.5028 -0.0642 0.0486  -0.0256 279 ILE A CA  
2208 C C   . ILE A 270 ? 0.3799 0.4076 0.5114 -0.0706 0.0409  -0.0310 279 ILE A C   
2209 O O   . ILE A 270 ? 0.3836 0.4280 0.5279 -0.0728 0.0328  -0.0359 279 ILE A O   
2210 C CB  . ILE A 270 ? 0.3680 0.3937 0.4804 -0.0549 0.0427  -0.0245 279 ILE A CB  
2211 C CG1 . ILE A 270 ? 0.3979 0.4275 0.5119 -0.0506 0.0513  -0.0232 279 ILE A CG1 
2212 C CG2 . ILE A 270 ? 0.3706 0.4084 0.4910 -0.0528 0.0309  -0.0276 279 ILE A CG2 
2213 C CD1 . ILE A 270 ? 0.4099 0.4322 0.5066 -0.0436 0.0502  -0.0231 279 ILE A CD1 
2214 N N   A GLN A 271 ? 0.4044 0.4148 0.5262 -0.0733 0.0439  -0.0301 280 GLN A N   
2215 N N   B GLN A 271 ? 0.4075 0.4177 0.5288 -0.0731 0.0439  -0.0299 280 GLN A N   
2216 C CA  A GLN A 271 ? 0.4048 0.4123 0.5313 -0.0804 0.0401  -0.0372 280 GLN A CA  
2217 C CA  B GLN A 271 ? 0.4100 0.4167 0.5357 -0.0801 0.0403  -0.0369 280 GLN A CA  
2218 C C   A GLN A 271 ? 0.3839 0.4008 0.5051 -0.0779 0.0270  -0.0423 280 GLN A C   
2219 C C   B GLN A 271 ? 0.3874 0.4041 0.5085 -0.0779 0.0271  -0.0422 280 GLN A C   
2220 O O   A GLN A 271 ? 0.3892 0.4202 0.5210 -0.0847 0.0208  -0.0503 280 GLN A O   
2221 O O   B GLN A 271 ? 0.3931 0.4239 0.5252 -0.0847 0.0212  -0.0501 280 GLN A O   
2222 C CB  A GLN A 271 ? 0.4025 0.4199 0.5514 -0.0921 0.0443  -0.0437 280 GLN A CB  
2223 C CB  B GLN A 271 ? 0.4145 0.4289 0.5619 -0.0918 0.0455  -0.0429 280 GLN A CB  
2224 C CG  A GLN A 271 ? 0.4174 0.4246 0.5734 -0.0963 0.0587  -0.0383 280 GLN A CG  
2225 C CG  B GLN A 271 ? 0.4494 0.4523 0.6024 -0.0953 0.0602  -0.0366 280 GLN A CG  
2226 C CD  A GLN A 271 ? 0.4362 0.4551 0.6172 -0.1093 0.0627  -0.0457 280 GLN A CD  
2227 C CD  B GLN A 271 ? 0.5013 0.4781 0.6432 -0.0947 0.0682  -0.0312 280 GLN A CD  
2228 O OE1 A GLN A 271 ? 0.4611 0.4993 0.6540 -0.1151 0.0534  -0.0550 280 GLN A OE1 
2229 O OE1 B GLN A 271 ? 0.5275 0.4937 0.6681 -0.0942 0.0796  -0.0219 280 GLN A OE1 
2230 N NE2 A GLN A 271 ? 0.4410 0.4504 0.6303 -0.1145 0.0765  -0.0409 280 GLN A NE2 
2231 N NE2 B GLN A 271 ? 0.5571 0.5243 0.6918 -0.0942 0.0629  -0.0360 280 GLN A NE2 
2232 N N   . GLN A 272 ? 0.3701 0.3807 0.4746 -0.0690 0.0228  -0.0376 281 GLN A N   
2233 C CA  . GLN A 272 ? 0.3800 0.3983 0.4780 -0.0659 0.0117  -0.0402 281 GLN A CA  
2234 C C   . GLN A 272 ? 0.3736 0.3861 0.4673 -0.0709 0.0094  -0.0470 281 GLN A C   
2235 O O   . GLN A 272 ? 0.3741 0.3987 0.4669 -0.0723 0.0008  -0.0518 281 GLN A O   
2236 C CB  . GLN A 272 ? 0.3700 0.3812 0.4520 -0.0565 0.0094  -0.0338 281 GLN A CB  
2237 C CG  . GLN A 272 ? 0.4353 0.4516 0.5192 -0.0511 0.0111  -0.0295 281 GLN A CG  
2238 C CD  . GLN A 272 ? 0.3396 0.3734 0.4354 -0.0490 0.0047  -0.0300 281 GLN A CD  
2239 O OE1 . GLN A 272 ? 0.3810 0.4274 0.4837 -0.0522 -0.0025 -0.0331 281 GLN A OE1 
2240 N NE2 . GLN A 272 ? 0.3765 0.4120 0.4751 -0.0434 0.0078  -0.0269 281 GLN A NE2 
2241 N N   . THR A 273 ? 0.3787 0.3725 0.4696 -0.0729 0.0179  -0.0468 282 THR A N   
2242 C CA  . THR A 273 ? 0.3815 0.3652 0.4696 -0.0770 0.0191  -0.0541 282 THR A CA  
2243 C C   . THR A 273 ? 0.4036 0.3885 0.5066 -0.0895 0.0235  -0.0649 282 THR A C   
2244 O O   . THR A 273 ? 0.4232 0.3991 0.5253 -0.0946 0.0259  -0.0739 282 THR A O   
2245 C CB  . THR A 273 ? 0.3732 0.3349 0.4523 -0.0709 0.0268  -0.0467 282 THR A CB  
2246 O OG1 . THR A 273 ? 0.3941 0.3465 0.4789 -0.0715 0.0367  -0.0394 282 THR A OG1 
2247 C CG2 . THR A 273 ? 0.3836 0.3470 0.4480 -0.0606 0.0210  -0.0386 282 THR A CG2 
2248 N N   . ALA A 274 ? 0.3920 0.3883 0.5096 -0.0951 0.0253  -0.0652 283 ALA A N   
2249 C CA  . ALA A 274 ? 0.4015 0.4018 0.5359 -0.1088 0.0292  -0.0761 283 ALA A CA  
2250 C C   . ALA A 274 ? 0.3852 0.4117 0.5245 -0.1161 0.0173  -0.0873 283 ALA A C   
2251 O O   . ALA A 274 ? 0.3454 0.3915 0.4814 -0.1099 0.0069  -0.0828 283 ALA A O   
2252 C CB  . ALA A 274 ? 0.4431 0.4467 0.5929 -0.1121 0.0369  -0.0709 283 ALA A CB  
2253 N N   . GLY A 275 ? 0.3601 0.3870 0.5072 -0.1295 0.0193  -0.1017 284 GLY A N   
2254 C CA  . GLY A 275 ? 0.3885 0.4452 0.5448 -0.1404 0.0090  -0.1133 284 GLY A CA  
2255 C C   . GLY A 275 ? 0.3877 0.4521 0.5320 -0.1461 0.0015  -0.1265 284 GLY A C   
2256 O O   . GLY A 275 ? 0.4322 0.5223 0.5840 -0.1578 -0.0063 -0.1379 284 GLY A O   
2257 N N   . GLY A 276 ? 0.3746 0.4200 0.5004 -0.1383 0.0035  -0.1253 285 GLY A N   
2258 C CA  . GLY A 276 ? 0.4191 0.4702 0.5316 -0.1434 -0.0014 -0.1385 285 GLY A CA  
2259 C C   . GLY A 276 ? 0.4092 0.4867 0.5085 -0.1371 -0.0162 -0.1335 285 GLY A C   
2260 O O   . GLY A 276 ? 0.4141 0.4998 0.5005 -0.1417 -0.0205 -0.1439 285 GLY A O   
2261 N N   . GLY A 277 ? 0.3908 0.4805 0.4931 -0.1266 -0.0226 -0.1175 286 GLY A N   
2262 C CA  . GLY A 277 ? 0.3757 0.4888 0.4684 -0.1196 -0.0353 -0.1097 286 GLY A CA  
2263 C C   . GLY A 277 ? 0.3595 0.4576 0.4333 -0.1079 -0.0347 -0.1019 286 GLY A C   
2264 O O   . GLY A 277 ? 0.3355 0.4060 0.4040 -0.1034 -0.0250 -0.1007 286 GLY A O   
2265 N N   . HIS A 278 ? 0.3822 0.5006 0.4475 -0.1027 -0.0452 -0.0948 287 HIS A N   
2266 C CA  . HIS A 278 ? 0.3826 0.4923 0.4309 -0.0930 -0.0459 -0.0872 287 HIS A CA  
2267 C C   . HIS A 278 ? 0.3563 0.4445 0.4054 -0.0813 -0.0401 -0.0745 287 HIS A C   
2268 O O   . HIS A 278 ? 0.3122 0.3813 0.3509 -0.0768 -0.0345 -0.0738 287 HIS A O   
2269 C CB  . HIS A 278 ? 0.4192 0.5571 0.4615 -0.0899 -0.0581 -0.0793 287 HIS A CB  
2270 C CG  . HIS A 278 ? 0.4480 0.5801 0.4725 -0.0828 -0.0585 -0.0733 287 HIS A CG  
2271 N ND1 . HIS A 278 ? 0.6087 0.7277 0.6320 -0.0713 -0.0566 -0.0594 287 HIS A ND1 
2272 C CD2 . HIS A 278 ? 0.5860 0.7243 0.5935 -0.0864 -0.0599 -0.0799 287 HIS A CD2 
2273 C CE1 . HIS A 278 ? 0.5350 0.6526 0.5430 -0.0682 -0.0569 -0.0569 287 HIS A CE1 
2274 N NE2 . HIS A 278 ? 0.6010 0.7303 0.5988 -0.0767 -0.0586 -0.0687 287 HIS A NE2 
2275 N N   . ALA A 279 ? 0.3301 0.4234 0.3917 -0.0767 -0.0414 -0.0652 288 ALA A N   
2276 C CA  . ALA A 279 ? 0.3093 0.3857 0.3707 -0.0669 -0.0366 -0.0546 288 ALA A CA  
2277 C C   . ALA A 279 ? 0.3138 0.3661 0.3753 -0.0681 -0.0258 -0.0579 288 ALA A C   
2278 O O   . ALA A 279 ? 0.2506 0.2866 0.3034 -0.0617 -0.0218 -0.0527 288 ALA A O   
2279 C CB  . ALA A 279 ? 0.3111 0.3992 0.3867 -0.0623 -0.0389 -0.0460 288 ALA A CB  
2280 N N   . ALA A 280 ? 0.2978 0.3497 0.3702 -0.0765 -0.0213 -0.0656 289 ALA A N   
2281 C CA  . ALA A 280 ? 0.3169 0.3460 0.3909 -0.0784 -0.0101 -0.0677 289 ALA A CA  
2282 C C   . ALA A 280 ? 0.3290 0.3413 0.3912 -0.0772 -0.0059 -0.0716 289 ALA A C   
2283 O O   . ALA A 280 ? 0.3479 0.3418 0.4065 -0.0714 0.0010  -0.0654 289 ALA A O   
2284 C CB  . ALA A 280 ? 0.3249 0.3575 0.4143 -0.0899 -0.0058 -0.0768 289 ALA A CB  
2285 N N   . GLN A 281 ? 0.3516 0.3723 0.4081 -0.0825 -0.0098 -0.0815 290 GLN A N   
2286 C CA  . GLN A 281 ? 0.3671 0.3741 0.4135 -0.0816 -0.0049 -0.0873 290 GLN A CA  
2287 C C   . GLN A 281 ? 0.3452 0.3461 0.3811 -0.0700 -0.0059 -0.0758 290 GLN A C   
2288 O O   . GLN A 281 ? 0.3287 0.3121 0.3622 -0.0652 0.0015  -0.0735 290 GLN A O   
2289 C CB  . GLN A 281 ? 0.3835 0.4060 0.4231 -0.0897 -0.0100 -0.1004 290 GLN A CB  
2290 C CG  . GLN A 281 ? 0.4340 0.4416 0.4653 -0.0909 -0.0020 -0.1105 290 GLN A CG  
2291 C CD  . GLN A 281 ? 0.5177 0.5408 0.5410 -0.1015 -0.0054 -0.1270 290 GLN A CD  
2292 O OE1 . GLN A 281 ? 0.6162 0.6581 0.6443 -0.1117 -0.0117 -0.1348 290 GLN A OE1 
2293 N NE2 . GLN A 281 ? 0.6905 0.7075 0.7018 -0.0994 -0.0010 -0.1329 290 GLN A NE2 
2294 N N   . PHE A 282 ? 0.3160 0.3320 0.3478 -0.0655 -0.0148 -0.0680 291 PHE A N   
2295 C CA  . PHE A 282 ? 0.3215 0.3340 0.3446 -0.0564 -0.0165 -0.0581 291 PHE A CA  
2296 C C   . PHE A 282 ? 0.3121 0.3099 0.3378 -0.0505 -0.0112 -0.0496 291 PHE A C   
2297 O O   . PHE A 282 ? 0.3236 0.3116 0.3443 -0.0455 -0.0077 -0.0458 291 PHE A O   
2298 C CB  . PHE A 282 ? 0.3197 0.3495 0.3408 -0.0537 -0.0257 -0.0513 291 PHE A CB  
2299 C CG  . PHE A 282 ? 0.3226 0.3481 0.3370 -0.0459 -0.0267 -0.0417 291 PHE A CG  
2300 C CD1 . PHE A 282 ? 0.3353 0.3607 0.3401 -0.0442 -0.0265 -0.0420 291 PHE A CD1 
2301 C CD2 . PHE A 282 ? 0.2911 0.3131 0.3094 -0.0413 -0.0270 -0.0336 291 PHE A CD2 
2302 C CE1 . PHE A 282 ? 0.3460 0.3687 0.3467 -0.0385 -0.0272 -0.0336 291 PHE A CE1 
2303 C CE2 . PHE A 282 ? 0.3259 0.3442 0.3390 -0.0362 -0.0277 -0.0268 291 PHE A CE2 
2304 C CZ  . PHE A 282 ? 0.3080 0.3271 0.3130 -0.0351 -0.0281 -0.0264 291 PHE A CZ  
2305 N N   . LEU A 283 ? 0.3008 0.2997 0.3344 -0.0514 -0.0106 -0.0465 292 LEU A N   
2306 C CA  . LEU A 283 ? 0.2936 0.2816 0.3274 -0.0468 -0.0056 -0.0386 292 LEU A CA  
2307 C C   . LEU A 283 ? 0.2799 0.2516 0.3151 -0.0468 0.0033  -0.0384 292 LEU A C   
2308 O O   . LEU A 283 ? 0.2615 0.2257 0.2922 -0.0410 0.0061  -0.0304 292 LEU A O   
2309 C CB  . LEU A 283 ? 0.2965 0.2905 0.3383 -0.0480 -0.0056 -0.0363 292 LEU A CB  
2310 C CG  . LEU A 283 ? 0.2628 0.2694 0.3050 -0.0447 -0.0124 -0.0328 292 LEU A CG  
2311 C CD1 . LEU A 283 ? 0.2789 0.2920 0.3327 -0.0458 -0.0104 -0.0319 292 LEU A CD1 
2312 C CD2 . LEU A 283 ? 0.2393 0.2407 0.2721 -0.0386 -0.0135 -0.0267 292 LEU A CD2 
2313 N N   . GLN A 284 ? 0.3041 0.2711 0.3463 -0.0534 0.0080  -0.0470 293 GLN A N   
2314 C CA  . GLN A 284 ? 0.3353 0.2839 0.3808 -0.0528 0.0180  -0.0469 293 GLN A CA  
2315 C C   . GLN A 284 ? 0.3163 0.2597 0.3550 -0.0466 0.0189  -0.0458 293 GLN A C   
2316 O O   . GLN A 284 ? 0.3361 0.2690 0.3748 -0.0398 0.0240  -0.0368 293 GLN A O   
2317 C CB  . GLN A 284 ? 0.3575 0.3008 0.4134 -0.0628 0.0239  -0.0588 293 GLN A CB  
2318 C CG  . GLN A 284 ? 0.4224 0.3427 0.4855 -0.0623 0.0369  -0.0576 293 GLN A CG  
2319 C CD  . GLN A 284 ? 0.4842 0.3954 0.5507 -0.0578 0.0430  -0.0433 293 GLN A CD  
2320 O OE1 . GLN A 284 ? 0.4860 0.4058 0.5547 -0.0604 0.0409  -0.0401 293 GLN A OE1 
2321 N NE2 . GLN A 284 ? 0.5328 0.4278 0.6003 -0.0505 0.0512  -0.0341 293 GLN A NE2 
2322 N N   . ASP A 285 ? 0.3428 0.2954 0.3761 -0.0487 0.0139  -0.0539 294 ASP A N   
2323 C CA  . ASP A 285 ? 0.3258 0.2764 0.3529 -0.0429 0.0150  -0.0532 294 ASP A CA  
2324 C C   . ASP A 285 ? 0.3089 0.2625 0.3314 -0.0340 0.0115  -0.0398 294 ASP A C   
2325 O O   . ASP A 285 ? 0.2727 0.2195 0.2962 -0.0275 0.0160  -0.0343 294 ASP A O   
2326 C CB  . ASP A 285 ? 0.3500 0.3143 0.3694 -0.0469 0.0092  -0.0624 294 ASP A CB  
2327 C CG  . ASP A 285 ? 0.4438 0.4050 0.4583 -0.0426 0.0134  -0.0648 294 ASP A CG  
2328 O OD1 . ASP A 285 ? 0.4619 0.4077 0.4825 -0.0402 0.0236  -0.0674 294 ASP A OD1 
2329 O OD2 . ASP A 285 ? 0.4661 0.4405 0.4720 -0.0413 0.0076  -0.0638 294 ASP A OD2 
2330 N N   . MET A 286 ? 0.3087 0.2726 0.3277 -0.0341 0.0039  -0.0349 295 MET A N   
2331 C CA  . MET A 286 ? 0.3020 0.2699 0.3163 -0.0281 0.0002  -0.0247 295 MET A CA  
2332 C C   . MET A 286 ? 0.2998 0.2595 0.3158 -0.0233 0.0052  -0.0156 295 MET A C   
2333 O O   . MET A 286 ? 0.3294 0.2933 0.3419 -0.0182 0.0030  -0.0081 295 MET A O   
2334 C CB  . MET A 286 ? 0.3095 0.2870 0.3212 -0.0298 -0.0065 -0.0231 295 MET A CB  
2335 C CG  . MET A 286 ? 0.3217 0.3101 0.3302 -0.0313 -0.0129 -0.0260 295 MET A CG  
2336 S SD  . MET A 286 ? 0.3155 0.3070 0.3184 -0.0282 -0.0133 -0.0254 295 MET A SD  
2337 C CE  . MET A 286 ? 0.3185 0.3087 0.3216 -0.0325 -0.0092 -0.0366 295 MET A CE  
2338 N N   . ARG A 287 ? 0.3069 0.2563 0.3290 -0.0252 0.0120  -0.0156 296 ARG A N   
2339 C CA  . ARG A 287 ? 0.3179 0.2591 0.3419 -0.0198 0.0179  -0.0047 296 ARG A CA  
2340 C C   . ARG A 287 ? 0.3354 0.2715 0.3630 -0.0126 0.0222  0.0002  296 ARG A C   
2341 O O   . ARG A 287 ? 0.3337 0.2710 0.3610 -0.0060 0.0231  0.0124  296 ARG A O   
2342 C CB  . ARG A 287 ? 0.3224 0.2522 0.3538 -0.0238 0.0260  -0.0048 296 ARG A CB  
2343 C CG  . ARG A 287 ? 0.3066 0.2433 0.3366 -0.0296 0.0231  -0.0076 296 ARG A CG  
2344 C CD  . ARG A 287 ? 0.3450 0.2714 0.3838 -0.0339 0.0320  -0.0069 296 ARG A CD  
2345 N NE  . ARG A 287 ? 0.3923 0.3274 0.4323 -0.0391 0.0301  -0.0097 296 ARG A NE  
2346 C CZ  . ARG A 287 ? 0.4255 0.3563 0.4715 -0.0428 0.0374  -0.0068 296 ARG A CZ  
2347 N NH1 . ARG A 287 ? 0.4639 0.3801 0.5151 -0.0421 0.0473  0.0000  296 ARG A NH1 
2348 N NH2 . ARG A 287 ? 0.3981 0.3392 0.4466 -0.0467 0.0356  -0.0098 296 ARG A NH2 
2349 N N   . ARG A 288 ? 0.3381 0.2711 0.3690 -0.0137 0.0245  -0.0092 297 ARG A N   
2350 C CA  . ARG A 288 ? 0.3876 0.3172 0.4234 -0.0062 0.0294  -0.0059 297 ARG A CA  
2351 C C   . ARG A 288 ? 0.3522 0.2978 0.3829 -0.0010 0.0217  0.0011  297 ARG A C   
2352 O O   . ARG A 288 ? 0.3581 0.3051 0.3948 0.0068  0.0249  0.0078  297 ARG A O   
2353 C CB  . ARG A 288 ? 0.4120 0.3349 0.4508 -0.0099 0.0349  -0.0204 297 ARG A CB  
2354 C CG  . ARG A 288 ? 0.4871 0.3928 0.5336 -0.0159 0.0443  -0.0292 297 ARG A CG  
2355 C CD  . ARG A 288 ? 0.5976 0.4996 0.6441 -0.0217 0.0489  -0.0469 297 ARG A CD  
2356 N NE  . ARG A 288 ? 0.7500 0.6511 0.7983 -0.0140 0.0540  -0.0468 297 ARG A NE  
2357 C CZ  . ARG A 288 ? 0.7360 0.6513 0.7759 -0.0136 0.0490  -0.0510 297 ARG A CZ  
2358 N NH1 . ARG A 288 ? 0.7258 0.6574 0.7540 -0.0200 0.0382  -0.0551 297 ARG A NH1 
2359 N NH2 . ARG A 288 ? 0.7901 0.7035 0.8348 -0.0059 0.0560  -0.0500 297 ARG A NH2 
2360 N N   . TYR A 289 ? 0.3315 0.2892 0.3534 -0.0054 0.0124  -0.0006 298 TYR A N   
2361 C CA  . TYR A 289 ? 0.3104 0.2830 0.3278 -0.0033 0.0049  0.0042  298 TYR A CA  
2362 C C   . TYR A 289 ? 0.3263 0.3059 0.3400 -0.0015 0.0006  0.0146  298 TYR A C   
2363 O O   . TYR A 289 ? 0.3315 0.3243 0.3423 -0.0008 -0.0055 0.0184  298 TYR A O   
2364 C CB  . TYR A 289 ? 0.2886 0.2682 0.2996 -0.0096 -0.0013 -0.0039 298 TYR A CB  
2365 C CG  . TYR A 289 ? 0.3043 0.2825 0.3158 -0.0115 0.0018  -0.0131 298 TYR A CG  
2366 C CD1 . TYR A 289 ? 0.2894 0.2579 0.3029 -0.0153 0.0070  -0.0221 298 TYR A CD1 
2367 C CD2 . TYR A 289 ? 0.3062 0.2939 0.3158 -0.0104 0.0001  -0.0135 298 TYR A CD2 
2368 C CE1 . TYR A 289 ? 0.2918 0.2609 0.3033 -0.0182 0.0099  -0.0324 298 TYR A CE1 
2369 C CE2 . TYR A 289 ? 0.2869 0.2749 0.2944 -0.0123 0.0037  -0.0223 298 TYR A CE2 
2370 C CZ  . TYR A 289 ? 0.2851 0.2643 0.2924 -0.0164 0.0082  -0.0322 298 TYR A CZ  
2371 O OH  . TYR A 289 ? 0.3168 0.2982 0.3196 -0.0195 0.0117  -0.0426 298 TYR A OH  
2372 N N   . MET A 290 ? 0.3274 0.2993 0.3411 -0.0015 0.0043  0.0187  299 MET A N   
2373 C CA  . MET A 290 ? 0.3172 0.2962 0.3252 0.0003  0.0017  0.0289  299 MET A CA  
2374 C C   . MET A 290 ? 0.3575 0.3386 0.3715 0.0091  0.0050  0.0425  299 MET A C   
2375 O O   . MET A 290 ? 0.3533 0.3227 0.3777 0.0137  0.0129  0.0439  299 MET A O   
2376 C CB  . MET A 290 ? 0.2981 0.2688 0.3031 -0.0035 0.0055  0.0286  299 MET A CB  
2377 C CG  . MET A 290 ? 0.2830 0.2535 0.2845 -0.0109 0.0027  0.0174  299 MET A CG  
2378 S SD  . MET A 290 ? 0.3077 0.2696 0.3100 -0.0149 0.0093  0.0175  299 MET A SD  
2379 C CE  . MET A 290 ? 0.2433 0.2090 0.2464 -0.0215 0.0050  0.0048  299 MET A CE  
2380 N N   . PRO A 291 ? 0.3467 0.3433 0.3548 0.0115  -0.0007 0.0527  300 PRO A N   
2381 C CA  . PRO A 291 ? 0.3727 0.3738 0.3873 0.0209  0.0021  0.0690  300 PRO A CA  
2382 C C   . PRO A 291 ? 0.3920 0.3753 0.4111 0.0240  0.0123  0.0760  300 PRO A C   
2383 O O   . PRO A 291 ? 0.4178 0.3939 0.4295 0.0179  0.0142  0.0719  300 PRO A O   
2384 C CB  . PRO A 291 ? 0.3627 0.3857 0.3657 0.0196  -0.0070 0.0765  300 PRO A CB  
2385 C CG  . PRO A 291 ? 0.3647 0.3952 0.3606 0.0108  -0.0145 0.0626  300 PRO A CG  
2386 C CD  . PRO A 291 ? 0.3441 0.3557 0.3402 0.0056  -0.0096 0.0498  300 PRO A CD  
2387 N N   . PRO A 292 ? 0.4169 0.3923 0.4498 0.0336  0.0202  0.0866  301 PRO A N   
2388 C CA  . PRO A 292 ? 0.4260 0.3796 0.4670 0.0361  0.0324  0.0921  301 PRO A CA  
2389 C C   . PRO A 292 ? 0.4412 0.3963 0.4724 0.0346  0.0333  0.1036  301 PRO A C   
2390 O O   . PRO A 292 ? 0.4433 0.3809 0.4766 0.0301  0.0417  0.1006  301 PRO A O   
2391 C CB  . PRO A 292 ? 0.4311 0.3807 0.4893 0.0489  0.0396  0.1052  301 PRO A CB  
2392 C CG  . PRO A 292 ? 0.4202 0.3971 0.4766 0.0538  0.0287  0.1121  301 PRO A CG  
2393 C CD  . PRO A 292 ? 0.4278 0.4143 0.4721 0.0431  0.0192  0.0946  301 PRO A CD  
2394 N N   . ALA A 293 ? 0.4415 0.4190 0.4620 0.0374  0.0249  0.1158  302 ALA A N   
2395 C CA  . ALA A 293 ? 0.4333 0.4165 0.4405 0.0355  0.0251  0.1262  302 ALA A CA  
2396 C C   . ALA A 293 ? 0.4097 0.3881 0.4052 0.0234  0.0246  0.1101  302 ALA A C   
2397 O O   . ALA A 293 ? 0.3945 0.3658 0.3855 0.0207  0.0311  0.1145  302 ALA A O   
2398 C CB  . ALA A 293 ? 0.4593 0.4721 0.4548 0.0390  0.0144  0.1390  302 ALA A CB  
2399 N N   . HIS A 294 ? 0.3964 0.3786 0.3892 0.0169  0.0178  0.0926  303 HIS A N   
2400 C CA  . HIS A 294 ? 0.3842 0.3635 0.3690 0.0070  0.0169  0.0777  303 HIS A CA  
2401 C C   . HIS A 294 ? 0.3940 0.3528 0.3905 0.0030  0.0253  0.0682  303 HIS A C   
2402 O O   . HIS A 294 ? 0.3943 0.3481 0.3884 -0.0029 0.0293  0.0636  303 HIS A O   
2403 C CB  . HIS A 294 ? 0.3667 0.3581 0.3458 0.0025  0.0068  0.0651  303 HIS A CB  
2404 C CG  . HIS A 294 ? 0.3674 0.3806 0.3357 0.0037  -0.0019 0.0715  303 HIS A CG  
2405 N ND1 . HIS A 294 ? 0.3490 0.3739 0.3146 0.0001  -0.0105 0.0627  303 HIS A ND1 
2406 C CD2 . HIS A 294 ? 0.3501 0.3770 0.3096 0.0073  -0.0034 0.0860  303 HIS A CD2 
2407 C CE1 . HIS A 294 ? 0.3857 0.4310 0.3422 0.0004  -0.0172 0.0698  303 HIS A CE1 
2408 N NE2 . HIS A 294 ? 0.4320 0.4802 0.3837 0.0050  -0.0136 0.0842  303 HIS A NE2 
2409 N N   . ARG A 295 ? 0.4270 0.3759 0.4362 0.0057  0.0279  0.0642  304 ARG A N   
2410 C CA  . ARG A 295 ? 0.4302 0.3593 0.4523 0.0025  0.0372  0.0565  304 ARG A CA  
2411 C C   . ARG A 295 ? 0.4442 0.3606 0.4708 0.0028  0.0480  0.0671  304 ARG A C   
2412 O O   . ARG A 295 ? 0.4479 0.3556 0.4785 -0.0048 0.0534  0.0597  304 ARG A O   
2413 C CB  . ARG A 295 ? 0.4592 0.3805 0.4929 0.0083  0.0404  0.0554  304 ARG A CB  
2414 C CG  . ARG A 295 ? 0.5124 0.4204 0.5550 0.0024  0.0451  0.0388  304 ARG A CG  
2415 C CD  . ARG A 295 ? 0.5029 0.4148 0.5484 0.0065  0.0425  0.0333  304 ARG A CD  
2416 N NE  . ARG A 295 ? 0.5974 0.5020 0.6539 0.0170  0.0501  0.0442  304 ARG A NE  
2417 C CZ  . ARG A 295 ? 0.5371 0.4521 0.5961 0.0247  0.0471  0.0488  304 ARG A CZ  
2418 N NH1 . ARG A 295 ? 0.4951 0.4283 0.5453 0.0225  0.0363  0.0437  304 ARG A NH1 
2419 N NH2 . ARG A 295 ? 0.6368 0.5442 0.7093 0.0353  0.0557  0.0598  304 ARG A NH2 
2420 N N   . ASN A 296 ? 0.4350 0.3524 0.4622 0.0118  0.0512  0.0858  305 ASN A N   
2421 C CA  . ASN A 296 ? 0.4537 0.3593 0.4851 0.0139  0.0623  0.1005  305 ASN A CA  
2422 C C   . ASN A 296 ? 0.4279 0.3416 0.4462 0.0075  0.0620  0.1020  305 ASN A C   
2423 O O   . ASN A 296 ? 0.4148 0.3157 0.4390 0.0034  0.0723  0.1047  305 ASN A O   
2424 C CB  . ASN A 296 ? 0.4712 0.3815 0.5046 0.0266  0.0639  0.1234  305 ASN A CB  
2425 C CG  . ASN A 296 ? 0.4867 0.3856 0.5376 0.0346  0.0684  0.1240  305 ASN A CG  
2426 O OD1 . ASN A 296 ? 0.4156 0.2987 0.4770 0.0299  0.0733  0.1075  305 ASN A OD1 
2427 N ND2 . ASN A 296 ? 0.4859 0.3946 0.5401 0.0469  0.0672  0.1432  305 ASN A ND2 
2428 N N   . PHE A 297 ? 0.4089 0.3435 0.4105 0.0062  0.0512  0.0997  306 PHE A N   
2429 C CA  . PHE A 297 ? 0.4242 0.3676 0.4121 0.0002  0.0513  0.0985  306 PHE A CA  
2430 C C   . PHE A 297 ? 0.4082 0.3430 0.4034 -0.0094 0.0549  0.0814  306 PHE A C   
2431 O O   . PHE A 297 ? 0.3990 0.3315 0.3931 -0.0139 0.0623  0.0833  306 PHE A O   
2432 C CB  . PHE A 297 ? 0.4161 0.3822 0.3856 -0.0002 0.0396  0.0960  306 PHE A CB  
2433 C CG  . PHE A 297 ? 0.4044 0.3795 0.3586 -0.0060 0.0411  0.0937  306 PHE A CG  
2434 C CD1 . PHE A 297 ? 0.4703 0.4498 0.4144 -0.0041 0.0475  0.1098  306 PHE A CD1 
2435 C CD2 . PHE A 297 ? 0.3827 0.3616 0.3332 -0.0130 0.0375  0.0760  306 PHE A CD2 
2436 C CE1 . PHE A 297 ? 0.4632 0.4514 0.3923 -0.0097 0.0505  0.1067  306 PHE A CE1 
2437 C CE2 . PHE A 297 ? 0.4123 0.3984 0.3502 -0.0178 0.0409  0.0727  306 PHE A CE2 
2438 C CZ  . PHE A 297 ? 0.4133 0.4045 0.3396 -0.0166 0.0475  0.0870  306 PHE A CZ  
2439 N N   . LEU A 298 ? 0.3828 0.3152 0.3858 -0.0124 0.0496  0.0658  307 LEU A N   
2440 C CA  . LEU A 298 ? 0.3786 0.3061 0.3909 -0.0209 0.0517  0.0507  307 LEU A CA  
2441 C C   . LEU A 298 ? 0.3680 0.2782 0.3960 -0.0247 0.0636  0.0518  307 LEU A C   
2442 O O   . LEU A 298 ? 0.3551 0.2644 0.3884 -0.0316 0.0691  0.0478  307 LEU A O   
2443 C CB  . LEU A 298 ? 0.3914 0.3217 0.4076 -0.0227 0.0433  0.0362  307 LEU A CB  
2444 C CG  . LEU A 298 ? 0.4316 0.3769 0.4370 -0.0233 0.0333  0.0296  307 LEU A CG  
2445 C CD1 . LEU A 298 ? 0.4484 0.3954 0.4579 -0.0234 0.0262  0.0198  307 LEU A CD1 
2446 C CD2 . LEU A 298 ? 0.4861 0.4362 0.4921 -0.0291 0.0351  0.0229  307 LEU A CD2 
2447 N N   . CYS A 299 ? 0.4017 0.2983 0.4387 -0.0203 0.0684  0.0570  308 CYS A N   
2448 C CA  . CYS A 299 ? 0.4169 0.2933 0.4701 -0.0237 0.0816  0.0588  308 CYS A CA  
2449 C C   . CYS A 299 ? 0.4523 0.3255 0.5043 -0.0243 0.0914  0.0736  308 CYS A C   
2450 O O   . CYS A 299 ? 0.4298 0.2934 0.4937 -0.0325 0.1008  0.0698  308 CYS A O   
2451 C CB  . CYS A 299 ? 0.4255 0.2875 0.4871 -0.0158 0.0862  0.0652  308 CYS A CB  
2452 S SG  . CYS A 299 ? 0.4957 0.3287 0.5784 -0.0187 0.1048  0.0693  308 CYS A SG  
2453 N N   . SER A 300 ? 0.4816 0.3645 0.5191 -0.0162 0.0893  0.0906  309 SER A N   
2454 C CA  . SER A 300 ? 0.5002 0.3844 0.5313 -0.0158 0.0976  0.1068  309 SER A CA  
2455 C C   . SER A 300 ? 0.4732 0.3662 0.5008 -0.0253 0.0990  0.0969  309 SER A C   
2456 O O   . SER A 300 ? 0.4688 0.3540 0.5037 -0.0303 0.1109  0.1023  309 SER A O   
2457 C CB  . SER A 300 ? 0.5313 0.4319 0.5431 -0.0063 0.0913  0.1240  309 SER A CB  
2458 O OG  . SER A 300 ? 0.7066 0.6090 0.7105 -0.0054 0.1002  0.1420  309 SER A OG  
2459 N N   . LEU A 301 ? 0.4398 0.3486 0.4580 -0.0275 0.0878  0.0831  310 LEU A N   
2460 C CA  . LEU A 301 ? 0.4593 0.3774 0.4768 -0.0351 0.0891  0.0728  310 LEU A CA  
2461 C C   . LEU A 301 ? 0.4491 0.3579 0.4886 -0.0441 0.0955  0.0617  310 LEU A C   
2462 O O   . LEU A 301 ? 0.4297 0.3412 0.4749 -0.0501 0.1035  0.0613  310 LEU A O   
2463 C CB  . LEU A 301 ? 0.4135 0.3473 0.4207 -0.0349 0.0768  0.0599  310 LEU A CB  
2464 C CG  . LEU A 301 ? 0.4399 0.3871 0.4250 -0.0292 0.0692  0.0656  310 LEU A CG  
2465 C CD1 . LEU A 301 ? 0.4178 0.3766 0.3968 -0.0317 0.0615  0.0508  310 LEU A CD1 
2466 C CD2 . LEU A 301 ? 0.4716 0.4242 0.4418 -0.0274 0.0765  0.0811  310 LEU A CD2 
2467 N N   . GLU A 302 ? 0.4726 0.3725 0.5244 -0.0456 0.0921  0.0521  311 GLU A N   
2468 C CA  . GLU A 302 ? 0.4984 0.3920 0.5707 -0.0558 0.0967  0.0393  311 GLU A CA  
2469 C C   . GLU A 302 ? 0.4923 0.3688 0.5786 -0.0605 0.1122  0.0478  311 GLU A C   
2470 O O   . GLU A 302 ? 0.4953 0.3714 0.5977 -0.0709 0.1179  0.0393  311 GLU A O   
2471 C CB  . GLU A 302 ? 0.4901 0.3797 0.5688 -0.0569 0.0892  0.0259  311 GLU A CB  
2472 C CG  . GLU A 302 ? 0.5271 0.4346 0.5978 -0.0558 0.0754  0.0153  311 GLU A CG  
2473 C CD  . GLU A 302 ? 0.5098 0.4162 0.5846 -0.0573 0.0683  0.0028  311 GLU A CD  
2474 O OE1 . GLU A 302 ? 0.5000 0.4208 0.5749 -0.0600 0.0590  -0.0078 311 GLU A OE1 
2475 O OE2 . GLU A 302 ? 0.6136 0.5051 0.6913 -0.0550 0.0724  0.0042  311 GLU A OE2 
2476 N N   . SER A 303 ? 0.5104 0.3739 0.5918 -0.0530 0.1190  0.0653  312 SER A N   
2477 C CA  . SER A 303 ? 0.5705 0.4151 0.6650 -0.0560 0.1354  0.0771  312 SER A CA  
2478 C C   . SER A 303 ? 0.5745 0.4269 0.6641 -0.0586 0.1439  0.0887  312 SER A C   
2479 O O   . SER A 303 ? 0.5711 0.4106 0.6752 -0.0649 0.1582  0.0948  312 SER A O   
2480 C CB  . SER A 303 ? 0.6022 0.4307 0.6948 -0.0449 0.1401  0.0947  312 SER A CB  
2481 O OG  . SER A 303 ? 0.6789 0.4973 0.7796 -0.0431 0.1360  0.0833  312 SER A OG  
2482 N N   . ASN A 304 ? 0.5866 0.4596 0.6561 -0.0544 0.1364  0.0911  313 ASN A N   
2483 C CA  . ASN A 304 ? 0.6240 0.5072 0.6859 -0.0569 0.1448  0.1000  313 ASN A CA  
2484 C C   . ASN A 304 ? 0.5944 0.4851 0.6727 -0.0683 0.1481  0.0843  313 ASN A C   
2485 O O   . ASN A 304 ? 0.5662 0.4617 0.6549 -0.0725 0.1391  0.0664  313 ASN A O   
2486 C CB  . ASN A 304 ? 0.6263 0.5292 0.6605 -0.0496 0.1359  0.1042  313 ASN A CB  
2487 C CG  . ASN A 304 ? 0.7153 0.6169 0.7333 -0.0387 0.1315  0.1210  313 ASN A CG  
2488 O OD1 . ASN A 304 ? 0.7956 0.6842 0.8176 -0.0348 0.1406  0.1393  313 ASN A OD1 
2489 N ND2 . ASN A 304 ? 0.8462 0.7623 0.8475 -0.0335 0.1176  0.1155  313 ASN A ND2 
2490 N N   . PRO A 305 ? 0.6547 0.5490 0.7360 -0.0733 0.1609  0.0920  314 PRO A N   
2491 C CA  . PRO A 305 ? 0.6449 0.5502 0.7447 -0.0837 0.1642  0.0777  314 PRO A CA  
2492 C C   . PRO A 305 ? 0.6184 0.5452 0.7114 -0.0817 0.1519  0.0629  314 PRO A C   
2493 O O   . PRO A 305 ? 0.6101 0.5445 0.6802 -0.0734 0.1443  0.0651  314 PRO A O   
2494 C CB  . PRO A 305 ? 0.6931 0.5993 0.7934 -0.0874 0.1814  0.0920  314 PRO A CB  
2495 C CG  . PRO A 305 ? 0.7197 0.6230 0.7931 -0.0771 0.1833  0.1123  314 PRO A CG  
2496 C CD  . PRO A 305 ? 0.6908 0.5811 0.7603 -0.0698 0.1736  0.1147  314 PRO A CD  
2497 N N   . SER A 306 ? 0.5953 0.5321 0.7098 -0.0897 0.1501  0.0480  315 SER A N   
2498 C CA  . SER A 306 ? 0.5634 0.5191 0.6773 -0.0873 0.1390  0.0346  315 SER A CA  
2499 C C   . SER A 306 ? 0.5440 0.5140 0.6474 -0.0842 0.1455  0.0376  315 SER A C   
2500 O O   . SER A 306 ? 0.5559 0.5296 0.6683 -0.0894 0.1593  0.0427  315 SER A O   
2501 C CB  . SER A 306 ? 0.5606 0.5260 0.7025 -0.0964 0.1353  0.0201  315 SER A CB  
2502 O OG  . SER A 306 ? 0.5704 0.5549 0.7143 -0.0929 0.1254  0.0101  315 SER A OG  
2503 N N   . VAL A 307 ? 0.4970 0.4744 0.5818 -0.0763 0.1367  0.0337  316 VAL A N   
2504 C CA  . VAL A 307 ? 0.5105 0.5015 0.5861 -0.0735 0.1421  0.0316  316 VAL A CA  
2505 C C   . VAL A 307 ? 0.4868 0.4930 0.5891 -0.0773 0.1439  0.0203  316 VAL A C   
2506 O O   . VAL A 307 ? 0.4646 0.4806 0.5727 -0.0791 0.1563  0.0212  316 VAL A O   
2507 C CB  . VAL A 307 ? 0.4959 0.4892 0.5471 -0.0654 0.1319  0.0275  316 VAL A CB  
2508 C CG1 . VAL A 307 ? 0.5375 0.5430 0.5802 -0.0632 0.1391  0.0222  316 VAL A CG1 
2509 C CG2 . VAL A 307 ? 0.5338 0.5172 0.5599 -0.0614 0.1293  0.0395  316 VAL A CG2 
2510 N N   . ARG A 308 ? 0.4373 0.4473 0.5557 -0.0781 0.1317  0.0108  317 ARG A N   
2511 C CA  . ARG A 308 ? 0.4442 0.4721 0.5900 -0.0810 0.1308  0.0017  317 ARG A CA  
2512 C C   . ARG A 308 ? 0.4555 0.4901 0.6251 -0.0907 0.1436  0.0041  317 ARG A C   
2513 O O   . ARG A 308 ? 0.4293 0.4801 0.6144 -0.0912 0.1513  0.0017  317 ARG A O   
2514 C CB  . ARG A 308 ? 0.4108 0.4426 0.5682 -0.0816 0.1150  -0.0065 317 ARG A CB  
2515 C CG  . ARG A 308 ? 0.4103 0.4649 0.5971 -0.0841 0.1120  -0.0140 317 ARG A CG  
2516 C CD  . ARG A 308 ? 0.4115 0.4737 0.6031 -0.0814 0.0951  -0.0206 317 ARG A CD  
2517 N NE  . ARG A 308 ? 0.3872 0.4729 0.6007 -0.0778 0.0924  -0.0241 317 ARG A NE  
2518 C CZ  . ARG A 308 ? 0.4086 0.5161 0.6516 -0.0844 0.0909  -0.0273 317 ARG A CZ  
2519 N NH1 . ARG A 308 ? 0.5200 0.6280 0.7744 -0.0969 0.0920  -0.0299 317 ARG A NH1 
2520 N NH2 . ARG A 308 ? 0.4154 0.5453 0.6785 -0.0787 0.0885  -0.0281 317 ARG A NH2 
2521 N N   . GLU A 309 ? 0.4901 0.5115 0.6641 -0.0983 0.1468  0.0086  318 GLU A N   
2522 C CA  . GLU A 309 ? 0.5070 0.5319 0.7048 -0.1095 0.1597  0.0109  318 GLU A CA  
2523 C C   . GLU A 309 ? 0.5073 0.5320 0.6967 -0.1088 0.1775  0.0218  318 GLU A C   
2524 O O   . GLU A 309 ? 0.5050 0.5432 0.7163 -0.1153 0.1887  0.0214  318 GLU A O   
2525 C CB  . GLU A 309 ? 0.5468 0.5531 0.7510 -0.1180 0.1603  0.0125  318 GLU A CB  
2526 C CG  . GLU A 309 ? 0.6079 0.6188 0.8265 -0.1229 0.1458  -0.0009 318 GLU A CG  
2527 C CD  . GLU A 309 ? 0.5854 0.6210 0.8362 -0.1326 0.1442  -0.0113 318 GLU A CD  
2528 O OE1 . GLU A 309 ? 0.5723 0.6252 0.8295 -0.1304 0.1299  -0.0206 318 GLU A OE1 
2529 O OE2 . GLU A 309 ? 0.6008 0.6405 0.8716 -0.1426 0.1572  -0.0091 318 GLU A OE2 
2530 N N   . PHE A 310 ? 0.5059 0.5178 0.6640 -0.1014 0.1799  0.0317  319 PHE A N   
2531 C CA  . PHE A 310 ? 0.5223 0.5367 0.6655 -0.0997 0.1957  0.0420  319 PHE A CA  
2532 C C   . PHE A 310 ? 0.5015 0.5366 0.6504 -0.0965 0.1999  0.0333  319 PHE A C   
2533 O O   . PHE A 310 ? 0.5313 0.5768 0.6927 -0.1008 0.2151  0.0360  319 PHE A O   
2534 C CB  . PHE A 310 ? 0.5290 0.5314 0.6351 -0.0917 0.1936  0.0525  319 PHE A CB  
2535 C CG  . PHE A 310 ? 0.5696 0.5750 0.6568 -0.0910 0.2097  0.0649  319 PHE A CG  
2536 C CD1 . PHE A 310 ? 0.5791 0.5992 0.6522 -0.0869 0.2146  0.0591  319 PHE A CD1 
2537 C CD2 . PHE A 310 ? 0.5662 0.5593 0.6490 -0.0944 0.2210  0.0827  319 PHE A CD2 
2538 C CE1 . PHE A 310 ? 0.5891 0.6139 0.6418 -0.0870 0.2301  0.0697  319 PHE A CE1 
2539 C CE2 . PHE A 310 ? 0.6410 0.6390 0.7042 -0.0938 0.2361  0.0960  319 PHE A CE2 
2540 C CZ  . PHE A 310 ? 0.5984 0.6135 0.6452 -0.0905 0.2404  0.0889  319 PHE A CZ  
2541 N N   . VAL A 311 ? 0.4805 0.5209 0.6219 -0.0886 0.1877  0.0233  320 VAL A N   
2542 C CA  . VAL A 311 ? 0.4930 0.5505 0.6416 -0.0839 0.1923  0.0146  320 VAL A CA  
2543 C C   . VAL A 311 ? 0.4866 0.5625 0.6756 -0.0892 0.1947  0.0088  320 VAL A C   
2544 O O   . VAL A 311 ? 0.4833 0.5738 0.6854 -0.0893 0.2083  0.0077  320 VAL A O   
2545 C CB  . VAL A 311 ? 0.4596 0.5160 0.5935 -0.0745 0.1792  0.0057  320 VAL A CB  
2546 C CG1 . VAL A 311 ? 0.4965 0.5683 0.6434 -0.0691 0.1856  -0.0036 320 VAL A CG1 
2547 C CG2 . VAL A 311 ? 0.4431 0.4866 0.5380 -0.0704 0.1781  0.0105  320 VAL A CG2 
2548 N N   . LEU A 312 ? 0.4812 0.5584 0.6895 -0.0937 0.1818  0.0048  321 LEU A N   
2549 C CA  . LEU A 312 ? 0.5024 0.6009 0.7501 -0.1004 0.1816  -0.0006 321 LEU A CA  
2550 C C   . LEU A 312 ? 0.5177 0.6233 0.7845 -0.1105 0.1994  0.0048  321 LEU A C   
2551 O O   . LEU A 312 ? 0.5171 0.6460 0.8141 -0.1130 0.2051  0.0012  321 LEU A O   
2552 C CB  . LEU A 312 ? 0.5174 0.6150 0.7779 -0.1066 0.1656  -0.0058 321 LEU A CB  
2553 C CG  . LEU A 312 ? 0.5583 0.6681 0.8255 -0.1001 0.1478  -0.0138 321 LEU A CG  
2554 C CD1 . LEU A 312 ? 0.5764 0.6811 0.8470 -0.1073 0.1338  -0.0183 321 LEU A CD1 
2555 C CD2 . LEU A 312 ? 0.5866 0.7267 0.8869 -0.0987 0.1492  -0.0177 321 LEU A CD2 
2556 N N   . SER A 313 ? 0.5290 0.6152 0.7802 -0.1160 0.2083  0.0145  322 SER A N   
2557 C CA  . SER A 313 ? 0.5426 0.6316 0.8116 -0.1269 0.2260  0.0215  322 SER A CA  
2558 C C   . SER A 313 ? 0.5609 0.6608 0.8252 -0.1236 0.2449  0.0268  322 SER A C   
2559 O O   . SER A 313 ? 0.5763 0.6874 0.8642 -0.1323 0.2598  0.0301  322 SER A O   
2560 C CB  . SER A 313 ? 0.5670 0.6292 0.8209 -0.1326 0.2304  0.0325  322 SER A CB  
2561 O OG  . SER A 313 ? 0.5826 0.6299 0.7983 -0.1234 0.2336  0.0428  322 SER A OG  
2562 N N   . LYS A 314 ? 0.5404 0.6378 0.7753 -0.1120 0.2449  0.0262  323 LYS A N   
2563 C CA  . LYS A 314 ? 0.5508 0.6510 0.7674 -0.1095 0.2642  0.0329  323 LYS A CA  
2564 C C   . LYS A 314 ? 0.5278 0.6519 0.7641 -0.1064 0.2765  0.0256  323 LYS A C   
2565 O O   . LYS A 314 ? 0.5564 0.6856 0.7848 -0.1076 0.2960  0.0313  323 LYS A O   
2566 C CB  . LYS A 314 ? 0.5816 0.6666 0.7527 -0.1008 0.2602  0.0364  323 LYS A CB  
2567 C CG  . LYS A 314 ? 0.6251 0.6883 0.7756 -0.1037 0.2562  0.0497  323 LYS A CG  
2568 C CD  . LYS A 314 ? 0.6955 0.7547 0.8368 -0.1093 0.2756  0.0663  323 LYS A CD  
2569 C CE  . LYS A 314 ? 0.7003 0.7374 0.8352 -0.1129 0.2724  0.0806  323 LYS A CE  
2570 N NZ  . LYS A 314 ? 0.6982 0.7307 0.8706 -0.1231 0.2707  0.0774  323 LYS A NZ  
2571 N N   . GLY A 315 ? 0.4576 0.5971 0.7197 -0.1020 0.2663  0.0142  324 GLY A N   
2572 C CA  . GLY A 315 ? 0.4249 0.5885 0.7123 -0.0977 0.2782  0.0079  324 GLY A CA  
2573 C C   . GLY A 315 ? 0.4046 0.5647 0.6632 -0.0875 0.2890  0.0039  324 GLY A C   
2574 O O   . GLY A 315 ? 0.4065 0.5794 0.6716 -0.0867 0.3086  0.0032  324 GLY A O   
2575 N N   . ASP A 316 ? 0.3967 0.5401 0.6242 -0.0805 0.2760  0.0000  325 ASP A N   
2576 C CA  . ASP A 316 ? 0.3980 0.5327 0.5884 -0.0738 0.2834  -0.0041 325 ASP A CA  
2577 C C   . ASP A 316 ? 0.3620 0.4940 0.5526 -0.0635 0.2710  -0.0165 325 ASP A C   
2578 O O   . ASP A 316 ? 0.3308 0.4491 0.5061 -0.0617 0.2529  -0.0171 325 ASP A O   
2579 C CB  . ASP A 316 ? 0.3997 0.5151 0.5493 -0.0776 0.2788  0.0056  325 ASP A CB  
2580 C CG  . ASP A 316 ? 0.4449 0.5553 0.5527 -0.0735 0.2875  0.0026  325 ASP A CG  
2581 O OD1 . ASP A 316 ? 0.4601 0.5735 0.5639 -0.0665 0.2897  -0.0110 325 ASP A OD1 
2582 O OD2 . ASP A 316 ? 0.4870 0.5909 0.5657 -0.0777 0.2924  0.0140  325 ASP A OD2 
2583 N N   . ALA A 317 ? 0.3861 0.5310 0.5961 -0.0565 0.2819  -0.0255 326 ALA A N   
2584 C CA  . ALA A 317 ? 0.3853 0.5278 0.6021 -0.0459 0.2736  -0.0362 326 ALA A CA  
2585 C C   . ALA A 317 ? 0.4060 0.5275 0.5802 -0.0430 0.2667  -0.0421 326 ALA A C   
2586 O O   . ALA A 317 ? 0.3798 0.4927 0.5538 -0.0383 0.2505  -0.0458 326 ALA A O   
2587 C CB  . ALA A 317 ? 0.3897 0.5476 0.6325 -0.0383 0.2916  -0.0440 326 ALA A CB  
2588 N N   . GLY A 318 ? 0.4463 0.5615 0.5843 -0.0467 0.2785  -0.0424 327 GLY A N   
2589 C CA  . GLY A 318 ? 0.4419 0.5410 0.5376 -0.0460 0.2719  -0.0480 327 GLY A CA  
2590 C C   . GLY A 318 ? 0.4279 0.5149 0.5105 -0.0485 0.2494  -0.0404 327 GLY A C   
2591 O O   . GLY A 318 ? 0.4133 0.4900 0.4857 -0.0446 0.2366  -0.0472 327 GLY A O   
2592 N N   . LEU A 319 ? 0.4217 0.5092 0.5065 -0.0551 0.2460  -0.0264 328 LEU A N   
2593 C CA  . LEU A 319 ? 0.4321 0.5082 0.5089 -0.0572 0.2266  -0.0187 328 LEU A CA  
2594 C C   . LEU A 319 ? 0.3945 0.4706 0.4989 -0.0536 0.2104  -0.0230 328 LEU A C   
2595 O O   . LEU A 319 ? 0.3577 0.4231 0.4494 -0.0518 0.1945  -0.0236 328 LEU A O   
2596 C CB  . LEU A 319 ? 0.4486 0.5237 0.5276 -0.0649 0.2292  -0.0033 328 LEU A CB  
2597 C CG  . LEU A 319 ? 0.5515 0.6198 0.5945 -0.0684 0.2342  0.0085  328 LEU A CG  
2598 C CD1 . LEU A 319 ? 0.5995 0.6646 0.6560 -0.0753 0.2378  0.0239  328 LEU A CD1 
2599 C CD2 . LEU A 319 ? 0.5445 0.6016 0.5576 -0.0654 0.2185  0.0088  328 LEU A CD2 
2600 N N   . ARG A 320 ? 0.3978 0.4879 0.5398 -0.0527 0.2143  -0.0248 329 ARG A N   
2601 C CA  . ARG A 320 ? 0.4042 0.4989 0.5732 -0.0490 0.1989  -0.0276 329 ARG A CA  
2602 C C   . ARG A 320 ? 0.3858 0.4733 0.5471 -0.0400 0.1923  -0.0367 329 ARG A C   
2603 O O   . ARG A 320 ? 0.3984 0.4796 0.5589 -0.0381 0.1755  -0.0365 329 ARG A O   
2604 C CB  . ARG A 320 ? 0.3905 0.5069 0.6025 -0.0495 0.2047  -0.0272 329 ARG A CB  
2605 C CG  . ARG A 320 ? 0.4426 0.5659 0.6699 -0.0605 0.2057  -0.0190 329 ARG A CG  
2606 C CD  . ARG A 320 ? 0.4659 0.6136 0.7384 -0.0619 0.2032  -0.0198 329 ARG A CD  
2607 N NE  . ARG A 320 ? 0.4816 0.6466 0.7759 -0.0556 0.2185  -0.0233 329 ARG A NE  
2608 C CZ  . ARG A 320 ? 0.5380 0.7138 0.8430 -0.0599 0.2376  -0.0211 329 ARG A CZ  
2609 N NH1 . ARG A 320 ? 0.6112 0.7819 0.9075 -0.0711 0.2445  -0.0141 329 ARG A NH1 
2610 N NH2 . ARG A 320 ? 0.5014 0.6931 0.8277 -0.0524 0.2514  -0.0253 329 ARG A NH2 
2611 N N   . GLU A 321 ? 0.4036 0.4913 0.5594 -0.0349 0.2066  -0.0450 330 GLU A N   
2612 C CA  . GLU A 321 ? 0.4497 0.5272 0.5980 -0.0272 0.2033  -0.0550 330 GLU A CA  
2613 C C   . GLU A 321 ? 0.4422 0.5026 0.5538 -0.0299 0.1917  -0.0563 330 GLU A C   
2614 O O   . GLU A 321 ? 0.4279 0.4799 0.5395 -0.0258 0.1799  -0.0597 330 GLU A O   
2615 C CB  . GLU A 321 ? 0.4706 0.5492 0.6175 -0.0228 0.2237  -0.0658 330 GLU A CB  
2616 C CG  . GLU A 321 ? 0.5223 0.6184 0.7101 -0.0170 0.2359  -0.0660 330 GLU A CG  
2617 C CD  . GLU A 321 ? 0.5972 0.6938 0.7805 -0.0137 0.2596  -0.0770 330 GLU A CD  
2618 O OE1 . GLU A 321 ? 0.7305 0.8115 0.8879 -0.0121 0.2634  -0.0886 330 GLU A OE1 
2619 O OE2 . GLU A 321 ? 0.6665 0.7796 0.8722 -0.0134 0.2748  -0.0751 330 GLU A OE2 
2620 N N   . ALA A 322 ? 0.4761 0.5329 0.5573 -0.0364 0.1958  -0.0527 331 ALA A N   
2621 C CA  . ALA A 322 ? 0.4606 0.5055 0.5077 -0.0392 0.1845  -0.0519 331 ALA A CA  
2622 C C   . ALA A 322 ? 0.4596 0.5001 0.5136 -0.0400 0.1655  -0.0434 331 ALA A C   
2623 O O   . ALA A 322 ? 0.4485 0.4801 0.4911 -0.0384 0.1528  -0.0462 331 ALA A O   
2624 C CB  . ALA A 322 ? 0.4984 0.5447 0.5148 -0.0452 0.1928  -0.0462 331 ALA A CB  
2625 N N   . TYR A 323 ? 0.4377 0.4845 0.5107 -0.0433 0.1646  -0.0341 332 TYR A N   
2626 C CA  . TYR A 323 ? 0.4085 0.4521 0.4917 -0.0446 0.1485  -0.0284 332 TYR A CA  
2627 C C   . TYR A 323 ? 0.3898 0.4349 0.4915 -0.0387 0.1379  -0.0343 332 TYR A C   
2628 O O   . TYR A 323 ? 0.3854 0.4225 0.4781 -0.0375 0.1243  -0.0342 332 TYR A O   
2629 C CB  . TYR A 323 ? 0.4032 0.4544 0.5083 -0.0504 0.1515  -0.0207 332 TYR A CB  
2630 C CG  . TYR A 323 ? 0.3912 0.4405 0.5090 -0.0524 0.1360  -0.0182 332 TYR A CG  
2631 C CD1 . TYR A 323 ? 0.4241 0.4611 0.5248 -0.0555 0.1283  -0.0121 332 TYR A CD1 
2632 C CD2 . TYR A 323 ? 0.3705 0.4318 0.5172 -0.0507 0.1291  -0.0220 332 TYR A CD2 
2633 C CE1 . TYR A 323 ? 0.4067 0.4415 0.5182 -0.0576 0.1153  -0.0119 332 TYR A CE1 
2634 C CE2 . TYR A 323 ? 0.3293 0.3909 0.4849 -0.0533 0.1148  -0.0211 332 TYR A CE2 
2635 C CZ  . TYR A 323 ? 0.3654 0.4129 0.5029 -0.0571 0.1086  -0.0172 332 TYR A CZ  
2636 O OH  . TYR A 323 ? 0.3513 0.3989 0.4969 -0.0599 0.0961  -0.0182 332 TYR A OH  
2637 N N   . ASP A 324 ? 0.3989 0.4555 0.5277 -0.0345 0.1447  -0.0382 333 ASP A N   
2638 C CA  . ASP A 324 ? 0.3944 0.4547 0.5440 -0.0275 0.1361  -0.0411 333 ASP A CA  
2639 C C   . ASP A 324 ? 0.3865 0.4324 0.5181 -0.0225 0.1329  -0.0477 333 ASP A C   
2640 O O   . ASP A 324 ? 0.3642 0.4074 0.5025 -0.0187 0.1209  -0.0469 333 ASP A O   
2641 C CB  . ASP A 324 ? 0.3951 0.4721 0.5785 -0.0224 0.1465  -0.0425 333 ASP A CB  
2642 C CG  . ASP A 324 ? 0.4036 0.4997 0.6156 -0.0270 0.1427  -0.0360 333 ASP A CG  
2643 O OD1 . ASP A 324 ? 0.3748 0.4688 0.5802 -0.0346 0.1331  -0.0317 333 ASP A OD1 
2644 O OD2 . ASP A 324 ? 0.3798 0.4938 0.6227 -0.0232 0.1496  -0.0358 333 ASP A OD2 
2645 N N   . ALA A 325 ? 0.4081 0.4456 0.5163 -0.0235 0.1438  -0.0546 334 ALA A N   
2646 C CA  . ALA A 325 ? 0.4240 0.4475 0.5126 -0.0216 0.1415  -0.0629 334 ALA A CA  
2647 C C   . ALA A 325 ? 0.4214 0.4368 0.4909 -0.0250 0.1249  -0.0587 334 ALA A C   
2648 O O   . ALA A 325 ? 0.4373 0.4440 0.5038 -0.0226 0.1177  -0.0626 334 ALA A O   
2649 C CB  . ALA A 325 ? 0.4416 0.4609 0.5059 -0.0245 0.1562  -0.0723 334 ALA A CB  
2650 N N   . CYS A 326 ? 0.4231 0.4410 0.4815 -0.0304 0.1201  -0.0503 335 CYS A N   
2651 C CA  . CYS A 326 ? 0.4038 0.4155 0.4482 -0.0327 0.1052  -0.0450 335 CYS A CA  
2652 C C   . CYS A 326 ? 0.3756 0.3892 0.4412 -0.0298 0.0930  -0.0418 335 CYS A C   
2653 O O   . CYS A 326 ? 0.3589 0.3660 0.4178 -0.0285 0.0826  -0.0425 335 CYS A O   
2654 C CB  . CYS A 326 ? 0.4180 0.4306 0.4490 -0.0379 0.1052  -0.0358 335 CYS A CB  
2655 S SG  . CYS A 326 ? 0.4266 0.4394 0.4265 -0.0414 0.1168  -0.0366 335 CYS A SG  
2656 N N   . VAL A 327 ? 0.5205 0.4735 0.3484 -0.1107 0.1088  0.0004  336 VAL A N   
2657 C CA  . VAL A 327 ? 0.4576 0.4264 0.3497 -0.0885 0.0959  -0.0009 336 VAL A CA  
2658 C C   . VAL A 327 ? 0.4285 0.3949 0.3357 -0.0671 0.1103  -0.0221 336 VAL A C   
2659 O O   . VAL A 327 ? 0.3911 0.3529 0.3179 -0.0540 0.0891  -0.0254 336 VAL A O   
2660 C CB  . VAL A 327 ? 0.4255 0.4271 0.3701 -0.0903 0.1026  0.0132  336 VAL A CB  
2661 C CG1 . VAL A 327 ? 0.4246 0.4426 0.4266 -0.0728 0.0889  0.0114  336 VAL A CG1 
2662 C CG2 . VAL A 327 ? 0.4744 0.4685 0.4078 -0.1113 0.0817  0.0351  336 VAL A CG2 
2663 N N   . LYS A 328 ? 0.4791 0.4462 0.3782 -0.0630 0.1491  -0.0354 337 LYS A N   
2664 C CA  . LYS A 328 ? 0.5043 0.4597 0.4168 -0.0420 0.1668  -0.0550 337 LYS A CA  
2665 C C   . LYS A 328 ? 0.5062 0.4240 0.3726 -0.0461 0.1447  -0.0671 337 LYS A C   
2666 O O   . LYS A 328 ? 0.4893 0.4025 0.3824 -0.0293 0.1362  -0.0734 337 LYS A O   
2667 C CB  . LYS A 328 ? 0.5435 0.4909 0.4409 -0.0378 0.2192  -0.0704 337 LYS A CB  
2668 C CG  . LYS A 328 ? 0.6221 0.6172 0.5934 -0.0237 0.2477  -0.0567 337 LYS A CG  
2669 C CD  . LYS A 328 ? 0.6814 0.6700 0.6289 -0.0236 0.3066  -0.0690 337 LYS A CD  
2670 C CE  . LYS A 328 ? 0.6923 0.7408 0.7282 -0.0094 0.3355  -0.0481 337 LYS A CE  
2671 N NZ  . LYS A 328 ? 0.7582 0.8059 0.7703 -0.0114 0.3975  -0.0568 337 LYS A NZ  
2672 N N   . ALA A 329 ? 0.5643 0.4586 0.3635 -0.0713 0.1337  -0.0661 338 ALA A N   
2673 C CA  . ALA A 329 ? 0.5854 0.4512 0.3438 -0.0816 0.1077  -0.0708 338 ALA A CA  
2674 C C   . ALA A 329 ? 0.5309 0.4143 0.3358 -0.0694 0.0707  -0.0558 338 ALA A C   
2675 O O   . ALA A 329 ? 0.5286 0.4014 0.3375 -0.0630 0.0583  -0.0618 338 ALA A O   
2676 C CB  . ALA A 329 ? 0.6448 0.4906 0.3266 -0.1160 0.0970  -0.0640 338 ALA A CB  
2677 N N   . LEU A 330 ? 0.5047 0.4114 0.3435 -0.0664 0.0568  -0.0375 339 LEU A N   
2678 C CA  . LEU A 330 ? 0.4531 0.3699 0.3312 -0.0532 0.0305  -0.0272 339 LEU A CA  
2679 C C   . LEU A 330 ? 0.4375 0.3661 0.3607 -0.0316 0.0364  -0.0367 339 LEU A C   
2680 O O   . LEU A 330 ? 0.3862 0.3132 0.3225 -0.0221 0.0214  -0.0370 339 LEU A O   
2681 C CB  . LEU A 330 ? 0.4399 0.3644 0.3333 -0.0578 0.0171  -0.0082 339 LEU A CB  
2682 C CG  . LEU A 330 ? 0.4812 0.3955 0.3445 -0.0754 -0.0011 0.0118  339 LEU A CG  
2683 C CD1 . LEU A 330 ? 0.5194 0.4336 0.4044 -0.0767 -0.0099 0.0296  339 LEU A CD1 
2684 C CD2 . LEU A 330 ? 0.5257 0.4360 0.3889 -0.0725 -0.0242 0.0203  339 LEU A CD2 
2685 N N   . VAL A 331 ? 0.4128 0.3569 0.3624 -0.0251 0.0576  -0.0404 340 VAL A N   
2686 C CA  . VAL A 331 ? 0.4039 0.3633 0.3997 -0.0069 0.0615  -0.0434 340 VAL A CA  
2687 C C   . VAL A 331 ? 0.4074 0.3463 0.3928 0.0023  0.0680  -0.0568 340 VAL A C   
2688 O O   . VAL A 331 ? 0.3816 0.3232 0.3883 0.0123  0.0542  -0.0549 340 VAL A O   
2689 C CB  . VAL A 331 ? 0.4082 0.3954 0.4445 -0.0022 0.0849  -0.0383 340 VAL A CB  
2690 C CG1 . VAL A 331 ? 0.4071 0.4123 0.4962 0.0169  0.0888  -0.0357 340 VAL A CG1 
2691 C CG2 . VAL A 331 ? 0.4129 0.4209 0.4662 -0.0146 0.0718  -0.0223 340 VAL A CG2 
2692 N N   . SER A 332 ? 0.4717 0.3856 0.4186 -0.0043 0.0898  -0.0704 341 SER A N   
2693 C CA  . SER A 332 ? 0.5042 0.3863 0.4331 0.0002  0.0981  -0.0858 341 SER A CA  
2694 C C   . SER A 332 ? 0.5030 0.3741 0.4129 -0.0084 0.0665  -0.0820 341 SER A C   
2695 O O   . SER A 332 ? 0.4529 0.3151 0.3784 0.0004  0.0612  -0.0844 341 SER A O   
2696 C CB  . SER A 332 ? 0.5335 0.3792 0.4055 -0.0124 0.1280  -0.1049 341 SER A CB  
2697 O OG  . SER A 332 ? 0.6262 0.4866 0.5227 -0.0016 0.1644  -0.1071 341 SER A OG  
2698 N N   . LEU A 333 ? 0.5393 0.4140 0.4216 -0.0254 0.0461  -0.0718 342 LEU A N   
2699 C CA  . LEU A 333 ? 0.5087 0.3861 0.3888 -0.0314 0.0167  -0.0604 342 LEU A CA  
2700 C C   . LEU A 333 ? 0.4322 0.3323 0.3620 -0.0121 0.0066  -0.0522 342 LEU A C   
2701 O O   . LEU A 333 ? 0.4098 0.3078 0.3489 -0.0086 -0.0023 -0.0511 342 LEU A O   
2702 C CB  . LEU A 333 ? 0.5472 0.4325 0.4074 -0.0477 -0.0018 -0.0433 342 LEU A CB  
2703 C CG  . LEU A 333 ? 0.5815 0.4742 0.4447 -0.0555 -0.0300 -0.0260 342 LEU A CG  
2704 C CD1 . LEU A 333 ? 0.6112 0.4796 0.4273 -0.0803 -0.0376 -0.0318 342 LEU A CD1 
2705 C CD2 . LEU A 333 ? 0.6032 0.5113 0.4733 -0.0610 -0.0468 -0.0019 342 LEU A CD2 
2706 N N   . ARG A 334 ? 0.3898 0.3089 0.3458 -0.0034 0.0081  -0.0465 343 ARG A N   
2707 C CA  . ARG A 334 ? 0.3466 0.2814 0.3360 0.0095  -0.0005 -0.0410 343 ARG A CA  
2708 C C   . ARG A 334 ? 0.3414 0.2806 0.3553 0.0205  0.0053  -0.0446 343 ARG A C   
2709 O O   . ARG A 334 ? 0.3272 0.2732 0.3540 0.0261  -0.0051 -0.0394 343 ARG A O   
2710 C CB  . ARG A 334 ? 0.3386 0.2835 0.3396 0.0090  -0.0023 -0.0355 343 ARG A CB  
2711 C CG  . ARG A 334 ? 0.3318 0.2688 0.3184 0.0031  -0.0120 -0.0269 343 ARG A CG  
2712 C CD  . ARG A 334 ? 0.3221 0.2564 0.3153 0.0008  -0.0143 -0.0224 343 ARG A CD  
2713 N NE  . ARG A 334 ? 0.3662 0.2878 0.3536 0.0011  -0.0225 -0.0117 343 ARG A NE  
2714 C CZ  . ARG A 334 ? 0.3772 0.2896 0.3569 -0.0077 -0.0255 -0.0007 343 ARG A CZ  
2715 N NH1 . ARG A 334 ? 0.3777 0.2928 0.3490 -0.0207 -0.0195 0.0000  343 ARG A NH1 
2716 N NH2 . ARG A 334 ? 0.3733 0.2757 0.3594 -0.0026 -0.0334 0.0135  343 ARG A NH2 
2717 N N   . SER A 335 ? 0.3538 0.2880 0.3747 0.0241  0.0239  -0.0515 344 SER A N   
2718 C CA  . SER A 335 ? 0.3575 0.2934 0.4103 0.0373  0.0309  -0.0504 344 SER A CA  
2719 C C   . SER A 335 ? 0.3679 0.2784 0.4047 0.0363  0.0266  -0.0552 344 SER A C   
2720 O O   . SER A 335 ? 0.3648 0.2811 0.4239 0.0430  0.0170  -0.0464 344 SER A O   
2721 C CB  . SER A 335 ? 0.3596 0.2950 0.4320 0.0457  0.0591  -0.0554 344 SER A CB  
2722 O OG  . SER A 335 ? 0.4026 0.3682 0.4968 0.0435  0.0608  -0.0461 344 SER A OG  
2723 N N   . TYR A 336 ? 0.3773 0.2592 0.3719 0.0235  0.0315  -0.0670 345 TYR A N   
2724 C CA  . TYR A 336 ? 0.4188 0.2746 0.3917 0.0142  0.0224  -0.0702 345 TYR A CA  
2725 C C   . TYR A 336 ? 0.3989 0.2779 0.3827 0.0109  -0.0026 -0.0542 345 TYR A C   
2726 O O   . TYR A 336 ? 0.3792 0.2540 0.3733 0.0112  -0.0104 -0.0483 345 TYR A O   
2727 C CB  . TYR A 336 ? 0.4748 0.2982 0.3911 -0.0078 0.0258  -0.0830 345 TYR A CB  
2728 C CG  . TYR A 336 ? 0.5296 0.3182 0.4190 -0.0230 0.0171  -0.0880 345 TYR A CG  
2729 C CD1 . TYR A 336 ? 0.5570 0.3000 0.4378 -0.0185 0.0377  -0.1046 345 TYR A CD1 
2730 C CD2 . TYR A 336 ? 0.5694 0.3695 0.4469 -0.0424 -0.0113 -0.0739 345 TYR A CD2 
2731 C CE1 . TYR A 336 ? 0.6156 0.3182 0.4674 -0.0368 0.0281  -0.1098 345 TYR A CE1 
2732 C CE2 . TYR A 336 ? 0.5687 0.3390 0.4231 -0.0622 -0.0231 -0.0752 345 TYR A CE2 
2733 C CZ  . TYR A 336 ? 0.5821 0.3004 0.4194 -0.0612 -0.0047 -0.0945 345 TYR A CZ  
2734 O OH  . TYR A 336 ? 0.7046 0.3859 0.5148 -0.0848 -0.0180 -0.0963 345 TYR A OH  
2735 N N   . HIS A 337 ? 0.3884 0.2900 0.3713 0.0086  -0.0117 -0.0464 346 HIS A N   
2736 C CA  . HIS A 337 ? 0.3569 0.2809 0.3541 0.0104  -0.0264 -0.0322 346 HIS A CA  
2737 C C   . HIS A 337 ? 0.3496 0.2877 0.3724 0.0229  -0.0265 -0.0270 346 HIS A C   
2738 O O   . HIS A 337 ? 0.3326 0.2795 0.3625 0.0224  -0.0333 -0.0177 346 HIS A O   
2739 C CB  . HIS A 337 ? 0.3771 0.3132 0.3718 0.0100  -0.0297 -0.0264 346 HIS A CB  
2740 C CG  . HIS A 337 ? 0.3087 0.2629 0.3212 0.0168  -0.0361 -0.0135 346 HIS A CG  
2741 N ND1 . HIS A 337 ? 0.3244 0.2845 0.3473 0.0283  -0.0305 -0.0150 346 HIS A ND1 
2742 C CD2 . HIS A 337 ? 0.3561 0.3234 0.3782 0.0134  -0.0451 0.0018  346 HIS A CD2 
2743 C CE1 . HIS A 337 ? 0.3130 0.2834 0.3474 0.0347  -0.0299 -0.0052 346 HIS A CE1 
2744 N NE2 . HIS A 337 ? 0.2532 0.2332 0.2952 0.0278  -0.0385 0.0077  346 HIS A NE2 
2745 N N   . LEU A 338 ? 0.3327 0.2760 0.3689 0.0307  -0.0202 -0.0298 347 LEU A N   
2746 C CA  . LEU A 338 ? 0.3393 0.2956 0.3946 0.0365  -0.0251 -0.0212 347 LEU A CA  
2747 C C   . LEU A 338 ? 0.3589 0.3061 0.4250 0.0378  -0.0272 -0.0151 347 LEU A C   
2748 O O   . LEU A 338 ? 0.3191 0.2763 0.3890 0.0367  -0.0355 -0.0038 347 LEU A O   
2749 C CB  . LEU A 338 ? 0.3472 0.3156 0.4224 0.0402  -0.0227 -0.0193 347 LEU A CB  
2750 C CG  . LEU A 338 ? 0.3942 0.3712 0.4578 0.0343  -0.0276 -0.0203 347 LEU A CG  
2751 C CD1 . LEU A 338 ? 0.4372 0.4269 0.5209 0.0323  -0.0250 -0.0177 347 LEU A CD1 
2752 C CD2 . LEU A 338 ? 0.3484 0.3305 0.4001 0.0299  -0.0380 -0.0146 347 LEU A CD2 
2753 N N   . GLN A 339 ? 0.3763 0.2993 0.4426 0.0389  -0.0175 -0.0232 348 GLN A N   
2754 C CA  . GLN A 339 ? 0.3990 0.3005 0.4743 0.0396  -0.0177 -0.0190 348 GLN A CA  
2755 C C   . GLN A 339 ? 0.3979 0.2955 0.4551 0.0256  -0.0301 -0.0135 348 GLN A C   
2756 O O   . GLN A 339 ? 0.4041 0.2988 0.4726 0.0236  -0.0372 -0.0011 348 GLN A O   
2757 C CB  . GLN A 339 ? 0.4205 0.2847 0.4919 0.0438  0.0018  -0.0343 348 GLN A CB  
2758 C CG  . GLN A 339 ? 0.4475 0.3243 0.5523 0.0605  0.0183  -0.0339 348 GLN A CG  
2759 C CD  . GLN A 339 ? 0.5032 0.3410 0.6009 0.0672  0.0475  -0.0521 348 GLN A CD  
2760 O OE1 . GLN A 339 ? 0.6516 0.4464 0.7426 0.0685  0.0564  -0.0590 348 GLN A OE1 
2761 N NE2 . GLN A 339 ? 0.5409 0.3889 0.6366 0.0702  0.0652  -0.0608 348 GLN A NE2 
2762 N N   . ILE A 340 ? 0.3884 0.2904 0.4233 0.0149  -0.0339 -0.0181 349 ILE A N   
2763 C CA  . ILE A 340 ? 0.3986 0.3134 0.4297 0.0021  -0.0467 -0.0059 349 ILE A CA  
2764 C C   . ILE A 340 ? 0.3646 0.3121 0.4146 0.0094  -0.0490 0.0094  349 ILE A C   
2765 O O   . ILE A 340 ? 0.3276 0.2821 0.3858 0.0025  -0.0549 0.0233  349 ILE A O   
2766 C CB  . ILE A 340 ? 0.4059 0.3279 0.4203 -0.0088 -0.0523 -0.0065 349 ILE A CB  
2767 C CG1 . ILE A 340 ? 0.4718 0.3556 0.4509 -0.0253 -0.0517 -0.0211 349 ILE A CG1 
2768 C CG2 . ILE A 340 ? 0.4186 0.3699 0.4483 -0.0181 -0.0651 0.0146  349 ILE A CG2 
2769 C CD1 . ILE A 340 ? 0.5571 0.4087 0.5195 -0.0448 -0.0597 -0.0219 349 ILE A CD1 
2770 N N   . VAL A 341 ? 0.3529 0.3158 0.4042 0.0204  -0.0432 0.0064  350 VAL A N   
2771 C CA  . VAL A 341 ? 0.3169 0.3012 0.3705 0.0247  -0.0409 0.0155  350 VAL A CA  
2772 C C   . VAL A 341 ? 0.3134 0.2978 0.3722 0.0226  -0.0460 0.0264  350 VAL A C   
2773 O O   . VAL A 341 ? 0.3029 0.3021 0.3591 0.0187  -0.0454 0.0390  350 VAL A O   
2774 C CB  . VAL A 341 ? 0.3176 0.3050 0.3603 0.0318  -0.0343 0.0061  350 VAL A CB  
2775 C CG1 . VAL A 341 ? 0.3342 0.3316 0.3633 0.0327  -0.0278 0.0103  350 VAL A CG1 
2776 C CG2 . VAL A 341 ? 0.3140 0.3003 0.3561 0.0343  -0.0304 0.0013  350 VAL A CG2 
2777 N N   . THR A 342 ? 0.3070 0.2767 0.3764 0.0258  -0.0493 0.0248  351 THR A N   
2778 C CA  . THR A 342 ? 0.3254 0.2937 0.4091 0.0247  -0.0570 0.0414  351 THR A CA  
2779 C C   . THR A 342 ? 0.3526 0.3103 0.4396 0.0154  -0.0611 0.0524  351 THR A C   
2780 O O   . THR A 342 ? 0.3541 0.3234 0.4422 0.0090  -0.0672 0.0712  351 THR A O   
2781 C CB  . THR A 342 ? 0.3363 0.2915 0.4456 0.0346  -0.0561 0.0410  351 THR A CB  
2782 O OG1 . THR A 342 ? 0.3346 0.3064 0.4449 0.0386  -0.0549 0.0353  351 THR A OG1 
2783 C CG2 . THR A 342 ? 0.3457 0.3021 0.4800 0.0355  -0.0669 0.0656  351 THR A CG2 
2784 N N   . LYS A 343 ? 0.3412 0.2754 0.4247 0.0106  -0.0591 0.0417  352 LYS A N   
2785 C CA  . LYS A 343 ? 0.3633 0.2816 0.4468 -0.0044 -0.0662 0.0512  352 LYS A CA  
2786 C C   . LYS A 343 ? 0.3509 0.3042 0.4341 -0.0155 -0.0696 0.0657  352 LYS A C   
2787 O O   . LYS A 343 ? 0.3691 0.3291 0.4605 -0.0264 -0.0754 0.0850  352 LYS A O   
2788 C CB  . LYS A 343 ? 0.3747 0.2523 0.4422 -0.0131 -0.0646 0.0333  352 LYS A CB  
2789 C CG  . LYS A 343 ? 0.4571 0.3146 0.5163 -0.0373 -0.0765 0.0418  352 LYS A CG  
2790 C CD  . LYS A 343 ? 0.4847 0.2885 0.5128 -0.0512 -0.0752 0.0206  352 LYS A CD  
2791 C CE  . LYS A 343 ? 0.4756 0.2583 0.4913 -0.0824 -0.0923 0.0311  352 LYS A CE  
2792 N NZ  . LYS A 343 ? 0.6234 0.3395 0.5936 -0.1028 -0.0917 0.0073  352 LYS A NZ  
2793 N N   . TYR A 344 ? 0.3206 0.2969 0.3997 -0.0116 -0.0640 0.0591  353 TYR A N   
2794 C CA  . TYR A 344 ? 0.3035 0.3153 0.3949 -0.0180 -0.0628 0.0745  353 TYR A CA  
2795 C C   . TYR A 344 ? 0.2863 0.3299 0.3796 -0.0070 -0.0475 0.0822  353 TYR A C   
2796 O O   . TYR A 344 ? 0.2682 0.3435 0.3787 -0.0102 -0.0402 0.0992  353 TYR A O   
2797 C CB  . TYR A 344 ? 0.3034 0.3204 0.3961 -0.0206 -0.0660 0.0691  353 TYR A CB  
2798 C CG  . TYR A 344 ? 0.3280 0.3189 0.4107 -0.0435 -0.0830 0.0687  353 TYR A CG  
2799 C CD1 . TYR A 344 ? 0.3665 0.3110 0.4209 -0.0461 -0.0836 0.0465  353 TYR A CD1 
2800 C CD2 . TYR A 344 ? 0.3507 0.3609 0.4496 -0.0653 -0.0969 0.0910  353 TYR A CD2 
2801 C CE1 . TYR A 344 ? 0.4326 0.3406 0.4627 -0.0709 -0.0960 0.0412  353 TYR A CE1 
2802 C CE2 . TYR A 344 ? 0.3877 0.3663 0.4665 -0.0937 -0.1158 0.0895  353 TYR A CE2 
2803 C CZ  . TYR A 344 ? 0.4173 0.3395 0.4555 -0.0971 -0.1145 0.0621  353 TYR A CZ  
2804 O OH  . TYR A 344 ? 0.4741 0.3537 0.4782 -0.1287 -0.1302 0.0559  353 TYR A OH  
2805 N N   . ILE A 345 ? 0.3093 0.3443 0.3840 0.0035  -0.0414 0.0708  354 ILE A N   
2806 C CA  . ILE A 345 ? 0.3186 0.3707 0.3769 0.0087  -0.0259 0.0729  354 ILE A CA  
2807 C C   . ILE A 345 ? 0.3263 0.3715 0.3648 0.0018  -0.0331 0.0799  354 ILE A C   
2808 O O   . ILE A 345 ? 0.3701 0.4303 0.3987 -0.0065 -0.0276 0.0957  354 ILE A O   
2809 C CB  . ILE A 345 ? 0.3216 0.3691 0.3664 0.0219  -0.0126 0.0540  354 ILE A CB  
2810 C CG1 . ILE A 345 ? 0.3372 0.4007 0.4096 0.0289  -0.0048 0.0580  354 ILE A CG1 
2811 C CG2 . ILE A 345 ? 0.3612 0.4087 0.3710 0.0231  0.0047  0.0493  354 ILE A CG2 
2812 C CD1 . ILE A 345 ? 0.3974 0.4522 0.4649 0.0434  0.0082  0.0439  354 ILE A CD1 
2813 N N   . LEU A 346 ? 0.3229 0.3501 0.3585 0.0041  -0.0453 0.0725  355 LEU A N   
2814 C CA  . LEU A 346 ? 0.3508 0.3781 0.3727 -0.0035 -0.0567 0.0851  355 LEU A CA  
2815 C C   . LEU A 346 ? 0.3689 0.3976 0.4045 -0.0134 -0.0674 0.1109  355 LEU A C   
2816 O O   . LEU A 346 ? 0.3603 0.4011 0.3739 -0.0255 -0.0700 0.1283  355 LEU A O   
2817 C CB  . LEU A 346 ? 0.3545 0.3712 0.3888 0.0018  -0.0689 0.0797  355 LEU A CB  
2818 C CG  . LEU A 346 ? 0.3785 0.3921 0.3998 0.0072  -0.0630 0.0583  355 LEU A CG  
2819 C CD1 . LEU A 346 ? 0.3714 0.3854 0.4146 0.0088  -0.0767 0.0632  355 LEU A CD1 
2820 C CD2 . LEU A 346 ? 0.4406 0.4562 0.4166 -0.0006 -0.0537 0.0501  355 LEU A CD2 
2821 N N   . ILE A 347 ? 0.3319 0.3433 0.3974 -0.0112 -0.0731 0.1130  356 ILE A N   
2822 C CA  . ILE A 347 ? 0.3707 0.3719 0.4526 -0.0208 -0.0847 0.1373  356 ILE A CA  
2823 C C   . ILE A 347 ? 0.3611 0.3845 0.4336 -0.0357 -0.0788 0.1543  356 ILE A C   
2824 O O   . ILE A 347 ? 0.3936 0.4265 0.4573 -0.0473 -0.0848 0.1788  356 ILE A O   
2825 C CB  . ILE A 347 ? 0.3689 0.3306 0.4775 -0.0156 -0.0893 0.1304  356 ILE A CB  
2826 C CG1 . ILE A 347 ? 0.4035 0.3511 0.5313 0.0001  -0.0923 0.1268  356 ILE A CG1 
2827 C CG2 . ILE A 347 ? 0.3915 0.3328 0.5138 -0.0288 -0.0990 0.1532  356 ILE A CG2 
2828 C CD1 . ILE A 347 ? 0.4301 0.3349 0.5769 0.0109  -0.0848 0.1104  356 ILE A CD1 
2829 N N   . PRO A 348 ? 0.3682 0.4049 0.4458 -0.0365 -0.0674 0.1458  357 PRO A N   
2830 C CA  . PRO A 348 ? 0.3582 0.4278 0.4368 -0.0478 -0.0564 0.1645  357 PRO A CA  
2831 C C   . PRO A 348 ? 0.3437 0.4365 0.3889 -0.0479 -0.0395 0.1688  357 PRO A C   
2832 O O   . PRO A 348 ? 0.3444 0.4549 0.3823 -0.0620 -0.0353 0.1924  357 PRO A O   
2833 C CB  . PRO A 348 ? 0.3413 0.4269 0.4388 -0.0428 -0.0470 0.1541  357 PRO A CB  
2834 C CG  . PRO A 348 ? 0.3630 0.4135 0.4664 -0.0403 -0.0618 0.1367  357 PRO A CG  
2835 C CD  . PRO A 348 ? 0.3394 0.3653 0.4269 -0.0290 -0.0654 0.1243  357 PRO A CD  
2836 N N   . ALA A 349 ? 0.3547 0.4425 0.3736 -0.0360 -0.0300 0.1463  358 ALA A N   
2837 C CA  . ALA A 349 ? 0.4174 0.5136 0.3877 -0.0407 -0.0135 0.1446  358 ALA A CA  
2838 C C   . ALA A 349 ? 0.4743 0.5668 0.4190 -0.0596 -0.0323 0.1675  358 ALA A C   
2839 O O   . ALA A 349 ? 0.5227 0.6282 0.4280 -0.0738 -0.0195 0.1794  358 ALA A O   
2840 C CB  . ALA A 349 ? 0.4139 0.4939 0.3567 -0.0296 -0.0052 0.1155  358 ALA A CB  
2841 N N   . SER A 350 ? 0.4584 0.5335 0.4264 -0.0595 -0.0608 0.1758  359 SER A N   
2842 C CA  . SER A 350 ? 0.5024 0.5762 0.4616 -0.0757 -0.0842 0.2061  359 SER A CA  
2843 C C   . SER A 350 ? 0.5311 0.6128 0.5046 -0.0900 -0.0873 0.2379  359 SER A C   
2844 O O   . SER A 350 ? 0.5735 0.6622 0.5236 -0.1087 -0.0992 0.2666  359 SER A O   
2845 C CB  . SER A 350 ? 0.4547 0.5099 0.4526 -0.0657 -0.1091 0.2102  359 SER A CB  
2846 O OG  . SER A 350 ? 0.3914 0.4270 0.4371 -0.0558 -0.1116 0.2113  359 SER A OG  
2847 N N   . GLN A 351 ? 0.5583 0.6382 0.5685 -0.0851 -0.0802 0.2352  360 GLN A N   
2848 C CA  . GLN A 351 ? 0.6176 0.7013 0.6481 -0.1017 -0.0858 0.2656  360 GLN A CA  
2849 C C   . GLN A 351 ? 0.6584 0.7808 0.6703 -0.1146 -0.0607 0.2776  360 GLN A C   
2850 O O   . GLN A 351 ? 0.7124 0.8443 0.7391 -0.1326 -0.0648 0.3074  360 GLN A O   
2851 C CB  . GLN A 351 ? 0.5918 0.6511 0.6665 -0.0975 -0.0934 0.2583  360 GLN A CB  
2852 C CG  . GLN A 351 ? 0.6259 0.6386 0.7238 -0.0860 -0.1122 0.2508  360 GLN A CG  
2853 C CD  . GLN A 351 ? 0.6444 0.6252 0.7650 -0.0842 -0.1132 0.2322  360 GLN A CD  
2854 O OE1 . GLN A 351 ? 0.7566 0.6934 0.8952 -0.0889 -0.1252 0.2393  360 GLN A OE1 
2855 N NE2 . GLN A 351 ? 0.6386 0.6372 0.7547 -0.0795 -0.1008 0.2093  360 GLN A NE2 
2856 N N   . GLN A 352 ? 0.6943 0.8370 0.6777 -0.1052 -0.0320 0.2559  361 GLN A N   
2857 C CA  . GLN A 352 ? 0.7457 0.9265 0.7188 -0.1118 0.0016  0.2660  361 GLN A CA  
2858 C C   . GLN A 352 ? 0.8370 1.0264 0.7521 -0.1336 0.0083  0.2873  361 GLN A C   
2859 O O   . GLN A 352 ? 0.8877 1.0562 0.7558 -0.1396 -0.0062 0.2823  361 GLN A O   
2860 C CB  . GLN A 352 ? 0.7392 0.9320 0.7092 -0.0894 0.0354  0.2351  361 GLN A CB  
2861 C CG  . GLN A 352 ? 0.7755 0.9504 0.6782 -0.0846 0.0531  0.2094  361 GLN A CG  
2862 C CD  . GLN A 352 ? 0.7663 0.9388 0.6758 -0.0590 0.0819  0.1775  361 GLN A CD  
2863 O OE1 . GLN A 352 ? 0.7701 0.9721 0.7206 -0.0464 0.1089  0.1819  361 GLN A OE1 
2864 N NE2 . GLN A 352 ? 0.7226 0.8616 0.5972 -0.0521 0.0751  0.1494  361 GLN A NE2 
2865 N N   . PRO A 353 ? 0.8898 1.1126 0.8071 -0.1491 0.0289  0.3141  362 PRO A N   
2866 C CA  . PRO A 353 ? 0.9553 1.1862 0.8109 -0.1748 0.0357  0.3380  362 PRO A CA  
2867 C C   . PRO A 353 ? 1.0167 1.2473 0.7951 -0.1728 0.0748  0.3117  362 PRO A C   
2868 O O   . PRO A 353 ? 1.0122 1.2451 0.7981 -0.1486 0.1074  0.2798  362 PRO A O   
2869 C CB  . PRO A 353 ? 0.9750 1.2448 0.8667 -0.1905 0.0500  0.3738  362 PRO A CB  
2870 C CG  . PRO A 353 ? 0.9265 1.2214 0.8802 -0.1687 0.0720  0.3589  362 PRO A CG  
2871 C CD  . PRO A 353 ? 0.8714 1.1305 0.8488 -0.1471 0.0459  0.3278  362 PRO A CD  
2872 N N   . GLY A 371 ? 0.8962 0.7583 0.5320 -0.0259 0.0944  -0.0639 380 GLY A N   
2873 C CA  . GLY A 371 ? 0.8043 0.7192 0.4979 -0.0231 0.0727  -0.0329 380 GLY A CA  
2874 C C   . GLY A 371 ? 0.7287 0.6634 0.4845 -0.0175 0.0382  -0.0217 380 GLY A C   
2875 O O   . GLY A 371 ? 0.6761 0.5944 0.4483 -0.0079 0.0371  -0.0352 380 GLY A O   
2876 N N   . GLY A 372 ? 0.6871 0.6531 0.4750 -0.0239 0.0127  0.0032  381 GLY A N   
2877 C CA  . GLY A 372 ? 0.6060 0.5881 0.4538 -0.0155 -0.0116 0.0132  381 GLY A CA  
2878 C C   . GLY A 372 ? 0.5950 0.5648 0.4395 -0.0235 -0.0316 0.0056  381 GLY A C   
2879 O O   . GLY A 372 ? 0.5441 0.5130 0.4239 -0.0108 -0.0329 -0.0012 381 GLY A O   
2880 N N   . THR A 373 ? 0.6133 0.5759 0.4137 -0.0482 -0.0483 0.0094  382 THR A N   
2881 C CA  . THR A 373 ? 0.6101 0.5673 0.4093 -0.0620 -0.0708 0.0075  382 THR A CA  
2882 C C   . THR A 373 ? 0.5930 0.5172 0.3737 -0.0568 -0.0544 -0.0202 382 THR A C   
2883 O O   . THR A 373 ? 0.5601 0.4884 0.3731 -0.0545 -0.0654 -0.0207 382 THR A O   
2884 C CB  . THR A 373 ? 0.6754 0.6320 0.4233 -0.0972 -0.0964 0.0209  382 THR A CB  
2885 O OG1 . THR A 373 ? 0.6692 0.6591 0.4476 -0.1003 -0.1160 0.0537  382 THR A OG1 
2886 C CG2 . THR A 373 ? 0.6945 0.6516 0.4461 -0.1167 -0.1235 0.0237  382 THR A CG2 
2887 N N   . ASP A 374 ? 0.6232 0.5139 0.3547 -0.0543 -0.0257 -0.0413 383 ASP A N   
2888 C CA  . ASP A 374 ? 0.6572 0.5080 0.3722 -0.0471 -0.0072 -0.0662 383 ASP A CA  
2889 C C   . ASP A 374 ? 0.5896 0.4550 0.3702 -0.0178 0.0024  -0.0642 383 ASP A C   
2890 O O   . ASP A 374 ? 0.5752 0.4235 0.3659 -0.0160 -0.0002 -0.0724 383 ASP A O   
2891 C CB  . ASP A 374 ? 0.7484 0.5537 0.3975 -0.0472 0.0285  -0.0895 383 ASP A CB  
2892 C CG  . ASP A 374 ? 0.8980 0.6678 0.4568 -0.0858 0.0182  -0.1004 383 ASP A CG  
2893 O OD1 . ASP A 374 ? 0.9238 0.7059 0.4776 -0.1138 -0.0210 -0.0876 383 ASP A OD1 
2894 O OD2 . ASP A 374 ? 1.0194 0.7490 0.5109 -0.0899 0.0503  -0.1205 383 ASP A OD2 
2895 N N   . LEU A 375 ? 0.5285 0.4251 0.3504 0.0003  0.0101  -0.0508 384 LEU A N   
2896 C CA  . LEU A 375 ? 0.4890 0.4024 0.3675 0.0208  0.0123  -0.0449 384 LEU A CA  
2897 C C   . LEU A 375 ? 0.4361 0.3644 0.3451 0.0156  -0.0120 -0.0377 384 LEU A C   
2898 O O   . LEU A 375 ? 0.4101 0.3315 0.3365 0.0216  -0.0115 -0.0420 384 LEU A O   
2899 C CB  . LEU A 375 ? 0.5005 0.4433 0.4111 0.0331  0.0209  -0.0300 384 LEU A CB  
2900 C CG  . LEU A 375 ? 0.5344 0.4727 0.4342 0.0449  0.0528  -0.0328 384 LEU A CG  
2901 C CD1 . LEU A 375 ? 0.5576 0.5339 0.4944 0.0502  0.0550  -0.0119 384 LEU A CD1 
2902 C CD2 . LEU A 375 ? 0.5055 0.4228 0.4190 0.0637  0.0738  -0.0423 384 LEU A CD2 
2903 N N   . MET A 376 ? 0.4168 0.3653 0.3341 0.0051  -0.0307 -0.0245 385 MET A N   
2904 C CA  . MET A 376 ? 0.3860 0.3506 0.3391 0.0036  -0.0472 -0.0160 385 MET A CA  
2905 C C   . MET A 376 ? 0.3923 0.3466 0.3359 -0.0087 -0.0554 -0.0224 385 MET A C   
2906 O O   . MET A 376 ? 0.3654 0.3262 0.3379 -0.0039 -0.0558 -0.0222 385 MET A O   
2907 C CB  . MET A 376 ? 0.3893 0.3760 0.3597 -0.0031 -0.0642 0.0038  385 MET A CB  
2908 C CG  . MET A 376 ? 0.4382 0.4337 0.4244 0.0056  -0.0600 0.0141  385 MET A CG  
2909 S SD  . MET A 376 ? 0.4113 0.4036 0.4304 0.0222  -0.0487 0.0082  385 MET A SD  
2910 C CE  . MET A 376 ? 0.3381 0.3357 0.3979 0.0269  -0.0562 0.0158  385 MET A CE  
2911 N N   . ASN A 377 ? 0.4243 0.3606 0.3226 -0.0279 -0.0616 -0.0279 386 ASN A N   
2912 C CA  . ASN A 377 ? 0.4708 0.3923 0.3533 -0.0468 -0.0729 -0.0331 386 ASN A CA  
2913 C C   . ASN A 377 ? 0.4943 0.3871 0.3743 -0.0371 -0.0566 -0.0492 386 ASN A C   
2914 O O   . ASN A 377 ? 0.4976 0.3922 0.3939 -0.0455 -0.0651 -0.0467 386 ASN A O   
2915 C CB  . ASN A 377 ? 0.5196 0.4161 0.3376 -0.0758 -0.0836 -0.0387 386 ASN A CB  
2916 C CG  . ASN A 377 ? 0.5672 0.4982 0.3923 -0.0966 -0.1132 -0.0131 386 ASN A CG  
2917 O OD1 . ASN A 377 ? 0.6065 0.5213 0.3731 -0.1252 -0.1264 -0.0132 386 ASN A OD1 
2918 N ND2 . ASN A 377 ? 0.4056 0.3807 0.3000 -0.0836 -0.1233 0.0098  386 ASN A ND2 
2919 N N   . PHE A 378 ? 0.4985 0.3680 0.3635 -0.0200 -0.0334 -0.0613 387 PHE A N   
2920 C CA  . PHE A 378 ? 0.4882 0.3342 0.3624 -0.0069 -0.0190 -0.0693 387 PHE A CA  
2921 C C   . PHE A 378 ? 0.4380 0.3142 0.3610 0.0025  -0.0248 -0.0568 387 PHE A C   
2922 O O   . PHE A 378 ? 0.4144 0.2827 0.3452 -0.0027 -0.0282 -0.0563 387 PHE A O   
2923 C CB  . PHE A 378 ? 0.5010 0.3278 0.3680 0.0141  0.0077  -0.0765 387 PHE A CB  
2924 C CG  . PHE A 378 ? 0.5020 0.3222 0.4011 0.0323  0.0178  -0.0722 387 PHE A CG  
2925 C CD1 . PHE A 378 ? 0.4638 0.2438 0.3504 0.0286  0.0209  -0.0799 387 PHE A CD1 
2926 C CD2 . PHE A 378 ? 0.3855 0.2386 0.3263 0.0490  0.0201  -0.0571 387 PHE A CD2 
2927 C CE1 . PHE A 378 ? 0.4998 0.2754 0.4186 0.0440  0.0267  -0.0698 387 PHE A CE1 
2928 C CE2 . PHE A 378 ? 0.3942 0.2453 0.3639 0.0613  0.0236  -0.0470 387 PHE A CE2 
2929 C CZ  . PHE A 378 ? 0.4436 0.2576 0.4043 0.0601  0.0269  -0.0519 387 PHE A CZ  
2930 N N   . LEU A 379 ? 0.3847 0.2912 0.3343 0.0132  -0.0251 -0.0473 388 LEU A N   
2931 C CA  . LEU A 379 ? 0.3531 0.2793 0.3348 0.0191  -0.0272 -0.0398 388 LEU A CA  
2932 C C   . LEU A 379 ? 0.3352 0.2768 0.3335 0.0085  -0.0363 -0.0351 388 LEU A C   
2933 O O   . LEU A 379 ? 0.3216 0.2671 0.3332 0.0092  -0.0325 -0.0334 388 LEU A O   
2934 C CB  . LEU A 379 ? 0.3439 0.2891 0.3420 0.0279  -0.0261 -0.0330 388 LEU A CB  
2935 C CG  . LEU A 379 ? 0.3737 0.3171 0.3716 0.0383  -0.0168 -0.0306 388 LEU A CG  
2936 C CD1 . LEU A 379 ? 0.3571 0.3186 0.3698 0.0398  -0.0204 -0.0220 388 LEU A CD1 
2937 C CD2 . LEU A 379 ? 0.3712 0.3079 0.3782 0.0439  -0.0130 -0.0273 388 LEU A CD2 
2938 N N   . LYS A 380 ? 0.3272 0.2811 0.3270 -0.0020 -0.0480 -0.0296 389 LYS A N   
2939 C CA  . LYS A 380 ? 0.3288 0.3069 0.3576 -0.0118 -0.0572 -0.0184 389 LYS A CA  
2940 C C   . LYS A 380 ? 0.3306 0.2958 0.3481 -0.0283 -0.0616 -0.0210 389 LYS A C   
2941 O O   . LYS A 380 ? 0.3115 0.2954 0.3577 -0.0314 -0.0594 -0.0132 389 LYS A O   
2942 C CB  . LYS A 380 ? 0.3462 0.3464 0.3860 -0.0208 -0.0742 -0.0038 389 LYS A CB  
2943 C CG  . LYS A 380 ? 0.3099 0.3260 0.3771 -0.0042 -0.0700 0.0049  389 LYS A CG  
2944 C CD  . LYS A 380 ? 0.3595 0.3944 0.4337 -0.0143 -0.0898 0.0242  389 LYS A CD  
2945 C CE  . LYS A 380 ? 0.2872 0.3278 0.3831 0.0011  -0.0861 0.0335  389 LYS A CE  
2946 N NZ  . LYS A 380 ? 0.3393 0.4029 0.4523 -0.0089 -0.1084 0.0606  389 LYS A NZ  
2947 N N   . THR A 381 ? 0.3489 0.2782 0.3234 -0.0388 -0.0644 -0.0324 390 THR A N   
2948 C CA  . THR A 381 ? 0.3912 0.2931 0.3483 -0.0550 -0.0672 -0.0372 390 THR A CA  
2949 C C   . THR A 381 ? 0.3812 0.2798 0.3555 -0.0431 -0.0540 -0.0361 390 THR A C   
2950 O O   . THR A 381 ? 0.3710 0.2790 0.3611 -0.0553 -0.0572 -0.0278 390 THR A O   
2951 C CB  . THR A 381 ? 0.4368 0.2849 0.3379 -0.0635 -0.0645 -0.0549 390 THR A CB  
2952 O OG1 . THR A 381 ? 0.4172 0.2676 0.2906 -0.0828 -0.0796 -0.0545 390 THR A OG1 
2953 C CG2 . THR A 381 ? 0.4992 0.3053 0.3789 -0.0815 -0.0669 -0.0611 390 THR A CG2 
2954 N N   . VAL A 382 ? 0.3565 0.2470 0.3291 -0.0223 -0.0410 -0.0405 391 VAL A N   
2955 C CA  . VAL A 382 ? 0.3591 0.2475 0.3422 -0.0145 -0.0330 -0.0354 391 VAL A CA  
2956 C C   . VAL A 382 ? 0.3611 0.2842 0.3690 -0.0160 -0.0299 -0.0270 391 VAL A C   
2957 O O   . VAL A 382 ? 0.3554 0.2792 0.3657 -0.0230 -0.0261 -0.0206 391 VAL A O   
2958 C CB  . VAL A 382 ? 0.3374 0.2160 0.3179 0.0046  -0.0245 -0.0363 391 VAL A CB  
2959 C CG1 . VAL A 382 ? 0.3624 0.2433 0.3517 0.0074  -0.0230 -0.0252 391 VAL A CG1 
2960 C CG2 . VAL A 382 ? 0.3796 0.2197 0.3396 0.0103  -0.0175 -0.0451 391 VAL A CG2 
2961 N N   . ARG A 383 ? 0.3471 0.2948 0.3713 -0.0090 -0.0285 -0.0268 392 ARG A N   
2962 C CA  . ARG A 383 ? 0.3317 0.3052 0.3802 -0.0073 -0.0184 -0.0220 392 ARG A CA  
2963 C C   . ARG A 383 ? 0.3224 0.3171 0.3949 -0.0208 -0.0195 -0.0119 392 ARG A C   
2964 O O   . ARG A 383 ? 0.3528 0.3592 0.4353 -0.0238 -0.0058 -0.0076 392 ARG A O   
2965 C CB  . ARG A 383 ? 0.3200 0.3088 0.3873 0.0046  -0.0156 -0.0221 392 ARG A CB  
2966 C CG  . ARG A 383 ? 0.3418 0.3455 0.4319 0.0110  0.0036  -0.0210 392 ARG A CG  
2967 C CD  . ARG A 383 ? 0.3654 0.3719 0.4733 0.0247  0.0087  -0.0218 392 ARG A CD  
2968 N NE  . ARG A 383 ? 0.4219 0.4509 0.5623 0.0256  -0.0055 -0.0078 392 ARG A NE  
2969 C CZ  . ARG A 383 ? 0.4156 0.4525 0.5847 0.0373  -0.0045 -0.0003 392 ARG A CZ  
2970 N NH1 . ARG A 383 ? 0.4488 0.4663 0.6166 0.0501  0.0131  -0.0094 392 ARG A NH1 
2971 N NH2 . ARG A 383 ? 0.4731 0.5339 0.6696 0.0333  -0.0231 0.0182  392 ARG A NH2 
2972 N N   . SER A 384 ? 0.3510 0.3525 0.4308 -0.0321 -0.0361 -0.0063 393 SER A N   
2973 C CA  . SER A 384 ? 0.3566 0.3858 0.4666 -0.0502 -0.0435 0.0092  393 SER A CA  
2974 C C   . SER A 384 ? 0.3710 0.3835 0.4662 -0.0663 -0.0422 0.0106  393 SER A C   
2975 O O   . SER A 384 ? 0.3545 0.3963 0.4805 -0.0753 -0.0348 0.0243  393 SER A O   
2976 C CB  . SER A 384 ? 0.3873 0.4220 0.4961 -0.0672 -0.0689 0.0165  393 SER A CB  
2977 O OG  . SER A 384 ? 0.4692 0.5324 0.6077 -0.0911 -0.0821 0.0355  393 SER A OG  
2978 N N   . THR A 385 ? 0.3825 0.3486 0.4353 -0.0687 -0.0468 -0.0011 394 THR A N   
2979 C CA  . THR A 385 ? 0.4159 0.3570 0.4538 -0.0820 -0.0461 0.0024  394 THR A CA  
2980 C C   . THR A 385 ? 0.3898 0.3476 0.4366 -0.0750 -0.0279 0.0091  394 THR A C   
2981 O O   . THR A 385 ? 0.3757 0.3413 0.4297 -0.0908 -0.0246 0.0212  394 THR A O   
2982 C CB  . THR A 385 ? 0.4463 0.3302 0.4445 -0.0783 -0.0498 -0.0099 394 THR A CB  
2983 O OG1 . THR A 385 ? 0.4642 0.3256 0.4409 -0.0899 -0.0626 -0.0196 394 THR A OG1 
2984 C CG2 . THR A 385 ? 0.4529 0.3055 0.4406 -0.0907 -0.0503 -0.0023 394 THR A CG2 
2985 N N   . THR A 386 ? 0.3588 0.3212 0.4005 -0.0554 -0.0166 0.0016  395 THR A N   
2986 C CA  . THR A 386 ? 0.3782 0.3516 0.4146 -0.0526 0.0013  0.0041  395 THR A CA  
2987 C C   . THR A 386 ? 0.3652 0.3781 0.4345 -0.0558 0.0197  0.0109  395 THR A C   
2988 O O   . THR A 386 ? 0.3792 0.4014 0.4466 -0.0681 0.0323  0.0200  395 THR A O   
2989 C CB  . THR A 386 ? 0.3680 0.3323 0.3868 -0.0362 0.0058  -0.0068 395 THR A CB  
2990 O OG1 . THR A 386 ? 0.3709 0.3097 0.3757 -0.0300 -0.0089 -0.0092 395 THR A OG1 
2991 C CG2 . THR A 386 ? 0.3615 0.3218 0.3530 -0.0418 0.0189  -0.0056 395 THR A CG2 
2992 N N   . GLU A 387 ? 0.3695 0.4072 0.4731 -0.0443 0.0226  0.0097  396 GLU A N   
2993 C CA  . GLU A 387 ? 0.3675 0.4487 0.5206 -0.0412 0.0431  0.0207  396 GLU A CA  
2994 C C   . GLU A 387 ? 0.3591 0.4683 0.5413 -0.0632 0.0383  0.0410  396 GLU A C   
2995 O O   . GLU A 387 ? 0.3470 0.4860 0.5550 -0.0655 0.0635  0.0512  396 GLU A O   
2996 C CB  . GLU A 387 ? 0.3563 0.4604 0.5521 -0.0265 0.0377  0.0247  396 GLU A CB  
2997 C CG  . GLU A 387 ? 0.4602 0.5426 0.6399 -0.0051 0.0472  0.0086  396 GLU A CG  
2998 C CD  . GLU A 387 ? 0.3634 0.4664 0.5868 0.0076  0.0381  0.0179  396 GLU A CD  
2999 O OE1 . GLU A 387 ? 0.3724 0.4871 0.6055 -0.0041 0.0094  0.0296  396 GLU A OE1 
3000 O OE2 . GLU A 387 ? 0.3855 0.4880 0.6289 0.0275  0.0591  0.0140  396 GLU A OE2 
3001 N N   . LYS A 388 ? 0.3728 0.4691 0.5475 -0.0813 0.0077  0.0461  397 LYS A N   
3002 C CA  . LYS A 388 ? 0.4127 0.5271 0.6087 -0.1097 -0.0045 0.0658  397 LYS A CA  
3003 C C   . LYS A 388 ? 0.4061 0.5039 0.5768 -0.1246 0.0059  0.0706  397 LYS A C   
3004 O O   . LYS A 388 ? 0.3731 0.4888 0.5647 -0.1498 -0.0004 0.0897  397 LYS A O   
3005 C CB  . LYS A 388 ? 0.4395 0.5272 0.6162 -0.1295 -0.0403 0.0646  397 LYS A CB  
3006 C CG  . LYS A 388 ? 0.4616 0.5820 0.6726 -0.1303 -0.0579 0.0739  397 LYS A CG  
3007 C CD  . LYS A 388 ? 0.5343 0.6102 0.6971 -0.1498 -0.0892 0.0632  397 LYS A CD  
3008 C CE  . LYS A 388 ? 0.6007 0.7127 0.7922 -0.1653 -0.1157 0.0808  397 LYS A CE  
3009 N NZ  . LYS A 388 ? 0.6036 0.6639 0.7305 -0.1895 -0.1433 0.0667  397 LYS A NZ  
3010 N N   . SER A 389 ? 0.4124 0.4776 0.5387 -0.1129 0.0182  0.0573  398 SER A N   
3011 C CA  . SER A 389 ? 0.4315 0.4854 0.5319 -0.1271 0.0291  0.0662  398 SER A CA  
3012 C C   . SER A 389 ? 0.4214 0.5118 0.5331 -0.1240 0.0661  0.0710  398 SER A C   
3013 O O   . SER A 389 ? 0.4429 0.5297 0.5304 -0.1398 0.0777  0.0812  398 SER A O   
3014 C CB  . SER A 389 ? 0.4344 0.4386 0.4824 -0.1206 0.0200  0.0564  398 SER A CB  
3015 O OG  . SER A 389 ? 0.4601 0.4278 0.4995 -0.1194 -0.0051 0.0503  398 SER A OG  
3016 N N   . LEU A 390 ? 0.4264 0.5474 0.5719 -0.1036 0.0873  0.0641  399 LEU A N   
3017 C CA  . LEU A 390 ? 0.4675 0.6198 0.6280 -0.0978 0.1314  0.0664  399 LEU A CA  
3018 C C   . LEU A 390 ? 0.4851 0.6831 0.6910 -0.1191 0.1400  0.0942  399 LEU A C   
3019 O O   . LEU A 390 ? 0.4700 0.6955 0.7265 -0.1298 0.1159  0.1120  399 LEU A O   
3020 C CB  . LEU A 390 ? 0.4393 0.6127 0.6414 -0.0687 0.1538  0.0568  399 LEU A CB  
3021 C CG  . LEU A 390 ? 0.4700 0.5994 0.6259 -0.0494 0.1553  0.0294  399 LEU A CG  
3022 C CD1 . LEU A 390 ? 0.4967 0.6451 0.7061 -0.0218 0.1702  0.0258  399 LEU A CD1 
3023 C CD2 . LEU A 390 ? 0.5157 0.6120 0.6017 -0.0544 0.1833  0.0129  399 LEU A CD2 
3024 N N   . LEU A 391 ? 0.5508 0.7550 0.7323 -0.1298 0.1723  0.0992  400 LEU A N   
3025 C CA  . LEU A 391 ? 0.6037 0.8554 0.8272 -0.1518 0.1871  0.1282  400 LEU A CA  
3026 C C   . LEU A 391 ? 0.6299 0.9459 0.9350 -0.1325 0.2264  0.1384  400 LEU A C   
3027 O O   . LEU A 391 ? 0.6358 1.0082 1.0159 -0.1453 0.2205  0.1687  400 LEU A O   
3028 C CB  . LEU A 391 ? 0.6525 0.8867 0.8135 -0.1724 0.2092  0.1321  400 LEU A CB  
3029 C CG  . LEU A 391 ? 0.6438 0.8156 0.7273 -0.1875 0.1749  0.1268  400 LEU A CG  
3030 C CD1 . LEU A 391 ? 0.7185 0.8809 0.7425 -0.2102 0.1973  0.1364  400 LEU A CD1 
3031 C CD2 . LEU A 391 ? 0.6152 0.7711 0.7176 -0.2051 0.1277  0.1424  400 LEU A CD2 
3032 N N   . LYS A 392 ? 0.6705 0.9759 0.9631 -0.1028 0.2662  0.1150  401 LYS A N   
3033 C CA  . LYS A 392 ? 0.6782 1.0354 1.0523 -0.0750 0.3106  0.1222  401 LYS A CA  
3034 C C   . LYS A 392 ? 0.6466 1.0093 1.0723 -0.0502 0.2851  0.1201  401 LYS A C   
3035 O O   . LYS A 392 ? 0.6674 0.9766 1.0408 -0.0374 0.2697  0.0928  401 LYS A O   
3036 C CB  . LYS A 392 ? 0.7489 1.0785 1.0735 -0.0567 0.3736  0.0950  401 LYS A CB  
3037 C CG  . LYS A 392 ? 0.7719 1.1550 1.1810 -0.0290 0.4367  0.1053  401 LYS A CG  
3038 C CD  . LYS A 392 ? 0.8367 1.1793 1.1739 -0.0191 0.5053  0.0742  401 LYS A CD  
3039 C CE  . LYS A 392 ? 0.8681 1.2574 1.2937 0.0152  0.5772  0.0819  401 LYS A CE  
3040 N NZ  . LYS A 392 ? 0.9730 1.3126 1.3157 0.0224  0.6512  0.0466  401 LYS A NZ  
3041 N N   . ILE B 2   ? 0.7491 0.9878 0.6314 0.0618  -0.1917 0.0964  11  ILE B N   
3042 C CA  . ILE B 2   ? 0.7157 0.9495 0.6122 0.0572  -0.1797 0.0621  11  ILE B CA  
3043 C C   . ILE B 2   ? 0.7311 0.9775 0.5858 0.0548  -0.1654 0.0518  11  ILE B C   
3044 O O   . ILE B 2   ? 0.7273 0.9714 0.5632 0.0519  -0.1493 0.0724  11  ILE B O   
3045 C CB  . ILE B 2   ? 0.6740 0.8790 0.6134 0.0528  -0.1625 0.0613  11  ILE B CB  
3046 C CG1 . ILE B 2   ? 0.6499 0.8476 0.6335 0.0571  -0.1748 0.0664  11  ILE B CG1 
3047 C CG2 . ILE B 2   ? 0.6516 0.8514 0.6023 0.0474  -0.1509 0.0307  11  ILE B CG2 
3048 C CD1 . ILE B 2   ? 0.6096 0.7820 0.6265 0.0560  -0.1595 0.0740  11  ILE B CD1 
3049 N N   . SER B 3   ? 0.7376 0.9976 0.5819 0.0563  -0.1717 0.0193  12  SER B N   
3050 C CA  . SER B 3   ? 0.7516 1.0268 0.5586 0.0571  -0.1596 0.0027  12  SER B CA  
3051 C C   . SER B 3   ? 0.7200 0.9775 0.5384 0.0514  -0.1327 0.0044  12  SER B C   
3052 O O   . SER B 3   ? 0.6837 0.9160 0.5418 0.0468  -0.1262 -0.0014 12  SER B O   
3053 C CB  . SER B 3   ? 0.7621 1.0467 0.5681 0.0604  -0.1732 -0.0379 12  SER B CB  
3054 O OG  . SER B 3   ? 0.7881 1.0915 0.5551 0.0647  -0.1639 -0.0562 12  SER B OG  
3055 N N   . LYS B 4   ? 0.7294 1.0038 0.5123 0.0518  -0.1173 0.0124  13  LYS B N   
3056 C CA  . LYS B 4   ? 0.7004 0.9635 0.4916 0.0464  -0.0924 0.0172  13  LYS B CA  
3057 C C   . LYS B 4   ? 0.6477 0.8981 0.4602 0.0463  -0.0859 -0.0172 13  LYS B C   
3058 O O   . LYS B 4   ? 0.5800 0.8132 0.4125 0.0414  -0.0693 -0.0145 13  LYS B O   
3059 C CB  . LYS B 4   ? 0.7458 1.0388 0.4948 0.0471  -0.0783 0.0322  13  LYS B CB  
3060 C CG  . LYS B 4   ? 0.7937 1.0963 0.5236 0.0446  -0.0823 0.0740  13  LYS B CG  
3061 C CD  . LYS B 4   ? 0.8328 1.1748 0.5151 0.0455  -0.0700 0.0875  13  LYS B CD  
3062 C CE  . LYS B 4   ? 0.8624 1.2094 0.5312 0.0399  -0.0726 0.1359  13  LYS B CE  
3063 N NZ  . LYS B 4   ? 0.9062 1.2959 0.5291 0.0389  -0.0582 0.1540  13  LYS B NZ  
3064 N N   . GLU B 5   ? 0.6577 0.9158 0.4670 0.0516  -0.1009 -0.0487 14  GLU B N   
3065 C CA  . GLU B 5   ? 0.6291 0.8709 0.4637 0.0512  -0.1005 -0.0810 14  GLU B CA  
3066 C C   . GLU B 5   ? 0.5744 0.7839 0.4578 0.0434  -0.1001 -0.0770 14  GLU B C   
3067 O O   . GLU B 5   ? 0.5631 0.7559 0.4680 0.0409  -0.0937 -0.0938 14  GLU B O   
3068 C CB  . GLU B 5   ? 0.6631 0.9177 0.4876 0.0578  -0.1219 -0.1142 14  GLU B CB  
3069 C CG  . GLU B 5   ? 0.6706 0.9239 0.5105 0.0566  -0.1463 -0.1144 14  GLU B CG  
3070 C CD  . GLU B 5   ? 0.7065 0.9770 0.5290 0.0636  -0.1692 -0.1472 14  GLU B CD  
3071 O OE1 . GLU B 5   ? 0.7167 0.9851 0.5374 0.0675  -0.1690 -0.1791 14  GLU B OE1 
3072 O OE2 . GLU B 5   ? 0.7274 1.0128 0.5395 0.0659  -0.1894 -0.1423 14  GLU B OE2 
3073 N N   . TYR B 6   ? 0.5352 0.7374 0.4355 0.0405  -0.1070 -0.0552 15  TYR B N   
3074 C CA  . TYR B 6   ? 0.4967 0.6736 0.4402 0.0343  -0.1030 -0.0491 15  TYR B CA  
3075 C C   . TYR B 6   ? 0.4792 0.6397 0.4291 0.0305  -0.0823 -0.0301 15  TYR B C   
3076 O O   . TYR B 6   ? 0.4752 0.6161 0.4556 0.0263  -0.0764 -0.0289 15  TYR B O   
3077 C CB  . TYR B 6   ? 0.4549 0.6333 0.4191 0.0347  -0.1188 -0.0378 15  TYR B CB  
3078 C CG  . TYR B 6   ? 0.4145 0.6063 0.3840 0.0363  -0.1414 -0.0588 15  TYR B CG  
3079 C CD1 . TYR B 6   ? 0.4065 0.5896 0.4022 0.0316  -0.1461 -0.0834 15  TYR B CD1 
3080 C CD2 . TYR B 6   ? 0.4048 0.6173 0.3545 0.0419  -0.1598 -0.0534 15  TYR B CD2 
3081 C CE1 . TYR B 6   ? 0.4000 0.5941 0.4049 0.0316  -0.1692 -0.1036 15  TYR B CE1 
3082 C CE2 . TYR B 6   ? 0.4990 0.7245 0.4550 0.0431  -0.1831 -0.0743 15  TYR B CE2 
3083 C CZ  . TYR B 6   ? 0.4347 0.6503 0.4198 0.0375  -0.1878 -0.1001 15  TYR B CZ  
3084 O OH  . TYR B 6   ? 0.4871 0.7143 0.4820 0.0375  -0.2131 -0.1211 15  TYR B OH  
3085 N N   . HIS B 7   ? 0.5065 0.6769 0.4283 0.0315  -0.0717 -0.0151 16  HIS B N   
3086 C CA  . HIS B 7   ? 0.4839 0.6402 0.4123 0.0269  -0.0535 0.0013  16  HIS B CA  
3087 C C   . HIS B 7   ? 0.4700 0.6044 0.4263 0.0244  -0.0542 0.0198  16  HIS B C   
3088 O O   . HIS B 7   ? 0.4470 0.5615 0.4255 0.0209  -0.0445 0.0188  16  HIS B O   
3089 C CB  . HIS B 7   ? 0.4973 0.6456 0.4343 0.0250  -0.0414 -0.0183 16  HIS B CB  
3090 C CG  . HIS B 7   ? 0.5656 0.7366 0.4757 0.0299  -0.0387 -0.0363 16  HIS B CG  
3091 N ND1 . HIS B 7   ? 0.6747 0.8685 0.5560 0.0313  -0.0283 -0.0242 16  HIS B ND1 
3092 C CD2 . HIS B 7   ? 0.5915 0.7675 0.5002 0.0345  -0.0456 -0.0664 16  HIS B CD2 
3093 C CE1 . HIS B 7   ? 0.6594 0.8744 0.5208 0.0380  -0.0272 -0.0477 16  HIS B CE1 
3094 N NE2 . HIS B 7   ? 0.6201 0.8223 0.4979 0.0406  -0.0388 -0.0748 16  HIS B NE2 
3095 N N   . ILE B 8   ? 0.4525 0.5924 0.4064 0.0276  -0.0671 0.0353  17  ILE B N   
3096 C CA  . ILE B 8   ? 0.4430 0.5657 0.4216 0.0286  -0.0707 0.0525  17  ILE B CA  
3097 C C   . ILE B 8   ? 0.4491 0.5728 0.4099 0.0279  -0.0702 0.0819  17  ILE B C   
3098 O O   . ILE B 8   ? 0.4310 0.5744 0.3652 0.0300  -0.0789 0.0925  17  ILE B O   
3099 C CB  . ILE B 8   ? 0.4267 0.5556 0.4234 0.0338  -0.0885 0.0478  17  ILE B CB  
3100 C CG1 . ILE B 8   ? 0.4340 0.5621 0.4536 0.0316  -0.0886 0.0223  17  ILE B CG1 
3101 C CG2 . ILE B 8   ? 0.4450 0.5592 0.4670 0.0379  -0.0928 0.0657  17  ILE B CG2 
3102 C CD1 . ILE B 8   ? 0.3959 0.5382 0.4313 0.0346  -0.1072 0.0140  17  ILE B CD1 
3103 N N   . ASP B 9   ? 0.4538 0.5562 0.4297 0.0244  -0.0609 0.0950  18  ASP B N   
3104 C CA  . ASP B 9   ? 0.4777 0.5752 0.4449 0.0212  -0.0602 0.1247  18  ASP B CA  
3105 C C   . ASP B 9   ? 0.5000 0.5854 0.4837 0.0271  -0.0764 0.1427  18  ASP B C   
3106 O O   . ASP B 9   ? 0.4914 0.5651 0.5027 0.0332  -0.0823 0.1312  18  ASP B O   
3107 C CB  . ASP B 9   ? 0.4903 0.5677 0.4719 0.0145  -0.0458 0.1279  18  ASP B CB  
3108 C CG  . ASP B 9   ? 0.5023 0.5752 0.4784 0.0080  -0.0447 0.1593  18  ASP B CG  
3109 O OD1 . ASP B 9   ? 0.5570 0.6534 0.5069 0.0028  -0.0374 0.1694  18  ASP B OD1 
3110 O OD2 . ASP B 9   ? 0.4991 0.5463 0.4982 0.0085  -0.0515 0.1736  18  ASP B OD2 
3111 N N   . GLU B 10  ? 0.5499 0.6394 0.5181 0.0256  -0.0836 0.1721  19  GLU B N   
3112 C CA  . GLU B 10  ? 0.5789 0.6552 0.5635 0.0322  -0.1015 0.1921  19  GLU B CA  
3113 C C   . GLU B 10  ? 0.5513 0.5922 0.5732 0.0337  -0.1007 0.1952  19  GLU B C   
3114 O O   . GLU B 10  ? 0.5609 0.5895 0.6093 0.0437  -0.1133 0.1934  19  GLU B O   
3115 C CB  . GLU B 10  ? 0.6317 0.7197 0.5896 0.0289  -0.1099 0.2271  19  GLU B CB  
3116 C CG  . GLU B 10  ? 0.6868 0.7716 0.6538 0.0385  -0.1336 0.2439  19  GLU B CG  
3117 C CD  . GLU B 10  ? 0.7736 0.8622 0.7197 0.0345  -0.1434 0.2855  19  GLU B CD  
3118 O OE1 . GLU B 10  ? 0.9021 0.9995 0.8256 0.0231  -0.1300 0.3030  19  GLU B OE1 
3119 O OE2 . GLU B 10  ? 0.8356 0.9197 0.7898 0.0428  -0.1648 0.3023  19  GLU B OE2 
3120 N N   . GLU B 11  ? 0.5360 0.5627 0.5611 0.0249  -0.0868 0.1980  20  GLU B N   
3121 C CA  . GLU B 11  ? 0.5388 0.5312 0.5963 0.0259  -0.0873 0.1994  20  GLU B CA  
3122 C C   . GLU B 11  ? 0.4827 0.4678 0.5592 0.0310  -0.0787 0.1668  20  GLU B C   
3123 O O   . GLU B 11  ? 0.4947 0.4638 0.5980 0.0408  -0.0856 0.1585  20  GLU B O   
3124 C CB  . GLU B 11  ? 0.5580 0.5384 0.6135 0.0130  -0.0787 0.2181  20  GLU B CB  
3125 C CG  . GLU B 11  ? 0.5943 0.5357 0.6841 0.0141  -0.0851 0.2228  20  GLU B CG  
3126 C CD  . GLU B 11  ? 0.6220 0.5516 0.7150 -0.0007 -0.0791 0.2425  20  GLU B CD  
3127 O OE1 . GLU B 11  ? 0.7213 0.6674 0.8008 -0.0098 -0.0629 0.2346  20  GLU B OE1 
3128 O OE2 . GLU B 11  ? 0.6552 0.5583 0.7683 -0.0032 -0.0915 0.2657  20  GLU B OE2 
3129 N N   . VAL B 12  ? 0.4361 0.4344 0.4986 0.0248  -0.0638 0.1491  21  VAL B N   
3130 C CA  . VAL B 12  ? 0.3970 0.3878 0.4745 0.0268  -0.0542 0.1227  21  VAL B CA  
3131 C C   . VAL B 12  ? 0.3565 0.3676 0.4316 0.0305  -0.0525 0.1008  21  VAL B C   
3132 O O   . VAL B 12  ? 0.3511 0.3594 0.4353 0.0302  -0.0436 0.0819  21  VAL B O   
3133 C CB  . VAL B 12  ? 0.3789 0.3624 0.4517 0.0171  -0.0401 0.1190  21  VAL B CB  
3134 C CG1 . VAL B 12  ? 0.4215 0.3829 0.5044 0.0118  -0.0436 0.1403  21  VAL B CG1 
3135 C CG2 . VAL B 12  ? 0.4160 0.4247 0.4625 0.0100  -0.0306 0.1159  21  VAL B CG2 
3136 N N   . GLY B 13  ? 0.3860 0.4170 0.4503 0.0335  -0.0626 0.1042  22  GLY B N   
3137 C CA  . GLY B 13  ? 0.3762 0.4257 0.4426 0.0358  -0.0646 0.0843  22  GLY B CA  
3138 C C   . GLY B 13  ? 0.3607 0.4169 0.4159 0.0289  -0.0524 0.0661  22  GLY B C   
3139 O O   . GLY B 13  ? 0.3462 0.4122 0.3767 0.0242  -0.0481 0.0678  22  GLY B O   
3140 N N   . PHE B 14  ? 0.3380 0.3903 0.4125 0.0291  -0.0469 0.0492  23  PHE B N   
3141 C CA  . PHE B 14  ? 0.3018 0.3571 0.3713 0.0233  -0.0379 0.0323  23  PHE B CA  
3142 C C   . PHE B 14  ? 0.2896 0.3304 0.3536 0.0186  -0.0248 0.0332  23  PHE B C   
3143 O O   . PHE B 14  ? 0.2754 0.3187 0.3322 0.0144  -0.0184 0.0219  23  PHE B O   
3144 C CB  . PHE B 14  ? 0.2836 0.3411 0.3774 0.0235  -0.0374 0.0185  23  PHE B CB  
3145 C CG  . PHE B 14  ? 0.2737 0.3489 0.3779 0.0261  -0.0507 0.0145  23  PHE B CG  
3146 C CD1 . PHE B 14  ? 0.3071 0.3954 0.3995 0.0229  -0.0583 0.0040  23  PHE B CD1 
3147 C CD2 . PHE B 14  ? 0.2775 0.3575 0.4054 0.0325  -0.0568 0.0194  23  PHE B CD2 
3148 C CE1 . PHE B 14  ? 0.3102 0.4153 0.4138 0.0246  -0.0734 -0.0010 23  PHE B CE1 
3149 C CE2 . PHE B 14  ? 0.3031 0.4024 0.4448 0.0345  -0.0707 0.0159  23  PHE B CE2 
3150 C CZ  . PHE B 14  ? 0.3196 0.4309 0.4490 0.0297  -0.0796 0.0060  23  PHE B CZ  
3151 N N   . ALA B 15  ? 0.3133 0.3381 0.3832 0.0196  -0.0226 0.0453  24  ALA B N   
3152 C CA  . ALA B 15  ? 0.3154 0.3282 0.3807 0.0141  -0.0128 0.0475  24  ALA B CA  
3153 C C   . ALA B 15  ? 0.3453 0.3719 0.3887 0.0088  -0.0091 0.0538  24  ALA B C   
3154 O O   . ALA B 15  ? 0.3608 0.4028 0.3892 0.0098  -0.0151 0.0632  24  ALA B O   
3155 C CB  . ALA B 15  ? 0.3384 0.3306 0.4160 0.0158  -0.0146 0.0590  24  ALA B CB  
3156 N N   . LEU B 16  ? 0.3251 0.3494 0.3665 0.0039  0.0008  0.0483  25  LEU B N   
3157 C CA  . LEU B 16  ? 0.3530 0.3936 0.3778 -0.0005 0.0072  0.0537  25  LEU B CA  
3158 C C   . LEU B 16  ? 0.3811 0.4163 0.4072 -0.0054 0.0070  0.0783  25  LEU B C   
3159 O O   . LEU B 16  ? 0.3872 0.4019 0.4299 -0.0083 0.0078  0.0824  25  LEU B O   
3160 C CB  . LEU B 16  ? 0.3109 0.3509 0.3395 -0.0032 0.0167  0.0399  25  LEU B CB  
3161 C CG  . LEU B 16  ? 0.3252 0.3871 0.3409 -0.0059 0.0254  0.0408  25  LEU B CG  
3162 C CD1 . LEU B 16  ? 0.3727 0.4582 0.3689 -0.0006 0.0235  0.0293  25  LEU B CD1 
3163 C CD2 . LEU B 16  ? 0.3093 0.3661 0.3364 -0.0076 0.0325  0.0290  25  LEU B CD2 
3164 N N   . PRO B 17  ? 0.4147 0.4677 0.4235 -0.0066 0.0046  0.0953  26  PRO B N   
3165 C CA  . PRO B 17  ? 0.4271 0.4733 0.4403 -0.0132 0.0034  0.1229  26  PRO B CA  
3166 C C   . PRO B 17  ? 0.4288 0.4805 0.4472 -0.0224 0.0155  0.1276  26  PRO B C   
3167 O O   . PRO B 17  ? 0.3952 0.4704 0.4017 -0.0225 0.0256  0.1161  26  PRO B O   
3168 C CB  . PRO B 17  ? 0.4562 0.5257 0.4456 -0.0125 -0.0013 0.1408  26  PRO B CB  
3169 C CG  . PRO B 17  ? 0.4889 0.5796 0.4593 -0.0053 -0.0018 0.1187  26  PRO B CG  
3170 C CD  . PRO B 17  ? 0.4248 0.5046 0.4093 -0.0024 0.0020  0.0906  26  PRO B CD  
3171 N N   A ASN B 18  ? 0.4338 0.4632 0.4730 -0.0290 0.0128  0.1423  27  ASN B N   
3172 N N   B ASN B 18  ? 0.4252 0.4556 0.4640 -0.0293 0.0131  0.1430  27  ASN B N   
3173 C CA  A ASN B 18  ? 0.4258 0.4581 0.4773 -0.0395 0.0213  0.1501  27  ASN B CA  
3174 C CA  B ASN B 18  ? 0.4157 0.4506 0.4660 -0.0398 0.0222  0.1504  27  ASN B CA  
3175 C C   A ASN B 18  ? 0.4020 0.4495 0.4516 -0.0382 0.0326  0.1268  27  ASN B C   
3176 C C   B ASN B 18  ? 0.3935 0.4423 0.4423 -0.0379 0.0330  0.1260  27  ASN B C   
3177 O O   A ASN B 18  ? 0.4024 0.4808 0.4415 -0.0410 0.0435  0.1292  27  ASN B O   
3178 O O   B ASN B 18  ? 0.3879 0.4677 0.4255 -0.0401 0.0440  0.1265  27  ASN B O   
3179 C CB  A ASN B 18  ? 0.4626 0.5169 0.5061 -0.0492 0.0253  0.1813  27  ASN B CB  
3180 C CB  B ASN B 18  ? 0.4450 0.5051 0.4853 -0.0492 0.0272  0.1805  27  ASN B CB  
3181 C CG  A ASN B 18  ? 0.5143 0.5485 0.5639 -0.0513 0.0114  0.2079  27  ASN B CG  
3182 C CG  B ASN B 18  ? 0.4440 0.5090 0.5042 -0.0627 0.0352  0.1943  27  ASN B CG  
3183 O OD1 A ASN B 18  ? 0.5566 0.6087 0.5860 -0.0509 0.0091  0.2267  27  ASN B OD1 
3184 O OD1 B ASN B 18  ? 0.4228 0.4634 0.5078 -0.0658 0.0317  0.1859  27  ASN B OD1 
3185 N ND2 A ASN B 18  ? 0.5195 0.5160 0.5965 -0.0522 0.0007  0.2084  27  ASN B ND2 
3186 N ND2 B ASN B 18  ? 0.4335 0.5333 0.4831 -0.0707 0.0457  0.2159  27  ASN B ND2 
3187 N N   . PRO B 19  ? 0.3858 0.4131 0.4454 -0.0327 0.0298  0.1044  28  PRO B N   
3188 C CA  . PRO B 19  ? 0.3561 0.3923 0.4165 -0.0305 0.0373  0.0832  28  PRO B CA  
3189 C C   . PRO B 19  ? 0.3621 0.4121 0.4343 -0.0389 0.0458  0.0891  28  PRO B C   
3190 O O   . PRO B 19  ? 0.3380 0.3788 0.4264 -0.0480 0.0436  0.1063  28  PRO B O   
3191 C CB  . PRO B 19  ? 0.3252 0.3327 0.3973 -0.0262 0.0309  0.0680  28  PRO B CB  
3192 C CG  . PRO B 19  ? 0.3418 0.3353 0.4126 -0.0215 0.0221  0.0733  28  PRO B CG  
3193 C CD  . PRO B 19  ? 0.3517 0.3483 0.4227 -0.0274 0.0193  0.0983  28  PRO B CD  
3194 N N   . GLN B 20  ? 0.3576 0.4301 0.4247 -0.0354 0.0544  0.0745  29  GLN B N   
3195 C CA  . GLN B 20  ? 0.3708 0.4600 0.4534 -0.0412 0.0627  0.0759  29  GLN B CA  
3196 C C   . GLN B 20  ? 0.3356 0.3979 0.4395 -0.0435 0.0560  0.0679  29  GLN B C   
3197 O O   . GLN B 20  ? 0.3159 0.3566 0.4168 -0.0369 0.0495  0.0524  29  GLN B O   
3198 C CB  . GLN B 20  ? 0.3779 0.4964 0.4512 -0.0332 0.0717  0.0578  29  GLN B CB  
3199 C CG  . GLN B 20  ? 0.3771 0.5244 0.4661 -0.0373 0.0826  0.0604  29  GLN B CG  
3200 C CD  . GLN B 20  ? 0.4076 0.5915 0.4833 -0.0274 0.0930  0.0449  29  GLN B CD  
3201 O OE1 . GLN B 20  ? 0.3472 0.5465 0.3978 -0.0224 0.0951  0.0445  29  GLN B OE1 
3202 N NE2 . GLN B 20  ? 0.3552 0.5538 0.4481 -0.0233 0.0982  0.0305  29  GLN B NE2 
3203 N N   . GLU B 21  ? 0.3294 0.3951 0.4546 -0.0534 0.0572  0.0794  30  GLU B N   
3204 C CA  . GLU B 21  ? 0.3631 0.4060 0.5085 -0.0564 0.0490  0.0721  30  GLU B CA  
3205 C C   . GLU B 21  ? 0.3343 0.3957 0.4932 -0.0555 0.0538  0.0605  30  GLU B C   
3206 O O   . GLU B 21  ? 0.3235 0.3673 0.4896 -0.0526 0.0463  0.0471  30  GLU B O   
3207 C CB  . GLU B 21  ? 0.3722 0.4021 0.5388 -0.0691 0.0426  0.0919  30  GLU B CB  
3208 C CG  . GLU B 21  ? 0.4531 0.4580 0.6140 -0.0695 0.0339  0.1035  30  GLU B CG  
3209 C CD  . GLU B 21  ? 0.4631 0.4519 0.6501 -0.0826 0.0252  0.1226  30  GLU B CD  
3210 O OE1 . GLU B 21  ? 0.4900 0.4684 0.6985 -0.0878 0.0188  0.1161  30  GLU B OE1 
3211 O OE2 . GLU B 21  ? 0.5463 0.5316 0.7334 -0.0878 0.0228  0.1446  30  GLU B OE2 
3212 N N   . ASN B 22  ? 0.3568 0.4556 0.5195 -0.0575 0.0660  0.0663  31  ASN B N   
3213 C CA  . ASN B 22  ? 0.3531 0.4751 0.5338 -0.0557 0.0712  0.0561  31  ASN B CA  
3214 C C   . ASN B 22  ? 0.3241 0.4739 0.4900 -0.0435 0.0813  0.0412  31  ASN B C   
3215 O O   . ASN B 22  ? 0.2944 0.4653 0.4422 -0.0419 0.0900  0.0474  31  ASN B O   
3216 C CB  . ASN B 22  ? 0.3740 0.5220 0.5812 -0.0692 0.0774  0.0760  31  ASN B CB  
3217 C CG  . ASN B 22  ? 0.4727 0.5909 0.6999 -0.0821 0.0645  0.0893  31  ASN B CG  
3218 O OD1 . ASN B 22  ? 0.5546 0.6473 0.7918 -0.0808 0.0521  0.0767  31  ASN B OD1 
3219 N ND2 . ASN B 22  ? 0.4766 0.5971 0.7091 -0.0942 0.0659  0.1145  31  ASN B ND2 
3220 N N   . LEU B 23  ? 0.3179 0.4669 0.4917 -0.0343 0.0787  0.0210  32  LEU B N   
3221 C CA  . LEU B 23  ? 0.3215 0.4954 0.4885 -0.0213 0.0861  0.0030  32  LEU B CA  
3222 C C   . LEU B 23  ? 0.3388 0.5580 0.5269 -0.0221 0.0989  0.0058  32  LEU B C   
3223 O O   . LEU B 23  ? 0.3201 0.5466 0.5325 -0.0335 0.0994  0.0205  32  LEU B O   
3224 C CB  . LEU B 23  ? 0.3057 0.4565 0.4767 -0.0111 0.0756  -0.0178 32  LEU B CB  
3225 C CG  . LEU B 23  ? 0.3091 0.4230 0.4604 -0.0086 0.0654  -0.0228 32  LEU B CG  
3226 C CD1 . LEU B 23  ? 0.3649 0.4571 0.5244 -0.0021 0.0549  -0.0367 32  LEU B CD1 
3227 C CD2 . LEU B 23  ? 0.3882 0.5099 0.5164 -0.0022 0.0691  -0.0296 32  LEU B CD2 
3228 N N   . PRO B 24  ? 0.3512 0.6026 0.5322 -0.0097 0.1090  -0.0096 33  PRO B N   
3229 C CA  . PRO B 24  ? 0.3571 0.6549 0.5624 -0.0067 0.1215  -0.0124 33  PRO B CA  
3230 C C   . PRO B 24  ? 0.3343 0.6237 0.5751 -0.0074 0.1129  -0.0175 33  PRO B C   
3231 O O   . PRO B 24  ? 0.3244 0.5741 0.5647 -0.0039 0.0975  -0.0273 33  PRO B O   
3232 C CB  . PRO B 24  ? 0.3625 0.6816 0.5528 0.0124  0.1274  -0.0388 33  PRO B CB  
3233 C CG  . PRO B 24  ? 0.3406 0.6394 0.4947 0.0137  0.1232  -0.0395 33  PRO B CG  
3234 C CD  . PRO B 24  ? 0.3882 0.6373 0.5405 0.0027  0.1087  -0.0266 33  PRO B CD  
3235 N N   . ASP B 25  ? 0.3358 0.6651 0.6071 -0.0121 0.1228  -0.0097 34  ASP B N   
3236 C CA  . ASP B 25  ? 0.3358 0.6639 0.6450 -0.0133 0.1138  -0.0133 34  ASP B CA  
3237 C C   . ASP B 25  ? 0.3213 0.6353 0.6356 0.0052  0.1036  -0.0404 34  ASP B C   
3238 O O   . ASP B 25  ? 0.2824 0.5724 0.6144 0.0047  0.0884  -0.0433 34  ASP B O   
3239 C CB  . ASP B 25  ? 0.3578 0.7424 0.7027 -0.0189 0.1286  -0.0033 34  ASP B CB  
3240 C CG  . ASP B 25  ? 0.4144 0.8109 0.7654 -0.0412 0.1356  0.0288  34  ASP B CG  
3241 O OD1 . ASP B 25  ? 0.4652 0.8200 0.8002 -0.0525 0.1248  0.0422  34  ASP B OD1 
3242 O OD2 . ASP B 25  ? 0.4723 0.9218 0.8468 -0.0472 0.1521  0.0411  34  ASP B OD2 
3243 N N   . PHE B 26  ? 0.3365 0.6652 0.6356 0.0216  0.1107  -0.0599 35  PHE B N   
3244 C CA  . PHE B 26  ? 0.3370 0.6465 0.6392 0.0398  0.0993  -0.0858 35  PHE B CA  
3245 C C   . PHE B 26  ? 0.3084 0.5599 0.6004 0.0362  0.0788  -0.0842 35  PHE B C   
3246 O O   . PHE B 26  ? 0.3026 0.5370 0.6117 0.0443  0.0654  -0.0944 35  PHE B O   
3247 C CB  . PHE B 26  ? 0.3629 0.6849 0.6406 0.0547  0.1069  -0.1057 35  PHE B CB  
3248 C CG  . PHE B 26  ? 0.3329 0.6450 0.6224 0.0751  0.0969  -0.1343 35  PHE B CG  
3249 C CD1 . PHE B 26  ? 0.3917 0.7427 0.7123 0.0899  0.1031  -0.1509 35  PHE B CD1 
3250 C CD2 . PHE B 26  ? 0.3455 0.6102 0.6183 0.0795  0.0809  -0.1443 35  PHE B CD2 
3251 C CE1 . PHE B 26  ? 0.4125 0.7511 0.7476 0.1103  0.0916  -0.1785 35  PHE B CE1 
3252 C CE2 . PHE B 26  ? 0.3653 0.6167 0.6525 0.0973  0.0693  -0.1691 35  PHE B CE2 
3253 C CZ  . PHE B 26  ? 0.3927 0.6791 0.7110 0.1135  0.0738  -0.1869 35  PHE B CZ  
3254 N N   . TYR B 27  ? 0.2963 0.5204 0.5616 0.0242  0.0765  -0.0698 36  TYR B N   
3255 C CA  . TYR B 27  ? 0.2809 0.4556 0.5324 0.0207  0.0604  -0.0674 36  TYR B CA  
3256 C C   . TYR B 27  ? 0.2841 0.4402 0.5450 0.0075  0.0512  -0.0518 36  TYR B C   
3257 O O   . TYR B 27  ? 0.2710 0.3909 0.5153 0.0037  0.0408  -0.0481 36  TYR B O   
3258 C CB  . TYR B 27  ? 0.2662 0.4226 0.4842 0.0186  0.0622  -0.0653 36  TYR B CB  
3259 C CG  . TYR B 27  ? 0.2343 0.4046 0.4421 0.0319  0.0670  -0.0839 36  TYR B CG  
3260 C CD1 . TYR B 27  ? 0.3017 0.4505 0.5126 0.0434  0.0557  -0.1017 36  TYR B CD1 
3261 C CD2 . TYR B 27  ? 0.3158 0.5215 0.5117 0.0335  0.0817  -0.0842 36  TYR B CD2 
3262 C CE1 . TYR B 27  ? 0.2793 0.4379 0.4834 0.0563  0.0572  -0.1223 36  TYR B CE1 
3263 C CE2 . TYR B 27  ? 0.3201 0.5395 0.5044 0.0475  0.0846  -0.1054 36  TYR B CE2 
3264 C CZ  . TYR B 27  ? 0.2791 0.4732 0.4688 0.0592  0.0714  -0.1261 36  TYR B CZ  
3265 O OH  . TYR B 27  ? 0.2887 0.4934 0.4696 0.0735  0.0715  -0.1501 36  TYR B OH  
3266 N N   . ASN B 28  ? 0.2921 0.4743 0.5807 0.0011  0.0544  -0.0441 37  ASN B N   
3267 C CA  . ASN B 28  ? 0.2902 0.4561 0.5914 -0.0112 0.0432  -0.0323 37  ASN B CA  
3268 C C   . ASN B 28  ? 0.2873 0.4167 0.5825 -0.0072 0.0246  -0.0388 37  ASN B C   
3269 O O   . ASN B 28  ? 0.3029 0.4059 0.5877 -0.0156 0.0152  -0.0316 37  ASN B O   
3270 C CB  . ASN B 28  ? 0.2956 0.4984 0.6365 -0.0167 0.0464  -0.0270 37  ASN B CB  
3271 C CG  . ASN B 28  ? 0.3087 0.5440 0.6569 -0.0287 0.0628  -0.0105 37  ASN B CG  
3272 O OD1 . ASN B 28  ? 0.3373 0.5625 0.6599 -0.0342 0.0690  -0.0010 37  ASN B OD1 
3273 N ND2 . ASN B 28  ? 0.2876 0.5643 0.6727 -0.0329 0.0696  -0.0055 37  ASN B ND2 
3274 N N   . ASP B 29  ? 0.2693 0.3979 0.5713 0.0063  0.0189  -0.0520 38  ASP B N   
3275 C CA  . ASP B 29  ? 0.3011 0.3968 0.5957 0.0102  0.0012  -0.0548 38  ASP B CA  
3276 C C   . ASP B 29  ? 0.3165 0.3775 0.5755 0.0076  -0.0012 -0.0514 38  ASP B C   
3277 O O   . ASP B 29  ? 0.3310 0.3674 0.5781 0.0045  -0.0130 -0.0471 38  ASP B O   
3278 C CB  . ASP B 29  ? 0.3235 0.4235 0.6352 0.0253  -0.0056 -0.0674 38  ASP B CB  
3279 C CG  . ASP B 29  ? 0.3485 0.4819 0.7001 0.0293  -0.0071 -0.0711 38  ASP B CG  
3280 O OD1 . ASP B 29  ? 0.3809 0.5261 0.7477 0.0185  -0.0093 -0.0623 38  ASP B OD1 
3281 O OD2 . ASP B 29  ? 0.4373 0.5855 0.8082 0.0437  -0.0071 -0.0840 38  ASP B OD2 
3282 N N   . TRP B 30  ? 0.3036 0.3657 0.5459 0.0095  0.0097  -0.0538 39  TRP B N   
3283 C CA  . TRP B 30  ? 0.3115 0.3465 0.5246 0.0062  0.0089  -0.0498 39  TRP B CA  
3284 C C   . TRP B 30  ? 0.3014 0.3289 0.5045 -0.0050 0.0101  -0.0387 39  TRP B C   
3285 O O   . TRP B 30  ? 0.3157 0.3194 0.5032 -0.0077 0.0028  -0.0355 39  TRP B O   
3286 C CB  . TRP B 30  ? 0.3139 0.3553 0.5144 0.0103  0.0187  -0.0554 39  TRP B CB  
3287 C CG  . TRP B 30  ? 0.3016 0.3435 0.5088 0.0220  0.0158  -0.0693 39  TRP B CG  
3288 C CD1 . TRP B 30  ? 0.2840 0.3176 0.5073 0.0296  0.0048  -0.0754 39  TRP B CD1 
3289 C CD2 . TRP B 30  ? 0.2699 0.3181 0.4681 0.0279  0.0216  -0.0797 39  TRP B CD2 
3290 N NE1 . TRP B 30  ? 0.3178 0.3500 0.5456 0.0400  0.0031  -0.0893 39  TRP B NE1 
3291 C CE2 . TRP B 30  ? 0.2954 0.3372 0.5075 0.0393  0.0132  -0.0938 39  TRP B CE2 
3292 C CE3 . TRP B 30  ? 0.2707 0.3288 0.4508 0.0252  0.0311  -0.0788 39  TRP B CE3 
3293 C CZ2 . TRP B 30  ? 0.3010 0.3448 0.5103 0.0480  0.0137  -0.1096 39  TRP B CZ2 
3294 C CZ3 . TRP B 30  ? 0.3021 0.3652 0.4764 0.0338  0.0320  -0.0938 39  TRP B CZ3 
3295 C CH2 . TRP B 30  ? 0.3297 0.3852 0.5190 0.0451  0.0231  -0.1104 39  TRP B CH2 
3296 N N   . MET B 31  ? 0.2945 0.3435 0.5077 -0.0112 0.0192  -0.0327 40  MET B N   
3297 C CA  . MET B 31  ? 0.3148 0.3555 0.5241 -0.0221 0.0191  -0.0214 40  MET B CA  
3298 C C   . MET B 31  ? 0.3204 0.3445 0.5370 -0.0268 0.0052  -0.0206 40  MET B C   
3299 O O   . MET B 31  ? 0.3229 0.3243 0.5249 -0.0304 -0.0001 -0.0183 40  MET B O   
3300 C CB  . MET B 31  ? 0.3221 0.3913 0.5466 -0.0295 0.0302  -0.0114 40  MET B CB  
3301 C CG  . MET B 31  ? 0.4479 0.5316 0.6561 -0.0261 0.0431  -0.0101 40  MET B CG  
3302 S SD  . MET B 31  ? 0.5507 0.6085 0.7290 -0.0283 0.0427  -0.0036 40  MET B SD  
3303 C CE  . MET B 31  ? 0.2730 0.3017 0.4564 -0.0374 0.0308  0.0043  40  MET B CE  
3304 N N   . PHE B 32  ? 0.2938 0.3299 0.5329 -0.0255 -0.0017 -0.0243 41  PHE B N   
3305 C CA  . PHE B 32  ? 0.3143 0.3360 0.5594 -0.0293 -0.0176 -0.0255 41  PHE B CA  
3306 C C   . PHE B 32  ? 0.3144 0.3068 0.5298 -0.0240 -0.0266 -0.0301 41  PHE B C   
3307 O O   . PHE B 32  ? 0.3300 0.3046 0.5347 -0.0278 -0.0350 -0.0307 41  PHE B O   
3308 C CB  . PHE B 32  ? 0.3197 0.3607 0.5943 -0.0269 -0.0256 -0.0292 41  PHE B CB  
3309 C CG  . PHE B 32  ? 0.2984 0.3233 0.5736 -0.0285 -0.0451 -0.0325 41  PHE B CG  
3310 C CD1 . PHE B 32  ? 0.3228 0.3418 0.6081 -0.0393 -0.0536 -0.0301 41  PHE B CD1 
3311 C CD2 . PHE B 32  ? 0.2731 0.2869 0.5370 -0.0191 -0.0565 -0.0377 41  PHE B CD2 
3312 C CE1 . PHE B 32  ? 0.3460 0.3503 0.6288 -0.0398 -0.0736 -0.0362 41  PHE B CE1 
3313 C CE2 . PHE B 32  ? 0.3536 0.3545 0.6125 -0.0199 -0.0752 -0.0405 41  PHE B CE2 
3314 C CZ  . PHE B 32  ? 0.3326 0.3294 0.5998 -0.0297 -0.0839 -0.0415 41  PHE B CZ  
3315 N N   . ILE B 33  ? 0.3241 0.3125 0.5272 -0.0152 -0.0250 -0.0334 42  ILE B N   
3316 C CA  . ILE B 33  ? 0.3265 0.2922 0.5028 -0.0113 -0.0315 -0.0342 42  ILE B CA  
3317 C C   . ILE B 33  ? 0.3279 0.2803 0.4817 -0.0141 -0.0246 -0.0321 42  ILE B C   
3318 O O   . ILE B 33  ? 0.3092 0.2470 0.4460 -0.0144 -0.0310 -0.0336 42  ILE B O   
3319 C CB  . ILE B 33  ? 0.3257 0.2892 0.4991 -0.0031 -0.0319 -0.0352 42  ILE B CB  
3320 C CG1 . ILE B 33  ? 0.3006 0.2746 0.4980 0.0020  -0.0420 -0.0380 42  ILE B CG1 
3321 C CG2 . ILE B 33  ? 0.3391 0.2822 0.4853 -0.0016 -0.0367 -0.0314 42  ILE B CG2 
3322 C CD1 . ILE B 33  ? 0.3166 0.2876 0.5197 0.0110  -0.0441 -0.0400 42  ILE B CD1 
3323 N N   . ALA B 34  ? 0.3306 0.2903 0.4848 -0.0151 -0.0124 -0.0299 43  ALA B N   
3324 C CA  . ALA B 34  ? 0.3397 0.2891 0.4766 -0.0166 -0.0063 -0.0274 43  ALA B CA  
3325 C C   . ALA B 34  ? 0.3657 0.3065 0.5049 -0.0221 -0.0108 -0.0262 43  ALA B C   
3326 O O   . ALA B 34  ? 0.3757 0.3014 0.4988 -0.0203 -0.0129 -0.0286 43  ALA B O   
3327 C CB  . ALA B 34  ? 0.3444 0.3060 0.4830 -0.0164 0.0052  -0.0249 43  ALA B CB  
3328 N N   . LYS B 35  ? 0.3490 0.3004 0.5109 -0.0286 -0.0126 -0.0229 44  LYS B N   
3329 C CA  . LYS B 35  ? 0.3695 0.3110 0.5410 -0.0358 -0.0195 -0.0208 44  LYS B CA  
3330 C C   . LYS B 35  ? 0.3884 0.3137 0.5547 -0.0343 -0.0349 -0.0305 44  LYS B C   
3331 O O   . LYS B 35  ? 0.3617 0.2714 0.5296 -0.0373 -0.0426 -0.0335 44  LYS B O   
3332 C CB  . LYS B 35  ? 0.3838 0.3444 0.5857 -0.0454 -0.0174 -0.0119 44  LYS B CB  
3333 C CG  . LYS B 35  ? 0.4432 0.4192 0.6469 -0.0485 -0.0031 -0.0003 44  LYS B CG  
3334 C CD  . LYS B 35  ? 0.3945 0.3951 0.6283 -0.0590 0.0009  0.0113  44  LYS B CD  
3335 C CE  . LYS B 35  ? 0.4080 0.4151 0.6426 -0.0661 0.0101  0.0277  44  LYS B CE  
3336 N NZ  . LYS B 35  ? 0.4180 0.4573 0.6803 -0.0766 0.0179  0.0419  44  LYS B NZ  
3337 N N   . HIS B 36  ? 0.3689 0.2976 0.5296 -0.0294 -0.0408 -0.0356 45  HIS B N   
3338 C CA  . HIS B 36  ? 0.3447 0.2622 0.4968 -0.0273 -0.0565 -0.0446 45  HIS B CA  
3339 C C   . HIS B 36  ? 0.3346 0.2450 0.4549 -0.0183 -0.0570 -0.0480 45  HIS B C   
3340 O O   . HIS B 36  ? 0.3226 0.2305 0.4334 -0.0152 -0.0694 -0.0527 45  HIS B O   
3341 C CB  . HIS B 36  ? 0.3352 0.2658 0.5132 -0.0311 -0.0671 -0.0448 45  HIS B CB  
3342 C CG  . HIS B 36  ? 0.3982 0.3362 0.6094 -0.0421 -0.0694 -0.0408 45  HIS B CG  
3343 N ND1 . HIS B 36  ? 0.4160 0.3402 0.6364 -0.0481 -0.0843 -0.0468 45  HIS B ND1 
3344 C CD2 . HIS B 36  ? 0.3643 0.3233 0.6025 -0.0489 -0.0587 -0.0305 45  HIS B CD2 
3345 C CE1 . HIS B 36  ? 0.4182 0.3531 0.6732 -0.0598 -0.0834 -0.0380 45  HIS B CE1 
3346 N NE2 . HIS B 36  ? 0.3634 0.3215 0.6282 -0.0605 -0.0667 -0.0271 45  HIS B NE2 
3347 N N   . LEU B 37  ? 0.3231 0.2317 0.4273 -0.0147 -0.0442 -0.0444 46  LEU B N   
3348 C CA  . LEU B 37  ? 0.3479 0.2528 0.4246 -0.0082 -0.0426 -0.0442 46  LEU B CA  
3349 C C   . LEU B 37  ? 0.3499 0.2461 0.4037 -0.0040 -0.0522 -0.0534 46  LEU B C   
3350 O O   . LEU B 37  ? 0.3710 0.2689 0.4080 -0.0005 -0.0589 -0.0524 46  LEU B O   
3351 C CB  . LEU B 37  ? 0.3608 0.2665 0.4283 -0.0065 -0.0282 -0.0395 46  LEU B CB  
3352 C CG  . LEU B 37  ? 0.3629 0.2770 0.4418 -0.0076 -0.0199 -0.0323 46  LEU B CG  
3353 C CD1 . LEU B 37  ? 0.3356 0.2495 0.4037 -0.0061 -0.0092 -0.0295 46  LEU B CD1 
3354 C CD2 . LEU B 37  ? 0.4308 0.3474 0.5122 -0.0057 -0.0255 -0.0285 46  LEU B CD2 
3355 N N   . PRO B 38  ? 0.3616 0.2486 0.4143 -0.0034 -0.0540 -0.0628 47  PRO B N   
3356 C CA  . PRO B 38  ? 0.3831 0.2631 0.4135 0.0027  -0.0642 -0.0761 47  PRO B CA  
3357 C C   . PRO B 38  ? 0.4089 0.2897 0.4389 0.0018  -0.0820 -0.0808 47  PRO B C   
3358 O O   . PRO B 38  ? 0.4363 0.3194 0.4377 0.0081  -0.0881 -0.0852 47  PRO B O   
3359 C CB  . PRO B 38  ? 0.3713 0.2379 0.4134 0.0024  -0.0671 -0.0865 47  PRO B CB  
3360 C CG  . PRO B 38  ? 0.3696 0.2385 0.4268 -0.0012 -0.0535 -0.0755 47  PRO B CG  
3361 C CD  . PRO B 38  ? 0.3536 0.2354 0.4241 -0.0072 -0.0483 -0.0621 47  PRO B CD  
3362 N N   . ASP B 39  ? 0.3833 0.2654 0.4450 -0.0060 -0.0899 -0.0787 48  ASP B N   
3363 C CA  . ASP B 39  ? 0.4050 0.2897 0.4738 -0.0076 -0.1089 -0.0835 48  ASP B CA  
3364 C C   . ASP B 39  ? 0.3759 0.2715 0.4354 -0.0043 -0.1101 -0.0732 48  ASP B C   
3365 O O   . ASP B 39  ? 0.3943 0.2910 0.4369 -0.0003 -0.1248 -0.0769 48  ASP B O   
3366 C CB  . ASP B 39  ? 0.3999 0.2879 0.5115 -0.0180 -0.1152 -0.0818 48  ASP B CB  
3367 C CG  . ASP B 39  ? 0.4350 0.3088 0.5606 -0.0231 -0.1177 -0.0891 48  ASP B CG  
3368 O OD1 . ASP B 39  ? 0.4479 0.3064 0.5539 -0.0175 -0.1265 -0.1042 48  ASP B OD1 
3369 O OD2 . ASP B 39  ? 0.4144 0.2927 0.5711 -0.0322 -0.1112 -0.0794 48  ASP B OD2 
3370 N N   . LEU B 40  ? 0.3572 0.2601 0.4282 -0.0055 -0.0963 -0.0606 49  LEU B N   
3371 C CA  . LEU B 40  ? 0.3711 0.2808 0.4401 -0.0022 -0.0984 -0.0502 49  LEU B CA  
3372 C C   . LEU B 40  ? 0.3823 0.2884 0.4132 0.0035  -0.0963 -0.0446 49  LEU B C   
3373 O O   . LEU B 40  ? 0.3837 0.2917 0.4035 0.0066  -0.1075 -0.0382 49  LEU B O   
3374 C CB  . LEU B 40  ? 0.2945 0.2118 0.3886 -0.0040 -0.0856 -0.0419 49  LEU B CB  
3375 C CG  . LEU B 40  ? 0.3408 0.2702 0.4738 -0.0092 -0.0870 -0.0442 49  LEU B CG  
3376 C CD1 . LEU B 40  ? 0.3004 0.2395 0.4501 -0.0091 -0.0714 -0.0390 49  LEU B CD1 
3377 C CD2 . LEU B 40  ? 0.3135 0.2517 0.4656 -0.0080 -0.1049 -0.0455 49  LEU B CD2 
3378 N N   . ILE B 41  ? 0.3871 0.2901 0.3992 0.0048  -0.0826 -0.0458 50  ILE B N   
3379 C CA  . ILE B 41  ? 0.4127 0.3178 0.3895 0.0093  -0.0780 -0.0397 50  ILE B CA  
3380 C C   . ILE B 41  ? 0.4495 0.3555 0.3973 0.0144  -0.0919 -0.0491 50  ILE B C   
3381 O O   . ILE B 41  ? 0.4942 0.4054 0.4192 0.0171  -0.0980 -0.0393 50  ILE B O   
3382 C CB  . ILE B 41  ? 0.4077 0.3141 0.3752 0.0102  -0.0595 -0.0400 50  ILE B CB  
3383 C CG1 . ILE B 41  ? 0.4048 0.3115 0.3961 0.0056  -0.0479 -0.0299 50  ILE B CG1 
3384 C CG2 . ILE B 41  ? 0.4389 0.3538 0.3708 0.0145  -0.0537 -0.0335 50  ILE B CG2 
3385 C CD1 . ILE B 41  ? 0.4236 0.3314 0.4162 0.0056  -0.0330 -0.0329 50  ILE B CD1 
3386 N N   A GLU B 42  ? 0.4634 0.3640 0.4125 0.0157  -0.0983 -0.0677 51  GLU B N   
3387 N N   B GLU B 42  ? 0.4583 0.3589 0.4071 0.0158  -0.0982 -0.0678 51  GLU B N   
3388 C CA  A GLU B 42  ? 0.4895 0.3903 0.4102 0.0220  -0.1131 -0.0824 51  GLU B CA  
3389 C CA  B GLU B 42  ? 0.4901 0.3908 0.4109 0.0220  -0.1135 -0.0827 51  GLU B CA  
3390 C C   A GLU B 42  ? 0.4963 0.4001 0.4170 0.0215  -0.1344 -0.0794 51  GLU B C   
3391 C C   B GLU B 42  ? 0.4948 0.3987 0.4152 0.0215  -0.1342 -0.0788 51  GLU B C   
3392 O O   A GLU B 42  ? 0.5133 0.4226 0.3989 0.0276  -0.1451 -0.0829 51  GLU B O   
3393 O O   B GLU B 42  ? 0.5133 0.4232 0.3983 0.0275  -0.1442 -0.0809 51  GLU B O   
3394 C CB  A GLU B 42  ? 0.5090 0.3985 0.4400 0.0229  -0.1190 -0.1048 51  GLU B CB  
3395 C CB  B GLU B 42  ? 0.5027 0.3919 0.4349 0.0226  -0.1206 -0.1053 51  GLU B CB  
3396 C CG  A GLU B 42  ? 0.5838 0.4731 0.4794 0.0327  -0.1301 -0.1256 51  GLU B CG  
3397 C CG  B GLU B 42  ? 0.5622 0.4508 0.4602 0.0319  -0.1346 -0.1265 51  GLU B CG  
3398 C CD  A GLU B 42  ? 0.6569 0.5554 0.5195 0.0419  -0.1123 -0.1282 51  GLU B CD  
3399 C CD  B GLU B 42  ? 0.5859 0.4585 0.5042 0.0309  -0.1510 -0.1498 51  GLU B CD  
3400 O OE1 A GLU B 42  ? 0.7061 0.5980 0.5805 0.0441  -0.1020 -0.1370 51  GLU B OE1 
3401 O OE1 B GLU B 42  ? 0.5883 0.4495 0.5351 0.0265  -0.1440 -0.1519 51  GLU B OE1 
3402 O OE2 A GLU B 42  ? 0.6811 0.5955 0.5077 0.0470  -0.1087 -0.1200 51  GLU B OE2 
3403 O OE2 B GLU B 42  ? 0.6099 0.4806 0.5158 0.0341  -0.1727 -0.1655 51  GLU B OE2 
3404 N N   . SER B 43  ? 0.4590 0.3618 0.4183 0.0151  -0.1406 -0.0731 52  SER B N   
3405 C CA  . SER B 43  ? 0.4815 0.3892 0.4493 0.0151  -0.1612 -0.0690 52  SER B CA  
3406 C C   . SER B 43  ? 0.4642 0.3769 0.4249 0.0172  -0.1600 -0.0473 52  SER B C   
3407 O O   . SER B 43  ? 0.4737 0.3901 0.4388 0.0190  -0.1782 -0.0420 52  SER B O   
3408 C CB  . SER B 43  ? 0.4518 0.3607 0.4693 0.0081  -0.1689 -0.0733 52  SER B CB  
3409 O OG  . SER B 43  ? 0.3988 0.3108 0.4445 0.0043  -0.1516 -0.0623 52  SER B OG  
3410 N N   . GLY B 44  ? 0.4629 0.3747 0.4155 0.0168  -0.1408 -0.0344 53  GLY B N   
3411 C CA  . GLY B 44  ? 0.4821 0.3945 0.4337 0.0174  -0.1403 -0.0127 53  GLY B CA  
3412 C C   . GLY B 44  ? 0.4674 0.3787 0.4640 0.0158  -0.1447 -0.0085 53  GLY B C   
3413 O O   . GLY B 44  ? 0.4323 0.3422 0.4349 0.0184  -0.1546 0.0055  53  GLY B O   
3414 N N   . GLN B 45  ? 0.4470 0.3600 0.4753 0.0123  -0.1373 -0.0202 54  GLN B N   
3415 C CA  . GLN B 45  ? 0.4319 0.3505 0.5039 0.0119  -0.1391 -0.0197 54  GLN B CA  
3416 C C   . GLN B 45  ? 0.3806 0.2982 0.4683 0.0105  -0.1196 -0.0163 54  GLN B C   
3417 O O   . GLN B 45  ? 0.3373 0.2609 0.4572 0.0123  -0.1191 -0.0162 54  GLN B O   
3418 C CB  . GLN B 45  ? 0.4437 0.3709 0.5431 0.0080  -0.1457 -0.0336 54  GLN B CB  
3419 C CG  . GLN B 45  ? 0.5270 0.4565 0.6199 0.0092  -0.1694 -0.0397 54  GLN B CG  
3420 C CD  . GLN B 45  ? 0.6058 0.5446 0.7244 0.0134  -0.1872 -0.0341 54  GLN B CD  
3421 O OE1 . GLN B 45  ? 0.6543 0.5983 0.7770 0.0138  -0.2081 -0.0400 54  GLN B OE1 
3422 N NE2 . GLN B 45  ? 0.6539 0.5944 0.7918 0.0175  -0.1808 -0.0242 54  GLN B NE2 
3423 N N   . LEU B 46  ? 0.3812 0.2932 0.4469 0.0082  -0.1043 -0.0148 55  LEU B N   
3424 C CA  . LEU B 46  ? 0.3793 0.2910 0.4582 0.0064  -0.0873 -0.0135 55  LEU B CA  
3425 C C   . LEU B 46  ? 0.3801 0.2877 0.4722 0.0096  -0.0892 -0.0037 55  LEU B C   
3426 O O   . LEU B 46  ? 0.3228 0.2348 0.4421 0.0112  -0.0841 -0.0082 55  LEU B O   
3427 C CB  . LEU B 46  ? 0.3719 0.2795 0.4246 0.0041  -0.0734 -0.0128 55  LEU B CB  
3428 C CG  . LEU B 46  ? 0.3927 0.3005 0.4537 0.0019  -0.0569 -0.0120 55  LEU B CG  
3429 C CD1 . LEU B 46  ? 0.4441 0.3465 0.5028 0.0020  -0.0543 0.0005  55  LEU B CD1 
3430 C CD2 . LEU B 46  ? 0.3726 0.2876 0.4633 0.0009  -0.0526 -0.0193 55  LEU B CD2 
3431 N N   . ARG B 47  ? 0.4119 0.3113 0.4847 0.0108  -0.0966 0.0098  56  ARG B N   
3432 C CA  . ARG B 47  ? 0.4485 0.3389 0.5356 0.0130  -0.1007 0.0212  56  ARG B CA  
3433 C C   . ARG B 47  ? 0.4300 0.3228 0.5513 0.0198  -0.1138 0.0164  56  ARG B C   
3434 O O   . ARG B 47  ? 0.4450 0.3354 0.5923 0.0233  -0.1111 0.0127  56  ARG B O   
3435 C CB  . ARG B 47  ? 0.4814 0.3634 0.5411 0.0112  -0.1067 0.0411  56  ARG B CB  
3436 C CG  . ARG B 47  ? 0.5155 0.3985 0.5533 0.0051  -0.0897 0.0461  56  ARG B CG  
3437 C CD  . ARG B 47  ? 0.5456 0.4305 0.5487 0.0025  -0.0912 0.0638  56  ARG B CD  
3438 N NE  . ARG B 47  ? 0.5286 0.4173 0.5210 -0.0034 -0.0742 0.0708  56  ARG B NE  
3439 C CZ  . ARG B 47  ? 0.5026 0.3997 0.4652 -0.0068 -0.0689 0.0866  56  ARG B CZ  
3440 N NH1 . ARG B 47  ? 0.4311 0.3332 0.3657 -0.0045 -0.0792 0.0969  56  ARG B NH1 
3441 N NH2 . ARG B 47  ? 0.4920 0.3958 0.4528 -0.0124 -0.0527 0.0922  56  ARG B NH2 
3442 N N   . GLU B 48  ? 0.4460 0.3459 0.5689 0.0223  -0.1278 0.0139  57  GLU B N   
3443 C CA  . GLU B 48  ? 0.4530 0.3609 0.6123 0.0293  -0.1406 0.0081  57  GLU B CA  
3444 C C   . GLU B 48  ? 0.4006 0.3238 0.5915 0.0302  -0.1274 -0.0076 57  GLU B C   
3445 O O   . GLU B 48  ? 0.3868 0.3147 0.6092 0.0378  -0.1293 -0.0125 57  GLU B O   
3446 C CB  . GLU B 48  ? 0.4533 0.3695 0.6085 0.0301  -0.1581 0.0066  57  GLU B CB  
3447 C CG  . GLU B 48  ? 0.5118 0.4409 0.7088 0.0375  -0.1726 0.0009  57  GLU B CG  
3448 C CD  . GLU B 48  ? 0.6153 0.5503 0.8071 0.0385  -0.1950 0.0024  57  GLU B CD  
3449 O OE1 . GLU B 48  ? 0.8225 0.7592 0.9889 0.0323  -0.1958 -0.0023 57  GLU B OE1 
3450 O OE2 . GLU B 48  ? 0.7947 0.7324 1.0093 0.0466  -0.2134 0.0069  57  GLU B OE2 
3451 N N   . ARG B 49  ? 0.3666 0.2981 0.5489 0.0232  -0.1144 -0.0153 58  ARG B N   
3452 C CA  . ARG B 49  ? 0.3446 0.2936 0.5528 0.0224  -0.1006 -0.0265 58  ARG B CA  
3453 C C   . ARG B 49  ? 0.3360 0.2816 0.5501 0.0261  -0.0885 -0.0288 58  ARG B C   
3454 O O   . ARG B 49  ? 0.3246 0.2853 0.5670 0.0321  -0.0841 -0.0380 58  ARG B O   
3455 C CB  . ARG B 49  ? 0.3196 0.2731 0.5153 0.0132  -0.0906 -0.0303 58  ARG B CB  
3456 C CG  . ARG B 49  ? 0.3670 0.3282 0.5702 0.0091  -0.1026 -0.0336 58  ARG B CG  
3457 C CD  . ARG B 49  ? 0.3868 0.3724 0.6334 0.0105  -0.1055 -0.0388 58  ARG B CD  
3458 N NE  . ARG B 49  ? 0.3344 0.3227 0.5966 0.0188  -0.1233 -0.0373 58  ARG B NE  
3459 C CZ  . ARG B 49  ? 0.4204 0.4298 0.7224 0.0253  -0.1264 -0.0415 58  ARG B CZ  
3460 N NH1 . ARG B 49  ? 0.3466 0.3807 0.6768 0.0244  -0.1109 -0.0477 58  ARG B NH1 
3461 N NH2 . ARG B 49  ? 0.4383 0.4461 0.7521 0.0338  -0.1456 -0.0390 58  ARG B NH2 
3462 N N   . VAL B 50  ? 0.3402 0.2683 0.5282 0.0229  -0.0836 -0.0216 59  VAL B N   
3463 C CA  . VAL B 50  ? 0.3415 0.2633 0.5342 0.0253  -0.0755 -0.0239 59  VAL B CA  
3464 C C   . VAL B 50  ? 0.3511 0.2658 0.5683 0.0349  -0.0881 -0.0246 59  VAL B C   
3465 O O   . VAL B 50  ? 0.3290 0.2496 0.5675 0.0416  -0.0838 -0.0365 59  VAL B O   
3466 C CB  . VAL B 50  ? 0.3173 0.2233 0.4809 0.0185  -0.0695 -0.0138 59  VAL B CB  
3467 C CG1 . VAL B 50  ? 0.3394 0.2356 0.5121 0.0202  -0.0667 -0.0149 59  VAL B CG1 
3468 C CG2 . VAL B 50  ? 0.3318 0.2457 0.4777 0.0119  -0.0560 -0.0171 59  VAL B CG2 
3469 N N   . GLU B 51  ? 0.4015 0.3037 0.6153 0.0366  -0.1046 -0.0125 60  GLU B N   
3470 C CA  . GLU B 51  ? 0.4216 0.3132 0.6609 0.0465  -0.1204 -0.0107 60  GLU B CA  
3471 C C   . GLU B 51  ? 0.4036 0.3157 0.6804 0.0577  -0.1240 -0.0266 60  GLU B C   
3472 O O   . GLU B 51  ? 0.3855 0.2929 0.6900 0.0687  -0.1311 -0.0339 60  GLU B O   
3473 C CB  . GLU B 51  ? 0.4420 0.3173 0.6657 0.0449  -0.1381 0.0097  60  GLU B CB  
3474 C CG  . GLU B 51  ? 0.4609 0.3179 0.6546 0.0353  -0.1340 0.0273  60  GLU B CG  
3475 C CD  . GLU B 51  ? 0.4949 0.3473 0.6569 0.0304  -0.1436 0.0476  60  GLU B CD  
3476 O OE1 . GLU B 51  ? 0.5380 0.3859 0.6714 0.0217  -0.1347 0.0598  60  GLU B OE1 
3477 O OE2 . GLU B 51  ? 0.5425 0.3983 0.7077 0.0355  -0.1597 0.0510  60  GLU B OE2 
3478 N N   . LYS B 52  ? 0.4042 0.3397 0.6842 0.0548  -0.1190 -0.0324 61  LYS B N   
3479 C CA  . LYS B 52  ? 0.4084 0.3718 0.7265 0.0634  -0.1192 -0.0461 61  LYS B CA  
3480 C C   . LYS B 52  ? 0.3681 0.3527 0.7002 0.0665  -0.0996 -0.0623 61  LYS B C   
3481 O O   . LYS B 52  ? 0.3822 0.3932 0.7478 0.0758  -0.0976 -0.0747 61  LYS B O   
3482 C CB  . LYS B 52  ? 0.4151 0.3967 0.7358 0.0571  -0.1237 -0.0439 61  LYS B CB  
3483 C CG  . LYS B 52  ? 0.5092 0.4894 0.8455 0.0635  -0.1474 -0.0381 61  LYS B CG  
3484 C CD  . LYS B 52  ? 0.6077 0.5571 0.9124 0.0619  -0.1625 -0.0210 61  LYS B CD  
3485 C CE  . LYS B 52  ? 0.6241 0.5728 0.9448 0.0698  -0.1883 -0.0139 61  LYS B CE  
3486 N NZ  . LYS B 52  ? 0.6534 0.6170 0.9678 0.0633  -0.1966 -0.0142 61  LYS B NZ  
3487 N N   . LEU B 53  ? 0.3534 0.3302 0.6603 0.0592  -0.0853 -0.0621 62  LEU B N   
3488 C CA  . LEU B 53  ? 0.3275 0.3239 0.6413 0.0623  -0.0677 -0.0763 62  LEU B CA  
3489 C C   . LEU B 53  ? 0.3433 0.3420 0.6838 0.0783  -0.0719 -0.0921 62  LEU B C   
3490 O O   . LEU B 53  ? 0.3327 0.3035 0.6758 0.0835  -0.0863 -0.0895 62  LEU B O   
3491 C CB  . LEU B 53  ? 0.3430 0.3250 0.6250 0.0533  -0.0566 -0.0726 62  LEU B CB  
3492 C CG  . LEU B 53  ? 0.3424 0.3256 0.5989 0.0396  -0.0478 -0.0624 62  LEU B CG  
3493 C CD1 . LEU B 53  ? 0.3541 0.3234 0.5854 0.0342  -0.0391 -0.0602 62  LEU B CD1 
3494 C CD2 . LEU B 53  ? 0.3907 0.4054 0.6600 0.0364  -0.0361 -0.0664 62  LEU B CD2 
3495 N N   . ASN B 54  ? 0.3323 0.3651 0.6931 0.0862  -0.0595 -0.1081 63  ASN B N   
3496 C CA  . ASN B 54  ? 0.3557 0.3951 0.7350 0.1022  -0.0581 -0.1291 63  ASN B CA  
3497 C C   . ASN B 54  ? 0.3581 0.3876 0.7100 0.0977  -0.0475 -0.1340 63  ASN B C   
3498 O O   . ASN B 54  ? 0.3268 0.3617 0.6526 0.0842  -0.0350 -0.1241 63  ASN B O   
3499 C CB  . ASN B 54  ? 0.3811 0.4684 0.7887 0.1125  -0.0456 -0.1448 63  ASN B CB  
3500 C CG  . ASN B 54  ? 0.4150 0.5188 0.8562 0.1173  -0.0560 -0.1412 63  ASN B CG  
3501 O OD1 . ASN B 54  ? 0.4517 0.5909 0.9052 0.1116  -0.0457 -0.1377 63  ASN B OD1 
3502 N ND2 . ASN B 54  ? 0.4016 0.4801 0.8599 0.1271  -0.0778 -0.1408 63  ASN B ND2 
3503 N N   . MET B 55  ? 0.3621 0.3762 0.7221 0.1093  -0.0545 -0.1498 64  MET B N   
3504 C CA  . MET B 55  ? 0.3757 0.3837 0.7147 0.1072  -0.0469 -0.1591 64  MET B CA  
3505 C C   . MET B 55  ? 0.3575 0.4092 0.6918 0.1116  -0.0264 -0.1737 64  MET B C   
3506 O O   . MET B 55  ? 0.3605 0.4392 0.7175 0.1278  -0.0230 -0.1942 64  MET B O   
3507 C CB  . MET B 55  ? 0.4001 0.3806 0.7546 0.1194  -0.0625 -0.1755 64  MET B CB  
3508 C CG  . MET B 55  ? 0.3863 0.3493 0.7185 0.1126  -0.0611 -0.1794 64  MET B CG  
3509 S SD  . MET B 55  ? 0.5125 0.4398 0.8690 0.1254  -0.0831 -0.1998 64  MET B SD  
3510 C CE  . MET B 55  ? 0.4943 0.3781 0.8650 0.1175  -0.1049 -0.1717 64  MET B CE  
3511 N N   . LEU B 56  ? 0.3290 0.3891 0.6342 0.0978  -0.0128 -0.1624 65  LEU B N   
3512 C CA  . LEU B 56  ? 0.3318 0.4334 0.6276 0.0992  0.0069  -0.1701 65  LEU B CA  
3513 C C   . LEU B 56  ? 0.3540 0.4522 0.6287 0.1028  0.0096  -0.1847 65  LEU B C   
3514 O O   . LEU B 56  ? 0.3501 0.4171 0.6071 0.0939  0.0024  -0.1770 65  LEU B O   
3515 C CB  . LEU B 56  ? 0.3093 0.4237 0.5897 0.0819  0.0186  -0.1469 65  LEU B CB  
3516 C CG  . LEU B 56  ? 0.2699 0.3909 0.5712 0.0767  0.0151  -0.1336 65  LEU B CG  
3517 C CD1 . LEU B 56  ? 0.3231 0.4480 0.6086 0.0587  0.0232  -0.1123 65  LEU B CD1 
3518 C CD2 . LEU B 56  ? 0.3367 0.4981 0.6709 0.0890  0.0211  -0.1463 65  LEU B CD2 
3519 N N   . SER B 57  ? 0.3644 0.4980 0.6419 0.1165  0.0199  -0.2066 66  SER B N   
3520 C CA  . SER B 57  ? 0.3840 0.5223 0.6391 0.1215  0.0228  -0.2235 66  SER B CA  
3521 C C   . SER B 57  ? 0.3844 0.5288 0.6063 0.1049  0.0338  -0.2033 66  SER B C   
3522 O O   . SER B 57  ? 0.3649 0.5305 0.5833 0.0948  0.0463  -0.1836 66  SER B O   
3523 C CB  . SER B 57  ? 0.3992 0.5828 0.6613 0.1409  0.0340  -0.2511 66  SER B CB  
3524 O OG  . SER B 57  ? 0.4129 0.6089 0.6463 0.1446  0.0389  -0.2657 66  SER B OG  
3525 N N   . ILE B 58  ? 0.3822 0.5071 0.5832 0.1021  0.0274  -0.2079 67  ILE B N   
3526 C CA  . ILE B 58  ? 0.3815 0.5136 0.5520 0.0893  0.0361  -0.1915 67  ILE B CA  
3527 C C   . ILE B 58  ? 0.3937 0.5689 0.5432 0.0968  0.0498  -0.2036 67  ILE B C   
3528 O O   . ILE B 58  ? 0.3673 0.5509 0.4906 0.0877  0.0559  -0.1900 67  ILE B O   
3529 C CB  . ILE B 58  ? 0.3959 0.4898 0.5548 0.0809  0.0225  -0.1872 67  ILE B CB  
3530 C CG1 . ILE B 58  ? 0.4241 0.5090 0.5841 0.0927  0.0102  -0.2159 67  ILE B CG1 
3531 C CG2 . ILE B 58  ? 0.3792 0.4364 0.5535 0.0718  0.0120  -0.1706 67  ILE B CG2 
3532 C CD1 . ILE B 58  ? 0.4295 0.4971 0.5720 0.0839  0.0025  -0.2122 67  ILE B CD1 
3533 N N   . ASP B 59  ? 0.4275 0.6310 0.5879 0.1144  0.0541  -0.2290 68  ASP B N   
3534 C CA  . ASP B 59  ? 0.4619 0.7103 0.5996 0.1248  0.0669  -0.2451 68  ASP B CA  
3535 C C   . ASP B 59  ? 0.4495 0.7415 0.5735 0.1153  0.0888  -0.2206 68  ASP B C   
3536 O O   . ASP B 59  ? 0.4495 0.7765 0.5455 0.1183  0.0999  -0.2234 68  ASP B O   
3537 C CB  . ASP B 59  ? 0.4959 0.7658 0.6516 0.1486  0.0664  -0.2817 68  ASP B CB  
3538 C CG  . ASP B 59  ? 0.5407 0.7687 0.7077 0.1595  0.0429  -0.3097 68  ASP B CG  
3539 O OD1 . ASP B 59  ? 0.5908 0.7783 0.7499 0.1480  0.0284  -0.3008 68  ASP B OD1 
3540 O OD2 . ASP B 59  ? 0.6120 0.8487 0.7992 0.1800  0.0383  -0.3410 68  ASP B OD2 
3541 N N   . HIS B 60  ? 0.4318 0.7211 0.5754 0.1031  0.0937  -0.1958 69  HIS B N   
3542 C CA  . HIS B 60  ? 0.4331 0.7574 0.5704 0.0903  0.1117  -0.1682 69  HIS B CA  
3543 C C   . HIS B 60  ? 0.4206 0.7202 0.5368 0.0712  0.1087  -0.1389 69  HIS B C   
3544 O O   . HIS B 60  ? 0.4210 0.7400 0.5353 0.0583  0.1200  -0.1127 69  HIS B O   
3545 C CB  . HIS B 60  ? 0.4429 0.7799 0.6167 0.0872  0.1168  -0.1586 69  HIS B CB  
3546 C CG  . HIS B 60  ? 0.4474 0.8054 0.6476 0.1073  0.1173  -0.1875 69  HIS B CG  
3547 N ND1 . HIS B 60  ? 0.5164 0.9298 0.7145 0.1217  0.1339  -0.2047 69  HIS B ND1 
3548 C CD2 . HIS B 60  ? 0.4831 0.8142 0.7120 0.1171  0.1023  -0.2031 69  HIS B CD2 
3549 C CE1 . HIS B 60  ? 0.5384 0.9582 0.7658 0.1405  0.1293  -0.2317 69  HIS B CE1 
3550 N NE2 . HIS B 60  ? 0.5478 0.9163 0.7948 0.1378  0.1092  -0.2302 69  HIS B NE2 
3551 N N   . LEU B 61  ? 0.3857 0.6437 0.4898 0.0695  0.0932  -0.1432 70  LEU B N   
3552 C CA  . LEU B 61  ? 0.3907 0.6292 0.4731 0.0558  0.0897  -0.1212 70  LEU B CA  
3553 C C   . LEU B 61  ? 0.4243 0.6831 0.4746 0.0621  0.0915  -0.1309 70  LEU B C   
3554 O O   . LEU B 61  ? 0.4340 0.6731 0.4758 0.0689  0.0786  -0.1501 70  LEU B O   
3555 C CB  . LEU B 61  ? 0.3614 0.5492 0.4513 0.0505  0.0730  -0.1198 70  LEU B CB  
3556 C CG  . LEU B 61  ? 0.3639 0.5300 0.4801 0.0451  0.0688  -0.1110 70  LEU B CG  
3557 C CD1 . LEU B 61  ? 0.3794 0.5019 0.5011 0.0439  0.0528  -0.1152 70  LEU B CD1 
3558 C CD2 . LEU B 61  ? 0.3061 0.4751 0.4238 0.0306  0.0755  -0.0833 70  LEU B CD2 
3559 N N   . THR B 62  ? 0.4366 0.7354 0.4697 0.0588  0.1065  -0.1159 71  THR B N   
3560 C CA  . THR B 62  ? 0.4809 0.8153 0.4819 0.0685  0.1122  -0.1282 71  THR B CA  
3561 C C   . THR B 62  ? 0.4929 0.8188 0.4632 0.0612  0.1055  -0.1129 71  THR B C   
3562 O O   . THR B 62  ? 0.5237 0.8764 0.4637 0.0697  0.1066  -0.1243 71  THR B O   
3563 C CB  . THR B 62  ? 0.4956 0.8884 0.4925 0.0700  0.1345  -0.1189 71  THR B CB  
3564 O OG1 . THR B 62  ? 0.5172 0.9143 0.5145 0.0513  0.1423  -0.0792 71  THR B OG1 
3565 C CG2 . THR B 62  ? 0.4921 0.9010 0.5230 0.0789  0.1418  -0.1351 71  THR B CG2 
3566 N N   . ASP B 63  ? 0.4677 0.7591 0.4451 0.0469  0.0982  -0.0883 72  ASP B N   
3567 C CA  . ASP B 63  ? 0.4683 0.7480 0.4224 0.0408  0.0897  -0.0733 72  ASP B CA  
3568 C C   . ASP B 63  ? 0.4387 0.6692 0.4084 0.0340  0.0746  -0.0694 72  ASP B C   
3569 O O   . ASP B 63  ? 0.4086 0.6146 0.4042 0.0317  0.0722  -0.0724 72  ASP B O   
3570 C CB  . ASP B 63  ? 0.4871 0.7907 0.4279 0.0297  0.1008  -0.0384 72  ASP B CB  
3571 C CG  . ASP B 63  ? 0.4954 0.7856 0.4646 0.0162  0.1065  -0.0136 72  ASP B CG  
3572 O OD1 . ASP B 63  ? 0.4629 0.7143 0.4545 0.0124  0.0973  -0.0157 72  ASP B OD1 
3573 O OD2 . ASP B 63  ? 0.5653 0.8856 0.5342 0.0087  0.1198  0.0089  72  ASP B OD2 
3574 N N   . HIS B 64  ? 0.4277 0.6475 0.3811 0.0315  0.0645  -0.0622 73  HIS B N   
3575 C CA  . HIS B 64  ? 0.4025 0.5827 0.3694 0.0266  0.0511  -0.0599 73  HIS B CA  
3576 C C   . HIS B 64  ? 0.3648 0.5212 0.3525 0.0162  0.0537  -0.0387 73  HIS B C   
3577 O O   . HIS B 64  ? 0.3508 0.4785 0.3571 0.0146  0.0474  -0.0444 73  HIS B O   
3578 C CB  . HIS B 64  ? 0.4306 0.6112 0.3778 0.0262  0.0407  -0.0532 73  HIS B CB  
3579 C CG  . HIS B 64  ? 0.4018 0.5490 0.3649 0.0223  0.0281  -0.0524 73  HIS B CG  
3580 N ND1 . HIS B 64  ? 0.4595 0.5909 0.4345 0.0260  0.0175  -0.0747 73  HIS B ND1 
3581 C CD2 . HIS B 64  ? 0.4273 0.5558 0.3988 0.0154  0.0248  -0.0320 73  HIS B CD2 
3582 C CE1 . HIS B 64  ? 0.4742 0.5825 0.4635 0.0205  0.0100  -0.0662 73  HIS B CE1 
3583 N NE2 . HIS B 64  ? 0.4200 0.5265 0.4068 0.0154  0.0144  -0.0422 73  HIS B NE2 
3584 N N   . LYS B 65  ? 0.3568 0.5254 0.3418 0.0088  0.0622  -0.0142 74  LYS B N   
3585 C CA  . LYS B 65  ? 0.3652 0.5105 0.3707 -0.0008 0.0626  0.0041  74  LYS B CA  
3586 C C   . LYS B 65  ? 0.3319 0.4717 0.3599 -0.0012 0.0671  -0.0050 74  LYS B C   
3587 O O   . LYS B 65  ? 0.3050 0.4165 0.3489 -0.0049 0.0616  -0.0034 74  LYS B O   
3588 C CB  . LYS B 65  ? 0.3750 0.5323 0.3759 -0.0098 0.0680  0.0336  74  LYS B CB  
3589 C CG  . LYS B 65  ? 0.4182 0.5700 0.4027 -0.0104 0.0593  0.0476  74  LYS B CG  
3590 C CD  . LYS B 65  ? 0.4342 0.5837 0.4232 -0.0208 0.0604  0.0798  74  LYS B CD  
3591 C CE  . LYS B 65  ? 0.4505 0.5988 0.4221 -0.0197 0.0509  0.0951  74  LYS B CE  
3592 N NZ  . LYS B 65  ? 0.4455 0.5861 0.4255 -0.0299 0.0494  0.1281  74  LYS B NZ  
3593 N N   . SER B 66  ? 0.3466 0.5151 0.3758 0.0036  0.0765  -0.0152 75  SER B N   
3594 C CA  . SER B 66  ? 0.3680 0.5331 0.4210 0.0052  0.0788  -0.0255 75  SER B CA  
3595 C C   . SER B 66  ? 0.3493 0.4859 0.4097 0.0117  0.0675  -0.0459 75  SER B C   
3596 O O   . SER B 66  ? 0.3557 0.4714 0.4340 0.0092  0.0634  -0.0460 75  SER B O   
3597 C CB  . SER B 66  ? 0.3747 0.5808 0.4306 0.0112  0.0915  -0.0338 75  SER B CB  
3598 O OG  . SER B 66  ? 0.5199 0.7449 0.5568 0.0236  0.0920  -0.0549 75  SER B OG  
3599 N N   . GLN B 67  ? 0.3553 0.4915 0.4019 0.0191  0.0616  -0.0617 76  GLN B N   
3600 C CA  . GLN B 67  ? 0.3528 0.4616 0.4082 0.0231  0.0496  -0.0779 76  GLN B CA  
3601 C C   . GLN B 67  ? 0.3215 0.3993 0.3814 0.0150  0.0423  -0.0651 76  GLN B C   
3602 O O   . GLN B 67  ? 0.3161 0.3715 0.3898 0.0143  0.0364  -0.0690 76  GLN B O   
3603 C CB  . GLN B 67  ? 0.3907 0.5078 0.4326 0.0316  0.0431  -0.0979 76  GLN B CB  
3604 C CG  . GLN B 67  ? 0.3736 0.5186 0.4133 0.0438  0.0483  -0.1197 76  GLN B CG  
3605 C CD  . GLN B 67  ? 0.4325 0.5915 0.4520 0.0526  0.0421  -0.1395 76  GLN B CD  
3606 O OE1 . GLN B 67  ? 0.4705 0.6182 0.4794 0.0489  0.0327  -0.1364 76  GLN B OE1 
3607 N NE2 . GLN B 67  ? 0.4759 0.6618 0.4909 0.0653  0.0469  -0.1615 76  GLN B NE2 
3608 N N   . ARG B 68  ? 0.3198 0.3981 0.3680 0.0098  0.0427  -0.0495 77  ARG B N   
3609 C CA  . ARG B 68  ? 0.3101 0.3637 0.3632 0.0043  0.0372  -0.0387 77  ARG B CA  
3610 C C   . ARG B 68  ? 0.3058 0.3458 0.3717 -0.0009 0.0399  -0.0289 77  ARG B C   
3611 O O   . ARG B 68  ? 0.2693 0.2886 0.3422 -0.0024 0.0354  -0.0287 77  ARG B O   
3612 C CB  . ARG B 68  ? 0.3250 0.3832 0.3653 0.0021  0.0354  -0.0255 77  ARG B CB  
3613 C CG  . ARG B 68  ? 0.3154 0.3830 0.3439 0.0069  0.0285  -0.0359 77  ARG B CG  
3614 C CD  . ARG B 68  ? 0.3280 0.3771 0.3680 0.0067  0.0194  -0.0440 77  ARG B CD  
3615 N NE  . ARG B 68  ? 0.3332 0.3685 0.3799 0.0029  0.0181  -0.0298 77  ARG B NE  
3616 C CZ  . ARG B 68  ? 0.3225 0.3615 0.3643 0.0033  0.0135  -0.0208 77  ARG B CZ  
3617 N NH1 . ARG B 68  ? 0.3017 0.3580 0.3292 0.0062  0.0088  -0.0228 77  ARG B NH1 
3618 N NH2 . ARG B 68  ? 0.3428 0.3691 0.3943 0.0020  0.0128  -0.0109 77  ARG B NH2 
3619 N N   . LEU B 69  ? 0.2963 0.3504 0.3653 -0.0037 0.0469  -0.0209 78  LEU B N   
3620 C CA  . LEU B 69  ? 0.2974 0.3408 0.3811 -0.0086 0.0474  -0.0143 78  LEU B CA  
3621 C C   . LEU B 69  ? 0.2904 0.3256 0.3856 -0.0048 0.0441  -0.0275 78  LEU B C   
3622 O O   . LEU B 69  ? 0.2832 0.2991 0.3849 -0.0072 0.0392  -0.0256 78  LEU B O   
3623 C CB  . LEU B 69  ? 0.2923 0.3566 0.3820 -0.0141 0.0551  -0.0019 78  LEU B CB  
3624 C CG  . LEU B 69  ? 0.2975 0.3530 0.4065 -0.0203 0.0535  0.0040  78  LEU B CG  
3625 C CD1 . LEU B 69  ? 0.3091 0.3337 0.4193 -0.0239 0.0449  0.0092  78  LEU B CD1 
3626 C CD2 . LEU B 69  ? 0.2813 0.3602 0.4006 -0.0278 0.0611  0.0184  78  LEU B CD2 
3627 N N   . ALA B 70  ? 0.2900 0.3402 0.3874 0.0019  0.0460  -0.0411 79  ALA B N   
3628 C CA  . ALA B 70  ? 0.2944 0.3358 0.4052 0.0069  0.0408  -0.0533 79  ALA B CA  
3629 C C   . ALA B 70  ? 0.3011 0.3160 0.4101 0.0066  0.0318  -0.0555 79  ALA B C   
3630 O O   . ALA B 70  ? 0.2974 0.2966 0.4147 0.0058  0.0264  -0.0543 79  ALA B O   
3631 C CB  . ALA B 70  ? 0.2866 0.3485 0.4011 0.0166  0.0432  -0.0703 79  ALA B CB  
3632 N N   . ARG B 71  ? 0.3198 0.3323 0.4183 0.0065  0.0300  -0.0569 80  ARG B N   
3633 C CA  . ARG B 71  ? 0.3186 0.3108 0.4177 0.0041  0.0232  -0.0556 80  ARG B CA  
3634 C C   . ARG B 71  ? 0.2997 0.2786 0.3974 -0.0011 0.0237  -0.0431 80  ARG B C   
3635 O O   . ARG B 71  ? 0.3053 0.2703 0.4072 -0.0024 0.0196  -0.0414 80  ARG B O   
3636 C CB  . ARG B 71  ? 0.3383 0.3347 0.4296 0.0042  0.0208  -0.0585 80  ARG B CB  
3637 C CG  . ARG B 71  ? 0.3433 0.3352 0.4424 0.0075  0.0125  -0.0731 80  ARG B CG  
3638 C CD  . ARG B 71  ? 0.3485 0.3406 0.4448 0.0051  0.0073  -0.0736 80  ARG B CD  
3639 N NE  . ARG B 71  ? 0.2990 0.2783 0.4018 -0.0014 0.0062  -0.0616 80  ARG B NE  
3640 C CZ  . ARG B 71  ? 0.2946 0.2603 0.4117 -0.0053 0.0004  -0.0609 80  ARG B CZ  
3641 N NH1 . ARG B 71  ? 0.2958 0.2527 0.4247 -0.0035 -0.0075 -0.0716 80  ARG B NH1 
3642 N NH2 . ARG B 71  ? 0.2713 0.2329 0.3920 -0.0109 0.0025  -0.0486 80  ARG B NH2 
3643 N N   . LEU B 72  ? 0.3040 0.2876 0.3955 -0.0037 0.0281  -0.0342 81  LEU B N   
3644 C CA  . LEU B 72  ? 0.2894 0.2605 0.3797 -0.0067 0.0277  -0.0260 81  LEU B CA  
3645 C C   . LEU B 72  ? 0.2794 0.2438 0.3761 -0.0074 0.0252  -0.0268 81  LEU B C   
3646 O O   . LEU B 72  ? 0.3164 0.2686 0.4104 -0.0077 0.0219  -0.0256 81  LEU B O   
3647 C CB  . LEU B 72  ? 0.2969 0.2719 0.3839 -0.0090 0.0304  -0.0171 81  LEU B CB  
3648 C CG  . LEU B 72  ? 0.2894 0.2504 0.3778 -0.0109 0.0281  -0.0116 81  LEU B CG  
3649 C CD1 . LEU B 72  ? 0.3450 0.2954 0.4290 -0.0081 0.0263  -0.0143 81  LEU B CD1 
3650 C CD2 . LEU B 72  ? 0.3092 0.2719 0.3983 -0.0133 0.0286  -0.0016 81  LEU B CD2 
3651 N N   . VAL B 73  ? 0.2885 0.2642 0.3936 -0.0071 0.0267  -0.0289 82  VAL B N   
3652 C CA  . VAL B 73  ? 0.2877 0.2609 0.4030 -0.0072 0.0226  -0.0303 82  VAL B CA  
3653 C C   . VAL B 73  ? 0.2932 0.2554 0.4100 -0.0037 0.0162  -0.0349 82  VAL B C   
3654 O O   . VAL B 73  ? 0.2828 0.2334 0.3969 -0.0047 0.0107  -0.0317 82  VAL B O   
3655 C CB  . VAL B 73  ? 0.2956 0.2902 0.4245 -0.0066 0.0268  -0.0325 82  VAL B CB  
3656 C CG1 . VAL B 73  ? 0.3256 0.3214 0.4700 -0.0039 0.0210  -0.0371 82  VAL B CG1 
3657 C CG2 . VAL B 73  ? 0.2929 0.2963 0.4246 -0.0134 0.0313  -0.0221 82  VAL B CG2 
3658 N N   . LEU B 74  ? 0.2974 0.2633 0.4186 0.0004  0.0158  -0.0421 83  LEU B N   
3659 C CA  . LEU B 74  ? 0.3110 0.2642 0.4385 0.0032  0.0078  -0.0450 83  LEU B CA  
3660 C C   . LEU B 74  ? 0.3038 0.2423 0.4215 -0.0011 0.0056  -0.0368 83  LEU B C   
3661 O O   . LEU B 74  ? 0.3311 0.2581 0.4496 -0.0018 -0.0007 -0.0312 83  LEU B O   
3662 C CB  . LEU B 74  ? 0.3040 0.2625 0.4411 0.0091  0.0060  -0.0574 83  LEU B CB  
3663 C CG  . LEU B 74  ? 0.3041 0.2818 0.4532 0.0161  0.0089  -0.0682 83  LEU B CG  
3664 C CD1 . LEU B 74  ? 0.3159 0.2986 0.4710 0.0239  0.0067  -0.0844 83  LEU B CD1 
3665 C CD2 . LEU B 74  ? 0.2936 0.2688 0.4578 0.0191  0.0027  -0.0674 83  LEU B CD2 
3666 N N   . GLY B 75  ? 0.3054 0.2471 0.4146 -0.0037 0.0109  -0.0347 84  GLY B N   
3667 C CA  . GLY B 75  ? 0.2992 0.2341 0.4010 -0.0074 0.0117  -0.0269 84  GLY B CA  
3668 C C   . GLY B 75  ? 0.2947 0.2249 0.3861 -0.0083 0.0122  -0.0204 84  GLY B C   
3669 O O   . GLY B 75  ? 0.3208 0.2456 0.4076 -0.0100 0.0103  -0.0136 84  GLY B O   
3670 N N   . CYS B 76  ? 0.3084 0.2413 0.3959 -0.0074 0.0140  -0.0222 85  CYS B N   
3671 C CA  . CYS B 76  ? 0.3134 0.2409 0.3910 -0.0072 0.0119  -0.0203 85  CYS B CA  
3672 C C   . CYS B 76  ? 0.3060 0.2284 0.3841 -0.0066 0.0041  -0.0188 85  CYS B C   
3673 O O   . CYS B 76  ? 0.3344 0.2527 0.3997 -0.0062 0.0016  -0.0148 85  CYS B O   
3674 C CB  . CYS B 76  ? 0.3279 0.2562 0.4071 -0.0074 0.0124  -0.0230 85  CYS B CB  
3675 S SG  . CYS B 76  ? 0.3226 0.2530 0.3991 -0.0068 0.0186  -0.0219 85  CYS B SG  
3676 N N   . ILE B 77  ? 0.2994 0.2246 0.3920 -0.0055 0.0003  -0.0220 86  ILE B N   
3677 C CA  . ILE B 77  ? 0.3053 0.2262 0.4032 -0.0036 -0.0092 -0.0205 86  ILE B CA  
3678 C C   . ILE B 77  ? 0.3021 0.2139 0.3952 -0.0042 -0.0129 -0.0122 86  ILE B C   
3679 O O   . ILE B 77  ? 0.3341 0.2403 0.4191 -0.0040 -0.0201 -0.0053 86  ILE B O   
3680 C CB  . ILE B 77  ? 0.2927 0.2218 0.4120 -0.0003 -0.0117 -0.0272 86  ILE B CB  
3681 C CG1 . ILE B 77  ? 0.3256 0.2664 0.4523 -0.0020 -0.0090 -0.0307 86  ILE B CG1 
3682 C CG2 . ILE B 77  ? 0.3410 0.2642 0.4697 0.0035  -0.0234 -0.0253 86  ILE B CG2 
3683 C CD1 . ILE B 77  ? 0.3257 0.2841 0.4743 0.0012  -0.0063 -0.0373 86  ILE B CD1 
3684 N N   . THR B 78  ? 0.2895 0.2003 0.3882 -0.0057 -0.0091 -0.0118 87  THR B N   
3685 C CA  . THR B 78  ? 0.2941 0.1961 0.3941 -0.0088 -0.0128 -0.0017 87  THR B CA  
3686 C C   . THR B 78  ? 0.3131 0.2172 0.3933 -0.0126 -0.0085 0.0101  87  THR B C   
3687 O O   . THR B 78  ? 0.3245 0.2233 0.3995 -0.0150 -0.0137 0.0229  87  THR B O   
3688 C CB  . THR B 78  ? 0.2957 0.1971 0.4099 -0.0102 -0.0113 -0.0064 87  THR B CB  
3689 O OG1 . THR B 78  ? 0.2731 0.1742 0.4035 -0.0044 -0.0162 -0.0189 87  THR B OG1 
3690 C CG2 . THR B 78  ? 0.3448 0.2364 0.4658 -0.0160 -0.0161 0.0057  87  THR B CG2 
3691 N N   A MET B 79  ? 0.2934 0.2065 0.3628 -0.0125 0.0009  0.0061  88  MET B N   
3692 N N   B MET B 79  ? 0.2885 0.2016 0.3580 -0.0126 0.0009  0.0062  88  MET B N   
3693 C CA  A MET B 79  ? 0.3174 0.2372 0.3678 -0.0134 0.0068  0.0132  88  MET B CA  
3694 C CA  B MET B 79  ? 0.3100 0.2297 0.3603 -0.0134 0.0067  0.0133  88  MET B CA  
3695 C C   A MET B 79  ? 0.3372 0.2549 0.3701 -0.0105 0.0006  0.0147  88  MET B C   
3696 C C   B MET B 79  ? 0.3321 0.2497 0.3649 -0.0104 0.0005  0.0147  88  MET B C   
3697 O O   A MET B 79  ? 0.3616 0.2827 0.3794 -0.0118 0.0005  0.0260  88  MET B O   
3698 O O   B MET B 79  ? 0.3573 0.2784 0.3748 -0.0118 0.0005  0.0259  88  MET B O   
3699 C CB  A MET B 79  ? 0.3206 0.2493 0.3663 -0.0110 0.0161  0.0052  88  MET B CB  
3700 C CB  B MET B 79  ? 0.3034 0.2320 0.3493 -0.0111 0.0160  0.0054  88  MET B CB  
3701 C CG  A MET B 79  ? 0.2956 0.2293 0.3560 -0.0133 0.0213  0.0039  88  MET B CG  
3702 C CG  B MET B 79  ? 0.2600 0.1942 0.3200 -0.0141 0.0214  0.0061  88  MET B CG  
3703 S SD  A MET B 79  ? 0.3634 0.2976 0.4395 -0.0210 0.0201  0.0154  88  MET B SD  
3704 S SD  B MET B 79  ? 0.3123 0.2531 0.3778 -0.0215 0.0245  0.0220  88  MET B SD  
3705 C CE  A MET B 79  ? 0.3490 0.2718 0.4429 -0.0201 0.0107  0.0058  88  MET B CE  
3706 C CE  B MET B 79  ? 0.2374 0.1912 0.3161 -0.0222 0.0318  0.0176  88  MET B CE  
3707 N N   . ALA B 80  ? 0.3422 0.2562 0.3780 -0.0070 -0.0053 0.0043  89  ALA B N   
3708 C CA  . ALA B 80  ? 0.3555 0.2673 0.3783 -0.0042 -0.0146 0.0032  89  ALA B CA  
3709 C C   . ALA B 80  ? 0.3695 0.2758 0.3932 -0.0051 -0.0250 0.0152  89  ALA B C   
3710 O O   . ALA B 80  ? 0.4309 0.3387 0.4341 -0.0040 -0.0305 0.0221  89  ALA B O   
3711 C CB  . ALA B 80  ? 0.3640 0.2740 0.3991 -0.0026 -0.0198 -0.0090 89  ALA B CB  
3712 N N   . TYR B 81  ? 0.3482 0.2483 0.3951 -0.0061 -0.0285 0.0174  90  TYR B N   
3713 C CA  . TYR B 81  ? 0.3609 0.2520 0.4154 -0.0058 -0.0407 0.0286  90  TYR B CA  
3714 C C   . TYR B 81  ? 0.3749 0.2641 0.4168 -0.0112 -0.0392 0.0481  90  TYR B C   
3715 O O   . TYR B 81  ? 0.3894 0.2755 0.4194 -0.0113 -0.0485 0.0620  90  TYR B O   
3716 C CB  . TYR B 81  ? 0.3392 0.2238 0.4244 -0.0037 -0.0447 0.0223  90  TYR B CB  
3717 C CG  . TYR B 81  ? 0.3711 0.2444 0.4690 -0.0009 -0.0602 0.0312  90  TYR B CG  
3718 C CD1 . TYR B 81  ? 0.3514 0.2265 0.4575 0.0052  -0.0713 0.0259  90  TYR B CD1 
3719 C CD2 . TYR B 81  ? 0.3464 0.2069 0.4504 -0.0048 -0.0653 0.0464  90  TYR B CD2 
3720 C CE1 . TYR B 81  ? 0.3399 0.2044 0.4592 0.0093  -0.0873 0.0346  90  TYR B CE1 
3721 C CE2 . TYR B 81  ? 0.3820 0.2290 0.4992 -0.0017 -0.0818 0.0567  90  TYR B CE2 
3722 C CZ  . TYR B 81  ? 0.3771 0.2262 0.5014 0.0062  -0.0929 0.0502  90  TYR B CZ  
3723 O OH  . TYR B 81  ? 0.4179 0.2534 0.5575 0.0107  -0.1109 0.0604  90  TYR B OH  
3724 N N   . VAL B 82  ? 0.3563 0.2489 0.4028 -0.0161 -0.0283 0.0507  91  VAL B N   
3725 C CA  . VAL B 82  ? 0.3671 0.2622 0.4070 -0.0234 -0.0248 0.0710  91  VAL B CA  
3726 C C   . VAL B 82  ? 0.3646 0.2753 0.3707 -0.0227 -0.0182 0.0779  91  VAL B C   
3727 O O   . VAL B 82  ? 0.4005 0.3129 0.3919 -0.0255 -0.0225 0.0967  91  VAL B O   
3728 C CB  . VAL B 82  ? 0.3449 0.2436 0.4018 -0.0292 -0.0150 0.0701  91  VAL B CB  
3729 C CG1 . VAL B 82  ? 0.3953 0.3035 0.4474 -0.0384 -0.0084 0.0921  91  VAL B CG1 
3730 C CG2 . VAL B 82  ? 0.3688 0.2514 0.4567 -0.0292 -0.0244 0.0632  91  VAL B CG2 
3731 N N   . TRP B 83  ? 0.3879 0.3100 0.3811 -0.0181 -0.0085 0.0623  92  TRP B N   
3732 C CA  . TRP B 83  ? 0.4113 0.3505 0.3725 -0.0151 -0.0011 0.0641  92  TRP B CA  
3733 C C   . TRP B 83  ? 0.4322 0.3701 0.3697 -0.0086 -0.0119 0.0580  92  TRP B C   
3734 O O   . TRP B 83  ? 0.4513 0.4033 0.3582 -0.0061 -0.0089 0.0629  92  TRP B O   
3735 C CB  . TRP B 83  ? 0.3934 0.3451 0.3533 -0.0116 0.0129  0.0495  92  TRP B CB  
3736 C CG  . TRP B 83  ? 0.3880 0.3448 0.3698 -0.0181 0.0223  0.0563  92  TRP B CG  
3737 C CD1 . TRP B 83  ? 0.3711 0.3248 0.3731 -0.0175 0.0256  0.0441  92  TRP B CD1 
3738 C CD2 . TRP B 83  ? 0.3773 0.3436 0.3652 -0.0272 0.0277  0.0780  92  TRP B CD2 
3739 N NE1 . TRP B 83  ? 0.3902 0.3508 0.4098 -0.0246 0.0317  0.0541  92  TRP B NE1 
3740 C CE2 . TRP B 83  ? 0.3942 0.3622 0.4081 -0.0314 0.0332  0.0751  92  TRP B CE2 
3741 C CE3 . TRP B 83  ? 0.4193 0.3935 0.3937 -0.0330 0.0278  0.1015  92  TRP B CE3 
3742 C CZ2 . TRP B 83  ? 0.4285 0.4055 0.4596 -0.0419 0.0380  0.0931  92  TRP B CZ2 
3743 C CZ3 . TRP B 83  ? 0.4640 0.4472 0.4552 -0.0443 0.0340  0.1224  92  TRP B CZ3 
3744 C CH2 . TRP B 83  ? 0.4372 0.4215 0.4584 -0.0489 0.0387  0.1171  92  TRP B CH2 
3745 N N   . GLY B 84  ? 0.4546 0.3788 0.4059 -0.0057 -0.0243 0.0469  93  GLY B N   
3746 C CA  . GLY B 84  ? 0.4947 0.4178 0.4289 -0.0001 -0.0375 0.0394  93  GLY B CA  
3747 C C   . GLY B 84  ? 0.5094 0.4416 0.4217 0.0059  -0.0327 0.0212  93  GLY B C   
3748 O O   . GLY B 84  ? 0.5013 0.4323 0.4262 0.0071  -0.0250 0.0072  93  GLY B O   
3749 N N   . LYS B 85  ? 0.5590 0.4999 0.4381 0.0105  -0.0383 0.0214  94  LYS B N   
3750 C CA  . LYS B 85  ? 0.6018 0.5516 0.4566 0.0184  -0.0352 0.0015  94  LYS B CA  
3751 C C   . LYS B 85  ? 0.6224 0.5910 0.4619 0.0207  -0.0153 0.0034  94  LYS B C   
3752 O O   . LYS B 85  ? 0.6402 0.6176 0.4615 0.0294  -0.0111 -0.0151 94  LYS B O   
3753 C CB  . LYS B 85  ? 0.6273 0.5814 0.4500 0.0241  -0.0507 -0.0028 94  LYS B CB  
3754 C CG  . LYS B 85  ? 0.6281 0.5672 0.4682 0.0239  -0.0716 -0.0127 94  LYS B CG  
3755 C CD  . LYS B 85  ? 0.6885 0.6331 0.4953 0.0304  -0.0889 -0.0213 94  LYS B CD  
3756 C CE  . LYS B 85  ? 0.6976 0.6297 0.5278 0.0294  -0.1107 -0.0320 94  LYS B CE  
3757 N NZ  . LYS B 85  ? 0.7426 0.6800 0.5427 0.0351  -0.1316 -0.0385 94  LYS B NZ  
3758 N N   . GLY B 86  ? 0.6284 0.6039 0.4782 0.0133  -0.0038 0.0245  95  GLY B N   
3759 C CA  . GLY B 86  ? 0.6657 0.6631 0.5081 0.0141  0.0156  0.0285  95  GLY B CA  
3760 C C   . GLY B 86  ? 0.7355 0.7590 0.5372 0.0189  0.0219  0.0350  95  GLY B C   
3761 O O   . GLY B 86  ? 0.7516 0.7961 0.5394 0.0267  0.0357  0.0233  95  GLY B O   
3762 N N   . HIS B 87  ? 0.7884 0.8119 0.5710 0.0153  0.0116  0.0536  96  HIS B N   
3763 C CA  . HIS B 87  ? 0.8544 0.9052 0.5937 0.0185  0.0167  0.0657  96  HIS B CA  
3764 C C   . HIS B 87  ? 0.8739 0.9344 0.6152 0.0056  0.0222  0.1049  96  HIS B C   
3765 O O   . HIS B 87  ? 0.9283 1.0117 0.6338 0.0057  0.0252  0.1225  96  HIS B O   
3766 C CB  . HIS B 87  ? 0.9160 0.9608 0.6241 0.0259  -0.0034 0.0559  96  HIS B CB  
3767 C CG  . HIS B 87  ? 0.9767 1.0084 0.6866 0.0364  -0.0131 0.0191  96  HIS B CG  
3768 N ND1 . HIS B 87  ? 1.0305 1.0723 0.7365 0.0461  -0.0014 -0.0062 96  HIS B ND1 
3769 C CD2 . HIS B 87  ? 0.9978 1.0072 0.7165 0.0383  -0.0346 0.0044  96  HIS B CD2 
3770 C CE1 . HIS B 87  ? 1.0352 1.0579 0.7476 0.0527  -0.0162 -0.0342 96  HIS B CE1 
3771 N NE2 . HIS B 87  ? 1.0224 1.0269 0.7430 0.0473  -0.0359 -0.0278 96  HIS B NE2 
3772 N N   . GLY B 88  ? 0.8458 0.8894 0.6285 -0.0056 0.0226  0.1186  97  GLY B N   
3773 C CA  . GLY B 88  ? 0.8557 0.9005 0.6496 -0.0195 0.0235  0.1557  97  GLY B CA  
3774 C C   . GLY B 88  ? 0.8595 0.8734 0.6702 -0.0250 0.0012  0.1705  97  GLY B C   
3775 O O   . GLY B 88  ? 0.8781 0.8854 0.7069 -0.0367 -0.0011 0.1997  97  GLY B O   
3776 N N   . ASP B 89  ? 0.8399 0.8354 0.6478 -0.0165 -0.0160 0.1511  98  ASP B N   
3777 C CA  . ASP B 89  ? 0.8140 0.7809 0.6463 -0.0191 -0.0371 0.1593  98  ASP B CA  
3778 C C   . ASP B 89  ? 0.7538 0.7019 0.6326 -0.0225 -0.0347 0.1476  98  ASP B C   
3779 O O   . ASP B 89  ? 0.7444 0.6901 0.6327 -0.0166 -0.0310 0.1203  98  ASP B O   
3780 C CB  . ASP B 89  ? 0.8284 0.7876 0.6458 -0.0089 -0.0555 0.1411  98  ASP B CB  
3781 C CG  . ASP B 89  ? 0.8562 0.7949 0.6890 -0.0101 -0.0785 0.1570  98  ASP B CG  
3782 O OD1 . ASP B 89  ? 0.7949 0.7140 0.6670 -0.0148 -0.0829 0.1638  98  ASP B OD1 
3783 O OD2 . ASP B 89  ? 0.9745 0.9170 0.7802 -0.0049 -0.0937 0.1612  98  ASP B OD2 
3784 N N   . VAL B 90  ? 0.7154 0.6505 0.6222 -0.0320 -0.0379 0.1688  99  VAL B N   
3785 C CA  . VAL B 90  ? 0.6700 0.5929 0.6166 -0.0367 -0.0328 0.1607  99  VAL B CA  
3786 C C   . VAL B 90  ? 0.6337 0.5278 0.6146 -0.0379 -0.0513 0.1655  99  VAL B C   
3787 O O   . VAL B 90  ? 0.6766 0.5607 0.6562 -0.0407 -0.0650 0.1884  99  VAL B O   
3788 C CB  . VAL B 90  ? 0.6935 0.6332 0.6449 -0.0478 -0.0162 0.1792  99  VAL B CB  
3789 C CG1 . VAL B 90  ? 0.6888 0.6114 0.6845 -0.0560 -0.0182 0.1808  99  VAL B CG1 
3790 C CG2 . VAL B 90  ? 0.6925 0.6599 0.6234 -0.0429 0.0036  0.1630  99  VAL B CG2 
3791 N N   . ARG B 91  ? 0.5802 0.4623 0.5912 -0.0350 -0.0520 0.1440  100 ARG B N   
3792 C CA  . ARG B 91  ? 0.5655 0.4227 0.6125 -0.0342 -0.0675 0.1435  100 ARG B CA  
3793 C C   . ARG B 91  ? 0.5395 0.3890 0.6157 -0.0425 -0.0629 0.1460  100 ARG B C   
3794 O O   . ARG B 91  ? 0.4664 0.3259 0.5469 -0.0427 -0.0501 0.1293  100 ARG B O   
3795 C CB  . ARG B 91  ? 0.5534 0.4058 0.6134 -0.0231 -0.0732 0.1156  100 ARG B CB  
3796 C CG  . ARG B 91  ? 0.5429 0.3995 0.5840 -0.0155 -0.0831 0.1125  100 ARG B CG  
3797 C CD  . ARG B 91  ? 0.6442 0.4855 0.6936 -0.0135 -0.1039 0.1306  100 ARG B CD  
3798 N NE  . ARG B 91  ? 0.6623 0.5131 0.6814 -0.0094 -0.1123 0.1360  100 ARG B NE  
3799 C CZ  . ARG B 91  ? 0.7009 0.5514 0.7255 -0.0006 -0.1263 0.1243  100 ARG B CZ  
3800 N NH1 . ARG B 91  ? 0.6867 0.5302 0.7475 0.0060  -0.1324 0.1067  100 ARG B NH1 
3801 N NH2 . ARG B 91  ? 0.7756 0.6357 0.7688 0.0020  -0.1348 0.1298  100 ARG B NH2 
3802 N N   . LYS B 92  ? 0.5430 0.3738 0.6406 -0.0495 -0.0755 0.1671  101 LYS B N   
3803 C CA  . LYS B 92  ? 0.5466 0.3658 0.6772 -0.0586 -0.0761 0.1702  101 LYS B CA  
3804 C C   . LYS B 92  ? 0.4957 0.2919 0.6613 -0.0506 -0.0896 0.1469  101 LYS B C   
3805 O O   . LYS B 92  ? 0.4458 0.2327 0.6380 -0.0556 -0.0912 0.1410  101 LYS B O   
3806 C CB  . LYS B 92  ? 0.6015 0.4122 0.7400 -0.0725 -0.0831 0.2075  101 LYS B CB  
3807 C CG  . LYS B 92  ? 0.6803 0.5198 0.7821 -0.0800 -0.0679 0.2320  101 LYS B CG  
3808 C CD  . LYS B 92  ? 0.6929 0.5318 0.8081 -0.0978 -0.0687 0.2701  101 LYS B CD  
3809 C CE  . LYS B 92  ? 0.7148 0.5882 0.7901 -0.1035 -0.0522 0.2947  101 LYS B CE  
3810 N NZ  . LYS B 92  ? 0.7550 0.6337 0.8447 -0.1229 -0.0504 0.3355  101 LYS B NZ  
3811 N N   . VAL B 93  ? 0.4871 0.2768 0.6531 -0.0376 -0.0992 0.1326  102 VAL B N   
3812 C CA  . VAL B 93  ? 0.4684 0.2427 0.6657 -0.0269 -0.1101 0.1079  102 VAL B CA  
3813 C C   . VAL B 93  ? 0.4389 0.2323 0.6249 -0.0160 -0.0998 0.0801  102 VAL B C   
3814 O O   . VAL B 93  ? 0.4474 0.2507 0.6153 -0.0108 -0.0999 0.0805  102 VAL B O   
3815 C CB  . VAL B 93  ? 0.4605 0.2111 0.6784 -0.0201 -0.1330 0.1169  102 VAL B CB  
3816 C CG1 . VAL B 93  ? 0.4502 0.1874 0.7031 -0.0071 -0.1434 0.0885  102 VAL B CG1 
3817 C CG2 . VAL B 93  ? 0.5106 0.2405 0.7392 -0.0328 -0.1447 0.1508  102 VAL B CG2 
3818 N N   . LEU B 94  ? 0.4200 0.2189 0.6171 -0.0133 -0.0921 0.0572  103 LEU B N   
3819 C CA  . LEU B 94  ? 0.3887 0.2051 0.5806 -0.0038 -0.0834 0.0328  103 LEU B CA  
3820 C C   . LEU B 94  ? 0.3950 0.2031 0.6145 0.0092  -0.0960 0.0160  103 LEU B C   
3821 O O   . LEU B 94  ? 0.3677 0.1619 0.6115 0.0121  -0.1039 0.0061  103 LEU B O   
3822 C CB  . LEU B 94  ? 0.3700 0.1987 0.5586 -0.0067 -0.0696 0.0186  103 LEU B CB  
3823 C CG  . LEU B 94  ? 0.3520 0.2014 0.5310 0.0000  -0.0580 -0.0007 103 LEU B CG  
3824 C CD1 . LEU B 94  ? 0.3583 0.2202 0.5120 -0.0020 -0.0503 0.0070  103 LEU B CD1 
3825 C CD2 . LEU B 94  ? 0.3478 0.2065 0.5257 -0.0024 -0.0481 -0.0125 103 LEU B CD2 
3826 N N   . PRO B 95  ? 0.4189 0.2365 0.6372 0.0176  -0.0990 0.0113  104 PRO B N   
3827 C CA  . PRO B 95  ? 0.4282 0.2429 0.6758 0.0315  -0.1105 -0.0044 104 PRO B CA  
3828 C C   . PRO B 95  ? 0.3994 0.2219 0.6638 0.0392  -0.1045 -0.0313 104 PRO B C   
3829 O O   . PRO B 95  ? 0.3769 0.2175 0.6260 0.0358  -0.0886 -0.0404 104 PRO B O   
3830 C CB  . PRO B 95  ? 0.4448 0.2798 0.6844 0.0363  -0.1079 -0.0071 104 PRO B CB  
3831 C CG  . PRO B 95  ? 0.4254 0.2615 0.6333 0.0258  -0.1044 0.0128  104 PRO B CG  
3832 C CD  . PRO B 95  ? 0.3845 0.2171 0.5766 0.0151  -0.0930 0.0193  104 PRO B CD  
3833 N N   . ARG B 96  ? 0.4186 0.2278 0.7136 0.0505  -0.1181 -0.0443 105 ARG B N   
3834 C CA  . ARG B 96  ? 0.4439 0.2603 0.7542 0.0601  -0.1145 -0.0729 105 ARG B CA  
3835 C C   . ARG B 96  ? 0.4307 0.2835 0.7334 0.0671  -0.0973 -0.0919 105 ARG B C   
3836 O O   . ARG B 96  ? 0.4356 0.3015 0.7323 0.0686  -0.0872 -0.1086 105 ARG B O   
3837 C CB  . ARG B 96  ? 0.4616 0.2570 0.8088 0.0743  -0.1343 -0.0866 105 ARG B CB  
3838 C CG  . ARG B 96  ? 0.4814 0.2865 0.8492 0.0892  -0.1418 -0.0925 105 ARG B CG  
3839 C CD  . ARG B 96  ? 0.4974 0.2824 0.9047 0.1060  -0.1615 -0.1101 105 ARG B CD  
3840 N NE  . ARG B 96  ? 0.5244 0.2668 0.9438 0.0986  -0.1822 -0.0893 105 ARG B NE  
3841 C CZ  . ARG B 96  ? 0.6414 0.3557 1.0781 0.0976  -0.1938 -0.0970 105 ARG B CZ  
3842 N NH1 . ARG B 96  ? 0.6384 0.3621 1.0803 0.1055  -0.1880 -0.1291 105 ARG B NH1 
3843 N NH2 . ARG B 96  ? 0.6464 0.3229 1.0963 0.0881  -0.2130 -0.0716 105 ARG B NH2 
3844 N N   A ASN B 97  ? 0.4294 0.2997 0.7328 0.0704  -0.0948 -0.0879 106 ASN B N   
3845 N N   B ASN B 97  ? 0.4199 0.2895 0.7236 0.0704  -0.0953 -0.0874 106 ASN B N   
3846 C CA  A ASN B 97  ? 0.4124 0.3190 0.7139 0.0753  -0.0789 -0.1022 106 ASN B CA  
3847 C CA  B ASN B 97  ? 0.3904 0.2963 0.6909 0.0744  -0.0794 -0.0998 106 ASN B CA  
3848 C C   A ASN B 97  ? 0.3928 0.3136 0.6639 0.0628  -0.0611 -0.0963 106 ASN B C   
3849 C C   B ASN B 97  ? 0.3822 0.3019 0.6538 0.0630  -0.0616 -0.0967 106 ASN B C   
3850 O O   A ASN B 97  ? 0.4040 0.3528 0.6727 0.0656  -0.0474 -0.1081 106 ASN B O   
3851 O O   B ASN B 97  ? 0.3906 0.3362 0.6604 0.0668  -0.0486 -0.1108 106 ASN B O   
3852 C CB  A ASN B 97  ? 0.4085 0.3304 0.7245 0.0805  -0.0829 -0.0984 106 ASN B CB  
3853 C CB  B ASN B 97  ? 0.3884 0.3076 0.6969 0.0761  -0.0828 -0.0914 106 ASN B CB  
3854 C CG  A ASN B 97  ? 0.4276 0.3454 0.7804 0.0978  -0.0983 -0.1113 106 ASN B CG  
3855 C CG  B ASN B 97  ? 0.3724 0.2782 0.6570 0.0627  -0.0866 -0.0664 106 ASN B CG  
3856 O OD1 A ASN B 97  ? 0.4259 0.3265 0.7938 0.1065  -0.1067 -0.1242 106 ASN B OD1 
3857 O OD1 B ASN B 97  ? 0.3979 0.2918 0.6575 0.0514  -0.0815 -0.0553 106 ASN B OD1 
3858 N ND2 A ASN B 97  ? 0.4239 0.3571 0.7941 0.1035  -0.1035 -0.1089 106 ASN B ND2 
3859 N ND2 B ASN B 97  ? 0.2950 0.2054 0.5878 0.0650  -0.0962 -0.0592 106 ASN B ND2 
3860 N N   . ILE B 98  ? 0.3834 0.2869 0.6329 0.0497  -0.0614 -0.0777 107 ILE B N   
3861 C CA  . ILE B 98  ? 0.3831 0.2947 0.6074 0.0396  -0.0473 -0.0736 107 ILE B CA  
3862 C C   . ILE B 98  ? 0.3681 0.2654 0.5892 0.0360  -0.0489 -0.0765 107 ILE B C   
3863 O O   . ILE B 98  ? 0.3489 0.2589 0.5593 0.0345  -0.0390 -0.0845 107 ILE B O   
3864 C CB  . ILE B 98  ? 0.4118 0.3212 0.6141 0.0288  -0.0440 -0.0542 107 ILE B CB  
3865 C CG1 . ILE B 98  ? 0.4562 0.3750 0.6375 0.0211  -0.0302 -0.0526 107 ILE B CG1 
3866 C CG2 . ILE B 98  ? 0.4266 0.3124 0.6230 0.0232  -0.0546 -0.0366 107 ILE B CG2 
3867 C CD1 . ILE B 98  ? 0.4437 0.3695 0.6099 0.0153  -0.0250 -0.0435 107 ILE B CD1 
3868 N N   . ALA B 99  ? 0.3583 0.3085 0.5412 0.0437  -0.0598 -0.0914 108 ALA B N   
3869 C CA  . ALA B 99  ? 0.3773 0.3138 0.5633 0.0420  -0.0647 -0.0888 108 ALA B CA  
3870 C C   . ALA B 99  ? 0.3717 0.3111 0.5654 0.0494  -0.0666 -0.1085 108 ALA B C   
3871 O O   . ALA B 99  ? 0.3831 0.3212 0.5678 0.0472  -0.0632 -0.1108 108 ALA B O   
3872 C CB  . ALA B 99  ? 0.3918 0.3123 0.5951 0.0413  -0.0781 -0.0756 108 ALA B CB  
3873 N N   . VAL B 100 ? 0.3614 0.3070 0.5710 0.0593  -0.0722 -0.1236 109 VAL B N   
3874 C CA  . VAL B 100 ? 0.3723 0.3248 0.5886 0.0693  -0.0747 -0.1454 109 VAL B CA  
3875 C C   . VAL B 100 ? 0.3527 0.3244 0.5464 0.0690  -0.0595 -0.1518 109 VAL B C   
3876 O O   . VAL B 100 ? 0.3678 0.3369 0.5552 0.0697  -0.0601 -0.1573 109 VAL B O   
3877 C CB  . VAL B 100 ? 0.3871 0.3461 0.6252 0.0821  -0.0832 -0.1620 109 VAL B CB  
3878 C CG1 . VAL B 100 ? 0.4146 0.3893 0.6544 0.0949  -0.0827 -0.1873 109 VAL B CG1 
3879 C CG2 . VAL B 100 ? 0.4254 0.3612 0.6901 0.0838  -0.1019 -0.1574 109 VAL B CG2 
3880 N N   . PRO B 101 ? 0.3528 0.3440 0.5362 0.0678  -0.0467 -0.1502 110 PRO B N   
3881 C CA  . PRO B 101 ? 0.3338 0.3436 0.4978 0.0667  -0.0324 -0.1523 110 PRO B CA  
3882 C C   . PRO B 101 ? 0.3225 0.3223 0.4685 0.0569  -0.0275 -0.1399 110 PRO B C   
3883 O O   . PRO B 101 ? 0.3413 0.3497 0.4752 0.0590  -0.0222 -0.1453 110 PRO B O   
3884 C CB  . PRO B 101 ? 0.3093 0.3371 0.4719 0.0638  -0.0217 -0.1469 110 PRO B CB  
3885 C CG  . PRO B 101 ? 0.3722 0.3881 0.5479 0.0614  -0.0301 -0.1401 110 PRO B CG  
3886 C CD  . PRO B 101 ? 0.3538 0.3523 0.5457 0.0678  -0.0458 -0.1465 110 PRO B CD  
3887 N N   . TYR B 102 ? 0.3207 0.3045 0.4646 0.0475  -0.0297 -0.1237 111 TYR B N   
3888 C CA  . TYR B 102 ? 0.3196 0.2941 0.4484 0.0390  -0.0259 -0.1118 111 TYR B CA  
3889 C C   . TYR B 102 ? 0.3144 0.2781 0.4472 0.0410  -0.0340 -0.1168 111 TYR B C   
3890 O O   . TYR B 102 ? 0.3062 0.2726 0.4258 0.0391  -0.0288 -0.1167 111 TYR B O   
3891 C CB  . TYR B 102 ? 0.3170 0.2800 0.4442 0.0310  -0.0277 -0.0950 111 TYR B CB  
3892 C CG  . TYR B 102 ? 0.3188 0.2762 0.4297 0.0230  -0.0222 -0.0826 111 TYR B CG  
3893 C CD1 . TYR B 102 ? 0.3372 0.3023 0.4332 0.0209  -0.0125 -0.0840 111 TYR B CD1 
3894 C CD2 . TYR B 102 ? 0.3205 0.2674 0.4312 0.0182  -0.0264 -0.0685 111 TYR B CD2 
3895 C CE1 . TYR B 102 ? 0.3053 0.2652 0.3881 0.0145  -0.0082 -0.0734 111 TYR B CE1 
3896 C CE2 . TYR B 102 ? 0.2982 0.2429 0.3946 0.0123  -0.0211 -0.0582 111 TYR B CE2 
3897 C CZ  . TYR B 102 ? 0.3189 0.2691 0.4020 0.0106  -0.0125 -0.0617 111 TYR B CZ  
3898 O OH  . TYR B 102 ? 0.2832 0.2312 0.3540 0.0059  -0.0080 -0.0526 111 TYR B OH  
3899 N N   . CYS B 103 ? 0.3381 0.2891 0.4914 0.0450  -0.0477 -0.1209 112 CYS B N   
3900 C CA  . CYS B 103 ? 0.3430 0.2825 0.5065 0.0470  -0.0582 -0.1270 112 CYS B CA  
3901 C C   . CYS B 103 ? 0.3527 0.3053 0.5131 0.0576  -0.0584 -0.1490 112 CYS B C   
3902 O O   . CYS B 103 ? 0.3399 0.2905 0.4955 0.0577  -0.0606 -0.1535 112 CYS B O   
3903 C CB  . CYS B 103 ? 0.3462 0.2678 0.5373 0.0482  -0.0745 -0.1247 112 CYS B CB  
3904 S SG  . CYS B 103 ? 0.4074 0.3155 0.6011 0.0362  -0.0756 -0.0958 112 CYS B SG  
3905 N N   . GLN B 104 ? 0.3511 0.3194 0.5146 0.0672  -0.0564 -0.1629 113 GLN B N   
3906 C CA  . GLN B 104 ? 0.3731 0.3615 0.5302 0.0795  -0.0541 -0.1839 113 GLN B CA  
3907 C C   . GLN B 104 ? 0.3577 0.3615 0.4880 0.0758  -0.0394 -0.1782 113 GLN B C   
3908 O O   . GLN B 104 ? 0.3632 0.3731 0.4853 0.0814  -0.0412 -0.1886 113 GLN B O   
3909 C CB  . GLN B 104 ? 0.3760 0.3839 0.5396 0.0896  -0.0508 -0.1956 113 GLN B CB  
3910 C CG  . GLN B 104 ? 0.3759 0.3728 0.5676 0.0989  -0.0677 -0.2094 113 GLN B CG  
3911 C CD  . GLN B 104 ? 0.4202 0.4387 0.6190 0.1093  -0.0638 -0.2209 113 GLN B CD  
3912 O OE1 . GLN B 104 ? 0.4427 0.4780 0.6313 0.1048  -0.0496 -0.2109 113 GLN B OE1 
3913 N NE2 . GLN B 104 ? 0.4046 0.4232 0.6240 0.1238  -0.0774 -0.2427 113 GLN B NE2 
3914 N N   . LEU B 105 ? 0.3596 0.3694 0.4778 0.0667  -0.0262 -0.1616 114 LEU B N   
3915 C CA  . LEU B 105 ? 0.3743 0.3961 0.4703 0.0619  -0.0128 -0.1528 114 LEU B CA  
3916 C C   . LEU B 105 ? 0.3519 0.3576 0.4402 0.0552  -0.0163 -0.1453 114 LEU B C   
3917 O O   . LEU B 105 ? 0.3041 0.3192 0.3780 0.0576  -0.0123 -0.1481 114 LEU B O   
3918 C CB  . LEU B 105 ? 0.3549 0.3814 0.4461 0.0528  -0.0014 -0.1368 114 LEU B CB  
3919 C CG  . LEU B 105 ? 0.4035 0.4429 0.4765 0.0475  0.0123  -0.1261 114 LEU B CG  
3920 C CD1 . LEU B 105 ? 0.4315 0.4999 0.4975 0.0572  0.0202  -0.1353 114 LEU B CD1 
3921 C CD2 . LEU B 105 ? 0.4148 0.4533 0.4902 0.0381  0.0191  -0.1119 114 LEU B CD2 
3922 N N   . SER B 106 ? 0.3554 0.3393 0.4537 0.0474  -0.0236 -0.1349 115 SER B N   
3923 C CA  . SER B 106 ? 0.3588 0.3286 0.4543 0.0410  -0.0275 -0.1269 115 SER B CA  
3924 C C   . SER B 106 ? 0.3568 0.3251 0.4590 0.0486  -0.0384 -0.1428 115 SER B C   
3925 O O   . SER B 106 ? 0.2745 0.2439 0.3663 0.0471  -0.0373 -0.1419 115 SER B O   
3926 C CB  . SER B 106 ? 0.3492 0.3003 0.4576 0.0330  -0.0337 -0.1125 115 SER B CB  
3927 O OG  . SER B 106 ? 0.2736 0.2271 0.3739 0.0271  -0.0249 -0.0996 115 SER B OG  
3928 N N   . LYS B 107 ? 0.3925 0.3586 0.5133 0.0576  -0.0501 -0.1588 116 LYS B N   
3929 C CA  . LYS B 107 ? 0.4236 0.3893 0.5534 0.0672  -0.0631 -0.1789 116 LYS B CA  
3930 C C   . LYS B 107 ? 0.4359 0.4260 0.5426 0.0763  -0.0550 -0.1912 116 LYS B C   
3931 O O   . LYS B 107 ? 0.4544 0.4452 0.5560 0.0789  -0.0602 -0.1982 116 LYS B O   
3932 C CB  . LYS B 107 ? 0.4450 0.4051 0.6003 0.0772  -0.0776 -0.1961 116 LYS B CB  
3933 C CG  . LYS B 107 ? 0.4714 0.4223 0.6452 0.0851  -0.0964 -0.2157 116 LYS B CG  
3934 C CD  . LYS B 107 ? 0.5412 0.4872 0.7417 0.0972  -0.1120 -0.2360 116 LYS B CD  
3935 C CE  . LYS B 107 ? 0.5369 0.4725 0.7589 0.1057  -0.1332 -0.2578 116 LYS B CE  
3936 N NZ  . LYS B 107 ? 0.5535 0.4829 0.8040 0.1187  -0.1501 -0.2795 116 LYS B NZ  
3937 N N   . LYS B 108 ? 0.4409 0.4529 0.5347 0.0811  -0.0422 -0.1924 117 LYS B N   
3938 C CA  . LYS B 108 ? 0.4519 0.4922 0.5231 0.0898  -0.0321 -0.1998 117 LYS B CA  
3939 C C   . LYS B 108 ? 0.4355 0.4765 0.4865 0.0817  -0.0239 -0.1849 117 LYS B C   
3940 O O   . LYS B 108 ? 0.4495 0.5045 0.4867 0.0894  -0.0245 -0.1940 117 LYS B O   
3941 C CB  . LYS B 108 ? 0.4628 0.5264 0.5281 0.0928  -0.0181 -0.1968 117 LYS B CB  
3942 C CG  . LYS B 108 ? 0.4964 0.5950 0.5419 0.1040  -0.0076 -0.2043 117 LYS B CG  
3943 C CD  . LYS B 108 ? 0.5162 0.6406 0.5638 0.1090  0.0038  -0.2044 117 LYS B CD  
3944 C CE  . LYS B 108 ? 0.6039 0.7686 0.6348 0.1245  0.0121  -0.2157 117 LYS B CE  
3945 N NZ  . LYS B 108 ? 0.6102 0.8029 0.6489 0.1331  0.0202  -0.2215 117 LYS B NZ  
3946 N N   . LEU B 109 ? 0.4011 0.4275 0.4509 0.0674  -0.0175 -0.1635 118 LEU B N   
3947 C CA  . LEU B 109 ? 0.4143 0.4387 0.4480 0.0593  -0.0104 -0.1484 118 LEU B CA  
3948 C C   . LEU B 109 ? 0.3920 0.3954 0.4338 0.0536  -0.0212 -0.1459 118 LEU B C   
3949 O O   . LEU B 109 ? 0.3946 0.3955 0.4254 0.0474  -0.0165 -0.1342 118 LEU B O   
3950 C CB  . LEU B 109 ? 0.3710 0.3932 0.3996 0.0483  0.0021  -0.1284 118 LEU B CB  
3951 C CG  . LEU B 109 ? 0.4288 0.4732 0.4514 0.0511  0.0144  -0.1261 118 LEU B CG  
3952 C CD1 . LEU B 109 ? 0.4098 0.4462 0.4353 0.0398  0.0217  -0.1091 118 LEU B CD1 
3953 C CD2 . LEU B 109 ? 0.4476 0.5154 0.4514 0.0564  0.0233  -0.1249 118 LEU B CD2 
3954 N N   . GLU B 110 ? 0.4058 0.3952 0.4695 0.0559  -0.0360 -0.1562 119 GLU B N   
3955 C CA  . GLU B 110 ? 0.4172 0.3880 0.4957 0.0503  -0.0478 -0.1533 119 GLU B CA  
3956 C C   . GLU B 110 ? 0.3884 0.3472 0.4660 0.0368  -0.0413 -0.1300 119 GLU B C   
3957 O O   . GLU B 110 ? 0.3884 0.3429 0.4643 0.0319  -0.0425 -0.1231 119 GLU B O   
3958 C CB  . GLU B 110 ? 0.4266 0.4048 0.4973 0.0564  -0.0536 -0.1648 119 GLU B CB  
3959 C CG  . GLU B 110 ? 0.5293 0.5228 0.5985 0.0724  -0.0612 -0.1906 119 GLU B CG  
3960 C CD  . GLU B 110 ? 0.5698 0.5714 0.6306 0.0794  -0.0688 -0.2030 119 GLU B CD  
3961 O OE1 . GLU B 110 ? 0.7318 0.7576 0.7713 0.0910  -0.0638 -0.2139 119 GLU B OE1 
3962 O OE2 . GLU B 110 ? 0.6536 0.6397 0.7296 0.0736  -0.0799 -0.2011 119 GLU B OE2 
3963 N N   . LEU B 111 ? 0.3560 0.3118 0.4347 0.0319  -0.0347 -0.1190 120 LEU B N   
3964 C CA  . LEU B 111 ? 0.3471 0.2942 0.4244 0.0213  -0.0292 -0.0990 120 LEU B CA  
3965 C C   . LEU B 111 ? 0.3381 0.2733 0.4352 0.0183  -0.0362 -0.0930 120 LEU B C   
3966 O O   . LEU B 111 ? 0.3448 0.2804 0.4519 0.0240  -0.0412 -0.1029 120 LEU B O   
3967 C CB  . LEU B 111 ? 0.3253 0.2817 0.3825 0.0186  -0.0147 -0.0904 120 LEU B CB  
3968 C CG  . LEU B 111 ? 0.3415 0.3084 0.3796 0.0196  -0.0069 -0.0900 120 LEU B CG  
3969 C CD1 . LEU B 111 ? 0.3413 0.3180 0.3665 0.0182  0.0054  -0.0837 120 LEU B CD1 
3970 C CD2 . LEU B 111 ? 0.3319 0.2918 0.3674 0.0139  -0.0073 -0.0800 120 LEU B CD2 
3971 N N   . PRO B 112 ? 0.3402 0.2671 0.4435 0.0102  -0.0367 -0.0761 121 PRO B N   
3972 C CA  . PRO B 112 ? 0.3501 0.2686 0.4702 0.0074  -0.0422 -0.0663 121 PRO B CA  
3973 C C   . PRO B 112 ? 0.3498 0.2738 0.4594 0.0085  -0.0347 -0.0642 121 PRO B C   
3974 O O   . PRO B 112 ? 0.3728 0.3052 0.4628 0.0075  -0.0238 -0.0628 121 PRO B O   
3975 C CB  . PRO B 112 ? 0.3498 0.2655 0.4720 -0.0007 -0.0404 -0.0470 121 PRO B CB  
3976 C CG  . PRO B 112 ? 0.3617 0.2799 0.4792 -0.0014 -0.0399 -0.0513 121 PRO B CG  
3977 C CD  . PRO B 112 ? 0.3598 0.2870 0.4558 0.0041  -0.0323 -0.0643 121 PRO B CD  
3978 N N   . PRO B 113 ? 0.3473 0.2663 0.4719 0.0105  -0.0416 -0.0640 122 PRO B N   
3979 C CA  . PRO B 113 ? 0.3315 0.2565 0.4483 0.0118  -0.0359 -0.0627 122 PRO B CA  
3980 C C   . PRO B 113 ? 0.3271 0.2533 0.4338 0.0061  -0.0303 -0.0453 122 PRO B C   
3981 O O   . PRO B 113 ? 0.3098 0.2335 0.4242 0.0057  -0.0346 -0.0360 122 PRO B O   
3982 C CB  . PRO B 113 ? 0.3568 0.2755 0.4957 0.0169  -0.0474 -0.0688 122 PRO B CB  
3983 C CG  . PRO B 113 ? 0.3615 0.2673 0.5210 0.0141  -0.0587 -0.0616 122 PRO B CG  
3984 C CD  . PRO B 113 ? 0.3508 0.2579 0.5031 0.0120  -0.0563 -0.0651 122 PRO B CD  
3985 N N   . ILE B 114 ? 0.3077 0.2391 0.3968 0.0029  -0.0212 -0.0416 123 ILE B N   
3986 C CA  . ILE B 114 ? 0.2898 0.2250 0.3663 -0.0004 -0.0155 -0.0293 123 ILE B CA  
3987 C C   . ILE B 114 ? 0.2897 0.2307 0.3486 -0.0013 -0.0060 -0.0335 123 ILE B C   
3988 O O   . ILE B 114 ? 0.2755 0.2171 0.3317 -0.0007 -0.0040 -0.0406 123 ILE B O   
3989 C CB  . ILE B 114 ? 0.2825 0.2158 0.3643 -0.0041 -0.0181 -0.0136 123 ILE B CB  
3990 C CG1 . ILE B 114 ? 0.2900 0.2314 0.3579 -0.0047 -0.0127 -0.0024 123 ILE B CG1 
3991 C CG2 . ILE B 114 ? 0.2837 0.2157 0.3662 -0.0065 -0.0170 -0.0145 123 ILE B CG2 
3992 C CD1 . ILE B 114 ? 0.2792 0.2243 0.3539 -0.0068 -0.0151 0.0158  123 ILE B CD1 
3993 N N   . LEU B 115 ? 0.2929 0.2380 0.3407 -0.0021 -0.0014 -0.0294 124 LEU B N   
3994 C CA  . LEU B 115 ? 0.2840 0.2325 0.3190 -0.0031 0.0059  -0.0323 124 LEU B CA  
3995 C C   . LEU B 115 ? 0.2935 0.2409 0.3229 -0.0048 0.0082  -0.0276 124 LEU B C   
3996 O O   . LEU B 115 ? 0.3402 0.2884 0.3696 -0.0056 0.0070  -0.0185 124 LEU B O   
3997 C CB  . LEU B 115 ? 0.2712 0.2229 0.2990 -0.0028 0.0074  -0.0303 124 LEU B CB  
3998 C CG  . LEU B 115 ? 0.2513 0.2044 0.2713 -0.0040 0.0127  -0.0341 124 LEU B CG  
3999 C CD1 . LEU B 115 ? 0.3371 0.2929 0.3637 -0.0047 0.0150  -0.0408 124 LEU B CD1 
4000 C CD2 . LEU B 115 ? 0.3025 0.2578 0.3168 -0.0024 0.0112  -0.0333 124 LEU B CD2 
4001 N N   . VAL B 116 ? 0.2787 0.2265 0.3039 -0.0050 0.0115  -0.0329 125 VAL B N   
4002 C CA  . VAL B 116 ? 0.3068 0.2542 0.3272 -0.0060 0.0132  -0.0297 125 VAL B CA  
4003 C C   . VAL B 116 ? 0.3238 0.2730 0.3326 -0.0064 0.0194  -0.0298 125 VAL B C   
4004 O O   . VAL B 116 ? 0.2790 0.2296 0.2860 -0.0065 0.0222  -0.0327 125 VAL B O   
4005 C CB  . VAL B 116 ? 0.2854 0.2318 0.3119 -0.0048 0.0093  -0.0356 125 VAL B CB  
4006 C CG1 . VAL B 116 ? 0.2487 0.1908 0.2917 -0.0044 0.0008  -0.0363 125 VAL B CG1 
4007 C CG2 . VAL B 116 ? 0.2683 0.2199 0.2892 -0.0020 0.0125  -0.0447 125 VAL B CG2 
4008 N N   . TYR B 117 ? 0.3305 0.2798 0.3347 -0.0067 0.0208  -0.0259 126 TYR B N   
4009 C CA  . TYR B 117 ? 0.3145 0.2638 0.3101 -0.0065 0.0251  -0.0254 126 TYR B CA  
4010 C C   . TYR B 117 ? 0.3221 0.2730 0.3154 -0.0066 0.0281  -0.0289 126 TYR B C   
4011 O O   . TYR B 117 ? 0.3133 0.2636 0.3048 -0.0076 0.0312  -0.0275 126 TYR B O   
4012 C CB  . TYR B 117 ? 0.3299 0.2802 0.3237 -0.0061 0.0248  -0.0217 126 TYR B CB  
4013 C CG  . TYR B 117 ? 0.3201 0.2696 0.3068 -0.0051 0.0279  -0.0204 126 TYR B CG  
4014 C CD1 . TYR B 117 ? 0.3281 0.2776 0.3119 -0.0033 0.0289  -0.0187 126 TYR B CD1 
4015 C CD2 . TYR B 117 ? 0.3138 0.2636 0.2969 -0.0047 0.0289  -0.0211 126 TYR B CD2 
4016 C CE1 . TYR B 117 ? 0.3322 0.2795 0.3125 -0.0015 0.0301  -0.0184 126 TYR B CE1 
4017 C CE2 . TYR B 117 ? 0.3768 0.3250 0.3553 -0.0037 0.0308  -0.0181 126 TYR B CE2 
4018 C CZ  . TYR B 117 ? 0.3687 0.3142 0.3471 -0.0023 0.0310  -0.0171 126 TYR B CZ  
4019 O OH  . TYR B 117 ? 0.3980 0.3403 0.3747 -0.0005 0.0313  -0.0151 126 TYR B OH  
4020 N N   . ALA B 118 ? 0.2928 0.2471 0.2878 -0.0051 0.0266  -0.0331 127 ALA B N   
4021 C CA  . ALA B 118 ? 0.2858 0.2473 0.2776 -0.0036 0.0302  -0.0359 127 ALA B CA  
4022 C C   . ALA B 118 ? 0.3078 0.2730 0.3045 -0.0047 0.0332  -0.0368 127 ALA B C   
4023 O O   . ALA B 118 ? 0.3349 0.3077 0.3301 -0.0049 0.0384  -0.0344 127 ALA B O   
4024 C CB  . ALA B 118 ? 0.3123 0.2791 0.3046 0.0005  0.0265  -0.0434 127 ALA B CB  
4025 N N   . ASP B 119 ? 0.3189 0.2805 0.3227 -0.0053 0.0300  -0.0389 128 ASP B N   
4026 C CA  . ASP B 119 ? 0.2942 0.2593 0.3048 -0.0065 0.0316  -0.0401 128 ASP B CA  
4027 C C   . ASP B 119 ? 0.2881 0.2486 0.2990 -0.0098 0.0328  -0.0355 128 ASP B C   
4028 O O   . ASP B 119 ? 0.3027 0.2668 0.3175 -0.0121 0.0365  -0.0326 128 ASP B O   
4029 C CB  . ASP B 119 ? 0.3003 0.2635 0.3189 -0.0050 0.0262  -0.0442 128 ASP B CB  
4030 C CG  . ASP B 119 ? 0.3254 0.2901 0.3482 -0.0012 0.0221  -0.0504 128 ASP B CG  
4031 O OD1 . ASP B 119 ? 0.2977 0.2710 0.3193 0.0021  0.0244  -0.0558 128 ASP B OD1 
4032 O OD2 . ASP B 119 ? 0.2876 0.2457 0.3160 -0.0009 0.0160  -0.0496 128 ASP B OD2 
4033 N N   . CYS B 120 ? 0.2855 0.2392 0.2938 -0.0094 0.0290  -0.0347 129 CYS B N   
4034 C CA  . CYS B 120 ? 0.3198 0.2698 0.3296 -0.0103 0.0274  -0.0346 129 CYS B CA  
4035 C C   . CYS B 120 ? 0.3098 0.2553 0.3165 -0.0110 0.0289  -0.0317 129 CYS B C   
4036 O O   . CYS B 120 ? 0.3046 0.2463 0.3160 -0.0114 0.0264  -0.0335 129 CYS B O   
4037 C CB  . CYS B 120 ? 0.3085 0.2575 0.3153 -0.0075 0.0227  -0.0357 129 CYS B CB  
4038 S SG  . CYS B 120 ? 0.3202 0.2692 0.3181 -0.0052 0.0226  -0.0307 129 CYS B SG  
4039 N N   . VAL B 121 ? 0.3268 0.2725 0.3273 -0.0106 0.0316  -0.0281 130 VAL B N   
4040 C CA  . VAL B 121 ? 0.3276 0.2692 0.3268 -0.0111 0.0329  -0.0241 130 VAL B CA  
4041 C C   . VAL B 121 ? 0.3269 0.2736 0.3274 -0.0133 0.0375  -0.0186 130 VAL B C   
4042 O O   . VAL B 121 ? 0.3132 0.2594 0.3222 -0.0164 0.0389  -0.0139 130 VAL B O   
4043 C CB  . VAL B 121 ? 0.3315 0.2711 0.3225 -0.0080 0.0319  -0.0232 130 VAL B CB  
4044 C CG1 . VAL B 121 ? 0.3668 0.3015 0.3579 -0.0075 0.0321  -0.0195 130 VAL B CG1 
4045 C CG2 . VAL B 121 ? 0.3300 0.2697 0.3190 -0.0050 0.0287  -0.0267 130 VAL B CG2 
4046 N N   . LEU B 122 ? 0.3226 0.2758 0.3162 -0.0114 0.0394  -0.0188 131 LEU B N   
4047 C CA  . LEU B 122 ? 0.3282 0.2899 0.3184 -0.0110 0.0438  -0.0134 131 LEU B CA  
4048 C C   . LEU B 122 ? 0.3496 0.3222 0.3470 -0.0129 0.0485  -0.0108 131 LEU B C   
4049 O O   . LEU B 122 ? 0.3396 0.3205 0.3369 -0.0138 0.0532  -0.0020 131 LEU B O   
4050 C CB  . LEU B 122 ? 0.3390 0.3062 0.3197 -0.0068 0.0426  -0.0175 131 LEU B CB  
4051 C CG  . LEU B 122 ? 0.3285 0.2882 0.3051 -0.0054 0.0384  -0.0184 131 LEU B CG  
4052 C CD1 . LEU B 122 ? 0.3303 0.2959 0.3018 -0.0018 0.0357  -0.0230 131 LEU B CD1 
4053 C CD2 . LEU B 122 ? 0.3310 0.2852 0.3061 -0.0060 0.0390  -0.0114 131 LEU B CD2 
4054 N N   . ALA B 123 ? 0.3497 0.3241 0.3542 -0.0134 0.0474  -0.0170 132 ALA B N   
4055 C CA  . ALA B 123 ? 0.3341 0.3216 0.3479 -0.0147 0.0520  -0.0154 132 ALA B CA  
4056 C C   . ALA B 123 ? 0.3205 0.3035 0.3501 -0.0197 0.0502  -0.0142 132 ALA B C   
4057 O O   . ALA B 123 ? 0.3101 0.3049 0.3512 -0.0218 0.0540  -0.0115 132 ALA B O   
4058 C CB  . ALA B 123 ? 0.3245 0.3208 0.3361 -0.0097 0.0513  -0.0253 132 ALA B CB  
4059 N N   . ASN B 124 ? 0.3046 0.2727 0.3356 -0.0209 0.0442  -0.0167 133 ASN B N   
4060 C CA  . ASN B 124 ? 0.3234 0.2859 0.3679 -0.0237 0.0393  -0.0199 133 ASN B CA  
4061 C C   . ASN B 124 ? 0.3110 0.2662 0.3678 -0.0282 0.0375  -0.0134 133 ASN B C   
4062 O O   . ASN B 124 ? 0.3142 0.2576 0.3742 -0.0275 0.0304  -0.0186 133 ASN B O   
4063 C CB  . ASN B 124 ? 0.2911 0.2450 0.3279 -0.0199 0.0327  -0.0286 133 ASN B CB  
4064 C CG  . ASN B 124 ? 0.3339 0.2849 0.3815 -0.0205 0.0263  -0.0346 133 ASN B CG  
4065 O OD1 . ASN B 124 ? 0.3299 0.2858 0.3931 -0.0241 0.0263  -0.0339 133 ASN B OD1 
4066 N ND2 . ASN B 124 ? 0.2874 0.2327 0.3269 -0.0163 0.0205  -0.0405 133 ASN B ND2 
4067 N N   . TRP B 125 ? 0.3221 0.2854 0.3867 -0.0320 0.0434  -0.0019 134 TRP B N   
4068 C CA  . TRP B 125 ? 0.3239 0.2789 0.4032 -0.0367 0.0409  0.0069  134 TRP B CA  
4069 C C   . TRP B 125 ? 0.3457 0.3138 0.4421 -0.0428 0.0474  0.0222  134 TRP B C   
4070 O O   . TRP B 125 ? 0.3494 0.3365 0.4411 -0.0420 0.0558  0.0268  134 TRP B O   
4071 C CB  . TRP B 125 ? 0.3256 0.2703 0.3920 -0.0335 0.0395  0.0092  134 TRP B CB  
4072 C CG  . TRP B 125 ? 0.3104 0.2659 0.3629 -0.0317 0.0471  0.0187  134 TRP B CG  
4073 C CD1 . TRP B 125 ? 0.3118 0.2742 0.3446 -0.0262 0.0499  0.0132  134 TRP B CD1 
4074 C CD2 . TRP B 125 ? 0.3504 0.3123 0.4089 -0.0348 0.0517  0.0354  134 TRP B CD2 
4075 N NE1 . TRP B 125 ? 0.3271 0.3003 0.3513 -0.0248 0.0555  0.0231  134 TRP B NE1 
4076 C CE2 . TRP B 125 ? 0.3396 0.3138 0.3779 -0.0298 0.0574  0.0380  134 TRP B CE2 
4077 C CE3 . TRP B 125 ? 0.3468 0.3056 0.4276 -0.0413 0.0508  0.0494  134 TRP B CE3 
4078 C CZ2 . TRP B 125 ? 0.3484 0.3340 0.3843 -0.0300 0.0629  0.0541  134 TRP B CZ2 
4079 C CZ3 . TRP B 125 ? 0.3654 0.3345 0.4463 -0.0428 0.0568  0.0681  134 TRP B CZ3 
4080 C CH2 . TRP B 125 ? 0.3933 0.3769 0.4500 -0.0367 0.0632  0.0704  134 TRP B CH2 
4081 N N   . LYS B 126 ? 0.3743 0.3329 0.4924 -0.0486 0.0426  0.0301  135 LYS B N   
4082 C CA  . LYS B 126 ? 0.3735 0.3432 0.5129 -0.0560 0.0480  0.0495  135 LYS B CA  
4083 C C   . LYS B 126 ? 0.3867 0.3385 0.5438 -0.0601 0.0406  0.0583  135 LYS B C   
4084 O O   . LYS B 126 ? 0.4086 0.3401 0.5672 -0.0575 0.0297  0.0455  135 LYS B O   
4085 C CB  . LYS B 126 ? 0.3655 0.3460 0.5295 -0.0617 0.0482  0.0499  135 LYS B CB  
4086 C CG  . LYS B 126 ? 0.3903 0.3530 0.5746 -0.0642 0.0348  0.0371  135 LYS B CG  
4087 C CD  . LYS B 126 ? 0.4130 0.3885 0.6234 -0.0699 0.0347  0.0379  135 LYS B CD  
4088 C CE  . LYS B 126 ? 0.4726 0.4560 0.7179 -0.0806 0.0371  0.0597  135 LYS B CE  
4089 N NZ  . LYS B 126 ? 0.4949 0.4969 0.7668 -0.0865 0.0396  0.0633  135 LYS B NZ  
4090 N N   . LYS B 127 ? 0.4186 0.3799 0.5891 -0.0657 0.0463  0.0806  136 LYS B N   
4091 C CA  . LYS B 127 ? 0.4484 0.3944 0.6470 -0.0721 0.0387  0.0935  136 LYS B CA  
4092 C C   . LYS B 127 ? 0.4811 0.4276 0.7180 -0.0813 0.0338  0.0971  136 LYS B C   
4093 O O   . LYS B 127 ? 0.4699 0.4387 0.7135 -0.0849 0.0423  0.1032  136 LYS B O   
4094 C CB  . LYS B 127 ? 0.4627 0.4211 0.6613 -0.0746 0.0473  0.1201  136 LYS B CB  
4095 C CG  . LYS B 127 ? 0.4799 0.4285 0.6542 -0.0674 0.0461  0.1199  136 LYS B CG  
4096 C CD  . LYS B 127 ? 0.4874 0.4494 0.6655 -0.0703 0.0533  0.1490  136 LYS B CD  
4097 C CE  . LYS B 127 ? 0.5417 0.4935 0.6993 -0.0633 0.0504  0.1501  136 LYS B CE  
4098 N NZ  . LYS B 127 ? 0.4993 0.4584 0.6680 -0.0669 0.0535  0.1803  136 LYS B NZ  
4099 N N   . LYS B 128 ? 0.5133 0.4363 0.7773 -0.0847 0.0193  0.0926  137 LYS B N   
4100 C CA  . LYS B 128 ? 0.5337 0.4551 0.8413 -0.0947 0.0120  0.0977  137 LYS B CA  
4101 C C   . LYS B 128 ? 0.5476 0.4812 0.8827 -0.1051 0.0189  0.1308  137 LYS B C   
4102 O O   . LYS B 128 ? 0.5572 0.5133 0.9118 -0.1126 0.0269  0.1451  137 LYS B O   
4103 C CB  . LYS B 128 ? 0.5407 0.4326 0.8695 -0.0935 -0.0081 0.0795  137 LYS B CB  
4104 C CG  . LYS B 128 ? 0.5498 0.4347 0.8538 -0.0832 -0.0148 0.0486  137 LYS B CG  
4105 C CD  . LYS B 128 ? 0.5688 0.4275 0.8883 -0.0787 -0.0344 0.0293  137 LYS B CD  
4106 C CE  . LYS B 128 ? 0.5923 0.4496 0.8956 -0.0697 -0.0420 0.0008  137 LYS B CE  
4107 N NZ  . LYS B 128 ? 0.6345 0.4701 0.9485 -0.0624 -0.0611 -0.0206 137 LYS B NZ  
4108 N N   . ASP B 129 ? 0.5889 0.5097 0.9256 -0.1049 0.0161  0.1439  138 ASP B N   
4109 C CA  . ASP B 129 ? 0.6306 0.5634 0.9888 -0.1134 0.0231  0.1788  138 ASP B CA  
4110 C C   . ASP B 129 ? 0.6555 0.6062 0.9726 -0.1059 0.0375  0.1901  138 ASP B C   
4111 O O   . ASP B 129 ? 0.6442 0.5785 0.9398 -0.0983 0.0328  0.1824  138 ASP B O   
4112 C CB  . ASP B 129 ? 0.6541 0.5578 1.0498 -0.1188 0.0068  0.1871  138 ASP B CB  
4113 C CG  . ASP B 129 ? 0.6561 0.5716 1.0851 -0.1302 0.0120  0.2271  138 ASP B CG  
4114 O OD1 . ASP B 129 ? 0.6498 0.5980 1.0630 -0.1312 0.0301  0.2493  138 ASP B OD1 
4115 O OD2 . ASP B 129 ? 0.6955 0.5883 1.1678 -0.1376 -0.0026 0.2367  138 ASP B OD2 
4116 N N   . PRO B 130 ? 0.6892 0.6753 0.9960 -0.1071 0.0545  0.2072  139 PRO B N   
4117 C CA  . PRO B 130 ? 0.6929 0.7004 0.9642 -0.0998 0.0676  0.2201  139 PRO B CA  
4118 C C   . PRO B 130 ? 0.7149 0.7133 0.9920 -0.1010 0.0647  0.2438  139 PRO B C   
4119 O O   . PRO B 130 ? 0.7291 0.7323 0.9719 -0.0920 0.0690  0.2437  139 PRO B O   
4120 C CB  . PRO B 130 ? 0.7186 0.7673 0.9937 -0.1030 0.0841  0.2387  139 PRO B CB  
4121 C CG  . PRO B 130 ? 0.7021 0.7505 0.9984 -0.1077 0.0808  0.2232  139 PRO B CG  
4122 C CD  . PRO B 130 ? 0.6963 0.7070 1.0246 -0.1141 0.0620  0.2135  139 PRO B CD  
4123 N N   . ASN B 131 ? 0.7209 0.7056 1.0430 -0.1120 0.0563  0.2636  140 ASN B N   
4124 C CA  . ASN B 131 ? 0.7350 0.7079 1.0695 -0.1139 0.0514  0.2879  140 ASN B CA  
4125 C C   . ASN B 131 ? 0.7302 0.6640 1.0608 -0.1077 0.0345  0.2677  140 ASN B C   
4126 O O   . ASN B 131 ? 0.7356 0.6583 1.0739 -0.1074 0.0294  0.2855  140 ASN B O   
4127 C CB  . ASN B 131 ? 0.7715 0.7453 1.1617 -0.1289 0.0480  0.3201  140 ASN B CB  
4128 C CG  . ASN B 131 ? 0.7861 0.8039 1.1831 -0.1352 0.0664  0.3466  140 ASN B CG  
4129 O OD1 . ASN B 131 ? 0.7499 0.7976 1.1095 -0.1272 0.0810  0.3384  140 ASN B OD1 
4130 N ND2 . ASN B 131 ? 0.8721 0.8951 1.3196 -0.1491 0.0651  0.3786  140 ASN B ND2 
4131 N N   . LYS B 132 ? 0.6994 0.6144 1.0195 -0.1021 0.0258  0.2321  141 LYS B N   
4132 C CA  . LYS B 132 ? 0.6845 0.5673 0.9984 -0.0941 0.0110  0.2101  141 LYS B CA  
4133 C C   . LYS B 132 ? 0.6536 0.5422 0.9166 -0.0812 0.0170  0.1883  141 LYS B C   
4134 O O   . LYS B 132 ? 0.6205 0.5310 0.8577 -0.0787 0.0286  0.1809  141 LYS B O   
4135 C CB  . LYS B 132 ? 0.6773 0.5347 1.0209 -0.0964 -0.0055 0.1866  141 LYS B CB  
4136 C CG  . LYS B 132 ? 0.7122 0.5514 1.1118 -0.1071 -0.0190 0.2041  141 LYS B CG  
4137 C CD  . LYS B 132 ? 0.7203 0.5300 1.1454 -0.1052 -0.0395 0.1747  141 LYS B CD  
4138 C CE  . LYS B 132 ? 0.7559 0.5443 1.2412 -0.1156 -0.0559 0.1906  141 LYS B CE  
4139 N NZ  . LYS B 132 ? 0.7559 0.5132 1.2627 -0.1098 -0.0788 0.1584  141 LYS B NZ  
4140 N N   . PRO B 133 ? 0.6343 0.5035 0.8856 -0.0729 0.0084  0.1781  142 PRO B N   
4141 C CA  . PRO B 133 ? 0.6073 0.4825 0.8151 -0.0617 0.0135  0.1600  142 PRO B CA  
4142 C C   . PRO B 133 ? 0.5598 0.4340 0.7508 -0.0570 0.0129  0.1294  142 PRO B C   
4143 O O   . PRO B 133 ? 0.5633 0.4310 0.7742 -0.0612 0.0074  0.1189  142 PRO B O   
4144 C CB  . PRO B 133 ? 0.6130 0.4668 0.8221 -0.0549 0.0026  0.1573  142 PRO B CB  
4145 C CG  . PRO B 133 ? 0.6684 0.4984 0.9211 -0.0606 -0.0117 0.1614  142 PRO B CG  
4146 C CD  . PRO B 133 ? 0.6562 0.4980 0.9368 -0.0734 -0.0068 0.1835  142 PRO B CD  
4147 N N   . LEU B 134 ? 0.5196 0.4016 0.6750 -0.0483 0.0181  0.1169  143 LEU B N   
4148 C CA  . LEU B 134 ? 0.4905 0.3726 0.6274 -0.0430 0.0179  0.0910  143 LEU B CA  
4149 C C   . LEU B 134 ? 0.4782 0.3385 0.6197 -0.0366 0.0053  0.0714  143 LEU B C   
4150 O O   . LEU B 134 ? 0.4602 0.3180 0.5831 -0.0285 0.0043  0.0637  143 LEU B O   
4151 C CB  . LEU B 134 ? 0.4808 0.3805 0.5824 -0.0371 0.0277  0.0874  143 LEU B CB  
4152 C CG  . LEU B 134 ? 0.5205 0.4454 0.6138 -0.0404 0.0399  0.1005  143 LEU B CG  
4153 C CD1 . LEU B 134 ? 0.5616 0.5012 0.6228 -0.0330 0.0462  0.0969  143 LEU B CD1 
4154 C CD2 . LEU B 134 ? 0.4978 0.4299 0.5985 -0.0444 0.0426  0.0916  143 LEU B CD2 
4155 N N   . THR B 135 ? 0.4776 0.3242 0.6458 -0.0396 -0.0047 0.0634  144 THR B N   
4156 C CA  . THR B 135 ? 0.4754 0.3049 0.6488 -0.0319 -0.0175 0.0406  144 THR B CA  
4157 C C   . THR B 135 ? 0.4472 0.2797 0.6216 -0.0320 -0.0200 0.0226  144 THR B C   
4158 O O   . THR B 135 ? 0.4143 0.2561 0.5980 -0.0400 -0.0153 0.0298  144 THR B O   
4159 C CB  . THR B 135 ? 0.5225 0.3301 0.7321 -0.0336 -0.0319 0.0442  144 THR B CB  
4160 O OG1 . THR B 135 ? 0.4741 0.2802 0.7155 -0.0447 -0.0347 0.0547  144 THR B OG1 
4161 C CG2 . THR B 135 ? 0.5569 0.3599 0.7690 -0.0333 -0.0313 0.0639  144 THR B CG2 
4162 N N   . TYR B 136 ? 0.4326 0.2590 0.5984 -0.0223 -0.0277 -0.0004 145 TYR B N   
4163 C CA  . TYR B 136 ? 0.4387 0.2691 0.6022 -0.0201 -0.0313 -0.0187 145 TYR B CA  
4164 C C   . TYR B 136 ? 0.4593 0.2836 0.6562 -0.0286 -0.0391 -0.0171 145 TYR B C   
4165 O O   . TYR B 136 ? 0.4379 0.2730 0.6336 -0.0327 -0.0354 -0.0192 145 TYR B O   
4166 C CB  . TYR B 136 ? 0.4188 0.2438 0.5730 -0.0069 -0.0409 -0.0424 145 TYR B CB  
4167 C CG  . TYR B 136 ? 0.4128 0.2472 0.5558 -0.0026 -0.0425 -0.0596 145 TYR B CG  
4168 C CD1 . TYR B 136 ? 0.3833 0.2343 0.4965 0.0003  -0.0318 -0.0606 145 TYR B CD1 
4169 C CD2 . TYR B 136 ? 0.4617 0.2886 0.6259 -0.0014 -0.0560 -0.0745 145 TYR B CD2 
4170 C CE1 . TYR B 136 ? 0.3962 0.2566 0.4993 0.0044  -0.0335 -0.0737 145 TYR B CE1 
4171 C CE2 . TYR B 136 ? 0.4344 0.2719 0.5866 0.0036  -0.0581 -0.0898 145 TYR B CE2 
4172 C CZ  . TYR B 136 ? 0.4025 0.2569 0.5234 0.0064  -0.0463 -0.0880 145 TYR B CZ  
4173 O OH  . TYR B 136 ? 0.4269 0.2923 0.5361 0.0114  -0.0483 -0.1002 145 TYR B OH  
4174 N N   . GLU B 137 ? 0.4588 0.2659 0.6878 -0.0315 -0.0504 -0.0125 146 GLU B N   
4175 C CA  . GLU B 137 ? 0.4908 0.2887 0.7590 -0.0393 -0.0618 -0.0130 146 GLU B CA  
4176 C C   . GLU B 137 ? 0.4661 0.2761 0.7500 -0.0536 -0.0513 0.0126  146 GLU B C   
4177 O O   . GLU B 137 ? 0.4752 0.2849 0.7883 -0.0611 -0.0573 0.0130  146 GLU B O   
4178 C CB  . GLU B 137 ? 0.5342 0.3081 0.8366 -0.0380 -0.0790 -0.0153 146 GLU B CB  
4179 C CG  . GLU B 137 ? 0.6378 0.4009 0.9287 -0.0219 -0.0912 -0.0432 146 GLU B CG  
4180 C CD  . GLU B 137 ? 0.7347 0.5016 0.9951 -0.0133 -0.0826 -0.0402 146 GLU B CD  
4181 O OE1 . GLU B 137 ? 0.7696 0.5405 1.0250 -0.0198 -0.0717 -0.0159 146 GLU B OE1 
4182 O OE2 . GLU B 137 ? 0.7601 0.5285 1.0010 0.0005  -0.0868 -0.0622 146 GLU B OE2 
4183 N N   . ASN B 138 ? 0.4473 0.2698 0.7130 -0.0564 -0.0364 0.0336  147 ASN B N   
4184 C CA  . ASN B 138 ? 0.4495 0.2907 0.7227 -0.0672 -0.0235 0.0577  147 ASN B CA  
4185 C C   . ASN B 138 ? 0.4192 0.2829 0.6583 -0.0645 -0.0092 0.0534  147 ASN B C   
4186 O O   . ASN B 138 ? 0.4336 0.3167 0.6679 -0.0696 0.0038  0.0714  147 ASN B O   
4187 C CB  . ASN B 138 ? 0.4490 0.2920 0.7264 -0.0712 -0.0173 0.0852  147 ASN B CB  
4188 C CG  . ASN B 138 ? 0.4605 0.3259 0.7500 -0.0819 -0.0045 0.1125  147 ASN B CG  
4189 O OD1 . ASN B 138 ? 0.4853 0.3551 0.8044 -0.0905 -0.0066 0.1168  147 ASN B OD1 
4190 N ND2 . ASN B 138 ? 0.4802 0.3623 0.7467 -0.0806 0.0087  0.1304  147 ASN B ND2 
4191 N N   . MET B 139 ? 0.4188 0.2813 0.6355 -0.0560 -0.0120 0.0299  148 MET B N   
4192 C CA  . MET B 139 ? 0.4184 0.2991 0.6057 -0.0530 -0.0007 0.0252  148 MET B CA  
4193 C C   . MET B 139 ? 0.3973 0.2788 0.5847 -0.0502 -0.0068 0.0054  148 MET B C   
4194 O O   . MET B 139 ? 0.3955 0.2633 0.5956 -0.0470 -0.0201 -0.0096 148 MET B O   
4195 C CB  . MET B 139 ? 0.3863 0.2684 0.5394 -0.0444 0.0047  0.0213  148 MET B CB  
4196 C CG  . MET B 139 ? 0.4300 0.3174 0.5775 -0.0464 0.0127  0.0414  148 MET B CG  
4197 S SD  . MET B 139 ? 0.4510 0.3359 0.5670 -0.0365 0.0146  0.0359  148 MET B SD  
4198 C CE  . MET B 139 ? 0.4246 0.3286 0.5124 -0.0336 0.0247  0.0286  148 MET B CE  
4199 N N   A ASP B 140 ? 0.3966 0.2947 0.5699 -0.0505 0.0021  0.0049  149 ASP B N   
4200 N N   B ASP B 140 ? 0.3929 0.2913 0.5670 -0.0508 0.0023  0.0054  149 ASP B N   
4201 C CA  A ASP B 140 ? 0.3952 0.2957 0.5613 -0.0460 -0.0027 -0.0131 149 ASP B CA  
4202 C CA  B ASP B 140 ? 0.3911 0.2931 0.5588 -0.0469 -0.0019 -0.0117 149 ASP B CA  
4203 C C   A ASP B 140 ? 0.3775 0.2924 0.5154 -0.0421 0.0078  -0.0140 149 ASP B C   
4204 C C   B ASP B 140 ? 0.3714 0.2857 0.5077 -0.0417 0.0079  -0.0142 149 ASP B C   
4205 O O   A ASP B 140 ? 0.3620 0.2879 0.4914 -0.0441 0.0186  -0.0017 149 ASP B O   
4206 O O   B ASP B 140 ? 0.3447 0.2674 0.4687 -0.0423 0.0179  -0.0030 149 ASP B O   
4207 C CB  A ASP B 140 ? 0.4009 0.3047 0.5977 -0.0529 -0.0083 -0.0138 149 ASP B CB  
4208 C CB  B ASP B 140 ? 0.3967 0.3071 0.5922 -0.0547 -0.0033 -0.0084 149 ASP B CB  
4209 C CG  A ASP B 140 ? 0.3998 0.2995 0.5958 -0.0469 -0.0200 -0.0352 149 ASP B CG  
4210 C CG  B ASP B 140 ? 0.3993 0.2959 0.6242 -0.0564 -0.0194 -0.0190 149 ASP B CG  
4211 O OD1 A ASP B 140 ? 0.3234 0.2235 0.4918 -0.0377 -0.0204 -0.0472 149 ASP B OD1 
4212 O OD1 B ASP B 140 ? 0.4510 0.3370 0.6662 -0.0480 -0.0300 -0.0376 149 ASP B OD1 
4213 O OD2 A ASP B 140 ? 0.3949 0.2926 0.6197 -0.0515 -0.0292 -0.0392 149 ASP B OD2 
4214 O OD2 B ASP B 140 ? 0.3727 0.2710 0.6317 -0.0659 -0.0219 -0.0090 149 ASP B OD2 
4215 N N   . VAL B 141 ? 0.3852 0.3006 0.5097 -0.0359 0.0036  -0.0289 150 VAL B N   
4216 C CA  . VAL B 141 ? 0.3763 0.3037 0.4804 -0.0327 0.0108  -0.0305 150 VAL B CA  
4217 C C   . VAL B 141 ? 0.3755 0.3146 0.4944 -0.0371 0.0128  -0.0291 150 VAL B C   
4218 O O   . VAL B 141 ? 0.3674 0.3050 0.5105 -0.0415 0.0065  -0.0304 150 VAL B O   
4219 C CB  . VAL B 141 ? 0.3709 0.2962 0.4553 -0.0243 0.0061  -0.0433 150 VAL B CB  
4220 C CG1 . VAL B 141 ? 0.4667 0.3856 0.5355 -0.0195 0.0068  -0.0432 150 VAL B CG1 
4221 C CG2 . VAL B 141 ? 0.4445 0.3663 0.5386 -0.0213 -0.0055 -0.0564 150 VAL B CG2 
4222 N N   . LEU B 142 ? 0.3566 0.3078 0.4633 -0.0355 0.0206  -0.0271 151 LEU B N   
4223 C CA  . LEU B 142 ? 0.3616 0.3262 0.4807 -0.0376 0.0227  -0.0275 151 LEU B CA  
4224 C C   . LEU B 142 ? 0.3716 0.3348 0.4879 -0.0331 0.0147  -0.0403 151 LEU B C   
4225 O O   . LEU B 142 ? 0.3777 0.3468 0.5122 -0.0354 0.0109  -0.0434 151 LEU B O   
4226 C CB  . LEU B 142 ? 0.3457 0.3254 0.4551 -0.0363 0.0337  -0.0214 151 LEU B CB  
4227 C CG  . LEU B 142 ? 0.3203 0.3060 0.4287 -0.0393 0.0422  -0.0077 151 LEU B CG  
4228 C CD1 . LEU B 142 ? 0.3347 0.3382 0.4315 -0.0353 0.0514  -0.0058 151 LEU B CD1 
4229 C CD2 . LEU B 142 ? 0.3267 0.3167 0.4622 -0.0475 0.0431  0.0041  151 LEU B CD2 
4230 N N   . PHE B 143 ? 0.3700 0.3272 0.4649 -0.0266 0.0122  -0.0463 152 PHE B N   
4231 C CA  . PHE B 143 ? 0.3549 0.3132 0.4444 -0.0214 0.0053  -0.0554 152 PHE B CA  
4232 C C   . PHE B 143 ? 0.3571 0.3077 0.4306 -0.0151 -0.0010 -0.0614 152 PHE B C   
4233 O O   . PHE B 143 ? 0.3377 0.2836 0.3975 -0.0133 0.0024  -0.0582 152 PHE B O   
4234 C CB  . PHE B 143 ? 0.3394 0.3057 0.4210 -0.0187 0.0098  -0.0541 152 PHE B CB  
4235 C CG  . PHE B 143 ? 0.3152 0.2932 0.4096 -0.0223 0.0169  -0.0498 152 PHE B CG  
4236 C CD1 . PHE B 143 ? 0.3534 0.3406 0.4674 -0.0243 0.0146  -0.0523 152 PHE B CD1 
4237 C CD2 . PHE B 143 ? 0.3345 0.3171 0.4218 -0.0228 0.0257  -0.0435 152 PHE B CD2 
4238 C CE1 . PHE B 143 ? 0.3178 0.3203 0.4443 -0.0267 0.0225  -0.0477 152 PHE B CE1 
4239 C CE2 . PHE B 143 ? 0.3436 0.3416 0.4406 -0.0242 0.0331  -0.0398 152 PHE B CE2 
4240 C CZ  . PHE B 143 ? 0.3785 0.3875 0.4954 -0.0261 0.0322  -0.0415 152 PHE B CZ  
4241 N N   . SER B 144 ? 0.3558 0.3075 0.4316 -0.0112 -0.0102 -0.0702 153 SER B N   
4242 C CA  . SER B 144 ? 0.3516 0.3023 0.4113 -0.0031 -0.0165 -0.0769 153 SER B CA  
4243 C C   . SER B 144 ? 0.3387 0.2980 0.3915 0.0017  -0.0201 -0.0783 153 SER B C   
4244 O O   . SER B 144 ? 0.3273 0.2908 0.3913 -0.0014 -0.0194 -0.0766 153 SER B O   
4245 C CB  . SER B 144 ? 0.3607 0.3064 0.4312 -0.0011 -0.0270 -0.0880 153 SER B CB  
4246 O OG  . SER B 144 ? 0.4225 0.3714 0.5117 -0.0031 -0.0344 -0.0940 153 SER B OG  
4247 N N   . PHE B 145 ? 0.3421 0.3058 0.3775 0.0098  -0.0239 -0.0807 154 PHE B N   
4248 C CA  . PHE B 145 ? 0.3311 0.3040 0.3585 0.0152  -0.0279 -0.0792 154 PHE B CA  
4249 C C   . PHE B 145 ? 0.3367 0.3154 0.3660 0.0216  -0.0398 -0.0911 154 PHE B C   
4250 O O   . PHE B 145 ? 0.3297 0.3126 0.3683 0.0216  -0.0451 -0.0932 154 PHE B O   
4251 C CB  . PHE B 145 ? 0.3624 0.3406 0.3699 0.0201  -0.0236 -0.0703 154 PHE B CB  
4252 C CG  . PHE B 145 ? 0.3360 0.3090 0.3441 0.0142  -0.0142 -0.0598 154 PHE B CG  
4253 C CD1 . PHE B 145 ? 0.3604 0.3329 0.3762 0.0110  -0.0127 -0.0539 154 PHE B CD1 
4254 C CD2 . PHE B 145 ? 0.3596 0.3282 0.3622 0.0126  -0.0083 -0.0574 154 PHE B CD2 
4255 C CE1 . PHE B 145 ? 0.3366 0.3045 0.3540 0.0069  -0.0060 -0.0472 154 PHE B CE1 
4256 C CE2 . PHE B 145 ? 0.3771 0.3417 0.3808 0.0079  -0.0013 -0.0493 154 PHE B CE2 
4257 C CZ  . PHE B 145 ? 0.3805 0.3448 0.3915 0.0052  -0.0005 -0.0449 154 PHE B CZ  
4258 N N   . ARG B 146 ? 0.3293 0.3088 0.3504 0.0280  -0.0449 -0.1002 155 ARG B N   
4259 C CA  . ARG B 146 ? 0.3499 0.3359 0.3709 0.0365  -0.0581 -0.1151 155 ARG B CA  
4260 C C   . ARG B 146 ? 0.3678 0.3441 0.4015 0.0361  -0.0643 -0.1282 155 ARG B C   
4261 O O   . ARG B 146 ? 0.3442 0.3119 0.3781 0.0327  -0.0578 -0.1245 155 ARG B O   
4262 C CB  . ARG B 146 ? 0.3519 0.3534 0.3462 0.0492  -0.0600 -0.1151 155 ARG B CB  
4263 C CG  . ARG B 146 ? 0.4075 0.4182 0.3895 0.0496  -0.0534 -0.0981 155 ARG B CG  
4264 C CD  . ARG B 146 ? 0.4042 0.4173 0.3965 0.0481  -0.0593 -0.0969 155 ARG B CD  
4265 N NE  . ARG B 146 ? 0.3978 0.4233 0.3838 0.0586  -0.0722 -0.1088 155 ARG B NE  
4266 C CZ  . ARG B 146 ? 0.5114 0.5547 0.4750 0.0702  -0.0751 -0.1051 155 ARG B CZ  
4267 N NH1 . ARG B 146 ? 0.5364 0.5876 0.4841 0.0717  -0.0656 -0.0880 155 ARG B NH1 
4268 N NH2 . ARG B 146 ? 0.5538 0.6093 0.5119 0.0806  -0.0881 -0.1182 155 ARG B NH2 
4269 N N   . ASP B 147 ? 0.4086 0.3860 0.4541 0.0402  -0.0784 -0.1440 156 ASP B N   
4270 C CA  . ASP B 147 ? 0.4328 0.3997 0.4937 0.0411  -0.0875 -0.1583 156 ASP B CA  
4271 C C   . ASP B 147 ? 0.4513 0.4249 0.4890 0.0548  -0.0901 -0.1677 156 ASP B C   
4272 O O   . ASP B 147 ? 0.4411 0.4318 0.4550 0.0664  -0.0920 -0.1704 156 ASP B O   
4273 C CB  . ASP B 147 ? 0.4583 0.4240 0.5434 0.0412  -0.1038 -0.1737 156 ASP B CB  
4274 C CG  . ASP B 147 ? 0.4658 0.4266 0.5793 0.0270  -0.1003 -0.1639 156 ASP B CG  
4275 O OD1 . ASP B 147 ? 0.4525 0.4053 0.5758 0.0160  -0.0883 -0.1496 156 ASP B OD1 
4276 O OD2 . ASP B 147 ? 0.4899 0.4572 0.6157 0.0278  -0.1100 -0.1710 156 ASP B OD2 
4277 N N   . GLY B 148 ? 0.4753 0.4371 0.5201 0.0537  -0.0896 -0.1713 157 GLY B N   
4278 C CA  . GLY B 148 ? 0.4739 0.4426 0.4980 0.0665  -0.0897 -0.1790 157 GLY B CA  
4279 C C   . GLY B 148 ? 0.4602 0.4391 0.4592 0.0674  -0.0736 -0.1617 157 GLY B C   
4280 O O   . GLY B 148 ? 0.4675 0.4586 0.4473 0.0794  -0.0726 -0.1666 157 GLY B O   
4281 N N   . ASP B 149 ? 0.4291 0.4044 0.4298 0.0556  -0.0615 -0.1422 158 ASP B N   
4282 C CA  . ASP B 149 ? 0.4161 0.3987 0.3985 0.0549  -0.0476 -0.1256 158 ASP B CA  
4283 C C   . ASP B 149 ? 0.4029 0.3750 0.3886 0.0512  -0.0408 -0.1215 158 ASP B C   
4284 O O   . ASP B 149 ? 0.3839 0.3617 0.3573 0.0506  -0.0305 -0.1091 158 ASP B O   
4285 C CB  . ASP B 149 ? 0.4068 0.3903 0.3899 0.0458  -0.0396 -0.1088 158 ASP B CB  
4286 C CG  . ASP B 149 ? 0.4122 0.3800 0.4164 0.0323  -0.0356 -0.1029 158 ASP B CG  
4287 O OD1 . ASP B 149 ? 0.4217 0.3775 0.4408 0.0283  -0.0379 -0.1081 158 ASP B OD1 
4288 O OD2 . ASP B 149 ? 0.3931 0.3618 0.3997 0.0263  -0.0304 -0.0926 158 ASP B OD2 
4289 N N   . CYS B 150 ? 0.4200 0.3765 0.4247 0.0482  -0.0473 -0.1306 159 CYS B N   
4290 C CA  . CYS B 150 ? 0.4274 0.3724 0.4381 0.0448  -0.0428 -0.1267 159 CYS B CA  
4291 C C   . CYS B 150 ? 0.4117 0.3524 0.4221 0.0336  -0.0296 -0.1074 159 CYS B C   
4292 O O   . CYS B 150 ? 0.3879 0.3272 0.3924 0.0337  -0.0231 -0.1010 159 CYS B O   
4293 C CB  . CYS B 150 ? 0.4419 0.3970 0.4361 0.0581  -0.0431 -0.1344 159 CYS B CB  
4294 S SG  . CYS B 150 ? 0.4700 0.4302 0.4651 0.0739  -0.0600 -0.1611 159 CYS B SG  
4295 N N   . SER B 151 ? 0.4042 0.3441 0.4216 0.0249  -0.0264 -0.0994 160 SER B N   
4296 C CA  . SER B 151 ? 0.3944 0.3324 0.4111 0.0161  -0.0153 -0.0839 160 SER B CA  
4297 C C   . SER B 151 ? 0.3812 0.3067 0.4128 0.0087  -0.0130 -0.0790 160 SER B C   
4298 O O   . SER B 151 ? 0.3611 0.2857 0.3871 0.0057  -0.0050 -0.0692 160 SER B O   
4299 C CB  . SER B 151 ? 0.4159 0.3590 0.4355 0.0111  -0.0130 -0.0785 160 SER B CB  
4300 O OG  . SER B 151 ? 0.4785 0.4178 0.5169 0.0069  -0.0190 -0.0837 160 SER B OG  
4301 N N   . LYS B 152 ? 0.3769 0.2934 0.4285 0.0063  -0.0210 -0.0854 161 LYS B N   
4302 C CA  . LYS B 152 ? 0.3818 0.2869 0.4496 -0.0002 -0.0198 -0.0783 161 LYS B CA  
4303 C C   . LYS B 152 ? 0.3640 0.2648 0.4219 0.0056  -0.0190 -0.0789 161 LYS B C   
4304 O O   . LYS B 152 ? 0.3070 0.2060 0.3615 0.0017  -0.0113 -0.0671 161 LYS B O   
4305 C CB  . LYS B 152 ? 0.4007 0.2963 0.4965 -0.0039 -0.0306 -0.0845 161 LYS B CB  
4306 C CG  . LYS B 152 ? 0.4465 0.3306 0.5631 -0.0116 -0.0300 -0.0736 161 LYS B CG  
4307 C CD  . LYS B 152 ? 0.4566 0.3308 0.6061 -0.0157 -0.0427 -0.0795 161 LYS B CD  
4308 C CE  . LYS B 152 ? 0.5243 0.3860 0.6976 -0.0228 -0.0439 -0.0672 161 LYS B CE  
4309 N NZ  . LYS B 152 ? 0.5927 0.4442 0.8046 -0.0284 -0.0577 -0.0716 161 LYS B NZ  
4310 N N   . GLY B 153 ? 0.3562 0.2573 0.4094 0.0160  -0.0274 -0.0934 162 GLY B N   
4311 C CA  . GLY B 153 ? 0.3704 0.2711 0.4137 0.0240  -0.0271 -0.0964 162 GLY B CA  
4312 C C   . GLY B 153 ? 0.3608 0.2718 0.3841 0.0239  -0.0150 -0.0849 162 GLY B C   
4313 O O   . GLY B 153 ? 0.3831 0.2898 0.4061 0.0225  -0.0108 -0.0775 162 GLY B O   
4314 N N   . PHE B 154 ? 0.3491 0.2733 0.3581 0.0250  -0.0104 -0.0826 163 PHE B N   
4315 C CA  . PHE B 154 ? 0.3404 0.2743 0.3347 0.0247  -0.0009 -0.0721 163 PHE B CA  
4316 C C   . PHE B 154 ? 0.3497 0.2779 0.3483 0.0147  0.0062  -0.0591 163 PHE B C   
4317 O O   . PHE B 154 ? 0.3496 0.2776 0.3442 0.0142  0.0107  -0.0526 163 PHE B O   
4318 C CB  . PHE B 154 ? 0.3558 0.3046 0.3375 0.0281  0.0009  -0.0710 163 PHE B CB  
4319 C CG  . PHE B 154 ? 0.3539 0.3117 0.3262 0.0266  0.0092  -0.0589 163 PHE B CG  
4320 C CD1 . PHE B 154 ? 0.3748 0.3403 0.3404 0.0323  0.0122  -0.0575 163 PHE B CD1 
4321 C CD2 . PHE B 154 ? 0.3537 0.3120 0.3271 0.0196  0.0132  -0.0497 163 PHE B CD2 
4322 C CE1 . PHE B 154 ? 0.3638 0.3376 0.3254 0.0298  0.0189  -0.0458 163 PHE B CE1 
4323 C CE2 . PHE B 154 ? 0.3628 0.3275 0.3322 0.0177  0.0187  -0.0393 163 PHE B CE2 
4324 C CZ  . PHE B 154 ? 0.3573 0.3298 0.3216 0.0223  0.0214  -0.0368 163 PHE B CZ  
4325 N N   . PHE B 155 ? 0.3514 0.2770 0.3581 0.0077  0.0067  -0.0561 164 PHE B N   
4326 C CA  . PHE B 155 ? 0.3371 0.2615 0.3461 0.0002  0.0135  -0.0455 164 PHE B CA  
4327 C C   . PHE B 155 ? 0.3561 0.2721 0.3736 -0.0030 0.0142  -0.0400 164 PHE B C   
4328 O O   . PHE B 155 ? 0.3033 0.2211 0.3155 -0.0050 0.0197  -0.0319 164 PHE B O   
4329 C CB  . PHE B 155 ? 0.3430 0.2701 0.3597 -0.0050 0.0143  -0.0444 164 PHE B CB  
4330 C CG  . PHE B 155 ? 0.3336 0.2686 0.3429 -0.0026 0.0138  -0.0466 164 PHE B CG  
4331 C CD1 . PHE B 155 ? 0.3309 0.2716 0.3286 0.0000  0.0169  -0.0426 164 PHE B CD1 
4332 C CD2 . PHE B 155 ? 0.3677 0.3048 0.3846 -0.0033 0.0097  -0.0513 164 PHE B CD2 
4333 C CE1 . PHE B 155 ? 0.3564 0.3039 0.3504 0.0017  0.0157  -0.0419 164 PHE B CE1 
4334 C CE2 . PHE B 155 ? 0.3537 0.2980 0.3647 -0.0007 0.0085  -0.0518 164 PHE B CE2 
4335 C CZ  . PHE B 155 ? 0.2685 0.2175 0.2683 0.0017  0.0116  -0.0463 164 PHE B CZ  
4336 N N   . LEU B 156 ? 0.3379 0.2449 0.3698 -0.0034 0.0078  -0.0440 165 LEU B N   
4337 C CA  . LEU B 156 ? 0.3698 0.2682 0.4132 -0.0071 0.0077  -0.0357 165 LEU B CA  
4338 C C   . LEU B 156 ? 0.3476 0.2420 0.3845 -0.0012 0.0065  -0.0364 165 LEU B C   
4339 O O   . LEU B 156 ? 0.3584 0.2511 0.3951 -0.0036 0.0101  -0.0260 165 LEU B O   
4340 C CB  . LEU B 156 ? 0.4048 0.2936 0.4722 -0.0111 0.0003  -0.0371 165 LEU B CB  
4341 C CG  . LEU B 156 ? 0.4582 0.3521 0.5385 -0.0188 0.0023  -0.0325 165 LEU B CG  
4342 C CD1 . LEU B 156 ? 0.5019 0.3853 0.6113 -0.0239 -0.0057 -0.0308 165 LEU B CD1 
4343 C CD2 . LEU B 156 ? 0.4548 0.3597 0.5287 -0.0241 0.0136  -0.0187 165 LEU B CD2 
4344 N N   . VAL B 157 ? 0.3606 0.2558 0.3916 0.0075  0.0015  -0.0483 166 VAL B N   
4345 C CA  . VAL B 157 ? 0.3667 0.2618 0.3913 0.0141  0.0013  -0.0492 166 VAL B CA  
4346 C C   . VAL B 157 ? 0.3502 0.2552 0.3603 0.0124  0.0102  -0.0399 166 VAL B C   
4347 O O   . VAL B 157 ? 0.3672 0.2700 0.3766 0.0126  0.0118  -0.0332 166 VAL B O   
4348 C CB  . VAL B 157 ? 0.3754 0.2747 0.3955 0.0256  -0.0047 -0.0645 166 VAL B CB  
4349 C CG1 . VAL B 157 ? 0.4070 0.3108 0.4202 0.0328  -0.0031 -0.0646 166 VAL B CG1 
4350 C CG2 . VAL B 157 ? 0.4140 0.3007 0.4523 0.0283  -0.0166 -0.0762 166 VAL B CG2 
4351 N N   . SER B 158 ? 0.3381 0.2531 0.3386 0.0109  0.0146  -0.0394 167 SER B N   
4352 C CA  . SER B 158 ? 0.3157 0.2388 0.3068 0.0086  0.0210  -0.0317 167 SER B CA  
4353 C C   . SER B 158 ? 0.3219 0.2413 0.3158 0.0028  0.0239  -0.0225 167 SER B C   
4354 O O   . SER B 158 ? 0.3237 0.2456 0.3128 0.0036  0.0259  -0.0176 167 SER B O   
4355 C CB  . SER B 158 ? 0.3023 0.2336 0.2883 0.0068  0.0233  -0.0320 167 SER B CB  
4356 O OG  . SER B 158 ? 0.2865 0.2259 0.2673 0.0129  0.0217  -0.0373 167 SER B OG  
4357 N N   . LEU B 159 ? 0.3071 0.2228 0.3091 -0.0023 0.0241  -0.0200 168 LEU B N   
4358 C CA  . LEU B 159 ? 0.3147 0.2314 0.3190 -0.0069 0.0278  -0.0097 168 LEU B CA  
4359 C C   . LEU B 159 ? 0.3226 0.2322 0.3316 -0.0058 0.0258  -0.0028 168 LEU B C   
4360 O O   . LEU B 159 ? 0.3126 0.2268 0.3155 -0.0060 0.0289  0.0054  168 LEU B O   
4361 C CB  . LEU B 159 ? 0.2985 0.2163 0.3135 -0.0125 0.0291  -0.0072 168 LEU B CB  
4362 C CG  . LEU B 159 ? 0.3449 0.2683 0.3637 -0.0169 0.0341  0.0054  168 LEU B CG  
4363 C CD1 . LEU B 159 ? 0.3405 0.2761 0.3443 -0.0150 0.0395  0.0075  168 LEU B CD1 
4364 C CD2 . LEU B 159 ? 0.3560 0.2821 0.3895 -0.0223 0.0351  0.0076  168 LEU B CD2 
4365 N N   . LEU B 160 ? 0.3225 0.2214 0.3431 -0.0039 0.0195  -0.0067 169 LEU B N   
4366 C CA  . LEU B 160 ? 0.3267 0.2167 0.3550 -0.0021 0.0157  -0.0006 169 LEU B CA  
4367 C C   . LEU B 160 ? 0.3315 0.2257 0.3474 0.0040  0.0164  -0.0015 169 LEU B C   
4368 O O   . LEU B 160 ? 0.3590 0.2525 0.3743 0.0042  0.0168  0.0082  169 LEU B O   
4369 C CB  . LEU B 160 ? 0.3613 0.2376 0.4073 0.0001  0.0063  -0.0084 169 LEU B CB  
4370 C CG  . LEU B 160 ? 0.3753 0.2462 0.4406 -0.0075 0.0039  -0.0043 169 LEU B CG  
4371 C CD1 . LEU B 160 ? 0.4268 0.2853 0.5096 -0.0041 -0.0076 -0.0178 169 LEU B CD1 
4372 C CD2 . LEU B 160 ? 0.4349 0.3033 0.5122 -0.0140 0.0061  0.0151  169 LEU B CD2 
4373 N N   . VAL B 161 ? 0.3261 0.2267 0.3330 0.0089  0.0168  -0.0117 170 VAL B N   
4374 C CA  . VAL B 161 ? 0.3550 0.2629 0.3530 0.0140  0.0180  -0.0121 170 VAL B CA  
4375 C C   . VAL B 161 ? 0.3834 0.2992 0.3725 0.0102  0.0227  -0.0040 170 VAL B C   
4376 O O   . VAL B 161 ? 0.3538 0.2715 0.3403 0.0123  0.0222  0.0012  170 VAL B O   
4377 C CB  . VAL B 161 ? 0.3580 0.2753 0.3502 0.0192  0.0186  -0.0218 170 VAL B CB  
4378 C CG1 . VAL B 161 ? 0.4269 0.3548 0.4135 0.0228  0.0207  -0.0199 170 VAL B CG1 
4379 C CG2 . VAL B 161 ? 0.3164 0.2291 0.3149 0.0260  0.0129  -0.0324 170 VAL B CG2 
4380 N N   . GLU B 162 ? 0.3820 0.3029 0.3673 0.0056  0.0263  -0.0041 171 GLU B N   
4381 C CA  . GLU B 162 ? 0.3930 0.3221 0.3709 0.0033  0.0295  0.0005  171 GLU B CA  
4382 C C   . GLU B 162 ? 0.4202 0.3491 0.3973 0.0026  0.0301  0.0108  171 GLU B C   
4383 O O   . GLU B 162 ? 0.4214 0.3568 0.3911 0.0050  0.0299  0.0138  171 GLU B O   
4384 C CB  . GLU B 162 ? 0.3932 0.3262 0.3706 -0.0006 0.0323  -0.0024 171 GLU B CB  
4385 C CG  . GLU B 162 ? 0.3782 0.3205 0.3490 -0.0015 0.0347  -0.0008 171 GLU B CG  
4386 C CD  . GLU B 162 ? 0.3536 0.3013 0.3209 0.0002  0.0327  -0.0064 171 GLU B CD  
4387 O OE1 . GLU B 162 ? 0.3254 0.2716 0.2960 0.0007  0.0311  -0.0097 171 GLU B OE1 
4388 O OE2 . GLU B 162 ? 0.3725 0.3274 0.3348 0.0015  0.0322  -0.0072 171 GLU B OE2 
4389 N N   . ILE B 163 ? 0.3951 0.3178 0.3812 -0.0005 0.0303  0.0170  172 ILE B N   
4390 C CA  . ILE B 163 ? 0.4018 0.3261 0.3896 -0.0019 0.0315  0.0309  172 ILE B CA  
4391 C C   . ILE B 163 ? 0.3880 0.3060 0.3774 0.0024  0.0269  0.0360  172 ILE B C   
4392 O O   . ILE B 163 ? 0.3718 0.2966 0.3545 0.0039  0.0277  0.0460  172 ILE B O   
4393 C CB  . ILE B 163 ? 0.4179 0.3372 0.4209 -0.0077 0.0324  0.0385  172 ILE B CB  
4394 C CG1 . ILE B 163 ? 0.4328 0.3625 0.4335 -0.0114 0.0379  0.0356  172 ILE B CG1 
4395 C CG2 . ILE B 163 ? 0.4461 0.3669 0.4548 -0.0095 0.0333  0.0572  172 ILE B CG2 
4396 C CD1 . ILE B 163 ? 0.4421 0.3667 0.4615 -0.0173 0.0375  0.0385  172 ILE B CD1 
4397 N N   . ALA B 164 ? 0.3855 0.2925 0.3831 0.0056  0.0216  0.0285  173 ALA B N   
4398 C CA  . ALA B 164 ? 0.4228 0.3240 0.4240 0.0111  0.0164  0.0312  173 ALA B CA  
4399 C C   . ALA B 164 ? 0.4079 0.3206 0.3955 0.0151  0.0174  0.0300  173 ALA B C   
4400 O O   . ALA B 164 ? 0.3953 0.3105 0.3799 0.0174  0.0157  0.0392  173 ALA B O   
4401 C CB  . ALA B 164 ? 0.4102 0.3013 0.4217 0.0158  0.0107  0.0194  173 ALA B CB  
4402 N N   . ALA B 165 ? 0.4157 0.3360 0.3970 0.0156  0.0195  0.0195  174 ALA B N   
4403 C CA  . ALA B 165 ? 0.4302 0.3615 0.4031 0.0181  0.0193  0.0172  174 ALA B CA  
4404 C C   . ALA B 165 ? 0.4517 0.3921 0.4145 0.0168  0.0208  0.0234  174 ALA B C   
4405 O O   . ALA B 165 ? 0.4847 0.4318 0.4422 0.0204  0.0178  0.0253  174 ALA B O   
4406 C CB  . ALA B 165 ? 0.4474 0.3846 0.4200 0.0172  0.0211  0.0075  174 ALA B CB  
4407 N N   . ALA B 166 ? 0.4668 0.4091 0.4269 0.0126  0.0250  0.0260  175 ALA B N   
4408 C CA  . ALA B 166 ? 0.4883 0.4434 0.4373 0.0130  0.0272  0.0297  175 ALA B CA  
4409 C C   . ALA B 166 ? 0.5123 0.4722 0.4563 0.0155  0.0269  0.0438  175 ALA B C   
4410 O O   . ALA B 166 ? 0.5012 0.4758 0.4327 0.0186  0.0278  0.0460  175 ALA B O   
4411 C CB  . ALA B 166 ? 0.5267 0.4852 0.4758 0.0088  0.0324  0.0284  175 ALA B CB  
4412 N N   . SER B 167 ? 0.4842 0.4328 0.4384 0.0149  0.0250  0.0533  176 SER B N   
4413 C CA  . SER B 167 ? 0.4962 0.4476 0.4482 0.0176  0.0233  0.0691  176 SER B CA  
4414 C C   . SER B 167 ? 0.4733 0.4338 0.4141 0.0246  0.0184  0.0670  176 SER B C   
4415 O O   . SER B 167 ? 0.4699 0.4410 0.4012 0.0281  0.0179  0.0787  176 SER B O   
4416 C CB  . SER B 167 ? 0.5327 0.4664 0.5027 0.0163  0.0193  0.0771  176 SER B CB  
4417 O OG  . SER B 167 ? 0.6263 0.5522 0.6091 0.0098  0.0222  0.0797  176 SER B OG  
4418 N N   . ALA B 168 ? 0.4381 0.3961 0.3807 0.0266  0.0148  0.0529  177 ALA B N   
4419 C CA  . ALA B 168 ? 0.4623 0.4297 0.3981 0.0324  0.0092  0.0484  177 ALA B CA  
4420 C C   . ALA B 168 ? 0.4640 0.4476 0.3863 0.0344  0.0088  0.0410  177 ALA B C   
4421 O O   . ALA B 168 ? 0.4188 0.4122 0.3344 0.0399  0.0029  0.0389  177 ALA B O   
4422 C CB  . ALA B 168 ? 0.4396 0.4011 0.3863 0.0334  0.0057  0.0377  177 ALA B CB  
4423 N N   . ILE B 169 ? 0.4522 0.4388 0.3719 0.0307  0.0139  0.0357  178 ILE B N   
4424 C CA  . ILE B 169 ? 0.4635 0.4644 0.3731 0.0336  0.0123  0.0250  178 ILE B CA  
4425 C C   . ILE B 169 ? 0.5002 0.5187 0.3931 0.0408  0.0107  0.0311  178 ILE B C   
4426 O O   . ILE B 169 ? 0.5065 0.5365 0.3919 0.0468  0.0040  0.0206  178 ILE B O   
4427 C CB  . ILE B 169 ? 0.4686 0.4700 0.3792 0.0293  0.0182  0.0195  178 ILE B CB  
4428 C CG1 . ILE B 169 ? 0.4295 0.4173 0.3542 0.0237  0.0183  0.0114  178 ILE B CG1 
4429 C CG2 . ILE B 169 ? 0.5108 0.5282 0.4111 0.0344  0.0157  0.0079  178 ILE B CG2 
4430 C CD1 . ILE B 169 ? 0.4381 0.4231 0.3659 0.0190  0.0245  0.0103  178 ILE B CD1 
4431 N N   . LYS B 170 ? 0.4847 0.5064 0.3730 0.0406  0.0162  0.0486  179 LYS B N   
4432 C CA  . LYS B 170 ? 0.5148 0.5567 0.3857 0.0480  0.0160  0.0586  179 LYS B CA  
4433 C C   . LYS B 170 ? 0.5150 0.5604 0.3805 0.0550  0.0067  0.0597  179 LYS B C   
4434 O O   . LYS B 170 ? 0.5557 0.6211 0.4040 0.0633  0.0044  0.0637  179 LYS B O   
4435 C CB  . LYS B 170 ? 0.5343 0.5785 0.4061 0.0449  0.0240  0.0818  179 LYS B CB  
4436 C CG  . LYS B 170 ? 0.5317 0.5559 0.4196 0.0406  0.0220  0.0961  179 LYS B CG  
4437 C CD  . LYS B 170 ? 0.5793 0.6069 0.4716 0.0373  0.0281  0.1215  179 LYS B CD  
4438 C CE  . LYS B 170 ? 0.5780 0.6057 0.4790 0.0296  0.0369  0.1234  179 LYS B CE  
4439 N NZ  . LYS B 170 ? 0.5862 0.5914 0.5039 0.0231  0.0355  0.1083  179 LYS B NZ  
4440 N N   . VAL B 171 ? 0.4918 0.5204 0.3717 0.0526  0.0016  0.0563  180 VAL B N   
4441 C CA  . VAL B 171 ? 0.5210 0.5520 0.4001 0.0588  -0.0078 0.0561  180 VAL B CA  
4442 C C   . VAL B 171 ? 0.5073 0.5480 0.3840 0.0630  -0.0162 0.0362  180 VAL B C   
4443 O O   . VAL B 171 ? 0.5197 0.5692 0.3920 0.0698  -0.0251 0.0340  180 VAL B O   
4444 C CB  . VAL B 171 ? 0.5146 0.5259 0.4129 0.0555  -0.0097 0.0596  180 VAL B CB  
4445 C CG1 . VAL B 171 ? 0.5534 0.5683 0.4525 0.0624  -0.0191 0.0610  180 VAL B CG1 
4446 C CG2 . VAL B 171 ? 0.5374 0.5360 0.4430 0.0512  -0.0039 0.0767  180 VAL B CG2 
4447 N N   . ILE B 172 ? 0.5121 0.5509 0.3938 0.0589  -0.0145 0.0218  181 ILE B N   
4448 C CA  . ILE B 172 ? 0.5184 0.5623 0.4055 0.0611  -0.0239 0.0028  181 ILE B CA  
4449 C C   . ILE B 172 ? 0.5342 0.5987 0.4049 0.0718  -0.0330 -0.0047 181 ILE B C   
4450 O O   . ILE B 172 ? 0.5459 0.6139 0.4232 0.0753  -0.0442 -0.0144 181 ILE B O   
4451 C CB  . ILE B 172 ? 0.5098 0.5473 0.4067 0.0549  -0.0209 -0.0093 181 ILE B CB  
4452 C CG1 . ILE B 172 ? 0.4932 0.5130 0.4078 0.0460  -0.0156 -0.0051 181 ILE B CG1 
4453 C CG2 . ILE B 172 ? 0.4945 0.5381 0.3987 0.0576  -0.0324 -0.0285 181 ILE B CG2 
4454 C CD1 . ILE B 172 ? 0.5021 0.5149 0.4241 0.0397  -0.0104 -0.0113 181 ILE B CD1 
4455 N N   . PRO B 173 ? 0.5657 0.6460 0.4158 0.0776  -0.0284 -0.0007 182 PRO B N   
4456 C CA  . PRO B 173 ? 0.5850 0.6887 0.4159 0.0902  -0.0370 -0.0078 182 PRO B CA  
4457 C C   . PRO B 173 ? 0.5960 0.7060 0.4198 0.0964  -0.0432 0.0039  182 PRO B C   
4458 O O   . PRO B 173 ? 0.5989 0.7241 0.4141 0.1061  -0.0551 -0.0072 182 PRO B O   
4459 C CB  . PRO B 173 ? 0.6022 0.7235 0.4129 0.0945  -0.0269 -0.0007 182 PRO B CB  
4460 C CG  . PRO B 173 ? 0.5927 0.6983 0.4165 0.0837  -0.0163 0.0017  182 PRO B CG  
4461 C CD  . PRO B 173 ? 0.5739 0.6548 0.4177 0.0738  -0.0154 0.0099  182 PRO B CD  
4462 N N   . THR B 174 ? 0.5867 0.6850 0.4152 0.0914  -0.0364 0.0252  183 THR B N   
4463 C CA  . THR B 174 ? 0.5841 0.6832 0.4122 0.0960  -0.0431 0.0367  183 THR B CA  
4464 C C   . THR B 174 ? 0.5430 0.6340 0.3897 0.0953  -0.0545 0.0216  183 THR B C   
4465 O O   . THR B 174 ? 0.5641 0.6662 0.4065 0.1034  -0.0657 0.0188  183 THR B O   
4466 C CB  . THR B 174 ? 0.5874 0.6707 0.4237 0.0901  -0.0350 0.0606  183 THR B CB  
4467 O OG1 . THR B 174 ? 0.6289 0.7185 0.4545 0.0882  -0.0237 0.0757  183 THR B OG1 
4468 C CG2 . THR B 174 ? 0.6001 0.6868 0.4337 0.0970  -0.0425 0.0742  183 THR B CG2 
4469 N N   . VAL B 175 ? 0.5115 0.5858 0.3794 0.0858  -0.0517 0.0131  184 VAL B N   
4470 C CA  . VAL B 175 ? 0.5121 0.5813 0.4016 0.0838  -0.0607 0.0015  184 VAL B CA  
4471 C C   . VAL B 175 ? 0.5162 0.6007 0.4037 0.0905  -0.0746 -0.0171 184 VAL B C   
4472 O O   . VAL B 175 ? 0.4359 0.5276 0.3286 0.0958  -0.0860 -0.0203 184 VAL B O   
4473 C CB  . VAL B 175 ? 0.4765 0.5293 0.3875 0.0728  -0.0540 -0.0028 184 VAL B CB  
4474 C CG1 . VAL B 175 ? 0.4815 0.5344 0.4164 0.0703  -0.0629 -0.0146 184 VAL B CG1 
4475 C CG2 . VAL B 175 ? 0.4448 0.4831 0.3607 0.0685  -0.0443 0.0126  184 VAL B CG2 
4476 N N   . PHE B 176 ? 0.5095 0.5995 0.3904 0.0912  -0.0748 -0.0302 185 PHE B N   
4477 C CA  . PHE B 176 ? 0.5370 0.6402 0.4186 0.0983  -0.0900 -0.0516 185 PHE B CA  
4478 C C   . PHE B 176 ? 0.5572 0.6827 0.4141 0.1126  -0.0987 -0.0525 185 PHE B C   
4479 O O   . PHE B 176 ? 0.5856 0.7206 0.4480 0.1191  -0.1146 -0.0670 185 PHE B O   
4480 C CB  . PHE B 176 ? 0.5631 0.6658 0.4457 0.0967  -0.0889 -0.0669 185 PHE B CB  
4481 C CG  . PHE B 176 ? 0.5490 0.6323 0.4581 0.0837  -0.0840 -0.0684 185 PHE B CG  
4482 C CD1 . PHE B 176 ? 0.5202 0.5958 0.4582 0.0774  -0.0917 -0.0722 185 PHE B CD1 
4483 C CD2 . PHE B 176 ? 0.6137 0.6888 0.5198 0.0780  -0.0717 -0.0647 185 PHE B CD2 
4484 C CE1 . PHE B 176 ? 0.5511 0.6124 0.5126 0.0660  -0.0863 -0.0709 185 PHE B CE1 
4485 C CE2 . PHE B 176 ? 0.5688 0.6278 0.4976 0.0670  -0.0676 -0.0651 185 PHE B CE2 
4486 C CZ  . PHE B 176 ? 0.5559 0.6086 0.5116 0.0611  -0.0746 -0.0674 185 PHE B CZ  
4487 N N   . LYS B 177 ? 0.5736 0.7088 0.4044 0.1176  -0.0887 -0.0365 186 LYS B N   
4488 C CA  . LYS B 177 ? 0.6066 0.7655 0.4112 0.1317  -0.0951 -0.0317 186 LYS B CA  
4489 C C   . LYS B 177 ? 0.5953 0.7517 0.4074 0.1336  -0.1031 -0.0220 186 LYS B C   
4490 O O   . LYS B 177 ? 0.6007 0.7744 0.4036 0.1448  -0.1170 -0.0300 186 LYS B O   
4491 C CB  . LYS B 177 ? 0.6309 0.8010 0.4102 0.1346  -0.0805 -0.0106 186 LYS B CB  
4492 C CG  . LYS B 177 ? 0.6867 0.8859 0.4363 0.1499  -0.0854 -0.0024 186 LYS B CG  
4493 C CD  . LYS B 177 ? 0.7209 0.9373 0.4470 0.1530  -0.0704 0.0162  186 LYS B CD  
4494 C CE  . LYS B 177 ? 0.7450 0.9955 0.4394 0.1696  -0.0747 0.0254  186 LYS B CE  
4495 N NZ  . LYS B 177 ? 0.7612 1.0332 0.4343 0.1725  -0.0589 0.0466  186 LYS B NZ  
4496 N N   . ALA B 178 ? 0.5760 0.7120 0.4052 0.1236  -0.0950 -0.0060 187 ALA B N   
4497 C CA  . ALA B 178 ? 0.5689 0.7004 0.4098 0.1250  -0.1019 0.0025  187 ALA B CA  
4498 C C   . ALA B 178 ? 0.5531 0.6869 0.4152 0.1257  -0.1172 -0.0180 187 ALA B C   
4499 O O   . ALA B 178 ? 0.5517 0.6970 0.4125 0.1342  -0.1300 -0.0195 187 ALA B O   
4500 C CB  . ALA B 178 ? 0.5510 0.6598 0.4092 0.1149  -0.0906 0.0187  187 ALA B CB  
4501 N N   . MET B 179 ? 0.5279 0.6517 0.4111 0.1167  -0.1166 -0.0327 188 MET B N   
4502 C CA  . MET B 179 ? 0.5614 0.6876 0.4700 0.1156  -0.1314 -0.0513 188 MET B CA  
4503 C C   . MET B 179 ? 0.5858 0.7319 0.4827 0.1276  -0.1488 -0.0702 188 MET B C   
4504 O O   . MET B 179 ? 0.5869 0.7425 0.4928 0.1333  -0.1637 -0.0766 188 MET B O   
4505 C CB  . MET B 179 ? 0.5422 0.6546 0.4754 0.1034  -0.1269 -0.0603 188 MET B CB  
4506 C CG  . MET B 179 ? 0.5457 0.6431 0.5004 0.0929  -0.1162 -0.0476 188 MET B CG  
4507 S SD  . MET B 179 ? 0.5865 0.6708 0.5657 0.0795  -0.1095 -0.0545 188 MET B SD  
4508 C CE  . MET B 179 ? 0.6131 0.7061 0.6169 0.0799  -0.1297 -0.0767 188 MET B CE  
4509 N N   . GLN B 180 ? 0.6155 0.7691 0.4932 0.1322  -0.1475 -0.0803 189 GLN B N   
4510 C CA  . GLN B 180 ? 0.6383 0.8129 0.5022 0.1459  -0.1642 -0.1019 189 GLN B CA  
4511 C C   . GLN B 180 ? 0.6708 0.8660 0.5105 0.1601  -0.1724 -0.0947 189 GLN B C   
4512 O O   . GLN B 180 ? 0.6853 0.8943 0.5283 0.1695  -0.1918 -0.1121 189 GLN B O   
4513 C CB  . GLN B 180 ? 0.6551 0.8372 0.4972 0.1507  -0.1579 -0.1106 189 GLN B CB  
4514 C CG  . GLN B 180 ? 0.7030 0.9053 0.5362 0.1651  -0.1765 -0.1396 189 GLN B CG  
4515 C CD  . GLN B 180 ? 0.6944 0.9076 0.5050 0.1719  -0.1694 -0.1486 189 GLN B CD  
4516 O OE1 . GLN B 180 ? 0.7263 0.9666 0.5063 0.1887  -0.1745 -0.1572 189 GLN B OE1 
4517 N NE2 . GLN B 180 ? 0.6780 0.8724 0.5034 0.1596  -0.1575 -0.1466 189 GLN B NE2 
4518 N N   . MET B 181 ? 0.6667 0.8634 0.4846 0.1614  -0.1584 -0.0686 190 MET B N   
4519 C CA  . MET B 181 ? 0.7007 0.9158 0.4953 0.1741  -0.1640 -0.0555 190 MET B CA  
4520 C C   . MET B 181 ? 0.6889 0.8949 0.5039 0.1712  -0.1698 -0.0446 190 MET B C   
4521 O O   . MET B 181 ? 0.6967 0.9164 0.4949 0.1817  -0.1755 -0.0324 190 MET B O   
4522 C CB  . MET B 181 ? 0.7354 0.9573 0.5005 0.1766  -0.1468 -0.0292 190 MET B CB  
4523 C CG  . MET B 181 ? 0.8098 1.0492 0.5496 0.1830  -0.1405 -0.0371 190 MET B CG  
4524 S SD  . MET B 181 ? 0.9957 1.2718 0.7094 0.2050  -0.1606 -0.0635 190 MET B SD  
4525 C CE  . MET B 181 ? 1.0012 1.2644 0.7436 0.1996  -0.1720 -0.1017 190 MET B CE  
4526 N N   . GLN B 182 ? 0.6599 0.8453 0.5103 0.1583  -0.1685 -0.0484 191 GLN B N   
4527 C CA  . GLN B 182 ? 0.6492 0.8266 0.5219 0.1553  -0.1718 -0.0384 191 GLN B CA  
4528 C C   . GLN B 182 ? 0.6453 0.8188 0.5014 0.1579  -0.1614 -0.0101 191 GLN B C   
4529 O O   . GLN B 182 ? 0.6858 0.8708 0.5324 0.1681  -0.1704 -0.0013 191 GLN B O   
4530 C CB  . GLN B 182 ? 0.6799 0.8739 0.5619 0.1647  -0.1940 -0.0536 191 GLN B CB  
4531 C CG  . GLN B 182 ? 0.7289 0.9237 0.6387 0.1602  -0.2073 -0.0809 191 GLN B CG  
4532 C CD  . GLN B 182 ? 0.7624 0.9426 0.7157 0.1465  -0.2056 -0.0807 191 GLN B CD  
4533 O OE1 . GLN B 182 ? 0.8356 1.0122 0.8009 0.1450  -0.2022 -0.0664 191 GLN B OE1 
4534 N NE2 . GLN B 182 ? 0.7215 0.8953 0.6999 0.1374  -0.2084 -0.0964 191 GLN B NE2 
4535 N N   . GLU B 183 ? 0.6121 0.7699 0.4657 0.1492  -0.1437 0.0038  192 GLU B N   
4536 C CA  . GLU B 183 ? 0.6089 0.7583 0.4538 0.1492  -0.1335 0.0309  192 GLU B CA  
4537 C C   . GLU B 183 ? 0.5641 0.6893 0.4379 0.1381  -0.1252 0.0360  192 GLU B C   
4538 O O   . GLU B 183 ? 0.5367 0.6473 0.4151 0.1285  -0.1120 0.0385  192 GLU B O   
4539 C CB  . GLU B 183 ? 0.6250 0.7784 0.4441 0.1491  -0.1206 0.0433  192 GLU B CB  
4540 C CG  . GLU B 183 ? 0.7330 0.9157 0.5191 0.1631  -0.1272 0.0432  192 GLU B CG  
4541 C CD  . GLU B 183 ? 0.8245 1.0189 0.5965 0.1737  -0.1334 0.0648  192 GLU B CD  
4542 O OE1 . GLU B 183 ? 0.8921 1.0707 0.6733 0.1692  -0.1267 0.0882  192 GLU B OE1 
4543 O OE2 . GLU B 183 ? 0.8839 1.1034 0.6362 0.1873  -0.1461 0.0580  192 GLU B OE2 
4544 N N   . ARG B 184 ? 0.5523 0.6758 0.4453 0.1407  -0.1337 0.0363  193 ARG B N   
4545 C CA  . ARG B 184 ? 0.5191 0.6255 0.4409 0.1331  -0.1279 0.0373  193 ARG B CA  
4546 C C   . ARG B 184 ? 0.4953 0.5831 0.4159 0.1293  -0.1152 0.0560  193 ARG B C   
4547 O O   . ARG B 184 ? 0.4453 0.5187 0.3799 0.1205  -0.1051 0.0530  193 ARG B O   
4548 C CB  . ARG B 184 ? 0.5375 0.6505 0.4785 0.1394  -0.1404 0.0351  193 ARG B CB  
4549 C CG  . ARG B 184 ? 0.5070 0.6078 0.4779 0.1345  -0.1349 0.0355  193 ARG B CG  
4550 C CD  . ARG B 184 ? 0.4923 0.5796 0.4633 0.1388  -0.1314 0.0541  193 ARG B CD  
4551 N NE  . ARG B 184 ? 0.5081 0.5891 0.5076 0.1381  -0.1295 0.0508  193 ARG B NE  
4552 C CZ  . ARG B 184 ? 0.5130 0.5795 0.5209 0.1411  -0.1262 0.0614  193 ARG B CZ  
4553 N NH1 . ARG B 184 ? 0.5866 0.6407 0.5797 0.1434  -0.1245 0.0787  193 ARG B NH1 
4554 N NH2 . ARG B 184 ? 0.4990 0.5646 0.5325 0.1423  -0.1249 0.0547  193 ARG B NH2 
4555 N N   . ASP B 185 ? 0.5150 0.6035 0.4209 0.1362  -0.1170 0.0754  194 ASP B N   
4556 C CA  . ASP B 185 ? 0.5129 0.5825 0.4219 0.1329  -0.1078 0.0948  194 ASP B CA  
4557 C C   . ASP B 185 ? 0.5052 0.5680 0.4043 0.1240  -0.0942 0.0971  194 ASP B C   
4558 O O   . ASP B 185 ? 0.4686 0.5125 0.3812 0.1168  -0.0856 0.1002  194 ASP B O   
4559 C CB  . ASP B 185 ? 0.5531 0.6266 0.4502 0.1419  -0.1138 0.1183  194 ASP B CB  
4560 C CG  . ASP B 185 ? 0.5340 0.6133 0.4425 0.1515  -0.1280 0.1174  194 ASP B CG  
4561 O OD1 . ASP B 185 ? 0.5574 0.6334 0.4885 0.1503  -0.1311 0.1017  194 ASP B OD1 
4562 O OD2 . ASP B 185 ? 0.5553 0.6446 0.4505 0.1608  -0.1359 0.1333  194 ASP B OD2 
4563 N N   . THR B 186 ? 0.5127 0.5921 0.3886 0.1256  -0.0932 0.0940  195 THR B N   
4564 C CA  . THR B 186 ? 0.4984 0.5752 0.3650 0.1180  -0.0809 0.0935  195 THR B CA  
4565 C C   . THR B 186 ? 0.4536 0.5182 0.3381 0.1083  -0.0755 0.0747  195 THR B C   
4566 O O   . THR B 186 ? 0.4387 0.4885 0.3297 0.1002  -0.0649 0.0788  195 THR B O   
4567 C CB  . THR B 186 ? 0.5071 0.6086 0.3458 0.1243  -0.0824 0.0895  195 THR B CB  
4568 O OG1 . THR B 186 ? 0.5873 0.7036 0.4077 0.1341  -0.0868 0.1094  195 THR B OG1 
4569 C CG2 . THR B 186 ? 0.5360 0.6369 0.3659 0.1174  -0.0692 0.0898  195 THR B CG2 
4570 N N   . LEU B 187 ? 0.4359 0.5074 0.3298 0.1091  -0.0833 0.0555  196 LEU B N   
4571 C CA  . LEU B 187 ? 0.4261 0.4886 0.3393 0.1001  -0.0789 0.0402  196 LEU B CA  
4572 C C   . LEU B 187 ? 0.4268 0.4718 0.3603 0.0955  -0.0727 0.0458  196 LEU B C   
4573 O O   . LEU B 187 ? 0.4162 0.4503 0.3565 0.0877  -0.0633 0.0427  196 LEU B O   
4574 C CB  . LEU B 187 ? 0.4105 0.4845 0.3366 0.1016  -0.0901 0.0221  196 LEU B CB  
4575 C CG  . LEU B 187 ? 0.3391 0.4068 0.2893 0.0923  -0.0866 0.0098  196 LEU B CG  
4576 C CD1 . LEU B 187 ? 0.3783 0.4395 0.3223 0.0849  -0.0772 0.0052  196 LEU B CD1 
4577 C CD2 . LEU B 187 ? 0.3928 0.4731 0.3593 0.0936  -0.0994 -0.0049 196 LEU B CD2 
4578 N N   . LEU B 188 ? 0.4371 0.4808 0.3800 0.1016  -0.0789 0.0525  197 LEU B N   
4579 C CA  . LEU B 188 ? 0.4523 0.4812 0.4141 0.1004  -0.0750 0.0564  197 LEU B CA  
4580 C C   . LEU B 188 ? 0.4419 0.4539 0.3992 0.0959  -0.0656 0.0678  197 LEU B C   
4581 O O   . LEU B 188 ? 0.4256 0.4265 0.3943 0.0906  -0.0585 0.0625  197 LEU B O   
4582 C CB  . LEU B 188 ? 0.4570 0.4878 0.4273 0.1099  -0.0848 0.0635  197 LEU B CB  
4583 C CG  . LEU B 188 ? 0.4709 0.4866 0.4598 0.1125  -0.0835 0.0683  197 LEU B CG  
4584 C CD1 . LEU B 188 ? 0.4869 0.5010 0.4937 0.1082  -0.0770 0.0544  197 LEU B CD1 
4585 C CD2 . LEU B 188 ? 0.5292 0.5500 0.5268 0.1230  -0.0952 0.0735  197 LEU B CD2 
4586 N N   . LYS B 189 ? 0.4875 0.4997 0.4288 0.0982  -0.0659 0.0838  198 LYS B N   
4587 C CA  . LYS B 189 ? 0.5093 0.5072 0.4491 0.0930  -0.0578 0.0973  198 LYS B CA  
4588 C C   . LYS B 189 ? 0.4883 0.4841 0.4241 0.0840  -0.0476 0.0880  198 LYS B C   
4589 O O   . LYS B 189 ? 0.4903 0.4707 0.4364 0.0784  -0.0414 0.0890  198 LYS B O   
4590 C CB  . LYS B 189 ? 0.5444 0.5495 0.4674 0.0968  -0.0594 0.1188  198 LYS B CB  
4591 C CG  . LYS B 189 ? 0.5469 0.5374 0.4749 0.0914  -0.0529 0.1377  198 LYS B CG  
4592 C CD  . LYS B 189 ? 0.6269 0.6299 0.5388 0.0952  -0.0537 0.1621  198 LYS B CD  
4593 C CE  . LYS B 189 ? 0.6865 0.6771 0.6072 0.0882  -0.0469 0.1833  198 LYS B CE  
4594 N NZ  . LYS B 189 ? 0.6690 0.6756 0.5753 0.0916  -0.0464 0.2110  198 LYS B NZ  
4595 N N   . ALA B 190 ? 0.4781 0.4892 0.4005 0.0834  -0.0474 0.0777  199 ALA B N   
4596 C CA  . ALA B 190 ? 0.4485 0.4592 0.3676 0.0759  -0.0392 0.0676  199 ALA B CA  
4597 C C   . ALA B 190 ? 0.4293 0.4294 0.3670 0.0705  -0.0360 0.0551  199 ALA B C   
4598 O O   . ALA B 190 ? 0.4452 0.4351 0.3864 0.0642  -0.0281 0.0544  199 ALA B O   
4599 C CB  . ALA B 190 ? 0.4397 0.4689 0.3445 0.0784  -0.0429 0.0561  199 ALA B CB  
4600 N N   . LEU B 191 ? 0.4018 0.4067 0.3518 0.0733  -0.0420 0.0460  200 LEU B N   
4601 C CA  . LEU B 191 ? 0.3800 0.3804 0.3475 0.0695  -0.0383 0.0361  200 LEU B CA  
4602 C C   . LEU B 191 ? 0.3654 0.3508 0.3428 0.0701  -0.0345 0.0411  200 LEU B C   
4603 O O   . LEU B 191 ? 0.3920 0.3715 0.3759 0.0659  -0.0281 0.0353  200 LEU B O   
4604 C CB  . LEU B 191 ? 0.3361 0.3486 0.3174 0.0727  -0.0453 0.0278  200 LEU B CB  
4605 C CG  . LEU B 191 ? 0.3444 0.3705 0.3238 0.0711  -0.0511 0.0184  200 LEU B CG  
4606 C CD1 . LEU B 191 ? 0.3247 0.3631 0.3215 0.0748  -0.0600 0.0131  200 LEU B CD1 
4607 C CD2 . LEU B 191 ? 0.3516 0.3759 0.3346 0.0628  -0.0450 0.0104  200 LEU B CD2 
4608 N N   . LEU B 192 ? 0.3889 0.3682 0.3682 0.0761  -0.0394 0.0514  201 LEU B N   
4609 C CA  . LEU B 192 ? 0.4362 0.3988 0.4273 0.0774  -0.0380 0.0551  201 LEU B CA  
4610 C C   . LEU B 192 ? 0.4325 0.3828 0.4189 0.0703  -0.0312 0.0602  201 LEU B C   
4611 O O   . LEU B 192 ? 0.4381 0.3767 0.4354 0.0693  -0.0287 0.0554  201 LEU B O   
4612 C CB  . LEU B 192 ? 0.4572 0.4138 0.4546 0.0853  -0.0465 0.0664  201 LEU B CB  
4613 C CG  . LEU B 192 ? 0.4738 0.4407 0.4814 0.0937  -0.0540 0.0605  201 LEU B CG  
4614 C CD1 . LEU B 192 ? 0.4898 0.4490 0.5028 0.1015  -0.0630 0.0737  201 LEU B CD1 
4615 C CD2 . LEU B 192 ? 0.5043 0.4735 0.5286 0.0960  -0.0513 0.0459  201 LEU B CD2 
4616 N N   . GLU B 193 ? 0.4618 0.4169 0.4328 0.0664  -0.0285 0.0689  202 GLU B N   
4617 C CA  . GLU B 193 ? 0.4794 0.4263 0.4475 0.0594  -0.0216 0.0747  202 GLU B CA  
4618 C C   . GLU B 193 ? 0.4626 0.4102 0.4310 0.0536  -0.0151 0.0602  202 GLU B C   
4619 O O   . GLU B 193 ? 0.4611 0.3973 0.4369 0.0495  -0.0113 0.0589  202 GLU B O   
4620 C CB  . GLU B 193 ? 0.5131 0.4708 0.4640 0.0581  -0.0195 0.0881  202 GLU B CB  
4621 C CG  . GLU B 193 ? 0.5660 0.5201 0.5147 0.0505  -0.0113 0.0948  202 GLU B CG  
4622 C CD  . GLU B 193 ? 0.6405 0.5752 0.6076 0.0472  -0.0116 0.1053  202 GLU B CD  
4623 O OE1 . GLU B 193 ? 0.6467 0.5715 0.6254 0.0517  -0.0187 0.1135  202 GLU B OE1 
4624 O OE2 . GLU B 193 ? 0.6303 0.5593 0.6021 0.0404  -0.0059 0.1048  202 GLU B OE2 
4625 N N   . ILE B 194 ? 0.4523 0.4131 0.4147 0.0535  -0.0150 0.0498  203 ILE B N   
4626 C CA  . ILE B 194 ? 0.4125 0.3751 0.3774 0.0484  -0.0099 0.0375  203 ILE B CA  
4627 C C   . ILE B 194 ? 0.3980 0.3530 0.3772 0.0495  -0.0087 0.0311  203 ILE B C   
4628 O O   . ILE B 194 ? 0.3748 0.3235 0.3562 0.0456  -0.0038 0.0271  203 ILE B O   
4629 C CB  . ILE B 194 ? 0.3941 0.3715 0.3564 0.0484  -0.0128 0.0284  203 ILE B CB  
4630 C CG1 . ILE B 194 ? 0.4490 0.4350 0.3952 0.0483  -0.0138 0.0305  203 ILE B CG1 
4631 C CG2 . ILE B 194 ? 0.3940 0.3727 0.3641 0.0433  -0.0086 0.0184  203 ILE B CG2 
4632 C CD1 . ILE B 194 ? 0.4447 0.4444 0.3896 0.0508  -0.0209 0.0212  203 ILE B CD1 
4633 N N   . ALA B 195 ? 0.3975 0.3552 0.3861 0.0561  -0.0136 0.0296  204 ALA B N   
4634 C CA  . ALA B 195 ? 0.3868 0.3416 0.3883 0.0602  -0.0129 0.0221  204 ALA B CA  
4635 C C   . ALA B 195 ? 0.4072 0.3447 0.4133 0.0605  -0.0127 0.0236  204 ALA B C   
4636 O O   . ALA B 195 ? 0.4030 0.3381 0.4131 0.0602  -0.0093 0.0151  204 ALA B O   
4637 C CB  . ALA B 195 ? 0.3936 0.3555 0.4050 0.0687  -0.0188 0.0210  204 ALA B CB  
4638 N N   . SER B 196 ? 0.4310 0.3574 0.4374 0.0611  -0.0170 0.0352  205 SER B N   
4639 C CA  . SER B 196 ? 0.4564 0.3646 0.4719 0.0600  -0.0187 0.0391  205 SER B CA  
4640 C C   . SER B 196 ? 0.4247 0.3297 0.4362 0.0519  -0.0122 0.0360  205 SER B C   
4641 O O   . SER B 196 ? 0.4040 0.2993 0.4251 0.0526  -0.0131 0.0282  205 SER B O   
4642 C CB  . SER B 196 ? 0.4589 0.3591 0.4758 0.0596  -0.0233 0.0572  205 SER B CB  
4643 O OG  . SER B 196 ? 0.5696 0.4516 0.6007 0.0574  -0.0262 0.0624  205 SER B OG  
4644 N N   . CYS B 197 ? 0.4402 0.3542 0.4381 0.0455  -0.0068 0.0406  206 CYS B N   
4645 C CA  . CYS B 197 ? 0.4290 0.3419 0.4231 0.0381  -0.0007 0.0381  206 CYS B CA  
4646 C C   . CYS B 197 ? 0.4131 0.3300 0.4080 0.0383  0.0024  0.0233  206 CYS B C   
4647 O O   . CYS B 197 ? 0.4524 0.3625 0.4514 0.0356  0.0040  0.0185  206 CYS B O   
4648 C CB  . CYS B 197 ? 0.4377 0.3619 0.4170 0.0335  0.0037  0.0444  206 CYS B CB  
4649 S SG  . CYS B 197 ? 0.5312 0.4554 0.5071 0.0330  0.0025  0.0652  206 CYS B SG  
4650 N N   . LEU B 198 ? 0.3964 0.3261 0.3885 0.0412  0.0029  0.0172  207 LEU B N   
4651 C CA  . LEU B 198 ? 0.3857 0.3230 0.3796 0.0418  0.0063  0.0066  207 LEU B CA  
4652 C C   . LEU B 198 ? 0.3778 0.3105 0.3811 0.0489  0.0040  -0.0014 207 LEU B C   
4653 O O   . LEU B 198 ? 0.3574 0.2928 0.3605 0.0492  0.0069  -0.0092 207 LEU B O   
4654 C CB  . LEU B 198 ? 0.3851 0.3384 0.3785 0.0426  0.0069  0.0048  207 LEU B CB  
4655 C CG  . LEU B 198 ? 0.3609 0.3200 0.3465 0.0369  0.0073  0.0081  207 LEU B CG  
4656 C CD1 . LEU B 198 ? 0.3667 0.3401 0.3583 0.0380  0.0055  0.0056  207 LEU B CD1 
4657 C CD2 . LEU B 198 ? 0.3645 0.3215 0.3450 0.0304  0.0118  0.0061  207 LEU B CD2 
4658 N N   . GLU B 199 ? 0.3792 0.3059 0.3905 0.0557  -0.0019 -0.0002 208 GLU B N   
4659 C CA  . GLU B 199 ? 0.4226 0.3425 0.4449 0.0642  -0.0065 -0.0097 208 GLU B CA  
4660 C C   . GLU B 199 ? 0.4227 0.3250 0.4502 0.0608  -0.0091 -0.0108 208 GLU B C   
4661 O O   . GLU B 199 ? 0.4461 0.3466 0.4785 0.0657  -0.0110 -0.0232 208 GLU B O   
4662 C CB  . GLU B 199 ? 0.4238 0.3395 0.4561 0.0725  -0.0138 -0.0076 208 GLU B CB  
4663 C CG  . GLU B 199 ? 0.4567 0.3919 0.4886 0.0781  -0.0123 -0.0098 208 GLU B CG  
4664 C CD  . GLU B 199 ? 0.4832 0.4152 0.5229 0.0843  -0.0196 -0.0039 208 GLU B CD  
4665 O OE1 . GLU B 199 ? 0.4822 0.3960 0.5301 0.0867  -0.0268 0.0005  208 GLU B OE1 
4666 O OE2 . GLU B 199 ? 0.4494 0.3974 0.4892 0.0867  -0.0190 -0.0030 208 GLU B OE2 
4667 N N   . LYS B 200 ? 0.4326 0.3242 0.4601 0.0529  -0.0096 0.0020  209 LYS B N   
4668 C CA  . LYS B 200 ? 0.4681 0.3451 0.5038 0.0476  -0.0116 0.0034  209 LYS B CA  
4669 C C   . LYS B 200 ? 0.4339 0.3172 0.4620 0.0432  -0.0059 -0.0049 209 LYS B C   
4670 O O   . LYS B 200 ? 0.4519 0.3275 0.4883 0.0445  -0.0096 -0.0140 209 LYS B O   
4671 C CB  . LYS B 200 ? 0.4789 0.3489 0.5162 0.0398  -0.0114 0.0221  209 LYS B CB  
4672 C CG  . LYS B 200 ? 0.5815 0.4391 0.6332 0.0441  -0.0199 0.0314  209 LYS B CG  
4673 C CD  . LYS B 200 ? 0.5935 0.4501 0.6441 0.0374  -0.0184 0.0537  209 LYS B CD  
4674 C CE  . LYS B 200 ? 0.6526 0.4970 0.7186 0.0424  -0.0278 0.0648  209 LYS B CE  
4675 N NZ  . LYS B 200 ? 0.7133 0.5611 0.7760 0.0371  -0.0258 0.0895  209 LYS B NZ  
4676 N N   . ALA B 201 ? 0.4246 0.3220 0.4385 0.0388  0.0016  -0.0024 210 ALA B N   
4677 C CA  . ALA B 201 ? 0.4223 0.3270 0.4290 0.0352  0.0067  -0.0091 210 ALA B CA  
4678 C C   . ALA B 201 ? 0.4265 0.3362 0.4352 0.0429  0.0052  -0.0233 210 ALA B C   
4679 O O   . ALA B 201 ? 0.4535 0.3620 0.4618 0.0415  0.0054  -0.0298 210 ALA B O   
4680 C CB  . ALA B 201 ? 0.4160 0.3349 0.4110 0.0314  0.0127  -0.0053 210 ALA B CB  
4681 N N   . LEU B 202 ? 0.4289 0.3463 0.4392 0.0518  0.0036  -0.0284 211 LEU B N   
4682 C CA  . LEU B 202 ? 0.4256 0.3530 0.4363 0.0617  0.0027  -0.0422 211 LEU B CA  
4683 C C   . LEU B 202 ? 0.4225 0.3350 0.4439 0.0672  -0.0060 -0.0533 211 LEU B C   
4684 O O   . LEU B 202 ? 0.3947 0.3120 0.4137 0.0714  -0.0070 -0.0648 211 LEU B O   
4685 C CB  . LEU B 202 ? 0.4353 0.3779 0.4473 0.0708  0.0035  -0.0444 211 LEU B CB  
4686 C CG  . LEU B 202 ? 0.4445 0.4011 0.4575 0.0843  0.0025  -0.0592 211 LEU B CG  
4687 C CD1 . LEU B 202 ? 0.4217 0.3941 0.4242 0.0839  0.0085  -0.0628 211 LEU B CD1 
4688 C CD2 . LEU B 202 ? 0.4549 0.4290 0.4713 0.0926  0.0043  -0.0593 211 LEU B CD2 
4689 N N   . GLN B 203 ? 0.4275 0.3225 0.4621 0.0676  -0.0134 -0.0497 212 GLN B N   
4690 C CA  . GLN B 203 ? 0.4552 0.3324 0.5060 0.0715  -0.0240 -0.0594 212 GLN B CA  
4691 C C   . GLN B 203 ? 0.4300 0.2998 0.4825 0.0628  -0.0241 -0.0595 212 GLN B C   
4692 O O   . GLN B 203 ? 0.4684 0.3345 0.5275 0.0683  -0.0310 -0.0745 212 GLN B O   
4693 C CB  . GLN B 203 ? 0.5061 0.3642 0.5742 0.0711  -0.0322 -0.0505 212 GLN B CB  
4694 C CG  . GLN B 203 ? 0.5477 0.4119 0.6177 0.0819  -0.0346 -0.0531 212 GLN B CG  
4695 C CD  . GLN B 203 ? 0.6046 0.4793 0.6760 0.0974  -0.0386 -0.0751 212 GLN B CD  
4696 O OE1 . GLN B 203 ? 0.6110 0.4762 0.6931 0.1032  -0.0474 -0.0899 212 GLN B OE1 
4697 N NE2 . GLN B 203 ? 0.5783 0.4752 0.6397 0.1047  -0.0323 -0.0777 212 GLN B NE2 
4698 N N   . VAL B 204 ? 0.4214 0.2911 0.4679 0.0505  -0.0171 -0.0441 213 VAL B N   
4699 C CA  . VAL B 204 ? 0.4326 0.2992 0.4800 0.0416  -0.0154 -0.0425 213 VAL B CA  
4700 C C   . VAL B 204 ? 0.4226 0.3034 0.4576 0.0455  -0.0123 -0.0553 213 VAL B C   
4701 O O   . VAL B 204 ? 0.4215 0.2978 0.4622 0.0451  -0.0168 -0.0639 213 VAL B O   
4702 C CB  . VAL B 204 ? 0.4208 0.2903 0.4614 0.0300  -0.0070 -0.0244 213 VAL B CB  
4703 C CG1 . VAL B 204 ? 0.4189 0.2899 0.4589 0.0220  -0.0037 -0.0238 213 VAL B CG1 
4704 C CG2 . VAL B 204 ? 0.4388 0.2962 0.4920 0.0259  -0.0101 -0.0091 213 VAL B CG2 
4705 N N   . PHE B 205 ? 0.3967 0.2951 0.4164 0.0494  -0.0053 -0.0554 214 PHE B N   
4706 C CA  . PHE B 205 ? 0.4084 0.3238 0.4161 0.0537  -0.0015 -0.0638 214 PHE B CA  
4707 C C   . PHE B 205 ? 0.3997 0.3160 0.4115 0.0657  -0.0098 -0.0824 214 PHE B C   
4708 O O   . PHE B 205 ? 0.3756 0.2991 0.3815 0.0675  -0.0103 -0.0899 214 PHE B O   
4709 C CB  . PHE B 205 ? 0.4142 0.3491 0.4109 0.0563  0.0063  -0.0585 214 PHE B CB  
4710 C CG  . PHE B 205 ? 0.3865 0.3395 0.3716 0.0555  0.0129  -0.0573 214 PHE B CG  
4711 C CD1 . PHE B 205 ? 0.4257 0.3817 0.4068 0.0573  0.0111  -0.0650 214 PHE B CD1 
4712 C CD2 . PHE B 205 ? 0.3808 0.3488 0.3610 0.0533  0.0198  -0.0479 214 PHE B CD2 
4713 C CE1 . PHE B 205 ? 0.4210 0.3944 0.3921 0.0571  0.0167  -0.0614 214 PHE B CE1 
4714 C CE2 . PHE B 205 ? 0.4060 0.3906 0.3794 0.0521  0.0252  -0.0440 214 PHE B CE2 
4715 C CZ  . PHE B 205 ? 0.4189 0.4063 0.3870 0.0541  0.0239  -0.0498 214 PHE B CZ  
4716 N N   . HIS B 206 ? 0.4394 0.3485 0.4619 0.0747  -0.0175 -0.0907 215 HIS B N   
4717 C CA  . HIS B 206 ? 0.4804 0.3896 0.5088 0.0884  -0.0278 -0.1120 215 HIS B CA  
4718 C C   . HIS B 206 ? 0.4728 0.3697 0.5102 0.0852  -0.0361 -0.1206 215 HIS B C   
4719 O O   . HIS B 206 ? 0.4625 0.3670 0.4975 0.0964  -0.0427 -0.1392 215 HIS B O   
4720 C CB  . HIS B 206 ? 0.5205 0.4173 0.5653 0.0974  -0.0376 -0.1196 215 HIS B CB  
4721 C CG  . HIS B 206 ? 0.5340 0.4458 0.5722 0.1045  -0.0317 -0.1162 215 HIS B CG  
4722 N ND1 . HIS B 206 ? 0.5755 0.4812 0.6265 0.1155  -0.0399 -0.1247 215 HIS B ND1 
4723 C CD2 . HIS B 206 ? 0.5849 0.5176 0.6080 0.1021  -0.0194 -0.1053 215 HIS B CD2 
4724 C CE1 . HIS B 206 ? 0.6308 0.5545 0.6738 0.1197  -0.0321 -0.1191 215 HIS B CE1 
4725 N NE2 . HIS B 206 ? 0.6161 0.5563 0.6430 0.1113  -0.0198 -0.1071 215 HIS B NE2 
4726 N N   . GLN B 207 ? 0.4565 0.3371 0.5043 0.0708  -0.0358 -0.1075 216 GLN B N   
4727 C CA  . GLN B 207 ? 0.4832 0.3539 0.5421 0.0654  -0.0426 -0.1128 216 GLN B CA  
4728 C C   . GLN B 207 ? 0.4520 0.3397 0.4941 0.0669  -0.0386 -0.1189 216 GLN B C   
4729 O O   . GLN B 207 ? 0.4671 0.3493 0.5182 0.0664  -0.0468 -0.1286 216 GLN B O   
4730 C CB  . GLN B 207 ? 0.4867 0.3433 0.5582 0.0491  -0.0396 -0.0937 216 GLN B CB  
4731 C CG  . GLN B 207 ? 0.5367 0.3744 0.6293 0.0457  -0.0455 -0.0846 216 GLN B CG  
4732 C CD  . GLN B 207 ? 0.5580 0.3897 0.6586 0.0303  -0.0395 -0.0627 216 GLN B CD  
4733 O OE1 . GLN B 207 ? 0.5659 0.3933 0.6788 0.0227  -0.0417 -0.0611 216 GLN B OE1 
4734 N NE2 . GLN B 207 ? 0.6304 0.4643 0.7240 0.0266  -0.0319 -0.0461 216 GLN B NE2 
4735 N N   . ILE B 208 ? 0.4433 0.3513 0.4638 0.0681  -0.0271 -0.1122 217 ILE B N   
4736 C CA  . ILE B 208 ? 0.4053 0.3300 0.4106 0.0691  -0.0230 -0.1143 217 ILE B CA  
4737 C C   . ILE B 208 ? 0.4217 0.3545 0.4247 0.0831  -0.0331 -0.1360 217 ILE B C   
4738 O O   . ILE B 208 ? 0.3962 0.3320 0.3970 0.0822  -0.0365 -0.1411 217 ILE B O   
4739 C CB  . ILE B 208 ? 0.4141 0.3597 0.4007 0.0689  -0.0101 -0.1021 217 ILE B CB  
4740 C CG1 . ILE B 208 ? 0.4341 0.3921 0.4094 0.0652  -0.0055 -0.0974 217 ILE B CG1 
4741 C CG2 . ILE B 208 ? 0.3718 0.3359 0.3497 0.0832  -0.0089 -0.1098 217 ILE B CG2 
4742 C CD1 . ILE B 208 ? 0.4850 0.4316 0.4656 0.0505  -0.0017 -0.0844 217 ILE B CD1 
4743 N N   . HIS B 209 ? 0.4076 0.3439 0.4122 0.0968  -0.0390 -0.1500 218 HIS B N   
4744 C CA  . HIS B 209 ? 0.4395 0.3864 0.4408 0.1135  -0.0495 -0.1739 218 HIS B CA  
4745 C C   . HIS B 209 ? 0.4617 0.3884 0.4834 0.1120  -0.0654 -0.1883 218 HIS B C   
4746 O O   . HIS B 209 ? 0.4586 0.3954 0.4750 0.1227  -0.0740 -0.2065 218 HIS B O   
4747 C CB  . HIS B 209 ? 0.4580 0.4124 0.4596 0.1293  -0.0529 -0.1867 218 HIS B CB  
4748 C CG  . HIS B 209 ? 0.4784 0.4561 0.4631 0.1317  -0.0381 -0.1736 218 HIS B CG  
4749 N ND1 . HIS B 209 ? 0.5022 0.5127 0.4649 0.1402  -0.0296 -0.1727 218 HIS B ND1 
4750 C CD2 . HIS B 209 ? 0.4841 0.4584 0.4727 0.1264  -0.0309 -0.1597 218 HIS B CD2 
4751 C CE1 . HIS B 209 ? 0.5275 0.5532 0.4840 0.1392  -0.0177 -0.1585 218 HIS B CE1 
4752 N NE2 . HIS B 209 ? 0.4864 0.4904 0.4579 0.1312  -0.0187 -0.1515 218 HIS B NE2 
4753 N N   . ASP B 210 ? 0.4683 0.3684 0.5138 0.0988  -0.0693 -0.1791 219 ASP B N   
4754 C CA  . ASP B 210 ? 0.4815 0.3606 0.5539 0.0949  -0.0847 -0.1894 219 ASP B CA  
4755 C C   . ASP B 210 ? 0.4505 0.3302 0.5234 0.0832  -0.0824 -0.1820 219 ASP B C   
4756 O O   . ASP B 210 ? 0.4699 0.3395 0.5619 0.0827  -0.0958 -0.1942 219 ASP B O   
4757 C CB  . ASP B 210 ? 0.5015 0.3538 0.6025 0.0849  -0.0893 -0.1784 219 ASP B CB  
4758 C CG  . ASP B 210 ? 0.5369 0.3846 0.6429 0.0967  -0.0945 -0.1867 219 ASP B CG  
4759 O OD1 . ASP B 210 ? 0.6465 0.5007 0.7515 0.1142  -0.1054 -0.2116 219 ASP B OD1 
4760 O OD2 . ASP B 210 ? 0.5908 0.4295 0.7021 0.0892  -0.0881 -0.1687 219 ASP B OD2 
4761 N N   . HIS B 211 ? 0.4232 0.3142 0.4784 0.0741  -0.0668 -0.1628 220 HIS B N   
4762 C CA  . HIS B 211 ? 0.4137 0.3040 0.4722 0.0620  -0.0639 -0.1537 220 HIS B CA  
4763 C C   . HIS B 211 ? 0.4193 0.3319 0.4521 0.0651  -0.0558 -0.1515 220 HIS B C   
4764 O O   . HIS B 211 ? 0.4051 0.3183 0.4410 0.0572  -0.0551 -0.1467 220 HIS B O   
4765 C CB  . HIS B 211 ? 0.3882 0.2669 0.4574 0.0455  -0.0545 -0.1307 220 HIS B CB  
4766 C CG  . HIS B 211 ? 0.3597 0.2178 0.4549 0.0412  -0.0615 -0.1276 220 HIS B CG  
4767 N ND1 . HIS B 211 ? 0.4255 0.2678 0.5500 0.0400  -0.0766 -0.1376 220 HIS B ND1 
4768 C CD2 . HIS B 211 ? 0.3802 0.2307 0.4785 0.0380  -0.0565 -0.1146 220 HIS B CD2 
4769 C CE1 . HIS B 211 ? 0.4341 0.2594 0.5798 0.0358  -0.0804 -0.1296 220 HIS B CE1 
4770 N NE2 . HIS B 211 ? 0.3982 0.2286 0.5271 0.0348  -0.0681 -0.1153 220 HIS B NE2 
4771 N N   . VAL B 212 ? 0.4254 0.3574 0.4352 0.0764  -0.0502 -0.1540 221 VAL B N   
4772 C CA  . VAL B 212 ? 0.4337 0.3885 0.4207 0.0800  -0.0430 -0.1495 221 VAL B CA  
4773 C C   . VAL B 212 ? 0.4343 0.4103 0.4055 0.0992  -0.0487 -0.1673 221 VAL B C   
4774 O O   . VAL B 212 ? 0.4104 0.3921 0.3780 0.1093  -0.0487 -0.1742 221 VAL B O   
4775 C CB  . VAL B 212 ? 0.4231 0.3869 0.3972 0.0735  -0.0273 -0.1284 221 VAL B CB  
4776 C CG1 . VAL B 212 ? 0.4511 0.4330 0.4095 0.0730  -0.0213 -0.1195 221 VAL B CG1 
4777 C CG2 . VAL B 212 ? 0.4503 0.3951 0.4384 0.0581  -0.0222 -0.1136 221 VAL B CG2 
4778 N N   . ASN B 213 ? 0.4470 0.4364 0.4084 0.1050  -0.0535 -0.1746 222 ASN B N   
4779 C CA  . ASN B 213 ? 0.4680 0.4838 0.4099 0.1245  -0.0582 -0.1904 222 ASN B CA  
4780 C C   . ASN B 213 ? 0.4445 0.4876 0.3625 0.1258  -0.0437 -0.1713 222 ASN B C   
4781 O O   . ASN B 213 ? 0.4267 0.4674 0.3443 0.1139  -0.0377 -0.1544 222 ASN B O   
4782 C CB  . ASN B 213 ? 0.5237 0.5389 0.4701 0.1304  -0.0738 -0.2093 222 ASN B CB  
4783 C CG  . ASN B 213 ? 0.5689 0.6176 0.4886 0.1485  -0.0757 -0.2185 222 ASN B CG  
4784 O OD1 . ASN B 213 ? 0.7008 0.7621 0.6088 0.1459  -0.0721 -0.2078 222 ASN B OD1 
4785 N ND2 . ASN B 213 ? 0.6626 0.7275 0.5725 0.1677  -0.0815 -0.2382 222 ASN B ND2 
4786 N N   . PRO B 214 ? 0.4400 0.5093 0.3409 0.1398  -0.0380 -0.1729 223 PRO B N   
4787 C CA  . PRO B 214 ? 0.4512 0.5482 0.3336 0.1402  -0.0240 -0.1516 223 PRO B CA  
4788 C C   . PRO B 214 ? 0.4491 0.5608 0.3193 0.1403  -0.0242 -0.1436 223 PRO B C   
4789 O O   . PRO B 214 ? 0.4283 0.5407 0.2984 0.1285  -0.0149 -0.1204 223 PRO B O   
4790 C CB  . PRO B 214 ? 0.4586 0.5855 0.3263 0.1593  -0.0214 -0.1608 223 PRO B CB  
4791 C CG  . PRO B 214 ? 0.4700 0.5761 0.3534 0.1627  -0.0296 -0.1795 223 PRO B CG  
4792 C CD  . PRO B 214 ? 0.4796 0.5551 0.3804 0.1557  -0.0439 -0.1929 223 PRO B CD  
4793 N N   . LYS B 215 ? 0.4832 0.6054 0.3450 0.1538  -0.0362 -0.1633 224 LYS B N   
4794 C CA  . LYS B 215 ? 0.5045 0.6420 0.3538 0.1562  -0.0386 -0.1576 224 LYS B CA  
4795 C C   . LYS B 215 ? 0.4914 0.6030 0.3569 0.1372  -0.0392 -0.1455 224 LYS B C   
4796 O O   . LYS B 215 ? 0.4977 0.6181 0.3574 0.1310  -0.0322 -0.1247 224 LYS B O   
4797 C CB  . LYS B 215 ? 0.5459 0.6966 0.3856 0.1749  -0.0543 -0.1857 224 LYS B CB  
4798 C CG  . LYS B 215 ? 0.5610 0.7326 0.3846 0.1808  -0.0582 -0.1814 224 LYS B CG  
4799 C CD  . LYS B 215 ? 0.6438 0.8319 0.4560 0.2022  -0.0750 -0.2123 224 LYS B CD  
4800 C CE  . LYS B 215 ? 0.6356 0.8473 0.4294 0.2095  -0.0792 -0.2072 224 LYS B CE  
4801 N NZ  . LYS B 215 ? 0.6616 0.8912 0.4433 0.2316  -0.0971 -0.2393 224 LYS B NZ  
4802 N N   . ALA B 216 ? 0.4552 0.5364 0.3427 0.1284  -0.0479 -0.1577 225 ALA B N   
4803 C CA  . ALA B 216 ? 0.4434 0.5021 0.3481 0.1110  -0.0478 -0.1473 225 ALA B CA  
4804 C C   . ALA B 216 ? 0.4305 0.4832 0.3383 0.0971  -0.0333 -0.1223 225 ALA B C   
4805 O O   . ALA B 216 ? 0.3907 0.4408 0.3013 0.0881  -0.0300 -0.1082 225 ALA B O   
4806 C CB  . ALA B 216 ? 0.4417 0.4724 0.3716 0.1040  -0.0577 -0.1619 225 ALA B CB  
4807 N N   . PHE B 217 ? 0.4133 0.4634 0.3220 0.0959  -0.0259 -0.1182 226 PHE B N   
4808 C CA  . PHE B 217 ? 0.4123 0.4575 0.3246 0.0839  -0.0138 -0.0969 226 PHE B CA  
4809 C C   . PHE B 217 ? 0.4192 0.4868 0.3186 0.0853  -0.0063 -0.0782 226 PHE B C   
4810 O O   . PHE B 217 ? 0.4124 0.4728 0.3186 0.0745  -0.0026 -0.0632 226 PHE B O   
4811 C CB  . PHE B 217 ? 0.4174 0.4597 0.3323 0.0845  -0.0084 -0.0966 226 PHE B CB  
4812 C CG  . PHE B 217 ? 0.3780 0.4155 0.2979 0.0727  0.0022  -0.0767 226 PHE B CG  
4813 C CD1 . PHE B 217 ? 0.4123 0.4265 0.3467 0.0594  0.0028  -0.0724 226 PHE B CD1 
4814 C CD2 . PHE B 217 ? 0.4103 0.4686 0.3215 0.0752  0.0110  -0.0620 226 PHE B CD2 
4815 C CE1 . PHE B 217 ? 0.4258 0.4362 0.3647 0.0499  0.0106  -0.0570 226 PHE B CE1 
4816 C CE2 . PHE B 217 ? 0.4249 0.4775 0.3443 0.0640  0.0184  -0.0451 226 PHE B CE2 
4817 C CZ  . PHE B 217 ? 0.4139 0.4418 0.3464 0.0519  0.0175  -0.0442 226 PHE B CZ  
4818 N N   . PHE B 218 ? 0.4476 0.5430 0.3300 0.0992  -0.0044 -0.0789 227 PHE B N   
4819 C CA  . PHE B 218 ? 0.4809 0.6022 0.3522 0.1014  0.0035  -0.0579 227 PHE B CA  
4820 C C   . PHE B 218 ? 0.4994 0.6252 0.3668 0.1010  -0.0015 -0.0519 227 PHE B C   
4821 O O   . PHE B 218 ? 0.4637 0.5897 0.3364 0.0923  0.0033  -0.0311 227 PHE B O   
4822 C CB  . PHE B 218 ? 0.4958 0.6512 0.3488 0.1185  0.0069  -0.0610 227 PHE B CB  
4823 C CG  . PHE B 218 ? 0.5021 0.6883 0.3455 0.1207  0.0163  -0.0358 227 PHE B CG  
4824 C CD1 . PHE B 218 ? 0.4918 0.6826 0.3444 0.1122  0.0274  -0.0148 227 PHE B CD1 
4825 C CD2 . PHE B 218 ? 0.5144 0.7260 0.3410 0.1314  0.0134  -0.0321 227 PHE B CD2 
4826 C CE1 . PHE B 218 ? 0.5149 0.7346 0.3636 0.1130  0.0357  0.0113  227 PHE B CE1 
4827 C CE2 . PHE B 218 ? 0.5299 0.7717 0.3495 0.1330  0.0223  -0.0050 227 PHE B CE2 
4828 C CZ  . PHE B 218 ? 0.5273 0.7727 0.3596 0.1232  0.0336  0.0175  227 PHE B CZ  
4829 N N   . SER B 219 ? 0.5297 0.6591 0.3897 0.1110  -0.0123 -0.0708 228 SER B N   
4830 C CA  . SER B 219 ? 0.5480 0.6859 0.4019 0.1136  -0.0185 -0.0667 228 SER B CA  
4831 C C   . SER B 219 ? 0.5354 0.6457 0.4084 0.0994  -0.0231 -0.0654 228 SER B C   
4832 O O   . SER B 219 ? 0.5437 0.6593 0.4155 0.0986  -0.0259 -0.0556 228 SER B O   
4833 C CB  . SER B 219 ? 0.5868 0.7428 0.4248 0.1316  -0.0298 -0.0890 228 SER B CB  
4834 O OG  . SER B 219 ? 0.6425 0.7753 0.4936 0.1308  -0.0408 -0.1144 228 SER B OG  
4835 N N   . VAL B 220 ? 0.5226 0.6056 0.4133 0.0890  -0.0236 -0.0739 229 VAL B N   
4836 C CA  . VAL B 220 ? 0.5147 0.5757 0.4236 0.0772  -0.0277 -0.0747 229 VAL B CA  
4837 C C   . VAL B 220 ? 0.5077 0.5505 0.4310 0.0629  -0.0189 -0.0622 229 VAL B C   
4838 O O   . VAL B 220 ? 0.4976 0.5379 0.4267 0.0561  -0.0160 -0.0479 229 VAL B O   
4839 C CB  . VAL B 220 ? 0.5380 0.5856 0.4580 0.0785  -0.0391 -0.0979 229 VAL B CB  
4840 C CG1 . VAL B 220 ? 0.5392 0.5713 0.4778 0.0680  -0.0430 -0.0972 229 VAL B CG1 
4841 C CG2 . VAL B 220 ? 0.5642 0.6306 0.4697 0.0947  -0.0497 -0.1140 229 VAL B CG2 
4842 N N   . LEU B 221 ? 0.4806 0.5113 0.4101 0.0593  -0.0158 -0.0681 230 LEU B N   
4843 C CA  . LEU B 221 ? 0.4638 0.4775 0.4065 0.0468  -0.0090 -0.0593 230 LEU B CA  
4844 C C   . LEU B 221 ? 0.4606 0.4813 0.4004 0.0433  -0.0005 -0.0406 230 LEU B C   
4845 O O   . LEU B 221 ? 0.4563 0.4669 0.4067 0.0343  0.0020  -0.0319 230 LEU B O   
4846 C CB  . LEU B 221 ? 0.4696 0.4704 0.4189 0.0447  -0.0083 -0.0686 230 LEU B CB  
4847 C CG  . LEU B 221 ? 0.4330 0.4171 0.3953 0.0330  -0.0028 -0.0621 230 LEU B CG  
4848 C CD1 . LEU B 221 ? 0.4427 0.4177 0.4178 0.0252  -0.0048 -0.0616 230 LEU B CD1 
4849 C CD2 . LEU B 221 ? 0.4726 0.4459 0.4408 0.0326  -0.0036 -0.0700 230 LEU B CD2 
4850 N N   . ARG B 222 ? 0.4521 0.4911 0.3796 0.0508  0.0033  -0.0349 231 ARG B N   
4851 C CA  . ARG B 222 ? 0.4558 0.5049 0.3838 0.0476  0.0105  -0.0151 231 ARG B CA  
4852 C C   . ARG B 222 ? 0.4429 0.4908 0.3782 0.0424  0.0087  -0.0015 231 ARG B C   
4853 O O   . ARG B 222 ? 0.4392 0.4796 0.3867 0.0340  0.0116  0.0104  231 ARG B O   
4854 C CB  . ARG B 222 ? 0.4699 0.5464 0.3829 0.0588  0.0143  -0.0101 231 ARG B CB  
4855 C CG  . ARG B 222 ? 0.4876 0.5787 0.4042 0.0554  0.0220  0.0130  231 ARG B CG  
4856 C CD  . ARG B 222 ? 0.4853 0.6085 0.3871 0.0675  0.0270  0.0183  231 ARG B CD  
4857 N NE  . ARG B 222 ? 0.5698 0.7126 0.4563 0.0780  0.0229  0.0181  231 ARG B NE  
4858 C CZ  . ARG B 222 ? 0.5781 0.7339 0.4644 0.0772  0.0232  0.0377  231 ARG B CZ  
4859 N NH1 . ARG B 222 ? 0.6080 0.7585 0.5115 0.0658  0.0267  0.0597  231 ARG B NH1 
4860 N NH2 . ARG B 222 ? 0.5868 0.7612 0.4567 0.0885  0.0185  0.0350  231 ARG B NH2 
4861 N N   . ILE B 223 ? 0.4646 0.5194 0.3938 0.0480  0.0025  -0.0046 232 ILE B N   
4862 C CA  . ILE B 223 ? 0.4483 0.5020 0.3850 0.0446  -0.0010 0.0072  232 ILE B CA  
4863 C C   . ILE B 223 ? 0.4151 0.4453 0.3702 0.0339  -0.0024 0.0042  232 ILE B C   
4864 O O   . ILE B 223 ? 0.3948 0.4195 0.3621 0.0277  -0.0014 0.0170  232 ILE B O   
4865 C CB  . ILE B 223 ? 0.4866 0.5517 0.4128 0.0537  -0.0091 0.0008  232 ILE B CB  
4866 C CG1 . ILE B 223 ? 0.5659 0.6608 0.4736 0.0650  -0.0073 0.0116  232 ILE B CG1 
4867 C CG2 . ILE B 223 ? 0.5160 0.5722 0.4545 0.0492  -0.0150 0.0065  232 ILE B CG2 
4868 C CD1 . ILE B 223 ? 0.6018 0.7105 0.4938 0.0750  -0.0052 -0.0016 232 ILE B CD1 
4869 N N   . TYR B 224 ? 0.3678 0.3853 0.3265 0.0323  -0.0051 -0.0127 233 TYR B N   
4870 C CA  . TYR B 224 ? 0.3643 0.3646 0.3391 0.0240  -0.0057 -0.0164 233 TYR B CA  
4871 C C   . TYR B 224 ? 0.3563 0.3470 0.3386 0.0170  0.0002  -0.0120 233 TYR B C   
4872 O O   . TYR B 224 ? 0.4006 0.3818 0.3951 0.0119  -0.0003 -0.0110 233 TYR B O   
4873 C CB  . TYR B 224 ? 0.3553 0.3482 0.3344 0.0236  -0.0095 -0.0327 233 TYR B CB  
4874 C CG  . TYR B 224 ? 0.3741 0.3754 0.3500 0.0299  -0.0176 -0.0376 233 TYR B CG  
4875 C CD1 . TYR B 224 ? 0.3745 0.3755 0.3591 0.0289  -0.0219 -0.0333 233 TYR B CD1 
4876 C CD2 . TYR B 224 ? 0.2860 0.2969 0.2503 0.0382  -0.0221 -0.0473 233 TYR B CD2 
4877 C CE1 . TYR B 224 ? 0.3436 0.3537 0.3249 0.0353  -0.0302 -0.0372 233 TYR B CE1 
4878 C CE2 . TYR B 224 ? 0.3800 0.4006 0.3402 0.0453  -0.0310 -0.0529 233 TYR B CE2 
4879 C CZ  . TYR B 224 ? 0.3290 0.3493 0.2975 0.0435  -0.0348 -0.0470 233 TYR B CZ  
4880 O OH  . TYR B 224 ? 0.3469 0.3774 0.3114 0.0508  -0.0443 -0.0522 233 TYR B OH  
4881 N N   . LEU B 225 ? 0.3721 0.3665 0.3472 0.0180  0.0051  -0.0104 234 LEU B N   
4882 C CA  . LEU B 225 ? 0.3685 0.3563 0.3501 0.0123  0.0098  -0.0053 234 LEU B CA  
4883 C C   . LEU B 225 ? 0.3630 0.3560 0.3518 0.0100  0.0104  0.0107  234 LEU B C   
4884 O O   . LEU B 225 ? 0.3945 0.3804 0.3928 0.0049  0.0117  0.0135  234 LEU B O   
4885 C CB  . LEU B 225 ? 0.3632 0.3532 0.3368 0.0145  0.0141  -0.0099 234 LEU B CB  
4886 C CG  . LEU B 225 ? 0.3818 0.3640 0.3534 0.0157  0.0126  -0.0242 234 LEU B CG  
4887 C CD1 . LEU B 225 ? 0.3945 0.3790 0.3596 0.0191  0.0154  -0.0275 234 LEU B CD1 
4888 C CD2 . LEU B 225 ? 0.4125 0.3813 0.3949 0.0087  0.0127  -0.0283 234 LEU B CD2 
4889 N N   A SER B 226 ? 0.3894 0.3953 0.3751 0.0138  0.0087  0.0219  235 SER B N   
4890 N N   B SER B 226 ? 0.3856 0.3914 0.3713 0.0139  0.0086  0.0217  235 SER B N   
4891 C CA  A SER B 226 ? 0.3981 0.4105 0.3943 0.0109  0.0090  0.0409  235 SER B CA  
4892 C CA  B SER B 226 ? 0.3934 0.4057 0.3895 0.0111  0.0087  0.0408  235 SER B CA  
4893 C C   A SER B 226 ? 0.4078 0.4061 0.4233 0.0054  0.0028  0.0441  235 SER B C   
4894 C C   B SER B 226 ? 0.4042 0.4017 0.4199 0.0052  0.0028  0.0434  235 SER B C   
4895 O O   A SER B 226 ? 0.4118 0.4023 0.4290 0.0063  -0.0017 0.0351  235 SER B O   
4896 O O   B SER B 226 ? 0.4056 0.3940 0.4236 0.0057  -0.0015 0.0332  235 SER B O   
4897 C CB  A SER B 226 ? 0.4029 0.4373 0.3893 0.0173  0.0100  0.0548  235 SER B CB  
4898 C CB  B SER B 226 ? 0.3922 0.4253 0.3790 0.0175  0.0086  0.0541  235 SER B CB  
4899 O OG  A SER B 226 ? 0.4172 0.4525 0.4003 0.0211  0.0041  0.0534  235 SER B OG  
4900 O OG  B SER B 226 ? 0.3915 0.4409 0.3599 0.0251  0.0135  0.0493  235 SER B OG  
4901 N N   . GLY B 227 ? 0.3986 0.3943 0.4307 0.0001  0.0018  0.0560  236 GLY B N   
4902 C CA  . GLY B 227 ? 0.3868 0.3678 0.4409 -0.0045 -0.0058 0.0571  236 GLY B CA  
4903 C C   . GLY B 227 ? 0.3803 0.3661 0.4498 -0.0058 -0.0111 0.0778  236 GLY B C   
4904 O O   . GLY B 227 ? 0.3902 0.3921 0.4496 -0.0018 -0.0090 0.0908  236 GLY B O   
4905 N N   . TRP B 228 ? 0.3787 0.3508 0.4737 -0.0107 -0.0188 0.0808  237 TRP B N   
4906 C CA  . TRP B 228 ? 0.3895 0.3620 0.5067 -0.0132 -0.0261 0.1019  237 TRP B CA  
4907 C C   . TRP B 228 ? 0.4000 0.3641 0.5462 -0.0206 -0.0314 0.1099  237 TRP B C   
4908 O O   . TRP B 228 ? 0.3986 0.3473 0.5710 -0.0231 -0.0425 0.1099  237 TRP B O   
4909 C CB  . TRP B 228 ? 0.3695 0.3313 0.4943 -0.0101 -0.0350 0.0967  237 TRP B CB  
4910 C CG  . TRP B 228 ? 0.3318 0.2791 0.4553 -0.0081 -0.0374 0.0706  237 TRP B CG  
4911 C CD1 . TRP B 228 ? 0.3291 0.2603 0.4736 -0.0096 -0.0454 0.0591  237 TRP B CD1 
4912 C CD2 . TRP B 228 ? 0.3141 0.2642 0.4155 -0.0035 -0.0322 0.0529  237 TRP B CD2 
4913 N NE1 . TRP B 228 ? 0.3278 0.2547 0.4621 -0.0057 -0.0437 0.0365  237 TRP B NE1 
4914 C CE2 . TRP B 228 ? 0.2871 0.2249 0.3968 -0.0029 -0.0356 0.0336  237 TRP B CE2 
4915 C CE3 . TRP B 228 ? 0.3626 0.3255 0.4398 0.0005  -0.0256 0.0511  237 TRP B CE3 
4916 C CZ2 . TRP B 228 ? 0.3444 0.2835 0.4401 0.0003  -0.0312 0.0161  237 TRP B CZ2 
4917 C CZ3 . TRP B 228 ? 0.3104 0.2712 0.3764 0.0031  -0.0233 0.0321  237 TRP B CZ3 
4918 C CH2 . TRP B 228 ? 0.2775 0.2270 0.3534 0.0024  -0.0254 0.0165  237 TRP B CH2 
4919 N N   . LYS B 229 ? 0.4284 0.4032 0.5710 -0.0234 -0.0242 0.1156  238 LYS B N   
4920 C CA  . LYS B 229 ? 0.4543 0.4271 0.6257 -0.0309 -0.0285 0.1284  238 LYS B CA  
4921 C C   . LYS B 229 ? 0.4817 0.4801 0.6488 -0.0322 -0.0189 0.1521  238 LYS B C   
4922 O O   . LYS B 229 ? 0.5116 0.5232 0.6557 -0.0289 -0.0087 0.1459  238 LYS B O   
4923 C CB  . LYS B 229 ? 0.4342 0.3954 0.6079 -0.0325 -0.0299 0.1076  238 LYS B CB  
4924 C CG  . LYS B 229 ? 0.4593 0.4201 0.6629 -0.0401 -0.0349 0.1185  238 LYS B CG  
4925 C CD  . LYS B 229 ? 0.4868 0.4302 0.7004 -0.0405 -0.0431 0.0954  238 LYS B CD  
4926 C CE  . LYS B 229 ? 0.5274 0.4712 0.7698 -0.0475 -0.0488 0.1031  238 LYS B CE  
4927 N NZ  . LYS B 229 ? 0.5570 0.4876 0.8008 -0.0454 -0.0559 0.0771  238 LYS B NZ  
4928 N N   . GLY B 230 ? 0.5334 0.5401 0.7236 -0.0366 -0.0224 0.1799  239 GLY B N   
4929 C CA  . GLY B 230 ? 0.5529 0.5902 0.7384 -0.0364 -0.0123 0.2067  239 GLY B CA  
4930 C C   . GLY B 230 ? 0.5783 0.6363 0.7278 -0.0263 -0.0035 0.2082  239 GLY B C   
4931 O O   . GLY B 230 ? 0.5890 0.6754 0.7228 -0.0223 0.0074  0.2198  239 GLY B O   
4932 N N   . ASN B 231 ? 0.5695 0.6151 0.7068 -0.0213 -0.0089 0.1955  240 ASN B N   
4933 C CA  . ASN B 231 ? 0.5806 0.6433 0.6854 -0.0111 -0.0036 0.1934  240 ASN B CA  
4934 C C   . ASN B 231 ? 0.6050 0.6771 0.7191 -0.0100 -0.0087 0.2190  240 ASN B C   
4935 O O   . ASN B 231 ? 0.6141 0.6653 0.7470 -0.0128 -0.0197 0.2179  240 ASN B O   
4936 C CB  . ASN B 231 ? 0.5888 0.6329 0.6753 -0.0063 -0.0065 0.1619  240 ASN B CB  
4937 C CG  . ASN B 231 ? 0.5843 0.6457 0.6370 0.0045  -0.0015 0.1538  240 ASN B CG  
4938 O OD1 . ASN B 231 ? 0.5414 0.6269 0.5838 0.0101  0.0011  0.1717  240 ASN B OD1 
4939 N ND2 . ASN B 231 ? 0.5745 0.6248 0.6112 0.0077  -0.0009 0.1267  240 ASN B ND2 
4940 N N   . PRO B 232 ? 0.6296 0.7349 0.7311 -0.0051 -0.0008 0.2425  241 PRO B N   
4941 C CA  . PRO B 232 ? 0.6479 0.7666 0.7551 -0.0029 -0.0050 0.2699  241 PRO B CA  
4942 C C   . PRO B 232 ? 0.6560 0.7629 0.7501 0.0040  -0.0136 0.2566  241 PRO B C   
4943 O O   . PRO B 232 ? 0.6500 0.7532 0.7612 0.0026  -0.0221 0.2757  241 PRO B O   
4944 C CB  . PRO B 232 ? 0.6566 0.8185 0.7397 0.0054  0.0076  0.2884  241 PRO B CB  
4945 C CG  . PRO B 232 ? 0.6519 0.8207 0.7353 0.0024  0.0168  0.2817  241 PRO B CG  
4946 C CD  . PRO B 232 ? 0.6219 0.7568 0.7036 -0.0003 0.0123  0.2458  241 PRO B CD  
4947 N N   . GLN B 233 ? 0.6709 0.7721 0.7377 0.0110  -0.0119 0.2253  242 GLN B N   
4948 C CA  . GLN B 233 ? 0.6760 0.7656 0.7326 0.0170  -0.0202 0.2091  242 GLN B CA  
4949 C C   . GLN B 233 ? 0.6642 0.7213 0.7506 0.0101  -0.0320 0.2027  242 GLN B C   
4950 O O   . GLN B 233 ? 0.6570 0.7086 0.7473 0.0136  -0.0408 0.2047  242 GLN B O   
4951 C CB  . GLN B 233 ? 0.6659 0.7541 0.6943 0.0237  -0.0164 0.1767  242 GLN B CB  
4952 C CG  . GLN B 233 ? 0.7258 0.8459 0.7228 0.0343  -0.0081 0.1776  242 GLN B CG  
4953 C CD  . GLN B 233 ? 0.7225 0.8387 0.6962 0.0415  -0.0084 0.1456  242 GLN B CD  
4954 O OE1 . GLN B 233 ? 0.8479 0.9762 0.8032 0.0513  -0.0125 0.1393  242 GLN B OE1 
4955 N NE2 . GLN B 233 ? 0.7799 0.8790 0.7562 0.0367  -0.0051 0.1257  242 GLN B NE2 
4956 N N   . LEU B 234 ? 0.6410 0.6780 0.7473 0.0017  -0.0327 0.1933  243 LEU B N   
4957 C CA  . LEU B 234 ? 0.6498 0.6583 0.7878 -0.0040 -0.0444 0.1875  243 LEU B CA  
4958 C C   . LEU B 234 ? 0.6390 0.6415 0.8088 -0.0138 -0.0466 0.2042  243 LEU B C   
4959 O O   . LEU B 234 ? 0.6216 0.6086 0.8018 -0.0184 -0.0474 0.1875  243 LEU B O   
4960 C CB  . LEU B 234 ? 0.6534 0.6426 0.7845 -0.0028 -0.0452 0.1526  243 LEU B CB  
4961 C CG  . LEU B 234 ? 0.6496 0.6417 0.7559 0.0052  -0.0444 0.1333  243 LEU B CG  
4962 C CD1 . LEU B 234 ? 0.6797 0.6884 0.7548 0.0092  -0.0334 0.1239  243 LEU B CD1 
4963 C CD2 . LEU B 234 ? 0.6484 0.6194 0.7638 0.0049  -0.0495 0.1073  243 LEU B CD2 
4964 N N   . SER B 235 ? 0.6461 0.6624 0.8322 -0.0167 -0.0479 0.2380  244 SER B N   
4965 C CA  . SER B 235 ? 0.6368 0.6526 0.8567 -0.0269 -0.0497 0.2600  244 SER B CA  
4966 C C   . SER B 235 ? 0.6053 0.5887 0.8615 -0.0339 -0.0627 0.2457  244 SER B C   
4967 O O   . SER B 235 ? 0.6008 0.5806 0.8742 -0.0409 -0.0622 0.2453  244 SER B O   
4968 C CB  . SER B 235 ? 0.6826 0.7149 0.9215 -0.0293 -0.0525 0.3012  244 SER B CB  
4969 O OG  . SER B 235 ? 0.7493 0.8182 0.9562 -0.0225 -0.0393 0.3175  244 SER B OG  
4970 N N   . ASP B 236 ? 0.5831 0.5446 0.8512 -0.0310 -0.0751 0.2332  245 ASP B N   
4971 C CA  . ASP B 236 ? 0.5653 0.4971 0.8675 -0.0348 -0.0894 0.2165  245 ASP B CA  
4972 C C   . ASP B 236 ? 0.5203 0.4388 0.8038 -0.0293 -0.0885 0.1764  245 ASP B C   
4973 O O   . ASP B 236 ? 0.4946 0.3911 0.8012 -0.0292 -0.1003 0.1581  245 ASP B O   
4974 C CB  . ASP B 236 ? 0.6231 0.5397 0.9572 -0.0344 -0.1055 0.2293  245 ASP B CB  
4975 C CG  . ASP B 236 ? 0.7113 0.6413 1.0685 -0.0406 -0.1073 0.2729  245 ASP B CG  
4976 O OD1 . ASP B 236 ? 0.7380 0.6651 1.1282 -0.0501 -0.1112 0.2889  245 ASP B OD1 
4977 O OD2 . ASP B 236 ? 0.7727 0.7177 1.1157 -0.0358 -0.1051 0.2920  245 ASP B OD2 
4978 N N   . GLY B 237 ? 0.4566 0.3893 0.6997 -0.0243 -0.0748 0.1630  246 GLY B N   
4979 C CA  . GLY B 237 ? 0.4341 0.3579 0.6586 -0.0195 -0.0723 0.1293  246 GLY B CA  
4980 C C   . GLY B 237 ? 0.4249 0.3449 0.6394 -0.0119 -0.0758 0.1163  246 GLY B C   
4981 O O   . GLY B 237 ? 0.4296 0.3569 0.6429 -0.0093 -0.0782 0.1327  246 GLY B O   
4982 N N   . LEU B 238 ? 0.4180 0.3286 0.6259 -0.0081 -0.0760 0.0876  247 LEU B N   
4983 C CA  . LEU B 238 ? 0.3991 0.3083 0.5979 -0.0010 -0.0779 0.0720  247 LEU B CA  
4984 C C   . LEU B 238 ? 0.3869 0.2784 0.6145 0.0022  -0.0916 0.0586  247 LEU B C   
4985 O O   . LEU B 238 ? 0.3715 0.2525 0.6132 0.0012  -0.0958 0.0452  247 LEU B O   
4986 C CB  . LEU B 238 ? 0.4035 0.3196 0.5740 0.0016  -0.0666 0.0501  247 LEU B CB  
4987 C CG  . LEU B 238 ? 0.3748 0.2952 0.5331 0.0077  -0.0655 0.0361  247 LEU B CG  
4988 C CD1 . LEU B 238 ? 0.4070 0.3405 0.5500 0.0098  -0.0635 0.0509  247 LEU B CD1 
4989 C CD2 . LEU B 238 ? 0.3842 0.3088 0.5236 0.0085  -0.0558 0.0158  247 LEU B CD2 
4990 N N   . VAL B 239 ? 0.3926 0.2817 0.6288 0.0072  -0.0993 0.0608  248 VAL B N   
4991 C CA  . VAL B 239 ? 0.4086 0.2832 0.6694 0.0129  -0.1119 0.0437  248 VAL B CA  
4992 C C   . VAL B 239 ? 0.3885 0.2696 0.6306 0.0189  -0.1044 0.0155  248 VAL B C   
4993 O O   . VAL B 239 ? 0.3785 0.2714 0.6004 0.0215  -0.0975 0.0136  248 VAL B O   
4994 C CB  . VAL B 239 ? 0.4244 0.2946 0.7041 0.0167  -0.1238 0.0578  248 VAL B CB  
4995 C CG1 . VAL B 239 ? 0.4459 0.3024 0.7508 0.0246  -0.1370 0.0364  248 VAL B CG1 
4996 C CG2 . VAL B 239 ? 0.4247 0.2894 0.7271 0.0102  -0.1315 0.0888  248 VAL B CG2 
4997 N N   . TYR B 240 ? 0.3741 0.2491 0.6237 0.0211  -0.1061 -0.0055 249 TYR B N   
4998 C CA  . TYR B 240 ? 0.3724 0.2549 0.6103 0.0277  -0.1004 -0.0313 249 TYR B CA  
4999 C C   . TYR B 240 ? 0.3843 0.2600 0.6470 0.0367  -0.1133 -0.0446 249 TYR B C   
5000 O O   . TYR B 240 ? 0.3944 0.2605 0.6776 0.0413  -0.1232 -0.0594 249 TYR B O   
5001 C CB  . TYR B 240 ? 0.3995 0.2829 0.6302 0.0270  -0.0954 -0.0462 249 TYR B CB  
5002 C CG  . TYR B 240 ? 0.3684 0.2596 0.5741 0.0193  -0.0823 -0.0353 249 TYR B CG  
5003 C CD1 . TYR B 240 ? 0.3258 0.2119 0.5370 0.0119  -0.0839 -0.0159 249 TYR B CD1 
5004 C CD2 . TYR B 240 ? 0.3693 0.2737 0.5488 0.0195  -0.0687 -0.0438 249 TYR B CD2 
5005 C CE1 . TYR B 240 ? 0.4022 0.2970 0.5916 0.0063  -0.0722 -0.0072 249 TYR B CE1 
5006 C CE2 . TYR B 240 ? 0.3846 0.2947 0.5433 0.0135  -0.0582 -0.0350 249 TYR B CE2 
5007 C CZ  . TYR B 240 ? 0.3534 0.2591 0.5165 0.0075  -0.0599 -0.0177 249 TYR B CZ  
5008 O OH  . TYR B 240 ? 0.3707 0.2835 0.5145 0.0029  -0.0498 -0.0102 249 TYR B OH  
5009 N N   . GLU B 241 ? 0.3855 0.2668 0.6471 0.0401  -0.1142 -0.0403 250 GLU B N   
5010 C CA  . GLU B 241 ? 0.3936 0.2680 0.6813 0.0487  -0.1280 -0.0481 250 GLU B CA  
5011 C C   . GLU B 241 ? 0.3962 0.2745 0.6913 0.0583  -0.1293 -0.0782 250 GLU B C   
5012 O O   . GLU B 241 ? 0.4015 0.2958 0.6756 0.0595  -0.1161 -0.0912 250 GLU B O   
5013 C CB  . GLU B 241 ? 0.3987 0.2829 0.6788 0.0509  -0.1266 -0.0402 250 GLU B CB  
5014 C CG  . GLU B 241 ? 0.4370 0.3131 0.7461 0.0594  -0.1425 -0.0427 250 GLU B CG  
5015 C CD  . GLU B 241 ? 0.4455 0.3339 0.7461 0.0626  -0.1410 -0.0381 250 GLU B CD  
5016 O OE1 . GLU B 241 ? 0.5023 0.4072 0.7821 0.0626  -0.1288 -0.0486 250 GLU B OE1 
5017 O OE2 . GLU B 241 ? 0.5243 0.4061 0.8406 0.0650  -0.1529 -0.0234 250 GLU B OE2 
5018 N N   . GLY B 242 ? 0.4167 0.2815 0.7428 0.0656  -0.1455 -0.0888 251 GLY B N   
5019 C CA  . GLY B 242 ? 0.4171 0.2875 0.7518 0.0775  -0.1486 -0.1195 251 GLY B CA  
5020 C C   . GLY B 242 ? 0.4168 0.2872 0.7460 0.0779  -0.1466 -0.1342 251 GLY B C   
5021 O O   . GLY B 242 ? 0.4296 0.3051 0.7675 0.0896  -0.1516 -0.1606 251 GLY B O   
5022 N N   . PHE B 243 ? 0.4185 0.2851 0.7334 0.0666  -0.1399 -0.1186 252 PHE B N   
5023 C CA  . PHE B 243 ? 0.4323 0.2991 0.7418 0.0665  -0.1387 -0.1312 252 PHE B CA  
5024 C C   . PHE B 243 ? 0.4368 0.2814 0.7731 0.0608  -0.1540 -0.1209 252 PHE B C   
5025 O O   . PHE B 243 ? 0.4452 0.2813 0.8022 0.0676  -0.1674 -0.1400 252 PHE B O   
5026 C CB  . PHE B 243 ? 0.4176 0.3001 0.6908 0.0593  -0.1189 -0.1251 252 PHE B CB  
5027 C CG  . PHE B 243 ? 0.4258 0.3153 0.6892 0.0634  -0.1162 -0.1437 252 PHE B CG  
5028 C CD1 . PHE B 243 ? 0.4540 0.3618 0.7086 0.0751  -0.1115 -0.1676 252 PHE B CD1 
5029 C CD2 . PHE B 243 ? 0.4306 0.3106 0.6956 0.0566  -0.1193 -0.1376 252 PHE B CD2 
5030 C CE1 . PHE B 243 ? 0.4147 0.3318 0.6588 0.0806  -0.1097 -0.1847 252 PHE B CE1 
5031 C CE2 . PHE B 243 ? 0.4219 0.3090 0.6783 0.0616  -0.1186 -0.1558 252 PHE B CE2 
5032 C CZ  . PHE B 243 ? 0.4102 0.3160 0.6546 0.0740  -0.1139 -0.1792 252 PHE B CZ  
5033 N N   . TRP B 244 ? 0.4438 0.2811 0.7812 0.0489  -0.1524 -0.0911 253 TRP B N   
5034 C CA  . TRP B 244 ? 0.4879 0.3053 0.8574 0.0420  -0.1674 -0.0743 253 TRP B CA  
5035 C C   . TRP B 244 ? 0.5046 0.3143 0.8910 0.0383  -0.1739 -0.0482 253 TRP B C   
5036 O O   . TRP B 244 ? 0.4920 0.3139 0.8551 0.0363  -0.1622 -0.0346 253 TRP B O   
5037 C CB  . TRP B 244 ? 0.4843 0.3043 0.8412 0.0301  -0.1585 -0.0574 253 TRP B CB  
5038 C CG  . TRP B 244 ? 0.4958 0.3230 0.8365 0.0323  -0.1528 -0.0778 253 TRP B CG  
5039 C CD1 . TRP B 244 ? 0.4984 0.3175 0.8583 0.0383  -0.1659 -0.1002 253 TRP B CD1 
5040 C CD2 . TRP B 244 ? 0.4312 0.2753 0.7338 0.0287  -0.1335 -0.0768 253 TRP B CD2 
5041 N NE1 . TRP B 244 ? 0.4955 0.3275 0.8291 0.0391  -0.1553 -0.1128 253 TRP B NE1 
5042 C CE2 . TRP B 244 ? 0.4354 0.2819 0.7347 0.0329  -0.1353 -0.0979 253 TRP B CE2 
5043 C CE3 . TRP B 244 ? 0.4486 0.3062 0.7207 0.0233  -0.1162 -0.0615 253 TRP B CE3 
5044 C CZ2 . TRP B 244 ? 0.4458 0.3072 0.7126 0.0311  -0.1198 -0.1013 253 TRP B CZ2 
5045 C CZ3 . TRP B 244 ? 0.3931 0.2637 0.6352 0.0215  -0.1016 -0.0663 253 TRP B CZ3 
5046 C CH2 . TRP B 244 ? 0.4424 0.3146 0.6822 0.0251  -0.1031 -0.0848 253 TRP B CH2 
5047 N N   . GLU B 245 ? 0.5496 0.3391 0.9774 0.0375  -0.1935 -0.0406 254 GLU B N   
5048 C CA  . GLU B 245 ? 0.5715 0.3525 1.0202 0.0343  -0.2021 -0.0131 254 GLU B CA  
5049 C C   . GLU B 245 ? 0.5803 0.3679 1.0193 0.0211  -0.1929 0.0246  254 GLU B C   
5050 O O   . GLU B 245 ? 0.6035 0.3983 1.0342 0.0199  -0.1893 0.0467  254 GLU B O   
5051 C CB  . GLU B 245 ? 0.6224 0.3786 1.1231 0.0379  -0.2276 -0.0164 254 GLU B CB  
5052 C CG  . GLU B 245 ? 0.6581 0.4101 1.1706 0.0538  -0.2383 -0.0503 254 GLU B CG  
5053 C CD  . GLU B 245 ? 0.6779 0.4069 1.2395 0.0582  -0.2628 -0.0452 254 GLU B CD  
5054 O OE1 . GLU B 245 ? 0.6260 0.3570 1.1895 0.0658  -0.2657 -0.0454 254 GLU B OE1 
5055 O OE2 . GLU B 245 ? 0.7913 0.5001 1.3917 0.0538  -0.2800 -0.0407 254 GLU B OE2 
5056 N N   . ASP B 246 ? 0.5437 0.3314 0.9835 0.0124  -0.1892 0.0313  255 ASP B N   
5057 C CA  . ASP B 246 ? 0.5198 0.3170 0.9526 0.0006  -0.1800 0.0664  255 ASP B CA  
5058 C C   . ASP B 246 ? 0.4878 0.3067 0.8733 -0.0015 -0.1577 0.0640  255 ASP B C   
5059 O O   . ASP B 246 ? 0.4600 0.2828 0.8255 0.0031  -0.1511 0.0368  255 ASP B O   
5060 C CB  . ASP B 246 ? 0.5208 0.3052 0.9912 -0.0084 -0.1914 0.0787  255 ASP B CB  
5061 C CG  . ASP B 246 ? 0.5883 0.3509 1.1110 -0.0091 -0.2143 0.0916  255 ASP B CG  
5062 O OD1 . ASP B 246 ? 0.5592 0.3208 1.0861 -0.0054 -0.2183 0.1048  255 ASP B OD1 
5063 O OD2 . ASP B 246 ? 0.6180 0.3641 1.1796 -0.0130 -0.2296 0.0884  255 ASP B OD2 
5064 N N   . PRO B 247 ? 0.4734 0.3077 0.8418 -0.0078 -0.1466 0.0930  256 PRO B N   
5065 C CA  . PRO B 247 ? 0.4566 0.3104 0.7823 -0.0087 -0.1270 0.0894  256 PRO B CA  
5066 C C   . PRO B 247 ? 0.4282 0.2821 0.7532 -0.0141 -0.1226 0.0821  256 PRO B C   
5067 O O   . PRO B 247 ? 0.4129 0.2578 0.7692 -0.0205 -0.1319 0.0936  256 PRO B O   
5068 C CB  . PRO B 247 ? 0.4626 0.3331 0.7759 -0.0124 -0.1195 0.1222  256 PRO B CB  
5069 C CG  . PRO B 247 ? 0.4882 0.3488 0.8431 -0.0183 -0.1331 0.1492  256 PRO B CG  
5070 C CD  . PRO B 247 ? 0.4910 0.3275 0.8780 -0.0133 -0.1513 0.1301  256 PRO B CD  
5071 N N   . LYS B 248 ? 0.4043 0.2679 0.6964 -0.0114 -0.1097 0.0631  257 LYS B N   
5072 C CA  . LYS B 248 ? 0.4102 0.2751 0.6974 -0.0148 -0.1052 0.0533  257 LYS B CA  
5073 C C   . LYS B 248 ? 0.4211 0.3049 0.6750 -0.0180 -0.0877 0.0640  257 LYS B C   
5074 O O   . LYS B 248 ? 0.3927 0.2871 0.6185 -0.0140 -0.0781 0.0616  257 LYS B O   
5075 C CB  . LYS B 248 ? 0.4080 0.2680 0.6868 -0.0074 -0.1065 0.0197  257 LYS B CB  
5076 C CG  . LYS B 248 ? 0.4426 0.2861 0.7522 -0.0011 -0.1241 0.0031  257 LYS B CG  
5077 C CD  . LYS B 248 ? 0.4624 0.2916 0.8080 -0.0047 -0.1394 0.0022  257 LYS B CD  
5078 C CE  . LYS B 248 ? 0.5219 0.3325 0.9067 -0.0003 -0.1597 -0.0031 257 LYS B CE  
5079 N NZ  . LYS B 248 ? 0.5668 0.3624 0.9866 -0.0008 -0.1770 -0.0153 257 LYS B NZ  
5080 N N   . GLU B 249 ? 0.4140 0.3023 0.6740 -0.0246 -0.0849 0.0752  258 GLU B N   
5081 C CA  . GLU B 249 ? 0.4188 0.3256 0.6511 -0.0268 -0.0695 0.0847  258 GLU B CA  
5082 C C   . GLU B 249 ? 0.3985 0.3059 0.6109 -0.0247 -0.0629 0.0617  258 GLU B C   
5083 O O   . GLU B 249 ? 0.3667 0.2646 0.5948 -0.0258 -0.0701 0.0498  258 GLU B O   
5084 C CB  . GLU B 249 ? 0.4379 0.3531 0.6897 -0.0350 -0.0692 0.1117  258 GLU B CB  
5085 C CG  . GLU B 249 ? 0.4780 0.4026 0.7395 -0.0370 -0.0699 0.1419  258 GLU B CG  
5086 C CD  . GLU B 249 ? 0.5204 0.4623 0.7935 -0.0443 -0.0644 0.1703  258 GLU B CD  
5087 O OE1 . GLU B 249 ? 0.5919 0.5253 0.9003 -0.0516 -0.0734 0.1775  258 GLU B OE1 
5088 O OE2 . GLU B 249 ? 0.5747 0.5400 0.8229 -0.0421 -0.0516 0.1846  258 GLU B OE2 
5089 N N   . PHE B 250 ? 0.3964 0.3149 0.5753 -0.0211 -0.0503 0.0554  259 PHE B N   
5090 C CA  . PHE B 250 ? 0.3716 0.2926 0.5303 -0.0196 -0.0428 0.0383  259 PHE B CA  
5091 C C   . PHE B 250 ? 0.3573 0.2940 0.4910 -0.0198 -0.0299 0.0471  259 PHE B C   
5092 O O   . PHE B 250 ? 0.3431 0.2885 0.4647 -0.0176 -0.0257 0.0561  259 PHE B O   
5093 C CB  . PHE B 250 ? 0.3793 0.2953 0.5259 -0.0134 -0.0425 0.0156  259 PHE B CB  
5094 C CG  . PHE B 250 ? 0.3587 0.2620 0.5281 -0.0106 -0.0551 0.0022  259 PHE B CG  
5095 C CD1 . PHE B 250 ? 0.4033 0.3001 0.5870 -0.0111 -0.0623 -0.0075 259 PHE B CD1 
5096 C CD2 . PHE B 250 ? 0.3466 0.2450 0.5238 -0.0062 -0.0610 -0.0024 259 PHE B CD2 
5097 C CE1 . PHE B 250 ? 0.4201 0.3059 0.6254 -0.0066 -0.0756 -0.0232 259 PHE B CE1 
5098 C CE2 . PHE B 250 ? 0.3985 0.2858 0.5980 -0.0018 -0.0736 -0.0172 259 PHE B CE2 
5099 C CZ  . PHE B 250 ? 0.4628 0.3437 0.6762 -0.0015 -0.0812 -0.0283 259 PHE B CZ  
5100 N N   . ALA B 251 ? 0.3570 0.2977 0.4835 -0.0213 -0.0247 0.0435  260 ALA B N   
5101 C CA  . ALA B 251 ? 0.3772 0.3326 0.4825 -0.0204 -0.0136 0.0502  260 ALA B CA  
5102 C C   . ALA B 251 ? 0.3544 0.3110 0.4337 -0.0154 -0.0070 0.0362  260 ALA B C   
5103 O O   . ALA B 251 ? 0.3429 0.2909 0.4187 -0.0137 -0.0083 0.0200  260 ALA B O   
5104 C CB  . ALA B 251 ? 0.3847 0.3437 0.4933 -0.0233 -0.0112 0.0505  260 ALA B CB  
5105 N N   . GLY B 252 ? 0.3491 0.3184 0.4118 -0.0125 -0.0002 0.0428  261 GLY B N   
5106 C CA  . GLY B 252 ? 0.3558 0.3266 0.3971 -0.0081 0.0049  0.0304  261 GLY B CA  
5107 C C   . GLY B 252 ? 0.3528 0.3221 0.3858 -0.0083 0.0096  0.0214  261 GLY B C   
5108 O O   . GLY B 252 ? 0.3445 0.3140 0.3858 -0.0111 0.0094  0.0250  261 GLY B O   
5109 N N   . GLY B 253 ? 0.3404 0.3080 0.3591 -0.0055 0.0130  0.0103  262 GLY B N   
5110 C CA  . GLY B 253 ? 0.3418 0.3067 0.3533 -0.0055 0.0167  0.0026  262 GLY B CA  
5111 C C   . GLY B 253 ? 0.3219 0.2958 0.3299 -0.0044 0.0205  0.0092  262 GLY B C   
5112 O O   . GLY B 253 ? 0.3173 0.3032 0.3220 -0.0017 0.0224  0.0174  262 GLY B O   
5113 N N   . SER B 254 ? 0.3443 0.3147 0.3532 -0.0057 0.0214  0.0056  263 SER B N   
5114 C CA  . SER B 254 ? 0.3317 0.3105 0.3388 -0.0043 0.0247  0.0101  263 SER B CA  
5115 C C   . SER B 254 ? 0.3378 0.3094 0.3398 -0.0040 0.0255  0.0017  263 SER B C   
5116 O O   . SER B 254 ? 0.3144 0.2779 0.3194 -0.0063 0.0228  -0.0036 263 SER B O   
5117 C CB  . SER B 254 ? 0.3349 0.3193 0.3581 -0.0081 0.0224  0.0210  263 SER B CB  
5118 O OG  . SER B 254 ? 0.3587 0.3514 0.3826 -0.0071 0.0253  0.0239  263 SER B OG  
5119 N N   . ALA B 255 ? 0.3111 0.2869 0.3056 -0.0003 0.0287  0.0005  264 ALA B N   
5120 C CA  . ALA B 255 ? 0.3168 0.2870 0.3086 0.0000  0.0288  -0.0041 264 ALA B CA  
5121 C C   . ALA B 255 ? 0.2924 0.2664 0.2938 -0.0022 0.0266  0.0000  264 ALA B C   
5122 O O   . ALA B 255 ? 0.2830 0.2539 0.2824 -0.0016 0.0256  -0.0032 264 ALA B O   
5123 C CB  . ALA B 255 ? 0.3165 0.2877 0.3004 0.0051  0.0311  -0.0074 264 ALA B CB  
5124 N N   . GLY B 256 ? 0.2926 0.2736 0.3060 -0.0049 0.0251  0.0077  265 GLY B N   
5125 C CA  . GLY B 256 ? 0.2842 0.2649 0.3125 -0.0087 0.0197  0.0096  265 GLY B CA  
5126 C C   . GLY B 256 ? 0.2871 0.2566 0.3162 -0.0100 0.0143  0.0003  265 GLY B C   
5127 O O   . GLY B 256 ? 0.2763 0.2444 0.3135 -0.0108 0.0085  -0.0035 265 GLY B O   
5128 N N   . GLN B 257 ? 0.2740 0.2375 0.2951 -0.0092 0.0157  -0.0044 266 GLN B N   
5129 C CA  . GLN B 257 ? 0.2912 0.2482 0.3102 -0.0085 0.0125  -0.0141 266 GLN B CA  
5130 C C   . GLN B 257 ? 0.3019 0.2584 0.3067 -0.0057 0.0158  -0.0191 266 GLN B C   
5131 O O   . GLN B 257 ? 0.3201 0.2760 0.3213 -0.0040 0.0144  -0.0260 266 GLN B O   
5132 C CB  . GLN B 257 ? 0.2791 0.2324 0.2978 -0.0088 0.0128  -0.0161 266 GLN B CB  
5133 C CG  . GLN B 257 ? 0.3035 0.2572 0.3361 -0.0113 0.0092  -0.0089 266 GLN B CG  
5134 C CD  . GLN B 257 ? 0.3219 0.2733 0.3525 -0.0106 0.0098  -0.0097 266 GLN B CD  
5135 O OE1 . GLN B 257 ? 0.3423 0.2935 0.3610 -0.0088 0.0142  -0.0139 266 GLN B OE1 
5136 N NE2 . GLN B 257 ? 0.2744 0.2240 0.3192 -0.0123 0.0044  -0.0048 266 GLN B NE2 
5137 N N   . SER B 258 ? 0.3113 0.2697 0.3090 -0.0044 0.0199  -0.0152 267 SER B N   
5138 C CA  . SER B 258 ? 0.3114 0.2688 0.2988 -0.0021 0.0221  -0.0169 267 SER B CA  
5139 C C   . SER B 258 ? 0.3219 0.2827 0.3108 -0.0006 0.0175  -0.0191 267 SER B C   
5140 O O   . SER B 258 ? 0.3171 0.2813 0.3146 -0.0012 0.0145  -0.0166 267 SER B O   
5141 C CB  . SER B 258 ? 0.3342 0.2909 0.3171 -0.0003 0.0256  -0.0130 267 SER B CB  
5142 O OG  . SER B 258 ? 0.3473 0.3025 0.3240 0.0017  0.0261  -0.0123 267 SER B OG  
5143 N N   . SER B 259 ? 0.3425 0.3048 0.3238 0.0017  0.0169  -0.0235 268 SER B N   
5144 C CA  . SER B 259 ? 0.3603 0.3277 0.3403 0.0048  0.0115  -0.0273 268 SER B CA  
5145 C C   . SER B 259 ? 0.3829 0.3522 0.3574 0.0070  0.0123  -0.0218 268 SER B C   
5146 O O   . SER B 259 ? 0.3811 0.3549 0.3583 0.0091  0.0064  -0.0244 268 SER B O   
5147 C CB  . SER B 259 ? 0.3515 0.3245 0.3230 0.0088  0.0105  -0.0345 268 SER B CB  
5148 O OG  . SER B 259 ? 0.3407 0.3123 0.3203 0.0082  0.0076  -0.0419 268 SER B OG  
5149 N N   A VAL B 260 ? 0.3916 0.3570 0.3605 0.0068  0.0180  -0.0153 269 VAL B N   
5150 N N   B VAL B 260 ? 0.3934 0.3588 0.3626 0.0068  0.0179  -0.0153 269 VAL B N   
5151 C CA  A VAL B 260 ? 0.3933 0.3591 0.3586 0.0097  0.0178  -0.0100 269 VAL B CA  
5152 C CA  B VAL B 260 ? 0.3916 0.3576 0.3568 0.0097  0.0177  -0.0102 269 VAL B CA  
5153 C C   A VAL B 260 ? 0.3854 0.3540 0.3604 0.0103  0.0148  -0.0095 269 VAL B C   
5154 C C   B VAL B 260 ? 0.3854 0.3538 0.3601 0.0103  0.0150  -0.0093 269 VAL B C   
5155 O O   A VAL B 260 ? 0.4023 0.3756 0.3781 0.0130  0.0104  -0.0094 269 VAL B O   
5156 O O   B VAL B 260 ? 0.4060 0.3789 0.3813 0.0131  0.0108  -0.0089 269 VAL B O   
5157 C CB  A VAL B 260 ? 0.4064 0.3652 0.3682 0.0099  0.0225  -0.0036 269 VAL B CB  
5158 C CB  B VAL B 260 ? 0.4040 0.3635 0.3644 0.0097  0.0226  -0.0038 269 VAL B CB  
5159 C CG1 A VAL B 260 ? 0.4430 0.4030 0.3971 0.0098  0.0252  0.0004  269 VAL B CG1 
5160 C CG1 B VAL B 260 ? 0.3829 0.3361 0.3496 0.0084  0.0249  -0.0040 269 VAL B CG1 
5161 C CG2 A VAL B 260 ? 0.3972 0.3503 0.3644 0.0076  0.0253  -0.0048 269 VAL B CG2 
5162 C CG2 B VAL B 260 ? 0.4272 0.3871 0.3836 0.0134  0.0209  0.0025  269 VAL B CG2 
5163 N N   . PHE B 261 ? 0.3822 0.3502 0.3647 0.0081  0.0172  -0.0086 270 PHE B N   
5164 C CA  . PHE B 261 ? 0.3796 0.3547 0.3725 0.0088  0.0163  -0.0061 270 PHE B CA  
5165 C C   . PHE B 261 ? 0.3728 0.3543 0.3784 0.0063  0.0104  -0.0072 270 PHE B C   
5166 O O   . PHE B 261 ? 0.3756 0.3644 0.3897 0.0076  0.0072  -0.0056 270 PHE B O   
5167 C CB  . PHE B 261 ? 0.4197 0.3965 0.4149 0.0088  0.0213  -0.0039 270 PHE B CB  
5168 C CG  . PHE B 261 ? 0.4713 0.4405 0.4575 0.0117  0.0243  -0.0053 270 PHE B CG  
5169 C CD1 . PHE B 261 ? 0.5096 0.4765 0.4938 0.0165  0.0234  -0.0048 270 PHE B CD1 
5170 C CD2 . PHE B 261 ? 0.4775 0.4408 0.4597 0.0098  0.0266  -0.0072 270 PHE B CD2 
5171 C CE1 . PHE B 261 ? 0.5130 0.4707 0.4935 0.0188  0.0241  -0.0061 270 PHE B CE1 
5172 C CE2 . PHE B 261 ? 0.4717 0.4270 0.4498 0.0119  0.0275  -0.0090 270 PHE B CE2 
5173 C CZ  . PHE B 261 ? 0.4707 0.4225 0.4490 0.0161  0.0260  -0.0083 270 PHE B CZ  
5174 N N   . GLN B 262 ? 0.3421 0.3208 0.3512 0.0030  0.0077  -0.0108 271 GLN B N   
5175 C CA  . GLN B 262 ? 0.3416 0.3233 0.3650 0.0010  -0.0007 -0.0145 271 GLN B CA  
5176 C C   . GLN B 262 ? 0.3417 0.3261 0.3601 0.0053  -0.0073 -0.0205 271 GLN B C   
5177 O O   . GLN B 262 ? 0.3479 0.3379 0.3806 0.0048  -0.0145 -0.0218 271 GLN B O   
5178 C CB  . GLN B 262 ? 0.3456 0.3218 0.3737 -0.0016 -0.0038 -0.0194 271 GLN B CB  
5179 C CG  . GLN B 262 ? 0.3338 0.3095 0.3718 -0.0061 0.0000  -0.0118 271 GLN B CG  
5180 C CD  . GLN B 262 ? 0.2978 0.2723 0.3583 -0.0106 -0.0081 -0.0115 271 GLN B CD  
5181 O OE1 . GLN B 262 ? 0.2693 0.2452 0.3442 -0.0112 -0.0172 -0.0157 271 GLN B OE1 
5182 N NE2 . GLN B 262 ? 0.2636 0.2354 0.3293 -0.0135 -0.0060 -0.0065 271 GLN B NE2 
5183 N N   A CYS B 263 ? 0.3502 0.3325 0.3498 0.0094  -0.0050 -0.0231 272 CYS B N   
5184 N N   B CYS B 263 ? 0.3432 0.3255 0.3428 0.0094  -0.0050 -0.0231 272 CYS B N   
5185 C CA  A CYS B 263 ? 0.3711 0.3589 0.3625 0.0149  -0.0110 -0.0278 272 CYS B CA  
5186 C CA  B CYS B 263 ? 0.3591 0.3468 0.3502 0.0149  -0.0107 -0.0276 272 CYS B CA  
5187 C C   A CYS B 263 ? 0.3638 0.3559 0.3572 0.0173  -0.0122 -0.0223 272 CYS B C   
5188 C C   B CYS B 263 ? 0.3565 0.3485 0.3504 0.0172  -0.0122 -0.0223 272 CYS B C   
5189 O O   A CYS B 263 ? 0.3632 0.3617 0.3607 0.0203  -0.0207 -0.0267 272 CYS B O   
5190 O O   B CYS B 263 ? 0.3555 0.3540 0.3543 0.0199  -0.0208 -0.0267 272 CYS B O   
5191 C CB  A CYS B 263 ? 0.3892 0.3778 0.3604 0.0189  -0.0072 -0.0287 272 CYS B CB  
5192 C CB  B CYS B 263 ? 0.3697 0.3577 0.3404 0.0188  -0.0063 -0.0275 272 CYS B CB  
5193 S SG  A CYS B 263 ? 0.4557 0.4413 0.4133 0.0206  0.0012  -0.0165 272 CYS B SG  
5194 S SG  B CYS B 263 ? 0.3812 0.3729 0.3477 0.0212  -0.0100 -0.0397 272 CYS B SG  
5195 N N   . PHE B 264 ? 0.3489 0.3379 0.3407 0.0169  -0.0050 -0.0144 273 PHE B N   
5196 C CA  . PHE B 264 ? 0.3716 0.3651 0.3679 0.0202  -0.0064 -0.0100 273 PHE B CA  
5197 C C   . PHE B 264 ? 0.3399 0.3419 0.3571 0.0177  -0.0097 -0.0097 273 PHE B C   
5198 O O   . PHE B 264 ? 0.3550 0.3644 0.3793 0.0205  -0.0150 -0.0095 273 PHE B O   
5199 C CB  . PHE B 264 ? 0.3800 0.3675 0.3693 0.0224  0.0005  -0.0040 273 PHE B CB  
5200 C CG  . PHE B 264 ? 0.3816 0.3631 0.3552 0.0250  0.0017  -0.0010 273 PHE B CG  
5201 C CD1 . PHE B 264 ? 0.4196 0.4059 0.3860 0.0296  -0.0037 0.0006  273 PHE B CD1 
5202 C CD2 . PHE B 264 ? 0.4151 0.3884 0.3824 0.0227  0.0077  0.0014  273 PHE B CD2 
5203 C CE1 . PHE B 264 ? 0.4708 0.4551 0.4232 0.0319  -0.0020 0.0067  273 PHE B CE1 
5204 C CE2 . PHE B 264 ? 0.4434 0.4138 0.3997 0.0240  0.0091  0.0070  273 PHE B CE2 
5205 C CZ  . PHE B 264 ? 0.4737 0.4503 0.4223 0.0286  0.0048  0.0108  273 PHE B CZ  
5206 N N   . ASP B 265 ? 0.3359 0.3385 0.3646 0.0122  -0.0072 -0.0084 274 ASP B N   
5207 C CA  . ASP B 265 ? 0.3546 0.3672 0.4073 0.0083  -0.0112 -0.0057 274 ASP B CA  
5208 C C   . ASP B 265 ? 0.3461 0.3606 0.4095 0.0078  -0.0235 -0.0130 274 ASP B C   
5209 O O   . ASP B 265 ? 0.3646 0.3886 0.4445 0.0078  -0.0291 -0.0119 274 ASP B O   
5210 C CB  . ASP B 265 ? 0.3752 0.3881 0.4388 0.0023  -0.0071 -0.0007 274 ASP B CB  
5211 C CG  . ASP B 265 ? 0.4205 0.4385 0.4791 0.0039  0.0035  0.0066  274 ASP B CG  
5212 O OD1 . ASP B 265 ? 0.4905 0.5150 0.5461 0.0091  0.0065  0.0081  274 ASP B OD1 
5213 O OD2 . ASP B 265 ? 0.5059 0.5221 0.5638 0.0011  0.0079  0.0098  274 ASP B OD2 
5214 N N   . VAL B 266 ? 0.3523 0.3594 0.4072 0.0083  -0.0281 -0.0218 275 VAL B N   
5215 C CA  . VAL B 266 ? 0.3556 0.3648 0.4178 0.0102  -0.0415 -0.0328 275 VAL B CA  
5216 C C   . VAL B 266 ? 0.3616 0.3774 0.4131 0.0173  -0.0460 -0.0352 275 VAL B C   
5217 O O   . VAL B 266 ? 0.3660 0.3891 0.4339 0.0178  -0.0561 -0.0386 275 VAL B O   
5218 C CB  . VAL B 266 ? 0.3630 0.3656 0.4143 0.0122  -0.0449 -0.0437 275 VAL B CB  
5219 C CG1 . VAL B 266 ? 0.3908 0.3981 0.4445 0.0179  -0.0597 -0.0585 275 VAL B CG1 
5220 C CG2 . VAL B 266 ? 0.3060 0.3019 0.3739 0.0054  -0.0443 -0.0422 275 VAL B CG2 
5221 N N   . LEU B 267 ? 0.3684 0.3819 0.3947 0.0224  -0.0392 -0.0322 276 LEU B N   
5222 C CA  . LEU B 267 ? 0.3908 0.4103 0.4048 0.0298  -0.0433 -0.0320 276 LEU B CA  
5223 C C   . LEU B 267 ? 0.3697 0.3962 0.4007 0.0298  -0.0460 -0.0271 276 LEU B C   
5224 O O   . LEU B 267 ? 0.4142 0.4488 0.4500 0.0340  -0.0562 -0.0316 276 LEU B O   
5225 C CB  . LEU B 267 ? 0.3865 0.4012 0.3767 0.0334  -0.0340 -0.0244 276 LEU B CB  
5226 C CG  . LEU B 267 ? 0.4363 0.4565 0.4117 0.0412  -0.0376 -0.0207 276 LEU B CG  
5227 C CD1 . LEU B 267 ? 0.5031 0.5320 0.4644 0.0473  -0.0454 -0.0295 276 LEU B CD1 
5228 C CD2 . LEU B 267 ? 0.4715 0.4841 0.4334 0.0421  -0.0278 -0.0091 276 LEU B CD2 
5229 N N   . LEU B 268 ? 0.3544 0.3803 0.3952 0.0261  -0.0372 -0.0187 277 LEU B N   
5230 C CA  . LEU B 268 ? 0.3699 0.4057 0.4271 0.0272  -0.0378 -0.0136 277 LEU B CA  
5231 C C   . LEU B 268 ? 0.3744 0.4206 0.4624 0.0212  -0.0437 -0.0139 277 LEU B C   
5232 O O   . LEU B 268 ? 0.3709 0.4290 0.4762 0.0213  -0.0429 -0.0084 277 LEU B O   
5233 C CB  . LEU B 268 ? 0.3481 0.3820 0.4008 0.0284  -0.0259 -0.0057 277 LEU B CB  
5234 C CG  . LEU B 268 ? 0.3745 0.3969 0.4033 0.0334  -0.0214 -0.0039 277 LEU B CG  
5235 C CD1 . LEU B 268 ? 0.3809 0.3985 0.4073 0.0336  -0.0114 0.0001  277 LEU B CD1 
5236 C CD2 . LEU B 268 ? 0.4177 0.4426 0.4414 0.0408  -0.0275 -0.0024 277 LEU B CD2 
5237 N N   . GLY B 269 ? 0.3772 0.4196 0.4746 0.0161  -0.0501 -0.0199 278 GLY B N   
5238 C CA  . GLY B 269 ? 0.3853 0.4356 0.5168 0.0093  -0.0581 -0.0193 278 GLY B CA  
5239 C C   . GLY B 269 ? 0.3598 0.4181 0.5103 0.0027  -0.0481 -0.0057 278 GLY B C   
5240 O O   . GLY B 269 ? 0.3698 0.4411 0.5507 -0.0020 -0.0518 0.0003  278 GLY B O   
5241 N N   . ILE B 270 ? 0.3862 0.4389 0.5192 0.0029  -0.0356 -0.0004 279 ILE B N   
5242 C CA  . ILE B 270 ? 0.3999 0.4627 0.5454 -0.0014 -0.0251 0.0124  279 ILE B CA  
5243 C C   . ILE B 270 ? 0.4366 0.4997 0.6084 -0.0110 -0.0296 0.0176  279 ILE B C   
5244 O O   . ILE B 270 ? 0.4760 0.5545 0.6718 -0.0160 -0.0257 0.0309  279 ILE B O   
5245 C CB  . ILE B 270 ? 0.3859 0.4424 0.5042 0.0030  -0.0126 0.0141  279 ILE B CB  
5246 C CG1 . ILE B 270 ? 0.4357 0.4942 0.5388 0.0120  -0.0098 0.0115  279 ILE B CG1 
5247 C CG2 . ILE B 270 ? 0.3956 0.4638 0.5230 -0.0001 -0.0024 0.0259  279 ILE B CG2 
5248 C CD1 . ILE B 270 ? 0.3799 0.4276 0.4574 0.0171  -0.0017 0.0096  279 ILE B CD1 
5249 N N   . GLN B 271 ? 0.4766 0.5245 0.6459 -0.0129 -0.0386 0.0077  280 GLN B N   
5250 C CA  . GLN B 271 ? 0.4784 0.5227 0.6761 -0.0213 -0.0470 0.0100  280 GLN B CA  
5251 C C   . GLN B 271 ? 0.4501 0.4982 0.6537 -0.0266 -0.0363 0.0255  280 GLN B C   
5252 O O   . GLN B 271 ? 0.4147 0.4754 0.6485 -0.0336 -0.0360 0.0401  280 GLN B O   
5253 C CB  . GLN B 271 ? 0.4945 0.5487 0.7299 -0.0261 -0.0596 0.0114  280 GLN B CB  
5254 C CG  . GLN B 271 ? 0.5576 0.6069 0.7895 -0.0206 -0.0742 -0.0066 280 GLN B CG  
5255 C CD  . GLN B 271 ? 0.5799 0.6400 0.8516 -0.0254 -0.0876 -0.0058 280 GLN B CD  
5256 O OE1 . GLN B 271 ? 0.6959 0.7733 0.9819 -0.0269 -0.0824 0.0057  280 GLN B OE1 
5257 N NE2 . GLN B 271 ? 0.6560 0.7071 0.9475 -0.0272 -0.1057 -0.0190 280 GLN B NE2 
5258 N N   . GLN B 272 ? 0.4513 0.4900 0.6262 -0.0231 -0.0276 0.0230  281 GLN B N   
5259 C CA  . GLN B 272 ? 0.4565 0.4987 0.6307 -0.0261 -0.0178 0.0358  281 GLN B CA  
5260 C C   . GLN B 272 ? 0.4656 0.5005 0.6639 -0.0339 -0.0254 0.0406  281 GLN B C   
5261 O O   . GLN B 272 ? 0.4786 0.5215 0.6866 -0.0380 -0.0191 0.0562  281 GLN B O   
5262 C CB  . GLN B 272 ? 0.4604 0.4931 0.5995 -0.0201 -0.0089 0.0296  281 GLN B CB  
5263 C CG  . GLN B 272 ? 0.4678 0.5066 0.5858 -0.0124 -0.0010 0.0273  281 GLN B CG  
5264 C CD  . GLN B 272 ? 0.4515 0.5098 0.5729 -0.0106 0.0094  0.0397  281 GLN B CD  
5265 O OE1 . GLN B 272 ? 0.4377 0.5096 0.5795 -0.0156 0.0114  0.0530  281 GLN B OE1 
5266 N NE2 . GLN B 272 ? 0.4309 0.4920 0.5329 -0.0025 0.0159  0.0354  281 GLN B NE2 
5267 N N   . THR B 273 ? 0.4640 0.4847 0.6715 -0.0348 -0.0394 0.0269  282 THR B N   
5268 C CA  . THR B 273 ? 0.4545 0.4644 0.6861 -0.0408 -0.0495 0.0276  282 THR B CA  
5269 C C   . THR B 273 ? 0.4413 0.4546 0.7171 -0.0482 -0.0635 0.0318  282 THR B C   
5270 O O   . THR B 273 ? 0.4323 0.4339 0.7335 -0.0527 -0.0761 0.0294  282 THR B O   
5271 C CB  . THR B 273 ? 0.4632 0.4548 0.6767 -0.0352 -0.0568 0.0068  282 THR B CB  
5272 O OG1 . THR B 273 ? 0.4770 0.4668 0.6881 -0.0302 -0.0674 -0.0105 282 THR B OG1 
5273 C CG2 . THR B 273 ? 0.4370 0.4257 0.6116 -0.0292 -0.0433 0.0042  282 THR B CG2 
5274 N N   . ALA B 274 ? 0.4339 0.4632 0.7219 -0.0494 -0.0623 0.0382  283 ALA B N   
5275 C CA  . ALA B 274 ? 0.4457 0.4813 0.7798 -0.0572 -0.0755 0.0440  283 ALA B CA  
5276 C C   . ALA B 274 ? 0.4429 0.4939 0.8090 -0.0672 -0.0690 0.0723  283 ALA B C   
5277 O O   . ALA B 274 ? 0.4426 0.5047 0.7905 -0.0660 -0.0526 0.0870  283 ALA B O   
5278 C CB  . ALA B 274 ? 0.4431 0.4909 0.7773 -0.0535 -0.0779 0.0376  283 ALA B CB  
5279 N N   . GLY B 275 ? 0.4428 0.4961 0.8579 -0.0767 -0.0826 0.0802  284 GLY B N   
5280 C CA  . GLY B 275 ? 0.4476 0.5199 0.9007 -0.0874 -0.0775 0.1106  284 GLY B CA  
5281 C C   . GLY B 275 ? 0.4296 0.4948 0.8921 -0.0929 -0.0755 0.1268  284 GLY B C   
5282 O O   . GLY B 275 ? 0.4183 0.4615 0.8602 -0.0887 -0.0794 0.1126  284 GLY B O   
5283 N N   . GLY B 276 ? 0.4172 0.5037 0.9108 -0.1019 -0.0686 0.1580  285 GLY B N   
5284 C CA  . GLY B 276 ? 0.4394 0.5223 0.9518 -0.1089 -0.0686 0.1792  285 GLY B CA  
5285 C C   . GLY B 276 ? 0.4509 0.5535 0.9322 -0.1048 -0.0471 0.1988  285 GLY B C   
5286 O O   . GLY B 276 ? 0.4358 0.5543 0.9423 -0.1122 -0.0423 0.2291  285 GLY B O   
5287 N N   . GLY B 277 ? 0.4453 0.5472 0.8733 -0.0926 -0.0352 0.1816  286 GLY B N   
5288 C CA  . GLY B 277 ? 0.4309 0.5505 0.8243 -0.0860 -0.0162 0.1939  286 GLY B CA  
5289 C C   . GLY B 277 ? 0.4245 0.5218 0.7823 -0.0796 -0.0157 0.1793  286 GLY B C   
5290 O O   . GLY B 277 ? 0.4240 0.4934 0.7742 -0.0777 -0.0272 0.1556  286 GLY B O   
5291 N N   . HIS B 278 ? 0.4145 0.5268 0.7498 -0.0753 -0.0023 0.1930  287 HIS B N   
5292 C CA  . HIS B 278 ? 0.4045 0.4988 0.7099 -0.0698 -0.0017 0.1827  287 HIS B CA  
5293 C C   . HIS B 278 ? 0.3523 0.4337 0.6140 -0.0592 0.0020  0.1539  287 HIS B C   
5294 O O   . HIS B 278 ? 0.3075 0.3656 0.5543 -0.0568 -0.0038 0.1377  287 HIS B O   
5295 C CB  . HIS B 278 ? 0.4388 0.5553 0.7346 -0.0678 0.0102  0.2065  287 HIS B CB  
5296 C CG  . HIS B 278 ? 0.5092 0.6374 0.8477 -0.0785 0.0065  0.2383  287 HIS B CG  
5297 N ND1 . HIS B 278 ? 0.6047 0.7082 0.9761 -0.0872 -0.0095 0.2412  287 HIS B ND1 
5298 C CD2 . HIS B 278 ? 0.6058 0.7689 0.9615 -0.0816 0.0165  0.2699  287 HIS B CD2 
5299 C CE1 . HIS B 278 ? 0.6146 0.7350 1.0237 -0.0963 -0.0100 0.2744  287 HIS B CE1 
5300 N NE2 . HIS B 278 ? 0.6142 0.7724 1.0141 -0.0934 0.0065  0.2934  287 HIS B NE2 
5301 N N   . ALA B 279 ? 0.3232 0.4203 0.5666 -0.0529 0.0113  0.1485  288 ALA B N   
5302 C CA  . ALA B 279 ? 0.3294 0.4141 0.5354 -0.0436 0.0142  0.1239  288 ALA B CA  
5303 C C   . ALA B 279 ? 0.3023 0.3607 0.5115 -0.0451 0.0012  0.1029  288 ALA B C   
5304 O O   . ALA B 279 ? 0.3051 0.3457 0.4905 -0.0406 -0.0002 0.0862  288 ALA B O   
5305 C CB  . ALA B 279 ? 0.3284 0.4340 0.5205 -0.0365 0.0242  0.1225  288 ALA B CB  
5306 N N   . ALA B 280 ? 0.3148 0.3731 0.5547 -0.0511 -0.0084 0.1042  289 ALA B N   
5307 C CA  . ALA B 280 ? 0.3180 0.3549 0.5651 -0.0519 -0.0229 0.0844  289 ALA B CA  
5308 C C   . ALA B 280 ? 0.3185 0.3338 0.5688 -0.0533 -0.0321 0.0766  289 ALA B C   
5309 O O   . ALA B 280 ? 0.3089 0.3081 0.5404 -0.0480 -0.0370 0.0557  289 ALA B O   
5310 C CB  . ALA B 280 ? 0.3486 0.3916 0.6354 -0.0589 -0.0336 0.0897  289 ALA B CB  
5311 N N   . GLN B 281 ? 0.2886 0.3055 0.5633 -0.0599 -0.0343 0.0946  290 GLN B N   
5312 C CA  . GLN B 281 ? 0.3248 0.3219 0.6071 -0.0611 -0.0439 0.0890  290 GLN B CA  
5313 C C   . GLN B 281 ? 0.3119 0.3025 0.5544 -0.0533 -0.0353 0.0783  290 GLN B C   
5314 O O   . GLN B 281 ? 0.3131 0.2862 0.5467 -0.0495 -0.0422 0.0598  290 GLN B O   
5315 C CB  . GLN B 281 ? 0.3346 0.3371 0.6508 -0.0697 -0.0465 0.1152  290 GLN B CB  
5316 C CG  . GLN B 281 ? 0.4847 0.4651 0.8297 -0.0734 -0.0637 0.1099  290 GLN B CG  
5317 C CD  . GLN B 281 ? 0.4418 0.4108 0.8200 -0.0769 -0.0817 0.0964  290 GLN B CD  
5318 O OE1 . GLN B 281 ? 0.5404 0.5213 0.9319 -0.0800 -0.0821 0.0996  290 GLN B OE1 
5319 N NE2 . GLN B 281 ? 0.5433 0.4900 0.9358 -0.0754 -0.0977 0.0799  290 GLN B NE2 
5320 N N   . PHE B 282 ? 0.3045 0.3108 0.5241 -0.0502 -0.0205 0.0892  291 PHE B N   
5321 C CA  . PHE B 282 ? 0.3083 0.3103 0.4934 -0.0433 -0.0128 0.0805  291 PHE B CA  
5322 C C   . PHE B 282 ? 0.2832 0.2747 0.4430 -0.0371 -0.0125 0.0572  291 PHE B C   
5323 O O   . PHE B 282 ? 0.2566 0.2350 0.4024 -0.0337 -0.0145 0.0442  291 PHE B O   
5324 C CB  . PHE B 282 ? 0.3180 0.3410 0.4849 -0.0398 0.0013  0.0943  291 PHE B CB  
5325 C CG  . PHE B 282 ? 0.3498 0.3680 0.4838 -0.0326 0.0075  0.0835  291 PHE B CG  
5326 C CD1 . PHE B 282 ? 0.3555 0.3660 0.4876 -0.0326 0.0051  0.0856  291 PHE B CD1 
5327 C CD2 . PHE B 282 ? 0.3869 0.4070 0.4947 -0.0260 0.0142  0.0707  291 PHE B CD2 
5328 C CE1 . PHE B 282 ? 0.3720 0.3785 0.4768 -0.0264 0.0097  0.0750  291 PHE B CE1 
5329 C CE2 . PHE B 282 ? 0.3676 0.3822 0.4499 -0.0203 0.0183  0.0608  291 PHE B CE2 
5330 C CZ  . PHE B 282 ? 0.3913 0.3998 0.4724 -0.0207 0.0161  0.0628  291 PHE B CZ  
5331 N N   . LEU B 283 ? 0.2622 0.2613 0.4169 -0.0353 -0.0099 0.0535  292 LEU B N   
5332 C CA  . LEU B 283 ? 0.2605 0.2512 0.3923 -0.0294 -0.0098 0.0346  292 LEU B CA  
5333 C C   . LEU B 283 ? 0.2721 0.2482 0.4132 -0.0295 -0.0224 0.0192  292 LEU B C   
5334 O O   . LEU B 283 ? 0.3020 0.2701 0.4228 -0.0243 -0.0221 0.0049  292 LEU B O   
5335 C CB  . LEU B 283 ? 0.2413 0.2434 0.3676 -0.0269 -0.0054 0.0349  292 LEU B CB  
5336 C CG  . LEU B 283 ? 0.2756 0.2925 0.3866 -0.0232 0.0072  0.0440  292 LEU B CG  
5337 C CD1 . LEU B 283 ? 0.3105 0.3395 0.4225 -0.0205 0.0097  0.0446  292 LEU B CD1 
5338 C CD2 . LEU B 283 ? 0.2345 0.2438 0.3167 -0.0175 0.0131  0.0351  292 LEU B CD2 
5339 N N   . GLN B 284 ? 0.2780 0.2522 0.4509 -0.0347 -0.0338 0.0220  293 GLN B N   
5340 C CA  . GLN B 284 ? 0.3153 0.2758 0.5008 -0.0334 -0.0483 0.0055  293 GLN B CA  
5341 C C   . GLN B 284 ? 0.3164 0.2658 0.4951 -0.0311 -0.0493 -0.0005 293 GLN B C   
5342 O O   . GLN B 284 ? 0.3365 0.2792 0.5015 -0.0248 -0.0529 -0.0188 293 GLN B O   
5343 C CB  . GLN B 284 ? 0.2993 0.2583 0.5267 -0.0401 -0.0626 0.0103  293 GLN B CB  
5344 C CG  . GLN B 284 ? 0.3818 0.3251 0.6276 -0.0382 -0.0799 -0.0074 293 GLN B CG  
5345 C CD  . GLN B 284 ? 0.4020 0.3428 0.6898 -0.0437 -0.0969 -0.0079 293 GLN B CD  
5346 O OE1 . GLN B 284 ? 0.5145 0.4556 0.8035 -0.0396 -0.1062 -0.0244 293 GLN B OE1 
5347 N NE2 . GLN B 284 ? 0.3793 0.3185 0.7030 -0.0528 -0.1016 0.0110  293 GLN B NE2 
5348 N N   A ASP B 285 ? 0.3190 0.2689 0.5070 -0.0354 -0.0459 0.0154  294 ASP B N   
5349 N N   B ASP B 285 ? 0.3092 0.2592 0.4973 -0.0354 -0.0459 0.0154  294 ASP B N   
5350 C CA  A ASP B 285 ? 0.3200 0.2603 0.5036 -0.0332 -0.0471 0.0114  294 ASP B CA  
5351 C CA  B ASP B 285 ? 0.3173 0.2577 0.5006 -0.0332 -0.0470 0.0115  294 ASP B CA  
5352 C C   A ASP B 285 ? 0.3221 0.2629 0.4698 -0.0263 -0.0371 0.0002  294 ASP B C   
5353 C C   B ASP B 285 ? 0.3192 0.2600 0.4668 -0.0263 -0.0372 -0.0001 294 ASP B C   
5354 O O   A ASP B 285 ? 0.3101 0.2430 0.4525 -0.0220 -0.0408 -0.0134 294 ASP B O   
5355 O O   B ASP B 285 ? 0.3056 0.2386 0.4479 -0.0218 -0.0410 -0.0140 294 ASP B O   
5356 C CB  A ASP B 285 ? 0.3286 0.2729 0.5254 -0.0385 -0.0440 0.0338  294 ASP B CB  
5357 C CB  B ASP B 285 ? 0.3234 0.2681 0.5184 -0.0382 -0.0432 0.0336  294 ASP B CB  
5358 C CG  A ASP B 285 ? 0.3643 0.2974 0.5647 -0.0367 -0.0488 0.0309  294 ASP B CG  
5359 C CG  B ASP B 285 ? 0.3762 0.3195 0.6126 -0.0462 -0.0541 0.0484  294 ASP B CG  
5360 O OD1 A ASP B 285 ? 0.3615 0.2821 0.5680 -0.0329 -0.0589 0.0127  294 ASP B OD1 
5361 O OD1 B ASP B 285 ? 0.3784 0.3143 0.6378 -0.0477 -0.0669 0.0387  294 ASP B OD1 
5362 O OD2 A ASP B 285 ? 0.4321 0.3708 0.6293 -0.0382 -0.0428 0.0469  294 ASP B OD2 
5363 O OD2 B ASP B 285 ? 0.3866 0.3374 0.6337 -0.0507 -0.0502 0.0708  294 ASP B OD2 
5364 N N   . MET B 286 ? 0.3026 0.2531 0.4283 -0.0252 -0.0251 0.0055  295 MET B N   
5365 C CA  . MET B 286 ? 0.3001 0.2508 0.3961 -0.0200 -0.0161 -0.0026 295 MET B CA  
5366 C C   . MET B 286 ? 0.3016 0.2489 0.3852 -0.0148 -0.0185 -0.0201 295 MET B C   
5367 O O   . MET B 286 ? 0.3353 0.2818 0.4013 -0.0112 -0.0134 -0.0269 295 MET B O   
5368 C CB  . MET B 286 ? 0.3035 0.2642 0.3831 -0.0194 -0.0049 0.0065  295 MET B CB  
5369 C CG  . MET B 286 ? 0.3071 0.2756 0.3899 -0.0214 -0.0001 0.0220  295 MET B CG  
5370 S SD  . MET B 286 ? 0.3321 0.2939 0.4124 -0.0205 -0.0012 0.0217  295 MET B SD  
5371 C CE  . MET B 286 ? 0.3829 0.3401 0.4969 -0.0261 -0.0124 0.0318  295 MET B CE  
5372 N N   . ARG B 287 ? 0.3152 0.2626 0.4095 -0.0143 -0.0268 -0.0268 296 ARG B N   
5373 C CA  . ARG B 287 ? 0.3273 0.2744 0.4112 -0.0079 -0.0311 -0.0439 296 ARG B CA  
5374 C C   . ARG B 287 ? 0.3472 0.2892 0.4336 -0.0037 -0.0364 -0.0564 296 ARG B C   
5375 O O   . ARG B 287 ? 0.3479 0.2944 0.4169 0.0027  -0.0338 -0.0675 296 ARG B O   
5376 C CB  . ARG B 287 ? 0.3087 0.2574 0.4069 -0.0074 -0.0419 -0.0501 296 ARG B CB  
5377 C CG  . ARG B 287 ? 0.3355 0.2916 0.4295 -0.0097 -0.0367 -0.0403 296 ARG B CG  
5378 C CD  . ARG B 287 ? 0.3612 0.3200 0.4666 -0.0080 -0.0477 -0.0486 296 ARG B CD  
5379 N NE  . ARG B 287 ? 0.3675 0.3345 0.4709 -0.0098 -0.0429 -0.0390 296 ARG B NE  
5380 C CZ  . ARG B 287 ? 0.3835 0.3554 0.4946 -0.0082 -0.0511 -0.0442 296 ARG B CZ  
5381 N NH1 . ARG B 287 ? 0.3820 0.3515 0.5030 -0.0045 -0.0652 -0.0599 296 ARG B NH1 
5382 N NH2 . ARG B 287 ? 0.3883 0.3684 0.4977 -0.0093 -0.0459 -0.0349 296 ARG B NH2 
5383 N N   A ARG B 288 ? 0.3377 0.2720 0.4469 -0.0070 -0.0437 -0.0532 297 ARG B N   
5384 N N   B ARG B 288 ? 0.3487 0.2830 0.4577 -0.0069 -0.0437 -0.0535 297 ARG B N   
5385 C CA  A ARG B 288 ? 0.3324 0.2610 0.4479 -0.0029 -0.0492 -0.0638 297 ARG B CA  
5386 C CA  B ARG B 288 ? 0.3530 0.2821 0.4673 -0.0023 -0.0493 -0.0651 297 ARG B CA  
5387 C C   A ARG B 288 ? 0.3098 0.2416 0.4049 -0.0010 -0.0377 -0.0619 297 ARG B C   
5388 C C   B ARG B 288 ? 0.3222 0.2533 0.4193 -0.0015 -0.0382 -0.0610 297 ARG B C   
5389 O O   A ARG B 288 ? 0.2839 0.2158 0.3776 0.0045  -0.0397 -0.0736 297 ARG B O   
5390 O O   B ARG B 288 ? 0.3050 0.2342 0.4046 0.0029  -0.0411 -0.0706 297 ARG B O   
5391 C CB  A ARG B 288 ? 0.3206 0.2392 0.4676 -0.0081 -0.0593 -0.0557 297 ARG B CB  
5392 C CB  B ARG B 288 ? 0.3547 0.2731 0.5034 -0.0059 -0.0632 -0.0630 297 ARG B CB  
5393 C CG  A ARG B 288 ? 0.3311 0.2445 0.5076 -0.0110 -0.0738 -0.0575 297 ARG B CG  
5394 C CG  B ARG B 288 ? 0.4116 0.3270 0.5796 -0.0034 -0.0786 -0.0769 297 ARG B CG  
5395 C CD  A ARG B 288 ? 0.3855 0.2977 0.5646 -0.0022 -0.0861 -0.0829 297 ARG B CD  
5396 C CD  B ARG B 288 ? 0.4160 0.3220 0.6231 -0.0111 -0.0914 -0.0667 297 ARG B CD  
5397 N NE  A ARG B 288 ? 0.3777 0.2994 0.5405 0.0006  -0.0838 -0.0890 297 ARG B NE  
5398 N NE  B ARG B 288 ? 0.4226 0.3191 0.6481 -0.0138 -0.0952 -0.0585 297 ARG B NE  
5399 C CZ  A ARG B 288 ? 0.3378 0.2653 0.4891 0.0103  -0.0895 -0.1099 297 ARG B CZ  
5400 C CZ  B ARG B 288 ? 0.4037 0.2998 0.6410 -0.0223 -0.0906 -0.0343 297 ARG B CZ  
5401 N NH1 A ARG B 288 ? 0.1926 0.1190 0.3455 0.0194  -0.0973 -0.1292 297 ARG B NH1 
5402 N NH1 B ARG B 288 ? 0.3332 0.2391 0.5672 -0.0290 -0.0813 -0.0152 297 ARG B NH1 
5403 N NH2 A ARG B 288 ? 0.4124 0.3492 0.5489 0.0121  -0.0871 -0.1114 297 ARG B NH2 
5404 N NH2 B ARG B 288 ? 0.3134 0.2007 0.5664 -0.0229 -0.0958 -0.0289 297 ARG B NH2 
5405 N N   . TYR B 289 ? 0.3179 0.2536 0.3993 -0.0050 -0.0264 -0.0483 298 TYR B N   
5406 C CA  . TYR B 289 ? 0.3133 0.2517 0.3780 -0.0041 -0.0165 -0.0459 298 TYR B CA  
5407 C C   . TYR B 289 ? 0.3304 0.2762 0.3730 -0.0009 -0.0082 -0.0507 298 TYR B C   
5408 O O   . TYR B 289 ? 0.3383 0.2865 0.3692 -0.0009 -0.0003 -0.0482 298 TYR B O   
5409 C CB  . TYR B 289 ? 0.3153 0.2542 0.3795 -0.0090 -0.0111 -0.0299 298 TYR B CB  
5410 C CG  . TYR B 289 ? 0.2783 0.2124 0.3632 -0.0121 -0.0179 -0.0212 298 TYR B CG  
5411 C CD1 . TYR B 289 ? 0.2677 0.1985 0.3753 -0.0156 -0.0267 -0.0163 298 TYR B CD1 
5412 C CD2 . TYR B 289 ? 0.2995 0.2329 0.3832 -0.0120 -0.0161 -0.0162 298 TYR B CD2 
5413 C CE1 . TYR B 289 ? 0.2859 0.2125 0.4158 -0.0192 -0.0334 -0.0048 298 TYR B CE1 
5414 C CE2 . TYR B 289 ? 0.3170 0.2468 0.4196 -0.0145 -0.0226 -0.0058 298 TYR B CE2 
5415 C CZ  . TYR B 289 ? 0.3125 0.2388 0.4386 -0.0184 -0.0309 0.0011  298 TYR B CZ  
5416 O OH  . TYR B 289 ? 0.2790 0.2021 0.4262 -0.0215 -0.0373 0.0147  298 TYR B OH  
5417 N N   . MET B 290 ? 0.3282 0.2777 0.3667 0.0019  -0.0107 -0.0568 299 MET B N   
5418 C CA  . MET B 290 ? 0.3398 0.2977 0.3587 0.0056  -0.0039 -0.0598 299 MET B CA  
5419 C C   . MET B 290 ? 0.3764 0.3418 0.3918 0.0129  -0.0063 -0.0737 299 MET B C   
5420 O O   . MET B 290 ? 0.4038 0.3667 0.4326 0.0162  -0.0165 -0.0845 299 MET B O   
5421 C CB  . MET B 290 ? 0.3421 0.3029 0.3573 0.0062  -0.0061 -0.0588 299 MET B CB  
5422 C CG  . MET B 290 ? 0.3580 0.3152 0.3776 0.0007  -0.0040 -0.0465 299 MET B CG  
5423 S SD  . MET B 290 ? 0.3279 0.2897 0.3471 0.0023  -0.0086 -0.0473 299 MET B SD  
5424 C CE  . MET B 290 ? 0.2574 0.2183 0.2824 -0.0033 -0.0035 -0.0322 299 MET B CE  
5425 N N   . PRO B 291 ? 0.3641 0.3400 0.3631 0.0159  0.0023  -0.0734 300 PRO B N   
5426 C CA  . PRO B 291 ? 0.3775 0.3666 0.3711 0.0247  0.0011  -0.0865 300 PRO B CA  
5427 C C   . PRO B 291 ? 0.3871 0.3807 0.3809 0.0315  -0.0091 -0.0989 300 PRO B C   
5428 O O   . PRO B 291 ? 0.3714 0.3627 0.3620 0.0293  -0.0108 -0.0937 300 PRO B O   
5429 C CB  . PRO B 291 ? 0.3737 0.3757 0.3502 0.0253  0.0132  -0.0782 300 PRO B CB  
5430 C CG  . PRO B 291 ? 0.3822 0.3736 0.3601 0.0165  0.0193  -0.0637 300 PRO B CG  
5431 C CD  . PRO B 291 ? 0.3653 0.3429 0.3524 0.0121  0.0128  -0.0611 300 PRO B CD  
5432 N N   . PRO B 292 ? 0.3692 0.3695 0.3679 0.0404  -0.0169 -0.1164 301 PRO B N   
5433 C CA  . PRO B 292 ? 0.4005 0.4029 0.4042 0.0476  -0.0304 -0.1321 301 PRO B CA  
5434 C C   . PRO B 292 ? 0.4149 0.4306 0.3995 0.0524  -0.0290 -0.1319 301 PRO B C   
5435 O O   . PRO B 292 ? 0.3986 0.4097 0.3902 0.0527  -0.0394 -0.1367 301 PRO B O   
5436 C CB  . PRO B 292 ? 0.4260 0.4377 0.4341 0.0589  -0.0367 -0.1523 301 PRO B CB  
5437 C CG  . PRO B 292 ? 0.4157 0.4370 0.4145 0.0586  -0.0230 -0.1453 301 PRO B CG  
5438 C CD  . PRO B 292 ? 0.3813 0.3881 0.3831 0.0452  -0.0148 -0.1243 301 PRO B CD  
5439 N N   . ALA B 293 ? 0.4264 0.4592 0.3894 0.0559  -0.0166 -0.1252 302 ALA B N   
5440 C CA  . ALA B 293 ? 0.4353 0.4819 0.3786 0.0603  -0.0139 -0.1208 302 ALA B CA  
5441 C C   . ALA B 293 ? 0.3890 0.4217 0.3348 0.0507  -0.0128 -0.1053 302 ALA B C   
5442 O O   . ALA B 293 ? 0.4254 0.4629 0.3641 0.0539  -0.0175 -0.1058 302 ALA B O   
5443 C CB  . ALA B 293 ? 0.4400 0.5079 0.3634 0.0643  0.0002  -0.1118 302 ALA B CB  
5444 N N   . HIS B 294 ? 0.4257 0.4427 0.3818 0.0400  -0.0074 -0.0927 303 HIS B N   
5445 C CA  . HIS B 294 ? 0.4078 0.4133 0.3672 0.0321  -0.0058 -0.0793 303 HIS B CA  
5446 C C   . HIS B 294 ? 0.4199 0.4150 0.3981 0.0294  -0.0178 -0.0848 303 HIS B C   
5447 O O   . HIS B 294 ? 0.4096 0.4039 0.3883 0.0280  -0.0205 -0.0801 303 HIS B O   
5448 C CB  . HIS B 294 ? 0.3844 0.3805 0.3464 0.0237  0.0040  -0.0656 303 HIS B CB  
5449 C CG  . HIS B 294 ? 0.4142 0.4197 0.3631 0.0246  0.0149  -0.0579 303 HIS B CG  
5450 N ND1 . HIS B 294 ? 0.4152 0.4143 0.3678 0.0184  0.0224  -0.0488 303 HIS B ND1 
5451 C CD2 . HIS B 294 ? 0.3896 0.4123 0.3235 0.0309  0.0192  -0.0569 303 HIS B CD2 
5452 C CE1 . HIS B 294 ? 0.4129 0.4232 0.3565 0.0197  0.0305  -0.0422 303 HIS B CE1 
5453 N NE2 . HIS B 294 ? 0.3960 0.4217 0.3277 0.0272  0.0295  -0.0455 303 HIS B NE2 
5454 N N   . ARG B 295 ? 0.4350 0.4230 0.4311 0.0286  -0.0254 -0.0938 304 ARG B N   
5455 C CA  . ARG B 295 ? 0.4479 0.4278 0.4670 0.0270  -0.0395 -0.1007 304 ARG B CA  
5456 C C   . ARG B 295 ? 0.4288 0.4183 0.4436 0.0351  -0.0497 -0.1137 304 ARG B C   
5457 O O   . ARG B 295 ? 0.4487 0.4355 0.4737 0.0320  -0.0561 -0.1109 304 ARG B O   
5458 C CB  . ARG B 295 ? 0.4510 0.4230 0.4907 0.0275  -0.0486 -0.1111 304 ARG B CB  
5459 C CG  . ARG B 295 ? 0.5361 0.5013 0.5785 0.0223  -0.0403 -0.1019 304 ARG B CG  
5460 C CD  . ARG B 295 ? 0.4830 0.4358 0.5534 0.0195  -0.0511 -0.1052 304 ARG B CD  
5461 N NE  . ARG B 295 ? 0.5523 0.5067 0.6302 0.0286  -0.0616 -0.1255 304 ARG B NE  
5462 C CZ  . ARG B 295 ? 0.6171 0.5755 0.6893 0.0338  -0.0578 -0.1324 304 ARG B CZ  
5463 N NH1 . ARG B 295 ? 0.4804 0.4414 0.5391 0.0302  -0.0438 -0.1202 304 ARG B NH1 
5464 N NH2 . ARG B 295 ? 0.5957 0.5566 0.6768 0.0438  -0.0691 -0.1532 304 ARG B NH2 
5465 N N   . ASN B 296 ? 0.4629 0.4658 0.4626 0.0461  -0.0511 -0.1279 305 ASN B N   
5466 C CA  . ASN B 296 ? 0.4900 0.5061 0.4815 0.0569  -0.0616 -0.1433 305 ASN B CA  
5467 C C   . ASN B 296 ? 0.4588 0.4811 0.4359 0.0561  -0.0578 -0.1320 305 ASN B C   
5468 O O   . ASN B 296 ? 0.4676 0.4928 0.4504 0.0596  -0.0698 -0.1402 305 ASN B O   
5469 C CB  . ASN B 296 ? 0.5357 0.5718 0.5059 0.0703  -0.0590 -0.1566 305 ASN B CB  
5470 C CG  . ASN B 296 ? 0.6138 0.6476 0.5991 0.0761  -0.0680 -0.1759 305 ASN B CG  
5471 O OD1 . ASN B 296 ? 0.7134 0.7293 0.7269 0.0707  -0.0792 -0.1806 305 ASN B OD1 
5472 N ND2 . ASN B 296 ? 0.5858 0.6394 0.5535 0.0878  -0.0632 -0.1862 305 ASN B ND2 
5473 N N   . PHE B 297 ? 0.4394 0.4640 0.3999 0.0521  -0.0422 -0.1139 306 PHE B N   
5474 C CA  . PHE B 297 ? 0.4223 0.4514 0.3697 0.0514  -0.0377 -0.1010 306 PHE B CA  
5475 C C   . PHE B 297 ? 0.3998 0.4165 0.3668 0.0435  -0.0435 -0.0953 306 PHE B C   
5476 O O   . PHE B 297 ? 0.3981 0.4203 0.3635 0.0467  -0.0501 -0.0965 306 PHE B O   
5477 C CB  . PHE B 297 ? 0.4102 0.4403 0.3428 0.0475  -0.0214 -0.0828 306 PHE B CB  
5478 C CG  . PHE B 297 ? 0.4038 0.4373 0.3248 0.0475  -0.0175 -0.0691 306 PHE B CG  
5479 C CD1 . PHE B 297 ? 0.4745 0.5259 0.3762 0.0571  -0.0192 -0.0701 306 PHE B CD1 
5480 C CD2 . PHE B 297 ? 0.4177 0.4380 0.3472 0.0391  -0.0130 -0.0557 306 PHE B CD2 
5481 C CE1 . PHE B 297 ? 0.4894 0.5430 0.3821 0.0574  -0.0167 -0.0562 306 PHE B CE1 
5482 C CE2 . PHE B 297 ? 0.3981 0.4203 0.3194 0.0400  -0.0108 -0.0439 306 PHE B CE2 
5483 C CZ  . PHE B 297 ? 0.4710 0.5086 0.3750 0.0486  -0.0128 -0.0433 306 PHE B CZ  
5484 N N   . LEU B 298 ? 0.4010 0.4038 0.3865 0.0340  -0.0409 -0.0886 307 LEU B N   
5485 C CA  . LEU B 298 ? 0.3922 0.3870 0.3992 0.0266  -0.0454 -0.0819 307 LEU B CA  
5486 C C   . LEU B 298 ? 0.3933 0.3899 0.4194 0.0290  -0.0622 -0.0950 307 LEU B C   
5487 O O   . LEU B 298 ? 0.3463 0.3458 0.3797 0.0277  -0.0667 -0.0913 307 LEU B O   
5488 C CB  . LEU B 298 ? 0.4054 0.3888 0.4296 0.0176  -0.0411 -0.0738 307 LEU B CB  
5489 C CG  . LEU B 298 ? 0.4737 0.4537 0.4892 0.0125  -0.0271 -0.0580 307 LEU B CG  
5490 C CD1 . LEU B 298 ? 0.4425 0.4145 0.4715 0.0063  -0.0245 -0.0530 307 LEU B CD1 
5491 C CD2 . LEU B 298 ? 0.5744 0.5567 0.5937 0.0102  -0.0256 -0.0482 307 LEU B CD2 
5492 N N   . CYS B 299 ? 0.4033 0.3982 0.4398 0.0327  -0.0727 -0.1110 308 CYS B N   
5493 C CA  . CYS B 299 ? 0.4105 0.4052 0.4698 0.0350  -0.0916 -0.1258 308 CYS B CA  
5494 C C   . CYS B 299 ? 0.4241 0.4335 0.4658 0.0462  -0.0991 -0.1379 308 CYS B C   
5495 O O   . CYS B 299 ? 0.3971 0.4081 0.4562 0.0468  -0.1132 -0.1451 308 CYS B O   
5496 C CB  . CYS B 299 ? 0.4437 0.4301 0.5244 0.0362  -0.1032 -0.1407 308 CYS B CB  
5497 S SG  . CYS B 299 ? 0.5409 0.5378 0.6004 0.0519  -0.1074 -0.1649 308 CYS B SG  
5498 N N   A SER B 300 ? 0.4251 0.4467 0.4339 0.0550  -0.0901 -0.1389 309 SER B N   
5499 N N   B SER B 300 ? 0.4288 0.4504 0.4375 0.0549  -0.0900 -0.1388 309 SER B N   
5500 C CA  A SER B 300 ? 0.4453 0.4841 0.4323 0.0662  -0.0948 -0.1459 309 SER B CA  
5501 C CA  B SER B 300 ? 0.4520 0.4908 0.4384 0.0662  -0.0943 -0.1454 309 SER B CA  
5502 C C   A SER B 300 ? 0.4312 0.4706 0.4169 0.0620  -0.0920 -0.1306 309 SER B C   
5503 C C   B SER B 300 ? 0.4345 0.4738 0.4210 0.0618  -0.0922 -0.1307 309 SER B C   
5504 O O   A SER B 300 ? 0.4256 0.4748 0.4096 0.0687  -0.1034 -0.1387 309 SER B O   
5505 O O   B SER B 300 ? 0.4270 0.4754 0.4130 0.0682  -0.1040 -0.1390 309 SER B O   
5506 C CB  A SER B 300 ? 0.4630 0.5174 0.4164 0.0756  -0.0836 -0.1455 309 SER B CB  
5507 C CB  B SER B 300 ? 0.4734 0.5277 0.4256 0.0750  -0.0821 -0.1432 309 SER B CB  
5508 O OG  A SER B 300 ? 0.4196 0.4761 0.3752 0.0813  -0.0868 -0.1616 309 SER B OG  
5509 O OG  B SER B 300 ? 0.4486 0.4998 0.3880 0.0681  -0.0648 -0.1200 309 SER B OG  
5510 N N   . LEU B 301 ? 0.4262 0.4563 0.4138 0.0520  -0.0782 -0.1104 310 LEU B N   
5511 C CA  . LEU B 301 ? 0.4239 0.4537 0.4152 0.0480  -0.0760 -0.0968 310 LEU B CA  
5512 C C   . LEU B 301 ? 0.4289 0.4552 0.4523 0.0431  -0.0892 -0.1015 310 LEU B C   
5513 O O   . LEU B 301 ? 0.4322 0.4653 0.4592 0.0453  -0.0956 -0.1005 310 LEU B O   
5514 C CB  . LEU B 301 ? 0.3944 0.4151 0.3833 0.0397  -0.0597 -0.0774 310 LEU B CB  
5515 C CG  . LEU B 301 ? 0.4454 0.4672 0.4089 0.0417  -0.0457 -0.0679 310 LEU B CG  
5516 C CD1 . LEU B 301 ? 0.4229 0.4351 0.3899 0.0342  -0.0343 -0.0518 310 LEU B CD1 
5517 C CD2 . LEU B 301 ? 0.4928 0.5282 0.4320 0.0512  -0.0460 -0.0664 310 LEU B CD2 
5518 N N   . GLU B 302 ? 0.4425 0.4592 0.4914 0.0364  -0.0939 -0.1057 311 GLU B N   
5519 C CA  . GLU B 302 ? 0.4394 0.4531 0.5252 0.0303  -0.1074 -0.1088 311 GLU B CA  
5520 C C   . GLU B 302 ? 0.4313 0.4527 0.5244 0.0387  -0.1275 -0.1291 311 GLU B C   
5521 O O   . GLU B 302 ? 0.4387 0.4622 0.5579 0.0352  -0.1384 -0.1296 311 GLU B O   
5522 C CB  . GLU B 302 ? 0.4228 0.4243 0.5351 0.0216  -0.1088 -0.1073 311 GLU B CB  
5523 C CG  . GLU B 302 ? 0.4498 0.4458 0.5591 0.0131  -0.0909 -0.0867 311 GLU B CG  
5524 C CD  . GLU B 302 ? 0.4682 0.4538 0.6014 0.0053  -0.0921 -0.0830 311 GLU B CD  
5525 O OE1 . GLU B 302 ? 0.5303 0.5097 0.6663 0.0088  -0.0999 -0.0969 311 GLU B OE1 
5526 O OE2 . GLU B 302 ? 0.5509 0.5358 0.6995 -0.0035 -0.0848 -0.0657 311 GLU B OE2 
5527 N N   . SER B 303 ? 0.4645 0.4924 0.5348 0.0506  -0.1323 -0.1461 312 SER B N   
5528 C CA  . SER B 303 ? 0.5017 0.5395 0.5745 0.0616  -0.1525 -0.1689 312 SER B CA  
5529 C C   . SER B 303 ? 0.5138 0.5672 0.5652 0.0698  -0.1543 -0.1675 312 SER B C   
5530 O O   . SER B 303 ? 0.5295 0.5919 0.5870 0.0781  -0.1727 -0.1852 312 SER B O   
5531 C CB  . SER B 303 ? 0.5261 0.5689 0.5822 0.0735  -0.1576 -0.1896 312 SER B CB  
5532 O OG  . SER B 303 ? 0.6322 0.6887 0.6461 0.0823  -0.1433 -0.1842 312 SER B OG  
5533 N N   . ASN B 304 ? 0.5146 0.5708 0.5422 0.0682  -0.1368 -0.1473 313 ASN B N   
5534 C CA  . ASN B 304 ? 0.5202 0.5894 0.5295 0.0753  -0.1379 -0.1421 313 ASN B CA  
5535 C C   . ASN B 304 ? 0.5045 0.5707 0.5428 0.0672  -0.1429 -0.1336 313 ASN B C   
5536 O O   . ASN B 304 ? 0.4959 0.5509 0.5625 0.0551  -0.1394 -0.1257 313 ASN B O   
5537 C CB  . ASN B 304 ? 0.5283 0.6009 0.5039 0.0773  -0.1187 -0.1236 313 ASN B CB  
5538 C CG  . ASN B 304 ? 0.5753 0.6601 0.5195 0.0884  -0.1154 -0.1312 313 ASN B CG  
5539 O OD1 . ASN B 304 ? 0.7197 0.8225 0.6412 0.1008  -0.1210 -0.1364 313 ASN B OD1 
5540 N ND2 . ASN B 304 ? 0.6581 0.7360 0.6010 0.0848  -0.1061 -0.1313 313 ASN B ND2 
5541 N N   . PRO B 305 ? 0.5217 0.6001 0.5535 0.0742  -0.1510 -0.1345 314 PRO B N   
5542 C CA  . PRO B 305 ? 0.5059 0.5844 0.5655 0.0674  -0.1550 -0.1259 314 PRO B CA  
5543 C C   . PRO B 305 ? 0.4679 0.5386 0.5309 0.0577  -0.1360 -0.1027 314 PRO B C   
5544 O O   . PRO B 305 ? 0.4566 0.5227 0.4943 0.0583  -0.1204 -0.0918 314 PRO B O   
5545 C CB  . PRO B 305 ? 0.5252 0.6193 0.5671 0.0795  -0.1647 -0.1299 314 PRO B CB  
5546 C CG  . PRO B 305 ? 0.5339 0.6377 0.5493 0.0926  -0.1730 -0.1477 314 PRO B CG  
5547 C CD  . PRO B 305 ? 0.5424 0.6376 0.5419 0.0897  -0.1575 -0.1433 314 PRO B CD  
5548 N N   . SER B 306 ? 0.4595 0.5305 0.5554 0.0495  -0.1382 -0.0960 315 SER B N   
5549 C CA  . SER B 306 ? 0.4465 0.5136 0.5491 0.0416  -0.1217 -0.0767 315 SER B CA  
5550 C C   . SER B 306 ? 0.4370 0.5095 0.5193 0.0483  -0.1149 -0.0661 315 SER B C   
5551 O O   . SER B 306 ? 0.4305 0.5133 0.5167 0.0541  -0.1255 -0.0694 315 SER B O   
5552 C CB  . SER B 306 ? 0.4268 0.4973 0.5730 0.0314  -0.1260 -0.0721 315 SER B CB  
5553 O OG  . SER B 306 ? 0.4310 0.5040 0.5826 0.0268  -0.1110 -0.0547 315 SER B OG  
5554 N N   . VAL B 307 ? 0.4326 0.4975 0.4950 0.0476  -0.0985 -0.0539 316 VAL B N   
5555 C CA  . VAL B 307 ? 0.4452 0.5116 0.4937 0.0527  -0.0915 -0.0424 316 VAL B CA  
5556 C C   . VAL B 307 ? 0.4235 0.4969 0.4993 0.0495  -0.0909 -0.0358 316 VAL B C   
5557 O O   . VAL B 307 ? 0.4160 0.4969 0.4923 0.0558  -0.0951 -0.0328 316 VAL B O   
5558 C CB  . VAL B 307 ? 0.4687 0.5235 0.4963 0.0515  -0.0753 -0.0319 316 VAL B CB  
5559 C CG1 . VAL B 307 ? 0.5340 0.5881 0.5527 0.0569  -0.0704 -0.0206 316 VAL B CG1 
5560 C CG2 . VAL B 307 ? 0.5494 0.6004 0.5511 0.0546  -0.0739 -0.0362 316 VAL B CG2 
5561 N N   . ARG B 308 ? 0.3913 0.4642 0.4897 0.0405  -0.0850 -0.0325 317 ARG B N   
5562 C CA  . ARG B 308 ? 0.3915 0.4760 0.5185 0.0371  -0.0828 -0.0253 317 ARG B CA  
5563 C C   . ARG B 308 ? 0.3915 0.4897 0.5422 0.0387  -0.0983 -0.0311 317 ARG B C   
5564 O O   . ARG B 308 ? 0.3597 0.4686 0.5191 0.0429  -0.0986 -0.0264 317 ARG B O   
5565 C CB  . ARG B 308 ? 0.3852 0.4701 0.5334 0.0268  -0.0757 -0.0200 317 ARG B CB  
5566 C CG  . ARG B 308 ? 0.3665 0.4684 0.5434 0.0237  -0.0708 -0.0100 317 ARG B CG  
5567 C CD  . ARG B 308 ? 0.3778 0.4822 0.5687 0.0153  -0.0603 -0.0007 317 ARG B CD  
5568 N NE  . ARG B 308 ? 0.3868 0.5092 0.5908 0.0166  -0.0497 0.0102  317 ARG B NE  
5569 C CZ  . ARG B 308 ? 0.4107 0.5543 0.6490 0.0130  -0.0519 0.0171  317 ARG B CZ  
5570 N NH1 . ARG B 308 ? 0.5033 0.6509 0.7702 0.0066  -0.0659 0.0142  317 ARG B NH1 
5571 N NH2 . ARG B 308 ? 0.4024 0.5650 0.6484 0.0162  -0.0404 0.0265  317 ARG B NH2 
5572 N N   A GLU B 309 ? 0.4137 0.5117 0.5767 0.0360  -0.1122 -0.0425 318 GLU B N   
5573 N N   B GLU B 309 ? 0.4134 0.5111 0.5758 0.0360  -0.1122 -0.0426 318 GLU B N   
5574 C CA  A GLU B 309 ? 0.4273 0.5379 0.6161 0.0373  -0.1296 -0.0502 318 GLU B CA  
5575 C CA  B GLU B 309 ? 0.4289 0.5391 0.6172 0.0373  -0.1299 -0.0507 318 GLU B CA  
5576 C C   A GLU B 309 ? 0.4358 0.5510 0.6016 0.0497  -0.1387 -0.0563 318 GLU B C   
5577 C C   B GLU B 309 ? 0.4340 0.5492 0.5996 0.0496  -0.1381 -0.0558 318 GLU B C   
5578 O O   A GLU B 309 ? 0.4607 0.5890 0.6453 0.0526  -0.1491 -0.0579 318 GLU B O   
5579 O O   B GLU B 309 ? 0.4535 0.5818 0.6378 0.0525  -0.1473 -0.0564 318 GLU B O   
5580 C CB  A GLU B 309 ? 0.4445 0.5523 0.6562 0.0315  -0.1444 -0.0628 318 GLU B CB  
5581 C CB  B GLU B 309 ? 0.4409 0.5478 0.6503 0.0320  -0.1451 -0.0641 318 GLU B CB  
5582 C CG  A GLU B 309 ? 0.4739 0.5794 0.7170 0.0182  -0.1381 -0.0539 318 GLU B CG  
5583 C CG  B GLU B 309 ? 0.4902 0.5943 0.6783 0.0416  -0.1608 -0.0832 318 GLU B CG  
5584 C CD  A GLU B 309 ? 0.5003 0.6220 0.7758 0.0119  -0.1310 -0.0380 318 GLU B CD  
5585 C CD  B GLU B 309 ? 0.4944 0.5951 0.7101 0.0370  -0.1777 -0.0986 318 GLU B CD  
5586 O OE1 A GLU B 309 ? 0.4474 0.5834 0.7453 0.0136  -0.1415 -0.0399 318 GLU B OE1 
5587 O OE1 B GLU B 309 ? 0.5331 0.6420 0.7889 0.0320  -0.1914 -0.1016 318 GLU B OE1 
5588 O OE2 A GLU B 309 ? 0.5244 0.6469 0.8024 0.0062  -0.1149 -0.0239 318 GLU B OE2 
5589 O OE2 B GLU B 309 ? 0.5224 0.6126 0.7222 0.0385  -0.1783 -0.1081 318 GLU B OE2 
5590 N N   . PHE B 310 ? 0.4338 0.5401 0.5606 0.0569  -0.1346 -0.0579 319 PHE B N   
5591 C CA  . PHE B 310 ? 0.4575 0.5688 0.5589 0.0689  -0.1397 -0.0578 319 PHE B CA  
5592 C C   . PHE B 310 ? 0.4464 0.5611 0.5515 0.0716  -0.1318 -0.0442 319 PHE B C   
5593 O O   . PHE B 310 ? 0.4361 0.5616 0.5470 0.0784  -0.1418 -0.0449 319 PHE B O   
5594 C CB  . PHE B 310 ? 0.4589 0.5617 0.5200 0.0747  -0.1336 -0.0573 319 PHE B CB  
5595 C CG  . PHE B 310 ? 0.4565 0.5668 0.4911 0.0872  -0.1399 -0.0554 319 PHE B CG  
5596 C CD1 . PHE B 310 ? 0.5079 0.6153 0.5309 0.0912  -0.1316 -0.0398 319 PHE B CD1 
5597 C CD2 . PHE B 310 ? 0.5323 0.6533 0.5541 0.0959  -0.1552 -0.0692 319 PHE B CD2 
5598 C CE1 . PHE B 310 ? 0.4996 0.6140 0.4997 0.1026  -0.1378 -0.0349 319 PHE B CE1 
5599 C CE2 . PHE B 310 ? 0.5214 0.6524 0.5168 0.1084  -0.1610 -0.0654 319 PHE B CE2 
5600 C CZ  . PHE B 310 ? 0.5555 0.6830 0.5405 0.1112  -0.1519 -0.0466 319 PHE B CZ  
5601 N N   . VAL B 311 ? 0.4404 0.5466 0.5431 0.0671  -0.1150 -0.0333 320 VAL B N   
5602 C CA  . VAL B 311 ? 0.4569 0.5656 0.5637 0.0709  -0.1073 -0.0227 320 VAL B CA  
5603 C C   . VAL B 311 ? 0.4595 0.5852 0.6037 0.0683  -0.1112 -0.0224 320 VAL B C   
5604 O O   . VAL B 311 ? 0.4259 0.5608 0.5769 0.0755  -0.1153 -0.0197 320 VAL B O   
5605 C CB  . VAL B 311 ? 0.4495 0.5455 0.5447 0.0679  -0.0898 -0.0142 320 VAL B CB  
5606 C CG1 . VAL B 311 ? 0.4618 0.5626 0.5678 0.0722  -0.0831 -0.0069 320 VAL B CG1 
5607 C CG2 . VAL B 311 ? 0.4606 0.5422 0.5216 0.0717  -0.0865 -0.0115 320 VAL B CG2 
5608 N N   . LEU B 312 ? 0.4728 0.6038 0.6429 0.0582  -0.1102 -0.0240 321 LEU B N   
5609 C CA  . LEU B 312 ? 0.4870 0.6376 0.6975 0.0541  -0.1141 -0.0217 321 LEU B CA  
5610 C C   . LEU B 312 ? 0.5093 0.6720 0.7344 0.0592  -0.1329 -0.0296 321 LEU B C   
5611 O O   . LEU B 312 ? 0.5125 0.6929 0.7652 0.0602  -0.1352 -0.0260 321 LEU B O   
5612 C CB  . LEU B 312 ? 0.5064 0.6598 0.7441 0.0412  -0.1124 -0.0204 321 LEU B CB  
5613 C CG  . LEU B 312 ? 0.5318 0.6892 0.7765 0.0357  -0.0939 -0.0080 321 LEU B CG  
5614 C CD1 . LEU B 312 ? 0.5769 0.7305 0.8383 0.0238  -0.0930 -0.0060 321 LEU B CD1 
5615 C CD2 . LEU B 312 ? 0.5773 0.7592 0.8508 0.0370  -0.0891 0.0008  321 LEU B CD2 
5616 N N   . SER B 313 ? 0.5237 0.6792 0.7303 0.0633  -0.1462 -0.0408 322 SER B N   
5617 C CA  . SER B 313 ? 0.5388 0.7060 0.7566 0.0693  -0.1663 -0.0509 322 SER B CA  
5618 C C   . SER B 313 ? 0.5498 0.7227 0.7506 0.0823  -0.1705 -0.0478 322 SER B C   
5619 O O   . SER B 313 ? 0.5397 0.7260 0.7561 0.0870  -0.1867 -0.0545 322 SER B O   
5620 C CB  . SER B 313 ? 0.5606 0.7211 0.7641 0.0709  -0.1804 -0.0665 322 SER B CB  
5621 O OG  . SER B 313 ? 0.5851 0.7350 0.7429 0.0794  -0.1757 -0.0663 322 SER B OG  
5622 N N   . LYS B 314 ? 0.5435 0.7060 0.7156 0.0879  -0.1575 -0.0377 323 LYS B N   
5623 C CA  . LYS B 314 ? 0.5401 0.7023 0.6872 0.1009  -0.1635 -0.0344 323 LYS B CA  
5624 C C   . LYS B 314 ? 0.5488 0.7190 0.7086 0.1081  -0.1622 -0.0260 323 LYS B C   
5625 O O   . LYS B 314 ? 0.5850 0.7561 0.7285 0.1191  -0.1704 -0.0230 323 LYS B O   
5626 C CB  . LYS B 314 ? 0.5672 0.7119 0.6739 0.1039  -0.1538 -0.0282 323 LYS B CB  
5627 C CG  . LYS B 314 ? 0.5848 0.7261 0.6716 0.1027  -0.1594 -0.0381 323 LYS B CG  
5628 C CD  . LYS B 314 ? 0.6441 0.7952 0.7108 0.1144  -0.1755 -0.0439 323 LYS B CD  
5629 C CE  . LYS B 314 ? 0.6707 0.8250 0.7288 0.1141  -0.1852 -0.0602 323 LYS B CE  
5630 N NZ  . LYS B 314 ? 0.7502 0.9130 0.8463 0.1082  -0.1988 -0.0751 323 LYS B NZ  
5631 N N   . GLY B 315 ? 0.4919 0.6700 0.6806 0.1030  -0.1527 -0.0220 324 GLY B N   
5632 C CA  . GLY B 315 ? 0.4508 0.6389 0.6546 0.1108  -0.1506 -0.0158 324 GLY B CA  
5633 C C   . GLY B 315 ? 0.4363 0.6086 0.6116 0.1206  -0.1455 -0.0078 324 GLY B C   
5634 O O   . GLY B 315 ? 0.4506 0.6267 0.6260 0.1313  -0.1537 -0.0049 324 GLY B O   
5635 N N   . ASP B 316 ? 0.4197 0.5736 0.5730 0.1166  -0.1329 -0.0039 325 ASP B N   
5636 C CA  . ASP B 316 ? 0.3996 0.5349 0.5254 0.1232  -0.1290 0.0045  325 ASP B CA  
5637 C C   . ASP B 316 ? 0.3569 0.4815 0.4840 0.1205  -0.1129 0.0078  325 ASP B C   
5638 O O   . ASP B 316 ? 0.3801 0.4958 0.4977 0.1120  -0.1034 0.0069  325 ASP B O   
5639 C CB  . ASP B 316 ? 0.4046 0.5296 0.4999 0.1209  -0.1322 0.0047  325 ASP B CB  
5640 C CG  . ASP B 316 ? 0.4403 0.5489 0.5084 0.1270  -0.1297 0.0164  325 ASP B CG  
5641 O OD1 . ASP B 316 ? 0.4858 0.5817 0.5554 0.1283  -0.1207 0.0231  325 ASP B OD1 
5642 O OD2 . ASP B 316 ? 0.4620 0.5715 0.5078 0.1308  -0.1373 0.0191  325 ASP B OD2 
5643 N N   . ALA B 317 ? 0.3488 0.4754 0.4885 0.1288  -0.1109 0.0101  326 ALA B N   
5644 C CA  . ALA B 317 ? 0.3443 0.4642 0.4876 0.1291  -0.0975 0.0101  326 ALA B CA  
5645 C C   . ALA B 317 ? 0.3484 0.4428 0.4657 0.1264  -0.0912 0.0149  326 ALA B C   
5646 O O   . ALA B 317 ? 0.3516 0.4408 0.4657 0.1201  -0.0800 0.0127  326 ALA B O   
5647 C CB  . ALA B 317 ? 0.3365 0.4626 0.4967 0.1419  -0.0997 0.0097  326 ALA B CB  
5648 N N   . GLY B 318 ? 0.3802 0.4609 0.4803 0.1310  -0.0987 0.0228  327 GLY B N   
5649 C CA  . GLY B 318 ? 0.3959 0.4551 0.4729 0.1274  -0.0941 0.0301  327 GLY B CA  
5650 C C   . GLY B 318 ? 0.3842 0.4417 0.4485 0.1158  -0.0862 0.0267  327 GLY B C   
5651 O O   . GLY B 318 ? 0.3673 0.4130 0.4271 0.1111  -0.0762 0.0264  327 GLY B O   
5652 N N   . LEU B 319 ? 0.3793 0.4486 0.4396 0.1121  -0.0919 0.0227  328 LEU B N   
5653 C CA  . LEU B 319 ? 0.3867 0.4550 0.4376 0.1021  -0.0865 0.0178  328 LEU B CA  
5654 C C   . LEU B 319 ? 0.3498 0.4220 0.4173 0.0947  -0.0766 0.0117  328 LEU B C   
5655 O O   . LEU B 319 ? 0.3243 0.3875 0.3826 0.0877  -0.0680 0.0111  328 LEU B O   
5656 C CB  . LEU B 319 ? 0.4230 0.5045 0.4716 0.1011  -0.0972 0.0112  328 LEU B CB  
5657 C CG  . LEU B 319 ? 0.4863 0.5664 0.5079 0.1052  -0.1040 0.0147  328 LEU B CG  
5658 C CD1 . LEU B 319 ? 0.5573 0.6527 0.5826 0.1051  -0.1160 0.0026  328 LEU B CD1 
5659 C CD2 . LEU B 319 ? 0.4902 0.5571 0.4900 0.1004  -0.0939 0.0194  328 LEU B CD2 
5660 N N   . ARG B 320 ? 0.3470 0.4353 0.4394 0.0965  -0.0779 0.0082  329 ARG B N   
5661 C CA  . ARG B 320 ? 0.3554 0.4527 0.4651 0.0906  -0.0679 0.0053  329 ARG B CA  
5662 C C   . ARG B 320 ? 0.3357 0.4214 0.4378 0.0924  -0.0564 0.0069  329 ARG B C   
5663 O O   . ARG B 320 ? 0.3224 0.4065 0.4227 0.0856  -0.0473 0.0058  329 ARG B O   
5664 C CB  . ARG B 320 ? 0.3482 0.4691 0.4874 0.0937  -0.0708 0.0036  329 ARG B CB  
5665 C CG  . ARG B 320 ? 0.3934 0.5282 0.5482 0.0889  -0.0819 0.0002  329 ARG B CG  
5666 C CD  . ARG B 320 ? 0.4298 0.5906 0.6200 0.0875  -0.0810 0.0005  329 ARG B CD  
5667 N NE  . ARG B 320 ? 0.5013 0.6720 0.7009 0.0988  -0.0795 0.0019  329 ARG B NE  
5668 C CZ  . ARG B 320 ? 0.5682 0.7432 0.7721 0.1080  -0.0908 0.0009  329 ARG B CZ  
5669 N NH1 . ARG B 320 ? 0.6350 0.8068 0.8327 0.1077  -0.1048 -0.0014 329 ARG B NH1 
5670 N NH2 . ARG B 320 ? 0.5730 0.7569 0.7874 0.1188  -0.0887 0.0014  329 ARG B NH2 
5671 N N   . GLU B 321 ? 0.3386 0.4160 0.4377 0.1021  -0.0583 0.0090  330 GLU B N   
5672 C CA  . GLU B 321 ? 0.3693 0.4339 0.4634 0.1054  -0.0506 0.0083  330 GLU B CA  
5673 C C   . GLU B 321 ? 0.3507 0.3948 0.4236 0.0983  -0.0465 0.0114  330 GLU B C   
5674 O O   . GLU B 321 ? 0.3401 0.3786 0.4104 0.0957  -0.0382 0.0085  330 GLU B O   
5675 C CB  . GLU B 321 ? 0.3630 0.4198 0.4615 0.1176  -0.0568 0.0096  330 GLU B CB  
5676 C CG  . GLU B 321 ? 0.4743 0.5524 0.5958 0.1269  -0.0589 0.0046  330 GLU B CG  
5677 C CD  . GLU B 321 ? 0.5297 0.5998 0.6568 0.1393  -0.0687 0.0065  330 GLU B CD  
5678 O OE1 . GLU B 321 ? 0.7171 0.7633 0.8337 0.1416  -0.0714 0.0108  330 GLU B OE1 
5679 O OE2 . GLU B 321 ? 0.6489 0.7366 0.7931 0.1465  -0.0744 0.0046  330 GLU B OE2 
5680 N N   . ALA B 322 ? 0.3431 0.3788 0.4013 0.0962  -0.0525 0.0173  331 ALA B N   
5681 C CA  . ALA B 322 ? 0.3531 0.3735 0.3921 0.0896  -0.0483 0.0212  331 ALA B CA  
5682 C C   . ALA B 322 ? 0.3489 0.3747 0.3863 0.0800  -0.0417 0.0157  331 ALA B C   
5683 O O   . ALA B 322 ? 0.3505 0.3662 0.3808 0.0752  -0.0342 0.0153  331 ALA B O   
5684 C CB  . ALA B 322 ? 0.3477 0.3646 0.3711 0.0909  -0.0556 0.0292  331 ALA B CB  
5685 N N   . TYR B 323 ? 0.3520 0.3931 0.3984 0.0772  -0.0456 0.0115  332 TYR B N   
5686 C CA  . TYR B 323 ? 0.3307 0.3776 0.3820 0.0682  -0.0411 0.0070  332 TYR B CA  
5687 C C   . TYR B 323 ? 0.3243 0.3743 0.3854 0.0664  -0.0308 0.0060  332 TYR B C   
5688 O O   . TYR B 323 ? 0.2905 0.3337 0.3446 0.0604  -0.0242 0.0054  332 TYR B O   
5689 C CB  . TYR B 323 ? 0.3286 0.3921 0.3966 0.0660  -0.0492 0.0030  332 TYR B CB  
5690 C CG  . TYR B 323 ? 0.3476 0.4165 0.4273 0.0564  -0.0456 0.0002  332 TYR B CG  
5691 C CD1 . TYR B 323 ? 0.3492 0.4108 0.4191 0.0508  -0.0479 -0.0036 332 TYR B CD1 
5692 C CD2 . TYR B 323 ? 0.3344 0.4173 0.4360 0.0538  -0.0396 0.0023  332 TYR B CD2 
5693 C CE1 . TYR B 323 ? 0.3161 0.3806 0.3994 0.0422  -0.0459 -0.0054 332 TYR B CE1 
5694 C CE2 . TYR B 323 ? 0.3079 0.3958 0.4221 0.0447  -0.0365 0.0030  332 TYR B CE2 
5695 C CZ  . TYR B 323 ? 0.3221 0.3991 0.4280 0.0386  -0.0403 -0.0009 332 TYR B CZ  
5696 O OH  . TYR B 323 ? 0.3149 0.3952 0.4361 0.0298  -0.0385 0.0005  332 TYR B OH  
5697 N N   . ASP B 324 ? 0.3108 0.3731 0.3874 0.0728  -0.0298 0.0054  333 ASP B N   
5698 C CA  . ASP B 324 ? 0.3087 0.3798 0.3935 0.0738  -0.0199 0.0039  333 ASP B CA  
5699 C C   . ASP B 324 ? 0.3277 0.3820 0.3980 0.0766  -0.0146 0.0020  333 ASP B C   
5700 O O   . ASP B 324 ? 0.3379 0.3958 0.4074 0.0745  -0.0066 0.0001  333 ASP B O   
5701 C CB  . ASP B 324 ? 0.2764 0.3681 0.3805 0.0823  -0.0197 0.0027  333 ASP B CB  
5702 C CG  . ASP B 324 ? 0.3092 0.4254 0.4357 0.0770  -0.0195 0.0055  333 ASP B CG  
5703 O OD1 . ASP B 324 ? 0.2974 0.4129 0.4263 0.0667  -0.0208 0.0077  333 ASP B OD1 
5704 O OD2 . ASP B 324 ? 0.3119 0.4493 0.4566 0.0835  -0.0183 0.0056  333 ASP B OD2 
5705 N N   . ALA B 325 ? 0.3446 0.3814 0.4053 0.0813  -0.0198 0.0032  334 ALA B N   
5706 C CA  . ALA B 325 ? 0.3581 0.3763 0.4086 0.0827  -0.0168 0.0018  334 ALA B CA  
5707 C C   . ALA B 325 ? 0.3710 0.3805 0.4088 0.0726  -0.0118 0.0031  334 ALA B C   
5708 O O   . ALA B 325 ? 0.4067 0.4100 0.4411 0.0720  -0.0066 -0.0004 334 ALA B O   
5709 C CB  . ALA B 325 ? 0.3676 0.3688 0.4145 0.0880  -0.0244 0.0064  334 ALA B CB  
5710 N N   . CYS B 326 ? 0.3736 0.3840 0.4053 0.0656  -0.0140 0.0066  335 CYS B N   
5711 C CA  . CYS B 326 ? 0.3454 0.3502 0.3672 0.0568  -0.0096 0.0065  335 CYS B CA  
5712 C C   . CYS B 326 ? 0.3333 0.3497 0.3635 0.0528  -0.0033 0.0033  335 CYS B C   
5713 O O   . CYS B 326 ? 0.3330 0.3433 0.3573 0.0496  0.0023  0.0019  335 CYS B O   
5714 C CB  . CYS B 326 ? 0.3574 0.3633 0.3719 0.0526  -0.0148 0.0081  335 CYS B CB  
5715 S SG  . CYS B 326 ? 0.3405 0.3367 0.3404 0.0568  -0.0206 0.0152  335 CYS B SG  
5716 N N   . VAL B 327 ? 0.3376 0.3042 0.3442 0.0113  -0.0297 0.0235  336 VAL B N   
5717 C CA  . VAL B 327 ? 0.3193 0.3147 0.3541 0.0138  -0.0142 0.0142  336 VAL B CA  
5718 C C   . VAL B 327 ? 0.3382 0.3310 0.3828 0.0278  -0.0064 0.0090  336 VAL B C   
5719 O O   . VAL B 327 ? 0.3127 0.3106 0.3590 0.0236  0.0087  0.0044  336 VAL B O   
5720 C CB  . VAL B 327 ? 0.2907 0.3224 0.3555 0.0158  -0.0199 0.0127  336 VAL B CB  
5721 C CG1 . VAL B 327 ? 0.2953 0.3554 0.3846 0.0127  -0.0046 0.0086  336 VAL B CG1 
5722 C CG2 . VAL B 327 ? 0.3428 0.3733 0.3952 0.0007  -0.0289 0.0140  336 VAL B CG2 
5723 N N   . LYS B 328 ? 0.3654 0.3482 0.4141 0.0467  -0.0197 0.0082  337 LYS B N   
5724 C CA  . LYS B 328 ? 0.3615 0.3377 0.4156 0.0650  -0.0169 -0.0015 337 LYS B CA  
5725 C C   . LYS B 328 ? 0.3753 0.3147 0.4030 0.0531  -0.0112 -0.0007 337 LYS B C   
5726 O O   . LYS B 328 ? 0.3500 0.2952 0.3822 0.0591  -0.0004 -0.0103 337 LYS B O   
5727 C CB  . LYS B 328 ? 0.3962 0.3562 0.4538 0.0914  -0.0395 -0.0051 337 LYS B CB  
5728 C CG  . LYS B 328 ? 0.4887 0.4410 0.5513 0.1172  -0.0405 -0.0213 337 LYS B CG  
5729 C CD  . LYS B 328 ? 0.4843 0.4292 0.5571 0.1515  -0.0655 -0.0300 337 LYS B CD  
5730 C CE  . LYS B 328 ? 0.5220 0.4426 0.5899 0.1802  -0.0723 -0.0500 337 LYS B CE  
5731 N NZ  . LYS B 328 ? 0.5743 0.4957 0.6575 0.2230  -0.0974 -0.0653 337 LYS B NZ  
5732 N N   . ALA B 329 ? 0.3916 0.2996 0.3915 0.0346  -0.0187 0.0111  338 ALA B N   
5733 C CA  . ALA B 329 ? 0.4253 0.3113 0.4036 0.0165  -0.0125 0.0136  338 ALA B CA  
5734 C C   . ALA B 329 ? 0.3797 0.2978 0.3683 0.0084  0.0091  0.0062  338 ALA B C   
5735 O O   . ALA B 329 ? 0.4059 0.3197 0.3925 0.0068  0.0157  0.0002  338 ALA B O   
5736 C CB  . ALA B 329 ? 0.4413 0.3035 0.3885 -0.0068 -0.0219 0.0299  338 ALA B CB  
5737 N N   . LEU B 330 ? 0.3771 0.3230 0.3758 0.0048  0.0164  0.0057  339 LEU B N   
5738 C CA  . LEU B 330 ? 0.3611 0.3288 0.3688 0.0016  0.0312  -0.0013 339 LEU B CA  
5739 C C   . LEU B 330 ? 0.3550 0.3370 0.3807 0.0144  0.0381  -0.0070 339 LEU B C   
5740 O O   . LEU B 330 ? 0.3287 0.3147 0.3530 0.0136  0.0468  -0.0115 339 LEU B O   
5741 C CB  . LEU B 330 ? 0.3392 0.3212 0.3490 -0.0049 0.0315  -0.0016 339 LEU B CB  
5742 C CG  . LEU B 330 ? 0.3789 0.3583 0.3666 -0.0169 0.0291  -0.0006 339 LEU B CG  
5743 C CD1 . LEU B 330 ? 0.3770 0.3658 0.3655 -0.0185 0.0248  -0.0052 339 LEU B CD1 
5744 C CD2 . LEU B 330 ? 0.3779 0.3650 0.3562 -0.0236 0.0392  -0.0065 339 LEU B CD2 
5745 N N   . VAL B 331 ? 0.3459 0.3413 0.3878 0.0266  0.0339  -0.0072 340 VAL B N   
5746 C CA  . VAL B 331 ? 0.3414 0.3620 0.3986 0.0389  0.0423  -0.0133 340 VAL B CA  
5747 C C   . VAL B 331 ? 0.3489 0.3504 0.3936 0.0492  0.0427  -0.0225 340 VAL B C   
5748 O O   . VAL B 331 ? 0.3359 0.3494 0.3788 0.0502  0.0529  -0.0270 340 VAL B O   
5749 C CB  . VAL B 331 ? 0.3258 0.3784 0.4070 0.0527  0.0378  -0.0149 340 VAL B CB  
5750 C CG1 . VAL B 331 ? 0.3301 0.4191 0.4244 0.0678  0.0486  -0.0242 340 VAL B CG1 
5751 C CG2 . VAL B 331 ? 0.2792 0.3553 0.3752 0.0379  0.0366  -0.0060 340 VAL B CG2 
5752 N N   . SER B 332 ? 0.3623 0.3297 0.3950 0.0551  0.0286  -0.0242 341 SER B N   
5753 C CA  . SER B 332 ? 0.4125 0.3511 0.4304 0.0625  0.0232  -0.0340 341 SER B CA  
5754 C C   . SER B 332 ? 0.3702 0.3030 0.3755 0.0443  0.0313  -0.0331 341 SER B C   
5755 O O   . SER B 332 ? 0.3619 0.2950 0.3626 0.0504  0.0344  -0.0434 341 SER B O   
5756 C CB  . SER B 332 ? 0.4333 0.3225 0.4352 0.0656  0.0010  -0.0316 341 SER B CB  
5757 O OG  . SER B 332 ? 0.5258 0.4204 0.5408 0.0902  -0.0104 -0.0366 341 SER B OG  
5758 N N   . LEU B 333 ? 0.3945 0.3275 0.3946 0.0240  0.0337  -0.0228 342 LEU B N   
5759 C CA  . LEU B 333 ? 0.3921 0.3322 0.3862 0.0096  0.0410  -0.0239 342 LEU B CA  
5760 C C   . LEU B 333 ? 0.3639 0.3300 0.3671 0.0175  0.0523  -0.0296 342 LEU B C   
5761 O O   . LEU B 333 ? 0.3587 0.3260 0.3568 0.0181  0.0538  -0.0364 342 LEU B O   
5762 C CB  . LEU B 333 ? 0.4063 0.3560 0.3962 -0.0076 0.0434  -0.0162 342 LEU B CB  
5763 C CG  . LEU B 333 ? 0.4359 0.4012 0.4219 -0.0216 0.0488  -0.0194 342 LEU B CG  
5764 C CD1 . LEU B 333 ? 0.5041 0.4486 0.4762 -0.0393 0.0402  -0.0151 342 LEU B CD1 
5765 C CD2 . LEU B 333 ? 0.4887 0.4786 0.4746 -0.0287 0.0545  -0.0186 342 LEU B CD2 
5766 N N   . ARG B 334 ? 0.3337 0.3183 0.3482 0.0212  0.0574  -0.0252 343 ARG B N   
5767 C CA  . ARG B 334 ? 0.3086 0.3115 0.3268 0.0236  0.0651  -0.0246 343 ARG B CA  
5768 C C   . ARG B 334 ? 0.3103 0.3256 0.3274 0.0354  0.0696  -0.0300 343 ARG B C   
5769 O O   . ARG B 334 ? 0.2791 0.3026 0.2886 0.0357  0.0739  -0.0304 343 ARG B O   
5770 C CB  . ARG B 334 ? 0.3145 0.3277 0.3426 0.0183  0.0656  -0.0160 343 ARG B CB  
5771 C CG  . ARG B 334 ? 0.3063 0.3092 0.3302 0.0101  0.0611  -0.0161 343 ARG B CG  
5772 C CD  . ARG B 334 ? 0.3343 0.3375 0.3639 0.0045  0.0571  -0.0107 343 ARG B CD  
5773 N NE  . ARG B 334 ? 0.3334 0.3267 0.3548 0.0030  0.0521  -0.0175 343 ARG B NE  
5774 C CZ  . ARG B 334 ? 0.3695 0.3601 0.3876 -0.0007 0.0467  -0.0207 343 ARG B CZ  
5775 N NH1 . ARG B 334 ? 0.3620 0.3553 0.3846 -0.0052 0.0430  -0.0151 343 ARG B NH1 
5776 N NH2 . ARG B 334 ? 0.4134 0.4025 0.4227 0.0026  0.0438  -0.0319 343 ARG B NH2 
5777 N N   . SER B 335 ? 0.2977 0.3160 0.3203 0.0477  0.0673  -0.0356 344 SER B N   
5778 C CA  . SER B 335 ? 0.3154 0.3508 0.3353 0.0642  0.0716  -0.0470 344 SER B CA  
5779 C C   . SER B 335 ? 0.3360 0.3466 0.3370 0.0675  0.0659  -0.0591 344 SER B C   
5780 O O   . SER B 335 ? 0.3421 0.3681 0.3328 0.0733  0.0715  -0.0658 344 SER B O   
5781 C CB  . SER B 335 ? 0.3496 0.3949 0.3819 0.0832  0.0668  -0.0555 344 SER B CB  
5782 O OG  . SER B 335 ? 0.3238 0.3983 0.3767 0.0781  0.0703  -0.0447 344 SER B OG  
5783 N N   . TYR B 336 ? 0.3493 0.3227 0.3438 0.0608  0.0535  -0.0605 345 TYR B N   
5784 C CA  . TYR B 336 ? 0.3733 0.3221 0.3519 0.0554  0.0453  -0.0695 345 TYR B CA  
5785 C C   . TYR B 336 ? 0.3386 0.3065 0.3150 0.0440  0.0522  -0.0659 345 TYR B C   
5786 O O   . TYR B 336 ? 0.3371 0.3061 0.3023 0.0471  0.0499  -0.0757 345 TYR B O   
5787 C CB  . TYR B 336 ? 0.3817 0.2921 0.3541 0.0398  0.0312  -0.0643 345 TYR B CB  
5788 C CG  . TYR B 336 ? 0.4619 0.3443 0.4190 0.0301  0.0188  -0.0731 345 TYR B CG  
5789 C CD1 . TYR B 336 ? 0.4813 0.3287 0.4247 0.0455  0.0038  -0.0894 345 TYR B CD1 
5790 C CD2 . TYR B 336 ? 0.4491 0.3422 0.4065 0.0065  0.0201  -0.0677 345 TYR B CD2 
5791 C CE1 . TYR B 336 ? 0.5629 0.3783 0.4904 0.0333  -0.0116 -0.0983 345 TYR B CE1 
5792 C CE2 . TYR B 336 ? 0.4938 0.3663 0.4401 -0.0073 0.0070  -0.0751 345 TYR B CE2 
5793 C CZ  . TYR B 336 ? 0.5229 0.3527 0.4530 0.0040  -0.0096 -0.0894 345 TYR B CZ  
5794 O OH  . TYR B 336 ? 0.6010 0.4055 0.5187 -0.0125 -0.0257 -0.0973 345 TYR B OH  
5795 N N   . HIS B 337 ? 0.3353 0.3165 0.3212 0.0336  0.0579  -0.0537 346 HIS B N   
5796 C CA  . HIS B 337 ? 0.3264 0.3233 0.3124 0.0282  0.0606  -0.0512 346 HIS B CA  
5797 C C   . HIS B 337 ? 0.3387 0.3513 0.3165 0.0379  0.0655  -0.0506 346 HIS B C   
5798 O O   . HIS B 337 ? 0.3490 0.3668 0.3185 0.0383  0.0620  -0.0537 346 HIS B O   
5799 C CB  . HIS B 337 ? 0.3074 0.3102 0.3035 0.0210  0.0628  -0.0423 346 HIS B CB  
5800 C CG  . HIS B 337 ? 0.3107 0.3257 0.3081 0.0218  0.0617  -0.0426 346 HIS B CG  
5801 N ND1 . HIS B 337 ? 0.3147 0.3298 0.3101 0.0272  0.0619  -0.0353 346 HIS B ND1 
5802 C CD2 . HIS B 337 ? 0.3090 0.3370 0.3100 0.0186  0.0580  -0.0494 346 HIS B CD2 
5803 C CE1 . HIS B 337 ? 0.2926 0.3116 0.2881 0.0315  0.0556  -0.0388 346 HIS B CE1 
5804 N NE2 . HIS B 337 ? 0.2714 0.3046 0.2729 0.0282  0.0544  -0.0490 346 HIS B NE2 
5805 N N   . LEU B 338 ? 0.3653 0.3902 0.3447 0.0443  0.0728  -0.0459 347 LEU B N   
5806 C CA  . LEU B 338 ? 0.3636 0.4103 0.3306 0.0496  0.0794  -0.0431 347 LEU B CA  
5807 C C   . LEU B 338 ? 0.3809 0.4286 0.3297 0.0599  0.0766  -0.0593 347 LEU B C   
5808 O O   . LEU B 338 ? 0.4017 0.4597 0.3333 0.0602  0.0765  -0.0571 347 LEU B O   
5809 C CB  . LEU B 338 ? 0.3738 0.4477 0.3491 0.0522  0.0896  -0.0371 347 LEU B CB  
5810 C CG  . LEU B 338 ? 0.4204 0.4995 0.4100 0.0385  0.0915  -0.0191 347 LEU B CG  
5811 C CD1 . LEU B 338 ? 0.4181 0.5366 0.4211 0.0404  0.1014  -0.0164 347 LEU B CD1 
5812 C CD2 . LEU B 338 ? 0.4031 0.4741 0.3802 0.0263  0.0883  -0.0030 347 LEU B CD2 
5813 N N   . GLN B 339 ? 0.3631 0.3956 0.3125 0.0686  0.0712  -0.0755 348 GLN B N   
5814 C CA  . GLN B 339 ? 0.4193 0.4424 0.3497 0.0783  0.0635  -0.0951 348 GLN B CA  
5815 C C   . GLN B 339 ? 0.3943 0.4048 0.3186 0.0656  0.0532  -0.0957 348 GLN B C   
5816 O O   . GLN B 339 ? 0.4604 0.4767 0.3665 0.0700  0.0485  -0.1053 348 GLN B O   
5817 C CB  . GLN B 339 ? 0.4659 0.4578 0.3966 0.0884  0.0523  -0.1121 348 GLN B CB  
5818 C CG  . GLN B 339 ? 0.5077 0.5122 0.4485 0.1074  0.0574  -0.1175 348 GLN B CG  
5819 C CD  . GLN B 339 ? 0.5771 0.5350 0.5154 0.1188  0.0385  -0.1329 348 GLN B CD  
5820 O OE1 . GLN B 339 ? 0.6587 0.6043 0.6109 0.1211  0.0341  -0.1264 348 GLN B OE1 
5821 N NE2 . GLN B 339 ? 0.6696 0.5955 0.5872 0.1247  0.0235  -0.1528 348 GLN B NE2 
5822 N N   . ILE B 340 ? 0.3708 0.3708 0.3111 0.0506  0.0494  -0.0867 349 ILE B N   
5823 C CA  . ILE B 340 ? 0.4020 0.4051 0.3449 0.0385  0.0409  -0.0875 349 ILE B CA  
5824 C C   . ILE B 340 ? 0.3980 0.4234 0.3347 0.0439  0.0424  -0.0810 349 ILE B C   
5825 O O   . ILE B 340 ? 0.4282 0.4610 0.3558 0.0443  0.0332  -0.0886 349 ILE B O   
5826 C CB  . ILE B 340 ? 0.3816 0.3826 0.3436 0.0222  0.0402  -0.0797 349 ILE B CB  
5827 C CG1 . ILE B 340 ? 0.4152 0.3858 0.3751 0.0119  0.0324  -0.0835 349 ILE B CG1 
5828 C CG2 . ILE B 340 ? 0.3738 0.3993 0.3460 0.0131  0.0352  -0.0809 349 ILE B CG2 
5829 C CD1 . ILE B 340 ? 0.4751 0.4265 0.4231 0.0034  0.0172  -0.0967 349 ILE B CD1 
5830 N N   . VAL B 341 ? 0.3954 0.4277 0.3347 0.0470  0.0508  -0.0662 350 VAL B N   
5831 C CA  . VAL B 341 ? 0.3913 0.4325 0.3184 0.0511  0.0480  -0.0557 350 VAL B CA  
5832 C C   . VAL B 341 ? 0.3936 0.4447 0.2931 0.0579  0.0485  -0.0593 350 VAL B C   
5833 O O   . VAL B 341 ? 0.4208 0.4765 0.3046 0.0610  0.0388  -0.0578 350 VAL B O   
5834 C CB  . VAL B 341 ? 0.3808 0.4176 0.3124 0.0481  0.0531  -0.0371 350 VAL B CB  
5835 C CG1 . VAL B 341 ? 0.4298 0.4630 0.3418 0.0501  0.0449  -0.0226 350 VAL B CG1 
5836 C CG2 . VAL B 341 ? 0.3396 0.3686 0.2933 0.0445  0.0505  -0.0379 350 VAL B CG2 
5837 N N   . THR B 342 ? 0.4147 0.4726 0.3071 0.0629  0.0584  -0.0658 351 THR B N   
5838 C CA  . THR B 342 ? 0.4253 0.5002 0.2885 0.0720  0.0605  -0.0745 351 THR B CA  
5839 C C   . THR B 342 ? 0.4491 0.5147 0.2999 0.0754  0.0452  -0.0939 351 THR B C   
5840 O O   . THR B 342 ? 0.5150 0.5922 0.3399 0.0789  0.0395  -0.0942 351 THR B O   
5841 C CB  . THR B 342 ? 0.4300 0.5213 0.2920 0.0828  0.0733  -0.0856 351 THR B CB  
5842 O OG1 . THR B 342 ? 0.4260 0.5348 0.3023 0.0759  0.0863  -0.0662 351 THR B OG1 
5843 C CG2 . THR B 342 ? 0.4760 0.5947 0.3045 0.0954  0.0775  -0.0991 351 THR B CG2 
5844 N N   . LYS B 343 ? 0.4486 0.4929 0.3160 0.0713  0.0368  -0.1080 352 LYS B N   
5845 C CA  . LYS B 343 ? 0.4559 0.4899 0.3147 0.0685  0.0197  -0.1266 352 LYS B CA  
5846 C C   . LYS B 343 ? 0.4459 0.4932 0.3126 0.0601  0.0086  -0.1195 352 LYS B C   
5847 O O   . LYS B 343 ? 0.4630 0.5184 0.3123 0.0625  -0.0040 -0.1291 352 LYS B O   
5848 C CB  . LYS B 343 ? 0.4694 0.4724 0.3418 0.0598  0.0111  -0.1390 352 LYS B CB  
5849 C CG  . LYS B 343 ? 0.4803 0.4677 0.3439 0.0503  -0.0098 -0.1576 352 LYS B CG  
5850 C CD  . LYS B 343 ? 0.4984 0.4463 0.3714 0.0351  -0.0215 -0.1640 352 LYS B CD  
5851 C CE  . LYS B 343 ? 0.5221 0.4606 0.3940 0.0138  -0.0435 -0.1751 352 LYS B CE  
5852 N NZ  . LYS B 343 ? 0.5077 0.3957 0.3787 -0.0047 -0.0601 -0.1805 352 LYS B NZ  
5853 N N   . TYR B 344 ? 0.4177 0.4702 0.3103 0.0531  0.0116  -0.1054 353 TYR B N   
5854 C CA  . TYR B 344 ? 0.4068 0.4781 0.3152 0.0491  -0.0002 -0.1043 353 TYR B CA  
5855 C C   . TYR B 344 ? 0.4380 0.5189 0.3364 0.0616  -0.0048 -0.0904 353 TYR B C   
5856 O O   . TYR B 344 ? 0.4199 0.5186 0.3255 0.0658  -0.0198 -0.0940 353 TYR B O   
5857 C CB  . TYR B 344 ? 0.3825 0.4598 0.3237 0.0365  0.0031  -0.1026 353 TYR B CB  
5858 C CG  . TYR B 344 ? 0.3560 0.4250 0.3043 0.0176  -0.0025 -0.1142 353 TYR B CG  
5859 C CD1 . TYR B 344 ? 0.3998 0.4361 0.3418 0.0125  0.0028  -0.1148 353 TYR B CD1 
5860 C CD2 . TYR B 344 ? 0.3897 0.4820 0.3501 0.0038  -0.0163 -0.1239 353 TYR B CD2 
5861 C CE1 . TYR B 344 ? 0.4256 0.4407 0.3684 -0.0068 -0.0078 -0.1227 353 TYR B CE1 
5862 C CE2 . TYR B 344 ? 0.4095 0.4882 0.3733 -0.0204 -0.0248 -0.1313 353 TYR B CE2 
5863 C CZ  . TYR B 344 ? 0.3880 0.4222 0.3403 -0.0260 -0.0216 -0.1297 353 TYR B CZ  
5864 O OH  . TYR B 344 ? 0.4346 0.4426 0.3850 -0.0514 -0.0350 -0.1343 353 TYR B OH  
5865 N N   . ILE B 345 ? 0.4394 0.5088 0.3210 0.0666  0.0055  -0.0744 354 ILE B N   
5866 C CA  . ILE B 345 ? 0.4763 0.5415 0.3409 0.0741  -0.0022 -0.0561 354 ILE B CA  
5867 C C   . ILE B 345 ? 0.5054 0.5716 0.3294 0.0749  0.0019  -0.0455 354 ILE B C   
5868 O O   . ILE B 345 ? 0.5549 0.6246 0.3529 0.0805  -0.0123 -0.0417 354 ILE B O   
5869 C CB  . ILE B 345 ? 0.4663 0.5156 0.3470 0.0730  0.0019  -0.0410 354 ILE B CB  
5870 C CG1 . ILE B 345 ? 0.4541 0.5132 0.3691 0.0765  -0.0049 -0.0534 354 ILE B CG1 
5871 C CG2 . ILE B 345 ? 0.5340 0.5636 0.3890 0.0771  -0.0096 -0.0181 354 ILE B CG2 
5872 C CD1 . ILE B 345 ? 0.4733 0.5187 0.4047 0.0772  -0.0011 -0.0466 354 ILE B CD1 
5873 N N   . LEU B 346 ? 0.5158 0.5851 0.3339 0.0697  0.0207  -0.0408 355 LEU B N   
5874 C CA  . LEU B 346 ? 0.5476 0.6314 0.3281 0.0678  0.0290  -0.0280 355 LEU B CA  
5875 C C   . LEU B 346 ? 0.5727 0.6737 0.3218 0.0758  0.0244  -0.0452 355 LEU B C   
5876 O O   . LEU B 346 ? 0.6027 0.7139 0.3133 0.0750  0.0204  -0.0319 355 LEU B O   
5877 C CB  . LEU B 346 ? 0.5504 0.6499 0.3381 0.0622  0.0514  -0.0242 355 LEU B CB  
5878 C CG  . LEU B 346 ? 0.5500 0.6359 0.3657 0.0520  0.0568  -0.0079 355 LEU B CG  
5879 C CD1 . LEU B 346 ? 0.5419 0.6570 0.3627 0.0476  0.0776  -0.0059 355 LEU B CD1 
5880 C CD2 . LEU B 346 ? 0.5814 0.6444 0.3845 0.0425  0.0442  0.0203  355 LEU B CD2 
5881 N N   . ILE B 347 ? 0.5687 0.6693 0.3301 0.0819  0.0225  -0.0740 356 ILE B N   
5882 C CA  . ILE B 347 ? 0.5963 0.7079 0.3271 0.0905  0.0153  -0.0964 356 ILE B CA  
5883 C C   . ILE B 347 ? 0.5954 0.7053 0.3134 0.0912  -0.0086 -0.0964 356 ILE B C   
5884 O O   . ILE B 347 ? 0.6475 0.7711 0.3243 0.0956  -0.0143 -0.0933 356 ILE B O   
5885 C CB  . ILE B 347 ? 0.5852 0.6859 0.3286 0.0963  0.0163  -0.1279 356 ILE B CB  
5886 C CG1 . ILE B 347 ? 0.6393 0.7543 0.3812 0.1046  0.0378  -0.1310 356 ILE B CG1 
5887 C CG2 . ILE B 347 ? 0.6654 0.7658 0.3793 0.1040  0.0001  -0.1553 356 ILE B CG2 
5888 C CD1 . ILE B 347 ? 0.6566 0.7492 0.4161 0.1131  0.0359  -0.1572 356 ILE B CD1 
5889 N N   . PRO B 348 ? 0.5634 0.6638 0.3159 0.0873  -0.0229 -0.1004 357 PRO B N   
5890 C CA  . PRO B 348 ? 0.5784 0.6866 0.3267 0.0908  -0.0469 -0.0993 357 PRO B CA  
5891 C C   . PRO B 348 ? 0.6080 0.7140 0.3254 0.0966  -0.0544 -0.0717 357 PRO B C   
5892 O O   . PRO B 348 ? 0.6335 0.7475 0.3194 0.1026  -0.0724 -0.0717 357 PRO B O   
5893 C CB  . PRO B 348 ? 0.5287 0.6381 0.3271 0.0860  -0.0526 -0.1024 357 PRO B CB  
5894 C CG  . PRO B 348 ? 0.5114 0.6113 0.3308 0.0758  -0.0383 -0.1151 357 PRO B CG  
5895 C CD  . PRO B 348 ? 0.5354 0.6251 0.3319 0.0795  -0.0183 -0.1075 357 PRO B CD  
5896 N N   . ALA B 349 ? 0.5820 0.6732 0.3053 0.0929  -0.0434 -0.0477 358 ALA B N   
5897 C CA  . ALA B 349 ? 0.6496 0.7265 0.3390 0.0925  -0.0516 -0.0164 358 ALA B CA  
5898 C C   . ALA B 349 ? 0.7220 0.8148 0.3554 0.0882  -0.0457 -0.0075 358 ALA B C   
5899 O O   . ALA B 349 ? 0.7990 0.8852 0.3938 0.0898  -0.0640 0.0109  358 ALA B O   
5900 C CB  . ALA B 349 ? 0.6124 0.6679 0.3173 0.0836  -0.0397 0.0056  358 ALA B CB  
5901 N N   . SER B 350 ? 0.7391 0.8548 0.3668 0.0846  -0.0217 -0.0216 359 SER B N   
5902 C CA  . SER B 350 ? 0.8123 0.9570 0.3875 0.0832  -0.0119 -0.0203 359 SER B CA  
5903 C C   . SER B 350 ? 0.8767 1.0311 0.4209 0.0943  -0.0317 -0.0412 359 SER B C   
5904 O O   . SER B 350 ? 0.9335 1.1049 0.4236 0.0930  -0.0350 -0.0300 359 SER B O   
5905 C CB  . SER B 350 ? 0.7860 0.9587 0.3693 0.0846  0.0167  -0.0393 359 SER B CB  
5906 O OG  . SER B 350 ? 0.7367 0.9067 0.3376 0.0978  0.0125  -0.0790 359 SER B OG  
5907 N N   . GLN B 351 ? 0.8859 1.0316 0.4630 0.1019  -0.0454 -0.0704 360 GLN B N   
5908 C CA  . GLN B 351 ? 0.9419 1.0958 0.4979 0.1098  -0.0680 -0.0944 360 GLN B CA  
5909 C C   . GLN B 351 ? 0.9947 1.1432 0.5420 0.1136  -0.0992 -0.0792 360 GLN B C   
5910 O O   . GLN B 351 ? 1.0352 1.1949 0.5645 0.1193  -0.1208 -0.0975 360 GLN B O   
5911 C CB  . GLN B 351 ? 0.9020 1.0485 0.4984 0.1101  -0.0725 -0.1299 360 GLN B CB  
5912 C CG  . GLN B 351 ? 0.9097 1.0542 0.5089 0.1125  -0.0502 -0.1513 360 GLN B CG  
5913 C CD  . GLN B 351 ? 0.8742 0.9957 0.5185 0.1069  -0.0552 -0.1742 360 GLN B CD  
5914 O OE1 . GLN B 351 ? 0.8997 1.0139 0.5847 0.0969  -0.0638 -0.1661 360 GLN B OE1 
5915 N NE2 . GLN B 351 ? 0.7864 0.8968 0.4214 0.1137  -0.0507 -0.2026 360 GLN B NE2 
5916 N N   A GLN B 352 ? 1.0045 1.1343 0.5651 0.1126  -0.1049 -0.0488 361 GLN B N   
5917 N N   B GLN B 352 ? 1.0059 1.1358 0.5634 0.1123  -0.1041 -0.0476 361 GLN B N   
5918 C CA  A GLN B 352 ? 1.0389 1.1601 0.5967 0.1228  -0.1384 -0.0369 361 GLN B CA  
5919 C CA  B GLN B 352 ? 1.0391 1.1583 0.5950 0.1222  -0.1370 -0.0339 361 GLN B CA  
5920 C C   A GLN B 352 ? 1.1279 1.2459 0.6152 0.1232  -0.1523 -0.0116 361 GLN B C   
5921 C C   B GLN B 352 ? 1.1287 1.2466 0.6140 0.1229  -0.1520 -0.0106 361 GLN B C   
5922 O O   A GLN B 352 ? 1.1648 1.2802 0.6136 0.1108  -0.1332 0.0121  361 GLN B O   
5923 O O   B GLN B 352 ? 1.1670 1.2836 0.6116 0.1106  -0.1333 0.0126  361 GLN B O   
5924 C CB  A GLN B 352 ? 1.0168 1.1130 0.6155 0.1270  -0.1439 -0.0196 361 GLN B CB  
5925 C CB  B GLN B 352 ? 1.0197 1.1102 0.6090 0.1239  -0.1391 -0.0115 361 GLN B CB  
5926 C CG  A GLN B 352 ? 1.0454 1.1074 0.6140 0.1201  -0.1408 0.0203  361 GLN B CG  
5927 C CG  B GLN B 352 ? 1.0025 1.0931 0.6319 0.1413  -0.1681 -0.0203 361 GLN B CG  
5928 C CD  A GLN B 352 ? 1.0016 1.0372 0.6157 0.1221  -0.1384 0.0274  361 GLN B CD  
5929 C CD  B GLN B 352 ? 0.9176 1.0377 0.6075 0.1402  -0.1609 -0.0538 361 GLN B CD  
5930 O OE1 A GLN B 352 ? 0.9709 1.0067 0.6245 0.1387  -0.1565 0.0136  361 GLN B OE1 
5931 O OE1 B GLN B 352 ? 0.8959 1.0275 0.5925 0.1272  -0.1405 -0.0718 361 GLN B OE1 
5932 N NE2 A GLN B 352 ? 0.9715 0.9903 0.5805 0.1057  -0.1165 0.0471  361 GLN B NE2 
5933 N NE2 B GLN B 352 ? 0.8492 0.9825 0.5821 0.1541  -0.1794 -0.0620 361 GLN B NE2 
5934 N N   . PRO B 353 ? 1.1710 1.2944 0.6405 0.1354  -0.1861 -0.0154 362 PRO B N   
5935 C CA  . PRO B 353 ? 1.2559 1.3732 0.6529 0.1357  -0.2044 0.0115  362 PRO B CA  
5936 C C   . PRO B 353 ? 1.3047 1.3778 0.6849 0.1353  -0.2206 0.0562  362 PRO B C   
5937 O O   . PRO B 353 ? 1.3258 1.3822 0.6821 0.1172  -0.2002 0.0854  362 PRO B O   
5938 C CB  . PRO B 353 ? 1.2869 1.4236 0.6821 0.1511  -0.2397 -0.0112 362 PRO B CB  
5939 C CG  . PRO B 353 ? 1.2175 1.3605 0.6912 0.1607  -0.2483 -0.0332 362 PRO B CG  
5940 C CD  . PRO B 353 ? 1.1454 1.2866 0.6607 0.1478  -0.2106 -0.0440 362 PRO B CD  
5941 N N   . GLY B 371 ? 0.9237 0.7125 0.5918 0.0002  -0.0938 0.1795  380 GLY B N   
5942 C CA  . GLY B 371 ? 0.8412 0.6477 0.5575 0.0298  -0.0890 0.1387  380 GLY B CA  
5943 C C   . GLY B 371 ? 0.7628 0.6288 0.5121 0.0236  -0.0522 0.1180  380 GLY B C   
5944 O O   . GLY B 371 ? 0.6912 0.5564 0.4721 0.0214  -0.0431 0.1074  380 GLY B O   
5945 N N   . GLY B 372 ? 0.7544 0.6679 0.4929 0.0226  -0.0341 0.1116  381 GLY B N   
5946 C CA  . GLY B 372 ? 0.6964 0.6599 0.4615 0.0218  -0.0043 0.0896  381 GLY B CA  
5947 C C   . GLY B 372 ? 0.6900 0.6679 0.4663 -0.0004 0.0153  0.1022  381 GLY B C   
5948 O O   . GLY B 372 ? 0.6432 0.6348 0.4543 0.0029  0.0282  0.0848  381 GLY B O   
5949 N N   . THR B 373 ? 0.7368 0.7140 0.4827 -0.0252 0.0157  0.1345  382 THR B N   
5950 C CA  . THR B 373 ? 0.7301 0.7258 0.4870 -0.0523 0.0309  0.1518  382 THR B CA  
5951 C C   . THR B 373 ? 0.6931 0.6432 0.4772 -0.0555 0.0171  0.1519  382 THR B C   
5952 O O   . THR B 373 ? 0.6561 0.6293 0.4722 -0.0605 0.0316  0.1425  382 THR B O   
5953 C CB  . THR B 373 ? 0.8022 0.8061 0.5162 -0.0855 0.0305  0.1923  382 THR B CB  
5954 O OG1 . THR B 373 ? 0.8575 0.9225 0.5492 -0.0823 0.0508  0.1866  382 THR B OG1 
5955 C CG2 . THR B 373 ? 0.8122 0.8328 0.5399 -0.1207 0.0406  0.2151  382 THR B CG2 
5956 N N   . ASP B 374 ? 0.7098 0.5954 0.4795 -0.0497 -0.0132 0.1604  383 ASP B N   
5957 C CA  . ASP B 374 ? 0.7128 0.5498 0.5029 -0.0474 -0.0305 0.1553  383 ASP B CA  
5958 C C   . ASP B 374 ? 0.6167 0.4757 0.4483 -0.0239 -0.0186 0.1188  383 ASP B C   
5959 O O   . ASP B 374 ? 0.5662 0.4227 0.4210 -0.0315 -0.0146 0.1139  383 ASP B O   
5960 C CB  . ASP B 374 ? 0.7636 0.5278 0.5297 -0.0339 -0.0685 0.1625  383 ASP B CB  
5961 C CG  . ASP B 374 ? 0.9289 0.6482 0.6503 -0.0643 -0.0887 0.2055  383 ASP B CG  
5962 O OD1 . ASP B 374 ? 1.0082 0.7512 0.7226 -0.1022 -0.0736 0.2313  383 ASP B OD1 
5963 O OD2 . ASP B 374 ? 1.0528 0.7135 0.7454 -0.0508 -0.1218 0.2144  383 ASP B OD2 
5964 N N   . LEU B 375 ? 0.5761 0.4573 0.4147 0.0011  -0.0144 0.0954  384 LEU B N   
5965 C CA  . LEU B 375 ? 0.5439 0.4478 0.4170 0.0184  -0.0037 0.0646  384 LEU B CA  
5966 C C   . LEU B 375 ? 0.5044 0.4482 0.3971 0.0068  0.0219  0.0601  384 LEU B C   
5967 O O   . LEU B 375 ? 0.4841 0.4287 0.4010 0.0081  0.0260  0.0485  384 LEU B O   
5968 C CB  . LEU B 375 ? 0.5371 0.4612 0.4121 0.0397  -0.0054 0.0444  384 LEU B CB  
5969 C CG  . LEU B 375 ? 0.5897 0.4869 0.4567 0.0604  -0.0321 0.0394  384 LEU B CG  
5970 C CD1 . LEU B 375 ? 0.5996 0.5314 0.4708 0.0750  -0.0311 0.0212  384 LEU B CD1 
5971 C CD2 . LEU B 375 ? 0.5696 0.4459 0.4580 0.0746  -0.0443 0.0241  384 LEU B CD2 
5972 N N   . MET B 376 ? 0.5002 0.4789 0.3807 -0.0017 0.0374  0.0677  385 MET B N   
5973 C CA  . MET B 376 ? 0.4780 0.4983 0.3772 -0.0068 0.0591  0.0611  385 MET B CA  
5974 C C   . MET B 376 ? 0.4553 0.4780 0.3667 -0.0282 0.0618  0.0780  385 MET B C   
5975 O O   . MET B 376 ? 0.4230 0.4640 0.3605 -0.0270 0.0707  0.0676  385 MET B O   
5976 C CB  . MET B 376 ? 0.5080 0.5709 0.3895 -0.0057 0.0741  0.0604  385 MET B CB  
5977 C CG  . MET B 376 ? 0.5245 0.5895 0.3980 0.0148  0.0718  0.0382  385 MET B CG  
5978 S SD  . MET B 376 ? 0.5109 0.5774 0.4160 0.0300  0.0764  0.0081  385 MET B SD  
5979 C CE  . MET B 376 ? 0.4938 0.6052 0.4007 0.0358  0.0954  -0.0024 385 MET B CE  
5980 N N   . ASN B 377 ? 0.4919 0.4938 0.3831 -0.0496 0.0512  0.1052  386 ASN B N   
5981 C CA  . ASN B 377 ? 0.5075 0.5068 0.4102 -0.0759 0.0491  0.1230  386 ASN B CA  
5982 C C   . ASN B 377 ? 0.4804 0.4421 0.4044 -0.0687 0.0358  0.1091  386 ASN B C   
5983 O O   . ASN B 377 ? 0.4182 0.3997 0.3663 -0.0782 0.0420  0.1068  386 ASN B O   
5984 C CB  . ASN B 377 ? 0.5554 0.5279 0.4266 -0.1058 0.0351  0.1585  386 ASN B CB  
5985 C CG  . ASN B 377 ? 0.6075 0.6376 0.4586 -0.1226 0.0541  0.1767  386 ASN B CG  
5986 O OD1 . ASN B 377 ? 0.6058 0.6203 0.4238 -0.1493 0.0447  0.2089  386 ASN B OD1 
5987 N ND2 . ASN B 377 ? 0.5188 0.6142 0.3865 -0.1065 0.0793  0.1556  386 ASN B ND2 
5988 N N   . PHE B 378 ? 0.4867 0.4016 0.4021 -0.0495 0.0177  0.0975  387 PHE B N   
5989 C CA  . PHE B 378 ? 0.4642 0.3522 0.3966 -0.0372 0.0071  0.0784  387 PHE B CA  
5990 C C   . PHE B 378 ? 0.4089 0.3373 0.3679 -0.0268 0.0258  0.0578  387 PHE B C   
5991 O O   . PHE B 378 ? 0.3843 0.3140 0.3594 -0.0329 0.0256  0.0535  387 PHE B O   
5992 C CB  . PHE B 378 ? 0.4794 0.3300 0.4014 -0.0121 -0.0118 0.0637  387 PHE B CB  
5993 C CG  . PHE B 378 ? 0.4597 0.3074 0.4004 0.0059  -0.0145 0.0371  387 PHE B CG  
5994 C CD1 . PHE B 378 ? 0.4722 0.2898 0.4162 -0.0004 -0.0274 0.0345  387 PHE B CD1 
5995 C CD2 . PHE B 378 ? 0.3942 0.2731 0.3474 0.0255  -0.0039 0.0151  387 PHE B CD2 
5996 C CE1 . PHE B 378 ? 0.4634 0.2848 0.4199 0.0161  -0.0284 0.0090  387 PHE B CE1 
5997 C CE2 . PHE B 378 ? 0.3885 0.2741 0.3557 0.0378  -0.0041 -0.0068 387 PHE B CE2 
5998 C CZ  . PHE B 378 ? 0.3899 0.2492 0.3576 0.0347  -0.0151 -0.0107 387 PHE B CZ  
5999 N N   . LEU B 379 ? 0.3903 0.3467 0.3507 -0.0123 0.0386  0.0458  388 LEU B N   
6000 C CA  . LEU B 379 ? 0.3383 0.3214 0.3180 -0.0035 0.0515  0.0286  388 LEU B CA  
6001 C C   . LEU B 379 ? 0.3170 0.3318 0.3120 -0.0142 0.0633  0.0347  388 LEU B C   
6002 O O   . LEU B 379 ? 0.3069 0.3273 0.3184 -0.0116 0.0647  0.0260  388 LEU B O   
6003 C CB  . LEU B 379 ? 0.3377 0.3364 0.3123 0.0107  0.0582  0.0157  388 LEU B CB  
6004 C CG  . LEU B 379 ? 0.3392 0.3217 0.3077 0.0232  0.0471  0.0051  388 LEU B CG  
6005 C CD1 . LEU B 379 ? 0.3326 0.3329 0.2945 0.0311  0.0517  -0.0044 388 LEU B CD1 
6006 C CD2 . LEU B 379 ? 0.3132 0.2914 0.2962 0.0284  0.0438  -0.0092 388 LEU B CD2 
6007 N N   . LYS B 380 ? 0.3525 0.3929 0.3417 -0.0259 0.0709  0.0496  389 LYS B N   
6008 C CA  . LYS B 380 ? 0.3497 0.4350 0.3580 -0.0351 0.0824  0.0544  389 LYS B CA  
6009 C C   . LYS B 380 ? 0.3580 0.4344 0.3814 -0.0541 0.0730  0.0647  389 LYS B C   
6010 O O   . LYS B 380 ? 0.3150 0.4205 0.3622 -0.0535 0.0772  0.0592  389 LYS B O   
6011 C CB  . LYS B 380 ? 0.3888 0.5163 0.3858 -0.0454 0.0949  0.0679  389 LYS B CB  
6012 C CG  . LYS B 380 ? 0.4046 0.5562 0.3911 -0.0229 0.1064  0.0508  389 LYS B CG  
6013 C CD  . LYS B 380 ? 0.4500 0.6468 0.4181 -0.0337 0.1191  0.0641  389 LYS B CD  
6014 C CE  . LYS B 380 ? 0.5204 0.7369 0.4718 -0.0099 0.1276  0.0438  389 LYS B CE  
6015 N NZ  . LYS B 380 ? 0.5435 0.8055 0.4686 -0.0217 0.1398  0.0579  389 LYS B NZ  
6016 N N   . THR B 381 ? 0.3576 0.3903 0.3661 -0.0694 0.0569  0.0781  390 THR B N   
6017 C CA  . THR B 381 ? 0.3886 0.4003 0.4070 -0.0877 0.0424  0.0847  390 THR B CA  
6018 C C   . THR B 381 ? 0.3703 0.3700 0.4016 -0.0706 0.0380  0.0629  390 THR B C   
6019 O O   . THR B 381 ? 0.3474 0.3624 0.3971 -0.0794 0.0353  0.0622  390 THR B O   
6020 C CB  . THR B 381 ? 0.4348 0.3844 0.4284 -0.1021 0.0194  0.0990  390 THR B CB  
6021 O OG1 . THR B 381 ? 0.4500 0.4103 0.4270 -0.1246 0.0221  0.1254  390 THR B OG1 
6022 C CG2 . THR B 381 ? 0.4356 0.3539 0.4362 -0.1206 -0.0001 0.1018  390 THR B CG2 
6023 N N   . VAL B 382 ? 0.3752 0.3530 0.3962 -0.0482 0.0370  0.0463  391 VAL B N   
6024 C CA  . VAL B 382 ? 0.3472 0.3177 0.3743 -0.0350 0.0343  0.0279  391 VAL B CA  
6025 C C   . VAL B 382 ? 0.3409 0.3488 0.3846 -0.0289 0.0467  0.0229  391 VAL B C   
6026 O O   . VAL B 382 ? 0.3059 0.3169 0.3586 -0.0296 0.0422  0.0181  391 VAL B O   
6027 C CB  . VAL B 382 ? 0.3658 0.3155 0.3795 -0.0163 0.0312  0.0127  391 VAL B CB  
6028 C CG1 . VAL B 382 ? 0.3571 0.3121 0.3745 -0.0071 0.0324  -0.0037 391 VAL B CG1 
6029 C CG2 . VAL B 382 ? 0.3801 0.2872 0.3783 -0.0154 0.0126  0.0135  391 VAL B CG2 
6030 N N   . ARG B 383 ? 0.3316 0.3643 0.3765 -0.0210 0.0594  0.0229  392 ARG B N   
6031 C CA  . ARG B 383 ? 0.3343 0.3968 0.3936 -0.0111 0.0669  0.0167  392 ARG B CA  
6032 C C   . ARG B 383 ? 0.3408 0.4363 0.4224 -0.0217 0.0659  0.0245  392 ARG B C   
6033 O O   . ARG B 383 ? 0.3157 0.4196 0.4102 -0.0153 0.0612  0.0189  392 ARG B O   
6034 C CB  . ARG B 383 ? 0.3152 0.3981 0.3696 0.0008  0.0781  0.0121  392 ARG B CB  
6035 C CG  . ARG B 383 ? 0.2889 0.3878 0.3538 0.0184  0.0803  -0.0002 392 ARG B CG  
6036 C CD  . ARG B 383 ? 0.3412 0.4699 0.4037 0.0319  0.0905  -0.0078 392 ARG B CD  
6037 N NE  . ARG B 383 ? 0.3342 0.4874 0.4133 0.0512  0.0897  -0.0200 392 ARG B NE  
6038 C CZ  . ARG B 383 ? 0.3742 0.5722 0.4783 0.0512  0.0918  -0.0170 392 ARG B CZ  
6039 N NH1 . ARG B 383 ? 0.4108 0.6334 0.5256 0.0270  0.0954  0.0000  392 ARG B NH1 
6040 N NH2 . ARG B 383 ? 0.3899 0.6082 0.5091 0.0760  0.0876  -0.0321 392 ARG B NH2 
6041 N N   . SER B 384 ? 0.3649 0.4812 0.4503 -0.0398 0.0690  0.0391  393 SER B N   
6042 C CA  . SER B 384 ? 0.3690 0.5285 0.4795 -0.0562 0.0687  0.0487  393 SER B CA  
6043 C C   . SER B 384 ? 0.3863 0.5247 0.5051 -0.0665 0.0520  0.0484  393 SER B C   
6044 O O   . SER B 384 ? 0.3617 0.5360 0.5050 -0.0663 0.0492  0.0463  393 SER B O   
6045 C CB  . SER B 384 ? 0.3867 0.5651 0.4931 -0.0837 0.0727  0.0698  393 SER B CB  
6046 O OG  . SER B 384 ? 0.4216 0.6498 0.5554 -0.1055 0.0723  0.0805  393 SER B OG  
6047 N N   . THR B 385 ? 0.3820 0.4649 0.4799 -0.0729 0.0392  0.0481  394 THR B N   
6048 C CA  . THR B 385 ? 0.4097 0.4672 0.5079 -0.0795 0.0220  0.0429  394 THR B CA  
6049 C C   . THR B 385 ? 0.3725 0.4389 0.4755 -0.0598 0.0221  0.0292  394 THR B C   
6050 O O   . THR B 385 ? 0.3452 0.4205 0.4588 -0.0651 0.0109  0.0276  394 THR B O   
6051 C CB  . THR B 385 ? 0.4080 0.4047 0.4793 -0.0794 0.0086  0.0373  394 THR B CB  
6052 O OG1 . THR B 385 ? 0.4615 0.4386 0.5233 -0.0972 0.0033  0.0530  394 THR B OG1 
6053 C CG2 . THR B 385 ? 0.4684 0.4400 0.5361 -0.0851 -0.0105 0.0281  394 THR B CG2 
6054 N N   . THR B 386 ? 0.3463 0.4073 0.4388 -0.0399 0.0320  0.0211  395 THR B N   
6055 C CA  . THR B 386 ? 0.3432 0.4045 0.4341 -0.0244 0.0303  0.0127  395 THR B CA  
6056 C C   . THR B 386 ? 0.3224 0.4246 0.4383 -0.0165 0.0305  0.0143  395 THR B C   
6057 O O   . THR B 386 ? 0.3135 0.4207 0.4359 -0.0135 0.0190  0.0129  395 THR B O   
6058 C CB  . THR B 386 ? 0.3456 0.3887 0.4190 -0.0107 0.0387  0.0061  395 THR B CB  
6059 O OG1 . THR B 386 ? 0.3417 0.3610 0.3989 -0.0148 0.0397  0.0033  395 THR B OG1 
6060 C CG2 . THR B 386 ? 0.3615 0.3906 0.4235 -0.0035 0.0327  0.0017  395 THR B CG2 
6061 N N   . GLU B 387 ? 0.3314 0.4663 0.4603 -0.0107 0.0427  0.0154  396 GLU B N   
6062 C CA  . GLU B 387 ? 0.3368 0.5224 0.4931 0.0032  0.0443  0.0118  396 GLU B CA  
6063 C C   . GLU B 387 ? 0.3451 0.5706 0.5295 -0.0114 0.0354  0.0182  396 GLU B C   
6064 O O   . GLU B 387 ? 0.3301 0.5875 0.5363 0.0037  0.0276  0.0125  396 GLU B O   
6065 C CB  . GLU B 387 ? 0.3261 0.5497 0.4885 0.0099  0.0615  0.0098  396 GLU B CB  
6066 C CG  . GLU B 387 ? 0.3694 0.6401 0.5533 0.0388  0.0641  -0.0042 396 GLU B CG  
6067 C CD  . GLU B 387 ? 0.4420 0.7930 0.6653 0.0337  0.0670  -0.0017 396 GLU B CD  
6068 O OE1 . GLU B 387 ? 0.4677 0.8466 0.6994 0.0022  0.0733  0.0141  396 GLU B OE1 
6069 O OE2 . GLU B 387 ? 0.5324 0.9194 0.7788 0.0611  0.0609  -0.0155 396 GLU B OE2 
6070 N N   . LYS B 388 ? 0.3701 0.5903 0.5533 -0.0406 0.0332  0.0298  397 LYS B N   
6071 C CA  . LYS B 388 ? 0.3934 0.6496 0.6029 -0.0625 0.0226  0.0375  397 LYS B CA  
6072 C C   . LYS B 388 ? 0.3908 0.6176 0.5945 -0.0631 0.0015  0.0325  397 LYS B C   
6073 O O   . LYS B 388 ? 0.3818 0.6396 0.6085 -0.0784 -0.0111 0.0361  397 LYS B O   
6074 C CB  . LYS B 388 ? 0.4237 0.6790 0.6309 -0.0979 0.0245  0.0540  397 LYS B CB  
6075 C CG  . LYS B 388 ? 0.4445 0.7603 0.6662 -0.1035 0.0447  0.0628  397 LYS B CG  
6076 C CD  . LYS B 388 ? 0.4964 0.8105 0.7120 -0.1449 0.0440  0.0855  397 LYS B CD  
6077 C CE  . LYS B 388 ? 0.5167 0.9242 0.7594 -0.1610 0.0620  0.0976  397 LYS B CE  
6078 N NZ  . LYS B 388 ? 0.4881 0.9319 0.7263 -0.1307 0.0847  0.0866  397 LYS B NZ  
6079 N N   . SER B 389 ? 0.3739 0.5472 0.5463 -0.0483 -0.0021 0.0246  398 SER B N   
6080 C CA  . SER B 389 ? 0.3776 0.5286 0.5375 -0.0447 -0.0198 0.0194  398 SER B CA  
6081 C C   . SER B 389 ? 0.3586 0.5286 0.5281 -0.0207 -0.0269 0.0160  398 SER B C   
6082 O O   . SER B 389 ? 0.3573 0.5156 0.5169 -0.0188 -0.0441 0.0149  398 SER B O   
6083 C CB  . SER B 389 ? 0.3946 0.4894 0.5149 -0.0429 -0.0195 0.0134  398 SER B CB  
6084 O OG  . SER B 389 ? 0.4288 0.5003 0.5399 -0.0595 -0.0194 0.0136  398 SER B OG  
6085 N N   . LEU B 390 ? 0.3420 0.5376 0.5270 -0.0008 -0.0166 0.0133  399 LEU B N   
6086 C CA  . LEU B 390 ? 0.3401 0.5509 0.5368 0.0268  -0.0285 0.0080  399 LEU B CA  
6087 C C   . LEU B 390 ? 0.3347 0.5995 0.5669 0.0246  -0.0439 0.0086  399 LEU B C   
6088 O O   . LEU B 390 ? 0.3281 0.6483 0.5927 0.0084  -0.0368 0.0111  399 LEU B O   
6089 C CB  . LEU B 390 ? 0.3236 0.5556 0.5326 0.0518  -0.0162 -0.0005 399 LEU B CB  
6090 C CG  . LEU B 390 ? 0.3154 0.4942 0.4911 0.0603  -0.0073 -0.0037 399 LEU B CG  
6091 C CD1 . LEU B 390 ? 0.3348 0.5445 0.5251 0.0825  0.0050  -0.0154 399 LEU B CD1 
6092 C CD2 . LEU B 390 ? 0.3319 0.4546 0.4784 0.0715  -0.0252 -0.0024 399 LEU B CD2 
6093 N N   . LEU B 391 ? 0.3585 0.6091 0.5837 0.0383  -0.0664 0.0080  400 LEU B N   
6094 C CA  . LEU B 391 ? 0.3798 0.6828 0.6389 0.0388  -0.0856 0.0075  400 LEU B CA  
6095 C C   . LEU B 391 ? 0.3820 0.7536 0.6863 0.0681  -0.0846 -0.0023 400 LEU B C   
6096 O O   . LEU B 391 ? 0.3727 0.8222 0.7226 0.0603  -0.0853 -0.0039 400 LEU B O   
6097 C CB  . LEU B 391 ? 0.4017 0.6648 0.6326 0.0455  -0.1126 0.0109  400 LEU B CB  
6098 C CG  . LEU B 391 ? 0.3964 0.6006 0.5793 0.0210  -0.1130 0.0163  400 LEU B CG  
6099 C CD1 . LEU B 391 ? 0.4741 0.6446 0.6235 0.0292  -0.1380 0.0214  400 LEU B CD1 
6100 C CD2 . LEU B 391 ? 0.3905 0.6130 0.5845 -0.0109 -0.1120 0.0155  400 LEU B CD2 
6101 N N   . LYS B 392 ? 0.4187 0.7621 0.7096 0.1013  -0.0842 -0.0101 401 LYS B N   
6102 C CA  . LYS B 392 ? 0.4403 0.8387 0.7664 0.1387  -0.0832 -0.0260 401 LYS B CA  
6103 C C   . LYS B 392 ? 0.4391 0.8279 0.7534 0.1430  -0.0568 -0.0327 401 LYS B C   
6104 O O   . LYS B 392 ? 0.4136 0.7316 0.6860 0.1298  -0.0496 -0.0258 401 LYS B O   
6105 C CB  . LYS B 392 ? 0.4875 0.8428 0.7994 0.1782  -0.1136 -0.0320 401 LYS B CB  
6106 C CG  . LYS B 392 ? 0.4906 0.8979 0.8390 0.2266  -0.1214 -0.0539 401 LYS B CG  
6107 C CD  . LYS B 392 ? 0.5620 0.9039 0.8870 0.2650  -0.1582 -0.0573 401 LYS B CD  
6108 C CE  . LYS B 392 ? 0.6010 0.9988 0.9670 0.3214  -0.1722 -0.0843 401 LYS B CE  
6109 N NZ  . LYS B 392 ? 0.6613 0.9814 1.0005 0.3613  -0.2148 -0.0867 401 LYS B NZ  
6110 N N   . GLU B 393 ? 0.4492 0.9153 0.8003 0.1621  -0.0429 -0.0473 402 GLU B N   
6111 C CA  . GLU B 393 ? 0.4501 0.9154 0.7888 0.1700  -0.0191 -0.0565 402 GLU B CA  
6112 C C   . GLU B 393 ? 0.4884 0.8643 0.7858 0.1966  -0.0305 -0.0649 402 GLU B C   
6113 O O   . GLU B 393 ? 0.5364 0.8904 0.8345 0.2333  -0.0554 -0.0766 402 GLU B O   
6114 C CB  . GLU B 393 ? 0.4382 1.0090 0.8213 0.1958  -0.0057 -0.0761 402 GLU B CB  
6115 C CG  . GLU B 393 ? 0.3690 1.0304 0.7832 0.1583  0.0181  -0.0646 402 GLU B CG  
6116 C CD  . GLU B 393 ? 0.3957 1.1740 0.8527 0.1840  0.0338  -0.0850 402 GLU B CD  
6117 O OE1 . GLU B 393 ? 0.2711 1.0465 0.7134 0.2162  0.0440  -0.1050 402 GLU B OE1 
6118 O OE2 . GLU B 393 ? 0.3692 1.2472 0.8747 0.1723  0.0354  -0.0827 402 GLU B OE2 
6119 N N   . GLY B 394 ? 0.4909 0.8153 0.7531 0.1774  -0.0151 -0.0586 403 GLY B N   
6120 C CA  . GLY B 394 ? 0.5361 0.7742 0.7575 0.1913  -0.0254 -0.0631 403 GLY B CA  
6121 C C   . GLY B 394 ? 0.5742 0.8173 0.7980 0.2336  -0.0282 -0.0890 403 GLY B C   
6122 O O   . GLY B 394 ? 0.5520 0.8715 0.8115 0.2614  -0.0244 -0.1074 403 GLY B O   
# 
