data_9D7L
# 
_entry.id   9D7L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9D7L         pdb_00009d7l 10.2210/pdb9d7l/pdb 
WWPDB D_1000285004 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-02-05 
2 'Structure model' 1 1 2025-02-19 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9D7L 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              tannerjj@missouri.edu 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Tanner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8314-113X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tanner, J.J.' 1 ? 
'Meeks, K.R.'  2 ? 
'Ji, J.'       3 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_id_ASTM           ABBIA4 
_citation.journal_id_CSD            0158 
_citation.journal_id_ISSN           1096-0384 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            765 
_citation.language                  ? 
_citation.page_first                110319 
_citation.page_last                 110319 
_citation.title                     
;Biochemical, structural, and cellular characterization of S-but-3-yn-2-ylglycine as a mechanism-based covalent inactivator of the flavoenzyme proline dehydrogenase.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2025.110319 
_citation.pdbx_database_id_PubMed   39870289 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Meeks, K.R.'    1 ? 
primary 'Ji, J.'         2 ? 
primary 'Scott, G.K.'    3 ? 
primary 'Campbell, A.C.' 4 ? 
primary 'Nix, J.C.'      5 ? 
primary 'Tadeo, A.'      6 ? 
primary 'Ellerby, L.M.'  7 ? 
primary 'Benz, C.C.'     8 ? 
primary 'Tanner, J.J.'   9 ? 
# 
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 'Bifunctional protein PutA' 43773.988 2   1.5.5.2,1.2.1.88 'residues 84-189 replaced by SSGS' ? ? 
2 non-polymer syn 
;{[(3E)-4-{10-[(2S,3S,4R)-5-{[(R)-{[(R)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-2,3,4-trihydroxypentyl]-7,8-dimethyl-2,4-dioxo-2,3,4,10-tetrahydrobenzo[g]pteridin-5(1H)-yl}but-3-en-2-ylidene]amino}acetic acid (non-preferred name)
;
912.691   2   ?                ?                                  ? ? 
3 non-polymer syn 'FORMIC ACID' 46.025    2   ?                ?                                  ? ? 
4 water       nat water 18.015    258 ?                ?                                  ? ? 
# 
_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       
;SRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGKHSGSGSSGSMMGEQFVTGETIREALK
RSKELEEKGFSYSYDMLGEAATTAADAERYYRDYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELL
PRVKALALLAKNYDIGLNIDAEEADRLELSLDLLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMV
RLVKGAYWDAEIKRAQLDGLADFPVFTRKIHTDVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEF
QCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGKHSGSGSSGSMMGEQFVTGETIREALK
RSKELEEKGFSYSYDMLGEAATTAADAERYYRDYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELL
PRVKALALLAKNYDIGLNIDAEEADRLELSLDLLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMV
RLVKGAYWDAEIKRAQLDGLADFPVFTRKIHTDVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEF
QCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVR
;
_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 
;{[(3E)-4-{10-[(2S,3S,4R)-5-{[(R)-{[(R)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-2,3,4-trihydroxypentyl]-7,8-dimethyl-2,4-dioxo-2,3,4,10-tetrahydrobenzo[g]pteridin-5(1H)-yl}but-3-en-2-ylidene]amino}acetic acid (non-preferred name)
;
A1BC6 
3 'FORMIC ACID' FMT   
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ARG n 
1 3   PRO n 
1 4   GLN n 
1 5   SER n 
1 6   THR n 
1 7   LEU n 
1 8   ARG n 
1 9   ARG n 
1 10  ALA n 
1 11  ILE n 
1 12  THR n 
1 13  ALA n 
1 14  ALA n 
1 15  TYR n 
1 16  ARG n 
1 17  ARG n 
1 18  PRO n 
1 19  GLU n 
1 20  THR n 
1 21  GLU n 
1 22  CYS n 
1 23  LEU n 
1 24  PRO n 
1 25  PRO n 
1 26  LEU n 
1 27  VAL n 
1 28  GLU n 
1 29  ALA n 
1 30  ALA n 
1 31  THR n 
1 32  GLN n 
1 33  SER n 
1 34  LYS n 
1 35  GLU n 
1 36  ILE n 
1 37  ARG n 
1 38  ASP n 
1 39  ALA n 
1 40  ALA n 
1 41  ALA n 
1 42  SER n 
1 43  THR n 
1 44  ALA n 
1 45  ARG n 
1 46  LYS n 
1 47  LEU n 
1 48  ILE n 
1 49  GLU n 
1 50  ALA n 
1 51  LEU n 
1 52  ARG n 
1 53  GLY n 
1 54  LYS n 
1 55  HIS n 
1 56  SER n 
1 57  GLY n 
1 58  SER n 
1 59  GLY n 
1 60  SER n 
1 61  SER n 
1 62  GLY n 
1 63  SER n 
1 64  MET n 
1 65  MET n 
1 66  GLY n 
1 67  GLU n 
1 68  GLN n 
1 69  PHE n 
1 70  VAL n 
1 71  THR n 
1 72  GLY n 
1 73  GLU n 
1 74  THR n 
1 75  ILE n 
1 76  ARG n 
1 77  GLU n 
1 78  ALA n 
1 79  LEU n 
1 80  LYS n 
1 81  ARG n 
1 82  SER n 
1 83  LYS n 
1 84  GLU n 
1 85  LEU n 
1 86  GLU n 
1 87  GLU n 
1 88  LYS n 
1 89  GLY n 
1 90  PHE n 
1 91  SER n 
1 92  TYR n 
1 93  SER n 
1 94  TYR n 
1 95  ASP n 
1 96  MET n 
1 97  LEU n 
1 98  GLY n 
1 99  GLU n 
1 100 ALA n 
1 101 ALA n 
1 102 THR n 
1 103 THR n 
1 104 ALA n 
1 105 ALA n 
1 106 ASP n 
1 107 ALA n 
1 108 GLU n 
1 109 ARG n 
1 110 TYR n 
1 111 TYR n 
1 112 ARG n 
1 113 ASP n 
1 114 TYR n 
1 115 GLU n 
1 116 SER n 
1 117 ALA n 
1 118 ILE n 
1 119 HIS n 
1 120 ALA n 
1 121 ILE n 
1 122 GLY n 
1 123 LYS n 
1 124 ALA n 
1 125 SER n 
1 126 ALA n 
1 127 GLY n 
1 128 ARG n 
1 129 GLY n 
1 130 ILE n 
1 131 TYR n 
1 132 GLU n 
1 133 GLY n 
1 134 PRO n 
1 135 GLY n 
1 136 ILE n 
1 137 SER n 
1 138 ILE n 
1 139 LYS n 
1 140 LEU n 
1 141 SER n 
1 142 ALA n 
1 143 LEU n 
1 144 HIS n 
1 145 PRO n 
1 146 ARG n 
1 147 TYR n 
1 148 SER n 
1 149 ARG n 
1 150 ALA n 
1 151 GLN n 
1 152 ALA n 
1 153 ALA n 
1 154 ARG n 
1 155 VAL n 
1 156 MET n 
1 157 GLY n 
1 158 GLU n 
1 159 LEU n 
1 160 LEU n 
1 161 PRO n 
1 162 ARG n 
1 163 VAL n 
1 164 LYS n 
1 165 ALA n 
1 166 LEU n 
1 167 ALA n 
1 168 LEU n 
1 169 LEU n 
1 170 ALA n 
1 171 LYS n 
1 172 ASN n 
1 173 TYR n 
1 174 ASP n 
1 175 ILE n 
1 176 GLY n 
1 177 LEU n 
1 178 ASN n 
1 179 ILE n 
1 180 ASP n 
1 181 ALA n 
1 182 GLU n 
1 183 GLU n 
1 184 ALA n 
1 185 ASP n 
1 186 ARG n 
1 187 LEU n 
1 188 GLU n 
1 189 LEU n 
1 190 SER n 
1 191 LEU n 
1 192 ASP n 
1 193 LEU n 
1 194 LEU n 
1 195 GLU n 
1 196 VAL n 
1 197 LEU n 
1 198 CYS n 
1 199 LEU n 
1 200 ASP n 
1 201 GLY n 
1 202 ASP n 
1 203 LEU n 
1 204 SER n 
1 205 GLY n 
1 206 TRP n 
1 207 ASN n 
1 208 GLY n 
1 209 MET n 
1 210 GLY n 
1 211 PHE n 
1 212 VAL n 
1 213 VAL n 
1 214 GLN n 
1 215 ALA n 
1 216 TYR n 
1 217 GLY n 
1 218 LYS n 
1 219 ARG n 
1 220 CYS n 
1 221 PRO n 
1 222 PHE n 
1 223 VAL n 
1 224 LEU n 
1 225 ASP n 
1 226 PHE n 
1 227 ILE n 
1 228 ILE n 
1 229 ASP n 
1 230 LEU n 
1 231 ALA n 
1 232 ARG n 
1 233 ARG n 
1 234 SER n 
1 235 GLY n 
1 236 ARG n 
1 237 ARG n 
1 238 ILE n 
1 239 MET n 
1 240 VAL n 
1 241 ARG n 
1 242 LEU n 
1 243 VAL n 
1 244 LYS n 
1 245 GLY n 
1 246 ALA n 
1 247 TYR n 
1 248 TRP n 
1 249 ASP n 
1 250 ALA n 
1 251 GLU n 
1 252 ILE n 
1 253 LYS n 
1 254 ARG n 
1 255 ALA n 
1 256 GLN n 
1 257 LEU n 
1 258 ASP n 
1 259 GLY n 
1 260 LEU n 
1 261 ALA n 
1 262 ASP n 
1 263 PHE n 
1 264 PRO n 
1 265 VAL n 
1 266 PHE n 
1 267 THR n 
1 268 ARG n 
1 269 LYS n 
1 270 ILE n 
1 271 HIS n 
1 272 THR n 
1 273 ASP n 
1 274 VAL n 
1 275 SER n 
1 276 TYR n 
1 277 ILE n 
1 278 ALA n 
1 279 CYS n 
1 280 ALA n 
1 281 ALA n 
1 282 LYS n 
1 283 LEU n 
1 284 LEU n 
1 285 ALA n 
1 286 ALA n 
1 287 THR n 
1 288 ASP n 
1 289 VAL n 
1 290 VAL n 
1 291 PHE n 
1 292 PRO n 
1 293 GLN n 
1 294 PHE n 
1 295 ALA n 
1 296 THR n 
1 297 HIS n 
1 298 ASN n 
1 299 ALA n 
1 300 GLN n 
1 301 THR n 
1 302 LEU n 
1 303 ALA n 
1 304 ALA n 
1 305 ILE n 
1 306 TYR n 
1 307 HIS n 
1 308 MET n 
1 309 ALA n 
1 310 GLY n 
1 311 LYS n 
1 312 ASP n 
1 313 PHE n 
1 314 HIS n 
1 315 VAL n 
1 316 GLY n 
1 317 LYS n 
1 318 TYR n 
1 319 GLU n 
1 320 PHE n 
1 321 GLN n 
1 322 CYS n 
1 323 LEU n 
1 324 HIS n 
1 325 GLY n 
1 326 MET n 
1 327 GLY n 
1 328 GLU n 
1 329 PRO n 
1 330 LEU n 
1 331 TYR n 
1 332 GLU n 
1 333 GLU n 
1 334 VAL n 
1 335 VAL n 
1 336 GLY n 
1 337 ARG n 
1 338 GLY n 
1 339 LYS n 
1 340 LEU n 
1 341 ASP n 
1 342 ARG n 
1 343 PRO n 
1 344 CYS n 
1 345 ARG n 
1 346 ILE n 
1 347 TYR n 
1 348 ALA n 
1 349 PRO n 
1 350 VAL n 
1 351 GLY n 
1 352 THR n 
1 353 HIS n 
1 354 GLU n 
1 355 THR n 
1 356 LEU n 
1 357 LEU n 
1 358 ALA n 
1 359 TYR n 
1 360 LEU n 
1 361 VAL n 
1 362 ARG n 
1 363 ARG n 
1 364 LEU n 
1 365 LEU n 
1 366 GLU n 
1 367 ASN n 
1 368 GLY n 
1 369 ALA n 
1 370 ASN n 
1 371 SER n 
1 372 SER n 
1 373 PHE n 
1 374 VAL n 
1 375 HIS n 
1 376 ARG n 
1 377 ILE n 
1 378 ASN n 
1 379 ASP n 
1 380 PRO n 
1 381 LYS n 
1 382 VAL n 
1 383 SER n 
1 384 ILE n 
1 385 ASP n 
1 386 GLU n 
1 387 LEU n 
1 388 ILE n 
1 389 ALA n 
1 390 ASP n 
1 391 PRO n 
1 392 VAL n 
1 393 GLU n 
1 394 VAL n 
1 395 VAL n 
1 396 ARG n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1  59  ? ? 'putA, SM11_chr0102' ? SM11 ? ? ? ? 'Sinorhizobium meliloti' 707241 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 60 396 ? ? 'putA, SM11_chr0102' ? SM11 ? ? ? ? 'Sinorhizobium meliloti' 707241 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BC6 non-polymer         . 
;{[(3E)-4-{10-[(2S,3S,4R)-5-{[(R)-{[(R)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-2,3,4-trihydroxypentyl]-7,8-dimethyl-2,4-dioxo-2,3,4,10-tetrahydrobenzo[g]pteridin-5(1H)-yl}but-3-en-2-ylidene]amino}acetic acid (non-preferred name)
;
? 'C33 H42 N10 O17 P2' 912.691 
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 
FMT   non-polymer         . 'FORMIC ACID' ? 'C H2 O2'            46.025  
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  
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 
# 
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   SER 1   25  ?   ?   ?   A . n 
A 1 2   ARG 2   26  ?   ?   ?   A . n 
A 1 3   PRO 3   27  27  PRO PRO A . n 
A 1 4   GLN 4   28  28  GLN GLN A . n 
A 1 5   SER 5   29  29  SER SER A . n 
A 1 6   THR 6   30  30  THR THR A . n 
A 1 7   LEU 7   31  31  LEU LEU A . n 
A 1 8   ARG 8   32  32  ARG ARG A . n 
A 1 9   ARG 9   33  33  ARG ARG A . n 
A 1 10  ALA 10  34  34  ALA ALA A . n 
A 1 11  ILE 11  35  35  ILE ILE A . n 
A 1 12  THR 12  36  36  THR THR A . n 
A 1 13  ALA 13  37  37  ALA ALA A . n 
A 1 14  ALA 14  38  38  ALA ALA A . n 
A 1 15  TYR 15  39  39  TYR TYR A . n 
A 1 16  ARG 16  40  40  ARG ARG A . n 
A 1 17  ARG 17  41  41  ARG ARG A . n 
A 1 18  PRO 18  42  42  PRO PRO A . n 
A 1 19  GLU 19  43  43  GLU GLU A . n 
A 1 20  THR 20  44  44  THR THR A . n 
A 1 21  GLU 21  45  45  GLU GLU A . n 
A 1 22  CYS 22  46  46  CYS CYS A . n 
A 1 23  LEU 23  47  47  LEU LEU A . n 
A 1 24  PRO 24  48  48  PRO PRO A . n 
A 1 25  PRO 25  49  49  PRO PRO A . n 
A 1 26  LEU 26  50  50  LEU LEU A . n 
A 1 27  VAL 27  51  51  VAL VAL A . n 
A 1 28  GLU 28  52  52  GLU GLU A . n 
A 1 29  ALA 29  53  53  ALA ALA A . n 
A 1 30  ALA 30  54  54  ALA ALA A . n 
A 1 31  THR 31  55  55  THR THR A . n 
A 1 32  GLN 32  56  56  GLN GLN A . n 
A 1 33  SER 33  57  57  SER SER A . n 
A 1 34  LYS 34  58  58  LYS LYS A . n 
A 1 35  GLU 35  59  59  GLU GLU A . n 
A 1 36  ILE 36  60  60  ILE ILE A . n 
A 1 37  ARG 37  61  61  ARG ARG A . n 
A 1 38  ASP 38  62  62  ASP ASP A . n 
A 1 39  ALA 39  63  63  ALA ALA A . n 
A 1 40  ALA 40  64  64  ALA ALA A . n 
A 1 41  ALA 41  65  65  ALA ALA A . n 
A 1 42  SER 42  66  66  SER SER A . n 
A 1 43  THR 43  67  67  THR THR A . n 
A 1 44  ALA 44  68  68  ALA ALA A . n 
A 1 45  ARG 45  69  69  ARG ARG A . n 
A 1 46  LYS 46  70  70  LYS LYS A . n 
A 1 47  LEU 47  71  71  LEU LEU A . n 
A 1 48  ILE 48  72  72  ILE ILE A . n 
A 1 49  GLU 49  73  73  GLU GLU A . n 
A 1 50  ALA 50  74  74  ALA ALA A . n 
A 1 51  LEU 51  75  75  LEU LEU A . n 
A 1 52  ARG 52  76  76  ARG ARG A . n 
A 1 53  GLY 53  77  77  GLY GLY A . n 
A 1 54  LYS 54  78  78  LYS LYS A . n 
A 1 55  HIS 55  79  79  HIS HIS A . n 
A 1 56  SER 56  182 ?   ?   ?   A . n 
A 1 57  GLY 57  183 ?   ?   ?   A . n 
A 1 58  SER 58  184 ?   ?   ?   A . n 
A 1 59  GLY 59  185 ?   ?   ?   A . n 
A 1 60  SER 60  186 ?   ?   ?   A . n 
A 1 61  SER 61  187 ?   ?   ?   A . n 
A 1 62  GLY 62  188 ?   ?   ?   A . n 
A 1 63  SER 63  189 ?   ?   ?   A . n 
A 1 64  MET 64  190 ?   ?   ?   A . n 
A 1 65  MET 65  191 ?   ?   ?   A . n 
A 1 66  GLY 66  192 192 GLY GLY A . n 
A 1 67  GLU 67  193 193 GLU GLU A . n 
A 1 68  GLN 68  194 194 GLN GLN A . n 
A 1 69  PHE 69  195 195 PHE PHE A . n 
A 1 70  VAL 70  196 196 VAL VAL A . n 
A 1 71  THR 71  197 197 THR THR A . n 
A 1 72  GLY 72  198 198 GLY GLY A . n 
A 1 73  GLU 73  199 199 GLU GLU A . n 
A 1 74  THR 74  200 200 THR THR A . n 
A 1 75  ILE 75  201 201 ILE ILE A . n 
A 1 76  ARG 76  202 202 ARG ARG A . n 
A 1 77  GLU 77  203 203 GLU GLU A . n 
A 1 78  ALA 78  204 204 ALA ALA A . n 
A 1 79  LEU 79  205 205 LEU LEU A . n 
A 1 80  LYS 80  206 206 LYS LYS A . n 
A 1 81  ARG 81  207 207 ARG ARG A . n 
A 1 82  SER 82  208 208 SER SER A . n 
A 1 83  LYS 83  209 209 LYS LYS A . n 
A 1 84  GLU 84  210 210 GLU GLU A . n 
A 1 85  LEU 85  211 211 LEU LEU A . n 
A 1 86  GLU 86  212 212 GLU GLU A . n 
A 1 87  GLU 87  213 213 GLU GLU A . n 
A 1 88  LYS 88  214 214 LYS LYS A . n 
A 1 89  GLY 89  215 215 GLY GLY A . n 
A 1 90  PHE 90  216 216 PHE PHE A . n 
A 1 91  SER 91  217 217 SER SER A . n 
A 1 92  TYR 92  218 218 TYR TYR A . n 
A 1 93  SER 93  219 219 SER SER A . n 
A 1 94  TYR 94  220 220 TYR TYR A . n 
A 1 95  ASP 95  221 221 ASP ASP A . n 
A 1 96  MET 96  222 222 MET MET A . n 
A 1 97  LEU 97  223 223 LEU LEU A . n 
A 1 98  GLY 98  224 224 GLY GLY A . n 
A 1 99  GLU 99  225 225 GLU GLU A . n 
A 1 100 ALA 100 226 226 ALA ALA A . n 
A 1 101 ALA 101 227 227 ALA ALA A . n 
A 1 102 THR 102 228 228 THR THR A . n 
A 1 103 THR 103 229 229 THR THR A . n 
A 1 104 ALA 104 230 230 ALA ALA A . n 
A 1 105 ALA 105 231 231 ALA ALA A . n 
A 1 106 ASP 106 232 232 ASP ASP A . n 
A 1 107 ALA 107 233 233 ALA ALA A . n 
A 1 108 GLU 108 234 234 GLU GLU A . n 
A 1 109 ARG 109 235 235 ARG ARG A . n 
A 1 110 TYR 110 236 236 TYR TYR A . n 
A 1 111 TYR 111 237 237 TYR TYR A . n 
A 1 112 ARG 112 238 238 ARG ARG A . n 
A 1 113 ASP 113 239 239 ASP ASP A . n 
A 1 114 TYR 114 240 240 TYR TYR A . n 
A 1 115 GLU 115 241 241 GLU GLU A . n 
A 1 116 SER 116 242 242 SER SER A . n 
A 1 117 ALA 117 243 243 ALA ALA A . n 
A 1 118 ILE 118 244 244 ILE ILE A . n 
A 1 119 HIS 119 245 245 HIS HIS A . n 
A 1 120 ALA 120 246 246 ALA ALA A . n 
A 1 121 ILE 121 247 247 ILE ILE A . n 
A 1 122 GLY 122 248 248 GLY GLY A . n 
A 1 123 LYS 123 249 249 LYS LYS A . n 
A 1 124 ALA 124 250 250 ALA ALA A . n 
A 1 125 SER 125 251 251 SER SER A . n 
A 1 126 ALA 126 252 252 ALA ALA A . n 
A 1 127 GLY 127 253 253 GLY GLY A . n 
A 1 128 ARG 128 254 254 ARG ARG A . n 
A 1 129 GLY 129 255 255 GLY GLY A . n 
A 1 130 ILE 130 256 256 ILE ILE A . n 
A 1 131 TYR 131 257 257 TYR TYR A . n 
A 1 132 GLU 132 258 258 GLU GLU A . n 
A 1 133 GLY 133 259 259 GLY GLY A . n 
A 1 134 PRO 134 260 260 PRO PRO A . n 
A 1 135 GLY 135 261 261 GLY GLY A . n 
A 1 136 ILE 136 262 262 ILE ILE A . n 
A 1 137 SER 137 263 263 SER SER A . n 
A 1 138 ILE 138 264 264 ILE ILE A . n 
A 1 139 LYS 139 265 265 LYS LYS A . n 
A 1 140 LEU 140 266 266 LEU LEU A . n 
A 1 141 SER 141 267 267 SER SER A . n 
A 1 142 ALA 142 268 268 ALA ALA A . n 
A 1 143 LEU 143 269 269 LEU LEU A . n 
A 1 144 HIS 144 270 270 HIS HIS A . n 
A 1 145 PRO 145 271 271 PRO PRO A . n 
A 1 146 ARG 146 272 272 ARG ARG A . n 
A 1 147 TYR 147 273 273 TYR TYR A . n 
A 1 148 SER 148 274 274 SER SER A . n 
A 1 149 ARG 149 275 275 ARG ARG A . n 
A 1 150 ALA 150 276 276 ALA ALA A . n 
A 1 151 GLN 151 277 277 GLN GLN A . n 
A 1 152 ALA 152 278 278 ALA ALA A . n 
A 1 153 ALA 153 279 279 ALA ALA A . n 
A 1 154 ARG 154 280 280 ARG ARG A . n 
A 1 155 VAL 155 281 281 VAL VAL A . n 
A 1 156 MET 156 282 282 MET MET A . n 
A 1 157 GLY 157 283 283 GLY GLY A . n 
A 1 158 GLU 158 284 284 GLU GLU A . n 
A 1 159 LEU 159 285 285 LEU LEU A . n 
A 1 160 LEU 160 286 286 LEU LEU A . n 
A 1 161 PRO 161 287 287 PRO PRO A . n 
A 1 162 ARG 162 288 288 ARG ARG A . n 
A 1 163 VAL 163 289 289 VAL VAL A . n 
A 1 164 LYS 164 290 290 LYS LYS A . n 
A 1 165 ALA 165 291 291 ALA ALA A . n 
A 1 166 LEU 166 292 292 LEU LEU A . n 
A 1 167 ALA 167 293 293 ALA ALA A . n 
A 1 168 LEU 168 294 294 LEU LEU A . n 
A 1 169 LEU 169 295 295 LEU LEU A . n 
A 1 170 ALA 170 296 296 ALA ALA A . n 
A 1 171 LYS 171 297 297 LYS LYS A . n 
A 1 172 ASN 172 298 298 ASN ASN A . n 
A 1 173 TYR 173 299 299 TYR TYR A . n 
A 1 174 ASP 174 300 300 ASP ASP A . n 
A 1 175 ILE 175 301 301 ILE ILE A . n 
A 1 176 GLY 176 302 302 GLY GLY A . n 
A 1 177 LEU 177 303 303 LEU LEU A . n 
A 1 178 ASN 178 304 304 ASN ASN A . n 
A 1 179 ILE 179 305 305 ILE ILE A . n 
A 1 180 ASP 180 306 306 ASP ASP A . n 
A 1 181 ALA 181 307 307 ALA ALA A . n 
A 1 182 GLU 182 308 308 GLU GLU A . n 
A 1 183 GLU 183 309 309 GLU GLU A . n 
A 1 184 ALA 184 310 310 ALA ALA A . n 
A 1 185 ASP 185 311 311 ASP ASP A . n 
A 1 186 ARG 186 312 312 ARG ARG A . n 
A 1 187 LEU 187 313 313 LEU LEU A . n 
A 1 188 GLU 188 314 314 GLU GLU A . n 
A 1 189 LEU 189 315 315 LEU LEU A . n 
A 1 190 SER 190 316 316 SER SER A . n 
A 1 191 LEU 191 317 317 LEU LEU A . n 
A 1 192 ASP 192 318 318 ASP ASP A . n 
A 1 193 LEU 193 319 319 LEU LEU A . n 
A 1 194 LEU 194 320 320 LEU LEU A . n 
A 1 195 GLU 195 321 321 GLU GLU A . n 
A 1 196 VAL 196 322 322 VAL VAL A . n 
A 1 197 LEU 197 323 323 LEU LEU A . n 
A 1 198 CYS 198 324 324 CYS CYS A . n 
A 1 199 LEU 199 325 325 LEU LEU A . n 
A 1 200 ASP 200 326 326 ASP ASP A . n 
A 1 201 GLY 201 327 327 GLY GLY A . n 
A 1 202 ASP 202 328 328 ASP ASP A . n 
A 1 203 LEU 203 329 329 LEU LEU A . n 
A 1 204 SER 204 330 330 SER SER A . n 
A 1 205 GLY 205 331 331 GLY GLY A . n 
A 1 206 TRP 206 332 332 TRP TRP A . n 
A 1 207 ASN 207 333 333 ASN ASN A . n 
A 1 208 GLY 208 334 334 GLY GLY A . n 
A 1 209 MET 209 335 335 MET MET A . n 
A 1 210 GLY 210 336 336 GLY GLY A . n 
A 1 211 PHE 211 337 337 PHE PHE A . n 
A 1 212 VAL 212 338 338 VAL VAL A . n 
A 1 213 VAL 213 339 339 VAL VAL A . n 
A 1 214 GLN 214 340 340 GLN GLN A . n 
A 1 215 ALA 215 341 341 ALA ALA A . n 
A 1 216 TYR 216 342 342 TYR TYR A . n 
A 1 217 GLY 217 343 343 GLY GLY A . n 
A 1 218 LYS 218 344 344 LYS LYS A . n 
A 1 219 ARG 219 345 345 ARG ARG A . n 
A 1 220 CYS 220 346 346 CYS CYS A . n 
A 1 221 PRO 221 347 347 PRO PRO A . n 
A 1 222 PHE 222 348 348 PHE PHE A . n 
A 1 223 VAL 223 349 349 VAL VAL A . n 
A 1 224 LEU 224 350 350 LEU LEU A . n 
A 1 225 ASP 225 351 351 ASP ASP A . n 
A 1 226 PHE 226 352 352 PHE PHE A . n 
A 1 227 ILE 227 353 353 ILE ILE A . n 
A 1 228 ILE 228 354 354 ILE ILE A . n 
A 1 229 ASP 229 355 355 ASP ASP A . n 
A 1 230 LEU 230 356 356 LEU LEU A . n 
A 1 231 ALA 231 357 357 ALA ALA A . n 
A 1 232 ARG 232 358 358 ARG ARG A . n 
A 1 233 ARG 233 359 359 ARG ARG A . n 
A 1 234 SER 234 360 360 SER SER A . n 
A 1 235 GLY 235 361 361 GLY GLY A . n 
A 1 236 ARG 236 362 362 ARG ARG A . n 
A 1 237 ARG 237 363 363 ARG ARG A . n 
A 1 238 ILE 238 364 364 ILE ILE A . n 
A 1 239 MET 239 365 365 MET MET A . n 
A 1 240 VAL 240 366 366 VAL VAL A . n 
A 1 241 ARG 241 367 367 ARG ARG A . n 
A 1 242 LEU 242 368 368 LEU LEU A . n 
A 1 243 VAL 243 369 369 VAL VAL A . n 
A 1 244 LYS 244 370 370 LYS LYS A . n 
A 1 245 GLY 245 371 371 GLY GLY A . n 
A 1 246 ALA 246 372 372 ALA ALA A . n 
A 1 247 TYR 247 373 373 TYR TYR A . n 
A 1 248 TRP 248 374 374 TRP TRP A . n 
A 1 249 ASP 249 375 375 ASP ASP A . n 
A 1 250 ALA 250 376 376 ALA ALA A . n 
A 1 251 GLU 251 377 377 GLU GLU A . n 
A 1 252 ILE 252 378 378 ILE ILE A . n 
A 1 253 LYS 253 379 379 LYS LYS A . n 
A 1 254 ARG 254 380 380 ARG ARG A . n 
A 1 255 ALA 255 381 381 ALA ALA A . n 
A 1 256 GLN 256 382 382 GLN GLN A . n 
A 1 257 LEU 257 383 383 LEU LEU A . n 
A 1 258 ASP 258 384 384 ASP ASP A . n 
A 1 259 GLY 259 385 ?   ?   ?   A . n 
A 1 260 LEU 260 386 ?   ?   ?   A . n 
A 1 261 ALA 261 387 387 ALA ALA A . n 
A 1 262 ASP 262 388 388 ASP ASP A . n 
A 1 263 PHE 263 389 389 PHE PHE A . n 
A 1 264 PRO 264 390 390 PRO PRO A . n 
A 1 265 VAL 265 391 391 VAL VAL A . n 
A 1 266 PHE 266 392 392 PHE PHE A . n 
A 1 267 THR 267 393 393 THR THR A . n 
A 1 268 ARG 268 394 394 ARG ARG A . n 
A 1 269 LYS 269 395 395 LYS LYS A . n 
A 1 270 ILE 270 396 396 ILE ILE A . n 
A 1 271 HIS 271 397 397 HIS HIS A . n 
A 1 272 THR 272 398 398 THR THR A . n 
A 1 273 ASP 273 399 399 ASP ASP A . n 
A 1 274 VAL 274 400 400 VAL VAL A . n 
A 1 275 SER 275 401 401 SER SER A . n 
A 1 276 TYR 276 402 402 TYR TYR A . n 
A 1 277 ILE 277 403 403 ILE ILE A . n 
A 1 278 ALA 278 404 404 ALA ALA A . n 
A 1 279 CYS 279 405 405 CYS CYS A . n 
A 1 280 ALA 280 406 406 ALA ALA A . n 
A 1 281 ALA 281 407 407 ALA ALA A . n 
A 1 282 LYS 282 408 408 LYS LYS A . n 
A 1 283 LEU 283 409 409 LEU LEU A . n 
A 1 284 LEU 284 410 410 LEU LEU A . n 
A 1 285 ALA 285 411 411 ALA ALA A . n 
A 1 286 ALA 286 412 412 ALA ALA A . n 
A 1 287 THR 287 413 413 THR THR A . n 
A 1 288 ASP 288 414 414 ASP ASP A . n 
A 1 289 VAL 289 415 415 VAL VAL A . n 
A 1 290 VAL 290 416 416 VAL VAL A . n 
A 1 291 PHE 291 417 417 PHE PHE A . n 
A 1 292 PRO 292 418 418 PRO PRO A . n 
A 1 293 GLN 293 419 419 GLN GLN A . n 
A 1 294 PHE 294 420 420 PHE PHE A . n 
A 1 295 ALA 295 421 421 ALA ALA A . n 
A 1 296 THR 296 422 422 THR THR A . n 
A 1 297 HIS 297 423 423 HIS HIS A . n 
A 1 298 ASN 298 424 424 ASN ASN A . n 
A 1 299 ALA 299 425 425 ALA ALA A . n 
A 1 300 GLN 300 426 426 GLN GLN A . n 
A 1 301 THR 301 427 427 THR THR A . n 
A 1 302 LEU 302 428 428 LEU LEU A . n 
A 1 303 ALA 303 429 429 ALA ALA A . n 
A 1 304 ALA 304 430 430 ALA ALA A . n 
A 1 305 ILE 305 431 431 ILE ILE A . n 
A 1 306 TYR 306 432 432 TYR TYR A . n 
A 1 307 HIS 307 433 433 HIS HIS A . n 
A 1 308 MET 308 434 434 MET MET A . n 
A 1 309 ALA 309 435 435 ALA ALA A . n 
A 1 310 GLY 310 436 436 GLY GLY A . n 
A 1 311 LYS 311 437 437 LYS LYS A . n 
A 1 312 ASP 312 438 438 ASP ASP A . n 
A 1 313 PHE 313 439 439 PHE PHE A . n 
A 1 314 HIS 314 440 440 HIS HIS A . n 
A 1 315 VAL 315 441 441 VAL VAL A . n 
A 1 316 GLY 316 442 442 GLY GLY A . n 
A 1 317 LYS 317 443 443 LYS LYS A . n 
A 1 318 TYR 318 444 444 TYR TYR A . n 
A 1 319 GLU 319 445 445 GLU GLU A . n 
A 1 320 PHE 320 446 446 PHE PHE A . n 
A 1 321 GLN 321 447 447 GLN GLN A . n 
A 1 322 CYS 322 448 448 CYS CYS A . n 
A 1 323 LEU 323 449 449 LEU LEU A . n 
A 1 324 HIS 324 450 450 HIS HIS A . n 
A 1 325 GLY 325 451 451 GLY GLY A . n 
A 1 326 MET 326 452 452 MET MET A . n 
A 1 327 GLY 327 453 453 GLY GLY A . n 
A 1 328 GLU 328 454 454 GLU GLU A . n 
A 1 329 PRO 329 455 455 PRO PRO A . n 
A 1 330 LEU 330 456 456 LEU LEU A . n 
A 1 331 TYR 331 457 457 TYR TYR A . n 
A 1 332 GLU 332 458 458 GLU GLU A . n 
A 1 333 GLU 333 459 459 GLU GLU A . n 
A 1 334 VAL 334 460 460 VAL VAL A . n 
A 1 335 VAL 335 461 461 VAL VAL A . n 
A 1 336 GLY 336 462 462 GLY GLY A . n 
A 1 337 ARG 337 463 463 ARG ARG A . n 
A 1 338 GLY 338 464 464 GLY GLY A . n 
A 1 339 LYS 339 465 465 LYS LYS A . n 
A 1 340 LEU 340 466 466 LEU LEU A . n 
A 1 341 ASP 341 467 467 ASP ASP A . n 
A 1 342 ARG 342 468 468 ARG ARG A . n 
A 1 343 PRO 343 469 469 PRO PRO A . n 
A 1 344 CYS 344 470 470 CYS CYS A . n 
A 1 345 ARG 345 471 471 ARG ARG A . n 
A 1 346 ILE 346 472 472 ILE ILE A . n 
A 1 347 TYR 347 473 473 TYR TYR A . n 
A 1 348 ALA 348 474 474 ALA ALA A . n 
A 1 349 PRO 349 475 475 PRO PRO A . n 
A 1 350 VAL 350 476 476 VAL VAL A . n 
A 1 351 GLY 351 477 477 GLY GLY A . n 
A 1 352 THR 352 478 478 THR THR A . n 
A 1 353 HIS 353 479 479 HIS HIS A . n 
A 1 354 GLU 354 480 480 GLU GLU A . n 
A 1 355 THR 355 481 481 THR THR A . n 
A 1 356 LEU 356 482 482 LEU LEU A . n 
A 1 357 LEU 357 483 483 LEU LEU A . n 
A 1 358 ALA 358 484 484 ALA ALA A . n 
A 1 359 TYR 359 485 485 TYR TYR A . n 
A 1 360 LEU 360 486 486 LEU LEU A . n 
A 1 361 VAL 361 487 487 VAL VAL A . n 
A 1 362 ARG 362 488 488 ARG ARG A . n 
A 1 363 ARG 363 489 489 ARG ARG A . n 
A 1 364 LEU 364 490 490 LEU LEU A . n 
A 1 365 LEU 365 491 491 LEU LEU A . n 
A 1 366 GLU 366 492 492 GLU GLU A . n 
A 1 367 ASN 367 493 493 ASN ASN A . n 
A 1 368 GLY 368 494 494 GLY GLY A . n 
A 1 369 ALA 369 495 495 ALA ALA A . n 
A 1 370 ASN 370 496 496 ASN ASN A . n 
A 1 371 SER 371 497 497 SER SER A . n 
A 1 372 SER 372 498 498 SER SER A . n 
A 1 373 PHE 373 499 499 PHE PHE A . n 
A 1 374 VAL 374 500 500 VAL VAL A . n 
A 1 375 HIS 375 501 501 HIS HIS A . n 
A 1 376 ARG 376 502 502 ARG ARG A . n 
A 1 377 ILE 377 503 503 ILE ILE A . n 
A 1 378 ASN 378 504 504 ASN ASN A . n 
A 1 379 ASP 379 505 505 ASP ASP A . n 
A 1 380 PRO 380 506 506 PRO PRO A . n 
A 1 381 LYS 381 507 507 LYS LYS A . n 
A 1 382 VAL 382 508 508 VAL VAL A . n 
A 1 383 SER 383 509 509 SER SER A . n 
A 1 384 ILE 384 510 510 ILE ILE A . n 
A 1 385 ASP 385 511 511 ASP ASP A . n 
A 1 386 GLU 386 512 512 GLU GLU A . n 
A 1 387 LEU 387 513 513 LEU LEU A . n 
A 1 388 ILE 388 514 514 ILE ILE A . n 
A 1 389 ALA 389 515 515 ALA ALA A . n 
A 1 390 ASP 390 516 516 ASP ASP A . n 
A 1 391 PRO 391 517 517 PRO PRO A . n 
A 1 392 VAL 392 518 518 VAL VAL A . n 
A 1 393 GLU 393 519 519 GLU GLU A . n 
A 1 394 VAL 394 520 520 VAL VAL A . n 
A 1 395 VAL 395 521 ?   ?   ?   A . n 
A 1 396 ARG 396 522 ?   ?   ?   A . n 
B 1 1   SER 1   25  ?   ?   ?   B . n 
B 1 2   ARG 2   26  26  ARG ARG B . n 
B 1 3   PRO 3   27  27  PRO PRO B . n 
B 1 4   GLN 4   28  28  GLN GLN B . n 
B 1 5   SER 5   29  29  SER SER B . n 
B 1 6   THR 6   30  30  THR THR B . n 
B 1 7   LEU 7   31  31  LEU LEU B . n 
B 1 8   ARG 8   32  32  ARG ARG B . n 
B 1 9   ARG 9   33  33  ARG ARG B . n 
B 1 10  ALA 10  34  34  ALA ALA B . n 
B 1 11  ILE 11  35  35  ILE ILE B . n 
B 1 12  THR 12  36  36  THR THR B . n 
B 1 13  ALA 13  37  37  ALA ALA B . n 
B 1 14  ALA 14  38  38  ALA ALA B . n 
B 1 15  TYR 15  39  39  TYR TYR B . n 
B 1 16  ARG 16  40  40  ARG ARG B . n 
B 1 17  ARG 17  41  41  ARG ARG B . n 
B 1 18  PRO 18  42  42  PRO PRO B . n 
B 1 19  GLU 19  43  43  GLU GLU B . n 
B 1 20  THR 20  44  44  THR THR B . n 
B 1 21  GLU 21  45  45  GLU GLU B . n 
B 1 22  CYS 22  46  46  CYS CYS B . n 
B 1 23  LEU 23  47  47  LEU LEU B . n 
B 1 24  PRO 24  48  48  PRO PRO B . n 
B 1 25  PRO 25  49  49  PRO PRO B . n 
B 1 26  LEU 26  50  50  LEU LEU B . n 
B 1 27  VAL 27  51  51  VAL VAL B . n 
B 1 28  GLU 28  52  52  GLU GLU B . n 
B 1 29  ALA 29  53  53  ALA ALA B . n 
B 1 30  ALA 30  54  54  ALA ALA B . n 
B 1 31  THR 31  55  55  THR THR B . n 
B 1 32  GLN 32  56  56  GLN GLN B . n 
B 1 33  SER 33  57  57  SER SER B . n 
B 1 34  LYS 34  58  58  LYS LYS B . n 
B 1 35  GLU 35  59  59  GLU GLU B . n 
B 1 36  ILE 36  60  60  ILE ILE B . n 
B 1 37  ARG 37  61  61  ARG ARG B . n 
B 1 38  ASP 38  62  62  ASP ASP B . n 
B 1 39  ALA 39  63  63  ALA ALA B . n 
B 1 40  ALA 40  64  64  ALA ALA B . n 
B 1 41  ALA 41  65  65  ALA ALA B . n 
B 1 42  SER 42  66  66  SER SER B . n 
B 1 43  THR 43  67  67  THR THR B . n 
B 1 44  ALA 44  68  68  ALA ALA B . n 
B 1 45  ARG 45  69  69  ARG ARG B . n 
B 1 46  LYS 46  70  70  LYS LYS B . n 
B 1 47  LEU 47  71  71  LEU LEU B . n 
B 1 48  ILE 48  72  72  ILE ILE B . n 
B 1 49  GLU 49  73  73  GLU GLU B . n 
B 1 50  ALA 50  74  74  ALA ALA B . n 
B 1 51  LEU 51  75  75  LEU LEU B . n 
B 1 52  ARG 52  76  76  ARG ARG B . n 
B 1 53  GLY 53  77  77  GLY GLY B . n 
B 1 54  LYS 54  78  78  LYS LYS B . n 
B 1 55  HIS 55  79  79  HIS HIS B . n 
B 1 56  SER 56  182 ?   ?   ?   B . n 
B 1 57  GLY 57  183 ?   ?   ?   B . n 
B 1 58  SER 58  184 ?   ?   ?   B . n 
B 1 59  GLY 59  185 ?   ?   ?   B . n 
B 1 60  SER 60  186 ?   ?   ?   B . n 
B 1 61  SER 61  187 ?   ?   ?   B . n 
B 1 62  GLY 62  188 ?   ?   ?   B . n 
B 1 63  SER 63  189 ?   ?   ?   B . n 
B 1 64  MET 64  190 ?   ?   ?   B . n 
B 1 65  MET 65  191 ?   ?   ?   B . n 
B 1 66  GLY 66  192 192 GLY GLY B . n 
B 1 67  GLU 67  193 193 GLU GLU B . n 
B 1 68  GLN 68  194 194 GLN GLN B . n 
B 1 69  PHE 69  195 195 PHE PHE B . n 
B 1 70  VAL 70  196 196 VAL VAL B . n 
B 1 71  THR 71  197 197 THR THR B . n 
B 1 72  GLY 72  198 198 GLY GLY B . n 
B 1 73  GLU 73  199 199 GLU GLU B . n 
B 1 74  THR 74  200 200 THR THR B . n 
B 1 75  ILE 75  201 201 ILE ILE B . n 
B 1 76  ARG 76  202 202 ARG ARG B . n 
B 1 77  GLU 77  203 203 GLU GLU B . n 
B 1 78  ALA 78  204 204 ALA ALA B . n 
B 1 79  LEU 79  205 205 LEU LEU B . n 
B 1 80  LYS 80  206 206 LYS LYS B . n 
B 1 81  ARG 81  207 207 ARG ARG B . n 
B 1 82  SER 82  208 208 SER SER B . n 
B 1 83  LYS 83  209 209 LYS LYS B . n 
B 1 84  GLU 84  210 210 GLU GLU B . n 
B 1 85  LEU 85  211 211 LEU LEU B . n 
B 1 86  GLU 86  212 212 GLU GLU B . n 
B 1 87  GLU 87  213 213 GLU GLU B . n 
B 1 88  LYS 88  214 214 LYS LYS B . n 
B 1 89  GLY 89  215 215 GLY GLY B . n 
B 1 90  PHE 90  216 216 PHE PHE B . n 
B 1 91  SER 91  217 217 SER SER B . n 
B 1 92  TYR 92  218 218 TYR TYR B . n 
B 1 93  SER 93  219 219 SER SER B . n 
B 1 94  TYR 94  220 220 TYR TYR B . n 
B 1 95  ASP 95  221 221 ASP ASP B . n 
B 1 96  MET 96  222 222 MET MET B . n 
B 1 97  LEU 97  223 223 LEU LEU B . n 
B 1 98  GLY 98  224 224 GLY GLY B . n 
B 1 99  GLU 99  225 225 GLU GLU B . n 
B 1 100 ALA 100 226 226 ALA ALA B . n 
B 1 101 ALA 101 227 227 ALA ALA B . n 
B 1 102 THR 102 228 228 THR THR B . n 
B 1 103 THR 103 229 229 THR THR B . n 
B 1 104 ALA 104 230 230 ALA ALA B . n 
B 1 105 ALA 105 231 231 ALA ALA B . n 
B 1 106 ASP 106 232 232 ASP ASP B . n 
B 1 107 ALA 107 233 233 ALA ALA B . n 
B 1 108 GLU 108 234 234 GLU GLU B . n 
B 1 109 ARG 109 235 235 ARG ARG B . n 
B 1 110 TYR 110 236 236 TYR TYR B . n 
B 1 111 TYR 111 237 237 TYR TYR B . n 
B 1 112 ARG 112 238 238 ARG ARG B . n 
B 1 113 ASP 113 239 239 ASP ASP B . n 
B 1 114 TYR 114 240 240 TYR TYR B . n 
B 1 115 GLU 115 241 241 GLU GLU B . n 
B 1 116 SER 116 242 242 SER SER B . n 
B 1 117 ALA 117 243 243 ALA ALA B . n 
B 1 118 ILE 118 244 244 ILE ILE B . n 
B 1 119 HIS 119 245 245 HIS HIS B . n 
B 1 120 ALA 120 246 246 ALA ALA B . n 
B 1 121 ILE 121 247 247 ILE ILE B . n 
B 1 122 GLY 122 248 248 GLY GLY B . n 
B 1 123 LYS 123 249 249 LYS LYS B . n 
B 1 124 ALA 124 250 250 ALA ALA B . n 
B 1 125 SER 125 251 251 SER SER B . n 
B 1 126 ALA 126 252 252 ALA ALA B . n 
B 1 127 GLY 127 253 253 GLY GLY B . n 
B 1 128 ARG 128 254 254 ARG ARG B . n 
B 1 129 GLY 129 255 255 GLY GLY B . n 
B 1 130 ILE 130 256 256 ILE ILE B . n 
B 1 131 TYR 131 257 257 TYR TYR B . n 
B 1 132 GLU 132 258 258 GLU GLU B . n 
B 1 133 GLY 133 259 259 GLY GLY B . n 
B 1 134 PRO 134 260 260 PRO PRO B . n 
B 1 135 GLY 135 261 261 GLY GLY B . n 
B 1 136 ILE 136 262 262 ILE ILE B . n 
B 1 137 SER 137 263 263 SER SER B . n 
B 1 138 ILE 138 264 264 ILE ILE B . n 
B 1 139 LYS 139 265 265 LYS LYS B . n 
B 1 140 LEU 140 266 266 LEU LEU B . n 
B 1 141 SER 141 267 267 SER SER B . n 
B 1 142 ALA 142 268 268 ALA ALA B . n 
B 1 143 LEU 143 269 269 LEU LEU B . n 
B 1 144 HIS 144 270 270 HIS HIS B . n 
B 1 145 PRO 145 271 271 PRO PRO B . n 
B 1 146 ARG 146 272 272 ARG ARG B . n 
B 1 147 TYR 147 273 273 TYR TYR B . n 
B 1 148 SER 148 274 274 SER SER B . n 
B 1 149 ARG 149 275 275 ARG ARG B . n 
B 1 150 ALA 150 276 276 ALA ALA B . n 
B 1 151 GLN 151 277 277 GLN GLN B . n 
B 1 152 ALA 152 278 278 ALA ALA B . n 
B 1 153 ALA 153 279 279 ALA ALA B . n 
B 1 154 ARG 154 280 280 ARG ARG B . n 
B 1 155 VAL 155 281 281 VAL VAL B . n 
B 1 156 MET 156 282 282 MET MET B . n 
B 1 157 GLY 157 283 283 GLY GLY B . n 
B 1 158 GLU 158 284 284 GLU GLU B . n 
B 1 159 LEU 159 285 285 LEU LEU B . n 
B 1 160 LEU 160 286 286 LEU LEU B . n 
B 1 161 PRO 161 287 287 PRO PRO B . n 
B 1 162 ARG 162 288 288 ARG ARG B . n 
B 1 163 VAL 163 289 289 VAL VAL B . n 
B 1 164 LYS 164 290 290 LYS LYS B . n 
B 1 165 ALA 165 291 291 ALA ALA B . n 
B 1 166 LEU 166 292 292 LEU LEU B . n 
B 1 167 ALA 167 293 293 ALA ALA B . n 
B 1 168 LEU 168 294 294 LEU LEU B . n 
B 1 169 LEU 169 295 295 LEU LEU B . n 
B 1 170 ALA 170 296 296 ALA ALA B . n 
B 1 171 LYS 171 297 297 LYS LYS B . n 
B 1 172 ASN 172 298 298 ASN ASN B . n 
B 1 173 TYR 173 299 299 TYR TYR B . n 
B 1 174 ASP 174 300 300 ASP ASP B . n 
B 1 175 ILE 175 301 301 ILE ILE B . n 
B 1 176 GLY 176 302 302 GLY GLY B . n 
B 1 177 LEU 177 303 303 LEU LEU B . n 
B 1 178 ASN 178 304 304 ASN ASN B . n 
B 1 179 ILE 179 305 305 ILE ILE B . n 
B 1 180 ASP 180 306 306 ASP ASP B . n 
B 1 181 ALA 181 307 307 ALA ALA B . n 
B 1 182 GLU 182 308 308 GLU GLU B . n 
B 1 183 GLU 183 309 309 GLU GLU B . n 
B 1 184 ALA 184 310 310 ALA ALA B . n 
B 1 185 ASP 185 311 311 ASP ASP B . n 
B 1 186 ARG 186 312 312 ARG ARG B . n 
B 1 187 LEU 187 313 313 LEU LEU B . n 
B 1 188 GLU 188 314 314 GLU GLU B . n 
B 1 189 LEU 189 315 315 LEU LEU B . n 
B 1 190 SER 190 316 316 SER SER B . n 
B 1 191 LEU 191 317 317 LEU LEU B . n 
B 1 192 ASP 192 318 318 ASP ASP B . n 
B 1 193 LEU 193 319 319 LEU LEU B . n 
B 1 194 LEU 194 320 320 LEU LEU B . n 
B 1 195 GLU 195 321 321 GLU GLU B . n 
B 1 196 VAL 196 322 322 VAL VAL B . n 
B 1 197 LEU 197 323 323 LEU LEU B . n 
B 1 198 CYS 198 324 324 CYS CYS B . n 
B 1 199 LEU 199 325 325 LEU LEU B . n 
B 1 200 ASP 200 326 326 ASP ASP B . n 
B 1 201 GLY 201 327 327 GLY GLY B . n 
B 1 202 ASP 202 328 328 ASP ASP B . n 
B 1 203 LEU 203 329 329 LEU LEU B . n 
B 1 204 SER 204 330 330 SER SER B . n 
B 1 205 GLY 205 331 331 GLY GLY B . n 
B 1 206 TRP 206 332 332 TRP TRP B . n 
B 1 207 ASN 207 333 333 ASN ASN B . n 
B 1 208 GLY 208 334 334 GLY GLY B . n 
B 1 209 MET 209 335 335 MET MET B . n 
B 1 210 GLY 210 336 336 GLY GLY B . n 
B 1 211 PHE 211 337 337 PHE PHE B . n 
B 1 212 VAL 212 338 338 VAL VAL B . n 
B 1 213 VAL 213 339 339 VAL VAL B . n 
B 1 214 GLN 214 340 340 GLN GLN B . n 
B 1 215 ALA 215 341 341 ALA ALA B . n 
B 1 216 TYR 216 342 342 TYR TYR B . n 
B 1 217 GLY 217 343 343 GLY GLY B . n 
B 1 218 LYS 218 344 344 LYS LYS B . n 
B 1 219 ARG 219 345 345 ARG ARG B . n 
B 1 220 CYS 220 346 346 CYS CYS B . n 
B 1 221 PRO 221 347 347 PRO PRO B . n 
B 1 222 PHE 222 348 348 PHE PHE B . n 
B 1 223 VAL 223 349 349 VAL VAL B . n 
B 1 224 LEU 224 350 350 LEU LEU B . n 
B 1 225 ASP 225 351 351 ASP ASP B . n 
B 1 226 PHE 226 352 352 PHE PHE B . n 
B 1 227 ILE 227 353 353 ILE ILE B . n 
B 1 228 ILE 228 354 354 ILE ILE B . n 
B 1 229 ASP 229 355 355 ASP ASP B . n 
B 1 230 LEU 230 356 356 LEU LEU B . n 
B 1 231 ALA 231 357 357 ALA ALA B . n 
B 1 232 ARG 232 358 358 ARG ARG B . n 
B 1 233 ARG 233 359 359 ARG ARG B . n 
B 1 234 SER 234 360 360 SER SER B . n 
B 1 235 GLY 235 361 361 GLY GLY B . n 
B 1 236 ARG 236 362 362 ARG ARG B . n 
B 1 237 ARG 237 363 363 ARG ARG B . n 
B 1 238 ILE 238 364 364 ILE ILE B . n 
B 1 239 MET 239 365 365 MET MET B . n 
B 1 240 VAL 240 366 366 VAL VAL B . n 
B 1 241 ARG 241 367 367 ARG ARG B . n 
B 1 242 LEU 242 368 368 LEU LEU B . n 
B 1 243 VAL 243 369 369 VAL VAL B . n 
B 1 244 LYS 244 370 370 LYS LYS B . n 
B 1 245 GLY 245 371 371 GLY GLY B . n 
B 1 246 ALA 246 372 372 ALA ALA B . n 
B 1 247 TYR 247 373 373 TYR TYR B . n 
B 1 248 TRP 248 374 374 TRP TRP B . n 
B 1 249 ASP 249 375 375 ASP ASP B . n 
B 1 250 ALA 250 376 376 ALA ALA B . n 
B 1 251 GLU 251 377 377 GLU GLU B . n 
B 1 252 ILE 252 378 378 ILE ILE B . n 
B 1 253 LYS 253 379 379 LYS LYS B . n 
B 1 254 ARG 254 380 380 ARG ARG B . n 
B 1 255 ALA 255 381 381 ALA ALA B . n 
B 1 256 GLN 256 382 382 GLN GLN B . n 
B 1 257 LEU 257 383 383 LEU LEU B . n 
B 1 258 ASP 258 384 384 ASP ASP B . n 
B 1 259 GLY 259 385 385 GLY GLY B . n 
B 1 260 LEU 260 386 386 LEU LEU B . n 
B 1 261 ALA 261 387 387 ALA ALA B . n 
B 1 262 ASP 262 388 388 ASP ASP B . n 
B 1 263 PHE 263 389 389 PHE PHE B . n 
B 1 264 PRO 264 390 390 PRO PRO B . n 
B 1 265 VAL 265 391 391 VAL VAL B . n 
B 1 266 PHE 266 392 392 PHE PHE B . n 
B 1 267 THR 267 393 393 THR THR B . n 
B 1 268 ARG 268 394 394 ARG ARG B . n 
B 1 269 LYS 269 395 395 LYS LYS B . n 
B 1 270 ILE 270 396 396 ILE ILE B . n 
B 1 271 HIS 271 397 397 HIS HIS B . n 
B 1 272 THR 272 398 398 THR THR B . n 
B 1 273 ASP 273 399 399 ASP ASP B . n 
B 1 274 VAL 274 400 400 VAL VAL B . n 
B 1 275 SER 275 401 401 SER SER B . n 
B 1 276 TYR 276 402 402 TYR TYR B . n 
B 1 277 ILE 277 403 403 ILE ILE B . n 
B 1 278 ALA 278 404 404 ALA ALA B . n 
B 1 279 CYS 279 405 405 CYS CYS B . n 
B 1 280 ALA 280 406 406 ALA ALA B . n 
B 1 281 ALA 281 407 407 ALA ALA B . n 
B 1 282 LYS 282 408 408 LYS LYS B . n 
B 1 283 LEU 283 409 409 LEU LEU B . n 
B 1 284 LEU 284 410 410 LEU LEU B . n 
B 1 285 ALA 285 411 411 ALA ALA B . n 
B 1 286 ALA 286 412 412 ALA ALA B . n 
B 1 287 THR 287 413 413 THR THR B . n 
B 1 288 ASP 288 414 414 ASP ASP B . n 
B 1 289 VAL 289 415 415 VAL VAL B . n 
B 1 290 VAL 290 416 416 VAL VAL B . n 
B 1 291 PHE 291 417 417 PHE PHE B . n 
B 1 292 PRO 292 418 418 PRO PRO B . n 
B 1 293 GLN 293 419 419 GLN GLN B . n 
B 1 294 PHE 294 420 420 PHE PHE B . n 
B 1 295 ALA 295 421 421 ALA ALA B . n 
B 1 296 THR 296 422 422 THR THR B . n 
B 1 297 HIS 297 423 423 HIS HIS B . n 
B 1 298 ASN 298 424 424 ASN ASN B . n 
B 1 299 ALA 299 425 425 ALA ALA B . n 
B 1 300 GLN 300 426 426 GLN GLN B . n 
B 1 301 THR 301 427 427 THR THR B . n 
B 1 302 LEU 302 428 428 LEU LEU B . n 
B 1 303 ALA 303 429 429 ALA ALA B . n 
B 1 304 ALA 304 430 430 ALA ALA B . n 
B 1 305 ILE 305 431 431 ILE ILE B . n 
B 1 306 TYR 306 432 432 TYR TYR B . n 
B 1 307 HIS 307 433 433 HIS HIS B . n 
B 1 308 MET 308 434 434 MET MET B . n 
B 1 309 ALA 309 435 435 ALA ALA B . n 
B 1 310 GLY 310 436 436 GLY GLY B . n 
B 1 311 LYS 311 437 437 LYS LYS B . n 
B 1 312 ASP 312 438 438 ASP ASP B . n 
B 1 313 PHE 313 439 439 PHE PHE B . n 
B 1 314 HIS 314 440 440 HIS HIS B . n 
B 1 315 VAL 315 441 441 VAL VAL B . n 
B 1 316 GLY 316 442 442 GLY GLY B . n 
B 1 317 LYS 317 443 443 LYS LYS B . n 
B 1 318 TYR 318 444 444 TYR TYR B . n 
B 1 319 GLU 319 445 445 GLU GLU B . n 
B 1 320 PHE 320 446 446 PHE PHE B . n 
B 1 321 GLN 321 447 447 GLN GLN B . n 
B 1 322 CYS 322 448 448 CYS CYS B . n 
B 1 323 LEU 323 449 449 LEU LEU B . n 
B 1 324 HIS 324 450 450 HIS HIS B . n 
B 1 325 GLY 325 451 451 GLY GLY B . n 
B 1 326 MET 326 452 452 MET MET B . n 
B 1 327 GLY 327 453 453 GLY GLY B . n 
B 1 328 GLU 328 454 454 GLU GLU B . n 
B 1 329 PRO 329 455 455 PRO PRO B . n 
B 1 330 LEU 330 456 456 LEU LEU B . n 
B 1 331 TYR 331 457 457 TYR TYR B . n 
B 1 332 GLU 332 458 458 GLU GLU B . n 
B 1 333 GLU 333 459 459 GLU GLU B . n 
B 1 334 VAL 334 460 460 VAL VAL B . n 
B 1 335 VAL 335 461 461 VAL VAL B . n 
B 1 336 GLY 336 462 462 GLY GLY B . n 
B 1 337 ARG 337 463 463 ARG ARG B . n 
B 1 338 GLY 338 464 464 GLY GLY B . n 
B 1 339 LYS 339 465 465 LYS LYS B . n 
B 1 340 LEU 340 466 466 LEU LEU B . n 
B 1 341 ASP 341 467 467 ASP ASP B . n 
B 1 342 ARG 342 468 468 ARG ARG B . n 
B 1 343 PRO 343 469 469 PRO PRO B . n 
B 1 344 CYS 344 470 470 CYS CYS B . n 
B 1 345 ARG 345 471 471 ARG ARG B . n 
B 1 346 ILE 346 472 472 ILE ILE B . n 
B 1 347 TYR 347 473 473 TYR TYR B . n 
B 1 348 ALA 348 474 474 ALA ALA B . n 
B 1 349 PRO 349 475 475 PRO PRO B . n 
B 1 350 VAL 350 476 476 VAL VAL B . n 
B 1 351 GLY 351 477 477 GLY GLY B . n 
B 1 352 THR 352 478 478 THR THR B . n 
B 1 353 HIS 353 479 479 HIS HIS B . n 
B 1 354 GLU 354 480 480 GLU GLU B . n 
B 1 355 THR 355 481 481 THR THR B . n 
B 1 356 LEU 356 482 482 LEU LEU B . n 
B 1 357 LEU 357 483 483 LEU LEU B . n 
B 1 358 ALA 358 484 484 ALA ALA B . n 
B 1 359 TYR 359 485 485 TYR TYR B . n 
B 1 360 LEU 360 486 486 LEU LEU B . n 
B 1 361 VAL 361 487 487 VAL VAL B . n 
B 1 362 ARG 362 488 488 ARG ARG B . n 
B 1 363 ARG 363 489 489 ARG ARG B . n 
B 1 364 LEU 364 490 490 LEU LEU B . n 
B 1 365 LEU 365 491 491 LEU LEU B . n 
B 1 366 GLU 366 492 492 GLU GLU B . n 
B 1 367 ASN 367 493 493 ASN ASN B . n 
B 1 368 GLY 368 494 494 GLY GLY B . n 
B 1 369 ALA 369 495 495 ALA ALA B . n 
B 1 370 ASN 370 496 496 ASN ASN B . n 
B 1 371 SER 371 497 497 SER SER B . n 
B 1 372 SER 372 498 498 SER SER B . n 
B 1 373 PHE 373 499 499 PHE PHE B . n 
B 1 374 VAL 374 500 500 VAL VAL B . n 
B 1 375 HIS 375 501 501 HIS HIS B . n 
B 1 376 ARG 376 502 502 ARG ARG B . n 
B 1 377 ILE 377 503 503 ILE ILE B . n 
B 1 378 ASN 378 504 504 ASN ASN B . n 
B 1 379 ASP 379 505 505 ASP ASP B . n 
B 1 380 PRO 380 506 506 PRO PRO B . n 
B 1 381 LYS 381 507 507 LYS LYS B . n 
B 1 382 VAL 382 508 508 VAL VAL B . n 
B 1 383 SER 383 509 509 SER SER B . n 
B 1 384 ILE 384 510 510 ILE ILE B . n 
B 1 385 ASP 385 511 511 ASP ASP B . n 
B 1 386 GLU 386 512 512 GLU GLU B . n 
B 1 387 LEU 387 513 513 LEU LEU B . n 
B 1 388 ILE 388 514 514 ILE ILE B . n 
B 1 389 ALA 389 515 515 ALA ALA B . n 
B 1 390 ASP 390 516 516 ASP ASP B . n 
B 1 391 PRO 391 517 517 PRO PRO B . n 
B 1 392 VAL 392 518 518 VAL VAL B . n 
B 1 393 GLU 393 519 519 GLU GLU B . n 
B 1 394 VAL 394 520 520 VAL VAL B . n 
B 1 395 VAL 395 521 521 VAL VAL B . n 
B 1 396 ARG 396 522 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BC6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BC6 
_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 A1BC6 1   601 601 A1BC6 FDA A . 
D 3 FMT   1   602 603 FMT   FMT A . 
E 2 A1BC6 1   601 601 A1BC6 FDA B . 
F 3 FMT   1   602 603 FMT   FMT B . 
G 4 HOH   1   701 289 HOH   HOH A . 
G 4 HOH   2   702 178 HOH   HOH A . 
G 4 HOH   3   703 96  HOH   HOH A . 
G 4 HOH   4   704 101 HOH   HOH A . 
G 4 HOH   5   705 130 HOH   HOH A . 
G 4 HOH   6   706 262 HOH   HOH A . 
G 4 HOH   7   707 80  HOH   HOH A . 
G 4 HOH   8   708 59  HOH   HOH A . 
G 4 HOH   9   709 144 HOH   HOH A . 
G 4 HOH   10  710 28  HOH   HOH A . 
G 4 HOH   11  711 49  HOH   HOH A . 
G 4 HOH   12  712 232 HOH   HOH A . 
G 4 HOH   13  713 60  HOH   HOH A . 
G 4 HOH   14  714 107 HOH   HOH A . 
G 4 HOH   15  715 57  HOH   HOH A . 
G 4 HOH   16  716 159 HOH   HOH A . 
G 4 HOH   17  717 256 HOH   HOH A . 
G 4 HOH   18  718 255 HOH   HOH A . 
G 4 HOH   19  719 79  HOH   HOH A . 
G 4 HOH   20  720 218 HOH   HOH A . 
G 4 HOH   21  721 7   HOH   HOH A . 
G 4 HOH   22  722 75  HOH   HOH A . 
G 4 HOH   23  723 146 HOH   HOH A . 
G 4 HOH   24  724 253 HOH   HOH A . 
G 4 HOH   25  725 43  HOH   HOH A . 
G 4 HOH   26  726 87  HOH   HOH A . 
G 4 HOH   27  727 176 HOH   HOH A . 
G 4 HOH   28  728 6   HOH   HOH A . 
G 4 HOH   29  729 220 HOH   HOH A . 
G 4 HOH   30  730 3   HOH   HOH A . 
G 4 HOH   31  731 123 HOH   HOH A . 
G 4 HOH   32  732 259 HOH   HOH A . 
G 4 HOH   33  733 99  HOH   HOH A . 
G 4 HOH   34  734 72  HOH   HOH A . 
G 4 HOH   35  735 171 HOH   HOH A . 
G 4 HOH   36  736 76  HOH   HOH A . 
G 4 HOH   37  737 164 HOH   HOH A . 
G 4 HOH   38  738 4   HOH   HOH A . 
G 4 HOH   39  739 222 HOH   HOH A . 
G 4 HOH   40  740 267 HOH   HOH A . 
G 4 HOH   41  741 106 HOH   HOH A . 
G 4 HOH   42  742 117 HOH   HOH A . 
G 4 HOH   43  743 266 HOH   HOH A . 
G 4 HOH   44  744 145 HOH   HOH A . 
G 4 HOH   45  745 244 HOH   HOH A . 
G 4 HOH   46  746 143 HOH   HOH A . 
G 4 HOH   47  747 52  HOH   HOH A . 
G 4 HOH   48  748 2   HOH   HOH A . 
G 4 HOH   49  749 92  HOH   HOH A . 
G 4 HOH   50  750 29  HOH   HOH A . 
G 4 HOH   51  751 168 HOH   HOH A . 
G 4 HOH   52  752 125 HOH   HOH A . 
G 4 HOH   53  753 216 HOH   HOH A . 
G 4 HOH   54  754 37  HOH   HOH A . 
G 4 HOH   55  755 31  HOH   HOH A . 
G 4 HOH   56  756 105 HOH   HOH A . 
G 4 HOH   57  757 64  HOH   HOH A . 
G 4 HOH   58  758 63  HOH   HOH A . 
G 4 HOH   59  759 226 HOH   HOH A . 
G 4 HOH   60  760 81  HOH   HOH A . 
G 4 HOH   61  761 207 HOH   HOH A . 
G 4 HOH   62  762 177 HOH   HOH A . 
G 4 HOH   63  763 173 HOH   HOH A . 
G 4 HOH   64  764 271 HOH   HOH A . 
G 4 HOH   65  765 9   HOH   HOH A . 
G 4 HOH   66  766 90  HOH   HOH A . 
G 4 HOH   67  767 134 HOH   HOH A . 
G 4 HOH   68  768 196 HOH   HOH A . 
G 4 HOH   69  769 24  HOH   HOH A . 
G 4 HOH   70  770 40  HOH   HOH A . 
G 4 HOH   71  771 86  HOH   HOH A . 
G 4 HOH   72  772 27  HOH   HOH A . 
G 4 HOH   73  773 198 HOH   HOH A . 
G 4 HOH   74  774 16  HOH   HOH A . 
G 4 HOH   75  775 68  HOH   HOH A . 
G 4 HOH   76  776 188 HOH   HOH A . 
G 4 HOH   77  777 228 HOH   HOH A . 
G 4 HOH   78  778 5   HOH   HOH A . 
G 4 HOH   79  779 88  HOH   HOH A . 
G 4 HOH   80  780 22  HOH   HOH A . 
G 4 HOH   81  781 128 HOH   HOH A . 
G 4 HOH   82  782 169 HOH   HOH A . 
G 4 HOH   83  783 47  HOH   HOH A . 
G 4 HOH   84  784 233 HOH   HOH A . 
G 4 HOH   85  785 122 HOH   HOH A . 
G 4 HOH   86  786 44  HOH   HOH A . 
G 4 HOH   87  787 58  HOH   HOH A . 
G 4 HOH   88  788 71  HOH   HOH A . 
G 4 HOH   89  789 167 HOH   HOH A . 
G 4 HOH   90  790 12  HOH   HOH A . 
G 4 HOH   91  791 102 HOH   HOH A . 
G 4 HOH   92  792 36  HOH   HOH A . 
G 4 HOH   93  793 240 HOH   HOH A . 
G 4 HOH   94  794 73  HOH   HOH A . 
G 4 HOH   95  795 110 HOH   HOH A . 
G 4 HOH   96  796 170 HOH   HOH A . 
G 4 HOH   97  797 11  HOH   HOH A . 
G 4 HOH   98  798 84  HOH   HOH A . 
G 4 HOH   99  799 119 HOH   HOH A . 
G 4 HOH   100 800 141 HOH   HOH A . 
G 4 HOH   101 801 179 HOH   HOH A . 
G 4 HOH   102 802 139 HOH   HOH A . 
G 4 HOH   103 803 120 HOH   HOH A . 
G 4 HOH   104 804 89  HOH   HOH A . 
G 4 HOH   105 805 183 HOH   HOH A . 
G 4 HOH   106 806 208 HOH   HOH A . 
G 4 HOH   107 807 189 HOH   HOH A . 
G 4 HOH   108 808 23  HOH   HOH A . 
G 4 HOH   109 809 270 HOH   HOH A . 
G 4 HOH   110 810 166 HOH   HOH A . 
G 4 HOH   111 811 152 HOH   HOH A . 
G 4 HOH   112 812 211 HOH   HOH A . 
G 4 HOH   113 813 181 HOH   HOH A . 
G 4 HOH   114 814 190 HOH   HOH A . 
G 4 HOH   115 815 163 HOH   HOH A . 
G 4 HOH   116 816 140 HOH   HOH A . 
G 4 HOH   117 817 234 HOH   HOH A . 
G 4 HOH   118 818 195 HOH   HOH A . 
G 4 HOH   119 819 54  HOH   HOH A . 
G 4 HOH   120 820 246 HOH   HOH A . 
G 4 HOH   121 821 85  HOH   HOH A . 
G 4 HOH   122 822 138 HOH   HOH A . 
G 4 HOH   123 823 263 HOH   HOH A . 
G 4 HOH   124 824 277 HOH   HOH A . 
G 4 HOH   125 825 280 HOH   HOH A . 
G 4 HOH   126 826 83  HOH   HOH A . 
G 4 HOH   127 827 243 HOH   HOH A . 
G 4 HOH   128 828 184 HOH   HOH A . 
G 4 HOH   129 829 229 HOH   HOH A . 
G 4 HOH   130 830 214 HOH   HOH A . 
G 4 HOH   131 831 239 HOH   HOH A . 
G 4 HOH   132 832 241 HOH   HOH A . 
G 4 HOH   133 833 192 HOH   HOH A . 
G 4 HOH   134 834 245 HOH   HOH A . 
G 4 HOH   135 835 104 HOH   HOH A . 
G 4 HOH   136 836 275 HOH   HOH A . 
G 4 HOH   137 837 124 HOH   HOH A . 
G 4 HOH   138 838 223 HOH   HOH A . 
G 4 HOH   139 839 230 HOH   HOH A . 
G 4 HOH   140 840 67  HOH   HOH A . 
G 4 HOH   141 841 200 HOH   HOH A . 
G 4 HOH   142 842 278 HOH   HOH A . 
G 4 HOH   143 843 212 HOH   HOH A . 
H 4 HOH   1   701 264 HOH   HOH B . 
H 4 HOH   2   702 30  HOH   HOH B . 
H 4 HOH   3   703 172 HOH   HOH B . 
H 4 HOH   4   704 191 HOH   HOH B . 
H 4 HOH   5   705 268 HOH   HOH B . 
H 4 HOH   6   706 111 HOH   HOH B . 
H 4 HOH   7   707 18  HOH   HOH B . 
H 4 HOH   8   708 45  HOH   HOH B . 
H 4 HOH   9   709 14  HOH   HOH B . 
H 4 HOH   10  710 282 HOH   HOH B . 
H 4 HOH   11  711 121 HOH   HOH B . 
H 4 HOH   12  712 53  HOH   HOH B . 
H 4 HOH   13  713 257 HOH   HOH B . 
H 4 HOH   14  714 155 HOH   HOH B . 
H 4 HOH   15  715 56  HOH   HOH B . 
H 4 HOH   16  716 247 HOH   HOH B . 
H 4 HOH   17  717 199 HOH   HOH B . 
H 4 HOH   18  718 202 HOH   HOH B . 
H 4 HOH   19  719 156 HOH   HOH B . 
H 4 HOH   20  720 19  HOH   HOH B . 
H 4 HOH   21  721 65  HOH   HOH B . 
H 4 HOH   22  722 91  HOH   HOH B . 
H 4 HOH   23  723 187 HOH   HOH B . 
H 4 HOH   24  724 42  HOH   HOH B . 
H 4 HOH   25  725 35  HOH   HOH B . 
H 4 HOH   26  726 39  HOH   HOH B . 
H 4 HOH   27  727 224 HOH   HOH B . 
H 4 HOH   28  728 205 HOH   HOH B . 
H 4 HOH   29  729 51  HOH   HOH B . 
H 4 HOH   30  730 32  HOH   HOH B . 
H 4 HOH   31  731 142 HOH   HOH B . 
H 4 HOH   32  732 34  HOH   HOH B . 
H 4 HOH   33  733 61  HOH   HOH B . 
H 4 HOH   34  734 1   HOH   HOH B . 
H 4 HOH   35  735 132 HOH   HOH B . 
H 4 HOH   36  736 108 HOH   HOH B . 
H 4 HOH   37  737 20  HOH   HOH B . 
H 4 HOH   38  738 165 HOH   HOH B . 
H 4 HOH   39  739 276 HOH   HOH B . 
H 4 HOH   40  740 15  HOH   HOH B . 
H 4 HOH   41  741 158 HOH   HOH B . 
H 4 HOH   42  742 260 HOH   HOH B . 
H 4 HOH   43  743 10  HOH   HOH B . 
H 4 HOH   44  744 154 HOH   HOH B . 
H 4 HOH   45  745 151 HOH   HOH B . 
H 4 HOH   46  746 13  HOH   HOH B . 
H 4 HOH   47  747 210 HOH   HOH B . 
H 4 HOH   48  748 286 HOH   HOH B . 
H 4 HOH   49  749 8   HOH   HOH B . 
H 4 HOH   50  750 62  HOH   HOH B . 
H 4 HOH   51  751 193 HOH   HOH B . 
H 4 HOH   52  752 94  HOH   HOH B . 
H 4 HOH   53  753 55  HOH   HOH B . 
H 4 HOH   54  754 17  HOH   HOH B . 
H 4 HOH   55  755 21  HOH   HOH B . 
H 4 HOH   56  756 265 HOH   HOH B . 
H 4 HOH   57  757 127 HOH   HOH B . 
H 4 HOH   58  758 115 HOH   HOH B . 
H 4 HOH   59  759 251 HOH   HOH B . 
H 4 HOH   60  760 26  HOH   HOH B . 
H 4 HOH   61  761 100 HOH   HOH B . 
H 4 HOH   62  762 38  HOH   HOH B . 
H 4 HOH   63  763 153 HOH   HOH B . 
H 4 HOH   64  764 66  HOH   HOH B . 
H 4 HOH   65  765 281 HOH   HOH B . 
H 4 HOH   66  766 95  HOH   HOH B . 
H 4 HOH   67  767 70  HOH   HOH B . 
H 4 HOH   68  768 157 HOH   HOH B . 
H 4 HOH   69  769 74  HOH   HOH B . 
H 4 HOH   70  770 129 HOH   HOH B . 
H 4 HOH   71  771 269 HOH   HOH B . 
H 4 HOH   72  772 126 HOH   HOH B . 
H 4 HOH   73  773 136 HOH   HOH B . 
H 4 HOH   74  774 114 HOH   HOH B . 
H 4 HOH   75  775 69  HOH   HOH B . 
H 4 HOH   76  776 182 HOH   HOH B . 
H 4 HOH   77  777 174 HOH   HOH B . 
H 4 HOH   78  778 33  HOH   HOH B . 
H 4 HOH   79  779 77  HOH   HOH B . 
H 4 HOH   80  780 46  HOH   HOH B . 
H 4 HOH   81  781 273 HOH   HOH B . 
H 4 HOH   82  782 41  HOH   HOH B . 
H 4 HOH   83  783 25  HOH   HOH B . 
H 4 HOH   84  784 180 HOH   HOH B . 
H 4 HOH   85  785 112 HOH   HOH B . 
H 4 HOH   86  786 113 HOH   HOH B . 
H 4 HOH   87  787 97  HOH   HOH B . 
H 4 HOH   88  788 201 HOH   HOH B . 
H 4 HOH   89  789 215 HOH   HOH B . 
H 4 HOH   90  790 48  HOH   HOH B . 
H 4 HOH   91  791 109 HOH   HOH B . 
H 4 HOH   92  792 231 HOH   HOH B . 
H 4 HOH   93  793 162 HOH   HOH B . 
H 4 HOH   94  794 82  HOH   HOH B . 
H 4 HOH   95  795 186 HOH   HOH B . 
H 4 HOH   96  796 221 HOH   HOH B . 
H 4 HOH   97  797 194 HOH   HOH B . 
H 4 HOH   98  798 197 HOH   HOH B . 
H 4 HOH   99  799 219 HOH   HOH B . 
H 4 HOH   100 800 213 HOH   HOH B . 
H 4 HOH   101 801 160 HOH   HOH B . 
H 4 HOH   102 802 225 HOH   HOH B . 
H 4 HOH   103 803 116 HOH   HOH B . 
H 4 HOH   104 804 285 HOH   HOH B . 
H 4 HOH   105 805 78  HOH   HOH B . 
H 4 HOH   106 806 217 HOH   HOH B . 
H 4 HOH   107 807 238 HOH   HOH B . 
H 4 HOH   108 808 242 HOH   HOH B . 
H 4 HOH   109 809 137 HOH   HOH B . 
H 4 HOH   110 810 249 HOH   HOH B . 
H 4 HOH   111 811 250 HOH   HOH B . 
H 4 HOH   112 812 209 HOH   HOH B . 
H 4 HOH   113 813 93  HOH   HOH B . 
H 4 HOH   114 814 248 HOH   HOH B . 
H 4 HOH   115 815 185 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 1 A GLN 28  ? CG  ? A GLN 4   CG  
2   1 Y 1 A GLN 28  ? CD  ? A GLN 4   CD  
3   1 Y 1 A GLN 28  ? OE1 ? A GLN 4   OE1 
4   1 Y 1 A GLN 28  ? NE2 ? A GLN 4   NE2 
5   1 Y 1 A ARG 32  ? CG  ? A ARG 8   CG  
6   1 Y 1 A ARG 32  ? CD  ? A ARG 8   CD  
7   1 Y 1 A ARG 32  ? NE  ? A ARG 8   NE  
8   1 Y 1 A ARG 32  ? CZ  ? A ARG 8   CZ  
9   1 Y 1 A ARG 32  ? NH1 ? A ARG 8   NH1 
10  1 Y 1 A ARG 32  ? NH2 ? A ARG 8   NH2 
11  1 Y 1 A ARG 33  ? CG  ? A ARG 9   CG  
12  1 Y 1 A ARG 33  ? CD  ? A ARG 9   CD  
13  1 Y 1 A ARG 33  ? NE  ? A ARG 9   NE  
14  1 Y 1 A ARG 33  ? CZ  ? A ARG 9   CZ  
15  1 Y 1 A ARG 33  ? NH1 ? A ARG 9   NH1 
16  1 Y 1 A ARG 33  ? NH2 ? A ARG 9   NH2 
17  1 Y 1 A THR 36  ? OG1 ? A THR 12  OG1 
18  1 Y 1 A THR 36  ? CG2 ? A THR 12  CG2 
19  1 Y 1 A THR 44  ? OG1 ? A THR 20  OG1 
20  1 Y 1 A THR 44  ? CG2 ? A THR 20  CG2 
21  1 Y 1 A GLU 45  ? CG  ? A GLU 21  CG  
22  1 Y 1 A GLU 45  ? CD  ? A GLU 21  CD  
23  1 Y 1 A GLU 45  ? OE1 ? A GLU 21  OE1 
24  1 Y 1 A GLU 45  ? OE2 ? A GLU 21  OE2 
25  1 Y 1 A VAL 51  ? CG1 ? A VAL 27  CG1 
26  1 Y 1 A VAL 51  ? CG2 ? A VAL 27  CG2 
27  1 Y 1 A GLU 52  ? CG  ? A GLU 28  CG  
28  1 Y 1 A GLU 52  ? CD  ? A GLU 28  CD  
29  1 Y 1 A GLU 52  ? OE1 ? A GLU 28  OE1 
30  1 Y 1 A GLU 52  ? OE2 ? A GLU 28  OE2 
31  1 Y 1 A GLN 56  ? CG  ? A GLN 32  CG  
32  1 Y 1 A GLN 56  ? CD  ? A GLN 32  CD  
33  1 Y 1 A GLN 56  ? OE1 ? A GLN 32  OE1 
34  1 Y 1 A GLN 56  ? NE2 ? A GLN 32  NE2 
35  1 Y 1 A GLU 59  ? CG  ? A GLU 35  CG  
36  1 Y 1 A GLU 59  ? CD  ? A GLU 35  CD  
37  1 Y 1 A GLU 59  ? OE1 ? A GLU 35  OE1 
38  1 Y 1 A GLU 59  ? OE2 ? A GLU 35  OE2 
39  1 Y 1 A SER 66  ? OG  ? A SER 42  OG  
40  1 Y 1 A LYS 70  ? CG  ? A LYS 46  CG  
41  1 Y 1 A LYS 70  ? CD  ? A LYS 46  CD  
42  1 Y 1 A LYS 70  ? CE  ? A LYS 46  CE  
43  1 Y 1 A LYS 70  ? NZ  ? A LYS 46  NZ  
44  1 Y 1 A LYS 78  ? CG  ? A LYS 54  CG  
45  1 Y 1 A LYS 78  ? CD  ? A LYS 54  CD  
46  1 Y 1 A LYS 78  ? CE  ? A LYS 54  CE  
47  1 Y 1 A LYS 78  ? NZ  ? A LYS 54  NZ  
48  1 Y 1 A HIS 79  ? CG  ? A HIS 55  CG  
49  1 Y 1 A HIS 79  ? ND1 ? A HIS 55  ND1 
50  1 Y 1 A HIS 79  ? CD2 ? A HIS 55  CD2 
51  1 Y 1 A HIS 79  ? CE1 ? A HIS 55  CE1 
52  1 Y 1 A HIS 79  ? NE2 ? A HIS 55  NE2 
53  1 Y 1 A GLU 193 ? CG  ? A GLU 67  CG  
54  1 Y 1 A GLU 193 ? CD  ? A GLU 67  CD  
55  1 Y 1 A GLU 193 ? OE1 ? A GLU 67  OE1 
56  1 Y 1 A GLU 193 ? OE2 ? A GLU 67  OE2 
57  1 Y 1 A ARG 202 ? CG  ? A ARG 76  CG  
58  1 Y 1 A ARG 202 ? CD  ? A ARG 76  CD  
59  1 Y 1 A ARG 202 ? NE  ? A ARG 76  NE  
60  1 Y 1 A ARG 202 ? CZ  ? A ARG 76  CZ  
61  1 Y 1 A ARG 202 ? NH1 ? A ARG 76  NH1 
62  1 Y 1 A ARG 202 ? NH2 ? A ARG 76  NH2 
63  1 Y 1 A GLU 203 ? CG  ? A GLU 77  CG  
64  1 Y 1 A GLU 203 ? CD  ? A GLU 77  CD  
65  1 Y 1 A GLU 203 ? OE1 ? A GLU 77  OE1 
66  1 Y 1 A GLU 203 ? OE2 ? A GLU 77  OE2 
67  1 Y 1 A LYS 206 ? CG  ? A LYS 80  CG  
68  1 Y 1 A LYS 206 ? CD  ? A LYS 80  CD  
69  1 Y 1 A LYS 206 ? CE  ? A LYS 80  CE  
70  1 Y 1 A LYS 206 ? NZ  ? A LYS 80  NZ  
71  1 Y 1 A LYS 209 ? CG  ? A LYS 83  CG  
72  1 Y 1 A LYS 209 ? CD  ? A LYS 83  CD  
73  1 Y 1 A LYS 209 ? CE  ? A LYS 83  CE  
74  1 Y 1 A LYS 209 ? NZ  ? A LYS 83  NZ  
75  1 Y 1 A GLU 210 ? CG  ? A GLU 84  CG  
76  1 Y 1 A GLU 210 ? CD  ? A GLU 84  CD  
77  1 Y 1 A GLU 210 ? OE1 ? A GLU 84  OE1 
78  1 Y 1 A GLU 210 ? OE2 ? A GLU 84  OE2 
79  1 Y 1 A LEU 223 ? CG  ? A LEU 97  CG  
80  1 Y 1 A LEU 223 ? CD1 ? A LEU 97  CD1 
81  1 Y 1 A LEU 223 ? CD2 ? A LEU 97  CD2 
82  1 Y 1 A THR 229 ? OG1 ? A THR 103 OG1 
83  1 Y 1 A THR 229 ? CG2 ? A THR 103 CG2 
84  1 Y 1 A GLU 234 ? CG  ? A GLU 108 CG  
85  1 Y 1 A GLU 234 ? CD  ? A GLU 108 CD  
86  1 Y 1 A GLU 234 ? OE1 ? A GLU 108 OE1 
87  1 Y 1 A GLU 234 ? OE2 ? A GLU 108 OE2 
88  1 Y 1 A ARG 235 ? CG  ? A ARG 109 CG  
89  1 Y 1 A ARG 235 ? CD  ? A ARG 109 CD  
90  1 Y 1 A ARG 235 ? NE  ? A ARG 109 NE  
91  1 Y 1 A ARG 235 ? CZ  ? A ARG 109 CZ  
92  1 Y 1 A ARG 235 ? NH1 ? A ARG 109 NH1 
93  1 Y 1 A ARG 235 ? NH2 ? A ARG 109 NH2 
94  1 Y 1 A ARG 238 ? CG  ? A ARG 112 CG  
95  1 Y 1 A ARG 238 ? CD  ? A ARG 112 CD  
96  1 Y 1 A ARG 238 ? NE  ? A ARG 112 NE  
97  1 Y 1 A ARG 238 ? CZ  ? A ARG 112 CZ  
98  1 Y 1 A ARG 238 ? NH1 ? A ARG 112 NH1 
99  1 Y 1 A ARG 238 ? NH2 ? A ARG 112 NH2 
100 1 Y 1 A ARG 272 ? CG  ? A ARG 146 CG  
101 1 Y 1 A ARG 272 ? CD  ? A ARG 146 CD  
102 1 Y 1 A ARG 272 ? NE  ? A ARG 146 NE  
103 1 Y 1 A ARG 272 ? CZ  ? A ARG 146 CZ  
104 1 Y 1 A ARG 272 ? NH1 ? A ARG 146 NH1 
105 1 Y 1 A ARG 272 ? NH2 ? A ARG 146 NH2 
106 1 Y 1 A SER 274 ? OG  ? A SER 148 OG  
107 1 Y 1 A ARG 275 ? CG  ? A ARG 149 CG  
108 1 Y 1 A ARG 275 ? CD  ? A ARG 149 CD  
109 1 Y 1 A ARG 275 ? NE  ? A ARG 149 NE  
110 1 Y 1 A ARG 275 ? CZ  ? A ARG 149 CZ  
111 1 Y 1 A ARG 275 ? NH1 ? A ARG 149 NH1 
112 1 Y 1 A ARG 275 ? NH2 ? A ARG 149 NH2 
113 1 Y 1 A GLN 277 ? CG  ? A GLN 151 CG  
114 1 Y 1 A GLN 277 ? CD  ? A GLN 151 CD  
115 1 Y 1 A GLN 277 ? OE1 ? A GLN 151 OE1 
116 1 Y 1 A GLN 277 ? NE2 ? A GLN 151 NE2 
117 1 Y 1 A ARG 280 ? CG  ? A ARG 154 CG  
118 1 Y 1 A ARG 280 ? CD  ? A ARG 154 CD  
119 1 Y 1 A ARG 280 ? NE  ? A ARG 154 NE  
120 1 Y 1 A ARG 280 ? CZ  ? A ARG 154 CZ  
121 1 Y 1 A ARG 280 ? NH1 ? A ARG 154 NH1 
122 1 Y 1 A ARG 280 ? NH2 ? A ARG 154 NH2 
123 1 Y 1 A VAL 281 ? CG1 ? A VAL 155 CG1 
124 1 Y 1 A VAL 281 ? CG2 ? A VAL 155 CG2 
125 1 Y 1 A GLU 284 ? CG  ? A GLU 158 CG  
126 1 Y 1 A GLU 284 ? CD  ? A GLU 158 CD  
127 1 Y 1 A GLU 284 ? OE1 ? A GLU 158 OE1 
128 1 Y 1 A GLU 284 ? OE2 ? A GLU 158 OE2 
129 1 Y 1 A LEU 294 ? CG  ? A LEU 168 CG  
130 1 Y 1 A LEU 294 ? CD1 ? A LEU 168 CD1 
131 1 Y 1 A LEU 294 ? CD2 ? A LEU 168 CD2 
132 1 Y 1 A LEU 315 ? CG  ? A LEU 189 CG  
133 1 Y 1 A LEU 315 ? CD1 ? A LEU 189 CD1 
134 1 Y 1 A LEU 315 ? CD2 ? A LEU 189 CD2 
135 1 Y 1 A SER 330 ? OG  ? A SER 204 OG  
136 1 Y 1 A LYS 379 ? CG  ? A LYS 253 CG  
137 1 Y 1 A LYS 379 ? CD  ? A LYS 253 CD  
138 1 Y 1 A LYS 379 ? CE  ? A LYS 253 CE  
139 1 Y 1 A LYS 379 ? NZ  ? A LYS 253 NZ  
140 1 Y 1 A ARG 380 ? CG  ? A ARG 254 CG  
141 1 Y 1 A ARG 380 ? CD  ? A ARG 254 CD  
142 1 Y 1 A ARG 380 ? NE  ? A ARG 254 NE  
143 1 Y 1 A ARG 380 ? CZ  ? A ARG 254 CZ  
144 1 Y 1 A ARG 380 ? NH1 ? A ARG 254 NH1 
145 1 Y 1 A ARG 380 ? NH2 ? A ARG 254 NH2 
146 1 Y 1 A LEU 383 ? CG  ? A LEU 257 CG  
147 1 Y 1 A LEU 383 ? CD1 ? A LEU 257 CD1 
148 1 Y 1 A LEU 383 ? CD2 ? A LEU 257 CD2 
149 1 Y 1 A ASP 384 ? CG  ? A ASP 258 CG  
150 1 Y 1 A ASP 384 ? OD1 ? A ASP 258 OD1 
151 1 Y 1 A ASP 384 ? OD2 ? A ASP 258 OD2 
152 1 Y 1 A ASP 388 ? CG  ? A ASP 262 CG  
153 1 Y 1 A ASP 388 ? OD1 ? A ASP 262 OD1 
154 1 Y 1 A ASP 388 ? OD2 ? A ASP 262 OD2 
155 1 Y 1 A ARG 394 ? CG  ? A ARG 268 CG  
156 1 Y 1 A ARG 394 ? CD  ? A ARG 268 CD  
157 1 Y 1 A ARG 394 ? NE  ? A ARG 268 NE  
158 1 Y 1 A ARG 394 ? CZ  ? A ARG 268 CZ  
159 1 Y 1 A ARG 394 ? NH1 ? A ARG 268 NH1 
160 1 Y 1 A ARG 394 ? NH2 ? A ARG 268 NH2 
161 1 Y 1 A LYS 437 ? CG  ? A LYS 311 CG  
162 1 Y 1 A LYS 437 ? CD  ? A LYS 311 CD  
163 1 Y 1 A LYS 437 ? CE  ? A LYS 311 CE  
164 1 Y 1 A LYS 437 ? NZ  ? A LYS 311 NZ  
165 1 Y 1 A ARG 463 ? CG  ? A ARG 337 CG  
166 1 Y 1 A ARG 463 ? CD  ? A ARG 337 CD  
167 1 Y 1 A ARG 463 ? NE  ? A ARG 337 NE  
168 1 Y 1 A ARG 463 ? CZ  ? A ARG 337 CZ  
169 1 Y 1 A ARG 463 ? NH1 ? A ARG 337 NH1 
170 1 Y 1 A ARG 463 ? NH2 ? A ARG 337 NH2 
171 1 Y 1 A LEU 482 ? CG  ? A LEU 356 CG  
172 1 Y 1 A LEU 482 ? CD1 ? A LEU 356 CD1 
173 1 Y 1 A LEU 482 ? CD2 ? A LEU 356 CD2 
174 1 Y 1 A LEU 486 ? CG  ? A LEU 360 CG  
175 1 Y 1 A LEU 486 ? CD1 ? A LEU 360 CD1 
176 1 Y 1 A LEU 486 ? CD2 ? A LEU 360 CD2 
177 1 Y 1 A ASN 496 ? CG  ? A ASN 370 CG  
178 1 Y 1 A ASN 496 ? OD1 ? A ASN 370 OD1 
179 1 Y 1 A ASN 496 ? ND2 ? A ASN 370 ND2 
180 1 Y 1 A LYS 507 ? CG  ? A LYS 381 CG  
181 1 Y 1 A LYS 507 ? CD  ? A LYS 381 CD  
182 1 Y 1 A LYS 507 ? CE  ? A LYS 381 CE  
183 1 Y 1 A LYS 507 ? NZ  ? A LYS 381 NZ  
184 1 Y 1 A VAL 520 ? CG1 ? A VAL 394 CG1 
185 1 Y 1 A VAL 520 ? CG2 ? A VAL 394 CG2 
186 1 Y 1 B ARG 26  ? CG  ? B ARG 2   CG  
187 1 Y 1 B ARG 26  ? CD  ? B ARG 2   CD  
188 1 Y 1 B ARG 26  ? NE  ? B ARG 2   NE  
189 1 Y 1 B ARG 26  ? CZ  ? B ARG 2   CZ  
190 1 Y 1 B ARG 26  ? NH1 ? B ARG 2   NH1 
191 1 Y 1 B ARG 26  ? NH2 ? B ARG 2   NH2 
192 1 Y 1 B SER 29  ? OG  ? B SER 5   OG  
193 1 Y 1 B ARG 33  ? CG  ? B ARG 9   CG  
194 1 Y 1 B ARG 33  ? CD  ? B ARG 9   CD  
195 1 Y 1 B ARG 33  ? NE  ? B ARG 9   NE  
196 1 Y 1 B ARG 33  ? CZ  ? B ARG 9   CZ  
197 1 Y 1 B ARG 33  ? NH1 ? B ARG 9   NH1 
198 1 Y 1 B ARG 33  ? NH2 ? B ARG 9   NH2 
199 1 Y 1 B ARG 40  ? CG  ? B ARG 16  CG  
200 1 Y 1 B ARG 40  ? CD  ? B ARG 16  CD  
201 1 Y 1 B ARG 40  ? NE  ? B ARG 16  NE  
202 1 Y 1 B ARG 40  ? CZ  ? B ARG 16  CZ  
203 1 Y 1 B ARG 40  ? NH1 ? B ARG 16  NH1 
204 1 Y 1 B ARG 40  ? NH2 ? B ARG 16  NH2 
205 1 Y 1 B VAL 51  ? CG1 ? B VAL 27  CG1 
206 1 Y 1 B VAL 51  ? CG2 ? B VAL 27  CG2 
207 1 Y 1 B GLU 52  ? CG  ? B GLU 28  CG  
208 1 Y 1 B GLU 52  ? CD  ? B GLU 28  CD  
209 1 Y 1 B GLU 52  ? OE1 ? B GLU 28  OE1 
210 1 Y 1 B GLU 52  ? OE2 ? B GLU 28  OE2 
211 1 Y 1 B THR 55  ? OG1 ? B THR 31  OG1 
212 1 Y 1 B THR 55  ? CG2 ? B THR 31  CG2 
213 1 Y 1 B GLN 56  ? CG  ? B GLN 32  CG  
214 1 Y 1 B GLN 56  ? CD  ? B GLN 32  CD  
215 1 Y 1 B GLN 56  ? OE1 ? B GLN 32  OE1 
216 1 Y 1 B GLN 56  ? NE2 ? B GLN 32  NE2 
217 1 Y 1 B SER 57  ? OG  ? B SER 33  OG  
218 1 Y 1 B LYS 58  ? CG  ? B LYS 34  CG  
219 1 Y 1 B LYS 58  ? CD  ? B LYS 34  CD  
220 1 Y 1 B LYS 58  ? CE  ? B LYS 34  CE  
221 1 Y 1 B LYS 58  ? NZ  ? B LYS 34  NZ  
222 1 Y 1 B GLU 59  ? CG  ? B GLU 35  CG  
223 1 Y 1 B GLU 59  ? CD  ? B GLU 35  CD  
224 1 Y 1 B GLU 59  ? OE1 ? B GLU 35  OE1 
225 1 Y 1 B GLU 59  ? OE2 ? B GLU 35  OE2 
226 1 Y 1 B ASP 62  ? CG  ? B ASP 38  CG  
227 1 Y 1 B ASP 62  ? OD1 ? B ASP 38  OD1 
228 1 Y 1 B ASP 62  ? OD2 ? B ASP 38  OD2 
229 1 Y 1 B GLU 73  ? CG  ? B GLU 49  CG  
230 1 Y 1 B GLU 73  ? CD  ? B GLU 49  CD  
231 1 Y 1 B GLU 73  ? OE1 ? B GLU 49  OE1 
232 1 Y 1 B GLU 73  ? OE2 ? B GLU 49  OE2 
233 1 Y 1 B LYS 78  ? CG  ? B LYS 54  CG  
234 1 Y 1 B LYS 78  ? CD  ? B LYS 54  CD  
235 1 Y 1 B LYS 78  ? CE  ? B LYS 54  CE  
236 1 Y 1 B LYS 78  ? NZ  ? B LYS 54  NZ  
237 1 Y 1 B HIS 79  ? CG  ? B HIS 55  CG  
238 1 Y 1 B HIS 79  ? ND1 ? B HIS 55  ND1 
239 1 Y 1 B HIS 79  ? CD2 ? B HIS 55  CD2 
240 1 Y 1 B HIS 79  ? CE1 ? B HIS 55  CE1 
241 1 Y 1 B HIS 79  ? NE2 ? B HIS 55  NE2 
242 1 Y 1 B GLU 193 ? CG  ? B GLU 67  CG  
243 1 Y 1 B GLU 193 ? CD  ? B GLU 67  CD  
244 1 Y 1 B GLU 193 ? OE1 ? B GLU 67  OE1 
245 1 Y 1 B GLU 193 ? OE2 ? B GLU 67  OE2 
246 1 Y 1 B VAL 196 ? CG1 ? B VAL 70  CG1 
247 1 Y 1 B VAL 196 ? CG2 ? B VAL 70  CG2 
248 1 Y 1 B THR 197 ? OG1 ? B THR 71  OG1 
249 1 Y 1 B THR 197 ? CG2 ? B THR 71  CG2 
250 1 Y 1 B GLU 199 ? CG  ? B GLU 73  CG  
251 1 Y 1 B GLU 199 ? CD  ? B GLU 73  CD  
252 1 Y 1 B GLU 199 ? OE1 ? B GLU 73  OE1 
253 1 Y 1 B GLU 199 ? OE2 ? B GLU 73  OE2 
254 1 Y 1 B THR 200 ? OG1 ? B THR 74  OG1 
255 1 Y 1 B THR 200 ? CG2 ? B THR 74  CG2 
256 1 Y 1 B ILE 201 ? CG1 ? B ILE 75  CG1 
257 1 Y 1 B ILE 201 ? CG2 ? B ILE 75  CG2 
258 1 Y 1 B ILE 201 ? CD1 ? B ILE 75  CD1 
259 1 Y 1 B ARG 202 ? CG  ? B ARG 76  CG  
260 1 Y 1 B ARG 202 ? CD  ? B ARG 76  CD  
261 1 Y 1 B ARG 202 ? NE  ? B ARG 76  NE  
262 1 Y 1 B ARG 202 ? CZ  ? B ARG 76  CZ  
263 1 Y 1 B ARG 202 ? NH1 ? B ARG 76  NH1 
264 1 Y 1 B ARG 202 ? NH2 ? B ARG 76  NH2 
265 1 Y 1 B GLU 203 ? CG  ? B GLU 77  CG  
266 1 Y 1 B GLU 203 ? CD  ? B GLU 77  CD  
267 1 Y 1 B GLU 203 ? OE1 ? B GLU 77  OE1 
268 1 Y 1 B GLU 203 ? OE2 ? B GLU 77  OE2 
269 1 Y 1 B LEU 205 ? CG  ? B LEU 79  CG  
270 1 Y 1 B LEU 205 ? CD1 ? B LEU 79  CD1 
271 1 Y 1 B LEU 205 ? CD2 ? B LEU 79  CD2 
272 1 Y 1 B LYS 206 ? CG  ? B LYS 80  CG  
273 1 Y 1 B LYS 206 ? CD  ? B LYS 80  CD  
274 1 Y 1 B LYS 206 ? CE  ? B LYS 80  CE  
275 1 Y 1 B LYS 206 ? NZ  ? B LYS 80  NZ  
276 1 Y 1 B ARG 207 ? CG  ? B ARG 81  CG  
277 1 Y 1 B ARG 207 ? CD  ? B ARG 81  CD  
278 1 Y 1 B ARG 207 ? NE  ? B ARG 81  NE  
279 1 Y 1 B ARG 207 ? CZ  ? B ARG 81  CZ  
280 1 Y 1 B ARG 207 ? NH1 ? B ARG 81  NH1 
281 1 Y 1 B ARG 207 ? NH2 ? B ARG 81  NH2 
282 1 Y 1 B SER 208 ? OG  ? B SER 82  OG  
283 1 Y 1 B LYS 209 ? CG  ? B LYS 83  CG  
284 1 Y 1 B LYS 209 ? CD  ? B LYS 83  CD  
285 1 Y 1 B LYS 209 ? CE  ? B LYS 83  CE  
286 1 Y 1 B LYS 209 ? NZ  ? B LYS 83  NZ  
287 1 Y 1 B GLU 210 ? CG  ? B GLU 84  CG  
288 1 Y 1 B GLU 210 ? CD  ? B GLU 84  CD  
289 1 Y 1 B GLU 210 ? OE1 ? B GLU 84  OE1 
290 1 Y 1 B GLU 210 ? OE2 ? B GLU 84  OE2 
291 1 Y 1 B GLU 213 ? CG  ? B GLU 87  CG  
292 1 Y 1 B GLU 213 ? CD  ? B GLU 87  CD  
293 1 Y 1 B GLU 213 ? OE1 ? B GLU 87  OE1 
294 1 Y 1 B GLU 213 ? OE2 ? B GLU 87  OE2 
295 1 Y 1 B LYS 214 ? CG  ? B LYS 88  CG  
296 1 Y 1 B LYS 214 ? CD  ? B LYS 88  CD  
297 1 Y 1 B LYS 214 ? CE  ? B LYS 88  CE  
298 1 Y 1 B LYS 214 ? NZ  ? B LYS 88  NZ  
299 1 Y 1 B LEU 223 ? CG  ? B LEU 97  CG  
300 1 Y 1 B LEU 223 ? CD1 ? B LEU 97  CD1 
301 1 Y 1 B LEU 223 ? CD2 ? B LEU 97  CD2 
302 1 Y 1 B THR 228 ? OG1 ? B THR 102 OG1 
303 1 Y 1 B THR 228 ? CG2 ? B THR 102 CG2 
304 1 Y 1 B THR 229 ? OG1 ? B THR 103 OG1 
305 1 Y 1 B THR 229 ? CG2 ? B THR 103 CG2 
306 1 Y 1 B ASP 232 ? CG  ? B ASP 106 CG  
307 1 Y 1 B ASP 232 ? OD1 ? B ASP 106 OD1 
308 1 Y 1 B ASP 232 ? OD2 ? B ASP 106 OD2 
309 1 Y 1 B GLU 234 ? CG  ? B GLU 108 CG  
310 1 Y 1 B GLU 234 ? CD  ? B GLU 108 CD  
311 1 Y 1 B GLU 234 ? OE1 ? B GLU 108 OE1 
312 1 Y 1 B GLU 234 ? OE2 ? B GLU 108 OE2 
313 1 Y 1 B ARG 235 ? CG  ? B ARG 109 CG  
314 1 Y 1 B ARG 235 ? CD  ? B ARG 109 CD  
315 1 Y 1 B ARG 235 ? NE  ? B ARG 109 NE  
316 1 Y 1 B ARG 235 ? CZ  ? B ARG 109 CZ  
317 1 Y 1 B ARG 235 ? NH1 ? B ARG 109 NH1 
318 1 Y 1 B ARG 235 ? NH2 ? B ARG 109 NH2 
319 1 Y 1 B ARG 238 ? CG  ? B ARG 112 CG  
320 1 Y 1 B ARG 238 ? CD  ? B ARG 112 CD  
321 1 Y 1 B ARG 238 ? NE  ? B ARG 112 NE  
322 1 Y 1 B ARG 238 ? CZ  ? B ARG 112 CZ  
323 1 Y 1 B ARG 238 ? NH1 ? B ARG 112 NH1 
324 1 Y 1 B ARG 238 ? NH2 ? B ARG 112 NH2 
325 1 Y 1 B ASP 239 ? CG  ? B ASP 113 CG  
326 1 Y 1 B ASP 239 ? OD1 ? B ASP 113 OD1 
327 1 Y 1 B ASP 239 ? OD2 ? B ASP 113 OD2 
328 1 Y 1 B SER 242 ? OG  ? B SER 116 OG  
329 1 Y 1 B LYS 249 ? CG  ? B LYS 123 CG  
330 1 Y 1 B LYS 249 ? CD  ? B LYS 123 CD  
331 1 Y 1 B LYS 249 ? CE  ? B LYS 123 CE  
332 1 Y 1 B LYS 249 ? NZ  ? B LYS 123 NZ  
333 1 Y 1 B GLU 258 ? CG  ? B GLU 132 CG  
334 1 Y 1 B GLU 258 ? CD  ? B GLU 132 CD  
335 1 Y 1 B GLU 258 ? OE1 ? B GLU 132 OE1 
336 1 Y 1 B GLU 258 ? OE2 ? B GLU 132 OE2 
337 1 Y 1 B ARG 272 ? CG  ? B ARG 146 CG  
338 1 Y 1 B ARG 272 ? CD  ? B ARG 146 CD  
339 1 Y 1 B ARG 272 ? NE  ? B ARG 146 NE  
340 1 Y 1 B ARG 272 ? CZ  ? B ARG 146 CZ  
341 1 Y 1 B ARG 272 ? NH1 ? B ARG 146 NH1 
342 1 Y 1 B ARG 272 ? NH2 ? B ARG 146 NH2 
343 1 Y 1 B SER 274 ? OG  ? B SER 148 OG  
344 1 Y 1 B ARG 275 ? CG  ? B ARG 149 CG  
345 1 Y 1 B ARG 275 ? CD  ? B ARG 149 CD  
346 1 Y 1 B ARG 275 ? NE  ? B ARG 149 NE  
347 1 Y 1 B ARG 275 ? CZ  ? B ARG 149 CZ  
348 1 Y 1 B ARG 275 ? NH1 ? B ARG 149 NH1 
349 1 Y 1 B ARG 275 ? NH2 ? B ARG 149 NH2 
350 1 Y 1 B GLN 277 ? CG  ? B GLN 151 CG  
351 1 Y 1 B GLN 277 ? CD  ? B GLN 151 CD  
352 1 Y 1 B GLN 277 ? OE1 ? B GLN 151 OE1 
353 1 Y 1 B GLN 277 ? NE2 ? B GLN 151 NE2 
354 1 Y 1 B ARG 280 ? CG  ? B ARG 154 CG  
355 1 Y 1 B ARG 280 ? CD  ? B ARG 154 CD  
356 1 Y 1 B ARG 280 ? NE  ? B ARG 154 NE  
357 1 Y 1 B ARG 280 ? CZ  ? B ARG 154 CZ  
358 1 Y 1 B ARG 280 ? NH1 ? B ARG 154 NH1 
359 1 Y 1 B ARG 280 ? NH2 ? B ARG 154 NH2 
360 1 Y 1 B VAL 281 ? CG1 ? B VAL 155 CG1 
361 1 Y 1 B VAL 281 ? CG2 ? B VAL 155 CG2 
362 1 Y 1 B GLU 284 ? CG  ? B GLU 158 CG  
363 1 Y 1 B GLU 284 ? CD  ? B GLU 158 CD  
364 1 Y 1 B GLU 284 ? OE1 ? B GLU 158 OE1 
365 1 Y 1 B GLU 284 ? OE2 ? B GLU 158 OE2 
366 1 Y 1 B LEU 286 ? CG  ? B LEU 160 CG  
367 1 Y 1 B LEU 286 ? CD1 ? B LEU 160 CD1 
368 1 Y 1 B LEU 286 ? CD2 ? B LEU 160 CD2 
369 1 Y 1 B ARG 288 ? CG  ? B ARG 162 CG  
370 1 Y 1 B ARG 288 ? CD  ? B ARG 162 CD  
371 1 Y 1 B ARG 288 ? NE  ? B ARG 162 NE  
372 1 Y 1 B ARG 288 ? CZ  ? B ARG 162 CZ  
373 1 Y 1 B ARG 288 ? NH1 ? B ARG 162 NH1 
374 1 Y 1 B ARG 288 ? NH2 ? B ARG 162 NH2 
375 1 Y 1 B GLU 314 ? CG  ? B GLU 188 CG  
376 1 Y 1 B GLU 314 ? CD  ? B GLU 188 CD  
377 1 Y 1 B GLU 314 ? OE1 ? B GLU 188 OE1 
378 1 Y 1 B GLU 314 ? OE2 ? B GLU 188 OE2 
379 1 Y 1 B LEU 315 ? CG  ? B LEU 189 CG  
380 1 Y 1 B LEU 315 ? CD1 ? B LEU 189 CD1 
381 1 Y 1 B LEU 315 ? CD2 ? B LEU 189 CD2 
382 1 Y 1 B LYS 379 ? CG  ? B LYS 253 CG  
383 1 Y 1 B LYS 379 ? CD  ? B LYS 253 CD  
384 1 Y 1 B LYS 379 ? CE  ? B LYS 253 CE  
385 1 Y 1 B LYS 379 ? NZ  ? B LYS 253 NZ  
386 1 Y 1 B LEU 383 ? CG  ? B LEU 257 CG  
387 1 Y 1 B LEU 383 ? CD1 ? B LEU 257 CD1 
388 1 Y 1 B LEU 383 ? CD2 ? B LEU 257 CD2 
389 1 Y 1 B ARG 394 ? CG  ? B ARG 268 CG  
390 1 Y 1 B ARG 394 ? CD  ? B ARG 268 CD  
391 1 Y 1 B ARG 394 ? NE  ? B ARG 268 NE  
392 1 Y 1 B ARG 394 ? CZ  ? B ARG 268 CZ  
393 1 Y 1 B ARG 394 ? NH1 ? B ARG 268 NH1 
394 1 Y 1 B ARG 394 ? NH2 ? B ARG 268 NH2 
395 1 Y 1 B LYS 437 ? CG  ? B LYS 311 CG  
396 1 Y 1 B LYS 437 ? CD  ? B LYS 311 CD  
397 1 Y 1 B LYS 437 ? CE  ? B LYS 311 CE  
398 1 Y 1 B LYS 437 ? NZ  ? B LYS 311 NZ  
399 1 Y 1 B ASP 438 ? CG  ? B ASP 312 CG  
400 1 Y 1 B ASP 438 ? OD1 ? B ASP 312 OD1 
401 1 Y 1 B ASP 438 ? OD2 ? B ASP 312 OD2 
402 1 Y 1 B VAL 441 ? CG1 ? B VAL 315 CG1 
403 1 Y 1 B VAL 441 ? CG2 ? B VAL 315 CG2 
404 1 Y 1 B GLU 458 ? CG  ? B GLU 332 CG  
405 1 Y 1 B GLU 458 ? CD  ? B GLU 332 CD  
406 1 Y 1 B GLU 458 ? OE1 ? B GLU 332 OE1 
407 1 Y 1 B GLU 458 ? OE2 ? B GLU 332 OE2 
408 1 Y 1 B ARG 463 ? CG  ? B ARG 337 CG  
409 1 Y 1 B ARG 463 ? CD  ? B ARG 337 CD  
410 1 Y 1 B ARG 463 ? NE  ? B ARG 337 NE  
411 1 Y 1 B ARG 463 ? CZ  ? B ARG 337 CZ  
412 1 Y 1 B ARG 463 ? NH1 ? B ARG 337 NH1 
413 1 Y 1 B ARG 463 ? NH2 ? B ARG 337 NH2 
414 1 Y 1 B VAL 476 ? CG1 ? B VAL 350 CG1 
415 1 Y 1 B VAL 476 ? CG2 ? B VAL 350 CG2 
416 1 Y 1 B THR 478 ? OG1 ? B THR 352 OG1 
417 1 Y 1 B THR 478 ? CG2 ? B THR 352 CG2 
418 1 Y 1 B HIS 479 ? CG  ? B HIS 353 CG  
419 1 Y 1 B HIS 479 ? ND1 ? B HIS 353 ND1 
420 1 Y 1 B HIS 479 ? CD2 ? B HIS 353 CD2 
421 1 Y 1 B HIS 479 ? CE1 ? B HIS 353 CE1 
422 1 Y 1 B HIS 479 ? NE2 ? B HIS 353 NE2 
423 1 Y 1 B GLU 480 ? CG  ? B GLU 354 CG  
424 1 Y 1 B GLU 480 ? CD  ? B GLU 354 CD  
425 1 Y 1 B GLU 480 ? OE1 ? B GLU 354 OE1 
426 1 Y 1 B GLU 480 ? OE2 ? B GLU 354 OE2 
427 1 Y 1 B THR 481 ? OG1 ? B THR 355 OG1 
428 1 Y 1 B THR 481 ? CG2 ? B THR 355 CG2 
429 1 Y 1 B LEU 482 ? CG  ? B LEU 356 CG  
430 1 Y 1 B LEU 482 ? CD1 ? B LEU 356 CD1 
431 1 Y 1 B LEU 482 ? CD2 ? B LEU 356 CD2 
432 1 Y 1 B LEU 483 ? CG  ? B LEU 357 CG  
433 1 Y 1 B LEU 483 ? CD1 ? B LEU 357 CD1 
434 1 Y 1 B LEU 483 ? CD2 ? B LEU 357 CD2 
435 1 Y 1 B LEU 486 ? CG  ? B LEU 360 CG  
436 1 Y 1 B LEU 486 ? CD1 ? B LEU 360 CD1 
437 1 Y 1 B LEU 486 ? CD2 ? B LEU 360 CD2 
438 1 Y 1 B ASN 496 ? CG  ? B ASN 370 CG  
439 1 Y 1 B ASN 496 ? OD1 ? B ASN 370 OD1 
440 1 Y 1 B ASN 496 ? ND2 ? B ASN 370 ND2 
441 1 Y 1 B LYS 507 ? CG  ? B LYS 381 CG  
442 1 Y 1 B LYS 507 ? CD  ? B LYS 381 CD  
443 1 Y 1 B LYS 507 ? CE  ? B LYS 381 CE  
444 1 Y 1 B LYS 507 ? NZ  ? B LYS 381 NZ  
445 1 Y 1 B GLU 512 ? CG  ? B GLU 386 CG  
446 1 Y 1 B GLU 512 ? CD  ? B GLU 386 CD  
447 1 Y 1 B GLU 512 ? OE1 ? B GLU 386 OE1 
448 1 Y 1 B GLU 512 ? OE2 ? B GLU 386 OE2 
449 1 Y 1 B VAL 518 ? CG1 ? B VAL 392 CG1 
450 1 Y 1 B VAL 518 ? CG2 ? B VAL 392 CG2 
451 1 Y 1 B GLU 519 ? CG  ? B GLU 393 CG  
452 1 Y 1 B GLU 519 ? CD  ? B GLU 393 CD  
453 1 Y 1 B GLU 519 ? OE1 ? B GLU 393 OE1 
454 1 Y 1 B GLU 519 ? OE2 ? B GLU 393 OE2 
455 1 Y 1 B VAL 520 ? CG1 ? B VAL 394 CG1 
456 1 Y 1 B VAL 520 ? CG2 ? B VAL 394 CG2 
457 1 Y 1 B VAL 521 ? CG1 ? B VAL 395 CG1 
458 1 Y 1 B VAL 521 ? CG2 ? B VAL 395 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  103.96 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.27 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  109.32 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9D7L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.528 
_cell.length_a_esd                 ? 
_cell.length_b                     54.242 
_cell.length_b_esd                 ? 
_cell.length_c                     75.600 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9D7L 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9D7L 
_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             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.42 
_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              ? 
_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    
;Resevoir contained 0.2 M sodium formate and 20% (w/v) PEG 3350. Enzyme was incubated with 10 mM S-methyl N-propargylglycine. Crystal was soaked in cryobuffer containing 20% PEG 200
;
_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 EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-01 
_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   1.000042 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000042 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9D7L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.68 
_reflns.d_resolution_low                               48.44 
_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                                     136243 
_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                           91.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.88 
_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                                0.072 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.062 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.68 
_reflns_shell.d_res_low                                     1.71 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           13758 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3567 
_reflns_shell.percent_possible_obs                          90.7 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.9 
_reflns_shell.pdbx_chi_squared                              0.73 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.6 
_reflns_shell.pdbx_Rrim_I_all                               2.312 
_reflns_shell.pdbx_Rpim_I_all                               1.169 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.315 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.992 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9D7L 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.68 
_refine.ls_d_res_low                             48.44 
_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                     136243 
_refine.ls_number_reflns_R_free                  6880 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.21 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2006 
_refine.ls_R_factor_R_free                       0.2264 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1993 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.19 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.01 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5510 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         120 
_refine_hist.number_atoms_solvent             258 
_refine_hist.number_atoms_total               5888 
_refine_hist.d_res_high                       1.68 
_refine_hist.d_res_low                        48.44 
# 
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' ? 0.006  ? 5758 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.923  ? 7854 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.763 ? 2031 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046  ? 898  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 1018 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.68 1.70  . . 224 4238 87.00 . . . . 0.3762 . . . . . . . . . . . 0.3650 
'X-RAY DIFFRACTION' 1.70 1.72  . . 212 4479 90.00 . . . . 0.3590 . . . . . . . . . . . 0.3877 
'X-RAY DIFFRACTION' 1.72 1.74  . . 244 4317 90.00 . . . . 0.3466 . . . . . . . . . . . 0.4009 
'X-RAY DIFFRACTION' 1.74 1.76  . . 238 4422 91.00 . . . . 0.3362 . . . . . . . . . . . 0.3516 
'X-RAY DIFFRACTION' 1.76 1.79  . . 236 4514 91.00 . . . . 0.3305 . . . . . . . . . . . 0.3550 
'X-RAY DIFFRACTION' 1.79 1.81  . . 235 4424 89.00 . . . . 0.3290 . . . . . . . . . . . 0.3091 
'X-RAY DIFFRACTION' 1.81 1.84  . . 219 4364 92.00 . . . . 0.3014 . . . . . . . . . . . 0.3310 
'X-RAY DIFFRACTION' 1.84 1.86  . . 251 4471 90.00 . . . . 0.2972 . . . . . . . . . . . 0.3279 
'X-RAY DIFFRACTION' 1.86 1.89  . . 234 4317 90.00 . . . . 0.3032 . . . . . . . . . . . 0.3598 
'X-RAY DIFFRACTION' 1.89 1.92  . . 219 4424 90.00 . . . . 0.2869 . . . . . . . . . . . 0.3212 
'X-RAY DIFFRACTION' 1.92 1.96  . . 241 4315 89.00 . . . . 0.2729 . . . . . . . . . . . 0.2825 
'X-RAY DIFFRACTION' 1.96 1.99  . . 197 4514 90.00 . . . . 0.2486 . . . . . . . . . . . 0.2568 
'X-RAY DIFFRACTION' 1.99 2.03  . . 229 4291 88.00 . . . . 0.2322 . . . . . . . . . . . 0.2802 
'X-RAY DIFFRACTION' 2.03 2.07  . . 214 4248 88.00 . . . . 0.2310 . . . . . . . . . . . 0.3022 
'X-RAY DIFFRACTION' 2.07 2.12  . . 236 4385 89.00 . . . . 0.2260 . . . . . . . . . . . 0.2525 
'X-RAY DIFFRACTION' 2.12 2.17  . . 275 4119 85.00 . . . . 0.2200 . . . . . . . . . . . 0.2794 
'X-RAY DIFFRACTION' 2.17 2.22  . . 243 4120 85.00 . . . . 0.2304 . . . . . . . . . . . 0.2515 
'X-RAY DIFFRACTION' 2.22 2.28  . . 220 3637 75.00 . . . . 0.2330 . . . . . . . . . . . 0.2989 
'X-RAY DIFFRACTION' 2.28 2.35  . . 195 4155 84.00 . . . . 0.2155 . . . . . . . . . . . 0.2682 
'X-RAY DIFFRACTION' 2.35 2.42  . . 219 4600 93.00 . . . . 0.2099 . . . . . . . . . . . 0.2223 
'X-RAY DIFFRACTION' 2.42 2.51  . . 263 4429 93.00 . . . . 0.2102 . . . . . . . . . . . 0.2565 
'X-RAY DIFFRACTION' 2.51 2.61  . . 248 4537 92.00 . . . . 0.2087 . . . . . . . . . . . 0.2411 
'X-RAY DIFFRACTION' 2.61 2.73  . . 222 4501 91.00 . . . . 0.2081 . . . . . . . . . . . 0.2479 
'X-RAY DIFFRACTION' 2.73 2.87  . . 239 4424 91.00 . . . . 0.2127 . . . . . . . . . . . 0.2513 
'X-RAY DIFFRACTION' 2.87 3.05  . . 248 4320 89.00 . . . . 0.2096 . . . . . . . . . . . 0.1922 
'X-RAY DIFFRACTION' 3.05 3.29  . . 221 4314 88.00 . . . . 0.1865 . . . . . . . . . . . 0.2279 
'X-RAY DIFFRACTION' 3.29 3.62  . . 210 4106 84.00 . . . . 0.1805 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 3.62 4.14  . . 206 3896 80.00 . . . . 0.1640 . . . . . . . . . . . 0.1728 
'X-RAY DIFFRACTION' 4.14 5.22  . . 218 4020 83.00 . . . . 0.1491 . . . . . . . . . . . 0.1594 
'X-RAY DIFFRACTION' 5.22 48.44 . . 224 4462 91.00 . . . . 0.1694 . . . . . . . . . . . 0.1892 
# 
_struct.entry_id                     9D7L 
_struct.title                        
'Minimal PutA proline dehydrogenase domain (design #2) covalently inactivated by (S)-but-3-yn-2-ylglycine' 
_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        9D7L 
_struct_keywords.text            'BETA/ALPHA BARREL, FLAVOENZYME, PROLINE CATABOLISM, 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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP F7X6I3_SINMM F7X6I3 ? 1 RPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGKHSGSG 26  
2 UNP F7X6I3_SINMM F7X6I3 ? 1 
;MMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYRDYESAIHAIGKASAGRGIYEGPGISIKLSAL
HPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLDLLEVLCLDGDLSGWNGMGFVVQAYGKRCPFV
LDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHTDVSYIACAAKLLAATDVVFPQFATHNAQTLA
AIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVHRINDPKVS
IDELIADPVEVVR
;
190 
# 
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 9D7L A 2  ? 59  ? F7X6I3 26  ? 83  ? 26  185 
2 2 9D7L A 64 ? 396 ? F7X6I3 190 ? 522 ? 190 522 
3 1 9D7L B 2  ? 59  ? F7X6I3 26  ? 83  ? 26  185 
4 2 9D7L B 64 ? 396 ? F7X6I3 190 ? 522 ? 190 522 
# 
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 9D7L SER A 1  ? UNP F7X6I3 ? ? 'expression tag' 25  1  
1 9D7L SER A 60 ? UNP F7X6I3 ? ? linker           186 2  
1 9D7L SER A 61 ? UNP F7X6I3 ? ? linker           187 3  
1 9D7L GLY A 62 ? UNP F7X6I3 ? ? linker           188 4  
1 9D7L SER A 63 ? UNP F7X6I3 ? ? linker           189 5  
3 9D7L SER B 1  ? UNP F7X6I3 ? ? 'expression tag' 25  6  
3 9D7L SER B 60 ? UNP F7X6I3 ? ? linker           186 7  
3 9D7L SER B 61 ? UNP F7X6I3 ? ? linker           187 8  
3 9D7L GLY B 62 ? UNP F7X6I3 ? ? linker           188 9  
3 9D7L SER B 63 ? UNP F7X6I3 ? ? linker           189 10 
# 
_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 
# 
_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_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 5   ? TYR A 15  ? SER A 29  TYR A 39  1 ? 11 
HELX_P HELX_P2  AA2 PRO A 18  ? THR A 31  ? PRO A 42  THR A 55  1 ? 14 
HELX_P HELX_P3  AA3 SER A 33  ? LYS A 54  ? SER A 57  LYS A 78  1 ? 22 
HELX_P HELX_P4  AA4 GLY A 66  ? VAL A 70  ? GLY A 192 VAL A 196 5 ? 5  
HELX_P HELX_P5  AA5 THR A 74  ? GLU A 87  ? THR A 200 GLU A 213 1 ? 14 
HELX_P HELX_P6  AA6 THR A 103 ? ALA A 126 ? THR A 229 ALA A 252 1 ? 24 
HELX_P HELX_P7  AA7 ARG A 128 ? GLY A 133 ? ARG A 254 GLY A 259 1 ? 6  
HELX_P HELX_P8  AA8 LYS A 139 ? LEU A 143 ? LYS A 265 LEU A 269 5 ? 5  
HELX_P HELX_P9  AA9 GLN A 151 ? ASP A 174 ? GLN A 277 ASP A 300 1 ? 24 
HELX_P HELX_P10 AB1 GLU A 183 ? ASP A 185 ? GLU A 309 ASP A 311 5 ? 3  
HELX_P HELX_P11 AB2 ARG A 186 ? LEU A 199 ? ARG A 312 LEU A 325 1 ? 14 
HELX_P HELX_P12 AB3 ASP A 200 ? SER A 204 ? ASP A 326 SER A 330 5 ? 5  
HELX_P HELX_P13 AB4 ARG A 219 ? GLY A 235 ? ARG A 345 GLY A 361 1 ? 17 
HELX_P HELX_P14 AB5 TYR A 247 ? ASP A 258 ? TYR A 373 ASP A 384 1 ? 12 
HELX_P HELX_P15 AB6 ARG A 268 ? ALA A 285 ? ARG A 394 ALA A 411 1 ? 18 
HELX_P HELX_P16 AB7 ASN A 298 ? ALA A 309 ? ASN A 424 ALA A 435 1 ? 12 
HELX_P HELX_P17 AB8 GLY A 327 ? GLU A 332 ? GLY A 453 GLU A 458 1 ? 6  
HELX_P HELX_P18 AB9 LEU A 356 ? ALA A 369 ? LEU A 482 ALA A 495 1 ? 14 
HELX_P HELX_P19 AC1 SER A 372 ? ILE A 377 ? SER A 498 ILE A 503 1 ? 6  
HELX_P HELX_P20 AC2 SER A 383 ? ILE A 388 ? SER A 509 ILE A 514 1 ? 6  
HELX_P HELX_P21 AC3 GLN B 4   ? ARG B 16  ? GLN B 28  ARG B 40  1 ? 13 
HELX_P HELX_P22 AC4 PRO B 18  ? THR B 31  ? PRO B 42  THR B 55  1 ? 14 
HELX_P HELX_P23 AC5 SER B 33  ? HIS B 55  ? SER B 57  HIS B 79  1 ? 23 
HELX_P HELX_P24 AC6 GLY B 66  ? VAL B 70  ? GLY B 192 VAL B 196 5 ? 5  
HELX_P HELX_P25 AC7 THR B 74  ? ARG B 81  ? THR B 200 ARG B 207 1 ? 8  
HELX_P HELX_P26 AC8 SER B 82  ? LYS B 88  ? SER B 208 LYS B 214 1 ? 7  
HELX_P HELX_P27 AC9 THR B 103 ? ALA B 126 ? THR B 229 ALA B 252 1 ? 24 
HELX_P HELX_P28 AD1 ARG B 128 ? GLY B 133 ? ARG B 254 GLY B 259 1 ? 6  
HELX_P HELX_P29 AD2 LYS B 139 ? LEU B 143 ? LYS B 265 LEU B 269 5 ? 5  
HELX_P HELX_P30 AD3 GLN B 151 ? ASP B 174 ? GLN B 277 ASP B 300 1 ? 24 
HELX_P HELX_P31 AD4 GLU B 183 ? ASP B 185 ? GLU B 309 ASP B 311 5 ? 3  
HELX_P HELX_P32 AD5 ARG B 186 ? ASP B 200 ? ARG B 312 ASP B 326 1 ? 15 
HELX_P HELX_P33 AD6 GLY B 201 ? SER B 204 ? GLY B 327 SER B 330 5 ? 4  
HELX_P HELX_P34 AD7 ARG B 219 ? GLY B 235 ? ARG B 345 GLY B 361 1 ? 17 
HELX_P HELX_P35 AD8 TYR B 247 ? ASP B 258 ? TYR B 373 ASP B 384 1 ? 12 
HELX_P HELX_P36 AD9 ARG B 268 ? ALA B 285 ? ARG B 394 ALA B 411 1 ? 18 
HELX_P HELX_P37 AE1 ASN B 298 ? ALA B 309 ? ASN B 424 ALA B 435 1 ? 12 
HELX_P HELX_P38 AE2 GLY B 327 ? GLU B 332 ? GLY B 453 GLU B 458 1 ? 6  
HELX_P HELX_P39 AE3 THR B 355 ? ALA B 369 ? THR B 481 ALA B 495 1 ? 15 
HELX_P HELX_P40 AE4 SER B 372 ? ILE B 377 ? SER B 498 ILE B 503 1 ? 6  
HELX_P HELX_P41 AE5 SER B 383 ? ILE B 388 ? SER B 509 ILE B 514 1 ? 6  
HELX_P HELX_P42 AE6 ASP B 390 ? VAL B 395 ? ASP B 516 VAL B 521 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? A LYS 139 NZ ? ? ? 1_555 C A1BC6 . C02 ? ? A LYS 265 A A1BC6 601 1_555 ? ? ? ? ? ? ? 1.357 doub ? 
covale2 covale one ? B LYS 139 NZ ? ? ? 1_555 E A1BC6 . C02 ? ? B LYS 265 B A1BC6 601 1_555 ? ? ? ? ? ? ? 1.359 doub ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1BC6 C . ? LYS A 139 ? A1BC6 A 601 ? 1_555 LYS A 265 ? 1_555 C02 NZ LYS 1 A1BC6 None 'Covalent chemical modification' 
2 A1BC6 E . ? LYS B 139 ? A1BC6 B 601 ? 1_555 LYS B 265 ? 1_555 C02 NZ LYS 1 A1BC6 None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 9 ? 
# 
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 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA1 7 8 ? parallel 
AA1 8 9 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 6 7 ? parallel 
AA2 7 8 ? parallel 
AA2 8 9 ? 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 PHE A 90  ? MET A 96  ? PHE A 216 MET A 222 
AA1 2 GLY A 135 ? ILE A 138 ? GLY A 261 ILE A 264 
AA1 3 LEU A 177 ? ILE A 179 ? LEU A 303 ILE A 305 
AA1 4 MET A 209 ? GLN A 214 ? MET A 335 GLN A 340 
AA1 5 ILE A 238 ? VAL A 243 ? ILE A 364 VAL A 369 
AA1 6 VAL A 290 ? ALA A 295 ? VAL A 416 ALA A 421 
AA1 7 GLU A 319 ? LEU A 323 ? GLU A 445 LEU A 449 
AA1 8 CYS A 344 ? VAL A 350 ? CYS A 470 VAL A 476 
AA1 9 PHE A 90  ? MET A 96  ? PHE A 216 MET A 222 
AA2 1 SER B 91  ? MET B 96  ? SER B 217 MET B 222 
AA2 2 GLY B 135 ? ILE B 138 ? GLY B 261 ILE B 264 
AA2 3 GLY B 176 ? ILE B 179 ? GLY B 302 ILE B 305 
AA2 4 MET B 209 ? GLN B 214 ? MET B 335 GLN B 340 
AA2 5 ILE B 238 ? VAL B 243 ? ILE B 364 VAL B 369 
AA2 6 VAL B 290 ? ALA B 295 ? VAL B 416 ALA B 421 
AA2 7 GLU B 319 ? LEU B 323 ? GLU B 445 LEU B 449 
AA2 8 CYS B 344 ? VAL B 350 ? CYS B 470 VAL B 476 
AA2 9 SER B 91  ? MET B 96  ? SER B 217 MET B 222 
# 
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 TYR A 94  ? N TYR A 220 O GLY A 135 ? O GLY A 261 
AA1 2 3 N ILE A 138 ? N ILE A 264 O ASN A 178 ? O ASN A 304 
AA1 3 4 N LEU A 177 ? N LEU A 303 O GLY A 210 ? O GLY A 336 
AA1 4 5 N PHE A 211 ? N PHE A 337 O MET A 239 ? O MET A 365 
AA1 5 6 N VAL A 240 ? N VAL A 366 O GLN A 293 ? O GLN A 419 
AA1 6 7 N PHE A 294 ? N PHE A 420 O GLU A 319 ? O GLU A 445 
AA1 7 8 N CYS A 322 ? N CYS A 448 O TYR A 347 ? O TYR A 473 
AA1 8 9 O ILE A 346 ? O ILE A 472 N SER A 91  ? N SER A 217 
AA2 1 2 N TYR B 94  ? N TYR B 220 O SER B 137 ? O SER B 263 
AA2 2 3 N ILE B 136 ? N ILE B 262 O GLY B 176 ? O GLY B 302 
AA2 3 4 N LEU B 177 ? N LEU B 303 O GLY B 210 ? O GLY B 336 
AA2 4 5 N VAL B 213 ? N VAL B 339 O ARG B 241 ? O ARG B 367 
AA2 5 6 N VAL B 240 ? N VAL B 366 O GLN B 293 ? O GLN B 419 
AA2 6 7 N PHE B 294 ? N PHE B 420 O GLU B 319 ? O GLU B 445 
AA2 7 8 N CYS B 322 ? N CYS B 448 O TYR B 347 ? O TYR B 473 
AA2 8 9 O ILE B 346 ? O ILE B 472 N SER B 91  ? N SER B 217 
# 
_pdbx_entry_details.entry_id                   9D7L 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD2 A ASP 438 ? ? NZ A LYS 443 ? ? 2.15 
2 1 OE2 A GLU 212 ? ? O  A HOH 701 ? ? 2.18 
# 
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 MET A 222 ? ? -69.38  88.36   
2 1 ARG A 272 ? ? -145.69 49.78   
3 1 GLU A 308 ? ? -116.31 -128.13 
4 1 LYS A 465 ? ? -115.80 -122.01 
5 1 LEU B 223 ? ? -40.63  100.06  
6 1 GLU B 308 ? ? -117.28 -135.61 
7 1 LYS B 465 ? ? -100.57 -122.96 
8 1 THR B 478 ? ? -89.42  -143.35 
9 1 THR B 481 ? ? 74.63   -31.26  
# 
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 11.6160 20.0749 52.5567 0.2810 ? 0.0392 ? 0.0128 ? 0.2430 ? -0.0152 ? 0.1986 ? 2.2481 ? 0.2609 ? 
0.3343 ? 2.5281 ? -0.6382 ? 4.0321 ? -0.0264 ? -0.0127 ? -0.0252 ? -0.0513 ? 0.0533 ? 0.1015 ? 0.1542  ? -0.4098 ? -0.0275 ? 
2 'X-RAY DIFFRACTION' ? refined 26.1900 5.3923  17.1213 0.2888 ? 0.0267 ? 0.0277 ? 0.3254 ? 0.0106  ? 0.2340 ? 2.8235 ? 0.6702 ? 
0.0019 ? 2.7239 ? -1.3088 ? 4.2679 ? -0.0380 ? 0.1100  ? 0.1162  ? 0.0924  ? 0.1470 ? 0.1198 ? -0.2619 ? -0.4305 ? -0.0665 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'chain A and peptide' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'chain B and peptide' 
# 
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 SER 25  ? A SER 1   
2  1 Y 1 A ARG 26  ? A ARG 2   
3  1 Y 1 A SER 182 ? A SER 56  
4  1 Y 1 A GLY 183 ? A GLY 57  
5  1 Y 1 A SER 184 ? A SER 58  
6  1 Y 1 A GLY 185 ? A GLY 59  
7  1 Y 1 A SER 186 ? A SER 60  
8  1 Y 1 A SER 187 ? A SER 61  
9  1 Y 1 A GLY 188 ? A GLY 62  
10 1 Y 1 A SER 189 ? A SER 63  
11 1 Y 1 A MET 190 ? A MET 64  
12 1 Y 1 A MET 191 ? A MET 65  
13 1 Y 1 A GLY 385 ? A GLY 259 
14 1 Y 1 A LEU 386 ? A LEU 260 
15 1 Y 1 A VAL 521 ? A VAL 395 
16 1 Y 1 A ARG 522 ? A ARG 396 
17 1 Y 1 B SER 25  ? B SER 1   
18 1 Y 1 B SER 182 ? B SER 56  
19 1 Y 1 B GLY 183 ? B GLY 57  
20 1 Y 1 B SER 184 ? B SER 58  
21 1 Y 1 B GLY 185 ? B GLY 59  
22 1 Y 1 B SER 186 ? B SER 60  
23 1 Y 1 B SER 187 ? B SER 61  
24 1 Y 1 B GLY 188 ? B GLY 62  
25 1 Y 1 B SER 189 ? B SER 63  
26 1 Y 1 B MET 190 ? B MET 64  
27 1 Y 1 B MET 191 ? B MET 65  
28 1 Y 1 B ARG 522 ? B ARG 396 
# 
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 
A1BC6 PA    P N N 1   
A1BC6 O1A   O N N 2   
A1BC6 O2A   O N N 3   
A1BC6 O5B   O N N 4   
A1BC6 C5B   C N N 5   
A1BC6 C4B   C N R 6   
A1BC6 O4B   O N N 7   
A1BC6 C3B   C N S 8   
A1BC6 O3B   O N N 9   
A1BC6 C2B   C N R 10  
A1BC6 O2B   O N N 11  
A1BC6 C1B   C N R 12  
A1BC6 N9A   N Y N 13  
A1BC6 C8A   C Y N 14  
A1BC6 N7A   N Y N 15  
A1BC6 C5A   C Y N 16  
A1BC6 C6A   C Y N 17  
A1BC6 N6A   N N N 18  
A1BC6 N1A   N Y N 19  
A1BC6 C2A   C Y N 20  
A1BC6 N3A   N Y N 21  
A1BC6 C4A   C Y N 22  
A1BC6 N1    N N N 23  
A1BC6 C2    C N N 24  
A1BC6 O2    O N N 25  
A1BC6 N3    N N N 26  
A1BC6 C4    C N N 27  
A1BC6 O4    O N N 28  
A1BC6 C4X   C N N 29  
A1BC6 N5    N N N 30  
A1BC6 C5X   C Y N 31  
A1BC6 C6    C Y N 32  
A1BC6 C7    C Y N 33  
A1BC6 C7M   C N N 34  
A1BC6 C8    C Y N 35  
A1BC6 C8M   C N N 36  
A1BC6 C9    C Y N 37  
A1BC6 C9A   C Y N 38  
A1BC6 N10   N N N 39  
A1BC6 C10   C N N 40  
A1BC6 "C1'" C N N 41  
A1BC6 "C2'" C N S 42  
A1BC6 "O2'" O N N 43  
A1BC6 "C3'" C N S 44  
A1BC6 "O3'" O N N 45  
A1BC6 "C4'" C N R 46  
A1BC6 "O4'" O N N 47  
A1BC6 "C5'" C N N 48  
A1BC6 "O5'" O N N 49  
A1BC6 P     P N N 50  
A1BC6 O1P   O N N 51  
A1BC6 O2P   O N N 52  
A1BC6 O3P   O N N 53  
A1BC6 C01   C N N 54  
A1BC6 C02   C N N 55  
A1BC6 C04   C N N 56  
A1BC6 C05   C N N 57  
A1BC6 H1    H N N 58  
A1BC6 H2    H N N 59  
A1BC6 H3    H N N 60  
A1BC6 H4    H N N 61  
A1BC6 H5    H N N 62  
A1BC6 H6    H N N 63  
A1BC6 H7    H N N 64  
A1BC6 H8    H N N 65  
A1BC6 H9    H N N 66  
A1BC6 H10   H N N 67  
A1BC6 H11   H N N 68  
A1BC6 H12   H N N 69  
A1BC6 H13   H N N 70  
A1BC6 H14   H N N 71  
A1BC6 H15   H N N 72  
A1BC6 H16   H N N 73  
A1BC6 H17   H N N 74  
A1BC6 H18   H N N 75  
A1BC6 H19   H N N 76  
A1BC6 H20   H N N 77  
A1BC6 H21   H N N 78  
A1BC6 H22   H N N 79  
A1BC6 H23   H N N 80  
A1BC6 H24   H N N 81  
A1BC6 H25   H N N 82  
A1BC6 H26   H N N 83  
A1BC6 H27   H N N 84  
A1BC6 H28   H N N 85  
A1BC6 H29   H N N 86  
A1BC6 H30   H N N 87  
A1BC6 H31   H N N 88  
A1BC6 H32   H N N 89  
A1BC6 H33   H N N 90  
A1BC6 H34   H N N 91  
A1BC6 H35   H N N 92  
A1BC6 H36   H N N 93  
A1BC6 H37   H N N 94  
A1BC6 H40   H N N 95  
A1BC6 H41   H N N 96  
A1BC6 N     N N N 97  
A1BC6 CA    C N N 98  
A1BC6 C     C N N 99  
A1BC6 O     O N N 100 
A1BC6 OXT   O N N 101 
A1BC6 HA2   H N N 102 
A1BC6 HA3   H N N 103 
A1BC6 HXT   H N N 104 
ALA   N     N N N 105 
ALA   CA    C N S 106 
ALA   C     C N N 107 
ALA   O     O N N 108 
ALA   CB    C N N 109 
ALA   OXT   O N N 110 
ALA   H     H N N 111 
ALA   H2    H N N 112 
ALA   HA    H N N 113 
ALA   HB1   H N N 114 
ALA   HB2   H N N 115 
ALA   HB3   H N N 116 
ALA   HXT   H N N 117 
ARG   N     N N N 118 
ARG   CA    C N S 119 
ARG   C     C N N 120 
ARG   O     O N N 121 
ARG   CB    C N N 122 
ARG   CG    C N N 123 
ARG   CD    C N N 124 
ARG   NE    N N N 125 
ARG   CZ    C N N 126 
ARG   NH1   N N N 127 
ARG   NH2   N N N 128 
ARG   OXT   O N N 129 
ARG   H     H N N 130 
ARG   H2    H N N 131 
ARG   HA    H N N 132 
ARG   HB2   H N N 133 
ARG   HB3   H N N 134 
ARG   HG2   H N N 135 
ARG   HG3   H N N 136 
ARG   HD2   H N N 137 
ARG   HD3   H N N 138 
ARG   HE    H N N 139 
ARG   HH11  H N N 140 
ARG   HH12  H N N 141 
ARG   HH21  H N N 142 
ARG   HH22  H N N 143 
ARG   HXT   H N N 144 
ASN   N     N N N 145 
ASN   CA    C N S 146 
ASN   C     C N N 147 
ASN   O     O N N 148 
ASN   CB    C N N 149 
ASN   CG    C N N 150 
ASN   OD1   O N N 151 
ASN   ND2   N N N 152 
ASN   OXT   O N N 153 
ASN   H     H N N 154 
ASN   H2    H N N 155 
ASN   HA    H N N 156 
ASN   HB2   H N N 157 
ASN   HB3   H N N 158 
ASN   HD21  H N N 159 
ASN   HD22  H N N 160 
ASN   HXT   H N N 161 
ASP   N     N N N 162 
ASP   CA    C N S 163 
ASP   C     C N N 164 
ASP   O     O N N 165 
ASP   CB    C N N 166 
ASP   CG    C N N 167 
ASP   OD1   O N N 168 
ASP   OD2   O N N 169 
ASP   OXT   O N N 170 
ASP   H     H N N 171 
ASP   H2    H N N 172 
ASP   HA    H N N 173 
ASP   HB2   H N N 174 
ASP   HB3   H N N 175 
ASP   HD2   H N N 176 
ASP   HXT   H N N 177 
CYS   N     N N N 178 
CYS   CA    C N R 179 
CYS   C     C N N 180 
CYS   O     O N N 181 
CYS   CB    C N N 182 
CYS   SG    S N N 183 
CYS   OXT   O N N 184 
CYS   H     H N N 185 
CYS   H2    H N N 186 
CYS   HA    H N N 187 
CYS   HB2   H N N 188 
CYS   HB3   H N N 189 
CYS   HG    H N N 190 
CYS   HXT   H N N 191 
FMT   C     C N N 192 
FMT   O1    O N N 193 
FMT   O2    O N N 194 
FMT   H     H N N 195 
FMT   HO2   H N N 196 
GLN   N     N N N 197 
GLN   CA    C N S 198 
GLN   C     C N N 199 
GLN   O     O N N 200 
GLN   CB    C N N 201 
GLN   CG    C N N 202 
GLN   CD    C N N 203 
GLN   OE1   O N N 204 
GLN   NE2   N N N 205 
GLN   OXT   O N N 206 
GLN   H     H N N 207 
GLN   H2    H N N 208 
GLN   HA    H N N 209 
GLN   HB2   H N N 210 
GLN   HB3   H N N 211 
GLN   HG2   H N N 212 
GLN   HG3   H N N 213 
GLN   HE21  H N N 214 
GLN   HE22  H N N 215 
GLN   HXT   H N N 216 
GLU   N     N N N 217 
GLU   CA    C N S 218 
GLU   C     C N N 219 
GLU   O     O N N 220 
GLU   CB    C N N 221 
GLU   CG    C N N 222 
GLU   CD    C N N 223 
GLU   OE1   O N N 224 
GLU   OE2   O N N 225 
GLU   OXT   O N N 226 
GLU   H     H N N 227 
GLU   H2    H N N 228 
GLU   HA    H N N 229 
GLU   HB2   H N N 230 
GLU   HB3   H N N 231 
GLU   HG2   H N N 232 
GLU   HG3   H N N 233 
GLU   HE2   H N N 234 
GLU   HXT   H N N 235 
GLY   N     N N N 236 
GLY   CA    C N N 237 
GLY   C     C N N 238 
GLY   O     O N N 239 
GLY   OXT   O N N 240 
GLY   H     H N N 241 
GLY   H2    H N N 242 
GLY   HA2   H N N 243 
GLY   HA3   H N N 244 
GLY   HXT   H N N 245 
HIS   N     N N N 246 
HIS   CA    C N S 247 
HIS   C     C N N 248 
HIS   O     O N N 249 
HIS   CB    C N N 250 
HIS   CG    C Y N 251 
HIS   ND1   N Y N 252 
HIS   CD2   C Y N 253 
HIS   CE1   C Y N 254 
HIS   NE2   N Y N 255 
HIS   OXT   O N N 256 
HIS   H     H N N 257 
HIS   H2    H N N 258 
HIS   HA    H N N 259 
HIS   HB2   H N N 260 
HIS   HB3   H N N 261 
HIS   HD1   H N N 262 
HIS   HD2   H N N 263 
HIS   HE1   H N N 264 
HIS   HE2   H N N 265 
HIS   HXT   H N N 266 
HOH   O     O N N 267 
HOH   H1    H N N 268 
HOH   H2    H N N 269 
ILE   N     N N N 270 
ILE   CA    C N S 271 
ILE   C     C N N 272 
ILE   O     O N N 273 
ILE   CB    C N S 274 
ILE   CG1   C N N 275 
ILE   CG2   C N N 276 
ILE   CD1   C N N 277 
ILE   OXT   O N N 278 
ILE   H     H N N 279 
ILE   H2    H N N 280 
ILE   HA    H N N 281 
ILE   HB    H N N 282 
ILE   HG12  H N N 283 
ILE   HG13  H N N 284 
ILE   HG21  H N N 285 
ILE   HG22  H N N 286 
ILE   HG23  H N N 287 
ILE   HD11  H N N 288 
ILE   HD12  H N N 289 
ILE   HD13  H N N 290 
ILE   HXT   H N N 291 
LEU   N     N N N 292 
LEU   CA    C N S 293 
LEU   C     C N N 294 
LEU   O     O N N 295 
LEU   CB    C N N 296 
LEU   CG    C N N 297 
LEU   CD1   C N N 298 
LEU   CD2   C N N 299 
LEU   OXT   O N N 300 
LEU   H     H N N 301 
LEU   H2    H N N 302 
LEU   HA    H N N 303 
LEU   HB2   H N N 304 
LEU   HB3   H N N 305 
LEU   HG    H N N 306 
LEU   HD11  H N N 307 
LEU   HD12  H N N 308 
LEU   HD13  H N N 309 
LEU   HD21  H N N 310 
LEU   HD22  H N N 311 
LEU   HD23  H N N 312 
LEU   HXT   H N N 313 
LYS   N     N N N 314 
LYS   CA    C N S 315 
LYS   C     C N N 316 
LYS   O     O N N 317 
LYS   CB    C N N 318 
LYS   CG    C N N 319 
LYS   CD    C N N 320 
LYS   CE    C N N 321 
LYS   NZ    N N N 322 
LYS   OXT   O N N 323 
LYS   H     H N N 324 
LYS   H2    H N N 325 
LYS   HA    H N N 326 
LYS   HB2   H N N 327 
LYS   HB3   H N N 328 
LYS   HG2   H N N 329 
LYS   HG3   H N N 330 
LYS   HD2   H N N 331 
LYS   HD3   H N N 332 
LYS   HE2   H N N 333 
LYS   HE3   H N N 334 
LYS   HZ1   H N N 335 
LYS   HZ2   H N N 336 
LYS   HZ3   H N N 337 
LYS   HXT   H N N 338 
MET   N     N N N 339 
MET   CA    C N S 340 
MET   C     C N N 341 
MET   O     O N N 342 
MET   CB    C N N 343 
MET   CG    C N N 344 
MET   SD    S N N 345 
MET   CE    C N N 346 
MET   OXT   O N N 347 
MET   H     H N N 348 
MET   H2    H N N 349 
MET   HA    H N N 350 
MET   HB2   H N N 351 
MET   HB3   H N N 352 
MET   HG2   H N N 353 
MET   HG3   H N N 354 
MET   HE1   H N N 355 
MET   HE2   H N N 356 
MET   HE3   H N N 357 
MET   HXT   H N N 358 
PHE   N     N N N 359 
PHE   CA    C N S 360 
PHE   C     C N N 361 
PHE   O     O N N 362 
PHE   CB    C N N 363 
PHE   CG    C Y N 364 
PHE   CD1   C Y N 365 
PHE   CD2   C Y N 366 
PHE   CE1   C Y N 367 
PHE   CE2   C Y N 368 
PHE   CZ    C Y N 369 
PHE   OXT   O N N 370 
PHE   H     H N N 371 
PHE   H2    H N N 372 
PHE   HA    H N N 373 
PHE   HB2   H N N 374 
PHE   HB3   H N N 375 
PHE   HD1   H N N 376 
PHE   HD2   H N N 377 
PHE   HE1   H N N 378 
PHE   HE2   H N N 379 
PHE   HZ    H N N 380 
PHE   HXT   H N N 381 
PRO   N     N N N 382 
PRO   CA    C N S 383 
PRO   C     C N N 384 
PRO   O     O N N 385 
PRO   CB    C N N 386 
PRO   CG    C N N 387 
PRO   CD    C N N 388 
PRO   OXT   O N N 389 
PRO   H     H N N 390 
PRO   HA    H N N 391 
PRO   HB2   H N N 392 
PRO   HB3   H N N 393 
PRO   HG2   H N N 394 
PRO   HG3   H N N 395 
PRO   HD2   H N N 396 
PRO   HD3   H N N 397 
PRO   HXT   H N N 398 
SER   N     N N N 399 
SER   CA    C N S 400 
SER   C     C N N 401 
SER   O     O N N 402 
SER   CB    C N N 403 
SER   OG    O N N 404 
SER   OXT   O N N 405 
SER   H     H N N 406 
SER   H2    H N N 407 
SER   HA    H N N 408 
SER   HB2   H N N 409 
SER   HB3   H N N 410 
SER   HG    H N N 411 
SER   HXT   H N N 412 
THR   N     N N N 413 
THR   CA    C N S 414 
THR   C     C N N 415 
THR   O     O N N 416 
THR   CB    C N R 417 
THR   OG1   O N N 418 
THR   CG2   C N N 419 
THR   OXT   O N N 420 
THR   H     H N N 421 
THR   H2    H N N 422 
THR   HA    H N N 423 
THR   HB    H N N 424 
THR   HG1   H N N 425 
THR   HG21  H N N 426 
THR   HG22  H N N 427 
THR   HG23  H N N 428 
THR   HXT   H N N 429 
TRP   N     N N N 430 
TRP   CA    C N S 431 
TRP   C     C N N 432 
TRP   O     O N N 433 
TRP   CB    C N N 434 
TRP   CG    C Y N 435 
TRP   CD1   C Y N 436 
TRP   CD2   C Y N 437 
TRP   NE1   N Y N 438 
TRP   CE2   C Y N 439 
TRP   CE3   C Y N 440 
TRP   CZ2   C Y N 441 
TRP   CZ3   C Y N 442 
TRP   CH2   C Y N 443 
TRP   OXT   O N N 444 
TRP   H     H N N 445 
TRP   H2    H N N 446 
TRP   HA    H N N 447 
TRP   HB2   H N N 448 
TRP   HB3   H N N 449 
TRP   HD1   H N N 450 
TRP   HE1   H N N 451 
TRP   HE3   H N N 452 
TRP   HZ2   H N N 453 
TRP   HZ3   H N N 454 
TRP   HH2   H N N 455 
TRP   HXT   H N N 456 
TYR   N     N N N 457 
TYR   CA    C N S 458 
TYR   C     C N N 459 
TYR   O     O N N 460 
TYR   CB    C N N 461 
TYR   CG    C Y N 462 
TYR   CD1   C Y N 463 
TYR   CD2   C Y N 464 
TYR   CE1   C Y N 465 
TYR   CE2   C Y N 466 
TYR   CZ    C Y N 467 
TYR   OH    O N N 468 
TYR   OXT   O N N 469 
TYR   H     H N N 470 
TYR   H2    H N N 471 
TYR   HA    H N N 472 
TYR   HB2   H N N 473 
TYR   HB3   H N N 474 
TYR   HD1   H N N 475 
TYR   HD2   H N N 476 
TYR   HE1   H N N 477 
TYR   HE2   H N N 478 
TYR   HH    H N N 479 
TYR   HXT   H N N 480 
VAL   N     N N N 481 
VAL   CA    C N S 482 
VAL   C     C N N 483 
VAL   O     O N N 484 
VAL   CB    C N N 485 
VAL   CG1   C N N 486 
VAL   CG2   C N N 487 
VAL   OXT   O N N 488 
VAL   H     H N N 489 
VAL   H2    H N N 490 
VAL   HA    H N N 491 
VAL   HB    H N N 492 
VAL   HG11  H N N 493 
VAL   HG12  H N N 494 
VAL   HG13  H N N 495 
VAL   HG21  H N N 496 
VAL   HG22  H N N 497 
VAL   HG23  H N N 498 
VAL   HXT   H N N 499 
# 
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 
A1BC6 N6A   C6A   sing N N 1   
A1BC6 C6A   N1A   doub Y N 2   
A1BC6 C6A   C5A   sing Y N 3   
A1BC6 N1A   C2A   sing Y N 4   
A1BC6 N7A   C5A   sing Y N 5   
A1BC6 N7A   C8A   doub Y N 6   
A1BC6 C5A   C4A   doub Y N 7   
A1BC6 C2A   N3A   doub Y N 8   
A1BC6 C8A   N9A   sing Y N 9   
A1BC6 C4A   N3A   sing Y N 10  
A1BC6 C4A   N9A   sing Y N 11  
A1BC6 N9A   C1B   sing N N 12  
A1BC6 C1B   C2B   sing N N 13  
A1BC6 C1B   O4B   sing N N 14  
A1BC6 C2B   C3B   sing N N 15  
A1BC6 C2B   O2B   sing N N 16  
A1BC6 O4B   C4B   sing N N 17  
A1BC6 C3B   C4B   sing N N 18  
A1BC6 C3B   O3B   sing N N 19  
A1BC6 C4B   C5B   sing N N 20  
A1BC6 C5B   O5B   sing N N 21  
A1BC6 O2A   PA    doub N N 22  
A1BC6 O5B   PA    sing N N 23  
A1BC6 PA    O1A   sing N N 24  
A1BC6 PA    O3P   sing N N 25  
A1BC6 "O4'" "C4'" sing N N 26  
A1BC6 O3P   P     sing N N 27  
A1BC6 O2    C2    doub N N 28  
A1BC6 "C5'" "C4'" sing N N 29  
A1BC6 "C5'" "O5'" sing N N 30  
A1BC6 "C4'" "C3'" sing N N 31  
A1BC6 "O5'" P     sing N N 32  
A1BC6 "C3'" "O3'" sing N N 33  
A1BC6 "C3'" "C2'" sing N N 34  
A1BC6 "O2'" "C2'" sing N N 35  
A1BC6 P     O2P   doub N N 36  
A1BC6 P     O1P   sing N N 37  
A1BC6 C2    N1    sing N N 38  
A1BC6 C2    N3    sing N N 39  
A1BC6 N1    C10   sing N N 40  
A1BC6 "C2'" "C1'" sing N N 41  
A1BC6 "C1'" N10   sing N N 42  
A1BC6 N3    C4    sing N N 43  
A1BC6 C10   N10   sing N N 44  
A1BC6 C10   C4X   doub N N 45  
A1BC6 N10   C9A   sing N N 46  
A1BC6 C4    C4X   sing N N 47  
A1BC6 C4    O4    doub N N 48  
A1BC6 C02   C01   sing N N 49  
A1BC6 C02   C04   sing N N 50  
A1BC6 C4X   N5    sing N N 51  
A1BC6 C04   C05   doub N E 52  
A1BC6 C9A   C9    doub Y N 53  
A1BC6 C9A   C5X   sing Y N 54  
A1BC6 C9    C8    sing Y N 55  
A1BC6 C05   N5    sing N N 56  
A1BC6 N5    C5X   sing N N 57  
A1BC6 C5X   C6    doub Y N 58  
A1BC6 C8    C8M   sing N N 59  
A1BC6 C8    C7    doub Y N 60  
A1BC6 C6    C7    sing Y N 61  
A1BC6 C7    C7M   sing N N 62  
A1BC6 O1A   H1    sing N N 63  
A1BC6 C5B   H2    sing N N 64  
A1BC6 C5B   H3    sing N N 65  
A1BC6 C4B   H4    sing N N 66  
A1BC6 C3B   H5    sing N N 67  
A1BC6 O3B   H6    sing N N 68  
A1BC6 C2B   H7    sing N N 69  
A1BC6 O2B   H8    sing N N 70  
A1BC6 C1B   H9    sing N N 71  
A1BC6 C8A   H10   sing N N 72  
A1BC6 N6A   H11   sing N N 73  
A1BC6 N6A   H12   sing N N 74  
A1BC6 C2A   H13   sing N N 75  
A1BC6 N1    H14   sing N N 76  
A1BC6 N3    H15   sing N N 77  
A1BC6 C6    H16   sing N N 78  
A1BC6 C7M   H17   sing N N 79  
A1BC6 C7M   H18   sing N N 80  
A1BC6 C7M   H19   sing N N 81  
A1BC6 C8M   H20   sing N N 82  
A1BC6 C8M   H21   sing N N 83  
A1BC6 C8M   H22   sing N N 84  
A1BC6 C9    H23   sing N N 85  
A1BC6 "C1'" H24   sing N N 86  
A1BC6 "C1'" H25   sing N N 87  
A1BC6 "C2'" H26   sing N N 88  
A1BC6 "O2'" H27   sing N N 89  
A1BC6 "C3'" H28   sing N N 90  
A1BC6 "O3'" H29   sing N N 91  
A1BC6 "C4'" H30   sing N N 92  
A1BC6 "O4'" H31   sing N N 93  
A1BC6 "C5'" H32   sing N N 94  
A1BC6 "C5'" H33   sing N N 95  
A1BC6 O1P   H34   sing N N 96  
A1BC6 C01   H35   sing N N 97  
A1BC6 C01   H36   sing N N 98  
A1BC6 C01   H37   sing N N 99  
A1BC6 C04   H40   sing N N 100 
A1BC6 C05   H41   sing N N 101 
A1BC6 C02   N     doub N N 102 
A1BC6 N     CA    sing N N 103 
A1BC6 CA    C     sing N N 104 
A1BC6 C     O     doub N N 105 
A1BC6 C     OXT   sing N N 106 
A1BC6 CA    HA2   sing N N 107 
A1BC6 CA    HA3   sing N N 108 
A1BC6 OXT   HXT   sing N N 109 
ALA   N     CA    sing N N 110 
ALA   N     H     sing N N 111 
ALA   N     H2    sing N N 112 
ALA   CA    C     sing N N 113 
ALA   CA    CB    sing N N 114 
ALA   CA    HA    sing N N 115 
ALA   C     O     doub N N 116 
ALA   C     OXT   sing N N 117 
ALA   CB    HB1   sing N N 118 
ALA   CB    HB2   sing N N 119 
ALA   CB    HB3   sing N N 120 
ALA   OXT   HXT   sing N N 121 
ARG   N     CA    sing N N 122 
ARG   N     H     sing N N 123 
ARG   N     H2    sing N N 124 
ARG   CA    C     sing N N 125 
ARG   CA    CB    sing N N 126 
ARG   CA    HA    sing N N 127 
ARG   C     O     doub N N 128 
ARG   C     OXT   sing N N 129 
ARG   CB    CG    sing N N 130 
ARG   CB    HB2   sing N N 131 
ARG   CB    HB3   sing N N 132 
ARG   CG    CD    sing N N 133 
ARG   CG    HG2   sing N N 134 
ARG   CG    HG3   sing N N 135 
ARG   CD    NE    sing N N 136 
ARG   CD    HD2   sing N N 137 
ARG   CD    HD3   sing N N 138 
ARG   NE    CZ    sing N N 139 
ARG   NE    HE    sing N N 140 
ARG   CZ    NH1   sing N N 141 
ARG   CZ    NH2   doub N N 142 
ARG   NH1   HH11  sing N N 143 
ARG   NH1   HH12  sing N N 144 
ARG   NH2   HH21  sing N N 145 
ARG   NH2   HH22  sing N N 146 
ARG   OXT   HXT   sing N N 147 
ASN   N     CA    sing N N 148 
ASN   N     H     sing N N 149 
ASN   N     H2    sing N N 150 
ASN   CA    C     sing N N 151 
ASN   CA    CB    sing N N 152 
ASN   CA    HA    sing N N 153 
ASN   C     O     doub N N 154 
ASN   C     OXT   sing N N 155 
ASN   CB    CG    sing N N 156 
ASN   CB    HB2   sing N N 157 
ASN   CB    HB3   sing N N 158 
ASN   CG    OD1   doub N N 159 
ASN   CG    ND2   sing N N 160 
ASN   ND2   HD21  sing N N 161 
ASN   ND2   HD22  sing N N 162 
ASN   OXT   HXT   sing N N 163 
ASP   N     CA    sing N N 164 
ASP   N     H     sing N N 165 
ASP   N     H2    sing N N 166 
ASP   CA    C     sing N N 167 
ASP   CA    CB    sing N N 168 
ASP   CA    HA    sing N N 169 
ASP   C     O     doub N N 170 
ASP   C     OXT   sing N N 171 
ASP   CB    CG    sing N N 172 
ASP   CB    HB2   sing N N 173 
ASP   CB    HB3   sing N N 174 
ASP   CG    OD1   doub N N 175 
ASP   CG    OD2   sing N N 176 
ASP   OD2   HD2   sing N N 177 
ASP   OXT   HXT   sing N N 178 
CYS   N     CA    sing N N 179 
CYS   N     H     sing N N 180 
CYS   N     H2    sing N N 181 
CYS   CA    C     sing N N 182 
CYS   CA    CB    sing N N 183 
CYS   CA    HA    sing N N 184 
CYS   C     O     doub N N 185 
CYS   C     OXT   sing N N 186 
CYS   CB    SG    sing N N 187 
CYS   CB    HB2   sing N N 188 
CYS   CB    HB3   sing N N 189 
CYS   SG    HG    sing N N 190 
CYS   OXT   HXT   sing N N 191 
FMT   C     O1    doub N N 192 
FMT   C     O2    sing N N 193 
FMT   C     H     sing N N 194 
FMT   O2    HO2   sing N N 195 
GLN   N     CA    sing N N 196 
GLN   N     H     sing N N 197 
GLN   N     H2    sing N N 198 
GLN   CA    C     sing N N 199 
GLN   CA    CB    sing N N 200 
GLN   CA    HA    sing N N 201 
GLN   C     O     doub N N 202 
GLN   C     OXT   sing N N 203 
GLN   CB    CG    sing N N 204 
GLN   CB    HB2   sing N N 205 
GLN   CB    HB3   sing N N 206 
GLN   CG    CD    sing N N 207 
GLN   CG    HG2   sing N N 208 
GLN   CG    HG3   sing N N 209 
GLN   CD    OE1   doub N N 210 
GLN   CD    NE2   sing N N 211 
GLN   NE2   HE21  sing N N 212 
GLN   NE2   HE22  sing N N 213 
GLN   OXT   HXT   sing N N 214 
GLU   N     CA    sing N N 215 
GLU   N     H     sing N N 216 
GLU   N     H2    sing N N 217 
GLU   CA    C     sing N N 218 
GLU   CA    CB    sing N N 219 
GLU   CA    HA    sing N N 220 
GLU   C     O     doub N N 221 
GLU   C     OXT   sing N N 222 
GLU   CB    CG    sing N N 223 
GLU   CB    HB2   sing N N 224 
GLU   CB    HB3   sing N N 225 
GLU   CG    CD    sing N N 226 
GLU   CG    HG2   sing N N 227 
GLU   CG    HG3   sing N N 228 
GLU   CD    OE1   doub N N 229 
GLU   CD    OE2   sing N N 230 
GLU   OE2   HE2   sing N N 231 
GLU   OXT   HXT   sing N N 232 
GLY   N     CA    sing N N 233 
GLY   N     H     sing N N 234 
GLY   N     H2    sing N N 235 
GLY   CA    C     sing N N 236 
GLY   CA    HA2   sing N N 237 
GLY   CA    HA3   sing N N 238 
GLY   C     O     doub N N 239 
GLY   C     OXT   sing N N 240 
GLY   OXT   HXT   sing N N 241 
HIS   N     CA    sing N N 242 
HIS   N     H     sing N N 243 
HIS   N     H2    sing N N 244 
HIS   CA    C     sing N N 245 
HIS   CA    CB    sing N N 246 
HIS   CA    HA    sing N N 247 
HIS   C     O     doub N N 248 
HIS   C     OXT   sing N N 249 
HIS   CB    CG    sing N N 250 
HIS   CB    HB2   sing N N 251 
HIS   CB    HB3   sing N N 252 
HIS   CG    ND1   sing Y N 253 
HIS   CG    CD2   doub Y N 254 
HIS   ND1   CE1   doub Y N 255 
HIS   ND1   HD1   sing N N 256 
HIS   CD2   NE2   sing Y N 257 
HIS   CD2   HD2   sing N N 258 
HIS   CE1   NE2   sing Y N 259 
HIS   CE1   HE1   sing N N 260 
HIS   NE2   HE2   sing N N 261 
HIS   OXT   HXT   sing N N 262 
HOH   O     H1    sing N N 263 
HOH   O     H2    sing N N 264 
ILE   N     CA    sing N N 265 
ILE   N     H     sing N N 266 
ILE   N     H2    sing N N 267 
ILE   CA    C     sing N N 268 
ILE   CA    CB    sing N N 269 
ILE   CA    HA    sing N N 270 
ILE   C     O     doub N N 271 
ILE   C     OXT   sing N N 272 
ILE   CB    CG1   sing N N 273 
ILE   CB    CG2   sing N N 274 
ILE   CB    HB    sing N N 275 
ILE   CG1   CD1   sing N N 276 
ILE   CG1   HG12  sing N N 277 
ILE   CG1   HG13  sing N N 278 
ILE   CG2   HG21  sing N N 279 
ILE   CG2   HG22  sing N N 280 
ILE   CG2   HG23  sing N N 281 
ILE   CD1   HD11  sing N N 282 
ILE   CD1   HD12  sing N N 283 
ILE   CD1   HD13  sing N N 284 
ILE   OXT   HXT   sing N N 285 
LEU   N     CA    sing N N 286 
LEU   N     H     sing N N 287 
LEU   N     H2    sing N N 288 
LEU   CA    C     sing N N 289 
LEU   CA    CB    sing N N 290 
LEU   CA    HA    sing N N 291 
LEU   C     O     doub N N 292 
LEU   C     OXT   sing N N 293 
LEU   CB    CG    sing N N 294 
LEU   CB    HB2   sing N N 295 
LEU   CB    HB3   sing N N 296 
LEU   CG    CD1   sing N N 297 
LEU   CG    CD2   sing N N 298 
LEU   CG    HG    sing N N 299 
LEU   CD1   HD11  sing N N 300 
LEU   CD1   HD12  sing N N 301 
LEU   CD1   HD13  sing N N 302 
LEU   CD2   HD21  sing N N 303 
LEU   CD2   HD22  sing N N 304 
LEU   CD2   HD23  sing N N 305 
LEU   OXT   HXT   sing N N 306 
LYS   N     CA    sing N N 307 
LYS   N     H     sing N N 308 
LYS   N     H2    sing N N 309 
LYS   CA    C     sing N N 310 
LYS   CA    CB    sing N N 311 
LYS   CA    HA    sing N N 312 
LYS   C     O     doub N N 313 
LYS   C     OXT   sing N N 314 
LYS   CB    CG    sing N N 315 
LYS   CB    HB2   sing N N 316 
LYS   CB    HB3   sing N N 317 
LYS   CG    CD    sing N N 318 
LYS   CG    HG2   sing N N 319 
LYS   CG    HG3   sing N N 320 
LYS   CD    CE    sing N N 321 
LYS   CD    HD2   sing N N 322 
LYS   CD    HD3   sing N N 323 
LYS   CE    NZ    sing N N 324 
LYS   CE    HE2   sing N N 325 
LYS   CE    HE3   sing N N 326 
LYS   NZ    HZ1   sing N N 327 
LYS   NZ    HZ2   sing N N 328 
LYS   NZ    HZ3   sing N N 329 
LYS   OXT   HXT   sing N N 330 
MET   N     CA    sing N N 331 
MET   N     H     sing N N 332 
MET   N     H2    sing N N 333 
MET   CA    C     sing N N 334 
MET   CA    CB    sing N N 335 
MET   CA    HA    sing N N 336 
MET   C     O     doub N N 337 
MET   C     OXT   sing N N 338 
MET   CB    CG    sing N N 339 
MET   CB    HB2   sing N N 340 
MET   CB    HB3   sing N N 341 
MET   CG    SD    sing N N 342 
MET   CG    HG2   sing N N 343 
MET   CG    HG3   sing N N 344 
MET   SD    CE    sing N N 345 
MET   CE    HE1   sing N N 346 
MET   CE    HE2   sing N N 347 
MET   CE    HE3   sing N N 348 
MET   OXT   HXT   sing N N 349 
PHE   N     CA    sing N N 350 
PHE   N     H     sing N N 351 
PHE   N     H2    sing N N 352 
PHE   CA    C     sing N N 353 
PHE   CA    CB    sing N N 354 
PHE   CA    HA    sing N N 355 
PHE   C     O     doub N N 356 
PHE   C     OXT   sing N N 357 
PHE   CB    CG    sing N N 358 
PHE   CB    HB2   sing N N 359 
PHE   CB    HB3   sing N N 360 
PHE   CG    CD1   doub Y N 361 
PHE   CG    CD2   sing Y N 362 
PHE   CD1   CE1   sing Y N 363 
PHE   CD1   HD1   sing N N 364 
PHE   CD2   CE2   doub Y N 365 
PHE   CD2   HD2   sing N N 366 
PHE   CE1   CZ    doub Y N 367 
PHE   CE1   HE1   sing N N 368 
PHE   CE2   CZ    sing Y N 369 
PHE   CE2   HE2   sing N N 370 
PHE   CZ    HZ    sing N N 371 
PHE   OXT   HXT   sing N N 372 
PRO   N     CA    sing N N 373 
PRO   N     CD    sing N N 374 
PRO   N     H     sing N N 375 
PRO   CA    C     sing N N 376 
PRO   CA    CB    sing N N 377 
PRO   CA    HA    sing N N 378 
PRO   C     O     doub N N 379 
PRO   C     OXT   sing N N 380 
PRO   CB    CG    sing N N 381 
PRO   CB    HB2   sing N N 382 
PRO   CB    HB3   sing N N 383 
PRO   CG    CD    sing N N 384 
PRO   CG    HG2   sing N N 385 
PRO   CG    HG3   sing N N 386 
PRO   CD    HD2   sing N N 387 
PRO   CD    HD3   sing N N 388 
PRO   OXT   HXT   sing N N 389 
SER   N     CA    sing N N 390 
SER   N     H     sing N N 391 
SER   N     H2    sing N N 392 
SER   CA    C     sing N N 393 
SER   CA    CB    sing N N 394 
SER   CA    HA    sing N N 395 
SER   C     O     doub N N 396 
SER   C     OXT   sing N N 397 
SER   CB    OG    sing N N 398 
SER   CB    HB2   sing N N 399 
SER   CB    HB3   sing N N 400 
SER   OG    HG    sing N N 401 
SER   OXT   HXT   sing N N 402 
THR   N     CA    sing N N 403 
THR   N     H     sing N N 404 
THR   N     H2    sing N N 405 
THR   CA    C     sing N N 406 
THR   CA    CB    sing N N 407 
THR   CA    HA    sing N N 408 
THR   C     O     doub N N 409 
THR   C     OXT   sing N N 410 
THR   CB    OG1   sing N N 411 
THR   CB    CG2   sing N N 412 
THR   CB    HB    sing N N 413 
THR   OG1   HG1   sing N N 414 
THR   CG2   HG21  sing N N 415 
THR   CG2   HG22  sing N N 416 
THR   CG2   HG23  sing N N 417 
THR   OXT   HXT   sing N N 418 
TRP   N     CA    sing N N 419 
TRP   N     H     sing N N 420 
TRP   N     H2    sing N N 421 
TRP   CA    C     sing N N 422 
TRP   CA    CB    sing N N 423 
TRP   CA    HA    sing N N 424 
TRP   C     O     doub N N 425 
TRP   C     OXT   sing N N 426 
TRP   CB    CG    sing N N 427 
TRP   CB    HB2   sing N N 428 
TRP   CB    HB3   sing N N 429 
TRP   CG    CD1   doub Y N 430 
TRP   CG    CD2   sing Y N 431 
TRP   CD1   NE1   sing Y N 432 
TRP   CD1   HD1   sing N N 433 
TRP   CD2   CE2   doub Y N 434 
TRP   CD2   CE3   sing Y N 435 
TRP   NE1   CE2   sing Y N 436 
TRP   NE1   HE1   sing N N 437 
TRP   CE2   CZ2   sing Y N 438 
TRP   CE3   CZ3   doub Y N 439 
TRP   CE3   HE3   sing N N 440 
TRP   CZ2   CH2   doub Y N 441 
TRP   CZ2   HZ2   sing N N 442 
TRP   CZ3   CH2   sing Y N 443 
TRP   CZ3   HZ3   sing N N 444 
TRP   CH2   HH2   sing N N 445 
TRP   OXT   HXT   sing N N 446 
TYR   N     CA    sing N N 447 
TYR   N     H     sing N N 448 
TYR   N     H2    sing N N 449 
TYR   CA    C     sing N N 450 
TYR   CA    CB    sing N N 451 
TYR   CA    HA    sing N N 452 
TYR   C     O     doub N N 453 
TYR   C     OXT   sing N N 454 
TYR   CB    CG    sing N N 455 
TYR   CB    HB2   sing N N 456 
TYR   CB    HB3   sing N N 457 
TYR   CG    CD1   doub Y N 458 
TYR   CG    CD2   sing Y N 459 
TYR   CD1   CE1   sing Y N 460 
TYR   CD1   HD1   sing N N 461 
TYR   CD2   CE2   doub Y N 462 
TYR   CD2   HD2   sing N N 463 
TYR   CE1   CZ    doub Y N 464 
TYR   CE1   HE1   sing N N 465 
TYR   CE2   CZ    sing Y N 466 
TYR   CE2   HE2   sing N N 467 
TYR   CZ    OH    sing N N 468 
TYR   OH    HH    sing N N 469 
TYR   OXT   HXT   sing N N 470 
VAL   N     CA    sing N N 471 
VAL   N     H     sing N N 472 
VAL   N     H2    sing N N 473 
VAL   CA    C     sing N N 474 
VAL   CA    CB    sing N N 475 
VAL   CA    HA    sing N N 476 
VAL   C     O     doub N N 477 
VAL   C     OXT   sing N N 478 
VAL   CB    CG1   sing N N 479 
VAL   CB    CG2   sing N N 480 
VAL   CB    HB    sing N N 481 
VAL   CG1   HG11  sing N N 482 
VAL   CG1   HG12  sing N N 483 
VAL   CG1   HG13  sing N N 484 
VAL   CG2   HG21  sing N N 485 
VAL   CG2   HG22  sing N N 486 
VAL   CG2   HG23  sing N N 487 
VAL   OXT   HXT   sing N N 488 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R01GM132640 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8DKP 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9D7L 
_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]   0.020607 
_atom_sites.fract_transf_matrix[1][2]   0.007224 
_atom_sites.fract_transf_matrix[1][3]   0.006414 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019536 
_atom_sites.fract_transf_matrix[2][3]   0.006675 
_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]   0.014206 
_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 
N 
O 
P 
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     . PRO   A 1 3   ? -15.382 13.537  52.853 1.00 97.86  ? 27  PRO   A N     1 
ATOM   2    C CA    . PRO   A 1 3   ? -14.063 14.088  53.178 1.00 102.76 ? 27  PRO   A CA    1 
ATOM   3    C C     . PRO   A 1 3   ? -13.653 15.217  52.240 1.00 105.62 ? 27  PRO   A C     1 
ATOM   4    O O     . PRO   A 1 3   ? -12.615 15.121  51.583 1.00 104.08 ? 27  PRO   A O     1 
ATOM   5    C CB    . PRO   A 1 3   ? -13.133 12.882  53.012 1.00 101.27 ? 27  PRO   A CB    1 
ATOM   6    C CG    . PRO   A 1 3   ? -13.866 11.944  52.051 1.00 99.17  ? 27  PRO   A CG    1 
ATOM   7    C CD    . PRO   A 1 3   ? -15.281 12.454  51.862 1.00 94.14  ? 27  PRO   A CD    1 
ATOM   8    N N     . GLN   A 1 4   ? -14.459 16.277  52.182 1.00 109.49 ? 28  GLN   A N     1 
ATOM   9    C CA    . GLN   A 1 4   ? -14.243 17.374  51.239 1.00 109.31 ? 28  GLN   A CA    1 
ATOM   10   C C     . GLN   A 1 4   ? -14.371 18.716  51.962 1.00 103.72 ? 28  GLN   A C     1 
ATOM   11   O O     . GLN   A 1 4   ? -15.157 19.580  51.574 1.00 105.13 ? 28  GLN   A O     1 
ATOM   12   C CB    . GLN   A 1 4   ? -15.224 17.281  50.068 1.00 107.97 ? 28  GLN   A CB    1 
ATOM   13   N N     . SER   A 1 5   ? -13.574 18.898  53.015 1.00 83.68  ? 29  SER   A N     1 
ATOM   14   C CA    . SER   A 1 5   ? -13.642 20.120  53.803 1.00 73.81  ? 29  SER   A CA    1 
ATOM   15   C C     . SER   A 1 5   ? -13.287 21.338  52.944 1.00 67.85  ? 29  SER   A C     1 
ATOM   16   O O     . SER   A 1 5   ? -12.775 21.222  51.829 1.00 67.62  ? 29  SER   A O     1 
ATOM   17   C CB    . SER   A 1 5   ? -12.716 20.028  55.018 1.00 68.86  ? 29  SER   A CB    1 
ATOM   18   O OG    . SER   A 1 5   ? -11.367 19.889  54.621 1.00 65.50  ? 29  SER   A OG    1 
ATOM   19   N N     . THR   A 1 6   ? -13.600 22.527  53.470 1.00 64.91  ? 30  THR   A N     1 
ATOM   20   C CA    . THR   A 1 6   ? -13.309 23.753  52.729 1.00 65.77  ? 30  THR   A CA    1 
ATOM   21   C C     . THR   A 1 6   ? -11.814 23.916  52.491 1.00 60.16  ? 30  THR   A C     1 
ATOM   22   O O     . THR   A 1 6   ? -11.402 24.427  51.444 1.00 60.73  ? 30  THR   A O     1 
ATOM   23   C CB    . THR   A 1 6   ? -13.873 24.974  53.467 1.00 66.25  ? 30  THR   A CB    1 
ATOM   24   O OG1   . THR   A 1 6   ? -15.301 24.985  53.357 1.00 70.88  ? 30  THR   A OG1   1 
ATOM   25   C CG2   . THR   A 1 6   ? -13.325 26.273  52.882 1.00 65.55  ? 30  THR   A CG2   1 
ATOM   26   N N     . LEU   A 1 7   ? -10.983 23.476  53.437 1.00 60.58  ? 31  LEU   A N     1 
ATOM   27   C CA    . LEU   A 1 7   ? -9.543  23.509  53.203 1.00 58.66  ? 31  LEU   A CA    1 
ATOM   28   C C     . LEU   A 1 7   ? -9.138  22.528  52.110 1.00 53.72  ? 31  LEU   A C     1 
ATOM   29   O O     . LEU   A 1 7   ? -8.319  22.862  51.247 1.00 51.79  ? 31  LEU   A O     1 
ATOM   30   C CB    . LEU   A 1 7   ? -8.790  23.218  54.500 1.00 56.31  ? 31  LEU   A CB    1 
ATOM   31   C CG    . LEU   A 1 7   ? -9.003  24.346  55.510 1.00 61.68  ? 31  LEU   A CG    1 
ATOM   32   C CD1   . LEU   A 1 7   ? -8.400  23.980  56.848 1.00 59.58  ? 31  LEU   A CD1   1 
ATOM   33   C CD2   . LEU   A 1 7   ? -8.412  25.651  54.986 1.00 59.53  ? 31  LEU   A CD2   1 
ATOM   34   N N     . ARG   A 1 8   ? -9.710  21.319  52.123 1.00 59.72  ? 32  ARG   A N     1 
ATOM   35   C CA    . ARG   A 1 8   ? -9.370  20.325  51.109 1.00 53.74  ? 32  ARG   A CA    1 
ATOM   36   C C     . ARG   A 1 8   ? -9.904  20.719  49.737 1.00 60.55  ? 32  ARG   A C     1 
ATOM   37   O O     . ARG   A 1 8   ? -9.241  20.472  48.721 1.00 61.61  ? 32  ARG   A O     1 
ATOM   38   C CB    . ARG   A 1 8   ? -9.897  18.951  51.528 1.00 59.64  ? 32  ARG   A CB    1 
ATOM   39   N N     . ARG   A 1 9   ? -11.088 21.336  49.686 1.00 59.99  ? 33  ARG   A N     1 
ATOM   40   C CA    . ARG   A 1 9   ? -11.611 21.833  48.418 1.00 58.55  ? 33  ARG   A CA    1 
ATOM   41   C C     . ARG   A 1 9   ? -10.719 22.929  47.851 1.00 58.20  ? 33  ARG   A C     1 
ATOM   42   O O     . ARG   A 1 9   ? -10.538 23.018  46.632 1.00 60.49  ? 33  ARG   A O     1 
ATOM   43   C CB    . ARG   A 1 9   ? -13.044 22.343  48.597 1.00 62.83  ? 33  ARG   A CB    1 
ATOM   44   N N     . ALA   A 1 10  ? -10.146 23.768  48.721 1.00 56.32  ? 34  ALA   A N     1 
ATOM   45   C CA    . ALA   A 1 10  ? -9.264  24.829  48.251 1.00 53.13  ? 34  ALA   A CA    1 
ATOM   46   C C     . ALA   A 1 10  ? -7.998  24.255  47.639 1.00 54.08  ? 34  ALA   A C     1 
ATOM   47   O O     . ALA   A 1 10  ? -7.483  24.790  46.652 1.00 53.50  ? 34  ALA   A O     1 
ATOM   48   C CB    . ALA   A 1 10  ? -8.911  25.779  49.394 1.00 57.59  ? 34  ALA   A CB    1 
ATOM   49   N N     . ILE   A 1 11  ? -7.463  23.179  48.225 1.00 53.41  ? 35  ILE   A N     1 
ATOM   50   C CA    . ILE   A 1 11  ? -6.316  22.506  47.620 1.00 51.18  ? 35  ILE   A CA    1 
ATOM   51   C C     . ILE   A 1 11  ? -6.680  21.983  46.240 1.00 54.82  ? 35  ILE   A C     1 
ATOM   52   O O     . ILE   A 1 11  ? -5.991  22.249  45.253 1.00 50.38  ? 35  ILE   A O     1 
ATOM   53   C CB    . ILE   A 1 11  ? -5.821  21.361  48.513 1.00 50.99  ? 35  ILE   A CB    1 
ATOM   54   C CG1   . ILE   A 1 11  ? -5.316  21.889  49.854 1.00 49.42  ? 35  ILE   A CG1   1 
ATOM   55   C CG2   . ILE   A 1 11  ? -4.737  20.570  47.779 1.00 51.64  ? 35  ILE   A CG2   1 
ATOM   56   C CD1   . ILE   A 1 11  ? -5.211  20.819  50.875 1.00 46.17  ? 35  ILE   A CD1   1 
ATOM   57   N N     . THR   A 1 12  ? -7.771  21.219  46.158 1.00 57.77  ? 36  THR   A N     1 
ATOM   58   C CA    . THR   A 1 12  ? -8.140  20.597  44.894 1.00 57.36  ? 36  THR   A CA    1 
ATOM   59   C C     . THR   A 1 12  ? -8.476  21.638  43.830 1.00 56.52  ? 36  THR   A C     1 
ATOM   60   O O     . THR   A 1 12  ? -8.284  21.389  42.635 1.00 54.05  ? 36  THR   A O     1 
ATOM   61   C CB    . THR   A 1 12  ? -9.314  19.643  45.116 1.00 61.99  ? 36  THR   A CB    1 
ATOM   62   N N     . ALA   A 1 13  ? -8.958  22.814  44.242 1.00 57.99  ? 37  ALA   A N     1 
ATOM   63   C CA    . ALA   A 1 13  ? -9.325  23.863  43.298 1.00 54.76  ? 37  ALA   A CA    1 
ATOM   64   C C     . ALA   A 1 13  ? -8.124  24.618  42.735 1.00 53.63  ? 37  ALA   A C     1 
ATOM   65   O O     . ALA   A 1 13  ? -8.252  25.278  41.697 1.00 53.21  ? 37  ALA   A O     1 
ATOM   66   C CB    . ALA   A 1 13  ? -10.289 24.854  43.965 1.00 57.65  ? 37  ALA   A CB    1 
ATOM   67   N N     . ALA   A 1 14  ? -6.973  24.547  43.390 1.00 51.22  ? 38  ALA   A N     1 
ATOM   68   C CA    . ALA   A 1 14  ? -5.775  25.239  42.940 1.00 54.73  ? 38  ALA   A CA    1 
ATOM   69   C C     . ALA   A 1 14  ? -4.909  24.387  42.023 1.00 51.80  ? 38  ALA   A C     1 
ATOM   70   O O     . ALA   A 1 14  ? -3.942  24.910  41.459 1.00 50.48  ? 38  ALA   A O     1 
ATOM   71   C CB    . ALA   A 1 14  ? -4.940  25.686  44.149 1.00 48.61  ? 38  ALA   A CB    1 
ATOM   72   N N     . TYR   A 1 15  ? -5.266  23.109  41.850 1.00 51.57  ? 39  TYR   A N     1 
ATOM   73   C CA    . TYR   A 1 15  ? -4.390  22.114  41.230 1.00 52.80  ? 39  TYR   A CA    1 
ATOM   74   C C     . TYR   A 1 15  ? -3.779  22.631  39.938 1.00 52.44  ? 39  TYR   A C     1 
ATOM   75   O O     . TYR   A 1 15  ? -2.554  22.615  39.764 1.00 52.34  ? 39  TYR   A O     1 
ATOM   76   C CB    . TYR   A 1 15  ? -5.185  20.834  40.968 1.00 56.78  ? 39  TYR   A CB    1 
ATOM   77   C CG    . TYR   A 1 15  ? -4.367  19.613  40.622 1.00 55.65  ? 39  TYR   A CG    1 
ATOM   78   C CD1   . TYR   A 1 15  ? -3.004  19.582  40.831 1.00 50.92  ? 39  TYR   A CD1   1 
ATOM   79   C CD2   . TYR   A 1 15  ? -4.970  18.490  40.066 1.00 62.40  ? 39  TYR   A CD2   1 
ATOM   80   C CE1   . TYR   A 1 15  ? -2.256  18.461  40.517 1.00 54.05  ? 39  TYR   A CE1   1 
ATOM   81   C CE2   . TYR   A 1 15  ? -4.228  17.361  39.746 1.00 63.90  ? 39  TYR   A CE2   1 
ATOM   82   C CZ    . TYR   A 1 15  ? -2.870  17.354  39.977 1.00 58.27  ? 39  TYR   A CZ    1 
ATOM   83   O OH    . TYR   A 1 15  ? -2.119  16.242  39.661 1.00 57.61  ? 39  TYR   A OH    1 
ATOM   84   N N     . ARG   A 1 16  ? -4.615  23.102  39.029 1.00 54.20  ? 40  ARG   A N     1 
ATOM   85   C CA    . ARG   A 1 16  ? -4.157  23.647  37.762 1.00 59.62  ? 40  ARG   A CA    1 
ATOM   86   C C     . ARG   A 1 16  ? -4.723  25.042  37.560 1.00 61.81  ? 40  ARG   A C     1 
ATOM   87   O O     . ARG   A 1 16  ? -5.060  25.445  36.442 1.00 62.45  ? 40  ARG   A O     1 
ATOM   88   C CB    . ARG   A 1 16  ? -4.537  22.726  36.606 1.00 64.78  ? 40  ARG   A CB    1 
ATOM   89   C CG    . ARG   A 1 16  ? -4.111  21.284  36.824 1.00 65.02  ? 40  ARG   A CG    1 
ATOM   90   C CD    . ARG   A 1 16  ? -4.442  20.402  35.620 1.00 69.07  ? 40  ARG   A CD    1 
ATOM   91   N NE    . ARG   A 1 16  ? -4.238  18.992  35.931 1.00 73.47  ? 40  ARG   A NE    1 
ATOM   92   C CZ    . ARG   A 1 16  ? -3.051  18.407  36.021 1.00 70.93  ? 40  ARG   A CZ    1 
ATOM   93   N NH1   . ARG   A 1 16  ? -1.929  19.079  35.807 1.00 67.98  ? 40  ARG   A NH1   1 
ATOM   94   N NH2   . ARG   A 1 16  ? -2.985  17.117  36.334 1.00 72.31  ? 40  ARG   A NH2   1 
ATOM   95   N N     . ARG   A 1 17  ? -4.851  25.793  38.651 1.00 59.93  ? 41  ARG   A N     1 
ATOM   96   C CA    . ARG   A 1 17  ? -5.289  27.174  38.539 1.00 60.28  ? 41  ARG   A CA    1 
ATOM   97   C C     . ARG   A 1 17  ? -4.317  27.939  37.646 1.00 57.27  ? 41  ARG   A C     1 
ATOM   98   O O     . ARG   A 1 17  ? -3.101  27.719  37.728 1.00 52.83  ? 41  ARG   A O     1 
ATOM   99   C CB    . ARG   A 1 17  ? -5.357  27.833  39.919 1.00 59.17  ? 41  ARG   A CB    1 
ATOM   100  C CG    . ARG   A 1 17  ? -5.646  29.335  39.869 1.00 57.16  ? 41  ARG   A CG    1 
ATOM   101  C CD    . ARG   A 1 17  ? -5.897  29.854  41.257 1.00 58.28  ? 41  ARG   A CD    1 
ATOM   102  N NE    . ARG   A 1 17  ? -7.116  29.269  41.796 1.00 61.18  ? 41  ARG   A NE    1 
ATOM   103  C CZ    . ARG   A 1 17  ? -7.261  28.884  43.054 1.00 58.22  ? 41  ARG   A CZ    1 
ATOM   104  N NH1   . ARG   A 1 17  ? -6.277  29.012  43.931 1.00 53.51  ? 41  ARG   A NH1   1 
ATOM   105  N NH2   . ARG   A 1 17  ? -8.418  28.348  43.438 1.00 58.64  ? 41  ARG   A NH2   1 
ATOM   106  N N     . PRO   A 1 18  ? -4.811  28.821  36.781 1.00 55.86  ? 42  PRO   A N     1 
ATOM   107  C CA    . PRO   A 1 18  ? -3.916  29.617  35.935 1.00 55.76  ? 42  PRO   A CA    1 
ATOM   108  C C     . PRO   A 1 18  ? -2.846  30.324  36.752 1.00 58.35  ? 42  PRO   A C     1 
ATOM   109  O O     . PRO   A 1 18  ? -3.128  30.924  37.794 1.00 53.05  ? 42  PRO   A O     1 
ATOM   110  C CB    . PRO   A 1 18  ? -4.866  30.613  35.266 1.00 56.45  ? 42  PRO   A CB    1 
ATOM   111  C CG    . PRO   A 1 18  ? -6.180  29.900  35.226 1.00 60.55  ? 42  PRO   A CG    1 
ATOM   112  C CD    . PRO   A 1 18  ? -6.232  29.032  36.445 1.00 57.44  ? 42  PRO   A CD    1 
ATOM   113  N N     . GLU   A 1 19  ? -1.598  30.223  36.278 1.00 52.41  ? 43  GLU   A N     1 
ATOM   114  C CA    . GLU   A 1 19  ? -0.476  30.813  37.000 1.00 55.59  ? 43  GLU   A CA    1 
ATOM   115  C C     . GLU   A 1 19  ? -0.705  32.300  37.257 1.00 53.42  ? 43  GLU   A C     1 
ATOM   116  O O     . GLU   A 1 19  ? -0.393  32.805  38.342 1.00 58.09  ? 43  GLU   A O     1 
ATOM   117  C CB    . GLU   A 1 19  ? 0.817   30.577  36.213 1.00 47.40  ? 43  GLU   A CB    1 
ATOM   118  C CG    . GLU   A 1 19  ? 2.087   31.057  36.869 1.00 52.52  ? 43  GLU   A CG    1 
ATOM   119  C CD    . GLU   A 1 19  ? 3.320   30.371  36.285 1.00 47.00  ? 43  GLU   A CD    1 
ATOM   120  O OE1   . GLU   A 1 19  ? 3.166   29.590  35.316 1.00 53.44  ? 43  GLU   A OE1   1 
ATOM   121  O OE2   . GLU   A 1 19  ? 4.434   30.622  36.780 1.00 44.05  ? 43  GLU   A OE2   1 
ATOM   122  N N     . THR   A 1 20  ? -1.276  33.008  36.285 1.00 54.08  ? 44  THR   A N     1 
ATOM   123  C CA    . THR   A 1 20  ? -1.496  34.441  36.449 1.00 56.43  ? 44  THR   A CA    1 
ATOM   124  C C     . THR   A 1 20  ? -2.390  34.736  37.650 1.00 58.59  ? 44  THR   A C     1 
ATOM   125  O O     . THR   A 1 20  ? -2.195  35.741  38.343 1.00 61.06  ? 44  THR   A O     1 
ATOM   126  C CB    . THR   A 1 20  ? -2.101  35.025  35.170 1.00 53.26  ? 44  THR   A CB    1 
ATOM   127  N N     . GLU   A 1 21  ? -3.377  33.875  37.910 1.00 56.37  ? 45  GLU   A N     1 
ATOM   128  C CA    . GLU   A 1 21  ? -4.270  34.076  39.046 1.00 58.30  ? 45  GLU   A CA    1 
ATOM   129  C C     . GLU   A 1 21  ? -3.670  33.601  40.360 1.00 57.22  ? 45  GLU   A C     1 
ATOM   130  O O     . GLU   A 1 21  ? -4.090  34.072  41.425 1.00 55.06  ? 45  GLU   A O     1 
ATOM   131  C CB    . GLU   A 1 21  ? -5.601  33.359  38.804 1.00 64.57  ? 45  GLU   A CB    1 
ATOM   132  N N     . CYS   A 1 22  ? -2.705  32.678  40.320 1.00 56.61  ? 46  CYS   A N     1 
ATOM   133  C CA    . CYS   A 1 22  ? -2.094  32.223  41.559 1.00 53.67  ? 46  CYS   A CA    1 
ATOM   134  C C     . CYS   A 1 22  ? -1.218  33.295  42.182 1.00 53.67  ? 46  CYS   A C     1 
ATOM   135  O O     . CYS   A 1 22  ? -0.957  33.249  43.385 1.00 50.63  ? 46  CYS   A O     1 
ATOM   136  C CB    . CYS   A 1 22  ? -1.252  30.965  41.318 1.00 53.63  ? 46  CYS   A CB    1 
ATOM   137  S SG    . CYS   A 1 22  ? -2.196  29.483  40.939 1.00 51.82  ? 46  CYS   A SG    1 
ATOM   138  N N     . LEU   A 1 23  ? -0.752  34.253  41.394 1.00 50.94  ? 47  LEU   A N     1 
ATOM   139  C CA    . LEU   A 1 23  ? 0.368   35.075  41.844 1.00 51.46  ? 47  LEU   A CA    1 
ATOM   140  C C     . LEU   A 1 23  ? -0.022  36.198  42.803 1.00 52.36  ? 47  LEU   A C     1 
ATOM   141  O O     . LEU   A 1 23  ? 0.656   36.360  43.829 1.00 55.88  ? 47  LEU   A O     1 
ATOM   142  C CB    . LEU   A 1 23  ? 1.119   35.650  40.640 1.00 55.03  ? 47  LEU   A CB    1 
ATOM   143  C CG    . LEU   A 1 23  ? 2.403   34.944  40.215 1.00 53.99  ? 47  LEU   A CG    1 
ATOM   144  C CD1   . LEU   A 1 23  ? 3.526   35.201  41.215 1.00 52.57  ? 47  LEU   A CD1   1 
ATOM   145  C CD2   . LEU   A 1 23  ? 2.160   33.451  40.078 1.00 53.51  ? 47  LEU   A CD2   1 
ATOM   146  N N     . PRO   A 1 24  ? -1.065  36.988  42.537 1.00 54.21  ? 48  PRO   A N     1 
ATOM   147  C CA    . PRO   A 1 24  ? -1.327  38.170  43.375 1.00 54.17  ? 48  PRO   A CA    1 
ATOM   148  C C     . PRO   A 1 24  ? -1.425  37.837  44.855 1.00 53.55  ? 48  PRO   A C     1 
ATOM   149  O O     . PRO   A 1 24  ? -0.829  38.555  45.671 1.00 57.99  ? 48  PRO   A O     1 
ATOM   150  C CB    . PRO   A 1 24  ? -2.655  38.712  42.821 1.00 57.46  ? 48  PRO   A CB    1 
ATOM   151  C CG    . PRO   A 1 24  ? -2.619  38.326  41.393 1.00 58.68  ? 48  PRO   A CG    1 
ATOM   152  C CD    . PRO   A 1 24  ? -1.961  36.976  41.357 1.00 55.71  ? 48  PRO   A CD    1 
ATOM   153  N N     . PRO   A 1 25  ? -2.159  36.787  45.269 1.00 54.93  ? 49  PRO   A N     1 
ATOM   154  C CA    . PRO   A 1 25  ? -2.115  36.437  46.703 1.00 51.67  ? 49  PRO   A CA    1 
ATOM   155  C C     . PRO   A 1 25  ? -0.719  36.134  47.202 1.00 55.93  ? 49  PRO   A C     1 
ATOM   156  O O     . PRO   A 1 25  ? -0.374  36.484  48.341 1.00 54.51  ? 49  PRO   A O     1 
ATOM   157  C CB    . PRO   A 1 25  ? -3.034  35.206  46.803 1.00 55.73  ? 49  PRO   A CB    1 
ATOM   158  C CG    . PRO   A 1 25  ? -3.243  34.743  45.397 1.00 55.98  ? 49  PRO   A CG    1 
ATOM   159  C CD    . PRO   A 1 25  ? -3.185  35.987  44.573 1.00 53.93  ? 49  PRO   A CD    1 
ATOM   160  N N     . LEU   A 1 26  ? 0.099   35.478  46.380 1.00 51.98  ? 50  LEU   A N     1 
ATOM   161  C CA    . LEU   A 1 26  ? 1.453   35.147  46.803 1.00 49.36  ? 50  LEU   A CA    1 
ATOM   162  C C     . LEU   A 1 26  ? 2.323   36.390  46.879 1.00 49.12  ? 50  LEU   A C     1 
ATOM   163  O O     . LEU   A 1 26  ? 3.081   36.568  47.838 1.00 48.55  ? 50  LEU   A O     1 
ATOM   164  C CB    . LEU   A 1 26  ? 2.066   34.125  45.848 1.00 45.01  ? 50  LEU   A CB    1 
ATOM   165  C CG    . LEU   A 1 26  ? 1.350   32.775  45.767 1.00 46.63  ? 50  LEU   A CG    1 
ATOM   166  C CD1   . LEU   A 1 26  ? 2.030   31.895  44.750 1.00 46.55  ? 50  LEU   A CD1   1 
ATOM   167  C CD2   . LEU   A 1 26  ? 1.236   32.069  47.121 1.00 47.47  ? 50  LEU   A CD2   1 
ATOM   168  N N     . VAL   A 1 27  ? 2.246   37.252  45.859 1.00 48.68  ? 51  VAL   A N     1 
ATOM   169  C CA    . VAL   A 1 27  ? 3.011   38.495  45.864 1.00 51.39  ? 51  VAL   A CA    1 
ATOM   170  C C     . VAL   A 1 27  ? 2.677   39.321  47.100 1.00 52.75  ? 51  VAL   A C     1 
ATOM   171  O O     . VAL   A 1 27  ? 3.572   39.860  47.765 1.00 51.91  ? 51  VAL   A O     1 
ATOM   172  C CB    . VAL   A 1 27  ? 2.752   39.292  44.567 1.00 49.43  ? 51  VAL   A CB    1 
ATOM   173  N N     . GLU   A 1 28  ? 1.388   39.417  47.441 1.00 51.83  ? 52  GLU   A N     1 
ATOM   174  C CA    . GLU   A 1 28  ? 0.988   40.195  48.612 1.00 54.33  ? 52  GLU   A CA    1 
ATOM   175  C C     . GLU   A 1 28  ? 1.437   39.526  49.909 1.00 55.84  ? 52  GLU   A C     1 
ATOM   176  O O     . GLU   A 1 28  ? 1.957   40.195  50.810 1.00 56.46  ? 52  GLU   A O     1 
ATOM   177  C CB    . GLU   A 1 28  ? -0.526  40.406  48.613 1.00 58.01  ? 52  GLU   A CB    1 
ATOM   178  N N     . ALA   A 1 29  ? 1.252   38.208  50.023 1.00 53.67  ? 53  ALA   A N     1 
ATOM   179  C CA    . ALA   A 1 29  ? 1.701   37.501  51.213 1.00 52.01  ? 53  ALA   A CA    1 
ATOM   180  C C     . ALA   A 1 29  ? 3.218   37.454  51.320 1.00 51.47  ? 53  ALA   A C     1 
ATOM   181  O O     . ALA   A 1 29  ? 3.739   37.233  52.417 1.00 49.56  ? 53  ALA   A O     1 
ATOM   182  C CB    . ALA   A 1 29  ? 1.140   36.078  51.234 1.00 51.18  ? 53  ALA   A CB    1 
ATOM   183  N N     . ALA   A 1 30  ? 3.936   37.652  50.212 1.00 50.57  ? 54  ALA   A N     1 
ATOM   184  C CA    . ALA   A 1 30  ? 5.390   37.617  50.220 1.00 49.26  ? 54  ALA   A CA    1 
ATOM   185  C C     . ALA   A 1 30  ? 6.034   38.988  50.359 1.00 55.24  ? 54  ALA   A C     1 
ATOM   186  O O     . ALA   A 1 30  ? 7.260   39.063  50.499 1.00 55.29  ? 54  ALA   A O     1 
ATOM   187  C CB    . ALA   A 1 30  ? 5.914   36.952  48.943 1.00 45.98  ? 54  ALA   A CB    1 
ATOM   188  N N     . THR   A 1 31  ? 5.261   40.070  50.304 1.00 55.80  ? 55  THR   A N     1 
ATOM   189  C CA    . THR   A 1 31  ? 5.841   41.396  50.444 1.00 56.05  ? 55  THR   A CA    1 
ATOM   190  C C     . THR   A 1 31  ? 6.152   41.665  51.912 1.00 53.82  ? 55  THR   A C     1 
ATOM   191  O O     . THR   A 1 31  ? 5.291   41.503  52.781 1.00 56.71  ? 55  THR   A O     1 
ATOM   192  C CB    . THR   A 1 31  ? 4.899   42.464  49.890 1.00 56.99  ? 55  THR   A CB    1 
ATOM   193  O OG1   . THR   A 1 31  ? 4.646   42.194  48.506 1.00 61.33  ? 55  THR   A OG1   1 
ATOM   194  C CG2   . THR   A 1 31  ? 5.527   43.841  50.014 1.00 58.91  ? 55  THR   A CG2   1 
ATOM   195  N N     . GLN   A 1 32  ? 7.395   42.038  52.187 1.00 55.83  ? 56  GLN   A N     1 
ATOM   196  C CA    . GLN   A 1 32  ? 7.839   42.392  53.524 1.00 54.11  ? 56  GLN   A CA    1 
ATOM   197  C C     . GLN   A 1 32  ? 8.075   43.896  53.601 1.00 57.00  ? 56  GLN   A C     1 
ATOM   198  O O     . GLN   A 1 32  ? 8.151   44.589  52.581 1.00 57.22  ? 56  GLN   A O     1 
ATOM   199  C CB    . GLN   A 1 32  ? 9.109   41.612  53.899 1.00 57.54  ? 56  GLN   A CB    1 
ATOM   200  N N     . SER   A 1 33  ? 8.172   44.402  54.831 1.00 53.97  ? 57  SER   A N     1 
ATOM   201  C CA    . SER   A 1 33  ? 8.421   45.823  55.023 1.00 56.35  ? 57  SER   A CA    1 
ATOM   202  C C     . SER   A 1 33  ? 9.762   46.218  54.408 1.00 55.50  ? 57  SER   A C     1 
ATOM   203  O O     . SER   A 1 33  ? 10.643  45.382  54.185 1.00 56.51  ? 57  SER   A O     1 
ATOM   204  C CB    . SER   A 1 33  ? 8.409   46.173  56.511 1.00 58.03  ? 57  SER   A CB    1 
ATOM   205  O OG    . SER   A 1 33  ? 9.442   45.484  57.200 1.00 58.48  ? 57  SER   A OG    1 
ATOM   206  N N     . LYS   A 1 34  ? 9.912   47.517  54.139 1.00 56.44  ? 58  LYS   A N     1 
ATOM   207  C CA    . LYS   A 1 34  ? 11.194  48.019  53.655 1.00 58.11  ? 58  LYS   A CA    1 
ATOM   208  C C     . LYS   A 1 34  ? 12.316  47.687  54.629 1.00 57.57  ? 58  LYS   A C     1 
ATOM   209  O O     . LYS   A 1 34  ? 13.414  47.304  54.209 1.00 55.72  ? 58  LYS   A O     1 
ATOM   210  C CB    . LYS   A 1 34  ? 11.135  49.532  53.414 1.00 58.41  ? 58  LYS   A CB    1 
ATOM   211  C CG    . LYS   A 1 34  ? 12.497  50.124  53.032 1.00 59.85  ? 58  LYS   A CG    1 
ATOM   212  C CD    . LYS   A 1 34  ? 12.466  51.615  52.767 1.00 63.97  ? 58  LYS   A CD    1 
ATOM   213  C CE    . LYS   A 1 34  ? 13.864  52.153  52.460 1.00 64.42  ? 58  LYS   A CE    1 
ATOM   214  N NZ    . LYS   A 1 34  ? 13.880  53.638  52.292 1.00 69.02  ? 58  LYS   A NZ    1 
ATOM   215  N N     . GLU   A 1 35  ? 12.056  47.813  55.935 1.00 54.21  ? 59  GLU   A N     1 
ATOM   216  C CA    . GLU   A 1 35  ? 13.096  47.548  56.925 1.00 56.26  ? 59  GLU   A CA    1 
ATOM   217  C C     . GLU   A 1 35  ? 13.560  46.100  56.865 1.00 56.18  ? 59  GLU   A C     1 
ATOM   218  O O     . GLU   A 1 35  ? 14.763  45.822  56.925 1.00 55.50  ? 59  GLU   A O     1 
ATOM   219  C CB    . GLU   A 1 35  ? 12.591  47.883  58.328 1.00 59.01  ? 59  GLU   A CB    1 
ATOM   220  N N     . ILE   A 1 36  ? 12.614  45.163  56.760 1.00 52.39  ? 60  ILE   A N     1 
ATOM   221  C CA    . ILE   A 1 36  ? 12.964  43.752  56.661 1.00 54.34  ? 60  ILE   A CA    1 
ATOM   222  C C     . ILE   A 1 36  ? 13.661  43.464  55.338 1.00 50.92  ? 60  ILE   A C     1 
ATOM   223  O O     . ILE   A 1 36  ? 14.632  42.704  55.287 1.00 48.54  ? 60  ILE   A O     1 
ATOM   224  C CB    . ILE   A 1 36  ? 11.704  42.885  56.854 1.00 53.88  ? 60  ILE   A CB    1 
ATOM   225  C CG1   . ILE   A 1 36  ? 11.306  42.866  58.330 1.00 53.49  ? 60  ILE   A CG1   1 
ATOM   226  C CG2   . ILE   A 1 36  ? 11.913  41.462  56.325 1.00 49.65  ? 60  ILE   A CG2   1 
ATOM   227  C CD1   . ILE   A 1 36  ? 10.194  41.898  58.657 1.00 55.35  ? 60  ILE   A CD1   1 
ATOM   228  N N     . ARG   A 1 37  ? 13.194  44.081  54.247 1.00 51.55  ? 61  ARG   A N     1 
ATOM   229  C CA    . ARG   A 1 37  ? 13.833  43.854  52.956 1.00 53.67  ? 61  ARG   A CA    1 
ATOM   230  C C     . ARG   A 1 37  ? 15.271  44.353  52.965 1.00 51.60  ? 61  ARG   A C     1 
ATOM   231  O O     . ARG   A 1 37  ? 16.179  43.674  52.464 1.00 45.02  ? 61  ARG   A O     1 
ATOM   232  C CB    . ARG   A 1 37  ? 13.020  44.529  51.845 1.00 55.22  ? 61  ARG   A CB    1 
ATOM   233  C CG    . ARG   A 1 37  ? 11.720  43.791  51.532 1.00 55.80  ? 61  ARG   A CG    1 
ATOM   234  C CD    . ARG   A 1 37  ? 11.017  44.332  50.284 1.00 57.46  ? 61  ARG   A CD    1 
ATOM   235  N NE    . ARG   A 1 37  ? 10.337  45.597  50.526 1.00 61.92  ? 61  ARG   A NE    1 
ATOM   236  C CZ    . ARG   A 1 37  ? 10.863  46.786  50.268 1.00 63.09  ? 61  ARG   A CZ    1 
ATOM   237  N NH1   . ARG   A 1 37  ? 12.086  46.907  49.776 1.00 67.34  ? 61  ARG   A NH1   1 
ATOM   238  N NH2   . ARG   A 1 37  ? 10.143  47.881  50.504 1.00 60.28  ? 61  ARG   A NH2   1 
ATOM   239  N N     . ASP   A 1 38  ? 15.494  45.532  53.545 1.00 50.71  ? 62  ASP   A N     1 
ATOM   240  C CA    . ASP   A 1 38  ? 16.836  46.094  53.630 1.00 52.71  ? 62  ASP   A CA    1 
ATOM   241  C C     . ASP   A 1 38  ? 17.737  45.212  54.482 1.00 51.37  ? 62  ASP   A C     1 
ATOM   242  O O     . ASP   A 1 38  ? 18.887  44.942  54.119 1.00 52.77  ? 62  ASP   A O     1 
ATOM   243  C CB    . ASP   A 1 38  ? 16.774  47.511  54.206 1.00 53.52  ? 62  ASP   A CB    1 
ATOM   244  C CG    . ASP   A 1 38  ? 16.229  48.528  53.215 1.00 56.46  ? 62  ASP   A CG    1 
ATOM   245  O OD1   . ASP   A 1 38  ? 16.018  48.162  52.036 1.00 55.18  ? 62  ASP   A OD1   1 
ATOM   246  O OD2   . ASP   A 1 38  ? 16.009  49.695  53.617 1.00 61.72  ? 62  ASP   A OD2   1 
ATOM   247  N N     . ALA   A 1 39  ? 17.231  44.754  55.628 1.00 52.16  ? 63  ALA   A N     1 
ATOM   248  C CA    . ALA   A 1 39  ? 18.049  43.917  56.502 1.00 47.49  ? 63  ALA   A CA    1 
ATOM   249  C C     . ALA   A 1 39  ? 18.338  42.563  55.861 1.00 47.76  ? 63  ALA   A C     1 
ATOM   250  O O     . ALA   A 1 39  ? 19.449  42.039  55.992 1.00 48.90  ? 63  ALA   A O     1 
ATOM   251  C CB    . ALA   A 1 39  ? 17.367  43.756  57.859 1.00 49.36  ? 63  ALA   A CB    1 
ATOM   252  N N     . ALA   A 1 40  ? 17.354  41.988  55.149 1.00 46.53  ? 64  ALA   A N     1 
ATOM   253  C CA    . ALA   A 1 40  ? 17.561  40.727  54.441 1.00 45.43  ? 64  ALA   A CA    1 
ATOM   254  C C     . ALA   A 1 40  ? 18.536  40.884  53.286 1.00 45.59  ? 64  ALA   A C     1 
ATOM   255  O O     . ALA   A 1 40  ? 19.290  39.957  52.980 1.00 42.75  ? 64  ALA   A O     1 
ATOM   256  C CB    . ALA   A 1 40  ? 16.234  40.182  53.912 1.00 40.66  ? 64  ALA   A CB    1 
ATOM   257  N N     . ALA   A 1 41  ? 18.520  42.033  52.615 1.00 44.57  ? 65  ALA   A N     1 
ATOM   258  C CA    . ALA   A 1 41  ? 19.491  42.249  51.555 1.00 45.28  ? 65  ALA   A CA    1 
ATOM   259  C C     . ALA   A 1 41  ? 20.896  42.340  52.127 1.00 47.78  ? 65  ALA   A C     1 
ATOM   260  O O     . ALA   A 1 41  ? 21.850  41.833  51.527 1.00 47.72  ? 65  ALA   A O     1 
ATOM   261  C CB    . ALA   A 1 41  ? 19.139  43.508  50.767 1.00 47.22  ? 65  ALA   A CB    1 
ATOM   262  N N     . SER   A 1 42  ? 21.034  42.954  53.304 1.00 47.08  ? 66  SER   A N     1 
ATOM   263  C CA    . SER   A 1 42  ? 22.345  43.062  53.931 1.00 48.31  ? 66  SER   A CA    1 
ATOM   264  C C     . SER   A 1 42  ? 22.852  41.691  54.356 1.00 45.69  ? 66  SER   A C     1 
ATOM   265  O O     . SER   A 1 42  ? 23.994  41.328  54.062 1.00 47.73  ? 66  SER   A O     1 
ATOM   266  C CB    . SER   A 1 42  ? 22.285  44.019  55.126 1.00 49.53  ? 66  SER   A CB    1 
ATOM   267  N N     . THR   A 1 43  ? 22.002  40.903  55.026 1.00 44.28  ? 67  THR   A N     1 
ATOM   268  C CA    . THR   A 1 43  ? 22.380  39.543  55.398 1.00 40.62  ? 67  THR   A CA    1 
ATOM   269  C C     . THR   A 1 43  ? 22.712  38.705  54.172 1.00 43.86  ? 67  THR   A C     1 
ATOM   270  O O     . THR   A 1 43  ? 23.736  38.012  54.139 1.00 42.55  ? 67  THR   A O     1 
ATOM   271  C CB    . THR   A 1 43  ? 21.256  38.892  56.200 1.00 42.31  ? 67  THR   A CB    1 
ATOM   272  O OG1   . THR   A 1 43  ? 21.038  39.646  57.398 1.00 44.79  ? 67  THR   A OG1   1 
ATOM   273  C CG2   . THR   A 1 43  ? 21.609  37.443  56.562 1.00 41.39  ? 67  THR   A CG2   1 
ATOM   274  N N     . ALA   A 1 44  ? 21.848  38.754  53.152 1.00 41.71  ? 68  ALA   A N     1 
ATOM   275  C CA    . ALA   A 1 44  ? 22.089  37.994  51.930 1.00 40.30  ? 68  ALA   A CA    1 
ATOM   276  C C     . ALA   A 1 44  ? 23.409  38.385  51.284 1.00 42.62  ? 68  ALA   A C     1 
ATOM   277  O O     . ALA   A 1 44  ? 24.151  37.518  50.813 1.00 44.65  ? 68  ALA   A O     1 
ATOM   278  C CB    . ALA   A 1 44  ? 20.941  38.192  50.947 1.00 40.01  ? 68  ALA   A CB    1 
ATOM   279  N N     . ARG   A 1 45  ? 23.721  39.682  51.245 1.00 43.20  ? 69  ARG   A N     1 
ATOM   280  C CA    . ARG   A 1 45  ? 24.997  40.101  50.669 1.00 44.25  ? 69  ARG   A CA    1 
ATOM   281  C C     . ARG   A 1 45  ? 26.163  39.506  51.452 1.00 46.33  ? 69  ARG   A C     1 
ATOM   282  O O     . ARG   A 1 45  ? 27.091  38.936  50.866 1.00 46.88  ? 69  ARG   A O     1 
ATOM   283  C CB    . ARG   A 1 45  ? 25.103  41.625  50.628 1.00 47.43  ? 69  ARG   A CB    1 
ATOM   284  C CG    . ARG   A 1 45  ? 26.390  42.091  49.963 1.00 51.07  ? 69  ARG   A CG    1 
ATOM   285  C CD    . ARG   A 1 45  ? 26.480  43.597  49.850 1.00 56.38  ? 69  ARG   A CD    1 
ATOM   286  N NE    . ARG   A 1 45  ? 25.388  44.171  49.074 1.00 60.44  ? 69  ARG   A NE    1 
ATOM   287  C CZ    . ARG   A 1 45  ? 25.436  44.406  47.770 1.00 60.82  ? 69  ARG   A CZ    1 
ATOM   288  N NH1   . ARG   A 1 45  ? 26.498  44.087  47.049 1.00 60.94  ? 69  ARG   A NH1   1 
ATOM   289  N NH2   . ARG   A 1 45  ? 24.393  44.981  47.176 1.00 59.94  ? 69  ARG   A NH2   1 
ATOM   290  N N     . LYS   A 1 46  ? 26.110  39.603  52.785 1.00 44.69  ? 70  LYS   A N     1 
ATOM   291  C CA    . LYS   A 1 46  ? 27.172  39.057  53.623 1.00 44.91  ? 70  LYS   A CA    1 
ATOM   292  C C     . LYS   A 1 46  ? 27.335  37.556  53.412 1.00 44.07  ? 70  LYS   A C     1 
ATOM   293  O O     . LYS   A 1 46  ? 28.462  37.058  53.300 1.00 46.26  ? 70  LYS   A O     1 
ATOM   294  C CB    . LYS   A 1 46  ? 26.885  39.361  55.096 1.00 46.08  ? 70  LYS   A CB    1 
ATOM   295  N N     . LEU   A 1 47  ? 26.225  36.817  53.359 1.00 40.40  ? 71  LEU   A N     1 
ATOM   296  C CA    . LEU   A 1 47  ? 26.302  35.382  53.100 1.00 41.64  ? 71  LEU   A CA    1 
ATOM   297  C C     . LEU   A 1 47  ? 26.909  35.095  51.731 1.00 47.28  ? 71  LEU   A C     1 
ATOM   298  O O     . LEU   A 1 47  ? 27.754  34.198  51.585 1.00 46.38  ? 71  LEU   A O     1 
ATOM   299  C CB    . LEU   A 1 47  ? 24.910  34.757  53.187 1.00 41.58  ? 71  LEU   A CB    1 
ATOM   300  C CG    . LEU   A 1 47  ? 24.197  34.821  54.527 1.00 38.81  ? 71  LEU   A CG    1 
ATOM   301  C CD1   . LEU   A 1 47  ? 22.757  34.350  54.351 1.00 36.19  ? 71  LEU   A CD1   1 
ATOM   302  C CD2   . LEU   A 1 47  ? 24.949  33.953  55.538 1.00 41.46  ? 71  LEU   A CD2   1 
ATOM   303  N N     . ILE   A 1 48  ? 26.473  35.837  50.710 1.00 43.14  ? 72  ILE   A N     1 
ATOM   304  C CA    . ILE   A 1 48  ? 26.958  35.611  49.355 1.00 43.56  ? 72  ILE   A CA    1 
ATOM   305  C C     . ILE   A 1 48  ? 28.424  35.998  49.235 1.00 44.99  ? 72  ILE   A C     1 
ATOM   306  O O     . ILE   A 1 48  ? 29.199  35.334  48.538 1.00 48.02  ? 72  ILE   A O     1 
ATOM   307  C CB    . ILE   A 1 48  ? 26.068  36.374  48.356 1.00 46.35  ? 72  ILE   A CB    1 
ATOM   308  C CG1   . ILE   A 1 48  ? 24.700  35.693  48.290 1.00 42.93  ? 72  ILE   A CG1   1 
ATOM   309  C CG2   . ILE   A 1 48  ? 26.718  36.442  46.978 1.00 45.25  ? 72  ILE   A CG2   1 
ATOM   310  C CD1   . ILE   A 1 48  ? 23.646  36.503  47.632 1.00 45.35  ? 72  ILE   A CD1   1 
ATOM   311  N N     . GLU   A 1 49  ? 28.833  37.069  49.911 1.00 45.47  ? 73  GLU   A N     1 
ATOM   312  C CA    . GLU   A 1 49  ? 30.242  37.447  49.873 1.00 49.27  ? 73  GLU   A CA    1 
ATOM   313  C C     . GLU   A 1 49  ? 31.110  36.399  50.563 1.00 48.67  ? 73  GLU   A C     1 
ATOM   314  O O     . GLU   A 1 49  ? 32.226  36.115  50.111 1.00 50.36  ? 73  GLU   A O     1 
ATOM   315  C CB    . GLU   A 1 49  ? 30.438  38.828  50.499 1.00 48.57  ? 73  GLU   A CB    1 
ATOM   316  C CG    . GLU   A 1 49  ? 30.134  39.960  49.513 1.00 56.81  ? 73  GLU   A CG    1 
ATOM   317  C CD    . GLU   A 1 49  ? 30.094  41.337  50.155 1.00 60.68  ? 73  GLU   A CD    1 
ATOM   318  O OE1   . GLU   A 1 49  ? 30.069  41.418  51.404 1.00 62.59  ? 73  GLU   A OE1   1 
ATOM   319  O OE2   . GLU   A 1 49  ? 30.078  42.340  49.406 1.00 62.48  ? 73  GLU   A OE2   1 
ATOM   320  N N     . ALA   A 1 50  ? 30.611  35.801  51.645 1.00 49.51  ? 74  ALA   A N     1 
ATOM   321  C CA    . ALA   A 1 50  ? 31.314  34.668  52.235 1.00 48.52  ? 74  ALA   A CA    1 
ATOM   322  C C     . ALA   A 1 50  ? 31.302  33.469  51.294 1.00 49.96  ? 74  ALA   A C     1 
ATOM   323  O O     . ALA   A 1 50  ? 32.311  32.769  51.160 1.00 51.19  ? 74  ALA   A O     1 
ATOM   324  C CB    . ALA   A 1 50  ? 30.690  34.304  53.582 1.00 48.22  ? 74  ALA   A CB    1 
ATOM   325  N N     . LEU   A 1 51  ? 30.174  33.227  50.620 1.00 48.08  ? 75  LEU   A N     1 
ATOM   326  C CA    . LEU   A 1 51  ? 30.078  32.082  49.721 1.00 46.13  ? 75  LEU   A CA    1 
ATOM   327  C C     . LEU   A 1 51  ? 31.059  32.209  48.565 1.00 52.86  ? 75  LEU   A C     1 
ATOM   328  O O     . LEU   A 1 51  ? 31.789  31.265  48.248 1.00 58.31  ? 75  LEU   A O     1 
ATOM   329  C CB    . LEU   A 1 51  ? 28.650  31.938  49.206 1.00 46.10  ? 75  LEU   A CB    1 
ATOM   330  C CG    . LEU   A 1 51  ? 27.683  31.157  50.091 1.00 45.76  ? 75  LEU   A CG    1 
ATOM   331  C CD1   . LEU   A 1 51  ? 26.281  31.167  49.498 1.00 45.48  ? 75  LEU   A CD1   1 
ATOM   332  C CD2   . LEU   A 1 51  ? 28.163  29.731  50.280 1.00 43.30  ? 75  LEU   A CD2   1 
ATOM   333  N N     . ARG   A 1 52  ? 31.095  33.374  47.922 1.00 51.99  ? 76  ARG   A N     1 
ATOM   334  C CA    . ARG   A 1 52  ? 32.047  33.572  46.839 1.00 54.40  ? 76  ARG   A CA    1 
ATOM   335  C C     . ARG   A 1 52  ? 33.472  33.752  47.337 1.00 57.68  ? 76  ARG   A C     1 
ATOM   336  O O     . ARG   A 1 52  ? 34.398  33.742  46.519 1.00 65.37  ? 76  ARG   A O     1 
ATOM   337  C CB    . ARG   A 1 52  ? 31.632  34.777  45.994 1.00 52.52  ? 76  ARG   A CB    1 
ATOM   338  C CG    . ARG   A 1 52  ? 30.346  34.531  45.247 1.00 50.43  ? 76  ARG   A CG    1 
ATOM   339  C CD    . ARG   A 1 52  ? 30.059  35.619  44.233 1.00 52.20  ? 76  ARG   A CD    1 
ATOM   340  N NE    . ARG   A 1 52  ? 29.135  35.135  43.217 1.00 48.97  ? 76  ARG   A NE    1 
ATOM   341  C CZ    . ARG   A 1 52  ? 28.650  35.878  42.233 1.00 50.90  ? 76  ARG   A CZ    1 
ATOM   342  N NH1   . ARG   A 1 52  ? 28.938  37.167  42.134 1.00 51.66  ? 76  ARG   A NH1   1 
ATOM   343  N NH2   . ARG   A 1 52  ? 27.857  35.314  41.325 1.00 48.74  ? 76  ARG   A NH2   1 
ATOM   344  N N     . GLY   A 1 53  ? 33.669  33.908  48.645 1.00 56.63  ? 77  GLY   A N     1 
ATOM   345  C CA    . GLY   A 1 53  ? 35.014  34.095  49.163 1.00 63.33  ? 77  GLY   A CA    1 
ATOM   346  C C     . GLY   A 1 53  ? 35.851  32.830  49.098 1.00 69.10  ? 77  GLY   A C     1 
ATOM   347  O O     . GLY   A 1 53  ? 37.002  32.857  48.652 1.00 73.46  ? 77  GLY   A O     1 
ATOM   348  N N     . LYS   A 1 54  ? 35.288  31.707  49.538 1.00 66.67  ? 78  LYS   A N     1 
ATOM   349  C CA    . LYS   A 1 54  ? 36.038  30.456  49.626 1.00 72.54  ? 78  LYS   A CA    1 
ATOM   350  C C     . LYS   A 1 54  ? 35.725  29.570  48.420 1.00 77.68  ? 78  LYS   A C     1 
ATOM   351  O O     . LYS   A 1 54  ? 35.161  28.479  48.535 1.00 81.13  ? 78  LYS   A O     1 
ATOM   352  C CB    . LYS   A 1 54  ? 35.731  29.750  50.943 1.00 73.85  ? 78  LYS   A CB    1 
ATOM   353  N N     . HIS   A 1 55  ? 36.112  30.071  47.248 1.00 81.34  ? 79  HIS   A N     1 
ATOM   354  C CA    . HIS   A 1 55  ? 35.981  29.344  45.984 1.00 81.35  ? 79  HIS   A CA    1 
ATOM   355  C C     . HIS   A 1 55  ? 34.575  28.779  45.772 1.00 84.40  ? 79  HIS   A C     1 
ATOM   356  O O     . HIS   A 1 55  ? 34.330  27.594  46.006 1.00 85.44  ? 79  HIS   A O     1 
ATOM   357  C CB    . HIS   A 1 55  ? 37.012  28.215  45.913 1.00 76.93  ? 79  HIS   A CB    1 
ATOM   358  N N     . GLY   A 1 66  ? 29.028  11.810  41.919 1.00 64.90  ? 192 GLY   A N     1 
ATOM   359  C CA    . GLY   A 1 66  ? 27.954  12.235  42.802 1.00 61.70  ? 192 GLY   A CA    1 
ATOM   360  C C     . GLY   A 1 66  ? 28.198  11.937  44.273 1.00 61.08  ? 192 GLY   A C     1 
ATOM   361  O O     . GLY   A 1 66  ? 27.364  12.264  45.134 1.00 55.69  ? 192 GLY   A O     1 
ATOM   362  N N     . GLU   A 1 67  ? 29.357  11.327  44.551 1.00 59.72  ? 193 GLU   A N     1 
ATOM   363  C CA    . GLU   A 1 67  ? 29.719  10.932  45.909 1.00 56.04  ? 193 GLU   A CA    1 
ATOM   364  C C     . GLU   A 1 67  ? 29.586  12.077  46.901 1.00 49.31  ? 193 GLU   A C     1 
ATOM   365  O O     . GLU   A 1 67  ? 29.372  11.843  48.096 1.00 49.40  ? 193 GLU   A O     1 
ATOM   366  C CB    . GLU   A 1 67  ? 31.151  10.396  45.926 1.00 57.83  ? 193 GLU   A CB    1 
ATOM   367  N N     . GLN   A 1 68  ? 29.707  13.321  46.435 1.00 49.31  ? 194 GLN   A N     1 
ATOM   368  C CA    . GLN   A 1 68  ? 29.617  14.447  47.353 1.00 47.57  ? 194 GLN   A CA    1 
ATOM   369  C C     . GLN   A 1 68  ? 28.227  14.583  47.968 1.00 42.66  ? 194 GLN   A C     1 
ATOM   370  O O     . GLN   A 1 68  ? 28.085  15.240  48.999 1.00 38.49  ? 194 GLN   A O     1 
ATOM   371  C CB    . GLN   A 1 68  ? 30.002  15.742  46.639 1.00 50.34  ? 194 GLN   A CB    1 
ATOM   372  C CG    . GLN   A 1 68  ? 28.991  16.202  45.609 1.00 50.25  ? 194 GLN   A CG    1 
ATOM   373  C CD    . GLN   A 1 68  ? 29.444  15.977  44.175 1.00 55.99  ? 194 GLN   A CD    1 
ATOM   374  O OE1   . GLN   A 1 68  ? 29.823  14.863  43.787 1.00 57.54  ? 194 GLN   A OE1   1 
ATOM   375  N NE2   . GLN   A 1 68  ? 29.409  17.043  43.374 1.00 55.25  ? 194 GLN   A NE2   1 
ATOM   376  N N     . PHE   A 1 69  ? 27.210  13.960  47.370 1.00 43.02  ? 195 PHE   A N     1 
ATOM   377  C CA    . PHE   A 1 69  ? 25.837  14.047  47.856 1.00 40.99  ? 195 PHE   A CA    1 
ATOM   378  C C     . PHE   A 1 69  ? 25.419  12.858  48.707 1.00 39.18  ? 195 PHE   A C     1 
ATOM   379  O O     . PHE   A 1 69  ? 24.321  12.879  49.267 1.00 40.24  ? 195 PHE   A O     1 
ATOM   380  C CB    . PHE   A 1 69  ? 24.871  14.180  46.671 1.00 40.97  ? 195 PHE   A CB    1 
ATOM   381  C CG    . PHE   A 1 69  ? 25.173  15.342  45.787 1.00 40.92  ? 195 PHE   A CG    1 
ATOM   382  C CD1   . PHE   A 1 69  ? 25.020  16.633  46.248 1.00 39.45  ? 195 PHE   A CD1   1 
ATOM   383  C CD2   . PHE   A 1 69  ? 25.610  15.143  44.481 1.00 45.83  ? 195 PHE   A CD2   1 
ATOM   384  C CE1   . PHE   A 1 69  ? 25.305  17.709  45.433 1.00 42.48  ? 195 PHE   A CE1   1 
ATOM   385  C CE2   . PHE   A 1 69  ? 25.890  16.215  43.664 1.00 45.31  ? 195 PHE   A CE2   1 
ATOM   386  C CZ    . PHE   A 1 69  ? 25.739  17.495  44.137 1.00 43.16  ? 195 PHE   A CZ    1 
ATOM   387  N N     . VAL   A 1 70  ? 26.253  11.837  48.823 1.00 41.31  ? 196 VAL   A N     1 
ATOM   388  C CA    . VAL   A 1 70  ? 25.962  10.677  49.653 1.00 43.73  ? 196 VAL   A CA    1 
ATOM   389  C C     . VAL   A 1 70  ? 26.761  10.798  50.941 1.00 42.91  ? 196 VAL   A C     1 
ATOM   390  O O     . VAL   A 1 70  ? 27.989  10.955  50.906 1.00 48.80  ? 196 VAL   A O     1 
ATOM   391  C CB    . VAL   A 1 70  ? 26.301  9.370   48.921 1.00 47.75  ? 196 VAL   A CB    1 
ATOM   392  C CG1   . VAL   A 1 70  ? 25.761  8.190   49.700 1.00 46.94  ? 196 VAL   A CG1   1 
ATOM   393  C CG2   . VAL   A 1 70  ? 25.750  9.401   47.491 1.00 51.55  ? 196 VAL   A CG2   1 
ATOM   394  N N     . THR   A 1 71  ? 26.073  10.730  52.080 1.00 43.21  ? 197 THR   A N     1 
ATOM   395  C CA    A THR   A 1 71  ? 26.761  10.815  53.361 0.48 45.05  ? 197 THR   A CA    1 
ATOM   396  C CA    B THR   A 1 71  ? 26.788  10.815  53.349 0.52 44.67  ? 197 THR   A CA    1 
ATOM   397  C C     . THR   A 1 71  ? 27.514  9.527   53.674 1.00 45.91  ? 197 THR   A C     1 
ATOM   398  O O     . THR   A 1 71  ? 28.553  9.566   54.337 1.00 49.86  ? 197 THR   A O     1 
ATOM   399  C CB    A THR   A 1 71  ? 25.750  11.139  54.462 0.48 42.40  ? 197 THR   A CB    1 
ATOM   400  C CB    B THR   A 1 71  ? 25.852  11.148  54.509 0.52 43.11  ? 197 THR   A CB    1 
ATOM   401  O OG1   A THR   A 1 71  ? 24.905  12.210  54.020 0.48 40.44  ? 197 THR   A OG1   1 
ATOM   402  O OG1   B THR   A 1 71  ? 24.912  10.083  54.704 0.52 40.68  ? 197 THR   A OG1   1 
ATOM   403  C CG2   A THR   A 1 71  ? 26.456  11.575  55.731 0.48 41.36  ? 197 THR   A CG2   1 
ATOM   404  C CG2   B THR   A 1 71  ? 25.135  12.431  54.233 0.52 40.36  ? 197 THR   A CG2   1 
ATOM   405  N N     . GLY   A 1 72  ? 27.002  8.398   53.205 1.00 45.93  ? 198 GLY   A N     1 
ATOM   406  C CA    . GLY   A 1 72  ? 27.638  7.113   53.436 1.00 46.48  ? 198 GLY   A CA    1 
ATOM   407  C C     . GLY   A 1 72  ? 26.804  6.030   52.789 1.00 45.85  ? 198 GLY   A C     1 
ATOM   408  O O     . GLY   A 1 72  ? 25.707  6.276   52.275 1.00 46.77  ? 198 GLY   A O     1 
ATOM   409  N N     . GLU   A 1 73  ? 27.338  4.813   52.818 1.00 46.54  ? 199 GLU   A N     1 
ATOM   410  C CA    . GLU   A 1 73  ? 26.597  3.702   52.237 1.00 48.20  ? 199 GLU   A CA    1 
ATOM   411  C C     . GLU   A 1 73  ? 25.662  3.042   53.237 1.00 47.65  ? 199 GLU   A C     1 
ATOM   412  O O     . GLU   A 1 73  ? 24.632  2.486   52.843 1.00 48.68  ? 199 GLU   A O     1 
ATOM   413  C CB    . GLU   A 1 73  ? 27.554  2.659   51.654 1.00 48.13  ? 199 GLU   A CB    1 
ATOM   414  C CG    . GLU   A 1 73  ? 26.836  1.584   50.851 1.00 53.63  ? 199 GLU   A CG    1 
ATOM   415  C CD    . GLU   A 1 73  ? 27.788  0.590   50.208 1.00 60.06  ? 199 GLU   A CD    1 
ATOM   416  O OE1   . GLU   A 1 73  ? 28.763  1.042   49.567 1.00 64.90  ? 199 GLU   A OE1   1 
ATOM   417  O OE2   . GLU   A 1 73  ? 27.569  -0.636  50.354 1.00 57.50  ? 199 GLU   A OE2   1 
ATOM   418  N N     . THR   A 1 74  ? 25.991  3.101   54.520 1.00 48.11  ? 200 THR   A N     1 
ATOM   419  C CA    . THR   A 1 74  ? 25.194  2.502   55.572 1.00 46.95  ? 200 THR   A CA    1 
ATOM   420  C C     . THR   A 1 74  ? 24.860  3.562   56.605 1.00 41.82  ? 200 THR   A C     1 
ATOM   421  O O     . THR   A 1 74  ? 25.561  4.566   56.736 1.00 43.13  ? 200 THR   A O     1 
ATOM   422  C CB    . THR   A 1 74  ? 25.946  1.396   56.274 1.00 44.75  ? 200 THR   A CB    1 
ATOM   423  O OG1   . THR   A 1 74  ? 27.032  1.999   56.987 1.00 47.63  ? 200 THR   A OG1   1 
ATOM   424  C CG2   . THR   A 1 74  ? 26.493  0.381   55.260 1.00 49.94  ? 200 THR   A CG2   1 
ATOM   425  N N     . ILE   A 1 75  ? 23.779  3.325   57.345 1.00 41.16  ? 201 ILE   A N     1 
ATOM   426  C CA    . ILE   A 1 75  ? 23.424  4.255   58.411 1.00 42.82  ? 201 ILE   A CA    1 
ATOM   427  C C     . ILE   A 1 75  ? 24.536  4.312   59.453 1.00 43.94  ? 201 ILE   A C     1 
ATOM   428  O O     . ILE   A 1 75  ? 24.806  5.375   60.021 1.00 45.65  ? 201 ILE   A O     1 
ATOM   429  C CB    . ILE   A 1 75  ? 22.067  3.873   59.038 1.00 39.53  ? 201 ILE   A CB    1 
ATOM   430  C CG1   . ILE   A 1 75  ? 21.578  4.986   59.969 1.00 39.36  ? 201 ILE   A CG1   1 
ATOM   431  C CG2   . ILE   A 1 75  ? 22.162  2.565   59.782 1.00 45.32  ? 201 ILE   A CG2   1 
ATOM   432  C CD1   . ILE   A 1 75  ? 21.236  6.266   59.220 1.00 39.39  ? 201 ILE   A CD1   1 
ATOM   433  N N     . ARG   A 1 76  ? 25.224  3.190   59.698 1.00 44.54  ? 202 ARG   A N     1 
ATOM   434  C CA    . ARG   A 1 76  ? 26.334  3.212   60.648 1.00 44.06  ? 202 ARG   A CA    1 
ATOM   435  C C     . ARG   A 1 76  ? 27.452  4.131   60.162 1.00 48.29  ? 202 ARG   A C     1 
ATOM   436  O O     . ARG   A 1 76  ? 27.984  4.935   60.935 1.00 49.80  ? 202 ARG   A O     1 
ATOM   437  C CB    . ARG   A 1 76  ? 26.851  1.791   60.894 1.00 47.08  ? 202 ARG   A CB    1 
ATOM   438  N N     . GLU   A 1 77  ? 27.794  4.055   58.872 1.00 49.25  ? 203 GLU   A N     1 
ATOM   439  C CA    . GLU   A 1 77  ? 28.771  4.982   58.307 1.00 47.00  ? 203 GLU   A CA    1 
ATOM   440  C C     . GLU   A 1 77  ? 28.272  6.424   58.361 1.00 48.64  ? 203 GLU   A C     1 
ATOM   441  O O     . GLU   A 1 77  ? 29.036  7.340   58.683 1.00 50.59  ? 203 GLU   A O     1 
ATOM   442  C CB    . GLU   A 1 77  ? 29.097  4.581   56.866 1.00 50.07  ? 203 GLU   A CB    1 
ATOM   443  N N     . ALA   A 1 78  ? 27.000  6.654   58.023 1.00 46.26  ? 204 ALA   A N     1 
ATOM   444  C CA    . ALA   A 1 78  ? 26.480  8.021   58.013 1.00 45.95  ? 204 ALA   A CA    1 
ATOM   445  C C     . ALA   A 1 78  ? 26.476  8.621   59.414 1.00 45.21  ? 204 ALA   A C     1 
ATOM   446  O O     . ALA   A 1 78  ? 26.812  9.795   59.593 1.00 42.89  ? 204 ALA   A O     1 
ATOM   447  C CB    . ALA   A 1 78  ? 25.073  8.050   57.418 1.00 43.83  ? 204 ALA   A CB    1 
ATOM   448  N N     . LEU   A 1 79  ? 26.119  7.823   60.423 1.00 45.61  ? 205 LEU   A N     1 
ATOM   449  C CA    . LEU   A 1 79  ? 26.098  8.323   61.797 1.00 48.28  ? 205 LEU   A CA    1 
ATOM   450  C C     . LEU   A 1 79  ? 27.494  8.726   62.269 1.00 49.41  ? 205 LEU   A C     1 
ATOM   451  O O     . LEU   A 1 79  ? 27.657  9.757   62.936 1.00 49.47  ? 205 LEU   A O     1 
ATOM   452  C CB    . LEU   A 1 79  ? 25.491  7.270   62.729 1.00 46.84  ? 205 LEU   A CB    1 
ATOM   453  C CG    . LEU   A 1 79  ? 23.974  7.076   62.591 1.00 44.92  ? 205 LEU   A CG    1 
ATOM   454  C CD1   . LEU   A 1 79  ? 23.506  5.833   63.331 1.00 43.57  ? 205 LEU   A CD1   1 
ATOM   455  C CD2   . LEU   A 1 79  ? 23.200  8.320   63.070 1.00 40.21  ? 205 LEU   A CD2   1 
ATOM   456  N N     . LYS   A 1 80  ? 28.516  7.939   61.927 1.00 50.88  ? 206 LYS   A N     1 
ATOM   457  C CA    . LYS   A 1 80  ? 29.877  8.280   62.344 1.00 52.18  ? 206 LYS   A CA    1 
ATOM   458  C C     . LYS   A 1 80  ? 30.347  9.579   61.694 1.00 54.43  ? 206 LYS   A C     1 
ATOM   459  O O     . LYS   A 1 80  ? 31.034  10.390  62.327 1.00 54.25  ? 206 LYS   A O     1 
ATOM   460  C CB    . LYS   A 1 80  ? 30.836  7.135   62.012 1.00 57.33  ? 206 LYS   A CB    1 
ATOM   461  N N     . ARG   A 1 81  ? 29.984  9.800   60.434 1.00 52.49  ? 207 ARG   A N     1 
ATOM   462  C CA    . ARG   A 1 81  ? 30.447  10.981  59.723 1.00 52.56  ? 207 ARG   A CA    1 
ATOM   463  C C     . ARG   A 1 81  ? 29.651  12.228  60.076 1.00 48.77  ? 207 ARG   A C     1 
ATOM   464  O O     . ARG   A 1 81  ? 30.001  13.317  59.613 1.00 50.49  ? 207 ARG   A O     1 
ATOM   465  C CB    . ARG   A 1 81  ? 30.403  10.724  58.216 1.00 54.53  ? 207 ARG   A CB    1 
ATOM   466  C CG    . ARG   A 1 81  ? 31.181  9.480   57.814 1.00 59.38  ? 207 ARG   A CG    1 
ATOM   467  C CD    . ARG   A 1 81  ? 32.195  9.769   56.729 1.00 64.13  ? 207 ARG   A CD    1 
ATOM   468  N NE    . ARG   A 1 81  ? 31.609  9.635   55.403 1.00 66.79  ? 207 ARG   A NE    1 
ATOM   469  C CZ    . ARG   A 1 81  ? 31.838  8.619   54.581 1.00 69.03  ? 207 ARG   A CZ    1 
ATOM   470  N NH1   . ARG   A 1 81  ? 32.652  7.626   54.915 1.00 69.64  ? 207 ARG   A NH1   1 
ATOM   471  N NH2   . ARG   A 1 81  ? 31.243  8.604   53.391 1.00 66.08  ? 207 ARG   A NH2   1 
ATOM   472  N N     . SER   A 1 82  ? 28.622  12.100  60.911 1.00 52.45  ? 208 SER   A N     1 
ATOM   473  C CA    . SER   A 1 82  ? 27.762  13.217  61.275 1.00 45.77  ? 208 SER   A CA    1 
ATOM   474  C C     . SER   A 1 82  ? 28.154  13.896  62.582 1.00 47.04  ? 208 SER   A C     1 
ATOM   475  O O     . SER   A 1 82  ? 27.735  15.034  62.812 1.00 45.02  ? 208 SER   A O     1 
ATOM   476  C CB    . SER   A 1 82  ? 26.311  12.737  61.382 1.00 44.95  ? 208 SER   A CB    1 
ATOM   477  O OG    . SER   A 1 82  ? 25.894  12.106  60.174 1.00 43.47  ? 208 SER   A OG    1 
ATOM   478  N N     . LYS   A 1 83  ? 28.951  13.238  63.432 1.00 49.10  ? 209 LYS   A N     1 
ATOM   479  C CA    . LYS   A 1 83  ? 29.304  13.821  64.727 1.00 46.17  ? 209 LYS   A CA    1 
ATOM   480  C C     . LYS   A 1 83  ? 29.998  15.172  64.559 1.00 46.98  ? 209 LYS   A C     1 
ATOM   481  O O     . LYS   A 1 83  ? 29.726  16.113  65.314 1.00 50.41  ? 209 LYS   A O     1 
ATOM   482  C CB    . LYS   A 1 83  ? 30.190  12.850  65.517 1.00 50.32  ? 209 LYS   A CB    1 
ATOM   483  N N     . GLU   A 1 84  ? 30.864  15.296  63.550 1.00 47.31  ? 210 GLU   A N     1 
ATOM   484  C CA    . GLU   A 1 84  ? 31.620  16.530  63.334 1.00 48.55  ? 210 GLU   A CA    1 
ATOM   485  C C     . GLU   A 1 84  ? 30.704  17.738  63.190 1.00 48.48  ? 210 GLU   A C     1 
ATOM   486  O O     . GLU   A 1 84  ? 30.876  18.754  63.874 1.00 44.67  ? 210 GLU   A O     1 
ATOM   487  C CB    . GLU   A 1 84  ? 32.504  16.393  62.091 1.00 49.44  ? 210 GLU   A CB    1 
ATOM   488  N N     . LEU   A 1 85  ? 29.734  17.657  62.277 1.00 44.74  ? 211 LEU   A N     1 
ATOM   489  C CA    . LEU   A 1 85  ? 28.855  18.796  62.080 1.00 42.72  ? 211 LEU   A CA    1 
ATOM   490  C C     . LEU   A 1 85  ? 27.809  18.897  63.180 1.00 42.22  ? 211 LEU   A C     1 
ATOM   491  O O     . LEU   A 1 85  ? 27.319  19.996  63.457 1.00 39.84  ? 211 LEU   A O     1 
ATOM   492  C CB    . LEU   A 1 85  ? 28.193  18.725  60.705 1.00 43.46  ? 211 LEU   A CB    1 
ATOM   493  C CG    . LEU   A 1 85  ? 29.186  18.933  59.560 1.00 42.97  ? 211 LEU   A CG    1 
ATOM   494  C CD1   . LEU   A 1 85  ? 28.499  18.813  58.221 1.00 44.79  ? 211 LEU   A CD1   1 
ATOM   495  C CD2   . LEU   A 1 85  ? 29.889  20.284  59.699 1.00 45.50  ? 211 LEU   A CD2   1 
ATOM   496  N N     . GLU   A 1 86  ? 27.459  17.785  63.830 1.00 37.65  ? 212 GLU   A N     1 
ATOM   497  C CA    . GLU   A 1 86  ? 26.426  17.873  64.858 1.00 43.49  ? 212 GLU   A CA    1 
ATOM   498  C C     . GLU   A 1 86  ? 26.865  18.771  66.006 1.00 42.10  ? 212 GLU   A C     1 
ATOM   499  O O     . GLU   A 1 86  ? 26.055  19.530  66.547 1.00 47.46  ? 212 GLU   A O     1 
ATOM   500  C CB    . GLU   A 1 86  ? 26.033  16.482  65.356 1.00 45.50  ? 212 GLU   A CB    1 
ATOM   501  C CG    . GLU   A 1 86  ? 25.140  15.761  64.358 1.00 46.48  ? 212 GLU   A CG    1 
ATOM   502  C CD    . GLU   A 1 86  ? 24.667  14.413  64.841 1.00 51.05  ? 212 GLU   A CD    1 
ATOM   503  O OE1   . GLU   A 1 86  ? 25.403  13.762  65.615 1.00 50.50  ? 212 GLU   A OE1   1 
ATOM   504  O OE2   . GLU   A 1 86  ? 23.549  14.010  64.438 1.00 50.10  ? 212 GLU   A OE2   1 
ATOM   505  N N     . GLU   A 1 87  ? 28.145  18.724  66.371 1.00 47.60  ? 213 GLU   A N     1 
ATOM   506  C CA    . GLU   A 1 87  ? 28.633  19.568  67.456 1.00 48.22  ? 213 GLU   A CA    1 
ATOM   507  C C     . GLU   A 1 87  ? 28.914  20.996  67.010 1.00 47.84  ? 213 GLU   A C     1 
ATOM   508  O O     . GLU   A 1 87  ? 29.286  21.827  67.845 1.00 54.16  ? 213 GLU   A O     1 
ATOM   509  C CB    . GLU   A 1 87  ? 29.892  18.963  68.085 1.00 50.74  ? 213 GLU   A CB    1 
ATOM   510  C CG    . GLU   A 1 87  ? 29.731  17.525  68.590 1.00 55.75  ? 213 GLU   A CG    1 
ATOM   511  C CD    . GLU   A 1 87  ? 28.842  17.388  69.833 1.00 61.41  ? 213 GLU   A CD    1 
ATOM   512  O OE1   . GLU   A 1 87  ? 28.381  18.413  70.392 1.00 61.85  ? 213 GLU   A OE1   1 
ATOM   513  O OE2   . GLU   A 1 87  ? 28.605  16.234  70.252 1.00 60.47  ? 213 GLU   A OE2   1 
ATOM   514  N N     . LYS   A 1 88  ? 28.757  21.304  65.721 1.00 46.46  ? 214 LYS   A N     1 
ATOM   515  C CA    . LYS   A 1 88  ? 28.800  22.690  65.273 1.00 47.35  ? 214 LYS   A CA    1 
ATOM   516  C C     . LYS   A 1 88  ? 27.425  23.330  65.246 1.00 46.16  ? 214 LYS   A C     1 
ATOM   517  O O     . LYS   A 1 88  ? 27.325  24.528  64.976 1.00 48.88  ? 214 LYS   A O     1 
ATOM   518  C CB    . LYS   A 1 88  ? 29.430  22.800  63.882 1.00 44.69  ? 214 LYS   A CB    1 
ATOM   519  C CG    . LYS   A 1 88  ? 30.960  22.821  63.887 1.00 52.68  ? 214 LYS   A CG    1 
ATOM   520  C CD    . LYS   A 1 88  ? 31.508  23.033  62.477 1.00 58.57  ? 214 LYS   A CD    1 
ATOM   521  C CE    . LYS   A 1 88  ? 33.021  23.161  62.485 1.00 59.88  ? 214 LYS   A CE    1 
ATOM   522  N NZ    . LYS   A 1 88  ? 33.578  23.288  61.107 1.00 60.02  ? 214 LYS   A NZ    1 
ATOM   523  N N     . GLY   A 1 89  ? 26.374  22.567  65.521 1.00 45.65  ? 215 GLY   A N     1 
ATOM   524  C CA    . GLY   A 1 89  ? 25.020  23.086  65.530 1.00 46.87  ? 215 GLY   A CA    1 
ATOM   525  C C     . GLY   A 1 89  ? 24.126  22.492  64.471 1.00 42.27  ? 215 GLY   A C     1 
ATOM   526  O O     . GLY   A 1 89  ? 22.933  22.824  64.433 1.00 44.41  ? 215 GLY   A O     1 
ATOM   527  N N     . PHE   A 1 90  ? 24.646  21.630  63.608 1.00 37.33  ? 216 PHE   A N     1 
ATOM   528  C CA    . PHE   A 1 90  ? 23.824  20.983  62.603 1.00 37.22  ? 216 PHE   A CA    1 
ATOM   529  C C     . PHE   A 1 90  ? 23.107  19.786  63.209 1.00 38.79  ? 216 PHE   A C     1 
ATOM   530  O O     . PHE   A 1 90  ? 23.590  19.162  64.150 1.00 39.34  ? 216 PHE   A O     1 
ATOM   531  C CB    . PHE   A 1 90  ? 24.679  20.503  61.438 1.00 35.97  ? 216 PHE   A CB    1 
ATOM   532  C CG    . PHE   A 1 90  ? 25.215  21.601  60.569 1.00 39.39  ? 216 PHE   A CG    1 
ATOM   533  C CD1   . PHE   A 1 90  ? 24.470  22.087  59.500 1.00 33.08  ? 216 PHE   A CD1   1 
ATOM   534  C CD2   . PHE   A 1 90  ? 26.472  22.129  60.801 1.00 37.67  ? 216 PHE   A CD2   1 
ATOM   535  C CE1   . PHE   A 1 90  ? 24.978  23.067  58.668 1.00 34.19  ? 216 PHE   A CE1   1 
ATOM   536  C CE2   . PHE   A 1 90  ? 26.982  23.119  59.987 1.00 37.51  ? 216 PHE   A CE2   1 
ATOM   537  C CZ    . PHE   A 1 90  ? 26.236  23.591  58.921 1.00 35.19  ? 216 PHE   A CZ    1 
ATOM   538  N N     . SER   A 1 91  ? 21.949  19.466  62.658 1.00 34.74  ? 217 SER   A N     1 
ATOM   539  C CA    . SER   A 1 91  ? 21.315  18.185  62.913 1.00 32.40  ? 217 SER   A CA    1 
ATOM   540  C C     . SER   A 1 91  ? 21.184  17.452  61.582 1.00 30.61  ? 217 SER   A C     1 
ATOM   541  O O     . SER   A 1 91  ? 21.491  17.995  60.517 1.00 31.17  ? 217 SER   A O     1 
ATOM   542  C CB    . SER   A 1 91  ? 19.957  18.371  63.587 1.00 33.14  ? 217 SER   A CB    1 
ATOM   543  O OG    . SER   A 1 91  ? 19.110  19.084  62.726 1.00 35.18  ? 217 SER   A OG    1 
ATOM   544  N N     . TYR   A 1 92  ? 20.683  16.225  61.632 1.00 30.90  ? 218 TYR   A N     1 
ATOM   545  C CA    . TYR   A 1 92  ? 20.554  15.442  60.416 1.00 28.80  ? 218 TYR   A CA    1 
ATOM   546  C C     . TYR   A 1 92  ? 19.162  14.861  60.268 1.00 28.48  ? 218 TYR   A C     1 
ATOM   547  O O     . TYR   A 1 92  ? 18.450  14.599  61.243 1.00 30.56  ? 218 TYR   A O     1 
ATOM   548  C CB    . TYR   A 1 92  ? 21.563  14.311  60.366 1.00 32.41  ? 218 TYR   A CB    1 
ATOM   549  C CG    . TYR   A 1 92  ? 22.953  14.785  60.037 1.00 34.67  ? 218 TYR   A CG    1 
ATOM   550  C CD1   . TYR   A 1 92  ? 23.777  15.313  61.020 1.00 35.64  ? 218 TYR   A CD1   1 
ATOM   551  C CD2   . TYR   A 1 92  ? 23.445  14.690  58.743 1.00 30.99  ? 218 TYR   A CD2   1 
ATOM   552  C CE1   . TYR   A 1 92  ? 25.036  15.761  60.720 1.00 34.07  ? 218 TYR   A CE1   1 
ATOM   553  C CE2   . TYR   A 1 92  ? 24.704  15.128  58.427 1.00 31.40  ? 218 TYR   A CE2   1 
ATOM   554  C CZ    . TYR   A 1 92  ? 25.504  15.656  59.417 1.00 37.34  ? 218 TYR   A CZ    1 
ATOM   555  O OH    . TYR   A 1 92  ? 26.774  16.082  59.099 1.00 40.82  ? 218 TYR   A OH    1 
ATOM   556  N N     . SER   A 1 93  ? 18.796  14.647  59.019 1.00 27.11  ? 219 SER   A N     1 
ATOM   557  C CA    . SER   A 1 93  ? 17.662  13.805  58.679 1.00 30.42  ? 219 SER   A CA    1 
ATOM   558  C C     . SER   A 1 93  ? 18.178  12.774  57.687 1.00 31.31  ? 219 SER   A C     1 
ATOM   559  O O     . SER   A 1 93  ? 18.567  13.117  56.566 1.00 30.22  ? 219 SER   A O     1 
ATOM   560  C CB    . SER   A 1 93  ? 16.515  14.622  58.101 1.00 30.29  ? 219 SER   A CB    1 
ATOM   561  O OG    . SER   A 1 93  ? 15.435  13.767  57.811 1.00 31.65  ? 219 SER   A OG    1 
ATOM   562  N N     . TYR   A 1 94  ? 18.200  11.519  58.092 1.00 28.04  ? 220 TYR   A N     1 
ATOM   563  C CA    . TYR   A 1 94  ? 18.771  10.478  57.258 1.00 32.32  ? 220 TYR   A CA    1 
ATOM   564  C C     . TYR   A 1 94  ? 17.716  9.889   56.341 1.00 33.78  ? 220 TYR   A C     1 
ATOM   565  O O     . TYR   A 1 94  ? 16.567  9.698   56.736 1.00 33.13  ? 220 TYR   A O     1 
ATOM   566  C CB    . TYR   A 1 94  ? 19.372  9.381   58.129 1.00 33.75  ? 220 TYR   A CB    1 
ATOM   567  C CG    . TYR   A 1 94  ? 20.498  9.908   58.961 1.00 33.35  ? 220 TYR   A CG    1 
ATOM   568  C CD1   . TYR   A 1 94  ? 21.778  9.993   58.436 1.00 33.90  ? 220 TYR   A CD1   1 
ATOM   569  C CD2   . TYR   A 1 94  ? 20.278  10.360  60.257 1.00 31.43  ? 220 TYR   A CD2   1 
ATOM   570  C CE1   . TYR   A 1 94  ? 22.810  10.500  59.175 1.00 33.97  ? 220 TYR   A CE1   1 
ATOM   571  C CE2   . TYR   A 1 94  ? 21.311  10.865  61.013 1.00 33.80  ? 220 TYR   A CE2   1 
ATOM   572  C CZ    . TYR   A 1 94  ? 22.572  10.943  60.462 1.00 38.45  ? 220 TYR   A CZ    1 
ATOM   573  O OH    . TYR   A 1 94  ? 23.616  11.438  61.213 1.00 36.37  ? 220 TYR   A OH    1 
ATOM   574  N N     . ASP   A 1 95  ? 18.121  9.565   55.121 1.00 34.09  ? 221 ASP   A N     1 
ATOM   575  C CA    . ASP   A 1 95  ? 17.217  8.921   54.185 1.00 33.66  ? 221 ASP   A CA    1 
ATOM   576  C C     . ASP   A 1 95  ? 17.918  7.687   53.638 1.00 35.09  ? 221 ASP   A C     1 
ATOM   577  O O     . ASP   A 1 95  ? 18.943  7.800   52.963 1.00 37.59  ? 221 ASP   A O     1 
ATOM   578  C CB    . ASP   A 1 95  ? 16.814  9.889   53.081 1.00 33.44  ? 221 ASP   A CB    1 
ATOM   579  C CG    . ASP   A 1 95  ? 15.854  9.276   52.091 1.00 42.12  ? 221 ASP   A CG    1 
ATOM   580  O OD1   . ASP   A 1 95  ? 15.404  8.134   52.302 1.00 42.05  ? 221 ASP   A OD1   1 
ATOM   581  O OD2   . ASP   A 1 95  ? 15.564  9.946   51.081 1.00 39.52  ? 221 ASP   A OD2   1 
ATOM   582  N N     . MET   A 1 96  ? 17.396  6.513   53.977 1.00 41.23  ? 222 MET   A N     1 
ATOM   583  C CA    . MET   A 1 96  ? 17.827  5.288   53.328 1.00 42.30  ? 222 MET   A CA    1 
ATOM   584  C C     . MET   A 1 96  ? 17.321  5.338   51.908 1.00 44.44  ? 222 MET   A C     1 
ATOM   585  O O     . MET   A 1 96  ? 16.212  4.873   51.634 1.00 51.00  ? 222 MET   A O     1 
ATOM   586  C CB    . MET   A 1 96  ? 17.278  4.062   54.038 1.00 47.63  ? 222 MET   A CB    1 
ATOM   587  C CG    . MET   A 1 96  ? 17.748  3.942   55.437 1.00 45.77  ? 222 MET   A CG    1 
ATOM   588  S SD    . MET   A 1 96  ? 19.525  4.130   55.587 1.00 55.40  ? 222 MET   A SD    1 
ATOM   589  C CE    . MET   A 1 96  ? 20.096  2.832   54.491 1.00 42.68  ? 222 MET   A CE    1 
ATOM   590  N N     . LEU   A 1 97  ? 18.115  5.922   51.018 1.00 42.66  ? 223 LEU   A N     1 
ATOM   591  C CA    . LEU   A 1 97  ? 17.652  6.305   49.688 1.00 47.22  ? 223 LEU   A CA    1 
ATOM   592  C C     . LEU   A 1 97  ? 17.033  5.131   48.938 1.00 50.07  ? 223 LEU   A C     1 
ATOM   593  O O     . LEU   A 1 97  ? 17.700  4.132   48.655 1.00 52.93  ? 223 LEU   A O     1 
ATOM   594  C CB    . LEU   A 1 97  ? 18.807  6.902   48.877 1.00 52.47  ? 223 LEU   A CB    1 
ATOM   595  N N     . GLY   A 1 98  ? 15.740  5.237   48.674 1.00 52.04  ? 224 GLY   A N     1 
ATOM   596  C CA    . GLY   A 1 98  ? 15.065  4.363   47.731 1.00 48.13  ? 224 GLY   A CA    1 
ATOM   597  C C     . GLY   A 1 98  ? 13.848  5.088   47.211 1.00 46.90  ? 224 GLY   A C     1 
ATOM   598  O O     . GLY   A 1 98  ? 13.292  5.966   47.883 1.00 46.30  ? 224 GLY   A O     1 
ATOM   599  N N     . GLU   A 1 99  ? 13.437  4.735   46.001 1.00 48.31  ? 225 GLU   A N     1 
ATOM   600  C CA    . GLU   A 1 99  ? 12.266  5.382   45.435 1.00 44.76  ? 225 GLU   A CA    1 
ATOM   601  C C     . GLU   A 1 99  ? 11.815  4.583   44.229 1.00 46.28  ? 225 GLU   A C     1 
ATOM   602  O O     . GLU   A 1 99  ? 12.569  3.774   43.682 1.00 46.99  ? 225 GLU   A O     1 
ATOM   603  C CB    . GLU   A 1 99  ? 12.548  6.844   45.050 1.00 43.86  ? 225 GLU   A CB    1 
ATOM   604  C CG    . GLU   A 1 99  ? 13.661  7.042   44.035 1.00 45.23  ? 225 GLU   A CG    1 
ATOM   605  C CD    . GLU   A 1 99  ? 13.873  8.512   43.706 1.00 45.63  ? 225 GLU   A CD    1 
ATOM   606  O OE1   . GLU   A 1 99  ? 14.624  9.182   44.439 1.00 46.66  ? 225 GLU   A OE1   1 
ATOM   607  O OE2   . GLU   A 1 99  ? 13.272  9.009   42.725 1.00 45.93  ? 225 GLU   A OE2   1 
ATOM   608  N N     . ALA   A 1 100 ? 10.568  4.818   43.832 1.00 48.46  ? 226 ALA   A N     1 
ATOM   609  C CA    . ALA   A 1 100 ? 9.995   4.208   42.640 1.00 43.92  ? 226 ALA   A CA    1 
ATOM   610  C C     . ALA   A 1 100 ? 10.190  2.698   42.658 1.00 50.98  ? 226 ALA   A C     1 
ATOM   611  O O     . ALA   A 1 100 ? 10.691  2.090   41.709 1.00 51.92  ? 226 ALA   A O     1 
ATOM   612  C CB    . ALA   A 1 100 ? 10.592  4.828   41.373 1.00 51.55  ? 226 ALA   A CB    1 
ATOM   613  N N     . ALA   A 1 101 ? 9.816   2.091   43.779 1.00 49.73  ? 227 ALA   A N     1 
ATOM   614  C CA    . ALA   A 1 101 ? 9.827   0.643   43.865 1.00 52.69  ? 227 ALA   A CA    1 
ATOM   615  C C     . ALA   A 1 101 ? 8.922   0.079   42.785 1.00 57.80  ? 227 ALA   A C     1 
ATOM   616  O O     . ALA   A 1 101 ? 7.779   0.516   42.625 1.00 58.31  ? 227 ALA   A O     1 
ATOM   617  C CB    . ALA   A 1 101 ? 9.365   0.181   45.246 1.00 53.88  ? 227 ALA   A CB    1 
ATOM   618  N N     . THR   A 1 102 ? 9.447   -0.871  42.021 1.00 58.39  ? 228 THR   A N     1 
ATOM   619  C CA    . THR   A 1 102 ? 8.684   -1.462  40.933 1.00 59.92  ? 228 THR   A CA    1 
ATOM   620  C C     . THR   A 1 102 ? 8.156   -2.847  41.270 1.00 61.42  ? 228 THR   A C     1 
ATOM   621  O O     . THR   A 1 102 ? 7.254   -3.335  40.579 1.00 65.78  ? 228 THR   A O     1 
ATOM   622  C CB    . THR   A 1 102 ? 9.542   -1.538  39.664 1.00 62.57  ? 228 THR   A CB    1 
ATOM   623  O OG1   . THR   A 1 102 ? 10.657  -2.409  39.897 1.00 65.45  ? 228 THR   A OG1   1 
ATOM   624  C CG2   . THR   A 1 102 ? 10.056  -0.143  39.292 1.00 56.85  ? 228 THR   A CG2   1 
ATOM   625  N N     . THR   A 1 103 ? 8.691   -3.481  42.308 1.00 61.12  ? 229 THR   A N     1 
ATOM   626  C CA    . THR   A 1 103 ? 8.300   -4.818  42.715 1.00 64.55  ? 229 THR   A CA    1 
ATOM   627  C C     . THR   A 1 103 ? 7.910   -4.816  44.185 1.00 65.48  ? 229 THR   A C     1 
ATOM   628  O O     . THR   A 1 103 ? 8.314   -3.942  44.957 1.00 61.83  ? 229 THR   A O     1 
ATOM   629  C CB    . THR   A 1 103 ? 9.432   -5.827  42.490 1.00 68.84  ? 229 THR   A CB    1 
ATOM   630  N N     . ALA   A 1 104 ? 7.104   -5.808  44.565 1.00 64.90  ? 230 ALA   A N     1 
ATOM   631  C CA    . ALA   A 1 104 ? 6.772   -5.976  45.975 1.00 65.49  ? 230 ALA   A CA    1 
ATOM   632  C C     . ALA   A 1 104 ? 8.022   -6.274  46.792 1.00 66.37  ? 230 ALA   A C     1 
ATOM   633  O O     . ALA   A 1 104 ? 8.164   -5.793  47.923 1.00 63.39  ? 230 ALA   A O     1 
ATOM   634  C CB    . ALA   A 1 104 ? 5.738   -7.087  46.144 1.00 67.93  ? 230 ALA   A CB    1 
ATOM   635  N N     . ALA   A 1 105 ? 8.943   -7.063  46.229 1.00 66.17  ? 231 ALA   A N     1 
ATOM   636  C CA    . ALA   A 1 105 ? 10.192  -7.357  46.922 1.00 64.99  ? 231 ALA   A CA    1 
ATOM   637  C C     . ALA   A 1 105 ? 11.045  -6.109  47.100 1.00 62.88  ? 231 ALA   A C     1 
ATOM   638  O O     . ALA   A 1 105 ? 11.724  -5.967  48.124 1.00 61.14  ? 231 ALA   A O     1 
ATOM   639  C CB    . ALA   A 1 105 ? 10.970  -8.432  46.165 1.00 69.42  ? 231 ALA   A CB    1 
ATOM   640  N N     . ASP   A 1 106 ? 11.026  -5.195  46.125 1.00 62.03  ? 232 ASP   A N     1 
ATOM   641  C CA    . ASP   A 1 106 ? 11.754  -3.942  46.285 1.00 60.65  ? 232 ASP   A CA    1 
ATOM   642  C C     . ASP   A 1 106 ? 11.134  -3.088  47.381 1.00 56.14  ? 232 ASP   A C     1 
ATOM   643  O O     . ASP   A 1 106 ? 11.850  -2.517  48.213 1.00 54.35  ? 232 ASP   A O     1 
ATOM   644  C CB    . ASP   A 1 106 ? 11.781  -3.162  44.969 1.00 62.16  ? 232 ASP   A CB    1 
ATOM   645  C CG    . ASP   A 1 106 ? 12.284  -3.986  43.802 1.00 67.18  ? 232 ASP   A CG    1 
ATOM   646  O OD1   . ASP   A 1 106 ? 12.245  -5.235  43.876 1.00 72.35  ? 232 ASP   A OD1   1 
ATOM   647  O OD2   . ASP   A 1 106 ? 12.714  -3.373  42.799 1.00 68.93  ? 232 ASP   A OD2   1 
ATOM   648  N N     . ALA   A 1 107 ? 9.803   -2.990  47.397 1.00 55.34  ? 233 ALA   A N     1 
ATOM   649  C CA    . ALA   A 1 107 ? 9.140   -2.210  48.434 1.00 57.03  ? 233 ALA   A CA    1 
ATOM   650  C C     . ALA   A 1 107 ? 9.384   -2.805  49.811 1.00 57.82  ? 233 ALA   A C     1 
ATOM   651  O O     . ALA   A 1 107 ? 9.489   -2.066  50.795 1.00 56.16  ? 233 ALA   A O     1 
ATOM   652  C CB    . ALA   A 1 107 ? 7.643   -2.114  48.144 1.00 59.32  ? 233 ALA   A CB    1 
ATOM   653  N N     . GLU   A 1 108 ? 9.501   -4.130  49.898 1.00 58.55  ? 234 GLU   A N     1 
ATOM   654  C CA    . GLU   A 1 108 ? 9.788   -4.756  51.185 1.00 58.06  ? 234 GLU   A CA    1 
ATOM   655  C C     . GLU   A 1 108 ? 11.209  -4.443  51.637 1.00 58.28  ? 234 GLU   A C     1 
ATOM   656  O O     . GLU   A 1 108 ? 11.435  -4.088  52.799 1.00 56.07  ? 234 GLU   A O     1 
ATOM   657  C CB    . GLU   A 1 108 ? 9.558   -6.265  51.104 1.00 59.76  ? 234 GLU   A CB    1 
ATOM   658  N N     . ARG   A 1 109 ? 12.180  -4.541  50.725 1.00 58.09  ? 235 ARG   A N     1 
ATOM   659  C CA    . ARG   A 1 109 ? 13.569  -4.281  51.098 1.00 56.66  ? 235 ARG   A CA    1 
ATOM   660  C C     . ARG   A 1 109 ? 13.757  -2.842  51.558 1.00 53.56  ? 235 ARG   A C     1 
ATOM   661  O O     . ARG   A 1 109 ? 14.447  -2.581  52.549 1.00 52.35  ? 235 ARG   A O     1 
ATOM   662  C CB    . ARG   A 1 109 ? 14.501  -4.596  49.927 1.00 60.76  ? 235 ARG   A CB    1 
ATOM   663  N N     . TYR   A 1 110 ? 13.163  -1.886  50.839 1.00 52.03  ? 236 TYR   A N     1 
ATOM   664  C CA    . TYR   A 1 110 ? 13.238  -0.501  51.284 1.00 51.74  ? 236 TYR   A CA    1 
ATOM   665  C C     . TYR   A 1 110 ? 12.613  -0.345  52.664 1.00 49.55  ? 236 TYR   A C     1 
ATOM   666  O O     . TYR   A 1 110 ? 13.177  0.321   53.536 1.00 49.92  ? 236 TYR   A O     1 
ATOM   667  C CB    . TYR   A 1 110 ? 12.556  0.418   50.275 1.00 49.71  ? 236 TYR   A CB    1 
ATOM   668  C CG    . TYR   A 1 110 ? 13.286  0.541   48.953 1.00 50.20  ? 236 TYR   A CG    1 
ATOM   669  C CD1   . TYR   A 1 110 ? 14.656  0.761   48.907 1.00 50.08  ? 236 TYR   A CD1   1 
ATOM   670  C CD2   . TYR   A 1 110 ? 12.597  0.443   47.753 1.00 50.92  ? 236 TYR   A CD2   1 
ATOM   671  C CE1   . TYR   A 1 110 ? 15.327  0.869   47.688 1.00 52.38  ? 236 TYR   A CE1   1 
ATOM   672  C CE2   . TYR   A 1 110 ? 13.253  0.555   46.534 1.00 54.43  ? 236 TYR   A CE2   1 
ATOM   673  C CZ    . TYR   A 1 110 ? 14.617  0.773   46.506 1.00 54.87  ? 236 TYR   A CZ    1 
ATOM   674  O OH    . TYR   A 1 110 ? 15.263  0.876   45.288 1.00 54.36  ? 236 TYR   A OH    1 
ATOM   675  N N     . TYR   A 1 111 ? 11.457  -0.970  52.883 1.00 49.74  ? 237 TYR   A N     1 
ATOM   676  C CA    . TYR   A 1 111 ? 10.816  -0.885  54.187 1.00 52.06  ? 237 TYR   A CA    1 
ATOM   677  C C     . TYR   A 1 111 ? 11.739  -1.405  55.281 1.00 50.23  ? 237 TYR   A C     1 
ATOM   678  O O     . TYR   A 1 111 ? 11.972  -0.721  56.284 1.00 49.52  ? 237 TYR   A O     1 
ATOM   679  C CB    . TYR   A 1 111 ? 9.498   -1.658  54.181 1.00 52.19  ? 237 TYR   A CB    1 
ATOM   680  C CG    . TYR   A 1 111 ? 8.849   -1.713  55.543 1.00 52.26  ? 237 TYR   A CG    1 
ATOM   681  C CD1   . TYR   A 1 111 ? 8.064   -0.665  56.006 1.00 55.90  ? 237 TYR   A CD1   1 
ATOM   682  C CD2   . TYR   A 1 111 ? 9.023   -2.814  56.371 1.00 59.24  ? 237 TYR   A CD2   1 
ATOM   683  C CE1   . TYR   A 1 111 ? 7.469   -0.713  57.263 1.00 56.43  ? 237 TYR   A CE1   1 
ATOM   684  C CE2   . TYR   A 1 111 ? 8.436   -2.868  57.623 1.00 60.16  ? 237 TYR   A CE2   1 
ATOM   685  C CZ    . TYR   A 1 111 ? 7.660   -1.814  58.059 1.00 58.12  ? 237 TYR   A CZ    1 
ATOM   686  O OH    . TYR   A 1 111 ? 7.075   -1.882  59.304 1.00 62.74  ? 237 TYR   A OH    1 
ATOM   687  N N     . ARG   A 1 112 ? 12.286  -2.609  55.096 1.00 52.58  ? 238 ARG   A N     1 
ATOM   688  C CA    . ARG   A 1 112 ? 13.211  -3.158  56.083 1.00 51.95  ? 238 ARG   A CA    1 
ATOM   689  C C     . ARG   A 1 112 ? 14.457  -2.293  56.218 1.00 52.71  ? 238 ARG   A C     1 
ATOM   690  O O     . ARG   A 1 112 ? 15.077  -2.265  57.288 1.00 51.60  ? 238 ARG   A O     1 
ATOM   691  C CB    . ARG   A 1 112 ? 13.588  -4.598  55.723 1.00 53.97  ? 238 ARG   A CB    1 
ATOM   692  N N     . ASP   A 1 113 ? 14.821  -1.550  55.165 1.00 48.84  ? 239 ASP   A N     1 
ATOM   693  C CA    . ASP   A 1 113 ? 15.935  -0.615  55.295 1.00 50.81  ? 239 ASP   A CA    1 
ATOM   694  C C     . ASP   A 1 113 ? 15.542  0.604   56.117 1.00 47.47  ? 239 ASP   A C     1 
ATOM   695  O O     . ASP   A 1 113 ? 16.335  1.087   56.935 1.00 48.05  ? 239 ASP   A O     1 
ATOM   696  C CB    . ASP   A 1 113 ? 16.446  -0.187  53.918 1.00 53.58  ? 239 ASP   A CB    1 
ATOM   697  C CG    . ASP   A 1 113 ? 17.614  -1.036  53.452 1.00 59.89  ? 239 ASP   A CG    1 
ATOM   698  O OD1   . ASP   A 1 113 ? 17.420  -2.254  53.274 1.00 58.34  ? 239 ASP   A OD1   1 
ATOM   699  O OD2   . ASP   A 1 113 ? 18.727  -0.491  53.287 1.00 65.65  ? 239 ASP   A OD2   1 
ATOM   700  N N     . TYR   A 1 114 ? 14.340  1.138   55.888 1.00 47.49  ? 240 TYR   A N     1 
ATOM   701  C CA    . TYR   A 1 114 ? 13.857  2.254   56.700 1.00 45.87  ? 240 TYR   A CA    1 
ATOM   702  C C     . TYR   A 1 114 ? 13.645  1.820   58.147 1.00 45.91  ? 240 TYR   A C     1 
ATOM   703  O O     . TYR   A 1 114 ? 13.998  2.543   59.087 1.00 45.39  ? 240 TYR   A O     1 
ATOM   704  C CB    . TYR   A 1 114 ? 12.548  2.794   56.129 1.00 44.31  ? 240 TYR   A CB    1 
ATOM   705  C CG    . TYR   A 1 114 ? 12.690  3.711   54.948 1.00 42.71  ? 240 TYR   A CG    1 
ATOM   706  C CD1   . TYR   A 1 114 ? 13.660  4.702   54.923 1.00 45.25  ? 240 TYR   A CD1   1 
ATOM   707  C CD2   . TYR   A 1 114 ? 11.837  3.603   53.862 1.00 47.16  ? 240 TYR   A CD2   1 
ATOM   708  C CE1   . TYR   A 1 114 ? 13.776  5.564   53.835 1.00 44.53  ? 240 TYR   A CE1   1 
ATOM   709  C CE2   . TYR   A 1 114 ? 11.951  4.455   52.766 1.00 42.23  ? 240 TYR   A CE2   1 
ATOM   710  C CZ    . TYR   A 1 114 ? 12.923  5.423   52.757 1.00 44.32  ? 240 TYR   A CZ    1 
ATOM   711  O OH    . TYR   A 1 114 ? 13.027  6.275   51.675 1.00 44.57  ? 240 TYR   A OH    1 
ATOM   712  N N     . GLU   A 1 115 ? 13.052  0.649   58.335 1.00 46.08  ? 241 GLU   A N     1 
ATOM   713  C CA    . GLU   A 1 115 ? 12.829  0.121   59.677 1.00 48.44  ? 241 GLU   A CA    1 
ATOM   714  C C     . GLU   A 1 115 ? 14.133  0.035   60.468 1.00 48.59  ? 241 GLU   A C     1 
ATOM   715  O O     . GLU   A 1 115 ? 14.222  0.532   61.596 1.00 48.92  ? 241 GLU   A O     1 
ATOM   716  C CB    . GLU   A 1 115 ? 12.161  -1.249  59.577 1.00 51.33  ? 241 GLU   A CB    1 
ATOM   717  C CG    . GLU   A 1 115 ? 11.793  -1.868  60.901 1.00 55.95  ? 241 GLU   A CG    1 
ATOM   718  C CD    . GLU   A 1 115 ? 11.158  -3.225  60.725 1.00 58.54  ? 241 GLU   A CD    1 
ATOM   719  O OE1   . GLU   A 1 115 ? 11.568  -3.956  59.792 1.00 60.01  ? 241 GLU   A OE1   1 
ATOM   720  O OE2   . GLU   A 1 115 ? 10.236  -3.555  61.500 1.00 59.31  ? 241 GLU   A OE2   1 
ATOM   721  N N     . SER   A 1 116 ? 15.162  -0.588  59.887 1.00 48.23  ? 242 SER   A N     1 
ATOM   722  C CA    . SER   A 1 116 ? 16.424  -0.734  60.603 1.00 48.32  ? 242 SER   A CA    1 
ATOM   723  C C     . SER   A 1 116 ? 17.138  0.603   60.767 1.00 47.23  ? 242 SER   A C     1 
ATOM   724  O O     . SER   A 1 116 ? 17.807  0.820   61.787 1.00 48.70  ? 242 SER   A O     1 
ATOM   725  C CB    . SER   A 1 116 ? 17.320  -1.759  59.894 1.00 50.55  ? 242 SER   A CB    1 
ATOM   726  O OG    . SER   A 1 116 ? 18.077  -1.167  58.853 1.00 53.26  ? 242 SER   A OG    1 
ATOM   727  N N     . ALA   A 1 117 ? 16.997  1.512   59.791 1.00 45.41  ? 243 ALA   A N     1 
ATOM   728  C CA    . ALA   A 1 117 ? 17.559  2.852   59.930 1.00 43.20  ? 243 ALA   A CA    1 
ATOM   729  C C     . ALA   A 1 117 ? 16.950  3.591   61.106 1.00 42.55  ? 243 ALA   A C     1 
ATOM   730  O O     . ALA   A 1 117 ? 17.656  4.294   61.834 1.00 41.27  ? 243 ALA   A O     1 
ATOM   731  C CB    . ALA   A 1 117 ? 17.334  3.665   58.659 1.00 43.42  ? 243 ALA   A CB    1 
ATOM   732  N N     . ILE   A 1 118 ? 15.632  3.474   61.281 1.00 41.50  ? 244 ILE   A N     1 
ATOM   733  C CA    . ILE   A 1 118 ? 14.964  4.126   62.403 1.00 42.82  ? 244 ILE   A CA    1 
ATOM   734  C C     . ILE   A 1 118 ? 15.524  3.616   63.722 1.00 42.43  ? 244 ILE   A C     1 
ATOM   735  O O     . ILE   A 1 118 ? 15.734  4.389   64.666 1.00 42.94  ? 244 ILE   A O     1 
ATOM   736  C CB    . ILE   A 1 118 ? 13.441  3.909   62.313 1.00 44.95  ? 244 ILE   A CB    1 
ATOM   737  C CG1   . ILE   A 1 118 ? 12.862  4.704   61.146 1.00 45.42  ? 244 ILE   A CG1   1 
ATOM   738  C CG2   . ILE   A 1 118 ? 12.757  4.292   63.625 1.00 44.68  ? 244 ILE   A CG2   1 
ATOM   739  C CD1   . ILE   A 1 118 ? 11.451  4.298   60.774 1.00 45.95  ? 244 ILE   A CD1   1 
ATOM   740  N N     . HIS   A 1 119 ? 15.799  2.314   63.806 1.00 46.68  ? 245 HIS   A N     1 
ATOM   741  C CA    . HIS   A 1 119 ? 16.366  1.787   65.045 1.00 45.63  ? 245 HIS   A CA    1 
ATOM   742  C C     . HIS   A 1 119 ? 17.743  2.375   65.301 1.00 45.71  ? 245 HIS   A C     1 
ATOM   743  O O     . HIS   A 1 119 ? 18.051  2.782   66.426 1.00 47.21  ? 245 HIS   A O     1 
ATOM   744  C CB    . HIS   A 1 119 ? 16.422  0.260   65.008 1.00 49.40  ? 245 HIS   A CB    1 
ATOM   745  C CG    . HIS   A 1 119 ? 15.082  -0.383  65.172 1.00 52.91  ? 245 HIS   A CG    1 
ATOM   746  N ND1   . HIS   A 1 119 ? 14.289  -0.174  66.283 1.00 49.46  ? 245 HIS   A ND1   1 
ATOM   747  C CD2   . HIS   A 1 119 ? 14.390  -1.221  64.366 1.00 53.61  ? 245 HIS   A CD2   1 
ATOM   748  C CE1   . HIS   A 1 119 ? 13.161  -0.847  66.143 1.00 53.70  ? 245 HIS   A CE1   1 
ATOM   749  N NE2   . HIS   A 1 119 ? 13.201  -1.498  64.994 1.00 53.28  ? 245 HIS   A NE2   1 
ATOM   750  N N     . ALA   A 1 120 ? 18.575  2.455   64.263 1.00 41.13  ? 246 ALA   A N     1 
ATOM   751  C CA    . ALA   A 1 120 ? 19.923  2.987   64.431 1.00 45.95  ? 246 ALA   A CA    1 
ATOM   752  C C     . ALA   A 1 120 ? 19.896  4.473   64.767 1.00 42.37  ? 246 ALA   A C     1 
ATOM   753  O O     . ALA   A 1 120 ? 20.625  4.931   65.654 1.00 43.64  ? 246 ALA   A O     1 
ATOM   754  C CB    . ALA   A 1 120 ? 20.751  2.739   63.168 1.00 46.10  ? 246 ALA   A CB    1 
ATOM   755  N N     . ILE   A 1 121 ? 19.074  5.247   64.051 1.00 41.19  ? 247 ILE   A N     1 
ATOM   756  C CA    . ILE   A 1 121 ? 18.966  6.677   64.315 1.00 40.39  ? 247 ILE   A CA    1 
ATOM   757  C C     . ILE   A 1 121 ? 18.333  6.924   65.674 1.00 41.32  ? 247 ILE   A C     1 
ATOM   758  O O     . ILE   A 1 121 ? 18.739  7.832   66.412 1.00 41.89  ? 247 ILE   A O     1 
ATOM   759  C CB    . ILE   A 1 121 ? 18.158  7.345   63.197 1.00 38.08  ? 247 ILE   A CB    1 
ATOM   760  C CG1   . ILE   A 1 121 ? 18.883  7.165   61.868 1.00 34.16  ? 247 ILE   A CG1   1 
ATOM   761  C CG2   . ILE   A 1 121 ? 17.894  8.821   63.523 1.00 34.71  ? 247 ILE   A CG2   1 
ATOM   762  C CD1   . ILE   A 1 121 ? 17.968  7.475   60.682 1.00 38.12  ? 247 ILE   A CD1   1 
ATOM   763  N N     . GLY   A 1 122 ? 17.306  6.145   66.006 1.00 38.28  ? 248 GLY   A N     1 
ATOM   764  C CA    . GLY   A 1 122 ? 16.659  6.304   67.295 1.00 43.66  ? 248 GLY   A CA    1 
ATOM   765  C C     . GLY   A 1 122 ? 17.612  6.074   68.448 1.00 44.55  ? 248 GLY   A C     1 
ATOM   766  O O     . GLY   A 1 122 ? 17.655  6.855   69.401 1.00 48.12  ? 248 GLY   A O     1 
ATOM   767  N N     . LYS   A 1 123 ? 18.381  4.985   68.385 1.00 43.98  ? 249 LYS   A N     1 
ATOM   768  C CA    . LYS   A 1 123 ? 19.353  4.720   69.440 1.00 46.88  ? 249 LYS   A CA    1 
ATOM   769  C C     . LYS   A 1 123 ? 20.431  5.794   69.467 1.00 44.28  ? 249 LYS   A C     1 
ATOM   770  O O     . LYS   A 1 123 ? 20.862  6.225   70.544 1.00 45.55  ? 249 LYS   A O     1 
ATOM   771  C CB    . LYS   A 1 123 ? 19.974  3.336   69.251 1.00 46.32  ? 249 LYS   A CB    1 
ATOM   772  C CG    . LYS   A 1 123 ? 18.977  2.205   69.429 1.00 50.23  ? 249 LYS   A CG    1 
ATOM   773  C CD    . LYS   A 1 123 ? 19.571  0.861   69.077 1.00 53.15  ? 249 LYS   A CD    1 
ATOM   774  C CE    . LYS   A 1 123 ? 18.468  -0.148  68.848 1.00 54.44  ? 249 LYS   A CE    1 
ATOM   775  N NZ    . LYS   A 1 123 ? 18.983  -1.446  68.365 1.00 59.51  ? 249 LYS   A NZ    1 
ATOM   776  N N     . ALA   A 1 124 ? 20.875  6.244   68.289 1.00 44.64  ? 250 ALA   A N     1 
ATOM   777  C CA    . ALA   A 1 124 ? 21.881  7.297   68.247 1.00 42.54  ? 250 ALA   A CA    1 
ATOM   778  C C     . ALA   A 1 124 ? 21.321  8.608   68.774 1.00 42.87  ? 250 ALA   A C     1 
ATOM   779  O O     . ALA   A 1 124 ? 22.039  9.381   69.416 1.00 45.77  ? 250 ALA   A O     1 
ATOM   780  C CB    . ALA   A 1 124 ? 22.409  7.470   66.823 1.00 42.94  ? 250 ALA   A CB    1 
ATOM   781  N N     . SER   A 1 125 ? 20.044  8.881   68.508 1.00 39.93  ? 251 SER   A N     1 
ATOM   782  C CA    . SER   A 1 125 ? 19.437  10.098  69.034 1.00 41.73  ? 251 SER   A CA    1 
ATOM   783  C C     . SER   A 1 125 ? 19.539  10.121  70.548 1.00 43.47  ? 251 SER   A C     1 
ATOM   784  O O     . SER   A 1 125 ? 19.917  11.134  71.140 1.00 44.37  ? 251 SER   A O     1 
ATOM   785  C CB    . SER   A 1 125 ? 17.977  10.194  68.597 1.00 43.41  ? 251 SER   A CB    1 
ATOM   786  O OG    . SER   A 1 125 ? 17.304  11.212  69.311 1.00 39.55  ? 251 SER   A OG    1 
ATOM   787  N N     . ALA   A 1 126 ? 19.228  9.001   71.176 1.00 38.53  ? 252 ALA   A N     1 
ATOM   788  C CA    . ALA   A 1 126 ? 19.454  8.803   72.611 1.00 46.45  ? 252 ALA   A CA    1 
ATOM   789  C C     . ALA   A 1 126 ? 18.690  9.827   73.452 1.00 47.70  ? 252 ALA   A C     1 
ATOM   790  O O     . ALA   A 1 126 ? 19.218  10.401  74.408 1.00 50.75  ? 252 ALA   A O     1 
ATOM   791  C CB    . ALA   A 1 126 ? 20.953  8.822   72.941 1.00 44.96  ? 252 ALA   A CB    1 
ATOM   792  N N     . GLY   A 1 127 ? 17.422  10.031  73.107 1.00 45.18  ? 253 GLY   A N     1 
ATOM   793  C CA    . GLY   A 1 127 ? 16.554  10.902  73.873 1.00 48.77  ? 253 GLY   A CA    1 
ATOM   794  C C     . GLY   A 1 127 ? 16.725  12.381  73.612 1.00 46.23  ? 253 GLY   A C     1 
ATOM   795  O O     . GLY   A 1 127 ? 16.118  13.193  74.328 1.00 47.08  ? 253 GLY   A O     1 
ATOM   796  N N     . ARG   A 1 128 ? 17.546  12.763  72.631 1.00 43.75  ? 254 ARG   A N     1 
ATOM   797  C CA    . ARG   A 1 128 ? 17.668  14.169  72.271 1.00 44.05  ? 254 ARG   A CA    1 
ATOM   798  C C     . ARG   A 1 128 ? 16.356  14.743  71.758 1.00 40.48  ? 254 ARG   A C     1 
ATOM   799  O O     . ARG   A 1 128 ? 16.164  15.960  71.816 1.00 45.71  ? 254 ARG   A O     1 
ATOM   800  C CB    . ARG   A 1 128 ? 18.776  14.353  71.238 1.00 44.74  ? 254 ARG   A CB    1 
ATOM   801  C CG    . ARG   A 1 128 ? 20.180  14.361  71.837 1.00 44.31  ? 254 ARG   A CG    1 
ATOM   802  C CD    . ARG   A 1 128 ? 21.239  14.571  70.757 1.00 46.84  ? 254 ARG   A CD    1 
ATOM   803  N NE    . ARG   A 1 128 ? 21.487  13.338  70.016 1.00 48.66  ? 254 ARG   A NE    1 
ATOM   804  C CZ    . ARG   A 1 128 ? 22.232  13.241  68.923 1.00 46.02  ? 254 ARG   A CZ    1 
ATOM   805  N NH1   . ARG   A 1 128 ? 22.774  14.307  68.355 1.00 50.29  ? 254 ARG   A NH1   1 
ATOM   806  N NH2   . ARG   A 1 128 ? 22.437  12.041  68.385 1.00 48.85  ? 254 ARG   A NH2   1 
ATOM   807  N N     . GLY   A 1 129 ? 15.442  13.901  71.289 1.00 41.89  ? 255 GLY   A N     1 
ATOM   808  C CA    . GLY   A 1 129 ? 14.141  14.370  70.869 1.00 41.76  ? 255 GLY   A CA    1 
ATOM   809  C C     . GLY   A 1 129 ? 14.142  14.878  69.441 1.00 41.53  ? 255 GLY   A C     1 
ATOM   810  O O     . GLY   A 1 129 ? 15.139  14.834  68.711 1.00 39.68  ? 255 GLY   A O     1 
ATOM   811  N N     . ILE   A 1 130 ? 12.980  15.395  69.039 1.00 39.98  ? 256 ILE   A N     1 
ATOM   812  C CA    . ILE   A 1 130 ? 12.729  15.592  67.614 1.00 37.65  ? 256 ILE   A CA    1 
ATOM   813  C C     . ILE   A 1 130 ? 13.428  16.812  67.025 1.00 37.44  ? 256 ILE   A C     1 
ATOM   814  O O     . ILE   A 1 130 ? 13.561  16.896  65.795 1.00 36.27  ? 256 ILE   A O     1 
ATOM   815  C CB    . ILE   A 1 130 ? 11.222  15.699  67.340 1.00 38.40  ? 256 ILE   A CB    1 
ATOM   816  C CG1   . ILE   A 1 130 ? 10.643  16.922  68.026 1.00 39.40  ? 256 ILE   A CG1   1 
ATOM   817  C CG2   . ILE   A 1 130 ? 10.481  14.459  67.806 1.00 38.69  ? 256 ILE   A CG2   1 
ATOM   818  C CD1   . ILE   A 1 130 ? 9.192   17.151  67.673 1.00 42.76  ? 256 ILE   A CD1   1 
ATOM   819  N N     . TYR   A 1 131 ? 13.881  17.762  67.846 1.00 39.16  ? 257 TYR   A N     1 
ATOM   820  C CA    . TYR   A 1 131 ? 14.486  18.977  67.300 1.00 36.83  ? 257 TYR   A CA    1 
ATOM   821  C C     . TYR   A 1 131 ? 15.994  18.998  67.420 1.00 39.57  ? 257 TYR   A C     1 
ATOM   822  O O     . TYR   A 1 131 ? 16.680  19.436  66.491 1.00 42.68  ? 257 TYR   A O     1 
ATOM   823  C CB    . TYR   A 1 131 ? 13.934  20.226  67.996 1.00 37.25  ? 257 TYR   A CB    1 
ATOM   824  C CG    . TYR   A 1 131 ? 12.441  20.285  67.987 1.00 38.59  ? 257 TYR   A CG    1 
ATOM   825  C CD1   . TYR   A 1 131 ? 11.744  20.352  66.785 1.00 40.01  ? 257 TYR   A CD1   1 
ATOM   826  C CD2   . TYR   A 1 131 ? 11.722  20.258  69.169 1.00 41.80  ? 257 TYR   A CD2   1 
ATOM   827  C CE1   . TYR   A 1 131 ? 10.373  20.400  66.774 1.00 39.50  ? 257 TYR   A CE1   1 
ATOM   828  C CE2   . TYR   A 1 131 ? 10.354  20.304  69.165 1.00 42.19  ? 257 TYR   A CE2   1 
ATOM   829  C CZ    . TYR   A 1 131 ? 9.683   20.377  67.961 1.00 40.96  ? 257 TYR   A CZ    1 
ATOM   830  O OH    . TYR   A 1 131 ? 8.308   20.417  67.971 1.00 40.40  ? 257 TYR   A OH    1 
ATOM   831  N N     . GLU   A 1 132 ? 16.513  18.572  68.566 1.00 40.03  ? 258 GLU   A N     1 
ATOM   832  C CA    . GLU   A 1 132 ? 17.948  18.531  68.785 1.00 41.48  ? 258 GLU   A CA    1 
ATOM   833  C C     . GLU   A 1 132 ? 18.573  17.271  68.216 1.00 43.66  ? 258 GLU   A C     1 
ATOM   834  O O     . GLU   A 1 132 ? 19.773  17.263  67.921 1.00 47.33  ? 258 GLU   A O     1 
ATOM   835  C CB    . GLU   A 1 132 ? 18.242  18.635  70.281 1.00 44.93  ? 258 GLU   A CB    1 
ATOM   836  C CG    . GLU   A 1 132 ? 18.105  20.045  70.805 1.00 54.10  ? 258 GLU   A CG    1 
ATOM   837  C CD    . GLU   A 1 132 ? 19.396  20.834  70.657 1.00 63.44  ? 258 GLU   A CD    1 
ATOM   838  O OE1   . GLU   A 1 132 ? 20.484  20.248  70.881 1.00 62.51  ? 258 GLU   A OE1   1 
ATOM   839  O OE2   . GLU   A 1 132 ? 19.322  22.035  70.315 1.00 64.25  ? 258 GLU   A OE2   1 
ATOM   840  N N     . GLY   A 1 133 ? 17.790  16.207  68.061 1.00 37.16  ? 259 GLY   A N     1 
ATOM   841  C CA    . GLY   A 1 133 ? 18.322  14.943  67.623 1.00 36.76  ? 259 GLY   A CA    1 
ATOM   842  C C     . GLY   A 1 133 ? 18.028  14.680  66.164 1.00 35.62  ? 259 GLY   A C     1 
ATOM   843  O O     . GLY   A 1 133 ? 17.250  15.383  65.523 1.00 34.53  ? 259 GLY   A O     1 
ATOM   844  N N     . PRO   A 1 134 ? 18.640  13.635  65.624 1.00 36.46  ? 260 PRO   A N     1 
ATOM   845  C CA    . PRO   A 1 134 ? 18.436  13.304  64.216 1.00 33.05  ? 260 PRO   A CA    1 
ATOM   846  C C     . PRO   A 1 134 ? 17.043  12.738  63.987 1.00 35.07  ? 260 PRO   A C     1 
ATOM   847  O O     . PRO   A 1 134 ? 16.350  12.295  64.909 1.00 35.35  ? 260 PRO   A O     1 
ATOM   848  C CB    . PRO   A 1 134 ? 19.523  12.256  63.936 1.00 32.66  ? 260 PRO   A CB    1 
ATOM   849  C CG    . PRO   A 1 134 ? 19.796  11.625  65.283 1.00 33.08  ? 260 PRO   A CG    1 
ATOM   850  C CD    . PRO   A 1 134 ? 19.507  12.668  66.321 1.00 36.05  ? 260 PRO   A CD    1 
ATOM   851  N N     . GLY   A 1 135 ? 16.632  12.775  62.729 1.00 31.54  ? 261 GLY   A N     1 
ATOM   852  C CA    . GLY   A 1 135 ? 15.391  12.151  62.339 1.00 34.44  ? 261 GLY   A CA    1 
ATOM   853  C C     . GLY   A 1 135 ? 15.592  11.387  61.045 1.00 33.45  ? 261 GLY   A C     1 
ATOM   854  O O     . GLY   A 1 135 ? 16.719  11.237  60.563 1.00 29.24  ? 261 GLY   A O     1 
ATOM   855  N N     . ILE   A 1 136 ? 14.503  10.875  60.496 1.00 31.60  ? 262 ILE   A N     1 
ATOM   856  C CA    . ILE   A 1 136 ? 14.529  10.117  59.261 1.00 30.22  ? 262 ILE   A CA    1 
ATOM   857  C C     . ILE   A 1 136 ? 13.557  10.773  58.301 1.00 34.48  ? 262 ILE   A C     1 
ATOM   858  O O     . ILE   A 1 136 ? 12.609  11.451  58.711 1.00 33.55  ? 262 ILE   A O     1 
ATOM   859  C CB    . ILE   A 1 136 ? 14.159  8.633   59.458 1.00 35.47  ? 262 ILE   A CB    1 
ATOM   860  C CG1   . ILE   A 1 136 ? 14.495  7.820   58.212 1.00 36.54  ? 262 ILE   A CG1   1 
ATOM   861  C CG2   . ILE   A 1 136 ? 12.686  8.488   59.774 1.00 37.20  ? 262 ILE   A CG2   1 
ATOM   862  C CD1   . ILE   A 1 136 ? 14.460  6.310   58.419 1.00 41.99  ? 262 ILE   A CD1   1 
ATOM   863  N N     . SER   A 1 137 ? 13.822  10.586  57.017 1.00 31.78  ? 263 SER   A N     1 
ATOM   864  C CA    . SER   A 1 137 ? 12.900  10.966  55.956 1.00 32.68  ? 263 SER   A CA    1 
ATOM   865  C C     . SER   A 1 137 ? 12.667  9.766   55.059 1.00 36.73  ? 263 SER   A C     1 
ATOM   866  O O     . SER   A 1 137 ? 13.580  8.966   54.821 1.00 34.92  ? 263 SER   A O     1 
ATOM   867  C CB    . SER   A 1 137 ? 13.440  12.141  55.125 1.00 30.20  ? 263 SER   A CB    1 
ATOM   868  O OG    . SER   A 1 137 ? 13.470  13.335  55.895 1.00 32.14  ? 263 SER   A OG    1 
ATOM   869  N N     . ILE   A 1 138 ? 11.442  9.638   54.557 1.00 31.83  ? 264 ILE   A N     1 
ATOM   870  C CA    . ILE   A 1 138 ? 11.082  8.529   53.695 1.00 35.76  ? 264 ILE   A CA    1 
ATOM   871  C C     . ILE   A 1 138 ? 10.417  9.088   52.448 1.00 33.75  ? 264 ILE   A C     1 
ATOM   872  O O     . ILE   A 1 138 ? 9.864   10.190  52.449 1.00 33.10  ? 264 ILE   A O     1 
ATOM   873  C CB    . ILE   A 1 138 ? 10.151  7.522   54.386 1.00 36.73  ? 264 ILE   A CB    1 
ATOM   874  C CG1   . ILE   A 1 138 ? 8.809   8.176   54.735 1.00 35.87  ? 264 ILE   A CG1   1 
ATOM   875  C CG2   . ILE   A 1 138 ? 10.813  6.979   55.652 1.00 40.93  ? 264 ILE   A CG2   1 
ATOM   876  C CD1   . ILE   A 1 138 ? 7.793   7.192   55.329 1.00 39.72  ? 264 ILE   A CD1   1 
ATOM   877  N N     . LYS   A 1 139 ? 10.489  8.308   51.385 1.00 36.30  ? 265 LYS   A N     1 
ATOM   878  C CA    . LYS   A 1 139 ? 9.752   8.564   50.156 1.00 38.36  ? 265 LYS   A CA    1 
ATOM   879  C C     . LYS   A 1 139 ? 8.697   7.474   50.018 1.00 40.08  ? 265 LYS   A C     1 
ATOM   880  O O     . LYS   A 1 139 ? 9.028   6.282   49.999 1.00 39.04  ? 265 LYS   A O     1 
ATOM   881  C CB    . LYS   A 1 139 ? 10.687  8.599   48.945 1.00 38.35  ? 265 LYS   A CB    1 
ATOM   882  C CG    . LYS   A 1 139 ? 11.704  9.747   48.982 1.00 37.07  ? 265 LYS   A CG    1 
ATOM   883  C CD    . LYS   A 1 139 ? 12.401  9.958   47.633 1.00 40.49  ? 265 LYS   A CD    1 
ATOM   884  C CE    . LYS   A 1 139 ? 13.594  10.894  47.804 1.00 38.67  ? 265 LYS   A CE    1 
ATOM   885  N NZ    . LYS   A 1 139 ? 13.171  12.221  48.318 1.00 37.41  ? 265 LYS   A NZ    1 
ATOM   886  N N     . LEU   A 1 140 ? 7.425   7.875   49.948 1.00 39.29  ? 266 LEU   A N     1 
ATOM   887  C CA    . LEU   A 1 140 ? 6.360   6.877   49.895 1.00 42.09  ? 266 LEU   A CA    1 
ATOM   888  C C     . LEU   A 1 140 ? 6.490   5.983   48.669 1.00 42.98  ? 266 LEU   A C     1 
ATOM   889  O O     . LEU   A 1 140 ? 6.046   4.828   48.688 1.00 44.27  ? 266 LEU   A O     1 
ATOM   890  C CB    . LEU   A 1 140 ? 4.992   7.559   49.916 1.00 43.12  ? 266 LEU   A CB    1 
ATOM   891  C CG    . LEU   A 1 140 ? 4.683   8.403   51.155 1.00 43.06  ? 266 LEU   A CG    1 
ATOM   892  C CD1   . LEU   A 1 140 ? 3.296   9.017   51.036 1.00 43.38  ? 266 LEU   A CD1   1 
ATOM   893  C CD2   . LEU   A 1 140 ? 4.802   7.556   52.411 1.00 44.67  ? 266 LEU   A CD2   1 
ATOM   894  N N     . SER   A 1 141 ? 7.116   6.482   47.602 1.00 45.63  ? 267 SER   A N     1 
ATOM   895  C CA    . SER   A 1 141 ? 7.265   5.674   46.396 1.00 43.68  ? 267 SER   A CA    1 
ATOM   896  C C     . SER   A 1 141 ? 8.221   4.504   46.593 1.00 42.89  ? 267 SER   A C     1 
ATOM   897  O O     . SER   A 1 141 ? 8.221   3.575   45.777 1.00 44.93  ? 267 SER   A O     1 
ATOM   898  C CB    . SER   A 1 141 ? 7.742   6.539   45.226 1.00 44.25  ? 267 SER   A CB    1 
ATOM   899  O OG    . SER   A 1 141 ? 9.114   6.856   45.360 1.00 42.25  ? 267 SER   A OG    1 
ATOM   900  N N     . ALA   A 1 142 ? 9.042   4.538   47.640 1.00 42.58  ? 268 ALA   A N     1 
ATOM   901  C CA    . ALA   A 1 142 ? 9.872   3.390   47.981 1.00 47.69  ? 268 ALA   A CA    1 
ATOM   902  C C     . ALA   A 1 142 ? 9.083   2.272   48.652 1.00 46.66  ? 268 ALA   A C     1 
ATOM   903  O O     . ALA   A 1 142 ? 9.527   1.121   48.641 1.00 48.41  ? 268 ALA   A O     1 
ATOM   904  C CB    . ALA   A 1 142 ? 11.013  3.832   48.903 1.00 44.54  ? 268 ALA   A CB    1 
ATOM   905  N N     . LEU   A 1 143 ? 7.923   2.576   49.225 1.00 47.83  ? 269 LEU   A N     1 
ATOM   906  C CA    . LEU   A 1 143 ? 7.220   1.645   50.094 1.00 47.85  ? 269 LEU   A CA    1 
ATOM   907  C C     . LEU   A 1 143 ? 6.029   0.973   49.432 1.00 52.56  ? 269 LEU   A C     1 
ATOM   908  O O     . LEU   A 1 143 ? 5.416   0.089   50.042 1.00 55.28  ? 269 LEU   A O     1 
ATOM   909  C CB    . LEU   A 1 143 ? 6.763   2.374   51.355 1.00 45.83  ? 269 LEU   A CB    1 
ATOM   910  C CG    . LEU   A 1 143 ? 7.905   3.082   52.071 1.00 46.43  ? 269 LEU   A CG    1 
ATOM   911  C CD1   . LEU   A 1 143 ? 7.354   3.974   53.166 1.00 46.37  ? 269 LEU   A CD1   1 
ATOM   912  C CD2   . LEU   A 1 143 ? 8.868   2.047   52.624 1.00 47.22  ? 269 LEU   A CD2   1 
ATOM   913  N N     . HIS   A 1 144 ? 5.703   1.345   48.197 1.00 54.48  ? 270 HIS   A N     1 
ATOM   914  C CA    . HIS   A 1 144 ? 4.568   0.784   47.485 1.00 54.16  ? 270 HIS   A CA    1 
ATOM   915  C C     . HIS   A 1 144 ? 5.000   0.436   46.067 1.00 58.08  ? 270 HIS   A C     1 
ATOM   916  O O     . HIS   A 1 144 ? 5.457   1.317   45.331 1.00 55.53  ? 270 HIS   A O     1 
ATOM   917  C CB    . HIS   A 1 144 ? 3.405   1.771   47.474 1.00 55.68  ? 270 HIS   A CB    1 
ATOM   918  C CG    . HIS   A 1 144 ? 2.094   1.145   47.130 1.00 61.85  ? 270 HIS   A CG    1 
ATOM   919  N ND1   . HIS   A 1 144 ? 1.724   0.856   45.834 1.00 65.11  ? 270 HIS   A ND1   1 
ATOM   920  C CD2   . HIS   A 1 144 ? 1.070   0.736   47.915 1.00 65.87  ? 270 HIS   A CD2   1 
ATOM   921  C CE1   . HIS   A 1 144 ? 0.524   0.302   45.836 1.00 65.76  ? 270 HIS   A CE1   1 
ATOM   922  N NE2   . HIS   A 1 144 ? 0.106   0.220   47.086 1.00 70.00  ? 270 HIS   A NE2   1 
ATOM   923  N N     . PRO   A 1 145 ? 4.845   -0.824  45.643 1.00 56.68  ? 271 PRO   A N     1 
ATOM   924  C CA    . PRO   A 1 145 ? 5.502   -1.282  44.405 1.00 60.40  ? 271 PRO   A CA    1 
ATOM   925  C C     . PRO   A 1 145 ? 4.976   -0.645  43.128 1.00 62.65  ? 271 PRO   A C     1 
ATOM   926  O O     . PRO   A 1 145 ? 5.550   -0.890  42.056 1.00 67.47  ? 271 PRO   A O     1 
ATOM   927  C CB    . PRO   A 1 145 ? 5.233   -2.790  44.407 1.00 61.41  ? 271 PRO   A CB    1 
ATOM   928  C CG    . PRO   A 1 145 ? 3.955   -2.931  45.161 1.00 62.37  ? 271 PRO   A CG    1 
ATOM   929  C CD    . PRO   A 1 145 ? 3.997   -1.871  46.238 1.00 56.85  ? 271 PRO   A CD    1 
ATOM   930  N N     . ARG   A 1 146 ? 3.901   0.127   43.183 1.00 60.76  ? 272 ARG   A N     1 
ATOM   931  C CA    . ARG   A 1 146 ? 3.395   0.782   41.983 1.00 63.92  ? 272 ARG   A CA    1 
ATOM   932  C C     . ARG   A 1 146 ? 2.820   2.135   42.383 1.00 66.04  ? 272 ARG   A C     1 
ATOM   933  O O     . ARG   A 1 146 ? 1.698   2.493   42.022 1.00 69.64  ? 272 ARG   A O     1 
ATOM   934  C CB    . ARG   A 1 146 ? 2.366   -0.098  41.270 1.00 66.92  ? 272 ARG   A CB    1 
ATOM   935  N N     . TYR   A 1 147 ? 3.611   2.900   43.143 1.00 60.94  ? 273 TYR   A N     1 
ATOM   936  C CA    . TYR   A 1 147 ? 3.109   4.100   43.802 1.00 59.34  ? 273 TYR   A CA    1 
ATOM   937  C C     . TYR   A 1 147 ? 2.516   5.086   42.804 1.00 61.35  ? 273 TYR   A C     1 
ATOM   938  O O     . TYR   A 1 147 ? 1.426   5.627   43.025 1.00 61.56  ? 273 TYR   A O     1 
ATOM   939  C CB    . TYR   A 1 147 ? 4.237   4.753   44.596 1.00 50.63  ? 273 TYR   A CB    1 
ATOM   940  C CG    . TYR   A 1 147 ? 3.789   5.934   45.409 1.00 53.50  ? 273 TYR   A CG    1 
ATOM   941  C CD1   . TYR   A 1 147 ? 2.820   5.785   46.390 1.00 48.35  ? 273 TYR   A CD1   1 
ATOM   942  C CD2   . TYR   A 1 147 ? 4.338   7.195   45.211 1.00 49.21  ? 273 TYR   A CD2   1 
ATOM   943  C CE1   . TYR   A 1 147 ? 2.403   6.850   47.141 1.00 49.84  ? 273 TYR   A CE1   1 
ATOM   944  C CE2   . TYR   A 1 147 ? 3.932   8.269   45.975 1.00 47.71  ? 273 TYR   A CE2   1 
ATOM   945  C CZ    . TYR   A 1 147 ? 2.962   8.086   46.936 1.00 45.86  ? 273 TYR   A CZ    1 
ATOM   946  O OH    . TYR   A 1 147 ? 2.531   9.138   47.707 1.00 51.91  ? 273 TYR   A OH    1 
ATOM   947  N N     . SER   A 1 148 ? 3.225   5.339   41.702 1.00 60.33  ? 274 SER   A N     1 
ATOM   948  C CA    . SER   A 1 148 ? 2.778   6.318   40.720 1.00 64.48  ? 274 SER   A CA    1 
ATOM   949  C C     . SER   A 1 148 ? 1.681   5.793   39.804 1.00 69.17  ? 274 SER   A C     1 
ATOM   950  O O     . SER   A 1 148 ? 0.972   6.600   39.195 1.00 71.24  ? 274 SER   A O     1 
ATOM   951  C CB    . SER   A 1 148 ? 3.959   6.790   39.867 1.00 64.25  ? 274 SER   A CB    1 
ATOM   952  N N     . ARG   A 1 149 ? 1.521   4.473   39.690 1.00 73.31  ? 275 ARG   A N     1 
ATOM   953  C CA    . ARG   A 1 149 ? 0.601   3.885   38.723 1.00 73.46  ? 275 ARG   A CA    1 
ATOM   954  C C     . ARG   A 1 149 ? -0.647  3.291   39.354 1.00 76.30  ? 275 ARG   A C     1 
ATOM   955  O O     . ARG   A 1 149 ? -1.536  2.845   38.622 1.00 77.08  ? 275 ARG   A O     1 
ATOM   956  C CB    . ARG   A 1 149 ? 1.315   2.806   37.900 1.00 70.96  ? 275 ARG   A CB    1 
ATOM   957  N N     . ALA   A 1 150 ? -0.745  3.270   40.678 1.00 85.81  ? 276 ALA   A N     1 
ATOM   958  C CA    . ALA   A 1 150 ? -1.865  2.642   41.363 1.00 91.98  ? 276 ALA   A CA    1 
ATOM   959  C C     . ALA   A 1 150 ? -2.844  3.696   41.862 1.00 96.89  ? 276 ALA   A C     1 
ATOM   960  O O     . ALA   A 1 150 ? -2.441  4.788   42.277 1.00 93.43  ? 276 ALA   A O     1 
ATOM   961  C CB    . ALA   A 1 150 ? -1.378  1.787   42.535 1.00 92.84  ? 276 ALA   A CB    1 
ATOM   962  N N     . GLN   A 1 151 ? -4.132  3.353   41.827 1.00 89.87  ? 277 GLN   A N     1 
ATOM   963  C CA    . GLN   A 1 151 ? -5.171  4.254   42.307 1.00 88.72  ? 277 GLN   A CA    1 
ATOM   964  C C     . GLN   A 1 151 ? -4.987  4.536   43.795 1.00 91.67  ? 277 GLN   A C     1 
ATOM   965  O O     . GLN   A 1 151 ? -4.467  3.709   44.550 1.00 91.60  ? 277 GLN   A O     1 
ATOM   966  C CB    . GLN   A 1 151 ? -6.555  3.658   42.045 1.00 82.52  ? 277 GLN   A CB    1 
ATOM   967  N N     . ALA   A 1 152 ? -5.426  5.726   44.214 1.00 93.52  ? 278 ALA   A N     1 
ATOM   968  C CA    . ALA   A 1 152 ? -5.178  6.170   45.581 1.00 92.22  ? 278 ALA   A CA    1 
ATOM   969  C C     . ALA   A 1 152 ? -5.854  5.273   46.606 1.00 92.61  ? 278 ALA   A C     1 
ATOM   970  O O     . ALA   A 1 152 ? -5.371  5.156   47.736 1.00 96.58  ? 278 ALA   A O     1 
ATOM   971  C CB    . ALA   A 1 152 ? -5.645  7.615   45.757 1.00 97.92  ? 278 ALA   A CB    1 
ATOM   972  N N     . ALA   A 1 153 ? -6.965  4.634   46.243 1.00 96.83  ? 279 ALA   A N     1 
ATOM   973  C CA    . ALA   A 1 153 ? -7.667  3.787   47.202 1.00 101.12 ? 279 ALA   A CA    1 
ATOM   974  C C     . ALA   A 1 153 ? -6.800  2.609   47.631 1.00 99.32  ? 279 ALA   A C     1 
ATOM   975  O O     . ALA   A 1 153 ? -6.571  2.393   48.828 1.00 99.20  ? 279 ALA   A O     1 
ATOM   976  C CB    . ALA   A 1 153 ? -8.990  3.301   46.606 1.00 98.35  ? 279 ALA   A CB    1 
ATOM   977  N N     . ARG   A 1 154 ? -6.305  1.835   46.663 1.00 92.40  ? 280 ARG   A N     1 
ATOM   978  C CA    . ARG   A 1 154 ? -5.493  0.671   46.997 1.00 89.94  ? 280 ARG   A CA    1 
ATOM   979  C C     . ARG   A 1 154 ? -4.122  1.077   47.515 1.00 86.91  ? 280 ARG   A C     1 
ATOM   980  O O     . ARG   A 1 154 ? -3.525  0.349   48.317 1.00 85.31  ? 280 ARG   A O     1 
ATOM   981  C CB    . ARG   A 1 154 ? -5.353  -0.243  45.779 1.00 84.49  ? 280 ARG   A CB    1 
ATOM   982  N N     . VAL   A 1 155 ? -3.612  2.230   47.078 1.00 87.40  ? 281 VAL   A N     1 
ATOM   983  C CA    . VAL   A 1 155 ? -2.303  2.681   47.539 1.00 85.02  ? 281 VAL   A CA    1 
ATOM   984  C C     . VAL   A 1 155 ? -2.370  3.116   48.998 1.00 87.61  ? 281 VAL   A C     1 
ATOM   985  O O     . VAL   A 1 155 ? -1.447  2.857   49.777 1.00 80.56  ? 281 VAL   A O     1 
ATOM   986  C CB    . VAL   A 1 155 ? -1.776  3.810   46.635 1.00 83.49  ? 281 VAL   A CB    1 
ATOM   987  N N     . MET   A 1 156 ? -3.459  3.782   49.389 1.00 92.12  ? 282 MET   A N     1 
ATOM   988  C CA    . MET   A 1 156 ? -3.622  4.216   50.775 1.00 88.35  ? 282 MET   A CA    1 
ATOM   989  C C     . MET   A 1 156 ? -3.656  3.027   51.726 1.00 86.15  ? 282 MET   A C     1 
ATOM   990  O O     . MET   A 1 156 ? -2.925  2.991   52.721 1.00 84.55  ? 282 MET   A O     1 
ATOM   991  C CB    . MET   A 1 156 ? -4.900  5.047   50.906 1.00 93.83  ? 282 MET   A CB    1 
ATOM   992  C CG    . MET   A 1 156 ? -5.447  5.187   52.322 1.00 93.73  ? 282 MET   A CG    1 
ATOM   993  S SD    . MET   A 1 156 ? -4.679  6.538   53.236 1.00 97.48  ? 282 MET   A SD    1 
ATOM   994  C CE    . MET   A 1 156 ? -4.602  7.799   51.966 1.00 78.65  ? 282 MET   A CE    1 
ATOM   995  N N     . GLY   A 1 157 ? -4.493  2.032   51.426 1.00 95.03  ? 283 GLY   A N     1 
ATOM   996  C CA    . GLY   A 1 157 ? -4.739  0.945   52.359 1.00 95.89  ? 283 GLY   A CA    1 
ATOM   997  C C     . GLY   A 1 157 ? -3.578  -0.009  52.547 1.00 97.95  ? 283 GLY   A C     1 
ATOM   998  O O     . GLY   A 1 157 ? -3.506  -0.677  53.583 1.00 95.56  ? 283 GLY   A O     1 
ATOM   999  N N     . GLU   A 1 158 ? -2.681  -0.107  51.564 1.00 85.80  ? 284 GLU   A N     1 
ATOM   1000 C CA    . GLU   A 1 158 ? -1.496  -0.945  51.704 1.00 82.19  ? 284 GLU   A CA    1 
ATOM   1001 C C     . GLU   A 1 158 ? -0.297  -0.174  52.233 1.00 75.20  ? 284 GLU   A C     1 
ATOM   1002 O O     . GLU   A 1 158 ? 0.594   -0.772  52.847 1.00 72.66  ? 284 GLU   A O     1 
ATOM   1003 C CB    . GLU   A 1 158 ? -1.137  -1.586  50.359 1.00 81.76  ? 284 GLU   A CB    1 
ATOM   1004 N N     . LEU   A 1 159 ? -0.270  1.137   52.029 1.00 72.32  ? 285 LEU   A N     1 
ATOM   1005 C CA    . LEU   A 1 159 ? 0.849   1.960   52.451 1.00 68.40  ? 285 LEU   A CA    1 
ATOM   1006 C C     . LEU   A 1 159 ? 0.687   2.467   53.876 1.00 63.51  ? 285 LEU   A C     1 
ATOM   1007 O O     . LEU   A 1 159 ? 1.671   2.536   54.623 1.00 58.09  ? 285 LEU   A O     1 
ATOM   1008 C CB    . LEU   A 1 159 ? 1.002   3.144   51.501 1.00 66.58  ? 285 LEU   A CB    1 
ATOM   1009 C CG    . LEU   A 1 159 ? 2.376   3.786   51.474 1.00 60.88  ? 285 LEU   A CG    1 
ATOM   1010 C CD1   . LEU   A 1 159 ? 3.374   2.720   51.107 1.00 60.68  ? 285 LEU   A CD1   1 
ATOM   1011 C CD2   . LEU   A 1 159 ? 2.371   4.897   50.454 1.00 54.97  ? 285 LEU   A CD2   1 
ATOM   1012 N N     . LEU   A 1 160 ? -0.532  2.846   54.253 1.00 64.01  ? 286 LEU   A N     1 
ATOM   1013 C CA    . LEU   A 1 160 ? -0.787  3.342   55.604 1.00 62.14  ? 286 LEU   A CA    1 
ATOM   1014 C C     . LEU   A 1 160 ? -0.281  2.404   56.693 1.00 60.61  ? 286 LEU   A C     1 
ATOM   1015 O O     . LEU   A 1 160 ? 0.382   2.887   57.625 1.00 59.70  ? 286 LEU   A O     1 
ATOM   1016 C CB    . LEU   A 1 160 ? -2.289  3.616   55.775 1.00 65.21  ? 286 LEU   A CB    1 
ATOM   1017 C CG    . LEU   A 1 160 ? -2.771  3.957   57.188 1.00 64.03  ? 286 LEU   A CG    1 
ATOM   1018 C CD1   . LEU   A 1 160 ? -2.097  5.226   57.692 1.00 59.31  ? 286 LEU   A CD1   1 
ATOM   1019 C CD2   . LEU   A 1 160 ? -4.289  4.097   57.220 1.00 60.84  ? 286 LEU   A CD2   1 
ATOM   1020 N N     . PRO   A 1 161 ? -0.528  1.089   56.648 1.00 59.17  ? 287 PRO   A N     1 
ATOM   1021 C CA    . PRO   A 1 161 ? -0.001  0.228   57.717 1.00 60.95  ? 287 PRO   A CA    1 
ATOM   1022 C C     . PRO   A 1 161 ? 1.509   0.247   57.797 1.00 59.64  ? 287 PRO   A C     1 
ATOM   1023 O O     . PRO   A 1 161 ? 2.057   0.143   58.900 1.00 56.21  ? 287 PRO   A O     1 
ATOM   1024 C CB    . PRO   A 1 161 ? -0.540  -1.163  57.348 1.00 60.81  ? 287 PRO   A CB    1 
ATOM   1025 C CG    . PRO   A 1 161 ? -0.813  -1.092  55.880 1.00 67.42  ? 287 PRO   A CG    1 
ATOM   1026 C CD    . PRO   A 1 161 ? -1.294  0.310   55.656 1.00 67.39  ? 287 PRO   A CD    1 
ATOM   1027 N N     . ARG   A 1 162 ? 2.199   0.404   56.664 1.00 56.29  ? 288 ARG   A N     1 
ATOM   1028 C CA    . ARG   A 1 162 ? 3.659   0.431   56.689 1.00 56.66  ? 288 ARG   A CA    1 
ATOM   1029 C C     . ARG   A 1 162 ? 4.185   1.742   57.267 1.00 53.86  ? 288 ARG   A C     1 
ATOM   1030 O O     . ARG   A 1 162 ? 5.099   1.735   58.103 1.00 53.39  ? 288 ARG   A O     1 
ATOM   1031 C CB    . ARG   A 1 162 ? 4.213   0.187   55.281 1.00 55.56  ? 288 ARG   A CB    1 
ATOM   1032 C CG    . ARG   A 1 162 ? 4.326   -1.296  54.908 1.00 60.32  ? 288 ARG   A CG    1 
ATOM   1033 C CD    . ARG   A 1 162 ? 4.110   -1.508  53.408 1.00 64.12  ? 288 ARG   A CD    1 
ATOM   1034 N NE    . ARG   A 1 162 ? 4.302   -2.894  52.988 1.00 66.25  ? 288 ARG   A NE    1 
ATOM   1035 C CZ    . ARG   A 1 162 ? 5.114   -3.275  52.008 1.00 61.78  ? 288 ARG   A CZ    1 
ATOM   1036 N NH1   . ARG   A 1 162 ? 5.828   -2.395  51.317 1.00 61.95  ? 288 ARG   A NH1   1 
ATOM   1037 N NH2   . ARG   A 1 162 ? 5.202   -4.566  51.702 1.00 65.85  ? 288 ARG   A NH2   1 
ATOM   1038 N N     . VAL   A 1 163 ? 3.622   2.877   56.848 1.00 52.61  ? 289 VAL   A N     1 
ATOM   1039 C CA    . VAL   A 1 163 ? 4.091   4.150   57.383 1.00 53.65  ? 289 VAL   A CA    1 
ATOM   1040 C C     . VAL   A 1 163 ? 3.757   4.261   58.868 1.00 52.09  ? 289 VAL   A C     1 
ATOM   1041 O O     . VAL   A 1 163 ? 4.553   4.781   59.658 1.00 50.74  ? 289 VAL   A O     1 
ATOM   1042 C CB    . VAL   A 1 163 ? 3.505   5.322   56.580 1.00 48.40  ? 289 VAL   A CB    1 
ATOM   1043 C CG1   . VAL   A 1 163 ? 4.004   6.632   57.145 1.00 49.23  ? 289 VAL   A CG1   1 
ATOM   1044 C CG2   . VAL   A 1 163 ? 3.885   5.192   55.113 1.00 52.09  ? 289 VAL   A CG2   1 
ATOM   1045 N N     . LYS   A 1 164 ? 2.580   3.774   59.269 1.00 53.89  ? 290 LYS   A N     1 
ATOM   1046 C CA    . LYS   A 1 164 ? 2.214   3.783   60.684 1.00 51.20  ? 290 LYS   A CA    1 
ATOM   1047 C C     . LYS   A 1 164 ? 3.256   3.042   61.513 1.00 52.46  ? 290 LYS   A C     1 
ATOM   1048 O O     . LYS   A 1 164 ? 3.706   3.537   62.555 1.00 51.04  ? 290 LYS   A O     1 
ATOM   1049 C CB    . LYS   A 1 164 ? 0.830   3.153   60.872 1.00 61.40  ? 290 LYS   A CB    1 
ATOM   1050 C CG    . LYS   A 1 164 ? -0.013  3.732   62.032 1.00 62.78  ? 290 LYS   A CG    1 
ATOM   1051 C CD    . LYS   A 1 164 ? 0.514   3.373   63.406 1.00 63.51  ? 290 LYS   A CD    1 
ATOM   1052 C CE    . LYS   A 1 164 ? -0.417  2.395   64.137 1.00 71.81  ? 290 LYS   A CE    1 
ATOM   1053 N NZ    . LYS   A 1 164 ? -1.833  2.889   64.246 1.00 72.43  ? 290 LYS   A NZ    1 
ATOM   1054 N N     . ALA   A 1 165 ? 3.653   1.845   61.060 1.00 49.93  ? 291 ALA   A N     1 
ATOM   1055 C CA    . ALA   A 1 165 ? 4.631   1.055   61.799 1.00 54.64  ? 291 ALA   A CA    1 
ATOM   1056 C C     . ALA   A 1 165 ? 5.950   1.801   61.924 1.00 51.60  ? 291 ALA   A C     1 
ATOM   1057 O O     . ALA   A 1 165 ? 6.589   1.772   62.983 1.00 49.58  ? 291 ALA   A O     1 
ATOM   1058 C CB    . ALA   A 1 165 ? 4.839   -0.292  61.113 1.00 55.71  ? 291 ALA   A CB    1 
ATOM   1059 N N     . LEU   A 1 166 ? 6.370   2.482   60.851 1.00 50.34  ? 292 LEU   A N     1 
ATOM   1060 C CA    . LEU   A 1 166 ? 7.576   3.299   60.921 1.00 49.44  ? 292 LEU   A CA    1 
ATOM   1061 C C     . LEU   A 1 166 ? 7.380   4.485   61.854 1.00 46.71  ? 292 LEU   A C     1 
ATOM   1062 O O     . LEU   A 1 166 ? 8.277   4.822   62.632 1.00 45.26  ? 292 LEU   A O     1 
ATOM   1063 C CB    . LEU   A 1 166 ? 7.968   3.786   59.526 1.00 48.28  ? 292 LEU   A CB    1 
ATOM   1064 C CG    . LEU   A 1 166 ? 8.278   2.714   58.475 1.00 49.87  ? 292 LEU   A CG    1 
ATOM   1065 C CD1   . LEU   A 1 166 ? 8.583   3.359   57.140 1.00 46.98  ? 292 LEU   A CD1   1 
ATOM   1066 C CD2   . LEU   A 1 166 ? 9.424   1.797   58.914 1.00 49.80  ? 292 LEU   A CD2   1 
ATOM   1067 N N     . ALA   A 1 167 ? 6.221   5.142   61.780 1.00 47.96  ? 293 ALA   A N     1 
ATOM   1068 C CA    . ALA   A 1 167 ? 5.983   6.297   62.635 1.00 45.92  ? 293 ALA   A CA    1 
ATOM   1069 C C     . ALA   A 1 167 ? 5.938   5.882   64.099 1.00 46.08  ? 293 ALA   A C     1 
ATOM   1070 O O     . ALA   A 1 167 ? 6.439   6.601   64.968 1.00 47.81  ? 293 ALA   A O     1 
ATOM   1071 C CB    . ALA   A 1 167 ? 4.690   7.002   62.231 1.00 46.12  ? 293 ALA   A CB    1 
ATOM   1072 N N     . LEU   A 1 168 ? 5.369   4.711   64.385 1.00 46.98  ? 294 LEU   A N     1 
ATOM   1073 C CA    . LEU   A 1 168 ? 5.352   4.224   65.761 1.00 47.47  ? 294 LEU   A CA    1 
ATOM   1074 C C     . LEU   A 1 168 ? 6.763   3.939   66.264 1.00 49.71  ? 294 LEU   A C     1 
ATOM   1075 O O     . LEU   A 1 168 ? 7.067   4.180   67.437 1.00 48.80  ? 294 LEU   A O     1 
ATOM   1076 C CB    . LEU   A 1 168 ? 4.479   2.975   65.872 1.00 49.58  ? 294 LEU   A CB    1 
ATOM   1077 N N     . LEU   A 1 169 ? 7.635   3.414   65.396 1.00 48.02  ? 295 LEU   A N     1 
ATOM   1078 C CA    . LEU   A 1 169 ? 9.026   3.203   65.785 1.00 46.77  ? 295 LEU   A CA    1 
ATOM   1079 C C     . LEU   A 1 169 ? 9.732   4.528   66.030 1.00 47.75  ? 295 LEU   A C     1 
ATOM   1080 O O     . LEU   A 1 169 ? 10.513  4.656   66.981 1.00 44.94  ? 295 LEU   A O     1 
ATOM   1081 C CB    . LEU   A 1 169 ? 9.768   2.403   64.715 1.00 47.38  ? 295 LEU   A CB    1 
ATOM   1082 C CG    . LEU   A 1 169 ? 9.504   0.903   64.570 1.00 50.69  ? 295 LEU   A CG    1 
ATOM   1083 C CD1   . LEU   A 1 169 ? 10.376  0.332   63.459 1.00 50.50  ? 295 LEU   A CD1   1 
ATOM   1084 C CD2   . LEU   A 1 169 ? 9.710   0.124   65.892 1.00 47.25  ? 295 LEU   A CD2   1 
ATOM   1085 N N     . ALA   A 1 170 ? 9.490   5.520   65.167 1.00 42.81  ? 296 ALA   A N     1 
ATOM   1086 C CA    . ALA   A 1 170 ? 10.014  6.858   65.419 1.00 43.96  ? 296 ALA   A CA    1 
ATOM   1087 C C     . ALA   A 1 170 ? 9.449   7.431   66.708 1.00 42.46  ? 296 ALA   A C     1 
ATOM   1088 O O     . ALA   A 1 170 ? 10.172  8.067   67.482 1.00 42.45  ? 296 ALA   A O     1 
ATOM   1089 C CB    . ALA   A 1 170 ? 9.698   7.775   64.236 1.00 39.56  ? 296 ALA   A CB    1 
ATOM   1090 N N     . LYS   A 1 171 ? 8.156   7.213   66.959 1.00 44.06  ? 297 LYS   A N     1 
ATOM   1091 C CA    . LYS   A 1 171 ? 7.570   7.638   68.223 1.00 44.87  ? 297 LYS   A CA    1 
ATOM   1092 C C     . LYS   A 1 171 ? 8.276   6.982   69.399 1.00 45.87  ? 297 LYS   A C     1 
ATOM   1093 O O     . LYS   A 1 171 ? 8.576   7.649   70.395 1.00 45.98  ? 297 LYS   A O     1 
ATOM   1094 C CB    . LYS   A 1 171 ? 6.076   7.319   68.260 1.00 46.72  ? 297 LYS   A CB    1 
ATOM   1095 C CG    . LYS   A 1 171 ? 5.479   7.425   69.664 1.00 47.99  ? 297 LYS   A CG    1 
ATOM   1096 C CD    . LYS   A 1 171 ? 3.965   7.337   69.671 1.00 52.34  ? 297 LYS   A CD    1 
ATOM   1097 C CE    . LYS   A 1 171 ? 3.437   7.653   71.057 1.00 52.14  ? 297 LYS   A CE    1 
ATOM   1098 N NZ    . LYS   A 1 171 ? 2.019   7.256   71.261 1.00 58.58  ? 297 LYS   A NZ    1 
ATOM   1099 N N     . ASN   A 1 172 ? 8.557   5.678   69.296 1.00 46.70  ? 298 ASN   A N     1 
ATOM   1100 C CA    . ASN   A 1 172 ? 9.222   4.975   70.393 1.00 48.45  ? 298 ASN   A CA    1 
ATOM   1101 C C     . ASN   A 1 172 ? 10.552  5.620   70.755 1.00 46.73  ? 298 ASN   A C     1 
ATOM   1102 O O     . ASN   A 1 172 ? 10.931  5.641   71.934 1.00 51.09  ? 298 ASN   A O     1 
ATOM   1103 C CB    . ASN   A 1 172 ? 9.443   3.497   70.036 1.00 52.55  ? 298 ASN   A CB    1 
ATOM   1104 C CG    . ASN   A 1 172 ? 8.194   2.653   70.213 1.00 58.49  ? 298 ASN   A CG    1 
ATOM   1105 O OD1   . ASN   A 1 172 ? 7.344   2.939   71.066 1.00 64.89  ? 298 ASN   A OD1   1 
ATOM   1106 N ND2   . ASN   A 1 172 ? 8.084   1.588   69.420 1.00 59.66  ? 298 ASN   A ND2   1 
ATOM   1107 N N     . TYR   A 1 173 ? 11.279  6.132   69.762 1.00 47.68  ? 299 TYR   A N     1 
ATOM   1108 C CA    . TYR   A 1 173 ? 12.567  6.765   69.992 1.00 46.01  ? 299 TYR   A CA    1 
ATOM   1109 C C     . TYR   A 1 173 ? 12.474  8.279   70.101 1.00 46.17  ? 299 TYR   A C     1 
ATOM   1110 O O     . TYR   A 1 173 ? 13.480  8.923   70.414 1.00 47.29  ? 299 TYR   A O     1 
ATOM   1111 C CB    . TYR   A 1 173 ? 13.540  6.402   68.865 1.00 44.77  ? 299 TYR   A CB    1 
ATOM   1112 C CG    . TYR   A 1 173 ? 13.913  4.928   68.794 1.00 44.48  ? 299 TYR   A CG    1 
ATOM   1113 C CD1   . TYR   A 1 173 ? 14.778  4.362   69.721 1.00 47.01  ? 299 TYR   A CD1   1 
ATOM   1114 C CD2   . TYR   A 1 173 ? 13.434  4.119   67.770 1.00 47.85  ? 299 TYR   A CD2   1 
ATOM   1115 C CE1   . TYR   A 1 173 ? 15.130  3.028   69.644 1.00 50.37  ? 299 TYR   A CE1   1 
ATOM   1116 C CE2   . TYR   A 1 173 ? 13.781  2.783   67.691 1.00 49.39  ? 299 TYR   A CE2   1 
ATOM   1117 C CZ    . TYR   A 1 173 ? 14.626  2.243   68.627 1.00 49.21  ? 299 TYR   A CZ    1 
ATOM   1118 O OH    . TYR   A 1 173 ? 14.976  0.911   68.551 1.00 49.72  ? 299 TYR   A OH    1 
ATOM   1119 N N     . ASP   A 1 174 ? 11.295  8.851   69.850 1.00 42.38  ? 300 ASP   A N     1 
ATOM   1120 C CA    . ASP   A 1 174 ? 11.089  10.301  69.820 1.00 39.10  ? 300 ASP   A CA    1 
ATOM   1121 C C     . ASP   A 1 174 ? 12.040  10.973  68.831 1.00 40.61  ? 300 ASP   A C     1 
ATOM   1122 O O     . ASP   A 1 174 ? 12.762  11.912  69.158 1.00 40.39  ? 300 ASP   A O     1 
ATOM   1123 C CB    . ASP   A 1 174 ? 11.214  10.912  71.225 1.00 42.86  ? 300 ASP   A CB    1 
ATOM   1124 C CG    . ASP   A 1 174 ? 10.554  12.277  71.311 1.00 46.83  ? 300 ASP   A CG    1 
ATOM   1125 O OD1   . ASP   A 1 174 ? 9.542   12.487  70.605 1.00 46.87  ? 300 ASP   A OD1   1 
ATOM   1126 O OD2   . ASP   A 1 174 ? 11.058  13.147  72.045 1.00 49.79  ? 300 ASP   A OD2   1 
ATOM   1127 N N     . ILE   A 1 175 ? 12.029  10.480  67.594 1.00 37.98  ? 301 ILE   A N     1 
ATOM   1128 C CA    . ILE   A 1 175 ? 12.731  11.120  66.490 1.00 36.28  ? 301 ILE   A CA    1 
ATOM   1129 C C     . ILE   A 1 175 ? 11.722  11.576  65.451 1.00 39.06  ? 301 ILE   A C     1 
ATOM   1130 O O     . ILE   A 1 175 ? 10.582  11.108  65.398 1.00 37.92  ? 301 ILE   A O     1 
ATOM   1131 C CB    . ILE   A 1 175 ? 13.775  10.183  65.853 1.00 36.74  ? 301 ILE   A CB    1 
ATOM   1132 C CG1   . ILE   A 1 175 ? 13.088  9.024   65.141 1.00 39.14  ? 301 ILE   A CG1   1 
ATOM   1133 C CG2   . ILE   A 1 175 ? 14.698  9.632   66.927 1.00 37.18  ? 301 ILE   A CG2   1 
ATOM   1134 C CD1   . ILE   A 1 175 ? 14.044  8.172   64.305 1.00 39.23  ? 301 ILE   A CD1   1 
ATOM   1135 N N     . GLY   A 1 176 ? 12.166  12.512  64.618 1.00 34.02  ? 302 GLY   A N     1 
ATOM   1136 C CA    . GLY   A 1 176 ? 11.352  12.957  63.502 1.00 37.53  ? 302 GLY   A CA    1 
ATOM   1137 C C     . GLY   A 1 176 ? 11.250  11.896  62.424 1.00 35.40  ? 302 GLY   A C     1 
ATOM   1138 O O     . GLY   A 1 176 ? 12.210  11.182  62.123 1.00 33.28  ? 302 GLY   A O     1 
ATOM   1139 N N     . LEU   A 1 177 ? 10.057  11.797  61.836 1.00 37.50  ? 303 LEU   A N     1 
ATOM   1140 C CA    . LEU   A 1 177 ? 9.822   10.972  60.657 1.00 34.18  ? 303 LEU   A CA    1 
ATOM   1141 C C     . LEU   A 1 177 ? 9.146   11.874  59.644 1.00 35.62  ? 303 LEU   A C     1 
ATOM   1142 O O     . LEU   A 1 177 ? 8.025   12.333  59.871 1.00 36.48  ? 303 LEU   A O     1 
ATOM   1143 C CB    . LEU   A 1 177 ? 8.959   9.752   60.972 1.00 36.29  ? 303 LEU   A CB    1 
ATOM   1144 C CG    . LEU   A 1 177 ? 8.753   8.798   59.791 1.00 39.95  ? 303 LEU   A CG    1 
ATOM   1145 C CD1   . LEU   A 1 177 ? 8.833   7.356   60.208 1.00 43.19  ? 303 LEU   A CD1   1 
ATOM   1146 C CD2   . LEU   A 1 177 ? 7.418   9.046   59.104 1.00 45.82  ? 303 LEU   A CD2   1 
ATOM   1147 N N     . ASN   A 1 178 ? 9.838   12.155  58.552 1.00 31.53  ? 304 ASN   A N     1 
ATOM   1148 C CA    . ASN   A 1 178 ? 9.359   13.090  57.549 1.00 34.03  ? 304 ASN   A CA    1 
ATOM   1149 C C     . ASN   A 1 178 ? 8.935   12.339  56.294 1.00 34.19  ? 304 ASN   A C     1 
ATOM   1150 O O     . ASN   A 1 178 ? 9.661   11.460  55.815 1.00 35.33  ? 304 ASN   A O     1 
ATOM   1151 C CB    . ASN   A 1 178 ? 10.448  14.104  57.215 1.00 35.27  ? 304 ASN   A CB    1 
ATOM   1152 C CG    . ASN   A 1 178 ? 10.075  14.958  56.071 1.00 34.09  ? 304 ASN   A CG    1 
ATOM   1153 O OD1   . ASN   A 1 178 ? 10.369  14.634  54.928 1.00 35.00  ? 304 ASN   A OD1   1 
ATOM   1154 N ND2   . ASN   A 1 178 ? 9.404   16.055  56.358 1.00 32.90  ? 304 ASN   A ND2   1 
ATOM   1155 N N     . ILE   A 1 179 ? 7.755   12.670  55.777 1.00 32.34  ? 305 ILE   A N     1 
ATOM   1156 C CA    . ILE   A 1 179 ? 7.296   12.151  54.491 1.00 32.74  ? 305 ILE   A CA    1 
ATOM   1157 C C     . ILE   A 1 179 ? 7.734   13.133  53.406 1.00 29.92  ? 305 ILE   A C     1 
ATOM   1158 O O     . ILE   A 1 179 ? 7.255   14.268  53.362 1.00 32.45  ? 305 ILE   A O     1 
ATOM   1159 C CB    . ILE   A 1 179 ? 5.776   11.951  54.454 1.00 33.55  ? 305 ILE   A CB    1 
ATOM   1160 C CG1   . ILE   A 1 179 ? 5.344   10.858  55.421 1.00 39.52  ? 305 ILE   A CG1   1 
ATOM   1161 C CG2   . ILE   A 1 179 ? 5.348   11.562  53.030 1.00 37.00  ? 305 ILE   A CG2   1 
ATOM   1162 C CD1   . ILE   A 1 179 ? 3.862   10.584  55.361 1.00 41.54  ? 305 ILE   A CD1   1 
ATOM   1163 N N     . ASP   A 1 180 ? 8.644   12.696  52.537 1.00 31.74  ? 306 ASP   A N     1 
ATOM   1164 C CA    . ASP   A 1 180 ? 9.099   13.537  51.434 1.00 29.77  ? 306 ASP   A CA    1 
ATOM   1165 C C     . ASP   A 1 180 ? 7.993   13.710  50.396 1.00 32.20  ? 306 ASP   A C     1 
ATOM   1166 O O     . ASP   A 1 180 ? 7.070   12.901  50.293 1.00 32.84  ? 306 ASP   A O     1 
ATOM   1167 C CB    . ASP   A 1 180 ? 10.318  12.925  50.747 1.00 31.45  ? 306 ASP   A CB    1 
ATOM   1168 C CG    . ASP   A 1 180 ? 11.552  12.944  51.628 1.00 31.92  ? 306 ASP   A CG    1 
ATOM   1169 O OD1   . ASP   A 1 180 ? 11.568  13.704  52.602 1.00 32.08  ? 306 ASP   A OD1   1 
ATOM   1170 O OD2   . ASP   A 1 180 ? 12.505  12.192  51.334 1.00 34.89  ? 306 ASP   A OD2   1 
ATOM   1171 N N     . ALA   A 1 181 ? 8.113   14.775  49.614 1.00 29.86  ? 307 ALA   A N     1 
ATOM   1172 C CA    . ALA   A 1 181 ? 7.154   15.093  48.562 1.00 33.24  ? 307 ALA   A CA    1 
ATOM   1173 C C     . ALA   A 1 181 ? 7.727   14.697  47.209 1.00 33.60  ? 307 ALA   A C     1 
ATOM   1174 O O     . ALA   A 1 181 ? 8.874   15.032  46.893 1.00 31.35  ? 307 ALA   A O     1 
ATOM   1175 C CB    . ALA   A 1 181 ? 6.829   16.581  48.577 1.00 29.40  ? 307 ALA   A CB    1 
ATOM   1176 N N     . GLU   A 1 182 ? 6.934   13.987  46.414 1.00 32.64  ? 308 GLU   A N     1 
ATOM   1177 C CA    . GLU   A 1 182 ? 7.409   13.567  45.100 1.00 35.88  ? 308 GLU   A CA    1 
ATOM   1178 C C     . GLU   A 1 182 ? 6.578   14.204  43.979 1.00 36.14  ? 308 GLU   A C     1 
ATOM   1179 O O     . GLU   A 1 182 ? 6.417   15.428  43.960 1.00 32.68  ? 308 GLU   A O     1 
ATOM   1180 C CB    . GLU   A 1 182 ? 7.429   12.041  45.030 1.00 36.70  ? 308 GLU   A CB    1 
ATOM   1181 C CG    . GLU   A 1 182 ? 8.411   11.465  46.062 1.00 38.41  ? 308 GLU   A CG    1 
ATOM   1182 C CD    . GLU   A 1 182 ? 8.434   9.953   46.112 1.00 40.28  ? 308 GLU   A CD    1 
ATOM   1183 O OE1   . GLU   A 1 182 ? 9.111   9.346   45.259 1.00 41.46  ? 308 GLU   A OE1   1 
ATOM   1184 O OE2   . GLU   A 1 182 ? 7.801   9.375   47.019 1.00 38.77  ? 308 GLU   A OE2   1 
ATOM   1185 N N     . GLU   A 1 183 ? 6.060   13.409  43.040 1.00 38.51  ? 309 GLU   A N     1 
ATOM   1186 C CA    . GLU   A 1 183 ? 5.346   13.988  41.901 1.00 41.69  ? 309 GLU   A CA    1 
ATOM   1187 C C     . GLU   A 1 183 ? 4.067   14.695  42.355 1.00 40.30  ? 309 GLU   A C     1 
ATOM   1188 O O     . GLU   A 1 183 ? 3.475   14.359  43.382 1.00 43.33  ? 309 GLU   A O     1 
ATOM   1189 C CB    . GLU   A 1 183 ? 5.002   12.913  40.857 1.00 42.58  ? 309 GLU   A CB    1 
ATOM   1190 C CG    . GLU   A 1 183 ? 6.199   12.340  40.080 1.00 48.70  ? 309 GLU   A CG    1 
ATOM   1191 C CD    . GLU   A 1 183 ? 7.041   11.350  40.895 1.00 52.43  ? 309 GLU   A CD    1 
ATOM   1192 O OE1   . GLU   A 1 183 ? 6.558   10.846  41.937 1.00 50.90  ? 309 GLU   A OE1   1 
ATOM   1193 O OE2   . GLU   A 1 183 ? 8.195   11.078  40.486 1.00 57.34  ? 309 GLU   A OE2   1 
ATOM   1194 N N     . ALA   A 1 184 ? 3.625   15.670  41.548 1.00 45.60  ? 310 ALA   A N     1 
ATOM   1195 C CA    . ALA   A 1 184 ? 2.460   16.472  41.908 1.00 42.00  ? 310 ALA   A CA    1 
ATOM   1196 C C     . ALA   A 1 184 ? 1.199   15.624  42.057 1.00 41.51  ? 310 ALA   A C     1 
ATOM   1197 O O     . ALA   A 1 184 ? 0.340   15.931  42.897 1.00 42.60  ? 310 ALA   A O     1 
ATOM   1198 C CB    . ALA   A 1 184 ? 2.252   17.574  40.868 1.00 41.66  ? 310 ALA   A CB    1 
ATOM   1199 N N     . ASP   A 1 185 ? 1.075   14.550  41.288 1.00 42.54  ? 311 ASP   A N     1 
ATOM   1200 C CA    . ASP   A 1 185 ? -0.159  13.770  41.290 1.00 46.23  ? 311 ASP   A CA    1 
ATOM   1201 C C     . ASP   A 1 185 ? -0.229  12.786  42.452 1.00 49.18  ? 311 ASP   A C     1 
ATOM   1202 O O     . ASP   A 1 185 ? -1.168  11.986  42.519 1.00 51.39  ? 311 ASP   A O     1 
ATOM   1203 C CB    . ASP   A 1 185 ? -0.336  13.042  39.950 1.00 52.89  ? 311 ASP   A CB    1 
ATOM   1204 C CG    . ASP   A 1 185 ? 0.854   12.175  39.583 1.00 52.12  ? 311 ASP   A CG    1 
ATOM   1205 O OD1   . ASP   A 1 185 ? 1.696   11.909  40.461 1.00 56.37  ? 311 ASP   A OD1   1 
ATOM   1206 O OD2   . ASP   A 1 185 ? 0.946   11.762  38.407 1.00 59.53  ? 311 ASP   A OD2   1 
ATOM   1207 N N     . ARG   A 1 186 ? 0.736   12.829  43.364 1.00 45.48  ? 312 ARG   A N     1 
ATOM   1208 C CA    . ARG   A 1 186 ? 0.701   12.017  44.570 1.00 47.96  ? 312 ARG   A CA    1 
ATOM   1209 C C     . ARG   A 1 186 ? 0.545   12.856  45.830 1.00 48.81  ? 312 ARG   A C     1 
ATOM   1210 O O     . ARG   A 1 186 ? 0.444   12.290  46.920 1.00 46.51  ? 312 ARG   A O     1 
ATOM   1211 C CB    . ARG   A 1 186 ? 1.966   11.156  44.673 1.00 48.33  ? 312 ARG   A CB    1 
ATOM   1212 C CG    . ARG   A 1 186 ? 2.204   10.210  43.493 1.00 51.04  ? 312 ARG   A CG    1 
ATOM   1213 C CD    . ARG   A 1 186 ? 1.241   9.025   43.475 1.00 57.59  ? 312 ARG   A CD    1 
ATOM   1214 N NE    . ARG   A 1 186 ? -0.033  9.366   42.853 1.00 59.24  ? 312 ARG   A NE    1 
ATOM   1215 C CZ    . ARG   A 1 186 ? -0.948  8.490   42.462 1.00 61.97  ? 312 ARG   A CZ    1 
ATOM   1216 N NH1   . ARG   A 1 186 ? -0.760  7.187   42.587 1.00 69.36  ? 312 ARG   A NH1   1 
ATOM   1217 N NH2   . ARG   A 1 186 ? -2.079  8.934   41.925 1.00 63.41  ? 312 ARG   A NH2   1 
ATOM   1218 N N     . LEU   A 1 187 ? 0.515   14.186  45.700 1.00 44.76  ? 313 LEU   A N     1 
ATOM   1219 C CA    . LEU   A 1 187 ? 0.324   15.065  46.847 1.00 45.31  ? 313 LEU   A CA    1 
ATOM   1220 C C     . LEU   A 1 187 ? -0.937  14.695  47.619 1.00 50.07  ? 313 LEU   A C     1 
ATOM   1221 O O     . LEU   A 1 187 ? -0.911  14.572  48.850 1.00 47.16  ? 313 LEU   A O     1 
ATOM   1222 C CB    . LEU   A 1 187 ? 0.270   16.523  46.375 1.00 44.26  ? 313 LEU   A CB    1 
ATOM   1223 C CG    . LEU   A 1 187 ? 0.351   17.649  47.414 1.00 46.66  ? 313 LEU   A CG    1 
ATOM   1224 C CD1   . LEU   A 1 187 ? 0.829   18.941  46.776 1.00 41.77  ? 313 LEU   A CD1   1 
ATOM   1225 C CD2   . LEU   A 1 187 ? -0.989  17.883  48.091 1.00 48.93  ? 313 LEU   A CD2   1 
ATOM   1226 N N     . GLU   A 1 188 ? -2.051  14.514  46.905 1.00 48.00  ? 314 GLU   A N     1 
ATOM   1227 C CA    . GLU   A 1 188 ? -3.329  14.262  47.564 1.00 53.06  ? 314 GLU   A CA    1 
ATOM   1228 C C     . GLU   A 1 188 ? -3.308  12.963  48.356 1.00 51.33  ? 314 GLU   A C     1 
ATOM   1229 O O     . GLU   A 1 188 ? -3.867  12.893  49.455 1.00 53.81  ? 314 GLU   A O     1 
ATOM   1230 C CB    . GLU   A 1 188 ? -4.459  14.223  46.536 1.00 56.14  ? 314 GLU   A CB    1 
ATOM   1231 C CG    . GLU   A 1 188 ? -4.817  15.572  45.944 1.00 61.90  ? 314 GLU   A CG    1 
ATOM   1232 C CD    . GLU   A 1 188 ? -5.769  16.358  46.822 1.00 66.09  ? 314 GLU   A CD    1 
ATOM   1233 O OE1   . GLU   A 1 188 ? -6.338  15.765  47.767 1.00 67.79  ? 314 GLU   A OE1   1 
ATOM   1234 O OE2   . GLU   A 1 188 ? -5.949  17.568  46.563 1.00 66.84  ? 314 GLU   A OE2   1 
ATOM   1235 N N     . LEU   A 1 189 ? -2.705  11.911  47.798 1.00 50.87  ? 315 LEU   A N     1 
ATOM   1236 C CA    . LEU   A 1 189 ? -2.646  10.641  48.509 1.00 52.71  ? 315 LEU   A CA    1 
ATOM   1237 C C     . LEU   A 1 189 ? -1.798  10.769  49.768 1.00 53.08  ? 315 LEU   A C     1 
ATOM   1238 O O     . LEU   A 1 189 ? -2.194  10.318  50.849 1.00 50.52  ? 315 LEU   A O     1 
ATOM   1239 C CB    . LEU   A 1 189 ? -2.096  9.552   47.588 1.00 54.65  ? 315 LEU   A CB    1 
ATOM   1240 N N     . SER   A 1 190 ? -0.628  11.397  49.647 1.00 49.97  ? 316 SER   A N     1 
ATOM   1241 C CA    . SER   A 1 190 ? 0.223   11.569  50.817 1.00 48.24  ? 316 SER   A CA    1 
ATOM   1242 C C     . SER   A 1 190 ? -0.439  12.461  51.857 1.00 50.01  ? 316 SER   A C     1 
ATOM   1243 O O     . SER   A 1 190 ? -0.220  12.282  53.061 1.00 48.67  ? 316 SER   A O     1 
ATOM   1244 C CB    . SER   A 1 190 ? 1.573   12.147  50.403 1.00 45.57  ? 316 SER   A CB    1 
ATOM   1245 O OG    . SER   A 1 190 ? 1.420   13.474  49.947 1.00 41.79  ? 316 SER   A OG    1 
ATOM   1246 N N     . LEU   A 1 191 ? -1.271  13.401  51.415 1.00 47.84  ? 317 LEU   A N     1 
ATOM   1247 C CA    . LEU   A 1 191 ? -1.916  14.323  52.342 1.00 51.43  ? 317 LEU   A CA    1 
ATOM   1248 C C     . LEU   A 1 191 ? -2.994  13.626  53.166 1.00 51.02  ? 317 LEU   A C     1 
ATOM   1249 O O     . LEU   A 1 191 ? -3.127  13.884  54.369 1.00 50.68  ? 317 LEU   A O     1 
ATOM   1250 C CB    . LEU   A 1 191 ? -2.500  15.499  51.563 1.00 52.70  ? 317 LEU   A CB    1 
ATOM   1251 C CG    . LEU   A 1 191 ? -2.746  16.780  52.350 1.00 53.54  ? 317 LEU   A CG    1 
ATOM   1252 C CD1   . LEU   A 1 191 ? -1.493  17.209  53.115 1.00 44.74  ? 317 LEU   A CD1   1 
ATOM   1253 C CD2   . LEU   A 1 191 ? -3.188  17.858  51.394 1.00 50.44  ? 317 LEU   A CD2   1 
ATOM   1254 N N     . ASP   A 1 192 ? -3.782  12.753  52.539 1.00 48.57  ? 318 ASP   A N     1 
ATOM   1255 C CA    . ASP   A 1 192 ? -4.748  11.962  53.294 1.00 56.03  ? 318 ASP   A CA    1 
ATOM   1256 C C     . ASP   A 1 192 ? -4.048  11.000  54.249 1.00 55.56  ? 318 ASP   A C     1 
ATOM   1257 O O     . ASP   A 1 192 ? -4.575  10.704  55.329 1.00 56.57  ? 318 ASP   A O     1 
ATOM   1258 C CB    . ASP   A 1 192 ? -5.672  11.204  52.338 1.00 58.63  ? 318 ASP   A CB    1 
ATOM   1259 C CG    . ASP   A 1 192 ? -6.404  12.129  51.375 1.00 60.27  ? 318 ASP   A CG    1 
ATOM   1260 O OD1   . ASP   A 1 192 ? -6.380  13.361  51.592 1.00 60.80  ? 318 ASP   A OD1   1 
ATOM   1261 O OD2   . ASP   A 1 192 ? -6.996  11.622  50.400 1.00 63.68  ? 318 ASP   A OD2   1 
ATOM   1262 N N     . LEU   A 1 193 ? -2.856  10.526  53.874 1.00 55.40  ? 319 LEU   A N     1 
ATOM   1263 C CA    . LEU   A 1 193 ? -2.053  9.683   54.757 1.00 53.36  ? 319 LEU   A CA    1 
ATOM   1264 C C     . LEU   A 1 193 ? -1.611  10.446  55.998 1.00 50.32  ? 319 LEU   A C     1 
ATOM   1265 O O     . LEU   A 1 193 ? -1.669  9.931   57.121 1.00 50.76  ? 319 LEU   A O     1 
ATOM   1266 C CB    . LEU   A 1 193 ? -0.836  9.163   53.994 1.00 53.25  ? 319 LEU   A CB    1 
ATOM   1267 C CG    . LEU   A 1 193 ? -0.020  8.098   54.710 1.00 55.91  ? 319 LEU   A CG    1 
ATOM   1268 C CD1   . LEU   A 1 193 ? -0.856  6.848   54.806 1.00 59.12  ? 319 LEU   A CD1   1 
ATOM   1269 C CD2   . LEU   A 1 193 ? 1.297   7.822   53.988 1.00 54.76  ? 319 LEU   A CD2   1 
ATOM   1270 N N     . LEU   A 1 194 ? -1.140  11.676  55.805 1.00 49.00  ? 320 LEU   A N     1 
ATOM   1271 C CA    . LEU   A 1 194 ? -0.734  12.499  56.935 1.00 48.90  ? 320 LEU   A CA    1 
ATOM   1272 C C     . LEU   A 1 194 ? -1.907  12.766  57.868 1.00 51.69  ? 320 LEU   A C     1 
ATOM   1273 O O     . LEU   A 1 194 ? -1.744  12.774  59.093 1.00 50.90  ? 320 LEU   A O     1 
ATOM   1274 C CB    . LEU   A 1 194 ? -0.142  13.809  56.426 1.00 46.22  ? 320 LEU   A CB    1 
ATOM   1275 C CG    . LEU   A 1 194 ? 0.324   14.815  57.467 1.00 45.00  ? 320 LEU   A CG    1 
ATOM   1276 C CD1   . LEU   A 1 194 ? 1.609   14.340  58.078 1.00 42.72  ? 320 LEU   A CD1   1 
ATOM   1277 C CD2   . LEU   A 1 194 ? 0.495   16.179  56.831 1.00 41.65  ? 320 LEU   A CD2   1 
ATOM   1278 N N     . GLU   A 1 195 ? -3.097  12.986  57.309 1.00 48.81  ? 321 GLU   A N     1 
ATOM   1279 C CA    . GLU   A 1 195 ? -4.252  13.284  58.147 1.00 51.21  ? 321 GLU   A CA    1 
ATOM   1280 C C     . GLU   A 1 195 ? -4.634  12.085  59.002 1.00 54.72  ? 321 GLU   A C     1 
ATOM   1281 O O     . GLU   A 1 195 ? -4.930  12.233  60.195 1.00 53.20  ? 321 GLU   A O     1 
ATOM   1282 C CB    . GLU   A 1 195 ? -5.432  13.723  57.282 1.00 52.94  ? 321 GLU   A CB    1 
ATOM   1283 C CG    . GLU   A 1 195 ? -6.635  14.162  58.093 1.00 54.42  ? 321 GLU   A CG    1 
ATOM   1284 C CD    . GLU   A 1 195 ? -7.789  14.626  57.223 1.00 59.02  ? 321 GLU   A CD    1 
ATOM   1285 O OE1   . GLU   A 1 195 ? -7.863  14.211  56.043 1.00 61.60  ? 321 GLU   A OE1   1 
ATOM   1286 O OE2   . GLU   A 1 195 ? -8.626  15.407  57.727 1.00 65.93  ? 321 GLU   A OE2   1 
ATOM   1287 N N     . VAL   A 1 196 ? -4.630  10.886  58.414 1.00 54.42  ? 322 VAL   A N     1 
ATOM   1288 C CA    . VAL   A 1 196 ? -4.950  9.696   59.198 1.00 52.07  ? 322 VAL   A CA    1 
ATOM   1289 C C     . VAL   A 1 196 ? -3.925  9.505   60.303 1.00 54.30  ? 322 VAL   A C     1 
ATOM   1290 O O     . VAL   A 1 196 ? -4.274  9.171   61.441 1.00 55.70  ? 322 VAL   A O     1 
ATOM   1291 C CB    . VAL   A 1 196 ? -5.044  8.455   58.290 1.00 54.17  ? 322 VAL   A CB    1 
ATOM   1292 C CG1   . VAL   A 1 196 ? -5.211  7.190   59.127 1.00 54.35  ? 322 VAL   A CG1   1 
ATOM   1293 C CG2   . VAL   A 1 196 ? -6.203  8.598   57.316 1.00 55.55  ? 322 VAL   A CG2   1 
ATOM   1294 N N     . LEU   A 1 197 ? -2.645  9.727   59.993 1.00 53.92  ? 323 LEU   A N     1 
ATOM   1295 C CA    . LEU   A 1 197 ? -1.607  9.552   61.003 1.00 53.63  ? 323 LEU   A CA    1 
ATOM   1296 C C     . LEU   A 1 197 ? -1.746  10.572  62.123 1.00 53.81  ? 323 LEU   A C     1 
ATOM   1297 O O     . LEU   A 1 197 ? -1.582  10.235  63.301 1.00 53.22  ? 323 LEU   A O     1 
ATOM   1298 C CB    . LEU   A 1 197 ? -0.223  9.658   60.364 1.00 51.52  ? 323 LEU   A CB    1 
ATOM   1299 C CG    . LEU   A 1 197 ? 0.221   8.482   59.496 1.00 50.46  ? 323 LEU   A CG    1 
ATOM   1300 C CD1   . LEU   A 1 197 ? 1.623   8.731   58.966 1.00 50.82  ? 323 LEU   A CD1   1 
ATOM   1301 C CD2   . LEU   A 1 197 ? 0.170   7.182   60.276 1.00 52.41  ? 323 LEU   A CD2   1 
ATOM   1302 N N     . CYS   A 1 198 ? -2.029  11.828  61.777 1.00 53.13  ? 324 CYS   A N     1 
ATOM   1303 C CA    . CYS   A 1 198 ? -2.115  12.861  62.799 1.00 53.83  ? 324 CYS   A CA    1 
ATOM   1304 C C     . CYS   A 1 198 ? -3.354  12.703  63.661 1.00 54.54  ? 324 CYS   A C     1 
ATOM   1305 O O     . CYS   A 1 198 ? -3.387  13.230  64.777 1.00 54.88  ? 324 CYS   A O     1 
ATOM   1306 C CB    . CYS   A 1 198 ? -2.068  14.244  62.146 1.00 50.26  ? 324 CYS   A CB    1 
ATOM   1307 S SG    . CYS   A 1 198 ? -0.460  14.596  61.438 1.00 49.90  ? 324 CYS   A SG    1 
ATOM   1308 N N     . LEU   A 1 199 ? -4.355  11.967  63.184 1.00 56.13  ? 325 LEU   A N     1 
ATOM   1309 C CA    . LEU   A 1 199 ? -5.537  11.650  63.965 1.00 56.30  ? 325 LEU   A CA    1 
ATOM   1310 C C     . LEU   A 1 199 ? -5.451  10.282  64.631 1.00 57.08  ? 325 LEU   A C     1 
ATOM   1311 O O     . LEU   A 1 199 ? -6.384  9.895   65.335 1.00 57.01  ? 325 LEU   A O     1 
ATOM   1312 C CB    . LEU   A 1 199 ? -6.787  11.722  63.079 1.00 58.60  ? 325 LEU   A CB    1 
ATOM   1313 C CG    . LEU   A 1 199 ? -7.040  13.096  62.451 1.00 60.95  ? 325 LEU   A CG    1 
ATOM   1314 C CD1   . LEU   A 1 199 ? -8.235  13.051  61.501 1.00 62.47  ? 325 LEU   A CD1   1 
ATOM   1315 C CD2   . LEU   A 1 199 ? -7.255  14.135  63.550 1.00 62.79  ? 325 LEU   A CD2   1 
ATOM   1316 N N     . ASP   A 1 200 ? -4.362  9.544   64.426 1.00 56.65  ? 326 ASP   A N     1 
ATOM   1317 C CA    . ASP   A 1 200 ? -4.228  8.215   65.004 1.00 57.55  ? 326 ASP   A CA    1 
ATOM   1318 C C     . ASP   A 1 200 ? -3.778  8.332   66.454 1.00 59.98  ? 326 ASP   A C     1 
ATOM   1319 O O     . ASP   A 1 200 ? -2.772  8.987   66.749 1.00 58.60  ? 326 ASP   A O     1 
ATOM   1320 C CB    . ASP   A 1 200 ? -3.231  7.375   64.201 1.00 60.35  ? 326 ASP   A CB    1 
ATOM   1321 C CG    . ASP   A 1 200 ? -3.292  5.893   64.552 1.00 64.31  ? 326 ASP   A CG    1 
ATOM   1322 O OD1   . ASP   A 1 200 ? -3.634  5.555   65.708 1.00 67.81  ? 326 ASP   A OD1   1 
ATOM   1323 O OD2   . ASP   A 1 200 ? -3.002  5.059   63.668 1.00 67.59  ? 326 ASP   A OD2   1 
ATOM   1324 N N     . GLY   A 1 201 ? -4.524  7.688   67.353 1.00 61.36  ? 327 GLY   A N     1 
ATOM   1325 C CA    . GLY   A 1 201 ? -4.228  7.751   68.773 1.00 60.12  ? 327 GLY   A CA    1 
ATOM   1326 C C     . GLY   A 1 201 ? -2.989  6.986   69.184 1.00 62.27  ? 327 GLY   A C     1 
ATOM   1327 O O     . GLY   A 1 201 ? -2.436  7.257   70.257 1.00 63.31  ? 327 GLY   A O     1 
ATOM   1328 N N     . ASP   A 1 202 ? -2.537  6.034   68.361 1.00 61.40  ? 328 ASP   A N     1 
ATOM   1329 C CA    . ASP   A 1 202 ? -1.319  5.304   68.696 1.00 62.75  ? 328 ASP   A CA    1 
ATOM   1330 C C     . ASP   A 1 202 ? -0.085  6.202   68.663 1.00 59.40  ? 328 ASP   A C     1 
ATOM   1331 O O     . ASP   A 1 202 ? 0.942   5.847   69.250 1.00 57.54  ? 328 ASP   A O     1 
ATOM   1332 C CB    . ASP   A 1 202 ? -1.130  4.108   67.751 1.00 64.07  ? 328 ASP   A CB    1 
ATOM   1333 C CG    . ASP   A 1 202 ? -2.062  2.936   68.071 1.00 66.79  ? 328 ASP   A CG    1 
ATOM   1334 O OD1   . ASP   A 1 202 ? -2.623  2.880   69.188 1.00 67.54  ? 328 ASP   A OD1   1 
ATOM   1335 O OD2   . ASP   A 1 202 ? -2.226  2.054   67.200 1.00 68.19  ? 328 ASP   A OD2   1 
ATOM   1336 N N     . LEU   A 1 203 ? -0.166  7.363   68.014 1.00 58.33  ? 329 LEU   A N     1 
ATOM   1337 C CA    . LEU   A 1 203 ? 0.961   8.277   67.899 1.00 54.28  ? 329 LEU   A CA    1 
ATOM   1338 C C     . LEU   A 1 203 ? 0.817   9.511   68.779 1.00 52.44  ? 329 LEU   A C     1 
ATOM   1339 O O     . LEU   A 1 203 ? 1.580   10.469  68.609 1.00 54.63  ? 329 LEU   A O     1 
ATOM   1340 C CB    . LEU   A 1 203 ? 1.142   8.699   66.439 1.00 52.78  ? 329 LEU   A CB    1 
ATOM   1341 C CG    . LEU   A 1 203 ? 1.247   7.525   65.472 1.00 54.55  ? 329 LEU   A CG    1 
ATOM   1342 C CD1   . LEU   A 1 203 ? 1.197   8.019   64.020 1.00 50.52  ? 329 LEU   A CD1   1 
ATOM   1343 C CD2   . LEU   A 1 203 ? 2.518   6.726   65.739 1.00 50.54  ? 329 LEU   A CD2   1 
ATOM   1344 N N     . SER   A 1 204 ? -0.133  9.511   69.708 1.00 57.88  ? 330 SER   A N     1 
ATOM   1345 C CA    . SER   A 1 204 ? -0.400  10.688  70.523 1.00 55.26  ? 330 SER   A CA    1 
ATOM   1346 C C     . SER   A 1 204 ? 0.847   11.102  71.291 1.00 55.33  ? 330 SER   A C     1 
ATOM   1347 O O     . SER   A 1 204 ? 1.654   10.263  71.699 1.00 57.00  ? 330 SER   A O     1 
ATOM   1348 C CB    . SER   A 1 204 ? -1.552  10.409  71.492 1.00 59.05  ? 330 SER   A CB    1 
ATOM   1349 N N     . GLY   A 1 205 ? 1.008   12.413  71.471 1.00 54.17  ? 331 GLY   A N     1 
ATOM   1350 C CA    . GLY   A 1 205 ? 2.107   12.955  72.240 1.00 53.25  ? 331 GLY   A CA    1 
ATOM   1351 C C     . GLY   A 1 205 ? 3.423   13.037  71.508 1.00 53.84  ? 331 GLY   A C     1 
ATOM   1352 O O     . GLY   A 1 205 ? 4.389   13.579  72.062 1.00 55.49  ? 331 GLY   A O     1 
ATOM   1353 N N     . TRP   A 1 206 ? 3.495   12.523  70.286 1.00 48.04  ? 332 TRP   A N     1 
ATOM   1354 C CA    . TRP   A 1 206 ? 4.712   12.533  69.488 1.00 48.52  ? 332 TRP   A CA    1 
ATOM   1355 C C     . TRP   A 1 206 ? 4.564   13.564  68.382 1.00 46.28  ? 332 TRP   A C     1 
ATOM   1356 O O     . TRP   A 1 206 ? 3.652   13.466  67.552 1.00 47.49  ? 332 TRP   A O     1 
ATOM   1357 C CB    . TRP   A 1 206 ? 4.985   11.149  68.910 1.00 47.05  ? 332 TRP   A CB    1 
ATOM   1358 C CG    . TRP   A 1 206 ? 6.063   11.104  67.876 1.00 44.30  ? 332 TRP   A CG    1 
ATOM   1359 C CD1   . TRP   A 1 206 ? 7.394   11.327  68.062 1.00 43.23  ? 332 TRP   A CD1   1 
ATOM   1360 C CD2   . TRP   A 1 206 ? 5.899   10.778  66.496 1.00 45.34  ? 332 TRP   A CD2   1 
ATOM   1361 N NE1   . TRP   A 1 206 ? 8.072   11.167  66.882 1.00 42.05  ? 332 TRP   A NE1   1 
ATOM   1362 C CE2   . TRP   A 1 206 ? 7.176   10.834  65.901 1.00 42.68  ? 332 TRP   A CE2   1 
ATOM   1363 C CE3   . TRP   A 1 206 ? 4.796   10.457  65.701 1.00 44.07  ? 332 TRP   A CE3   1 
ATOM   1364 C CZ2   . TRP   A 1 206 ? 7.380   10.569  64.559 1.00 41.38  ? 332 TRP   A CZ2   1 
ATOM   1365 C CZ3   . TRP   A 1 206 ? 4.999   10.199  64.367 1.00 44.43  ? 332 TRP   A CZ3   1 
ATOM   1366 C CH2   . TRP   A 1 206 ? 6.282   10.261  63.803 1.00 43.67  ? 332 TRP   A CH2   1 
ATOM   1367 N N     . ASN   A 1 207 ? 5.458   14.550  68.371 1.00 45.10  ? 333 ASN   A N     1 
ATOM   1368 C CA    . ASN   A 1 207 ? 5.402   15.640  67.409 1.00 44.29  ? 333 ASN   A CA    1 
ATOM   1369 C C     . ASN   A 1 207 ? 6.417   15.479  66.284 1.00 41.15  ? 333 ASN   A C     1 
ATOM   1370 O O     . ASN   A 1 207 ? 6.814   16.468  65.661 1.00 41.94  ? 333 ASN   A O     1 
ATOM   1371 C CB    . ASN   A 1 207 ? 5.602   16.973  68.121 1.00 42.59  ? 333 ASN   A CB    1 
ATOM   1372 C CG    . ASN   A 1 207 ? 4.380   17.400  68.881 1.00 46.08  ? 333 ASN   A CG    1 
ATOM   1373 O OD1   . ASN   A 1 207 ? 3.253   17.093  68.484 1.00 44.02  ? 333 ASN   A OD1   1 
ATOM   1374 N ND2   . ASN   A 1 207 ? 4.585   18.094  69.994 1.00 47.20  ? 333 ASN   A ND2   1 
ATOM   1375 N N     . GLY   A 1 208 ? 6.831   14.248  66.001 1.00 39.86  ? 334 GLY   A N     1 
ATOM   1376 C CA    . GLY   A 1 208 ? 7.868   14.000  65.023 1.00 38.22  ? 334 GLY   A CA    1 
ATOM   1377 C C     . GLY   A 1 208 ? 7.390   13.773  63.612 1.00 36.69  ? 334 GLY   A C     1 
ATOM   1378 O O     . GLY   A 1 208 ? 8.216   13.631  62.702 1.00 35.32  ? 334 GLY   A O     1 
ATOM   1379 N N     . MET   A 1 209 ? 6.078   13.698  63.414 1.00 34.64  ? 335 MET   A N     1 
ATOM   1380 C CA    . MET   A 1 209 ? 5.555   13.528  62.069 1.00 36.67  ? 335 MET   A CA    1 
ATOM   1381 C C     . MET   A 1 209 ? 5.866   14.763  61.251 1.00 36.70  ? 335 MET   A C     1 
ATOM   1382 O O     . MET   A 1 209 ? 5.604   15.889  61.682 1.00 35.72  ? 335 MET   A O     1 
ATOM   1383 C CB    . MET   A 1 209 ? 4.051   13.289  62.081 1.00 41.50  ? 335 MET   A CB    1 
ATOM   1384 C CG    . MET   A 1 209 ? 3.536   12.852  60.718 1.00 41.35  ? 335 MET   A CG    1 
ATOM   1385 S SD    . MET   A 1 209 ? 4.052   11.147  60.457 1.00 53.34  ? 335 MET   A SD    1 
ATOM   1386 C CE    . MET   A 1 209 ? 4.445   11.110  58.746 1.00 46.68  ? 335 MET   A CE    1 
ATOM   1387 N N     . GLY   A 1 210 ? 6.436   14.547  60.077 1.00 33.62  ? 336 GLY   A N     1 
ATOM   1388 C CA    . GLY   A 1 210 ? 6.897   15.634  59.250 1.00 32.76  ? 336 GLY   A CA    1 
ATOM   1389 C C     . GLY   A 1 210 ? 6.358   15.471  57.847 1.00 31.80  ? 336 GLY   A C     1 
ATOM   1390 O O     . GLY   A 1 210 ? 6.036   14.369  57.404 1.00 32.28  ? 336 GLY   A O     1 
ATOM   1391 N N     . PHE   A 1 211 ? 6.265   16.594  57.146 1.00 29.12  ? 337 PHE   A N     1 
ATOM   1392 C CA    . PHE   A 1 211 ? 5.675   16.561  55.813 1.00 32.93  ? 337 PHE   A CA    1 
ATOM   1393 C C     . PHE   A 1 211 ? 6.300   17.650  54.962 1.00 29.16  ? 337 PHE   A C     1 
ATOM   1394 O O     . PHE   A 1 211 ? 6.480   18.776  55.423 1.00 34.85  ? 337 PHE   A O     1 
ATOM   1395 C CB    . PHE   A 1 211 ? 4.159   16.761  55.907 1.00 35.19  ? 337 PHE   A CB    1 
ATOM   1396 C CG    . PHE   A 1 211 ? 3.411   16.396  54.668 1.00 35.24  ? 337 PHE   A CG    1 
ATOM   1397 C CD1   . PHE   A 1 211 ? 3.042   15.083  54.436 1.00 35.59  ? 337 PHE   A CD1   1 
ATOM   1398 C CD2   . PHE   A 1 211 ? 3.060   17.363  53.744 1.00 36.31  ? 337 PHE   A CD2   1 
ATOM   1399 C CE1   . PHE   A 1 211 ? 2.328   14.745  53.319 1.00 39.67  ? 337 PHE   A CE1   1 
ATOM   1400 C CE2   . PHE   A 1 211 ? 2.342   17.022  52.620 1.00 35.50  ? 337 PHE   A CE2   1 
ATOM   1401 C CZ    . PHE   A 1 211 ? 1.984   15.713  52.407 1.00 38.63  ? 337 PHE   A CZ    1 
ATOM   1402 N N     . VAL   A 1 212 ? 6.615   17.322  53.715 1.00 31.59  ? 338 VAL   A N     1 
ATOM   1403 C CA    . VAL   A 1 212 ? 7.201   18.286  52.796 1.00 28.87  ? 338 VAL   A CA    1 
ATOM   1404 C C     . VAL   A 1 212 ? 6.093   18.891  51.960 1.00 31.16  ? 338 VAL   A C     1 
ATOM   1405 O O     . VAL   A 1 212 ? 5.190   18.180  51.494 1.00 32.60  ? 338 VAL   A O     1 
ATOM   1406 C CB    . VAL   A 1 212 ? 8.265   17.622  51.901 1.00 30.06  ? 338 VAL   A CB    1 
ATOM   1407 C CG1   . VAL   A 1 212 ? 8.909   18.667  50.995 1.00 31.09  ? 338 VAL   A CG1   1 
ATOM   1408 C CG2   . VAL   A 1 212 ? 9.298   16.948  52.769 1.00 31.81  ? 338 VAL   A CG2   1 
ATOM   1409 N N     . VAL   A 1 213 ? 6.158   20.203  51.759 1.00 30.21  ? 339 VAL   A N     1 
ATOM   1410 C CA    . VAL   A 1 213 ? 5.325   20.866  50.760 1.00 28.97  ? 339 VAL   A CA    1 
ATOM   1411 C C     . VAL   A 1 213 ? 6.249   21.602  49.813 1.00 29.85  ? 339 VAL   A C     1 
ATOM   1412 O O     . VAL   A 1 213 ? 7.244   22.192  50.247 1.00 30.76  ? 339 VAL   A O     1 
ATOM   1413 C CB    . VAL   A 1 213 ? 4.308   21.838  51.389 1.00 33.03  ? 339 VAL   A CB    1 
ATOM   1414 C CG1   . VAL   A 1 213 ? 3.272   22.241  50.344 1.00 34.42  ? 339 VAL   A CG1   1 
ATOM   1415 C CG2   . VAL   A 1 213 ? 3.629   21.186  52.571 1.00 36.36  ? 339 VAL   A CG2   1 
ATOM   1416 N N     . GLN   A 1 214 ? 5.921   21.549  48.518 1.00 30.30  ? 340 GLN   A N     1 
ATOM   1417 C CA    . GLN   A 1 214 ? 6.770   22.054  47.449 1.00 30.90  ? 340 GLN   A CA    1 
ATOM   1418 C C     . GLN   A 1 214 ? 6.190   23.376  46.977 1.00 32.97  ? 340 GLN   A C     1 
ATOM   1419 O O     . GLN   A 1 214 ? 5.038   23.422  46.520 1.00 30.34  ? 340 GLN   A O     1 
ATOM   1420 C CB    . GLN   A 1 214 ? 6.841   21.063  46.284 1.00 32.89  ? 340 GLN   A CB    1 
ATOM   1421 C CG    . GLN   A 1 214 ? 7.382   19.702  46.666 1.00 30.77  ? 340 GLN   A CG    1 
ATOM   1422 C CD    . GLN   A 1 214 ? 6.785   18.576  45.861 1.00 33.02  ? 340 GLN   A CD    1 
ATOM   1423 O OE1   . GLN   A 1 214 ? 5.559   18.471  45.714 1.00 34.16  ? 340 GLN   A OE1   1 
ATOM   1424 N NE2   . GLN   A 1 214 ? 7.649   17.717  45.320 1.00 30.33  ? 340 GLN   A NE2   1 
ATOM   1425 N N     . ALA   A 1 215 ? 6.977   24.445  47.102 1.00 29.68  ? 341 ALA   A N     1 
ATOM   1426 C CA    . ALA   A 1 215 ? 6.479   25.772  46.777 1.00 31.11  ? 341 ALA   A CA    1 
ATOM   1427 C C     . ALA   A 1 215 ? 6.371   26.011  45.281 1.00 33.54  ? 341 ALA   A C     1 
ATOM   1428 O O     . ALA   A 1 215 ? 5.731   26.984  44.881 1.00 32.40  ? 341 ALA   A O     1 
ATOM   1429 C CB    . ALA   A 1 215 ? 7.360   26.858  47.383 1.00 31.21  ? 341 ALA   A CB    1 
ATOM   1430 N N     . TYR   A 1 216 ? 6.960   25.175  44.441 1.00 29.68  ? 342 TYR   A N     1 
ATOM   1431 C CA    . TYR   A 1 216 ? 6.674   25.404  43.027 1.00 33.63  ? 342 TYR   A CA    1 
ATOM   1432 C C     . TYR   A 1 216 ? 5.281   24.926  42.644 1.00 34.66  ? 342 TYR   A C     1 
ATOM   1433 O O     . TYR   A 1 216 ? 4.862   25.156  41.513 1.00 35.32  ? 342 TYR   A O     1 
ATOM   1434 C CB    . TYR   A 1 216 ? 7.757   24.767  42.125 1.00 34.54  ? 342 TYR   A CB    1 
ATOM   1435 C CG    . TYR   A 1 216 ? 7.915   23.244  42.063 1.00 31.58  ? 342 TYR   A CG    1 
ATOM   1436 C CD1   . TYR   A 1 216 ? 7.000   22.376  42.634 1.00 33.67  ? 342 TYR   A CD1   1 
ATOM   1437 C CD2   . TYR   A 1 216 ? 9.009   22.692  41.417 1.00 32.61  ? 342 TYR   A CD2   1 
ATOM   1438 C CE1   . TYR   A 1 216 ? 7.171   21.002  42.563 1.00 33.64  ? 342 TYR   A CE1   1 
ATOM   1439 C CE2   . TYR   A 1 216 ? 9.178   21.325  41.326 1.00 31.78  ? 342 TYR   A CE2   1 
ATOM   1440 C CZ    . TYR   A 1 216 ? 8.274   20.484  41.914 1.00 31.34  ? 342 TYR   A CZ    1 
ATOM   1441 O OH    . TYR   A 1 216 ? 8.450   19.125  41.807 1.00 31.45  ? 342 TYR   A OH    1 
ATOM   1442 N N     . GLY   A 1 217 ? 4.553   24.280  43.553 1.00 32.59  ? 343 GLY   A N     1 
ATOM   1443 C CA    . GLY   A 1 217 ? 3.203   23.829  43.256 1.00 33.61  ? 343 GLY   A CA    1 
ATOM   1444 C C     . GLY   A 1 217 ? 2.167   24.902  43.555 1.00 39.53  ? 343 GLY   A C     1 
ATOM   1445 O O     . GLY   A 1 217 ? 2.262   25.624  44.547 1.00 37.41  ? 343 GLY   A O     1 
ATOM   1446 N N     . LYS   A 1 218 ? 1.159   24.978  42.688 1.00 40.13  ? 344 LYS   A N     1 
ATOM   1447 C CA    . LYS   A 1 218 ? 0.121   25.986  42.839 1.00 42.38  ? 344 LYS   A CA    1 
ATOM   1448 C C     . LYS   A 1 218 ? -0.755  25.722  44.045 1.00 41.93  ? 344 LYS   A C     1 
ATOM   1449 O O     . LYS   A 1 218 ? -1.451  26.633  44.502 1.00 39.92  ? 344 LYS   A O     1 
ATOM   1450 C CB    . LYS   A 1 218 ? -0.733  26.035  41.584 1.00 42.51  ? 344 LYS   A CB    1 
ATOM   1451 C CG    . LYS   A 1 218 ? 0.066   26.330  40.347 1.00 43.96  ? 344 LYS   A CG    1 
ATOM   1452 C CD    . LYS   A 1 218 ? -0.828  26.269  39.153 1.00 46.56  ? 344 LYS   A CD    1 
ATOM   1453 C CE    . LYS   A 1 218 ? -0.105  26.761  37.919 1.00 48.10  ? 344 LYS   A CE    1 
ATOM   1454 N NZ    . LYS   A 1 218 ? -1.042  26.689  36.784 1.00 49.01  ? 344 LYS   A NZ    1 
ATOM   1455 N N     . ARG   A 1 219 ? -0.731  24.500  44.568 1.00 41.87  ? 345 ARG   A N     1 
ATOM   1456 C CA    . ARG   A 1 219 ? -1.540  24.136  45.717 1.00 41.83  ? 345 ARG   A CA    1 
ATOM   1457 C C     . ARG   A 1 219 ? -0.849  24.436  47.035 1.00 43.28  ? 345 ARG   A C     1 
ATOM   1458 O O     . ARG   A 1 219 ? -1.513  24.440  48.078 1.00 38.49  ? 345 ARG   A O     1 
ATOM   1459 C CB    . ARG   A 1 219 ? -1.901  22.648  45.643 1.00 41.80  ? 345 ARG   A CB    1 
ATOM   1460 C CG    . ARG   A 1 219 ? -2.914  22.336  44.555 1.00 44.13  ? 345 ARG   A CG    1 
ATOM   1461 C CD    . ARG   A 1 219 ? -3.030  20.838  44.331 1.00 45.26  ? 345 ARG   A CD    1 
ATOM   1462 N NE    . ARG   A 1 219 ? -1.762  20.259  43.906 1.00 41.82  ? 345 ARG   A NE    1 
ATOM   1463 C CZ    . ARG   A 1 219 ? -1.536  18.958  43.785 1.00 43.74  ? 345 ARG   A CZ    1 
ATOM   1464 N NH1   . ARG   A 1 219 ? -2.470  18.064  44.059 1.00 45.19  ? 345 ARG   A NH1   1 
ATOM   1465 N NH2   . ARG   A 1 219 ? -0.340  18.542  43.380 1.00 37.33  ? 345 ARG   A NH2   1 
ATOM   1466 N N     . CYS   A 1 220 ? 0.450   24.723  46.992 1.00 39.60  ? 346 CYS   A N     1 
ATOM   1467 C CA    . CYS   A 1 220 ? 1.260   24.864  48.198 1.00 37.80  ? 346 CYS   A CA    1 
ATOM   1468 C C     . CYS   A 1 220 ? 0.608   25.695  49.295 1.00 39.39  ? 346 CYS   A C     1 
ATOM   1469 O O     . CYS   A 1 220 ? 0.515   25.200  50.429 1.00 38.17  ? 346 CYS   A O     1 
ATOM   1470 C CB    . CYS   A 1 220 ? 2.623   25.448  47.815 1.00 35.79  ? 346 CYS   A CB    1 
ATOM   1471 S SG    . CYS   A 1 220 ? 3.789   25.398  49.196 1.00 40.01  ? 346 CYS   A SG    1 
ATOM   1472 N N     . PRO   A 1 221 ? 0.140   26.928  49.057 1.00 38.27  ? 347 PRO   A N     1 
ATOM   1473 C CA    . PRO   A 1 221 ? -0.424  27.687  50.191 1.00 37.55  ? 347 PRO   A CA    1 
ATOM   1474 C C     . PRO   A 1 221 ? -1.648  27.032  50.799 1.00 44.26  ? 347 PRO   A C     1 
ATOM   1475 O O     . PRO   A 1 221 ? -1.823  27.048  52.022 1.00 45.57  ? 347 PRO   A O     1 
ATOM   1476 C CB    . PRO   A 1 221 ? -0.752  29.058  49.578 1.00 44.79  ? 347 PRO   A CB    1 
ATOM   1477 C CG    . PRO   A 1 221 ? -0.793  28.846  48.113 1.00 42.70  ? 347 PRO   A CG    1 
ATOM   1478 C CD    . PRO   A 1 221 ? 0.101   27.704  47.798 1.00 35.58  ? 347 PRO   A CD    1 
ATOM   1479 N N     . PHE   A 1 222 ? -2.510  26.454  49.970 1.00 38.69  ? 348 PHE   A N     1 
ATOM   1480 C CA    . PHE   A 1 222 ? -3.709  25.806  50.476 1.00 41.14  ? 348 PHE   A CA    1 
ATOM   1481 C C     . PHE   A 1 222 ? -3.392  24.494  51.170 1.00 42.44  ? 348 PHE   A C     1 
ATOM   1482 O O     . PHE   A 1 222 ? -4.073  24.122  52.145 1.00 40.65  ? 348 PHE   A O     1 
ATOM   1483 C CB    . PHE   A 1 222 ? -4.661  25.623  49.310 1.00 42.52  ? 348 PHE   A CB    1 
ATOM   1484 C CG    . PHE   A 1 222 ? -4.734  26.836  48.468 1.00 46.01  ? 348 PHE   A CG    1 
ATOM   1485 C CD1   . PHE   A 1 222 ? -5.502  27.908  48.871 1.00 44.85  ? 348 PHE   A CD1   1 
ATOM   1486 C CD2   . PHE   A 1 222 ? -3.972  26.948  47.317 1.00 45.18  ? 348 PHE   A CD2   1 
ATOM   1487 C CE1   . PHE   A 1 222 ? -5.544  29.057  48.115 1.00 52.26  ? 348 PHE   A CE1   1 
ATOM   1488 C CE2   . PHE   A 1 222 ? -4.007  28.092  46.565 1.00 46.76  ? 348 PHE   A CE2   1 
ATOM   1489 C CZ    . PHE   A 1 222 ? -4.793  29.145  46.955 1.00 48.86  ? 348 PHE   A CZ    1 
ATOM   1490 N N     . VAL   A 1 223 ? -2.362  23.790  50.691 1.00 42.42  ? 349 VAL   A N     1 
ATOM   1491 C CA    . VAL   A 1 223 ? -1.854  22.636  51.420 1.00 38.14  ? 349 VAL   A CA    1 
ATOM   1492 C C     . VAL   A 1 223 ? -1.348  23.065  52.787 1.00 39.77  ? 349 VAL   A C     1 
ATOM   1493 O O     . VAL   A 1 223 ? -1.559  22.370  53.784 1.00 40.27  ? 349 VAL   A O     1 
ATOM   1494 C CB    . VAL   A 1 223 ? -0.747  21.926  50.613 1.00 39.86  ? 349 VAL   A CB    1 
ATOM   1495 C CG1   . VAL   A 1 223 ? -0.089  20.848  51.473 1.00 40.99  ? 349 VAL   A CG1   1 
ATOM   1496 C CG2   . VAL   A 1 223 ? -1.316  21.317  49.344 1.00 39.58  ? 349 VAL   A CG2   1 
ATOM   1497 N N     . LEU   A 1 224 ? -0.680  24.218  52.862 1.00 37.82  ? 350 LEU   A N     1 
ATOM   1498 C CA    . LEU   A 1 224 ? -0.193  24.686  54.158 1.00 40.01  ? 350 LEU   A CA    1 
ATOM   1499 C C     . LEU   A 1 224 ? -1.332  25.117  55.077 1.00 39.13  ? 350 LEU   A C     1 
ATOM   1500 O O     . LEU   A 1 224 ? -1.285  24.845  56.278 1.00 43.84  ? 350 LEU   A O     1 
ATOM   1501 C CB    . LEU   A 1 224 ? 0.789   25.827  53.973 1.00 38.88  ? 350 LEU   A CB    1 
ATOM   1502 C CG    . LEU   A 1 224 ? 2.094   25.369  53.343 1.00 40.27  ? 350 LEU   A CG    1 
ATOM   1503 C CD1   . LEU   A 1 224 ? 2.890   26.575  53.051 1.00 39.72  ? 350 LEU   A CD1   1 
ATOM   1504 C CD2   . LEU   A 1 224 ? 2.846   24.452  54.302 1.00 41.12  ? 350 LEU   A CD2   1 
ATOM   1505 N N     . ASP   A 1 225 ? -2.347  25.811  54.546 1.00 40.25  ? 351 ASP   A N     1 
ATOM   1506 C CA    . ASP   A 1 225 ? -3.521  26.123  55.356 1.00 43.96  ? 351 ASP   A CA    1 
ATOM   1507 C C     . ASP   A 1 225 ? -4.126  24.851  55.926 1.00 45.44  ? 351 ASP   A C     1 
ATOM   1508 O O     . ASP   A 1 225 ? -4.562  24.815  57.084 1.00 46.55  ? 351 ASP   A O     1 
ATOM   1509 C CB    . ASP   A 1 225 ? -4.586  26.843  54.525 1.00 46.64  ? 351 ASP   A CB    1 
ATOM   1510 C CG    . ASP   A 1 225 ? -4.171  28.235  54.076 1.00 49.25  ? 351 ASP   A CG    1 
ATOM   1511 O OD1   . ASP   A 1 225 ? -3.353  28.879  54.768 1.00 51.77  ? 351 ASP   A OD1   1 
ATOM   1512 O OD2   . ASP   A 1 225 ? -4.682  28.681  53.019 1.00 50.00  ? 351 ASP   A OD2   1 
ATOM   1513 N N     . PHE   A 1 226 ? -4.181  23.801  55.108 1.00 43.93  ? 352 PHE   A N     1 
ATOM   1514 C CA    . PHE   A 1 226 ? -4.780  22.550  55.540 1.00 46.53  ? 352 PHE   A CA    1 
ATOM   1515 C C     . PHE   A 1 226 ? -3.943  21.909  56.626 1.00 44.32  ? 352 PHE   A C     1 
ATOM   1516 O O     . PHE   A 1 226 ? -4.484  21.393  57.607 1.00 48.88  ? 352 PHE   A O     1 
ATOM   1517 C CB    . PHE   A 1 226 ? -4.924  21.595  54.353 1.00 44.62  ? 352 PHE   A CB    1 
ATOM   1518 C CG    . PHE   A 1 226 ? -5.293  20.188  54.744 1.00 46.46  ? 352 PHE   A CG    1 
ATOM   1519 C CD1   . PHE   A 1 226 ? -6.617  19.838  54.959 1.00 49.90  ? 352 PHE   A CD1   1 
ATOM   1520 C CD2   . PHE   A 1 226 ? -4.316  19.215  54.900 1.00 48.34  ? 352 PHE   A CD2   1 
ATOM   1521 C CE1   . PHE   A 1 226 ? -6.965  18.542  55.323 1.00 53.48  ? 352 PHE   A CE1   1 
ATOM   1522 C CE2   . PHE   A 1 226 ? -4.657  17.919  55.269 1.00 49.77  ? 352 PHE   A CE2   1 
ATOM   1523 C CZ    . PHE   A 1 226 ? -5.981  17.584  55.480 1.00 51.30  ? 352 PHE   A CZ    1 
ATOM   1524 N N     . ILE   A 1 227 ? -2.626  21.934  56.457 1.00 39.64  ? 353 ILE   A N     1 
ATOM   1525 C CA    . ILE   A 1 227 ? -1.746  21.304  57.430 1.00 42.53  ? 353 ILE   A CA    1 
ATOM   1526 C C     . ILE   A 1 227 ? -1.726  22.099  58.727 1.00 42.95  ? 353 ILE   A C     1 
ATOM   1527 O O     . ILE   A 1 227 ? -1.765  21.523  59.820 1.00 40.04  ? 353 ILE   A O     1 
ATOM   1528 C CB    . ILE   A 1 227 ? -0.339  21.141  56.836 1.00 37.64  ? 353 ILE   A CB    1 
ATOM   1529 C CG1   . ILE   A 1 227 ? -0.348  20.112  55.705 1.00 38.44  ? 353 ILE   A CG1   1 
ATOM   1530 C CG2   . ILE   A 1 227 ? 0.665   20.707  57.919 1.00 36.22  ? 353 ILE   A CG2   1 
ATOM   1531 C CD1   . ILE   A 1 227 ? 0.965   20.045  54.946 1.00 39.52  ? 353 ILE   A CD1   1 
ATOM   1532 N N     . ILE   A 1 228 ? -1.646  23.428  58.631 1.00 40.36  ? 354 ILE   A N     1 
ATOM   1533 C CA    . ILE   A 1 228 ? -1.682  24.263  59.831 1.00 44.60  ? 354 ILE   A CA    1 
ATOM   1534 C C     . ILE   A 1 228 ? -2.946  23.986  60.633 1.00 48.06  ? 354 ILE   A C     1 
ATOM   1535 O O     . ILE   A 1 228 ? -2.896  23.772  61.850 1.00 46.77  ? 354 ILE   A O     1 
ATOM   1536 C CB    . ILE   A 1 228 ? -1.565  25.748  59.453 1.00 44.96  ? 354 ILE   A CB    1 
ATOM   1537 C CG1   . ILE   A 1 228 ? -0.202  26.010  58.799 1.00 43.19  ? 354 ILE   A CG1   1 
ATOM   1538 C CG2   . ILE   A 1 228 ? -1.774  26.632  60.677 1.00 46.54  ? 354 ILE   A CG2   1 
ATOM   1539 C CD1   . ILE   A 1 228 ? -0.052  27.400  58.221 1.00 43.34  ? 354 ILE   A CD1   1 
ATOM   1540 N N     . ASP   A 1 229 ? -4.102  23.978  59.964 1.00 44.90  ? 355 ASP   A N     1 
ATOM   1541 C CA    . ASP   A 1 229 ? -5.341  23.658  60.667 1.00 50.22  ? 355 ASP   A CA    1 
ATOM   1542 C C     . ASP   A 1 229 ? -5.325  22.228  61.201 1.00 49.93  ? 355 ASP   A C     1 
ATOM   1543 O O     . ASP   A 1 229 ? -5.846  21.960  62.290 1.00 50.00  ? 355 ASP   A O     1 
ATOM   1544 C CB    . ASP   A 1 229 ? -6.537  23.888  59.740 1.00 52.72  ? 355 ASP   A CB    1 
ATOM   1545 C CG    . ASP   A 1 229 ? -7.858  23.402  60.333 1.00 53.14  ? 355 ASP   A CG    1 
ATOM   1546 O OD1   . ASP   A 1 229 ? -8.448  24.108  61.188 1.00 59.49  ? 355 ASP   A OD1   1 
ATOM   1547 O OD2   . ASP   A 1 229 ? -8.318  22.311  59.930 1.00 56.15  ? 355 ASP   A OD2   1 
ATOM   1548 N N     . LEU   A 1 230 ? -4.731  21.296  60.452 1.00 48.04  ? 356 LEU   A N     1 
ATOM   1549 C CA    . LEU   A 1 230 ? -4.691  19.911  60.907 1.00 48.57  ? 356 LEU   A CA    1 
ATOM   1550 C C     . LEU   A 1 230 ? -3.841  19.774  62.160 1.00 46.97  ? 356 LEU   A C     1 
ATOM   1551 O O     . LEU   A 1 230 ? -4.199  19.041  63.082 1.00 48.36  ? 356 LEU   A O     1 
ATOM   1552 C CB    . LEU   A 1 230 ? -4.148  19.003  59.806 1.00 49.58  ? 356 LEU   A CB    1 
ATOM   1553 C CG    . LEU   A 1 230 ? -3.838  17.575  60.264 1.00 45.39  ? 356 LEU   A CG    1 
ATOM   1554 C CD1   . LEU   A 1 230 ? -5.104  16.862  60.682 1.00 48.80  ? 356 LEU   A CD1   1 
ATOM   1555 C CD2   . LEU   A 1 230 ? -3.127  16.797  59.169 1.00 47.70  ? 356 LEU   A CD2   1 
ATOM   1556 N N     . ALA   A 1 231 ? -2.698  20.457  62.194 1.00 44.90  ? 357 ALA   A N     1 
ATOM   1557 C CA    . ALA   A 1 231 ? -1.873  20.472  63.394 1.00 47.58  ? 357 ALA   A CA    1 
ATOM   1558 C C     . ALA   A 1 231 ? -2.632  21.057  64.579 1.00 49.56  ? 357 ALA   A C     1 
ATOM   1559 O O     . ALA   A 1 231 ? -2.618  20.497  65.684 1.00 53.52  ? 357 ALA   A O     1 
ATOM   1560 C CB    . ALA   A 1 231 ? -0.601  21.269  63.124 1.00 43.76  ? 357 ALA   A CB    1 
ATOM   1561 N N     . ARG   A 1 232 ? -3.319  22.181  64.368 1.00 51.50  ? 358 ARG   A N     1 
ATOM   1562 C CA    A ARG   A 1 232 ? -3.991  22.852  65.475 0.79 48.61  ? 358 ARG   A CA    1 
ATOM   1563 C CA    B ARG   A 1 232 ? -3.985  22.848  65.481 0.21 48.56  ? 358 ARG   A CA    1 
ATOM   1564 C C     . ARG   A 1 232 ? -5.125  22.004  66.037 1.00 52.36  ? 358 ARG   A C     1 
ATOM   1565 O O     . ARG   A 1 232 ? -5.299  21.918  67.261 1.00 53.37  ? 358 ARG   A O     1 
ATOM   1566 C CB    A ARG   A 1 232 ? -4.516  24.214  65.024 0.79 49.67  ? 358 ARG   A CB    1 
ATOM   1567 C CB    B ARG   A 1 232 ? -4.493  24.227  65.053 0.21 49.74  ? 358 ARG   A CB    1 
ATOM   1568 C CG    A ARG   A 1 232 ? -4.940  25.110  66.181 0.79 52.21  ? 358 ARG   A CG    1 
ATOM   1569 C CG    B ARG   A 1 232 ? -5.291  24.945  66.140 0.21 51.85  ? 358 ARG   A CG    1 
ATOM   1570 C CD    A ARG   A 1 232 ? -5.491  26.449  65.697 0.79 52.11  ? 358 ARG   A CD    1 
ATOM   1571 C CD    B ARG   A 1 232 ? -5.431  26.444  65.885 0.21 52.17  ? 358 ARG   A CD    1 
ATOM   1572 N NE    A ARG   A 1 232 ? -4.706  26.995  64.594 0.79 52.09  ? 358 ARG   A NE    1 
ATOM   1573 N NE    B ARG   A 1 232 ? -4.198  27.175  66.156 0.21 53.01  ? 358 ARG   A NE    1 
ATOM   1574 C CZ    A ARG   A 1 232 ? -3.670  27.810  64.742 0.79 52.98  ? 358 ARG   A CZ    1 
ATOM   1575 C CZ    B ARG   A 1 232 ? -3.377  27.635  65.221 0.21 52.52  ? 358 ARG   A CZ    1 
ATOM   1576 N NH1   A ARG   A 1 232 ? -3.238  28.173  65.944 0.79 53.83  ? 358 ARG   A NH1   1 
ATOM   1577 N NH1   B ARG   A 1 232 ? -3.630  27.464  63.933 0.21 51.72  ? 358 ARG   A NH1   1 
ATOM   1578 N NH2   A ARG   A 1 232 ? -3.053  28.274  63.658 0.79 50.89  ? 358 ARG   A NH2   1 
ATOM   1579 N NH2   B ARG   A 1 232 ? -2.278  28.288  65.588 0.21 52.18  ? 358 ARG   A NH2   1 
ATOM   1580 N N     . ARG   A 1 233 ? -5.914  21.368  65.163 1.00 50.37  ? 359 ARG   A N     1 
ATOM   1581 C CA    . ARG   A 1 233 ? -7.029  20.581  65.671 1.00 53.53  ? 359 ARG   A CA    1 
ATOM   1582 C C     . ARG   A 1 233 ? -6.600  19.196  66.141 1.00 52.93  ? 359 ARG   A C     1 
ATOM   1583 O O     . ARG   A 1 233 ? -7.258  18.622  67.009 1.00 55.58  ? 359 ARG   A O     1 
ATOM   1584 C CB    . ARG   A 1 233 ? -8.137  20.477  64.618 1.00 57.36  ? 359 ARG   A CB    1 
ATOM   1585 C CG    . ARG   A 1 233 ? -7.863  19.510  63.493 1.00 59.40  ? 359 ARG   A CG    1 
ATOM   1586 C CD    . ARG   A 1 233 ? -9.069  19.447  62.560 1.00 64.54  ? 359 ARG   A CD    1 
ATOM   1587 N NE    . ARG   A 1 233 ? -9.101  18.207  61.793 1.00 64.64  ? 359 ARG   A NE    1 
ATOM   1588 C CZ    . ARG   A 1 233 ? -8.711  18.087  60.535 1.00 60.20  ? 359 ARG   A CZ    1 
ATOM   1589 N NH1   . ARG   A 1 233 ? -8.241  19.119  59.853 1.00 60.07  ? 359 ARG   A NH1   1 
ATOM   1590 N NH2   . ARG   A 1 233 ? -8.802  16.900  59.940 1.00 66.74  ? 359 ARG   A NH2   1 
ATOM   1591 N N     . SER   A 1 234 ? -5.508  18.648  65.612 1.00 54.43  ? 360 SER   A N     1 
ATOM   1592 C CA    . SER   A 1 234 ? -5.075  17.326  66.043 1.00 56.23  ? 360 SER   A CA    1 
ATOM   1593 C C     . SER   A 1 234 ? -4.167  17.358  67.262 1.00 57.13  ? 360 SER   A C     1 
ATOM   1594 O O     . SER   A 1 234 ? -4.024  16.332  67.931 1.00 54.72  ? 360 SER   A O     1 
ATOM   1595 C CB    . SER   A 1 234 ? -4.336  16.596  64.922 1.00 50.90  ? 360 SER   A CB    1 
ATOM   1596 O OG    . SER   A 1 234 ? -3.015  17.083  64.809 1.00 50.58  ? 360 SER   A OG    1 
ATOM   1597 N N     . GLY   A 1 235 ? -3.540  18.492  67.558 1.00 54.81  ? 361 GLY   A N     1 
ATOM   1598 C CA    . GLY   A 1 235 ? -2.601  18.556  68.657 1.00 54.02  ? 361 GLY   A CA    1 
ATOM   1599 C C     . GLY   A 1 235 ? -1.231  18.027  68.319 1.00 51.66  ? 361 GLY   A C     1 
ATOM   1600 O O     . GLY   A 1 235 ? -0.410  17.847  69.227 1.00 53.04  ? 361 GLY   A O     1 
ATOM   1601 N N     . ARG   A 1 236 ? -0.962  17.761  67.046 1.00 48.12  ? 362 ARG   A N     1 
ATOM   1602 C CA    . ARG   A 1 236 ? 0.356   17.370  66.577 1.00 45.97  ? 362 ARG   A CA    1 
ATOM   1603 C C     . ARG   A 1 236 ? 1.048   18.606  66.032 1.00 46.76  ? 362 ARG   A C     1 
ATOM   1604 O O     . ARG   A 1 236 ? 0.550   19.230  65.094 1.00 49.62  ? 362 ARG   A O     1 
ATOM   1605 C CB    . ARG   A 1 236 ? 0.248   16.303  65.487 1.00 47.21  ? 362 ARG   A CB    1 
ATOM   1606 C CG    . ARG   A 1 236 ? -0.604  15.114  65.898 1.00 52.97  ? 362 ARG   A CG    1 
ATOM   1607 C CD    . ARG   A 1 236 ? 0.109   14.245  66.909 1.00 49.38  ? 362 ARG   A CD    1 
ATOM   1608 N NE    . ARG   A 1 236 ? -0.793  13.240  67.461 1.00 53.97  ? 362 ARG   A NE    1 
ATOM   1609 C CZ    . ARG   A 1 236 ? -1.103  12.101  66.855 1.00 53.16  ? 362 ARG   A CZ    1 
ATOM   1610 N NH1   . ARG   A 1 236 ? -0.564  11.769  65.690 1.00 51.29  ? 362 ARG   A NH1   1 
ATOM   1611 N NH2   . ARG   A 1 236 ? -1.984  11.283  67.425 1.00 53.29  ? 362 ARG   A NH2   1 
ATOM   1612 N N     . ARG   A 1 237 ? 2.205   18.945  66.585 1.00 43.13  ? 363 ARG   A N     1 
ATOM   1613 C CA    . ARG   A 1 237 ? 2.998   20.030  66.006 1.00 39.94  ? 363 ARG   A CA    1 
ATOM   1614 C C     . ARG   A 1 237 ? 3.727   19.494  64.775 1.00 41.67  ? 363 ARG   A C     1 
ATOM   1615 O O     . ARG   A 1 237 ? 4.883   19.064  64.840 1.00 41.70  ? 363 ARG   A O     1 
ATOM   1616 C CB    . ARG   A 1 237 ? 3.955   20.605  67.042 1.00 41.74  ? 363 ARG   A CB    1 
ATOM   1617 C CG    . ARG   A 1 237 ? 4.773   21.757  66.516 1.00 41.80  ? 363 ARG   A CG    1 
ATOM   1618 C CD    . ARG   A 1 237 ? 4.965   22.834  67.536 1.00 42.21  ? 363 ARG   A CD    1 
ATOM   1619 N NE    . ARG   A 1 237 ? 5.635   23.979  66.938 1.00 41.10  ? 363 ARG   A NE    1 
ATOM   1620 C CZ    . ARG   A 1 237 ? 6.949   24.139  66.897 1.00 42.02  ? 363 ARG   A CZ    1 
ATOM   1621 N NH1   . ARG   A 1 237 ? 7.770   23.246  67.425 1.00 39.51  ? 363 ARG   A NH1   1 
ATOM   1622 N NH2   . ARG   A 1 237 ? 7.452   25.217  66.301 1.00 40.33  ? 363 ARG   A NH2   1 
ATOM   1623 N N     . ILE   A 1 238 ? 3.043   19.533  63.625 1.00 37.46  ? 364 ILE   A N     1 
ATOM   1624 C CA    . ILE   A 1 238 ? 3.553   18.898  62.417 1.00 36.80  ? 364 ILE   A CA    1 
ATOM   1625 C C     . ILE   A 1 238 ? 4.799   19.626  61.940 1.00 37.48  ? 364 ILE   A C     1 
ATOM   1626 O O     . ILE   A 1 238 ? 4.826   20.860  61.845 1.00 35.98  ? 364 ILE   A O     1 
ATOM   1627 C CB    . ILE   A 1 238 ? 2.483   18.886  61.311 1.00 39.26  ? 364 ILE   A CB    1 
ATOM   1628 C CG1   . ILE   A 1 238 ? 1.229   18.154  61.786 1.00 43.03  ? 364 ILE   A CG1   1 
ATOM   1629 C CG2   . ILE   A 1 238 ? 3.055   18.256  60.033 1.00 34.90  ? 364 ILE   A CG2   1 
ATOM   1630 C CD1   . ILE   A 1 238 ? 0.051   18.263  60.786 1.00 41.33  ? 364 ILE   A CD1   1 
ATOM   1631 N N     . MET   A 1 239 ? 5.845   18.861  61.643 1.00 34.92  ? 365 MET   A N     1 
ATOM   1632 C CA    . MET   A 1 239 ? 7.056   19.433  61.090 1.00 30.46  ? 365 MET   A CA    1 
ATOM   1633 C C     . MET   A 1 239 ? 6.823   19.576  59.598 1.00 33.48  ? 365 MET   A C     1 
ATOM   1634 O O     . MET   A 1 239 ? 6.509   18.594  58.923 1.00 34.22  ? 365 MET   A O     1 
ATOM   1635 C CB    . MET   A 1 239 ? 8.259   18.541  61.373 1.00 34.59  ? 365 MET   A CB    1 
ATOM   1636 C CG    . MET   A 1 239 ? 8.298   17.967  62.766 1.00 40.88  ? 365 MET   A CG    1 
ATOM   1637 S SD    . MET   A 1 239 ? 9.832   17.042  63.025 1.00 39.20  ? 365 MET   A SD    1 
ATOM   1638 C CE    . MET   A 1 239 ? 9.967   16.044  61.545 1.00 37.79  ? 365 MET   A CE    1 
ATOM   1639 N N     . VAL   A 1 240 ? 6.915   20.792  59.088 1.00 31.21  ? 366 VAL   A N     1 
ATOM   1640 C CA    . VAL   A 1 240 ? 6.595   21.042  57.695 1.00 28.99  ? 366 VAL   A CA    1 
ATOM   1641 C C     . VAL   A 1 240 ? 7.866   21.526  57.037 1.00 28.53  ? 366 VAL   A C     1 
ATOM   1642 O O     . VAL   A 1 240 ? 8.352   22.620  57.347 1.00 30.16  ? 366 VAL   A O     1 
ATOM   1643 C CB    . VAL   A 1 240 ? 5.477   22.066  57.522 1.00 33.28  ? 366 VAL   A CB    1 
ATOM   1644 C CG1   . VAL   A 1 240 ? 5.289   22.308  56.040 1.00 30.10  ? 366 VAL   A CG1   1 
ATOM   1645 C CG2   . VAL   A 1 240 ? 4.210   21.558  58.154 1.00 34.64  ? 366 VAL   A CG2   1 
ATOM   1646 N N     . ARG   A 1 241 ? 8.422   20.705  56.165 1.00 26.57  ? 367 ARG   A N     1 
ATOM   1647 C CA    . ARG   A 1 241 ? 9.587   21.102  55.399 1.00 26.97  ? 367 ARG   A CA    1 
ATOM   1648 C C     . ARG   A 1 241 ? 9.114   21.769  54.118 1.00 30.19  ? 367 ARG   A C     1 
ATOM   1649 O O     . ARG   A 1 241 ? 8.487   21.124  53.265 1.00 30.45  ? 367 ARG   A O     1 
ATOM   1650 C CB    . ARG   A 1 241 ? 10.486  19.911  55.073 1.00 28.87  ? 367 ARG   A CB    1 
ATOM   1651 C CG    . ARG   A 1 241 ? 11.731  20.322  54.262 1.00 28.05  ? 367 ARG   A CG    1 
ATOM   1652 C CD    . ARG   A 1 241 ? 12.396  19.125  53.570 1.00 27.17  ? 367 ARG   A CD    1 
ATOM   1653 N NE    . ARG   A 1 241 ? 12.739  18.114  54.568 1.00 29.15  ? 367 ARG   A NE    1 
ATOM   1654 C CZ    . ARG   A 1 241 ? 12.770  16.815  54.324 1.00 30.59  ? 367 ARG   A CZ    1 
ATOM   1655 N NH1   . ARG   A 1 241 ? 12.481  16.332  53.120 1.00 29.24  ? 367 ARG   A NH1   1 
ATOM   1656 N NH2   . ARG   A 1 241 ? 13.058  15.978  55.322 1.00 30.35  ? 367 ARG   A NH2   1 
ATOM   1657 N N     . LEU   A 1 242 ? 9.422   23.046  53.982 1.00 26.30  ? 368 LEU   A N     1 
ATOM   1658 C CA    . LEU   A 1 242 ? 9.063   23.805  52.778 1.00 26.45  ? 368 LEU   A CA    1 
ATOM   1659 C C     . LEU   A 1 242 ? 10.246  23.729  51.827 1.00 27.51  ? 368 LEU   A C     1 
ATOM   1660 O O     . LEU   A 1 242 ? 11.324  24.243  52.139 1.00 26.10  ? 368 LEU   A O     1 
ATOM   1661 C CB    . LEU   A 1 242 ? 8.749   25.244  53.140 1.00 27.73  ? 368 LEU   A CB    1 
ATOM   1662 C CG    . LEU   A 1 242 ? 8.277   26.096  51.959 1.00 27.71  ? 368 LEU   A CG    1 
ATOM   1663 C CD1   . LEU   A 1 242 ? 6.894   25.632  51.541 1.00 31.91  ? 368 LEU   A CD1   1 
ATOM   1664 C CD2   . LEU   A 1 242 ? 8.285   27.565  52.346 1.00 29.85  ? 368 LEU   A CD2   1 
ATOM   1665 N N     . VAL   A 1 243 ? 10.056  23.069  50.694 1.00 26.56  ? 369 VAL   A N     1 
ATOM   1666 C CA    . VAL   A 1 243 ? 11.053  23.016  49.631 1.00 26.72  ? 369 VAL   A CA    1 
ATOM   1667 C C     . VAL   A 1 243 ? 10.480  23.747  48.431 1.00 27.60  ? 369 VAL   A C     1 
ATOM   1668 O O     . VAL   A 1 243 ? 9.270   23.911  48.308 1.00 29.43  ? 369 VAL   A O     1 
ATOM   1669 C CB    . VAL   A 1 243 ? 11.420  21.581  49.223 1.00 27.29  ? 369 VAL   A CB    1 
ATOM   1670 C CG1   . VAL   A 1 243 ? 11.896  20.800  50.459 1.00 27.47  ? 369 VAL   A CG1   1 
ATOM   1671 C CG2   . VAL   A 1 243 ? 10.221  20.911  48.569 1.00 27.81  ? 369 VAL   A CG2   1 
ATOM   1672 N N     . LYS   A 1 244 ? 11.354  24.139  47.514 1.00 26.32  ? 370 LYS   A N     1 
ATOM   1673 C CA    . LYS   A 1 244 ? 10.802  24.674  46.264 1.00 28.88  ? 370 LYS   A CA    1 
ATOM   1674 C C     . LYS   A 1 244 ? 10.296  23.555  45.376 1.00 30.77  ? 370 LYS   A C     1 
ATOM   1675 O O     . LYS   A 1 244 ? 9.210   23.662  44.800 1.00 33.17  ? 370 LYS   A O     1 
ATOM   1676 C CB    . LYS   A 1 244 ? 11.833  25.551  45.543 1.00 28.57  ? 370 LYS   A CB    1 
ATOM   1677 C CG    . LYS   A 1 244 ? 11.972  26.887  46.284 1.00 30.16  ? 370 LYS   A CG    1 
ATOM   1678 C CD    . LYS   A 1 244 ? 13.052  27.804  45.764 1.00 32.35  ? 370 LYS   A CD    1 
ATOM   1679 C CE    . LYS   A 1 244 ? 13.170  28.986  46.746 1.00 33.55  ? 370 LYS   A CE    1 
ATOM   1680 N NZ    . LYS   A 1 244 ? 14.319  29.889  46.469 1.00 32.85  ? 370 LYS   A NZ    1 
ATOM   1681 N N     . GLY   A 1 245 ? 11.044  22.458  45.279 1.00 30.26  ? 371 GLY   A N     1 
ATOM   1682 C CA    . GLY   A 1 245 ? 10.587  21.344  44.484 1.00 29.82  ? 371 GLY   A CA    1 
ATOM   1683 C C     . GLY   A 1 245 ? 11.669  20.754  43.605 1.00 30.01  ? 371 GLY   A C     1 
ATOM   1684 O O     . GLY   A 1 245 ? 12.389  21.478  42.900 1.00 29.99  ? 371 GLY   A O     1 
ATOM   1685 N N     . ALA   A 1 246 ? 11.749  19.426  43.583 1.00 27.86  ? 372 ALA   A N     1 
ATOM   1686 C CA    . ALA   A 1 246 ? 12.848  18.734  42.908 1.00 29.65  ? 372 ALA   A CA    1 
ATOM   1687 C C     . ALA   A 1 246 ? 12.519  18.214  41.508 1.00 30.96  ? 372 ALA   A C     1 
ATOM   1688 O O     . ALA   A 1 246 ? 13.441  17.797  40.785 1.00 28.93  ? 372 ALA   A O     1 
ATOM   1689 C CB    . ALA   A 1 246 ? 13.309  17.550  43.763 1.00 28.85  ? 372 ALA   A CB    1 
ATOM   1690 N N     . TYR   A 1 247 ? 11.245  18.196  41.112 1.00 30.88  ? 373 TYR   A N     1 
ATOM   1691 C CA    . TYR   A 1 247 ? 10.796  17.472  39.930 1.00 32.93  ? 373 TYR   A CA    1 
ATOM   1692 C C     . TYR   A 1 247 ? 10.272  18.393  38.840 1.00 34.48  ? 373 TYR   A C     1 
ATOM   1693 O O     . TYR   A 1 247 ? 9.409   17.989  38.074 1.00 35.52  ? 373 TYR   A O     1 
ATOM   1694 C CB    . TYR   A 1 247 ? 9.703   16.463  40.289 1.00 32.06  ? 373 TYR   A CB    1 
ATOM   1695 C CG    . TYR   A 1 247 ? 10.101  15.508  41.395 1.00 34.97  ? 373 TYR   A CG    1 
ATOM   1696 C CD1   . TYR   A 1 247 ? 10.008  15.890  42.723 1.00 35.49  ? 373 TYR   A CD1   1 
ATOM   1697 C CD2   . TYR   A 1 247 ? 10.557  14.221  41.092 1.00 36.35  ? 373 TYR   A CD2   1 
ATOM   1698 C CE1   . TYR   A 1 247 ? 10.392  15.022  43.749 1.00 35.72  ? 373 TYR   A CE1   1 
ATOM   1699 C CE2   . TYR   A 1 247 ? 10.929  13.350  42.102 1.00 36.71  ? 373 TYR   A CE2   1 
ATOM   1700 C CZ    . TYR   A 1 247 ? 10.838  13.762  43.426 1.00 36.13  ? 373 TYR   A CZ    1 
ATOM   1701 O OH    . TYR   A 1 247 ? 11.201  12.908  44.434 1.00 37.84  ? 373 TYR   A OH    1 
ATOM   1702 N N     . TRP   A 1 248 ? 10.761  19.628  38.773 1.00 36.02  ? 374 TRP   A N     1 
ATOM   1703 C CA    . TRP   A 1 248 ? 10.165  20.591  37.849 1.00 36.31  ? 374 TRP   A CA    1 
ATOM   1704 C C     . TRP   A 1 248 ? 10.203  20.086  36.412 1.00 40.74  ? 374 TRP   A C     1 
ATOM   1705 O O     . TRP   A 1 248 ? 9.169   20.022  35.737 1.00 40.50  ? 374 TRP   A O     1 
ATOM   1706 C CB    . TRP   A 1 248 ? 10.868  21.941  37.957 1.00 35.50  ? 374 TRP   A CB    1 
ATOM   1707 C CG    . TRP   A 1 248 ? 10.154  22.991  37.125 1.00 36.47  ? 374 TRP   A CG    1 
ATOM   1708 C CD1   . TRP   A 1 248 ? 9.064   23.711  37.497 1.00 36.28  ? 374 TRP   A CD1   1 
ATOM   1709 C CD2   . TRP   A 1 248 ? 10.494  23.424  35.810 1.00 39.21  ? 374 TRP   A CD2   1 
ATOM   1710 N NE1   . TRP   A 1 248 ? 8.691   24.564  36.487 1.00 39.02  ? 374 TRP   A NE1   1 
ATOM   1711 C CE2   . TRP   A 1 248 ? 9.552   24.400  35.435 1.00 39.10  ? 374 TRP   A CE2   1 
ATOM   1712 C CE3   . TRP   A 1 248 ? 11.492  23.064  34.897 1.00 41.39  ? 374 TRP   A CE3   1 
ATOM   1713 C CZ2   . TRP   A 1 248 ? 9.592   25.040  34.199 1.00 42.16  ? 374 TRP   A CZ2   1 
ATOM   1714 C CZ3   . TRP   A 1 248 ? 11.530  23.697  33.674 1.00 44.91  ? 374 TRP   A CZ3   1 
ATOM   1715 C CH2   . TRP   A 1 248 ? 10.583  24.671  33.330 1.00 45.83  ? 374 TRP   A CH2   1 
ATOM   1716 N N     . ASP   A 1 249 ? 11.384  19.699  35.931 1.00 39.11  ? 375 ASP   A N     1 
ATOM   1717 C CA    . ASP   A 1 249 ? 11.495  19.252  34.547 1.00 42.48  ? 375 ASP   A CA    1 
ATOM   1718 C C     . ASP   A 1 249 ? 10.537  18.104  34.252 1.00 41.28  ? 375 ASP   A C     1 
ATOM   1719 O O     . ASP   A 1 249 ? 9.930   18.056  33.174 1.00 46.29  ? 375 ASP   A O     1 
ATOM   1720 C CB    . ASP   A 1 249 ? 12.940  18.860  34.246 1.00 46.28  ? 375 ASP   A CB    1 
ATOM   1721 C CG    . ASP   A 1 249 ? 13.816  20.070  33.962 1.00 50.81  ? 375 ASP   A CG    1 
ATOM   1722 O OD1   . ASP   A 1 249 ? 13.597  20.725  32.923 1.00 55.35  ? 375 ASP   A OD1   1 
ATOM   1723 O OD2   . ASP   A 1 249 ? 14.709  20.384  34.783 1.00 50.69  ? 375 ASP   A OD2   1 
ATOM   1724 N N     . ALA   A 1 250 ? 10.360  17.191  35.209 1.00 44.81  ? 376 ALA   A N     1 
ATOM   1725 C CA    . ALA   A 1 250 ? 9.482   16.046  34.987 1.00 47.13  ? 376 ALA   A CA    1 
ATOM   1726 C C     . ALA   A 1 250 ? 8.011   16.450  35.002 1.00 45.68  ? 376 ALA   A C     1 
ATOM   1727 O O     . ALA   A 1 250 ? 7.214   15.929  34.212 1.00 46.65  ? 376 ALA   A O     1 
ATOM   1728 C CB    . ALA   A 1 250 ? 9.750   14.966  36.036 1.00 42.55  ? 376 ALA   A CB    1 
ATOM   1729 N N     . GLU   A 1 251 ? 7.628   17.369  35.894 1.00 41.80  ? 377 GLU   A N     1 
ATOM   1730 C CA    . GLU   A 1 251 ? 6.242   17.832  35.912 1.00 41.57  ? 377 GLU   A CA    1 
ATOM   1731 C C     . GLU   A 1 251 ? 5.872   18.536  34.614 1.00 45.81  ? 377 GLU   A C     1 
ATOM   1732 O O     . GLU   A 1 251 ? 4.763   18.354  34.099 1.00 47.77  ? 377 GLU   A O     1 
ATOM   1733 C CB    . GLU   A 1 251 ? 6.011   18.767  37.098 1.00 37.98  ? 377 GLU   A CB    1 
ATOM   1734 C CG    . GLU   A 1 251 ? 6.290   18.132  38.448 1.00 39.55  ? 377 GLU   A CG    1 
ATOM   1735 C CD    . GLU   A 1 251 ? 5.299   17.053  38.824 1.00 40.02  ? 377 GLU   A CD    1 
ATOM   1736 O OE1   . GLU   A 1 251 ? 4.348   16.800  38.060 1.00 47.71  ? 377 GLU   A OE1   1 
ATOM   1737 O OE2   . GLU   A 1 251 ? 5.469   16.451  39.908 1.00 39.85  ? 377 GLU   A OE2   1 
ATOM   1738 N N     . ILE   A 1 252 ? 6.783   19.357  34.084 1.00 45.51  ? 378 ILE   A N     1 
ATOM   1739 C CA    . ILE   A 1 252 ? 6.537   20.028  32.809 1.00 49.10  ? 378 ILE   A CA    1 
ATOM   1740 C C     . ILE   A 1 252 ? 6.322   18.999  31.709 1.00 52.14  ? 378 ILE   A C     1 
ATOM   1741 O O     . ILE   A 1 252 ? 5.376   19.096  30.918 1.00 56.18  ? 378 ILE   A O     1 
ATOM   1742 C CB    . ILE   A 1 252 ? 7.698   20.979  32.460 1.00 46.41  ? 378 ILE   A CB    1 
ATOM   1743 C CG1   . ILE   A 1 252 ? 7.790   22.102  33.483 1.00 47.50  ? 378 ILE   A CG1   1 
ATOM   1744 C CG2   . ILE   A 1 252 ? 7.542   21.532  31.032 1.00 52.22  ? 378 ILE   A CG2   1 
ATOM   1745 C CD1   . ILE   A 1 252 ? 6.493   22.844  33.672 1.00 47.81  ? 378 ILE   A CD1   1 
ATOM   1746 N N     . LYS   A 1 253 ? 7.187   17.981  31.663 1.00 49.35  ? 379 LYS   A N     1 
ATOM   1747 C CA    . LYS   A 1 253 ? 7.163   17.021  30.563 1.00 54.13  ? 379 LYS   A CA    1 
ATOM   1748 C C     . LYS   A 1 253 ? 5.983   16.064  30.667 1.00 55.30  ? 379 LYS   A C     1 
ATOM   1749 O O     . LYS   A 1 253 ? 5.441   15.640  29.642 1.00 63.23  ? 379 LYS   A O     1 
ATOM   1750 C CB    . LYS   A 1 253 ? 8.480   16.246  30.522 1.00 55.83  ? 379 LYS   A CB    1 
ATOM   1751 N N     . ARG   A 1 254 ? 5.570   15.707  31.881 1.00 55.10  ? 380 ARG   A N     1 
ATOM   1752 C CA    . ARG   A 1 254 ? 4.339   14.938  32.027 1.00 55.63  ? 380 ARG   A CA    1 
ATOM   1753 C C     . ARG   A 1 254 ? 3.117   15.785  31.696 1.00 62.92  ? 380 ARG   A C     1 
ATOM   1754 O O     . ARG   A 1 254 ? 2.146   15.275  31.125 1.00 66.79  ? 380 ARG   A O     1 
ATOM   1755 C CB    . ARG   A 1 254 ? 4.230   14.365  33.444 1.00 57.43  ? 380 ARG   A CB    1 
ATOM   1756 N N     . ALA   A 1 255 ? 3.149   17.079  32.027 1.00 60.46  ? 381 ALA   A N     1 
ATOM   1757 C CA    . ALA   A 1 255 ? 2.010   17.942  31.732 1.00 59.86  ? 381 ALA   A CA    1 
ATOM   1758 C C     . ALA   A 1 255 ? 1.843   18.144  30.233 1.00 65.95  ? 381 ALA   A C     1 
ATOM   1759 O O     . ALA   A 1 255 ? 0.727   18.065  29.705 1.00 66.70  ? 381 ALA   A O     1 
ATOM   1760 C CB    . ALA   A 1 255 ? 2.172   19.284  32.437 1.00 57.70  ? 381 ALA   A CB    1 
ATOM   1761 N N     . GLN   A 1 256 ? 2.943   18.413  29.527 1.00 62.53  ? 382 GLN   A N     1 
ATOM   1762 C CA    . GLN   A 1 256 ? 2.849   18.602  28.084 1.00 64.50  ? 382 GLN   A CA    1 
ATOM   1763 C C     . GLN   A 1 256 ? 2.412   17.326  27.376 1.00 70.78  ? 382 GLN   A C     1 
ATOM   1764 O O     . GLN   A 1 256 ? 1.709   17.394  26.362 1.00 71.75  ? 382 GLN   A O     1 
ATOM   1765 C CB    . GLN   A 1 256 ? 4.184   19.097  27.533 1.00 61.56  ? 382 GLN   A CB    1 
ATOM   1766 C CG    . GLN   A 1 256 ? 4.627   20.409  28.140 1.00 63.19  ? 382 GLN   A CG    1 
ATOM   1767 C CD    . GLN   A 1 256 ? 5.797   21.026  27.412 1.00 62.43  ? 382 GLN   A CD    1 
ATOM   1768 O OE1   . GLN   A 1 256 ? 5.615   21.857  26.516 1.00 71.14  ? 382 GLN   A OE1   1 
ATOM   1769 N NE2   . GLN   A 1 256 ? 7.008   20.629  27.790 1.00 60.85  ? 382 GLN   A NE2   1 
ATOM   1770 N N     . LEU   A 1 257 ? 2.794   16.158  27.901 1.00 69.14  ? 383 LEU   A N     1 
ATOM   1771 C CA    . LEU   A 1 257 ? 2.383   14.899  27.283 1.00 75.83  ? 383 LEU   A CA    1 
ATOM   1772 C C     . LEU   A 1 257 ? 0.896   14.636  27.503 1.00 79.13  ? 383 LEU   A C     1 
ATOM   1773 O O     . LEU   A 1 257 ? 0.155   14.366  26.550 1.00 77.29  ? 383 LEU   A O     1 
ATOM   1774 C CB    . LEU   A 1 257 ? 3.221   13.746  27.833 1.00 73.25  ? 383 LEU   A CB    1 
ATOM   1775 N N     . ASP   A 1 258 ? 0.443   14.709  28.753 1.00 80.74  ? 384 ASP   A N     1 
ATOM   1776 C CA    . ASP   A 1 258 ? -0.972  14.531  29.071 1.00 82.02  ? 384 ASP   A CA    1 
ATOM   1777 C C     . ASP   A 1 258 ? -1.771  15.801  28.770 1.00 82.22  ? 384 ASP   A C     1 
ATOM   1778 O O     . ASP   A 1 258 ? -1.705  16.351  27.664 1.00 80.61  ? 384 ASP   A O     1 
ATOM   1779 C CB    . ASP   A 1 258 ? -1.145  14.135  30.543 1.00 84.54  ? 384 ASP   A CB    1 
ATOM   1780 N N     . ALA   A 1 261 ? -3.914  21.762  29.251 1.00 84.78  ? 387 ALA   A N     1 
ATOM   1781 C CA    . ALA   A 1 261 ? -2.567  22.316  29.232 1.00 86.97  ? 387 ALA   A CA    1 
ATOM   1782 C C     . ALA   A 1 261 ? -2.411  23.406  30.283 1.00 85.43  ? 387 ALA   A C     1 
ATOM   1783 O O     . ALA   A 1 261 ? -2.095  24.552  29.956 1.00 84.85  ? 387 ALA   A O     1 
ATOM   1784 C CB    . ALA   A 1 261 ? -2.232  22.861  27.856 1.00 93.76  ? 387 ALA   A CB    1 
ATOM   1785 N N     . ASP   A 1 262 ? -2.658  23.041  31.540 1.00 78.79  ? 388 ASP   A N     1 
ATOM   1786 C CA    . ASP   A 1 262 ? -2.356  23.885  32.690 1.00 68.22  ? 388 ASP   A CA    1 
ATOM   1787 C C     . ASP   A 1 262 ? -1.524  23.071  33.665 1.00 67.75  ? 388 ASP   A C     1 
ATOM   1788 O O     . ASP   A 1 262 ? -1.933  21.987  34.096 1.00 70.16  ? 388 ASP   A O     1 
ATOM   1789 C CB    . ASP   A 1 262 ? -3.625  24.405  33.373 1.00 73.95  ? 388 ASP   A CB    1 
ATOM   1790 N N     . PHE   A 1 263 ? -0.380  23.586  34.001 1.00 62.10  ? 389 PHE   A N     1 
ATOM   1791 C CA    . PHE   A 1 263 ? 0.570   22.839  34.792 1.00 51.05  ? 389 PHE   A CA    1 
ATOM   1792 C C     . PHE   A 1 263 ? 0.210   22.925  36.275 1.00 54.19  ? 389 PHE   A C     1 
ATOM   1793 O O     . PHE   A 1 263 ? -0.394  23.905  36.719 1.00 53.08  ? 389 PHE   A O     1 
ATOM   1794 C CB    . PHE   A 1 263 ? 1.977   23.377  34.553 1.00 52.61  ? 389 PHE   A CB    1 
ATOM   1795 C CG    . PHE   A 1 263 ? 2.367   23.420  33.094 1.00 56.03  ? 389 PHE   A CG    1 
ATOM   1796 C CD1   . PHE   A 1 263 ? 1.903   24.427  32.262 1.00 59.18  ? 389 PHE   A CD1   1 
ATOM   1797 C CD2   . PHE   A 1 263 ? 3.205   22.463  32.563 1.00 57.32  ? 389 PHE   A CD2   1 
ATOM   1798 C CE1   . PHE   A 1 263 ? 2.253   24.463  30.916 1.00 60.83  ? 389 PHE   A CE1   1 
ATOM   1799 C CE2   . PHE   A 1 263 ? 3.566   22.494  31.221 1.00 54.20  ? 389 PHE   A CE2   1 
ATOM   1800 C CZ    . PHE   A 1 263 ? 3.084   23.495  30.397 1.00 57.93  ? 389 PHE   A CZ    1 
ATOM   1801 N N     . PRO   A 1 264 ? 0.540   21.894  37.056 1.00 48.11  ? 390 PRO   A N     1 
ATOM   1802 C CA    . PRO   A 1 264 ? 0.355   21.986  38.514 1.00 45.55  ? 390 PRO   A CA    1 
ATOM   1803 C C     . PRO   A 1 264 ? 1.482   22.730  39.202 1.00 44.06  ? 390 PRO   A C     1 
ATOM   1804 O O     . PRO   A 1 264 ? 1.392   22.996  40.411 1.00 39.44  ? 390 PRO   A O     1 
ATOM   1805 C CB    . PRO   A 1 264 ? 0.308   20.518  38.951 1.00 47.71  ? 390 PRO   A CB    1 
ATOM   1806 C CG    . PRO   A 1 264 ? 1.156   19.814  37.952 1.00 51.15  ? 390 PRO   A CG    1 
ATOM   1807 C CD    . PRO   A 1 264 ? 1.026   20.565  36.644 1.00 50.70  ? 390 PRO   A CD    1 
ATOM   1808 N N     . VAL   A 1 265 ? 2.524   23.090  38.463 1.00 40.66  ? 391 VAL   A N     1 
ATOM   1809 C CA    . VAL   A 1 265 ? 3.651   23.832  38.995 1.00 37.99  ? 391 VAL   A CA    1 
ATOM   1810 C C     . VAL   A 1 265 ? 3.765   25.151  38.242 1.00 40.36  ? 391 VAL   A C     1 
ATOM   1811 O O     . VAL   A 1 265 ? 3.266   25.312  37.118 1.00 40.24  ? 391 VAL   A O     1 
ATOM   1812 C CB    . VAL   A 1 265 ? 4.964   23.029  38.905 1.00 39.04  ? 391 VAL   A CB    1 
ATOM   1813 C CG1   . VAL   A 1 265 ? 4.891   21.808  39.785 1.00 37.63  ? 391 VAL   A CG1   1 
ATOM   1814 C CG2   . VAL   A 1 265 ? 5.237   22.611  37.484 1.00 37.17  ? 391 VAL   A CG2   1 
ATOM   1815 N N     . PHE   A 1 266 ? 4.442   26.105  38.875 1.00 38.23  ? 392 PHE   A N     1 
ATOM   1816 C CA    . PHE   A 1 266 ? 4.754   27.339  38.176 1.00 37.15  ? 392 PHE   A CA    1 
ATOM   1817 C C     . PHE   A 1 266 ? 5.740   27.042  37.049 1.00 40.48  ? 392 PHE   A C     1 
ATOM   1818 O O     . PHE   A 1 266 ? 6.415   26.010  37.043 1.00 39.27  ? 392 PHE   A O     1 
ATOM   1819 C CB    . PHE   A 1 266 ? 5.307   28.375  39.158 1.00 39.25  ? 392 PHE   A CB    1 
ATOM   1820 C CG    . PHE   A 1 266 ? 4.327   28.748  40.230 1.00 37.19  ? 392 PHE   A CG    1 
ATOM   1821 C CD1   . PHE   A 1 266 ? 3.128   29.363  39.909 1.00 41.39  ? 392 PHE   A CD1   1 
ATOM   1822 C CD2   . PHE   A 1 266 ? 4.581   28.441  41.553 1.00 35.99  ? 392 PHE   A CD2   1 
ATOM   1823 C CE1   . PHE   A 1 266 ? 2.218   29.691  40.905 1.00 43.22  ? 392 PHE   A CE1   1 
ATOM   1824 C CE2   . PHE   A 1 266 ? 3.673   28.760  42.540 1.00 40.42  ? 392 PHE   A CE2   1 
ATOM   1825 C CZ    . PHE   A 1 266 ? 2.496   29.387  42.219 1.00 40.40  ? 392 PHE   A CZ    1 
ATOM   1826 N N     . THR   A 1 267 ? 5.779   27.937  36.058 1.00 39.31  ? 393 THR   A N     1 
ATOM   1827 C CA    . THR   A 1 267 ? 6.689   27.792  34.934 1.00 42.68  ? 393 THR   A CA    1 
ATOM   1828 C C     . THR   A 1 267 ? 7.740   28.882  34.891 1.00 40.27  ? 393 THR   A C     1 
ATOM   1829 O O     . THR   A 1 267 ? 8.579   28.866  33.988 1.00 41.01  ? 393 THR   A O     1 
ATOM   1830 C CB    . THR   A 1 267 ? 5.939   27.802  33.599 1.00 45.94  ? 393 THR   A CB    1 
ATOM   1831 O OG1   . THR   A 1 267 ? 5.297   29.069  33.447 1.00 46.29  ? 393 THR   A OG1   1 
ATOM   1832 C CG2   . THR   A 1 267 ? 4.903   26.692  33.535 1.00 49.37  ? 393 THR   A CG2   1 
ATOM   1833 N N     . ARG   A 1 268 ? 7.694   29.840  35.814 1.00 39.31  ? 394 ARG   A N     1 
ATOM   1834 C CA    . ARG   A 1 268 ? 8.715   30.867  35.972 1.00 39.85  ? 394 ARG   A CA    1 
ATOM   1835 C C     . ARG   A 1 268 ? 9.360   30.678  37.331 1.00 37.43  ? 394 ARG   A C     1 
ATOM   1836 O O     . ARG   A 1 268 ? 8.659   30.553  38.340 1.00 39.73  ? 394 ARG   A O     1 
ATOM   1837 C CB    . ARG   A 1 268 ? 8.125   32.276  35.874 1.00 41.95  ? 394 ARG   A CB    1 
ATOM   1838 N N     . LYS   A 1 269 ? 10.691  30.627  37.356 1.00 37.00  ? 395 LYS   A N     1 
ATOM   1839 C CA    . LYS   A 1 269 ? 11.366  30.332  38.613 1.00 40.04  ? 395 LYS   A CA    1 
ATOM   1840 C C     . LYS   A 1 269 ? 11.024  31.378  39.662 1.00 38.89  ? 395 LYS   A C     1 
ATOM   1841 O O     . LYS   A 1 269 ? 10.884  31.066  40.848 1.00 38.07  ? 395 LYS   A O     1 
ATOM   1842 C CB    . LYS   A 1 269 ? 12.869  30.256  38.387 1.00 35.46  ? 395 LYS   A CB    1 
ATOM   1843 C CG    . LYS   A 1 269 ? 13.616  29.613  39.535 1.00 34.10  ? 395 LYS   A CG    1 
ATOM   1844 C CD    . LYS   A 1 269 ? 14.187  30.639  40.454 1.00 40.26  ? 395 LYS   A CD    1 
ATOM   1845 C CE    . LYS   A 1 269 ? 15.013  29.942  41.544 1.00 31.52  ? 395 LYS   A CE    1 
ATOM   1846 N NZ    . LYS   A 1 269 ? 15.392  30.923  42.565 1.00 34.73  ? 395 LYS   A NZ    1 
ATOM   1847 N N     . ILE   A 1 270 ? 10.842  32.625  39.227 1.00 40.23  ? 396 ILE   A N     1 
ATOM   1848 C CA    . ILE   A 1 270 ? 10.584  33.699  40.173 1.00 38.08  ? 396 ILE   A CA    1 
ATOM   1849 C C     . ILE   A 1 270 ? 9.232   33.517  40.857 1.00 36.85  ? 396 ILE   A C     1 
ATOM   1850 O O     . ILE   A 1 270 ? 9.062   33.912  42.012 1.00 37.89  ? 396 ILE   A O     1 
ATOM   1851 C CB    . ILE   A 1 270 ? 10.709  35.046  39.435 1.00 43.97  ? 396 ILE   A CB    1 
ATOM   1852 C CG1   . ILE   A 1 270 ? 10.535  36.210  40.403 1.00 47.74  ? 396 ILE   A CG1   1 
ATOM   1853 C CG2   . ILE   A 1 270 ? 9.710   35.132  38.283 1.00 45.74  ? 396 ILE   A CG2   1 
ATOM   1854 C CD1   . ILE   A 1 270 ? 11.520  37.323  40.164 1.00 51.67  ? 396 ILE   A CD1   1 
ATOM   1855 N N     . HIS   A 1 271 ? 8.250   32.923  40.170 1.00 38.00  ? 397 HIS   A N     1 
ATOM   1856 C CA    . HIS   A 1 271 ? 6.978   32.619  40.818 1.00 37.23  ? 397 HIS   A CA    1 
ATOM   1857 C C     . HIS   A 1 271 ? 7.143   31.579  41.920 1.00 35.41  ? 397 HIS   A C     1 
ATOM   1858 O O     . HIS   A 1 271 ? 6.475   31.655  42.957 1.00 33.14  ? 397 HIS   A O     1 
ATOM   1859 C CB    . HIS   A 1 271 ? 5.972   32.123  39.799 1.00 36.40  ? 397 HIS   A CB    1 
ATOM   1860 C CG    . HIS   A 1 271 ? 5.655   33.143  38.750 1.00 43.01  ? 397 HIS   A CG    1 
ATOM   1861 N ND1   . HIS   A 1 271 ? 4.951   32.854  37.601 1.00 45.09  ? 397 HIS   A ND1   1 
ATOM   1862 C CD2   . HIS   A 1 271 ? 5.969   34.456  38.677 1.00 45.49  ? 397 HIS   A CD2   1 
ATOM   1863 C CE1   . HIS   A 1 271 ? 4.842   33.945  36.865 1.00 47.82  ? 397 HIS   A CE1   1 
ATOM   1864 N NE2   . HIS   A 1 271 ? 5.451   34.932  37.496 1.00 45.30  ? 397 HIS   A NE2   1 
ATOM   1865 N N     . THR   A 1 272 ? 7.980   30.575  41.691 1.00 32.99  ? 398 THR   A N     1 
ATOM   1866 C CA    . THR   A 1 272 ? 8.313   29.651  42.775 1.00 30.39  ? 398 THR   A CA    1 
ATOM   1867 C C     . THR   A 1 272 ? 8.981   30.381  43.933 1.00 32.41  ? 398 THR   A C     1 
ATOM   1868 O O     . THR   A 1 272 ? 8.663   30.126  45.104 1.00 34.93  ? 398 THR   A O     1 
ATOM   1869 C CB    . THR   A 1 272 ? 9.202   28.530  42.240 1.00 30.52  ? 398 THR   A CB    1 
ATOM   1870 O OG1   . THR   A 1 272 ? 8.459   27.768  41.286 1.00 30.58  ? 398 THR   A OG1   1 
ATOM   1871 C CG2   . THR   A 1 272 ? 9.661   27.603  43.401 1.00 33.13  ? 398 THR   A CG2   1 
ATOM   1872 N N     . ASP   A 1 273 ? 9.895   31.308  43.632 1.00 33.98  ? 399 ASP   A N     1 
ATOM   1873 C CA    . ASP   A 1 273 ? 10.551  32.056  44.700 1.00 35.76  ? 399 ASP   A CA    1 
ATOM   1874 C C     . ASP   A 1 273 ? 9.541   32.873  45.489 1.00 34.96  ? 399 ASP   A C     1 
ATOM   1875 O O     . ASP   A 1 273 ? 9.591   32.911  46.721 1.00 36.81  ? 399 ASP   A O     1 
ATOM   1876 C CB    . ASP   A 1 273 ? 11.640  32.968  44.133 1.00 32.55  ? 399 ASP   A CB    1 
ATOM   1877 C CG    . ASP   A 1 273 ? 12.887  32.211  43.748 1.00 36.87  ? 399 ASP   A CG    1 
ATOM   1878 O OD1   . ASP   A 1 273 ? 13.031  31.058  44.187 1.00 39.85  ? 399 ASP   A OD1   1 
ATOM   1879 O OD2   . ASP   A 1 273 ? 13.733  32.762  43.006 1.00 39.08  ? 399 ASP   A OD2   1 
ATOM   1880 N N     . VAL   A 1 274 ? 8.608   33.534  44.795 1.00 31.22  ? 400 VAL   A N     1 
ATOM   1881 C CA    . VAL   A 1 274 ? 7.596   34.303  45.514 1.00 35.50  ? 400 VAL   A CA    1 
ATOM   1882 C C     . VAL   A 1 274 ? 6.697   33.379  46.329 1.00 36.79  ? 400 VAL   A C     1 
ATOM   1883 O O     . VAL   A 1 274 ? 6.369   33.669  47.485 1.00 36.80  ? 400 VAL   A O     1 
ATOM   1884 C CB    . VAL   A 1 274 ? 6.794   35.152  44.520 1.00 37.64  ? 400 VAL   A CB    1 
ATOM   1885 C CG1   . VAL   A 1 274 ? 5.646   35.843  45.227 1.00 42.67  ? 400 VAL   A CG1   1 
ATOM   1886 C CG2   . VAL   A 1 274 ? 7.718   36.149  43.856 1.00 41.78  ? 400 VAL   A CG2   1 
ATOM   1887 N N     . SER   A 1 275 ? 6.283   32.259  45.733 1.00 37.03  ? 401 SER   A N     1 
ATOM   1888 C CA    . SER   A 1 275 ? 5.491   31.252  46.435 1.00 34.30  ? 401 SER   A CA    1 
ATOM   1889 C C     . SER   A 1 275 ? 6.196   30.767  47.698 1.00 33.39  ? 401 SER   A C     1 
ATOM   1890 O O     . SER   A 1 275 ? 5.569   30.605  48.750 1.00 35.33  ? 401 SER   A O     1 
ATOM   1891 C CB    . SER   A 1 275 ? 5.232   30.075  45.492 1.00 37.67  ? 401 SER   A CB    1 
ATOM   1892 O OG    . SER   A 1 275 ? 4.507   29.032  46.111 1.00 35.28  ? 401 SER   A OG    1 
ATOM   1893 N N     . TYR   A 1 276 ? 7.502   30.517  47.610 1.00 34.81  ? 402 TYR   A N     1 
ATOM   1894 C CA    . TYR   A 1 276 ? 8.231   30.051  48.780 1.00 34.66  ? 402 TYR   A CA    1 
ATOM   1895 C C     . TYR   A 1 276 ? 8.151   31.069  49.913 1.00 33.06  ? 402 TYR   A C     1 
ATOM   1896 O O     . TYR   A 1 276 ? 7.855   30.718  51.060 1.00 33.92  ? 402 TYR   A O     1 
ATOM   1897 C CB    . TYR   A 1 276 ? 9.684   29.766  48.400 1.00 26.74  ? 402 TYR   A CB    1 
ATOM   1898 C CG    . TYR   A 1 276 ? 10.448  29.032  49.466 1.00 29.44  ? 402 TYR   A CG    1 
ATOM   1899 C CD1   . TYR   A 1 276 ? 10.978  29.711  50.558 1.00 29.25  ? 402 TYR   A CD1   1 
ATOM   1900 C CD2   . TYR   A 1 276 ? 10.640  27.680  49.365 1.00 28.59  ? 402 TYR   A CD2   1 
ATOM   1901 C CE1   . TYR   A 1 276 ? 11.674  29.032  51.558 1.00 29.13  ? 402 TYR   A CE1   1 
ATOM   1902 C CE2   . TYR   A 1 276 ? 11.352  26.988  50.349 1.00 28.50  ? 402 TYR   A CE2   1 
ATOM   1903 C CZ    . TYR   A 1 276 ? 11.864  27.676  51.425 1.00 27.96  ? 402 TYR   A CZ    1 
ATOM   1904 O OH    . TYR   A 1 276 ? 12.569  26.988  52.389 1.00 28.47  ? 402 TYR   A OH    1 
ATOM   1905 N N     . ILE   A 1 277 ? 8.457   32.329  49.614 1.00 30.17  ? 403 ILE   A N     1 
ATOM   1906 C CA    . ILE   A 1 277 ? 8.435   33.375  50.638 1.00 32.85  ? 403 ILE   A CA    1 
ATOM   1907 C C     . ILE   A 1 277 ? 7.028   33.545  51.191 1.00 36.18  ? 403 ILE   A C     1 
ATOM   1908 O O     . ILE   A 1 277 ? 6.832   33.692  52.404 1.00 38.04  ? 403 ILE   A O     1 
ATOM   1909 C CB    . ILE   A 1 277 ? 8.956   34.700  50.055 1.00 36.75  ? 403 ILE   A CB    1 
ATOM   1910 C CG1   . ILE   A 1 277 ? 10.403  34.531  49.575 1.00 36.55  ? 403 ILE   A CG1   1 
ATOM   1911 C CG2   . ILE   A 1 277 ? 8.784   35.847  51.067 1.00 39.73  ? 403 ILE   A CG2   1 
ATOM   1912 C CD1   . ILE   A 1 277 ? 11.367  34.232  50.667 1.00 37.94  ? 403 ILE   A CD1   1 
ATOM   1913 N N     . ALA   A 1 278 ? 6.030   33.582  50.305 1.00 38.67  ? 404 ALA   A N     1 
ATOM   1914 C CA    . ALA   A 1 278 ? 4.652   33.680  50.773 1.00 37.24  ? 404 ALA   A CA    1 
ATOM   1915 C C     . ALA   A 1 278 ? 4.343   32.552  51.744 1.00 38.95  ? 404 ALA   A C     1 
ATOM   1916 O O     . ALA   A 1 278 ? 3.768   32.771  52.813 1.00 38.09  ? 404 ALA   A O     1 
ATOM   1917 C CB    . ALA   A 1 278 ? 3.677   33.648  49.602 1.00 41.11  ? 404 ALA   A CB    1 
ATOM   1918 N N     . CYS   A 1 279 ? 4.723   31.333  51.382 1.00 36.08  ? 405 CYS   A N     1 
ATOM   1919 C CA    . CYS   A 1 279 ? 4.423   30.188  52.226 1.00 37.83  ? 405 CYS   A CA    1 
ATOM   1920 C C     . CYS   A 1 279 ? 5.254   30.200  53.504 1.00 36.99  ? 405 CYS   A C     1 
ATOM   1921 O O     . CYS   A 1 279 ? 4.801   29.704  54.541 1.00 37.59  ? 405 CYS   A O     1 
ATOM   1922 C CB    . CYS   A 1 279 ? 4.648   28.913  51.426 1.00 35.40  ? 405 CYS   A CB    1 
ATOM   1923 S SG    . CYS   A 1 279 ? 3.416   28.794  50.070 1.00 45.45  ? 405 CYS   A SG    1 
ATOM   1924 N N     . ALA   A 1 280 ? 6.466   30.754  53.447 1.00 34.87  ? 406 ALA   A N     1 
ATOM   1925 C CA    . ALA   A 1 280 ? 7.270   30.906  54.655 1.00 33.29  ? 406 ALA   A CA    1 
ATOM   1926 C C     . ALA   A 1 280 ? 6.628   31.869  55.635 1.00 40.18  ? 406 ALA   A C     1 
ATOM   1927 O O     . ALA   A 1 280 ? 6.679   31.656  56.851 1.00 37.01  ? 406 ALA   A O     1 
ATOM   1928 C CB    . ALA   A 1 280 ? 8.669   31.399  54.302 1.00 32.24  ? 406 ALA   A CB    1 
ATOM   1929 N N     . ALA   A 1 281 ? 6.074   32.969  55.131 1.00 38.00  ? 407 ALA   A N     1 
ATOM   1930 C CA    . ALA   A 1 281 ? 5.364   33.892  56.006 1.00 38.71  ? 407 ALA   A CA    1 
ATOM   1931 C C     . ALA   A 1 281 ? 4.187   33.208  56.678 1.00 40.33  ? 407 ALA   A C     1 
ATOM   1932 O O     . ALA   A 1 281 ? 3.927   33.428  57.866 1.00 42.67  ? 407 ALA   A O     1 
ATOM   1933 C CB    . ALA   A 1 281 ? 4.896   35.106  55.208 1.00 44.23  ? 407 ALA   A CB    1 
ATOM   1934 N N     . LYS   A 1 282 ? 3.466   32.372  55.933 1.00 39.87  ? 408 LYS   A N     1 
ATOM   1935 C CA    . LYS   A 1 282 ? 2.328   31.671  56.512 1.00 38.85  ? 408 LYS   A CA    1 
ATOM   1936 C C     . LYS   A 1 282 ? 2.793   30.687  57.574 1.00 38.42  ? 408 LYS   A C     1 
ATOM   1937 O O     . LYS   A 1 282 ? 2.173   30.575  58.640 1.00 41.57  ? 408 LYS   A O     1 
ATOM   1938 C CB    . LYS   A 1 282 ? 1.555   30.948  55.411 1.00 42.00  ? 408 LYS   A CB    1 
ATOM   1939 C CG    . LYS   A 1 282 ? 0.382   30.135  55.906 1.00 45.19  ? 408 LYS   A CG    1 
ATOM   1940 C CD    . LYS   A 1 282 ? -0.245  29.357  54.747 1.00 48.49  ? 408 LYS   A CD    1 
ATOM   1941 C CE    . LYS   A 1 282 ? -0.639  30.282  53.596 1.00 49.05  ? 408 LYS   A CE    1 
ATOM   1942 N NZ    . LYS   A 1 282 ? -1.790  31.179  53.918 1.00 49.41  ? 408 LYS   A NZ    1 
ATOM   1943 N N     . LEU   A 1 283 ? 3.888   29.974  57.293 1.00 38.10  ? 409 LEU   A N     1 
ATOM   1944 C CA    . LEU   A 1 283 ? 4.443   29.038  58.265 1.00 38.73  ? 409 LEU   A CA    1 
ATOM   1945 C C     . LEU   A 1 283 ? 4.954   29.768  59.501 1.00 38.67  ? 409 LEU   A C     1 
ATOM   1946 O O     . LEU   A 1 283 ? 4.746   29.306  60.623 1.00 38.24  ? 409 LEU   A O     1 
ATOM   1947 C CB    . LEU   A 1 283 ? 5.554   28.222  57.625 1.00 36.69  ? 409 LEU   A CB    1 
ATOM   1948 C CG    . LEU   A 1 283 ? 5.079   27.083  56.725 1.00 36.39  ? 409 LEU   A CG    1 
ATOM   1949 C CD1   . LEU   A 1 283 ? 6.248   26.502  55.957 1.00 31.69  ? 409 LEU   A CD1   1 
ATOM   1950 C CD2   . LEU   A 1 283 ? 4.429   26.000  57.588 1.00 38.42  ? 409 LEU   A CD2   1 
ATOM   1951 N N     . LEU   A 1 284 ? 5.635   30.901  59.312 1.00 39.73  ? 410 LEU   A N     1 
ATOM   1952 C CA    . LEU   A 1 284 ? 6.199   31.625  60.446 1.00 43.02  ? 410 LEU   A CA    1 
ATOM   1953 C C     . LEU   A 1 284 ? 5.115   32.206  61.341 1.00 41.35  ? 410 LEU   A C     1 
ATOM   1954 O O     . LEU   A 1 284 ? 5.346   32.399  62.539 1.00 41.30  ? 410 LEU   A O     1 
ATOM   1955 C CB    . LEU   A 1 284 ? 7.130   32.731  59.959 1.00 39.69  ? 410 LEU   A CB    1 
ATOM   1956 C CG    . LEU   A 1 284 ? 8.474   32.234  59.450 1.00 40.94  ? 410 LEU   A CG    1 
ATOM   1957 C CD1   . LEU   A 1 284 ? 9.241   33.371  58.800 1.00 41.13  ? 410 LEU   A CD1   1 
ATOM   1958 C CD2   . LEU   A 1 284 ? 9.243   31.646  60.621 1.00 39.95  ? 410 LEU   A CD2   1 
ATOM   1959 N N     . ALA   A 1 285 ? 3.939   32.489  60.789 1.00 41.81  ? 411 ALA   A N     1 
ATOM   1960 C CA    . ALA   A 1 285 ? 2.828   32.965  61.595 1.00 45.74  ? 411 ALA   A CA    1 
ATOM   1961 C C     . ALA   A 1 285 ? 2.158   31.853  62.378 1.00 42.38  ? 411 ALA   A C     1 
ATOM   1962 O O     . ALA   A 1 285 ? 1.285   32.142  63.204 1.00 48.02  ? 411 ALA   A O     1 
ATOM   1963 C CB    . ALA   A 1 285 ? 1.791   33.652  60.701 1.00 43.99  ? 411 ALA   A CB    1 
ATOM   1964 N N     . ALA   A 1 286 ? 2.545   30.600  62.153 1.00 44.45  ? 412 ALA   A N     1 
ATOM   1965 C CA    . ALA   A 1 286 ? 1.871   29.456  62.754 1.00 45.77  ? 412 ALA   A CA    1 
ATOM   1966 C C     . ALA   A 1 286 ? 2.836   28.564  63.534 1.00 43.86  ? 412 ALA   A C     1 
ATOM   1967 O O     . ALA   A 1 286 ? 2.588   27.369  63.686 1.00 42.16  ? 412 ALA   A O     1 
ATOM   1968 C CB    . ALA   A 1 286 ? 1.152   28.642  61.681 1.00 45.46  ? 412 ALA   A CB    1 
ATOM   1969 N N     . THR   A 1 287 ? 3.938   29.134  64.037 1.00 42.45  ? 413 THR   A N     1 
ATOM   1970 C CA    . THR   A 1 287 ? 4.940   28.329  64.726 1.00 42.61  ? 413 THR   A CA    1 
ATOM   1971 C C     . THR   A 1 287 ? 4.417   27.762  66.035 1.00 45.76  ? 413 THR   A C     1 
ATOM   1972 O O     . THR   A 1 287 ? 5.037   26.848  66.586 1.00 44.32  ? 413 THR   A O     1 
ATOM   1973 C CB    . THR   A 1 287 ? 6.214   29.143  64.985 1.00 42.08  ? 413 THR   A CB    1 
ATOM   1974 O OG1   . THR   A 1 287 ? 5.886   30.358  65.675 1.00 44.75  ? 413 THR   A OG1   1 
ATOM   1975 C CG2   . THR   A 1 287 ? 6.944   29.448  63.646 1.00 39.20  ? 413 THR   A CG2   1 
ATOM   1976 N N     . ASP   A 1 288 ? 3.292   28.271  66.536 1.00 46.07  ? 414 ASP   A N     1 
ATOM   1977 C CA    . ASP   A 1 288 ? 2.656   27.638  67.683 1.00 47.08  ? 414 ASP   A CA    1 
ATOM   1978 C C     . ASP   A 1 288 ? 2.293   26.188  67.380 1.00 46.22  ? 414 ASP   A C     1 
ATOM   1979 O O     . ASP   A 1 288 ? 2.499   25.303  68.221 1.00 48.84  ? 414 ASP   A O     1 
ATOM   1980 C CB    . ASP   A 1 288 ? 1.414   28.426  68.106 1.00 47.96  ? 414 ASP   A CB    1 
ATOM   1981 C CG    . ASP   A 1 288 ? 1.751   29.780  68.716 1.00 54.29  ? 414 ASP   A CG    1 
ATOM   1982 O OD1   . ASP   A 1 288 ? 2.868   29.918  69.261 1.00 56.16  ? 414 ASP   A OD1   1 
ATOM   1983 O OD2   . ASP   A 1 288 ? 0.892   30.701  68.675 1.00 58.42  ? 414 ASP   A OD2   1 
ATOM   1984 N N     . VAL   A 1 289 ? 1.778   25.916  66.180 1.00 45.13  ? 415 VAL   A N     1 
ATOM   1985 C CA    . VAL   A 1 289 ? 1.192   24.614  65.883 1.00 44.35  ? 415 VAL   A CA    1 
ATOM   1986 C C     . VAL   A 1 289 ? 1.977   23.795  64.859 1.00 42.28  ? 415 VAL   A C     1 
ATOM   1987 O O     . VAL   A 1 289 ? 1.746   22.580  64.764 1.00 45.35  ? 415 VAL   A O     1 
ATOM   1988 C CB    . VAL   A 1 289 ? -0.278  24.759  65.438 1.00 44.53  ? 415 VAL   A CB    1 
ATOM   1989 C CG1   . VAL   A 1 289 ? -1.121  25.355  66.570 1.00 51.07  ? 415 VAL   A CG1   1 
ATOM   1990 C CG2   . VAL   A 1 289 ? -0.363  25.612  64.177 1.00 44.42  ? 415 VAL   A CG2   1 
ATOM   1991 N N     . VAL   A 1 290 ? 2.883   24.399  64.085 1.00 36.45  ? 416 VAL   A N     1 
ATOM   1992 C CA    . VAL   A 1 290 ? 3.743   23.649  63.184 1.00 36.59  ? 416 VAL   A CA    1 
ATOM   1993 C C     . VAL   A 1 290 ? 5.183   24.051  63.458 1.00 37.26  ? 416 VAL   A C     1 
ATOM   1994 O O     . VAL   A 1 290 ? 5.463   25.110  64.024 1.00 37.49  ? 416 VAL   A O     1 
ATOM   1995 C CB    . VAL   A 1 290 ? 3.382   23.862  61.693 1.00 41.05  ? 416 VAL   A CB    1 
ATOM   1996 C CG1   . VAL   A 1 290 ? 1.965   23.378  61.426 1.00 37.86  ? 416 VAL   A CG1   1 
ATOM   1997 C CG2   . VAL   A 1 290 ? 3.524   25.333  61.290 1.00 36.54  ? 416 VAL   A CG2   1 
ATOM   1998 N N     . PHE   A 1 291 ? 6.097   23.156  63.081 1.00 33.89  ? 417 PHE   A N     1 
ATOM   1999 C CA    . PHE   A 1 291 ? 7.537   23.376  63.127 1.00 36.24  ? 417 PHE   A CA    1 
ATOM   2000 C C     . PHE   A 1 291 ? 8.010   23.594  61.691 1.00 35.78  ? 417 PHE   A C     1 
ATOM   2001 O O     . PHE   A 1 291 ? 8.259   22.628  60.953 1.00 32.62  ? 417 PHE   A O     1 
ATOM   2002 C CB    . PHE   A 1 291 ? 8.239   22.175  63.775 1.00 35.19  ? 417 PHE   A CB    1 
ATOM   2003 C CG    . PHE   A 1 291 ? 9.740   22.282  63.804 1.00 34.61  ? 417 PHE   A CG    1 
ATOM   2004 C CD1   . PHE   A 1 291 ? 10.362  23.338  64.451 1.00 35.87  ? 417 PHE   A CD1   1 
ATOM   2005 C CD2   . PHE   A 1 291 ? 10.527  21.301  63.226 1.00 31.97  ? 417 PHE   A CD2   1 
ATOM   2006 C CE1   . PHE   A 1 291 ? 11.747  23.428  64.483 1.00 35.23  ? 417 PHE   A CE1   1 
ATOM   2007 C CE2   . PHE   A 1 291 ? 11.902  21.388  63.259 1.00 32.03  ? 417 PHE   A CE2   1 
ATOM   2008 C CZ    . PHE   A 1 291 ? 12.508  22.453  63.890 1.00 32.34  ? 417 PHE   A CZ    1 
ATOM   2009 N N     . PRO   A 1 292 ? 8.115   24.839  61.232 1.00 34.75  ? 418 PRO   A N     1 
ATOM   2010 C CA    . PRO   A 1 292 ? 8.595   25.074  59.869 1.00 32.67  ? 418 PRO   A CA    1 
ATOM   2011 C C     . PRO   A 1 292 ? 10.066  24.741  59.725 1.00 30.85  ? 418 PRO   A C     1 
ATOM   2012 O O     . PRO   A 1 292 ? 10.898  25.073  60.577 1.00 29.19  ? 418 PRO   A O     1 
ATOM   2013 C CB    . PRO   A 1 292 ? 8.338   26.569  59.641 1.00 33.35  ? 418 PRO   A CB    1 
ATOM   2014 C CG    . PRO   A 1 292 ? 7.382   26.973  60.741 1.00 35.79  ? 418 PRO   A CG    1 
ATOM   2015 C CD    . PRO   A 1 292 ? 7.734   26.085  61.907 1.00 33.46  ? 418 PRO   A CD    1 
ATOM   2016 N N     . GLN   A 1 293 ? 10.370  24.075  58.622 1.00 29.23  ? 419 GLN   A N     1 
ATOM   2017 C CA    . GLN   A 1 293 ? 11.720  23.650  58.285 1.00 26.21  ? 419 GLN   A CA    1 
ATOM   2018 C C     . GLN   A 1 293 ? 11.996  24.204  56.906 1.00 27.92  ? 419 GLN   A C     1 
ATOM   2019 O O     . GLN   A 1 293 ? 11.404  23.747  55.927 1.00 27.00  ? 419 GLN   A O     1 
ATOM   2020 C CB    . GLN   A 1 293 ? 11.818  22.138  58.310 1.00 31.89  ? 419 GLN   A CB    1 
ATOM   2021 C CG    . GLN   A 1 293 ? 11.566  21.579  59.705 1.00 29.41  ? 419 GLN   A CG    1 
ATOM   2022 C CD    . GLN   A 1 293 ? 11.262  20.121  59.660 1.00 33.91  ? 419 GLN   A CD    1 
ATOM   2023 O OE1   . GLN   A 1 293 ? 10.452  19.677  58.847 1.00 31.58  ? 419 GLN   A OE1   1 
ATOM   2024 N NE2   . GLN   A 1 293 ? 11.925  19.347  60.511 1.00 30.75  ? 419 GLN   A NE2   1 
ATOM   2025 N N     . PHE   A 1 294 ? 12.842  25.214  56.833 1.00 28.97  ? 420 PHE   A N     1 
ATOM   2026 C CA    . PHE   A 1 294 ? 13.001  25.950  55.585 1.00 27.01  ? 420 PHE   A CA    1 
ATOM   2027 C C     . PHE   A 1 294 ? 14.178  25.368  54.827 1.00 27.08  ? 420 PHE   A C     1 
ATOM   2028 O O     . PHE   A 1 294 ? 15.334  25.699  55.083 1.00 27.39  ? 420 PHE   A O     1 
ATOM   2029 C CB    . PHE   A 1 294 ? 13.147  27.429  55.874 1.00 27.84  ? 420 PHE   A CB    1 
ATOM   2030 C CG    . PHE   A 1 294 ? 11.909  28.021  56.475 1.00 30.56  ? 420 PHE   A CG    1 
ATOM   2031 C CD1   . PHE   A 1 294 ? 10.745  28.122  55.725 1.00 34.53  ? 420 PHE   A CD1   1 
ATOM   2032 C CD2   . PHE   A 1 294 ? 11.899  28.445  57.792 1.00 33.44  ? 420 PHE   A CD2   1 
ATOM   2033 C CE1   . PHE   A 1 294 ? 9.593   28.670  56.284 1.00 34.65  ? 420 PHE   A CE1   1 
ATOM   2034 C CE2   . PHE   A 1 294 ? 10.754  28.989  58.365 1.00 36.16  ? 420 PHE   A CE2   1 
ATOM   2035 C CZ    . PHE   A 1 294 ? 9.597   29.095  57.607 1.00 33.92  ? 420 PHE   A CZ    1 
ATOM   2036 N N     . ALA   A 1 295 ? 13.854  24.523  53.865 1.00 27.27  ? 421 ALA   A N     1 
ATOM   2037 C CA    . ALA   A 1 295 ? 14.834  23.801  53.075 1.00 25.34  ? 421 ALA   A CA    1 
ATOM   2038 C C     . ALA   A 1 295 ? 15.212  24.664  51.873 1.00 29.13  ? 421 ALA   A C     1 
ATOM   2039 O O     . ALA   A 1 295 ? 14.431  24.779  50.931 1.00 31.65  ? 421 ALA   A O     1 
ATOM   2040 C CB    . ALA   A 1 295 ? 14.224  22.485  52.622 1.00 26.13  ? 421 ALA   A CB    1 
ATOM   2041 N N     . THR   A 1 296 ? 16.412  25.242  51.887 1.00 26.58  ? 422 THR   A N     1 
ATOM   2042 C CA    . THR   A 1 296 ? 16.872  26.038  50.754 1.00 25.43  ? 422 THR   A CA    1 
ATOM   2043 C C     . THR   A 1 296 ? 18.385  26.173  50.815 1.00 28.96  ? 422 THR   A C     1 
ATOM   2044 O O     . THR   A 1 296 ? 18.971  26.190  51.902 1.00 26.50  ? 422 THR   A O     1 
ATOM   2045 C CB    . THR   A 1 296 ? 16.225  27.436  50.753 1.00 27.22  ? 422 THR   A CB    1 
ATOM   2046 O OG1   . THR   A 1 296 ? 16.647  28.145  49.578 1.00 29.20  ? 422 THR   A OG1   1 
ATOM   2047 C CG2   . THR   A 1 296 ? 16.644  28.247  51.985 1.00 31.75  ? 422 THR   A CG2   1 
ATOM   2048 N N     . HIS   A 1 297 ? 19.000  26.309  49.641 1.00 28.01  ? 423 HIS   A N     1 
ATOM   2049 C CA    . HIS   A 1 297 ? 20.421  26.622  49.517 1.00 29.10  ? 423 HIS   A CA    1 
ATOM   2050 C C     . HIS   A 1 297 ? 20.629  28.032  49.005 1.00 31.20  ? 423 HIS   A C     1 
ATOM   2051 O O     . HIS   A 1 297 ? 21.762  28.422  48.701 1.00 31.18  ? 423 HIS   A O     1 
ATOM   2052 C CB    . HIS   A 1 297 ? 21.114  25.624  48.580 1.00 30.71  ? 423 HIS   A CB    1 
ATOM   2053 C CG    . HIS   A 1 297 ? 20.893  24.202  48.972 1.00 30.24  ? 423 HIS   A CG    1 
ATOM   2054 N ND1   . HIS   A 1 297 ? 20.269  23.296  48.148 1.00 30.88  ? 423 HIS   A ND1   1 
ATOM   2055 C CD2   . HIS   A 1 297 ? 21.149  23.546  50.130 1.00 31.36  ? 423 HIS   A CD2   1 
ATOM   2056 C CE1   . HIS   A 1 297 ? 20.177  22.131  48.763 1.00 29.56  ? 423 HIS   A CE1   1 
ATOM   2057 N NE2   . HIS   A 1 297 ? 20.687  22.262  49.976 1.00 29.08  ? 423 HIS   A NE2   1 
ATOM   2058 N N     . ASN   A 1 298 ? 19.552  28.796  48.910 1.00 28.34  ? 424 ASN   A N     1 
ATOM   2059 C CA    . ASN   A 1 298 ? 19.553  30.114  48.305 1.00 31.17  ? 424 ASN   A CA    1 
ATOM   2060 C C     . ASN   A 1 298 ? 19.743  31.139  49.411 1.00 29.10  ? 424 ASN   A C     1 
ATOM   2061 O O     . ASN   A 1 298 ? 18.876  31.277  50.277 1.00 27.77  ? 424 ASN   A O     1 
ATOM   2062 C CB    . ASN   A 1 298 ? 18.230  30.323  47.567 1.00 31.68  ? 424 ASN   A CB    1 
ATOM   2063 C CG    . ASN   A 1 298 ? 18.121  31.691  46.902 1.00 33.25  ? 424 ASN   A CG    1 
ATOM   2064 O OD1   . ASN   A 1 298 ? 18.627  32.682  47.415 1.00 31.81  ? 424 ASN   A OD1   1 
ATOM   2065 N ND2   . ASN   A 1 298 ? 17.425  31.746  45.760 1.00 30.71  ? 424 ASN   A ND2   1 
ATOM   2066 N N     . ALA   A 1 299 ? 20.863  31.869  49.363 1.00 33.48  ? 425 ALA   A N     1 
ATOM   2067 C CA    . ALA   A 1 299 ? 21.202  32.800  50.436 1.00 30.92  ? 425 ALA   A CA    1 
ATOM   2068 C C     . ALA   A 1 299 ? 20.164  33.900  50.568 1.00 33.58  ? 425 ALA   A C     1 
ATOM   2069 O O     . ALA   A 1 299 ? 19.926  34.397  51.676 1.00 33.91  ? 425 ALA   A O     1 
ATOM   2070 C CB    . ALA   A 1 299 ? 22.577  33.417  50.182 1.00 33.19  ? 425 ALA   A CB    1 
ATOM   2071 N N     . GLN   A 1 300 ? 19.557  34.300  49.444 1.00 33.50  ? 426 GLN   A N     1 
ATOM   2072 C CA    . GLN   A 1 300 ? 18.534  35.339  49.470 1.00 34.12  ? 426 GLN   A CA    1 
ATOM   2073 C C     . GLN   A 1 300 ? 17.279  34.822  50.152 1.00 33.56  ? 426 GLN   A C     1 
ATOM   2074 O O     . GLN   A 1 300 ? 16.717  35.487  51.028 1.00 34.74  ? 426 GLN   A O     1 
ATOM   2075 C CB    . GLN   A 1 300 ? 18.226  35.810  48.039 1.00 34.42  ? 426 GLN   A CB    1 
ATOM   2076 C CG    . GLN   A 1 300 ? 17.469  37.140  47.935 1.00 37.83  ? 426 GLN   A CG    1 
ATOM   2077 C CD    . GLN   A 1 300 ? 16.015  37.053  48.381 1.00 39.85  ? 426 GLN   A CD    1 
ATOM   2078 O OE1   . GLN   A 1 300 ? 15.344  36.042  48.173 1.00 41.40  ? 426 GLN   A OE1   1 
ATOM   2079 N NE2   . GLN   A 1 300 ? 15.531  38.113  49.007 1.00 44.92  ? 426 GLN   A NE2   1 
ATOM   2080 N N     . THR   A 1 301 ? 16.850  33.615  49.782 1.00 31.20  ? 427 THR   A N     1 
ATOM   2081 C CA    . THR   A 1 301 ? 15.702  33.001  50.430 1.00 30.57  ? 427 THR   A CA    1 
ATOM   2082 C C     . THR   A 1 301 ? 15.948  32.857  51.925 1.00 33.07  ? 427 THR   A C     1 
ATOM   2083 O O     . THR   A 1 301 ? 15.097  33.208  52.750 1.00 32.35  ? 427 THR   A O     1 
ATOM   2084 C CB    . THR   A 1 301 ? 15.426  31.631  49.819 1.00 30.27  ? 427 THR   A CB    1 
ATOM   2085 O OG1   . THR   A 1 301 ? 15.367  31.739  48.387 1.00 30.95  ? 427 THR   A OG1   1 
ATOM   2086 C CG2   . THR   A 1 301 ? 14.106  31.085  50.339 1.00 31.70  ? 427 THR   A CG2   1 
ATOM   2087 N N     . LEU   A 1 302 ? 17.115  32.334  52.280 1.00 29.13  ? 428 LEU   A N     1 
ATOM   2088 C CA    . LEU   A 1 302 ? 17.467  32.167  53.689 1.00 31.88  ? 428 LEU   A CA    1 
ATOM   2089 C C     . LEU   A 1 302 ? 17.405  33.495  54.425 1.00 34.13  ? 428 LEU   A C     1 
ATOM   2090 O O     . LEU   A 1 302 ? 16.763  33.603  55.476 1.00 34.06  ? 428 LEU   A O     1 
ATOM   2091 C CB    . LEU   A 1 302 ? 18.864  31.552  53.787 1.00 31.88  ? 428 LEU   A CB    1 
ATOM   2092 C CG    . LEU   A 1 302 ? 19.451  31.068  55.117 1.00 33.80  ? 428 LEU   A CG    1 
ATOM   2093 C CD1   . LEU   A 1 302 ? 20.656  30.280  54.749 1.00 33.38  ? 428 LEU   A CD1   1 
ATOM   2094 C CD2   . LEU   A 1 302 ? 19.864  32.182  56.029 1.00 31.89  ? 428 LEU   A CD2   1 
ATOM   2095 N N     . ALA   A 1 303 ? 18.081  34.519  53.889 1.00 34.19  ? 429 ALA   A N     1 
ATOM   2096 C CA    . ALA   A 1 303 ? 18.123  35.813  54.565 1.00 34.00  ? 429 ALA   A CA    1 
ATOM   2097 C C     . ALA   A 1 303 ? 16.723  36.377  54.750 1.00 37.31  ? 429 ALA   A C     1 
ATOM   2098 O O     . ALA   A 1 303 ? 16.401  36.935  55.805 1.00 39.98  ? 429 ALA   A O     1 
ATOM   2099 C CB    . ALA   A 1 303 ? 18.984  36.796  53.774 1.00 36.78  ? 429 ALA   A CB    1 
ATOM   2100 N N     . ALA   A 1 304 ? 15.870  36.227  53.743 1.00 35.69  ? 430 ALA   A N     1 
ATOM   2101 C CA    . ALA   A 1 304 ? 14.508  36.737  53.872 1.00 36.60  ? 430 ALA   A CA    1 
ATOM   2102 C C     . ALA   A 1 304 ? 13.762  36.029  54.994 1.00 37.31  ? 430 ALA   A C     1 
ATOM   2103 O O     . ALA   A 1 304 ? 13.110  36.680  55.813 1.00 40.86  ? 430 ALA   A O     1 
ATOM   2104 C CB    . ALA   A 1 304 ? 13.764  36.588  52.544 1.00 36.77  ? 430 ALA   A CB    1 
ATOM   2105 N N     . ILE   A 1 305 ? 13.864  34.699  55.065 1.00 38.31  ? 431 ILE   A N     1 
ATOM   2106 C CA    . ILE   A 1 305 ? 13.164  33.969  56.118 1.00 36.19  ? 431 ILE   A CA    1 
ATOM   2107 C C     . ILE   A 1 305 ? 13.743  34.333  57.472 1.00 37.40  ? 431 ILE   A C     1 
ATOM   2108 O O     . ILE   A 1 305 ? 13.016  34.497  58.455 1.00 37.55  ? 431 ILE   A O     1 
ATOM   2109 C CB    . ILE   A 1 305 ? 13.223  32.452  55.871 1.00 34.17  ? 431 ILE   A CB    1 
ATOM   2110 C CG1   . ILE   A 1 305 ? 12.084  32.002  54.966 1.00 39.42  ? 431 ILE   A CG1   1 
ATOM   2111 C CG2   . ILE   A 1 305 ? 13.074  31.672  57.184 1.00 38.14  ? 431 ILE   A CG2   1 
ATOM   2112 C CD1   . ILE   A 1 305 ? 12.059  32.653  53.668 1.00 40.95  ? 431 ILE   A CD1   1 
ATOM   2113 N N     . TYR   A 1 306 ? 15.062  34.482  57.535 1.00 37.70  ? 432 TYR   A N     1 
ATOM   2114 C CA    . TYR   A 1 306 ? 15.723  34.774  58.799 1.00 36.49  ? 432 TYR   A CA    1 
ATOM   2115 C C     . TYR   A 1 306 ? 15.203  36.066  59.404 1.00 38.52  ? 432 TYR   A C     1 
ATOM   2116 O O     . TYR   A 1 306 ? 15.002  36.161  60.621 1.00 41.69  ? 432 TYR   A O     1 
ATOM   2117 C CB    . TYR   A 1 306 ? 17.228  34.845  58.560 1.00 37.46  ? 432 TYR   A CB    1 
ATOM   2118 C CG    . TYR   A 1 306 ? 18.044  35.411  59.693 1.00 39.54  ? 432 TYR   A CG    1 
ATOM   2119 C CD1   . TYR   A 1 306 ? 18.202  34.710  60.890 1.00 37.20  ? 432 TYR   A CD1   1 
ATOM   2120 C CD2   . TYR   A 1 306 ? 18.688  36.631  59.560 1.00 41.28  ? 432 TYR   A CD2   1 
ATOM   2121 C CE1   . TYR   A 1 306 ? 18.970  35.221  61.915 1.00 39.89  ? 432 TYR   A CE1   1 
ATOM   2122 C CE2   . TYR   A 1 306 ? 19.454  37.152  60.586 1.00 40.54  ? 432 TYR   A CE2   1 
ATOM   2123 C CZ    . TYR   A 1 306 ? 19.596  36.441  61.754 1.00 42.74  ? 432 TYR   A CZ    1 
ATOM   2124 O OH    . TYR   A 1 306 ? 20.359  36.972  62.764 1.00 44.78  ? 432 TYR   A OH    1 
ATOM   2125 N N     . HIS   A 1 307 ? 14.975  37.075  58.570 1.00 42.48  ? 433 HIS   A N     1 
ATOM   2126 C CA    . HIS   A 1 307 ? 14.470  38.337  59.080 1.00 42.29  ? 433 HIS   A CA    1 
ATOM   2127 C C     . HIS   A 1 307 ? 12.955  38.328  59.214 1.00 42.73  ? 433 HIS   A C     1 
ATOM   2128 O O     . HIS   A 1 307 ? 12.424  38.920  60.156 1.00 43.58  ? 433 HIS   A O     1 
ATOM   2129 C CB    . HIS   A 1 307 ? 14.957  39.470  58.183 1.00 42.95  ? 433 HIS   A CB    1 
ATOM   2130 C CG    . HIS   A 1 307 ? 16.430  39.700  58.288 1.00 44.50  ? 433 HIS   A CG    1 
ATOM   2131 N ND1   . HIS   A 1 307 ? 16.980  40.530  59.242 1.00 46.60  ? 433 HIS   A ND1   1 
ATOM   2132 C CD2   . HIS   A 1 307 ? 17.470  39.173  57.599 1.00 40.87  ? 433 HIS   A CD2   1 
ATOM   2133 C CE1   . HIS   A 1 307 ? 18.296  40.523  59.120 1.00 46.85  ? 433 HIS   A CE1   1 
ATOM   2134 N NE2   . HIS   A 1 307 ? 18.619  39.709  58.132 1.00 43.20  ? 433 HIS   A NE2   1 
ATOM   2135 N N     . MET   A 1 308 ? 12.254  37.631  58.317 1.00 42.00  ? 434 MET   A N     1 
ATOM   2136 C CA    . MET   A 1 308 ? 10.809  37.476  58.463 1.00 41.01  ? 434 MET   A CA    1 
ATOM   2137 C C     . MET   A 1 308 ? 10.434  36.854  59.795 1.00 42.55  ? 434 MET   A C     1 
ATOM   2138 O O     . MET   A 1 308 ? 9.357   37.129  60.326 1.00 45.51  ? 434 MET   A O     1 
ATOM   2139 C CB    . MET   A 1 308 ? 10.257  36.615  57.330 1.00 44.45  ? 434 MET   A CB    1 
ATOM   2140 C CG    . MET   A 1 308 ? 9.899   37.393  56.082 1.00 50.67  ? 434 MET   A CG    1 
ATOM   2141 S SD    . MET   A 1 308 ? 9.604   36.256  54.715 1.00 57.33  ? 434 MET   A SD    1 
ATOM   2142 C CE    . MET   A 1 308 ? 8.638   35.025  55.597 1.00 48.17  ? 434 MET   A CE    1 
ATOM   2143 N N     . ALA   A 1 309 ? 11.292  35.992  60.331 1.00 42.89  ? 435 ALA   A N     1 
ATOM   2144 C CA    . ALA   A 1 309 ? 10.995  35.280  61.561 1.00 44.79  ? 435 ALA   A CA    1 
ATOM   2145 C C     . ALA   A 1 309 ? 11.125  36.153  62.801 1.00 47.25  ? 435 ALA   A C     1 
ATOM   2146 O O     . ALA   A 1 309 ? 10.726  35.722  63.889 1.00 46.17  ? 435 ALA   A O     1 
ATOM   2147 C CB    . ALA   A 1 309 ? 11.913  34.068  61.669 1.00 38.56  ? 435 ALA   A CB    1 
ATOM   2148 N N     . GLY   A 1 310 ? 11.671  37.358  62.666 1.00 46.83  ? 436 GLY   A N     1 
ATOM   2149 C CA    . GLY   A 1 310 ? 11.793  38.263  63.785 1.00 48.22  ? 436 GLY   A CA    1 
ATOM   2150 C C     . GLY   A 1 310 ? 12.995  37.962  64.664 1.00 50.37  ? 436 GLY   A C     1 
ATOM   2151 O O     . GLY   A 1 310 ? 13.818  37.083  64.393 1.00 50.40  ? 436 GLY   A O     1 
ATOM   2152 N N     . LYS   A 1 311 ? 13.079  38.723  65.756 1.00 51.07  ? 437 LYS   A N     1 
ATOM   2153 C CA    . LYS   A 1 311 ? 14.186  38.591  66.692 1.00 54.59  ? 437 LYS   A CA    1 
ATOM   2154 C C     . LYS   A 1 311 ? 13.999  37.429  67.658 1.00 54.88  ? 437 LYS   A C     1 
ATOM   2155 O O     . LYS   A 1 311 ? 14.989  36.939  68.212 1.00 56.69  ? 437 LYS   A O     1 
ATOM   2156 C CB    . LYS   A 1 311 ? 14.367  39.897  67.477 1.00 53.05  ? 437 LYS   A CB    1 
ATOM   2157 N N     . ASP   A 1 312 ? 12.764  36.974  67.864 1.00 51.17  ? 438 ASP   A N     1 
ATOM   2158 C CA    . ASP   A 1 312 ? 12.482  35.923  68.834 1.00 52.44  ? 438 ASP   A CA    1 
ATOM   2159 C C     . ASP   A 1 312 ? 12.838  34.564  68.241 1.00 52.32  ? 438 ASP   A C     1 
ATOM   2160 O O     . ASP   A 1 312 ? 12.290  34.171  67.205 1.00 50.48  ? 438 ASP   A O     1 
ATOM   2161 C CB    . ASP   A 1 312 ? 11.009  35.960  69.242 1.00 54.91  ? 438 ASP   A CB    1 
ATOM   2162 C CG    . ASP   A 1 312 ? 10.563  34.692  69.961 1.00 59.09  ? 438 ASP   A CG    1 
ATOM   2163 O OD1   . ASP   A 1 312 ? 10.990  34.460  71.117 1.00 63.48  ? 438 ASP   A OD1   1 
ATOM   2164 O OD2   . ASP   A 1 312 ? 9.771   33.926  69.370 1.00 62.10  ? 438 ASP   A OD2   1 
ATOM   2165 N N     . PHE   A 1 313 ? 13.745  33.842  68.897 1.00 48.25  ? 439 PHE   A N     1 
ATOM   2166 C CA    . PHE   A 1 313 ? 14.049  32.497  68.446 1.00 48.11  ? 439 PHE   A CA    1 
ATOM   2167 C C     . PHE   A 1 313 ? 14.344  31.589  69.629 1.00 46.60  ? 439 PHE   A C     1 
ATOM   2168 O O     . PHE   A 1 313 ? 14.923  32.011  70.631 1.00 49.81  ? 439 PHE   A O     1 
ATOM   2169 C CB    . PHE   A 1 313 ? 15.230  32.456  67.478 1.00 43.29  ? 439 PHE   A CB    1 
ATOM   2170 C CG    . PHE   A 1 313 ? 15.467  31.093  66.939 1.00 42.18  ? 439 PHE   A CG    1 
ATOM   2171 C CD1   . PHE   A 1 313 ? 14.656  30.598  65.938 1.00 40.30  ? 439 PHE   A CD1   1 
ATOM   2172 C CD2   . PHE   A 1 313 ? 16.425  30.268  67.492 1.00 39.08  ? 439 PHE   A CD2   1 
ATOM   2173 C CE1   . PHE   A 1 313 ? 14.839  29.325  65.449 1.00 38.06  ? 439 PHE   A CE1   1 
ATOM   2174 C CE2   . PHE   A 1 313 ? 16.601  28.997  67.017 1.00 37.80  ? 439 PHE   A CE2   1 
ATOM   2175 C CZ    . PHE   A 1 313 ? 15.807  28.520  65.996 1.00 38.09  ? 439 PHE   A CZ    1 
ATOM   2176 N N     . HIS   A 1 314 ? 13.947  30.327  69.486 1.00 45.18  ? 440 HIS   A N     1 
ATOM   2177 C CA    . HIS   A 1 314 ? 14.336  29.270  70.409 1.00 43.92  ? 440 HIS   A CA    1 
ATOM   2178 C C     . HIS   A 1 314 ? 14.378  27.978  69.612 1.00 41.79  ? 440 HIS   A C     1 
ATOM   2179 O O     . HIS   A 1 314 ? 13.652  27.822  68.632 1.00 41.03  ? 440 HIS   A O     1 
ATOM   2180 C CB    . HIS   A 1 314 ? 13.369  29.135  71.600 1.00 43.38  ? 440 HIS   A CB    1 
ATOM   2181 C CG    . HIS   A 1 314 ? 11.948  28.907  71.186 1.00 45.83  ? 440 HIS   A CG    1 
ATOM   2182 N ND1   . HIS   A 1 314 ? 11.425  27.652  70.968 1.00 45.98  ? 440 HIS   A ND1   1 
ATOM   2183 C CD2   . HIS   A 1 314 ? 10.948  29.781  70.925 1.00 47.37  ? 440 HIS   A CD2   1 
ATOM   2184 C CE1   . HIS   A 1 314 ? 10.165  27.763  70.587 1.00 43.22  ? 440 HIS   A CE1   1 
ATOM   2185 N NE2   . HIS   A 1 314 ? 9.847   29.043  70.569 1.00 47.73  ? 440 HIS   A NE2   1 
ATOM   2186 N N     . VAL   A 1 315 ? 15.242  27.051  70.031 1.00 43.81  ? 441 VAL   A N     1 
ATOM   2187 C CA    . VAL   A 1 315 ? 15.305  25.770  69.342 1.00 40.01  ? 441 VAL   A CA    1 
ATOM   2188 C C     . VAL   A 1 315 ? 13.952  25.085  69.445 1.00 41.89  ? 441 VAL   A C     1 
ATOM   2189 O O     . VAL   A 1 315 ? 13.403  24.910  70.544 1.00 41.87  ? 441 VAL   A O     1 
ATOM   2190 C CB    . VAL   A 1 315 ? 16.425  24.906  69.924 1.00 47.93  ? 441 VAL   A CB    1 
ATOM   2191 C CG1   . VAL   A 1 315 ? 16.469  23.565  69.200 1.00 44.79  ? 441 VAL   A CG1   1 
ATOM   2192 C CG2   . VAL   A 1 315 ? 17.747  25.638  69.807 1.00 48.03  ? 441 VAL   A CG2   1 
ATOM   2193 N N     . GLY   A 1 316 ? 13.400  24.709  68.292 1.00 38.55  ? 442 GLY   A N     1 
ATOM   2194 C CA    . GLY   A 1 316 ? 12.056  24.183  68.193 1.00 41.13  ? 442 GLY   A CA    1 
ATOM   2195 C C     . GLY   A 1 316 ? 11.066  25.133  67.560 1.00 38.01  ? 442 GLY   A C     1 
ATOM   2196 O O     . GLY   A 1 316 ? 9.976   24.698  67.163 1.00 39.69  ? 442 GLY   A O     1 
ATOM   2197 N N     . LYS   A 1 317 ? 11.409  26.419  67.446 1.00 39.18  ? 443 LYS   A N     1 
ATOM   2198 C CA    . LYS   A 1 317 ? 10.527  27.351  66.750 1.00 41.06  ? 443 LYS   A CA    1 
ATOM   2199 C C     . LYS   A 1 317 ? 10.487  27.060  65.253 1.00 38.12  ? 443 LYS   A C     1 
ATOM   2200 O O     . LYS   A 1 317 ? 9.420   26.840  64.675 1.00 36.81  ? 443 LYS   A O     1 
ATOM   2201 C CB    . LYS   A 1 317 ? 10.972  28.789  67.006 1.00 40.61  ? 443 LYS   A CB    1 
ATOM   2202 C CG    . LYS   A 1 317 ? 10.009  29.790  66.381 1.00 43.76  ? 443 LYS   A CG    1 
ATOM   2203 C CD    . LYS   A 1 317 ? 10.351  31.210  66.716 1.00 47.66  ? 443 LYS   A CD    1 
ATOM   2204 C CE    . LYS   A 1 317 ? 9.073   32.023  66.876 1.00 52.73  ? 443 LYS   A CE    1 
ATOM   2205 N NZ    . LYS   A 1 317 ? 9.356   33.401  67.322 1.00 53.09  ? 443 LYS   A NZ    1 
ATOM   2206 N N     . TYR   A 1 318 ? 11.647  27.067  64.606 1.00 33.50  ? 444 TYR   A N     1 
ATOM   2207 C CA    . TYR   A 1 318 ? 11.777  26.664  63.215 1.00 32.42  ? 444 TYR   A CA    1 
ATOM   2208 C C     . TYR   A 1 318 ? 13.229  26.280  63.017 1.00 32.63  ? 444 TYR   A C     1 
ATOM   2209 O O     . TYR   A 1 318 ? 14.066  26.509  63.891 1.00 31.19  ? 444 TYR   A O     1 
ATOM   2210 C CB    . TYR   A 1 318 ? 11.346  27.790  62.272 1.00 34.69  ? 444 TYR   A CB    1 
ATOM   2211 C CG    . TYR   A 1 318 ? 12.364  28.897  62.103 1.00 33.67  ? 444 TYR   A CG    1 
ATOM   2212 C CD1   . TYR   A 1 318 ? 13.354  28.783  61.139 1.00 36.58  ? 444 TYR   A CD1   1 
ATOM   2213 C CD2   . TYR   A 1 318 ? 12.312  30.063  62.858 1.00 38.88  ? 444 TYR   A CD2   1 
ATOM   2214 C CE1   . TYR   A 1 318 ? 14.279  29.756  60.947 1.00 38.90  ? 444 TYR   A CE1   1 
ATOM   2215 C CE2   . TYR   A 1 318 ? 13.266  31.069  62.672 1.00 39.80  ? 444 TYR   A CE2   1 
ATOM   2216 C CZ    . TYR   A 1 318 ? 14.246  30.888  61.704 1.00 41.77  ? 444 TYR   A CZ    1 
ATOM   2217 O OH    . TYR   A 1 318 ? 15.211  31.834  61.432 1.00 44.96  ? 444 TYR   A OH    1 
ATOM   2218 N N     . GLU   A 1 319 ? 13.531  25.699  61.857 1.00 32.73  ? 445 GLU   A N     1 
ATOM   2219 C CA    . GLU   A 1 319 ? 14.914  25.430  61.512 1.00 29.52  ? 445 GLU   A CA    1 
ATOM   2220 C C     . GLU   A 1 319 ? 15.074  25.596  60.013 1.00 29.51  ? 445 GLU   A C     1 
ATOM   2221 O O     . GLU   A 1 319 ? 14.096  25.609  59.263 1.00 29.50  ? 445 GLU   A O     1 
ATOM   2222 C CB    . GLU   A 1 319 ? 15.348  24.017  61.926 1.00 30.41  ? 445 GLU   A CB    1 
ATOM   2223 C CG    . GLU   A 1 319 ? 14.613  22.927  61.145 1.00 30.58  ? 445 GLU   A CG    1 
ATOM   2224 C CD    . GLU   A 1 319 ? 14.964  21.531  61.632 1.00 32.45  ? 445 GLU   A CD    1 
ATOM   2225 O OE1   . GLU   A 1 319 ? 15.590  21.425  62.712 1.00 30.38  ? 445 GLU   A OE1   1 
ATOM   2226 O OE2   . GLU   A 1 319 ? 14.621  20.549  60.939 1.00 32.36  ? 445 GLU   A OE2   1 
ATOM   2227 N N     . PHE   A 1 320 ? 16.322  25.696  59.588 1.00 28.87  ? 446 PHE   A N     1 
ATOM   2228 C CA    . PHE   A 1 320 ? 16.643  25.620  58.173 1.00 27.39  ? 446 PHE   A CA    1 
ATOM   2229 C C     . PHE   A 1 320 ? 17.037  24.189  57.835 1.00 26.48  ? 446 PHE   A C     1 
ATOM   2230 O O     . PHE   A 1 320 ? 17.313  23.368  58.717 1.00 26.79  ? 446 PHE   A O     1 
ATOM   2231 C CB    . PHE   A 1 320 ? 17.764  26.600  57.828 1.00 28.69  ? 446 PHE   A CB    1 
ATOM   2232 C CG    . PHE   A 1 320 ? 17.380  28.039  57.970 1.00 30.55  ? 446 PHE   A CG    1 
ATOM   2233 C CD1   . PHE   A 1 320 ? 16.632  28.669  56.992 1.00 30.63  ? 446 PHE   A CD1   1 
ATOM   2234 C CD2   . PHE   A 1 320 ? 17.776  28.769  59.066 1.00 32.21  ? 446 PHE   A CD2   1 
ATOM   2235 C CE1   . PHE   A 1 320 ? 16.271  30.003  57.120 1.00 31.15  ? 446 PHE   A CE1   1 
ATOM   2236 C CE2   . PHE   A 1 320 ? 17.421  30.097  59.208 1.00 32.38  ? 446 PHE   A CE2   1 
ATOM   2237 C CZ    . PHE   A 1 320 ? 16.667  30.723  58.227 1.00 33.27  ? 446 PHE   A CZ    1 
ATOM   2238 N N     . GLN   A 1 321 ? 17.043  23.871  56.545 1.00 26.53  ? 447 GLN   A N     1 
ATOM   2239 C CA    . GLN   A 1 321 ? 17.493  22.551  56.127 1.00 24.80  ? 447 GLN   A CA    1 
ATOM   2240 C C     . GLN   A 1 321 ? 18.281  22.692  54.842 1.00 25.46  ? 447 GLN   A C     1 
ATOM   2241 O O     . GLN   A 1 321 ? 18.162  23.677  54.123 1.00 25.30  ? 447 GLN   A O     1 
ATOM   2242 C CB    . GLN   A 1 321 ? 16.334  21.571  55.941 1.00 24.94  ? 447 GLN   A CB    1 
ATOM   2243 C CG    . GLN   A 1 321 ? 15.566  21.302  57.246 1.00 28.25  ? 447 GLN   A CG    1 
ATOM   2244 C CD    . GLN   A 1 321 ? 14.703  20.074  57.177 1.00 27.19  ? 447 GLN   A CD    1 
ATOM   2245 O OE1   . GLN   A 1 321 ? 14.416  19.566  56.097 1.00 29.53  ? 447 GLN   A OE1   1 
ATOM   2246 N NE2   . GLN   A 1 321 ? 14.290  19.577  58.338 1.00 30.19  ? 447 GLN   A NE2   1 
ATOM   2247 N N     . CYS   A 1 322 ? 19.138  21.710  54.594 1.00 27.82  ? 448 CYS   A N     1 
ATOM   2248 C CA    . CYS   A 1 322 ? 19.904  21.682  53.362 1.00 25.00  ? 448 CYS   A CA    1 
ATOM   2249 C C     . CYS   A 1 322 ? 20.192  20.231  53.019 1.00 26.86  ? 448 CYS   A C     1 
ATOM   2250 O O     . CYS   A 1 322 ? 20.002  19.330  53.837 1.00 28.69  ? 448 CYS   A O     1 
ATOM   2251 C CB    . CYS   A 1 322 ? 21.195  22.490  53.484 1.00 26.51  ? 448 CYS   A CB    1 
ATOM   2252 S SG    . CYS   A 1 322 ? 22.381  21.721  54.617 1.00 31.81  ? 448 CYS   A SG    1 
ATOM   2253 N N     . LEU   A 1 323 ? 20.594  20.012  51.775 1.00 25.30  ? 449 LEU   A N     1 
ATOM   2254 C CA    . LEU   A 1 323 ? 21.038  18.705  51.314 1.00 26.96  ? 449 LEU   A CA    1 
ATOM   2255 C C     . LEU   A 1 323 ? 22.512  18.540  51.599 1.00 28.75  ? 449 LEU   A C     1 
ATOM   2256 O O     . LEU   A 1 323 ? 23.301  19.470  51.409 1.00 30.04  ? 449 LEU   A O     1 
ATOM   2257 C CB    . LEU   A 1 323 ? 20.808  18.535  49.813 1.00 24.93  ? 449 LEU   A CB    1 
ATOM   2258 C CG    . LEU   A 1 323 ? 19.342  18.534  49.395 1.00 26.65  ? 449 LEU   A CG    1 
ATOM   2259 C CD1   . LEU   A 1 323 ? 19.206  18.417  47.872 1.00 27.35  ? 449 LEU   A CD1   1 
ATOM   2260 C CD2   . LEU   A 1 323 ? 18.597  17.397  50.088 1.00 25.64  ? 449 LEU   A CD2   1 
ATOM   2261 N N     . HIS   A 1 324 ? 22.881  17.338  52.026 1.00 27.76  ? 450 HIS   A N     1 
ATOM   2262 C CA    . HIS   A 1 324 ? 24.282  17.007  52.190 1.00 33.74  ? 450 HIS   A CA    1 
ATOM   2263 C C     . HIS   A 1 324 ? 25.033  17.266  50.900 1.00 32.22  ? 450 HIS   A C     1 
ATOM   2264 O O     . HIS   A 1 324 ? 24.598  16.855  49.823 1.00 30.30  ? 450 HIS   A O     1 
ATOM   2265 C CB    . HIS   A 1 324 ? 24.451  15.539  52.569 1.00 32.70  ? 450 HIS   A CB    1 
ATOM   2266 C CG    . HIS   A 1 324 ? 25.881  15.101  52.596 1.00 38.43  ? 450 HIS   A CG    1 
ATOM   2267 N ND1   . HIS   A 1 324 ? 26.738  15.433  53.622 1.00 38.85  ? 450 HIS   A ND1   1 
ATOM   2268 C CD2   . HIS   A 1 324 ? 26.609  14.369  51.720 1.00 39.90  ? 450 HIS   A CD2   1 
ATOM   2269 C CE1   . HIS   A 1 324 ? 27.932  14.922  53.379 1.00 40.96  ? 450 HIS   A CE1   1 
ATOM   2270 N NE2   . HIS   A 1 324 ? 27.881  14.266  52.234 1.00 40.70  ? 450 HIS   A NE2   1 
ATOM   2271 N N     . GLY   A 1 325 ? 26.186  17.920  51.026 1.00 33.42  ? 451 GLY   A N     1 
ATOM   2272 C CA    . GLY   A 1 325 ? 27.035  18.200  49.896 1.00 33.91  ? 451 GLY   A CA    1 
ATOM   2273 C C     . GLY   A 1 325 ? 26.675  19.452  49.137 1.00 36.94  ? 451 GLY   A C     1 
ATOM   2274 O O     . GLY   A 1 325 ? 27.415  19.838  48.239 1.00 37.26  ? 451 GLY   A O     1 
ATOM   2275 N N     . MET   A 1 326 ? 25.561  20.096  49.467 1.00 37.41  ? 452 MET   A N     1 
ATOM   2276 C CA    . MET   A 1 326 ? 25.162  21.352  48.851 1.00 33.89  ? 452 MET   A CA    1 
ATOM   2277 C C     . MET   A 1 326 ? 25.132  22.520  49.814 1.00 34.93  ? 452 MET   A C     1 
ATOM   2278 O O     . MET   A 1 326 ? 25.435  23.643  49.406 1.00 38.20  ? 452 MET   A O     1 
ATOM   2279 C CB    . MET   A 1 326 ? 23.770  21.217  48.228 1.00 32.43  ? 452 MET   A CB    1 
ATOM   2280 C CG    . MET   A 1 326 ? 23.739  20.247  47.087 1.00 37.35  ? 452 MET   A CG    1 
ATOM   2281 S SD    . MET   A 1 326 ? 22.218  20.341  46.129 1.00 42.84  ? 452 MET   A SD    1 
ATOM   2282 C CE    . MET   A 1 326 ? 22.213  22.068  45.606 1.00 38.77  ? 452 MET   A CE    1 
ATOM   2283 N N     . GLY   A 1 327 ? 24.769  22.297  51.068 1.00 34.63  ? 453 GLY   A N     1 
ATOM   2284 C CA    . GLY   A 1 327 ? 24.378  23.414  51.910 1.00 33.55  ? 453 GLY   A CA    1 
ATOM   2285 C C     . GLY   A 1 327 ? 25.398  23.809  52.946 1.00 33.59  ? 453 GLY   A C     1 
ATOM   2286 O O     . GLY   A 1 327 ? 25.342  24.913  53.492 1.00 33.85  ? 453 GLY   A O     1 
ATOM   2287 N N     . GLU   A 1 328 ? 26.344  22.921  53.223 1.00 37.66  ? 454 GLU   A N     1 
ATOM   2288 C CA    . GLU   A 1 328 ? 27.277  23.195  54.311 1.00 34.09  ? 454 GLU   A CA    1 
ATOM   2289 C C     . GLU   A 1 328 ? 28.047  24.504  54.138 1.00 34.61  ? 454 GLU   A C     1 
ATOM   2290 O O     . GLU   A 1 328 ? 28.124  25.262  55.119 1.00 36.34  ? 454 GLU   A O     1 
ATOM   2291 C CB    . GLU   A 1 328 ? 28.189  21.983  54.498 1.00 37.64  ? 454 GLU   A CB    1 
ATOM   2292 C CG    . GLU   A 1 328 ? 27.412  20.749  54.988 1.00 38.56  ? 454 GLU   A CG    1 
ATOM   2293 C CD    . GLU   A 1 328 ? 27.132  19.725  53.890 1.00 40.93  ? 454 GLU   A CD    1 
ATOM   2294 O OE1   . GLU   A 1 328 ? 27.089  20.116  52.700 1.00 40.01  ? 454 GLU   A OE1   1 
ATOM   2295 O OE2   . GLU   A 1 328 ? 26.972  18.524  54.222 1.00 44.45  ? 454 GLU   A OE2   1 
ATOM   2296 N N     . PRO   A 1 329 ? 28.565  24.875  52.954 1.00 37.41  ? 455 PRO   A N     1 
ATOM   2297 C CA    . PRO   A 1 329 ? 29.242  26.183  52.862 1.00 38.53  ? 455 PRO   A CA    1 
ATOM   2298 C C     . PRO   A 1 329 ? 28.337  27.367  53.191 1.00 37.71  ? 455 PRO   A C     1 
ATOM   2299 O O     . PRO   A 1 329 ? 28.787  28.318  53.838 1.00 39.33  ? 455 PRO   A O     1 
ATOM   2300 C CB    . PRO   A 1 329 ? 29.733  26.219  51.409 1.00 40.20  ? 455 PRO   A CB    1 
ATOM   2301 C CG    . PRO   A 1 329 ? 29.841  24.781  51.020 1.00 38.05  ? 455 PRO   A CG    1 
ATOM   2302 C CD    . PRO   A 1 329 ? 28.698  24.110  51.700 1.00 35.46  ? 455 PRO   A CD    1 
ATOM   2303 N N     . LEU   A 1 330 ? 27.076  27.355  52.759 1.00 31.17  ? 456 LEU   A N     1 
ATOM   2304 C CA    . LEU   A 1 330 ? 26.166  28.425  53.170 1.00 32.66  ? 456 LEU   A CA    1 
ATOM   2305 C C     . LEU   A 1 330 ? 25.847  28.344  54.658 1.00 31.90  ? 456 LEU   A C     1 
ATOM   2306 O O     . LEU   A 1 330 ? 25.890  29.349  55.377 1.00 33.08  ? 456 LEU   A O     1 
ATOM   2307 C CB    . LEU   A 1 330 ? 24.876  28.356  52.364 1.00 34.14  ? 456 LEU   A CB    1 
ATOM   2308 C CG    . LEU   A 1 330 ? 23.751  29.287  52.842 1.00 31.57  ? 456 LEU   A CG    1 
ATOM   2309 C CD1   . LEU   A 1 330 ? 24.154  30.740  52.673 1.00 35.37  ? 456 LEU   A CD1   1 
ATOM   2310 C CD2   . LEU   A 1 330 ? 22.489  28.980  52.051 1.00 33.62  ? 456 LEU   A CD2   1 
ATOM   2311 N N     . TYR   A 1 331 ? 25.504  27.157  55.138 1.00 31.49  ? 457 TYR   A N     1 
ATOM   2312 C CA    . TYR   A 1 331 ? 25.019  27.066  56.506 1.00 31.04  ? 457 TYR   A CA    1 
ATOM   2313 C C     . TYR   A 1 331 ? 26.123  27.119  57.548 1.00 32.98  ? 457 TYR   A C     1 
ATOM   2314 O O     . TYR   A 1 331 ? 25.824  27.392  58.716 1.00 31.18  ? 457 TYR   A O     1 
ATOM   2315 C CB    . TYR   A 1 331 ? 24.167  25.819  56.661 1.00 26.89  ? 457 TYR   A CB    1 
ATOM   2316 C CG    . TYR   A 1 331 ? 22.801  26.126  56.076 1.00 29.82  ? 457 TYR   A CG    1 
ATOM   2317 C CD1   . TYR   A 1 331 ? 21.898  26.884  56.790 1.00 26.68  ? 457 TYR   A CD1   1 
ATOM   2318 C CD2   . TYR   A 1 331 ? 22.459  25.703  54.806 1.00 28.06  ? 457 TYR   A CD2   1 
ATOM   2319 C CE1   . TYR   A 1 331 ? 20.645  27.209  56.259 1.00 27.62  ? 457 TYR   A CE1   1 
ATOM   2320 C CE2   . TYR   A 1 331 ? 21.205  26.006  54.252 1.00 28.35  ? 457 TYR   A CE2   1 
ATOM   2321 C CZ    . TYR   A 1 331 ? 20.307  26.761  54.993 1.00 27.55  ? 457 TYR   A CZ    1 
ATOM   2322 O OH    . TYR   A 1 331 ? 19.070  27.064  54.494 1.00 28.83  ? 457 TYR   A OH    1 
ATOM   2323 N N     . GLU   A 1 332 ? 27.381  26.928  57.147 1.00 34.02  ? 458 GLU   A N     1 
ATOM   2324 C CA    . GLU   A 1 332 ? 28.479  27.253  58.050 1.00 35.53  ? 458 GLU   A CA    1 
ATOM   2325 C C     . GLU   A 1 332 ? 28.590  28.750  58.298 1.00 36.15  ? 458 GLU   A C     1 
ATOM   2326 O O     . GLU   A 1 332 ? 29.330  29.165  59.197 1.00 37.49  ? 458 GLU   A O     1 
ATOM   2327 C CB    . GLU   A 1 332 ? 29.802  26.696  57.497 1.00 36.85  ? 458 GLU   A CB    1 
ATOM   2328 C CG    . GLU   A 1 332 ? 29.888  25.167  57.603 1.00 41.87  ? 458 GLU   A CG    1 
ATOM   2329 C CD    . GLU   A 1 332 ? 31.096  24.555  56.878 1.00 51.35  ? 458 GLU   A CD    1 
ATOM   2330 O OE1   . GLU   A 1 332 ? 31.807  25.276  56.138 1.00 48.43  ? 458 GLU   A OE1   1 
ATOM   2331 O OE2   . GLU   A 1 332 ? 31.325  23.336  57.045 1.00 53.71  ? 458 GLU   A OE2   1 
ATOM   2332 N N     . GLU   A 1 333 ? 27.880  29.569  57.518 1.00 35.09  ? 459 GLU   A N     1 
ATOM   2333 C CA    . GLU   A 1 333 ? 27.725  30.987  57.802 1.00 37.33  ? 459 GLU   A CA    1 
ATOM   2334 C C     . GLU   A 1 333 ? 26.457  31.283  58.594 1.00 36.36  ? 459 GLU   A C     1 
ATOM   2335 O O     . GLU   A 1 333 ? 26.159  32.450  58.850 1.00 38.10  ? 459 GLU   A O     1 
ATOM   2336 C CB    . GLU   A 1 333 ? 27.722  31.797  56.489 1.00 38.91  ? 459 GLU   A CB    1 
ATOM   2337 C CG    . GLU   A 1 333 ? 28.969  31.591  55.619 1.00 40.35  ? 459 GLU   A CG    1 
ATOM   2338 C CD    . GLU   A 1 333 ? 30.262  31.923  56.352 1.00 45.91  ? 459 GLU   A CD    1 
ATOM   2339 O OE1   . GLU   A 1 333 ? 30.250  32.830  57.211 1.00 46.39  ? 459 GLU   A OE1   1 
ATOM   2340 O OE2   . GLU   A 1 333 ? 31.295  31.276  56.072 1.00 50.11  ? 459 GLU   A OE2   1 
ATOM   2341 N N     . VAL   A 1 334 ? 25.703  30.257  58.975 1.00 33.44  ? 460 VAL   A N     1 
ATOM   2342 C CA    . VAL   A 1 334 ? 24.404  30.412  59.616 1.00 34.46  ? 460 VAL   A CA    1 
ATOM   2343 C C     . VAL   A 1 334 ? 24.392  29.813  61.021 1.00 37.35  ? 460 VAL   A C     1 
ATOM   2344 O O     . VAL   A 1 334 ? 24.026  30.483  61.991 1.00 38.70  ? 460 VAL   A O     1 
ATOM   2345 C CB    . VAL   A 1 334 ? 23.285  29.794  58.752 1.00 34.31  ? 460 VAL   A CB    1 
ATOM   2346 C CG1   . VAL   A 1 334 ? 21.962  29.799  59.512 1.00 36.12  ? 460 VAL   A CG1   1 
ATOM   2347 C CG2   . VAL   A 1 334 ? 23.161  30.558  57.444 1.00 35.70  ? 460 VAL   A CG2   1 
ATOM   2348 N N     . VAL   A 1 335 ? 24.785  28.546  61.145 1.00 37.32  ? 461 VAL   A N     1 
ATOM   2349 C CA    . VAL   A 1 335 ? 24.697  27.846  62.422 1.00 38.26  ? 461 VAL   A CA    1 
ATOM   2350 C C     . VAL   A 1 335 ? 25.742  28.386  63.389 1.00 41.13  ? 461 VAL   A C     1 
ATOM   2351 O O     . VAL   A 1 335 ? 26.832  28.822  62.993 1.00 41.66  ? 461 VAL   A O     1 
ATOM   2352 C CB    . VAL   A 1 335 ? 24.865  26.323  62.239 1.00 39.91  ? 461 VAL   A CB    1 
ATOM   2353 C CG1   . VAL   A 1 335 ? 23.790  25.760  61.307 1.00 33.49  ? 461 VAL   A CG1   1 
ATOM   2354 C CG2   . VAL   A 1 335 ? 26.267  25.982  61.743 1.00 42.15  ? 461 VAL   A CG2   1 
ATOM   2355 N N     . GLY   A 1 336 ? 25.412  28.353  64.666 1.00 43.01  ? 462 GLY   A N     1 
ATOM   2356 C CA    . GLY   A 1 336 ? 26.431  28.680  65.643 1.00 45.18  ? 462 GLY   A CA    1 
ATOM   2357 C C     . GLY   A 1 336 ? 26.340  30.115  66.124 1.00 47.41  ? 462 GLY   A C     1 
ATOM   2358 O O     . GLY   A 1 336 ? 25.834  31.009  65.431 1.00 43.23  ? 462 GLY   A O     1 
ATOM   2359 N N     . ARG   A 1 337 ? 26.863  30.344  67.334 1.00 45.16  ? 463 ARG   A N     1 
ATOM   2360 C CA    . ARG   A 1 337 ? 26.753  31.639  67.993 1.00 48.17  ? 463 ARG   A CA    1 
ATOM   2361 C C     . ARG   A 1 337 ? 27.579  32.722  67.309 1.00 50.79  ? 463 ARG   A C     1 
ATOM   2362 O O     . ARG   A 1 337 ? 27.252  33.907  67.444 1.00 51.13  ? 463 ARG   A O     1 
ATOM   2363 C CB    . ARG   A 1 337 ? 27.164  31.509  69.464 1.00 46.81  ? 463 ARG   A CB    1 
ATOM   2364 N N     . GLY   A 1 338 ? 28.639  32.352  66.589 1.00 48.46  ? 464 GLY   A N     1 
ATOM   2365 C CA    . GLY   A 1 338 ? 29.412  33.341  65.865 1.00 46.03  ? 464 GLY   A CA    1 
ATOM   2366 C C     . GLY   A 1 338 ? 28.832  33.730  64.528 1.00 46.68  ? 464 GLY   A C     1 
ATOM   2367 O O     . GLY   A 1 338 ? 29.330  34.651  63.872 1.00 46.41  ? 464 GLY   A O     1 
ATOM   2368 N N     . LYS   A 1 339 ? 27.758  33.056  64.116 1.00 41.49  ? 465 LYS   A N     1 
ATOM   2369 C CA    . LYS   A 1 339 ? 27.120  33.325  62.830 1.00 42.01  ? 465 LYS   A CA    1 
ATOM   2370 C C     . LYS   A 1 339 ? 25.720  33.844  63.132 1.00 39.83  ? 465 LYS   A C     1 
ATOM   2371 O O     . LYS   A 1 339 ? 25.585  34.839  63.843 1.00 43.52  ? 465 LYS   A O     1 
ATOM   2372 C CB    . LYS   A 1 339 ? 27.170  32.098  61.936 1.00 41.19  ? 465 LYS   A CB    1 
ATOM   2373 C CG    . LYS   A 1 339 ? 28.584  31.603  61.649 1.00 41.31  ? 465 LYS   A CG    1 
ATOM   2374 C CD    . LYS   A 1 339 ? 29.426  32.708  61.036 1.00 43.21  ? 465 LYS   A CD    1 
ATOM   2375 C CE    . LYS   A 1 339 ? 30.699  32.162  60.392 1.00 46.62  ? 465 LYS   A CE    1 
ATOM   2376 N NZ    . LYS   A 1 339 ? 31.387  33.204  59.555 1.00 50.90  ? 465 LYS   A NZ    1 
ATOM   2377 N N     . LEU   A 1 340 ? 24.678  33.193  62.633 1.00 40.79  ? 466 LEU   A N     1 
ATOM   2378 C CA    . LEU   A 1 340 ? 23.317  33.665  62.825 1.00 43.69  ? 466 LEU   A CA    1 
ATOM   2379 C C     . LEU   A 1 340 ? 22.589  32.937  63.941 1.00 41.38  ? 466 LEU   A C     1 
ATOM   2380 O O     . LEU   A 1 340 ? 21.463  33.316  64.269 1.00 40.28  ? 466 LEU   A O     1 
ATOM   2381 C CB    . LEU   A 1 340 ? 22.522  33.525  61.526 1.00 38.46  ? 466 LEU   A CB    1 
ATOM   2382 C CG    . LEU   A 1 340 ? 23.058  34.192  60.261 1.00 35.79  ? 466 LEU   A CG    1 
ATOM   2383 C CD1   . LEU   A 1 340 ? 22.025  34.060  59.145 1.00 39.39  ? 466 LEU   A CD1   1 
ATOM   2384 C CD2   . LEU   A 1 340 ? 23.393  35.635  60.513 1.00 40.97  ? 466 LEU   A CD2   1 
ATOM   2385 N N     . ASP   A 1 341 ? 23.194  31.899  64.518 1.00 43.35  ? 467 ASP   A N     1 
ATOM   2386 C CA    . ASP   A 1 341 ? 22.625  31.158  65.644 1.00 40.93  ? 467 ASP   A CA    1 
ATOM   2387 C C     . ASP   A 1 341 ? 21.232  30.615  65.316 1.00 39.60  ? 467 ASP   A C     1 
ATOM   2388 O O     . ASP   A 1 341 ? 20.290  30.707  66.108 1.00 41.21  ? 467 ASP   A O     1 
ATOM   2389 C CB    . ASP   A 1 341 ? 22.596  32.015  66.907 1.00 45.35  ? 467 ASP   A CB    1 
ATOM   2390 C CG    . ASP   A 1 341 ? 22.608  31.183  68.172 1.00 46.81  ? 467 ASP   A CG    1 
ATOM   2391 O OD1   . ASP   A 1 341 ? 22.894  29.963  68.091 1.00 51.77  ? 467 ASP   A OD1   1 
ATOM   2392 O OD2   . ASP   A 1 341 ? 22.338  31.750  69.251 1.00 56.83  ? 467 ASP   A OD2   1 
ATOM   2393 N N     . ARG   A 1 342 ? 21.109  30.043  64.124 1.00 39.30  ? 468 ARG   A N     1 
ATOM   2394 C CA    . ARG   A 1 342 ? 19.915  29.350  63.705 1.00 36.29  ? 468 ARG   A CA    1 
ATOM   2395 C C     . ARG   A 1 342 ? 20.310  27.942  63.295 1.00 34.09  ? 468 ARG   A C     1 
ATOM   2396 O O     . ARG   A 1 342 ? 21.318  27.763  62.607 1.00 36.73  ? 468 ARG   A O     1 
ATOM   2397 C CB    . ARG   A 1 342 ? 19.233  30.064  62.516 1.00 32.45  ? 468 ARG   A CB    1 
ATOM   2398 C CG    . ARG   A 1 342 ? 18.781  31.493  62.846 1.00 38.49  ? 468 ARG   A CG    1 
ATOM   2399 C CD    . ARG   A 1 342 ? 17.624  31.473  63.822 1.00 37.16  ? 468 ARG   A CD    1 
ATOM   2400 N NE    . ARG   A 1 342 ? 17.196  32.824  64.170 1.00 41.19  ? 468 ARG   A NE    1 
ATOM   2401 C CZ    . ARG   A 1 342 ? 17.649  33.514  65.207 1.00 43.25  ? 468 ARG   A CZ    1 
ATOM   2402 N NH1   . ARG   A 1 342 ? 18.522  32.995  66.059 1.00 39.80  ? 468 ARG   A NH1   1 
ATOM   2403 N NH2   . ARG   A 1 342 ? 17.211  34.757  65.401 1.00 42.19  ? 468 ARG   A NH2   1 
ATOM   2404 N N     . PRO   A 1 343 ? 19.535  26.937  63.673 1.00 32.02  ? 469 PRO   A N     1 
ATOM   2405 C CA    . PRO   A 1 343 ? 19.919  25.557  63.369 1.00 31.19  ? 469 PRO   A CA    1 
ATOM   2406 C C     . PRO   A 1 343 ? 19.642  25.206  61.922 1.00 31.42  ? 469 PRO   A C     1 
ATOM   2407 O O     . PRO   A 1 343 ? 18.812  25.812  61.238 1.00 30.59  ? 469 PRO   A O     1 
ATOM   2408 C CB    . PRO   A 1 343 ? 19.040  24.729  64.315 1.00 35.59  ? 469 PRO   A CB    1 
ATOM   2409 C CG    . PRO   A 1 343 ? 17.794  25.562  64.446 1.00 35.07  ? 469 PRO   A CG    1 
ATOM   2410 C CD    . PRO   A 1 343 ? 18.255  27.009  64.395 1.00 33.86  ? 469 PRO   A CD    1 
ATOM   2411 N N     . CYS   A 1 344 ? 20.359  24.196  61.457 1.00 30.90  ? 470 CYS   A N     1 
ATOM   2412 C CA    . CYS   A 1 344 ? 20.127  23.671  60.124 1.00 29.67  ? 470 CYS   A CA    1 
ATOM   2413 C C     . CYS   A 1 344 ? 20.190  22.160  60.191 1.00 30.75  ? 470 CYS   A C     1 
ATOM   2414 O O     . CYS   A 1 344 ? 21.127  21.615  60.783 1.00 32.61  ? 470 CYS   A O     1 
ATOM   2415 C CB    . CYS   A 1 344 ? 21.161  24.192  59.125 1.00 30.91  ? 470 CYS   A CB    1 
ATOM   2416 S SG    . CYS   A 1 344 ? 20.949  23.456  57.484 1.00 32.60  ? 470 CYS   A SG    1 
ATOM   2417 N N     . ARG   A 1 345 ? 19.204  21.489  59.601 1.00 27.30  ? 471 ARG   A N     1 
ATOM   2418 C CA    . ARG   A 1 345 ? 19.203  20.032  59.534 1.00 28.82  ? 471 ARG   A CA    1 
ATOM   2419 C C     . ARG   A 1 345 ? 19.669  19.602  58.151 1.00 30.15  ? 471 ARG   A C     1 
ATOM   2420 O O     . ARG   A 1 345 ? 19.055  19.967  57.145 1.00 26.56  ? 471 ARG   A O     1 
ATOM   2421 C CB    . ARG   A 1 345 ? 17.820  19.465  59.836 1.00 27.83  ? 471 ARG   A CB    1 
ATOM   2422 C CG    . ARG   A 1 345 ? 17.763  17.946  59.949 1.00 28.70  ? 471 ARG   A CG    1 
ATOM   2423 C CD    . ARG   A 1 345 ? 16.358  17.499  60.268 1.00 29.71  ? 471 ARG   A CD    1 
ATOM   2424 N NE    . ARG   A 1 345 ? 15.884  18.212  61.444 1.00 31.69  ? 471 ARG   A NE    1 
ATOM   2425 C CZ    . ARG   A 1 345 ? 16.173  17.830  62.677 1.00 32.40  ? 471 ARG   A CZ    1 
ATOM   2426 N NH1   . ARG   A 1 345 ? 16.863  16.722  62.907 1.00 32.42  ? 471 ARG   A NH1   1 
ATOM   2427 N NH2   . ARG   A 1 345 ? 15.771  18.580  63.704 1.00 34.15  ? 471 ARG   A NH2   1 
ATOM   2428 N N     . ILE   A 1 346 ? 20.745  18.830  58.112 1.00 27.08  ? 472 ILE   A N     1 
ATOM   2429 C CA    . ILE   A 1 346 ? 21.307  18.338  56.867 1.00 27.26  ? 472 ILE   A CA    1 
ATOM   2430 C C     . ILE   A 1 346 ? 20.568  17.075  56.469 1.00 28.34  ? 472 ILE   A C     1 
ATOM   2431 O O     . ILE   A 1 346 ? 20.429  16.152  57.273 1.00 29.17  ? 472 ILE   A O     1 
ATOM   2432 C CB    . ILE   A 1 346 ? 22.807  18.066  57.039 1.00 30.05  ? 472 ILE   A CB    1 
ATOM   2433 C CG1   . ILE   A 1 346 ? 23.527  19.358  57.383 1.00 30.81  ? 472 ILE   A CG1   1 
ATOM   2434 C CG2   . ILE   A 1 346 ? 23.370  17.391  55.802 1.00 29.90  ? 472 ILE   A CG2   1 
ATOM   2435 C CD1   . ILE   A 1 346 ? 24.925  19.093  57.937 1.00 32.27  ? 472 ILE   A CD1   1 
ATOM   2436 N N     . TYR   A 1 347 ? 20.048  17.053  55.244 1.00 26.80  ? 473 TYR   A N     1 
ATOM   2437 C CA    . TYR   A 1 347 ? 19.411  15.867  54.704 1.00 28.30  ? 473 TYR   A CA    1 
ATOM   2438 C C     . TYR   A 1 347 ? 20.513  14.933  54.246 1.00 31.96  ? 473 TYR   A C     1 
ATOM   2439 O O     . TYR   A 1 347 ? 21.338  15.326  53.419 1.00 29.76  ? 473 TYR   A O     1 
ATOM   2440 C CB    . TYR   A 1 347 ? 18.514  16.238  53.526 1.00 27.58  ? 473 TYR   A CB    1 
ATOM   2441 C CG    . TYR   A 1 347 ? 17.576  15.141  53.118 1.00 29.75  ? 473 TYR   A CG    1 
ATOM   2442 C CD1   . TYR   A 1 347 ? 17.959  14.163  52.212 1.00 31.82  ? 473 TYR   A CD1   1 
ATOM   2443 C CD2   . TYR   A 1 347 ? 16.284  15.107  53.615 1.00 30.57  ? 473 TYR   A CD2   1 
ATOM   2444 C CE1   . TYR   A 1 347 ? 17.079  13.151  51.842 1.00 33.29  ? 473 TYR   A CE1   1 
ATOM   2445 C CE2   . TYR   A 1 347 ? 15.413  14.123  53.244 1.00 29.81  ? 473 TYR   A CE2   1 
ATOM   2446 C CZ    . TYR   A 1 347 ? 15.808  13.144  52.373 1.00 30.31  ? 473 TYR   A CZ    1 
ATOM   2447 O OH    . TYR   A 1 347 ? 14.913  12.166  52.031 1.00 34.86  ? 473 TYR   A OH    1 
ATOM   2448 N N     . ALA   A 1 348 ? 20.546  13.717  54.793 1.00 29.31  ? 474 ALA   A N     1 
ATOM   2449 C CA    . ALA   A 1 348 ? 21.670  12.803  54.605 1.00 30.49  ? 474 ALA   A CA    1 
ATOM   2450 C C     . ALA   A 1 348 ? 21.247  11.563  53.831 1.00 32.28  ? 474 ALA   A C     1 
ATOM   2451 O O     . ALA   A 1 348 ? 20.694  10.618  54.422 1.00 30.83  ? 474 ALA   A O     1 
ATOM   2452 C CB    . ALA   A 1 348 ? 22.236  12.419  55.977 1.00 33.17  ? 474 ALA   A CB    1 
ATOM   2453 N N     . PRO   A 1 349 ? 21.469  11.513  52.515 1.00 29.76  ? 475 PRO   A N     1 
ATOM   2454 C CA    . PRO   A 1 349 ? 21.150  10.296  51.769 1.00 32.61  ? 475 PRO   A CA    1 
ATOM   2455 C C     . PRO   A 1 349 ? 22.125  9.199   52.143 1.00 37.34  ? 475 PRO   A C     1 
ATOM   2456 O O     . PRO   A 1 349 ? 23.324  9.442   52.302 1.00 38.08  ? 475 PRO   A O     1 
ATOM   2457 C CB    . PRO   A 1 349 ? 21.304  10.718  50.296 1.00 34.65  ? 475 PRO   A CB    1 
ATOM   2458 C CG    . PRO   A 1 349 ? 21.273  12.198  50.316 1.00 32.66  ? 475 PRO   A CG    1 
ATOM   2459 C CD    . PRO   A 1 349 ? 21.856  12.623  51.627 1.00 31.96  ? 475 PRO   A CD    1 
ATOM   2460 N N     . VAL   A 1 350 ? 21.594  7.991   52.314 1.00 35.50  ? 476 VAL   A N     1 
ATOM   2461 C CA    . VAL   A 1 350 ? 22.379  6.834   52.715 1.00 37.89  ? 476 VAL   A CA    1 
ATOM   2462 C C     . VAL   A 1 350 ? 22.051  5.692   51.764 1.00 40.22  ? 476 VAL   A C     1 
ATOM   2463 O O     . VAL   A 1 350 ? 20.884  5.306   51.636 1.00 41.28  ? 476 VAL   A O     1 
ATOM   2464 C CB    . VAL   A 1 350 ? 22.084  6.429   54.171 1.00 39.09  ? 476 VAL   A CB    1 
ATOM   2465 C CG1   . VAL   A 1 350 ? 22.937  5.244   54.586 1.00 42.83  ? 476 VAL   A CG1   1 
ATOM   2466 C CG2   . VAL   A 1 350 ? 22.284  7.635   55.105 1.00 39.33  ? 476 VAL   A CG2   1 
ATOM   2467 N N     . GLY   A 1 351 ? 23.062  5.148   51.112 1.00 36.04  ? 477 GLY   A N     1 
ATOM   2468 C CA    . GLY   A 1 351 ? 22.828  4.023   50.229 1.00 43.24  ? 477 GLY   A CA    1 
ATOM   2469 C C     . GLY   A 1 351 ? 23.962  3.818   49.250 1.00 46.51  ? 477 GLY   A C     1 
ATOM   2470 O O     . GLY   A 1 351 ? 24.954  4.548   49.234 1.00 44.20  ? 477 GLY   A O     1 
ATOM   2471 N N     . THR   A 1 352 ? 23.788  2.780   48.435 1.00 50.70  ? 478 THR   A N     1 
ATOM   2472 C CA    . THR   A 1 352 ? 24.690  2.488   47.330 1.00 55.72  ? 478 THR   A CA    1 
ATOM   2473 C C     . THR   A 1 352 ? 24.566  3.557   46.248 1.00 54.03  ? 478 THR   A C     1 
ATOM   2474 O O     . THR   A 1 352 ? 23.611  4.340   46.214 1.00 57.25  ? 478 THR   A O     1 
ATOM   2475 C CB    . THR   A 1 352 ? 24.375  1.123   46.721 1.00 57.43  ? 478 THR   A CB    1 
ATOM   2476 O OG1   . THR   A 1 352 ? 23.123  1.199   46.024 1.00 56.61  ? 478 THR   A OG1   1 
ATOM   2477 C CG2   . THR   A 1 352 ? 24.280  0.061   47.811 1.00 55.12  ? 478 THR   A CG2   1 
ATOM   2478 N N     . HIS   A 1 353 ? 25.548  3.585   45.347 1.00 62.14  ? 479 HIS   A N     1 
ATOM   2479 C CA    . HIS   A 1 353 ? 25.469  4.546   44.251 1.00 61.30  ? 479 HIS   A CA    1 
ATOM   2480 C C     . HIS   A 1 353 ? 24.308  4.222   43.317 1.00 59.36  ? 479 HIS   A C     1 
ATOM   2481 O O     . HIS   A 1 353 ? 23.678  5.138   42.778 1.00 58.65  ? 479 HIS   A O     1 
ATOM   2482 C CB    . HIS   A 1 353 ? 26.790  4.598   43.478 1.00 65.92  ? 479 HIS   A CB    1 
ATOM   2483 C CG    . HIS   A 1 353 ? 27.067  5.934   42.853 1.00 69.80  ? 479 HIS   A CG    1 
ATOM   2484 N ND1   . HIS   A 1 353 ? 27.003  6.149   41.493 1.00 68.63  ? 479 HIS   A ND1   1 
ATOM   2485 C CD2   . HIS   A 1 353 ? 27.396  7.127   43.407 1.00 68.13  ? 479 HIS   A CD2   1 
ATOM   2486 C CE1   . HIS   A 1 353 ? 27.288  7.414   41.234 1.00 65.84  ? 479 HIS   A CE1   1 
ATOM   2487 N NE2   . HIS   A 1 353 ? 27.529  8.029   42.378 1.00 70.17  ? 479 HIS   A NE2   1 
ATOM   2488 N N     . GLU   A 1 354 ? 23.983  2.936   43.151 1.00 54.99  ? 480 GLU   A N     1 
ATOM   2489 C CA    . GLU   A 1 354 ? 22.892  2.559   42.258 1.00 55.61  ? 480 GLU   A CA    1 
ATOM   2490 C C     . GLU   A 1 354 ? 21.536  3.018   42.791 1.00 54.64  ? 480 GLU   A C     1 
ATOM   2491 O O     . GLU   A 1 354 ? 20.706  3.528   42.031 1.00 55.03  ? 480 GLU   A O     1 
ATOM   2492 C CB    . GLU   A 1 354 ? 22.894  1.051   42.029 1.00 57.09  ? 480 GLU   A CB    1 
ATOM   2493 C CG    . GLU   A 1 354 ? 21.985  0.602   40.892 1.00 60.51  ? 480 GLU   A CG    1 
ATOM   2494 C CD    . GLU   A 1 354 ? 22.563  0.880   39.499 1.00 63.50  ? 480 GLU   A CD    1 
ATOM   2495 O OE1   . GLU   A 1 354 ? 23.491  1.712   39.365 1.00 61.52  ? 480 GLU   A OE1   1 
ATOM   2496 O OE2   . GLU   A 1 354 ? 22.080  0.260   38.528 1.00 65.17  ? 480 GLU   A OE2   1 
ATOM   2497 N N     . THR   A 1 355 ? 21.281  2.843   44.090 1.00 50.93  ? 481 THR   A N     1 
ATOM   2498 C CA    . THR   A 1 355 ? 19.978  3.241   44.614 1.00 55.54  ? 481 THR   A CA    1 
ATOM   2499 C C     . THR   A 1 355 ? 19.781  4.751   44.605 1.00 52.75  ? 481 THR   A C     1 
ATOM   2500 O O     . THR   A 1 355 ? 18.640  5.214   44.704 1.00 53.86  ? 481 THR   A O     1 
ATOM   2501 C CB    . THR   A 1 355 ? 19.777  2.719   46.035 1.00 55.69  ? 481 THR   A CB    1 
ATOM   2502 O OG1   . THR   A 1 355 ? 18.430  2.986   46.445 1.00 58.87  ? 481 THR   A OG1   1 
ATOM   2503 C CG2   . THR   A 1 355 ? 20.722  3.424   47.004 1.00 52.60  ? 481 THR   A CG2   1 
ATOM   2504 N N     . LEU   A 1 356 ? 20.855  5.528   44.478 1.00 50.26  ? 482 LEU   A N     1 
ATOM   2505 C CA    . LEU   A 1 356 ? 20.781  6.978   44.568 1.00 49.92  ? 482 LEU   A CA    1 
ATOM   2506 C C     . LEU   A 1 356 ? 20.909  7.659   43.211 1.00 47.58  ? 482 LEU   A C     1 
ATOM   2507 O O     . LEU   A 1 356 ? 21.001  8.891   43.152 1.00 41.37  ? 482 LEU   A O     1 
ATOM   2508 C CB    . LEU   A 1 356 ? 21.858  7.493   45.525 1.00 54.68  ? 482 LEU   A CB    1 
ATOM   2509 N N     . LEU   A 1 357 ? 20.910  6.887   42.122 1.00 47.72  ? 483 LEU   A N     1 
ATOM   2510 C CA    . LEU   A 1 357 ? 21.077  7.468   40.795 1.00 44.83  ? 483 LEU   A CA    1 
ATOM   2511 C C     . LEU   A 1 357 ? 19.986  8.484   40.497 1.00 44.09  ? 483 LEU   A C     1 
ATOM   2512 O O     . LEU   A 1 357 ? 20.268  9.591   40.026 1.00 45.48  ? 483 LEU   A O     1 
ATOM   2513 C CB    . LEU   A 1 357 ? 21.085  6.363   39.745 1.00 50.45  ? 483 LEU   A CB    1 
ATOM   2514 C CG    . LEU   A 1 357 ? 22.005  6.595   38.555 1.00 53.38  ? 483 LEU   A CG    1 
ATOM   2515 C CD1   . LEU   A 1 357 ? 23.334  7.177   39.005 1.00 54.50  ? 483 LEU   A CD1   1 
ATOM   2516 C CD2   . LEU   A 1 357 ? 22.223  5.281   37.854 1.00 52.29  ? 483 LEU   A CD2   1 
ATOM   2517 N N     . ALA   A 1 358 ? 18.728  8.130   40.769 1.00 42.78  ? 484 ALA   A N     1 
ATOM   2518 C CA    . ALA   A 1 358 ? 17.634  9.051   40.467 1.00 45.31  ? 484 ALA   A CA    1 
ATOM   2519 C C     . ALA   A 1 358 ? 17.771  10.348  41.255 1.00 41.71  ? 484 ALA   A C     1 
ATOM   2520 O O     . ALA   A 1 358 ? 17.499  11.437  40.732 1.00 40.94  ? 484 ALA   A O     1 
ATOM   2521 C CB    . ALA   A 1 358 ? 16.288  8.389   40.761 1.00 48.89  ? 484 ALA   A CB    1 
ATOM   2522 N N     . TYR   A 1 359 ? 18.189  10.245  42.520 1.00 38.37  ? 485 TYR   A N     1 
ATOM   2523 C CA    . TYR   A 1 359 ? 18.466  11.417  43.343 1.00 37.35  ? 485 TYR   A CA    1 
ATOM   2524 C C     . TYR   A 1 359 ? 19.599  12.254  42.758 1.00 37.19  ? 485 TYR   A C     1 
ATOM   2525 O O     . TYR   A 1 359 ? 19.503  13.483  42.692 1.00 34.66  ? 485 TYR   A O     1 
ATOM   2526 C CB    . TYR   A 1 359 ? 18.802  10.952  44.759 1.00 34.46  ? 485 TYR   A CB    1 
ATOM   2527 C CG    . TYR   A 1 359 ? 19.200  12.032  45.743 1.00 34.62  ? 485 TYR   A CG    1 
ATOM   2528 C CD1   . TYR   A 1 359 ? 18.239  12.708  46.493 1.00 32.52  ? 485 TYR   A CD1   1 
ATOM   2529 C CD2   . TYR   A 1 359 ? 20.539  12.355  45.947 1.00 32.73  ? 485 TYR   A CD2   1 
ATOM   2530 C CE1   . TYR   A 1 359 ? 18.599  13.689  47.422 1.00 30.74  ? 485 TYR   A CE1   1 
ATOM   2531 C CE2   . TYR   A 1 359 ? 20.905  13.346  46.866 1.00 31.02  ? 485 TYR   A CE2   1 
ATOM   2532 C CZ    . TYR   A 1 359 ? 19.936  14.009  47.591 1.00 30.14  ? 485 TYR   A CZ    1 
ATOM   2533 O OH    . TYR   A 1 359 ? 20.297  14.962  48.516 1.00 29.98  ? 485 TYR   A OH    1 
ATOM   2534 N N     . LEU   A 1 360 ? 20.679  11.610  42.321 1.00 36.97  ? 486 LEU   A N     1 
ATOM   2535 C CA    . LEU   A 1 360 ? 21.787  12.361  41.734 1.00 38.56  ? 486 LEU   A CA    1 
ATOM   2536 C C     . LEU   A 1 360 ? 21.369  13.046  40.435 1.00 38.09  ? 486 LEU   A C     1 
ATOM   2537 O O     . LEU   A 1 360 ? 21.814  14.164  40.141 1.00 40.45  ? 486 LEU   A O     1 
ATOM   2538 C CB    . LEU   A 1 360 ? 22.983  11.439  41.506 1.00 42.24  ? 486 LEU   A CB    1 
ATOM   2539 N N     . VAL   A 1 361 ? 20.499  12.409  39.651 1.00 39.59  ? 487 VAL   A N     1 
ATOM   2540 C CA    . VAL   A 1 361 ? 19.984  13.084  38.460 1.00 36.49  ? 487 VAL   A CA    1 
ATOM   2541 C C     . VAL   A 1 361 ? 19.299  14.382  38.859 1.00 37.90  ? 487 VAL   A C     1 
ATOM   2542 O O     . VAL   A 1 361 ? 19.546  15.444  38.274 1.00 40.80  ? 487 VAL   A O     1 
ATOM   2543 C CB    . VAL   A 1 361 ? 19.029  12.168  37.671 1.00 40.47  ? 487 VAL   A CB    1 
ATOM   2544 C CG1   . VAL   A 1 361 ? 18.251  12.985  36.606 1.00 46.24  ? 487 VAL   A CG1   1 
ATOM   2545 C CG2   . VAL   A 1 361 ? 19.795  11.071  36.970 1.00 41.71  ? 487 VAL   A CG2   1 
ATOM   2546 N N     . ARG   A 1 362 ? 18.458  14.327  39.897 1.00 38.11  ? 488 ARG   A N     1 
ATOM   2547 C CA    . ARG   A 1 362 ? 17.785  15.538  40.345 1.00 36.80  ? 488 ARG   A CA    1 
ATOM   2548 C C     . ARG   A 1 362 ? 18.785  16.570  40.848 1.00 38.70  ? 488 ARG   A C     1 
ATOM   2549 O O     . ARG   A 1 362 ? 18.595  17.774  40.634 1.00 39.60  ? 488 ARG   A O     1 
ATOM   2550 C CB    . ARG   A 1 362 ? 16.735  15.196  41.403 1.00 36.66  ? 488 ARG   A CB    1 
ATOM   2551 C CG    . ARG   A 1 362 ? 15.553  14.459  40.775 1.00 35.84  ? 488 ARG   A CG    1 
ATOM   2552 C CD    . ARG   A 1 362 ? 14.389  14.399  41.721 1.00 37.78  ? 488 ARG   A CD    1 
ATOM   2553 N NE    . ARG   A 1 362 ? 14.720  13.674  42.936 1.00 35.96  ? 488 ARG   A NE    1 
ATOM   2554 C CZ    . ARG   A 1 362 ? 14.571  12.368  43.087 1.00 38.11  ? 488 ARG   A CZ    1 
ATOM   2555 N NH1   . ARG   A 1 362 ? 14.120  11.608  42.107 1.00 38.67  ? 488 ARG   A NH1   1 
ATOM   2556 N NH2   . ARG   A 1 362 ? 14.850  11.817  44.268 1.00 39.05  ? 488 ARG   A NH2   1 
ATOM   2557 N N     . ARG   A 1 363 ? 19.869  16.122  41.501 1.00 34.34  ? 489 ARG   A N     1 
ATOM   2558 C CA    . ARG   A 1 363 ? 20.907  17.061  41.921 1.00 36.49  ? 489 ARG   A CA    1 
ATOM   2559 C C     . ARG   A 1 363 ? 21.613  17.681  40.724 1.00 36.74  ? 489 ARG   A C     1 
ATOM   2560 O O     . ARG   A 1 363 ? 22.033  18.843  40.781 1.00 36.14  ? 489 ARG   A O     1 
ATOM   2561 C CB    . ARG   A 1 363 ? 21.933  16.383  42.828 1.00 34.89  ? 489 ARG   A CB    1 
ATOM   2562 C CG    . ARG   A 1 363 ? 21.363  15.754  44.088 1.00 35.34  ? 489 ARG   A CG    1 
ATOM   2563 C CD    . ARG   A 1 363 ? 20.904  16.802  45.128 1.00 35.25  ? 489 ARG   A CD    1 
ATOM   2564 N NE    . ARG   A 1 363 ? 19.687  17.513  44.748 1.00 33.78  ? 489 ARG   A NE    1 
ATOM   2565 C CZ    . ARG   A 1 363 ? 18.484  16.961  44.717 1.00 35.42  ? 489 ARG   A CZ    1 
ATOM   2566 N NH1   . ARG   A 1 363 ? 18.312  15.666  44.942 1.00 30.87  ? 489 ARG   A NH1   1 
ATOM   2567 N NH2   . ARG   A 1 363 ? 17.422  17.729  44.477 1.00 34.53  ? 489 ARG   A NH2   1 
ATOM   2568 N N     . LEU   A 1 364 ? 21.775  16.916  39.635 1.00 39.05  ? 490 LEU   A N     1 
ATOM   2569 C CA    . LEU   A 1 364 ? 22.325  17.479  38.407 1.00 37.99  ? 490 LEU   A CA    1 
ATOM   2570 C C     . LEU   A 1 364 ? 21.395  18.541  37.832 1.00 42.85  ? 490 LEU   A C     1 
ATOM   2571 O O     . LEU   A 1 364 ? 21.832  19.638  37.458 1.00 41.23  ? 490 LEU   A O     1 
ATOM   2572 C CB    . LEU   A 1 364 ? 22.571  16.356  37.395 1.00 36.68  ? 490 LEU   A CB    1 
ATOM   2573 C CG    . LEU   A 1 364 ? 23.054  16.685  35.978 1.00 42.63  ? 490 LEU   A CG    1 
ATOM   2574 C CD1   . LEU   A 1 364 ? 24.216  17.649  36.031 1.00 48.73  ? 490 LEU   A CD1   1 
ATOM   2575 C CD2   . LEU   A 1 364 ? 23.453  15.416  35.257 1.00 44.74  ? 490 LEU   A CD2   1 
ATOM   2576 N N     . LEU   A 1 365 ? 20.100  18.234  37.763 1.00 39.99  ? 491 LEU   A N     1 
ATOM   2577 C CA    . LEU   A 1 365 ? 19.139  19.208  37.259 1.00 41.84  ? 491 LEU   A CA    1 
ATOM   2578 C C     . LEU   A 1 365 ? 19.123  20.455  38.124 1.00 40.69  ? 491 LEU   A C     1 
ATOM   2579 O O     . LEU   A 1 365 ? 19.060  21.578  37.613 1.00 43.88  ? 491 LEU   A O     1 
ATOM   2580 C CB    . LEU   A 1 365 ? 17.749  18.576  37.193 1.00 43.34  ? 491 LEU   A CB    1 
ATOM   2581 C CG    . LEU   A 1 365 ? 17.670  17.465  36.141 1.00 42.21  ? 491 LEU   A CG    1 
ATOM   2582 C CD1   . LEU   A 1 365 ? 16.346  16.741  36.250 1.00 46.92  ? 491 LEU   A CD1   1 
ATOM   2583 C CD2   . LEU   A 1 365 ? 17.841  18.062  34.762 1.00 45.52  ? 491 LEU   A CD2   1 
ATOM   2584 N N     . GLU   A 1 366 ? 19.205  20.269  39.439 1.00 38.40  ? 492 GLU   A N     1 
ATOM   2585 C CA    . GLU   A 1 366 ? 19.204  21.386  40.367 1.00 40.57  ? 492 GLU   A CA    1 
ATOM   2586 C C     . GLU   A 1 366 ? 20.497  22.183  40.269 1.00 42.23  ? 492 GLU   A C     1 
ATOM   2587 O O     . GLU   A 1 366 ? 20.468  23.414  40.187 1.00 44.56  ? 492 GLU   A O     1 
ATOM   2588 C CB    . GLU   A 1 366 ? 18.998  20.859  41.785 1.00 36.83  ? 492 GLU   A CB    1 
ATOM   2589 C CG    . GLU   A 1 366 ? 19.020  21.924  42.842 1.00 38.90  ? 492 GLU   A CG    1 
ATOM   2590 C CD    . GLU   A 1 366 ? 18.829  21.347  44.235 1.00 35.28  ? 492 GLU   A CD    1 
ATOM   2591 O OE1   . GLU   A 1 366 ? 18.779  20.100  44.382 1.00 38.66  ? 492 GLU   A OE1   1 
ATOM   2592 O OE2   . GLU   A 1 366 ? 18.742  22.141  45.184 1.00 35.27  ? 492 GLU   A OE2   1 
ATOM   2593 N N     . ASN   A 1 367 ? 21.644  21.502  40.272 1.00 37.01  ? 493 ASN   A N     1 
ATOM   2594 C CA    . ASN   A 1 367 ? 22.910  22.223  40.313 1.00 39.38  ? 493 ASN   A CA    1 
ATOM   2595 C C     . ASN   A 1 367 ? 23.294  22.800  38.956 1.00 41.64  ? 493 ASN   A C     1 
ATOM   2596 O O     . ASN   A 1 367 ? 24.020  23.799  38.900 1.00 43.01  ? 493 ASN   A O     1 
ATOM   2597 C CB    . ASN   A 1 367 ? 24.028  21.310  40.817 1.00 41.05  ? 493 ASN   A CB    1 
ATOM   2598 C CG    . ASN   A 1 367 ? 24.039  21.188  42.331 1.00 43.35  ? 493 ASN   A CG    1 
ATOM   2599 O OD1   . ASN   A 1 367 ? 24.702  21.962  43.019 1.00 47.51  ? 493 ASN   A OD1   1 
ATOM   2600 N ND2   . ASN   A 1 367 ? 23.290  20.228  42.856 1.00 41.24  ? 493 ASN   A ND2   1 
ATOM   2601 N N     . GLY   A 1 368 ? 22.827  22.195  37.863 1.00 42.08  ? 494 GLY   A N     1 
ATOM   2602 C CA    . GLY   A 1 368 ? 23.251  22.602  36.538 1.00 41.84  ? 494 GLY   A CA    1 
ATOM   2603 C C     . GLY   A 1 368 ? 22.369  23.609  35.844 1.00 44.39  ? 494 GLY   A C     1 
ATOM   2604 O O     . GLY   A 1 368 ? 22.715  24.081  34.762 1.00 43.83  ? 494 GLY   A O     1 
ATOM   2605 N N     . ALA   A 1 369 ? 21.228  23.952  36.424 1.00 43.05  ? 495 ALA   A N     1 
ATOM   2606 C CA    . ALA   A 1 369 ? 20.315  24.882  35.778 1.00 42.74  ? 495 ALA   A CA    1 
ATOM   2607 C C     . ALA   A 1 369 ? 20.809  26.312  35.957 1.00 41.93  ? 495 ALA   A C     1 
ATOM   2608 O O     . ALA   A 1 369 ? 21.153  26.724  37.073 1.00 42.29  ? 495 ALA   A O     1 
ATOM   2609 C CB    . ALA   A 1 369 ? 18.912  24.724  36.365 1.00 44.37  ? 495 ALA   A CB    1 
ATOM   2610 N N     . ASN   A 1 370 ? 20.822  27.079  34.858 1.00 42.86  ? 496 ASN   A N     1 
ATOM   2611 C CA    . ASN   A 1 370 ? 21.229  28.478  34.942 1.00 43.14  ? 496 ASN   A CA    1 
ATOM   2612 C C     . ASN   A 1 370 ? 20.378  29.262  35.937 1.00 44.00  ? 496 ASN   A C     1 
ATOM   2613 O O     . ASN   A 1 370 ? 20.830  30.278  36.478 1.00 44.80  ? 496 ASN   A O     1 
ATOM   2614 C CB    . ASN   A 1 370 ? 21.171  29.131  33.556 1.00 48.33  ? 496 ASN   A CB    1 
ATOM   2615 N N     . SER   A 1 371 ? 19.160  28.796  36.220 1.00 41.21  ? 497 SER   A N     1 
ATOM   2616 C CA    . SER   A 1 371 ? 18.291  29.509  37.144 1.00 41.51  ? 497 SER   A CA    1 
ATOM   2617 C C     . SER   A 1 371 ? 18.582  29.194  38.605 1.00 40.11  ? 497 SER   A C     1 
ATOM   2618 O O     . SER   A 1 371 ? 18.078  29.897  39.481 1.00 39.02  ? 497 SER   A O     1 
ATOM   2619 C CB    . SER   A 1 371 ? 16.825  29.188  36.853 1.00 40.53  ? 497 SER   A CB    1 
ATOM   2620 O OG    . SER   A 1 371 ? 16.555  27.817  37.062 1.00 41.79  ? 497 SER   A OG    1 
ATOM   2621 N N     . SER   A 1 372 ? 19.365  28.165  38.895 1.00 38.90  ? 498 SER   A N     1 
ATOM   2622 C CA    . SER   A 1 372 ? 19.571  27.773  40.283 1.00 37.64  ? 498 SER   A CA    1 
ATOM   2623 C C     . SER   A 1 372 ? 20.576  28.685  40.969 1.00 36.38  ? 498 SER   A C     1 
ATOM   2624 O O     . SER   A 1 372 ? 21.635  28.998  40.416 1.00 34.04  ? 498 SER   A O     1 
ATOM   2625 C CB    . SER   A 1 372 ? 20.049  26.327  40.366 1.00 39.39  ? 498 SER   A CB    1 
ATOM   2626 O OG    . SER   A 1 372 ? 19.012  25.436  39.987 1.00 37.41  ? 498 SER   A OG    1 
ATOM   2627 N N     . PHE   A 1 373 ? 20.237  29.095  42.194 1.00 36.86  ? 499 PHE   A N     1 
ATOM   2628 C CA    . PHE   A 1 373 ? 21.165  29.875  43.005 1.00 36.60  ? 499 PHE   A CA    1 
ATOM   2629 C C     . PHE   A 1 373 ? 22.539  29.223  43.057 1.00 33.41  ? 499 PHE   A C     1 
ATOM   2630 O O     . PHE   A 1 373 ? 23.565  29.898  42.932 1.00 35.84  ? 499 PHE   A O     1 
ATOM   2631 C CB    . PHE   A 1 373 ? 20.617  30.043  44.427 1.00 36.20  ? 499 PHE   A CB    1 
ATOM   2632 C CG    . PHE   A 1 373 ? 21.589  30.708  45.357 1.00 34.02  ? 499 PHE   A CG    1 
ATOM   2633 C CD1   . PHE   A 1 373 ? 22.534  29.964  46.047 1.00 33.23  ? 499 PHE   A CD1   1 
ATOM   2634 C CD2   . PHE   A 1 373 ? 21.606  32.084  45.481 1.00 36.58  ? 499 PHE   A CD2   1 
ATOM   2635 C CE1   . PHE   A 1 373 ? 23.451  30.577  46.874 1.00 36.53  ? 499 PHE   A CE1   1 
ATOM   2636 C CE2   . PHE   A 1 373 ? 22.523  32.704  46.313 1.00 37.06  ? 499 PHE   A CE2   1 
ATOM   2637 C CZ    . PHE   A 1 373 ? 23.439  31.943  47.018 1.00 36.13  ? 499 PHE   A CZ    1 
ATOM   2638 N N     . VAL   A 1 374 ? 22.581  27.909  43.272 1.00 37.71  ? 500 VAL   A N     1 
ATOM   2639 C CA    . VAL   A 1 374 ? 23.871  27.257  43.434 1.00 35.89  ? 500 VAL   A CA    1 
ATOM   2640 C C     . VAL   A 1 374 ? 24.646  27.270  42.134 1.00 38.63  ? 500 VAL   A C     1 
ATOM   2641 O O     . VAL   A 1 374 ? 25.883  27.225  42.139 1.00 39.20  ? 500 VAL   A O     1 
ATOM   2642 C CB    . VAL   A 1 374 ? 23.685  25.828  43.977 1.00 39.15  ? 500 VAL   A CB    1 
ATOM   2643 C CG1   . VAL   A 1 374 ? 22.973  25.874  45.301 1.00 38.15  ? 500 VAL   A CG1   1 
ATOM   2644 C CG2   . VAL   A 1 374 ? 22.917  24.955  42.983 1.00 38.88  ? 500 VAL   A CG2   1 
ATOM   2645 N N     . HIS   A 1 375 ? 23.957  27.371  40.999 1.00 37.13  ? 501 HIS   A N     1 
ATOM   2646 C CA    . HIS   A 1 375 ? 24.691  27.548  39.757 1.00 37.35  ? 501 HIS   A CA    1 
ATOM   2647 C C     . HIS   A 1 375 ? 25.127  28.996  39.599 1.00 43.38  ? 501 HIS   A C     1 
ATOM   2648 O O     . HIS   A 1 375 ? 26.279  29.277  39.252 1.00 43.27  ? 501 HIS   A O     1 
ATOM   2649 C CB    . HIS   A 1 375 ? 23.829  27.124  38.571 1.00 42.20  ? 501 HIS   A CB    1 
ATOM   2650 C CG    . HIS   A 1 375 ? 24.564  27.150  37.268 1.00 42.50  ? 501 HIS   A CG    1 
ATOM   2651 N ND1   . HIS   A 1 375 ? 24.688  28.292  36.508 1.00 45.65  ? 501 HIS   A ND1   1 
ATOM   2652 C CD2   . HIS   A 1 375 ? 25.247  26.183  36.609 1.00 46.38  ? 501 HIS   A CD2   1 
ATOM   2653 C CE1   . HIS   A 1 375 ? 25.397  28.024  35.425 1.00 47.23  ? 501 HIS   A CE1   1 
ATOM   2654 N NE2   . HIS   A 1 375 ? 25.751  26.751  35.465 1.00 48.12  ? 501 HIS   A NE2   1 
ATOM   2655 N N     . ARG   A 1 376 ? 24.209  29.925  39.864 1.00 40.56  ? 502 ARG   A N     1 
ATOM   2656 C CA    . ARG   A 1 376 ? 24.488  31.339  39.669 1.00 40.83  ? 502 ARG   A CA    1 
ATOM   2657 C C     . ARG   A 1 376 ? 25.602  31.830  40.577 1.00 40.89  ? 502 ARG   A C     1 
ATOM   2658 O O     . ARG   A 1 376 ? 26.370  32.715  40.186 1.00 43.72  ? 502 ARG   A O     1 
ATOM   2659 C CB    . ARG   A 1 376 ? 23.204  32.132  39.895 1.00 39.94  ? 502 ARG   A CB    1 
ATOM   2660 C CG    . ARG   A 1 376 ? 22.282  32.033  38.707 1.00 42.50  ? 502 ARG   A CG    1 
ATOM   2661 C CD    . ARG   A 1 376 ? 20.839  32.005  39.141 1.00 45.28  ? 502 ARG   A CD    1 
ATOM   2662 N NE    . ARG   A 1 376 ? 20.508  33.157  39.965 1.00 45.63  ? 502 ARG   A NE    1 
ATOM   2663 C CZ    . ARG   A 1 376 ? 20.207  34.358  39.498 1.00 48.18  ? 502 ARG   A CZ    1 
ATOM   2664 N NH1   . ARG   A 1 376 ? 20.221  34.620  38.201 1.00 50.29  ? 502 ARG   A NH1   1 
ATOM   2665 N NH2   . ARG   A 1 376 ? 19.884  35.320  40.356 1.00 50.17  ? 502 ARG   A NH2   1 
ATOM   2666 N N     . ILE   A 1 377 ? 25.722  31.258  41.777 1.00 43.64  ? 503 ILE   A N     1 
ATOM   2667 C CA    . ILE   A 1 377 ? 26.715  31.730  42.733 1.00 42.98  ? 503 ILE   A CA    1 
ATOM   2668 C C     . ILE   A 1 377 ? 28.122  31.518  42.196 1.00 46.40  ? 503 ILE   A C     1 
ATOM   2669 O O     . ILE   A 1 377 ? 29.055  32.218  42.605 1.00 48.87  ? 503 ILE   A O     1 
ATOM   2670 C CB    . ILE   A 1 377 ? 26.508  31.033  44.092 1.00 44.46  ? 503 ILE   A CB    1 
ATOM   2671 C CG1   . ILE   A 1 377 ? 27.310  31.734  45.187 1.00 45.26  ? 503 ILE   A CG1   1 
ATOM   2672 C CG2   . ILE   A 1 377 ? 26.894  29.571  44.003 1.00 43.97  ? 503 ILE   A CG2   1 
ATOM   2673 C CD1   . ILE   A 1 377 ? 26.696  33.018  45.652 1.00 46.06  ? 503 ILE   A CD1   1 
ATOM   2674 N N     . ASN   A 1 378 ? 28.289  30.586  41.257 1.00 44.03  ? 504 ASN   A N     1 
ATOM   2675 C CA    . ASN   A 1 378 ? 29.559  30.313  40.594 1.00 50.40  ? 504 ASN   A CA    1 
ATOM   2676 C C     . ASN   A 1 378 ? 29.649  30.943  39.215 1.00 50.13  ? 504 ASN   A C     1 
ATOM   2677 O O     . ASN   A 1 378 ? 30.669  30.792  38.537 1.00 52.67  ? 504 ASN   A O     1 
ATOM   2678 C CB    . ASN   A 1 378 ? 29.769  28.804  40.472 1.00 51.89  ? 504 ASN   A CB    1 
ATOM   2679 C CG    . ASN   A 1 378 ? 29.863  28.132  41.814 1.00 54.02  ? 504 ASN   A CG    1 
ATOM   2680 O OD1   . ASN   A 1 378 ? 30.319  28.736  42.788 1.00 56.35  ? 504 ASN   A OD1   1 
ATOM   2681 N ND2   . ASN   A 1 378 ? 29.426  26.878  41.886 1.00 57.84  ? 504 ASN   A ND2   1 
ATOM   2682 N N     . ASP   A 1 379 ? 28.609  31.646  38.789 1.00 49.84  ? 505 ASP   A N     1 
ATOM   2683 C CA    . ASP   A 1 379 ? 28.552  32.192  37.445 1.00 52.51  ? 505 ASP   A CA    1 
ATOM   2684 C C     . ASP   A 1 379 ? 29.182  33.579  37.453 1.00 55.28  ? 505 ASP   A C     1 
ATOM   2685 O O     . ASP   A 1 379 ? 28.612  34.498  38.060 1.00 52.57  ? 505 ASP   A O     1 
ATOM   2686 C CB    . ASP   A 1 379 ? 27.107  32.254  36.973 1.00 51.16  ? 505 ASP   A CB    1 
ATOM   2687 C CG    . ASP   A 1 379 ? 26.987  32.476  35.486 1.00 56.80  ? 505 ASP   A CG    1 
ATOM   2688 O OD1   . ASP   A 1 379 ? 27.844  33.183  34.927 1.00 59.37  ? 505 ASP   A OD1   1 
ATOM   2689 O OD2   . ASP   A 1 379 ? 26.035  31.938  34.878 1.00 59.67  ? 505 ASP   A OD2   1 
ATOM   2690 N N     . PRO   A 1 380 ? 30.338  33.784  36.811 1.00 59.12  ? 506 PRO   A N     1 
ATOM   2691 C CA    . PRO   A 1 380 ? 30.942  35.126  36.796 1.00 59.32  ? 506 PRO   A CA    1 
ATOM   2692 C C     . PRO   A 1 380 ? 30.139  36.154  36.007 1.00 63.24  ? 506 PRO   A C     1 
ATOM   2693 O O     . PRO   A 1 380 ? 30.483  37.344  36.047 1.00 63.50  ? 506 PRO   A O     1 
ATOM   2694 C CB    . PRO   A 1 380 ? 32.319  34.884  36.160 1.00 62.21  ? 506 PRO   A CB    1 
ATOM   2695 C CG    . PRO   A 1 380 ? 32.123  33.678  35.302 1.00 65.18  ? 506 PRO   A CG    1 
ATOM   2696 C CD    . PRO   A 1 380 ? 31.132  32.813  36.035 1.00 59.05  ? 506 PRO   A CD    1 
ATOM   2697 N N     . LYS   A 1 381 ? 29.098  35.742  35.281 1.00 59.68  ? 507 LYS   A N     1 
ATOM   2698 C CA    . LYS   A 1 381 ? 28.199  36.703  34.659 1.00 59.44  ? 507 LYS   A CA    1 
ATOM   2699 C C     . LYS   A 1 381 ? 27.166  37.256  35.635 1.00 56.24  ? 507 LYS   A C     1 
ATOM   2700 O O     . LYS   A 1 381 ? 26.552  38.288  35.341 1.00 55.21  ? 507 LYS   A O     1 
ATOM   2701 C CB    . LYS   A 1 381 ? 27.485  36.060  33.467 1.00 61.55  ? 507 LYS   A CB    1 
ATOM   2702 N N     . VAL   A 1 382 ? 26.970  36.606  36.782 1.00 54.79  ? 508 VAL   A N     1 
ATOM   2703 C CA    . VAL   A 1 382 ? 25.927  36.968  37.739 1.00 51.33  ? 508 VAL   A CA    1 
ATOM   2704 C C     . VAL   A 1 382 ? 26.545  37.795  38.858 1.00 53.01  ? 508 VAL   A C     1 
ATOM   2705 O O     . VAL   A 1 382 ? 27.435  37.326  39.576 1.00 51.82  ? 508 VAL   A O     1 
ATOM   2706 C CB    . VAL   A 1 382 ? 25.223  35.725  38.309 1.00 51.17  ? 508 VAL   A CB    1 
ATOM   2707 C CG1   . VAL   A 1 382 ? 24.130  36.138  39.282 1.00 45.65  ? 508 VAL   A CG1   1 
ATOM   2708 C CG2   . VAL   A 1 382 ? 24.657  34.851  37.189 1.00 49.45  ? 508 VAL   A CG2   1 
ATOM   2709 N N     . SER   A 1 383 ? 26.043  39.009  39.036 1.00 52.25  ? 509 SER   A N     1 
ATOM   2710 C CA    . SER   A 1 383 ? 26.520  39.901  40.076 1.00 49.73  ? 509 SER   A CA    1 
ATOM   2711 C C     . SER   A 1 383 ? 25.884  39.542  41.418 1.00 51.38  ? 509 SER   A C     1 
ATOM   2712 O O     . SER   A 1 383 ? 24.916  38.780  41.498 1.00 47.40  ? 509 SER   A O     1 
ATOM   2713 C CB    . SER   A 1 383 ? 26.205  41.352  39.712 1.00 53.20  ? 509 SER   A CB    1 
ATOM   2714 O OG    . SER   A 1 383 ? 24.830  41.614  39.936 1.00 57.09  ? 509 SER   A OG    1 
ATOM   2715 N N     . ILE   A 1 384 ? 26.444  40.109  42.486 1.00 48.40  ? 510 ILE   A N     1 
ATOM   2716 C CA    . ILE   A 1 384 ? 25.865  39.925  43.810 1.00 51.78  ? 510 ILE   A CA    1 
ATOM   2717 C C     . ILE   A 1 384 ? 24.545  40.680  43.931 1.00 47.35  ? 510 ILE   A C     1 
ATOM   2718 O O     . ILE   A 1 384 ? 23.602  40.203  44.574 1.00 45.26  ? 510 ILE   A O     1 
ATOM   2719 C CB    . ILE   A 1 384 ? 26.880  40.344  44.892 1.00 56.35  ? 510 ILE   A CB    1 
ATOM   2720 C CG1   . ILE   A 1 384 ? 27.984  39.285  44.986 1.00 58.12  ? 510 ILE   A CG1   1 
ATOM   2721 C CG2   . ILE   A 1 384 ? 26.204  40.526  46.246 1.00 50.68  ? 510 ILE   A CG2   1 
ATOM   2722 C CD1   . ILE   A 1 384 ? 29.320  39.808  45.506 1.00 63.40  ? 510 ILE   A CD1   1 
ATOM   2723 N N     . ASP   A 1 385 ? 24.451  41.864  43.312 1.00 49.21  ? 511 ASP   A N     1 
ATOM   2724 C CA    . ASP   A 1 385 ? 23.192  42.603  43.332 1.00 46.85  ? 511 ASP   A CA    1 
ATOM   2725 C C     . ASP   A 1 385 ? 22.055  41.759  42.772 1.00 46.65  ? 511 ASP   A C     1 
ATOM   2726 O O     . ASP   A 1 385 ? 20.968  41.693  43.357 1.00 46.37  ? 511 ASP   A O     1 
ATOM   2727 C CB    . ASP   A 1 385 ? 23.341  43.907  42.550 1.00 50.66  ? 511 ASP   A CB    1 
ATOM   2728 C CG    . ASP   A 1 385 ? 24.488  44.764  43.061 1.00 58.37  ? 511 ASP   A CG    1 
ATOM   2729 O OD1   . ASP   A 1 385 ? 24.652  44.876  44.297 1.00 59.30  ? 511 ASP   A OD1   1 
ATOM   2730 O OD2   . ASP   A 1 385 ? 25.230  45.317  42.224 1.00 59.53  ? 511 ASP   A OD2   1 
ATOM   2731 N N     . GLU   A 1 386 ? 22.303  41.069  41.662 1.00 47.79  ? 512 GLU   A N     1 
ATOM   2732 C CA    . GLU   A 1 386 ? 21.308  40.152  41.116 1.00 45.73  ? 512 GLU   A CA    1 
ATOM   2733 C C     . GLU   A 1 386 ? 21.012  39.009  42.080 1.00 46.61  ? 512 GLU   A C     1 
ATOM   2734 O O     . GLU   A 1 386 ? 19.865  38.560  42.200 1.00 42.90  ? 512 GLU   A O     1 
ATOM   2735 C CB    . GLU   A 1 386 ? 21.801  39.618  39.774 1.00 48.43  ? 512 GLU   A CB    1 
ATOM   2736 C CG    . GLU   A 1 386 ? 21.021  38.456  39.228 1.00 48.79  ? 512 GLU   A CG    1 
ATOM   2737 C CD    . GLU   A 1 386 ? 19.625  38.835  38.801 1.00 54.11  ? 512 GLU   A CD    1 
ATOM   2738 O OE1   . GLU   A 1 386 ? 19.320  40.046  38.713 1.00 54.11  ? 512 GLU   A OE1   1 
ATOM   2739 O OE2   . GLU   A 1 386 ? 18.824  37.911  38.546 1.00 59.97  ? 512 GLU   A OE2   1 
ATOM   2740 N N     . LEU   A 1 387 ? 22.030  38.527  42.790 1.00 44.53  ? 513 LEU   A N     1 
ATOM   2741 C CA    . LEU   A 1 387 ? 21.796  37.406  43.689 1.00 44.30  ? 513 LEU   A CA    1 
ATOM   2742 C C     . LEU   A 1 387 ? 20.978  37.801  44.913 1.00 43.91  ? 513 LEU   A C     1 
ATOM   2743 O O     . LEU   A 1 387 ? 20.294  36.947  45.496 1.00 41.74  ? 513 LEU   A O     1 
ATOM   2744 C CB    . LEU   A 1 387 ? 23.129  36.796  44.115 1.00 42.29  ? 513 LEU   A CB    1 
ATOM   2745 C CG    . LEU   A 1 387 ? 23.780  35.882  43.080 1.00 43.07  ? 513 LEU   A CG    1 
ATOM   2746 C CD1   . LEU   A 1 387 ? 25.232  35.601  43.449 1.00 45.88  ? 513 LEU   A CD1   1 
ATOM   2747 C CD2   . LEU   A 1 387 ? 22.989  34.595  42.955 1.00 43.09  ? 513 LEU   A CD2   1 
ATOM   2748 N N     . ILE   A 1 388 ? 21.046  39.064  45.339 1.00 43.06  ? 514 ILE   A N     1 
ATOM   2749 C CA    . ILE   A 1 388 ? 20.282  39.504  46.502 1.00 44.20  ? 514 ILE   A CA    1 
ATOM   2750 C C     . ILE   A 1 388 ? 18.959  40.148  46.122 1.00 44.67  ? 514 ILE   A C     1 
ATOM   2751 O O     . ILE   A 1 388 ? 18.268  40.686  47.001 1.00 43.80  ? 514 ILE   A O     1 
ATOM   2752 C CB    . ILE   A 1 388 ? 21.093  40.478  47.380 1.00 47.72  ? 514 ILE   A CB    1 
ATOM   2753 C CG1   . ILE   A 1 388 ? 21.350  41.775  46.622 1.00 48.33  ? 514 ILE   A CG1   1 
ATOM   2754 C CG2   . ILE   A 1 388 ? 22.395  39.829  47.833 1.00 44.15  ? 514 ILE   A CG2   1 
ATOM   2755 C CD1   . ILE   A 1 388 ? 21.672  42.958  47.512 1.00 52.36  ? 514 ILE   A CD1   1 
ATOM   2756 N N     . ALA   A 1 389 ? 18.600  40.137  44.837 1.00 44.06  ? 515 ALA   A N     1 
ATOM   2757 C CA    . ALA   A 1 389 ? 17.329  40.693  44.403 1.00 46.95  ? 515 ALA   A CA    1 
ATOM   2758 C C     . ALA   A 1 389 ? 16.178  40.049  45.163 1.00 47.72  ? 515 ALA   A C     1 
ATOM   2759 O O     . ALA   A 1 389 ? 16.155  38.837  45.375 1.00 42.37  ? 515 ALA   A O     1 
ATOM   2760 C CB    . ALA   A 1 389 ? 17.149  40.481  42.899 1.00 45.38  ? 515 ALA   A CB    1 
ATOM   2761 N N     . ASP   A 1 390 ? 15.234  40.871  45.589 1.00 46.92  ? 516 ASP   A N     1 
ATOM   2762 C CA    . ASP   A 1 390 ? 14.020  40.360  46.213 1.00 49.31  ? 516 ASP   A CA    1 
ATOM   2763 C C     . ASP   A 1 390 ? 13.058  39.898  45.125 1.00 53.75  ? 516 ASP   A C     1 
ATOM   2764 O O     . ASP   A 1 390 ? 12.644  40.714  44.289 1.00 50.51  ? 516 ASP   A O     1 
ATOM   2765 C CB    . ASP   A 1 390 ? 13.376  41.440  47.078 1.00 54.10  ? 516 ASP   A CB    1 
ATOM   2766 C CG    . ASP   A 1 390 ? 12.097  40.977  47.760 1.00 54.73  ? 516 ASP   A CG    1 
ATOM   2767 O OD1   . ASP   A 1 390 ? 11.663  39.828  47.565 1.00 58.04  ? 516 ASP   A OD1   1 
ATOM   2768 O OD2   . ASP   A 1 390 ? 11.516  41.772  48.507 1.00 60.84  ? 516 ASP   A OD2   1 
ATOM   2769 N N     . PRO   A 1 391 ? 12.676  38.618  45.104 1.00 49.44  ? 517 PRO   A N     1 
ATOM   2770 C CA    . PRO   A 1 391 ? 11.819  38.116  44.015 1.00 52.76  ? 517 PRO   A CA    1 
ATOM   2771 C C     . PRO   A 1 391 ? 10.531  38.897  43.820 1.00 55.27  ? 517 PRO   A C     1 
ATOM   2772 O O     . PRO   A 1 391 ? 10.121  39.112  42.674 1.00 56.04  ? 517 PRO   A O     1 
ATOM   2773 C CB    . PRO   A 1 391 ? 11.541  36.669  44.445 1.00 48.07  ? 517 PRO   A CB    1 
ATOM   2774 C CG    . PRO   A 1 391 ? 12.700  36.304  45.280 1.00 45.75  ? 517 PRO   A CG    1 
ATOM   2775 C CD    . PRO   A 1 391 ? 13.127  37.542  46.000 1.00 47.68  ? 517 PRO   A CD    1 
ATOM   2776 N N     . VAL   A 1 392 ? 9.878   39.326  44.902 1.00 55.26  ? 518 VAL   A N     1 
ATOM   2777 C CA    . VAL   A 1 392 ? 8.641   40.094  44.763 1.00 59.51  ? 518 VAL   A CA    1 
ATOM   2778 C C     . VAL   A 1 392 ? 8.901   41.395  44.018 1.00 59.15  ? 518 VAL   A C     1 
ATOM   2779 O O     . VAL   A 1 392 ? 8.142   41.777  43.121 1.00 62.73  ? 518 VAL   A O     1 
ATOM   2780 C CB    . VAL   A 1 392 ? 8.012   40.353  46.142 1.00 59.85  ? 518 VAL   A CB    1 
ATOM   2781 C CG1   . VAL   A 1 392 ? 6.770   41.209  45.998 1.00 62.70  ? 518 VAL   A CG1   1 
ATOM   2782 C CG2   . VAL   A 1 392 ? 7.680   39.047  46.794 1.00 57.99  ? 518 VAL   A CG2   1 
ATOM   2783 N N     . GLU   A 1 393 ? 9.987   42.086  44.365 1.00 63.93  ? 519 GLU   A N     1 
ATOM   2784 C CA    . GLU   A 1 393 ? 10.360  43.295  43.644 1.00 65.99  ? 519 GLU   A CA    1 
ATOM   2785 C C     . GLU   A 1 393 ? 10.578  43.015  42.163 1.00 63.21  ? 519 GLU   A C     1 
ATOM   2786 O O     . GLU   A 1 393 ? 10.181  43.814  41.311 1.00 68.90  ? 519 GLU   A O     1 
ATOM   2787 C CB    . GLU   A 1 393 ? 11.618  43.905  44.260 1.00 65.77  ? 519 GLU   A CB    1 
ATOM   2788 C CG    . GLU   A 1 393 ? 11.394  44.587  45.599 1.00 69.28  ? 519 GLU   A CG    1 
ATOM   2789 C CD    . GLU   A 1 393 ? 12.699  44.861  46.328 1.00 75.23  ? 519 GLU   A CD    1 
ATOM   2790 O OE1   . GLU   A 1 393 ? 13.771  44.619  45.731 1.00 78.92  ? 519 GLU   A OE1   1 
ATOM   2791 O OE2   . GLU   A 1 393 ? 12.657  45.300  47.498 1.00 76.39  ? 519 GLU   A OE2   1 
ATOM   2792 N N     . VAL   A 1 394 ? 11.198  41.888  41.832 1.00 60.67  ? 520 VAL   A N     1 
ATOM   2793 C CA    . VAL   A 1 394 ? 11.529  41.604  40.442 1.00 62.66  ? 520 VAL   A CA    1 
ATOM   2794 C C     . VAL   A 1 394 ? 10.326  41.041  39.685 1.00 63.75  ? 520 VAL   A C     1 
ATOM   2795 O O     . VAL   A 1 394 ? 9.222   40.945  40.224 1.00 63.58  ? 520 VAL   A O     1 
ATOM   2796 C CB    . VAL   A 1 394 ? 12.728  40.641  40.354 1.00 58.08  ? 520 VAL   A CB    1 
ATOM   2797 N N     . ARG   B 1 2   ? 5.262   -5.690  -1.200 1.00 77.57  ? 26  ARG   B N     1 
ATOM   2798 C CA    . ARG   B 1 2   ? 5.713   -4.393  -0.706 1.00 74.14  ? 26  ARG   B CA    1 
ATOM   2799 C C     . ARG   B 1 2   ? 7.235   -4.291  -0.758 1.00 70.17  ? 26  ARG   B C     1 
ATOM   2800 O O     . ARG   B 1 2   ? 7.936   -5.276  -0.534 1.00 68.99  ? 26  ARG   B O     1 
ATOM   2801 C CB    . ARG   B 1 2   ? 5.216   -4.154  0.725  1.00 72.79  ? 26  ARG   B CB    1 
ATOM   2802 N N     . PRO   B 1 3   ? 7.744   -3.101  -1.071 1.00 68.43  ? 27  PRO   B N     1 
ATOM   2803 C CA    . PRO   B 1 3   ? 9.199   -2.917  -1.148 1.00 64.93  ? 27  PRO   B CA    1 
ATOM   2804 C C     . PRO   B 1 3   ? 9.886   -3.276  0.164  1.00 66.80  ? 27  PRO   B C     1 
ATOM   2805 O O     . PRO   B 1 3   ? 9.469   -2.850  1.246  1.00 63.55  ? 27  PRO   B O     1 
ATOM   2806 C CB    . PRO   B 1 3   ? 9.346   -1.429  -1.480 1.00 64.12  ? 27  PRO   B CB    1 
ATOM   2807 C CG    . PRO   B 1 3   ? 8.082   -1.084  -2.194 1.00 68.25  ? 27  PRO   B CG    1 
ATOM   2808 C CD    . PRO   B 1 3   ? 7.008   -1.920  -1.560 1.00 70.31  ? 27  PRO   B CD    1 
ATOM   2809 N N     . GLN   B 1 4   ? 10.949  -4.079  0.049  1.00 62.21  ? 28  GLN   B N     1 
ATOM   2810 C CA    . GLN   B 1 4   ? 11.723  -4.550  1.191  1.00 62.35  ? 28  GLN   B CA    1 
ATOM   2811 C C     . GLN   B 1 4   ? 10.815  -5.164  2.255  1.00 63.51  ? 28  GLN   B C     1 
ATOM   2812 O O     . GLN   B 1 4   ? 11.068  -5.042  3.452  1.00 60.99  ? 28  GLN   B O     1 
ATOM   2813 C CB    . GLN   B 1 4   ? 12.587  -3.421  1.770  1.00 58.91  ? 28  GLN   B CB    1 
ATOM   2814 C CG    . GLN   B 1 4   ? 13.722  -2.955  0.822  1.00 60.78  ? 28  GLN   B CG    1 
ATOM   2815 C CD    . GLN   B 1 4   ? 13.212  -2.249  -0.445 1.00 60.72  ? 28  GLN   B CD    1 
ATOM   2816 O OE1   . GLN   B 1 4   ? 12.592  -1.189  -0.365 1.00 61.83  ? 28  GLN   B OE1   1 
ATOM   2817 N NE2   . GLN   B 1 4   ? 13.476  -2.840  -1.619 1.00 58.54  ? 28  GLN   B NE2   1 
ATOM   2818 N N     . SER   B 1 5   ? 9.741   -5.829  1.810  1.00 66.77  ? 29  SER   B N     1 
ATOM   2819 C CA    . SER   B 1 5   ? 8.780   -6.399  2.746  1.00 62.69  ? 29  SER   B CA    1 
ATOM   2820 C C     . SER   B 1 5   ? 9.455   -7.370  3.707  1.00 62.81  ? 29  SER   B C     1 
ATOM   2821 O O     . SER   B 1 5   ? 9.202   -7.335  4.916  1.00 59.83  ? 29  SER   B O     1 
ATOM   2822 C CB    . SER   B 1 5   ? 7.649   -7.099  1.989  1.00 67.39  ? 29  SER   B CB    1 
ATOM   2823 N N     . THR   B 1 6   ? 10.319  -8.244  3.187  1.00 60.82  ? 30  THR   B N     1 
ATOM   2824 C CA    . THR   B 1 6   ? 10.926  -9.260  4.037  1.00 62.33  ? 30  THR   B CA    1 
ATOM   2825 C C     . THR   B 1 6   ? 11.801  -8.621  5.104  1.00 59.38  ? 30  THR   B C     1 
ATOM   2826 O O     . THR   B 1 6   ? 11.725  -8.984  6.286  1.00 56.96  ? 30  THR   B O     1 
ATOM   2827 C CB    . THR   B 1 6   ? 11.724  -10.247 3.186  1.00 61.99  ? 30  THR   B CB    1 
ATOM   2828 O OG1   . THR   B 1 6   ? 10.817  -11.058 2.433  1.00 65.19  ? 30  THR   B OG1   1 
ATOM   2829 C CG2   . THR   B 1 6   ? 12.571  -11.149 4.066  1.00 63.10  ? 30  THR   B CG2   1 
ATOM   2830 N N     . LEU   B 1 7   ? 12.609  -7.640  4.713  1.00 59.44  ? 31  LEU   B N     1 
ATOM   2831 C CA    . LEU   B 1 7   ? 13.465  -6.953  5.672  1.00 56.02  ? 31  LEU   B CA    1 
ATOM   2832 C C     . LEU   B 1 7   ? 12.658  -6.116  6.654  1.00 53.52  ? 31  LEU   B C     1 
ATOM   2833 O O     . LEU   B 1 7   ? 12.989  -6.055  7.845  1.00 51.51  ? 31  LEU   B O     1 
ATOM   2834 C CB    . LEU   B 1 7   ? 14.454  -6.076  4.925  1.00 54.52  ? 31  LEU   B CB    1 
ATOM   2835 C CG    . LEU   B 1 7   ? 15.460  -6.858  4.100  1.00 52.63  ? 31  LEU   B CG    1 
ATOM   2836 C CD1   . LEU   B 1 7   ? 16.180  -5.883  3.201  1.00 50.75  ? 31  LEU   B CD1   1 
ATOM   2837 C CD2   . LEU   B 1 7   ? 16.438  -7.569  5.021  1.00 51.48  ? 31  LEU   B CD2   1 
ATOM   2838 N N     . ARG   B 1 8   ? 11.616  -5.437  6.173  1.00 56.20  ? 32  ARG   B N     1 
ATOM   2839 C CA    . ARG   B 1 8   ? 10.811  -4.619  7.071  1.00 57.88  ? 32  ARG   B CA    1 
ATOM   2840 C C     . ARG   B 1 8   ? 10.017  -5.486  8.038  1.00 54.84  ? 32  ARG   B C     1 
ATOM   2841 O O     . ARG   B 1 8   ? 9.944   -5.179  9.233  1.00 52.98  ? 32  ARG   B O     1 
ATOM   2842 C CB    . ARG   B 1 8   ? 9.882   -3.708  6.272  1.00 55.32  ? 32  ARG   B CB    1 
ATOM   2843 C CG    . ARG   B 1 8   ? 10.565  -2.496  5.650  1.00 57.75  ? 32  ARG   B CG    1 
ATOM   2844 C CD    . ARG   B 1 8   ? 9.515   -1.424  5.362  1.00 67.22  ? 32  ARG   B CD    1 
ATOM   2845 N NE    . ARG   B 1 8   ? 9.977   -0.369  4.468  1.00 65.84  ? 32  ARG   B NE    1 
ATOM   2846 C CZ    . ARG   B 1 8   ? 10.507  0.778   4.872  1.00 62.34  ? 32  ARG   B CZ    1 
ATOM   2847 N NH1   . ARG   B 1 8   ? 10.710  1.033   6.154  1.00 67.16  ? 32  ARG   B NH1   1 
ATOM   2848 N NH2   . ARG   B 1 8   ? 10.824  1.700   3.966  1.00 60.54  ? 32  ARG   B NH2   1 
ATOM   2849 N N     . ARG   B 1 9   ? 9.424   -6.579  7.540  1.00 55.03  ? 33  ARG   B N     1 
ATOM   2850 C CA    . ARG   B 1 9   ? 8.699   -7.496  8.414  1.00 56.72  ? 33  ARG   B CA    1 
ATOM   2851 C C     . ARG   B 1 9   ? 9.594   -8.029  9.522  1.00 57.41  ? 33  ARG   B C     1 
ATOM   2852 O O     . ARG   B 1 9   ? 9.136   -8.227  10.657 1.00 55.06  ? 33  ARG   B O     1 
ATOM   2853 C CB    . ARG   B 1 9   ? 8.125   -8.657  7.603  1.00 61.10  ? 33  ARG   B CB    1 
ATOM   2854 N N     . ALA   B 1 10  ? 10.872  -8.271  9.211  1.00 53.56  ? 34  ALA   B N     1 
ATOM   2855 C CA    . ALA   B 1 10  ? 11.794  -8.798  10.208 1.00 50.29  ? 34  ALA   B CA    1 
ATOM   2856 C C     . ALA   B 1 10  ? 12.044  -7.785  11.317 1.00 52.05  ? 34  ALA   B C     1 
ATOM   2857 O O     . ALA   B 1 10  ? 12.189  -8.159  12.484 1.00 49.53  ? 34  ALA   B O     1 
ATOM   2858 C CB    . ALA   B 1 10  ? 13.110  -9.200  9.543  1.00 48.50  ? 34  ALA   B CB    1 
ATOM   2859 N N     . ILE   B 1 11  ? 12.111  -6.498  10.966 1.00 53.46  ? 35  ILE   B N     1 
ATOM   2860 C CA    . ILE   B 1 11  ? 12.253  -5.453  11.976 1.00 49.96  ? 35  ILE   B CA    1 
ATOM   2861 C C     . ILE   B 1 11  ? 11.043  -5.444  12.896 1.00 53.00  ? 35  ILE   B C     1 
ATOM   2862 O O     . ILE   B 1 11  ? 11.172  -5.545  14.123 1.00 51.95  ? 35  ILE   B O     1 
ATOM   2863 C CB    . ILE   B 1 11  ? 12.449  -4.082  11.307 1.00 50.79  ? 35  ILE   B CB    1 
ATOM   2864 C CG1   . ILE   B 1 11  ? 13.760  -4.047  10.516 1.00 46.58  ? 35  ILE   B CG1   1 
ATOM   2865 C CG2   . ILE   B 1 11  ? 12.418  -2.984  12.358 1.00 49.12  ? 35  ILE   B CG2   1 
ATOM   2866 C CD1   . ILE   B 1 11  ? 13.907  -2.813  9.623  1.00 44.95  ? 35  ILE   B CD1   1 
ATOM   2867 N N     . THR   B 1 12  ? 9.847   -5.313  12.312 1.00 52.38  ? 36  THR   B N     1 
ATOM   2868 C CA    . THR   B 1 12  ? 8.615   -5.374  13.095 1.00 55.58  ? 36  THR   B CA    1 
ATOM   2869 C C     . THR   B 1 12  ? 8.556   -6.644  13.935 1.00 56.46  ? 36  THR   B C     1 
ATOM   2870 O O     . THR   B 1 12  ? 8.168   -6.607  15.111 1.00 58.77  ? 36  THR   B O     1 
ATOM   2871 C CB    . THR   B 1 12  ? 7.402   -5.294  12.162 1.00 56.34  ? 36  THR   B CB    1 
ATOM   2872 O OG1   . THR   B 1 12  ? 7.522   -4.148  11.313 1.00 57.40  ? 36  THR   B OG1   1 
ATOM   2873 C CG2   . THR   B 1 12  ? 6.105   -5.186  12.954 1.00 60.68  ? 36  THR   B CG2   1 
ATOM   2874 N N     . ALA   B 1 13  ? 8.944   -7.781  13.349 1.00 54.68  ? 37  ALA   B N     1 
ATOM   2875 C CA    . ALA   B 1 13  ? 8.868   -9.048  14.066 1.00 55.01  ? 37  ALA   B CA    1 
ATOM   2876 C C     . ALA   B 1 13  ? 9.787   -9.065  15.280 1.00 55.73  ? 37  ALA   B C     1 
ATOM   2877 O O     . ALA   B 1 13  ? 9.463   -9.689  16.293 1.00 54.34  ? 37  ALA   B O     1 
ATOM   2878 C CB    . ALA   B 1 13  ? 9.213   -10.203 13.127 1.00 57.40  ? 37  ALA   B CB    1 
ATOM   2879 N N     . ALA   B 1 14  ? 10.931  -8.386  15.198 1.00 57.14  ? 38  ALA   B N     1 
ATOM   2880 C CA    . ALA   B 1 14  ? 11.868  -8.362  16.314 1.00 53.64  ? 38  ALA   B CA    1 
ATOM   2881 C C     . ALA   B 1 14  ? 11.429  -7.412  17.420 1.00 56.94  ? 38  ALA   B C     1 
ATOM   2882 O O     . ALA   B 1 14  ? 11.742  -7.651  18.595 1.00 52.62  ? 38  ALA   B O     1 
ATOM   2883 C CB    . ALA   B 1 14  ? 13.255  -7.967  15.813 1.00 49.53  ? 38  ALA   B CB    1 
ATOM   2884 N N     . TYR   B 1 15  ? 10.746  -6.322  17.056 1.00 58.08  ? 39  TYR   B N     1 
ATOM   2885 C CA    . TYR   B 1 15  ? 10.206  -5.369  18.021 1.00 58.25  ? 39  TYR   B CA    1 
ATOM   2886 C C     . TYR   B 1 15  ? 9.507   -6.074  19.175 1.00 63.45  ? 39  TYR   B C     1 
ATOM   2887 O O     . TYR   B 1 15  ? 9.741   -5.765  20.346 1.00 63.01  ? 39  TYR   B O     1 
ATOM   2888 C CB    . TYR   B 1 15  ? 9.228   -4.438  17.310 1.00 57.90  ? 39  TYR   B CB    1 
ATOM   2889 C CG    . TYR   B 1 15  ? 9.087   -3.045  17.875 1.00 57.80  ? 39  TYR   B CG    1 
ATOM   2890 C CD1   . TYR   B 1 15  ? 9.927   -2.571  18.879 1.00 56.95  ? 39  TYR   B CD1   1 
ATOM   2891 C CD2   . TYR   B 1 15  ? 8.100   -2.195  17.387 1.00 64.32  ? 39  TYR   B CD2   1 
ATOM   2892 C CE1   . TYR   B 1 15  ? 9.783   -1.279  19.378 1.00 54.72  ? 39  TYR   B CE1   1 
ATOM   2893 C CE2   . TYR   B 1 15  ? 7.945   -0.914  17.875 1.00 63.14  ? 39  TYR   B CE2   1 
ATOM   2894 C CZ    . TYR   B 1 15  ? 8.783   -0.459  18.870 1.00 58.89  ? 39  TYR   B CZ    1 
ATOM   2895 O OH    . TYR   B 1 15  ? 8.602   0.827   19.329 1.00 61.89  ? 39  TYR   B OH    1 
ATOM   2896 N N     . ARG   B 1 16  ? 8.657   -7.043  18.852 1.00 75.87  ? 40  ARG   B N     1 
ATOM   2897 C CA    . ARG   B 1 16  ? 7.840   -7.735  19.838 1.00 77.64  ? 40  ARG   B CA    1 
ATOM   2898 C C     . ARG   B 1 16  ? 8.457   -9.044  20.315 1.00 77.84  ? 40  ARG   B C     1 
ATOM   2899 O O     . ARG   B 1 16  ? 7.830   -9.748  21.115 1.00 77.80  ? 40  ARG   B O     1 
ATOM   2900 C CB    . ARG   B 1 16  ? 6.445   -8.004  19.259 1.00 77.89  ? 40  ARG   B CB    1 
ATOM   2901 N N     . ARG   B 1 17  ? 9.657   -9.386  19.858 1.00 64.81  ? 41  ARG   B N     1 
ATOM   2902 C CA    . ARG   B 1 17  ? 10.199  -10.705 20.146 1.00 59.71  ? 41  ARG   B CA    1 
ATOM   2903 C C     . ARG   B 1 17  ? 10.608  -10.790 21.612 1.00 59.86  ? 41  ARG   B C     1 
ATOM   2904 O O     . ARG   B 1 17  ? 11.232  -9.856  22.131 1.00 56.92  ? 41  ARG   B O     1 
ATOM   2905 C CB    . ARG   B 1 17  ? 11.394  -11.019 19.248 1.00 59.65  ? 41  ARG   B CB    1 
ATOM   2906 C CG    . ARG   B 1 17  ? 11.957  -12.420 19.475 1.00 57.64  ? 41  ARG   B CG    1 
ATOM   2907 C CD    . ARG   B 1 17  ? 12.785  -12.918 18.298 1.00 57.54  ? 41  ARG   B CD    1 
ATOM   2908 N NE    . ARG   B 1 17  ? 11.996  -12.946 17.071 1.00 55.34  ? 41  ARG   B NE    1 
ATOM   2909 C CZ    . ARG   B 1 17  ? 12.325  -12.334 15.942 1.00 52.77  ? 41  ARG   B CZ    1 
ATOM   2910 N NH1   . ARG   B 1 17  ? 13.469  -11.683 15.814 1.00 47.98  ? 41  ARG   B NH1   1 
ATOM   2911 N NH2   . ARG   B 1 17  ? 11.484  -12.383 14.912 1.00 51.93  ? 41  ARG   B NH2   1 
ATOM   2912 N N     . PRO   B 1 18  ? 10.262  -11.869 22.313 1.00 58.72  ? 42  PRO   B N     1 
ATOM   2913 C CA    . PRO   B 1 18  ? 10.747  -12.034 23.688 1.00 58.58  ? 42  PRO   B CA    1 
ATOM   2914 C C     . PRO   B 1 18  ? 12.267  -11.995 23.730 1.00 57.87  ? 42  PRO   B C     1 
ATOM   2915 O O     . PRO   B 1 18  ? 12.944  -12.445 22.805 1.00 57.33  ? 42  PRO   B O     1 
ATOM   2916 C CB    . PRO   B 1 18  ? 10.198  -13.404 24.093 1.00 59.41  ? 42  PRO   B CB    1 
ATOM   2917 C CG    . PRO   B 1 18  ? 8.950   -13.542 23.285 1.00 62.64  ? 42  PRO   B CG    1 
ATOM   2918 C CD    . PRO   B 1 18  ? 9.282   -12.906 21.949 1.00 62.38  ? 42  PRO   B CD    1 
ATOM   2919 N N     . GLU   B 1 19  ? 12.798  -11.426 24.814 1.00 56.81  ? 43  GLU   B N     1 
ATOM   2920 C CA    . GLU   B 1 19  ? 14.238  -11.205 24.915 1.00 56.01  ? 43  GLU   B CA    1 
ATOM   2921 C C     . GLU   B 1 19  ? 15.022  -12.511 24.812 1.00 54.58  ? 43  GLU   B C     1 
ATOM   2922 O O     . GLU   B 1 19  ? 16.052  -12.573 24.130 1.00 52.97  ? 43  GLU   B O     1 
ATOM   2923 C CB    . GLU   B 1 19  ? 14.556  -10.483 26.227 1.00 52.62  ? 43  GLU   B CB    1 
ATOM   2924 C CG    . GLU   B 1 19  ? 16.023  -10.107 26.396 1.00 51.29  ? 43  GLU   B CG    1 
ATOM   2925 C CD    . GLU   B 1 19  ? 16.239  -9.145  27.557 1.00 48.10  ? 43  GLU   B CD    1 
ATOM   2926 O OE1   . GLU   B 1 19  ? 15.228  -8.708  28.149 1.00 47.34  ? 43  GLU   B OE1   1 
ATOM   2927 O OE2   . GLU   B 1 19  ? 17.411  -8.827  27.873 1.00 46.16  ? 43  GLU   B OE2   1 
ATOM   2928 N N     . THR   B 1 20  ? 14.555  -13.567 25.480 1.00 57.54  ? 44  THR   B N     1 
ATOM   2929 C CA    . THR   B 1 20  ? 15.286  -14.828 25.417 1.00 59.70  ? 44  THR   B CA    1 
ATOM   2930 C C     . THR   B 1 20  ? 15.365  -15.358 23.986 1.00 58.60  ? 44  THR   B C     1 
ATOM   2931 O O     . THR   B 1 20  ? 16.351  -16.010 23.622 1.00 56.45  ? 44  THR   B O     1 
ATOM   2932 C CB    . THR   B 1 20  ? 14.650  -15.858 26.358 1.00 59.05  ? 44  THR   B CB    1 
ATOM   2933 O OG1   . THR   B 1 20  ? 13.314  -16.143 25.933 1.00 64.88  ? 44  THR   B OG1   1 
ATOM   2934 C CG2   . THR   B 1 20  ? 14.606  -15.317 27.777 1.00 57.07  ? 44  THR   B CG2   1 
ATOM   2935 N N     . GLU   B 1 21  ? 14.362  -15.048 23.151 1.00 56.28  ? 45  GLU   B N     1 
ATOM   2936 C CA    . GLU   B 1 21  ? 14.365  -15.516 21.766 1.00 58.02  ? 45  GLU   B CA    1 
ATOM   2937 C C     . GLU   B 1 21  ? 15.348  -14.742 20.895 1.00 55.81  ? 45  GLU   B C     1 
ATOM   2938 O O     . GLU   B 1 21  ? 15.861  -15.290 19.912 1.00 56.61  ? 45  GLU   B O     1 
ATOM   2939 C CB    . GLU   B 1 21  ? 12.962  -15.415 21.164 1.00 58.61  ? 45  GLU   B CB    1 
ATOM   2940 C CG    . GLU   B 1 21  ? 11.980  -16.489 21.605 1.00 61.64  ? 45  GLU   B CG    1 
ATOM   2941 C CD    . GLU   B 1 21  ? 10.690  -16.461 20.793 1.00 66.34  ? 45  GLU   B CD    1 
ATOM   2942 O OE1   . GLU   B 1 21  ? 10.450  -15.459 20.087 1.00 66.53  ? 45  GLU   B OE1   1 
ATOM   2943 O OE2   . GLU   B 1 21  ? 9.919   -17.441 20.850 1.00 73.44  ? 45  GLU   B OE2   1 
ATOM   2944 N N     . CYS   B 1 22  ? 15.602  -13.470 21.216 1.00 55.32  ? 46  CYS   B N     1 
ATOM   2945 C CA    . CYS   B 1 22  ? 16.528  -12.671 20.420 1.00 52.74  ? 46  CYS   B CA    1 
ATOM   2946 C C     . CYS   B 1 22  ? 17.980  -13.093 20.606 1.00 51.64  ? 46  CYS   B C     1 
ATOM   2947 O O     . CYS   B 1 22  ? 18.810  -12.802 19.740 1.00 50.57  ? 46  CYS   B O     1 
ATOM   2948 C CB    . CYS   B 1 22  ? 16.408  -11.186 20.780 1.00 52.33  ? 46  CYS   B CB    1 
ATOM   2949 S SG    . CYS   B 1 22  ? 14.763  -10.431 20.652 1.00 50.32  ? 46  CYS   B SG    1 
ATOM   2950 N N     . LEU   B 1 23  ? 18.310  -13.753 21.712 1.00 55.20  ? 47  LEU   B N     1 
ATOM   2951 C CA    . LEU   B 1 23  ? 19.703  -13.884 22.133 1.00 52.84  ? 47  LEU   B CA    1 
ATOM   2952 C C     . LEU   B 1 23  ? 20.518  -14.948 21.391 1.00 52.32  ? 47  LEU   B C     1 
ATOM   2953 O O     . LEU   B 1 23  ? 21.670  -14.673 21.034 1.00 53.86  ? 47  LEU   B O     1 
ATOM   2954 C CB    . LEU   B 1 23  ? 19.768  -14.155 23.640 1.00 53.46  ? 47  LEU   B CB    1 
ATOM   2955 C CG    . LEU   B 1 23  ? 20.428  -13.064 24.483 1.00 52.16  ? 47  LEU   B CG    1 
ATOM   2956 C CD1   . LEU   B 1 23  ? 21.907  -12.922 24.140 1.00 51.50  ? 47  LEU   B CD1   1 
ATOM   2957 C CD2   . LEU   B 1 23  ? 19.705  -11.749 24.282 1.00 49.96  ? 47  LEU   B CD2   1 
ATOM   2958 N N     . PRO   B 1 24  ? 20.012  -16.161 21.167 1.00 53.72  ? 48  PRO   B N     1 
ATOM   2959 C CA    . PRO   B 1 24  ? 20.865  -17.222 20.589 1.00 55.86  ? 48  PRO   B CA    1 
ATOM   2960 C C     . PRO   B 1 24  ? 21.500  -16.820 19.265 1.00 56.42  ? 48  PRO   B C     1 
ATOM   2961 O O     . PRO   B 1 24  ? 22.708  -17.038 19.080 1.00 54.46  ? 48  PRO   B O     1 
ATOM   2962 C CB    . PRO   B 1 24  ? 19.894  -18.400 20.430 1.00 60.10  ? 48  PRO   B CB    1 
ATOM   2963 C CG    . PRO   B 1 24  ? 18.942  -18.210 21.565 1.00 59.36  ? 48  PRO   B CG    1 
ATOM   2964 C CD    . PRO   B 1 24  ? 18.719  -16.716 21.619 1.00 57.31  ? 48  PRO   B CD    1 
ATOM   2965 N N     . PRO   B 1 25  ? 20.758  -16.228 18.315 1.00 56.04  ? 49  PRO   B N     1 
ATOM   2966 C CA    . PRO   B 1 25  ? 21.436  -15.814 17.072 1.00 53.45  ? 49  PRO   B CA    1 
ATOM   2967 C C     . PRO   B 1 25  ? 22.511  -14.765 17.297 1.00 52.91  ? 49  PRO   B C     1 
ATOM   2968 O O     . PRO   B 1 25  ? 23.569  -14.819 16.656 1.00 53.00  ? 49  PRO   B O     1 
ATOM   2969 C CB    . PRO   B 1 25  ? 20.287  -15.290 16.195 1.00 57.08  ? 49  PRO   B CB    1 
ATOM   2970 C CG    . PRO   B 1 25  ? 19.201  -14.966 17.135 1.00 56.88  ? 49  PRO   B CG    1 
ATOM   2971 C CD    . PRO   B 1 25  ? 19.305  -15.985 18.225 1.00 57.73  ? 49  PRO   B CD    1 
ATOM   2972 N N     . LEU   B 1 26  ? 22.273  -13.812 18.202 1.00 51.64  ? 50  LEU   B N     1 
ATOM   2973 C CA    . LEU   B 1 26  ? 23.304  -12.834 18.532 1.00 49.44  ? 50  LEU   B CA    1 
ATOM   2974 C C     . LEU   B 1 26  ? 24.539  -13.517 19.098 1.00 49.73  ? 50  LEU   B C     1 
ATOM   2975 O O     . LEU   B 1 26  ? 25.670  -13.160 18.747 1.00 49.40  ? 50  LEU   B O     1 
ATOM   2976 C CB    . LEU   B 1 26  ? 22.758  -11.810 19.528 1.00 45.46  ? 50  LEU   B CB    1 
ATOM   2977 C CG    . LEU   B 1 26  ? 21.588  -10.951 19.046 1.00 46.64  ? 50  LEU   B CG    1 
ATOM   2978 C CD1   . LEU   B 1 26  ? 20.963  -10.186 20.219 1.00 42.40  ? 50  LEU   B CD1   1 
ATOM   2979 C CD2   . LEU   B 1 26  ? 22.056  -9.999  17.962 1.00 44.15  ? 50  LEU   B CD2   1 
ATOM   2980 N N     . VAL   B 1 27  ? 24.340  -14.506 19.976 1.00 51.75  ? 51  VAL   B N     1 
ATOM   2981 C CA    . VAL   B 1 27  ? 25.465  -15.228 20.564 1.00 49.09  ? 51  VAL   B CA    1 
ATOM   2982 C C     . VAL   B 1 27  ? 26.267  -15.933 19.480 1.00 51.53  ? 51  VAL   B C     1 
ATOM   2983 O O     . VAL   B 1 27  ? 27.503  -15.925 19.499 1.00 52.13  ? 51  VAL   B O     1 
ATOM   2984 C CB    . VAL   B 1 27  ? 24.965  -16.218 21.633 1.00 51.28  ? 51  VAL   B CB    1 
ATOM   2985 N N     . GLU   B 1 28  ? 25.578  -16.543 18.513 1.00 48.94  ? 52  GLU   B N     1 
ATOM   2986 C CA    . GLU   B 1 28  ? 26.262  -17.267 17.445 1.00 55.11  ? 52  GLU   B CA    1 
ATOM   2987 C C     . GLU   B 1 28  ? 27.106  -16.332 16.585 1.00 54.07  ? 52  GLU   B C     1 
ATOM   2988 O O     . GLU   B 1 28  ? 28.239  -16.667 16.217 1.00 55.70  ? 52  GLU   B O     1 
ATOM   2989 C CB    . GLU   B 1 28  ? 25.242  -18.015 16.583 1.00 59.97  ? 52  GLU   B CB    1 
ATOM   2990 N N     . ALA   B 1 29  ? 26.575  -15.154 16.251 1.00 51.67  ? 53  ALA   B N     1 
ATOM   2991 C CA    . ALA   B 1 29  ? 27.353  -14.216 15.452 1.00 53.10  ? 53  ALA   B CA    1 
ATOM   2992 C C     . ALA   B 1 29  ? 28.479  -13.588 16.259 1.00 52.18  ? 53  ALA   B C     1 
ATOM   2993 O O     . ALA   B 1 29  ? 29.509  -13.210 15.691 1.00 54.13  ? 53  ALA   B O     1 
ATOM   2994 C CB    . ALA   B 1 29  ? 26.447  -13.126 14.879 1.00 49.28  ? 53  ALA   B CB    1 
ATOM   2995 N N     . ALA   B 1 30  ? 28.302  -13.457 17.573 1.00 51.38  ? 54  ALA   B N     1 
ATOM   2996 C CA    . ALA   B 1 30  ? 29.279  -12.763 18.400 1.00 49.72  ? 54  ALA   B CA    1 
ATOM   2997 C C     . ALA   B 1 30  ? 30.419  -13.657 18.871 1.00 56.87  ? 54  ALA   B C     1 
ATOM   2998 O O     . ALA   B 1 30  ? 31.435  -13.132 19.341 1.00 57.71  ? 54  ALA   B O     1 
ATOM   2999 C CB    . ALA   B 1 30  ? 28.589  -12.133 19.613 1.00 45.22  ? 54  ALA   B CB    1 
ATOM   3000 N N     . THR   B 1 31  ? 30.276  -14.981 18.767 1.00 58.12  ? 55  THR   B N     1 
ATOM   3001 C CA    . THR   B 1 31  ? 31.350  -15.899 19.136 1.00 60.65  ? 55  THR   B CA    1 
ATOM   3002 C C     . THR   B 1 31  ? 32.473  -15.816 18.108 1.00 58.37  ? 55  THR   B C     1 
ATOM   3003 O O     . THR   B 1 31  ? 32.241  -16.006 16.910 1.00 57.85  ? 55  THR   B O     1 
ATOM   3004 C CB    . THR   B 1 31  ? 30.824  -17.333 19.237 1.00 59.03  ? 55  THR   B CB    1 
ATOM   3005 N N     . GLN   B 1 32  ? 33.683  -15.526 18.573 1.00 61.21  ? 56  GLN   B N     1 
ATOM   3006 C CA    . GLN   B 1 32  ? 34.856  -15.450 17.715 1.00 60.90  ? 56  GLN   B CA    1 
ATOM   3007 C C     . GLN   B 1 32  ? 35.812  -16.587 18.049 1.00 61.24  ? 56  GLN   B C     1 
ATOM   3008 O O     . GLN   B 1 32  ? 35.608  -17.344 19.003 1.00 61.65  ? 56  GLN   B O     1 
ATOM   3009 C CB    . GLN   B 1 32  ? 35.559  -14.095 17.860 1.00 57.32  ? 56  GLN   B CB    1 
ATOM   3010 N N     . SER   B 1 33  ? 36.867  -16.691 17.243 1.00 62.87  ? 57  SER   B N     1 
ATOM   3011 C CA    . SER   B 1 33  ? 37.865  -17.736 17.411 1.00 61.82  ? 57  SER   B CA    1 
ATOM   3012 C C     . SER   B 1 33  ? 38.536  -17.630 18.779 1.00 62.21  ? 57  SER   B C     1 
ATOM   3013 O O     . SER   B 1 33  ? 38.493  -16.596 19.443 1.00 61.48  ? 57  SER   B O     1 
ATOM   3014 C CB    . SER   B 1 33  ? 38.917  -17.645 16.303 1.00 61.11  ? 57  SER   B CB    1 
ATOM   3015 N N     . LYS   B 1 34  ? 39.170  -18.726 19.200 1.00 64.50  ? 58  LYS   B N     1 
ATOM   3016 C CA    . LYS   B 1 34  ? 39.907  -18.704 20.462 1.00 67.07  ? 58  LYS   B CA    1 
ATOM   3017 C C     . LYS   B 1 34  ? 41.182  -17.875 20.355 1.00 66.59  ? 58  LYS   B C     1 
ATOM   3018 O O     . LYS   B 1 34  ? 41.599  -17.251 21.338 1.00 64.73  ? 58  LYS   B O     1 
ATOM   3019 C CB    . LYS   B 1 34  ? 40.239  -20.129 20.908 1.00 70.51  ? 58  LYS   B CB    1 
ATOM   3020 N N     . GLU   B 1 35  ? 41.820  -17.864 19.181 1.00 67.43  ? 59  GLU   B N     1 
ATOM   3021 C CA    . GLU   B 1 35  ? 42.992  -17.018 18.994 1.00 65.47  ? 59  GLU   B CA    1 
ATOM   3022 C C     . GLU   B 1 35  ? 42.611  -15.545 18.997 1.00 63.24  ? 59  GLU   B C     1 
ATOM   3023 O O     . GLU   B 1 35  ? 43.383  -14.710 19.479 1.00 64.45  ? 59  GLU   B O     1 
ATOM   3024 C CB    . GLU   B 1 35  ? 43.712  -17.388 17.695 1.00 66.10  ? 59  GLU   B CB    1 
ATOM   3025 N N     . ILE   B 1 36  ? 41.422  -15.214 18.482 1.00 59.37  ? 60  ILE   B N     1 
ATOM   3026 C CA    . ILE   B 1 36  ? 40.951  -13.832 18.495 1.00 58.58  ? 60  ILE   B CA    1 
ATOM   3027 C C     . ILE   B 1 36  ? 40.538  -13.419 19.903 1.00 56.35  ? 60  ILE   B C     1 
ATOM   3028 O O     . ILE   B 1 36  ? 40.869  -12.319 20.362 1.00 52.42  ? 60  ILE   B O     1 
ATOM   3029 C CB    . ILE   B 1 36  ? 39.799  -13.649 17.488 1.00 57.23  ? 60  ILE   B CB    1 
ATOM   3030 C CG1   . ILE   B 1 36  ? 40.342  -13.584 16.058 1.00 57.12  ? 60  ILE   B CG1   1 
ATOM   3031 C CG2   . ILE   B 1 36  ? 38.980  -12.406 17.812 1.00 50.43  ? 60  ILE   B CG2   1 
ATOM   3032 C CD1   . ILE   B 1 36  ? 39.338  -13.067 15.048 1.00 55.68  ? 60  ILE   B CD1   1 
ATOM   3033 N N     . ARG   B 1 37  ? 39.806  -14.286 20.609 1.00 55.41  ? 61  ARG   B N     1 
ATOM   3034 C CA    . ARG   B 1 37  ? 39.422  -13.962 21.978 1.00 55.90  ? 61  ARG   B CA    1 
ATOM   3035 C C     . ARG   B 1 37  ? 40.650  -13.709 22.840 1.00 52.48  ? 61  ARG   B C     1 
ATOM   3036 O O     . ARG   B 1 37  ? 40.662  -12.787 23.661 1.00 47.36  ? 61  ARG   B O     1 
ATOM   3037 C CB    . ARG   B 1 37  ? 38.565  -15.083 22.571 1.00 59.13  ? 61  ARG   B CB    1 
ATOM   3038 C CG    . ARG   B 1 37  ? 37.114  -15.041 22.113 1.00 61.09  ? 61  ARG   B CG    1 
ATOM   3039 C CD    . ARG   B 1 37  ? 36.250  -16.065 22.839 1.00 59.98  ? 61  ARG   B CD    1 
ATOM   3040 N NE    . ARG   B 1 37  ? 36.617  -17.435 22.505 1.00 60.93  ? 61  ARG   B NE    1 
ATOM   3041 C CZ    . ARG   B 1 37  ? 37.264  -18.255 23.321 1.00 63.72  ? 61  ARG   B CZ    1 
ATOM   3042 N NH1   . ARG   B 1 37  ? 37.618  -17.879 24.539 1.00 65.07  ? 61  ARG   B NH1   1 
ATOM   3043 N NH2   . ARG   B 1 37  ? 37.559  -19.485 22.906 1.00 62.31  ? 61  ARG   B NH2   1 
ATOM   3044 N N     . ASP   B 1 38  ? 41.702  -14.500 22.644 1.00 53.93  ? 62  ASP   B N     1 
ATOM   3045 C CA    . ASP   B 1 38  ? 42.920  -14.323 23.429 1.00 54.91  ? 62  ASP   B CA    1 
ATOM   3046 C C     . ASP   B 1 38  ? 43.607  -13.013 23.082 1.00 52.61  ? 62  ASP   B C     1 
ATOM   3047 O O     . ASP   B 1 38  ? 44.121  -12.317 23.966 1.00 50.10  ? 62  ASP   B O     1 
ATOM   3048 C CB    . ASP   B 1 38  ? 43.868  -15.498 23.204 1.00 57.54  ? 62  ASP   B CB    1 
ATOM   3049 N N     . ALA   B 1 39  ? 43.636  -12.665 21.795 1.00 50.72  ? 63  ALA   B N     1 
ATOM   3050 C CA    . ALA   B 1 39  ? 44.233  -11.402 21.395 1.00 46.80  ? 63  ALA   B CA    1 
ATOM   3051 C C     . ALA   B 1 39  ? 43.394  -10.233 21.889 1.00 47.66  ? 63  ALA   B C     1 
ATOM   3052 O O     . ALA   B 1 39  ? 43.937  -9.242  22.393 1.00 46.55  ? 63  ALA   B O     1 
ATOM   3053 C CB    . ALA   B 1 39  ? 44.391  -11.362 19.877 1.00 52.40  ? 63  ALA   B CB    1 
ATOM   3054 N N     . ALA   B 1 40  ? 42.065  -10.340 21.768 1.00 46.76  ? 64  ALA   B N     1 
ATOM   3055 C CA    . ALA   B 1 40  ? 41.184  -9.303  22.291 1.00 45.82  ? 64  ALA   B CA    1 
ATOM   3056 C C     . ALA   B 1 40  ? 41.370  -9.113  23.792 1.00 43.36  ? 64  ALA   B C     1 
ATOM   3057 O O     . ALA   B 1 40  ? 41.363  -7.982  24.285 1.00 40.10  ? 64  ALA   B O     1 
ATOM   3058 C CB    . ALA   B 1 40  ? 39.721  -9.633  21.972 1.00 40.76  ? 64  ALA   B CB    1 
ATOM   3059 N N     . ALA   B 1 41  ? 41.526  -10.204 24.542 1.00 44.76  ? 65  ALA   B N     1 
ATOM   3060 C CA    . ALA   B 1 41  ? 41.687  -10.053 25.983 1.00 42.95  ? 65  ALA   B CA    1 
ATOM   3061 C C     . ALA   B 1 41  ? 43.014  -9.383  26.309 1.00 46.76  ? 65  ALA   B C     1 
ATOM   3062 O O     . ALA   B 1 41  ? 43.102  -8.580  27.245 1.00 44.28  ? 65  ALA   B O     1 
ATOM   3063 C CB    . ALA   B 1 41  ? 41.580  -11.414 26.667 1.00 44.41  ? 65  ALA   B CB    1 
ATOM   3064 N N     . SER   B 1 42  ? 44.055  -9.707  25.538 1.00 45.38  ? 66  SER   B N     1 
ATOM   3065 C CA    . SER   B 1 42  ? 45.349  -9.058  25.706 1.00 43.57  ? 66  SER   B CA    1 
ATOM   3066 C C     . SER   B 1 42  ? 45.256  -7.573  25.401 1.00 42.96  ? 66  SER   B C     1 
ATOM   3067 O O     . SER   B 1 42  ? 45.753  -6.739  26.163 1.00 45.63  ? 66  SER   B O     1 
ATOM   3068 C CB    . SER   B 1 42  ? 46.377  -9.730  24.801 1.00 46.05  ? 66  SER   B CB    1 
ATOM   3069 O OG    . SER   B 1 42  ? 46.490  -11.106 25.128 1.00 57.09  ? 66  SER   B OG    1 
ATOM   3070 N N     . THR   B 1 43  ? 44.617  -7.225  24.283 1.00 40.40  ? 67  THR   B N     1 
ATOM   3071 C CA    . THR   B 1 43  ? 44.451  -5.821  23.922 1.00 42.60  ? 67  THR   B CA    1 
ATOM   3072 C C     . THR   B 1 43  ? 43.618  -5.078  24.959 1.00 40.17  ? 67  THR   B C     1 
ATOM   3073 O O     . THR   B 1 43  ? 43.977  -3.971  25.381 1.00 41.48  ? 67  THR   B O     1 
ATOM   3074 C CB    . THR   B 1 43  ? 43.809  -5.722  22.542 1.00 39.51  ? 67  THR   B CB    1 
ATOM   3075 O OG1   . THR   B 1 43  ? 44.713  -6.261  21.572 1.00 42.75  ? 67  THR   B OG1   1 
ATOM   3076 C CG2   . THR   B 1 43  ? 43.457  -4.271  22.200 1.00 38.97  ? 67  THR   B CG2   1 
ATOM   3077 N N     . ALA   B 1 44  ? 42.500  -5.673  25.388 1.00 38.57  ? 68  ALA   B N     1 
ATOM   3078 C CA    . ALA   B 1 44  ? 41.654  -5.010  26.376 1.00 38.85  ? 68  ALA   B CA    1 
ATOM   3079 C C     . ALA   B 1 44  ? 42.385  -4.843  27.698 1.00 40.51  ? 68  ALA   B C     1 
ATOM   3080 O O     . ALA   B 1 44  ? 42.247  -3.816  28.368 1.00 39.26  ? 68  ALA   B O     1 
ATOM   3081 C CB    . ALA   B 1 44  ? 40.358  -5.791  26.580 1.00 39.12  ? 68  ALA   B CB    1 
ATOM   3082 N N     . ARG   B 1 45  ? 43.161  -5.848  28.097 1.00 41.79  ? 69  ARG   B N     1 
ATOM   3083 C CA    . ARG   B 1 45  ? 43.970  -5.701  29.299 1.00 45.59  ? 69  ARG   B CA    1 
ATOM   3084 C C     . ARG   B 1 45  ? 44.917  -4.512  29.170 1.00 46.96  ? 69  ARG   B C     1 
ATOM   3085 O O     . ARG   B 1 45  ? 45.023  -3.680  30.082 1.00 44.99  ? 69  ARG   B O     1 
ATOM   3086 C CB    . ARG   B 1 45  ? 44.751  -6.987  29.561 1.00 43.87  ? 69  ARG   B CB    1 
ATOM   3087 C CG    . ARG   B 1 45  ? 45.616  -6.938  30.819 1.00 48.99  ? 69  ARG   B CG    1 
ATOM   3088 C CD    . ARG   B 1 45  ? 46.324  -8.251  31.065 1.00 52.03  ? 69  ARG   B CD    1 
ATOM   3089 N NE    . ARG   B 1 45  ? 45.407  -9.360  31.297 1.00 53.77  ? 69  ARG   B NE    1 
ATOM   3090 C CZ    . ARG   B 1 45  ? 44.990  -9.749  32.495 1.00 54.34  ? 69  ARG   B CZ    1 
ATOM   3091 N NH1   . ARG   B 1 45  ? 45.315  -9.082  33.589 1.00 55.23  ? 69  ARG   B NH1   1 
ATOM   3092 N NH2   . ARG   B 1 45  ? 44.231  -10.839 32.597 1.00 54.58  ? 69  ARG   B NH2   1 
ATOM   3093 N N     . LYS   B 1 46  ? 45.620  -4.423  28.037 1.00 43.80  ? 70  LYS   B N     1 
ATOM   3094 C CA    . LYS   B 1 46  ? 46.552  -3.320  27.819 1.00 44.60  ? 70  LYS   B CA    1 
ATOM   3095 C C     . LYS   B 1 46  ? 45.833  -1.981  27.837 1.00 44.33  ? 70  LYS   B C     1 
ATOM   3096 O O     . LYS   B 1 46  ? 46.319  -1.014  28.430 1.00 43.69  ? 70  LYS   B O     1 
ATOM   3097 C CB    . LYS   B 1 46  ? 47.288  -3.512  26.491 1.00 48.71  ? 70  LYS   B CB    1 
ATOM   3098 C CG    . LYS   B 1 46  ? 48.011  -2.270  25.985 1.00 52.57  ? 70  LYS   B CG    1 
ATOM   3099 C CD    . LYS   B 1 46  ? 48.767  -2.550  24.692 1.00 51.74  ? 70  LYS   B CD    1 
ATOM   3100 C CE    . LYS   B 1 46  ? 47.832  -2.928  23.557 1.00 46.71  ? 70  LYS   B CE    1 
ATOM   3101 N NZ    . LYS   B 1 46  ? 48.586  -3.226  22.296 1.00 50.50  ? 70  LYS   B NZ    1 
ATOM   3102 N N     . LEU   B 1 47  ? 44.668  -1.905  27.194 1.00 41.68  ? 71  LEU   B N     1 
ATOM   3103 C CA    . LEU   B 1 47  ? 43.923  -0.650  27.176 1.00 42.39  ? 71  LEU   B CA    1 
ATOM   3104 C C     . LEU   B 1 47  ? 43.479  -0.246  28.572 1.00 40.79  ? 71  LEU   B C     1 
ATOM   3105 O O     . LEU   B 1 47  ? 43.520  0.935   28.926 1.00 42.55  ? 71  LEU   B O     1 
ATOM   3106 C CB    . LEU   B 1 47  ? 42.703  -0.776  26.270 1.00 35.33  ? 71  LEU   B CB    1 
ATOM   3107 C CG    . LEU   B 1 47  ? 42.988  -0.859  24.778 1.00 39.99  ? 71  LEU   B CG    1 
ATOM   3108 C CD1   . LEU   B 1 47  ? 41.686  -1.120  24.040 1.00 35.01  ? 71  LEU   B CD1   1 
ATOM   3109 C CD2   . LEU   B 1 47  ? 43.620  0.431   24.319 1.00 37.04  ? 71  LEU   B CD2   1 
ATOM   3110 N N     . ILE   B 1 48  ? 43.020  -1.214  29.367 1.00 40.79  ? 72  ILE   B N     1 
ATOM   3111 C CA    . ILE   B 1 48  ? 42.506  -0.911  30.697 1.00 42.63  ? 72  ILE   B CA    1 
ATOM   3112 C C     . ILE   B 1 48  ? 43.641  -0.575  31.649 1.00 45.52  ? 72  ILE   B C     1 
ATOM   3113 O O     . ILE   B 1 48  ? 43.507  0.313   32.498 1.00 48.02  ? 72  ILE   B O     1 
ATOM   3114 C CB    . ILE   B 1 48  ? 41.661  -2.087  31.214 1.00 45.33  ? 72  ILE   B CB    1 
ATOM   3115 C CG1   . ILE   B 1 48  ? 40.400  -2.221  30.376 1.00 44.97  ? 72  ILE   B CG1   1 
ATOM   3116 C CG2   . ILE   B 1 48  ? 41.306  -1.912  32.694 1.00 48.18  ? 72  ILE   B CG2   1 
ATOM   3117 C CD1   . ILE   B 1 48  ? 39.723  -3.521  30.596 1.00 47.78  ? 72  ILE   B CD1   1 
ATOM   3118 N N     . GLU   B 1 49  ? 44.781  -1.261  31.523 1.00 46.67  ? 73  GLU   B N     1 
ATOM   3119 C CA    . GLU   B 1 49  ? 45.901  -0.922  32.395 1.00 49.45  ? 73  GLU   B CA    1 
ATOM   3120 C C     . GLU   B 1 49  ? 46.462  0.452   32.056 1.00 50.39  ? 73  GLU   B C     1 
ATOM   3121 O O     . GLU   B 1 49  ? 46.926  1.170   32.951 1.00 53.26  ? 73  GLU   B O     1 
ATOM   3122 C CB    . GLU   B 1 49  ? 46.997  -1.994  32.325 1.00 48.27  ? 73  GLU   B CB    1 
ATOM   3123 N N     . ALA   B 1 50  ? 46.427  0.836   30.780 1.00 50.79  ? 74  ALA   B N     1 
ATOM   3124 C CA    . ALA   B 1 50  ? 46.789  2.199   30.419 1.00 51.58  ? 74  ALA   B CA    1 
ATOM   3125 C C     . ALA   B 1 50  ? 45.815  3.200   31.031 1.00 54.48  ? 74  ALA   B C     1 
ATOM   3126 O O     . ALA   B 1 50  ? 46.232  4.225   31.582 1.00 59.12  ? 74  ALA   B O     1 
ATOM   3127 C CB    . ALA   B 1 50  ? 46.834  2.344   28.895 1.00 52.47  ? 74  ALA   B CB    1 
ATOM   3128 N N     . LEU   B 1 51  ? 44.512  2.914   30.953 1.00 50.44  ? 75  LEU   B N     1 
ATOM   3129 C CA    . LEU   B 1 51  ? 43.511  3.841   31.475 1.00 53.10  ? 75  LEU   B CA    1 
ATOM   3130 C C     . LEU   B 1 51  ? 43.627  3.982   32.987 1.00 56.25  ? 75  LEU   B C     1 
ATOM   3131 O O     . LEU   B 1 51  ? 43.857  5.078   33.507 1.00 63.44  ? 75  LEU   B O     1 
ATOM   3132 C CB    . LEU   B 1 51  ? 42.112  3.367   31.101 1.00 46.96  ? 75  LEU   B CB    1 
ATOM   3133 C CG    . LEU   B 1 51  ? 41.599  3.709   29.710 1.00 45.74  ? 75  LEU   B CG    1 
ATOM   3134 C CD1   . LEU   B 1 51  ? 40.284  3.017   29.511 1.00 44.35  ? 75  LEU   B CD1   1 
ATOM   3135 C CD2   . LEU   B 1 51  ? 41.443  5.202   29.601 1.00 45.13  ? 75  LEU   B CD2   1 
ATOM   3136 N N     . ARG   B 1 52  ? 43.461  2.874   33.710 1.00 56.88  ? 76  ARG   B N     1 
ATOM   3137 C CA    . ARG   B 1 52  ? 43.549  2.912   35.165 1.00 57.31  ? 76  ARG   B CA    1 
ATOM   3138 C C     . ARG   B 1 52  ? 44.888  3.451   35.650 1.00 64.16  ? 76  ARG   B C     1 
ATOM   3139 O O     . ARG   B 1 52  ? 44.984  3.887   36.801 1.00 68.57  ? 76  ARG   B O     1 
ATOM   3140 C CB    . ARG   B 1 52  ? 43.312  1.513   35.750 1.00 56.95  ? 76  ARG   B CB    1 
ATOM   3141 C CG    . ARG   B 1 52  ? 41.853  1.056   35.760 1.00 50.58  ? 76  ARG   B CG    1 
ATOM   3142 C CD    . ARG   B 1 52  ? 41.686  -0.288  36.475 1.00 54.21  ? 76  ARG   B CD    1 
ATOM   3143 N NE    . ARG   B 1 52  ? 40.302  -0.518  36.878 1.00 51.03  ? 76  ARG   B NE    1 
ATOM   3144 C CZ    . ARG   B 1 52  ? 39.860  -1.611  37.491 1.00 54.61  ? 76  ARG   B CZ    1 
ATOM   3145 N NH1   . ARG   B 1 52  ? 40.656  -2.646  37.728 1.00 52.16  ? 76  ARG   B NH1   1 
ATOM   3146 N NH2   . ARG   B 1 52  ? 38.589  -1.664  37.888 1.00 50.15  ? 76  ARG   B NH2   1 
ATOM   3147 N N     . GLY   B 1 53  ? 45.914  3.449   34.800 1.00 64.96  ? 77  GLY   B N     1 
ATOM   3148 C CA    . GLY   B 1 53  ? 47.249  3.832   35.212 1.00 65.29  ? 77  GLY   B CA    1 
ATOM   3149 C C     . GLY   B 1 53  ? 47.633  5.281   34.982 1.00 70.80  ? 77  GLY   B C     1 
ATOM   3150 O O     . GLY   B 1 53  ? 48.609  5.753   35.573 1.00 72.53  ? 77  GLY   B O     1 
ATOM   3151 N N     . LYS   B 1 54  ? 46.884  6.005   34.142 1.00 71.23  ? 78  LYS   B N     1 
ATOM   3152 C CA    . LYS   B 1 54  ? 47.271  7.350   33.733 1.00 74.67  ? 78  LYS   B CA    1 
ATOM   3153 C C     . LYS   B 1 54  ? 46.329  8.452   34.194 1.00 80.61  ? 78  LYS   B C     1 
ATOM   3154 O O     . LYS   B 1 54  ? 46.770  9.602   34.306 1.00 84.55  ? 78  LYS   B O     1 
ATOM   3155 C CB    . LYS   B 1 54  ? 47.398  7.430   32.201 1.00 73.70  ? 78  LYS   B CB    1 
ATOM   3156 N N     . HIS   B 1 55  ? 45.063  8.152   34.456 1.00 84.50  ? 79  HIS   B N     1 
ATOM   3157 C CA    . HIS   B 1 55  ? 44.112  9.184   34.852 1.00 85.08  ? 79  HIS   B CA    1 
ATOM   3158 C C     . HIS   B 1 55  ? 43.043  8.608   35.771 1.00 86.69  ? 79  HIS   B C     1 
ATOM   3159 O O     . HIS   B 1 55  ? 43.307  7.678   36.533 1.00 87.10  ? 79  HIS   B O     1 
ATOM   3160 C CB    . HIS   B 1 55  ? 43.466  9.821   33.617 1.00 88.56  ? 79  HIS   B CB    1 
ATOM   3161 N N     . GLY   B 1 66  ? 29.090  19.302  35.227 1.00 87.37  ? 192 GLY   B N     1 
ATOM   3162 C CA    . GLY   B 1 66  ? 29.996  18.519  34.406 1.00 82.81  ? 192 GLY   B CA    1 
ATOM   3163 C C     . GLY   B 1 66  ? 30.255  19.085  33.018 1.00 81.44  ? 192 GLY   B C     1 
ATOM   3164 O O     . GLY   B 1 66  ? 29.848  18.495  32.019 1.00 81.73  ? 192 GLY   B O     1 
ATOM   3165 N N     . GLU   B 1 67  ? 30.954  20.224  32.956 1.00 81.91  ? 193 GLU   B N     1 
ATOM   3166 C CA    . GLU   B 1 67  ? 31.220  20.933  31.703 1.00 78.10  ? 193 GLU   B CA    1 
ATOM   3167 C C     . GLU   B 1 67  ? 32.208  20.209  30.791 1.00 73.98  ? 193 GLU   B C     1 
ATOM   3168 O O     . GLU   B 1 67  ? 32.442  20.675  29.668 1.00 71.01  ? 193 GLU   B O     1 
ATOM   3169 C CB    . GLU   B 1 67  ? 31.738  22.342  32.007 1.00 77.48  ? 193 GLU   B CB    1 
ATOM   3170 N N     . GLN   B 1 68  ? 32.787  19.090  31.232 1.00 71.21  ? 194 GLN   B N     1 
ATOM   3171 C CA    . GLN   B 1 68  ? 33.782  18.387  30.432 1.00 65.65  ? 194 GLN   B CA    1 
ATOM   3172 C C     . GLN   B 1 68  ? 33.185  17.707  29.206 1.00 62.49  ? 194 GLN   B C     1 
ATOM   3173 O O     . GLN   B 1 68  ? 33.943  17.266  28.335 1.00 58.26  ? 194 GLN   B O     1 
ATOM   3174 C CB    . GLN   B 1 68  ? 34.511  17.348  31.291 1.00 64.61  ? 194 GLN   B CB    1 
ATOM   3175 C CG    . GLN   B 1 68  ? 33.664  16.138  31.684 1.00 65.37  ? 194 GLN   B CG    1 
ATOM   3176 C CD    . GLN   B 1 68  ? 32.926  16.319  33.008 1.00 69.43  ? 194 GLN   B CD    1 
ATOM   3177 O OE1   . GLN   B 1 68  ? 32.793  17.434  33.515 1.00 73.48  ? 194 GLN   B OE1   1 
ATOM   3178 N NE2   . GLN   B 1 68  ? 32.453  15.213  33.576 1.00 69.31  ? 194 GLN   B NE2   1 
ATOM   3179 N N     . PHE   B 1 69  ? 31.860  17.603  29.120 1.00 61.58  ? 195 PHE   B N     1 
ATOM   3180 C CA    . PHE   B 1 69  ? 31.211  16.965  27.986 1.00 57.89  ? 195 PHE   B CA    1 
ATOM   3181 C C     . PHE   B 1 69  ? 30.905  17.929  26.851 1.00 56.39  ? 195 PHE   B C     1 
ATOM   3182 O O     . PHE   B 1 69  ? 30.588  17.471  25.751 1.00 55.45  ? 195 PHE   B O     1 
ATOM   3183 C CB    . PHE   B 1 69  ? 29.911  16.286  28.428 1.00 57.75  ? 195 PHE   B CB    1 
ATOM   3184 C CG    . PHE   B 1 69  ? 30.100  15.230  29.479 1.00 56.36  ? 195 PHE   B CG    1 
ATOM   3185 C CD1   . PHE   B 1 69  ? 30.820  14.080  29.206 1.00 56.00  ? 195 PHE   B CD1   1 
ATOM   3186 C CD2   . PHE   B 1 69  ? 29.539  15.380  30.735 1.00 60.75  ? 195 PHE   B CD2   1 
ATOM   3187 C CE1   . PHE   B 1 69  ? 30.991  13.113  30.169 1.00 55.33  ? 195 PHE   B CE1   1 
ATOM   3188 C CE2   . PHE   B 1 69  ? 29.706  14.406  31.705 1.00 62.39  ? 195 PHE   B CE2   1 
ATOM   3189 C CZ    . PHE   B 1 69  ? 30.430  13.270  31.415 1.00 59.32  ? 195 PHE   B CZ    1 
ATOM   3190 N N     . VAL   B 1 70  ? 30.996  19.236  27.081 1.00 60.29  ? 196 VAL   B N     1 
ATOM   3191 C CA    . VAL   B 1 70  ? 30.665  20.246  26.078 1.00 59.82  ? 196 VAL   B CA    1 
ATOM   3192 C C     . VAL   B 1 70  ? 31.957  20.758  25.453 1.00 60.93  ? 196 VAL   B C     1 
ATOM   3193 O O     . VAL   B 1 70  ? 32.824  21.292  26.156 1.00 61.85  ? 196 VAL   B O     1 
ATOM   3194 C CB    . VAL   B 1 70  ? 29.859  21.401  26.692 1.00 61.50  ? 196 VAL   B CB    1 
ATOM   3195 N N     . THR   B 1 71  ? 32.078  20.618  24.128 1.00 61.05  ? 197 THR   B N     1 
ATOM   3196 C CA    . THR   B 1 71  ? 33.277  21.089  23.437 1.00 62.06  ? 197 THR   B CA    1 
ATOM   3197 C C     . THR   B 1 71  ? 33.363  22.609  23.423 1.00 67.71  ? 197 THR   B C     1 
ATOM   3198 O O     . THR   B 1 71  ? 34.466  23.168  23.476 1.00 72.46  ? 197 THR   B O     1 
ATOM   3199 C CB    . THR   B 1 71  ? 33.314  20.553  22.004 1.00 62.28  ? 197 THR   B CB    1 
ATOM   3200 N N     . GLY   B 1 72  ? 32.223  23.289  23.357 1.00 64.46  ? 198 GLY   B N     1 
ATOM   3201 C CA    . GLY   B 1 72  ? 32.206  24.735  23.301 1.00 67.59  ? 198 GLY   B CA    1 
ATOM   3202 C C     . GLY   B 1 72  ? 30.802  25.287  23.189 1.00 68.39  ? 198 GLY   B C     1 
ATOM   3203 O O     . GLY   B 1 72  ? 29.871  24.564  22.816 1.00 65.81  ? 198 GLY   B O     1 
ATOM   3204 N N     . GLU   B 1 73  ? 30.632  26.567  23.521 1.00 68.13  ? 199 GLU   B N     1 
ATOM   3205 C CA    . GLU   B 1 73  ? 29.311  27.180  23.448 1.00 71.97  ? 199 GLU   B CA    1 
ATOM   3206 C C     . GLU   B 1 73  ? 28.932  27.536  22.014 1.00 69.92  ? 199 GLU   B C     1 
ATOM   3207 O O     . GLU   B 1 73  ? 27.741  27.560  21.674 1.00 68.40  ? 199 GLU   B O     1 
ATOM   3208 C CB    . GLU   B 1 73  ? 29.263  28.421  24.340 1.00 68.39  ? 199 GLU   B CB    1 
ATOM   3209 N N     . THR   B 1 74  ? 29.919  27.812  21.170 1.00 69.38  ? 200 THR   B N     1 
ATOM   3210 C CA    . THR   B 1 74  ? 29.687  28.083  19.763 1.00 67.01  ? 200 THR   B CA    1 
ATOM   3211 C C     . THR   B 1 74  ? 30.415  27.042  18.925 1.00 66.35  ? 200 THR   B C     1 
ATOM   3212 O O     . THR   B 1 74  ? 31.378  26.408  19.375 1.00 64.99  ? 200 THR   B O     1 
ATOM   3213 C CB    . THR   B 1 74  ? 30.152  29.497  19.371 1.00 65.52  ? 200 THR   B CB    1 
ATOM   3214 N N     . ILE   B 1 75  ? 29.926  26.851  17.697 1.00 64.60  ? 201 ILE   B N     1 
ATOM   3215 C CA    . ILE   B 1 75  ? 30.659  26.008  16.768 1.00 61.73  ? 201 ILE   B CA    1 
ATOM   3216 C C     . ILE   B 1 75  ? 31.984  26.654  16.403 1.00 64.69  ? 201 ILE   B C     1 
ATOM   3217 O O     . ILE   B 1 75  ? 32.895  25.968  15.922 1.00 68.16  ? 201 ILE   B O     1 
ATOM   3218 C CB    . ILE   B 1 75  ? 29.813  25.696  15.520 1.00 57.40  ? 201 ILE   B CB    1 
ATOM   3219 N N     . ARG   B 1 76  ? 32.123  27.962  16.646 1.00 67.58  ? 202 ARG   B N     1 
ATOM   3220 C CA    . ARG   B 1 76  ? 33.396  28.633  16.414 1.00 66.91  ? 202 ARG   B CA    1 
ATOM   3221 C C     . ARG   B 1 76  ? 34.451  28.160  17.407 1.00 68.94  ? 202 ARG   B C     1 
ATOM   3222 O O     . ARG   B 1 76  ? 35.549  27.750  17.014 1.00 68.10  ? 202 ARG   B O     1 
ATOM   3223 C CB    . ARG   B 1 76  ? 33.213  30.149  16.494 1.00 66.19  ? 202 ARG   B CB    1 
ATOM   3224 N N     . GLU   B 1 77  ? 34.131  28.198  18.704 1.00 76.20  ? 203 GLU   B N     1 
ATOM   3225 C CA    . GLU   B 1 77  ? 35.082  27.733  19.708 1.00 74.73  ? 203 GLU   B CA    1 
ATOM   3226 C C     . GLU   B 1 77  ? 35.303  26.230  19.611 1.00 75.02  ? 203 GLU   B C     1 
ATOM   3227 O O     . GLU   B 1 77  ? 36.417  25.749  19.856 1.00 74.36  ? 203 GLU   B O     1 
ATOM   3228 C CB    . GLU   B 1 77  ? 34.602  28.119  21.110 1.00 76.51  ? 203 GLU   B CB    1 
ATOM   3229 N N     . ALA   B 1 78  ? 34.263  25.476  19.249 1.00 71.22  ? 204 ALA   B N     1 
ATOM   3230 C CA    . ALA   B 1 78  ? 34.417  24.037  19.081 1.00 66.72  ? 204 ALA   B CA    1 
ATOM   3231 C C     . ALA   B 1 78  ? 35.363  23.713  17.930 1.00 68.98  ? 204 ALA   B C     1 
ATOM   3232 O O     . ALA   B 1 78  ? 36.204  22.814  18.047 1.00 64.11  ? 204 ALA   B O     1 
ATOM   3233 C CB    . ALA   B 1 78  ? 33.053  23.386  18.860 1.00 63.49  ? 204 ALA   B CB    1 
ATOM   3234 N N     . LEU   B 1 79  ? 35.249  24.442  16.811 1.00 64.86  ? 205 LEU   B N     1 
ATOM   3235 C CA    . LEU   B 1 79  ? 36.128  24.175  15.677 1.00 65.48  ? 205 LEU   B CA    1 
ATOM   3236 C C     . LEU   B 1 79  ? 37.567  24.579  15.975 1.00 69.15  ? 205 LEU   B C     1 
ATOM   3237 O O     . LEU   B 1 79  ? 38.503  23.939  15.480 1.00 71.58  ? 205 LEU   B O     1 
ATOM   3238 C CB    . LEU   B 1 79  ? 35.618  24.894  14.424 1.00 61.83  ? 205 LEU   B CB    1 
ATOM   3239 N N     . LYS   B 1 80  ? 37.770  25.623  16.780 1.00 71.49  ? 206 LYS   B N     1 
ATOM   3240 C CA    . LYS   B 1 80  ? 39.131  26.009  17.144 1.00 71.73  ? 206 LYS   B CA    1 
ATOM   3241 C C     . LYS   B 1 80  ? 39.778  24.946  18.023 1.00 70.79  ? 206 LYS   B C     1 
ATOM   3242 O O     . LYS   B 1 80  ? 40.923  24.544  17.786 1.00 72.41  ? 206 LYS   B O     1 
ATOM   3243 C CB    . LYS   B 1 80  ? 39.127  27.366  17.848 1.00 73.54  ? 206 LYS   B CB    1 
ATOM   3244 N N     . ARG   B 1 81  ? 39.044  24.456  19.027 1.00 72.16  ? 207 ARG   B N     1 
ATOM   3245 C CA    . ARG   B 1 81  ? 39.549  23.482  19.990 1.00 67.51  ? 207 ARG   B CA    1 
ATOM   3246 C C     . ARG   B 1 81  ? 39.831  22.112  19.383 1.00 68.79  ? 207 ARG   B C     1 
ATOM   3247 O O     . ARG   B 1 81  ? 40.302  21.224  20.105 1.00 64.61  ? 207 ARG   B O     1 
ATOM   3248 C CB    . ARG   B 1 81  ? 38.554  23.335  21.143 1.00 69.08  ? 207 ARG   B CB    1 
ATOM   3249 N N     . SER   B 1 82  ? 39.581  21.916  18.090 1.00 65.81  ? 208 SER   B N     1 
ATOM   3250 C CA    . SER   B 1 82  ? 39.696  20.597  17.484 1.00 63.27  ? 208 SER   B CA    1 
ATOM   3251 C C     . SER   B 1 82  ? 41.070  20.317  16.885 1.00 61.02  ? 208 SER   B C     1 
ATOM   3252 O O     . SER   B 1 82  ? 41.366  19.157  16.580 1.00 59.59  ? 208 SER   B O     1 
ATOM   3253 C CB    . SER   B 1 82  ? 38.631  20.428  16.393 1.00 60.07  ? 208 SER   B CB    1 
ATOM   3254 N N     . LYS   B 1 83  ? 41.912  21.339  16.718 1.00 63.56  ? 209 LYS   B N     1 
ATOM   3255 C CA    . LYS   B 1 83  ? 43.166  21.159  15.992 1.00 63.40  ? 209 LYS   B CA    1 
ATOM   3256 C C     . LYS   B 1 83  ? 44.095  20.187  16.706 1.00 61.76  ? 209 LYS   B C     1 
ATOM   3257 O O     . LYS   B 1 83  ? 44.736  19.349  16.063 1.00 60.80  ? 209 LYS   B O     1 
ATOM   3258 C CB    . LYS   B 1 83  ? 43.856  22.511  15.800 1.00 61.24  ? 209 LYS   B CB    1 
ATOM   3259 N N     . GLU   B 1 84  ? 44.178  20.285  18.036 1.00 62.84  ? 210 GLU   B N     1 
ATOM   3260 C CA    . GLU   B 1 84  ? 45.141  19.496  18.801 1.00 63.67  ? 210 GLU   B CA    1 
ATOM   3261 C C     . GLU   B 1 84  ? 44.986  18.003  18.527 1.00 60.24  ? 210 GLU   B C     1 
ATOM   3262 O O     . GLU   B 1 84  ? 45.903  17.352  18.013 1.00 61.03  ? 210 GLU   B O     1 
ATOM   3263 C CB    . GLU   B 1 84  ? 44.982  19.793  20.291 1.00 63.03  ? 210 GLU   B CB    1 
ATOM   3264 N N     . LEU   B 1 85  ? 43.821  17.441  18.843 1.00 57.99  ? 211 LEU   B N     1 
ATOM   3265 C CA    . LEU   B 1 85  ? 43.649  16.009  18.655 1.00 57.18  ? 211 LEU   B CA    1 
ATOM   3266 C C     . LEU   B 1 85  ? 43.410  15.621  17.201 1.00 56.93  ? 211 LEU   B C     1 
ATOM   3267 O O     . LEU   B 1 85  ? 43.567  14.441  16.863 1.00 55.08  ? 211 LEU   B O     1 
ATOM   3268 C CB    . LEU   B 1 85  ? 42.514  15.490  19.548 1.00 56.77  ? 211 LEU   B CB    1 
ATOM   3269 C CG    . LEU   B 1 85  ? 42.833  15.484  21.058 1.00 56.35  ? 211 LEU   B CG    1 
ATOM   3270 C CD1   . LEU   B 1 85  ? 41.697  14.884  21.885 1.00 52.77  ? 211 LEU   B CD1   1 
ATOM   3271 C CD2   . LEU   B 1 85  ? 44.146  14.761  21.364 1.00 57.57  ? 211 LEU   B CD2   1 
ATOM   3272 N N     . GLU   B 1 86  ? 43.060  16.568  16.325 1.00 55.67  ? 212 GLU   B N     1 
ATOM   3273 C CA    . GLU   B 1 86  ? 43.036  16.243  14.902 1.00 55.48  ? 212 GLU   B CA    1 
ATOM   3274 C C     . GLU   B 1 86  ? 44.447  15.992  14.380 1.00 58.06  ? 212 GLU   B C     1 
ATOM   3275 O O     . GLU   B 1 86  ? 44.674  15.038  13.626 1.00 55.70  ? 212 GLU   B O     1 
ATOM   3276 C CB    . GLU   B 1 86  ? 42.348  17.352  14.103 1.00 57.64  ? 212 GLU   B CB    1 
ATOM   3277 C CG    . GLU   B 1 86  ? 40.821  17.269  14.129 1.00 54.65  ? 212 GLU   B CG    1 
ATOM   3278 C CD    . GLU   B 1 86  ? 40.159  18.249  13.171 1.00 60.05  ? 212 GLU   B CD    1 
ATOM   3279 O OE1   . GLU   B 1 86  ? 40.881  19.064  12.546 1.00 57.24  ? 212 GLU   B OE1   1 
ATOM   3280 O OE2   . GLU   B 1 86  ? 38.911  18.193  13.037 1.00 57.05  ? 212 GLU   B OE2   1 
ATOM   3281 N N     . GLU   B 1 87  ? 45.412  16.824  14.785 1.00 60.27  ? 213 GLU   B N     1 
ATOM   3282 C CA    . GLU   B 1 87  ? 46.805  16.567  14.426 1.00 62.93  ? 213 GLU   B CA    1 
ATOM   3283 C C     . GLU   B 1 87  ? 47.287  15.238  14.993 1.00 69.52  ? 213 GLU   B C     1 
ATOM   3284 O O     . GLU   B 1 87  ? 48.139  14.576  14.387 1.00 75.21  ? 213 GLU   B O     1 
ATOM   3285 C CB    . GLU   B 1 87  ? 47.705  17.709  14.909 1.00 63.19  ? 213 GLU   B CB    1 
ATOM   3286 N N     . LYS   B 1 88  ? 46.755  14.830  16.149 1.00 63.39  ? 214 LYS   B N     1 
ATOM   3287 C CA    . LYS   B 1 88  ? 47.054  13.509  16.681 1.00 67.07  ? 214 LYS   B CA    1 
ATOM   3288 C C     . LYS   B 1 88  ? 46.394  12.397  15.872 1.00 66.75  ? 214 LYS   B C     1 
ATOM   3289 O O     . LYS   B 1 88  ? 46.769  11.230  16.028 1.00 67.27  ? 214 LYS   B O     1 
ATOM   3290 C CB    . LYS   B 1 88  ? 46.617  13.422  18.144 1.00 63.70  ? 214 LYS   B CB    1 
ATOM   3291 N N     . GLY   B 1 89  ? 45.415  12.725  15.025 1.00 59.14  ? 215 GLY   B N     1 
ATOM   3292 C CA    . GLY   B 1 89  ? 44.749  11.736  14.198 1.00 54.46  ? 215 GLY   B CA    1 
ATOM   3293 C C     . GLY   B 1 89  ? 43.290  11.484  14.527 1.00 51.81  ? 215 GLY   B C     1 
ATOM   3294 O O     . GLY   B 1 89  ? 42.680  10.601  13.908 1.00 47.28  ? 215 GLY   B O     1 
ATOM   3295 N N     . PHE   B 1 90  ? 42.716  12.203  15.487 1.00 46.14  ? 216 PHE   B N     1 
ATOM   3296 C CA    . PHE   B 1 90  ? 41.283  12.125  15.722 1.00 45.37  ? 216 PHE   B CA    1 
ATOM   3297 C C     . PHE   B 1 90  ? 40.530  12.905  14.649 1.00 45.94  ? 216 PHE   B C     1 
ATOM   3298 O O     . PHE   B 1 90  ? 41.087  13.767  13.972 1.00 44.15  ? 216 PHE   B O     1 
ATOM   3299 C CB    . PHE   B 1 90  ? 40.922  12.698  17.089 1.00 44.07  ? 216 PHE   B CB    1 
ATOM   3300 C CG    . PHE   B 1 90  ? 41.368  11.853  18.252 1.00 44.51  ? 216 PHE   B CG    1 
ATOM   3301 C CD1   . PHE   B 1 90  ? 42.637  11.984  18.776 1.00 48.36  ? 216 PHE   B CD1   1 
ATOM   3302 C CD2   . PHE   B 1 90  ? 40.494  10.953  18.845 1.00 42.27  ? 216 PHE   B CD2   1 
ATOM   3303 C CE1   . PHE   B 1 90  ? 43.035  11.216  19.873 1.00 44.42  ? 216 PHE   B CE1   1 
ATOM   3304 C CE2   . PHE   B 1 90  ? 40.888  10.184  19.929 1.00 41.40  ? 216 PHE   B CE2   1 
ATOM   3305 C CZ    . PHE   B 1 90  ? 42.155  10.319  20.443 1.00 42.35  ? 216 PHE   B CZ    1 
ATOM   3306 N N     . SER   B 1 91  ? 39.248  12.590  14.500 1.00 40.81  ? 217 SER   B N     1 
ATOM   3307 C CA    . SER   B 1 91  ? 38.322  13.418  13.736 1.00 38.21  ? 217 SER   B CA    1 
ATOM   3308 C C     . SER   B 1 91  ? 37.172  13.802  14.664 1.00 42.53  ? 217 SER   B C     1 
ATOM   3309 O O     . SER   B 1 91  ? 37.122  13.361  15.814 1.00 35.35  ? 217 SER   B O     1 
ATOM   3310 C CB    . SER   B 1 91  ? 37.811  12.680  12.502 1.00 40.54  ? 217 SER   B CB    1 
ATOM   3311 O OG    . SER   B 1 91  ? 37.123  11.514  12.889 1.00 41.53  ? 217 SER   B OG    1 
ATOM   3312 N N     . TYR   B 1 92  ? 36.248  14.639  14.173 1.00 41.31  ? 218 TYR   B N     1 
ATOM   3313 C CA    . TYR   B 1 92  ? 35.147  15.139  14.994 1.00 40.45  ? 218 TYR   B CA    1 
ATOM   3314 C C     . TYR   B 1 92  ? 33.803  15.019  14.278 1.00 39.64  ? 218 TYR   B C     1 
ATOM   3315 O O     . TYR   B 1 92  ? 33.715  15.032  13.046 1.00 37.09  ? 218 TYR   B O     1 
ATOM   3316 C CB    . TYR   B 1 92  ? 35.356  16.611  15.410 1.00 43.51  ? 218 TYR   B CB    1 
ATOM   3317 C CG    . TYR   B 1 92  ? 36.334  16.784  16.556 1.00 45.20  ? 218 TYR   B CG    1 
ATOM   3318 C CD1   . TYR   B 1 92  ? 37.699  16.891  16.316 1.00 46.90  ? 218 TYR   B CD1   1 
ATOM   3319 C CD2   . TYR   B 1 92  ? 35.891  16.840  17.873 1.00 44.64  ? 218 TYR   B CD2   1 
ATOM   3320 C CE1   . TYR   B 1 92  ? 38.602  17.048  17.352 1.00 48.50  ? 218 TYR   B CE1   1 
ATOM   3321 C CE2   . TYR   B 1 92  ? 36.793  16.992  18.933 1.00 44.94  ? 218 TYR   B CE2   1 
ATOM   3322 C CZ    . TYR   B 1 92  ? 38.146  17.093  18.662 1.00 48.92  ? 218 TYR   B CZ    1 
ATOM   3323 O OH    . TYR   B 1 92  ? 39.048  17.238  19.693 1.00 48.98  ? 218 TYR   B OH    1 
ATOM   3324 N N     . SER   B 1 93  ? 32.759  14.855  15.083 1.00 38.46  ? 219 SER   B N     1 
ATOM   3325 C CA    . SER   B 1 93  ? 31.371  15.014  14.660 1.00 40.03  ? 219 SER   B CA    1 
ATOM   3326 C C     . SER   B 1 93  ? 30.711  15.969  15.646 1.00 42.15  ? 219 SER   B C     1 
ATOM   3327 O O     . SER   B 1 93  ? 30.560  15.639  16.826 1.00 41.35  ? 219 SER   B O     1 
ATOM   3328 C CB    . SER   B 1 93  ? 30.631  13.679  14.631 1.00 40.14  ? 219 SER   B CB    1 
ATOM   3329 O OG    . SER   B 1 93  ? 29.262  13.884  14.331 1.00 41.27  ? 219 SER   B OG    1 
ATOM   3330 N N     . TYR   B 1 94  ? 30.313  17.141  15.174 1.00 38.98  ? 220 TYR   B N     1 
ATOM   3331 C CA    . TYR   B 1 94  ? 29.674  18.123  16.033 1.00 41.43  ? 220 TYR   B CA    1 
ATOM   3332 C C     . TYR   B 1 94  ? 28.166  17.921  16.043 1.00 45.11  ? 220 TYR   B C     1 
ATOM   3333 O O     . TYR   B 1 94  ? 27.566  17.485  15.055 1.00 43.69  ? 220 TYR   B O     1 
ATOM   3334 C CB    . TYR   B 1 94  ? 30.009  19.543  15.568 1.00 43.23  ? 220 TYR   B CB    1 
ATOM   3335 C CG    . TYR   B 1 94  ? 31.498  19.780  15.473 1.00 46.37  ? 220 TYR   B CG    1 
ATOM   3336 C CD1   . TYR   B 1 94  ? 32.224  20.219  16.581 1.00 47.36  ? 220 TYR   B CD1   1 
ATOM   3337 C CD2   . TYR   B 1 94  ? 32.189  19.528  14.291 1.00 44.79  ? 220 TYR   B CD2   1 
ATOM   3338 C CE1   . TYR   B 1 94  ? 33.593  20.424  16.507 1.00 50.67  ? 220 TYR   B CE1   1 
ATOM   3339 C CE2   . TYR   B 1 94  ? 33.564  19.733  14.207 1.00 46.09  ? 220 TYR   B CE2   1 
ATOM   3340 C CZ    . TYR   B 1 94  ? 34.260  20.183  15.316 1.00 51.51  ? 220 TYR   B CZ    1 
ATOM   3341 O OH    . TYR   B 1 94  ? 35.625  20.388  15.229 1.00 54.32  ? 220 TYR   B OH    1 
ATOM   3342 N N     . ASP   B 1 95  ? 27.561  18.219  17.190 1.00 48.71  ? 221 ASP   B N     1 
ATOM   3343 C CA    . ASP   B 1 95  ? 26.114  18.337  17.318 1.00 52.93  ? 221 ASP   B CA    1 
ATOM   3344 C C     . ASP   B 1 95  ? 25.806  19.689  17.946 1.00 55.65  ? 221 ASP   B C     1 
ATOM   3345 O O     . ASP   B 1 95  ? 26.288  19.988  19.043 1.00 54.25  ? 221 ASP   B O     1 
ATOM   3346 C CB    . ASP   B 1 95  ? 25.532  17.207  18.169 1.00 49.65  ? 221 ASP   B CB    1 
ATOM   3347 C CG    . ASP   B 1 95  ? 24.000  17.259  18.272 1.00 56.48  ? 221 ASP   B CG    1 
ATOM   3348 O OD1   . ASP   B 1 95  ? 23.395  18.344  18.148 1.00 59.88  ? 221 ASP   B OD1   1 
ATOM   3349 O OD2   . ASP   B 1 95  ? 23.391  16.193  18.504 1.00 55.26  ? 221 ASP   B OD2   1 
ATOM   3350 N N     . MET   B 1 96  ? 25.021  20.508  17.245 1.00 61.94  ? 222 MET   B N     1 
ATOM   3351 C CA    . MET   B 1 96  ? 24.464  21.703  17.864 1.00 64.82  ? 222 MET   B CA    1 
ATOM   3352 C C     . MET   B 1 96  ? 23.407  21.266  18.866 1.00 71.44  ? 222 MET   B C     1 
ATOM   3353 O O     . MET   B 1 96  ? 22.232  21.130  18.503 1.00 70.15  ? 222 MET   B O     1 
ATOM   3354 C CB    . MET   B 1 96  ? 23.866  22.643  16.815 1.00 64.47  ? 222 MET   B CB    1 
ATOM   3355 C CG    . MET   B 1 96  ? 24.820  23.001  15.694 1.00 63.60  ? 222 MET   B CG    1 
ATOM   3356 S SD    . MET   B 1 96  ? 26.350  23.792  16.249 1.00 69.13  ? 222 MET   B SD    1 
ATOM   3357 C CE    . MET   B 1 96  ? 25.696  25.242  17.082 1.00 63.45  ? 222 MET   B CE    1 
ATOM   3358 N N     . LEU   B 1 97  ? 23.830  21.021  20.113 1.00 87.29  ? 223 LEU   B N     1 
ATOM   3359 C CA    . LEU   B 1 97  ? 23.006  20.408  21.152 1.00 92.50  ? 223 LEU   B CA    1 
ATOM   3360 C C     . LEU   B 1 97  ? 21.575  20.931  21.134 1.00 94.60  ? 223 LEU   B C     1 
ATOM   3361 O O     . LEU   B 1 97  ? 21.294  22.032  21.620 1.00 90.78  ? 223 LEU   B O     1 
ATOM   3362 C CB    . LEU   B 1 97  ? 23.629  20.632  22.534 1.00 91.08  ? 223 LEU   B CB    1 
ATOM   3363 N N     . GLY   B 1 98  ? 20.679  20.146  20.540 1.00 78.46  ? 224 GLY   B N     1 
ATOM   3364 C CA    . GLY   B 1 98  ? 19.274  20.477  20.466 1.00 71.71  ? 224 GLY   B CA    1 
ATOM   3365 C C     . GLY   B 1 98  ? 18.419  19.237  20.319 1.00 67.16  ? 224 GLY   B C     1 
ATOM   3366 O O     . GLY   B 1 98  ? 18.755  18.328  19.554 1.00 62.38  ? 224 GLY   B O     1 
ATOM   3367 N N     . GLU   B 1 99  ? 17.316  19.175  21.058 1.00 64.17  ? 225 GLU   B N     1 
ATOM   3368 C CA    . GLU   B 1 99  ? 16.456  18.006  20.981 1.00 58.37  ? 225 GLU   B CA    1 
ATOM   3369 C C     . GLU   B 1 99  ? 15.099  18.343  21.564 1.00 61.27  ? 225 GLU   B C     1 
ATOM   3370 O O     . GLU   B 1 99  ? 14.957  19.274  22.358 1.00 61.31  ? 225 GLU   B O     1 
ATOM   3371 C CB    . GLU   B 1 99  ? 17.057  16.807  21.720 1.00 58.42  ? 225 GLU   B CB    1 
ATOM   3372 C CG    . GLU   B 1 99  ? 17.516  17.084  23.134 1.00 57.00  ? 225 GLU   B CG    1 
ATOM   3373 C CD    . GLU   B 1 99  ? 18.188  15.860  23.741 1.00 60.59  ? 225 GLU   B CD    1 
ATOM   3374 O OE1   . GLU   B 1 99  ? 17.463  14.983  24.255 1.00 57.89  ? 225 GLU   B OE1   1 
ATOM   3375 O OE2   . GLU   B 1 99  ? 19.434  15.755  23.665 1.00 60.10  ? 225 GLU   B OE2   1 
ATOM   3376 N N     . ALA   B 1 100 ? 14.108  17.554  21.152 1.00 62.20  ? 226 ALA   B N     1 
ATOM   3377 C CA    . ALA   B 1 100 ? 12.757  17.622  21.690 1.00 61.08  ? 226 ALA   B CA    1 
ATOM   3378 C C     . ALA   B 1 100 ? 12.182  19.027  21.516 1.00 66.99  ? 226 ALA   B C     1 
ATOM   3379 O O     . ALA   B 1 100 ? 11.895  19.737  22.481 1.00 71.76  ? 226 ALA   B O     1 
ATOM   3380 C CB    . ALA   B 1 100 ? 12.742  17.185  23.158 1.00 64.18  ? 226 ALA   B CB    1 
ATOM   3381 N N     . ALA   B 1 101 ? 12.041  19.420  20.251 1.00 65.07  ? 227 ALA   B N     1 
ATOM   3382 C CA    . ALA   B 1 101 ? 11.506  20.731  19.916 1.00 68.83  ? 227 ALA   B CA    1 
ATOM   3383 C C     . ALA   B 1 101 ? 10.109  20.875  20.491 1.00 75.36  ? 227 ALA   B C     1 
ATOM   3384 O O     . ALA   B 1 101 ? 9.199   20.129  20.114 1.00 79.32  ? 227 ALA   B O     1 
ATOM   3385 C CB    . ALA   B 1 101 ? 11.480  20.941  18.404 1.00 68.66  ? 227 ALA   B CB    1 
ATOM   3386 N N     . THR   B 1 102 ? 9.932   21.820  21.409 1.00 80.00  ? 228 THR   B N     1 
ATOM   3387 C CA    . THR   B 1 102 ? 8.646   22.034  22.047 1.00 75.83  ? 228 THR   B CA    1 
ATOM   3388 C C     . THR   B 1 102 ? 7.825   23.114  21.359 1.00 80.33  ? 228 THR   B C     1 
ATOM   3389 O O     . THR   B 1 102 ? 6.743   23.446  21.845 1.00 84.64  ? 228 THR   B O     1 
ATOM   3390 C CB    . THR   B 1 102 ? 8.839   22.395  23.525 1.00 80.47  ? 228 THR   B CB    1 
ATOM   3391 N N     . THR   B 1 103 ? 8.307   23.659  20.245 1.00 79.80  ? 229 THR   B N     1 
ATOM   3392 C CA    . THR   B 1 103 ? 7.588   24.685  19.504 1.00 84.02  ? 229 THR   B CA    1 
ATOM   3393 C C     . THR   B 1 103 ? 7.995   24.615  18.040 1.00 84.35  ? 229 THR   B C     1 
ATOM   3394 O O     . THR   B 1 103 ? 9.071   24.116  17.697 1.00 80.07  ? 229 THR   B O     1 
ATOM   3395 C CB    . THR   B 1 103 ? 7.864   26.088  20.060 1.00 87.64  ? 229 THR   B CB    1 
ATOM   3396 N N     . ALA   B 1 104 ? 7.112   25.120  17.174 1.00 85.41  ? 230 ALA   B N     1 
ATOM   3397 C CA    . ALA   B 1 104 ? 7.437   25.202  15.754 1.00 85.19  ? 230 ALA   B CA    1 
ATOM   3398 C C     . ALA   B 1 104 ? 8.570   26.191  15.510 1.00 86.60  ? 230 ALA   B C     1 
ATOM   3399 O O     . ALA   B 1 104 ? 9.425   25.967  14.645 1.00 82.23  ? 230 ALA   B O     1 
ATOM   3400 C CB    . ALA   B 1 104 ? 6.197   25.597  14.951 1.00 88.73  ? 230 ALA   B CB    1 
ATOM   3401 N N     . ALA   B 1 105 ? 8.583   27.299  16.257 1.00 88.81  ? 231 ALA   B N     1 
ATOM   3402 C CA    . ALA   B 1 105 ? 9.693   28.238  16.160 1.00 88.66  ? 231 ALA   B CA    1 
ATOM   3403 C C     . ALA   B 1 105 ? 10.988  27.615  16.654 1.00 83.39  ? 231 ALA   B C     1 
ATOM   3404 O O     . ALA   B 1 105 ? 12.066  27.939  16.143 1.00 80.40  ? 231 ALA   B O     1 
ATOM   3405 C CB    . ALA   B 1 105 ? 9.377   29.512  16.947 1.00 92.39  ? 231 ALA   B CB    1 
ATOM   3406 N N     . ASP   B 1 106 ? 10.898  26.716  17.640 1.00 85.70  ? 232 ASP   B N     1 
ATOM   3407 C CA    . ASP   B 1 106 ? 12.087  26.044  18.149 1.00 82.03  ? 232 ASP   B CA    1 
ATOM   3408 C C     . ASP   B 1 106 ? 12.713  25.151  17.085 1.00 78.68  ? 232 ASP   B C     1 
ATOM   3409 O O     . ASP   B 1 106 ? 13.941  25.119  16.935 1.00 74.13  ? 232 ASP   B O     1 
ATOM   3410 C CB    . ASP   B 1 106 ? 11.731  25.235  19.396 1.00 81.17  ? 232 ASP   B CB    1 
ATOM   3411 N N     . ALA   B 1 107 ? 11.881  24.431  16.324 1.00 79.92  ? 233 ALA   B N     1 
ATOM   3412 C CA    . ALA   B 1 107 ? 12.390  23.563  15.265 1.00 73.81  ? 233 ALA   B CA    1 
ATOM   3413 C C     . ALA   B 1 107 ? 13.124  24.365  14.198 1.00 75.94  ? 233 ALA   B C     1 
ATOM   3414 O O     . ALA   B 1 107 ? 14.250  24.027  13.818 1.00 72.36  ? 233 ALA   B O     1 
ATOM   3415 C CB    . ALA   B 1 107 ? 11.243  22.767  14.641 1.00 72.08  ? 233 ALA   B CB    1 
ATOM   3416 N N     . GLU   B 1 108 ? 12.495  25.436  13.697 1.00 75.99  ? 234 GLU   B N     1 
ATOM   3417 C CA    . GLU   B 1 108 ? 13.133  26.253  12.668 1.00 76.12  ? 234 GLU   B CA    1 
ATOM   3418 C C     . GLU   B 1 108 ? 14.421  26.881  13.187 1.00 78.16  ? 234 GLU   B C     1 
ATOM   3419 O O     . GLU   B 1 108 ? 15.401  27.016  12.442 1.00 77.05  ? 234 GLU   B O     1 
ATOM   3420 C CB    . GLU   B 1 108 ? 12.167  27.330  12.172 1.00 82.81  ? 234 GLU   B CB    1 
ATOM   3421 N N     . ARG   B 1 109 ? 14.445  27.251  14.470 1.00 77.41  ? 235 ARG   B N     1 
ATOM   3422 C CA    . ARG   B 1 109 ? 15.661  27.800  15.064 1.00 76.75  ? 235 ARG   B CA    1 
ATOM   3423 C C     . ARG   B 1 109 ? 16.781  26.771  15.065 1.00 77.59  ? 235 ARG   B C     1 
ATOM   3424 O O     . ARG   B 1 109 ? 17.907  27.062  14.642 1.00 77.55  ? 235 ARG   B O     1 
ATOM   3425 C CB    . ARG   B 1 109 ? 15.378  28.285  16.484 1.00 79.24  ? 235 ARG   B CB    1 
ATOM   3426 N N     . TYR   B 1 110 ? 16.493  25.562  15.562 1.00 73.99  ? 236 TYR   B N     1 
ATOM   3427 C CA    . TYR   B 1 110 ? 17.461  24.476  15.473 1.00 72.18  ? 236 TYR   B CA    1 
ATOM   3428 C C     . TYR   B 1 110 ? 17.908  24.264  14.038 1.00 67.84  ? 236 TYR   B C     1 
ATOM   3429 O O     . TYR   B 1 110 ? 19.101  24.087  13.771 1.00 69.36  ? 236 TYR   B O     1 
ATOM   3430 C CB    . TYR   B 1 110 ? 16.867  23.183  16.041 1.00 69.95  ? 236 TYR   B CB    1 
ATOM   3431 C CG    . TYR   B 1 110 ? 16.809  23.146  17.549 1.00 72.54  ? 236 TYR   B CG    1 
ATOM   3432 C CD1   . TYR   B 1 110 ? 17.919  23.474  18.313 1.00 71.35  ? 236 TYR   B CD1   1 
ATOM   3433 C CD2   . TYR   B 1 110 ? 15.636  22.798  18.210 1.00 72.11  ? 236 TYR   B CD2   1 
ATOM   3434 C CE1   . TYR   B 1 110 ? 17.869  23.447  19.687 1.00 73.80  ? 236 TYR   B CE1   1 
ATOM   3435 C CE2   . TYR   B 1 110 ? 15.574  22.767  19.584 1.00 71.64  ? 236 TYR   B CE2   1 
ATOM   3436 C CZ    . TYR   B 1 110 ? 16.694  23.091  20.321 1.00 77.74  ? 236 TYR   B CZ    1 
ATOM   3437 O OH    . TYR   B 1 110 ? 16.631  23.063  21.700 1.00 78.77  ? 236 TYR   B OH    1 
ATOM   3438 N N     . TYR   B 1 111 ? 16.963  24.293  13.097 1.00 67.70  ? 237 TYR   B N     1 
ATOM   3439 C CA    . TYR   B 1 111 ? 17.312  24.075  11.700 1.00 70.35  ? 237 TYR   B CA    1 
ATOM   3440 C C     . TYR   B 1 111 ? 18.338  25.099  11.230 1.00 70.39  ? 237 TYR   B C     1 
ATOM   3441 O O     . TYR   B 1 111 ? 19.346  24.742  10.604 1.00 67.47  ? 237 TYR   B O     1 
ATOM   3442 C CB    . TYR   B 1 111 ? 16.052  24.117  10.835 1.00 71.55  ? 237 TYR   B CB    1 
ATOM   3443 C CG    . TYR   B 1 111 ? 16.333  24.124  9.355  1.00 70.77  ? 237 TYR   B CG    1 
ATOM   3444 C CD1   . TYR   B 1 111 ? 16.691  22.959  8.697  1.00 65.99  ? 237 TYR   B CD1   1 
ATOM   3445 C CD2   . TYR   B 1 111 ? 16.229  25.298  8.610  1.00 76.33  ? 237 TYR   B CD2   1 
ATOM   3446 C CE1   . TYR   B 1 111 ? 16.956  22.956  7.348  1.00 65.19  ? 237 TYR   B CE1   1 
ATOM   3447 C CE2   . TYR   B 1 111 ? 16.484  25.306  7.248  1.00 74.89  ? 237 TYR   B CE2   1 
ATOM   3448 C CZ    . TYR   B 1 111 ? 16.853  24.127  6.627  1.00 70.24  ? 237 TYR   B CZ    1 
ATOM   3449 O OH    . TYR   B 1 111 ? 17.113  24.109  5.281  1.00 74.03  ? 237 TYR   B OH    1 
ATOM   3450 N N     . ARG   B 1 112 ? 18.115  26.375  11.553 1.00 69.68  ? 238 ARG   B N     1 
ATOM   3451 C CA    . ARG   B 1 112 ? 19.045  27.419  11.136 1.00 68.87  ? 238 ARG   B CA    1 
ATOM   3452 C C     . ARG   B 1 112 ? 20.399  27.254  11.816 1.00 69.89  ? 238 ARG   B C     1 
ATOM   3453 O O     . ARG   B 1 112 ? 21.446  27.483  11.196 1.00 68.86  ? 238 ARG   B O     1 
ATOM   3454 C CB    . ARG   B 1 112 ? 18.452  28.797  11.435 1.00 72.61  ? 238 ARG   B CB    1 
ATOM   3455 N N     . ASP   B 1 113 ? 20.402  26.845  13.088 1.00 68.88  ? 239 ASP   B N     1 
ATOM   3456 C CA    . ASP   B 1 113 ? 21.665  26.580  13.769 1.00 64.01  ? 239 ASP   B CA    1 
ATOM   3457 C C     . ASP   B 1 113 ? 22.392  25.396  13.138 1.00 65.12  ? 239 ASP   B C     1 
ATOM   3458 O O     . ASP   B 1 113 ? 23.621  25.419  13.007 1.00 65.52  ? 239 ASP   B O     1 
ATOM   3459 C CB    . ASP   B 1 113 ? 21.424  26.340  15.258 1.00 65.29  ? 239 ASP   B CB    1 
ATOM   3460 N N     . TYR   B 1 114 ? 21.650  24.352  12.749 1.00 64.07  ? 240 TYR   B N     1 
ATOM   3461 C CA    . TYR   B 1 114 ? 22.244  23.228  12.027 1.00 60.87  ? 240 TYR   B CA    1 
ATOM   3462 C C     . TYR   B 1 114 ? 22.750  23.665  10.655 1.00 59.34  ? 240 TYR   B C     1 
ATOM   3463 O O     . TYR   B 1 114 ? 23.850  23.288  10.229 1.00 55.63  ? 240 TYR   B O     1 
ATOM   3464 C CB    . TYR   B 1 114 ? 21.212  22.107  11.880 1.00 60.01  ? 240 TYR   B CB    1 
ATOM   3465 C CG    . TYR   B 1 114 ? 21.083  21.182  13.088 1.00 54.25  ? 240 TYR   B CG    1 
ATOM   3466 C CD1   . TYR   B 1 114 ? 22.212  20.733  13.768 1.00 58.34  ? 240 TYR   B CD1   1 
ATOM   3467 C CD2   . TYR   B 1 114 ? 19.841  20.734  13.523 1.00 58.07  ? 240 TYR   B CD2   1 
ATOM   3468 C CE1   . TYR   B 1 114 ? 22.107  19.870  14.865 1.00 56.12  ? 240 TYR   B CE1   1 
ATOM   3469 C CE2   . TYR   B 1 114 ? 19.720  19.877  14.623 1.00 55.25  ? 240 TYR   B CE2   1 
ATOM   3470 C CZ    . TYR   B 1 114 ? 20.860  19.449  15.286 1.00 56.57  ? 240 TYR   B CZ    1 
ATOM   3471 O OH    . TYR   B 1 114 ? 20.780  18.601  16.377 1.00 59.47  ? 240 TYR   B OH    1 
ATOM   3472 N N     . GLU   B 1 115 ? 21.951  24.455  9.947  1.00 61.41  ? 241 GLU   B N     1 
ATOM   3473 C CA    . GLU   B 1 115 ? 22.367  24.967  8.649  1.00 63.57  ? 241 GLU   B CA    1 
ATOM   3474 C C     . GLU   B 1 115 ? 23.653  25.779  8.763  1.00 61.60  ? 241 GLU   B C     1 
ATOM   3475 O O     . GLU   B 1 115 ? 24.635  25.509  8.063  1.00 56.55  ? 241 GLU   B O     1 
ATOM   3476 C CB    . GLU   B 1 115 ? 21.238  25.801  8.065  1.00 63.46  ? 241 GLU   B CB    1 
ATOM   3477 C CG    . GLU   B 1 115 ? 21.640  26.669  6.929  1.00 64.81  ? 241 GLU   B CG    1 
ATOM   3478 C CD    . GLU   B 1 115 ? 20.641  27.767  6.721  1.00 68.68  ? 241 GLU   B CD    1 
ATOM   3479 O OE1   . GLU   B 1 115 ? 20.448  28.561  7.667  1.00 72.13  ? 241 GLU   B OE1   1 
ATOM   3480 O OE2   . GLU   B 1 115 ? 20.027  27.812  5.636  1.00 68.93  ? 241 GLU   B OE2   1 
ATOM   3481 N N     . SER   B 1 116 ? 23.669  26.771  9.658  1.00 63.03  ? 242 SER   B N     1 
ATOM   3482 C CA    . SER   B 1 116 ? 24.868  27.585  9.829  1.00 63.02  ? 242 SER   B CA    1 
ATOM   3483 C C     . SER   B 1 116 ? 26.042  26.753  10.324 1.00 59.54  ? 242 SER   B C     1 
ATOM   3484 O O     . SER   B 1 116 ? 27.191  27.029  9.960  1.00 58.37  ? 242 SER   B O     1 
ATOM   3485 C CB    . SER   B 1 116 ? 24.591  28.744  10.789 1.00 66.04  ? 242 SER   B CB    1 
ATOM   3486 N N     . ALA   B 1 117 ? 25.777  25.724  11.139 1.00 57.70  ? 243 ALA   B N     1 
ATOM   3487 C CA    . ALA   B 1 117 ? 26.858  24.868  11.607 1.00 55.95  ? 243 ALA   B CA    1 
ATOM   3488 C C     . ALA   B 1 117 ? 27.473  24.075  10.465 1.00 51.92  ? 243 ALA   B C     1 
ATOM   3489 O O     . ALA   B 1 117 ? 28.695  23.914  10.406 1.00 52.91  ? 243 ALA   B O     1 
ATOM   3490 C CB    . ALA   B 1 117 ? 26.359  23.916  12.694 1.00 58.07  ? 243 ALA   B CB    1 
ATOM   3491 N N     . ILE   B 1 118 ? 26.650  23.567  9.549  1.00 54.94  ? 244 ILE   B N     1 
ATOM   3492 C CA    . ILE   B 1 118 ? 27.195  22.833  8.410  1.00 51.09  ? 244 ILE   B CA    1 
ATOM   3493 C C     . ILE   B 1 118 ? 28.097  23.735  7.570  1.00 51.62  ? 244 ILE   B C     1 
ATOM   3494 O O     . ILE   B 1 118 ? 29.176  23.316  7.138  1.00 50.05  ? 244 ILE   B O     1 
ATOM   3495 C CB    . ILE   B 1 118 ? 26.060  22.211  7.580  1.00 49.65  ? 244 ILE   B CB    1 
ATOM   3496 C CG1   . ILE   B 1 118 ? 25.421  21.055  8.350  1.00 48.57  ? 244 ILE   B CG1   1 
ATOM   3497 C CG2   . ILE   B 1 118 ? 26.582  21.733  6.225  1.00 48.31  ? 244 ILE   B CG2   1 
ATOM   3498 C CD1   . ILE   B 1 118 ? 24.161  20.500  7.719  1.00 50.95  ? 244 ILE   B CD1   1 
ATOM   3499 N N     . HIS   B 1 119 ? 27.687  24.990  7.349  1.00 52.62  ? 245 HIS   B N     1 
ATOM   3500 C CA    . HIS   B 1 119 ? 28.552  25.936  6.644  1.00 52.96  ? 245 HIS   B CA    1 
ATOM   3501 C C     . HIS   B 1 119 ? 29.886  26.109  7.367  1.00 55.03  ? 245 HIS   B C     1 
ATOM   3502 O O     . HIS   B 1 119 ? 30.947  26.163  6.730  1.00 52.82  ? 245 HIS   B O     1 
ATOM   3503 C CB    . HIS   B 1 119 ? 27.857  27.294  6.492  1.00 56.43  ? 245 HIS   B CB    1 
ATOM   3504 C CG    . HIS   B 1 119 ? 26.832  27.340  5.398  1.00 58.67  ? 245 HIS   B CG    1 
ATOM   3505 N ND1   . HIS   B 1 119 ? 27.128  27.031  4.088  1.00 60.19  ? 245 HIS   B ND1   1 
ATOM   3506 C CD2   . HIS   B 1 119 ? 25.519  27.676  5.417  1.00 59.63  ? 245 HIS   B CD2   1 
ATOM   3507 C CE1   . HIS   B 1 119 ? 26.041  27.165  3.349  1.00 59.67  ? 245 HIS   B CE1   1 
ATOM   3508 N NE2   . HIS   B 1 119 ? 25.050  27.547  4.133  1.00 61.23  ? 245 HIS   B NE2   1 
ATOM   3509 N N     . ALA   B 1 120 ? 29.849  26.219  8.698  1.00 52.16  ? 246 ALA   B N     1 
ATOM   3510 C CA    . ALA   B 1 120 ? 31.078  26.427  9.457  1.00 54.02  ? 246 ALA   B CA    1 
ATOM   3511 C C     . ALA   B 1 120 ? 31.918  25.160  9.497  1.00 48.68  ? 246 ALA   B C     1 
ATOM   3512 O O     . ALA   B 1 120 ? 33.145  25.219  9.365  1.00 48.85  ? 246 ALA   B O     1 
ATOM   3513 C CB    . ALA   B 1 120 ? 30.756  26.898  10.876 1.00 55.03  ? 246 ALA   B CB    1 
ATOM   3514 N N     . ILE   B 1 121 ? 31.275  24.004  9.666  1.00 47.03  ? 247 ILE   B N     1 
ATOM   3515 C CA    . ILE   B 1 121 ? 32.005  22.738  9.645  1.00 48.61  ? 247 ILE   B CA    1 
ATOM   3516 C C     . ILE   B 1 121 ? 32.535  22.450  8.246  1.00 47.17  ? 247 ILE   B C     1 
ATOM   3517 O O     . ILE   B 1 121 ? 33.653  21.942  8.079  1.00 44.63  ? 247 ILE   B O     1 
ATOM   3518 C CB    . ILE   B 1 121 ? 31.109  21.596  10.151 1.00 46.19  ? 247 ILE   B CB    1 
ATOM   3519 C CG1   . ILE   B 1 121 ? 30.631  21.876  11.573 1.00 45.90  ? 247 ILE   B CG1   1 
ATOM   3520 C CG2   . ILE   B 1 121 ? 31.856  20.272  10.099 1.00 43.06  ? 247 ILE   B CG2   1 
ATOM   3521 C CD1   . ILE   B 1 121 ? 29.446  21.038  11.976 1.00 43.59  ? 247 ILE   B CD1   1 
ATOM   3522 N N     . GLY   B 1 122 ? 31.747  22.775  7.220  1.00 48.19  ? 248 GLY   B N     1 
ATOM   3523 C CA    . GLY   B 1 122 ? 32.189  22.536  5.856  1.00 45.86  ? 248 GLY   B CA    1 
ATOM   3524 C C     . GLY   B 1 122 ? 33.389  23.378  5.479  1.00 47.37  ? 248 GLY   B C     1 
ATOM   3525 O O     . GLY   B 1 122 ? 34.308  22.900  4.812  1.00 48.89  ? 248 GLY   B O     1 
ATOM   3526 N N     . LYS   B 1 123 ? 33.397  24.645  5.899  1.00 49.11  ? 249 LYS   B N     1 
ATOM   3527 C CA    . LYS   B 1 123 ? 34.549  25.497  5.638  1.00 51.91  ? 249 LYS   B CA    1 
ATOM   3528 C C     . LYS   B 1 123 ? 35.782  24.997  6.378  1.00 50.16  ? 249 LYS   B C     1 
ATOM   3529 O O     . LYS   B 1 123 ? 36.872  24.933  5.801  1.00 51.55  ? 249 LYS   B O     1 
ATOM   3530 C CB    . LYS   B 1 123 ? 34.232  26.947  6.014  1.00 54.56  ? 249 LYS   B CB    1 
ATOM   3531 N N     . ALA   B 1 124 ? 35.631  24.617  7.649  1.00 52.63  ? 250 ALA   B N     1 
ATOM   3532 C CA    . ALA   B 1 124 ? 36.768  24.098  8.398  1.00 52.03  ? 250 ALA   B CA    1 
ATOM   3533 C C     . ALA   B 1 124 ? 37.292  22.806  7.784  1.00 51.30  ? 250 ALA   B C     1 
ATOM   3534 O O     . ALA   B 1 124 ? 38.507  22.598  7.703  1.00 55.01  ? 250 ALA   B O     1 
ATOM   3535 C CB    . ALA   B 1 124 ? 36.377  23.879  9.859  1.00 51.30  ? 250 ALA   B CB    1 
ATOM   3536 N N     . SER   B 1 125 ? 36.389  21.926  7.347  1.00 47.47  ? 251 SER   B N     1 
ATOM   3537 C CA    . SER   B 1 125 ? 36.809  20.676  6.721  1.00 47.83  ? 251 SER   B CA    1 
ATOM   3538 C C     . SER   B 1 125 ? 37.744  20.926  5.546  1.00 50.44  ? 251 SER   B C     1 
ATOM   3539 O O     . SER   B 1 125 ? 38.712  20.184  5.346  1.00 47.91  ? 251 SER   B O     1 
ATOM   3540 C CB    . SER   B 1 125 ? 35.584  19.885  6.270  1.00 48.37  ? 251 SER   B CB    1 
ATOM   3541 O OG    . SER   B 1 125 ? 35.967  18.780  5.476  1.00 45.93  ? 251 SER   B OG    1 
ATOM   3542 N N     . ALA   B 1 126 ? 37.471  21.976  4.766  1.00 45.83  ? 252 ALA   B N     1 
ATOM   3543 C CA    . ALA   B 1 126 ? 38.343  22.412  3.675  1.00 52.71  ? 252 ALA   B CA    1 
ATOM   3544 C C     . ALA   B 1 126 ? 38.651  21.273  2.710  1.00 53.73  ? 252 ALA   B C     1 
ATOM   3545 O O     . ALA   B 1 126 ? 39.770  21.134  2.217  1.00 58.20  ? 252 ALA   B O     1 
ATOM   3546 C CB    . ALA   B 1 126 ? 39.633  23.028  4.218  1.00 55.86  ? 252 ALA   B CB    1 
ATOM   3547 N N     . GLY   B 1 127 ? 37.652  20.439  2.444  1.00 52.65  ? 253 GLY   B N     1 
ATOM   3548 C CA    . GLY   B 1 127 ? 37.807  19.387  1.462  1.00 50.88  ? 253 GLY   B CA    1 
ATOM   3549 C C     . GLY   B 1 127 ? 38.475  18.123  1.954  1.00 48.92  ? 253 GLY   B C     1 
ATOM   3550 O O     . GLY   B 1 127 ? 38.899  17.307  1.124  1.00 52.54  ? 253 GLY   B O     1 
ATOM   3551 N N     . ARG   B 1 128 ? 38.580  17.921  3.269  1.00 48.99  ? 254 ARG   B N     1 
ATOM   3552 C CA    . ARG   B 1 128 ? 39.169  16.682  3.759  1.00 46.99  ? 254 ARG   B CA    1 
ATOM   3553 C C     . ARG   B 1 128 ? 38.270  15.470  3.554  1.00 46.15  ? 254 ARG   B C     1 
ATOM   3554 O O     . ARG   B 1 128 ? 38.729  14.344  3.759  1.00 48.88  ? 254 ARG   B O     1 
ATOM   3555 C CB    . ARG   B 1 128 ? 39.516  16.804  5.238  1.00 47.47  ? 254 ARG   B CB    1 
ATOM   3556 C CG    . ARG   B 1 128 ? 40.784  17.598  5.523  1.00 50.52  ? 254 ARG   B CG    1 
ATOM   3557 C CD    . ARG   B 1 128 ? 40.984  17.758  7.026  1.00 49.46  ? 254 ARG   B CD    1 
ATOM   3558 N NE    . ARG   B 1 128 ? 40.205  18.864  7.568  1.00 50.42  ? 254 ARG   B NE    1 
ATOM   3559 C CZ    . ARG   B 1 128 ? 40.071  19.120  8.862  1.00 53.26  ? 254 ARG   B CZ    1 
ATOM   3560 N NH1   . ARG   B 1 128 ? 40.603  18.328  9.782  1.00 50.23  ? 254 ARG   B NH1   1 
ATOM   3561 N NH2   . ARG   B 1 128 ? 39.377  20.190  9.245  1.00 53.02  ? 254 ARG   B NH2   1 
ATOM   3562 N N     . GLY   B 1 129 ? 37.016  15.659  3.171  1.00 45.07  ? 255 GLY   B N     1 
ATOM   3563 C CA    . GLY   B 1 129 ? 36.148  14.529  2.928  1.00 43.58  ? 255 GLY   B CA    1 
ATOM   3564 C C     . GLY   B 1 129 ? 35.451  14.034  4.180  1.00 42.82  ? 255 GLY   B C     1 
ATOM   3565 O O     . GLY   B 1 129 ? 35.664  14.497  5.307  1.00 41.83  ? 255 GLY   B O     1 
ATOM   3566 N N     . ILE   B 1 130 ? 34.593  13.039  3.967  1.00 41.75  ? 256 ILE   B N     1 
ATOM   3567 C CA    . ILE   B 1 130 ? 33.717  12.593  5.039  1.00 38.60  ? 256 ILE   B CA    1 
ATOM   3568 C C     . ILE   B 1 130 ? 34.414  11.690  6.046  1.00 36.83  ? 256 ILE   B C     1 
ATOM   3569 O O     . ILE   B 1 130 ? 33.866  11.466  7.130  1.00 40.05  ? 256 ILE   B O     1 
ATOM   3570 C CB    . ILE   B 1 130 ? 32.494  11.873  4.453  1.00 41.08  ? 256 ILE   B CB    1 
ATOM   3571 C CG1   . ILE   B 1 130 ? 32.927  10.545  3.835  1.00 42.37  ? 256 ILE   B CG1   1 
ATOM   3572 C CG2   . ILE   B 1 130 ? 31.803  12.759  3.419  1.00 38.60  ? 256 ILE   B CG2   1 
ATOM   3573 C CD1   . ILE   B 1 130 ? 31.822  9.813   3.115  1.00 43.83  ? 256 ILE   B CD1   1 
ATOM   3574 N N     . TYR   B 1 131 ? 35.603  11.174  5.734  1.00 38.79  ? 257 TYR   B N     1 
ATOM   3575 C CA    . TYR   B 1 131 ? 36.295  10.264  6.646  1.00 39.53  ? 257 TYR   B CA    1 
ATOM   3576 C C     . TYR   B 1 131 ? 37.365  10.965  7.476  1.00 35.75  ? 257 TYR   B C     1 
ATOM   3577 O O     . TYR   B 1 131 ? 37.449  10.757  8.687  1.00 41.05  ? 257 TYR   B O     1 
ATOM   3578 C CB    . TYR   B 1 131 ? 36.921  9.104   5.852  1.00 39.74  ? 257 TYR   B CB    1 
ATOM   3579 C CG    . TYR   B 1 131 ? 35.915  8.305   5.059  1.00 39.02  ? 257 TYR   B CG    1 
ATOM   3580 C CD1   . TYR   B 1 131 ? 34.795  7.766   5.675  1.00 36.33  ? 257 TYR   B CD1   1 
ATOM   3581 C CD2   . TYR   B 1 131 ? 36.079  8.107   3.687  1.00 39.47  ? 257 TYR   B CD2   1 
ATOM   3582 C CE1   . TYR   B 1 131 ? 33.874  7.048   4.960  1.00 37.56  ? 257 TYR   B CE1   1 
ATOM   3583 C CE2   . TYR   B 1 131 ? 35.156  7.388   2.957  1.00 39.77  ? 257 TYR   B CE2   1 
ATOM   3584 C CZ    . TYR   B 1 131 ? 34.058  6.855   3.602  1.00 38.35  ? 257 TYR   B CZ    1 
ATOM   3585 O OH    . TYR   B 1 131 ? 33.127  6.139   2.894  1.00 40.46  ? 257 TYR   B OH    1 
ATOM   3586 N N     . GLU   B 1 132 ? 38.191  11.789  6.844  1.00 40.13  ? 258 GLU   B N     1 
ATOM   3587 C CA    . GLU   B 1 132 ? 39.272  12.461  7.551  1.00 42.69  ? 258 GLU   B CA    1 
ATOM   3588 C C     . GLU   B 1 132 ? 38.827  13.778  8.168  1.00 44.78  ? 258 GLU   B C     1 
ATOM   3589 O O     . GLU   B 1 132 ? 39.430  14.236  9.146  1.00 46.13  ? 258 GLU   B O     1 
ATOM   3590 C CB    . GLU   B 1 132 ? 40.445  12.710  6.599  1.00 40.48  ? 258 GLU   B CB    1 
ATOM   3591 N N     . GLY   B 1 133 ? 37.783  14.394  7.624  1.00 43.51  ? 259 GLY   B N     1 
ATOM   3592 C CA    . GLY   B 1 133 ? 37.380  15.710  8.046  1.00 41.79  ? 259 GLY   B CA    1 
ATOM   3593 C C     . GLY   B 1 133 ? 36.176  15.656  8.952  1.00 39.52  ? 259 GLY   B C     1 
ATOM   3594 O O     . GLY   B 1 133 ? 35.580  14.596  9.167  1.00 39.61  ? 259 GLY   B O     1 
ATOM   3595 N N     . PRO   B 1 134 ? 35.801  16.802  9.514  1.00 40.63  ? 260 PRO   B N     1 
ATOM   3596 C CA    . PRO   B 1 134 ? 34.704  16.820  10.481 1.00 38.75  ? 260 PRO   B CA    1 
ATOM   3597 C C     . PRO   B 1 134 ? 33.366  16.549  9.822  1.00 41.33  ? 260 PRO   B C     1 
ATOM   3598 O O     . PRO   B 1 134 ? 33.188  16.688  8.607  1.00 42.62  ? 260 PRO   B O     1 
ATOM   3599 C CB    . PRO   B 1 134 ? 34.759  18.237  11.062 1.00 42.74  ? 260 PRO   B CB    1 
ATOM   3600 C CG    . PRO   B 1 134 ? 35.499  19.032  10.071 1.00 40.14  ? 260 PRO   B CG    1 
ATOM   3601 C CD    . PRO   B 1 134 ? 36.465  18.110  9.410  1.00 42.74  ? 260 PRO   B CD    1 
ATOM   3602 N N     . GLY   B 1 135 ? 32.418  16.133  10.662 1.00 37.83  ? 261 GLY   B N     1 
ATOM   3603 C CA    . GLY   B 1 135 ? 31.048  15.939  10.246 1.00 41.59  ? 261 GLY   B CA    1 
ATOM   3604 C C     . GLY   B 1 135 ? 30.103  16.519  11.277 1.00 40.38  ? 261 GLY   B C     1 
ATOM   3605 O O     . GLY   B 1 135 ? 30.523  17.056  12.302 1.00 35.95  ? 261 GLY   B O     1 
ATOM   3606 N N     . ILE   B 1 136 ? 28.815  16.415  10.973 1.00 39.76  ? 262 ILE   B N     1 
ATOM   3607 C CA    . ILE   B 1 136 ? 27.786  16.893  11.878 1.00 38.51  ? 262 ILE   B CA    1 
ATOM   3608 C C     . ILE   B 1 136 ? 26.863  15.730  12.197 1.00 39.02  ? 262 ILE   B C     1 
ATOM   3609 O O     . ILE   B 1 136 ? 26.736  14.774  11.420 1.00 36.10  ? 262 ILE   B O     1 
ATOM   3610 C CB    . ILE   B 1 136 ? 27.006  18.087  11.283 1.00 38.92  ? 262 ILE   B CB    1 
ATOM   3611 C CG1   . ILE   B 1 136 ? 26.359  18.916  12.392 1.00 40.33  ? 262 ILE   B CG1   1 
ATOM   3612 C CG2   . ILE   B 1 136 ? 25.980  17.610  10.255 1.00 42.15  ? 262 ILE   B CG2   1 
ATOM   3613 C CD1   . ILE   B 1 136 ? 25.491  20.056  11.893 1.00 45.78  ? 262 ILE   B CD1   1 
ATOM   3614 N N     . SER   B 1 137 ? 26.263  15.792  13.381 1.00 35.85  ? 263 SER   B N     1 
ATOM   3615 C CA    . SER   B 1 137 ? 25.237  14.859  13.806 1.00 34.67  ? 263 SER   B CA    1 
ATOM   3616 C C     . SER   B 1 137 ? 24.040  15.668  14.253 1.00 40.95  ? 263 SER   B C     1 
ATOM   3617 O O     . SER   B 1 137 ? 24.199  16.732  14.852 1.00 40.37  ? 263 SER   B O     1 
ATOM   3618 C CB    . SER   B 1 137 ? 25.717  13.964  14.959 1.00 36.21  ? 263 SER   B CB    1 
ATOM   3619 O OG    . SER   B 1 137 ? 26.846  13.247  14.540 1.00 36.99  ? 263 SER   B OG    1 
ATOM   3620 N N     . ILE   B 1 138 ? 22.849  15.171  13.951 1.00 39.00  ? 264 ILE   B N     1 
ATOM   3621 C CA    . ILE   B 1 138 ? 21.625  15.880  14.279 1.00 44.42  ? 264 ILE   B CA    1 
ATOM   3622 C C     . ILE   B 1 138 ? 20.652  14.904  14.919 1.00 40.40  ? 264 ILE   B C     1 
ATOM   3623 O O     . ILE   B 1 138 ? 20.674  13.696  14.661 1.00 37.85  ? 264 ILE   B O     1 
ATOM   3624 C CB    . ILE   B 1 138 ? 20.994  16.551  13.041 1.00 43.94  ? 264 ILE   B CB    1 
ATOM   3625 C CG1   . ILE   B 1 138 ? 20.457  15.494  12.081 1.00 41.96  ? 264 ILE   B CG1   1 
ATOM   3626 C CG2   . ILE   B 1 138 ? 22.015  17.442  12.316 1.00 45.26  ? 264 ILE   B CG2   1 
ATOM   3627 C CD1   . ILE   B 1 138 ? 19.692  16.084  10.901 1.00 40.44  ? 264 ILE   B CD1   1 
ATOM   3628 N N     . LYS   B 1 139 ? 19.818  15.430  15.792 1.00 39.97  ? 265 LYS   B N     1 
ATOM   3629 C CA    . LYS   B 1 139 ? 18.726  14.660  16.355 1.00 42.32  ? 265 LYS   B CA    1 
ATOM   3630 C C     . LYS   B 1 139 ? 17.450  15.147  15.687 1.00 45.95  ? 265 LYS   B C     1 
ATOM   3631 O O     . LYS   B 1 139 ? 17.166  16.351  15.686 1.00 49.72  ? 265 LYS   B O     1 
ATOM   3632 C CB    . LYS   B 1 139 ? 18.676  14.813  17.877 1.00 47.29  ? 265 LYS   B CB    1 
ATOM   3633 C CG    . LYS   B 1 139 ? 19.970  14.357  18.582 1.00 46.11  ? 265 LYS   B CG    1 
ATOM   3634 C CD    . LYS   B 1 139 ? 19.883  14.468  20.107 1.00 45.89  ? 265 LYS   B CD    1 
ATOM   3635 C CE    . LYS   B 1 139 ? 21.250  14.185  20.748 1.00 45.21  ? 265 LYS   B CE    1 
ATOM   3636 N NZ    . LYS   B 1 139 ? 21.859  12.895  20.281 1.00 43.73  ? 265 LYS   B NZ    1 
ATOM   3637 N N     . LEU   B 1 140 ? 16.699  14.218  15.096 1.00 45.82  ? 266 LEU   B N     1 
ATOM   3638 C CA    . LEU   B 1 140 ? 15.482  14.601  14.387 1.00 46.00  ? 266 LEU   B CA    1 
ATOM   3639 C C     . LEU   B 1 140 ? 14.450  15.259  15.296 1.00 53.44  ? 266 LEU   B C     1 
ATOM   3640 O O     . LEU   B 1 140 ? 13.583  15.986  14.801 1.00 53.25  ? 266 LEU   B O     1 
ATOM   3641 C CB    . LEU   B 1 140 ? 14.874  13.381  13.704 1.00 49.34  ? 266 LEU   B CB    1 
ATOM   3642 C CG    . LEU   B 1 140 ? 15.747  12.746  12.625 1.00 47.38  ? 266 LEU   B CG    1 
ATOM   3643 C CD1   . LEU   B 1 140 ? 15.103  11.471  12.122 1.00 48.99  ? 266 LEU   B CD1   1 
ATOM   3644 C CD2   . LEU   B 1 140 ? 15.997  13.726  11.485 1.00 48.03  ? 266 LEU   B CD2   1 
ATOM   3645 N N     . SER   B 1 141 ? 14.516  15.030  16.610 1.00 53.28  ? 267 SER   B N     1 
ATOM   3646 C CA    . SER   B 1 141 ? 13.566  15.662  17.516 1.00 52.58  ? 267 SER   B CA    1 
ATOM   3647 C C     . SER   B 1 141 ? 13.816  17.155  17.672 1.00 55.44  ? 267 SER   B C     1 
ATOM   3648 O O     . SER   B 1 141 ? 12.958  17.857  18.214 1.00 59.82  ? 267 SER   B O     1 
ATOM   3649 C CB    . SER   B 1 141 ? 13.614  14.987  18.889 1.00 53.99  ? 267 SER   B CB    1 
ATOM   3650 O OG    . SER   B 1 141 ? 14.852  15.249  19.521 1.00 52.43  ? 267 SER   B OG    1 
ATOM   3651 N N     . ALA   B 1 142 ? 14.972  17.649  17.229 1.00 57.51  ? 268 ALA   B N     1 
ATOM   3652 C CA    . ALA   B 1 142 ? 15.236  19.082  17.226 1.00 60.99  ? 268 ALA   B CA    1 
ATOM   3653 C C     . ALA   B 1 142 ? 14.575  19.789  16.054 1.00 59.66  ? 268 ALA   B C     1 
ATOM   3654 O O     . ALA   B 1 142 ? 14.335  21.001  16.123 1.00 62.69  ? 268 ALA   B O     1 
ATOM   3655 C CB    . ALA   B 1 142 ? 16.744  19.337  17.185 1.00 58.01  ? 268 ALA   B CB    1 
ATOM   3656 N N     . LEU   B 1 143 ? 14.273  19.062  14.986 1.00 57.30  ? 269 LEU   B N     1 
ATOM   3657 C CA    . LEU   B 1 143 ? 13.857  19.669  13.735 1.00 59.64  ? 269 LEU   B CA    1 
ATOM   3658 C C     . LEU   B 1 143 ? 12.358  19.609  13.506 1.00 63.18  ? 269 LEU   B C     1 
ATOM   3659 O O     . LEU   B 1 143 ? 11.876  20.169  12.518 1.00 62.36  ? 269 LEU   B O     1 
ATOM   3660 C CB    . LEU   B 1 143 ? 14.585  18.999  12.572 1.00 56.25  ? 269 LEU   B CB    1 
ATOM   3661 C CG    . LEU   B 1 143 ? 16.093  19.212  12.567 1.00 57.75  ? 269 LEU   B CG    1 
ATOM   3662 C CD1   . LEU   B 1 143 ? 16.746  18.406  11.450 1.00 53.96  ? 269 LEU   B CD1   1 
ATOM   3663 C CD2   . LEU   B 1 143 ? 16.396  20.684  12.413 1.00 60.32  ? 269 LEU   B CD2   1 
ATOM   3664 N N     . HIS   B 1 144 ? 11.603  18.954  14.387 1.00 63.17  ? 270 HIS   B N     1 
ATOM   3665 C CA    . HIS   B 1 144 ? 10.153  18.963  14.271 1.00 67.51  ? 270 HIS   B CA    1 
ATOM   3666 C C     . HIS   B 1 144 ? 9.532   19.222  15.636 1.00 70.12  ? 270 HIS   B C     1 
ATOM   3667 O O     . HIS   B 1 144 ? 9.931   18.588  16.630 1.00 68.38  ? 270 HIS   B O     1 
ATOM   3668 C CB    . HIS   B 1 144 ? 9.617   17.651  13.687 1.00 67.12  ? 270 HIS   B CB    1 
ATOM   3669 C CG    . HIS   B 1 144 ? 8.190   17.747  13.254 1.00 71.10  ? 270 HIS   B CG    1 
ATOM   3670 N ND1   . HIS   B 1 144 ? 7.136   17.597  14.130 1.00 75.70  ? 270 HIS   B ND1   1 
ATOM   3671 C CD2   . HIS   B 1 144 ? 7.641   18.028  12.048 1.00 74.74  ? 270 HIS   B CD2   1 
ATOM   3672 C CE1   . HIS   B 1 144 ? 5.998   17.768  13.479 1.00 76.90  ? 270 HIS   B CE1   1 
ATOM   3673 N NE2   . HIS   B 1 144 ? 6.277   18.026  12.213 1.00 75.50  ? 270 HIS   B NE2   1 
ATOM   3674 N N     . PRO   B 1 145 ? 8.564   20.138  15.735 1.00 71.63  ? 271 PRO   B N     1 
ATOM   3675 C CA    . PRO   B 1 145 ? 7.875   20.340  17.012 1.00 74.37  ? 271 PRO   B CA    1 
ATOM   3676 C C     . PRO   B 1 145 ? 7.032   19.124  17.357 1.00 75.06  ? 271 PRO   B C     1 
ATOM   3677 O O     . PRO   B 1 145 ? 6.390   18.529  16.489 1.00 77.63  ? 271 PRO   B O     1 
ATOM   3678 C CB    . PRO   B 1 145 ? 7.004   21.573  16.752 1.00 77.12  ? 271 PRO   B CB    1 
ATOM   3679 C CG    . PRO   B 1 145 ? 6.725   21.518  15.280 1.00 76.72  ? 271 PRO   B CG    1 
ATOM   3680 C CD    . PRO   B 1 145 ? 7.994   20.974  14.660 1.00 71.85  ? 271 PRO   B CD    1 
ATOM   3681 N N     . ARG   B 1 146 ? 7.047   18.757  18.637 1.00 75.30  ? 272 ARG   B N     1 
ATOM   3682 C CA    . ARG   B 1 146 ? 6.396   17.536  19.113 1.00 82.04  ? 272 ARG   B CA    1 
ATOM   3683 C C     . ARG   B 1 146 ? 6.730   16.353  18.202 1.00 80.57  ? 272 ARG   B C     1 
ATOM   3684 O O     . ARG   B 1 146 ? 5.849   15.671  17.673 1.00 80.78  ? 272 ARG   B O     1 
ATOM   3685 C CB    . ARG   B 1 146 ? 4.883   17.734  19.233 1.00 85.07  ? 272 ARG   B CB    1 
ATOM   3686 N N     . TYR   B 1 147 ? 8.033   16.137  17.996 1.00 77.46  ? 273 TYR   B N     1 
ATOM   3687 C CA    . TYR   B 1 147 ? 8.486   15.057  17.123 1.00 73.60  ? 273 TYR   B CA    1 
ATOM   3688 C C     . TYR   B 1 147 ? 7.984   13.706  17.613 1.00 76.19  ? 273 TYR   B C     1 
ATOM   3689 O O     . TYR   B 1 147 ? 7.557   12.866  16.813 1.00 74.93  ? 273 TYR   B O     1 
ATOM   3690 C CB    . TYR   B 1 147 ? 10.013  15.074  17.039 1.00 65.54  ? 273 TYR   B CB    1 
ATOM   3691 C CG    . TYR   B 1 147 ? 10.647  13.899  16.330 1.00 61.73  ? 273 TYR   B CG    1 
ATOM   3692 C CD1   . TYR   B 1 147 ? 10.532  13.742  14.954 1.00 63.84  ? 273 TYR   B CD1   1 
ATOM   3693 C CD2   . TYR   B 1 147 ? 11.400  12.962  17.035 1.00 59.03  ? 273 TYR   B CD2   1 
ATOM   3694 C CE1   . TYR   B 1 147 ? 11.144  12.673  14.299 1.00 57.88  ? 273 TYR   B CE1   1 
ATOM   3695 C CE2   . TYR   B 1 147 ? 12.013  11.898  16.390 1.00 55.67  ? 273 TYR   B CE2   1 
ATOM   3696 C CZ    . TYR   B 1 147 ? 11.873  11.751  15.027 1.00 56.27  ? 273 TYR   B CZ    1 
ATOM   3697 O OH    . TYR   B 1 147 ? 12.482  10.692  14.379 1.00 52.58  ? 273 TYR   B OH    1 
ATOM   3698 N N     . SER   B 1 148 ? 8.002   13.490  18.925 1.00 80.88  ? 274 SER   B N     1 
ATOM   3699 C CA    . SER   B 1 148 ? 7.569   12.229  19.512 1.00 81.64  ? 274 SER   B CA    1 
ATOM   3700 C C     . SER   B 1 148 ? 6.056   12.108  19.634 1.00 89.04  ? 274 SER   B C     1 
ATOM   3701 O O     . SER   B 1 148 ? 5.577   11.055  20.066 1.00 90.23  ? 274 SER   B O     1 
ATOM   3702 C CB    . SER   B 1 148 ? 8.204   12.051  20.892 1.00 81.52  ? 274 SER   B CB    1 
ATOM   3703 N N     . ARG   B 1 149 ? 5.297   13.142  19.265 1.00 94.63  ? 275 ARG   B N     1 
ATOM   3704 C CA    . ARG   B 1 149 ? 3.853   13.160  19.469 1.00 98.23  ? 275 ARG   B CA    1 
ATOM   3705 C C     . ARG   B 1 149 ? 3.050   13.269  18.182 1.00 102.47 ? 275 ARG   B C     1 
ATOM   3706 O O     . ARG   B 1 149 ? 2.015   12.610  18.056 1.00 102.22 ? 275 ARG   B O     1 
ATOM   3707 C CB    . ARG   B 1 149 ? 3.468   14.318  20.406 1.00 97.65  ? 275 ARG   B CB    1 
ATOM   3708 N N     . ALA   B 1 150 ? 3.482   14.091  17.226 1.00 98.18  ? 276 ALA   B N     1 
ATOM   3709 C CA    . ALA   B 1 150 ? 2.755   14.232  15.973 1.00 97.65  ? 276 ALA   B CA    1 
ATOM   3710 C C     . ALA   B 1 150 ? 2.932   12.986  15.104 1.00 101.83 ? 276 ALA   B C     1 
ATOM   3711 O O     . ALA   B 1 150 ? 3.851   12.183  15.295 1.00 100.60 ? 276 ALA   B O     1 
ATOM   3712 C CB    . ALA   B 1 150 ? 3.220   15.477  15.215 1.00 91.16  ? 276 ALA   B CB    1 
ATOM   3713 N N     . GLN   B 1 151 ? 2.032   12.840  14.130 1.00 108.70 ? 277 GLN   B N     1 
ATOM   3714 C CA    . GLN   B 1 151 ? 2.012   11.664  13.270 1.00 111.90 ? 277 GLN   B CA    1 
ATOM   3715 C C     . GLN   B 1 151 ? 3.217   11.652  12.325 1.00 111.28 ? 277 GLN   B C     1 
ATOM   3716 O O     . GLN   B 1 151 ? 3.957   12.631  12.196 1.00 111.15 ? 277 GLN   B O     1 
ATOM   3717 C CB    . GLN   B 1 151 ? 0.712   11.615  12.467 1.00 108.48 ? 277 GLN   B CB    1 
ATOM   3718 N N     . ALA   B 1 152 ? 3.406   10.513  11.655 1.00 95.81  ? 278 ALA   B N     1 
ATOM   3719 C CA    . ALA   B 1 152 ? 4.473   10.359  10.672 1.00 91.31  ? 278 ALA   B CA    1 
ATOM   3720 C C     . ALA   B 1 152 ? 4.115   10.945  9.314  1.00 89.54  ? 278 ALA   B C     1 
ATOM   3721 O O     . ALA   B 1 152 ? 5.000   11.082  8.461  1.00 87.57  ? 278 ALA   B O     1 
ATOM   3722 C CB    . ALA   B 1 152 ? 4.836   8.881   10.512 1.00 85.74  ? 278 ALA   B CB    1 
ATOM   3723 N N     . ALA   B 1 153 ? 2.849   11.286  9.089  1.00 86.68  ? 279 ALA   B N     1 
ATOM   3724 C CA    . ALA   B 1 153 ? 2.460   11.981  7.871  1.00 90.17  ? 279 ALA   B CA    1 
ATOM   3725 C C     . ALA   B 1 153 ? 3.108   13.359  7.845  1.00 90.94  ? 279 ALA   B C     1 
ATOM   3726 O O     . ALA   B 1 153 ? 3.945   13.645  6.983  1.00 88.83  ? 279 ALA   B O     1 
ATOM   3727 C CB    . ALA   B 1 153 ? 0.936   12.096  7.780  1.00 80.25  ? 279 ALA   B CB    1 
ATOM   3728 N N     . ARG   B 1 154 ? 2.734   14.210  8.806  1.00 94.03  ? 280 ARG   B N     1 
ATOM   3729 C CA    . ARG   B 1 154 ? 3.276   15.562  8.876  1.00 93.93  ? 280 ARG   B CA    1 
ATOM   3730 C C     . ARG   B 1 154 ? 4.732   15.577  9.314  1.00 90.50  ? 280 ARG   B C     1 
ATOM   3731 O O     . ARG   B 1 154 ? 5.428   16.568  9.070  1.00 89.76  ? 280 ARG   B O     1 
ATOM   3732 C CB    . ARG   B 1 154 ? 2.434   16.420  9.824  1.00 95.96  ? 280 ARG   B CB    1 
ATOM   3733 N N     . VAL   B 1 155 ? 5.205   14.512  9.960  1.00 95.86  ? 281 VAL   B N     1 
ATOM   3734 C CA    . VAL   B 1 155 ? 6.629   14.405  10.265 1.00 98.11  ? 281 VAL   B CA    1 
ATOM   3735 C C     . VAL   B 1 155 ? 7.428   14.253  8.978  1.00 99.04  ? 281 VAL   B C     1 
ATOM   3736 O O     . VAL   B 1 155 ? 8.297   15.071  8.665  1.00 97.98  ? 281 VAL   B O     1 
ATOM   3737 C CB    . VAL   B 1 155 ? 6.892   13.237  11.233 1.00 96.95  ? 281 VAL   B CB    1 
ATOM   3738 N N     . MET   B 1 156 ? 7.125   13.211  8.201  1.00 93.51  ? 282 MET   B N     1 
ATOM   3739 C CA    . MET   B 1 156 ? 7.819   13.001  6.935  1.00 89.43  ? 282 MET   B CA    1 
ATOM   3740 C C     . MET   B 1 156 ? 7.687   14.216  6.022  1.00 90.04  ? 282 MET   B C     1 
ATOM   3741 O O     . MET   B 1 156 ? 8.673   14.665  5.430  1.00 90.18  ? 282 MET   B O     1 
ATOM   3742 C CB    . MET   B 1 156 ? 7.269   11.754  6.245  1.00 91.34  ? 282 MET   B CB    1 
ATOM   3743 C CG    . MET   B 1 156 ? 8.240   11.065  5.305  1.00 91.33  ? 282 MET   B CG    1 
ATOM   3744 S SD    . MET   B 1 156 ? 9.527   10.168  6.200  1.00 90.17  ? 282 MET   B SD    1 
ATOM   3745 C CE    . MET   B 1 156 ? 10.071  9.042   4.920  1.00 75.29  ? 282 MET   B CE    1 
ATOM   3746 N N     . GLY   B 1 157 ? 6.482   14.781  5.919  1.00 86.05  ? 283 GLY   B N     1 
ATOM   3747 C CA    . GLY   B 1 157 ? 6.235   15.859  4.975  1.00 89.27  ? 283 GLY   B CA    1 
ATOM   3748 C C     . GLY   B 1 157 ? 6.905   17.175  5.316  1.00 85.19  ? 283 GLY   B C     1 
ATOM   3749 O O     . GLY   B 1 157 ? 7.080   18.014  4.427  1.00 83.85  ? 283 GLY   B O     1 
ATOM   3750 N N     . GLU   B 1 158 ? 7.266   17.387  6.580  1.00 81.78  ? 284 GLU   B N     1 
ATOM   3751 C CA    . GLU   B 1 158 ? 7.961   18.602  6.990  1.00 80.51  ? 284 GLU   B CA    1 
ATOM   3752 C C     . GLU   B 1 158 ? 9.393   18.361  7.442  1.00 78.20  ? 284 GLU   B C     1 
ATOM   3753 O O     . GLU   B 1 158 ? 10.234  19.255  7.313  1.00 76.36  ? 284 GLU   B O     1 
ATOM   3754 C CB    . GLU   B 1 158 ? 7.197   19.300  8.125  1.00 83.51  ? 284 GLU   B CB    1 
ATOM   3755 N N     . LEU   B 1 159 ? 9.694   17.177  7.965  1.00 76.00  ? 285 LEU   B N     1 
ATOM   3756 C CA    . LEU   B 1 159 ? 11.065  16.885  8.361  1.00 74.63  ? 285 LEU   B CA    1 
ATOM   3757 C C     . LEU   B 1 159 ? 11.923  16.529  7.155  1.00 67.67  ? 285 LEU   B C     1 
ATOM   3758 O O     . LEU   B 1 159 ? 13.036  17.045  7.009  1.00 66.25  ? 285 LEU   B O     1 
ATOM   3759 C CB    . LEU   B 1 159 ? 11.080  15.760  9.395  1.00 70.91  ? 285 LEU   B CB    1 
ATOM   3760 C CG    . LEU   B 1 159 ? 12.366  15.434  10.136 1.00 62.71  ? 285 LEU   B CG    1 
ATOM   3761 C CD1   . LEU   B 1 159 ? 13.067  16.697  10.547 1.00 59.99  ? 285 LEU   B CD1   1 
ATOM   3762 C CD2   . LEU   B 1 159 ? 12.002  14.621  11.353 1.00 58.67  ? 285 LEU   B CD2   1 
ATOM   3763 N N     . LEU   B 1 160 ? 11.424  15.651  6.281  1.00 66.45  ? 286 LEU   B N     1 
ATOM   3764 C CA    . LEU   B 1 160 ? 12.205  15.230  5.117  1.00 67.09  ? 286 LEU   B CA    1 
ATOM   3765 C C     . LEU   B 1 160 ? 12.723  16.399  4.291  1.00 68.37  ? 286 LEU   B C     1 
ATOM   3766 O O     . LEU   B 1 160 ? 13.918  16.394  3.951  1.00 65.10  ? 286 LEU   B O     1 
ATOM   3767 C CB    . LEU   B 1 160 ? 11.388  14.265  4.246  1.00 70.00  ? 286 LEU   B CB    1 
ATOM   3768 N N     . PRO   B 1 161 ? 11.921  17.418  3.946  1.00 64.86  ? 287 PRO   B N     1 
ATOM   3769 C CA    . PRO   B 1 161 ? 12.504  18.597  3.283  1.00 66.79  ? 287 PRO   B CA    1 
ATOM   3770 C C     . PRO   B 1 161 ? 13.578  19.293  4.102  1.00 65.63  ? 287 PRO   B C     1 
ATOM   3771 O O     . PRO   B 1 161 ? 14.526  19.839  3.521  1.00 62.07  ? 287 PRO   B O     1 
ATOM   3772 C CB    . PRO   B 1 161 ? 11.288  19.506  3.060  1.00 70.43  ? 287 PRO   B CB    1 
ATOM   3773 C CG    . PRO   B 1 161 ? 10.138  18.565  2.980  1.00 68.84  ? 287 PRO   B CG    1 
ATOM   3774 C CD    . PRO   B 1 161 ? 10.448  17.498  3.983  1.00 68.86  ? 287 PRO   B CD    1 
ATOM   3775 N N     . ARG   B 1 162 ? 13.467  19.285  5.433  1.00 65.67  ? 288 ARG   B N     1 
ATOM   3776 C CA    . ARG   B 1 162 ? 14.436  19.995  6.261  1.00 58.43  ? 288 ARG   B CA    1 
ATOM   3777 C C     . ARG   B 1 162 ? 15.752  19.235  6.347  1.00 60.04  ? 288 ARG   B C     1 
ATOM   3778 O O     . ARG   B 1 162 ? 16.829  19.839  6.280  1.00 56.51  ? 288 ARG   B O     1 
ATOM   3779 C CB    . ARG   B 1 162 ? 13.863  20.229  7.659  1.00 67.02  ? 288 ARG   B CB    1 
ATOM   3780 N N     . VAL   B 1 163 ? 15.680  17.911  6.490  1.00 55.91  ? 289 VAL   B N     1 
ATOM   3781 C CA    . VAL   B 1 163 ? 16.898  17.111  6.541  1.00 56.29  ? 289 VAL   B CA    1 
ATOM   3782 C C     . VAL   B 1 163 ? 17.509  16.987  5.152  1.00 55.15  ? 289 VAL   B C     1 
ATOM   3783 O O     . VAL   B 1 163 ? 18.734  16.905  5.002  1.00 47.92  ? 289 VAL   B O     1 
ATOM   3784 C CB    . VAL   B 1 163 ? 16.601  15.735  7.166  1.00 54.06  ? 289 VAL   B CB    1 
ATOM   3785 C CG1   . VAL   B 1 163 ? 17.856  14.875  7.205  1.00 48.19  ? 289 VAL   B CG1   1 
ATOM   3786 C CG2   . VAL   B 1 163 ? 16.024  15.904  8.578  1.00 52.81  ? 289 VAL   B CG2   1 
ATOM   3787 N N     . LYS   B 1 164 ? 16.688  16.978  4.110  1.00 52.77  ? 290 LYS   B N     1 
ATOM   3788 C CA    . LYS   B 1 164 ? 17.264  16.928  2.772  1.00 50.22  ? 290 LYS   B CA    1 
ATOM   3789 C C     . LYS   B 1 164 ? 18.080  18.179  2.478  1.00 51.44  ? 290 LYS   B C     1 
ATOM   3790 O O     . LYS   B 1 164 ? 19.179  18.091  1.913  1.00 52.21  ? 290 LYS   B O     1 
ATOM   3791 C CB    . LYS   B 1 164 ? 16.174  16.743  1.726  1.00 58.19  ? 290 LYS   B CB    1 
ATOM   3792 C CG    . LYS   B 1 164 ? 16.738  16.639  0.335  1.00 57.50  ? 290 LYS   B CG    1 
ATOM   3793 C CD    . LYS   B 1 164 ? 15.654  16.490  -0.676 1.00 57.92  ? 290 LYS   B CD    1 
ATOM   3794 C CE    . LYS   B 1 164 ? 16.172  16.898  -2.042 1.00 61.34  ? 290 LYS   B CE    1 
ATOM   3795 N NZ    . LYS   B 1 164 ? 15.202  16.511  -3.083 1.00 63.43  ? 290 LYS   B NZ    1 
ATOM   3796 N N     . ALA   B 1 165 ? 17.561  19.353  2.850  1.00 53.19  ? 291 ALA   B N     1 
ATOM   3797 C CA    . ALA   B 1 165 ? 18.323  20.586  2.686  1.00 55.30  ? 291 ALA   B CA    1 
ATOM   3798 C C     . ALA   B 1 165 ? 19.644  20.510  3.439  1.00 54.02  ? 291 ALA   B C     1 
ATOM   3799 O O     . ALA   B 1 165 ? 20.701  20.869  2.904  1.00 52.96  ? 291 ALA   B O     1 
ATOM   3800 C CB    . ALA   B 1 165 ? 17.504  21.782  3.166  1.00 58.33  ? 291 ALA   B CB    1 
ATOM   3801 N N     . LEU   B 1 166 ? 19.598  20.045  4.692  1.00 52.92  ? 292 LEU   B N     1 
ATOM   3802 C CA    . LEU   B 1 166 ? 20.820  19.850  5.462  1.00 51.51  ? 292 LEU   B CA    1 
ATOM   3803 C C     . LEU   B 1 166 ? 21.742  18.858  4.769  1.00 50.14  ? 292 LEU   B C     1 
ATOM   3804 O O     . LEU   B 1 166 ? 22.952  19.086  4.664  1.00 47.07  ? 292 LEU   B O     1 
ATOM   3805 C CB    . LEU   B 1 166 ? 20.484  19.373  6.884  1.00 49.23  ? 292 LEU   B CB    1 
ATOM   3806 C CG    . LEU   B 1 166 ? 19.731  20.394  7.743  1.00 54.95  ? 292 LEU   B CG    1 
ATOM   3807 C CD1   . LEU   B 1 166 ? 19.498  19.898  9.166  1.00 51.19  ? 292 LEU   B CD1   1 
ATOM   3808 C CD2   . LEU   B 1 166 ? 20.475  21.717  7.759  1.00 56.66  ? 292 LEU   B CD2   1 
ATOM   3809 N N     . ALA   B 1 167 ? 21.181  17.744  4.292  1.00 46.93  ? 293 ALA   B N     1 
ATOM   3810 C CA    . ALA   B 1 167 ? 21.980  16.747  3.589  1.00 51.47  ? 293 ALA   B CA    1 
ATOM   3811 C C     . ALA   B 1 167 ? 22.585  17.321  2.317  1.00 49.30  ? 293 ALA   B C     1 
ATOM   3812 O O     . ALA   B 1 167 ? 23.716  16.983  1.948  1.00 48.19  ? 293 ALA   B O     1 
ATOM   3813 C CB    . ALA   B 1 167 ? 21.128  15.520  3.270  1.00 52.76  ? 293 ALA   B CB    1 
ATOM   3814 N N     . LEU   B 1 168 ? 21.859  18.214  1.642  1.00 49.39  ? 294 LEU   B N     1 
ATOM   3815 C CA    . LEU   B 1 168 ? 22.430  18.845  0.459  1.00 52.04  ? 294 LEU   B CA    1 
ATOM   3816 C C     . LEU   B 1 168 ? 23.621  19.717  0.830  1.00 51.98  ? 294 LEU   B C     1 
ATOM   3817 O O     . LEU   B 1 168 ? 24.672  19.649  0.180  1.00 53.46  ? 294 LEU   B O     1 
ATOM   3818 C CB    . LEU   B 1 168 ? 21.366  19.650  -0.276 1.00 53.08  ? 294 LEU   B CB    1 
ATOM   3819 C CG    . LEU   B 1 168 ? 20.525  18.831  -1.256 1.00 55.05  ? 294 LEU   B CG    1 
ATOM   3820 C CD1   . LEU   B 1 168 ? 19.301  19.618  -1.714 1.00 60.13  ? 294 LEU   B CD1   1 
ATOM   3821 C CD2   . LEU   B 1 168 ? 21.374  18.422  -2.462 1.00 58.79  ? 294 LEU   B CD2   1 
ATOM   3822 N N     . LEU   B 1 169 ? 23.484  20.527  1.887  1.00 51.88  ? 295 LEU   B N     1 
ATOM   3823 C CA    . LEU   B 1 169 ? 24.599  21.364  2.321  1.00 48.61  ? 295 LEU   B CA    1 
ATOM   3824 C C     . LEU   B 1 169 ? 25.807  20.505  2.672  1.00 49.05  ? 295 LEU   B C     1 
ATOM   3825 O O     . LEU   B 1 169 ? 26.936  20.806  2.265  1.00 49.46  ? 295 LEU   B O     1 
ATOM   3826 C CB    . LEU   B 1 169 ? 24.191  22.238  3.512  1.00 50.14  ? 295 LEU   B CB    1 
ATOM   3827 C CG    . LEU   B 1 169 ? 23.120  23.322  3.354  1.00 56.84  ? 295 LEU   B CG    1 
ATOM   3828 C CD1   . LEU   B 1 169 ? 22.843  23.960  4.712  1.00 57.97  ? 295 LEU   B CD1   1 
ATOM   3829 C CD2   . LEU   B 1 169 ? 23.505  24.394  2.312  1.00 55.85  ? 295 LEU   B CD2   1 
ATOM   3830 N N     . ALA   B 1 170 ? 25.585  19.418  3.423  1.00 48.34  ? 296 ALA   B N     1 
ATOM   3831 C CA    . ALA   B 1 170 ? 26.688  18.524  3.765  1.00 45.10  ? 296 ALA   B CA    1 
ATOM   3832 C C     . ALA   B 1 170 ? 27.303  17.911  2.515  1.00 44.24  ? 296 ALA   B C     1 
ATOM   3833 O O     . ALA   B 1 170 ? 28.529  17.814  2.404  1.00 42.30  ? 296 ALA   B O     1 
ATOM   3834 C CB    . ALA   B 1 170 ? 26.224  17.426  4.735  1.00 42.49  ? 296 ALA   B CB    1 
ATOM   3835 N N     . LYS   B 1 171 ? 26.468  17.504  1.554  1.00 45.43  ? 297 LYS   B N     1 
ATOM   3836 C CA    . LYS   B 1 171 ? 26.997  17.040  0.275  1.00 45.97  ? 297 LYS   B CA    1 
ATOM   3837 C C     . LYS   B 1 171 ? 27.824  18.123  -0.404 1.00 49.27  ? 297 LYS   B C     1 
ATOM   3838 O O     . LYS   B 1 171 ? 28.884  17.836  -0.973 1.00 48.74  ? 297 LYS   B O     1 
ATOM   3839 C CB    . LYS   B 1 171 ? 25.863  16.596  -0.650 1.00 47.55  ? 297 LYS   B CB    1 
ATOM   3840 C CG    . LYS   B 1 171 ? 26.321  16.456  -2.095 1.00 46.26  ? 297 LYS   B CG    1 
ATOM   3841 C CD    . LYS   B 1 171 ? 25.252  15.900  -3.016 1.00 48.17  ? 297 LYS   B CD    1 
ATOM   3842 C CE    . LYS   B 1 171 ? 25.738  15.981  -4.466 1.00 54.76  ? 297 LYS   B CE    1 
ATOM   3843 N NZ    . LYS   B 1 171 ? 24.773  15.490  -5.493 1.00 56.71  ? 297 LYS   B NZ    1 
ATOM   3844 N N     . ASN   B 1 172 ? 27.349  19.374  -0.367 1.00 47.06  ? 298 ASN   B N     1 
ATOM   3845 C CA    . ASN   B 1 172 ? 28.077  20.465  -1.005 1.00 48.59  ? 298 ASN   B CA    1 
ATOM   3846 C C     . ASN   B 1 172 ? 29.471  20.636  -0.414 1.00 47.59  ? 298 ASN   B C     1 
ATOM   3847 O O     . ASN   B 1 172 ? 30.408  21.021  -1.122 1.00 49.75  ? 298 ASN   B O     1 
ATOM   3848 C CB    . ASN   B 1 172 ? 27.294  21.774  -0.869 1.00 52.26  ? 298 ASN   B CB    1 
ATOM   3849 C CG    . ASN   B 1 172 ? 25.965  21.767  -1.634 1.00 55.38  ? 298 ASN   B CG    1 
ATOM   3850 O OD1   . ASN   B 1 172 ? 25.718  20.920  -2.510 1.00 57.45  ? 298 ASN   B OD1   1 
ATOM   3851 N ND2   . ASN   B 1 172 ? 25.122  22.753  -1.338 1.00 58.21  ? 298 ASN   B ND2   1 
ATOM   3852 N N     . TYR   B 1 173 ? 29.626  20.393  0.880  1.00 45.58  ? 299 TYR   B N     1 
ATOM   3853 C CA    . TYR   B 1 173 ? 30.915  20.510  1.536  1.00 46.20  ? 299 TYR   B CA    1 
ATOM   3854 C C     . TYR   B 1 173 ? 31.628  19.171  1.668  1.00 45.23  ? 299 TYR   B C     1 
ATOM   3855 O O     . TYR   B 1 173 ? 32.762  19.141  2.148  1.00 48.01  ? 299 TYR   B O     1 
ATOM   3856 C CB    . TYR   B 1 173 ? 30.737  21.132  2.932  1.00 49.41  ? 299 TYR   B CB    1 
ATOM   3857 C CG    . TYR   B 1 173 ? 30.384  22.604  2.905  1.00 48.11  ? 299 TYR   B CG    1 
ATOM   3858 C CD1   . TYR   B 1 173 ? 31.345  23.559  2.606  1.00 49.35  ? 299 TYR   B CD1   1 
ATOM   3859 C CD2   . TYR   B 1 173 ? 29.093  23.037  3.191  1.00 49.59  ? 299 TYR   B CD2   1 
ATOM   3860 C CE1   . TYR   B 1 173 ? 31.032  24.911  2.580  1.00 52.30  ? 299 TYR   B CE1   1 
ATOM   3861 C CE2   . TYR   B 1 173 ? 28.768  24.389  3.173  1.00 51.30  ? 299 TYR   B CE2   1 
ATOM   3862 C CZ    . TYR   B 1 173 ? 29.741  25.315  2.861  1.00 53.27  ? 299 TYR   B CZ    1 
ATOM   3863 O OH    . TYR   B 1 173 ? 29.434  26.645  2.849  1.00 56.52  ? 299 TYR   B OH    1 
ATOM   3864 N N     . ASP   B 1 174 ? 30.984  18.079  1.249  1.00 45.73  ? 300 ASP   B N     1 
ATOM   3865 C CA    . ASP   B 1 174 ? 31.485  16.706  1.400  1.00 40.23  ? 300 ASP   B CA    1 
ATOM   3866 C C     . ASP   B 1 174 ? 31.855  16.390  2.845  1.00 42.95  ? 300 ASP   B C     1 
ATOM   3867 O O     . ASP   B 1 174 ? 32.954  15.924  3.141  1.00 45.40  ? 300 ASP   B O     1 
ATOM   3868 C CB    . ASP   B 1 174 ? 32.672  16.428  0.472  1.00 45.59  ? 300 ASP   B CB    1 
ATOM   3869 C CG    . ASP   B 1 174 ? 32.859  14.937  0.206  1.00 49.46  ? 300 ASP   B CG    1 
ATOM   3870 O OD1   . ASP   B 1 174 ? 31.859  14.186  0.311  1.00 46.60  ? 300 ASP   B OD1   1 
ATOM   3871 O OD2   . ASP   B 1 174 ? 33.993  14.523  -0.105 1.00 45.78  ? 300 ASP   B OD2   1 
ATOM   3872 N N     . ILE   B 1 175 ? 30.911  16.620  3.750  1.00 41.66  ? 301 ILE   B N     1 
ATOM   3873 C CA    . ILE   B 1 175 ? 31.094  16.282  5.152  1.00 39.51  ? 301 ILE   B CA    1 
ATOM   3874 C C     . ILE   B 1 175 ? 30.040  15.257  5.538  1.00 38.17  ? 301 ILE   B C     1 
ATOM   3875 O O     . ILE   B 1 175 ? 29.016  15.093  4.871  1.00 36.19  ? 301 ILE   B O     1 
ATOM   3876 C CB    . ILE   B 1 175 ? 31.013  17.518  6.076  1.00 41.12  ? 301 ILE   B CB    1 
ATOM   3877 C CG1   . ILE   B 1 175 ? 29.598  18.096  6.070  1.00 42.53  ? 301 ILE   B CG1   1 
ATOM   3878 C CG2   . ILE   B 1 175 ? 32.031  18.581  5.652  1.00 43.26  ? 301 ILE   B CG2   1 
ATOM   3879 C CD1   . ILE   B 1 175 ? 29.307  19.009  7.263  1.00 44.25  ? 301 ILE   B CD1   1 
ATOM   3880 N N     . GLY   B 1 176 ? 30.300  14.565  6.642  1.00 38.14  ? 302 GLY   B N     1 
ATOM   3881 C CA    . GLY   B 1 176 ? 29.327  13.630  7.152  1.00 35.18  ? 302 GLY   B CA    1 
ATOM   3882 C C     . GLY   B 1 176 ? 28.135  14.337  7.769  1.00 37.00  ? 302 GLY   B C     1 
ATOM   3883 O O     . GLY   B 1 176 ? 28.237  15.425  8.340  1.00 36.77  ? 302 GLY   B O     1 
ATOM   3884 N N     . LEU   B 1 177 ? 26.978  13.700  7.634  1.00 35.77  ? 303 LEU   B N     1 
ATOM   3885 C CA    . LEU   B 1 177 ? 25.757  14.144  8.289  1.00 35.56  ? 303 LEU   B CA    1 
ATOM   3886 C C     . LEU   B 1 177 ? 25.118  12.883  8.828  1.00 34.62  ? 303 LEU   B C     1 
ATOM   3887 O O     . LEU   B 1 177 ? 24.660  12.039  8.055  1.00 35.98  ? 303 LEU   B O     1 
ATOM   3888 C CB    . LEU   B 1 177 ? 24.815  14.880  7.341  1.00 38.74  ? 303 LEU   B CB    1 
ATOM   3889 C CG    . LEU   B 1 177 ? 23.688  15.638  8.048  1.00 45.22  ? 303 LEU   B CG    1 
ATOM   3890 C CD1   . LEU   B 1 177 ? 23.185  16.743  7.139  1.00 43.83  ? 303 LEU   B CD1   1 
ATOM   3891 C CD2   . LEU   B 1 177 ? 22.533  14.737  8.435  1.00 45.50  ? 303 LEU   B CD2   1 
ATOM   3892 N N     . ASN   B 1 178 ? 25.102  12.754  10.142 1.00 33.58  ? 304 ASN   B N     1 
ATOM   3893 C CA    . ASN   B 1 178 ? 24.616  11.561  10.799 1.00 31.46  ? 304 ASN   B CA    1 
ATOM   3894 C C     . ASN   B 1 178 ? 23.307  11.848  11.508 1.00 33.55  ? 304 ASN   B C     1 
ATOM   3895 O O     . ASN   B 1 178 ? 23.177  12.860  12.197 1.00 35.35  ? 304 ASN   B O     1 
ATOM   3896 C CB    . ASN   B 1 178 ? 25.622  11.064  11.829 1.00 34.94  ? 304 ASN   B CB    1 
ATOM   3897 C CG    . ASN   B 1 178 ? 25.030  10.026  12.723 1.00 33.31  ? 304 ASN   B CG    1 
ATOM   3898 O OD1   . ASN   B 1 178 ? 24.424  10.333  13.757 1.00 38.01  ? 304 ASN   B OD1   1 
ATOM   3899 N ND2   . ASN   B 1 178 ? 25.153  8.788   12.319 1.00 31.99  ? 304 ASN   B ND2   1 
ATOM   3900 N N     . ILE   B 1 179 ? 22.351  10.945  11.362 1.00 35.49  ? 305 ILE   B N     1 
ATOM   3901 C CA    . ILE   B 1 179 ? 21.083  11.053  12.070 1.00 31.29  ? 305 ILE   B CA    1 
ATOM   3902 C C     . ILE   B 1 179 ? 21.223  10.258  13.367 1.00 33.50  ? 305 ILE   B C     1 
ATOM   3903 O O     . ILE   B 1 179 ? 21.355  9.031   13.343 1.00 32.11  ? 305 ILE   B O     1 
ATOM   3904 C CB    . ILE   B 1 179 ? 19.926  10.532  11.221 1.00 36.09  ? 305 ILE   B CB    1 
ATOM   3905 C CG1   . ILE   B 1 179 ? 19.769  11.395  9.969  1.00 38.05  ? 305 ILE   B CG1   1 
ATOM   3906 C CG2   . ILE   B 1 179 ? 18.665  10.524  12.046 1.00 38.04  ? 305 ILE   B CG2   1 
ATOM   3907 C CD1   . ILE   B 1 179 ? 18.904  10.768  8.875  1.00 40.01  ? 305 ILE   B CD1   1 
ATOM   3908 N N     . ASP   B 1 180 ? 21.223  10.961  14.495 1.00 35.64  ? 306 ASP   B N     1 
ATOM   3909 C CA    . ASP   B 1 180 ? 21.283  10.303  15.794 1.00 34.09  ? 306 ASP   B CA    1 
ATOM   3910 C C     . ASP   B 1 180 ? 20.024  9.483   16.026 1.00 35.27  ? 306 ASP   B C     1 
ATOM   3911 O O     . ASP   B 1 180 ? 18.955  9.779   15.494 1.00 36.88  ? 306 ASP   B O     1 
ATOM   3912 C CB    . ASP   B 1 180 ? 21.433  11.338  16.911 1.00 35.21  ? 306 ASP   B CB    1 
ATOM   3913 C CG    . ASP   B 1 180 ? 22.792  12.019  16.897 1.00 36.35  ? 306 ASP   B CG    1 
ATOM   3914 O OD1   . ASP   B 1 180 ? 23.721  11.441  16.314 1.00 35.06  ? 306 ASP   B OD1   1 
ATOM   3915 O OD2   . ASP   B 1 180 ? 22.928  13.117  17.479 1.00 40.40  ? 306 ASP   B OD2   1 
ATOM   3916 N N     . ALA   B 1 181 ? 20.152  8.457   16.850 1.00 34.64  ? 307 ALA   B N     1 
ATOM   3917 C CA    . ALA   B 1 181 ? 19.027  7.613   17.225 1.00 35.40  ? 307 ALA   B CA    1 
ATOM   3918 C C     . ALA   B 1 181 ? 18.496  8.015   18.596 1.00 38.85  ? 307 ALA   B C     1 
ATOM   3919 O O     . ALA   B 1 181 ? 19.263  8.234   19.539 1.00 34.98  ? 307 ALA   B O     1 
ATOM   3920 C CB    . ALA   B 1 181 ? 19.443  6.138   17.220 1.00 29.98  ? 307 ALA   B CB    1 
ATOM   3921 N N     . GLU   B 1 182 ? 17.173  8.116   18.705 1.00 35.62  ? 308 GLU   B N     1 
ATOM   3922 C CA    . GLU   B 1 182 ? 16.568  8.562   19.951 1.00 39.84  ? 308 GLU   B CA    1 
ATOM   3923 C C     . GLU   B 1 182 ? 15.698  7.453   20.528 1.00 40.20  ? 308 GLU   B C     1 
ATOM   3924 O O     . GLU   B 1 182 ? 16.131  6.299   20.570 1.00 42.48  ? 308 GLU   B O     1 
ATOM   3925 C CB    . GLU   B 1 182 ? 15.813  9.871   19.703 1.00 43.45  ? 308 GLU   B CB    1 
ATOM   3926 C CG    . GLU   B 1 182 ? 16.772  10.911  19.120 1.00 40.05  ? 308 GLU   B CG    1 
ATOM   3927 C CD    . GLU   B 1 182 ? 16.162  12.289  18.960 1.00 43.55  ? 308 GLU   B CD    1 
ATOM   3928 O OE1   . GLU   B 1 182 ? 15.867  12.942  19.978 1.00 44.86  ? 308 GLU   B OE1   1 
ATOM   3929 O OE2   . GLU   B 1 182 ? 16.001  12.721  17.805 1.00 45.69  ? 308 GLU   B OE2   1 
ATOM   3930 N N     . GLU   B 1 183 ? 14.497  7.768   20.999 1.00 44.30  ? 309 GLU   B N     1 
ATOM   3931 C CA    . GLU   B 1 183 ? 13.701  6.734   21.646 1.00 43.28  ? 309 GLU   B CA    1 
ATOM   3932 C C     . GLU   B 1 183 ? 13.320  5.648   20.641 1.00 43.21  ? 309 GLU   B C     1 
ATOM   3933 O O     . GLU   B 1 183 ? 13.299  5.868   19.429 1.00 42.72  ? 309 GLU   B O     1 
ATOM   3934 C CB    . GLU   B 1 183 ? 12.454  7.336   22.294 1.00 47.55  ? 309 GLU   B CB    1 
ATOM   3935 C CG    . GLU   B 1 183 ? 12.756  8.157   23.531 1.00 52.08  ? 309 GLU   B CG    1 
ATOM   3936 C CD    . GLU   B 1 183 ? 13.096  9.601   23.205 1.00 55.51  ? 309 GLU   B CD    1 
ATOM   3937 O OE1   . GLU   B 1 183 ? 13.151  9.936   22.008 1.00 52.65  ? 309 GLU   B OE1   1 
ATOM   3938 O OE2   . GLU   B 1 183 ? 13.298  10.406  24.142 1.00 59.25  ? 309 GLU   B OE2   1 
ATOM   3939 N N     . ALA   B 1 184 ? 13.002  4.458   21.163 1.00 45.04  ? 310 ALA   B N     1 
ATOM   3940 C CA    . ALA   B 1 184 ? 12.719  3.332   20.276 1.00 43.92  ? 310 ALA   B CA    1 
ATOM   3941 C C     . ALA   B 1 184 ? 11.476  3.571   19.421 1.00 47.55  ? 310 ALA   B C     1 
ATOM   3942 O O     . ALA   B 1 184 ? 11.386  3.051   18.303 1.00 43.07  ? 310 ALA   B O     1 
ATOM   3943 C CB    . ALA   B 1 184 ? 12.562  2.044   21.080 1.00 44.06  ? 310 ALA   B CB    1 
ATOM   3944 N N     . ASP   B 1 185 ? 10.521  4.355   19.900 1.00 48.78  ? 311 ASP   B N     1 
ATOM   3945 C CA    . ASP   B 1 185 ? 9.330   4.546   19.081 1.00 47.72  ? 311 ASP   B CA    1 
ATOM   3946 C C     . ASP   B 1 185 ? 9.555   5.518   17.923 1.00 52.03  ? 311 ASP   B C     1 
ATOM   3947 O O     . ASP   B 1 185 ? 8.662   5.676   17.086 1.00 52.58  ? 311 ASP   B O     1 
ATOM   3948 C CB    . ASP   B 1 185 ? 8.138   4.992   19.948 1.00 56.93  ? 311 ASP   B CB    1 
ATOM   3949 C CG    . ASP   B 1 185 ? 8.272   6.412   20.486 1.00 58.10  ? 311 ASP   B CG    1 
ATOM   3950 O OD1   . ASP   B 1 185 ? 9.353   7.030   20.372 1.00 57.13  ? 311 ASP   B OD1   1 
ATOM   3951 O OD2   . ASP   B 1 185 ? 7.267   6.910   21.039 1.00 67.16  ? 311 ASP   B OD2   1 
ATOM   3952 N N     . ARG   B 1 186 ? 10.723  6.149   17.835 1.00 46.95  ? 312 ARG   B N     1 
ATOM   3953 C CA    . ARG   B 1 186 ? 11.067  7.022   16.722 1.00 49.62  ? 312 ARG   B CA    1 
ATOM   3954 C C     . ARG   B 1 186 ? 11.937  6.324   15.687 1.00 47.59  ? 312 ARG   B C     1 
ATOM   3955 O O     . ARG   B 1 186 ? 12.330  6.954   14.698 1.00 48.11  ? 312 ARG   B O     1 
ATOM   3956 C CB    . ARG   B 1 186 ? 11.800  8.271   17.221 1.00 52.32  ? 312 ARG   B CB    1 
ATOM   3957 C CG    . ARG   B 1 186 ? 11.196  8.941   18.450 1.00 54.75  ? 312 ARG   B CG    1 
ATOM   3958 C CD    . ARG   B 1 186 ? 9.951   9.713   18.101 1.00 58.21  ? 312 ARG   B CD    1 
ATOM   3959 N NE    . ARG   B 1 186 ? 8.763   8.871   18.104 1.00 65.39  ? 312 ARG   B NE    1 
ATOM   3960 C CZ    . ARG   B 1 186 ? 7.676   9.113   17.381 1.00 67.01  ? 312 ARG   B CZ    1 
ATOM   3961 N NH1   . ARG   B 1 186 ? 7.621   10.131  16.537 1.00 69.49  ? 312 ARG   B NH1   1 
ATOM   3962 N NH2   . ARG   B 1 186 ? 6.624   8.304   17.497 1.00 66.02  ? 312 ARG   B NH2   1 
ATOM   3963 N N     . LEU   B 1 187 ? 12.251  5.047   15.887 1.00 41.60  ? 313 LEU   B N     1 
ATOM   3964 C CA    . LEU   B 1 187 ? 13.187  4.374   14.991 1.00 41.91  ? 313 LEU   B CA    1 
ATOM   3965 C C     . LEU   B 1 187 ? 12.594  4.246   13.598 1.00 41.79  ? 313 LEU   B C     1 
ATOM   3966 O O     . LEU   B 1 187 ? 13.258  4.549   12.602 1.00 45.67  ? 313 LEU   B O     1 
ATOM   3967 C CB    . LEU   B 1 187 ? 13.560  2.998   15.558 1.00 45.41  ? 313 LEU   B CB    1 
ATOM   3968 C CG    . LEU   B 1 187 ? 14.675  2.184   14.879 1.00 41.33  ? 313 LEU   B CG    1 
ATOM   3969 C CD1   . LEU   B 1 187 ? 15.285  1.221   15.862 1.00 40.70  ? 313 LEU   B CD1   1 
ATOM   3970 C CD2   . LEU   B 1 187 ? 14.157  1.400   13.686 1.00 48.08  ? 313 LEU   B CD2   1 
ATOM   3971 N N     . GLU   B 1 188 ? 11.331  3.827   13.512 1.00 42.73  ? 314 GLU   B N     1 
ATOM   3972 C CA    . GLU   B 1 188 ? 10.723  3.529   12.213 1.00 44.90  ? 314 GLU   B CA    1 
ATOM   3973 C C     . GLU   B 1 188 ? 10.679  4.757   11.308 1.00 47.22  ? 314 GLU   B C     1 
ATOM   3974 O O     . GLU   B 1 188 ? 11.027  4.677   10.126 1.00 47.52  ? 314 GLU   B O     1 
ATOM   3975 C CB    . GLU   B 1 188 ? 9.318   2.966   12.414 1.00 49.87  ? 314 GLU   B CB    1 
ATOM   3976 N N     . LEU   B 1 189 ? 10.220  5.897   11.828 1.00 46.24  ? 315 LEU   B N     1 
ATOM   3977 C CA    . LEU   B 1 189 ? 10.136  7.080   10.974 1.00 47.48  ? 315 LEU   B CA    1 
ATOM   3978 C C     . LEU   B 1 189 ? 11.521  7.544   10.552 1.00 44.87  ? 315 LEU   B C     1 
ATOM   3979 O O     . LEU   B 1 189 ? 11.721  7.959   9.408  1.00 48.41  ? 315 LEU   B O     1 
ATOM   3980 C CB    . LEU   B 1 189 ? 9.380   8.206   11.680 1.00 49.68  ? 315 LEU   B CB    1 
ATOM   3981 N N     . SER   B 1 190 ? 12.498  7.460   11.461 1.00 44.02  ? 316 SER   B N     1 
ATOM   3982 C CA    . SER   B 1 190 ? 13.855  7.830   11.097 1.00 44.04  ? 316 SER   B CA    1 
ATOM   3983 C C     . SER   B 1 190 ? 14.410  6.906   10.026 1.00 45.99  ? 316 SER   B C     1 
ATOM   3984 O O     . SER   B 1 190 ? 15.198  7.339   9.179  1.00 45.53  ? 316 SER   B O     1 
ATOM   3985 C CB    . SER   B 1 190 ? 14.753  7.811   12.327 1.00 41.64  ? 316 SER   B CB    1 
ATOM   3986 O OG    . SER   B 1 190 ? 15.012  6.474   12.740 1.00 46.61  ? 316 SER   B OG    1 
ATOM   3987 N N     . LEU   B 1 191 ? 14.002  5.638   10.035 1.00 47.78  ? 317 LEU   B N     1 
ATOM   3988 C CA    . LEU   B 1 191 ? 14.509  4.703   9.039  1.00 42.50  ? 317 LEU   B CA    1 
ATOM   3989 C C     . LEU   B 1 191 ? 13.870  4.954   7.683  1.00 47.83  ? 317 LEU   B C     1 
ATOM   3990 O O     . LEU   B 1 191 ? 14.546  4.893   6.651  1.00 48.15  ? 317 LEU   B O     1 
ATOM   3991 C CB    . LEU   B 1 191 ? 14.266  3.267   9.493  1.00 47.15  ? 317 LEU   B CB    1 
ATOM   3992 C CG    . LEU   B 1 191 ? 15.060  2.206   8.732  1.00 50.55  ? 317 LEU   B CG    1 
ATOM   3993 C CD1   . LEU   B 1 191 ? 16.543  2.606   8.568  1.00 41.47  ? 317 LEU   B CD1   1 
ATOM   3994 C CD2   . LEU   B 1 191 ? 14.940  0.874   9.460  1.00 44.41  ? 317 LEU   B CD2   1 
ATOM   3995 N N     . ASP   B 1 192 ? 12.572  5.250   7.659  1.00 49.20  ? 318 ASP   B N     1 
ATOM   3996 C CA    . ASP   B 1 192 ? 11.954  5.639   6.397  1.00 48.98  ? 318 ASP   B CA    1 
ATOM   3997 C C     . ASP   B 1 192 ? 12.608  6.894   5.840  1.00 49.83  ? 318 ASP   B C     1 
ATOM   3998 O O     . ASP   B 1 192 ? 12.818  7.007   4.626  1.00 49.87  ? 318 ASP   B O     1 
ATOM   3999 C CB    . ASP   B 1 192 ? 10.453  5.851   6.583  1.00 52.54  ? 318 ASP   B CB    1 
ATOM   4000 C CG    . ASP   B 1 192 ? 9.749   4.598   7.050  1.00 59.25  ? 318 ASP   B CG    1 
ATOM   4001 O OD1   . ASP   B 1 192 ? 10.342  3.509   6.900  1.00 58.30  ? 318 ASP   B OD1   1 
ATOM   4002 O OD2   . ASP   B 1 192 ? 8.615   4.696   7.571  1.00 58.67  ? 318 ASP   B OD2   1 
ATOM   4003 N N     . LEU   B 1 193 ? 12.928  7.848   6.716  1.00 46.51  ? 319 LEU   B N     1 
ATOM   4004 C CA    . LEU   B 1 193 ? 13.592  9.077   6.296  1.00 48.73  ? 319 LEU   B CA    1 
ATOM   4005 C C     . LEU   B 1 193 ? 14.928  8.776   5.640  1.00 47.74  ? 319 LEU   B C     1 
ATOM   4006 O O     . LEU   B 1 193 ? 15.243  9.304   4.565  1.00 47.52  ? 319 LEU   B O     1 
ATOM   4007 C CB    . LEU   B 1 193 ? 13.794  9.998   7.497  1.00 48.12  ? 319 LEU   B CB    1 
ATOM   4008 C CG    . LEU   B 1 193 ? 14.549  11.287  7.174  1.00 53.69  ? 319 LEU   B CG    1 
ATOM   4009 C CD1   . LEU   B 1 193 ? 13.722  12.144  6.235  1.00 59.34  ? 319 LEU   B CD1   1 
ATOM   4010 C CD2   . LEU   B 1 193 ? 14.912  12.054  8.435  1.00 56.19  ? 319 LEU   B CD2   1 
ATOM   4011 N N     . LEU   B 1 194 ? 15.730  7.935   6.290  1.00 43.42  ? 320 LEU   B N     1 
ATOM   4012 C CA    . LEU   B 1 194 ? 17.020  7.542   5.733  1.00 45.72  ? 320 LEU   B CA    1 
ATOM   4013 C C     . LEU   B 1 194 ? 16.855  6.934   4.351  1.00 47.51  ? 320 LEU   B C     1 
ATOM   4014 O O     . LEU   B 1 194 ? 17.601  7.272   3.420  1.00 43.20  ? 320 LEU   B O     1 
ATOM   4015 C CB    . LEU   B 1 194 ? 17.718  6.550   6.666  1.00 43.57  ? 320 LEU   B CB    1 
ATOM   4016 C CG    . LEU   B 1 194 ? 19.065  6.018   6.150  1.00 42.01  ? 320 LEU   B CG    1 
ATOM   4017 C CD1   . LEU   B 1 194 ? 20.157  7.057   6.297  1.00 39.22  ? 320 LEU   B CD1   1 
ATOM   4018 C CD2   . LEU   B 1 194 ? 19.457  4.725   6.866  1.00 37.00  ? 320 LEU   B CD2   1 
ATOM   4019 N N     . GLU   B 1 195 ? 15.870  6.048   4.189  1.00 47.83  ? 321 GLU   B N     1 
ATOM   4020 C CA    . GLU   B 1 195 ? 15.667  5.411   2.893  1.00 44.13  ? 321 GLU   B CA    1 
ATOM   4021 C C     . GLU   B 1 195 ? 15.356  6.443   1.809  1.00 49.65  ? 321 GLU   B C     1 
ATOM   4022 O O     . GLU   B 1 195 ? 15.940  6.410   0.720  1.00 49.42  ? 321 GLU   B O     1 
ATOM   4023 C CB    . GLU   B 1 195 ? 14.547  4.370   2.987  1.00 45.89  ? 321 GLU   B CB    1 
ATOM   4024 C CG    . GLU   B 1 195 ? 14.209  3.760   1.634  1.00 47.24  ? 321 GLU   B CG    1 
ATOM   4025 C CD    . GLU   B 1 195 ? 13.176  2.663   1.710  1.00 54.34  ? 321 GLU   B CD    1 
ATOM   4026 O OE1   . GLU   B 1 195 ? 12.213  2.805   2.496  1.00 55.86  ? 321 GLU   B OE1   1 
ATOM   4027 O OE2   . GLU   B 1 195 ? 13.313  1.670   0.954  1.00 61.23  ? 321 GLU   B OE2   1 
ATOM   4028 N N     . VAL   B 1 196 ? 14.436  7.370   2.092  1.00 49.95  ? 322 VAL   B N     1 
ATOM   4029 C CA    . VAL   B 1 196 ? 14.049  8.364   1.090  1.00 49.33  ? 322 VAL   B CA    1 
ATOM   4030 C C     . VAL   B 1 196 ? 15.248  9.216   0.692  1.00 51.12  ? 322 VAL   B C     1 
ATOM   4031 O O     . VAL   B 1 196 ? 15.433  9.533   -0.486 1.00 54.26  ? 322 VAL   B O     1 
ATOM   4032 C CB    . VAL   B 1 196 ? 12.888  9.228   1.616  1.00 54.05  ? 322 VAL   B CB    1 
ATOM   4033 C CG1   . VAL   B 1 196 ? 12.628  10.403  0.688  1.00 57.60  ? 322 VAL   B CG1   1 
ATOM   4034 C CG2   . VAL   B 1 196 ? 11.631  8.386   1.776  1.00 56.54  ? 322 VAL   B CG2   1 
ATOM   4035 N N     . LEU   B 1 197 ? 16.093  9.581   1.661  1.00 51.42  ? 323 LEU   B N     1 
ATOM   4036 C CA    . LEU   B 1 197 ? 17.253  10.413  1.344  1.00 50.45  ? 323 LEU   B CA    1 
ATOM   4037 C C     . LEU   B 1 197 ? 18.287  9.640   0.537  1.00 50.95  ? 323 LEU   B C     1 
ATOM   4038 O O     . LEU   B 1 197 ? 18.894  10.185  -0.393 1.00 49.31  ? 323 LEU   B O     1 
ATOM   4039 C CB    . LEU   B 1 197 ? 17.885  10.953  2.627  1.00 50.66  ? 323 LEU   B CB    1 
ATOM   4040 C CG    . LEU   B 1 197 ? 17.086  11.938  3.481  1.00 49.48  ? 323 LEU   B CG    1 
ATOM   4041 C CD1   . LEU   B 1 197 ? 17.740  12.127  4.841  1.00 54.44  ? 323 LEU   B CD1   1 
ATOM   4042 C CD2   . LEU   B 1 197 ? 16.961  13.260  2.756  1.00 56.25  ? 323 LEU   B CD2   1 
ATOM   4043 N N     . CYS   B 1 198 ? 18.508  8.373   0.881  1.00 46.91  ? 324 CYS   B N     1 
ATOM   4044 C CA    . CYS   B 1 198 ? 19.504  7.579   0.173  1.00 50.17  ? 324 CYS   B CA    1 
ATOM   4045 C C     . CYS   B 1 198 ? 19.100  7.273   -1.257 1.00 51.21  ? 324 CYS   B C     1 
ATOM   4046 O O     . CYS   B 1 198 ? 19.972  7.025   -2.097 1.00 48.81  ? 324 CYS   B O     1 
ATOM   4047 C CB    . CYS   B 1 198 ? 19.765  6.278   0.925  1.00 45.37  ? 324 CYS   B CB    1 
ATOM   4048 S SG    . CYS   B 1 198 ? 20.766  6.547   2.391  1.00 46.66  ? 324 CYS   B SG    1 
ATOM   4049 N N     . LEU   B 1 199 ? 17.806  7.280   -1.551 1.00 52.40  ? 325 LEU   B N     1 
ATOM   4050 C CA    . LEU   B 1 199 ? 17.327  7.060   -2.904 1.00 52.36  ? 325 LEU   B CA    1 
ATOM   4051 C C     . LEU   B 1 199 ? 17.144  8.358   -3.682 1.00 55.44  ? 325 LEU   B C     1 
ATOM   4052 O O     . LEU   B 1 199 ? 16.934  8.311   -4.902 1.00 56.53  ? 325 LEU   B O     1 
ATOM   4053 C CB    . LEU   B 1 199 ? 16.006  6.283   -2.858 1.00 52.30  ? 325 LEU   B CB    1 
ATOM   4054 C CG    . LEU   B 1 199 ? 16.053  4.901   -2.196 1.00 53.80  ? 325 LEU   B CG    1 
ATOM   4055 C CD1   . LEU   B 1 199 ? 14.657  4.291   -2.043 1.00 53.48  ? 325 LEU   B CD1   1 
ATOM   4056 C CD2   . LEU   B 1 199 ? 16.960  3.965   -2.992 1.00 54.14  ? 325 LEU   B CD2   1 
ATOM   4057 N N     . ASP   B 1 200 ? 17.226  9.506   -3.011 1.00 53.57  ? 326 ASP   B N     1 
ATOM   4058 C CA    . ASP   B 1 200 ? 17.093  10.799  -3.671 1.00 56.92  ? 326 ASP   B CA    1 
ATOM   4059 C C     . ASP   B 1 200 ? 18.311  11.060  -4.548 1.00 55.33  ? 326 ASP   B C     1 
ATOM   4060 O O     . ASP   B 1 200 ? 19.447  11.115  -4.057 1.00 56.40  ? 326 ASP   B O     1 
ATOM   4061 C CB    . ASP   B 1 200 ? 16.933  11.893  -2.620 1.00 56.86  ? 326 ASP   B CB    1 
ATOM   4062 C CG    . ASP   B 1 200 ? 16.495  13.208  -3.204 1.00 61.46  ? 326 ASP   B CG    1 
ATOM   4063 O OD1   . ASP   B 1 200 ? 16.956  13.583  -4.305 1.00 60.35  ? 326 ASP   B OD1   1 
ATOM   4064 O OD2   . ASP   B 1 200 ? 15.667  13.875  -2.556 1.00 69.11  ? 326 ASP   B OD2   1 
ATOM   4065 N N     . GLY   B 1 201 ? 18.076  11.210  -5.849 1.00 57.82  ? 327 GLY   B N     1 
ATOM   4066 C CA    . GLY   B 1 201 ? 19.163  11.488  -6.766 1.00 61.36  ? 327 GLY   B CA    1 
ATOM   4067 C C     . GLY   B 1 201 ? 19.888  12.787  -6.487 1.00 59.22  ? 327 GLY   B C     1 
ATOM   4068 O O     . GLY   B 1 201 ? 21.057  12.928  -6.864 1.00 56.15  ? 327 GLY   B O     1 
ATOM   4069 N N     . ASP   B 1 202 ? 19.221  13.748  -5.844 1.00 56.48  ? 328 ASP   B N     1 
ATOM   4070 C CA    . ASP   B 1 202 ? 19.867  15.029  -5.578 1.00 57.65  ? 328 ASP   B CA    1 
ATOM   4071 C C     . ASP   B 1 202 ? 21.090  14.871  -4.681 1.00 57.31  ? 328 ASP   B C     1 
ATOM   4072 O O     . ASP   B 1 202 ? 21.946  15.760  -4.656 1.00 57.40  ? 328 ASP   B O     1 
ATOM   4073 C CB    . ASP   B 1 202 ? 18.883  16.014  -4.935 1.00 60.66  ? 328 ASP   B CB    1 
ATOM   4074 C CG    . ASP   B 1 202 ? 17.853  16.567  -5.919 1.00 62.96  ? 328 ASP   B CG    1 
ATOM   4075 O OD1   . ASP   B 1 202 ? 17.990  16.352  -7.147 1.00 64.00  ? 328 ASP   B OD1   1 
ATOM   4076 O OD2   . ASP   B 1 202 ? 16.902  17.238  -5.454 1.00 65.24  ? 328 ASP   B OD2   1 
ATOM   4077 N N     . LEU   B 1 203 ? 21.192  13.751  -3.967 1.00 54.11  ? 329 LEU   B N     1 
ATOM   4078 C CA    . LEU   B 1 203 ? 22.296  13.473  -3.055 1.00 48.49  ? 329 LEU   B CA    1 
ATOM   4079 C C     . LEU   B 1 203 ? 23.278  12.456  -3.621 1.00 49.24  ? 329 LEU   B C     1 
ATOM   4080 O O     . LEU   B 1 203 ? 24.157  11.977  -2.887 1.00 53.24  ? 329 LEU   B O     1 
ATOM   4081 C CB    . LEU   B 1 203 ? 21.747  12.982  -1.713 1.00 53.48  ? 329 LEU   B CB    1 
ATOM   4082 C CG    . LEU   B 1 203 ? 20.845  13.951  -0.957 1.00 53.93  ? 329 LEU   B CG    1 
ATOM   4083 C CD1   . LEU   B 1 203 ? 20.299  13.281  0.294  1.00 50.86  ? 329 LEU   B CD1   1 
ATOM   4084 C CD2   . LEU   B 1 203 ? 21.602  15.215  -0.597 1.00 53.60  ? 329 LEU   B CD2   1 
ATOM   4085 N N     . SER   B 1 204 ? 23.141  12.105  -4.900 1.00 57.39  ? 330 SER   B N     1 
ATOM   4086 C CA    . SER   B 1 204 ? 23.999  11.095  -5.502 1.00 53.80  ? 330 SER   B CA    1 
ATOM   4087 C C     . SER   B 1 204 ? 25.463  11.512  -5.418 1.00 54.46  ? 330 SER   B C     1 
ATOM   4088 O O     . SER   B 1 204 ? 25.799  12.699  -5.503 1.00 54.21  ? 330 SER   B O     1 
ATOM   4089 C CB    . SER   B 1 204 ? 23.597  10.864  -6.959 1.00 57.08  ? 330 SER   B CB    1 
ATOM   4090 O OG    . SER   B 1 204 ? 23.868  12.006  -7.741 1.00 61.79  ? 330 SER   B OG    1 
ATOM   4091 N N     . GLY   B 1 205 ? 26.335  10.523  -5.237 1.00 47.34  ? 331 GLY   B N     1 
ATOM   4092 C CA    . GLY   B 1 205 ? 27.759  10.752  -5.235 1.00 48.69  ? 331 GLY   B CA    1 
ATOM   4093 C C     . GLY   B 1 205 ? 28.321  11.184  -3.911 1.00 50.81  ? 331 GLY   B C     1 
ATOM   4094 O O     . GLY   B 1 205 ? 29.536  11.376  -3.803 1.00 56.12  ? 331 GLY   B O     1 
ATOM   4095 N N     . TRP   B 1 206 ? 27.480  11.343  -2.901 1.00 46.35  ? 332 TRP   B N     1 
ATOM   4096 C CA    . TRP   B 1 206 ? 27.906  11.722  -1.564 1.00 42.78  ? 332 TRP   B CA    1 
ATOM   4097 C C     . TRP   B 1 206 ? 27.625  10.554  -0.632 1.00 42.50  ? 332 TRP   B C     1 
ATOM   4098 O O     . TRP   B 1 206 ? 26.497  10.050  -0.583 1.00 45.18  ? 332 TRP   B O     1 
ATOM   4099 C CB    . TRP   B 1 206 ? 27.172  12.990  -1.130 1.00 44.23  ? 332 TRP   B CB    1 
ATOM   4100 C CG    . TRP   B 1 206 ? 27.246  13.336  0.328  1.00 44.49  ? 332 TRP   B CG    1 
ATOM   4101 C CD1   . TRP   B 1 206 ? 28.339  13.788  1.017  1.00 42.67  ? 332 TRP   B CD1   1 
ATOM   4102 C CD2   . TRP   B 1 206 ? 26.169  13.317  1.257  1.00 43.31  ? 332 TRP   B CD2   1 
ATOM   4103 N NE1   . TRP   B 1 206 ? 28.007  14.051  2.308  1.00 41.15  ? 332 TRP   B NE1   1 
ATOM   4104 C CE2   . TRP   B 1 206 ? 26.682  13.755  2.494  1.00 43.07  ? 332 TRP   B CE2   1 
ATOM   4105 C CE3   . TRP   B 1 206 ? 24.818  12.959  1.172  1.00 45.99  ? 332 TRP   B CE3   1 
ATOM   4106 C CZ2   . TRP   B 1 206 ? 25.901  13.841  3.634  1.00 43.46  ? 332 TRP   B CZ2   1 
ATOM   4107 C CZ3   . TRP   B 1 206 ? 24.044  13.046  2.305  1.00 43.87  ? 332 TRP   B CZ3   1 
ATOM   4108 C CH2   . TRP   B 1 206 ? 24.589  13.477  3.527  1.00 42.41  ? 332 TRP   B CH2   1 
ATOM   4109 N N     . ASN   B 1 207 ? 28.659  10.094  0.072  1.00 40.75  ? 333 ASN   B N     1 
ATOM   4110 C CA    . ASN   B 1 207 ? 28.514  8.994   1.013  1.00 41.20  ? 333 ASN   B CA    1 
ATOM   4111 C C     . ASN   B 1 207 ? 28.525  9.469   2.462  1.00 39.26  ? 333 ASN   B C     1 
ATOM   4112 O O     . ASN   B 1 207 ? 28.807  8.679   3.363  1.00 36.72  ? 333 ASN   B O     1 
ATOM   4113 C CB    . ASN   B 1 207 ? 29.605  7.949   0.786  1.00 41.89  ? 333 ASN   B CB    1 
ATOM   4114 C CG    . ASN   B 1 207 ? 29.406  7.189   -0.495 1.00 44.85  ? 333 ASN   B CG    1 
ATOM   4115 O OD1   . ASN   B 1 207 ? 28.279  7.001   -0.943 1.00 46.67  ? 333 ASN   B OD1   1 
ATOM   4116 N ND2   . ASN   B 1 207 ? 30.501  6.762   -1.111 1.00 49.17  ? 333 ASN   B ND2   1 
ATOM   4117 N N     . GLY   B 1 208 ? 28.230  10.742  2.702  1.00 37.56  ? 334 GLY   B N     1 
ATOM   4118 C CA    . GLY   B 1 208 ? 28.280  11.239  4.059  1.00 37.46  ? 334 GLY   B CA    1 
ATOM   4119 C C     . GLY   B 1 208 ? 27.050  10.997  4.900  1.00 32.52  ? 334 GLY   B C     1 
ATOM   4120 O O     . GLY   B 1 208 ? 27.040  11.360  6.076  1.00 34.72  ? 334 GLY   B O     1 
ATOM   4121 N N     . MET   B 1 209 ? 25.988  10.441  4.328  1.00 38.41  ? 335 MET   B N     1 
ATOM   4122 C CA    . MET   B 1 209 ? 24.776  10.184  5.096  1.00 35.71  ? 335 MET   B CA    1 
ATOM   4123 C C     . MET   B 1 209 ? 25.053  9.108   6.124  1.00 34.40  ? 335 MET   B C     1 
ATOM   4124 O O     . MET   B 1 209 ? 25.473  8.006   5.764  1.00 34.52  ? 335 MET   B O     1 
ATOM   4125 C CB    . MET   B 1 209 ? 23.650  9.735   4.170  1.00 39.22  ? 335 MET   B CB    1 
ATOM   4126 C CG    . MET   B 1 209 ? 22.338  9.590   4.883  1.00 45.66  ? 335 MET   B CG    1 
ATOM   4127 S SD    . MET   B 1 209 ? 21.553  11.192  5.079  1.00 53.57  ? 335 MET   B SD    1 
ATOM   4128 C CE    . MET   B 1 209 ? 21.721  11.511  6.807  1.00 46.62  ? 335 MET   B CE    1 
ATOM   4129 N N     . GLY   B 1 210 ? 24.790  9.415   7.395  1.00 32.56  ? 336 GLY   B N     1 
ATOM   4130 C CA    . GLY   B 1 210 ? 25.021  8.475   8.473  1.00 32.49  ? 336 GLY   B CA    1 
ATOM   4131 C C     . GLY   B 1 210 ? 23.776  8.181   9.285  1.00 32.02  ? 336 GLY   B C     1 
ATOM   4132 O O     . GLY   B 1 210 ? 22.807  8.943   9.253  1.00 31.82  ? 336 GLY   B O     1 
ATOM   4133 N N     . PHE   B 1 211 ? 23.771  7.063   10.008 1.00 27.81  ? 337 PHE   B N     1 
ATOM   4134 C CA    . PHE   B 1 211 ? 22.591  6.652   10.747 1.00 31.09  ? 337 PHE   B CA    1 
ATOM   4135 C C     . PHE   B 1 211 ? 23.055  5.876   11.971 1.00 29.58  ? 337 PHE   B C     1 
ATOM   4136 O O     . PHE   B 1 211 ? 23.963  5.053   11.869 1.00 29.69  ? 337 PHE   B O     1 
ATOM   4137 C CB    . PHE   B 1 211 ? 21.685  5.804   9.845  1.00 32.81  ? 337 PHE   B CB    1 
ATOM   4138 C CG    . PHE   B 1 211 ? 20.324  5.533   10.418 1.00 33.86  ? 337 PHE   B CG    1 
ATOM   4139 C CD1   . PHE   B 1 211 ? 19.323  6.482   10.328 1.00 36.16  ? 337 PHE   B CD1   1 
ATOM   4140 C CD2   . PHE   B 1 211 ? 20.032  4.314   10.996 1.00 31.28  ? 337 PHE   B CD2   1 
ATOM   4141 C CE1   . PHE   B 1 211 ? 18.066  6.234   10.832 1.00 37.33  ? 337 PHE   B CE1   1 
ATOM   4142 C CE2   . PHE   B 1 211 ? 18.769  4.061   11.527 1.00 34.51  ? 337 PHE   B CE2   1 
ATOM   4143 C CZ    . PHE   B 1 211 ? 17.783  5.025   11.433 1.00 37.31  ? 337 PHE   B CZ    1 
ATOM   4144 N N     . VAL   B 1 212 ? 22.453  6.155   13.124 1.00 29.07  ? 338 VAL   B N     1 
ATOM   4145 C CA    . VAL   B 1 212 ? 22.806  5.437   14.346 1.00 26.73  ? 338 VAL   B CA    1 
ATOM   4146 C C     . VAL   B 1 212 ? 21.883  4.248   14.510 1.00 30.03  ? 338 VAL   B C     1 
ATOM   4147 O O     . VAL   B 1 212 ? 20.665  4.363   14.315 1.00 29.83  ? 338 VAL   B O     1 
ATOM   4148 C CB    . VAL   B 1 212 ? 22.716  6.354   15.576 1.00 29.04  ? 338 VAL   B CB    1 
ATOM   4149 C CG1   . VAL   B 1 212 ? 23.064  5.556   16.807 1.00 28.26  ? 338 VAL   B CG1   1 
ATOM   4150 C CG2   . VAL   B 1 212 ? 23.657  7.549   15.400 1.00 31.51  ? 338 VAL   B CG2   1 
ATOM   4151 N N     . VAL   B 1 213 ? 22.437  3.112   14.944 1.00 29.01  ? 339 VAL   B N     1 
ATOM   4152 C CA    . VAL   B 1 213 ? 21.612  2.000   15.392 1.00 29.07  ? 339 VAL   B CA    1 
ATOM   4153 C C     . VAL   B 1 213 ? 22.047  1.611   16.794 1.00 30.48  ? 339 VAL   B C     1 
ATOM   4154 O O     . VAL   B 1 213 ? 23.245  1.551   17.082 1.00 27.95  ? 339 VAL   B O     1 
ATOM   4155 C CB    . VAL   B 1 213 ? 21.680  0.786   14.444 1.00 31.87  ? 339 VAL   B CB    1 
ATOM   4156 C CG1   . VAL   B 1 213 ? 20.567  -0.205  14.804 1.00 35.45  ? 339 VAL   B CG1   1 
ATOM   4157 C CG2   . VAL   B 1 213 ? 21.504  1.228   12.996 1.00 32.65  ? 339 VAL   B CG2   1 
ATOM   4158 N N     . GLN   B 1 214 ? 21.070  1.348   17.652 1.00 32.33  ? 340 GLN   B N     1 
ATOM   4159 C CA    . GLN   B 1 214 ? 21.282  1.139   19.084 1.00 28.59  ? 340 GLN   B CA    1 
ATOM   4160 C C     . GLN   B 1 214 ? 21.246  -0.354  19.374 1.00 31.97  ? 340 GLN   B C     1 
ATOM   4161 O O     . GLN   B 1 214 ? 20.204  -0.998  19.195 1.00 30.50  ? 340 GLN   B O     1 
ATOM   4162 C CB    . GLN   B 1 214 ? 20.214  1.875   19.889 1.00 31.12  ? 340 GLN   B CB    1 
ATOM   4163 C CG    . GLN   B 1 214 ? 20.194  3.366   19.614 1.00 32.63  ? 340 GLN   B CG    1 
ATOM   4164 C CD    . GLN   B 1 214 ? 18.829  3.979   19.786 1.00 33.45  ? 340 GLN   B CD    1 
ATOM   4165 O OE1   . GLN   B 1 214 ? 17.861  3.547   19.165 1.00 37.01  ? 340 GLN   B OE1   1 
ATOM   4166 N NE2   . GLN   B 1 214 ? 18.746  5.007   20.618 1.00 32.36  ? 340 GLN   B NE2   1 
ATOM   4167 N N     . ALA   B 1 215 ? 22.375  -0.895  19.843 1.00 29.33  ? 341 ALA   B N     1 
ATOM   4168 C CA    . ALA   B 1 215 ? 22.485  -2.335  20.060 1.00 31.41  ? 341 ALA   B CA    1 
ATOM   4169 C C     . ALA   B 1 215 ? 21.651  -2.833  21.232 1.00 33.17  ? 341 ALA   B C     1 
ATOM   4170 O O     . ALA   B 1 215 ? 21.415  -4.042  21.332 1.00 32.43  ? 341 ALA   B O     1 
ATOM   4171 C CB    . ALA   B 1 215 ? 23.948  -2.732  20.269 1.00 31.12  ? 341 ALA   B CB    1 
ATOM   4172 N N     . TYR   B 1 216 ? 21.170  -1.959  22.108 1.00 31.03  ? 342 TYR   B N     1 
ATOM   4173 C CA    . TYR   B 1 216 ? 20.287  -2.498  23.133 1.00 33.56  ? 342 TYR   B CA    1 
ATOM   4174 C C     . TYR   B 1 216 ? 18.891  -2.767  22.597 1.00 32.85  ? 342 TYR   B C     1 
ATOM   4175 O O     . TYR   B 1 216 ? 18.065  -3.320  23.314 1.00 36.44  ? 342 TYR   B O     1 
ATOM   4176 C CB    . TYR   B 1 216 ? 20.237  -1.588  24.370 1.00 31.97  ? 342 TYR   B CB    1 
ATOM   4177 C CG    . TYR   B 1 216 ? 19.642  -0.190  24.265 1.00 33.81  ? 342 TYR   B CG    1 
ATOM   4178 C CD1   . TYR   B 1 216 ? 18.931  0.243   23.146 1.00 33.42  ? 342 TYR   B CD1   1 
ATOM   4179 C CD2   . TYR   B 1 216 ? 19.784  0.699   25.319 1.00 33.72  ? 342 TYR   B CD2   1 
ATOM   4180 C CE1   . TYR   B 1 216 ? 18.401  1.521   23.094 1.00 33.68  ? 342 TYR   B CE1   1 
ATOM   4181 C CE2   . TYR   B 1 216 ? 19.257  1.971   25.273 1.00 35.58  ? 342 TYR   B CE2   1 
ATOM   4182 C CZ    . TYR   B 1 216 ? 18.556  2.379   24.147 1.00 32.99  ? 342 TYR   B CZ    1 
ATOM   4183 O OH    . TYR   B 1 216 ? 18.030  3.651   24.121 1.00 35.03  ? 342 TYR   B OH    1 
ATOM   4184 N N     . GLY   B 1 217 ? 18.613  -2.410  21.346 1.00 34.84  ? 343 GLY   B N     1 
ATOM   4185 C CA    . GLY   B 1 217 ? 17.305  -2.666  20.777 1.00 35.99  ? 343 GLY   B CA    1 
ATOM   4186 C C     . GLY   B 1 217 ? 17.241  -4.067  20.190 1.00 39.14  ? 343 GLY   B C     1 
ATOM   4187 O O     . GLY   B 1 217 ? 18.173  -4.521  19.534 1.00 36.52  ? 343 GLY   B O     1 
ATOM   4188 N N     . LYS   B 1 218 ? 16.121  -4.752  20.451 1.00 40.11  ? 344 LYS   B N     1 
ATOM   4189 C CA    . LYS   B 1 218 ? 15.863  -6.042  19.815 1.00 38.52  ? 344 LYS   B CA    1 
ATOM   4190 C C     . LYS   B 1 218 ? 15.902  -5.953  18.293 1.00 43.07  ? 344 LYS   B C     1 
ATOM   4191 O O     . LYS   B 1 218 ? 16.236  -6.938  17.628 1.00 43.32  ? 344 LYS   B O     1 
ATOM   4192 C CB    . LYS   B 1 218 ? 14.498  -6.577  20.257 1.00 43.64  ? 344 LYS   B CB    1 
ATOM   4193 C CG    . LYS   B 1 218 ? 14.375  -6.689  21.764 1.00 44.70  ? 344 LYS   B CG    1 
ATOM   4194 C CD    . LYS   B 1 218 ? 12.978  -7.117  22.178 1.00 48.85  ? 344 LYS   B CD    1 
ATOM   4195 C CE    . LYS   B 1 218 ? 12.985  -7.627  23.604 1.00 49.27  ? 344 LYS   B CE    1 
ATOM   4196 N NZ    . LYS   B 1 218 ? 11.614  -7.754  24.173 1.00 52.60  ? 344 LYS   B NZ    1 
ATOM   4197 N N     . ARG   B 1 219 ? 15.533  -4.806  17.721 1.00 41.38  ? 345 ARG   B N     1 
ATOM   4198 C CA    . ARG   B 1 219 ? 15.444  -4.698  16.269 1.00 39.41  ? 345 ARG   B CA    1 
ATOM   4199 C C     . ARG   B 1 219 ? 16.795  -4.487  15.607 1.00 38.94  ? 345 ARG   B C     1 
ATOM   4200 O O     . ARG   B 1 219 ? 16.875  -4.540  14.371 1.00 39.39  ? 345 ARG   B O     1 
ATOM   4201 C CB    . ARG   B 1 219 ? 14.510  -3.552  15.890 1.00 42.10  ? 345 ARG   B CB    1 
ATOM   4202 C CG    . ARG   B 1 219 ? 13.072  -3.772  16.321 1.00 46.27  ? 345 ARG   B CG    1 
ATOM   4203 C CD    . ARG   B 1 219 ? 12.268  -2.511  16.067 1.00 48.70  ? 345 ARG   B CD    1 
ATOM   4204 N NE    . ARG   B 1 219 ? 12.616  -1.463  17.022 1.00 47.03  ? 345 ARG   B NE    1 
ATOM   4205 C CZ    . ARG   B 1 219 ? 12.043  -0.268  17.060 1.00 50.88  ? 345 ARG   B CZ    1 
ATOM   4206 N NH1   . ARG   B 1 219 ? 11.087  0.071   16.205 1.00 46.60  ? 345 ARG   B NH1   1 
ATOM   4207 N NH2   . ARG   B 1 219 ? 12.433  0.608   17.978 1.00 45.84  ? 345 ARG   B NH2   1 
ATOM   4208 N N     . CYS   B 1 220 ? 17.849  -4.287  16.400 1.00 38.63  ? 346 CYS   B N     1 
ATOM   4209 C CA    . CYS   B 1 220 ? 19.128  -3.814  15.875 1.00 36.17  ? 346 CYS   B CA    1 
ATOM   4210 C C     . CYS   B 1 220 ? 19.665  -4.639  14.716 1.00 36.84  ? 346 CYS   B C     1 
ATOM   4211 O O     . CYS   B 1 220 ? 19.962  -4.045  13.670 1.00 37.01  ? 346 CYS   B O     1 
ATOM   4212 C CB    . CYS   B 1 220 ? 20.171  -3.735  16.997 1.00 33.94  ? 346 CYS   B CB    1 
ATOM   4213 S SG    . CYS   B 1 220 ? 21.729  -2.897  16.494 1.00 36.37  ? 346 CYS   B SG    1 
ATOM   4214 N N     . PRO   B 1 221 ? 19.822  -5.967  14.811 1.00 35.84  ? 347 PRO   B N     1 
ATOM   4215 C CA    . PRO   B 1 221 ? 20.435  -6.684  13.681 1.00 38.95  ? 347 PRO   B CA    1 
ATOM   4216 C C     . PRO   B 1 221 ? 19.592  -6.610  12.431 1.00 40.12  ? 347 PRO   B C     1 
ATOM   4217 O O     . PRO   B 1 221 ? 20.131  -6.592  11.318 1.00 40.31  ? 347 PRO   B O     1 
ATOM   4218 C CB    . PRO   B 1 221 ? 20.572  -8.121  14.196 1.00 41.94  ? 347 PRO   B CB    1 
ATOM   4219 C CG    . PRO   B 1 221 ? 19.581  -8.243  15.267 1.00 43.10  ? 347 PRO   B CG    1 
ATOM   4220 C CD    . PRO   B 1 221 ? 19.367  -6.892  15.864 1.00 35.61  ? 347 PRO   B CD    1 
ATOM   4221 N N     . PHE   B 1 222 ? 18.276  -6.517  12.588 1.00 36.64  ? 348 PHE   B N     1 
ATOM   4222 C CA    . PHE   B 1 222 ? 17.389  -6.463  11.435 1.00 38.96  ? 348 PHE   B CA    1 
ATOM   4223 C C     . PHE   B 1 222 ? 17.285  -5.059  10.853 1.00 38.56  ? 348 PHE   B C     1 
ATOM   4224 O O     . PHE   B 1 222 ? 17.052  -4.900  9.645  1.00 39.23  ? 348 PHE   B O     1 
ATOM   4225 C CB    . PHE   B 1 222 ? 16.041  -7.031  11.861 1.00 39.82  ? 348 PHE   B CB    1 
ATOM   4226 C CG    . PHE   B 1 222 ? 16.171  -8.341  12.572 1.00 41.69  ? 348 PHE   B CG    1 
ATOM   4227 C CD1   . PHE   B 1 222 ? 16.448  -9.498  11.871 1.00 44.69  ? 348 PHE   B CD1   1 
ATOM   4228 C CD2   . PHE   B 1 222 ? 16.079  -8.411  13.959 1.00 44.72  ? 348 PHE   B CD2   1 
ATOM   4229 C CE1   . PHE   B 1 222 ? 16.591  -10.713 12.525 1.00 46.24  ? 348 PHE   B CE1   1 
ATOM   4230 C CE2   . PHE   B 1 222 ? 16.221  -9.627  14.624 1.00 47.72  ? 348 PHE   B CE2   1 
ATOM   4231 C CZ    . PHE   B 1 222 ? 16.480  -10.778 13.906 1.00 47.16  ? 348 PHE   B CZ    1 
ATOM   4232 N N     . VAL   B 1 223 ? 17.440  -4.032  11.684 1.00 36.80  ? 349 VAL   B N     1 
ATOM   4233 C CA    . VAL   B 1 223 ? 17.631  -2.691  11.150 1.00 38.25  ? 349 VAL   B CA    1 
ATOM   4234 C C     . VAL   B 1 223 ? 18.930  -2.639  10.363 1.00 39.02  ? 349 VAL   B C     1 
ATOM   4235 O O     . VAL   B 1 223 ? 19.004  -2.048  9.281  1.00 37.60  ? 349 VAL   B O     1 
ATOM   4236 C CB    . VAL   B 1 223 ? 17.599  -1.663  12.298 1.00 36.23  ? 349 VAL   B CB    1 
ATOM   4237 C CG1   . VAL   B 1 223 ? 17.973  -0.276  11.798 1.00 33.26  ? 349 VAL   B CG1   1 
ATOM   4238 C CG2   . VAL   B 1 223 ? 16.206  -1.653  12.937 1.00 37.73  ? 349 VAL   B CG2   1 
ATOM   4239 N N     . LEU   B 1 224 ? 19.964  -3.303  10.868 1.00 38.46  ? 350 LEU   B N     1 
ATOM   4240 C CA    . LEU   B 1 224 ? 21.221  -3.328  10.136 1.00 37.09  ? 350 LEU   B CA    1 
ATOM   4241 C C     . LEU   B 1 224 ? 21.072  -4.047  8.797  1.00 37.59  ? 350 LEU   B C     1 
ATOM   4242 O O     . LEU   B 1 224 ? 21.605  -3.579  7.792  1.00 40.14  ? 350 LEU   B O     1 
ATOM   4243 C CB    . LEU   B 1 224 ? 22.312  -3.959  10.988 1.00 34.57  ? 350 LEU   B CB    1 
ATOM   4244 C CG    . LEU   B 1 224 ? 22.700  -3.062  12.162 1.00 37.53  ? 350 LEU   B CG    1 
ATOM   4245 C CD1   . LEU   B 1 224 ? 23.779  -3.713  12.936 1.00 37.51  ? 350 LEU   B CD1   1 
ATOM   4246 C CD2   . LEU   B 1 224 ? 23.186  -1.721  11.651 1.00 39.49  ? 350 LEU   B CD2   1 
ATOM   4247 N N     . ASP   B 1 225 ? 20.344  -5.173  8.758  1.00 38.36  ? 351 ASP   B N     1 
ATOM   4248 C CA    . ASP   B 1 225 ? 20.114  -5.853  7.483  1.00 39.49  ? 351 ASP   B CA    1 
ATOM   4249 C C     . ASP   B 1 225 ? 19.423  -4.926  6.496  1.00 41.19  ? 351 ASP   B C     1 
ATOM   4250 O O     . ASP   B 1 225 ? 19.712  -4.948  5.292  1.00 42.76  ? 351 ASP   B O     1 
ATOM   4251 C CB    . ASP   B 1 225 ? 19.263  -7.111  7.675  1.00 41.97  ? 351 ASP   B CB    1 
ATOM   4252 C CG    . ASP   B 1 225 ? 19.999  -8.214  8.403  1.00 45.24  ? 351 ASP   B CG    1 
ATOM   4253 O OD1   . ASP   B 1 225 ? 21.245  -8.186  8.417  1.00 47.05  ? 351 ASP   B OD1   1 
ATOM   4254 O OD2   . ASP   B 1 225 ? 19.323  -9.118  8.951  1.00 49.27  ? 351 ASP   B OD2   1 
ATOM   4255 N N     . PHE   B 1 226 ? 18.467  -4.135  6.986  1.00 42.02  ? 352 PHE   B N     1 
ATOM   4256 C CA    . PHE   B 1 226 ? 17.739  -3.231  6.112  1.00 41.18  ? 352 PHE   B CA    1 
ATOM   4257 C C     . PHE   B 1 226 ? 18.654  -2.132  5.602  1.00 40.18  ? 352 PHE   B C     1 
ATOM   4258 O O     . PHE   B 1 226 ? 18.577  -1.748  4.433  1.00 41.41  ? 352 PHE   B O     1 
ATOM   4259 C CB    . PHE   B 1 226 ? 16.541  -2.636  6.851  1.00 42.59  ? 352 PHE   B CB    1 
ATOM   4260 C CG    . PHE   B 1 226 ? 15.804  -1.606  6.063  1.00 45.46  ? 352 PHE   B CG    1 
ATOM   4261 C CD1   . PHE   B 1 226 ? 14.775  -1.968  5.216  1.00 47.39  ? 352 PHE   B CD1   1 
ATOM   4262 C CD2   . PHE   B 1 226 ? 16.149  -0.268  6.161  1.00 44.24  ? 352 PHE   B CD2   1 
ATOM   4263 C CE1   . PHE   B 1 226 ? 14.103  -1.016  4.488  1.00 53.66  ? 352 PHE   B CE1   1 
ATOM   4264 C CE2   . PHE   B 1 226 ? 15.491  0.681   5.428  1.00 48.36  ? 352 PHE   B CE2   1 
ATOM   4265 C CZ    . PHE   B 1 226 ? 14.464  0.313   4.597  1.00 48.75  ? 352 PHE   B CZ    1 
ATOM   4266 N N     . ILE   B 1 227 ? 19.549  -1.640  6.456  1.00 41.00  ? 353 ILE   B N     1 
ATOM   4267 C CA    . ILE   B 1 227 ? 20.420  -0.542  6.053  1.00 40.56  ? 353 ILE   B CA    1 
ATOM   4268 C C     . ILE   B 1 227 ? 21.475  -1.033  5.075  1.00 41.74  ? 353 ILE   B C     1 
ATOM   4269 O O     . ILE   B 1 227 ? 21.775  -0.367  4.075  1.00 38.30  ? 353 ILE   B O     1 
ATOM   4270 C CB    . ILE   B 1 227 ? 21.058  0.107   7.295  1.00 36.05  ? 353 ILE   B CB    1 
ATOM   4271 C CG1   . ILE   B 1 227 ? 20.005  0.876   8.085  1.00 36.17  ? 353 ILE   B CG1   1 
ATOM   4272 C CG2   . ILE   B 1 227 ? 22.194  1.040   6.902  1.00 35.17  ? 353 ILE   B CG2   1 
ATOM   4273 C CD1   . ILE   B 1 227 ? 20.548  1.358   9.435  1.00 38.31  ? 353 ILE   B CD1   1 
ATOM   4274 N N     . ILE   B 1 228 ? 22.071  -2.190  5.357  1.00 39.54  ? 354 ILE   B N     1 
ATOM   4275 C CA    . ILE   B 1 228 ? 23.026  -2.755  4.413  1.00 42.26  ? 354 ILE   B CA    1 
ATOM   4276 C C     . ILE   B 1 228 ? 22.359  -2.971  3.066  1.00 44.72  ? 354 ILE   B C     1 
ATOM   4277 O O     . ILE   B 1 228 ? 22.916  -2.621  2.020  1.00 45.84  ? 354 ILE   B O     1 
ATOM   4278 C CB    . ILE   B 1 228 ? 23.625  -4.055  4.967  1.00 42.33  ? 354 ILE   B CB    1 
ATOM   4279 C CG1   . ILE   B 1 228 ? 24.413  -3.758  6.244  1.00 38.88  ? 354 ILE   B CG1   1 
ATOM   4280 C CG2   . ILE   B 1 228 ? 24.522  -4.692  3.912  1.00 42.55  ? 354 ILE   B CG2   1 
ATOM   4281 C CD1   . ILE   B 1 228 ? 24.727  -4.995  7.055  1.00 38.46  ? 354 ILE   B CD1   1 
ATOM   4282 N N     . ASP   B 1 229 ? 21.138  -3.510  3.069  1.00 44.42  ? 355 ASP   B N     1 
ATOM   4283 C CA    . ASP   B 1 229 ? 20.432  -3.696  1.811  1.00 45.08  ? 355 ASP   B CA    1 
ATOM   4284 C C     . ASP   B 1 229 ? 20.134  -2.360  1.140  1.00 43.19  ? 355 ASP   B C     1 
ATOM   4285 O O     . ASP   B 1 229 ? 20.309  -2.224  -0.072 1.00 44.93  ? 355 ASP   B O     1 
ATOM   4286 C CB    . ASP   B 1 229 ? 19.147  -4.487  2.026  1.00 44.89  ? 355 ASP   B CB    1 
ATOM   4287 C CG    . ASP   B 1 229 ? 18.366  -4.655  0.738  1.00 49.10  ? 355 ASP   B CG    1 
ATOM   4288 O OD1   . ASP   B 1 229 ? 18.760  -5.503  -0.095 1.00 52.70  ? 355 ASP   B OD1   1 
ATOM   4289 O OD2   . ASP   B 1 229 ? 17.371  -3.924  0.541  1.00 53.75  ? 355 ASP   B OD2   1 
ATOM   4290 N N     . LEU   B 1 230 ? 19.721  -1.354  1.918  1.00 43.83  ? 356 LEU   B N     1 
ATOM   4291 C CA    . LEU   B 1 230 ? 19.497  -0.023  1.358  1.00 43.47  ? 356 LEU   B CA    1 
ATOM   4292 C C     . LEU   B 1 230 ? 20.764  0.525   0.726  1.00 42.32  ? 356 LEU   B C     1 
ATOM   4293 O O     . LEU   B 1 230 ? 20.720  1.155   -0.342 1.00 46.53  ? 356 LEU   B O     1 
ATOM   4294 C CB    . LEU   B 1 230 ? 18.996  0.930   2.446  1.00 43.22  ? 356 LEU   B CB    1 
ATOM   4295 C CG    . LEU   B 1 230 ? 18.886  2.404   2.030  1.00 42.39  ? 356 LEU   B CG    1 
ATOM   4296 C CD1   . LEU   B 1 230 ? 17.846  2.615   0.914  1.00 45.47  ? 356 LEU   B CD1   1 
ATOM   4297 C CD2   . LEU   B 1 230 ? 18.567  3.251   3.271  1.00 40.60  ? 356 LEU   B CD2   1 
ATOM   4298 N N     . ALA   B 1 231 ? 21.906  0.276   1.367  1.00 44.32  ? 357 ALA   B N     1 
ATOM   4299 C CA    . ALA   B 1 231 ? 23.182  0.719   0.826  1.00 44.61  ? 357 ALA   B CA    1 
ATOM   4300 C C     . ALA   B 1 231 ? 23.451  0.088   -0.533 1.00 45.73  ? 357 ALA   B C     1 
ATOM   4301 O O     . ALA   B 1 231 ? 23.990  0.739   -1.437 1.00 46.08  ? 357 ALA   B O     1 
ATOM   4302 C CB    . ALA   B 1 231 ? 24.286  0.372   1.820  1.00 39.70  ? 357 ALA   B CB    1 
ATOM   4303 N N     . ARG   B 1 232 ? 23.079  -1.182  -0.696 1.00 46.52  ? 358 ARG   B N     1 
ATOM   4304 C CA    . ARG   B 1 232 ? 23.330  -1.877  -1.951 1.00 46.86  ? 358 ARG   B CA    1 
ATOM   4305 C C     . ARG   B 1 232 ? 22.453  -1.330  -3.063 1.00 48.41  ? 358 ARG   B C     1 
ATOM   4306 O O     . ARG   B 1 232 ? 22.938  -1.036  -4.156 1.00 50.17  ? 358 ARG   B O     1 
ATOM   4307 C CB    . ARG   B 1 232 ? 23.106  -3.379  -1.779 1.00 46.99  ? 358 ARG   B CB    1 
ATOM   4308 C CG    . ARG   B 1 232 ? 23.954  -4.000  -0.660 1.00 45.24  ? 358 ARG   B CG    1 
ATOM   4309 C CD    . ARG   B 1 232 ? 24.015  -5.517  -0.778 1.00 46.78  ? 358 ARG   B CD    1 
ATOM   4310 N NE    . ARG   B 1 232 ? 24.643  -6.140  0.383  1.00 48.70  ? 358 ARG   B NE    1 
ATOM   4311 C CZ    . ARG   B 1 232 ? 25.951  -6.282  0.555  1.00 50.44  ? 358 ARG   B CZ    1 
ATOM   4312 N NH1   . ARG   B 1 232 ? 26.820  -5.842  -0.342 1.00 54.40  ? 358 ARG   B NH1   1 
ATOM   4313 N NH2   . ARG   B 1 232 ? 26.397  -6.881  1.656  1.00 51.84  ? 358 ARG   B NH2   1 
ATOM   4314 N N     . ARG   B 1 233 ? 21.159  -1.176  -2.803 1.00 49.05  ? 359 ARG   B N     1 
ATOM   4315 C CA    . ARG   B 1 233 ? 20.273  -0.757  -3.877 1.00 50.71  ? 359 ARG   B CA    1 
ATOM   4316 C C     . ARG   B 1 233 ? 20.299  0.749   -4.118 1.00 50.05  ? 359 ARG   B C     1 
ATOM   4317 O O     . ARG   B 1 233 ? 19.896  1.189   -5.196 1.00 51.46  ? 359 ARG   B O     1 
ATOM   4318 C CB    . ARG   B 1 233 ? 18.847  -1.250  -3.608 1.00 54.29  ? 359 ARG   B CB    1 
ATOM   4319 C CG    . ARG   B 1 233 ? 18.184  -0.658  -2.409 1.00 50.03  ? 359 ARG   B CG    1 
ATOM   4320 C CD    . ARG   B 1 233 ? 16.960  -1.483  -2.026 1.00 55.80  ? 359 ARG   B CD    1 
ATOM   4321 N NE    . ARG   B 1 233 ? 16.566  -1.212  -0.650 1.00 50.71  ? 359 ARG   B NE    1 
ATOM   4322 C CZ    . ARG   B 1 233 ? 15.700  -0.272  -0.296 1.00 52.87  ? 359 ARG   B CZ    1 
ATOM   4323 N NH1   . ARG   B 1 233 ? 15.087  0.475   -1.200 1.00 55.36  ? 359 ARG   B NH1   1 
ATOM   4324 N NH2   . ARG   B 1 233 ? 15.437  -0.085  0.998  1.00 51.41  ? 359 ARG   B NH2   1 
ATOM   4325 N N     . SER   B 1 234 ? 20.776  1.547   -3.165 1.00 50.43  ? 360 SER   B N     1 
ATOM   4326 C CA    . SER   B 1 234 ? 20.907  2.979   -3.404 1.00 52.49  ? 360 SER   B CA    1 
ATOM   4327 C C     . SER   B 1 234 ? 22.254  3.375   -3.987 1.00 52.49  ? 360 SER   B C     1 
ATOM   4328 O O     . SER   B 1 234 ? 22.357  4.454   -4.580 1.00 51.38  ? 360 SER   B O     1 
ATOM   4329 C CB    . SER   B 1 234 ? 20.705  3.762   -2.109 1.00 49.11  ? 360 SER   B CB    1 
ATOM   4330 O OG    . SER   B 1 234 ? 21.743  3.460   -1.185 1.00 48.09  ? 360 SER   B OG    1 
ATOM   4331 N N     . GLY   B 1 235 ? 23.287  2.554   -3.814 1.00 51.32  ? 361 GLY   B N     1 
ATOM   4332 C CA    . GLY   B 1 235 ? 24.622  2.931   -4.226 1.00 52.87  ? 361 GLY   B CA    1 
ATOM   4333 C C     . GLY   B 1 235 ? 25.319  3.895   -3.293 1.00 50.85  ? 361 GLY   B C     1 
ATOM   4334 O O     . GLY   B 1 235 ? 26.413  4.372   -3.623 1.00 54.70  ? 361 GLY   B O     1 
ATOM   4335 N N     . ARG   B 1 236 ? 24.713  4.213   -2.151 1.00 49.44  ? 362 ARG   B N     1 
ATOM   4336 C CA    . ARG   B 1 236 ? 25.341  5.013   -1.107 1.00 46.96  ? 362 ARG   B CA    1 
ATOM   4337 C C     . ARG   B 1 236 ? 26.091  4.118   -0.140 1.00 46.46  ? 362 ARG   B C     1 
ATOM   4338 O O     . ARG   B 1 236 ? 25.605  3.049   0.237  1.00 46.72  ? 362 ARG   B O     1 
ATOM   4339 C CB    . ARG   B 1 236 ? 24.287  5.805   -0.334 1.00 43.70  ? 362 ARG   B CB    1 
ATOM   4340 C CG    . ARG   B 1 236 ? 23.373  6.600   -1.240 1.00 50.64  ? 362 ARG   B CG    1 
ATOM   4341 C CD    . ARG   B 1 236 ? 24.103  7.781   -1.814 1.00 50.47  ? 362 ARG   B CD    1 
ATOM   4342 N NE    . ARG   B 1 236 ? 23.339  8.362   -2.907 1.00 51.19  ? 362 ARG   B NE    1 
ATOM   4343 C CZ    . ARG   B 1 236 ? 22.241  9.081   -2.736 1.00 51.02  ? 362 ARG   B CZ    1 
ATOM   4344 N NH1   . ARG   B 1 236 ? 21.787  9.371   -1.524 1.00 51.53  ? 362 ARG   B NH1   1 
ATOM   4345 N NH2   . ARG   B 1 236 ? 21.576  9.505   -3.803 1.00 56.26  ? 362 ARG   B NH2   1 
ATOM   4346 N N     . ARG   B 1 237 ? 27.243  4.597   0.325  1.00 47.08  ? 363 ARG   B N     1 
ATOM   4347 C CA    . ARG   B 1 237 ? 27.984  3.896   1.373  1.00 38.73  ? 363 ARG   B CA    1 
ATOM   4348 C C     . ARG   B 1 237 ? 27.615  4.463   2.744  1.00 40.11  ? 363 ARG   B C     1 
ATOM   4349 O O     . ARG   B 1 237 ? 28.320  5.285   3.330  1.00 43.91  ? 363 ARG   B O     1 
ATOM   4350 C CB    . ARG   B 1 237 ? 29.481  3.991   1.133  1.00 40.59  ? 363 ARG   B CB    1 
ATOM   4351 C CG    . ARG   B 1 237 ? 30.241  3.195   2.152  1.00 37.74  ? 363 ARG   B CG    1 
ATOM   4352 C CD    . ARG   B 1 237 ? 31.692  2.991   1.829  1.00 38.43  ? 363 ARG   B CD    1 
ATOM   4353 N NE    . ARG   B 1 237 ? 32.248  2.079   2.825  1.00 38.34  ? 363 ARG   B NE    1 
ATOM   4354 C CZ    . ARG   B 1 237 ? 33.311  2.324   3.582  1.00 37.70  ? 363 ARG   B CZ    1 
ATOM   4355 N NH1   . ARG   B 1 237 ? 33.987  3.457   3.489  1.00 37.38  ? 363 ARG   B NH1   1 
ATOM   4356 N NH2   . ARG   B 1 237 ? 33.708  1.402   4.451  1.00 37.27  ? 363 ARG   B NH2   1 
ATOM   4357 N N     . ILE   B 1 238 ? 26.522  3.941   3.296  1.00 36.24  ? 364 ILE   B N     1 
ATOM   4358 C CA    . ILE   B 1 238 ? 25.924  4.540   4.477  1.00 33.89  ? 364 ILE   B CA    1 
ATOM   4359 C C     . ILE   B 1 238 ? 26.876  4.433   5.657  1.00 36.11  ? 364 ILE   B C     1 
ATOM   4360 O O     . ILE   B 1 238 ? 27.403  3.356   5.960  1.00 35.03  ? 364 ILE   B O     1 
ATOM   4361 C CB    . ILE   B 1 238 ? 24.571  3.870   4.764  1.00 33.97  ? 364 ILE   B CB    1 
ATOM   4362 C CG1   . ILE   B 1 238 ? 23.728  3.845   3.481  1.00 39.92  ? 364 ILE   B CG1   1 
ATOM   4363 C CG2   . ILE   B 1 238 ? 23.838  4.605   5.883  1.00 34.72  ? 364 ILE   B CG2   1 
ATOM   4364 C CD1   . ILE   B 1 238 ? 22.428  3.067   3.624  1.00 41.80  ? 364 ILE   B CD1   1 
ATOM   4365 N N     . MET   B 1 239 ? 27.129  5.559   6.314  1.00 35.27  ? 365 MET   B N     1 
ATOM   4366 C CA    . MET   B 1 239 ? 27.870  5.523   7.566  1.00 32.88  ? 365 MET   B CA    1 
ATOM   4367 C C     . MET   B 1 239 ? 26.922  5.053   8.652  1.00 35.03  ? 365 MET   B C     1 
ATOM   4368 O O     . MET   B 1 239 ? 25.845  5.629   8.843  1.00 33.78  ? 365 MET   B O     1 
ATOM   4369 C CB    . MET   B 1 239 ? 28.436  6.895   7.900  1.00 32.93  ? 365 MET   B CB    1 
ATOM   4370 C CG    . MET   B 1 239 ? 28.998  7.600   6.697  1.00 36.11  ? 365 MET   B CG    1 
ATOM   4371 S SD    . MET   B 1 239 ? 29.852  9.110   7.147  1.00 39.62  ? 365 MET   B SD    1 
ATOM   4372 C CE    . MET   B 1 239 ? 28.746  9.834   8.362  1.00 40.35  ? 365 MET   B CE    1 
ATOM   4373 N N     . VAL   B 1 240 ? 27.303  3.986   9.346  1.00 31.41  ? 366 VAL   B N     1 
ATOM   4374 C CA    . VAL   B 1 240 ? 26.452  3.367   10.345 1.00 30.81  ? 366 VAL   B CA    1 
ATOM   4375 C C     . VAL   B 1 240 ? 27.166  3.497   11.671 1.00 27.65  ? 366 VAL   B C     1 
ATOM   4376 O O     . VAL   B 1 240 ? 28.223  2.892   11.879 1.00 31.16  ? 366 VAL   B O     1 
ATOM   4377 C CB    . VAL   B 1 240 ? 26.151  1.901   10.033 1.00 31.77  ? 366 VAL   B CB    1 
ATOM   4378 C CG1   . VAL   B 1 240 ? 25.278  1.319   11.128 1.00 29.35  ? 366 VAL   B CG1   1 
ATOM   4379 C CG2   . VAL   B 1 240 ? 25.447  1.807   8.705  1.00 30.17  ? 366 VAL   B CG2   1 
ATOM   4380 N N     . ARG   B 1 241 ? 26.629  4.322   12.543 1.00 26.10  ? 367 ARG   B N     1 
ATOM   4381 C CA    . ARG   B 1 241 ? 27.172  4.426   13.894 1.00 26.05  ? 367 ARG   B CA    1 
ATOM   4382 C C     . ARG   B 1 241 ? 26.453  3.429   14.787 1.00 29.64  ? 367 ARG   B C     1 
ATOM   4383 O O     . ARG   B 1 241 ? 25.256  3.566   15.049 1.00 29.20  ? 367 ARG   B O     1 
ATOM   4384 C CB    . ARG   B 1 241 ? 27.031  5.830   14.453 1.00 29.23  ? 367 ARG   B CB    1 
ATOM   4385 C CG    . ARG   B 1 241 ? 27.617  5.898   15.882 1.00 26.69  ? 367 ARG   B CG    1 
ATOM   4386 C CD    . ARG   B 1 241 ? 27.122  7.133   16.601 1.00 30.73  ? 367 ARG   B CD    1 
ATOM   4387 N NE    . ARG   B 1 241 ? 27.572  8.343   15.926 1.00 33.17  ? 367 ARG   B NE    1 
ATOM   4388 C CZ    . ARG   B 1 241 ? 26.928  9.501   15.974 1.00 33.69  ? 367 ARG   B CZ    1 
ATOM   4389 N NH1   . ARG   B 1 241 ? 25.813  9.642   16.672 1.00 34.37  ? 367 ARG   B NH1   1 
ATOM   4390 N NH2   . ARG   B 1 241 ? 27.401  10.536  15.284 1.00 36.29  ? 367 ARG   B NH2   1 
ATOM   4391 N N     . LEU   B 1 242 ? 27.189  2.429   15.268 1.00 27.96  ? 368 LEU   B N     1 
ATOM   4392 C CA    . LEU   B 1 242 ? 26.636  1.443   16.178 1.00 28.12  ? 368 LEU   B CA    1 
ATOM   4393 C C     . LEU   B 1 242 ? 26.889  1.928   17.596 1.00 26.31  ? 368 LEU   B C     1 
ATOM   4394 O O     . LEU   B 1 242 ? 28.049  2.098   17.989 1.00 27.73  ? 368 LEU   B O     1 
ATOM   4395 C CB    . LEU   B 1 242 ? 27.295  0.084   15.965 1.00 27.88  ? 368 LEU   B CB    1 
ATOM   4396 C CG    . LEU   B 1 242 ? 26.668  -1.050  16.775 1.00 25.84  ? 368 LEU   B CG    1 
ATOM   4397 C CD1   . LEU   B 1 242 ? 25.222  -1.252  16.300 1.00 31.42  ? 368 LEU   B CD1   1 
ATOM   4398 C CD2   . LEU   B 1 242 ? 27.513  -2.301  16.552 1.00 30.62  ? 368 LEU   B CD2   1 
ATOM   4399 N N     . VAL   B 1 243 ? 25.821  2.190   18.339 1.00 26.90  ? 369 VAL   B N     1 
ATOM   4400 C CA    . VAL   B 1 243 ? 25.924  2.523   19.754 1.00 27.09  ? 369 VAL   B CA    1 
ATOM   4401 C C     . VAL   B 1 243 ? 25.219  1.428   20.550 1.00 26.80  ? 369 VAL   B C     1 
ATOM   4402 O O     . VAL   B 1 243 ? 24.454  0.624   20.010 1.00 29.74  ? 369 VAL   B O     1 
ATOM   4403 C CB    . VAL   B 1 243 ? 25.335  3.911   20.085 1.00 28.35  ? 369 VAL   B CB    1 
ATOM   4404 C CG1   . VAL   B 1 243 ? 25.946  4.994   19.218 1.00 28.35  ? 369 VAL   B CG1   1 
ATOM   4405 C CG2   . VAL   B 1 243 ? 23.826  3.902   19.902 1.00 28.89  ? 369 VAL   B CG2   1 
ATOM   4406 N N     . LYS   B 1 244 ? 25.506  1.364   21.848 1.00 27.14  ? 370 LYS   B N     1 
ATOM   4407 C CA    . LYS   B 1 244 ? 24.662  0.487   22.639 1.00 27.39  ? 370 LYS   B CA    1 
ATOM   4408 C C     . LYS   B 1 244 ? 23.310  1.126   22.902 1.00 30.30  ? 370 LYS   B C     1 
ATOM   4409 O O     . LYS   B 1 244 ? 22.289  0.450   22.790 1.00 35.39  ? 370 LYS   B O     1 
ATOM   4410 C CB    . LYS   B 1 244 ? 25.371  0.076   23.940 1.00 28.43  ? 370 LYS   B CB    1 
ATOM   4411 C CG    . LYS   B 1 244 ? 26.568  -0.763  23.520 1.00 28.65  ? 370 LYS   B CG    1 
ATOM   4412 C CD    . LYS   B 1 244 ? 27.376  -1.282  24.667 1.00 27.80  ? 370 LYS   B CD    1 
ATOM   4413 C CE    . LYS   B 1 244 ? 28.629  -1.994  24.128 1.00 28.54  ? 370 LYS   B CE    1 
ATOM   4414 N NZ    . LYS   B 1 244 ? 29.508  -2.355  25.313 1.00 32.63  ? 370 LYS   B NZ    1 
ATOM   4415 N N     . GLY   B 1 245 ? 23.274  2.422   23.202 1.00 31.00  ? 371 GLY   B N     1 
ATOM   4416 C CA    . GLY   B 1 245 ? 21.996  3.093   23.386 1.00 31.42  ? 371 GLY   B CA    1 
ATOM   4417 C C     . GLY   B 1 245 ? 21.955  3.962   24.628 1.00 32.94  ? 371 GLY   B C     1 
ATOM   4418 O O     . GLY   B 1 245 ? 22.361  3.522   25.709 1.00 33.69  ? 371 GLY   B O     1 
ATOM   4419 N N     . ALA   B 1 246 ? 21.432  5.185   24.506 1.00 32.20  ? 372 ALA   B N     1 
ATOM   4420 C CA    . ALA   B 1 246 ? 21.514  6.185   25.571 1.00 31.63  ? 372 ALA   B CA    1 
ATOM   4421 C C     . ALA   B 1 246 ? 20.268  6.298   26.447 1.00 35.92  ? 372 ALA   B C     1 
ATOM   4422 O O     . ALA   B 1 246 ? 20.302  7.022   27.454 1.00 36.95  ? 372 ALA   B O     1 
ATOM   4423 C CB    . ALA   B 1 246 ? 21.790  7.571   24.970 1.00 36.63  ? 372 ALA   B CB    1 
ATOM   4424 N N     . TYR   B 1 247 ? 19.181  5.606   26.111 1.00 35.93  ? 373 TYR   B N     1 
ATOM   4425 C CA    . TYR   B 1 247 ? 17.884  5.875   26.725 1.00 36.26  ? 373 TYR   B CA    1 
ATOM   4426 C C     . TYR   B 1 247 ? 17.350  4.688   27.508 1.00 38.63  ? 373 TYR   B C     1 
ATOM   4427 O O     . TYR   B 1 247 ? 16.138  4.564   27.692 1.00 40.86  ? 373 TYR   B O     1 
ATOM   4428 C CB    . TYR   B 1 247 ? 16.864  6.266   25.660 1.00 37.12  ? 373 TYR   B CB    1 
ATOM   4429 C CG    . TYR   B 1 247 ? 17.253  7.453   24.825 1.00 39.79  ? 373 TYR   B CG    1 
ATOM   4430 C CD1   . TYR   B 1 247 ? 18.029  7.294   23.683 1.00 36.68  ? 373 TYR   B CD1   1 
ATOM   4431 C CD2   . TYR   B 1 247 ? 16.820  8.740   25.163 1.00 43.95  ? 373 TYR   B CD2   1 
ATOM   4432 C CE1   . TYR   B 1 247 ? 18.387  8.387   22.901 1.00 39.94  ? 373 TYR   B CE1   1 
ATOM   4433 C CE2   . TYR   B 1 247 ? 17.173  9.838   24.388 1.00 43.98  ? 373 TYR   B CE2   1 
ATOM   4434 C CZ    . TYR   B 1 247 ? 17.949  9.650   23.257 1.00 39.91  ? 373 TYR   B CZ    1 
ATOM   4435 O OH    . TYR   B 1 247 ? 18.319  10.715  22.477 1.00 41.17  ? 373 TYR   B OH    1 
ATOM   4436 N N     . TRP   B 1 248 ? 18.234  3.822   28.006 1.00 40.23  ? 374 TRP   B N     1 
ATOM   4437 C CA    . TRP   B 1 248 ? 17.767  2.551   28.549 1.00 41.54  ? 374 TRP   B CA    1 
ATOM   4438 C C     . TRP   B 1 248 ? 16.793  2.749   29.706 1.00 42.76  ? 374 TRP   B C     1 
ATOM   4439 O O     . TRP   B 1 248 ? 15.718  2.131   29.746 1.00 42.31  ? 374 TRP   B O     1 
ATOM   4440 C CB    . TRP   B 1 248 ? 18.951  1.694   28.991 1.00 40.64  ? 374 TRP   B CB    1 
ATOM   4441 C CG    . TRP   B 1 248 ? 18.482  0.365   29.443 1.00 40.59  ? 374 TRP   B CG    1 
ATOM   4442 C CD1   . TRP   B 1 248 ? 18.239  -0.713  28.655 1.00 41.04  ? 374 TRP   B CD1   1 
ATOM   4443 C CD2   . TRP   B 1 248 ? 18.194  -0.038  30.784 1.00 42.38  ? 374 TRP   B CD2   1 
ATOM   4444 N NE1   . TRP   B 1 248 ? 17.798  -1.762  29.415 1.00 36.56  ? 374 TRP   B NE1   1 
ATOM   4445 C CE2   . TRP   B 1 248 ? 17.771  -1.379  30.730 1.00 40.41  ? 374 TRP   B CE2   1 
ATOM   4446 C CE3   . TRP   B 1 248 ? 18.229  0.611   32.029 1.00 42.91  ? 374 TRP   B CE3   1 
ATOM   4447 C CZ2   . TRP   B 1 248 ? 17.399  -2.091  31.871 1.00 42.97  ? 374 TRP   B CZ2   1 
ATOM   4448 C CZ3   . TRP   B 1 248 ? 17.867  -0.097  33.152 1.00 46.21  ? 374 TRP   B CZ3   1 
ATOM   4449 C CH2   . TRP   B 1 248 ? 17.455  -1.436  33.069 1.00 46.19  ? 374 TRP   B CH2   1 
ATOM   4450 N N     . ASP   B 1 249 ? 17.147  3.604   30.668 1.00 44.98  ? 375 ASP   B N     1 
ATOM   4451 C CA    . ASP   B 1 249 ? 16.266  3.798   31.816 1.00 46.39  ? 375 ASP   B CA    1 
ATOM   4452 C C     . ASP   B 1 249 ? 14.929  4.373   31.379 1.00 43.90  ? 375 ASP   B C     1 
ATOM   4453 O O     . ASP   B 1 249 ? 13.872  3.975   31.889 1.00 49.61  ? 375 ASP   B O     1 
ATOM   4454 C CB    . ASP   B 1 249 ? 16.932  4.707   32.849 1.00 51.90  ? 375 ASP   B CB    1 
ATOM   4455 C CG    . ASP   B 1 249 ? 18.066  4.013   33.586 1.00 53.47  ? 375 ASP   B CG    1 
ATOM   4456 O OD1   . ASP   B 1 249 ? 17.788  3.027   34.303 1.00 57.64  ? 375 ASP   B OD1   1 
ATOM   4457 O OD2   . ASP   B 1 249 ? 19.232  4.439   33.427 1.00 56.62  ? 375 ASP   B OD2   1 
ATOM   4458 N N     . ALA   B 1 250 ? 14.961  5.299   30.422 1.00 47.97  ? 376 ALA   B N     1 
ATOM   4459 C CA    . ALA   B 1 250 ? 13.733  5.901   29.923 1.00 49.24  ? 376 ALA   B CA    1 
ATOM   4460 C C     . ALA   B 1 250 ? 12.875  4.877   29.196 1.00 47.22  ? 376 ALA   B C     1 
ATOM   4461 O O     . ALA   B 1 250 ? 11.661  4.813   29.420 1.00 51.25  ? 376 ALA   B O     1 
ATOM   4462 C CB    . ALA   B 1 250 ? 14.066  7.080   29.017 1.00 47.52  ? 376 ALA   B CB    1 
ATOM   4463 N N     . GLU   B 1 251 ? 13.494  4.046   28.350 1.00 46.81  ? 377 GLU   B N     1 
ATOM   4464 C CA    . GLU   B 1 251 ? 12.750  3.014   27.632 1.00 49.08  ? 377 GLU   B CA    1 
ATOM   4465 C C     . GLU   B 1 251 ? 12.075  2.037   28.585 1.00 47.38  ? 377 GLU   B C     1 
ATOM   4466 O O     . GLU   B 1 251 ? 10.929  1.635   28.359 1.00 49.21  ? 377 GLU   B O     1 
ATOM   4467 C CB    . GLU   B 1 251 ? 13.683  2.258   26.682 1.00 41.07  ? 377 GLU   B CB    1 
ATOM   4468 C CG    . GLU   B 1 251 ? 14.280  3.099   25.579 1.00 42.27  ? 377 GLU   B CG    1 
ATOM   4469 C CD    . GLU   B 1 251 ? 13.270  3.511   24.513 1.00 45.45  ? 377 GLU   B CD    1 
ATOM   4470 O OE1   . GLU   B 1 251 ? 12.062  3.223   24.641 1.00 48.02  ? 377 GLU   B OE1   1 
ATOM   4471 O OE2   . GLU   B 1 251 ? 13.705  4.133   23.532 1.00 48.69  ? 377 GLU   B OE2   1 
ATOM   4472 N N     . ILE   B 1 252 ? 12.783  1.609   29.637 1.00 46.49  ? 378 ILE   B N     1 
ATOM   4473 C CA    . ILE   B 1 252 ? 12.163  0.733   30.624 1.00 48.95  ? 378 ILE   B CA    1 
ATOM   4474 C C     . ILE   B 1 252 ? 10.952  1.413   31.237 1.00 51.72  ? 378 ILE   B C     1 
ATOM   4475 O O     . ILE   B 1 252 ? 9.886   0.804   31.386 1.00 53.38  ? 378 ILE   B O     1 
ATOM   4476 C CB    . ILE   B 1 252 ? 13.178  0.327   31.710 1.00 48.01  ? 378 ILE   B CB    1 
ATOM   4477 C CG1   . ILE   B 1 252 ? 14.304  -0.516  31.108 1.00 47.66  ? 378 ILE   B CG1   1 
ATOM   4478 C CG2   . ILE   B 1 252 ? 12.479  -0.417  32.853 1.00 52.40  ? 378 ILE   B CG2   1 
ATOM   4479 C CD1   . ILE   B 1 252 ? 13.824  -1.594  30.154 1.00 51.80  ? 378 ILE   B CD1   1 
ATOM   4480 N N     . LYS   B 1 253 ? 11.087  2.695   31.574 1.00 50.51  ? 379 LYS   B N     1 
ATOM   4481 C CA    . LYS   B 1 253 ? 10.005  3.392   32.262 1.00 54.59  ? 379 LYS   B CA    1 
ATOM   4482 C C     . LYS   B 1 253 ? 8.827   3.638   31.328 1.00 57.14  ? 379 LYS   B C     1 
ATOM   4483 O O     . LYS   B 1 253 ? 7.667   3.579   31.755 1.00 61.82  ? 379 LYS   B O     1 
ATOM   4484 C CB    . LYS   B 1 253 ? 10.522  4.706   32.843 1.00 57.59  ? 379 LYS   B CB    1 
ATOM   4485 N N     . ARG   B 1 254 ? 9.105   3.899   30.048 1.00 58.96  ? 380 ARG   B N     1 
ATOM   4486 C CA    . ARG   B 1 254 ? 8.037   4.118   29.077 1.00 60.60  ? 380 ARG   B CA    1 
ATOM   4487 C C     . ARG   B 1 254 ? 7.265   2.832   28.800 1.00 58.50  ? 380 ARG   B C     1 
ATOM   4488 O O     . ARG   B 1 254 ? 6.031   2.850   28.714 1.00 61.23  ? 380 ARG   B O     1 
ATOM   4489 C CB    . ARG   B 1 254 ? 8.633   4.686   27.788 1.00 64.32  ? 380 ARG   B CB    1 
ATOM   4490 C CG    . ARG   B 1 254 ? 7.672   4.764   26.617 1.00 65.78  ? 380 ARG   B CG    1 
ATOM   4491 C CD    . ARG   B 1 254 ? 8.350   5.426   25.437 1.00 70.87  ? 380 ARG   B CD    1 
ATOM   4492 N NE    . ARG   B 1 254 ? 8.546   6.852   25.670 1.00 75.40  ? 380 ARG   B NE    1 
ATOM   4493 C CZ    . ARG   B 1 254 ? 8.977   7.705   24.752 1.00 70.12  ? 380 ARG   B CZ    1 
ATOM   4494 N NH1   . ARG   B 1 254 ? 9.284   7.303   23.530 1.00 65.46  ? 380 ARG   B NH1   1 
ATOM   4495 N NH2   . ARG   B 1 254 ? 9.089   8.995   25.062 1.00 72.42  ? 380 ARG   B NH2   1 
ATOM   4496 N N     . ALA   B 1 255 ? 7.977   1.709   28.656 1.00 60.73  ? 381 ALA   B N     1 
ATOM   4497 C CA    . ALA   B 1 255 ? 7.327   0.429   28.389 1.00 60.73  ? 381 ALA   B CA    1 
ATOM   4498 C C     . ALA   B 1 255 ? 6.398   0.034   29.524 1.00 63.40  ? 381 ALA   B C     1 
ATOM   4499 O O     . ALA   B 1 255 ? 5.280   -0.436  29.286 1.00 63.59  ? 381 ALA   B O     1 
ATOM   4500 C CB    . ALA   B 1 255 ? 8.378   -0.659  28.159 1.00 56.01  ? 381 ALA   B CB    1 
ATOM   4501 N N     . GLN   B 1 256 ? 6.841   0.215   30.770 1.00 63.18  ? 382 GLN   B N     1 
ATOM   4502 C CA    . GLN   B 1 256 ? 5.972   -0.069  31.906 1.00 61.87  ? 382 GLN   B CA    1 
ATOM   4503 C C     . GLN   B 1 256 ? 4.782   0.888   31.955 1.00 65.54  ? 382 GLN   B C     1 
ATOM   4504 O O     . GLN   B 1 256 ? 3.648   0.465   32.214 1.00 69.01  ? 382 GLN   B O     1 
ATOM   4505 C CB    . GLN   B 1 256 ? 6.784   -0.009  33.199 1.00 66.52  ? 382 GLN   B CB    1 
ATOM   4506 C CG    . GLN   B 1 256 ? 7.908   -1.042  33.258 1.00 64.34  ? 382 GLN   B CG    1 
ATOM   4507 C CD    . GLN   B 1 256 ? 8.846   -0.839  34.441 1.00 68.25  ? 382 GLN   B CD    1 
ATOM   4508 O OE1   . GLN   B 1 256 ? 9.184   0.293   34.800 1.00 65.52  ? 382 GLN   B OE1   1 
ATOM   4509 N NE2   . GLN   B 1 256 ? 9.270   -1.941  35.052 1.00 69.72  ? 382 GLN   B NE2   1 
ATOM   4510 N N     . LEU   B 1 257 ? 5.011   2.179   31.704 1.00 65.16  ? 383 LEU   B N     1 
ATOM   4511 C CA    . LEU   B 1 257 ? 3.899   3.130   31.734 1.00 68.98  ? 383 LEU   B CA    1 
ATOM   4512 C C     . LEU   B 1 257 ? 2.984   2.993   30.520 1.00 70.24  ? 383 LEU   B C     1 
ATOM   4513 O O     . LEU   B 1 257 ? 1.776   3.230   30.642 1.00 74.33  ? 383 LEU   B O     1 
ATOM   4514 C CB    . LEU   B 1 257 ? 4.417   4.567   31.834 1.00 70.36  ? 383 LEU   B CB    1 
ATOM   4515 N N     . ASP   B 1 258 ? 3.526   2.616   29.352 1.00 67.12  ? 384 ASP   B N     1 
ATOM   4516 C CA    . ASP   B 1 258 ? 2.681   2.304   28.200 1.00 68.45  ? 384 ASP   B CA    1 
ATOM   4517 C C     . ASP   B 1 258 ? 1.940   0.980   28.359 1.00 70.37  ? 384 ASP   B C     1 
ATOM   4518 O O     . ASP   B 1 258 ? 1.104   0.652   27.507 1.00 72.24  ? 384 ASP   B O     1 
ATOM   4519 C CB    . ASP   B 1 258 ? 3.505   2.270   26.907 1.00 68.87  ? 384 ASP   B CB    1 
ATOM   4520 C CG    . ASP   B 1 258 ? 3.846   3.659   26.386 1.00 67.36  ? 384 ASP   B CG    1 
ATOM   4521 O OD1   . ASP   B 1 258 ? 3.373   4.653   26.979 1.00 70.70  ? 384 ASP   B OD1   1 
ATOM   4522 O OD2   . ASP   B 1 258 ? 4.595   3.754   25.391 1.00 76.95  ? 384 ASP   B OD2   1 
ATOM   4523 N N     . GLY   B 1 259 ? 2.231   0.215   29.414 1.00 70.20  ? 385 GLY   B N     1 
ATOM   4524 C CA    . GLY   B 1 259 ? 1.531   -1.023  29.694 1.00 72.43  ? 385 GLY   B CA    1 
ATOM   4525 C C     . GLY   B 1 259 ? 2.048   -2.236  28.957 1.00 70.03  ? 385 GLY   B C     1 
ATOM   4526 O O     . GLY   B 1 259 ? 1.376   -3.273  28.959 1.00 72.23  ? 385 GLY   B O     1 
ATOM   4527 N N     . LEU   B 1 260 ? 3.216   -2.143  28.334 1.00 65.92  ? 386 LEU   B N     1 
ATOM   4528 C CA    . LEU   B 1 260 ? 3.746   -3.251  27.555 1.00 66.45  ? 386 LEU   B CA    1 
ATOM   4529 C C     . LEU   B 1 260 ? 4.127   -4.416  28.463 1.00 67.20  ? 386 LEU   B C     1 
ATOM   4530 O O     . LEU   B 1 260 ? 4.553   -4.232  29.605 1.00 69.17  ? 386 LEU   B O     1 
ATOM   4531 C CB    . LEU   B 1 260 ? 4.965   -2.802  26.747 1.00 66.70  ? 386 LEU   B CB    1 
ATOM   4532 C CG    . LEU   B 1 260 ? 4.797   -1.509  25.946 1.00 65.72  ? 386 LEU   B CG    1 
ATOM   4533 C CD1   . LEU   B 1 260 ? 5.995   -1.248  25.049 1.00 59.69  ? 386 LEU   B CD1   1 
ATOM   4534 C CD2   . LEU   B 1 260 ? 3.528   -1.554  25.137 1.00 65.15  ? 386 LEU   B CD2   1 
ATOM   4535 N N     . ALA   B 1 261 ? 3.954   -5.628  27.940 1.00 65.75  ? 387 ALA   B N     1 
ATOM   4536 C CA    . ALA   B 1 261 ? 4.389   -6.840  28.619 1.00 66.74  ? 387 ALA   B CA    1 
ATOM   4537 C C     . ALA   B 1 261 ? 5.815   -7.238  28.252 1.00 67.66  ? 387 ALA   B C     1 
ATOM   4538 O O     . ALA   B 1 261 ? 6.401   -8.080  28.937 1.00 70.93  ? 387 ALA   B O     1 
ATOM   4539 C CB    . ALA   B 1 261 ? 3.429   -7.993  28.302 1.00 67.38  ? 387 ALA   B CB    1 
ATOM   4540 N N     . ASP   B 1 262 ? 6.378   -6.655  27.197 1.00 61.88  ? 388 ASP   B N     1 
ATOM   4541 C CA    . ASP   B 1 262 ? 7.731   -6.956  26.738 1.00 62.30  ? 388 ASP   B CA    1 
ATOM   4542 C C     . ASP   B 1 262 ? 8.357   -5.691  26.168 1.00 63.25  ? 388 ASP   B C     1 
ATOM   4543 O O     . ASP   B 1 262 ? 7.718   -4.964  25.397 1.00 63.42  ? 388 ASP   B O     1 
ATOM   4544 C CB    . ASP   B 1 262 ? 7.754   -8.062  25.671 1.00 67.99  ? 388 ASP   B CB    1 
ATOM   4545 C CG    . ASP   B 1 262 ? 8.082   -9.435  26.249 1.00 73.59  ? 388 ASP   B CG    1 
ATOM   4546 O OD1   . ASP   B 1 262 ? 8.911   -9.507  27.185 1.00 79.35  ? 388 ASP   B OD1   1 
ATOM   4547 O OD2   . ASP   B 1 262 ? 7.514   -10.444 25.769 1.00 69.61  ? 388 ASP   B OD2   1 
ATOM   4548 N N     . PHE   B 1 263 ? 9.627   -5.472  26.512 1.00 58.26  ? 389 PHE   B N     1 
ATOM   4549 C CA    . PHE   B 1 263 ? 10.357  -4.246  26.235 1.00 54.02  ? 389 PHE   B CA    1 
ATOM   4550 C C     . PHE   B 1 263 ? 10.930  -4.233  24.822 1.00 48.99  ? 389 PHE   B C     1 
ATOM   4551 O O     . PHE   B 1 263 ? 11.149  -5.282  24.217 1.00 50.28  ? 389 PHE   B O     1 
ATOM   4552 C CB    . PHE   B 1 263 ? 11.501  -4.091  27.235 1.00 53.63  ? 389 PHE   B CB    1 
ATOM   4553 C CG    . PHE   B 1 263 ? 11.066  -4.156  28.661 1.00 54.45  ? 389 PHE   B CG    1 
ATOM   4554 C CD1   . PHE   B 1 263 ? 10.690  -3.009  29.331 1.00 52.61  ? 389 PHE   B CD1   1 
ATOM   4555 C CD2   . PHE   B 1 263 ? 11.031  -5.370  29.336 1.00 56.62  ? 389 PHE   B CD2   1 
ATOM   4556 C CE1   . PHE   B 1 263 ? 10.280  -3.068  30.650 1.00 56.50  ? 389 PHE   B CE1   1 
ATOM   4557 C CE2   . PHE   B 1 263 ? 10.618  -5.438  30.651 1.00 57.14  ? 389 PHE   B CE2   1 
ATOM   4558 C CZ    . PHE   B 1 263 ? 10.242  -4.286  31.311 1.00 60.03  ? 389 PHE   B CZ    1 
ATOM   4559 N N     . PRO   B 1 264 ? 11.185  -3.044  24.269 1.00 47.19  ? 390 PRO   B N     1 
ATOM   4560 C CA    . PRO   B 1 264 ? 11.854  -2.969  22.963 1.00 46.12  ? 390 PRO   B CA    1 
ATOM   4561 C C     . PRO   B 1 264 ? 13.361  -3.088  23.055 1.00 44.45  ? 390 PRO   B C     1 
ATOM   4562 O O     . PRO   B 1 264 ? 14.027  -3.251  22.022 1.00 43.53  ? 390 PRO   B O     1 
ATOM   4563 C CB    . PRO   B 1 264 ? 11.443  -1.583  22.442 1.00 50.29  ? 390 PRO   B CB    1 
ATOM   4564 C CG    . PRO   B 1 264 ? 11.226  -0.774  23.696 1.00 49.52  ? 390 PRO   B CG    1 
ATOM   4565 C CD    . PRO   B 1 264 ? 10.633  -1.744  24.694 1.00 45.58  ? 390 PRO   B CD    1 
ATOM   4566 N N     . VAL   B 1 265 ? 13.905  -3.015  24.266 1.00 43.48  ? 391 VAL   B N     1 
ATOM   4567 C CA    . VAL   B 1 265 ? 15.328  -3.068  24.528 1.00 43.47  ? 391 VAL   B CA    1 
ATOM   4568 C C     . VAL   B 1 265 ? 15.605  -4.255  25.436 1.00 40.65  ? 391 VAL   B C     1 
ATOM   4569 O O     . VAL   B 1 265 ? 14.715  -4.776  26.112 1.00 41.95  ? 391 VAL   B O     1 
ATOM   4570 C CB    . VAL   B 1 265 ? 15.847  -1.765  25.170 1.00 41.47  ? 391 VAL   B CB    1 
ATOM   4571 C CG1   . VAL   B 1 265 ? 15.641  -0.597  24.222 1.00 37.25  ? 391 VAL   B CG1   1 
ATOM   4572 C CG2   . VAL   B 1 265 ? 15.135  -1.507  26.493 1.00 43.01  ? 391 VAL   B CG2   1 
ATOM   4573 N N     . PHE   B 1 266 ? 16.868  -4.675  25.450 1.00 40.26  ? 392 PHE   B N     1 
ATOM   4574 C CA    . PHE   B 1 266 ? 17.282  -5.719  26.368 1.00 39.87  ? 392 PHE   B CA    1 
ATOM   4575 C C     . PHE   B 1 266 ? 17.248  -5.212  27.813 1.00 42.70  ? 392 PHE   B C     1 
ATOM   4576 O O     . PHE   B 1 266 ? 17.347  -4.015  28.094 1.00 43.37  ? 392 PHE   B O     1 
ATOM   4577 C CB    . PHE   B 1 266 ? 18.680  -6.224  26.015 1.00 39.91  ? 392 PHE   B CB    1 
ATOM   4578 C CG    . PHE   B 1 266 ? 18.766  -6.828  24.645 1.00 38.33  ? 392 PHE   B CG    1 
ATOM   4579 C CD1   . PHE   B 1 266 ? 18.056  -7.975  24.331 1.00 43.17  ? 392 PHE   B CD1   1 
ATOM   4580 C CD2   . PHE   B 1 266 ? 19.555  -6.249  23.675 1.00 35.98  ? 392 PHE   B CD2   1 
ATOM   4581 C CE1   . PHE   B 1 266 ? 18.128  -8.528  23.052 1.00 43.03  ? 392 PHE   B CE1   1 
ATOM   4582 C CE2   . PHE   B 1 266 ? 19.634  -6.800  22.388 1.00 39.03  ? 392 PHE   B CE2   1 
ATOM   4583 C CZ    . PHE   B 1 266 ? 18.917  -7.934  22.084 1.00 40.61  ? 392 PHE   B CZ    1 
ATOM   4584 N N     . THR   B 1 267 ? 17.088  -6.147  28.732 1.00 41.22  ? 393 THR   B N     1 
ATOM   4585 C CA    . THR   B 1 267 ? 17.055  -5.829  30.152 1.00 40.84  ? 393 THR   B CA    1 
ATOM   4586 C C     . THR   B 1 267 ? 18.282  -6.316  30.903 1.00 41.90  ? 393 THR   B C     1 
ATOM   4587 O O     . THR   B 1 267 ? 18.446  -5.967  32.076 1.00 43.91  ? 393 THR   B O     1 
ATOM   4588 C CB    . THR   B 1 267 ? 15.797  -6.416  30.801 1.00 47.67  ? 393 THR   B CB    1 
ATOM   4589 O OG1   . THR   B 1 267 ? 15.794  -7.843  30.644 1.00 49.33  ? 393 THR   B OG1   1 
ATOM   4590 C CG2   . THR   B 1 267 ? 14.544  -5.816  30.160 1.00 49.88  ? 393 THR   B CG2   1 
ATOM   4591 N N     . ARG   B 1 268 ? 19.137  -7.116  30.277 1.00 43.94  ? 394 ARG   B N     1 
ATOM   4592 C CA    . ARG   B 1 268 ? 20.397  -7.529  30.877 1.00 39.59  ? 394 ARG   B CA    1 
ATOM   4593 C C     . ARG   B 1 268 ? 21.522  -6.855  30.112 1.00 37.63  ? 394 ARG   B C     1 
ATOM   4594 O O     . ARG   B 1 268 ? 21.581  -6.937  28.885 1.00 40.72  ? 394 ARG   B O     1 
ATOM   4595 C CB    . ARG   B 1 268 ? 20.551  -9.053  30.858 1.00 44.03  ? 394 ARG   B CB    1 
ATOM   4596 N N     . LYS   B 1 269 ? 22.395  -6.162  30.840 1.00 42.18  ? 395 LYS   B N     1 
ATOM   4597 C CA    . LYS   B 1 269 ? 23.410  -5.345  30.190 1.00 39.54  ? 395 LYS   B CA    1 
ATOM   4598 C C     . LYS   B 1 269 ? 24.304  -6.187  29.289 1.00 38.44  ? 395 LYS   B C     1 
ATOM   4599 O O     . LYS   B 1 269 ? 24.710  -5.743  28.214 1.00 37.43  ? 395 LYS   B O     1 
ATOM   4600 C CB    . LYS   B 1 269 ? 24.230  -4.608  31.246 1.00 37.61  ? 395 LYS   B CB    1 
ATOM   4601 C CG    . LYS   B 1 269 ? 25.080  -3.480  30.675 1.00 35.48  ? 395 LYS   B CG    1 
ATOM   4602 C CD    . LYS   B 1 269 ? 26.473  -3.940  30.329 1.00 35.39  ? 395 LYS   B CD    1 
ATOM   4603 C CE    . LYS   B 1 269 ? 27.318  -2.786  29.814 1.00 35.62  ? 395 LYS   B CE    1 
ATOM   4604 N NZ    . LYS   B 1 269 ? 28.558  -3.286  29.177 1.00 34.63  ? 395 LYS   B NZ    1 
ATOM   4605 N N     . ILE   B 1 270 ? 24.608  -7.415  29.707 1.00 40.08  ? 396 ILE   B N     1 
ATOM   4606 C CA    . ILE   B 1 270 ? 25.467  -8.263  28.888 1.00 38.91  ? 396 ILE   B CA    1 
ATOM   4607 C C     . ILE   B 1 270 ? 24.767  -8.665  27.596 1.00 37.95  ? 396 ILE   B C     1 
ATOM   4608 O O     . ILE   B 1 270 ? 25.421  -9.002  26.605 1.00 38.86  ? 396 ILE   B O     1 
ATOM   4609 C CB    . ILE   B 1 270 ? 25.903  -9.489  29.705 1.00 42.87  ? 396 ILE   B CB    1 
ATOM   4610 C CG1   . ILE   B 1 270 ? 27.025  -10.236 28.993 1.00 48.25  ? 396 ILE   B CG1   1 
ATOM   4611 C CG2   . ILE   B 1 270 ? 24.715  -10.401 29.968 1.00 44.62  ? 396 ILE   B CG2   1 
ATOM   4612 C CD1   . ILE   B 1 270 ? 27.686  -11.299 29.873 1.00 51.70  ? 396 ILE   B CD1   1 
ATOM   4613 N N     . HIS   B 1 271 ? 23.438  -8.665  27.578 1.00 38.31  ? 397 HIS   B N     1 
ATOM   4614 C CA    . HIS   B 1 271 ? 22.744  -8.938  26.328 1.00 39.03  ? 397 HIS   B CA    1 
ATOM   4615 C C     . HIS   B 1 271 ? 22.998  -7.826  25.324 1.00 36.34  ? 397 HIS   B C     1 
ATOM   4616 O O     . HIS   B 1 271 ? 23.192  -8.081  24.132 1.00 34.57  ? 397 HIS   B O     1 
ATOM   4617 C CB    . HIS   B 1 271 ? 21.250  -9.095  26.581 1.00 40.42  ? 397 HIS   B CB    1 
ATOM   4618 C CG    . HIS   B 1 271 ? 20.890  -10.343 27.322 1.00 44.78  ? 397 HIS   B CG    1 
ATOM   4619 N ND1   . HIS   B 1 271 ? 19.598  -10.633 27.708 1.00 44.86  ? 397 HIS   B ND1   1 
ATOM   4620 C CD2   . HIS   B 1 271 ? 21.651  -11.383 27.733 1.00 41.72  ? 397 HIS   B CD2   1 
ATOM   4621 C CE1   . HIS   B 1 271 ? 19.583  -11.794 28.340 1.00 48.97  ? 397 HIS   B CE1   1 
ATOM   4622 N NE2   . HIS   B 1 271 ? 20.815  -12.272 28.362 1.00 48.39  ? 397 HIS   B NE2   1 
ATOM   4623 N N     . THR   B 1 272 ? 23.015  -6.585  25.795 1.00 35.72  ? 398 THR   B N     1 
ATOM   4624 C CA    . THR   B 1 272 ? 23.381  -5.486  24.919 1.00 32.58  ? 398 THR   B CA    1 
ATOM   4625 C C     . THR   B 1 272 ? 24.815  -5.627  24.438 1.00 34.33  ? 398 THR   B C     1 
ATOM   4626 O O     . THR   B 1 272 ? 25.115  -5.290  23.286 1.00 33.31  ? 398 THR   B O     1 
ATOM   4627 C CB    . THR   B 1 272 ? 23.163  -4.168  25.651 1.00 31.87  ? 398 THR   B CB    1 
ATOM   4628 O OG1   . THR   B 1 272 ? 21.754  -4.002  25.872 1.00 33.31  ? 398 THR   B OG1   1 
ATOM   4629 C CG2   . THR   B 1 272 ? 23.670  -2.999  24.814 1.00 29.95  ? 398 THR   B CG2   1 
ATOM   4630 N N     . ASP   B 1 273 ? 25.705  -6.154  25.293 1.00 35.92  ? 399 ASP   B N     1 
ATOM   4631 C CA    . ASP   B 1 273 ? 27.101  -6.322  24.889 1.00 34.98  ? 399 ASP   B CA    1 
ATOM   4632 C C     . ASP   B 1 273 ? 27.234  -7.374  23.797 1.00 35.77  ? 399 ASP   B C     1 
ATOM   4633 O O     . ASP   B 1 273 ? 27.987  -7.187  22.836 1.00 36.36  ? 399 ASP   B O     1 
ATOM   4634 C CB    . ASP   B 1 273 ? 27.971  -6.706  26.093 1.00 35.38  ? 399 ASP   B CB    1 
ATOM   4635 C CG    . ASP   B 1 273 ? 28.229  -5.544  27.030 1.00 36.17  ? 399 ASP   B CG    1 
ATOM   4636 O OD1   . ASP   B 1 273 ? 28.079  -4.382  26.597 1.00 38.48  ? 399 ASP   B OD1   1 
ATOM   4637 O OD2   . ASP   B 1 273 ? 28.599  -5.789  28.201 1.00 38.44  ? 399 ASP   B OD2   1 
ATOM   4638 N N     . VAL   B 1 274 ? 26.525  -8.498  23.938 1.00 37.24  ? 400 VAL   B N     1 
ATOM   4639 C CA    . VAL   B 1 274 ? 26.536  -9.510  22.885 1.00 36.00  ? 400 VAL   B CA    1 
ATOM   4640 C C     . VAL   B 1 274 ? 25.901  -8.960  21.617 1.00 35.63  ? 400 VAL   B C     1 
ATOM   4641 O O     . VAL   B 1 274 ? 26.390  -9.203  20.512 1.00 36.21  ? 400 VAL   B O     1 
ATOM   4642 C CB    . VAL   B 1 274 ? 25.819  -10.785 23.351 1.00 37.58  ? 400 VAL   B CB    1 
ATOM   4643 C CG1   . VAL   B 1 274 ? 25.791  -11.800 22.222 1.00 40.56  ? 400 VAL   B CG1   1 
ATOM   4644 C CG2   . VAL   B 1 274 ? 26.524  -11.359 24.567 1.00 41.06  ? 400 VAL   B CG2   1 
ATOM   4645 N N     . SER   B 1 275 ? 24.771  -8.261  21.761 1.00 35.91  ? 401 SER   B N     1 
ATOM   4646 C CA    . SER   B 1 275 ? 24.111  -7.641  20.617 1.00 35.13  ? 401 SER   B CA    1 
ATOM   4647 C C     . SER   B 1 275 ? 25.073  -6.735  19.859 1.00 34.47  ? 401 SER   B C     1 
ATOM   4648 O O     . SER   B 1 275 ? 25.140  -6.769  18.625 1.00 34.53  ? 401 SER   B O     1 
ATOM   4649 C CB    . SER   B 1 275 ? 22.893  -6.856  21.110 1.00 36.09  ? 401 SER   B CB    1 
ATOM   4650 O OG    . SER   B 1 275 ? 22.203  -6.215  20.052 1.00 35.10  ? 401 SER   B OG    1 
ATOM   4651 N N     . TYR   B 1 276 ? 25.853  -5.941  20.592 1.00 34.97  ? 402 TYR   B N     1 
ATOM   4652 C CA    . TYR   B 1 276 ? 26.793  -5.024  19.960 1.00 33.20  ? 402 TYR   B CA    1 
ATOM   4653 C C     . TYR   B 1 276 ? 27.856  -5.776  19.177 1.00 34.90  ? 402 TYR   B C     1 
ATOM   4654 O O     . TYR   B 1 276 ? 28.174  -5.417  18.041 1.00 30.75  ? 402 TYR   B O     1 
ATOM   4655 C CB    . TYR   B 1 276 ? 27.438  -4.140  21.020 1.00 29.03  ? 402 TYR   B CB    1 
ATOM   4656 C CG    . TYR   B 1 276 ? 28.205  -2.969  20.444 1.00 28.44  ? 402 TYR   B CG    1 
ATOM   4657 C CD1   . TYR   B 1 276 ? 29.490  -3.121  19.969 1.00 30.01  ? 402 TYR   B CD1   1 
ATOM   4658 C CD2   . TYR   B 1 276 ? 27.640  -1.709  20.408 1.00 29.30  ? 402 TYR   B CD2   1 
ATOM   4659 C CE1   . TYR   B 1 276 ? 30.187  -2.041  19.468 1.00 30.19  ? 402 TYR   B CE1   1 
ATOM   4660 C CE2   . TYR   B 1 276 ? 28.323  -0.634  19.929 1.00 26.63  ? 402 TYR   B CE2   1 
ATOM   4661 C CZ    . TYR   B 1 276 ? 29.593  -0.800  19.448 1.00 29.12  ? 402 TYR   B CZ    1 
ATOM   4662 O OH    . TYR   B 1 276 ? 30.264  0.287   18.947 1.00 29.50  ? 402 TYR   B OH    1 
ATOM   4663 N N     . ILE   B 1 277 ? 28.440  -6.808  19.775 1.00 32.33  ? 403 ILE   B N     1 
ATOM   4664 C CA    . ILE   B 1 277 ? 29.486  -7.548  19.070 1.00 33.85  ? 403 ILE   B CA    1 
ATOM   4665 C C     . ILE   B 1 277 ? 28.911  -8.292  17.874 1.00 36.40  ? 403 ILE   B C     1 
ATOM   4666 O O     . ILE   B 1 277 ? 29.549  -8.379  16.815 1.00 37.38  ? 403 ILE   B O     1 
ATOM   4667 C CB    . ILE   B 1 277 ? 30.199  -8.509  20.030 1.00 38.48  ? 403 ILE   B CB    1 
ATOM   4668 C CG1   . ILE   B 1 277 ? 30.813  -7.726  21.173 1.00 35.42  ? 403 ILE   B CG1   1 
ATOM   4669 C CG2   . ILE   B 1 277 ? 31.279  -9.280  19.298 1.00 37.89  ? 403 ILE   B CG2   1 
ATOM   4670 C CD1   . ILE   B 1 277 ? 31.877  -6.800  20.719 1.00 35.98  ? 403 ILE   B CD1   1 
ATOM   4671 N N     . ALA   B 1 278 ? 27.720  -8.878  18.035 1.00 35.90  ? 404 ALA   B N     1 
ATOM   4672 C CA    . ALA   B 1 278 ? 27.062  -9.537  16.913 1.00 37.63  ? 404 ALA   B CA    1 
ATOM   4673 C C     . ALA   B 1 278 ? 26.779  -8.549  15.792 1.00 36.26  ? 404 ALA   B C     1 
ATOM   4674 O O     . ALA   B 1 278 ? 26.949  -8.867  14.617 1.00 38.12  ? 404 ALA   B O     1 
ATOM   4675 C CB    . ALA   B 1 278 ? 25.767  -10.199 17.374 1.00 39.53  ? 404 ALA   B CB    1 
ATOM   4676 N N     . CYS   B 1 279 ? 26.348  -7.341  16.136 1.00 36.14  ? 405 CYS   B N     1 
ATOM   4677 C CA    . CYS   B 1 279 ? 26.054  -6.366  15.091 1.00 32.56  ? 405 CYS   B CA    1 
ATOM   4678 C C     . CYS   B 1 279 ? 27.330  -5.851  14.440 1.00 35.90  ? 405 CYS   B C     1 
ATOM   4679 O O     . CYS   B 1 279 ? 27.368  -5.629  13.222 1.00 37.63  ? 405 CYS   B O     1 
ATOM   4680 C CB    . CYS   B 1 279 ? 25.222  -5.237  15.677 1.00 32.54  ? 405 CYS   B CB    1 
ATOM   4681 S SG    . CYS   B 1 279 ? 23.522  -5.812  15.941 1.00 42.07  ? 405 CYS   B SG    1 
ATOM   4682 N N     . ALA   B 1 280 ? 28.393  -5.687  15.223 1.00 33.95  ? 406 ALA   B N     1 
ATOM   4683 C CA    . ALA   B 1 280 ? 29.678  -5.300  14.654 1.00 34.58  ? 406 ALA   B CA    1 
ATOM   4684 C C     . ALA   B 1 280 ? 30.175  -6.325  13.641 1.00 39.02  ? 406 ALA   B C     1 
ATOM   4685 O O     . ALA   B 1 280 ? 30.743  -5.962  12.601 1.00 36.09  ? 406 ALA   B O     1 
ATOM   4686 C CB    . ALA   B 1 280 ? 30.704  -5.117  15.757 1.00 31.96  ? 406 ALA   B CB    1 
ATOM   4687 N N     . ALA   B 1 281 ? 29.991  -7.612  13.937 1.00 38.73  ? 407 ALA   B N     1 
ATOM   4688 C CA    . ALA   B 1 281 ? 30.371  -8.647  12.982 1.00 38.36  ? 407 ALA   B CA    1 
ATOM   4689 C C     . ALA   B 1 281 ? 29.592  -8.503  11.685 1.00 39.36  ? 407 ALA   B C     1 
ATOM   4690 O O     . ALA   B 1 281 ? 30.143  -8.680  10.590 1.00 42.33  ? 407 ALA   B O     1 
ATOM   4691 C CB    . ALA   B 1 281 ? 30.142  -10.027 13.600 1.00 43.40  ? 407 ALA   B CB    1 
ATOM   4692 N N     . LYS   B 1 282 ? 28.299  -8.193  11.787 1.00 39.66  ? 408 LYS   B N     1 
ATOM   4693 C CA    . LYS   B 1 282 ? 27.492  -7.995  10.588 1.00 39.27  ? 408 LYS   B CA    1 
ATOM   4694 C C     . LYS   B 1 282 ? 27.999  -6.799  9.785  1.00 37.47  ? 408 LYS   B C     1 
ATOM   4695 O O     . LYS   B 1 282 ? 28.155  -6.871  8.558  1.00 42.10  ? 408 LYS   B O     1 
ATOM   4696 C CB    . LYS   B 1 282 ? 26.027  -7.815  10.996 1.00 41.78  ? 408 LYS   B CB    1 
ATOM   4697 C CG    . LYS   B 1 282 ? 25.057  -7.604  9.843  1.00 44.04  ? 408 LYS   B CG    1 
ATOM   4698 C CD    . LYS   B 1 282 ? 23.684  -7.209  10.399 1.00 43.76  ? 408 LYS   B CD    1 
ATOM   4699 C CE    . LYS   B 1 282 ? 23.065  -8.316  11.244 1.00 42.17  ? 408 LYS   B CE    1 
ATOM   4700 N NZ    . LYS   B 1 282 ? 22.783  -9.541  10.465 1.00 48.37  ? 408 LYS   B NZ    1 
ATOM   4701 N N     . LEU   B 1 283 ? 28.292  -5.698  10.477 1.00 37.43  ? 409 LEU   B N     1 
ATOM   4702 C CA    . LEU   B 1 283 ? 28.796  -4.494  9.825  1.00 40.05  ? 409 LEU   B CA    1 
ATOM   4703 C C     . LEU   B 1 283 ? 30.164  -4.720  9.194  1.00 39.38  ? 409 LEU   B C     1 
ATOM   4704 O O     . LEU   B 1 283 ? 30.442  -4.210  8.104  1.00 36.95  ? 409 LEU   B O     1 
ATOM   4705 C CB    . LEU   B 1 283 ? 28.874  -3.359  10.840 1.00 34.56  ? 409 LEU   B CB    1 
ATOM   4706 C CG    . LEU   B 1 283 ? 27.532  -2.689  11.126 1.00 32.40  ? 409 LEU   B CG    1 
ATOM   4707 C CD1   . LEU   B 1 283 ? 27.650  -1.800  12.363 1.00 33.13  ? 409 LEU   B CD1   1 
ATOM   4708 C CD2   . LEU   B 1 283 ? 27.052  -1.891  9.894  1.00 33.25  ? 409 LEU   B CD2   1 
ATOM   4709 N N     . LEU   B 1 284 ? 31.044  -5.453  9.878  1.00 40.68  ? 410 LEU   B N     1 
ATOM   4710 C CA    . LEU   B 1 284 ? 32.406  -5.614  9.382  1.00 38.42  ? 410 LEU   B CA    1 
ATOM   4711 C C     . LEU   B 1 284 ? 32.469  -6.491  8.140  1.00 42.06  ? 410 LEU   B C     1 
ATOM   4712 O O     . LEU   B 1 284 ? 33.467  -6.454  7.417  1.00 45.16  ? 410 LEU   B O     1 
ATOM   4713 C CB    . LEU   B 1 284 ? 33.290  -6.175  10.494 1.00 38.85  ? 410 LEU   B CB    1 
ATOM   4714 C CG    . LEU   B 1 284 ? 33.711  -5.117  11.506 1.00 38.61  ? 410 LEU   B CG    1 
ATOM   4715 C CD1   . LEU   B 1 284 ? 34.230  -5.752  12.800 1.00 39.55  ? 410 LEU   B CD1   1 
ATOM   4716 C CD2   . LEU   B 1 284 ? 34.741  -4.164  10.886 1.00 37.30  ? 410 LEU   B CD2   1 
ATOM   4717 N N     . ALA   B 1 285 ? 31.420  -7.253  7.863  1.00 40.10  ? 411 ALA   B N     1 
ATOM   4718 C CA    . ALA   B 1 285 ? 31.326  -8.066  6.671  1.00 44.21  ? 411 ALA   B CA    1 
ATOM   4719 C C     . ALA   B 1 285 ? 30.707  -7.307  5.501  1.00 41.01  ? 411 ALA   B C     1 
ATOM   4720 O O     . ALA   B 1 285 ? 30.616  -7.855  4.400  1.00 45.54  ? 411 ALA   B O     1 
ATOM   4721 C CB    . ALA   B 1 285 ? 30.520  -9.332  6.978  1.00 45.02  ? 411 ALA   B CB    1 
ATOM   4722 N N     . ALA   B 1 286 ? 30.308  -6.051  5.713  1.00 40.33  ? 412 ALA   B N     1 
ATOM   4723 C CA    . ALA   B 1 286 ? 29.628  -5.247  4.705  1.00 42.64  ? 412 ALA   B CA    1 
ATOM   4724 C C     . ALA   B 1 286 ? 30.336  -3.918  4.469  1.00 41.70  ? 412 ALA   B C     1 
ATOM   4725 O O     . ALA   B 1 286 ? 29.706  -2.963  4.002  1.00 40.62  ? 412 ALA   B O     1 
ATOM   4726 C CB    . ALA   B 1 286 ? 28.170  -4.998  5.117  1.00 44.12  ? 412 ALA   B CB    1 
ATOM   4727 N N     . THR   B 1 287 ? 31.630  -3.823  4.789  1.00 39.65  ? 413 THR   B N     1 
ATOM   4728 C CA    . THR   B 1 287 ? 32.302  -2.535  4.668  1.00 42.15  ? 413 THR   B CA    1 
ATOM   4729 C C     . THR   B 1 287 ? 32.411  -2.048  3.225  1.00 40.76  ? 413 THR   B C     1 
ATOM   4730 O O     . THR   B 1 287 ? 32.769  -0.885  3.010  1.00 40.89  ? 413 THR   B O     1 
ATOM   4731 C CB    . THR   B 1 287 ? 33.697  -2.586  5.303  1.00 39.50  ? 413 THR   B CB    1 
ATOM   4732 O OG1   . THR   B 1 287 ? 34.482  -3.605  4.672  1.00 43.56  ? 413 THR   B OG1   1 
ATOM   4733 C CG2   . THR   B 1 287 ? 33.602  -2.829  6.817  1.00 39.65  ? 413 THR   B CG2   1 
ATOM   4734 N N     . ASP   B 1 288 ? 32.126  -2.898  2.233  1.00 41.79  ? 414 ASP   B N     1 
ATOM   4735 C CA    . ASP   B 1 288 ? 32.022  -2.411  0.863  1.00 42.61  ? 414 ASP   B CA    1 
ATOM   4736 C C     . ASP   B 1 288 ? 30.865  -1.431  0.688  1.00 43.34  ? 414 ASP   B C     1 
ATOM   4737 O O     . ASP   B 1 288 ? 30.958  -0.510  -0.131 1.00 47.34  ? 414 ASP   B O     1 
ATOM   4738 C CB    . ASP   B 1 288 ? 31.874  -3.585  -0.106 1.00 45.80  ? 414 ASP   B CB    1 
ATOM   4739 C CG    . ASP   B 1 288 ? 30.719  -4.509  0.250  1.00 49.86  ? 414 ASP   B CG    1 
ATOM   4740 O OD1   . ASP   B 1 288 ? 30.571  -4.827  1.448  1.00 50.99  ? 414 ASP   B OD1   1 
ATOM   4741 O OD2   . ASP   B 1 288 ? 29.976  -4.931  -0.671 1.00 57.64  ? 414 ASP   B OD2   1 
ATOM   4742 N N     . VAL   B 1 289 ? 29.768  -1.604  1.422  1.00 41.54  ? 415 VAL   B N     1 
ATOM   4743 C CA    . VAL   B 1 289 ? 28.589  -0.772  1.212  1.00 42.24  ? 415 VAL   B CA    1 
ATOM   4744 C C     . VAL   B 1 289 ? 28.192  0.032   2.434  1.00 38.84  ? 415 VAL   B C     1 
ATOM   4745 O O     . VAL   B 1 289 ? 27.329  0.913   2.315  1.00 40.08  ? 415 VAL   B O     1 
ATOM   4746 C CB    . VAL   B 1 289 ? 27.386  -1.596  0.702  1.00 44.14  ? 415 VAL   B CB    1 
ATOM   4747 C CG1   . VAL   B 1 289 ? 27.713  -2.221  -0.647 1.00 47.50  ? 415 VAL   B CG1   1 
ATOM   4748 C CG2   . VAL   B 1 289 ? 26.987  -2.648  1.719  1.00 42.25  ? 415 VAL   B CG2   1 
ATOM   4749 N N     . VAL   B 1 290 ? 28.773  -0.222  3.608  1.00 35.91  ? 416 VAL   B N     1 
ATOM   4750 C CA    . VAL   B 1 290 ? 28.561  0.651   4.747  1.00 36.00  ? 416 VAL   B CA    1 
ATOM   4751 C C     . VAL   B 1 290 ? 29.910  0.986   5.360  1.00 33.10  ? 416 VAL   B C     1 
ATOM   4752 O O     . VAL   B 1 290 ? 30.912  0.298   5.150  1.00 34.69  ? 416 VAL   B O     1 
ATOM   4753 C CB    . VAL   B 1 290 ? 27.614  0.039   5.799  1.00 38.94  ? 416 VAL   B CB    1 
ATOM   4754 C CG1   . VAL   B 1 290 ? 26.242  -0.182  5.191  1.00 36.01  ? 416 VAL   B CG1   1 
ATOM   4755 C CG2   . VAL   B 1 290 ? 28.176  -1.262  6.368  1.00 35.27  ? 416 VAL   B CG2   1 
ATOM   4756 N N     . PHE   B 1 291 ? 29.925  2.093   6.089  1.00 32.15  ? 417 PHE   B N     1 
ATOM   4757 C CA    . PHE   B 1 291 ? 31.105  2.545   6.815  1.00 32.13  ? 417 PHE   B CA    1 
ATOM   4758 C C     . PHE   B 1 291 ? 30.828  2.383   8.294  1.00 33.76  ? 417 PHE   B C     1 
ATOM   4759 O O     . PHE   B 1 291 ? 30.202  3.267   8.898  1.00 30.68  ? 417 PHE   B O     1 
ATOM   4760 C CB    . PHE   B 1 291 ? 31.417  4.006   6.492  1.00 34.39  ? 417 PHE   B CB    1 
ATOM   4761 C CG    . PHE   B 1 291 ? 32.565  4.557   7.277  1.00 32.85  ? 417 PHE   B CG    1 
ATOM   4762 C CD1   . PHE   B 1 291 ? 33.821  3.977   7.169  1.00 32.62  ? 417 PHE   B CD1   1 
ATOM   4763 C CD2   . PHE   B 1 291 ? 32.398  5.663   8.097  1.00 30.70  ? 417 PHE   B CD2   1 
ATOM   4764 C CE1   . PHE   B 1 291 ? 34.889  4.471   7.879  1.00 30.77  ? 417 PHE   B CE1   1 
ATOM   4765 C CE2   . PHE   B 1 291 ? 33.457  6.171   8.814  1.00 33.07  ? 417 PHE   B CE2   1 
ATOM   4766 C CZ    . PHE   B 1 291 ? 34.718  5.568   8.709  1.00 31.48  ? 417 PHE   B CZ    1 
ATOM   4767 N N     . PRO   B 1 292 ? 31.262  1.285   8.923  1.00 31.50  ? 418 PRO   B N     1 
ATOM   4768 C CA    . PRO   B 1 292 ? 30.911  1.062   10.328 1.00 31.24  ? 418 PRO   B CA    1 
ATOM   4769 C C     . PRO   B 1 292 ? 31.658  2.014   11.241 1.00 29.84  ? 418 PRO   B C     1 
ATOM   4770 O O     . PRO   B 1 292 ? 32.868  2.240   11.102 1.00 29.49  ? 418 PRO   B O     1 
ATOM   4771 C CB    . PRO   B 1 292 ? 31.315  -0.400  10.575 1.00 33.31  ? 418 PRO   B CB    1 
ATOM   4772 C CG    . PRO   B 1 292 ? 31.439  -1.012  9.164  1.00 32.33  ? 418 PRO   B CG    1 
ATOM   4773 C CD    . PRO   B 1 292 ? 31.972  0.131   8.341  1.00 31.99  ? 418 PRO   B CD    1 
ATOM   4774 N N     . GLN   B 1 293 ? 30.913  2.564   12.193 1.00 27.53  ? 419 GLN   B N     1 
ATOM   4775 C CA    . GLN   B 1 293 ? 31.406  3.542   13.150 1.00 27.54  ? 419 GLN   B CA    1 
ATOM   4776 C C     . GLN   B 1 293 ? 31.081  2.974   14.526 1.00 27.75  ? 419 GLN   B C     1 
ATOM   4777 O O     . GLN   B 1 293 ? 29.919  2.938   14.932 1.00 26.78  ? 419 GLN   B O     1 
ATOM   4778 C CB    . GLN   B 1 293 ? 30.753  4.889   12.914 1.00 29.49  ? 419 GLN   B CB    1 
ATOM   4779 C CG    . GLN   B 1 293 ? 31.105  5.437   11.545 1.00 28.61  ? 419 GLN   B CG    1 
ATOM   4780 C CD    . GLN   B 1 293 ? 30.312  6.655   11.213 1.00 30.13  ? 419 GLN   B CD    1 
ATOM   4781 O OE1   . GLN   B 1 293 ? 29.097  6.630   11.289 1.00 32.19  ? 419 GLN   B OE1   1 
ATOM   4782 N NE2   . GLN   B 1 293 ? 30.986  7.742   10.890 1.00 30.52  ? 419 GLN   B NE2   1 
ATOM   4783 N N     . PHE   B 1 294 ? 32.100  2.472   15.208 1.00 25.86  ? 420 PHE   B N     1 
ATOM   4784 C CA    . PHE   B 1 294 ? 31.889  1.739   16.453 1.00 29.45  ? 420 PHE   B CA    1 
ATOM   4785 C C     . PHE   B 1 294 ? 32.020  2.697   17.611 1.00 28.04  ? 420 PHE   B C     1 
ATOM   4786 O O     . PHE   B 1 294 ? 33.120  2.994   18.083 1.00 27.54  ? 420 PHE   B O     1 
ATOM   4787 C CB    . PHE   B 1 294 ? 32.858  0.575   16.548 1.00 28.19  ? 420 PHE   B CB    1 
ATOM   4788 C CG    . PHE   B 1 294 ? 32.668  -0.404  15.458 1.00 28.63  ? 420 PHE   B CG    1 
ATOM   4789 C CD1   . PHE   B 1 294 ? 31.472  -1.110  15.348 1.00 30.92  ? 420 PHE   B CD1   1 
ATOM   4790 C CD2   . PHE   B 1 294 ? 33.646  -0.595  14.507 1.00 27.49  ? 420 PHE   B CD2   1 
ATOM   4791 C CE1   . PHE   B 1 294 ? 31.290  -2.022  14.321 1.00 30.43  ? 420 PHE   B CE1   1 
ATOM   4792 C CE2   . PHE   B 1 294 ? 33.470  -1.506  13.482 1.00 30.74  ? 420 PHE   B CE2   1 
ATOM   4793 C CZ    . PHE   B 1 294 ? 32.279  -2.216  13.392 1.00 30.68  ? 420 PHE   B CZ    1 
ATOM   4794 N N     . ALA   B 1 295 ? 30.888  3.180   18.081 1.00 26.22  ? 421 ALA   B N     1 
ATOM   4795 C CA    . ALA   B 1 295 ? 30.860  4.137   19.176 1.00 27.87  ? 421 ALA   B CA    1 
ATOM   4796 C C     . ALA   B 1 295 ? 30.836  3.357   20.479 1.00 31.62  ? 421 ALA   B C     1 
ATOM   4797 O O     . ALA   B 1 295 ? 29.815  2.752   20.831 1.00 33.94  ? 421 ALA   B O     1 
ATOM   4798 C CB    . ALA   B 1 295 ? 29.638  5.042   19.060 1.00 27.94  ? 421 ALA   B CB    1 
ATOM   4799 N N     . THR   B 1 296 ? 31.946  3.390   21.208 1.00 27.42  ? 422 THR   B N     1 
ATOM   4800 C CA    . THR   B 1 296 ? 31.959  2.746   22.506 1.00 27.43  ? 422 THR   B CA    1 
ATOM   4801 C C     . THR   B 1 296 ? 33.077  3.362   23.328 1.00 29.89  ? 422 THR   B C     1 
ATOM   4802 O O     . THR   B 1 296 ? 34.055  3.859   22.776 1.00 28.77  ? 422 THR   B O     1 
ATOM   4803 C CB    . THR   B 1 296 ? 32.127  1.219   22.375 1.00 29.54  ? 422 THR   B CB    1 
ATOM   4804 O OG1   . THR   B 1 296 ? 32.078  0.632   23.685 1.00 30.70  ? 422 THR   B OG1   1 
ATOM   4805 C CG2   . THR   B 1 296 ? 33.454  0.842   21.670 1.00 33.36  ? 422 THR   B CG2   1 
ATOM   4806 N N     . HIS   B 1 297 ? 32.899  3.374   24.649 1.00 30.84  ? 423 HIS   B N     1 
ATOM   4807 C CA    . HIS   B 1 297 ? 33.988  3.705   25.556 1.00 31.19  ? 423 HIS   B CA    1 
ATOM   4808 C C     . HIS   B 1 297 ? 34.433  2.492   26.333 1.00 32.54  ? 423 HIS   B C     1 
ATOM   4809 O O     . HIS   B 1 297 ? 35.145  2.630   27.333 1.00 33.65  ? 423 HIS   B O     1 
ATOM   4810 C CB    . HIS   B 1 297 ? 33.578  4.804   26.524 1.00 34.44  ? 423 HIS   B CB    1 
ATOM   4811 C CG    . HIS   B 1 297 ? 32.956  5.965   25.844 1.00 35.46  ? 423 HIS   B CG    1 
ATOM   4812 N ND1   . HIS   B 1 297 ? 31.631  6.296   26.013 1.00 37.34  ? 423 HIS   B ND1   1 
ATOM   4813 C CD2   . HIS   B 1 297 ? 33.460  6.841   24.945 1.00 34.47  ? 423 HIS   B CD2   1 
ATOM   4814 C CE1   . HIS   B 1 297 ? 31.347  7.340   25.254 1.00 36.80  ? 423 HIS   B CE1   1 
ATOM   4815 N NE2   . HIS   B 1 297 ? 32.442  7.695   24.605 1.00 36.89  ? 423 HIS   B NE2   1 
ATOM   4816 N N     . ASN   B 1 298 ? 33.991  1.319   25.917 1.00 33.30  ? 424 ASN   B N     1 
ATOM   4817 C CA    . ASN   B 1 298 ? 34.249  0.083   26.629 1.00 32.03  ? 424 ASN   B CA    1 
ATOM   4818 C C     . ASN   B 1 298 ? 35.462  -0.549  25.966 1.00 31.11  ? 424 ASN   B C     1 
ATOM   4819 O O     . ASN   B 1 298 ? 35.406  -0.946  24.803 1.00 31.23  ? 424 ASN   B O     1 
ATOM   4820 C CB    . ASN   B 1 298 ? 33.018  -0.819  26.589 1.00 30.97  ? 424 ASN   B CB    1 
ATOM   4821 C CG    . ASN   B 1 298 ? 33.232  -2.143  27.307 1.00 32.27  ? 424 ASN   B CG    1 
ATOM   4822 O OD1   . ASN   B 1 298 ? 34.324  -2.696  27.286 1.00 34.01  ? 424 ASN   B OD1   1 
ATOM   4823 N ND2   . ASN   B 1 298 ? 32.179  -2.660  27.928 1.00 32.32  ? 424 ASN   B ND2   1 
ATOM   4824 N N     . ALA   B 1 299 ? 36.560  -0.644  26.724 1.00 32.84  ? 425 ALA   B N     1 
ATOM   4825 C CA    . ALA   B 1 299 ? 37.805  -1.122  26.139 1.00 34.01  ? 425 ALA   B CA    1 
ATOM   4826 C C     . ALA   B 1 299 ? 37.684  -2.571  25.717 1.00 32.12  ? 425 ALA   B C     1 
ATOM   4827 O O     . ALA   B 1 299 ? 38.376  -3.009  24.791 1.00 34.18  ? 425 ALA   B O     1 
ATOM   4828 C CB    . ALA   B 1 299 ? 38.955  -0.954  27.137 1.00 36.30  ? 425 ALA   B CB    1 
ATOM   4829 N N     . GLN   B 1 300 ? 36.825  -3.329  26.390 1.00 31.79  ? 426 GLN   B N     1 
ATOM   4830 C CA    . GLN   B 1 300 ? 36.641  -4.725  26.026 1.00 32.66  ? 426 GLN   B CA    1 
ATOM   4831 C C     . GLN   B 1 300 ? 35.880  -4.831  24.719 1.00 32.73  ? 426 GLN   B C     1 
ATOM   4832 O O     . GLN   B 1 300 ? 36.232  -5.619  23.842 1.00 34.84  ? 426 GLN   B O     1 
ATOM   4833 C CB    . GLN   B 1 300 ? 35.902  -5.461  27.148 1.00 33.91  ? 426 GLN   B CB    1 
ATOM   4834 C CG    . GLN   B 1 300 ? 35.978  -6.982  27.057 1.00 38.17  ? 426 GLN   B CG    1 
ATOM   4835 C CD    . GLN   B 1 300 ? 35.101  -7.563  25.952 1.00 39.23  ? 426 GLN   B CD    1 
ATOM   4836 O OE1   . GLN   B 1 300 ? 33.954  -7.158  25.787 1.00 40.82  ? 426 GLN   B OE1   1 
ATOM   4837 N NE2   . GLN   B 1 300 ? 35.643  -8.516  25.196 1.00 42.21  ? 426 GLN   B NE2   1 
ATOM   4838 N N     . THR   B 1 301 ? 34.822  -4.048  24.582 1.00 32.99  ? 427 THR   B N     1 
ATOM   4839 C CA    . THR   B 1 301 ? 34.122  -3.982  23.312 1.00 30.84  ? 427 THR   B CA    1 
ATOM   4840 C C     . THR   B 1 301 ? 35.062  -3.555  22.195 1.00 30.60  ? 427 THR   B C     1 
ATOM   4841 O O     . THR   B 1 301 ? 35.049  -4.124  21.095 1.00 32.36  ? 427 THR   B O     1 
ATOM   4842 C CB    . THR   B 1 301 ? 32.969  -2.996  23.430 1.00 30.70  ? 427 THR   B CB    1 
ATOM   4843 O OG1   . THR   B 1 301 ? 32.169  -3.334  24.572 1.00 28.34  ? 427 THR   B OG1   1 
ATOM   4844 C CG2   . THR   B 1 301 ? 32.114  -3.036  22.160 1.00 30.77  ? 427 THR   B CG2   1 
ATOM   4845 N N     . LEU   B 1 302 ? 35.850  -2.519  22.450 1.00 28.60  ? 428 LEU   B N     1 
ATOM   4846 C CA    . LEU   B 1 302 ? 36.743  -1.992  21.428 1.00 30.50  ? 428 LEU   B CA    1 
ATOM   4847 C C     . LEU   B 1 302 ? 37.763  -3.041  21.011 1.00 30.14  ? 428 LEU   B C     1 
ATOM   4848 O O     . LEU   B 1 302 ? 37.971  -3.283  19.817 1.00 34.84  ? 428 LEU   B O     1 
ATOM   4849 C CB    . LEU   B 1 302 ? 37.434  -0.735  21.955 1.00 32.75  ? 428 LEU   B CB    1 
ATOM   4850 C CG    . LEU   B 1 302 ? 38.312  0.182   21.098 1.00 34.35  ? 428 LEU   B CG    1 
ATOM   4851 C CD1   . LEU   B 1 302 ? 38.693  1.361   21.969 1.00 39.77  ? 428 LEU   B CD1   1 
ATOM   4852 C CD2   . LEU   B 1 302 ? 39.578  -0.480  20.611 1.00 31.49  ? 428 LEU   B CD2   1 
ATOM   4853 N N     . ALA   B 1 303 ? 38.407  -3.681  21.991 1.00 34.33  ? 429 ALA   B N     1 
ATOM   4854 C CA    . ALA   B 1 303 ? 39.371  -4.726  21.665 1.00 34.67  ? 429 ALA   B CA    1 
ATOM   4855 C C     . ALA   B 1 303 ? 38.729  -5.827  20.837 1.00 32.37  ? 429 ALA   B C     1 
ATOM   4856 O O     . ALA   B 1 303 ? 39.323  -6.318  19.871 1.00 36.36  ? 429 ALA   B O     1 
ATOM   4857 C CB    . ALA   B 1 303 ? 39.968  -5.307  22.944 1.00 34.84  ? 429 ALA   B CB    1 
ATOM   4858 N N     . ALA   B 1 304 ? 37.510  -6.228  21.199 1.00 34.49  ? 430 ALA   B N     1 
ATOM   4859 C CA    . ALA   B 1 304 ? 36.854  -7.317  20.485 1.00 34.13  ? 430 ALA   B CA    1 
ATOM   4860 C C     . ALA   B 1 304 ? 36.654  -6.965  19.021 1.00 34.40  ? 430 ALA   B C     1 
ATOM   4861 O O     . ALA   B 1 304 ? 36.968  -7.763  18.131 1.00 36.99  ? 430 ALA   B O     1 
ATOM   4862 C CB    . ALA   B 1 304 ? 35.520  -7.661  21.150 1.00 34.45  ? 430 ALA   B CB    1 
ATOM   4863 N N     . ILE   B 1 305 ? 36.134  -5.761  18.753 1.00 33.77  ? 431 ILE   B N     1 
ATOM   4864 C CA    . ILE   B 1 305 ? 35.924  -5.325  17.375 1.00 36.53  ? 431 ILE   B CA    1 
ATOM   4865 C C     . ILE   B 1 305 ? 37.255  -5.184  16.646 1.00 36.00  ? 431 ILE   B C     1 
ATOM   4866 O O     . ILE   B 1 305 ? 37.392  -5.576  15.480 1.00 38.83  ? 431 ILE   B O     1 
ATOM   4867 C CB    . ILE   B 1 305 ? 35.133  -4.008  17.360 1.00 36.07  ? 431 ILE   B CB    1 
ATOM   4868 C CG1   . ILE   B 1 305 ? 33.664  -4.301  17.670 1.00 38.44  ? 431 ILE   B CG1   1 
ATOM   4869 C CG2   . ILE   B 1 305 ? 35.334  -3.282  16.041 1.00 34.94  ? 431 ILE   B CG2   1 
ATOM   4870 C CD1   . ILE   B 1 305 ? 32.894  -3.115  18.008 1.00 36.35  ? 431 ILE   B CD1   1 
ATOM   4871 N N     . TYR   B 1 306 ? 38.238  -4.579  17.311 1.00 34.80  ? 432 TYR   B N     1 
ATOM   4872 C CA    . TYR   B 1 306 ? 39.556  -4.380  16.726 1.00 34.49  ? 432 TYR   B CA    1 
ATOM   4873 C C     . TYR   B 1 306 ? 40.104  -5.676  16.136 1.00 37.80  ? 432 TYR   B C     1 
ATOM   4874 O O     . TYR   B 1 306 ? 40.562  -5.705  14.989 1.00 39.92  ? 432 TYR   B O     1 
ATOM   4875 C CB    . TYR   B 1 306 ? 40.487  -3.814  17.804 1.00 34.77  ? 432 TYR   B CB    1 
ATOM   4876 C CG    . TYR   B 1 306 ? 41.941  -3.765  17.432 1.00 40.99  ? 432 TYR   B CG    1 
ATOM   4877 C CD1   . TYR   B 1 306 ? 42.404  -2.918  16.437 1.00 38.60  ? 432 TYR   B CD1   1 
ATOM   4878 C CD2   . TYR   B 1 306 ? 42.863  -4.546  18.109 1.00 41.13  ? 432 TYR   B CD2   1 
ATOM   4879 C CE1   . TYR   B 1 306 ? 43.761  -2.877  16.101 1.00 42.46  ? 432 TYR   B CE1   1 
ATOM   4880 C CE2   . TYR   B 1 306 ? 44.205  -4.512  17.785 1.00 40.72  ? 432 TYR   B CE2   1 
ATOM   4881 C CZ    . TYR   B 1 306 ? 44.649  -3.676  16.790 1.00 43.24  ? 432 TYR   B CZ    1 
ATOM   4882 O OH    . TYR   B 1 306 ? 45.993  -3.658  16.492 1.00 46.72  ? 432 TYR   B OH    1 
ATOM   4883 N N     . HIS   B 1 307 ? 40.024  -6.770  16.889 1.00 37.06  ? 433 HIS   B N     1 
ATOM   4884 C CA    . HIS   B 1 307 ? 40.552  -8.030  16.386 1.00 39.63  ? 433 HIS   B CA    1 
ATOM   4885 C C     . HIS   B 1 307 ? 39.565  -8.727  15.470 1.00 42.26  ? 433 HIS   B C     1 
ATOM   4886 O O     . HIS   B 1 307 ? 39.978  -9.489  14.592 1.00 43.42  ? 433 HIS   B O     1 
ATOM   4887 C CB    . HIS   B 1 307 ? 40.946  -8.941  17.547 1.00 43.56  ? 433 HIS   B CB    1 
ATOM   4888 C CG    . HIS   B 1 307 ? 42.128  -8.441  18.305 1.00 44.55  ? 433 HIS   B CG    1 
ATOM   4889 N ND1   . HIS   B 1 307 ? 43.425  -8.646  17.882 1.00 44.55  ? 433 HIS   B ND1   1 
ATOM   4890 C CD2   . HIS   B 1 307 ? 42.210  -7.716  19.443 1.00 41.38  ? 433 HIS   B CD2   1 
ATOM   4891 C CE1   . HIS   B 1 307 ? 44.256  -8.081  18.740 1.00 45.04  ? 433 HIS   B CE1   1 
ATOM   4892 N NE2   . HIS   B 1 307 ? 43.543  -7.500  19.690 1.00 41.01  ? 433 HIS   B NE2   1 
ATOM   4893 N N     . MET   B 1 308 ? 38.270  -8.470  15.647 1.00 41.00  ? 434 MET   B N     1 
ATOM   4894 C CA    . MET   B 1 308 ? 37.288  -9.048  14.741 1.00 42.35  ? 434 MET   B CA    1 
ATOM   4895 C C     . MET   B 1 308 ? 37.454  -8.513  13.328 1.00 44.31  ? 434 MET   B C     1 
ATOM   4896 O O     . MET   B 1 308 ? 37.208  -9.235  12.358 1.00 47.07  ? 434 MET   B O     1 
ATOM   4897 C CB    . MET   B 1 308 ? 35.880  -8.762  15.251 1.00 38.47  ? 434 MET   B CB    1 
ATOM   4898 C CG    . MET   B 1 308 ? 34.773  -9.332  14.386 1.00 45.70  ? 434 MET   B CG    1 
ATOM   4899 S SD    . MET   B 1 308 ? 33.183  -8.741  15.008 1.00 58.30  ? 434 MET   B SD    1 
ATOM   4900 C CE    . MET   B 1 308 ? 33.582  -8.643  16.766 1.00 43.79  ? 434 MET   B CE    1 
ATOM   4901 N N     . ALA   B 1 309 ? 37.866  -7.256  13.190 1.00 42.67  ? 435 ALA   B N     1 
ATOM   4902 C CA    . ALA   B 1 309 ? 37.986  -6.645  11.873 1.00 45.13  ? 435 ALA   B CA    1 
ATOM   4903 C C     . ALA   B 1 309 ? 39.140  -7.204  11.049 1.00 45.52  ? 435 ALA   B C     1 
ATOM   4904 O O     . ALA   B 1 309 ? 39.220  -6.917  9.848  1.00 46.29  ? 435 ALA   B O     1 
ATOM   4905 C CB    . ALA   B 1 309 ? 38.148  -5.140  12.032 1.00 41.16  ? 435 ALA   B CB    1 
ATOM   4906 N N     . GLY   B 1 310 ? 40.030  -7.981  11.650 1.00 49.59  ? 436 GLY   B N     1 
ATOM   4907 C CA    . GLY   B 1 310 ? 41.177  -8.497  10.932 1.00 48.76  ? 436 GLY   B CA    1 
ATOM   4908 C C     . GLY   B 1 310 ? 42.352  -7.540  10.934 1.00 45.21  ? 436 GLY   B C     1 
ATOM   4909 O O     . GLY   B 1 310 ? 42.340  -6.470  11.547 1.00 47.32  ? 436 GLY   B O     1 
ATOM   4910 N N     . LYS   B 1 311 ? 43.396  -7.941  10.209 1.00 52.37  ? 437 LYS   B N     1 
ATOM   4911 C CA    . LYS   B 1 311 ? 44.636  -7.177  10.157 1.00 53.21  ? 437 LYS   B CA    1 
ATOM   4912 C C     . LYS   B 1 311 ? 44.690  -6.184  9.002  1.00 52.21  ? 437 LYS   B C     1 
ATOM   4913 O O     . LYS   B 1 311 ? 45.543  -5.288  9.012  1.00 51.37  ? 437 LYS   B O     1 
ATOM   4914 C CB    . LYS   B 1 311 ? 45.833  -8.126  10.058 1.00 53.40  ? 437 LYS   B CB    1 
ATOM   4915 N N     . ASP   B 1 312 ? 43.821  -6.318  8.006  1.00 50.97  ? 438 ASP   B N     1 
ATOM   4916 C CA    . ASP   B 1 312 ? 43.817  -5.373  6.900  1.00 50.75  ? 438 ASP   B CA    1 
ATOM   4917 C C     . ASP   B 1 312 ? 43.030  -4.142  7.326  1.00 49.31  ? 438 ASP   B C     1 
ATOM   4918 O O     . ASP   B 1 312 ? 41.872  -4.256  7.742  1.00 51.83  ? 438 ASP   B O     1 
ATOM   4919 C CB    . ASP   B 1 312 ? 43.214  -6.005  5.648  1.00 55.35  ? 438 ASP   B CB    1 
ATOM   4920 N N     . PHE   B 1 313 ? 43.656  -2.971  7.253  1.00 46.84  ? 439 PHE   B N     1 
ATOM   4921 C CA    . PHE   B 1 313 ? 42.933  -1.759  7.601  1.00 40.35  ? 439 PHE   B CA    1 
ATOM   4922 C C     . PHE   B 1 313 ? 43.407  -0.602  6.738  1.00 45.01  ? 439 PHE   B C     1 
ATOM   4923 O O     . PHE   B 1 313 ? 44.584  -0.501  6.399  1.00 41.19  ? 439 PHE   B O     1 
ATOM   4924 C CB    . PHE   B 1 313 ? 43.091  -1.369  9.072  1.00 41.55  ? 439 PHE   B CB    1 
ATOM   4925 C CG    . PHE   B 1 313 ? 42.286  -0.160  9.436  1.00 38.59  ? 439 PHE   B CG    1 
ATOM   4926 C CD1   . PHE   B 1 313 ? 40.945  -0.280  9.708  1.00 36.91  ? 439 PHE   B CD1   1 
ATOM   4927 C CD2   . PHE   B 1 313 ? 42.857  1.099   9.447  1.00 37.79  ? 439 PHE   B CD2   1 
ATOM   4928 C CE1   . PHE   B 1 313 ? 40.193  0.821   10.002 1.00 34.72  ? 439 PHE   B CE1   1 
ATOM   4929 C CE2   . PHE   B 1 313 ? 42.102  2.203   9.748  1.00 37.88  ? 439 PHE   B CE2   1 
ATOM   4930 C CZ    . PHE   B 1 313 ? 40.763  2.057   10.012 1.00 34.80  ? 439 PHE   B CZ    1 
ATOM   4931 N N     . HIS   B 1 314 ? 42.472  0.290   6.419  1.00 42.26  ? 440 HIS   B N     1 
ATOM   4932 C CA    . HIS   B 1 314 ? 42.786  1.565   5.796  1.00 40.41  ? 440 HIS   B CA    1 
ATOM   4933 C C     . HIS   B 1 314 ? 41.752  2.552   6.304  1.00 38.16  ? 440 HIS   B C     1 
ATOM   4934 O O     . HIS   B 1 314 ? 40.629  2.162   6.638  1.00 38.54  ? 440 HIS   B O     1 
ATOM   4935 C CB    . HIS   B 1 314 ? 42.754  1.497   4.260  1.00 41.19  ? 440 HIS   B CB    1 
ATOM   4936 C CG    . HIS   B 1 314 ? 41.434  1.047   3.718  1.00 43.60  ? 440 HIS   B CG    1 
ATOM   4937 N ND1   . HIS   B 1 314 ? 41.131  -0.282  3.505  1.00 45.65  ? 440 HIS   B ND1   1 
ATOM   4938 C CD2   . HIS   B 1 314 ? 40.320  1.744   3.391  1.00 43.48  ? 440 HIS   B CD2   1 
ATOM   4939 C CE1   . HIS   B 1 314 ? 39.889  -0.382  3.065  1.00 44.63  ? 440 HIS   B CE1   1 
ATOM   4940 N NE2   . HIS   B 1 314 ? 39.373  0.833   2.991  1.00 42.81  ? 440 HIS   B NE2   1 
ATOM   4941 N N     . VAL   B 1 315 ? 42.135  3.827   6.391  1.00 39.86  ? 441 VAL   B N     1 
ATOM   4942 C CA    . VAL   B 1 315 ? 41.155  4.831   6.792  1.00 39.25  ? 441 VAL   B CA    1 
ATOM   4943 C C     . VAL   B 1 315 ? 40.041  4.843   5.761  1.00 35.54  ? 441 VAL   B C     1 
ATOM   4944 O O     . VAL   B 1 315 ? 40.292  4.904   4.549  1.00 41.49  ? 441 VAL   B O     1 
ATOM   4945 C CB    . VAL   B 1 315 ? 41.803  6.216   6.930  1.00 44.25  ? 441 VAL   B CB    1 
ATOM   4946 N N     . GLY   B 1 316 ? 38.815  4.808   6.242  1.00 36.16  ? 442 GLY   B N     1 
ATOM   4947 C CA    . GLY   B 1 316 ? 37.643  4.624   5.429  1.00 37.21  ? 442 GLY   B CA    1 
ATOM   4948 C C     . GLY   B 1 316 ? 37.050  3.244   5.536  1.00 38.37  ? 442 GLY   B C     1 
ATOM   4949 O O     . GLY   B 1 316 ? 35.903  3.041   5.114  1.00 37.59  ? 442 GLY   B O     1 
ATOM   4950 N N     . LYS   B 1 317 ? 37.806  2.281   6.071  1.00 39.04  ? 443 LYS   B N     1 
ATOM   4951 C CA    . LYS   B 1 317 ? 37.248  0.953   6.263  1.00 38.71  ? 443 LYS   B CA    1 
ATOM   4952 C C     . LYS   B 1 317 ? 36.191  0.970   7.357  1.00 35.46  ? 443 LYS   B C     1 
ATOM   4953 O O     . LYS   B 1 317 ? 35.031  0.609   7.128  1.00 37.20  ? 443 LYS   B O     1 
ATOM   4954 C CB    . LYS   B 1 317 ? 38.359  -0.046  6.578  1.00 36.88  ? 443 LYS   B CB    1 
ATOM   4955 C CG    . LYS   B 1 317 ? 37.812  -1.376  7.006  1.00 38.26  ? 443 LYS   B CG    1 
ATOM   4956 C CD    . LYS   B 1 317 ? 38.766  -2.508  6.719  1.00 42.39  ? 443 LYS   B CD    1 
ATOM   4957 C CE    . LYS   B 1 317 ? 38.147  -3.833  7.120  1.00 44.12  ? 443 LYS   B CE    1 
ATOM   4958 N NZ    . LYS   B 1 317 ? 38.904  -4.961  6.487  1.00 53.62  ? 443 LYS   B NZ    1 
ATOM   4959 N N     . TYR   B 1 318 ? 36.581  1.382   8.561  1.00 32.79  ? 444 TYR   B N     1 
ATOM   4960 C CA    . TYR   B 1 318 ? 35.674  1.590   9.675  1.00 31.94  ? 444 TYR   B CA    1 
ATOM   4961 C C     . TYR   B 1 318 ? 36.359  2.583   10.592 1.00 31.36  ? 444 TYR   B C     1 
ATOM   4962 O O     . TYR   B 1 318 ? 37.524  2.935   10.389 1.00 30.13  ? 444 TYR   B O     1 
ATOM   4963 C CB    . TYR   B 1 318 ? 35.335  0.271   10.392 1.00 30.45  ? 444 TYR   B CB    1 
ATOM   4964 C CG    . TYR   B 1 318 ? 36.465  -0.330  11.208 1.00 29.88  ? 444 TYR   B CG    1 
ATOM   4965 C CD1   . TYR   B 1 318 ? 36.663  0.059   12.529 1.00 32.99  ? 444 TYR   B CD1   1 
ATOM   4966 C CD2   . TYR   B 1 318 ? 37.289  -1.309  10.681 1.00 37.30  ? 444 TYR   B CD2   1 
ATOM   4967 C CE1   . TYR   B 1 318 ? 37.671  -0.484  13.294 1.00 38.47  ? 444 TYR   B CE1   1 
ATOM   4968 C CE2   . TYR   B 1 318 ? 38.314  -1.856  11.435 1.00 38.62  ? 444 TYR   B CE2   1 
ATOM   4969 C CZ    . TYR   B 1 318 ? 38.489  -1.441  12.748 1.00 39.69  ? 444 TYR   B CZ    1 
ATOM   4970 O OH    . TYR   B 1 318 ? 39.495  -1.984  13.524 1.00 46.29  ? 444 TYR   B OH    1 
ATOM   4971 N N     . GLU   B 1 319 ? 35.638  3.028   11.618 1.00 28.82  ? 445 GLU   B N     1 
ATOM   4972 C CA    . GLU   B 1 319 ? 36.281  3.850   12.629 1.00 30.34  ? 445 GLU   B CA    1 
ATOM   4973 C C     . GLU   B 1 319 ? 35.650  3.554   13.976 1.00 28.15  ? 445 GLU   B C     1 
ATOM   4974 O O     . GLU   B 1 319 ? 34.573  2.953   14.069 1.00 26.81  ? 445 GLU   B O     1 
ATOM   4975 C CB    . GLU   B 1 319 ? 36.165  5.351   12.319 1.00 30.29  ? 445 GLU   B CB    1 
ATOM   4976 C CG    . GLU   B 1 319 ? 34.730  5.867   12.405 1.00 30.27  ? 445 GLU   B CG    1 
ATOM   4977 C CD    . GLU   B 1 319 ? 34.585  7.313   11.934 1.00 31.83  ? 445 GLU   B CD    1 
ATOM   4978 O OE1   . GLU   B 1 319 ? 35.568  7.866   11.414 1.00 31.92  ? 445 GLU   B OE1   1 
ATOM   4979 O OE2   . GLU   B 1 319 ? 33.488  7.895   12.085 1.00 34.56  ? 445 GLU   B OE2   1 
ATOM   4980 N N     . PHE   B 1 320 ? 36.334  3.984   15.021 1.00 26.28  ? 446 PHE   B N     1 
ATOM   4981 C CA    . PHE   B 1 320 ? 35.724  4.030   16.340 1.00 25.29  ? 446 PHE   B CA    1 
ATOM   4982 C C     . PHE   B 1 320 ? 35.199  5.436   16.567 1.00 28.19  ? 446 PHE   B C     1 
ATOM   4983 O O     . PHE   B 1 320 ? 35.540  6.370   15.837 1.00 29.54  ? 446 PHE   B O     1 
ATOM   4984 C CB    . PHE   B 1 320 ? 36.723  3.636   17.434 1.00 29.61  ? 446 PHE   B CB    1 
ATOM   4985 C CG    . PHE   B 1 320 ? 37.170  2.209   17.340 1.00 28.56  ? 446 PHE   B CG    1 
ATOM   4986 C CD1   . PHE   B 1 320 ? 36.354  1.187   17.791 1.00 29.82  ? 446 PHE   B CD1   1 
ATOM   4987 C CD2   . PHE   B 1 320 ? 38.407  1.888   16.791 1.00 30.69  ? 446 PHE   B CD2   1 
ATOM   4988 C CE1   . PHE   B 1 320 ? 36.750  -0.135  17.684 1.00 30.93  ? 446 PHE   B CE1   1 
ATOM   4989 C CE2   . PHE   B 1 320 ? 38.808  0.571   16.704 1.00 31.45  ? 446 PHE   B CE2   1 
ATOM   4990 C CZ    . PHE   B 1 320 ? 37.968  -0.435  17.137 1.00 31.68  ? 446 PHE   B CZ    1 
ATOM   4991 N N     . GLN   B 1 321 ? 34.311  5.570   17.547 1.00 28.40  ? 447 GLN   B N     1 
ATOM   4992 C CA    . GLN   B 1 321 ? 33.800  6.881   17.931 1.00 27.93  ? 447 GLN   B CA    1 
ATOM   4993 C C     . GLN   B 1 321 ? 33.657  6.948   19.445 1.00 29.20  ? 447 GLN   B C     1 
ATOM   4994 O O     . GLN   B 1 321 ? 33.442  5.936   20.107 1.00 29.39  ? 447 GLN   B O     1 
ATOM   4995 C CB    . GLN   B 1 321 ? 32.449  7.181   17.277 1.00 27.30  ? 447 GLN   B CB    1 
ATOM   4996 C CG    . GLN   B 1 321 ? 32.510  7.215   15.779 1.00 28.41  ? 447 GLN   B CG    1 
ATOM   4997 C CD    . GLN   B 1 321 ? 31.269  7.832   15.200 1.00 30.23  ? 447 GLN   B CD    1 
ATOM   4998 O OE1   . GLN   B 1 321 ? 30.253  7.950   15.884 1.00 33.17  ? 447 GLN   B OE1   1 
ATOM   4999 N NE2   . GLN   B 1 321 ? 31.347  8.262   13.957 1.00 31.51  ? 447 GLN   B NE2   1 
ATOM   5000 N N     . CYS   B 1 322 ? 33.769  8.159   19.983 1.00 29.50  ? 448 CYS   B N     1 
ATOM   5001 C CA    . CYS   B 1 322 ? 33.617  8.374   21.405 1.00 30.58  ? 448 CYS   B CA    1 
ATOM   5002 C C     . CYS   B 1 322 ? 32.997  9.745   21.632 1.00 35.20  ? 448 CYS   B C     1 
ATOM   5003 O O     . CYS   B 1 322 ? 32.994  10.607  20.745 1.00 35.16  ? 448 CYS   B O     1 
ATOM   5004 C CB    . CYS   B 1 322 ? 34.959  8.277   22.129 1.00 30.72  ? 448 CYS   B CB    1 
ATOM   5005 S SG    . CYS   B 1 322 ? 36.027  9.666   21.758 1.00 36.04  ? 448 CYS   B SG    1 
ATOM   5006 N N     . LEU   B 1 323 ? 32.461  9.934   22.825 1.00 33.26  ? 449 LEU   B N     1 
ATOM   5007 C CA    . LEU   B 1 323 ? 31.937  11.230  23.238 1.00 35.39  ? 449 LEU   B CA    1 
ATOM   5008 C C     . LEU   B 1 323 ? 33.045  12.052  23.873 1.00 38.53  ? 449 LEU   B C     1 
ATOM   5009 O O     . LEU   B 1 323 ? 33.842  11.534  24.662 1.00 39.36  ? 449 LEU   B O     1 
ATOM   5010 C CB    . LEU   B 1 323 ? 30.782  11.066  24.227 1.00 36.42  ? 449 LEU   B CB    1 
ATOM   5011 C CG    . LEU   B 1 323 ? 29.571  10.282  23.728 1.00 35.72  ? 449 LEU   B CG    1 
ATOM   5012 C CD1   . LEU   B 1 323 ? 28.536  10.061  24.829 1.00 41.19  ? 449 LEU   B CD1   1 
ATOM   5013 C CD2   . LEU   B 1 323 ? 28.969  10.979  22.533 1.00 35.80  ? 449 LEU   B CD2   1 
ATOM   5014 N N     . HIS   B 1 324 ? 33.096  13.332  23.513 1.00 40.90  ? 450 HIS   B N     1 
ATOM   5015 C CA    . HIS   B 1 324 ? 34.019  14.261  24.144 1.00 41.63  ? 450 HIS   B CA    1 
ATOM   5016 C C     . HIS   B 1 324 ? 33.852  14.209  25.654 1.00 46.44  ? 450 HIS   B C     1 
ATOM   5017 O O     . HIS   B 1 324 ? 32.730  14.129  26.164 1.00 44.14  ? 450 HIS   B O     1 
ATOM   5018 C CB    . HIS   B 1 324 ? 33.764  15.684  23.647 1.00 45.73  ? 450 HIS   B CB    1 
ATOM   5019 C CG    . HIS   B 1 324 ? 34.459  16.742  24.445 1.00 51.42  ? 450 HIS   B CG    1 
ATOM   5020 N ND1   . HIS   B 1 324 ? 35.825  16.924  24.411 1.00 51.68  ? 450 HIS   B ND1   1 
ATOM   5021 C CD2   . HIS   B 1 324 ? 33.977  17.675  25.301 1.00 53.81  ? 450 HIS   B CD2   1 
ATOM   5022 C CE1   . HIS   B 1 324 ? 36.153  17.926  25.208 1.00 52.44  ? 450 HIS   B CE1   1 
ATOM   5023 N NE2   . HIS   B 1 324 ? 35.050  18.397  25.761 1.00 56.05  ? 450 HIS   B NE2   1 
ATOM   5024 N N     . GLY   B 1 325 ? 34.981  14.253  26.363 1.00 48.70  ? 451 GLY   B N     1 
ATOM   5025 C CA    . GLY   B 1 325 ? 34.979  14.189  27.810 1.00 47.00  ? 451 GLY   B CA    1 
ATOM   5026 C C     . GLY   B 1 325 ? 34.904  12.792  28.382 1.00 47.07  ? 451 GLY   B C     1 
ATOM   5027 O O     . GLY   B 1 325 ? 35.039  12.634  29.602 1.00 52.21  ? 451 GLY   B O     1 
ATOM   5028 N N     . MET   B 1 326 ? 34.683  11.781  27.552 1.00 46.40  ? 452 MET   B N     1 
ATOM   5029 C CA    . MET   B 1 326 ? 34.644  10.386  27.969 1.00 44.27  ? 452 MET   B CA    1 
ATOM   5030 C C     . MET   B 1 326 ? 35.687  9.525   27.282 1.00 42.35  ? 452 MET   B C     1 
ATOM   5031 O O     . MET   B 1 326 ? 36.312  8.686   27.932 1.00 40.95  ? 452 MET   B O     1 
ATOM   5032 C CB    . MET   B 1 326 ? 33.258  9.786   27.689 1.00 44.60  ? 452 MET   B CB    1 
ATOM   5033 C CG    . MET   B 1 326 ? 32.125  10.408  28.478 1.00 48.70  ? 452 MET   B CG    1 
ATOM   5034 S SD    . MET   B 1 326 ? 30.620  9.423   28.328 1.00 52.36  ? 452 MET   B SD    1 
ATOM   5035 C CE    . MET   B 1 326 ? 31.169  7.915   29.155 1.00 43.84  ? 452 MET   B CE    1 
ATOM   5036 N N     . GLY   B 1 327 ? 35.896  9.707   25.983 1.00 41.53  ? 453 GLY   B N     1 
ATOM   5037 C CA    . GLY   B 1 327 ? 36.639  8.723   25.224 1.00 39.62  ? 453 GLY   B CA    1 
ATOM   5038 C C     . GLY   B 1 327 ? 38.099  9.027   24.963 1.00 38.65  ? 453 GLY   B C     1 
ATOM   5039 O O     . GLY   B 1 327 ? 38.860  8.116   24.614 1.00 40.74  ? 453 GLY   B O     1 
ATOM   5040 N N     . GLU   B 1 328 ? 38.505  10.287  25.106 1.00 38.53  ? 454 GLU   B N     1 
ATOM   5041 C CA    . GLU   B 1 328 ? 39.865  10.651  24.709 1.00 41.50  ? 454 GLU   B CA    1 
ATOM   5042 C C     . GLU   B 1 328 ? 40.943  9.889   25.467 1.00 41.88  ? 454 GLU   B C     1 
ATOM   5043 O O     . GLU   B 1 328 ? 41.969  9.554   24.848 1.00 42.09  ? 454 GLU   B O     1 
ATOM   5044 C CB    . GLU   B 1 328 ? 40.076  12.163  24.848 1.00 43.70  ? 454 GLU   B CB    1 
ATOM   5045 C CG    . GLU   B 1 328 ? 39.270  12.970  23.836 1.00 43.95  ? 454 GLU   B CG    1 
ATOM   5046 C CD    . GLU   B 1 328 ? 37.988  13.545  24.424 1.00 46.54  ? 454 GLU   B CD    1 
ATOM   5047 O OE1   . GLU   B 1 328 ? 37.458  12.964  25.401 1.00 47.41  ? 454 GLU   B OE1   1 
ATOM   5048 O OE2   . GLU   B 1 328 ? 37.525  14.597  23.923 1.00 47.36  ? 454 GLU   B OE2   1 
ATOM   5049 N N     . PRO   B 1 329 ? 40.807  9.594   26.762 1.00 41.12  ? 455 PRO   B N     1 
ATOM   5050 C CA    . PRO   B 1 329 ? 41.838  8.758   27.395 1.00 41.51  ? 455 PRO   B CA    1 
ATOM   5051 C C     . PRO   B 1 329 ? 41.923  7.370   26.787 1.00 42.50  ? 455 PRO   B C     1 
ATOM   5052 O O     . PRO   B 1 329 ? 43.028  6.886   26.503 1.00 42.64  ? 455 PRO   B O     1 
ATOM   5053 C CB    . PRO   B 1 329 ? 41.405  8.733   28.867 1.00 40.19  ? 455 PRO   B CB    1 
ATOM   5054 C CG    . PRO   B 1 329 ? 40.749  10.052  29.063 1.00 39.05  ? 455 PRO   B CG    1 
ATOM   5055 C CD    . PRO   B 1 329 ? 39.964  10.259  27.778 1.00 39.96  ? 455 PRO   B CD    1 
ATOM   5056 N N     . LEU   B 1 330 ? 40.781  6.713   26.569 1.00 39.29  ? 456 LEU   B N     1 
ATOM   5057 C CA    . LEU   B 1 330 ? 40.810  5.386   25.971 1.00 37.89  ? 456 LEU   B CA    1 
ATOM   5058 C C     . LEU   B 1 330 ? 41.382  5.442   24.564 1.00 36.61  ? 456 LEU   B C     1 
ATOM   5059 O O     . LEU   B 1 330 ? 42.254  4.646   24.207 1.00 38.76  ? 456 LEU   B O     1 
ATOM   5060 C CB    . LEU   B 1 330 ? 39.414  4.771   25.953 1.00 35.60  ? 456 LEU   B CB    1 
ATOM   5061 C CG    . LEU   B 1 330 ? 39.326  3.451   25.185 1.00 34.47  ? 456 LEU   B CG    1 
ATOM   5062 C CD1   . LEU   B 1 330 ? 40.122  2.349   25.904 1.00 38.31  ? 456 LEU   B CD1   1 
ATOM   5063 C CD2   . LEU   B 1 330 ? 37.876  3.026   24.974 1.00 36.11  ? 456 LEU   B CD2   1 
ATOM   5064 N N     . TYR   B 1 331 ? 40.918  6.390   23.752 1.00 34.61  ? 457 TYR   B N     1 
ATOM   5065 C CA    . TYR   B 1 331 ? 41.344  6.388   22.360 1.00 37.59  ? 457 TYR   B CA    1 
ATOM   5066 C C     . TYR   B 1 331 ? 42.699  7.035   22.140 1.00 37.63  ? 457 TYR   B C     1 
ATOM   5067 O O     . TYR   B 1 331 ? 43.306  6.817   21.085 1.00 36.66  ? 457 TYR   B O     1 
ATOM   5068 C CB    . TYR   B 1 331 ? 40.268  7.042   21.514 1.00 34.60  ? 457 TYR   B CB    1 
ATOM   5069 C CG    . TYR   B 1 331 ? 39.126  6.081   21.352 1.00 34.89  ? 457 TYR   B CG    1 
ATOM   5070 C CD1   . TYR   B 1 331 ? 39.196  5.060   20.420 1.00 34.48  ? 457 TYR   B CD1   1 
ATOM   5071 C CD2   . TYR   B 1 331 ? 38.001  6.154   22.168 1.00 33.78  ? 457 TYR   B CD2   1 
ATOM   5072 C CE1   . TYR   B 1 331 ? 38.164  4.172   20.262 1.00 31.58  ? 457 TYR   B CE1   1 
ATOM   5073 C CE2   . TYR   B 1 331 ? 36.956  5.260   22.015 1.00 31.20  ? 457 TYR   B CE2   1 
ATOM   5074 C CZ    . TYR   B 1 331 ? 37.043  4.275   21.065 1.00 30.55  ? 457 TYR   B CZ    1 
ATOM   5075 O OH    . TYR   B 1 331 ? 36.013  3.381   20.890 1.00 30.76  ? 457 TYR   B OH    1 
ATOM   5076 N N     . GLU   B 1 332 ? 43.214  7.768   23.123 1.00 39.93  ? 458 GLU   B N     1 
ATOM   5077 C CA    . GLU   B 1 332 ? 44.635  8.075   23.104 1.00 39.79  ? 458 GLU   B CA    1 
ATOM   5078 C C     . GLU   B 1 332 ? 45.470  6.803   23.068 1.00 43.67  ? 458 GLU   B C     1 
ATOM   5079 O O     . GLU   B 1 332 ? 46.622  6.843   22.623 1.00 42.57  ? 458 GLU   B O     1 
ATOM   5080 C CB    . GLU   B 1 332 ? 45.021  8.916   24.323 1.00 42.40  ? 458 GLU   B CB    1 
ATOM   5081 N N     . GLU   B 1 333 ? 44.914  5.677   23.525 1.00 38.12  ? 459 GLU   B N     1 
ATOM   5082 C CA    . GLU   B 1 333 ? 45.606  4.398   23.467 1.00 41.59  ? 459 GLU   B CA    1 
ATOM   5083 C C     . GLU   B 1 333 ? 45.266  3.616   22.214 1.00 38.54  ? 459 GLU   B C     1 
ATOM   5084 O O     . GLU   B 1 333 ? 45.653  2.451   22.090 1.00 38.89  ? 459 GLU   B O     1 
ATOM   5085 C CB    . GLU   B 1 333 ? 45.283  3.572   24.714 1.00 41.34  ? 459 GLU   B CB    1 
ATOM   5086 C CG    . GLU   B 1 333 ? 45.441  4.366   25.986 1.00 42.40  ? 459 GLU   B CG    1 
ATOM   5087 C CD    . GLU   B 1 333 ? 46.883  4.779   26.238 1.00 48.46  ? 459 GLU   B CD    1 
ATOM   5088 O OE1   . GLU   B 1 333 ? 47.811  4.166   25.650 1.00 46.38  ? 459 GLU   B OE1   1 
ATOM   5089 O OE2   . GLU   B 1 333 ? 47.088  5.729   27.025 1.00 51.54  ? 459 GLU   B OE2   1 
ATOM   5090 N N     . VAL   B 1 334 ? 44.559  4.236   21.278 1.00 38.01  ? 460 VAL   B N     1 
ATOM   5091 C CA    . VAL   B 1 334 ? 44.037  3.564   20.097 1.00 35.55  ? 460 VAL   B CA    1 
ATOM   5092 C C     . VAL   B 1 334 ? 44.541  4.223   18.824 1.00 35.39  ? 460 VAL   B C     1 
ATOM   5093 O O     . VAL   B 1 334 ? 45.079  3.556   17.941 1.00 38.23  ? 460 VAL   B O     1 
ATOM   5094 C CB    . VAL   B 1 334 ? 42.496  3.526   20.114 1.00 34.39  ? 460 VAL   B CB    1 
ATOM   5095 C CG1   . VAL   B 1 334 ? 41.977  2.977   18.795 1.00 32.59  ? 460 VAL   B CG1   1 
ATOM   5096 C CG2   . VAL   B 1 334 ? 42.012  2.680   21.280 1.00 35.84  ? 460 VAL   B CG2   1 
ATOM   5097 N N     . VAL   B 1 335 ? 44.421  5.539   18.743 1.00 36.96  ? 461 VAL   B N     1 
ATOM   5098 C CA    . VAL   B 1 335 ? 44.745  6.311   17.548 1.00 37.71  ? 461 VAL   B CA    1 
ATOM   5099 C C     . VAL   B 1 335 ? 46.251  6.433   17.422 1.00 42.29  ? 461 VAL   B C     1 
ATOM   5100 O O     . VAL   B 1 335 ? 46.954  6.673   18.410 1.00 46.48  ? 461 VAL   B O     1 
ATOM   5101 C CB    . VAL   B 1 335 ? 44.082  7.700   17.621 1.00 43.31  ? 461 VAL   B CB    1 
ATOM   5102 C CG1   . VAL   B 1 335 ? 44.465  8.559   16.416 1.00 45.08  ? 461 VAL   B CG1   1 
ATOM   5103 C CG2   . VAL   B 1 335 ? 42.591  7.552   17.695 1.00 38.01  ? 461 VAL   B CG2   1 
ATOM   5104 N N     . GLY   B 1 336 ? 46.753  6.272   16.212 1.00 41.95  ? 462 GLY   B N     1 
ATOM   5105 C CA    . GLY   B 1 336 ? 48.179  6.492   16.069 1.00 46.61  ? 462 GLY   B CA    1 
ATOM   5106 C C     . GLY   B 1 336 ? 48.936  5.197   15.826 1.00 47.29  ? 462 GLY   B C     1 
ATOM   5107 O O     . GLY   B 1 336 ? 48.578  4.126   16.340 1.00 45.20  ? 462 GLY   B O     1 
ATOM   5108 N N     . ARG   B 1 337 ? 50.025  5.309   15.050 1.00 47.92  ? 463 ARG   B N     1 
ATOM   5109 C CA    . ARG   B 1 337 ? 50.814  4.143   14.662 1.00 47.90  ? 463 ARG   B CA    1 
ATOM   5110 C C     . ARG   B 1 337 ? 51.366  3.408   15.875 1.00 49.97  ? 463 ARG   B C     1 
ATOM   5111 O O     . ARG   B 1 337 ? 51.433  2.173   15.880 1.00 53.44  ? 463 ARG   B O     1 
ATOM   5112 C CB    . ARG   B 1 337 ? 51.958  4.564   13.732 1.00 48.98  ? 463 ARG   B CB    1 
ATOM   5113 N N     . GLY   B 1 338 ? 51.765  4.144   16.915 1.00 46.85  ? 464 GLY   B N     1 
ATOM   5114 C CA    . GLY   B 1 338 ? 52.324  3.499   18.093 1.00 50.43  ? 464 GLY   B CA    1 
ATOM   5115 C C     . GLY   B 1 338 ? 51.316  2.710   18.906 1.00 48.07  ? 464 GLY   B C     1 
ATOM   5116 O O     . GLY   B 1 338 ? 51.708  1.818   19.668 1.00 51.41  ? 464 GLY   B O     1 
ATOM   5117 N N     . LYS   B 1 339 ? 50.031  3.008   18.751 1.00 45.04  ? 465 LYS   B N     1 
ATOM   5118 C CA    . LYS   B 1 339 ? 48.978  2.349   19.507 1.00 43.59  ? 465 LYS   B CA    1 
ATOM   5119 C C     . LYS   B 1 339 ? 48.310  1.277   18.658 1.00 43.30  ? 465 LYS   B C     1 
ATOM   5120 O O     . LYS   B 1 339 ? 48.991  0.374   18.160 1.00 45.13  ? 465 LYS   B O     1 
ATOM   5121 C CB    . LYS   B 1 339 ? 47.968  3.385   19.991 1.00 42.11  ? 465 LYS   B CB    1 
ATOM   5122 C CG    . LYS   B 1 339 ? 48.615  4.420   20.882 1.00 45.30  ? 465 LYS   B CG    1 
ATOM   5123 C CD    . LYS   B 1 339 ? 49.370  3.727   22.004 1.00 43.42  ? 465 LYS   B CD    1 
ATOM   5124 C CE    . LYS   B 1 339 ? 50.275  4.698   22.741 1.00 56.26  ? 465 LYS   B CE    1 
ATOM   5125 N NZ    . LYS   B 1 339 ? 49.512  5.877   23.234 1.00 57.88  ? 465 LYS   B NZ    1 
ATOM   5126 N N     . LEU   B 1 340 ? 46.990  1.367   18.473 1.00 37.65  ? 466 LEU   B N     1 
ATOM   5127 C CA    . LEU   B 1 340 ? 46.277  0.400   17.647 1.00 41.39  ? 466 LEU   B CA    1 
ATOM   5128 C C     . LEU   B 1 340 ? 46.147  0.834   16.195 1.00 42.19  ? 466 LEU   B C     1 
ATOM   5129 O O     . LEU   B 1 340 ? 45.731  0.019   15.364 1.00 41.39  ? 466 LEU   B O     1 
ATOM   5130 C CB    . LEU   B 1 340 ? 44.873  0.134   18.204 1.00 38.78  ? 466 LEU   B CB    1 
ATOM   5131 C CG    . LEU   B 1 340 ? 44.752  -0.405  19.630 1.00 35.70  ? 466 LEU   B CG    1 
ATOM   5132 C CD1   . LEU   B 1 340 ? 43.363  -0.985  19.846 1.00 38.12  ? 466 LEU   B CD1   1 
ATOM   5133 C CD2   . LEU   B 1 340 ? 45.818  -1.441  19.932 1.00 41.21  ? 466 LEU   B CD2   1 
ATOM   5134 N N     . ASP   B 1 341 ? 46.472  2.091   15.881 1.00 41.22  ? 467 ASP   B N     1 
ATOM   5135 C CA    . ASP   B 1 341 ? 46.485  2.591   14.505 1.00 39.72  ? 467 ASP   B CA    1 
ATOM   5136 C C     . ASP   B 1 341 ? 45.087  2.523   13.905 1.00 39.08  ? 467 ASP   B C     1 
ATOM   5137 O O     . ASP   B 1 341 ? 44.900  2.159   12.740 1.00 38.23  ? 467 ASP   B O     1 
ATOM   5138 C CB    . ASP   B 1 341 ? 47.492  1.833   13.636 1.00 45.37  ? 467 ASP   B CB    1 
ATOM   5139 C CG    . ASP   B 1 341 ? 47.789  2.551   12.336 1.00 45.80  ? 467 ASP   B CG    1 
ATOM   5140 O OD1   . ASP   B 1 341 ? 47.474  3.757   12.254 1.00 45.25  ? 467 ASP   B OD1   1 
ATOM   5141 O OD2   . ASP   B 1 341 ? 48.328  1.912   11.405 1.00 46.63  ? 467 ASP   B OD2   1 
ATOM   5142 N N     . ARG   B 1 342 ? 44.096  2.841   14.729 1.00 37.47  ? 468 ARG   B N     1 
ATOM   5143 C CA    . ARG   B 1 342 ? 42.731  2.910   14.256 1.00 35.31  ? 468 ARG   B CA    1 
ATOM   5144 C C     . ARG   B 1 342 ? 42.178  4.293   14.569 1.00 34.31  ? 468 ARG   B C     1 
ATOM   5145 O O     . ARG   B 1 342 ? 42.488  4.870   15.621 1.00 33.78  ? 468 ARG   B O     1 
ATOM   5146 C CB    . ARG   B 1 342 ? 41.854  1.822   14.890 1.00 35.21  ? 468 ARG   B CB    1 
ATOM   5147 C CG    . ARG   B 1 342 ? 42.269  0.398   14.569 1.00 37.34  ? 468 ARG   B CG    1 
ATOM   5148 C CD    . ARG   B 1 342 ? 42.095  0.083   13.079 1.00 36.01  ? 468 ARG   B CD    1 
ATOM   5149 N NE    . ARG   B 1 342 ? 42.544  -1.266  12.749 1.00 37.16  ? 468 ARG   B NE    1 
ATOM   5150 C CZ    . ARG   B 1 342 ? 43.768  -1.569  12.340 1.00 41.05  ? 468 ARG   B CZ    1 
ATOM   5151 N NH1   . ARG   B 1 342 ? 44.700  -0.639  12.202 1.00 42.51  ? 468 ARG   B NH1   1 
ATOM   5152 N NH2   . ARG   B 1 342 ? 44.058  -2.831  12.035 1.00 43.31  ? 468 ARG   B NH2   1 
ATOM   5153 N N     . PRO   B 1 343 ? 41.398  4.867   13.660 1.00 34.14  ? 469 PRO   B N     1 
ATOM   5154 C CA    . PRO   B 1 343 ? 40.870  6.211   13.884 1.00 33.79  ? 469 PRO   B CA    1 
ATOM   5155 C C     . PRO   B 1 343 ? 39.703  6.222   14.860 1.00 31.20  ? 469 PRO   B C     1 
ATOM   5156 O O     . PRO   B 1 343 ? 39.023  5.222   15.110 1.00 30.22  ? 469 PRO   B O     1 
ATOM   5157 C CB    . PRO   B 1 343 ? 40.412  6.642   12.487 1.00 32.75  ? 469 PRO   B CB    1 
ATOM   5158 C CG    . PRO   B 1 343 ? 40.037  5.365   11.842 1.00 34.96  ? 469 PRO   B CG    1 
ATOM   5159 C CD    . PRO   B 1 343 ? 41.053  4.360   12.325 1.00 36.09  ? 469 PRO   B CD    1 
ATOM   5160 N N     . CYS   B 1 344 ? 39.482  7.397   15.424 1.00 33.23  ? 470 CYS   B N     1 
ATOM   5161 C CA    . CYS   B 1 344 ? 38.370  7.591   16.334 1.00 30.63  ? 470 CYS   B CA    1 
ATOM   5162 C C     . CYS   B 1 344 ? 37.801  8.967   16.077 1.00 33.31  ? 470 CYS   B C     1 
ATOM   5163 O O     . CYS   B 1 344 ? 38.552  9.944   16.050 1.00 35.88  ? 470 CYS   B O     1 
ATOM   5164 C CB    . CYS   B 1 344 ? 38.802  7.473   17.793 1.00 31.97  ? 470 CYS   B CB    1 
ATOM   5165 S SG    . CYS   B 1 344 ? 37.453  7.897   18.922 1.00 35.07  ? 470 CYS   B SG    1 
ATOM   5166 N N     . ARG   B 1 345 ? 36.484  9.041   15.880 1.00 30.70  ? 471 ARG   B N     1 
ATOM   5167 C CA    . ARG   B 1 345 ? 35.796  10.315  15.727 1.00 30.60  ? 471 ARG   B CA    1 
ATOM   5168 C C     . ARG   B 1 345 ? 35.205  10.722  17.073 1.00 32.19  ? 471 ARG   B C     1 
ATOM   5169 O O     . ARG   B 1 345 ? 34.434  9.971   17.672 1.00 33.19  ? 471 ARG   B O     1 
ATOM   5170 C CB    . ARG   B 1 345 ? 34.709  10.215  14.661 1.00 30.22  ? 471 ARG   B CB    1 
ATOM   5171 C CG    . ARG   B 1 345 ? 33.943  11.502  14.420 1.00 34.77  ? 471 ARG   B CG    1 
ATOM   5172 C CD    . ARG   B 1 345 ? 32.979  11.330  13.249 1.00 30.67  ? 471 ARG   B CD    1 
ATOM   5173 N NE    . ARG   B 1 345 ? 33.642  10.686  12.120 1.00 30.94  ? 471 ARG   B NE    1 
ATOM   5174 C CZ    . ARG   B 1 345 ? 34.303  11.333  11.172 1.00 35.01  ? 471 ARG   B CZ    1 
ATOM   5175 N NH1   . ARG   B 1 345 ? 34.328  12.660  11.125 1.00 34.99  ? 471 ARG   B NH1   1 
ATOM   5176 N NH2   . ARG   B 1 345 ? 34.964  10.634  10.253 1.00 35.93  ? 471 ARG   B NH2   1 
ATOM   5177 N N     . ILE   B 1 346 ? 35.586  11.893  17.548 1.00 33.79  ? 472 ILE   B N     1 
ATOM   5178 C CA    . ILE   B 1 346 ? 35.077  12.427  18.805 1.00 35.55  ? 472 ILE   B CA    1 
ATOM   5179 C C     . ILE   B 1 346 ? 33.763  13.151  18.532 1.00 38.99  ? 472 ILE   B C     1 
ATOM   5180 O O     . ILE   B 1 346 ? 33.704  14.046  17.685 1.00 37.56  ? 472 ILE   B O     1 
ATOM   5181 C CB    . ILE   B 1 346 ? 36.096  13.372  19.450 1.00 40.27  ? 472 ILE   B CB    1 
ATOM   5182 C CG1   . ILE   B 1 346 ? 37.381  12.612  19.792 1.00 37.65  ? 472 ILE   B CG1   1 
ATOM   5183 C CG2   . ILE   B 1 346 ? 35.493  14.043  20.673 1.00 39.85  ? 472 ILE   B CG2   1 
ATOM   5184 C CD1   . ILE   B 1 346 ? 38.549  13.532  20.137 1.00 43.07  ? 472 ILE   B CD1   1 
ATOM   5185 N N     . TYR   B 1 347 ? 32.707  12.748  19.227 1.00 40.17  ? 473 TYR   B N     1 
ATOM   5186 C CA    . TYR   B 1 347 ? 31.434  13.461  19.194 1.00 38.79  ? 473 TYR   B CA    1 
ATOM   5187 C C     . TYR   B 1 347 ? 31.539  14.688  20.094 1.00 36.75  ? 473 TYR   B C     1 
ATOM   5188 O O     . TYR   B 1 347 ? 31.861  14.572  21.282 1.00 40.45  ? 473 TYR   B O     1 
ATOM   5189 C CB    . TYR   B 1 347 ? 30.310  12.544  19.672 1.00 39.38  ? 473 TYR   B CB    1 
ATOM   5190 C CG    . TYR   B 1 347 ? 28.912  13.022  19.352 1.00 39.54  ? 473 TYR   B CG    1 
ATOM   5191 C CD1   . TYR   B 1 347 ? 28.270  13.970  20.151 1.00 39.88  ? 473 TYR   B CD1   1 
ATOM   5192 C CD2   . TYR   B 1 347 ? 28.216  12.483  18.280 1.00 40.76  ? 473 TYR   B CD2   1 
ATOM   5193 C CE1   . TYR   B 1 347 ? 26.973  14.401  19.847 1.00 46.35  ? 473 TYR   B CE1   1 
ATOM   5194 C CE2   . TYR   B 1 347 ? 26.924  12.900  17.976 1.00 39.36  ? 473 TYR   B CE2   1 
ATOM   5195 C CZ    . TYR   B 1 347 ? 26.312  13.856  18.745 1.00 43.00  ? 473 TYR   B CZ    1 
ATOM   5196 O OH    . TYR   B 1 347 ? 25.029  14.238  18.408 1.00 46.81  ? 473 TYR   B OH    1 
ATOM   5197 N N     . ALA   B 1 348 ? 31.260  15.860  19.533 1.00 39.51  ? 474 ALA   B N     1 
ATOM   5198 C CA    . ALA   B 1 348 ? 31.462  17.126  20.228 1.00 43.64  ? 474 ALA   B CA    1 
ATOM   5199 C C     . ALA   B 1 348 ? 30.138  17.866  20.342 1.00 44.02  ? 474 ALA   B C     1 
ATOM   5200 O O     . ALA   B 1 348 ? 29.673  18.466  19.357 1.00 44.89  ? 474 ALA   B O     1 
ATOM   5201 C CB    . ALA   B 1 348 ? 32.497  17.978  19.497 1.00 47.26  ? 474 ALA   B CB    1 
ATOM   5202 N N     . PRO   B 1 349 ? 29.486  17.838  21.502 1.00 44.61  ? 475 PRO   B N     1 
ATOM   5203 C CA    . PRO   B 1 349 ? 28.279  18.650  21.683 1.00 48.84  ? 475 PRO   B CA    1 
ATOM   5204 C C     . PRO   B 1 349 ? 28.637  20.118  21.769 1.00 52.48  ? 475 PRO   B C     1 
ATOM   5205 O O     . PRO   B 1 349 ? 29.626  20.499  22.401 1.00 54.11  ? 475 PRO   B O     1 
ATOM   5206 C CB    . PRO   B 1 349 ? 27.694  18.148  23.010 1.00 47.03  ? 475 PRO   B CB    1 
ATOM   5207 C CG    . PRO   B 1 349 ? 28.419  16.863  23.304 1.00 47.02  ? 475 PRO   B CG    1 
ATOM   5208 C CD    . PRO   B 1 349 ? 29.761  16.986  22.670 1.00 46.89  ? 475 PRO   B CD    1 
ATOM   5209 N N     . VAL   B 1 350 ? 27.816  20.943  21.128 1.00 54.25  ? 476 VAL   B N     1 
ATOM   5210 C CA    . VAL   B 1 350 ? 27.993  22.388  21.107 1.00 60.41  ? 476 VAL   B CA    1 
ATOM   5211 C C     . VAL   B 1 350 ? 26.712  23.015  21.631 1.00 61.95  ? 476 VAL   B C     1 
ATOM   5212 O O     . VAL   B 1 350 ? 25.617  22.651  21.191 1.00 66.84  ? 476 VAL   B O     1 
ATOM   5213 C CB    . VAL   B 1 350 ? 28.317  22.903  19.689 1.00 58.22  ? 476 VAL   B CB    1 
ATOM   5214 N N     . GLY   B 1 351 ? 26.843  23.927  22.578 1.00 60.92  ? 477 GLY   B N     1 
ATOM   5215 C CA    . GLY   B 1 351 ? 25.676  24.616  23.088 1.00 66.56  ? 477 GLY   B CA    1 
ATOM   5216 C C     . GLY   B 1 351 ? 25.920  25.196  24.462 1.00 72.83  ? 477 GLY   B C     1 
ATOM   5217 O O     . GLY   B 1 351 ? 27.009  25.096  25.026 1.00 72.53  ? 477 GLY   B O     1 
ATOM   5218 N N     . THR   B 1 352 ? 24.863  25.824  24.985 1.00 76.00  ? 478 THR   B N     1 
ATOM   5219 C CA    . THR   B 1 352 ? 24.875  26.421  26.315 1.00 79.59  ? 478 THR   B CA    1 
ATOM   5220 C C     . THR   B 1 352 ? 24.435  25.391  27.346 1.00 83.45  ? 478 THR   B C     1 
ATOM   5221 O O     . THR   B 1 352 ? 24.760  24.208  27.216 1.00 82.19  ? 478 THR   B O     1 
ATOM   5222 C CB    . THR   B 1 352 ? 23.965  27.649  26.365 1.00 77.69  ? 478 THR   B CB    1 
ATOM   5223 N N     . HIS   B 1 353 ? 23.692  25.822  28.368 1.00 88.84  ? 479 HIS   B N     1 
ATOM   5224 C CA    . HIS   B 1 353 ? 23.207  24.899  29.388 1.00 85.83  ? 479 HIS   B CA    1 
ATOM   5225 C C     . HIS   B 1 353 ? 21.883  24.248  29.010 1.00 85.54  ? 479 HIS   B C     1 
ATOM   5226 O O     . HIS   B 1 353 ? 21.655  23.081  29.355 1.00 81.45  ? 479 HIS   B O     1 
ATOM   5227 C CB    . HIS   B 1 353 ? 23.062  25.620  30.729 1.00 82.09  ? 479 HIS   B CB    1 
ATOM   5228 N N     . GLU   B 1 354 ? 21.014  24.967  28.305 1.00 103.11 ? 480 GLU   B N     1 
ATOM   5229 C CA    . GLU   B 1 354 ? 19.753  24.392  27.861 1.00 103.02 ? 480 GLU   B CA    1 
ATOM   5230 C C     . GLU   B 1 354 ? 19.997  23.375  26.751 1.00 103.00 ? 480 GLU   B C     1 
ATOM   5231 O O     . GLU   B 1 354 ? 20.814  23.603  25.852 1.00 102.18 ? 480 GLU   B O     1 
ATOM   5232 C CB    . GLU   B 1 354 ? 18.808  25.494  27.380 1.00 106.58 ? 480 GLU   B CB    1 
ATOM   5233 N N     . THR   B 1 355 ? 19.276  22.246  26.836 1.00 93.33  ? 481 THR   B N     1 
ATOM   5234 C CA    . THR   B 1 355 ? 19.419  21.053  25.998 1.00 86.99  ? 481 THR   B CA    1 
ATOM   5235 C C     . THR   B 1 355 ? 20.662  20.259  26.382 1.00 80.92  ? 481 THR   B C     1 
ATOM   5236 O O     . THR   B 1 355 ? 20.679  19.028  26.258 1.00 78.21  ? 481 THR   B O     1 
ATOM   5237 C CB    . THR   B 1 355 ? 19.450  21.398  24.502 1.00 84.97  ? 481 THR   B CB    1 
ATOM   5238 N N     . LEU   B 1 356 ? 21.707  20.943  26.852 1.00 76.84  ? 482 LEU   B N     1 
ATOM   5239 C CA    . LEU   B 1 356 ? 22.886  20.226  27.321 1.00 67.84  ? 482 LEU   B CA    1 
ATOM   5240 C C     . LEU   B 1 356 ? 22.579  19.451  28.595 1.00 63.83  ? 482 LEU   B C     1 
ATOM   5241 O O     . LEU   B 1 356 ? 23.072  18.330  28.774 1.00 58.21  ? 482 LEU   B O     1 
ATOM   5242 C CB    . LEU   B 1 356 ? 24.042  21.196  27.550 1.00 70.84  ? 482 LEU   B CB    1 
ATOM   5243 N N     . LEU   B 1 357 ? 21.756  20.028  29.485 1.00 61.60  ? 483 LEU   B N     1 
ATOM   5244 C CA    . LEU   B 1 357 ? 21.380  19.344  30.720 1.00 54.67  ? 483 LEU   B CA    1 
ATOM   5245 C C     . LEU   B 1 357 ? 20.744  17.988  30.433 1.00 56.82  ? 483 LEU   B C     1 
ATOM   5246 O O     . LEU   B 1 357 ? 21.037  17.002  31.118 1.00 55.54  ? 483 LEU   B O     1 
ATOM   5247 C CB    . LEU   B 1 357 ? 20.432  20.223  31.548 1.00 59.18  ? 483 LEU   B CB    1 
ATOM   5248 N N     . ALA   B 1 358 ? 19.883  17.913  29.413 1.00 55.68  ? 484 ALA   B N     1 
ATOM   5249 C CA    . ALA   B 1 358 ? 19.294  16.632  29.027 1.00 55.88  ? 484 ALA   B CA    1 
ATOM   5250 C C     . ALA   B 1 358 ? 20.354  15.658  28.532 1.00 51.38  ? 484 ALA   B C     1 
ATOM   5251 O O     . ALA   B 1 358 ? 20.270  14.451  28.789 1.00 51.42  ? 484 ALA   B O     1 
ATOM   5252 C CB    . ALA   B 1 358 ? 18.233  16.845  27.949 1.00 59.44  ? 484 ALA   B CB    1 
ATOM   5253 N N     . TYR   B 1 359 ? 21.339  16.158  27.788 1.00 50.81  ? 485 TYR   B N     1 
ATOM   5254 C CA    . TYR   B 1 359 ? 22.482  15.338  27.408 1.00 48.86  ? 485 TYR   B CA    1 
ATOM   5255 C C     . TYR   B 1 359 ? 23.288  14.937  28.636 1.00 48.58  ? 485 TYR   B C     1 
ATOM   5256 O O     . TYR   B 1 359 ? 23.682  13.774  28.777 1.00 43.99  ? 485 TYR   B O     1 
ATOM   5257 C CB    . TYR   B 1 359 ? 23.343  16.115  26.413 1.00 47.22  ? 485 TYR   B CB    1 
ATOM   5258 C CG    . TYR   B 1 359 ? 24.625  15.448  25.955 1.00 45.72  ? 485 TYR   B CG    1 
ATOM   5259 C CD1   . TYR   B 1 359 ? 24.632  14.576  24.879 1.00 45.03  ? 485 TYR   B CD1   1 
ATOM   5260 C CD2   . TYR   B 1 359 ? 25.832  15.728  26.581 1.00 42.76  ? 485 TYR   B CD2   1 
ATOM   5261 C CE1   . TYR   B 1 359 ? 25.810  13.987  24.437 1.00 42.47  ? 485 TYR   B CE1   1 
ATOM   5262 C CE2   . TYR   B 1 359 ? 26.999  15.145  26.162 1.00 46.14  ? 485 TYR   B CE2   1 
ATOM   5263 C CZ    . TYR   B 1 359 ? 26.987  14.279  25.091 1.00 45.34  ? 485 TYR   B CZ    1 
ATOM   5264 O OH    . TYR   B 1 359 ? 28.164  13.707  24.679 1.00 45.69  ? 485 TYR   B OH    1 
ATOM   5265 N N     . LEU   B 1 360 ? 23.508  15.885  29.548 1.00 47.23  ? 486 LEU   B N     1 
ATOM   5266 C CA    . LEU   B 1 360 ? 24.295  15.607  30.746 1.00 46.86  ? 486 LEU   B CA    1 
ATOM   5267 C C     . LEU   B 1 360 ? 23.613  14.570  31.638 1.00 47.60  ? 486 LEU   B C     1 
ATOM   5268 O O     . LEU   B 1 360 ? 24.288  13.738  32.261 1.00 47.79  ? 486 LEU   B O     1 
ATOM   5269 C CB    . LEU   B 1 360 ? 24.551  16.909  31.504 1.00 50.58  ? 486 LEU   B CB    1 
ATOM   5270 N N     . VAL   B 1 361 ? 22.276  14.593  31.704 1.00 46.28  ? 487 VAL   B N     1 
ATOM   5271 C CA    . VAL   B 1 361 ? 21.550  13.565  32.452 1.00 45.76  ? 487 VAL   B CA    1 
ATOM   5272 C C     . VAL   B 1 361 ? 21.819  12.190  31.855 1.00 47.88  ? 487 VAL   B C     1 
ATOM   5273 O O     . VAL   B 1 361 ? 22.107  11.228  32.577 1.00 45.16  ? 487 VAL   B O     1 
ATOM   5274 C CB    . VAL   B 1 361 ? 20.043  13.876  32.491 1.00 48.14  ? 487 VAL   B CB    1 
ATOM   5275 C CG1   . VAL   B 1 361 ? 19.250  12.704  33.071 1.00 51.55  ? 487 VAL   B CG1   1 
ATOM   5276 C CG2   . VAL   B 1 361 ? 19.796  15.102  33.341 1.00 51.99  ? 487 VAL   B CG2   1 
ATOM   5277 N N     . ARG   B 1 362 ? 21.740  12.076  30.526 1.00 47.90  ? 488 ARG   B N     1 
ATOM   5278 C CA    . ARG   B 1 362 ? 22.071  10.801  29.892 1.00 41.19  ? 488 ARG   B CA    1 
ATOM   5279 C C     . ARG   B 1 362 ? 23.520  10.423  30.153 1.00 42.62  ? 488 ARG   B C     1 
ATOM   5280 O O     . ARG   B 1 362 ? 23.825  9.248   30.369 1.00 45.59  ? 488 ARG   B O     1 
ATOM   5281 C CB    . ARG   B 1 362 ? 21.755  10.836  28.397 1.00 44.49  ? 488 ARG   B CB    1 
ATOM   5282 C CG    . ARG   B 1 362 ? 20.255  10.956  28.152 1.00 44.88  ? 488 ARG   B CG    1 
ATOM   5283 C CD    . ARG   B 1 362 ? 19.906  10.609  26.726 1.00 43.86  ? 488 ARG   B CD    1 
ATOM   5284 N NE    . ARG   B 1 362 ? 20.573  11.488  25.771 1.00 45.91  ? 488 ARG   B NE    1 
ATOM   5285 C CZ    . ARG   B 1 362 ? 20.086  12.649  25.349 1.00 45.67  ? 488 ARG   B CZ    1 
ATOM   5286 N NH1   . ARG   B 1 362 ? 18.931  13.120  25.792 1.00 47.78  ? 488 ARG   B NH1   1 
ATOM   5287 N NH2   . ARG   B 1 362 ? 20.771  13.348  24.443 1.00 48.25  ? 488 ARG   B NH2   1 
ATOM   5288 N N     . ARG   B 1 363 ? 24.423  11.408  30.197 1.00 44.28  ? 489 ARG   B N     1 
ATOM   5289 C CA    . ARG   B 1 363 ? 25.806  11.109  30.570 1.00 45.15  ? 489 ARG   B CA    1 
ATOM   5290 C C     . ARG   B 1 363 ? 25.900  10.675  32.027 1.00 47.42  ? 489 ARG   B C     1 
ATOM   5291 O O     . ARG   B 1 363 ? 26.698  9.793   32.371 1.00 45.13  ? 489 ARG   B O     1 
ATOM   5292 C CB    . ARG   B 1 363 ? 26.710  12.316  30.326 1.00 45.83  ? 489 ARG   B CB    1 
ATOM   5293 C CG    . ARG   B 1 363 ? 26.802  12.751  28.868 1.00 46.57  ? 489 ARG   B CG    1 
ATOM   5294 C CD    . ARG   B 1 363 ? 27.542  11.741  27.971 1.00 42.32  ? 489 ARG   B CD    1 
ATOM   5295 N NE    . ARG   B 1 363 ? 26.799  10.516  27.699 1.00 39.23  ? 489 ARG   B NE    1 
ATOM   5296 C CZ    . ARG   B 1 363 ? 25.681  10.446  26.988 1.00 45.24  ? 489 ARG   B CZ    1 
ATOM   5297 N NH1   . ARG   B 1 363 ? 25.079  11.534  26.526 1.00 43.41  ? 489 ARG   B NH1   1 
ATOM   5298 N NH2   . ARG   B 1 363 ? 25.150  9.252   26.731 1.00 47.02  ? 489 ARG   B NH2   1 
ATOM   5299 N N     . LEU   B 1 364 ? 25.107  11.294  32.898 1.00 46.72  ? 490 LEU   B N     1 
ATOM   5300 C CA    . LEU   B 1 364 ? 25.108  10.878  34.292 1.00 47.37  ? 490 LEU   B CA    1 
ATOM   5301 C C     . LEU   B 1 364 ? 24.583  9.460   34.439 1.00 50.10  ? 490 LEU   B C     1 
ATOM   5302 O O     . LEU   B 1 364 ? 25.150  8.659   35.191 1.00 49.05  ? 490 LEU   B O     1 
ATOM   5303 C CB    . LEU   B 1 364 ? 24.275  11.832  35.138 1.00 45.92  ? 490 LEU   B CB    1 
ATOM   5304 C CG    . LEU   B 1 364 ? 24.270  11.441  36.611 1.00 46.86  ? 490 LEU   B CG    1 
ATOM   5305 C CD1   . LEU   B 1 364 ? 25.699  11.272  37.099 1.00 53.87  ? 490 LEU   B CD1   1 
ATOM   5306 C CD2   . LEU   B 1 364 ? 23.540  12.492  37.432 1.00 50.64  ? 490 LEU   B CD2   1 
ATOM   5307 N N     . LEU   B 1 365 ? 23.485  9.139   33.754 1.00 49.35  ? 491 LEU   B N     1 
ATOM   5308 C CA    . LEU   B 1 365 ? 22.958  7.785   33.855 1.00 49.40  ? 491 LEU   B CA    1 
ATOM   5309 C C     . LEU   B 1 365 ? 23.944  6.782   33.277 1.00 48.03  ? 491 LEU   B C     1 
ATOM   5310 O O     . LEU   B 1 365 ? 24.013  5.637   33.736 1.00 52.81  ? 491 LEU   B O     1 
ATOM   5311 C CB    . LEU   B 1 365 ? 21.604  7.701   33.150 1.00 48.55  ? 491 LEU   B CB    1 
ATOM   5312 C CG    . LEU   B 1 365 ? 20.479  8.478   33.835 1.00 49.35  ? 491 LEU   B CG    1 
ATOM   5313 C CD1   . LEU   B 1 365 ? 19.265  8.491   32.935 1.00 55.59  ? 491 LEU   B CD1   1 
ATOM   5314 C CD2   . LEU   B 1 365 ? 20.140  7.857   35.175 1.00 52.61  ? 491 LEU   B CD2   1 
ATOM   5315 N N     . GLU   B 1 366 ? 24.741  7.213   32.304 1.00 45.35  ? 492 GLU   B N     1 
ATOM   5316 C CA    . GLU   B 1 366 ? 25.753  6.357   31.700 1.00 47.37  ? 492 GLU   B CA    1 
ATOM   5317 C C     . GLU   B 1 366 ? 26.978  6.237   32.595 1.00 46.79  ? 492 GLU   B C     1 
ATOM   5318 O O     . GLU   B 1 366 ? 27.482  5.138   32.821 1.00 48.71  ? 492 GLU   B O     1 
ATOM   5319 C CB    . GLU   B 1 366 ? 26.144  6.915   30.335 1.00 44.81  ? 492 GLU   B CB    1 
ATOM   5320 C CG    . GLU   B 1 366 ? 27.166  6.113   29.575 1.00 43.12  ? 492 GLU   B CG    1 
ATOM   5321 C CD    . GLU   B 1 366 ? 27.563  6.816   28.291 1.00 44.30  ? 492 GLU   B CD    1 
ATOM   5322 O OE1   . GLU   B 1 366 ? 27.060  7.940   28.053 1.00 44.60  ? 492 GLU   B OE1   1 
ATOM   5323 O OE2   . GLU   B 1 366 ? 28.372  6.254   27.520 1.00 44.54  ? 492 GLU   B OE2   1 
ATOM   5324 N N     . ASN   B 1 367 ? 27.475  7.356   33.109 1.00 46.44  ? 493 ASN   B N     1 
ATOM   5325 C CA    . ASN   B 1 367 ? 28.710  7.337   33.878 1.00 50.65  ? 493 ASN   B CA    1 
ATOM   5326 C C     . ASN   B 1 367 ? 28.512  6.833   35.302 1.00 49.62  ? 493 ASN   B C     1 
ATOM   5327 O O     . ASN   B 1 367 ? 29.495  6.457   35.954 1.00 53.06  ? 493 ASN   B O     1 
ATOM   5328 C CB    . ASN   B 1 367 ? 29.335  8.738   33.887 1.00 50.50  ? 493 ASN   B CB    1 
ATOM   5329 C CG    . ASN   B 1 367 ? 30.092  9.053   32.602 1.00 53.38  ? 493 ASN   B CG    1 
ATOM   5330 O OD1   . ASN   B 1 367 ? 31.301  8.818   32.513 1.00 56.36  ? 493 ASN   B OD1   1 
ATOM   5331 N ND2   . ASN   B 1 367 ? 29.387  9.577   31.596 1.00 49.83  ? 493 ASN   B ND2   1 
ATOM   5332 N N     . GLY   B 1 368 ? 27.275  6.809   35.800 1.00 50.71  ? 494 GLY   B N     1 
ATOM   5333 C CA    . GLY   B 1 368 ? 27.020  6.474   37.189 1.00 52.18  ? 494 GLY   B CA    1 
ATOM   5334 C C     . GLY   B 1 368 ? 26.448  5.091   37.430 1.00 53.25  ? 494 GLY   B C     1 
ATOM   5335 O O     . GLY   B 1 368 ? 26.373  4.639   38.576 1.00 50.96  ? 494 GLY   B O     1 
ATOM   5336 N N     . ALA   B 1 369 ? 26.042  4.404   36.366 1.00 50.97  ? 495 ALA   B N     1 
ATOM   5337 C CA    . ALA   B 1 369 ? 25.411  3.099   36.518 1.00 51.22  ? 495 ALA   B CA    1 
ATOM   5338 C C     . ALA   B 1 369 ? 26.446  2.022   36.849 1.00 48.47  ? 495 ALA   B C     1 
ATOM   5339 O O     . ALA   B 1 369 ? 27.535  1.976   36.257 1.00 46.20  ? 495 ALA   B O     1 
ATOM   5340 C CB    . ALA   B 1 369 ? 24.655  2.739   35.238 1.00 50.21  ? 495 ALA   B CB    1 
ATOM   5341 N N     . ASN   B 1 370 ? 26.081  1.129   37.775 1.00 50.94  ? 496 ASN   B N     1 
ATOM   5342 C CA    . ASN   B 1 370 ? 26.999  0.095   38.248 1.00 48.80  ? 496 ASN   B CA    1 
ATOM   5343 C C     . ASN   B 1 370 ? 27.406  -0.864  37.137 1.00 48.13  ? 496 ASN   B C     1 
ATOM   5344 O O     . ASN   B 1 370 ? 28.456  -1.506  37.239 1.00 48.58  ? 496 ASN   B O     1 
ATOM   5345 C CB    . ASN   B 1 370 ? 26.367  -0.682  39.407 1.00 51.94  ? 496 ASN   B CB    1 
ATOM   5346 N N     . SER   B 1 371 ? 26.613  -0.957  36.074 1.00 48.56  ? 497 SER   B N     1 
ATOM   5347 C CA    . SER   B 1 371 ? 26.912  -1.813  34.935 1.00 44.22  ? 497 SER   B CA    1 
ATOM   5348 C C     . SER   B 1 371 ? 27.773  -1.131  33.878 1.00 42.70  ? 497 SER   B C     1 
ATOM   5349 O O     . SER   B 1 371 ? 28.311  -1.815  33.000 1.00 42.93  ? 497 SER   B O     1 
ATOM   5350 C CB    . SER   B 1 371 ? 25.604  -2.301  34.299 1.00 42.27  ? 497 SER   B CB    1 
ATOM   5351 O OG    . SER   B 1 371 ? 24.865  -1.216  33.768 1.00 43.88  ? 497 SER   B OG    1 
ATOM   5352 N N     . SER   B 1 372 ? 27.914  0.190   33.929 1.00 40.37  ? 498 SER   B N     1 
ATOM   5353 C CA    . SER   B 1 372 ? 28.677  0.899   32.917 1.00 40.18  ? 498 SER   B CA    1 
ATOM   5354 C C     . SER   B 1 372 ? 30.172  0.664   33.064 1.00 39.98  ? 498 SER   B C     1 
ATOM   5355 O O     . SER   B 1 372 ? 30.722  0.713   34.166 1.00 38.88  ? 498 SER   B O     1 
ATOM   5356 C CB    . SER   B 1 372 ? 28.385  2.385   33.005 1.00 45.65  ? 498 SER   B CB    1 
ATOM   5357 O OG    . SER   B 1 372 ? 27.059  2.641   32.590 1.00 45.21  ? 498 SER   B OG    1 
ATOM   5358 N N     . PHE   B 1 373 ? 30.825  0.409   31.932 1.00 38.51  ? 499 PHE   B N     1 
ATOM   5359 C CA    . PHE   B 1 373 ? 32.276  0.255   31.904 1.00 39.17  ? 499 PHE   B CA    1 
ATOM   5360 C C     . PHE   B 1 373 ? 32.986  1.440   32.544 1.00 40.99  ? 499 PHE   B C     1 
ATOM   5361 O O     . PHE   B 1 373 ? 33.920  1.266   33.333 1.00 41.81  ? 499 PHE   B O     1 
ATOM   5362 C CB    . PHE   B 1 373 ? 32.748  0.086   30.457 1.00 36.93  ? 499 PHE   B CB    1 
ATOM   5363 C CG    . PHE   B 1 373 ? 34.247  0.035   30.315 1.00 35.34  ? 499 PHE   B CG    1 
ATOM   5364 C CD1   . PHE   B 1 373 ? 34.919  -1.174  30.402 1.00 38.50  ? 499 PHE   B CD1   1 
ATOM   5365 C CD2   . PHE   B 1 373 ? 34.980  1.193   30.084 1.00 36.73  ? 499 PHE   B CD2   1 
ATOM   5366 C CE1   . PHE   B 1 373 ? 36.303  -1.229  30.270 1.00 39.73  ? 499 PHE   B CE1   1 
ATOM   5367 C CE2   . PHE   B 1 373 ? 36.359  1.146   29.944 1.00 38.96  ? 499 PHE   B CE2   1 
ATOM   5368 C CZ    . PHE   B 1 373 ? 37.019  -0.069  30.035 1.00 40.33  ? 499 PHE   B CZ    1 
ATOM   5369 N N     . VAL   B 1 374 ? 32.579  2.662   32.189 1.00 41.21  ? 500 VAL   B N     1 
ATOM   5370 C CA    . VAL   B 1 374 ? 33.280  3.832   32.701 1.00 44.58  ? 500 VAL   B CA    1 
ATOM   5371 C C     . VAL   B 1 374 ? 33.089  3.987   34.204 1.00 47.23  ? 500 VAL   B C     1 
ATOM   5372 O O     . VAL   B 1 374 ? 33.916  4.621   34.868 1.00 52.45  ? 500 VAL   B O     1 
ATOM   5373 C CB    . VAL   B 1 374 ? 32.846  5.104   31.943 1.00 43.61  ? 500 VAL   B CB    1 
ATOM   5374 C CG1   . VAL   B 1 374 ? 33.099  4.927   30.451 1.00 41.73  ? 500 VAL   B CG1   1 
ATOM   5375 C CG2   . VAL   B 1 374 ? 31.387  5.429   32.211 1.00 44.71  ? 500 VAL   B CG2   1 
ATOM   5376 N N     . HIS   B 1 375 ? 32.033  3.398   34.772 1.00 46.21  ? 501 HIS   B N     1 
ATOM   5377 C CA    . HIS   B 1 375 ? 31.912  3.339   36.219 1.00 47.53  ? 501 HIS   B CA    1 
ATOM   5378 C C     . HIS   B 1 375 ? 32.757  2.202   36.782 1.00 46.65  ? 501 HIS   B C     1 
ATOM   5379 O O     . HIS   B 1 375 ? 33.488  2.383   37.764 1.00 47.77  ? 501 HIS   B O     1 
ATOM   5380 C CB    . HIS   B 1 375 ? 30.445  3.171   36.623 1.00 49.77  ? 501 HIS   B CB    1 
ATOM   5381 C CG    . HIS   B 1 375 ? 30.221  3.128   38.110 1.00 51.47  ? 501 HIS   B CG    1 
ATOM   5382 N ND1   . HIS   B 1 375 ? 30.222  1.953   38.837 1.00 53.92  ? 501 HIS   B ND1   1 
ATOM   5383 C CD2   . HIS   B 1 375 ? 29.990  4.120   39.007 1.00 55.53  ? 501 HIS   B CD2   1 
ATOM   5384 C CE1   . HIS   B 1 375 ? 30.002  2.224   40.112 1.00 57.96  ? 501 HIS   B CE1   1 
ATOM   5385 N NE2   . HIS   B 1 375 ? 29.855  3.531   40.241 1.00 58.74  ? 501 HIS   B NE2   1 
ATOM   5386 N N     . ARG   B 1 376 ? 32.678  1.029   36.152 1.00 47.61  ? 502 ARG   B N     1 
ATOM   5387 C CA    . ARG   B 1 376 ? 33.408  -0.134  36.644 1.00 43.07  ? 502 ARG   B CA    1 
ATOM   5388 C C     . ARG   B 1 376 ? 34.909  0.079   36.576 1.00 43.85  ? 502 ARG   B C     1 
ATOM   5389 O O     . ARG   B 1 376 ? 35.639  -0.404  37.447 1.00 47.60  ? 502 ARG   B O     1 
ATOM   5390 C CB    . ARG   B 1 376 ? 32.999  -1.372  35.844 1.00 41.18  ? 502 ARG   B CB    1 
ATOM   5391 C CG    . ARG   B 1 376 ? 31.566  -1.783  36.106 1.00 43.61  ? 502 ARG   B CG    1 
ATOM   5392 C CD    . ARG   B 1 376 ? 30.983  -2.643  35.003 1.00 45.05  ? 502 ARG   B CD    1 
ATOM   5393 N NE    . ARG   B 1 376 ? 31.741  -3.853  34.715 1.00 44.29  ? 502 ARG   B NE    1 
ATOM   5394 C CZ    . ARG   B 1 376 ? 31.658  -4.972  35.423 1.00 53.43  ? 502 ARG   B CZ    1 
ATOM   5395 N NH1   . ARG   B 1 376 ? 30.946  -5.033  36.536 1.00 54.62  ? 502 ARG   B NH1   1 
ATOM   5396 N NH2   . ARG   B 1 376 ? 32.305  -6.056  35.003 1.00 52.01  ? 502 ARG   B NH2   1 
ATOM   5397 N N     . ILE   B 1 377 ? 35.393  0.810   35.569 1.00 45.36  ? 503 ILE   B N     1 
ATOM   5398 C CA    . ILE   B 1 377 ? 36.834  1.024   35.491 1.00 48.39  ? 503 ILE   B CA    1 
ATOM   5399 C C     . ILE   B 1 377 ? 37.327  1.828   36.695 1.00 51.15  ? 503 ILE   B C     1 
ATOM   5400 O O     . ILE   B 1 377 ? 38.484  1.683   37.117 1.00 48.76  ? 503 ILE   B O     1 
ATOM   5401 C CB    . ILE   B 1 377 ? 37.209  1.676   34.145 1.00 48.51  ? 503 ILE   B CB    1 
ATOM   5402 C CG1   . ILE   B 1 377 ? 38.716  1.578   33.925 1.00 50.20  ? 503 ILE   B CG1   1 
ATOM   5403 C CG2   . ILE   B 1 377 ? 36.758  3.124   34.090 1.00 47.93  ? 503 ILE   B CG2   1 
ATOM   5404 C CD1   . ILE   B 1 377 ? 39.100  1.378   32.494 1.00 50.24  ? 503 ILE   B CD1   1 
ATOM   5405 N N     . ASN   B 1 378 ? 36.463  2.639   37.303 1.00 50.12  ? 504 ASN   B N     1 
ATOM   5406 C CA    . ASN   B 1 378 ? 36.827  3.386   38.501 1.00 53.46  ? 504 ASN   B CA    1 
ATOM   5407 C C     . ASN   B 1 378 ? 36.376  2.713   39.791 1.00 54.23  ? 504 ASN   B C     1 
ATOM   5408 O O     . ASN   B 1 378 ? 36.562  3.286   40.870 1.00 57.11  ? 504 ASN   B O     1 
ATOM   5409 C CB    . ASN   B 1 378 ? 36.248  4.804   38.441 1.00 55.98  ? 504 ASN   B CB    1 
ATOM   5410 C CG    . ASN   B 1 378 ? 36.809  5.623   37.284 1.00 57.39  ? 504 ASN   B CG    1 
ATOM   5411 O OD1   . ASN   B 1 378 ? 38.023  5.691   37.075 1.00 60.87  ? 504 ASN   B OD1   1 
ATOM   5412 N ND2   . ASN   B 1 378 ? 35.922  6.245   36.525 1.00 58.07  ? 504 ASN   B ND2   1 
ATOM   5413 N N     . ASP   B 1 379 ? 35.789  1.522   39.719 1.00 55.37  ? 505 ASP   B N     1 
ATOM   5414 C CA    . ASP   B 1 379 ? 35.297  0.856   40.921 1.00 55.76  ? 505 ASP   B CA    1 
ATOM   5415 C C     . ASP   B 1 379 ? 36.382  -0.042  41.500 1.00 61.37  ? 505 ASP   B C     1 
ATOM   5416 O O     . ASP   B 1 379 ? 36.868  -0.938  40.796 1.00 57.76  ? 505 ASP   B O     1 
ATOM   5417 C CB    . ASP   B 1 379 ? 34.051  0.043   40.610 1.00 57.44  ? 505 ASP   B CB    1 
ATOM   5418 C CG    . ASP   B 1 379 ? 33.441  -0.603  41.843 1.00 62.68  ? 505 ASP   B CG    1 
ATOM   5419 O OD1   . ASP   B 1 379 ? 33.949  -0.392  42.956 1.00 61.92  ? 505 ASP   B OD1   1 
ATOM   5420 O OD2   . ASP   B 1 379 ? 32.437  -1.329  41.691 1.00 69.53  ? 505 ASP   B OD2   1 
ATOM   5421 N N     . PRO   B 1 380 ? 36.787  0.155   42.760 1.00 62.46  ? 506 PRO   B N     1 
ATOM   5422 C CA    . PRO   B 1 380 ? 37.823  -0.715  43.347 1.00 67.56  ? 506 PRO   B CA    1 
ATOM   5423 C C     . PRO   B 1 380 ? 37.433  -2.182  43.441 1.00 67.42  ? 506 PRO   B C     1 
ATOM   5424 O O     . PRO   B 1 380 ? 38.321  -3.045  43.413 1.00 74.23  ? 506 PRO   B O     1 
ATOM   5425 C CB    . PRO   B 1 380 ? 38.041  -0.108  44.746 1.00 65.38  ? 506 PRO   B CB    1 
ATOM   5426 C CG    . PRO   B 1 380 ? 36.808  0.727   45.015 1.00 65.41  ? 506 PRO   B CG    1 
ATOM   5427 C CD    . PRO   B 1 380 ? 36.424  1.263   43.659 1.00 64.92  ? 506 PRO   B CD    1 
ATOM   5428 N N     . LYS   B 1 381 ? 36.145  -2.501  43.578 1.00 67.31  ? 507 LYS   B N     1 
ATOM   5429 C CA    . LYS   B 1 381 ? 35.730  -3.891  43.726 1.00 64.29  ? 507 LYS   B CA    1 
ATOM   5430 C C     . LYS   B 1 381 ? 35.737  -4.661  42.410 1.00 61.65  ? 507 LYS   B C     1 
ATOM   5431 O O     . LYS   B 1 381 ? 35.665  -5.894  42.429 1.00 58.64  ? 507 LYS   B O     1 
ATOM   5432 C CB    . LYS   B 1 381 ? 34.336  -3.961  44.353 1.00 68.52  ? 507 LYS   B CB    1 
ATOM   5433 N N     . VAL   B 1 382 ? 35.829  -3.980  41.275 1.00 56.57  ? 508 VAL   B N     1 
ATOM   5434 C CA    . VAL   B 1 382 ? 35.805  -4.626  39.969 1.00 54.20  ? 508 VAL   B CA    1 
ATOM   5435 C C     . VAL   B 1 382 ? 37.239  -4.835  39.500 1.00 53.99  ? 508 VAL   B C     1 
ATOM   5436 O O     . VAL   B 1 382 ? 38.001  -3.872  39.349 1.00 56.52  ? 508 VAL   B O     1 
ATOM   5437 C CB    . VAL   B 1 382 ? 35.011  -3.794  38.947 1.00 53.24  ? 508 VAL   B CB    1 
ATOM   5438 C CG1   . VAL   B 1 382 ? 35.013  -4.477  37.585 1.00 45.75  ? 508 VAL   B CG1   1 
ATOM   5439 C CG2   . VAL   B 1 382 ? 33.591  -3.564  39.436 1.00 54.05  ? 508 VAL   B CG2   1 
ATOM   5440 N N     . SER   B 1 383 ? 37.596  -6.083  39.228 1.00 52.61  ? 509 SER   B N     1 
ATOM   5441 C CA    . SER   B 1 383 ? 38.947  -6.413  38.805 1.00 49.17  ? 509 SER   B CA    1 
ATOM   5442 C C     . SER   B 1 383 ? 39.101  -6.245  37.298 1.00 49.86  ? 509 SER   B C     1 
ATOM   5443 O O     . SER   B 1 383 ? 38.131  -6.253  36.539 1.00 45.41  ? 509 SER   B O     1 
ATOM   5444 C CB    . SER   B 1 383 ? 39.293  -7.851  39.190 1.00 48.85  ? 509 SER   B CB    1 
ATOM   5445 O OG    . SER   B 1 383 ? 38.617  -8.760  38.333 1.00 52.49  ? 509 SER   B OG    1 
ATOM   5446 N N     . ILE   B 1 384 ? 40.358  -6.117  36.872 1.00 50.47  ? 510 ILE   B N     1 
ATOM   5447 C CA    . ILE   B 1 384 ? 40.665  -6.098  35.448 1.00 48.32  ? 510 ILE   B CA    1 
ATOM   5448 C C     . ILE   B 1 384 ? 40.209  -7.394  34.791 1.00 44.15  ? 510 ILE   B C     1 
ATOM   5449 O O     . ILE   B 1 384 ? 39.817  -7.405  33.613 1.00 44.76  ? 510 ILE   B O     1 
ATOM   5450 C CB    . ILE   B 1 384 ? 42.175  -5.838  35.254 1.00 49.88  ? 510 ILE   B CB    1 
ATOM   5451 C CG1   . ILE   B 1 384 ? 42.519  -5.625  33.775 1.00 54.38  ? 510 ILE   B CG1   1 
ATOM   5452 C CG2   . ILE   B 1 384 ? 43.001  -6.957  35.914 1.00 50.30  ? 510 ILE   B CG2   1 
ATOM   5453 C CD1   . ILE   B 1 384 ? 43.914  -5.072  33.561 1.00 55.12  ? 510 ILE   B CD1   1 
ATOM   5454 N N     . ASP   B 1 385 ? 40.221  -8.494  35.545 1.00 46.78  ? 511 ASP   B N     1 
ATOM   5455 C CA    . ASP   B 1 385 ? 39.706  -9.767  35.054 1.00 46.70  ? 511 ASP   B CA    1 
ATOM   5456 C C     . ASP   B 1 385 ? 38.274  -9.619  34.587 1.00 44.80  ? 511 ASP   B C     1 
ATOM   5457 O O     . ASP   B 1 385 ? 37.917  -10.063 33.493 1.00 45.42  ? 511 ASP   B O     1 
ATOM   5458 C CB    . ASP   B 1 385 ? 39.761  -10.840 36.157 1.00 46.81  ? 511 ASP   B CB    1 
ATOM   5459 C CG    . ASP   B 1 385 ? 41.127  -10.980 36.804 1.00 50.05  ? 511 ASP   B CG    1 
ATOM   5460 O OD1   . ASP   B 1 385 ? 41.777  -9.954  37.066 1.00 55.44  ? 511 ASP   B OD1   1 
ATOM   5461 O OD2   . ASP   B 1 385 ? 41.524  -12.132 37.117 1.00 53.02  ? 511 ASP   B OD2   1 
ATOM   5462 N N     . GLU   B 1 386 ? 37.424  -9.022  35.426 1.00 46.48  ? 512 GLU   B N     1 
ATOM   5463 C CA    . GLU   B 1 386 ? 36.024  -8.861  35.052 1.00 44.29  ? 512 GLU   B CA    1 
ATOM   5464 C C     . GLU   B 1 386 ? 35.878  -7.895  33.895 1.00 43.12  ? 512 GLU   B C     1 
ATOM   5465 O O     . GLU   B 1 386 ? 34.985  -8.056  33.061 1.00 45.02  ? 512 GLU   B O     1 
ATOM   5466 C CB    . GLU   B 1 386 ? 35.207  -8.376  36.252 1.00 50.27  ? 512 GLU   B CB    1 
ATOM   5467 N N     . LEU   B 1 387 ? 36.761  -6.902  33.820 1.00 43.50  ? 513 LEU   B N     1 
ATOM   5468 C CA    . LEU   B 1 387 ? 36.655  -5.877  32.795 1.00 43.08  ? 513 LEU   B CA    1 
ATOM   5469 C C     . LEU   B 1 387 ? 37.024  -6.398  31.414 1.00 42.14  ? 513 LEU   B C     1 
ATOM   5470 O O     . LEU   B 1 387 ? 36.476  -5.927  30.414 1.00 39.50  ? 513 LEU   B O     1 
ATOM   5471 C CB    . LEU   B 1 387 ? 37.539  -4.696  33.167 1.00 42.48  ? 513 LEU   B CB    1 
ATOM   5472 C CG    . LEU   B 1 387 ? 36.999  -3.841  34.306 1.00 44.53  ? 513 LEU   B CG    1 
ATOM   5473 C CD1   . LEU   B 1 387 ? 38.010  -2.787  34.705 1.00 44.11  ? 513 LEU   B CD1   1 
ATOM   5474 C CD2   . LEU   B 1 387 ? 35.694  -3.205  33.889 1.00 42.85  ? 513 LEU   B CD2   1 
ATOM   5475 N N     . ILE   B 1 388 ? 37.962  -7.339  31.326 1.00 40.80  ? 514 ILE   B N     1 
ATOM   5476 C CA    . ILE   B 1 388 ? 38.344  -7.903  30.039 1.00 41.95  ? 514 ILE   B CA    1 
ATOM   5477 C C     . ILE   B 1 388 ? 37.563  -9.174  29.730 1.00 43.39  ? 514 ILE   B C     1 
ATOM   5478 O O     . ILE   B 1 388 ? 37.834  -9.836  28.723 1.00 43.64  ? 514 ILE   B O     1 
ATOM   5479 C CB    . ILE   B 1 388 ? 39.857  -8.159  29.970 1.00 45.77  ? 514 ILE   B CB    1 
ATOM   5480 C CG1   . ILE   B 1 388 ? 40.247  -9.355  30.837 1.00 48.35  ? 514 ILE   B CG1   1 
ATOM   5481 C CG2   . ILE   B 1 388 ? 40.627  -6.934  30.428 1.00 45.88  ? 514 ILE   B CG2   1 
ATOM   5482 C CD1   . ILE   B 1 388 ? 41.664  -9.852  30.577 1.00 50.59  ? 514 ILE   B CD1   1 
ATOM   5483 N N     . ALA   B 1 389 ? 36.603  -9.534  30.582 1.00 41.93  ? 515 ALA   B N     1 
ATOM   5484 C CA    . ALA   B 1 389 ? 35.806  -10.732 30.369 1.00 42.33  ? 515 ALA   B CA    1 
ATOM   5485 C C     . ALA   B 1 389 ? 35.002  -10.620 29.088 1.00 43.26  ? 515 ALA   B C     1 
ATOM   5486 O O     . ALA   B 1 389 ? 34.396  -9.585  28.816 1.00 42.66  ? 515 ALA   B O     1 
ATOM   5487 C CB    . ALA   B 1 389 ? 34.863  -10.951 31.552 1.00 45.78  ? 515 ALA   B CB    1 
ATOM   5488 N N     . ASP   B 1 390 ? 35.003  -11.687 28.299 1.00 42.31  ? 516 ASP   B N     1 
ATOM   5489 C CA    . ASP   B 1 390 ? 34.276  -11.681 27.036 1.00 46.24  ? 516 ASP   B CA    1 
ATOM   5490 C C     . ASP   B 1 390 ? 32.798  -11.953 27.289 1.00 49.26  ? 516 ASP   B C     1 
ATOM   5491 O O     . ASP   B 1 390 ? 32.449  -13.041 27.756 1.00 46.61  ? 516 ASP   B O     1 
ATOM   5492 C CB    . ASP   B 1 390 ? 34.853  -12.720 26.077 1.00 50.41  ? 516 ASP   B CB    1 
ATOM   5493 C CG    . ASP   B 1 390 ? 33.923  -13.018 24.904 1.00 53.50  ? 516 ASP   B CG    1 
ATOM   5494 O OD1   . ASP   B 1 390 ? 33.295  -12.079 24.374 1.00 54.15  ? 516 ASP   B OD1   1 
ATOM   5495 O OD2   . ASP   B 1 390 ? 33.817  -14.197 24.508 1.00 61.09  ? 516 ASP   B OD2   1 
ATOM   5496 N N     . PRO   B 1 391 ? 31.905  -11.013 26.981 1.00 48.24  ? 517 PRO   B N     1 
ATOM   5497 C CA    . PRO   B 1 391 ? 30.476  -11.248 27.233 1.00 51.11  ? 517 PRO   B CA    1 
ATOM   5498 C C     . PRO   B 1 391 ? 29.882  -12.376 26.405 1.00 53.95  ? 517 PRO   B C     1 
ATOM   5499 O O     . PRO   B 1 391 ? 28.869  -12.953 26.819 1.00 56.00  ? 517 PRO   B O     1 
ATOM   5500 C CB    . PRO   B 1 391 ? 29.833  -9.896  26.889 1.00 49.22  ? 517 PRO   B CB    1 
ATOM   5501 C CG    . PRO   B 1 391 ? 30.787  -9.247  25.981 1.00 46.69  ? 517 PRO   B CG    1 
ATOM   5502 C CD    . PRO   B 1 391 ? 32.155  -9.684  26.405 1.00 44.85  ? 517 PRO   B CD    1 
ATOM   5503 N N     . VAL   B 1 392 ? 30.467  -12.710 25.253 1.00 56.29  ? 518 VAL   B N     1 
ATOM   5504 C CA    . VAL   B 1 392 ? 29.965  -13.843 24.479 1.00 57.95  ? 518 VAL   B CA    1 
ATOM   5505 C C     . VAL   B 1 392 ? 30.088  -15.130 25.285 1.00 59.43  ? 518 VAL   B C     1 
ATOM   5506 O O     . VAL   B 1 392 ? 29.207  -15.996 25.243 1.00 63.52  ? 518 VAL   B O     1 
ATOM   5507 C CB    . VAL   B 1 392 ? 30.702  -13.950 23.131 1.00 56.87  ? 518 VAL   B CB    1 
ATOM   5508 N N     . GLU   B 1 393 ? 31.171  -15.266 26.050 1.00 61.80  ? 519 GLU   B N     1 
ATOM   5509 C CA    . GLU   B 1 393 ? 31.393  -16.485 26.816 1.00 64.28  ? 519 GLU   B CA    1 
ATOM   5510 C C     . GLU   B 1 393 ? 30.554  -16.517 28.091 1.00 66.93  ? 519 GLU   B C     1 
ATOM   5511 O O     . GLU   B 1 393 ? 30.099  -17.588 28.509 1.00 71.30  ? 519 GLU   B O     1 
ATOM   5512 C CB    . GLU   B 1 393 ? 32.880  -16.630 27.145 1.00 63.42  ? 519 GLU   B CB    1 
ATOM   5513 N N     . VAL   B 1 394 ? 30.333  -15.362 28.720 1.00 61.79  ? 520 VAL   B N     1 
ATOM   5514 C CA    . VAL   B 1 394 ? 29.561  -15.335 29.957 1.00 62.86  ? 520 VAL   B CA    1 
ATOM   5515 C C     . VAL   B 1 394 ? 28.067  -15.483 29.681 1.00 63.39  ? 520 VAL   B C     1 
ATOM   5516 O O     . VAL   B 1 394 ? 27.336  -16.060 30.498 1.00 64.27  ? 520 VAL   B O     1 
ATOM   5517 C CB    . VAL   B 1 394 ? 29.864  -14.050 30.748 1.00 60.51  ? 520 VAL   B CB    1 
ATOM   5518 N N     . VAL   B 1 395 ? 27.591  -14.985 28.543 1.00 63.87  ? 521 VAL   B N     1 
ATOM   5519 C CA    . VAL   B 1 395 ? 26.189  -15.135 28.155 1.00 63.18  ? 521 VAL   B CA    1 
ATOM   5520 C C     . VAL   B 1 395 ? 25.910  -16.566 27.705 1.00 61.89  ? 521 VAL   B C     1 
ATOM   5521 O O     . VAL   B 1 395 ? 25.186  -17.305 28.370 1.00 64.64  ? 521 VAL   B O     1 
ATOM   5522 C CB    . VAL   B 1 395 ? 25.807  -14.141 27.044 1.00 55.60  ? 521 VAL   B CB    1 
HETATM 5523 P PA    . A1BC6 C 2 .   ? 16.809  28.058  44.093 1.00 30.72  ? 601 A1BC6 A PA    1 
HETATM 5524 O O1A   . A1BC6 C 2 .   ? 16.574  29.442  44.750 1.00 33.82  ? 601 A1BC6 A O1A   1 
HETATM 5525 O O2A   . A1BC6 C 2 .   ? 17.857  27.882  43.140 1.00 29.28  ? 601 A1BC6 A O2A   1 
HETATM 5526 O O5B   . A1BC6 C 2 .   ? 15.641  27.397  43.459 1.00 28.43  ? 601 A1BC6 A O5B   1 
HETATM 5527 C C5B   . A1BC6 C 2 .   ? 15.681  26.331  42.525 1.00 26.36  ? 601 A1BC6 A C5B   1 
HETATM 5528 C C4B   . A1BC6 C 2 .   ? 14.273  25.775  42.379 1.00 30.60  ? 601 A1BC6 A C4B   1 
HETATM 5529 O O4B   . A1BC6 C 2 .   ? 13.418  26.621  41.629 1.00 32.56  ? 601 A1BC6 A O4B   1 
HETATM 5530 C C3B   . A1BC6 C 2 .   ? 14.183  24.476  41.631 1.00 32.90  ? 601 A1BC6 A C3B   1 
HETATM 5531 O O3B   . A1BC6 C 2 .   ? 14.577  23.399  42.390 1.00 33.45  ? 601 A1BC6 A O3B   1 
HETATM 5532 C C2B   . A1BC6 C 2 .   ? 12.751  24.421  41.269 1.00 31.83  ? 601 A1BC6 A C2B   1 
HETATM 5533 O O2B   . A1BC6 C 2 .   ? 11.975  24.036  42.347 1.00 28.05  ? 601 A1BC6 A O2B   1 
HETATM 5534 C C1B   . A1BC6 C 2 .   ? 12.441  25.845  41.005 1.00 29.58  ? 601 A1BC6 A C1B   1 
HETATM 5535 N N9A   . A1BC6 C 2 .   ? 12.475  26.172  39.592 1.00 33.22  ? 601 A1BC6 A N9A   1 
HETATM 5536 C C8A   . A1BC6 C 2 .   ? 13.533  26.163  38.721 1.00 34.44  ? 601 A1BC6 A C8A   1 
HETATM 5537 N N7A   . A1BC6 C 2 .   ? 13.110  26.559  37.506 1.00 32.80  ? 601 A1BC6 A N7A   1 
HETATM 5538 C C5A   . A1BC6 C 2 .   ? 11.758  26.859  37.577 1.00 35.80  ? 601 A1BC6 A C5A   1 
HETATM 5539 C C6A   . A1BC6 C 2 .   ? 10.804  27.325  36.667 1.00 37.92  ? 601 A1BC6 A C6A   1 
HETATM 5540 N N6A   . A1BC6 C 2 .   ? 11.181  27.589  35.305 1.00 37.70  ? 601 A1BC6 A N6A   1 
HETATM 5541 N N1A   . A1BC6 C 2 .   ? 9.540   27.509  37.067 1.00 35.89  ? 601 A1BC6 A N1A   1 
HETATM 5542 C C2A   . A1BC6 C 2 .   ? 9.148   27.280  38.345 1.00 37.61  ? 601 A1BC6 A C2A   1 
HETATM 5543 N N3A   . A1BC6 C 2 .   ? 10.055  26.829  39.260 1.00 33.47  ? 601 A1BC6 A N3A   1 
HETATM 5544 C C4A   . A1BC6 C 2 .   ? 11.332  26.630  38.917 1.00 30.24  ? 601 A1BC6 A C4A   1 
HETATM 5545 N N1    . A1BC6 C 2 .   ? 12.347  18.398  46.729 1.00 26.63  ? 601 A1BC6 A N1    1 
HETATM 5546 C C2    . A1BC6 C 2 .   ? 11.057  17.843  46.668 1.00 28.66  ? 601 A1BC6 A C2    1 
HETATM 5547 O O2    . A1BC6 C 2 .   ? 10.291  18.118  45.604 1.00 26.97  ? 601 A1BC6 A O2    1 
HETATM 5548 N N3    . A1BC6 C 2 .   ? 10.537  16.995  47.641 1.00 25.65  ? 601 A1BC6 A N3    1 
HETATM 5549 C C4    . A1BC6 C 2 .   ? 11.292  16.668  48.747 1.00 26.49  ? 601 A1BC6 A C4    1 
HETATM 5550 O O4    . A1BC6 C 2 .   ? 10.716  15.845  49.639 1.00 27.87  ? 601 A1BC6 A O4    1 
HETATM 5551 C C4X   . A1BC6 C 2 .   ? 12.658  17.220  48.851 1.00 22.99  ? 601 A1BC6 A C4X   1 
HETATM 5552 N N5    . A1BC6 C 2 .   ? 13.567  16.797  49.897 1.00 26.12  ? 601 A1BC6 A N5    1 
HETATM 5553 C C5X   . A1BC6 C 2 .   ? 14.500  17.830  50.245 1.00 28.20  ? 601 A1BC6 A C5X   1 
HETATM 5554 C C6    . A1BC6 C 2 .   ? 14.963  17.922  51.646 1.00 24.03  ? 601 A1BC6 A C6    1 
HETATM 5555 C C7    . A1BC6 C 2 .   ? 15.834  18.965  52.001 1.00 26.15  ? 601 A1BC6 A C7    1 
HETATM 5556 C C7M   . A1BC6 C 2 .   ? 16.320  19.063  53.420 1.00 25.71  ? 601 A1BC6 A C7M   1 
HETATM 5557 C C8    . A1BC6 C 2 .   ? 16.261  19.914  51.031 1.00 24.75  ? 601 A1BC6 A C8    1 
HETATM 5558 C C8M   . A1BC6 C 2 .   ? 17.199  21.031  51.361 1.00 27.65  ? 601 A1BC6 A C8M   1 
HETATM 5559 C C9    . A1BC6 C 2 .   ? 15.814  19.824  49.688 1.00 26.71  ? 601 A1BC6 A C9    1 
HETATM 5560 C C9A   . A1BC6 C 2 .   ? 14.897  18.735  49.332 1.00 23.74  ? 601 A1BC6 A C9A   1 
HETATM 5561 N N10   . A1BC6 C 2 .   ? 14.376  18.671  47.988 1.00 28.29  ? 601 A1BC6 A N10   1 
HETATM 5562 C C10   . A1BC6 C 2 .   ? 13.128  18.049  47.873 1.00 26.58  ? 601 A1BC6 A C10   1 
HETATM 5563 C "C1'" . A1BC6 C 2 .   ? 14.979  19.384  46.882 1.00 27.33  ? 601 A1BC6 A "C1'" 1 
HETATM 5564 C "C2'" . A1BC6 C 2 .   ? 14.473  20.802  46.807 1.00 28.39  ? 601 A1BC6 A "C2'" 1 
HETATM 5565 O "O2'" . A1BC6 C 2 .   ? 13.225  20.870  46.198 1.00 26.62  ? 601 A1BC6 A "O2'" 1 
HETATM 5566 C "C3'" . A1BC6 C 2 .   ? 15.483  21.616  46.041 1.00 29.33  ? 601 A1BC6 A "C3'" 1 
HETATM 5567 O "O3'" . A1BC6 C 2 .   ? 16.696  21.542  46.725 1.00 30.51  ? 601 A1BC6 A "O3'" 1 
HETATM 5568 C "C4'" . A1BC6 C 2 .   ? 14.997  23.045  45.947 1.00 31.52  ? 601 A1BC6 A "C4'" 1 
HETATM 5569 O "O4'" . A1BC6 C 2 .   ? 14.067  23.127  44.907 1.00 33.81  ? 601 A1BC6 A "O4'" 1 
HETATM 5570 C "C5'" . A1BC6 C 2 .   ? 16.124  24.026  45.733 1.00 29.82  ? 601 A1BC6 A "C5'" 1 
HETATM 5571 O "O5'" . A1BC6 C 2 .   ? 15.637  25.321  45.977 1.00 29.92  ? 601 A1BC6 A "O5'" 1 
HETATM 5572 P P     . A1BC6 C 2 .   ? 16.715  26.348  46.421 1.00 31.80  ? 601 A1BC6 A P     1 
HETATM 5573 O O1P   . A1BC6 C 2 .   ? 17.894  25.695  47.225 1.00 27.24  ? 601 A1BC6 A O1P   1 
HETATM 5574 O O2P   . A1BC6 C 2 .   ? 15.856  27.444  47.154 1.00 30.65  ? 601 A1BC6 A O2P   1 
HETATM 5575 O O3P   . A1BC6 C 2 .   ? 17.289  26.993  45.042 1.00 32.34  ? 601 A1BC6 A O3P   1 
HETATM 5576 C C01   . A1BC6 C 2 .   ? 15.521  12.837  48.912 1.00 34.00  ? 601 A1BC6 A C01   1 
HETATM 5577 C C02   . A1BC6 C 2 .   ? 14.031  13.142  48.821 1.00 32.73  ? 601 A1BC6 A C02   1 
HETATM 5578 C C04   . A1BC6 C 2 .   ? 13.484  14.531  48.945 1.00 31.59  ? 601 A1BC6 A C04   1 
HETATM 5579 C C05   . A1BC6 C 2 .   ? 14.081  15.479  49.710 1.00 28.33  ? 601 A1BC6 A C05   1 
HETATM 5580 C C     . FMT   D 3 .   ? 14.987  15.271  45.831 0.85 30.22  ? 602 FMT   A C     1 
HETATM 5581 O O1    . FMT   D 3 .   ? 14.850  14.110  46.192 0.85 38.93  ? 602 FMT   A O1    1 
HETATM 5582 O O2    . FMT   D 3 .   ? 15.587  15.530  44.805 0.85 37.25  ? 602 FMT   A O2    1 
HETATM 5583 P PA    . A1BC6 E 2 .   ? 29.117  0.071   28.200 1.00 31.30  ? 601 A1BC6 B PA    1 
HETATM 5584 O O1A   . A1BC6 E 2 .   ? 29.838  -1.226  27.806 1.00 33.87  ? 601 A1BC6 B O1A   1 
HETATM 5585 O O2A   . A1BC6 E 2 .   ? 29.177  0.607   29.533 1.00 32.02  ? 601 A1BC6 B O2A   1 
HETATM 5586 O O5B   . A1BC6 E 2 .   ? 27.627  -0.011  28.051 1.00 31.48  ? 601 A1BC6 B O5B   1 
HETATM 5587 C C5B   . A1BC6 E 2 .   ? 26.689  0.916   28.575 1.00 33.96  ? 601 A1BC6 B C5B   1 
HETATM 5588 C C4B   . A1BC6 E 2 .   ? 25.342  0.675   27.879 1.00 32.31  ? 601 A1BC6 B C4B   1 
HETATM 5589 O O4B   . A1BC6 E 2 .   ? 24.786  -0.588  28.144 1.00 31.56  ? 601 A1BC6 B O4B   1 
HETATM 5590 C C3B   . A1BC6 E 2 .   ? 24.236  1.601   28.260 1.00 29.71  ? 601 A1BC6 B C3B   1 
HETATM 5591 O O3B   . A1BC6 E 2 .   ? 24.390  2.860   27.732 1.00 35.23  ? 601 A1BC6 B O3B   1 
HETATM 5592 C C2B   . A1BC6 E 2 .   ? 23.066  0.906   27.699 1.00 31.35  ? 601 A1BC6 B C2B   1 
HETATM 5593 O O2B   . A1BC6 E 2 .   ? 23.007  1.094   26.318 1.00 31.03  ? 601 A1BC6 B O2B   1 
HETATM 5594 C C1B   . A1BC6 E 2 .   ? 23.389  -0.501  27.997 1.00 32.45  ? 601 A1BC6 B C1B   1 
HETATM 5595 N N9A   . A1BC6 E 2 .   ? 22.759  -0.979  29.216 1.00 36.17  ? 601 A1BC6 B N9A   1 
HETATM 5596 C C8A   . A1BC6 E 2 .   ? 22.908  -0.521  30.521 1.00 40.24  ? 601 A1BC6 B C8A   1 
HETATM 5597 N N7A   . A1BC6 E 2 .   ? 22.158  -1.279  31.342 1.00 36.87  ? 601 A1BC6 B N7A   1 
HETATM 5598 C C5A   . A1BC6 E 2 .   ? 21.508  -2.270  30.609 1.00 38.85  ? 601 A1BC6 B C5A   1 
HETATM 5599 C C6A   . A1BC6 E 2 .   ? 20.635  -3.307  30.913 1.00 38.57  ? 601 A1BC6 B C6A   1 
HETATM 5600 N N6A   . A1BC6 E 2 .   ? 20.205  -3.545  32.269 1.00 38.96  ? 601 A1BC6 B N6A   1 
HETATM 5601 N N1A   . A1BC6 E 2 .   ? 20.165  -4.100  29.941 1.00 36.93  ? 601 A1BC6 B N1A   1 
HETATM 5602 C C2A   . A1BC6 E 2 .   ? 20.538  -3.931  28.643 1.00 40.23  ? 601 A1BC6 B C2A   1 
HETATM 5603 N N3A   . A1BC6 E 2 .   ? 21.392  -2.919  28.308 1.00 34.96  ? 601 A1BC6 B N3A   1 
HETATM 5604 C C4A   . A1BC6 E 2 .   ? 21.882  -2.087  29.236 1.00 36.20  ? 601 A1BC6 B C4A   1 
HETATM 5605 N N1    . A1BC6 E 2 .   ? 23.085  6.626   22.093 1.00 27.40  ? 601 A1BC6 B N1    1 
HETATM 5606 C C2    . A1BC6 E 2 .   ? 21.843  6.524   21.406 1.00 31.95  ? 601 A1BC6 B C2    1 
HETATM 5607 O O2    . A1BC6 E 2 .   ? 20.885  5.702   21.924 1.00 31.06  ? 601 A1BC6 B O2    1 
HETATM 5608 N N3    . A1BC6 E 2 .   ? 21.645  7.243   20.208 1.00 30.17  ? 601 A1BC6 B N3    1 
HETATM 5609 C C4    . A1BC6 E 2 .   ? 22.637  8.075   19.688 1.00 31.00  ? 601 A1BC6 B C4    1 
HETATM 5610 O O4    . A1BC6 E 2 .   ? 22.464  8.788   18.532 1.00 31.61  ? 601 A1BC6 B O4    1 
HETATM 5611 C C4X   . A1BC6 E 2 .   ? 23.917  8.201   20.412 1.00 30.47  ? 601 A1BC6 B C4X   1 
HETATM 5612 N N5    . A1BC6 E 2 .   ? 24.903  9.162   20.004 1.00 30.07  ? 601 A1BC6 B N5    1 
HETATM 5613 C C5X   . A1BC6 E 2 .   ? 26.259  8.753   20.344 1.00 31.77  ? 601 A1BC6 B C5X   1 
HETATM 5614 C C6    . A1BC6 E 2 .   ? 27.378  9.183   19.485 1.00 30.53  ? 601 A1BC6 B C6    1 
HETATM 5615 C C7    . A1BC6 E 2 .   ? 28.676  8.778   19.830 1.00 33.18  ? 601 A1BC6 B C7    1 
HETATM 5616 C C7M   . A1BC6 E 2 .   ? 29.828  9.207   18.965 1.00 32.35  ? 601 A1BC6 B C7M   1 
HETATM 5617 C C8    . A1BC6 E 2 .   ? 28.898  7.964   20.982 1.00 30.94  ? 601 A1BC6 B C8    1 
HETATM 5618 C C8M   . A1BC6 E 2 .   ? 30.288  7.525   21.361 1.00 30.79  ? 601 A1BC6 B C8M   1 
HETATM 5619 C C9    . A1BC6 E 2 .   ? 27.830  7.555   21.808 1.00 28.30  ? 601 A1BC6 B C9    1 
HETATM 5620 C C9A   . A1BC6 E 2 .   ? 26.470  7.976   21.445 1.00 28.56  ? 601 A1BC6 B C9A   1 
HETATM 5621 N N10   . A1BC6 E 2 .   ? 25.343  7.595   22.260 1.00 30.22  ? 601 A1BC6 B N10   1 
HETATM 5622 C C10   . A1BC6 E 2 .   ? 24.102  7.495   21.575 1.00 29.54  ? 601 A1BC6 B C10   1 
HETATM 5623 C "C1'" . A1BC6 E 2 .   ? 25.485  7.135   23.657 1.00 30.43  ? 601 A1BC6 B "C1'" 1 
HETATM 5624 C "C2'" . A1BC6 E 2 .   ? 25.745  5.655   23.663 1.00 26.56  ? 601 A1BC6 B "C2'" 1 
HETATM 5625 O "O2'" . A1BC6 E 2 .   ? 24.599  4.910   23.374 1.00 28.34  ? 601 A1BC6 B "O2'" 1 
HETATM 5626 C "C3'" . A1BC6 E 2 .   ? 26.334  5.287   25.006 1.00 33.73  ? 601 A1BC6 B "C3'" 1 
HETATM 5627 O "O3'" . A1BC6 E 2 .   ? 27.561  5.903   25.089 1.00 35.30  ? 601 A1BC6 B "O3'" 1 
HETATM 5628 C "C4'" . A1BC6 E 2 .   ? 26.610  3.816   25.073 1.00 33.80  ? 601 A1BC6 B "C4'" 1 
HETATM 5629 O "O4'" . A1BC6 E 2 .   ? 25.434  3.122   25.322 1.00 37.82  ? 601 A1BC6 B "O4'" 1 
HETATM 5630 C "C5'" . A1BC6 E 2 .   ? 27.675  3.531   26.140 1.00 30.57  ? 601 A1BC6 B "C5'" 1 
HETATM 5631 O "O5'" . A1BC6 E 2 .   ? 28.050  2.206   25.930 1.00 32.25  ? 601 A1BC6 B "O5'" 1 
HETATM 5632 P P     . A1BC6 E 2 .   ? 29.562  1.724   25.967 1.00 30.66  ? 601 A1BC6 B P     1 
HETATM 5633 O O1P   . A1BC6 E 2 .   ? 30.046  0.641   24.971 1.00 34.51  ? 601 A1BC6 B O1P   1 
HETATM 5634 O O2P   . A1BC6 E 2 .   ? 30.329  3.090   26.115 1.00 31.05  ? 601 A1BC6 B O2P   1 
HETATM 5635 O O3P   . A1BC6 E 2 .   ? 29.532  1.373   27.569 1.00 31.93  ? 601 A1BC6 B O3P   1 
HETATM 5636 C C01   . A1BC6 E 2 .   ? 24.074  13.425  21.306 1.00 39.52  ? 601 A1BC6 B C01   1 
HETATM 5637 C C02   . A1BC6 E 2 .   ? 23.142  12.518  20.521 1.00 37.54  ? 601 A1BC6 B C02   1 
HETATM 5638 C C04   . A1BC6 E 2 .   ? 23.417  11.063  20.279 1.00 35.55  ? 601 A1BC6 B C04   1 
HETATM 5639 C C05   . A1BC6 E 2 .   ? 24.673  10.550  20.259 1.00 33.74  ? 601 A1BC6 B C05   1 
HETATM 5640 C C     . FMT   F 3 .   ? 23.162  10.696  23.981 0.73 39.73  ? 602 FMT   B C     1 
HETATM 5641 O O1    . FMT   F 3 .   ? 22.534  11.423  23.213 0.73 42.63  ? 602 FMT   B O1    1 
HETATM 5642 O O2    . FMT   F 3 .   ? 22.929  10.653  25.191 0.73 41.75  ? 602 FMT   B O2    1 
HETATM 5643 O O     . HOH   G 4 .   ? 23.108  11.998  63.719 1.00 45.08  ? 701 HOH   A O     1 
HETATM 5644 O O     . HOH   G 4 .   ? -0.995  29.922  64.659 1.00 54.05  ? 702 HOH   A O     1 
HETATM 5645 O O     . HOH   G 4 .   ? 27.083  4.978   48.477 1.00 51.99  ? 703 HOH   A O     1 
HETATM 5646 O O     . HOH   G 4 .   ? 12.202  8.645   40.685 1.00 49.60  ? 704 HOH   A O     1 
HETATM 5647 O O     . HOH   G 4 .   ? 18.396  21.305  63.388 1.00 39.11  ? 705 HOH   A O     1 
HETATM 5648 O O     . HOH   G 4 .   ? 3.946   25.380  70.183 1.00 46.82  ? 706 HOH   A O     1 
HETATM 5649 O O     . HOH   G 4 .   ? 13.504  1.588   43.078 1.00 46.77  ? 707 HOH   A O     1 
HETATM 5650 O O     . HOH   G 4 .   ? 13.344  34.022  64.990 1.00 45.85  ? 708 HOH   A O     1 
HETATM 5651 O O     . HOH   G 4 .   ? -4.720  14.163  66.985 1.00 51.02  ? 709 HOH   A O     1 
HETATM 5652 O O     . HOH   G 4 .   ? -7.070  21.004  58.249 1.00 49.61  ? 710 HOH   A O     1 
HETATM 5653 O O     . HOH   G 4 .   ? 10.992  10.493  43.901 1.00 42.25  ? 711 HOH   A O     1 
HETATM 5654 O O     . HOH   G 4 .   ? 10.250  17.218  58.423 1.00 38.13  ? 712 HOH   A O     1 
HETATM 5655 O O     . HOH   G 4 .   ? 2.210   28.360  45.348 1.00 36.56  ? 713 HOH   A O     1 
HETATM 5656 O O     . HOH   G 4 .   ? 33.649  23.257  56.088 1.00 56.58  ? 714 HOH   A O     1 
HETATM 5657 O O     . HOH   G 4 .   ? 3.519   13.938  65.079 1.00 41.74  ? 715 HOH   A O     1 
HETATM 5658 O O     . HOH   G 4 .   ? 11.111  15.556  71.302 1.00 38.22  ? 716 HOH   A O     1 
HETATM 5659 O O     . HOH   G 4 .   ? 16.170  12.679  67.397 1.00 37.67  ? 717 HOH   A O     1 
HETATM 5660 O O     . HOH   G 4 .   ? 10.605  10.345  40.239 1.00 54.22  ? 718 HOH   A O     1 
HETATM 5661 O O     . HOH   G 4 .   ? 20.739  35.797  64.978 1.00 43.76  ? 719 HOH   A O     1 
HETATM 5662 O O     . HOH   G 4 .   ? 14.066  -3.956  59.317 1.00 54.29  ? 720 HOH   A O     1 
HETATM 5663 O O     . HOH   G 4 .   ? 19.580  24.509  45.579 1.00 29.36  ? 721 HOH   A O     1 
HETATM 5664 O O     . HOH   G 4 .   ? 22.938  39.220  59.035 1.00 48.11  ? 722 HOH   A O     1 
HETATM 5665 O O     . HOH   G 4 .   ? 13.835  25.599  72.956 1.00 43.62  ? 723 HOH   A O     1 
HETATM 5666 O O     . HOH   G 4 .   ? 21.776  16.660  66.464 1.00 43.85  ? 724 HOH   A O     1 
HETATM 5667 O O     . HOH   G 4 .   ? 29.993  16.375  50.253 1.00 45.89  ? 725 HOH   A O     1 
HETATM 5668 O O     . HOH   G 4 .   ? 14.469  33.825  47.216 1.00 40.21  ? 726 HOH   A O     1 
HETATM 5669 O O     . HOH   G 4 .   ? 1.806   15.854  70.191 1.00 52.49  ? 727 HOH   A O     1 
HETATM 5670 O O     . HOH   G 4 .   ? 13.829  24.890  48.445 1.00 28.61  ? 728 HOH   A O     1 
HETATM 5671 O O     . HOH   G 4 .   ? 19.181  -0.972  63.039 1.00 47.03  ? 729 HOH   A O     1 
HETATM 5672 O O     . HOH   G 4 .   ? 22.767  15.080  49.266 1.00 31.45  ? 730 HOH   A O     1 
HETATM 5673 O O     . HOH   G 4 .   ? 3.496   14.964  49.524 1.00 38.07  ? 731 HOH   A O     1 
HETATM 5674 O O     . HOH   G 4 .   ? 21.092  21.529  65.718 1.00 46.15  ? 732 HOH   A O     1 
HETATM 5675 O O     . HOH   G 4 .   ? 9.022   45.460  59.758 1.00 45.09  ? 733 HOH   A O     1 
HETATM 5676 O O     . HOH   G 4 .   ? 15.668  21.776  40.688 1.00 40.55  ? 734 HOH   A O     1 
HETATM 5677 O O     . HOH   G 4 .   ? 22.795  3.739   66.447 1.00 46.55  ? 735 HOH   A O     1 
HETATM 5678 O O     . HOH   G 4 .   ? -6.942  27.590  52.322 1.00 47.22  ? 736 HOH   A O     1 
HETATM 5679 O O     . HOH   G 4 .   ? 20.129  46.783  52.755 1.00 53.09  ? 737 HOH   A O     1 
HETATM 5680 O O     . HOH   G 4 .   ? 6.354   17.606  42.110 1.00 31.42  ? 738 HOH   A O     1 
HETATM 5681 O O     . HOH   G 4 .   ? 20.460  4.603   72.545 1.00 43.87  ? 739 HOH   A O     1 
HETATM 5682 O O     . HOH   G 4 .   ? 19.348  34.566  44.994 1.00 40.45  ? 740 HOH   A O     1 
HETATM 5683 O O     . HOH   G 4 .   ? -1.748  31.669  45.308 1.00 45.77  ? 741 HOH   A O     1 
HETATM 5684 O O     . HOH   G 4 .   ? 15.727  42.215  50.343 1.00 42.87  ? 742 HOH   A O     1 
HETATM 5685 O O     . HOH   G 4 .   ? 7.325   19.105  65.774 1.00 38.65  ? 743 HOH   A O     1 
HETATM 5686 O O     . HOH   G 4 .   ? 1.494   6.941   73.807 1.00 56.29  ? 744 HOH   A O     1 
HETATM 5687 O O     . HOH   G 4 .   ? 2.470   15.063  38.638 1.00 45.34  ? 745 HOH   A O     1 
HETATM 5688 O O     . HOH   G 4 .   ? 18.368  21.394  66.038 1.00 46.99  ? 746 HOH   A O     1 
HETATM 5689 O O     . HOH   G 4 .   ? 15.190  11.100  70.867 1.00 39.49  ? 747 HOH   A O     1 
HETATM 5690 O O     . HOH   G 4 .   ? 12.752  21.078  40.325 1.00 28.96  ? 748 HOH   A O     1 
HETATM 5691 O O     . HOH   G 4 .   ? 4.714   35.665  59.006 1.00 43.83  ? 749 HOH   A O     1 
HETATM 5692 O O     . HOH   G 4 .   ? 26.100  26.035  50.297 1.00 36.61  ? 750 HOH   A O     1 
HETATM 5693 O O     . HOH   G 4 .   ? 26.323  35.078  58.633 1.00 45.56  ? 751 HOH   A O     1 
HETATM 5694 O O     . HOH   G 4 .   ? 4.384   13.736  47.070 1.00 40.43  ? 752 HOH   A O     1 
HETATM 5695 O O     . HOH   G 4 .   ? 31.340  29.291  54.323 1.00 45.06  ? 753 HOH   A O     1 
HETATM 5696 O O     . HOH   G 4 .   ? 1.224   12.910  64.102 1.00 48.29  ? 754 HOH   A O     1 
HETATM 5697 O O     . HOH   G 4 .   ? 16.601  25.801  38.939 1.00 36.90  ? 755 HOH   A O     1 
HETATM 5698 O O     . HOH   G 4 .   ? -8.212  27.275  46.055 1.00 52.75  ? 756 HOH   A O     1 
HETATM 5699 O O     . HOH   G 4 .   ? 2.818   17.659  36.059 1.00 46.29  ? 757 HOH   A O     1 
HETATM 5700 O O     . HOH   G 4 .   ? 3.695   15.979  45.487 1.00 38.21  ? 758 HOH   A O     1 
HETATM 5701 O O     . HOH   G 4 .   ? -0.060  16.575  37.993 1.00 54.27  ? 759 HOH   A O     1 
HETATM 5702 O O     . HOH   G 4 .   ? 22.948  19.043  66.745 1.00 47.45  ? 760 HOH   A O     1 
HETATM 5703 O O     . HOH   G 4 .   ? 17.405  40.211  49.493 1.00 44.04  ? 761 HOH   A O     1 
HETATM 5704 O O     . HOH   G 4 .   ? 0.207   22.339  42.726 1.00 44.65  ? 762 HOH   A O     1 
HETATM 5705 O O     . HOH   G 4 .   ? 12.248  7.268   73.623 1.00 51.95  ? 763 HOH   A O     1 
HETATM 5706 O O     . HOH   G 4 .   ? 22.394  25.098  65.766 1.00 44.97  ? 764 HOH   A O     1 
HETATM 5707 O O     . HOH   G 4 .   ? 21.139  15.171  64.150 1.00 34.67  ? 765 HOH   A O     1 
HETATM 5708 O O     . HOH   G 4 .   ? 6.375   10.493  49.017 1.00 39.96  ? 766 HOH   A O     1 
HETATM 5709 O O     . HOH   G 4 .   ? -7.376  11.586  55.645 1.00 53.11  ? 767 HOH   A O     1 
HETATM 5710 O O     . HOH   G 4 .   ? 20.146  25.844  32.551 1.00 50.85  ? 768 HOH   A O     1 
HETATM 5711 O O     . HOH   G 4 .   ? 11.088  13.486  47.141 1.00 34.39  ? 769 HOH   A O     1 
HETATM 5712 O O     . HOH   G 4 .   ? 15.844  22.469  65.201 1.00 33.75  ? 770 HOH   A O     1 
HETATM 5713 O O     . HOH   G 4 .   ? 4.516   10.977  47.501 1.00 45.61  ? 771 HOH   A O     1 
HETATM 5714 O O     . HOH   G 4 .   ? 15.914  18.942  40.811 1.00 35.19  ? 772 HOH   A O     1 
HETATM 5715 O O     . HOH   G 4 .   ? -7.030  15.999  51.344 1.00 63.75  ? 773 HOH   A O     1 
HETATM 5716 O O     . HOH   G 4 .   ? 14.288  14.562  64.569 1.00 37.89  ? 774 HOH   A O     1 
HETATM 5717 O O     . HOH   G 4 .   ? 15.977  8.118   71.200 1.00 42.28  ? 775 HOH   A O     1 
HETATM 5718 O O     . HOH   G 4 .   ? 23.677  -0.887  36.606 1.00 52.08  ? 776 HOH   A O     1 
HETATM 5719 O O     . HOH   G 4 .   ? 13.914  19.540  37.278 1.00 44.97  ? 777 HOH   A O     1 
HETATM 5720 O O     . HOH   G 4 .   ? 14.803  24.726  65.924 1.00 33.23  ? 778 HOH   A O     1 
HETATM 5721 O O     . HOH   G 4 .   ? 27.104  16.364  56.188 1.00 42.26  ? 779 HOH   A O     1 
HETATM 5722 O O     . HOH   G 4 .   ? 20.033  26.320  43.797 1.00 32.24  ? 780 HOH   A O     1 
HETATM 5723 O O     . HOH   G 4 .   ? 16.762  22.151  35.320 1.00 48.69  ? 781 HOH   A O     1 
HETATM 5724 O O     . HOH   G 4 .   ? 30.105  12.751  51.575 1.00 54.11  ? 782 HOH   A O     1 
HETATM 5725 O O     . HOH   G 4 .   ? 13.493  14.234  59.732 1.00 37.44  ? 783 HOH   A O     1 
HETATM 5726 O O     . HOH   G 4 .   ? -6.640  25.156  51.975 1.00 46.06  ? 784 HOH   A O     1 
HETATM 5727 O O     . HOH   G 4 .   ? 12.463  16.409  36.839 1.00 43.83  ? 785 HOH   A O     1 
HETATM 5728 O O     . HOH   G 4 .   ? -0.492  29.239  44.526 1.00 39.33  ? 786 HOH   A O     1 
HETATM 5729 O O     . HOH   G 4 .   ? 14.627  17.955  70.643 1.00 37.34  ? 787 HOH   A O     1 
HETATM 5730 O O     . HOH   G 4 .   ? 17.541  7.582   43.751 1.00 45.10  ? 788 HOH   A O     1 
HETATM 5731 O O     . HOH   G 4 .   ? 28.865  35.242  57.178 1.00 49.07  ? 789 HOH   A O     1 
HETATM 5732 O O     . HOH   G 4 .   ? 5.218   15.398  51.494 1.00 35.04  ? 790 HOH   A O     1 
HETATM 5733 O O     . HOH   G 4 .   ? 2.748   21.845  46.625 1.00 36.74  ? 791 HOH   A O     1 
HETATM 5734 O O     . HOH   G 4 .   ? 24.438  27.690  48.931 1.00 35.77  ? 792 HOH   A O     1 
HETATM 5735 O O     . HOH   G 4 .   ? 20.624  42.653  58.441 1.00 50.26  ? 793 HOH   A O     1 
HETATM 5736 O O     . HOH   G 4 .   ? 4.165   19.079  43.374 1.00 34.71  ? 794 HOH   A O     1 
HETATM 5737 O O     . HOH   G 4 .   ? 26.131  24.497  46.837 1.00 44.09  ? 795 HOH   A O     1 
HETATM 5738 O O     . HOH   G 4 .   ? 22.401  0.921   56.947 1.00 47.45  ? 796 HOH   A O     1 
HETATM 5739 O O     . HOH   G 4 .   ? 3.970   19.733  47.652 1.00 31.48  ? 797 HOH   A O     1 
HETATM 5740 O O     . HOH   G 4 .   ? 7.562   14.447  70.272 1.00 41.02  ? 798 HOH   A O     1 
HETATM 5741 O O     . HOH   G 4 .   ? 19.760  33.057  42.669 1.00 42.07  ? 799 HOH   A O     1 
HETATM 5742 O O     . HOH   G 4 .   ? -0.680  14.229  70.149 1.00 55.80  ? 800 HOH   A O     1 
HETATM 5743 O O     . HOH   G 4 .   ? 1.492   30.786  65.660 1.00 47.28  ? 801 HOH   A O     1 
HETATM 5744 O O     . HOH   G 4 .   ? 29.037  40.892  41.693 1.00 53.65  ? 802 HOH   A O     1 
HETATM 5745 O O     . HOH   G 4 .   ? 6.939   42.722  56.746 1.00 49.25  ? 803 HOH   A O     1 
HETATM 5746 O O     . HOH   G 4 .   ? -2.130  15.206  44.084 1.00 44.06  ? 804 HOH   A O     1 
HETATM 5747 O O     . HOH   G 4 .   ? 12.000  31.076  34.881 1.00 38.67  ? 805 HOH   A O     1 
HETATM 5748 O O     . HOH   G 4 .   ? 22.173  38.999  61.950 1.00 55.42  ? 806 HOH   A O     1 
HETATM 5749 O O     . HOH   G 4 .   ? 7.567   33.654  63.802 1.00 45.09  ? 807 HOH   A O     1 
HETATM 5750 O O     . HOH   G 4 .   ? 3.119   17.749  49.581 1.00 32.72  ? 808 HOH   A O     1 
HETATM 5751 O O     . HOH   G 4 .   ? 22.900  27.418  65.650 1.00 45.63  ? 809 HOH   A O     1 
HETATM 5752 O O     . HOH   G 4 .   ? 26.186  43.158  53.968 1.00 50.24  ? 810 HOH   A O     1 
HETATM 5753 O O     . HOH   G 4 .   ? 4.140   16.354  64.172 1.00 43.00  ? 811 HOH   A O     1 
HETATM 5754 O O     . HOH   G 4 .   ? 27.450  4.214   63.683 1.00 54.43  ? 812 HOH   A O     1 
HETATM 5755 O O     . HOH   G 4 .   ? 11.180  19.539  31.014 1.00 50.24  ? 813 HOH   A O     1 
HETATM 5756 O O     . HOH   G 4 .   ? 6.788   34.403  66.347 1.00 53.75  ? 814 HOH   A O     1 
HETATM 5757 O O     . HOH   G 4 .   ? 17.861  36.727  67.617 1.00 56.54  ? 815 HOH   A O     1 
HETATM 5758 O O     . HOH   G 4 .   ? 17.118  17.851  56.481 1.00 35.61  ? 816 HOH   A O     1 
HETATM 5759 O O     . HOH   G 4 .   ? 15.927  34.054  44.697 1.00 40.86  ? 817 HOH   A O     1 
HETATM 5760 O O     . HOH   G 4 .   ? 28.119  2.643   46.472 1.00 59.13  ? 818 HOH   A O     1 
HETATM 5761 O O     . HOH   G 4 .   ? 12.993  16.910  58.163 1.00 33.49  ? 819 HOH   A O     1 
HETATM 5762 O O     . HOH   G 4 .   ? 19.533  34.497  68.428 1.00 48.63  ? 820 HOH   A O     1 
HETATM 5763 O O     . HOH   G 4 .   ? 17.681  5.449   41.581 1.00 52.99  ? 821 HOH   A O     1 
HETATM 5764 O O     . HOH   G 4 .   ? -0.662  41.439  44.839 1.00 49.38  ? 822 HOH   A O     1 
HETATM 5765 O O     . HOH   G 4 .   ? 8.098   13.301  33.044 1.00 50.32  ? 823 HOH   A O     1 
HETATM 5766 O O     . HOH   G 4 .   ? 26.366  14.392  68.400 1.00 58.44  ? 824 HOH   A O     1 
HETATM 5767 O O     . HOH   G 4 .   ? 12.425  32.180  47.487 1.00 36.72  ? 825 HOH   A O     1 
HETATM 5768 O O     . HOH   G 4 .   ? 17.183  17.878  73.923 1.00 46.71  ? 826 HOH   A O     1 
HETATM 5769 O O     . HOH   G 4 .   ? -4.249  31.260  43.944 1.00 49.23  ? 827 HOH   A O     1 
HETATM 5770 O O     . HOH   G 4 .   ? 12.000  33.576  36.554 1.00 43.19  ? 828 HOH   A O     1 
HETATM 5771 O O     . HOH   G 4 .   ? 8.005   39.876  60.158 1.00 55.63  ? 829 HOH   A O     1 
HETATM 5772 O O     . HOH   G 4 .   ? 10.071  49.532  57.676 1.00 54.54  ? 830 HOH   A O     1 
HETATM 5773 O O     . HOH   G 4 .   ? -12.137 23.548  56.523 1.00 56.00  ? 831 HOH   A O     1 
HETATM 5774 O O     . HOH   G 4 .   ? 24.066  0.164   58.941 1.00 45.79  ? 832 HOH   A O     1 
HETATM 5775 O O     . HOH   G 4 .   ? 8.165   25.826  69.818 1.00 45.93  ? 833 HOH   A O     1 
HETATM 5776 O O     . HOH   G 4 .   ? 0.598   16.828  35.360 1.00 59.16  ? 834 HOH   A O     1 
HETATM 5777 O O     . HOH   G 4 .   ? 13.874  15.413  61.797 1.00 38.13  ? 835 HOH   A O     1 
HETATM 5778 O O     . HOH   G 4 .   ? 15.936  44.318  48.667 1.00 46.85  ? 836 HOH   A O     1 
HETATM 5779 O O     . HOH   G 4 .   ? 13.386  15.317  34.288 1.00 49.03  ? 837 HOH   A O     1 
HETATM 5780 O O     . HOH   G 4 .   ? 13.021  17.126  73.521 1.00 48.83  ? 838 HOH   A O     1 
HETATM 5781 O O     . HOH   G 4 .   ? 9.151   23.609  70.946 1.00 48.38  ? 839 HOH   A O     1 
HETATM 5782 O O     . HOH   G 4 .   ? 26.205  27.085  46.933 1.00 45.47  ? 840 HOH   A O     1 
HETATM 5783 O O     . HOH   G 4 .   ? -8.550  29.687  50.673 1.00 57.07  ? 841 HOH   A O     1 
HETATM 5784 O O     . HOH   G 4 .   ? 14.533  20.307  72.397 1.00 50.01  ? 842 HOH   A O     1 
HETATM 5785 O O     . HOH   G 4 .   ? 24.524  2.575   64.400 1.00 56.11  ? 843 HOH   A O     1 
HETATM 5786 O O     . HOH   H 4 .   ? 8.165   2.286   35.586 1.00 57.69  ? 701 HOH   B O     1 
HETATM 5787 O O     . HOH   H 4 .   ? 30.518  14.663  25.444 1.00 46.10  ? 702 HOH   B O     1 
HETATM 5788 O O     . HOH   H 4 .   ? 28.503  13.442  10.501 1.00 44.50  ? 703 HOH   B O     1 
HETATM 5789 O O     . HOH   H 4 .   ? 38.058  -7.152  5.991  1.00 53.15  ? 704 HOH   B O     1 
HETATM 5790 O O     . HOH   H 4 .   ? 34.456  -4.650  30.115 1.00 43.67  ? 705 HOH   B O     1 
HETATM 5791 O O     . HOH   H 4 .   ? 29.739  -3.357  38.117 1.00 50.08  ? 706 HOH   B O     1 
HETATM 5792 O O     . HOH   H 4 .   ? 30.351  4.578   28.027 1.00 35.95  ? 707 HOH   B O     1 
HETATM 5793 O O     . HOH   H 4 .   ? 16.791  12.625  22.468 1.00 42.98  ? 708 HOH   B O     1 
HETATM 5794 O O     . HOH   H 4 .   ? 30.511  6.297   3.834  1.00 34.82  ? 709 HOH   B O     1 
HETATM 5795 O O     . HOH   H 4 .   ? 31.992  -5.665  25.376 1.00 42.94  ? 710 HOH   B O     1 
HETATM 5796 O O     . HOH   H 4 .   ? 46.826  -4.971  21.316 1.00 45.47  ? 711 HOH   B O     1 
HETATM 5797 O O     . HOH   H 4 .   ? 41.064  -4.217  13.055 1.00 43.23  ? 712 HOH   B O     1 
HETATM 5798 O O     . HOH   H 4 .   ? 34.523  16.557  6.505  1.00 42.83  ? 713 HOH   B O     1 
HETATM 5799 O O     . HOH   H 4 .   ? 28.870  4.691   -3.333 1.00 55.57  ? 714 HOH   B O     1 
HETATM 5800 O O     . HOH   H 4 .   ? 25.150  1.081   32.060 1.00 39.41  ? 715 HOH   B O     1 
HETATM 5801 O O     . HOH   H 4 .   ? 15.397  -6.582  8.407  1.00 45.09  ? 716 HOH   B O     1 
HETATM 5802 O O     . HOH   H 4 .   ? 16.154  4.190   22.506 1.00 35.72  ? 717 HOH   B O     1 
HETATM 5803 O O     . HOH   H 4 .   ? 25.176  9.318   1.452  1.00 40.15  ? 718 HOH   B O     1 
HETATM 5804 O O     . HOH   H 4 .   ? 27.770  7.172   -3.426 1.00 48.23  ? 719 HOH   B O     1 
HETATM 5805 O O     . HOH   H 4 .   ? 17.819  -8.717  18.529 1.00 39.42  ? 720 HOH   B O     1 
HETATM 5806 O O     . HOH   H 4 .   ? 19.503  5.016   30.962 1.00 47.79  ? 721 HOH   B O     1 
HETATM 5807 O O     . HOH   H 4 .   ? 20.781  -7.051  -0.046 1.00 43.14  ? 722 HOH   B O     1 
HETATM 5808 O O     . HOH   H 4 .   ? 29.895  -3.346  31.677 1.00 40.30  ? 723 HOH   B O     1 
HETATM 5809 O O     . HOH   H 4 .   ? 37.696  16.101  12.167 1.00 41.60  ? 724 HOH   B O     1 
HETATM 5810 O O     . HOH   H 4 .   ? 20.964  -6.982  4.298  1.00 40.48  ? 725 HOH   B O     1 
HETATM 5811 O O     . HOH   H 4 .   ? 18.242  3.502   14.650 1.00 31.25  ? 726 HOH   B O     1 
HETATM 5812 O O     . HOH   H 4 .   ? 29.934  15.551  -1.655 1.00 46.97  ? 727 HOH   B O     1 
HETATM 5813 O O     . HOH   H 4 .   ? 32.561  20.334  35.004 1.00 74.71  ? 728 HOH   B O     1 
HETATM 5814 O O     . HOH   H 4 .   ? 34.695  21.211  2.848  1.00 40.67  ? 729 HOH   B O     1 
HETATM 5815 O O     . HOH   H 4 .   ? 37.795  11.901  3.917  1.00 40.84  ? 730 HOH   B O     1 
HETATM 5816 O O     . HOH   H 4 .   ? 13.802  9.645   -2.535 1.00 52.60  ? 731 HOH   B O     1 
HETATM 5817 O O     . HOH   H 4 .   ? 9.974   2.882   16.100 1.00 42.58  ? 732 HOH   B O     1 
HETATM 5818 O O     . HOH   H 4 .   ? 17.001  6.291   14.439 1.00 36.94  ? 733 HOH   B O     1 
HETATM 5819 O O     . HOH   H 4 .   ? 28.022  2.144   22.658 1.00 30.59  ? 734 HOH   B O     1 
HETATM 5820 O O     . HOH   H 4 .   ? 27.517  8.729   11.108 1.00 34.09  ? 735 HOH   B O     1 
HETATM 5821 O O     . HOH   H 4 .   ? 33.358  3.926   39.899 1.00 49.75  ? 736 HOH   B O     1 
HETATM 5822 O O     . HOH   H 4 .   ? 19.793  -6.614  19.021 1.00 37.21  ? 737 HOH   B O     1 
HETATM 5823 O O     . HOH   H 4 .   ? 38.212  -9.503  26.111 1.00 45.03  ? 738 HOH   B O     1 
HETATM 5824 O O     . HOH   H 4 .   ? 38.337  -12.101 24.757 1.00 47.09  ? 739 HOH   B O     1 
HETATM 5825 O O     . HOH   H 4 .   ? 18.370  2.087   17.000 1.00 32.15  ? 740 HOH   B O     1 
HETATM 5826 O O     . HOH   H 4 .   ? 41.400  18.454  19.985 1.00 56.98  ? 741 HOH   B O     1 
HETATM 5827 O O     . HOH   H 4 .   ? 16.454  -2.287  2.442  1.00 46.93  ? 742 HOH   B O     1 
HETATM 5828 O O     . HOH   H 4 .   ? 20.186  10.682  20.562 1.00 36.13  ? 743 HOH   B O     1 
HETATM 5829 O O     . HOH   H 4 .   ? 10.120  1.556   25.803 1.00 48.16  ? 744 HOH   B O     1 
HETATM 5830 O O     . HOH   H 4 .   ? 37.485  26.260  3.548  1.00 53.02  ? 745 HOH   B O     1 
HETATM 5831 O O     . HOH   H 4 .   ? 16.814  11.423  15.538 1.00 38.66  ? 746 HOH   B O     1 
HETATM 5832 O O     . HOH   H 4 .   ? 39.265  21.299  11.719 1.00 55.83  ? 747 HOH   B O     1 
HETATM 5833 O O     . HOH   H 4 .   ? 46.352  6.243   13.523 1.00 48.40  ? 748 HOH   B O     1 
HETATM 5834 O O     . HOH   H 4 .   ? 38.415  5.108   8.921  1.00 32.27  ? 749 HOH   B O     1 
HETATM 5835 O O     . HOH   H 4 .   ? 38.328  6.854   28.032 1.00 35.98  ? 750 HOH   B O     1 
HETATM 5836 O O     . HOH   H 4 .   ? 45.453  7.726   27.913 1.00 49.52  ? 751 HOH   B O     1 
HETATM 5837 O O     . HOH   H 4 .   ? 14.125  -2.536  19.389 1.00 40.83  ? 752 HOH   B O     1 
HETATM 5838 O O     . HOH   H 4 .   ? 12.903  -10.720 13.122 1.00 50.56  ? 753 HOH   B O     1 
HETATM 5839 O O     . HOH   H 4 .   ? 21.166  3.794   28.154 1.00 34.68  ? 754 HOH   B O     1 
HETATM 5840 O O     . HOH   H 4 .   ? 32.622  13.672  8.178  1.00 36.45  ? 755 HOH   B O     1 
HETATM 5841 O O     . HOH   H 4 .   ? 32.530  -10.024 10.492 1.00 49.06  ? 756 HOH   B O     1 
HETATM 5842 O O     . HOH   H 4 .   ? 31.813  -5.336  28.452 1.00 40.88  ? 757 HOH   B O     1 
HETATM 5843 O O     . HOH   H 4 .   ? 14.765  9.807   15.635 1.00 45.28  ? 758 HOH   B O     1 
HETATM 5844 O O     . HOH   H 4 .   ? 0.193   -5.691  29.555 1.00 50.31  ? 759 HOH   B O     1 
HETATM 5845 O O     . HOH   H 4 .   ? 35.310  18.022  2.906  1.00 43.81  ? 760 HOH   B O     1 
HETATM 5846 O O     . HOH   H 4 .   ? 15.643  7.135   16.623 1.00 40.28  ? 761 HOH   B O     1 
HETATM 5847 O O     . HOH   H 4 .   ? 18.507  -11.218 17.483 1.00 46.24  ? 762 HOH   B O     1 
HETATM 5848 O O     . HOH   H 4 .   ? 10.183  4.364   22.933 1.00 46.08  ? 763 HOH   B O     1 
HETATM 5849 O O     . HOH   H 4 .   ? 19.442  7.069   13.871 1.00 35.05  ? 764 HOH   B O     1 
HETATM 5850 O O     . HOH   H 4 .   ? 29.981  -5.404  23.646 1.00 39.31  ? 765 HOH   B O     1 
HETATM 5851 O O     . HOH   H 4 .   ? 32.875  7.346   0.247  1.00 44.35  ? 766 HOH   B O     1 
HETATM 5852 O O     . HOH   H 4 .   ? 15.919  2.135   20.600 1.00 39.97  ? 767 HOH   B O     1 
HETATM 5853 O O     . HOH   H 4 .   ? 29.592  1.548   -1.449 1.00 45.90  ? 768 HOH   B O     1 
HETATM 5854 O O     . HOH   H 4 .   ? 29.060  10.095  13.070 1.00 32.82  ? 769 HOH   B O     1 
HETATM 5855 O O     . HOH   H 4 .   ? 22.715  -7.987  6.033  1.00 48.83  ? 770 HOH   B O     1 
HETATM 5856 O O     . HOH   H 4 .   ? 40.724  -4.315  10.307 1.00 48.39  ? 771 HOH   B O     1 
HETATM 5857 O O     . HOH   H 4 .   ? 47.455  0.435   22.916 1.00 40.71  ? 772 HOH   B O     1 
HETATM 5858 O O     . HOH   H 4 .   ? 22.636  6.968   29.053 1.00 44.53  ? 773 HOH   B O     1 
HETATM 5859 O O     . HOH   H 4 .   ? 8.782   6.192   14.249 1.00 45.33  ? 774 HOH   B O     1 
HETATM 5860 O O     . HOH   H 4 .   ? 34.776  12.109  1.153  1.00 41.14  ? 775 HOH   B O     1 
HETATM 5861 O O     . HOH   H 4 .   ? 13.484  2.804   34.448 1.00 48.13  ? 776 HOH   B O     1 
HETATM 5862 O O     . HOH   H 4 .   ? 27.624  19.592  -4.153 1.00 50.72  ? 777 HOH   B O     1 
HETATM 5863 O O     . HOH   H 4 .   ? 37.842  7.407   9.758  1.00 35.52  ? 778 HOH   B O     1 
HETATM 5864 O O     . HOH   H 4 .   ? 10.490  7.347   30.014 1.00 47.58  ? 779 HOH   B O     1 
HETATM 5865 O O     . HOH   H 4 .   ? 36.845  4.604   28.507 1.00 36.82  ? 780 HOH   B O     1 
HETATM 5866 O O     . HOH   H 4 .   ? 35.801  -8.168  40.050 1.00 52.75  ? 781 HOH   B O     1 
HETATM 5867 O O     . HOH   H 4 .   ? 30.493  3.104   30.187 1.00 40.17  ? 782 HOH   B O     1 
HETATM 5868 O O     . HOH   H 4 .   ? 15.583  4.965   17.880 1.00 37.10  ? 783 HOH   B O     1 
HETATM 5869 O O     . HOH   H 4 .   ? 34.764  0.282   1.231  1.00 46.62  ? 784 HOH   B O     1 
HETATM 5870 O O     . HOH   H 4 .   ? 23.628  3.364   31.949 1.00 46.56  ? 785 HOH   B O     1 
HETATM 5871 O O     . HOH   H 4 .   ? 16.455  -9.173  8.366  1.00 45.43  ? 786 HOH   B O     1 
HETATM 5872 O O     . HOH   H 4 .   ? 22.238  -6.020  33.761 1.00 38.92  ? 787 HOH   B O     1 
HETATM 5873 O O     . HOH   H 4 .   ? 26.054  7.672   2.913  1.00 42.11  ? 788 HOH   B O     1 
HETATM 5874 O O     . HOH   H 4 .   ? 46.853  -6.616  33.964 1.00 54.74  ? 789 HOH   B O     1 
HETATM 5875 O O     . HOH   H 4 .   ? 17.782  -0.649  17.557 1.00 36.80  ? 790 HOH   B O     1 
HETATM 5876 O O     . HOH   H 4 .   ? 22.267  -7.063  1.870  1.00 44.71  ? 791 HOH   B O     1 
HETATM 5877 O O     . HOH   H 4 .   ? 35.788  -14.248 29.609 1.00 52.09  ? 792 HOH   B O     1 
HETATM 5878 O O     . HOH   H 4 .   ? 46.256  -11.591 28.083 1.00 51.56  ? 793 HOH   B O     1 
HETATM 5879 O O     . HOH   H 4 .   ? 16.070  -12.808 16.906 1.00 50.69  ? 794 HOH   B O     1 
HETATM 5880 O O     . HOH   H 4 .   ? 24.487  -8.046  32.697 1.00 39.18  ? 795 HOH   B O     1 
HETATM 5881 O O     . HOH   H 4 .   ? 28.719  29.553  9.028  1.00 60.56  ? 796 HOH   B O     1 
HETATM 5882 O O     . HOH   H 4 .   ? 47.336  -1.687  10.948 1.00 49.88  ? 797 HOH   B O     1 
HETATM 5883 O O     . HOH   H 4 .   ? 42.603  -5.735  38.982 1.00 53.02  ? 798 HOH   B O     1 
HETATM 5884 O O     . HOH   H 4 .   ? 23.313  29.556  6.998  1.00 60.91  ? 799 HOH   B O     1 
HETATM 5885 O O     . HOH   H 4 .   ? 5.611   -5.076  16.125 1.00 62.72  ? 800 HOH   B O     1 
HETATM 5886 O O     . HOH   H 4 .   ? 10.003  -2.035  9.663  1.00 51.91  ? 801 HOH   B O     1 
HETATM 5887 O O     . HOH   H 4 .   ? 33.138  19.405  -1.573 1.00 55.31  ? 802 HOH   B O     1 
HETATM 5888 O O     . HOH   H 4 .   ? 15.270  -0.095  19.323 1.00 42.35  ? 803 HOH   B O     1 
HETATM 5889 O O     . HOH   H 4 .   ? 44.236  5.941   12.488 1.00 46.68  ? 804 HOH   B O     1 
HETATM 5890 O O     . HOH   H 4 .   ? 33.295  6.466   38.492 1.00 58.54  ? 805 HOH   B O     1 
HETATM 5891 O O     . HOH   H 4 .   ? 30.994  7.824   38.880 1.00 59.37  ? 806 HOH   B O     1 
HETATM 5892 O O     . HOH   H 4 .   ? 31.005  29.613  8.774  1.00 52.83  ? 807 HOH   B O     1 
HETATM 5893 O O     . HOH   H 4 .   ? 7.410   2.508   15.616 1.00 51.47  ? 808 HOH   B O     1 
HETATM 5894 O O     . HOH   H 4 .   ? 22.080  4.421   30.492 1.00 45.92  ? 809 HOH   B O     1 
HETATM 5895 O O     . HOH   H 4 .   ? 48.303  -9.705  28.359 1.00 52.60  ? 810 HOH   B O     1 
HETATM 5896 O O     . HOH   H 4 .   ? -0.041  -5.637  32.188 1.00 56.60  ? 811 HOH   B O     1 
HETATM 5897 O O     . HOH   H 4 .   ? 9.649   -0.206  12.194 1.00 54.51  ? 812 HOH   B O     1 
HETATM 5898 O O     . HOH   H 4 .   ? 13.862  -12.323 11.341 1.00 50.68  ? 813 HOH   B O     1 
HETATM 5899 O O     . HOH   H 4 .   ? 15.271  -11.493 8.938  1.00 50.26  ? 814 HOH   B O     1 
HETATM 5900 O O     . HOH   H 4 .   ? 28.805  -15.861 34.997 1.00 52.79  ? 815 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   . PRO A 3   ? 0.7699 1.7703 1.1782 -0.2549 -0.0388 0.1641  27  PRO A N   
2    C CA  . PRO A 3   ? 0.8572 1.8071 1.2401 -0.2292 -0.0283 0.1524  27  PRO A CA  
3    C C   . PRO A 3   ? 0.8940 1.8388 1.2804 -0.1947 -0.0388 0.1448  27  PRO A C   
4    O O   . PRO A 3   ? 0.9024 1.7930 1.2592 -0.1982 -0.0501 0.1358  27  PRO A O   
5    C CB  . PRO A 3   ? 0.8768 1.7547 1.2162 -0.2668 -0.0373 0.1477  27  PRO A CB  
6    C CG  . PRO A 3   ? 0.8498 1.7306 1.1874 -0.3058 -0.0607 0.1528  27  PRO A CG  
7    C CD  . PRO A 3   ? 0.7436 1.7061 1.1273 -0.2967 -0.0631 0.1634  27  PRO A CD  
8    N N   . GLN A 4   ? 0.9137 1.9119 1.3345 -0.1611 -0.0350 0.1486  28  GLN A N   
9    C CA  . GLN A 4   ? 0.9111 1.9058 1.3363 -0.1281 -0.0467 0.1441  28  GLN A CA  
10   C C   . GLN A 4   ? 0.8271 1.8430 1.2708 -0.0776 -0.0267 0.1416  28  GLN A C   
11   O O   . GLN A 4   ? 0.8231 1.8774 1.2940 -0.0515 -0.0305 0.1460  28  GLN A O   
12   C CB  . GLN A 4   ? 0.8756 1.9065 1.3203 -0.1410 -0.0703 0.1521  28  GLN A CB  
13   N N   . SER A 5   ? 0.5894 1.5749 1.0150 -0.0634 -0.0056 0.1339  29  SER A N   
14   C CA  . SER A 5   ? 0.4586 1.4527 0.8932 -0.0171 0.0145  0.1289  29  SER A CA  
15   C C   . SER A 5   ? 0.3906 1.3640 0.8233 0.0200  0.0041  0.1236  29  SER A C   
16   O O   . SER A 5   ? 0.4010 1.3480 0.8204 0.0104  -0.0167 0.1229  29  SER A O   
17   C CB  . SER A 5   ? 0.4181 1.3732 0.8252 -0.0120 0.0365  0.1201  29  SER A CB  
18   O OG  . SER A 5   ? 0.4060 1.3018 0.7810 -0.0164 0.0291  0.1117  29  SER A OG  
19   N N   . THR A 6   ? 0.3468 1.3291 0.7903 0.0624  0.0185  0.1201  30  THR A N   
20   C CA  . THR A 6   ? 0.3677 1.3242 0.8069 0.0988  0.0096  0.1160  30  THR A CA  
21   C C   . THR A 6   ? 0.3327 1.2194 0.7335 0.1036  0.0062  0.1056  30  THR A C   
22   O O   . THR A 6   ? 0.3520 1.2122 0.7432 0.1142  -0.0109 0.1055  30  THR A O   
23   C CB  . THR A 6   ? 0.3652 1.3342 0.8179 0.1421  0.0273  0.1124  30  THR A CB  
24   O OG1 . THR A 6   ? 0.3871 1.4252 0.8806 0.1424  0.0255  0.1235  30  THR A OG1 
25   C CG2 . THR A 6   ? 0.3770 1.2991 0.8144 0.1796  0.0206  0.1063  30  THR A CG2 
26   N N   . LEU A 7   ? 0.3556 1.2124 0.7335 0.0953  0.0218  0.0977  31  LEU A N   
27   C CA  . LEU A 7   ? 0.3630 1.1587 0.7072 0.0966  0.0181  0.0885  31  LEU A CA  
28   C C   . LEU A 7   ? 0.3053 1.0938 0.6421 0.0607  -0.0045 0.0929  31  LEU A C   
29   O O   . LEU A 7   ? 0.3083 1.0420 0.6175 0.0663  -0.0177 0.0877  31  LEU A O   
30   C CB  . LEU A 7   ? 0.3498 1.1180 0.6716 0.0948  0.0398  0.0796  31  LEU A CB  
31   C CG  . LEU A 7   ? 0.4223 1.1811 0.7400 0.1330  0.0597  0.0716  31  LEU A CG  
32   C CD1 . LEU A 7   ? 0.4117 1.1472 0.7048 0.1277  0.0803  0.0636  31  LEU A CD1 
33   C CD2 . LEU A 7   ? 0.4162 1.1275 0.7182 0.1688  0.0537  0.0638  31  LEU A CD2 
34   N N   . ARG A 8   ? 0.3676 1.1868 0.7147 0.0206  -0.0091 0.1001  32  ARG A N   
35   C CA  . ARG A 8   ? 0.3059 1.1009 0.6350 -0.0172 -0.0310 0.1012  32  ARG A CA  
36   C C   . ARG A 8   ? 0.3808 1.1973 0.7224 -0.0136 -0.0552 0.1075  32  ARG A C   
37   O O   . ARG A 8   ? 0.4193 1.1903 0.7312 -0.0261 -0.0728 0.1033  32  ARG A O   
38   C CB  . ARG A 8   ? 0.3686 1.1915 0.7060 -0.0621 -0.0301 0.1081  32  ARG A CB  
39   N N   . ARG A 9   ? 0.3477 1.2114 0.7202 0.0042  -0.0544 0.1152  33  ARG A N   
40   C CA  . ARG A 9   ? 0.3228 1.1988 0.7031 0.0118  -0.0762 0.1213  33  ARG A CA  
41   C C   . ARG A 9   ? 0.3412 1.1705 0.6997 0.0453  -0.0811 0.1161  33  ARG A C   
42   O O   . ARG A 9   ? 0.3810 1.1927 0.7246 0.0403  -0.1025 0.1185  33  ARG A O   
43   C CB  . ARG A 9   ? 0.3428 1.2808 0.7636 0.0277  -0.0725 0.1309  33  ARG A CB  
44   N N   . ALA A 10  ? 0.3279 1.1319 0.6801 0.0783  -0.0616 0.1090  34  ALA A N   
45   C CA  . ALA A 10  ? 0.3126 1.0652 0.6410 0.1090  -0.0653 0.1043  34  ALA A CA  
46   C C   . ALA A 10  ? 0.3591 1.0504 0.6453 0.0874  -0.0752 0.0973  34  ALA A C   
47   O O   . ALA A 10  ? 0.3722 1.0251 0.6352 0.0964  -0.0886 0.0976  34  ALA A O   
48   C CB  . ALA A 10  ? 0.3786 1.1067 0.7027 0.1446  -0.0416 0.0957  34  ALA A CB  
49   N N   . ILE A 11  ? 0.3662 1.0301 0.6329 0.0578  -0.0661 0.0894  35  ILE A N   
50   C CA  . ILE A 11  ? 0.3771 0.9699 0.5977 0.0346  -0.0732 0.0805  35  ILE A CA  
51   C C   . ILE A 11  ? 0.4213 1.0255 0.6363 0.0108  -0.0983 0.0861  35  ILE A C   
52   O O   . ILE A 11  ? 0.3903 0.9498 0.5743 0.0134  -0.1092 0.0832  35  ILE A O   
53   C CB  . ILE A 11  ? 0.3888 0.9557 0.5929 0.0078  -0.0605 0.0731  35  ILE A CB  
54   C CG1 . ILE A 11  ? 0.3762 0.9241 0.5773 0.0306  -0.0371 0.0665  35  ILE A CG1 
55   C CG2 . ILE A 11  ? 0.4344 0.9335 0.5940 -0.0152 -0.0691 0.0645  35  ILE A CG2 
56   C CD1 . ILE A 11  ? 0.3381 0.8826 0.5337 0.0064  -0.0248 0.0643  35  ILE A CD1 
57   N N   . THR A 12  ? 0.4288 1.0940 0.6723 -0.0146 -0.1078 0.0945  36  THR A N   
58   C CA  . THR A 12  ? 0.4232 1.0982 0.6578 -0.0427 -0.1334 0.0985  36  THR A CA  
59   C C   . THR A 12  ? 0.4040 1.0982 0.6454 -0.0188 -0.1509 0.1073  36  THR A C   
60   O O   . THR A 12  ? 0.3893 1.0615 0.6030 -0.0342 -0.1708 0.1069  36  THR A O   
61   C CB  . THR A 12  ? 0.4485 1.1902 0.7166 -0.0760 -0.1404 0.1071  36  THR A CB  
62   N N   . ALA A 13  ? 0.4028 1.1264 0.6741 0.0198  -0.1421 0.1139  37  ALA A N   
63   C CA  . ALA A 13  ? 0.3614 1.0852 0.6340 0.0448  -0.1549 0.1216  37  ALA A CA  
64   C C   . ALA A 13  ? 0.3803 1.0430 0.6144 0.0645  -0.1581 0.1184  37  ALA A C   
65   O O   . ALA A 13  ? 0.3827 1.0338 0.6055 0.0757  -0.1729 0.1251  37  ALA A O   
66   C CB  . ALA A 13  ? 0.3712 1.1351 0.6841 0.0791  -0.1424 0.1280  37  ALA A CB  
67   N N   . ALA A 14  ? 0.3780 0.9834 0.5849 0.0665  -0.1404 0.1061  38  ALA A N   
68   C CA  . ALA A 14  ? 0.4602 0.9933 0.6262 0.0813  -0.1378 0.1007  38  ALA A CA  
69   C C   . ALA A 14  ? 0.4548 0.9381 0.5752 0.0512  -0.1463 0.0931  38  ALA A C   
70   O O   . ALA A 14  ? 0.4675 0.8970 0.5537 0.0600  -0.1458 0.0905  38  ALA A O   
71   C CB  . ALA A 14  ? 0.3986 0.8907 0.5577 0.0997  -0.1130 0.0902  38  ALA A CB  
72   N N   . TYR A 15  ? 0.4466 0.9472 0.5654 0.0159  -0.1540 0.0898  39  TYR A N   
73   C CA  . TYR A 15  ? 0.4950 0.9423 0.5687 -0.0128 -0.1571 0.0785  39  TYR A CA  
74   C C   . TYR A 15  ? 0.5153 0.9255 0.5515 -0.0069 -0.1685 0.0798  39  TYR A C   
75   O O   . TYR A 15  ? 0.5463 0.8964 0.5460 -0.0059 -0.1584 0.0705  39  TYR A O   
76   C CB  . TYR A 15  ? 0.5332 1.0120 0.6121 -0.0505 -0.1710 0.0781  39  TYR A CB  
77   C CG  . TYR A 15  ? 0.5527 0.9745 0.5871 -0.0806 -0.1706 0.0638  39  TYR A CG  
78   C CD1 . TYR A 15  ? 0.5259 0.8815 0.5273 -0.0725 -0.1541 0.0522  39  TYR A CD1 
79   C CD2 . TYR A 15  ? 0.6371 1.0715 0.6624 -0.1171 -0.1875 0.0619  39  TYR A CD2 
80   C CE1 . TYR A 15  ? 0.5959 0.8999 0.5578 -0.0959 -0.1527 0.0389  39  TYR A CE1 
81   C CE2 . TYR A 15  ? 0.6903 1.0661 0.6715 -0.1425 -0.1868 0.0474  39  TYR A CE2 
82   C CZ  . TYR A 15  ? 0.6508 0.9620 0.6011 -0.1297 -0.1685 0.0360  39  TYR A CZ  
83   O OH  . TYR A 15  ? 0.6760 0.9292 0.5836 -0.1504 -0.1666 0.0215  39  TYR A OH  
84   N N   . ARG A 16  ? 0.5221 0.9702 0.5673 -0.0027 -0.1894 0.0926  40  ARG A N   
85   C CA  . ARG A 16  ? 0.6128 1.0308 0.6215 0.0028  -0.2018 0.0969  40  ARG A CA  
86   C C   . ARG A 16  ? 0.6234 1.0697 0.6552 0.0365  -0.2097 0.1141  40  ARG A C   
87   O O   . ARG A 16  ? 0.6330 1.0884 0.6514 0.0386  -0.2297 0.1251  40  ARG A O   
88   C CB  . ARG A 16  ? 0.6843 1.1100 0.6669 -0.0295 -0.2241 0.0956  40  ARG A CB  
89   C CG  . ARG A 16  ? 0.7047 1.1009 0.6648 -0.0627 -0.2177 0.0784  40  ARG A CG  
90   C CD  . ARG A 16  ? 0.7679 1.1623 0.6941 -0.0950 -0.2405 0.0747  40  ARG A CD  
91   N NE  . ARG A 16  ? 0.8378 1.2066 0.7473 -0.1268 -0.2359 0.0591  40  ARG A NE  
92   C CZ  . ARG A 16  ? 0.8402 1.1433 0.7116 -0.1313 -0.2193 0.0431  40  ARG A CZ  
93   N NH1 . ARG A 16  ? 0.8251 1.0855 0.6722 -0.1090 -0.2051 0.0403  40  ARG A NH1 
94   N NH2 . ARG A 16  ? 0.8697 1.1501 0.7279 -0.1590 -0.2169 0.0305  40  ARG A NH2 
95   N N   . ARG A 17  ? 0.5848 1.0426 0.6496 0.0641  -0.1942 0.1162  41  ARG A N   
96   C CA  . ARG A 17  ? 0.5778 1.0512 0.6613 0.1006  -0.1993 0.1310  41  ARG A CA  
97   C C   . ARG A 17  ? 0.5747 0.9876 0.6136 0.1099  -0.2020 0.1346  41  ARG A C   
98   O O   . ARG A 17  ? 0.5488 0.9044 0.5540 0.1004  -0.1878 0.1228  41  ARG A O   
99   C CB  . ARG A 17  ? 0.5513 1.0303 0.6665 0.1288  -0.1783 0.1280  41  ARG A CB  
100  C CG  . ARG A 17  ? 0.5259 0.9944 0.6515 0.1671  -0.1780 0.1380  41  ARG A CG  
101  C CD  . ARG A 17  ? 0.5267 1.0049 0.6829 0.1919  -0.1572 0.1323  41  ARG A CD  
102  N NE  . ARG A 17  ? 0.5268 1.0717 0.7259 0.1844  -0.1552 0.1326  41  ARG A NE  
103  C CZ  . ARG A 17  ? 0.4745 1.0418 0.6957 0.1850  -0.1366 0.1243  41  ARG A CZ  
104  N NH1 . ARG A 17  ? 0.4331 0.9617 0.6382 0.1936  -0.1193 0.1139  41  ARG A NH1 
105  N NH2 . ARG A 17  ? 0.4466 1.0761 0.7052 0.1753  -0.1353 0.1268  41  ARG A NH2 
106  N N   . PRO A 18  ? 0.5564 0.9725 0.5936 0.1254  -0.2170 0.1486  42  PRO A N   
107  C CA  . PRO A 18  ? 0.5879 0.9485 0.5824 0.1340  -0.2198 0.1552  42  PRO A CA  
108  C C   . PRO A 18  ? 0.6402 0.9519 0.6251 0.1529  -0.1989 0.1505  42  PRO A C   
109  O O   . PRO A 18  ? 0.5601 0.8801 0.5756 0.1771  -0.1877 0.1495  42  PRO A O   
110  C CB  . PRO A 18  ? 0.5876 0.9610 0.5963 0.1532  -0.2351 0.1701  42  PRO A CB  
111  C CG  . PRO A 18  ? 0.6063 1.0438 0.6506 0.1408  -0.2471 0.1701  42  PRO A CG  
112  C CD  . PRO A 18  ? 0.5483 1.0142 0.6200 0.1307  -0.2316 0.1578  42  PRO A CD  
113  N N   . GLU A 19  ? 0.5985 0.8535 0.5394 0.1386  -0.1910 0.1444  43  GLU A N   
114  C CA  . GLU A 19  ? 0.6601 0.8620 0.5901 0.1485  -0.1702 0.1370  43  GLU A CA  
115  C C   . GLU A 19  ? 0.6339 0.8210 0.5749 0.1829  -0.1712 0.1498  43  GLU A C   
116  O O   . GLU A 19  ? 0.6953 0.8623 0.6494 0.1983  -0.1557 0.1425  43  GLU A O   
117  C CB  . GLU A 19  ? 0.5887 0.7409 0.4715 0.1288  -0.1645 0.1331  43  GLU A CB  
118  C CG  . GLU A 19  ? 0.6744 0.7756 0.5456 0.1326  -0.1442 0.1256  43  GLU A CG  
119  C CD  . GLU A 19  ? 0.6274 0.6965 0.4618 0.1084  -0.1349 0.1171  43  GLU A CD  
120  O OE1 . GLU A 19  ? 0.7122 0.7930 0.5252 0.0906  -0.1441 0.1165  43  GLU A OE1 
121  O OE2 . GLU A 19  ? 0.6046 0.6379 0.4311 0.1076  -0.1186 0.1108  43  GLU A OE2 
122  N N   . THR A 20  ? 0.6424 0.8358 0.5767 0.1948  -0.1898 0.1681  44  THR A N   
123  C CA  . THR A 20  ? 0.6784 0.8438 0.6218 0.2216  -0.1889 0.1771  44  THR A CA  
124  C C   . THR A 20  ? 0.6801 0.8759 0.6702 0.2437  -0.1804 0.1704  44  THR A C   
125  O O   . THR A 20  ? 0.7213 0.8828 0.7159 0.2647  -0.1695 0.1683  44  THR A O   
126  C CB  . THR A 20  ? 0.6413 0.8080 0.5742 0.2233  -0.2098 0.1947  44  THR A CB  
127  N N   . GLU A 21  ? 0.6199 0.8787 0.6433 0.2373  -0.1845 0.1665  45  GLU A N   
128  C CA  . GLU A 21  ? 0.6179 0.9119 0.6854 0.2565  -0.1741 0.1603  45  GLU A CA  
129  C C   . GLU A 21  ? 0.6046 0.8924 0.6771 0.2552  -0.1527 0.1440  45  GLU A C   
130  O O   . GLU A 21  ? 0.5668 0.8616 0.6638 0.2749  -0.1390 0.1371  45  GLU A O   
131  C CB  . GLU A 21  ? 0.6612 1.0281 0.7640 0.2478  -0.1862 0.1642  45  GLU A CB  
132  N N   . CYS A 22  ? 0.6095 0.8838 0.6576 0.2328  -0.1495 0.1372  46  CYS A N   
133  C CA  . CYS A 22  ? 0.5763 0.8357 0.6273 0.2259  -0.1283 0.1195  46  CYS A CA  
134  C C   . CYS A 22  ? 0.6025 0.8007 0.6358 0.2448  -0.1152 0.1145  46  CYS A C   
135  O O   . CYS A 22  ? 0.5644 0.7539 0.6054 0.2488  -0.0985 0.1012  46  CYS A O   
136  C CB  . CYS A 22  ? 0.5884 0.8330 0.6162 0.1883  -0.1245 0.1087  46  CYS A CB  
137  S SG  . CYS A 22  ? 0.5383 0.8464 0.5844 0.1597  -0.1361 0.1084  46  CYS A SG  
138  N N   . LEU A 23  ? 0.5914 0.7454 0.5986 0.2543  -0.1232 0.1253  47  LEU A N   
139  C CA  . LEU A 23  ? 0.6288 0.7157 0.6107 0.2596  -0.1118 0.1195  47  LEU A CA  
140  C C   . LEU A 23  ? 0.6416 0.7100 0.6377 0.2864  -0.1025 0.1144  47  LEU A C   
141  O O   . LEU A 23  ? 0.6991 0.7362 0.6877 0.2881  -0.0881 0.1009  47  LEU A O   
142  C CB  . LEU A 23  ? 0.7014 0.7426 0.6468 0.2521  -0.1216 0.1326  47  LEU A CB  
143  C CG  . LEU A 23  ? 0.7071 0.7212 0.6232 0.2189  -0.1152 0.1262  47  LEU A CG  
144  C CD1 . LEU A 23  ? 0.7068 0.6769 0.6139 0.2146  -0.0982 0.1128  47  LEU A CD1 
145  C CD2 . LEU A 23  ? 0.6828 0.7418 0.6085 0.1951  -0.1154 0.1178  47  LEU A CD2 
146  N N   . PRO A 24  ? 0.6539 0.7375 0.6685 0.3049  -0.1095 0.1229  48  PRO A N   
147  C CA  . PRO A 24  ? 0.6609 0.7157 0.6816 0.3284  -0.0998 0.1166  48  PRO A CA  
148  C C   . PRO A 24  ? 0.6434 0.7123 0.6788 0.3336  -0.0813 0.0982  48  PRO A C   
149  O O   . PRO A 24  ? 0.7213 0.7417 0.7403 0.3400  -0.0703 0.0872  48  PRO A O   
150  C CB  . PRO A 24  ? 0.6825 0.7719 0.7289 0.3472  -0.1115 0.1293  48  PRO A CB  
151  C CG  . PRO A 24  ? 0.6978 0.7988 0.7330 0.3316  -0.1306 0.1458  48  PRO A CG  
152  C CD  . PRO A 24  ? 0.6576 0.7765 0.6828 0.3053  -0.1283 0.1395  48  PRO A CD  
153  N N   . PRO A 25  ? 0.6300 0.7631 0.6941 0.3292  -0.0775 0.0943  49  PRO A N   
154  C CA  . PRO A 25  ? 0.5830 0.7250 0.6552 0.3311  -0.0586 0.0774  49  PRO A CA  
155  C C   . PRO A 25  ? 0.6623 0.7576 0.7050 0.3159  -0.0506 0.0663  49  PRO A C   
156  O O   . PRO A 25  ? 0.6560 0.7249 0.6901 0.3212  -0.0367 0.0521  49  PRO A O   
157  C CB  . PRO A 25  ? 0.5969 0.8175 0.7029 0.3215  -0.0588 0.0794  49  PRO A CB  
158  C CG  . PRO A 25  ? 0.5915 0.8359 0.6995 0.3081  -0.0789 0.0949  49  PRO A CG  
159  C CD  . PRO A 25  ? 0.5850 0.7868 0.6773 0.3227  -0.0895 0.1051  49  PRO A CD  
160  N N   . LEU A 26  ? 0.6214 0.7066 0.6470 0.2964  -0.0595 0.0722  50  LEU A N   
161  C CA  . LEU A 26  ? 0.6110 0.6535 0.6109 0.2769  -0.0517 0.0616  50  LEU A CA  
162  C C   . LEU A 26  ? 0.6412 0.6129 0.6123 0.2856  -0.0509 0.0604  50  LEU A C   
163  O O   . LEU A 26  ? 0.6497 0.5877 0.6073 0.2818  -0.0404 0.0471  50  LEU A O   
164  C CB  . LEU A 26  ? 0.5576 0.6061 0.5465 0.2438  -0.0584 0.0658  50  LEU A CB  
165  C CG  . LEU A 26  ? 0.5506 0.6594 0.5619 0.2271  -0.0599 0.0652  50  LEU A CG  
166  C CD1 . LEU A 26  ? 0.5580 0.6600 0.5506 0.1974  -0.0667 0.0676  50  LEU A CD1 
167  C CD2 . LEU A 26  ? 0.5493 0.6792 0.5752 0.2224  -0.0451 0.0517  50  LEU A CD2 
168  N N   . VAL A 27  ? 0.6468 0.5951 0.6077 0.2903  -0.0621 0.0739  51  VAL A N   
169  C CA  . VAL A 27  ? 0.7119 0.5935 0.6470 0.2916  -0.0618 0.0739  51  VAL A CA  
170  C C   . VAL A 27  ? 0.7335 0.5977 0.6729 0.3080  -0.0510 0.0599  51  VAL A C   
171  O O   . VAL A 27  ? 0.7463 0.5615 0.6644 0.3016  -0.0451 0.0499  51  VAL A O   
172  C CB  . VAL A 27  ? 0.6950 0.5612 0.6219 0.2960  -0.0760 0.0928  51  VAL A CB  
173  N N   . GLU A 28  ? 0.6991 0.6047 0.6653 0.3283  -0.0484 0.0590  52  GLU A N   
174  C CA  . GLU A 28  ? 0.7351 0.6262 0.7030 0.3458  -0.0371 0.0455  52  GLU A CA  
175  C C   . GLU A 28  ? 0.7539 0.6499 0.7179 0.3365  -0.0230 0.0276  52  GLU A C   
176  O O   . GLU A 28  ? 0.7827 0.6357 0.7269 0.3376  -0.0158 0.0148  52  GLU A O   
177  C CB  . GLU A 28  ? 0.7550 0.6946 0.7544 0.3701  -0.0370 0.0502  52  GLU A CB  
178  N N   . ALA A 29  ? 0.7035 0.6508 0.6848 0.3262  -0.0198 0.0269  53  ALA A N   
179  C CA  . ALA A 29  ? 0.6824 0.6349 0.6590 0.3161  -0.0072 0.0118  53  ALA A CA  
180  C C   . ALA A 29  ? 0.7027 0.6034 0.6497 0.2960  -0.0084 0.0062  53  ALA A C   
181  O O   . ALA A 29  ? 0.6862 0.5748 0.6222 0.2889  0.0008  -0.0076 53  ALA A O   
182  C CB  . ALA A 29  ? 0.6407 0.6602 0.6435 0.3084  -0.0044 0.0144  53  ALA A CB  
183  N N   . ALA A 30  ? 0.7054 0.5772 0.6389 0.2858  -0.0196 0.0172  54  ALA A N   
184  C CA  . ALA A 30  ? 0.7124 0.5387 0.6205 0.2654  -0.0209 0.0139  54  ALA A CA  
185  C C   . ALA A 30  ? 0.8171 0.5808 0.7010 0.2646  -0.0233 0.0116  54  ALA A C   
186  O O   . ALA A 30  ? 0.8368 0.5632 0.7009 0.2459  -0.0242 0.0082  54  ALA A O   
187  C CB  . ALA A 30  ? 0.6686 0.5033 0.5751 0.2465  -0.0296 0.0274  54  ALA A CB  
188  N N   . THR A 31  ? 0.8277 0.5792 0.7133 0.2836  -0.0250 0.0139  55  THR A N   
189  C CA  . THR A 31  ? 0.8595 0.5491 0.7210 0.2827  -0.0279 0.0117  55  THR A CA  
190  C C   . THR A 31  ? 0.8422 0.5114 0.6912 0.2820  -0.0187 -0.0079 55  THR A C   
191  O O   . THR A 31  ? 0.8654 0.5632 0.7260 0.2977  -0.0097 -0.0177 55  THR A O   
192  C CB  . THR A 31  ? 0.8728 0.5534 0.7393 0.3051  -0.0330 0.0211  55  THR A CB  
193  O OG1 . THR A 31  ? 0.9182 0.6185 0.7936 0.3038  -0.0433 0.0403  55  THR A OG1 
194  C CG2 . THR A 31  ? 0.9288 0.5411 0.7685 0.3031  -0.0364 0.0193  55  THR A CG2 
195  N N   . GLN A 32  ? 0.8913 0.5137 0.7162 0.2621  -0.0214 -0.0129 56  GLN A N   
196  C CA  . GLN A 32  ? 0.8839 0.4804 0.6915 0.2579  -0.0160 -0.0308 56  GLN A CA  
197  C C   . GLN A 32  ? 0.9484 0.4845 0.7330 0.2612  -0.0209 -0.0327 56  GLN A C   
198  O O   . GLN A 32  ? 0.9609 0.4716 0.7415 0.2612  -0.0289 -0.0189 56  GLN A O   
199  C CB  . GLN A 32  ? 0.9318 0.5241 0.7303 0.2308  -0.0167 -0.0360 56  GLN A CB  
200  N N   . SER A 33  ? 0.9237 0.4358 0.6913 0.2639  -0.0161 -0.0497 57  SER A N   
201  C CA  . SER A 33  ? 0.9826 0.4334 0.7252 0.2663  -0.0207 -0.0539 57  SER A CA  
202  C C   . SER A 33  ? 0.9919 0.3994 0.7173 0.2374  -0.0317 -0.0456 57  SER A C   
203  O O   . SER A 33  ? 0.9984 0.4209 0.7277 0.2142  -0.0342 -0.0417 57  SER A O   
204  C CB  . SER A 33  ? 1.0161 0.4490 0.7398 0.2709  -0.0140 -0.0750 57  SER A CB  
205  O OG  . SER A 33  ? 1.0241 0.4595 0.7381 0.2458  -0.0148 -0.0834 57  SER A OG  
206  N N   . LYS A 34  ? 1.0283 0.3813 0.7348 0.2386  -0.0380 -0.0424 58  LYS A N   
207  C CA  . LYS A 34  ? 1.0699 0.3794 0.7586 0.2088  -0.0479 -0.0346 58  LYS A CA  
208  C C   . LYS A 34  ? 1.0705 0.3709 0.7458 0.1826  -0.0492 -0.0480 58  LYS A C   
209  O O   . LYS A 34  ? 1.0471 0.3472 0.7227 0.1541  -0.0549 -0.0401 58  LYS A O   
210  C CB  . LYS A 34  ? 1.1013 0.3492 0.7686 0.2144  -0.0540 -0.0313 58  LYS A CB  
211  C CG  . LYS A 34  ? 1.1416 0.3432 0.7892 0.1801  -0.0640 -0.0237 58  LYS A CG  
212  C CD  . LYS A 34  ? 1.2228 0.3603 0.8476 0.1837  -0.0705 -0.0193 58  LYS A CD  
213  C CE  . LYS A 34  ? 1.2484 0.3444 0.8549 0.1454  -0.0800 -0.0116 58  LYS A CE  
214  N NZ  . LYS A 34  ? 1.3377 0.3657 0.9189 0.1467  -0.0867 -0.0083 58  LYS A NZ  
215  N N   . GLU A 35  ? 1.0336 0.3288 0.6972 0.1918  -0.0441 -0.0677 59  GLU A N   
216  C CA  . GLU A 35  ? 1.0677 0.3537 0.7163 0.1673  -0.0471 -0.0805 59  GLU A CA  
217  C C   . GLU A 35  ? 1.0431 0.3799 0.7116 0.1533  -0.0452 -0.0773 59  GLU A C   
218  O O   . GLU A 35  ? 1.0381 0.3686 0.7022 0.1242  -0.0523 -0.0760 59  GLU A O   
219  C CB  . GLU A 35  ? 1.1119 0.3871 0.7429 0.1827  -0.0409 -0.1018 59  GLU A CB  
220  N N   . ILE A 36  ? 0.9705 0.3585 0.6616 0.1734  -0.0359 -0.0758 60  ILE A N   
221  C CA  . ILE A 36  ? 0.9736 0.4081 0.6831 0.1626  -0.0335 -0.0725 60  ILE A CA  
222  C C   . ILE A 36  ? 0.9262 0.3625 0.6462 0.1451  -0.0399 -0.0541 60  ILE A C   
223  O O   . ILE A 36  ? 0.8908 0.3387 0.6149 0.1231  -0.0429 -0.0519 60  ILE A O   
224  C CB  . ILE A 36  ? 0.9429 0.4307 0.6735 0.1876  -0.0221 -0.0746 60  ILE A CB  
225  C CG1 . ILE A 36  ? 0.9401 0.4330 0.6592 0.1971  -0.0145 -0.0930 60  ILE A CG1 
226  C CG2 . ILE A 36  ? 0.8667 0.4007 0.6190 0.1791  -0.0204 -0.0663 60  ILE A CG2 
227  C CD1 . ILE A 36  ? 0.9378 0.4873 0.6778 0.2160  -0.0024 -0.0948 60  ILE A CD1 
228  N N   . ARG A 37  ? 0.9370 0.3614 0.6604 0.1546  -0.0421 -0.0401 61  ARG A N   
229  C CA  . ARG A 37  ? 0.9614 0.3866 0.6912 0.1378  -0.0472 -0.0213 61  ARG A CA  
230  C C   . ARG A 37  ? 0.9527 0.3409 0.6670 0.1049  -0.0553 -0.0188 61  ARG A C   
231  O O   . ARG A 37  ? 0.8623 0.2644 0.5839 0.0827  -0.0571 -0.0098 61  ARG A O   
232  C CB  . ARG A 37  ? 0.9829 0.3998 0.7154 0.1545  -0.0491 -0.0064 61  ARG A CB  
233  C CG  . ARG A 37  ? 0.9665 0.4326 0.7211 0.1811  -0.0432 -0.0037 61  ARG A CG  
234  C CD  . ARG A 37  ? 0.9870 0.4503 0.7458 0.1946  -0.0477 0.0142  61  ARG A CD  
235  N NE  . ARG A 37  ? 1.0578 0.4877 0.8073 0.2136  -0.0491 0.0113  61  ARG A NE  
236  C CZ  . ARG A 37  ? 1.0976 0.4730 0.8265 0.2046  -0.0555 0.0166  61  ARG A CZ  
237  N NH1 . ARG A 37  ? 1.1638 0.5146 0.8804 0.1748  -0.0609 0.0256  61  ARG A NH1 
238  N NH2 . ARG A 37  ? 1.0747 0.4200 0.7955 0.2256  -0.0563 0.0134  61  ARG A NH2 
239  N N   . ASP A 38  ? 0.9636 0.3059 0.6571 0.1006  -0.0600 -0.0264 62  ASP A N   
240  C CA  . ASP A 38  ? 1.0049 0.3134 0.6845 0.0670  -0.0689 -0.0243 62  ASP A CA  
241  C C   . ASP A 38  ? 0.9792 0.3096 0.6630 0.0467  -0.0705 -0.0343 62  ASP A C   
242  O O   . ASP A 38  ? 0.9936 0.3284 0.6831 0.0169  -0.0756 -0.0252 62  ASP A O   
243  C CB  . ASP A 38  ? 1.0418 0.2957 0.6960 0.0689  -0.0739 -0.0330 62  ASP A CB  
244  C CG  . ASP A 38  ? 1.0916 0.3141 0.7395 0.0807  -0.0756 -0.0191 62  ASP A CG  
245  O OD1 . ASP A 38  ? 1.0636 0.3073 0.7258 0.0835  -0.0740 -0.0013 62  ASP A OD1 
246  O OD2 . ASP A 38  ? 1.1810 0.3562 0.8079 0.0874  -0.0788 -0.0259 62  ASP A OD2 
247  N N   . ALA A 39  ? 0.9844 0.3313 0.6663 0.0620  -0.0659 -0.0520 63  ALA A N   
248  C CA  . ALA A 39  ? 0.9177 0.2851 0.6016 0.0440  -0.0687 -0.0615 63  ALA A CA  
249  C C   . ALA A 39  ? 0.8985 0.3099 0.6063 0.0383  -0.0654 -0.0515 63  ALA A C   
250  O O   . ALA A 39  ? 0.9070 0.3298 0.6211 0.0123  -0.0712 -0.0496 63  ALA A O   
251  C CB  . ALA A 39  ? 0.9425 0.3174 0.6157 0.0626  -0.0635 -0.0812 63  ALA A CB  
252  N N   . ALA A 40  ? 0.8688 0.3076 0.5914 0.0617  -0.0566 -0.0446 64  ALA A N   
253  C CA  . ALA A 40  ? 0.8270 0.3212 0.5779 0.0562  -0.0512 -0.0337 64  ALA A CA  
254  C C   . ALA A 40  ? 0.8251 0.3217 0.5855 0.0313  -0.0543 -0.0152 64  ALA A C   
255  O O   . ALA A 40  ? 0.7659 0.3089 0.5494 0.0154  -0.0512 -0.0087 64  ALA A O   
256  C CB  . ALA A 40  ? 0.7521 0.2768 0.5162 0.0847  -0.0424 -0.0301 64  ALA A CB  
257  N N   . ALA A 41  ? 0.8346 0.2819 0.5768 0.0287  -0.0595 -0.0059 65  ALA A N   
258  C CA  . ALA A 41  ? 0.8411 0.2900 0.5895 0.0023  -0.0614 0.0128  65  ALA A CA  
259  C C   . ALA A 41  ? 0.8714 0.3209 0.6232 -0.0312 -0.0678 0.0107  65  ALA A C   
260  O O   . ALA A 41  ? 0.8505 0.3388 0.6238 -0.0529 -0.0648 0.0227  65  ALA A O   
261  C CB  . ALA A 41  ? 0.8921 0.2848 0.6174 0.0061  -0.0663 0.0248  65  ALA A CB  
262  N N   . SER A 42  ? 0.8827 0.2926 0.6137 -0.0351 -0.0765 -0.0051 66  SER A N   
263  C CA  . SER A 42  ? 0.8965 0.3087 0.6305 -0.0684 -0.0856 -0.0077 66  SER A CA  
264  C C   . SER A 42  ? 0.8291 0.3123 0.5944 -0.0720 -0.0810 -0.0107 66  SER A C   
265  O O   . SER A 42  ? 0.8351 0.3548 0.6237 -0.0971 -0.0822 -0.0004 66  SER A O   
266  C CB  . SER A 42  ? 0.9375 0.3017 0.6427 -0.0690 -0.0950 -0.0255 66  SER A CB  
267  N N   . THR A 43  ? 0.8035 0.3084 0.5707 -0.0464 -0.0752 -0.0234 67  THR A N   
268  C CA  . THR A 43  ? 0.7271 0.2946 0.5215 -0.0470 -0.0709 -0.0249 67  THR A CA  
269  C C   . THR A 43  ? 0.7418 0.3582 0.5664 -0.0500 -0.0612 -0.0083 67  THR A C   
270  O O   . THR A 43  ? 0.7030 0.3618 0.5519 -0.0658 -0.0609 -0.0027 67  THR A O   
271  C CB  . THR A 43  ? 0.7472 0.3250 0.5353 -0.0189 -0.0649 -0.0389 67  THR A CB  
272  O OG1 . THR A 43  ? 0.8036 0.3375 0.5606 -0.0163 -0.0725 -0.0558 67  THR A OG1 
273  C CG2 . THR A 43  ? 0.7074 0.3444 0.5209 -0.0193 -0.0608 -0.0387 67  THR A CG2 
274  N N   . ALA A 44  ? 0.7168 0.3287 0.5393 -0.0337 -0.0533 -0.0007 68  ALA A N   
275  C CA  . ALA A 44  ? 0.6780 0.3312 0.5222 -0.0358 -0.0438 0.0135  68  ALA A CA  
276  C C   . ALA A 44  ? 0.7017 0.3616 0.5560 -0.0647 -0.0451 0.0275  68  ALA A C   
277  O O   . ALA A 44  ? 0.7032 0.4112 0.5822 -0.0724 -0.0380 0.0345  68  ALA A O   
278  C CB  . ALA A 44  ? 0.6819 0.3222 0.5161 -0.0161 -0.0386 0.0199  68  ALA A CB  
279  N N   . ARG A 45  ? 0.7313 0.3435 0.5667 -0.0810 -0.0536 0.0319  69  ARG A N   
280  C CA  . ARG A 45  ? 0.7380 0.3590 0.5842 -0.1126 -0.0549 0.0468  69  ARG A CA  
281  C C   . ARG A 45  ? 0.7416 0.4053 0.6134 -0.1306 -0.0587 0.0430  69  ARG A C   
282  O O   . ARG A 45  ? 0.7229 0.4359 0.6224 -0.1435 -0.0515 0.0543  69  ARG A O   
283  C CB  . ARG A 45  ? 0.8097 0.3646 0.6279 -0.1296 -0.0654 0.0517  69  ARG A CB  
284  C CG  . ARG A 45  ? 0.8485 0.4140 0.6781 -0.1656 -0.0660 0.0697  69  ARG A CG  
285  C CD  . ARG A 45  ? 0.9498 0.4438 0.7487 -0.1850 -0.0769 0.0765  69  ARG A CD  
286  N NE  . ARG A 45  ? 1.0254 0.4735 0.7975 -0.1641 -0.0742 0.0830  69  ARG A NE  
287  C CZ  . ARG A 45  ? 1.0311 0.4798 0.8002 -0.1701 -0.0671 0.1038  69  ARG A CZ  
288  N NH1 . ARG A 45  ? 1.0096 0.5049 0.8011 -0.1956 -0.0590 0.1197  69  ARG A NH1 
289  N NH2 . ARG A 45  ? 1.0423 0.4489 0.7864 -0.1484 -0.0674 0.1089  69  ARG A NH2 
290  N N   . LYS A 46  ? 0.7294 0.3769 0.5917 -0.1297 -0.0697 0.0272  70  LYS A N   
291  C CA  . LYS A 46  ? 0.7115 0.3988 0.5961 -0.1457 -0.0765 0.0239  70  LYS A CA  
292  C C   . LYS A 46  ? 0.6685 0.4211 0.5847 -0.1310 -0.0652 0.0261  70  LYS A C   
293  O O   . LYS A 46  ? 0.6701 0.4709 0.6167 -0.1456 -0.0643 0.0344  70  LYS A O   
294  C CB  . LYS A 46  ? 0.7448 0.3998 0.6062 -0.1430 -0.0899 0.0051  70  LYS A CB  
295  N N   . LEU A 47  ? 0.6232 0.3783 0.5333 -0.1020 -0.0566 0.0191  71  LEU A N   
296  C CA  . LEU A 47  ? 0.6131 0.4209 0.5481 -0.0879 -0.0460 0.0209  71  LEU A CA  
297  C C   . LEU A 47  ? 0.6673 0.5071 0.6221 -0.0944 -0.0337 0.0361  71  LEU A C   
298  O O   . LEU A 47  ? 0.6304 0.5187 0.6132 -0.0961 -0.0280 0.0406  71  LEU A O   
299  C CB  . LEU A 47  ? 0.6197 0.4189 0.5414 -0.0596 -0.0397 0.0118  71  LEU A CB  
300  C CG  . LEU A 47  ? 0.5984 0.3749 0.5013 -0.0488 -0.0473 -0.0035 71  LEU A CG  
301  C CD1 . LEU A 47  ? 0.5703 0.3416 0.4630 -0.0231 -0.0390 -0.0088 71  LEU A CD1 
302  C CD2 . LEU A 47  ? 0.6159 0.4254 0.5339 -0.0530 -0.0528 -0.0074 71  LEU A CD2 
303  N N   . ILE A 48  ? 0.6292 0.4419 0.5682 -0.0962 -0.0290 0.0442  72  ILE A N   
304  C CA  . ILE A 48  ? 0.6213 0.4614 0.5724 -0.1020 -0.0160 0.0587  72  ILE A CA  
305  C C   . ILE A 48  ? 0.6233 0.4897 0.5963 -0.1305 -0.0170 0.0702  72  ILE A C   
306  O O   . ILE A 48  ? 0.6378 0.5520 0.6348 -0.1333 -0.0048 0.0789  72  ILE A O   
307  C CB  . ILE A 48  ? 0.6785 0.4798 0.6028 -0.0971 -0.0131 0.0658  72  ILE A CB  
308  C CG1 . ILE A 48  ? 0.6409 0.4366 0.5535 -0.0682 -0.0098 0.0564  72  ILE A CG1 
309  C CG2 . ILE A 48  ? 0.6556 0.4782 0.5856 -0.1099 -0.0011 0.0829  72  ILE A CG2 
310  C CD1 . ILE A 48  ? 0.6939 0.4490 0.5802 -0.0592 -0.0117 0.0611  72  ILE A CD1 
311  N N   . GLU A 49  ? 0.6418 0.4786 0.6071 -0.1523 -0.0311 0.0704  73  GLU A N   
312  C CA  . GLU A 49  ? 0.6722 0.5384 0.6615 -0.1832 -0.0340 0.0820  73  GLU A CA  
313  C C   . GLU A 49  ? 0.6326 0.5588 0.6578 -0.1813 -0.0348 0.0785  73  GLU A C   
314  O O   . GLU A 49  ? 0.6257 0.6045 0.6835 -0.1948 -0.0277 0.0904  73  GLU A O   
315  C CB  . GLU A 49  ? 0.6873 0.5020 0.6562 -0.2092 -0.0515 0.0816  73  GLU A CB  
316  C CG  . GLU A 49  ? 0.8162 0.5832 0.7592 -0.2212 -0.0491 0.0943  73  GLU A CG  
317  C CD  . GLU A 49  ? 0.8975 0.5967 0.8113 -0.2420 -0.0670 0.0910  73  GLU A CD  
318  O OE1 . GLU A 49  ? 0.9296 0.6124 0.8364 -0.2423 -0.0811 0.0752  73  GLU A OE1 
319  O OE2 . GLU A 49  ? 0.9404 0.5992 0.8345 -0.2578 -0.0672 0.1042  73  GLU A OE2 
320  N N   . ALA A 50  ? 0.6465 0.5678 0.6669 -0.1636 -0.0427 0.0633  74  ALA A N   
321  C CA  . ALA A 50  ? 0.6051 0.5813 0.6571 -0.1562 -0.0431 0.0613  74  ALA A CA  
322  C C   . ALA A 50  ? 0.6038 0.6206 0.6740 -0.1347 -0.0234 0.0655  74  ALA A C   
323  O O   . ALA A 50  ? 0.5894 0.6613 0.6942 -0.1353 -0.0177 0.0723  74  ALA A O   
324  C CB  . ALA A 50  ? 0.6131 0.5695 0.6495 -0.1421 -0.0555 0.0453  74  ALA A CB  
325  N N   . LEU A 51  ? 0.5965 0.5869 0.6435 -0.1152 -0.0133 0.0615  75  LEU A N   
326  C CA  . LEU A 51  ? 0.5582 0.5792 0.6153 -0.0954 0.0043  0.0631  75  LEU A CA  
327  C C   . LEU A 51  ? 0.6250 0.6820 0.7013 -0.1082 0.0183  0.0777  75  LEU A C   
328  O O   . LEU A 51  ? 0.6693 0.7742 0.7719 -0.0993 0.0298  0.0804  75  LEU A O   
329  C CB  . LEU A 51  ? 0.5804 0.5647 0.6067 -0.0768 0.0094  0.0565  75  LEU A CB  
330  C CG  . LEU A 51  ? 0.5840 0.5547 0.5998 -0.0560 0.0041  0.0427  75  LEU A CG  
331  C CD1 . LEU A 51  ? 0.5999 0.5395 0.5888 -0.0416 0.0083  0.0385  75  LEU A CD1 
332  C CD2 . LEU A 51  ? 0.5326 0.5424 0.5703 -0.0420 0.0104  0.0401  75  LEU A CD2 
333  N N   . ARG A 52  ? 0.6263 0.6602 0.6888 -0.1284 0.0184  0.0877  76  ARG A N   
334  C CA  . ARG A 52  ? 0.6394 0.7089 0.7186 -0.1437 0.0327  0.1035  76  ARG A CA  
335  C C   . ARG A 52  ? 0.6523 0.7692 0.7701 -0.1659 0.0283  0.1120  76  ARG A C   
336  O O   . ARG A 52  ? 0.7275 0.8887 0.8677 -0.1772 0.0424  0.1254  76  ARG A O   
337  C CB  . ARG A 52  ? 0.6396 0.6669 0.6893 -0.1601 0.0335  0.1141  76  ARG A CB  
338  C CG  . ARG A 52  ? 0.6351 0.6292 0.6518 -0.1382 0.0399  0.1094  76  ARG A CG  
339  C CD  . ARG A 52  ? 0.6781 0.6379 0.6674 -0.1526 0.0423  0.1236  76  ARG A CD  
340  N NE  . ARG A 52  ? 0.6483 0.5988 0.6135 -0.1325 0.0525  0.1227  76  ARG A NE  
341  C CZ  . ARG A 52  ? 0.6926 0.6127 0.6287 -0.1379 0.0546  0.1345  76  ARG A CZ  
342  N NH1 . ARG A 52  ? 0.7160 0.6054 0.6413 -0.1618 0.0476  0.1483  76  ARG A NH1 
343  N NH2 . ARG A 52  ? 0.6727 0.5910 0.5882 -0.1197 0.0627  0.1329  76  ARG A NH2 
344  N N   . GLY A 53  ? 0.6380 0.7498 0.7639 -0.1726 0.0091  0.1050  77  GLY A N   
345  C CA  . GLY A 53  ? 0.6941 0.8539 0.8580 -0.1956 0.0014  0.1136  77  GLY A CA  
346  C C   . GLY A 53  ? 0.7296 0.9606 0.9352 -0.1780 0.0129  0.1157  77  GLY A C   
347  O O   . GLY A 53  ? 0.7538 1.0418 0.9955 -0.1921 0.0214  0.1293  77  GLY A O   
348  N N   . LYS A 54  ? 0.7010 0.9297 0.9025 -0.1467 0.0137  0.1031  78  LYS A N   
349  C CA  . LYS A 54  ? 0.7434 1.0313 0.9816 -0.1262 0.0220  0.1040  78  LYS A CA  
350  C C   . LYS A 54  ? 0.8079 1.1041 1.0396 -0.1009 0.0471  0.1024  78  LYS A C   
351  O O   . LYS A 54  ? 0.8578 1.1444 1.0803 -0.0723 0.0514  0.0918  78  LYS A O   
352  C CB  . LYS A 54  ? 0.7635 1.0421 1.0003 -0.1098 0.0055  0.0926  78  LYS A CB  
353  N N   . HIS A 55  ? 0.8480 1.1605 1.0821 -0.1139 0.0636  0.1136  79  HIS A N   
354  C CA  . HIS A 55  ? 0.8466 1.1715 1.0728 -0.0940 0.0889  0.1132  79  HIS A CA  
355  C C   . HIS A 55  ? 0.9176 1.1880 1.1013 -0.0711 0.0901  0.0986  79  HIS A C   
356  O O   . HIS A 55  ? 0.9295 1.2025 1.1143 -0.0443 0.0933  0.0881  79  HIS A O   
357  C CB  . HIS A 55  ? 0.7552 1.1453 1.0224 -0.0736 0.1025  0.1146  79  HIS A CB  
358  N N   . GLY A 66  ? 0.8760 0.8084 0.7813 0.2119  0.1702  -0.0705 192 GLY A N   
359  C CA  . GLY A 66  ? 0.8439 0.7573 0.7430 0.1978  0.1543  -0.0659 192 GLY A CA  
360  C C   . GLY A 66  ? 0.8261 0.7419 0.7527 0.2057  0.1420  -0.0572 192 GLY A C   
361  O O   . GLY A 66  ? 0.7620 0.6663 0.6877 0.1907  0.1260  -0.0521 192 GLY A O   
362  N N   . GLU A 67  ? 0.7936 0.7288 0.7467 0.2246  0.1461  -0.0543 193 GLU A N   
363  C CA  . GLU A 67  ? 0.7375 0.6761 0.7157 0.2341  0.1335  -0.0449 193 GLU A CA  
364  C C   . GLU A 67  ? 0.6346 0.6023 0.6369 0.2208  0.1221  -0.0320 193 GLU A C   
365  O O   . GLU A 67  ? 0.6367 0.5946 0.6459 0.2190  0.1062  -0.0252 193 GLU A O   
366  C CB  . GLU A 67  ? 0.7391 0.7092 0.7490 0.2558  0.1408  -0.0416 193 GLU A CB  
367  N N   . GLN A 68  ? 0.6191 0.6215 0.6329 0.2039  0.1258  -0.0276 194 GLN A N   
368  C CA  . GLN A 68  ? 0.5817 0.6087 0.6170 0.1836  0.1106  -0.0162 194 GLN A CA  
369  C C   . GLN A 68  ? 0.5400 0.5304 0.5504 0.1660  0.0949  -0.0182 194 GLN A C   
370  O O   . GLN A 68  ? 0.4793 0.4803 0.5028 0.1539  0.0808  -0.0105 194 GLN A O   
371  C CB  . GLN A 68  ? 0.6002 0.6640 0.6484 0.1683  0.1181  -0.0112 194 GLN A CB  
372  C CG  . GLN A 68  ? 0.6188 0.6583 0.6323 0.1536  0.1227  -0.0179 194 GLN A CG  
373  C CD  . GLN A 68  ? 0.6932 0.7402 0.6940 0.1629  0.1442  -0.0240 194 GLN A CD  
374  O OE1 . GLN A 68  ? 0.7194 0.7552 0.7119 0.1848  0.1558  -0.0326 194 GLN A OE1 
375  N NE2 . GLN A 68  ? 0.6800 0.7434 0.6760 0.1467  0.1500  -0.0195 194 GLN A NE2 
376  N N   . PHE A 69  ? 0.5704 0.5194 0.5449 0.1641  0.0971  -0.0285 195 PHE A N   
377  C CA  . PHE A 69  ? 0.5614 0.4815 0.5146 0.1472  0.0839  -0.0299 195 PHE A CA  
378  C C   . PHE A 69  ? 0.5539 0.4398 0.4952 0.1537  0.0755  -0.0309 195 PHE A C   
379  O O   . PHE A 69  ? 0.5781 0.4453 0.5055 0.1393  0.0649  -0.0303 195 PHE A O   
380  C CB  . PHE A 69  ? 0.5781 0.4782 0.5003 0.1364  0.0887  -0.0388 195 PHE A CB  
381  C CG  . PHE A 69  ? 0.5662 0.4942 0.4942 0.1287  0.0963  -0.0361 195 PHE A CG  
382  C CD1 . PHE A 69  ? 0.5354 0.4846 0.4789 0.1140  0.0882  -0.0273 195 PHE A CD1 
383  C CD2 . PHE A 69  ? 0.6325 0.5623 0.5467 0.1359  0.1121  -0.0424 195 PHE A CD2 
384  C CE1 . PHE A 69  ? 0.5660 0.5358 0.5124 0.1056  0.0946  -0.0231 195 PHE A CE1 
385  C CE2 . PHE A 69  ? 0.6166 0.5714 0.5336 0.1272  0.1195  -0.0378 195 PHE A CE2 
386  C CZ  . PHE A 69  ? 0.5775 0.5513 0.5111 0.1115  0.1102  -0.0273 195 PHE A CZ  
387  N N   . VAL A 70  ? 0.5817 0.4595 0.5283 0.1752  0.0803  -0.0315 196 VAL A N   
388  C CA  . VAL A 70  ? 0.6288 0.4699 0.5628 0.1823  0.0719  -0.0302 196 VAL A CA  
389  C C   . VAL A 70  ? 0.5999 0.4667 0.5636 0.1900  0.0620  -0.0170 196 VAL A C   
390  O O   . VAL A 70  ? 0.6533 0.5548 0.6459 0.2057  0.0670  -0.0123 196 VAL A O   
391  C CB  . VAL A 70  ? 0.6983 0.5032 0.6126 0.2035  0.0825  -0.0399 196 VAL A CB  
392  C CG1 . VAL A 70  ? 0.7102 0.4684 0.6049 0.2035  0.0717  -0.0380 196 VAL A CG1 
393  C CG2 . VAL A 70  ? 0.7611 0.5503 0.6475 0.1953  0.0930  -0.0538 196 VAL A CG2 
394  N N   . THR A 71  ? 0.6108 0.4638 0.5673 0.1783  0.0479  -0.0103 197 THR A N   
395  C CA  A THR A 71  ? 0.6198 0.4939 0.5982 0.1839  0.0363  0.0024  197 THR A CA  
396  C CA  B THR A 71  ? 0.6146 0.4893 0.5935 0.1843  0.0365  0.0024  197 THR A CA  
397  C C   . THR A 71  ? 0.6364 0.4914 0.6166 0.2093  0.0356  0.0069  197 THR A C   
398  O O   . THR A 71  ? 0.6675 0.5522 0.6749 0.2227  0.0297  0.0171  197 THR A O   
399  C CB  A THR A 71  ? 0.5939 0.4580 0.5590 0.1638  0.0231  0.0076  197 THR A CB  
400  C CB  B THR A 71  ? 0.6014 0.4680 0.5687 0.1650  0.0227  0.0083  197 THR A CB  
401  O OG1 A THR A 71  ? 0.5676 0.4417 0.5271 0.1440  0.0254  0.0017  197 THR A OG1 
402  O OG1 B THR A 71  ? 0.5963 0.4158 0.5335 0.1615  0.0204  0.0072  197 THR A OG1 
403  C CG2 A THR A 71  ? 0.5643 0.4572 0.5498 0.1650  0.0104  0.0195  197 THR A CG2 
404  C CG2 B THR A 71  ? 0.5610 0.4451 0.5275 0.1442  0.0235  0.0039  197 THR A CG2 
405  N N   . GLY A 72  ? 0.6631 0.4678 0.6141 0.2159  0.0404  -0.0001 198 GLY A N   
406  C CA  . GLY A 72  ? 0.6791 0.4588 0.6283 0.2373  0.0393  0.0031  198 GLY A CA  
407  C C   . GLY A 72  ? 0.7020 0.4257 0.6145 0.2306  0.0430  -0.0076 198 GLY A C   
408  O O   . GLY A 72  ? 0.7287 0.4318 0.6166 0.2121  0.0453  -0.0159 198 GLY A O   
409  N N   . GLU A 73  ? 0.7199 0.4191 0.6291 0.2455  0.0427  -0.0070 199 GLU A N   
410  C CA  . GLU A 73  ? 0.7718 0.4146 0.6450 0.2389  0.0448  -0.0169 199 GLU A CA  
411  C C   . GLU A 73  ? 0.7874 0.3871 0.6360 0.2243  0.0316  -0.0077 199 GLU A C   
412  O O   . GLU A 73  ? 0.8254 0.3824 0.6417 0.2073  0.0311  -0.0149 199 GLU A O   
413  C CB  . GLU A 73  ? 0.7738 0.4042 0.6507 0.2621  0.0522  -0.0229 199 GLU A CB  
414  C CG  . GLU A 73  ? 0.8759 0.4483 0.7136 0.2552  0.0555  -0.0360 199 GLU A CG  
415  C CD  . GLU A 73  ? 0.9616 0.5197 0.8006 0.2801  0.0643  -0.0437 199 GLU A CD  
416  O OE1 . GLU A 73  ? 1.0012 0.6004 0.8645 0.2967  0.0760  -0.0485 199 GLU A OE1 
417  O OE2 . GLU A 73  ? 0.9544 0.4603 0.7701 0.2831  0.0598  -0.0447 199 GLU A OE2 
418  N N   . THR A 74  ? 0.7846 0.3962 0.6471 0.2289  0.0205  0.0087  200 THR A N   
419  C CA  . THR A 74  ? 0.7899 0.3647 0.6294 0.2149  0.0083  0.0205  200 THR A CA  
420  C C   . THR A 74  ? 0.7128 0.3165 0.5599 0.2038  -0.0003 0.0324  200 THR A C   
421  O O   . THR A 74  ? 0.7038 0.3558 0.5790 0.2128  0.0000  0.0346  200 THR A O   
422  C CB  . THR A 74  ? 0.7672 0.3229 0.6103 0.2322  0.0013  0.0316  200 THR A CB  
423  O OG1 . THR A 74  ? 0.7758 0.3804 0.6536 0.2489  -0.0042 0.0430  200 THR A OG1 
424  C CG2 . THR A 74  ? 0.8429 0.3730 0.6818 0.2492  0.0106  0.0194  200 THR A CG2 
425  N N   . ILE A 75  ? 0.7232 0.2970 0.5438 0.1830  -0.0080 0.0403  201 ILE A N   
426  C CA  . ILE A 75  ? 0.7325 0.3364 0.5582 0.1698  -0.0161 0.0514  201 ILE A CA  
427  C C   . ILE A 75  ? 0.7323 0.3600 0.5771 0.1888  -0.0265 0.0665  201 ILE A C   
428  O O   . ILE A 75  ? 0.7307 0.4078 0.5959 0.1833  -0.0311 0.0699  201 ILE A O   
429  C CB  . ILE A 75  ? 0.7103 0.2852 0.5063 0.1412  -0.0208 0.0579  201 ILE A CB  
430  C CG1 . ILE A 75  ? 0.6897 0.3106 0.4951 0.1229  -0.0250 0.0639  201 ILE A CG1 
431  C CG2 . ILE A 75  ? 0.8079 0.3330 0.5811 0.1465  -0.0290 0.0723  201 ILE A CG2 
432  C CD1 . ILE A 75  ? 0.6698 0.3332 0.4935 0.1134  -0.0172 0.0499  201 ILE A CD1 
433  N N   . ARG A 76  ? 0.7467 0.3532 0.5924 0.2047  -0.0304 0.0734  202 ARG A N   
434  C CA  . ARG A 76  ? 0.7233 0.3592 0.5916 0.2216  -0.0416 0.0881  202 ARG A CA  
435  C C   . ARG A 76  ? 0.7446 0.4372 0.6529 0.2384  -0.0379 0.0826  202 ARG A C   
436  O O   . ARG A 76  ? 0.7439 0.4779 0.6704 0.2405  -0.0480 0.0921  202 ARG A O   
437  C CB  . ARG A 76  ? 0.7739 0.3766 0.6384 0.2358  -0.0456 0.0959  202 ARG A CB  
438  N N   . GLU A 77  ? 0.7513 0.4481 0.6719 0.2480  -0.0235 0.0673  203 GLU A N   
439  C CA  . GLU A 77  ? 0.6916 0.4445 0.6495 0.2599  -0.0174 0.0622  203 GLU A CA  
440  C C   . GLU A 77  ? 0.7012 0.4846 0.6621 0.2442  -0.0176 0.0598  203 GLU A C   
441  O O   . GLU A 77  ? 0.6979 0.5348 0.6896 0.2443  -0.0226 0.0643  203 GLU A O   
442  C CB  . GLU A 77  ? 0.7309 0.4778 0.6936 0.2704  -0.0002 0.0459  203 GLU A CB  
443  N N   . ALA A 78  ? 0.6875 0.4477 0.6226 0.2196  -0.0126 0.0506  204 ALA A N   
444  C CA  . ALA A 78  ? 0.6690 0.4651 0.6118 0.1958  -0.0120 0.0453  204 ALA A CA  
445  C C   . ALA A 78  ? 0.6510 0.4700 0.5968 0.1843  -0.0268 0.0571  204 ALA A C   
446  O O   . ALA A 78  ? 0.6011 0.4621 0.5664 0.1761  -0.0297 0.0559  204 ALA A O   
447  C CB  . ALA A 78  ? 0.6606 0.4285 0.5762 0.1743  -0.0049 0.0347  204 ALA A CB  
448  N N   . LEU A 79  ? 0.6734 0.4625 0.5970 0.1829  -0.0366 0.0686  205 LEU A N   
449  C CA  . LEU A 79  ? 0.7022 0.5101 0.6221 0.1721  -0.0506 0.0797  205 LEU A CA  
450  C C   . LEU A 79  ? 0.6921 0.5425 0.6428 0.1869  -0.0615 0.0878  205 LEU A C   
451  O O   . LEU A 79  ? 0.6791 0.5632 0.6373 0.1744  -0.0699 0.0890  205 LEU A O   
452  C CB  . LEU A 79  ? 0.7090 0.4744 0.5963 0.1684  -0.0581 0.0925  205 LEU A CB  
453  C CG  . LEU A 79  ? 0.7048 0.4394 0.5625 0.1453  -0.0503 0.0873  205 LEU A CG  
454  C CD1 . LEU A 79  ? 0.7138 0.4013 0.5402 0.1425  -0.0562 0.1016  205 LEU A CD1 
455  C CD2 . LEU A 79  ? 0.6356 0.4011 0.4909 0.1231  -0.0495 0.0824  205 LEU A CD2 
456  N N   . LYS A 80  ? 0.7047 0.5549 0.6736 0.2135  -0.0617 0.0931  206 LYS A N   
457  C CA  . LYS A 80  ? 0.6935 0.5917 0.6973 0.2280  -0.0727 0.1023  206 LYS A CA  
458  C C   . LYS A 80  ? 0.6947 0.6437 0.7296 0.2190  -0.0667 0.0924  206 LYS A C   
459  O O   . LYS A 80  ? 0.6713 0.6632 0.7266 0.2126  -0.0792 0.0981  206 LYS A O   
460  C CB  . LYS A 80  ? 0.7563 0.6459 0.7762 0.2621  -0.0717 0.1097  206 LYS A CB  
461  N N   . ARG A 81  ? 0.6717 0.6147 0.7082 0.2166  -0.0488 0.0782  207 ARG A N   
462  C CA  . ARG A 81  ? 0.6486 0.6358 0.7125 0.2082  -0.0419 0.0705  207 ARG A CA  
463  C C   . ARG A 81  ? 0.6031 0.5960 0.6538 0.1790  -0.0457 0.0646  207 ARG A C   
464  O O   . ARG A 81  ? 0.6077 0.6330 0.6778 0.1687  -0.0425 0.0597  207 ARG A O   
465  C CB  . ARG A 81  ? 0.6757 0.6536 0.7428 0.2179  -0.0213 0.0585  207 ARG A CB  
466  C CG  . ARG A 81  ? 0.7371 0.7047 0.8142 0.2501  -0.0152 0.0617  207 ARG A CG  
467  C CD  . ARG A 81  ? 0.7721 0.7811 0.8833 0.2647  -0.0006 0.0571  207 ARG A CD  
468  N NE  . ARG A 81  ? 0.8211 0.8037 0.9130 0.2639  0.0190  0.0417  207 ARG A NE  
469  C CZ  . ARG A 81  ? 0.8602 0.8183 0.9443 0.2808  0.0314  0.0337  207 ARG A CZ  
470  N NH1 . ARG A 81  ? 0.8646 0.8207 0.9609 0.2993  0.0273  0.0391  207 ARG A NH1 
471  N NH2 . ARG A 81  ? 0.8378 0.7730 0.9001 0.2750  0.0470  0.0190  207 ARG A NH2 
472  N N   . SER A 82  ? 0.6707 0.6333 0.6890 0.1661  -0.0520 0.0658  208 SER A N   
473  C CA  . SER A 82  ? 0.5907 0.5549 0.5934 0.1422  -0.0538 0.0591  208 SER A CA  
474  C C   . SER A 82  ? 0.6000 0.5854 0.6019 0.1324  -0.0713 0.0658  208 SER A C   
475  O O   . SER A 82  ? 0.5745 0.5671 0.5690 0.1148  -0.0728 0.0587  208 SER A O   
476  C CB  . SER A 82  ? 0.6057 0.5290 0.5734 0.1330  -0.0480 0.0554  208 SER A CB  
477  O OG  . SER A 82  ? 0.5955 0.4963 0.5598 0.1390  -0.0339 0.0482  208 SER A OG  
478  N N   . LYS A 83  ? 0.6215 0.6151 0.6290 0.1440  -0.0853 0.0791  209 LYS A N   
479  C CA  . LYS A 83  ? 0.5803 0.5922 0.5816 0.1335  -0.1041 0.0856  209 LYS A CA  
480  C C   . LYS A 83  ? 0.5696 0.6203 0.5949 0.1206  -0.1090 0.0798  209 LYS A C   
481  O O   . LYS A 83  ? 0.6182 0.6706 0.6264 0.1025  -0.1180 0.0754  209 LYS A O   
482  C CB  . LYS A 83  ? 0.6283 0.6474 0.6364 0.1506  -0.1197 0.1028  209 LYS A CB  
483  N N   . GLU A 84  ? 0.5519 0.6315 0.6143 0.1290  -0.1021 0.0792  210 GLU A N   
484  C CA  . GLU A 84  ? 0.5463 0.6643 0.6343 0.1147  -0.1068 0.0762  210 GLU A CA  
485  C C   . GLU A 84  ? 0.5588 0.6585 0.6246 0.0924  -0.1014 0.0627  210 GLU A C   
486  O O   . GLU A 84  ? 0.5096 0.6183 0.5692 0.0745  -0.1142 0.0602  210 GLU A O   
487  C CB  . GLU A 84  ? 0.5336 0.6829 0.6622 0.1273  -0.0942 0.0775  210 GLU A CB  
488  N N   . LEU A 85  ? 0.5248 0.5975 0.5776 0.0938  -0.0833 0.0537  211 LEU A N   
489  C CA  . LEU A 85  ? 0.5109 0.5672 0.5450 0.0764  -0.0782 0.0421  211 LEU A CA  
490  C C   . LEU A 85  ? 0.5266 0.5549 0.5227 0.0688  -0.0838 0.0384  211 LEU A C   
491  O O   . LEU A 85  ? 0.5048 0.5243 0.4848 0.0547  -0.0855 0.0297  211 LEU A O   
492  C CB  . LEU A 85  ? 0.5248 0.5670 0.5595 0.0803  -0.0587 0.0349  211 LEU A CB  
493  C CG  . LEU A 85  ? 0.4976 0.5692 0.5658 0.0840  -0.0507 0.0368  211 LEU A CG  
494  C CD1 . LEU A 85  ? 0.5282 0.5832 0.5905 0.0878  -0.0323 0.0297  211 LEU A CD1 
495  C CD2 . LEU A 85  ? 0.5165 0.6127 0.5997 0.0658  -0.0593 0.0370  211 LEU A CD2 
496  N N   . GLU A 86  ? 0.4793 0.4923 0.4591 0.0782  -0.0861 0.0451  212 GLU A N   
497  C CA  . GLU A 86  ? 0.5733 0.5631 0.5160 0.0702  -0.0888 0.0423  212 GLU A CA  
498  C C   . GLU A 86  ? 0.5563 0.5564 0.4870 0.0580  -0.1054 0.0412  212 GLU A C   
499  O O   . GLU A 86  ? 0.6385 0.6232 0.5415 0.0476  -0.1041 0.0319  212 GLU A O   
500  C CB  . GLU A 86  ? 0.6106 0.5814 0.5369 0.0801  -0.0886 0.0524  212 GLU A CB  
501  C CG  . GLU A 86  ? 0.6311 0.5800 0.5550 0.0855  -0.0717 0.0492  212 GLU A CG  
502  C CD  . GLU A 86  ? 0.7039 0.6276 0.6081 0.0914  -0.0717 0.0592  212 GLU A CD  
503  O OE1 . GLU A 86  ? 0.6968 0.6222 0.5998 0.0992  -0.0841 0.0715  212 GLU A OE1 
504  O OE2 . GLU A 86  ? 0.7039 0.6059 0.5937 0.0872  -0.0601 0.0556  212 GLU A OE2 
505  N N   . GLU A 87  ? 0.6102 0.6372 0.5612 0.0592  -0.1211 0.0498  213 GLU A N   
506  C CA  . GLU A 87  ? 0.6191 0.6560 0.5570 0.0450  -0.1398 0.0484  213 GLU A CA  
507  C C   . GLU A 87  ? 0.6085 0.6529 0.5562 0.0290  -0.1407 0.0373  213 GLU A C   
508  O O   . GLU A 87  ? 0.6923 0.7395 0.6260 0.0141  -0.1565 0.0334  213 GLU A O   
509  C CB  . GLU A 87  ? 0.6351 0.7015 0.5915 0.0509  -0.1594 0.0636  213 GLU A CB  
510  C CG  . GLU A 87  ? 0.7061 0.7610 0.6512 0.0677  -0.1612 0.0773  213 GLU A CG  
511  C CD  . GLU A 87  ? 0.8035 0.8308 0.6990 0.0609  -0.1658 0.0773  213 GLU A CD  
512  O OE1 . GLU A 87  ? 0.8210 0.8395 0.6896 0.0450  -0.1681 0.0654  213 GLU A OE1 
513  O OE2 . GLU A 87  ? 0.8011 0.8138 0.6828 0.0719  -0.1664 0.0896  213 GLU A OE2 
514  N N   . LYS A 88  ? 0.5841 0.6289 0.5524 0.0305  -0.1252 0.0325  214 LYS A N   
515  C CA  . LYS A 88  ? 0.5956 0.6374 0.5659 0.0147  -0.1243 0.0224  214 LYS A CA  
516  C C   . LYS A 88  ? 0.6038 0.6089 0.5413 0.0118  -0.1128 0.0090  214 LYS A C   
517  O O   . LYS A 88  ? 0.6440 0.6374 0.5760 0.0001  -0.1125 0.0000  214 LYS A O   
518  C CB  . LYS A 88  ? 0.5418 0.6056 0.5506 0.0165  -0.1143 0.0258  214 LYS A CB  
519  C CG  . LYS A 88  ? 0.6157 0.7237 0.6620 0.0117  -0.1272 0.0364  214 LYS A CG  
520  C CD  . LYS A 88  ? 0.6710 0.8018 0.7525 0.0122  -0.1137 0.0392  214 LYS A CD  
521  C CE  . LYS A 88  ? 0.6568 0.8389 0.7795 0.0055  -0.1254 0.0502  214 LYS A CE  
522  N NZ  . LYS A 88  ? 0.6382 0.8470 0.7953 0.0070  -0.1095 0.0542  214 LYS A NZ  
523  N N   . GLY A 89  ? 0.6104 0.5977 0.5266 0.0223  -0.1035 0.0085  215 GLY A N   
524  C CA  . GLY A 89  ? 0.6439 0.6039 0.5330 0.0220  -0.0918 -0.0028 215 GLY A CA  
525  C C   . GLY A 89  ? 0.5849 0.5390 0.4824 0.0322  -0.0738 -0.0024 215 GLY A C   
526  O O   . GLY A 89  ? 0.6236 0.5610 0.5030 0.0336  -0.0637 -0.0100 215 GLY A O   
527  N N   . PHE A 90  ? 0.5090 0.4768 0.4327 0.0399  -0.0696 0.0058  216 PHE A N   
528  C CA  . PHE A 90  ? 0.5090 0.4686 0.4367 0.0479  -0.0544 0.0055  216 PHE A CA  
529  C C   . PHE A 90  ? 0.5382 0.4868 0.4489 0.0538  -0.0519 0.0106  216 PHE A C   
530  O O   . PHE A 90  ? 0.5464 0.4976 0.4506 0.0557  -0.0616 0.0184  216 PHE A O   
531  C CB  . PHE A 90  ? 0.4781 0.4530 0.4355 0.0544  -0.0499 0.0107  216 PHE A CB  
532  C CG  . PHE A 90  ? 0.5123 0.4978 0.4866 0.0473  -0.0480 0.0073  216 PHE A CG  
533  C CD1 . PHE A 90  ? 0.4367 0.4115 0.4086 0.0463  -0.0364 0.0017  216 PHE A CD1 
534  C CD2 . PHE A 90  ? 0.4769 0.4845 0.4698 0.0403  -0.0586 0.0113  216 PHE A CD2 
535  C CE1 . PHE A 90  ? 0.4441 0.4261 0.4291 0.0389  -0.0345 0.0009  216 PHE A CE1 
536  C CE2 . PHE A 90  ? 0.4667 0.4838 0.4749 0.0309  -0.0564 0.0101  216 PHE A CE2 
537  C CZ  . PHE A 90  ? 0.4439 0.4462 0.4468 0.0303  -0.0439 0.0052  216 PHE A CZ  
538  N N   . SER A 91  ? 0.4934 0.4301 0.3966 0.0554  -0.0397 0.0076  217 SER A N   
539  C CA  . SER A 91  ? 0.4713 0.3967 0.3630 0.0586  -0.0359 0.0140  217 SER A CA  
540  C C   . SER A 91  ? 0.4460 0.3658 0.3512 0.0639  -0.0269 0.0143  217 SER A C   
541  O O   . SER A 91  ? 0.4454 0.3722 0.3666 0.0652  -0.0226 0.0094  217 SER A O   
542  C CB  . SER A 91  ? 0.4909 0.4092 0.3589 0.0528  -0.0301 0.0106  217 SER A CB  
543  O OG  . SER A 91  ? 0.5148 0.4343 0.3877 0.0515  -0.0206 0.0021  217 SER A OG  
544  N N   . TYR A 92  ? 0.4581 0.3625 0.3535 0.0654  -0.0239 0.0199  218 TYR A N   
545  C CA  . TYR A 92  ? 0.4330 0.3261 0.3352 0.0696  -0.0164 0.0186  218 TYR A CA  
546  C C   . TYR A 92  ? 0.4390 0.3175 0.3254 0.0611  -0.0099 0.0180  218 TYR A C   
547  O O   . TYR A 92  ? 0.4720 0.3467 0.3423 0.0541  -0.0110 0.0228  218 TYR A O   
548  C CB  . TYR A 92  ? 0.4799 0.3633 0.3881 0.0815  -0.0201 0.0260  218 TYR A CB  
549  C CG  . TYR A 92  ? 0.4933 0.3982 0.4258 0.0909  -0.0235 0.0261  218 TYR A CG  
550  C CD1 . TYR A 92  ? 0.4970 0.4208 0.4365 0.0909  -0.0349 0.0312  218 TYR A CD1 
551  C CD2 . TYR A 92  ? 0.4403 0.3489 0.3884 0.0987  -0.0153 0.0215  218 TYR A CD2 
552  C CE1 . TYR A 92  ? 0.4601 0.4092 0.4254 0.0967  -0.0386 0.0325  218 TYR A CE1 
553  C CE2 . TYR A 92  ? 0.4285 0.3628 0.4016 0.1061  -0.0165 0.0229  218 TYR A CE2 
554  C CZ  . TYR A 92  ? 0.4929 0.4491 0.4769 0.1045  -0.0285 0.0290  218 TYR A CZ  
555  O OH  . TYR A 92  ? 0.5170 0.5042 0.5297 0.1095  -0.0304 0.0316  218 TYR A OH  
556  N N   . SER A 93  ? 0.4224 0.2946 0.3130 0.0606  -0.0033 0.0126  219 SER A N   
557  C CA  . SER A 93  ? 0.4739 0.3302 0.3517 0.0516  0.0008  0.0129  219 SER A CA  
558  C C   . SER A 93  ? 0.4932 0.3264 0.3700 0.0582  0.0027  0.0113  219 SER A C   
559  O O   . SER A 93  ? 0.4749 0.3127 0.3608 0.0636  0.0069  0.0042  219 SER A O   
560  C CB  . SER A 93  ? 0.4664 0.3379 0.3467 0.0431  0.0058  0.0064  219 SER A CB  
561  O OG  . SER A 93  ? 0.4906 0.3512 0.3607 0.0318  0.0080  0.0078  219 SER A OG  
562  N N   . TYR A 94  ? 0.4656 0.2714 0.3286 0.0582  0.0001  0.0179  220 TYR A N   
563  C CA  . TYR A 94  ? 0.5309 0.3080 0.3892 0.0678  0.0019  0.0155  220 TYR A CA  
564  C C   . TYR A 94  ? 0.5615 0.3173 0.4046 0.0548  0.0056  0.0093  220 TYR A C   
565  O O   . TYR A 94  ? 0.5575 0.3111 0.3902 0.0374  0.0042  0.0129  220 TYR A O   
566  C CB  . TYR A 94  ? 0.5608 0.3119 0.4094 0.0762  -0.0040 0.0263  220 TYR A CB  
567  C CG  . TYR A 94  ? 0.5427 0.3174 0.4072 0.0892  -0.0099 0.0327  220 TYR A CG  
568  C CD1 . TYR A 94  ? 0.5396 0.3250 0.4233 0.1080  -0.0089 0.0304  220 TYR A CD1 
569  C CD2 . TYR A 94  ? 0.5147 0.3044 0.3750 0.0818  -0.0164 0.0408  220 TYR A CD2 
570  C CE1 . TYR A 94  ? 0.5257 0.3379 0.4269 0.1173  -0.0161 0.0369  220 TYR A CE1 
571  C CE2 . TYR A 94  ? 0.5334 0.3448 0.4061 0.0913  -0.0242 0.0460  220 TYR A CE2 
572  C CZ  . TYR A 94  ? 0.5807 0.4046 0.4755 0.1081  -0.0249 0.0444  220 TYR A CZ  
573  O OH  . TYR A 94  ? 0.5406 0.3906 0.4505 0.1153  -0.0346 0.0506  220 TYR A OH  
574  N N   . ASP A 95  ? 0.5712 0.3122 0.4119 0.0625  0.0101  0.0002  221 ASP A N   
575  C CA  . ASP A 95  ? 0.5803 0.2965 0.4022 0.0496  0.0116  -0.0069 221 ASP A CA  
576  C C   . ASP A 95  ? 0.6187 0.2903 0.4241 0.0621  0.0135  -0.0113 221 ASP A C   
577  O O   . ASP A 95  ? 0.6471 0.3213 0.4598 0.0810  0.0194  -0.0176 221 ASP A O   
578  C CB  . ASP A 95  ? 0.5667 0.3080 0.3957 0.0450  0.0155  -0.0162 221 ASP A CB  
579  C CG  . ASP A 95  ? 0.6907 0.4102 0.4994 0.0298  0.0146  -0.0237 221 ASP A CG  
580  O OD1 . ASP A 95  ? 0.7079 0.3924 0.4974 0.0197  0.0109  -0.0219 221 ASP A OD1 
581  O OD2 . ASP A 95  ? 0.6517 0.3877 0.4622 0.0269  0.0166  -0.0309 221 ASP A OD2 
582  N N   . MET A 96  ? 0.7178 0.3481 0.5006 0.0523  0.0090  -0.0073 222 MET A N   
583  C CA  . MET A 96  ? 0.7566 0.3341 0.5165 0.0619  0.0106  -0.0139 222 MET A CA  
584  C C   . MET A 96  ? 0.7909 0.3607 0.5371 0.0532  0.0145  -0.0293 222 MET A C   
585  O O   . MET A 96  ? 0.8870 0.4368 0.6139 0.0295  0.0096  -0.0316 222 MET A O   
586  C CB  . MET A 96  ? 0.8482 0.3781 0.5836 0.0491  0.0035  -0.0050 222 MET A CB  
587  C CG  . MET A 96  ? 0.8205 0.3546 0.5638 0.0570  -0.0013 0.0115  222 MET A CG  
588  S SD  . MET A 96  ? 0.9309 0.4784 0.6958 0.0952  0.0015  0.0129  222 MET A SD  
589  C CE  . MET A 96  ? 0.7978 0.2846 0.5394 0.1136  0.0065  0.0009  222 MET A CE  
590  N N   . LEU A 97  ? 0.7588 0.3474 0.5149 0.0703  0.0227  -0.0387 223 LEU A N   
591  C CA  . LEU A 97  ? 0.8180 0.4124 0.5636 0.0618  0.0263  -0.0516 223 LEU A CA  
592  C C   . LEU A 97  ? 0.8851 0.4247 0.5927 0.0495  0.0235  -0.0622 223 LEU A C   
593  O O   . LEU A 97  ? 0.9436 0.4367 0.6308 0.0650  0.0274  -0.0690 223 LEU A O   
594  C CB  . LEU A 97  ? 0.8734 0.4892 0.6309 0.0846  0.0376  -0.0588 223 LEU A CB  
595  N N   . GLY A 98  ? 0.9114 0.4559 0.6098 0.0217  0.0159  -0.0630 224 GLY A N   
596  C CA  . GLY A 98  ? 0.8886 0.3892 0.5508 0.0050  0.0115  -0.0751 224 GLY A CA  
597  C C   . GLY A 98  ? 0.8597 0.3962 0.5262 -0.0201 0.0044  -0.0756 224 GLY A C   
598  O O   . GLY A 98  ? 0.8265 0.4111 0.5215 -0.0282 0.0015  -0.0641 224 GLY A O   
599  N N   . GLU A 99  ? 0.8949 0.4083 0.5322 -0.0313 0.0014  -0.0892 225 GLU A N   
600  C CA  . GLU A 99  ? 0.8368 0.3858 0.4780 -0.0548 -0.0076 -0.0889 225 GLU A CA  
601  C C   . GLU A 99  ? 0.8843 0.3910 0.4831 -0.0709 -0.0142 -0.1045 225 GLU A C   
602  O O   . GLU A 99  ? 0.9172 0.3788 0.4894 -0.0572 -0.0081 -0.1160 225 GLU A O   
603  C CB  . GLU A 99  ? 0.7984 0.4031 0.4651 -0.0412 -0.0019 -0.0865 225 GLU A CB  
604  C CG  . GLU A 99  ? 0.8240 0.4182 0.4764 -0.0187 0.0096  -0.0982 225 GLU A CG  
605  C CD  . GLU A 99  ? 0.8032 0.4505 0.4802 -0.0096 0.0140  -0.0930 225 GLU A CD  
606  O OE1 . GLU A 99  ? 0.7982 0.4707 0.5041 0.0068  0.0211  -0.0846 225 GLU A OE1 
607  O OE2 . GLU A 99  ? 0.8055 0.4680 0.4715 -0.0201 0.0091  -0.0965 225 GLU A OE2 
608  N N   . ALA A 100 ? 0.9041 0.4348 0.5025 -0.0988 -0.0270 -0.1028 226 ALA A N   
609  C CA  . ALA A 100 ? 0.8705 0.3693 0.4289 -0.1190 -0.0369 -0.1171 226 ALA A CA  
610  C C   . ALA A 100 ? 0.9861 0.4291 0.5216 -0.1212 -0.0372 -0.1211 226 ALA A C   
611  O O   . ALA A 100 ? 1.0155 0.4303 0.5269 -0.1104 -0.0329 -0.1330 226 ALA A O   
612  C CB  . ALA A 100 ? 0.9676 0.4779 0.5133 -0.1013 -0.0297 -0.1280 226 ALA A CB  
613  N N   . ALA A 101 ? 0.9729 0.4007 0.5161 -0.1344 -0.0416 -0.1101 227 ALA A N   
614  C CA  . ALA A 101 ? 1.0350 0.4108 0.5562 -0.1404 -0.0444 -0.1113 227 ALA A CA  
615  C C   . ALA A 101 ? 1.1121 0.4761 0.6080 -0.1665 -0.0566 -0.1199 227 ALA A C   
616  O O   . ALA A 101 ? 1.1040 0.5031 0.6086 -0.1950 -0.0690 -0.1153 227 ALA A O   
617  C CB  . ALA A 101 ? 1.0484 0.4169 0.5821 -0.1564 -0.0489 -0.0950 227 ALA A CB  
618  N N   . THR A 102 ? 1.1450 0.4628 0.6108 -0.1560 -0.0534 -0.1325 228 THR A N   
619  C CA  . THR A 102 ? 1.1799 0.4801 0.6167 -0.1790 -0.0648 -0.1424 228 THR A CA  
620  C C   . THR A 102 ? 1.2218 0.4735 0.6382 -0.2007 -0.0740 -0.1400 228 THR A C   
621  O O   . THR A 102 ? 1.2870 0.5290 0.6833 -0.2285 -0.0870 -0.1446 228 THR A O   
622  C CB  . THR A 102 ? 1.2281 0.5095 0.6396 -0.1553 -0.0555 -0.1603 228 THR A CB  
623  O OG1 . THR A 102 ? 1.2838 0.5191 0.6839 -0.1282 -0.0434 -0.1656 228 THR A OG1 
624  C CG2 . THR A 102 ? 1.1328 0.4637 0.5635 -0.1355 -0.0463 -0.1612 228 THR A CG2 
625  N N   . THR A 103 ? 1.2265 0.4484 0.6472 -0.1892 -0.0681 -0.1321 229 THR A N   
626  C CA  . THR A 103 ? 1.2937 0.4652 0.6937 -0.2073 -0.0758 -0.1284 229 THR A CA  
627  C C   . THR A 103 ? 1.2924 0.4783 0.7172 -0.2200 -0.0781 -0.1077 229 THR A C   
628  O O   . THR A 103 ? 1.2248 0.4458 0.6788 -0.2046 -0.0704 -0.0985 229 THR A O   
629  C CB  . THR A 103 ? 1.3770 0.4875 0.7511 -0.1782 -0.0664 -0.1393 229 THR A CB  
630  N N   . ALA A 104 ? 1.2989 0.4568 0.7103 -0.2496 -0.0887 -0.1001 230 ALA A N   
631  C CA  . ALA A 104 ? 1.2974 0.4633 0.7277 -0.2620 -0.0898 -0.0797 230 ALA A CA  
632  C C   . ALA A 104 ? 1.3181 0.4536 0.7501 -0.2268 -0.0782 -0.0756 230 ALA A C   
633  O O   . ALA A 104 ? 1.2633 0.4248 0.7205 -0.2215 -0.0738 -0.0602 230 ALA A O   
634  C CB  . ALA A 104 ? 1.3437 0.4814 0.7559 -0.3000 -0.1028 -0.0727 230 ALA A CB  
635  N N   . ALA A 105 ? 1.3419 0.4245 0.7479 -0.2018 -0.0731 -0.0889 231 ALA A N   
636  C CA  . ALA A 105 ? 1.3334 0.3919 0.7441 -0.1655 -0.0627 -0.0852 231 ALA A CA  
637  C C   . ALA A 105 ? 1.2802 0.3870 0.7220 -0.1350 -0.0510 -0.0847 231 ALA A C   
638  O O   . ALA A 105 ? 1.2498 0.3631 0.7103 -0.1153 -0.0454 -0.0727 231 ALA A O   
639  C CB  . ALA A 105 ? 1.4209 0.4176 0.7993 -0.1447 -0.0593 -0.1009 231 ALA A CB  
640  N N   . ASP A 106 ? 1.2562 0.3975 0.7033 -0.1312 -0.0478 -0.0969 232 ASP A N   
641  C CA  . ASP A 106 ? 1.2129 0.4019 0.6895 -0.1057 -0.0373 -0.0957 232 ASP A CA  
642  C C   . ASP A 106 ? 1.1320 0.3643 0.6368 -0.1218 -0.0406 -0.0784 232 ASP A C   
643  O O   . ASP A 106 ? 1.0952 0.3473 0.6227 -0.1003 -0.0333 -0.0696 232 ASP A O   
644  C CB  . ASP A 106 ? 1.2245 0.4398 0.6977 -0.1013 -0.0340 -0.1115 232 ASP A CB  
645  C CG  . ASP A 106 ? 1.3123 0.4863 0.7541 -0.0888 -0.0305 -0.1295 232 ASP A CG  
646  O OD1 . ASP A 106 ? 1.4034 0.5244 0.8211 -0.0936 -0.0347 -0.1312 232 ASP A OD1 
647  O OD2 . ASP A 106 ? 1.3283 0.5224 0.7684 -0.0744 -0.0232 -0.1418 232 ASP A OD2 
648  N N   . ALA A 107 ? 1.1157 0.3661 0.6207 -0.1599 -0.0516 -0.0730 233 ALA A N   
649  C CA  . ALA A 107 ? 1.1133 0.4077 0.6458 -0.1771 -0.0538 -0.0563 233 ALA A CA  
650  C C   . ALA A 107 ? 1.1285 0.4034 0.6650 -0.1746 -0.0523 -0.0390 233 ALA A C   
651  O O   . ALA A 107 ? 1.0895 0.3955 0.6489 -0.1700 -0.0482 -0.0261 233 ALA A O   
652  C CB  . ALA A 107 ? 1.1319 0.4549 0.6670 -0.2192 -0.0658 -0.0529 233 ALA A CB  
653  N N   . GLU A 108 ? 1.1634 0.3854 0.6759 -0.1768 -0.0558 -0.0382 234 GLU A N   
654  C CA  . GLU A 108 ? 1.1639 0.3646 0.6775 -0.1729 -0.0552 -0.0211 234 GLU A CA  
655  C C   . GLU A 108 ? 1.1632 0.3625 0.6888 -0.1303 -0.0454 -0.0202 234 GLU A C   
656  O O   . GLU A 108 ? 1.1235 0.3411 0.6658 -0.1243 -0.0432 -0.0041 234 GLU A O   
657  C CB  . GLU A 108 ? 1.2156 0.3564 0.6986 -0.1860 -0.0622 -0.0211 234 GLU A CB  
658  N N   . ARG A 109 ? 1.1686 0.3511 0.6873 -0.1006 -0.0393 -0.0366 235 ARG A N   
659  C CA  . ARG A 109 ? 1.1432 0.3315 0.6780 -0.0600 -0.0301 -0.0354 235 ARG A CA  
660  C C   . ARG A 109 ? 1.0751 0.3198 0.6402 -0.0515 -0.0251 -0.0295 235 ARG A C   
661  O O   . ARG A 109 ? 1.0497 0.3073 0.6320 -0.0329 -0.0225 -0.0171 235 ARG A O   
662  C CB  . ARG A 109 ? 1.2050 0.3740 0.7296 -0.0324 -0.0228 -0.0545 235 ARG A CB  
663  N N   . TYR A 110 ? 1.0424 0.3208 0.6137 -0.0645 -0.0245 -0.0381 236 TYR A N   
664  C CA  . TYR A 110 ? 1.0135 0.3413 0.6112 -0.0589 -0.0203 -0.0327 236 TYR A CA  
665  C C   . TYR A 110 ? 0.9783 0.3191 0.5853 -0.0778 -0.0246 -0.0121 236 TYR A C   
666  O O   . TYR A 110 ? 0.9679 0.3343 0.5943 -0.0610 -0.0207 -0.0019 236 TYR A O   
667  C CB  . TYR A 110 ? 0.9768 0.3351 0.5768 -0.0735 -0.0207 -0.0447 236 TYR A CB  
668  C CG  . TYR A 110 ? 0.9858 0.3425 0.5789 -0.0517 -0.0140 -0.0633 236 TYR A CG  
669  C CD1 . TYR A 110 ? 0.9776 0.3413 0.5837 -0.0148 -0.0034 -0.0663 236 TYR A CD1 
670  C CD2 . TYR A 110 ? 1.0020 0.3555 0.5771 -0.0695 -0.0184 -0.0763 236 TYR A CD2 
671  C CE1 . TYR A 110 ? 1.0073 0.3747 0.6083 0.0035  0.0047  -0.0818 236 TYR A CE1 
672  C CE2 . TYR A 110 ? 1.0496 0.4027 0.6157 -0.0507 -0.0114 -0.0921 236 TYR A CE2 
673  C CZ  . TYR A 110 ? 1.0484 0.4088 0.6276 -0.0144 0.0012  -0.0946 236 TYR A CZ  
674  O OH  . TYR A 110 ? 1.0435 0.4074 0.6146 0.0025  0.0097  -0.1090 236 TYR A OH  
675  N N   . TYR A 111 ? 0.9882 0.3183 0.5834 -0.1128 -0.0324 -0.0049 237 TYR A N   
676  C CA  . TYR A 111 ? 1.0090 0.3565 0.6126 -0.1329 -0.0345 0.0162  237 TYR A CA  
677  C C   . TYR A 111 ? 0.9933 0.3197 0.5955 -0.1104 -0.0330 0.0294  237 TYR A C   
678  O O   . TYR A 111 ? 0.9706 0.3240 0.5870 -0.1032 -0.0301 0.0428  237 TYR A O   
679  C CB  . TYR A 111 ? 1.0165 0.3576 0.6089 -0.1735 -0.0425 0.0220  237 TYR A CB  
680  C CG  . TYR A 111 ? 1.0078 0.3695 0.6083 -0.1942 -0.0425 0.0449  237 TYR A CG  
681  C CD1 . TYR A 111 ? 1.0242 0.4496 0.6501 -0.2102 -0.0388 0.0539  237 TYR A CD1 
682  C CD2 . TYR A 111 ? 1.1133 0.4389 0.6987 -0.1952 -0.0451 0.0575  237 TYR A CD2 
683  C CE1 . TYR A 111 ? 1.0203 0.4707 0.6532 -0.2279 -0.0363 0.0749  237 TYR A CE1 
684  C CE2 . TYR A 111 ? 1.1159 0.4632 0.7068 -0.2139 -0.0440 0.0788  237 TYR A CE2 
685  C CZ  . TYR A 111 ? 1.0620 0.4712 0.6753 -0.2307 -0.0389 0.0874  237 TYR A CZ  
686  O OH  . TYR A 111 ? 1.1100 0.5458 0.7281 -0.2478 -0.0355 0.1081  237 TYR A OH  
687  N N   . ARG A 112 ? 1.0450 0.3236 0.6293 -0.0986 -0.0354 0.0260  238 ARG A N   
688  C CA  . ARG A 112 ? 1.0435 0.3026 0.6277 -0.0758 -0.0355 0.0387  238 ARG A CA  
689  C C   . ARG A 112 ? 1.0369 0.3229 0.6428 -0.0386 -0.0295 0.0365  238 ARG A C   
690  O O   . ARG A 112 ? 1.0179 0.3106 0.6321 -0.0237 -0.0306 0.0511  238 ARG A O   
691  C CB  . ARG A 112 ? 1.0958 0.2972 0.6575 -0.0686 -0.0389 0.0337  238 ARG A CB  
692  N N   . ASP A 113 ? 0.9780 0.2836 0.5941 -0.0245 -0.0237 0.0192  239 ASP A N   
693  C CA  . ASP A 113 ? 0.9836 0.3229 0.6239 0.0074  -0.0178 0.0180  239 ASP A CA  
694  C C   . ASP A 113 ? 0.9203 0.3056 0.5779 -0.0014 -0.0175 0.0290  239 ASP A C   
695  O O   . ASP A 113 ? 0.9121 0.3252 0.5883 0.0182  -0.0172 0.0381  239 ASP A O   
696  C CB  . ASP A 113 ? 1.0129 0.3635 0.6593 0.0240  -0.0102 -0.0027 239 ASP A CB  
697  C CG  . ASP A 113 ? 1.1007 0.4287 0.7462 0.0533  -0.0063 -0.0101 239 ASP A CG  
698  O OD1 . ASP A 113 ? 1.1038 0.3861 0.7268 0.0471  -0.0098 -0.0119 239 ASP A OD1 
699  O OD2 . ASP A 113 ? 1.1564 0.5134 0.8246 0.0819  0.0004  -0.0134 239 ASP A OD2 
700  N N   . TYR A 114 ? 0.9073 0.3262 0.5710 -0.0300 -0.0175 0.0268  240 TYR A N   
701  C CA  . TYR A 114 ? 0.8561 0.3408 0.5460 -0.0381 -0.0156 0.0357  240 TYR A CA  
702  C C   . TYR A 114 ? 0.8617 0.3394 0.5435 -0.0477 -0.0192 0.0563  240 TYR A C   
703  O O   . TYR A 114 ? 0.8372 0.3525 0.5348 -0.0375 -0.0179 0.0647  240 TYR A O   
704  C CB  . TYR A 114 ? 0.8219 0.3420 0.5199 -0.0651 -0.0149 0.0300  240 TYR A CB  
705  C CG  . TYR A 114 ? 0.7862 0.3368 0.4996 -0.0550 -0.0111 0.0134  240 TYR A CG  
706  C CD1 . TYR A 114 ? 0.8005 0.3833 0.5355 -0.0285 -0.0059 0.0093  240 TYR A CD1 
707  C CD2 . TYR A 114 ? 0.8463 0.3943 0.5515 -0.0741 -0.0137 0.0031  240 TYR A CD2 
708  C CE1 . TYR A 114 ? 0.7785 0.3879 0.5255 -0.0211 -0.0021 -0.0038 240 TYR A CE1 
709  C CE2 . TYR A 114 ? 0.7711 0.3464 0.4871 -0.0653 -0.0108 -0.0104 240 TYR A CE2 
710  C CZ  . TYR A 114 ? 0.7812 0.3856 0.5173 -0.0387 -0.0044 -0.0133 240 TYR A CZ  
711  O OH  . TYR A 114 ? 0.7731 0.4027 0.5178 -0.0316 -0.0013 -0.0245 240 TYR A OH  
712  N N   . GLU A 115 ? 0.8895 0.3175 0.5438 -0.0693 -0.0241 0.0647  241 GLU A N   
713  C CA  . GLU A 115 ? 0.9282 0.3433 0.5692 -0.0808 -0.0274 0.0865  241 GLU A CA  
714  C C   . GLU A 115 ? 0.9343 0.3369 0.5751 -0.0494 -0.0301 0.0955  241 GLU A C   
715  O O   . GLU A 115 ? 0.9249 0.3608 0.5730 -0.0475 -0.0302 0.1085  241 GLU A O   
716  C CB  . GLU A 115 ? 0.9920 0.3530 0.6054 -0.1060 -0.0329 0.0919  241 GLU A CB  
717  C CG  . GLU A 115 ? 1.0551 0.4124 0.6585 -0.1210 -0.0353 0.1137  241 GLU A CG  
718  C CD  . GLU A 115 ? 1.1080 0.4239 0.6924 -0.1436 -0.0404 0.1159  241 GLU A CD  
719  O OE1 . GLU A 115 ? 1.1439 0.4182 0.7181 -0.1331 -0.0436 0.1018  241 GLU A OE1 
720  O OE2 . GLU A 115 ? 1.1161 0.4426 0.6951 -0.1721 -0.0405 0.1313  241 GLU A OE2 
721  N N   . SER A 116 ? 0.9430 0.3092 0.5803 -0.0233 -0.0320 0.0870  242 SER A N   
722  C CA  . SER A 116 ? 0.9409 0.3080 0.5869 0.0074  -0.0354 0.0953  242 SER A CA  
723  C C   . SER A 116 ? 0.9031 0.3186 0.5730 0.0278  -0.0332 0.0931  242 SER A C   
724  O O   . SER A 116 ? 0.9140 0.3464 0.5900 0.0414  -0.0382 0.1061  242 SER A O   
725  C CB  . SER A 116 ? 0.9815 0.3126 0.6265 0.0306  -0.0359 0.0856  242 SER A CB  
726  O OG  . SER A 116 ? 1.0036 0.3531 0.6668 0.0537  -0.0297 0.0679  242 SER A OG  
727  N N   . ALA A 117 ? 0.8604 0.3138 0.5511 0.0283  -0.0260 0.0751  243 ALA A N   
728  C CA  . ALA A 117 ? 0.8012 0.3169 0.5232 0.0422  -0.0231 0.0704  243 ALA A CA  
729  C C   . ALA A 117 ? 0.7779 0.3345 0.5044 0.0265  -0.0243 0.0815  243 ALA A C   
730  O O   . ALA A 117 ? 0.7465 0.3350 0.4868 0.0399  -0.0271 0.0860  243 ALA A O   
731  C CB  . ALA A 117 ? 0.7892 0.3328 0.5276 0.0410  -0.0154 0.0513  243 ALA A CB  
732  N N   . ILE A 118 ? 0.7676 0.3264 0.4829 -0.0023 -0.0219 0.0850  244 ILE A N   
733  C CA  . ILE A 118 ? 0.7708 0.3685 0.4877 -0.0167 -0.0203 0.0949  244 ILE A CA  
734  C C   . ILE A 118 ? 0.7773 0.3577 0.4772 -0.0106 -0.0273 0.1136  244 ILE A C   
735  O O   . ILE A 118 ? 0.7704 0.3860 0.4750 -0.0064 -0.0282 0.1186  244 ILE A O   
736  C CB  . ILE A 118 ? 0.7985 0.4019 0.5076 -0.0488 -0.0155 0.0972  244 ILE A CB  
737  C CG1 . ILE A 118 ? 0.7869 0.4221 0.5167 -0.0533 -0.0101 0.0799  244 ILE A CG1 
738  C CG2 . ILE A 118 ? 0.7857 0.4217 0.4901 -0.0631 -0.0122 0.1106  244 ILE A CG2 
739  C CD1 . ILE A 118 ? 0.7947 0.4318 0.5194 -0.0842 -0.0080 0.0811  244 ILE A CD1 
740  N N   . HIS A 119 ? 0.8578 0.3809 0.5348 -0.0093 -0.0335 0.1243  245 HIS A N   
741  C CA  . HIS A 119 ? 0.8570 0.3609 0.5159 -0.0020 -0.0420 0.1444  245 HIS A CA  
742  C C   . HIS A 119 ? 0.8441 0.3710 0.5216 0.0289  -0.0482 0.1427  245 HIS A C   
743  O O   . HIS A 119 ? 0.8566 0.4067 0.5306 0.0317  -0.0536 0.1538  245 HIS A O   
744  C CB  . HIS A 119 ? 0.9355 0.3722 0.5691 -0.0043 -0.0476 0.1551  245 HIS A CB  
745  C CG  . HIS A 119 ? 0.9909 0.4128 0.6064 -0.0397 -0.0439 0.1621  245 HIS A CG  
746  N ND1 . HIS A 119 ? 0.9430 0.3892 0.5470 -0.0620 -0.0413 0.1775  245 HIS A ND1 
747  C CD2 . HIS A 119 ? 1.0130 0.4027 0.6211 -0.0574 -0.0421 0.1553  245 HIS A CD2 
748  C CE1 . HIS A 119 ? 1.0042 0.4376 0.5986 -0.0921 -0.0375 0.1808  245 HIS A CE1 
749  N NE2 . HIS A 119 ? 1.0103 0.4078 0.6062 -0.0908 -0.0392 0.1677  245 HIS A NE2 
750  N N   . ALA A 120 ? 0.7805 0.3043 0.4778 0.0510  -0.0473 0.1288  246 ALA A N   
751  C CA  . ALA A 120 ? 0.8252 0.3758 0.5450 0.0791  -0.0531 0.1280  246 ALA A CA  
752  C C   . ALA A 120 ? 0.7522 0.3651 0.4924 0.0746  -0.0509 0.1207  246 ALA A C   
753  O O   . ALA A 120 ? 0.7585 0.3958 0.5040 0.0841  -0.0595 0.1284  246 ALA A O   
754  C CB  . ALA A 120 ? 0.8257 0.3630 0.5628 0.1025  -0.0494 0.1143  246 ALA A CB  
755  N N   . ILE A 121 ? 0.7259 0.3629 0.4763 0.0605  -0.0407 0.1058  247 ILE A N   
756  C CA  . ILE A 121 ? 0.6930 0.3818 0.4598 0.0566  -0.0381 0.0979  247 ILE A CA  
757  C C   . ILE A 121 ? 0.7068 0.4087 0.4543 0.0416  -0.0400 0.1090  247 ILE A C   
758  O O   . ILE A 121 ? 0.7023 0.4352 0.4540 0.0455  -0.0442 0.1087  247 ILE A O   
759  C CB  . ILE A 121 ? 0.6537 0.3598 0.4335 0.0465  -0.0273 0.0813  247 ILE A CB  
760  C CG1 . ILE A 121 ? 0.6025 0.2976 0.3979 0.0623  -0.0247 0.0700  247 ILE A CG1 
761  C CG2 . ILE A 121 ? 0.5913 0.3440 0.3837 0.0421  -0.0242 0.0738  247 ILE A CG2 
762  C CD1 . ILE A 121 ? 0.6497 0.3494 0.4491 0.0500  -0.0157 0.0562  247 ILE A CD1 
763  N N   . GLY A 122 ? 0.6837 0.3627 0.4082 0.0226  -0.0366 0.1185  248 GLY A N   
764  C CA  . GLY A 122 ? 0.7544 0.4467 0.4578 0.0077  -0.0359 0.1301  248 GLY A CA  
765  C C   . GLY A 122 ? 0.7731 0.4584 0.4614 0.0191  -0.0485 0.1449  248 GLY A C   
766  O O   . GLY A 122 ? 0.8112 0.5251 0.4920 0.0174  -0.0504 0.1462  248 GLY A O   
767  N N   . LYS A 123 ? 0.7813 0.4269 0.4630 0.0318  -0.0580 0.1562  249 LYS A N   
768  C CA  . LYS A 123 ? 0.8239 0.4641 0.4933 0.0451  -0.0726 0.1723  249 LYS A CA  
769  C C   . LYS A 123 ? 0.7689 0.4498 0.4639 0.0626  -0.0797 0.1626  249 LYS A C   
770  O O   . LYS A 123 ? 0.7820 0.4823 0.4664 0.0639  -0.0897 0.1703  249 LYS A O   
771  C CB  . LYS A 123 ? 0.8373 0.4251 0.4976 0.0593  -0.0813 0.1860  249 LYS A CB  
772  C CG  . LYS A 123 ? 0.9112 0.4549 0.5425 0.0385  -0.0768 0.1983  249 LYS A CG  
773  C CD  . LYS A 123 ? 0.9600 0.4627 0.5966 0.0524  -0.0812 0.2029  249 LYS A CD  
774  C CE  . LYS A 123 ? 0.9956 0.4595 0.6132 0.0283  -0.0740 0.2063  249 LYS A CE  
775  N NZ  . LYS A 123 ? 1.0744 0.4927 0.6940 0.0415  -0.0774 0.2074  249 LYS A NZ  
776  N N   . ALA A 124 ? 0.7582 0.4526 0.4853 0.0742  -0.0752 0.1461  250 ALA A N   
777  C CA  . ALA A 124 ? 0.7094 0.4440 0.4629 0.0870  -0.0814 0.1374  250 ALA A CA  
778  C C   . ALA A 124 ? 0.7033 0.4731 0.4525 0.0721  -0.0776 0.1278  250 ALA A C   
779  O O   . ALA A 124 ? 0.7299 0.5260 0.4831 0.0760  -0.0877 0.1272  250 ALA A O   
780  C CB  . ALA A 124 ? 0.7014 0.4422 0.4878 0.1006  -0.0750 0.1230  250 ALA A CB  
781  N N   . SER A 125 ? 0.6685 0.4391 0.4095 0.0553  -0.0636 0.1197  251 SER A N   
782  C CA  . SER A 125 ? 0.6834 0.4840 0.4181 0.0443  -0.0584 0.1101  251 SER A CA  
783  C C   . SER A 125 ? 0.7145 0.5182 0.4188 0.0395  -0.0671 0.1220  251 SER A C   
784  O O   . SER A 125 ? 0.7192 0.5461 0.4205 0.0402  -0.0726 0.1152  251 SER A O   
785  C CB  . SER A 125 ? 0.7054 0.5078 0.4363 0.0287  -0.0421 0.1033  251 SER A CB  
786  O OG  . SER A 125 ? 0.6518 0.4799 0.3712 0.0204  -0.0359 0.0966  251 SER A OG  
787  N N   . ALA A 126 ? 0.6693 0.4467 0.3480 0.0338  -0.0691 0.1399  252 ALA A N   
788  C CA  . ALA A 126 ? 0.7815 0.5565 0.4270 0.0305  -0.0795 0.1554  252 ALA A CA  
789  C C   . ALA A 126 ? 0.7959 0.5966 0.4197 0.0178  -0.0714 0.1471  252 ALA A C   
790  O O   . ALA A 126 ? 0.8362 0.6499 0.4422 0.0194  -0.0817 0.1476  252 ALA A O   
791  C CB  . ALA A 126 ? 0.7579 0.5379 0.4125 0.0478  -0.1001 0.1617  252 ALA A CB  
792  N N   . GLY A 127 ? 0.7614 0.5697 0.3854 0.0054  -0.0529 0.1394  253 GLY A N   
793  C CA  . GLY A 127 ? 0.8059 0.6380 0.4092 -0.0044 -0.0414 0.1317  253 GLY A CA  
794  C C   . GLY A 127 ? 0.7603 0.6175 0.3786 0.0028  -0.0395 0.1092  253 GLY A C   
795  O O   . GLY A 127 ? 0.7724 0.6463 0.3701 -0.0016 -0.0308 0.1008  253 GLY A O   
796  N N   . ARG A 128 ? 0.7175 0.5762 0.3688 0.0139  -0.0467 0.0994  254 ARG A N   
797  C CA  . ARG A 128 ? 0.7101 0.5878 0.3759 0.0186  -0.0446 0.0790  254 ARG A CA  
798  C C   . ARG A 128 ? 0.6581 0.5490 0.3310 0.0141  -0.0252 0.0669  254 ARG A C   
799  O O   . ARG A 128 ? 0.7202 0.6240 0.3925 0.0172  -0.0209 0.0512  254 ARG A O   
800  C CB  . ARG A 128 ? 0.7071 0.5850 0.4080 0.0292  -0.0546 0.0739  254 ARG A CB  
801  C CG  . ARG A 128 ? 0.7016 0.5810 0.4008 0.0354  -0.0751 0.0804  254 ARG A CG  
802  C CD  . ARG A 128 ? 0.7181 0.6051 0.4566 0.0455  -0.0820 0.0757  254 ARG A CD  
803  N NE  . ARG A 128 ? 0.7405 0.6126 0.4959 0.0538  -0.0812 0.0866  254 ARG A NE  
804  C CZ  . ARG A 128 ? 0.6945 0.5708 0.4832 0.0643  -0.0821 0.0836  254 ARG A CZ  
805  N NH1 . ARG A 128 ? 0.7341 0.6310 0.5457 0.0656  -0.0831 0.0715  254 ARG A NH1 
806  N NH2 . ARG A 128 ? 0.7341 0.5912 0.5309 0.0735  -0.0812 0.0930  254 ARG A NH2 
807  N N   . GLY A 129 ? 0.6750 0.5626 0.3539 0.0068  -0.0143 0.0744  255 GLY A N   
808  C CA  . GLY A 129 ? 0.6642 0.5707 0.3518 0.0020  0.0030  0.0656  255 GLY A CA  
809  C C   . GLY A 129 ? 0.6480 0.5595 0.3704 0.0085  0.0049  0.0532  255 GLY A C   
810  O O   . GLY A 129 ? 0.6225 0.5226 0.3625 0.0159  -0.0052 0.0512  255 GLY A O   
811  N N   . ILE A 130 ? 0.6182 0.5500 0.3507 0.0063  0.0188  0.0455  256 ILE A N   
812  C CA  . ILE A 130 ? 0.5772 0.5132 0.3402 0.0090  0.0211  0.0382  256 ILE A CA  
813  C C   . ILE A 130 ? 0.5695 0.5064 0.3467 0.0216  0.0162  0.0238  256 ILE A C   
814  O O   . ILE A 130 ? 0.5477 0.4827 0.3476 0.0245  0.0150  0.0196  256 ILE A O   
815  C CB  . ILE A 130 ? 0.5751 0.5366 0.3472 0.0024  0.0357  0.0369  256 ILE A CB  
816  C CG1 . ILE A 130 ? 0.5829 0.5670 0.3470 0.0107  0.0454  0.0264  256 ILE A CG1 
817  C CG2 . ILE A 130 ? 0.5825 0.5444 0.3432 -0.0145 0.0408  0.0525  256 ILE A CG2 
818  C CD1 . ILE A 130 ? 0.6094 0.6260 0.3894 0.0085  0.0599  0.0247  256 ILE A CD1 
819  N N   . TYR A 131 ? 0.5960 0.5338 0.3581 0.0275  0.0129  0.0163  257 TYR A N   
820  C CA  . TYR A 131 ? 0.5632 0.4989 0.3371 0.0363  0.0081  0.0032  257 TYR A CA  
821  C C   . TYR A 131 ? 0.6019 0.5250 0.3768 0.0379  -0.0075 0.0048  257 TYR A C   
822  O O   . TYR A 131 ? 0.6351 0.5559 0.4308 0.0415  -0.0124 0.0003  257 TYR A O   
823  C CB  . TYR A 131 ? 0.5720 0.5142 0.3293 0.0419  0.0148  -0.0094 257 TYR A CB  
824  C CG  . TYR A 131 ? 0.5816 0.5440 0.3407 0.0431  0.0313  -0.0107 257 TYR A CG  
825  C CD1 . TYR A 131 ? 0.5865 0.5607 0.3729 0.0452  0.0370  -0.0117 257 TYR A CD1 
826  C CD2 . TYR A 131 ? 0.6269 0.6004 0.3610 0.0419  0.0412  -0.0100 257 TYR A CD2 
827  C CE1 . TYR A 131 ? 0.5695 0.5692 0.3622 0.0463  0.0509  -0.0116 257 TYR A CE1 
828  C CE2 . TYR A 131 ? 0.6212 0.6207 0.3613 0.0434  0.0576  -0.0102 257 TYR A CE2 
829  C CZ  . TYR A 131 ? 0.5901 0.6043 0.3619 0.0457  0.0618  -0.0107 257 TYR A CZ  
830  O OH  . TYR A 131 ? 0.5687 0.6156 0.3507 0.0471  0.0771  -0.0095 257 TYR A OH  
831  N N   . GLU A 132 ? 0.6168 0.5347 0.3693 0.0348  -0.0155 0.0120  258 GLU A N   
832  C CA  . GLU A 132 ? 0.6363 0.5483 0.3916 0.0363  -0.0323 0.0155  258 GLU A CA  
833  C C   . GLU A 132 ? 0.6600 0.5662 0.4327 0.0384  -0.0376 0.0287  258 GLU A C   
834  O O   . GLU A 132 ? 0.7005 0.6082 0.4896 0.0430  -0.0490 0.0309  258 GLU A O   
835  C CB  . GLU A 132 ? 0.6919 0.6016 0.4135 0.0327  -0.0407 0.0180  258 GLU A CB  
836  C CG  . GLU A 132 ? 0.8144 0.7236 0.5177 0.0325  -0.0402 0.0017  258 GLU A CG  
837  C CD  . GLU A 132 ? 0.9300 0.8369 0.6436 0.0314  -0.0567 -0.0041 258 GLU A CD  
838  O OE1 . GLU A 132 ? 0.9147 0.8253 0.6349 0.0299  -0.0720 0.0066  258 GLU A OE1 
839  O OE2 . GLU A 132 ? 0.9412 0.8431 0.6570 0.0320  -0.0547 -0.0185 258 GLU A OE2 
840  N N   . GLY A 133 ? 0.5811 0.4804 0.3504 0.0352  -0.0296 0.0375  259 GLY A N   
841  C CA  . GLY A 133 ? 0.5776 0.4628 0.3564 0.0382  -0.0345 0.0494  259 GLY A CA  
842  C C   . GLY A 133 ? 0.5565 0.4379 0.3588 0.0401  -0.0267 0.0447  259 GLY A C   
843  O O   . GLY A 133 ? 0.5366 0.4282 0.3472 0.0375  -0.0174 0.0346  259 GLY A O   
844  N N   . PRO A 134 ? 0.5697 0.4349 0.3807 0.0458  -0.0306 0.0521  260 PRO A N   
845  C CA  . PRO A 134 ? 0.5233 0.3811 0.3514 0.0477  -0.0237 0.0466  260 PRO A CA  
846  C C   . PRO A 134 ? 0.5552 0.4045 0.3727 0.0351  -0.0143 0.0479  260 PRO A C   
847  O O   . PRO A 134 ? 0.5665 0.4121 0.3645 0.0254  -0.0128 0.0564  260 PRO A O   
848  C CB  . PRO A 134 ? 0.5224 0.3616 0.3568 0.0595  -0.0306 0.0544  260 PRO A CB  
849  C CG  . PRO A 134 ? 0.5378 0.3671 0.3520 0.0593  -0.0399 0.0687  260 PRO A CG  
850  C CD  . PRO A 134 ? 0.5724 0.4229 0.3745 0.0518  -0.0418 0.0661  260 PRO A CD  
851  N N   . GLY A 135 ? 0.5063 0.3551 0.3369 0.0339  -0.0082 0.0400  261 GLY A N   
852  C CA  . GLY A 135 ? 0.5475 0.3896 0.3716 0.0203  -0.0017 0.0413  261 GLY A CA  
853  C C   . GLY A 135 ? 0.5406 0.3603 0.3700 0.0222  -0.0015 0.0376  261 GLY A C   
854  O O   . GLY A 135 ? 0.4884 0.2975 0.3253 0.0360  -0.0048 0.0353  261 GLY A O   
855  N N   . ILE A 136 ? 0.5208 0.3343 0.3454 0.0079  0.0025  0.0371  262 ILE A N   
856  C CA  . ILE A 136 ? 0.5122 0.3007 0.3353 0.0066  0.0024  0.0319  262 ILE A CA  
857  C C   . ILE A 136 ? 0.5553 0.3664 0.3886 -0.0022 0.0065  0.0231  262 ILE A C   
858  O O   . ILE A 136 ? 0.5314 0.3726 0.3709 -0.0104 0.0097  0.0242  262 ILE A O   
859  C CB  . ILE A 136 ? 0.5987 0.3484 0.4007 -0.0057 -0.0003 0.0406  262 ILE A CB  
860  C CG1 . ILE A 136 ? 0.6264 0.3405 0.4215 -0.0023 -0.0012 0.0328  262 ILE A CG1 
861  C CG2 . ILE A 136 ? 0.6177 0.3812 0.4146 -0.0297 0.0026  0.0459  262 ILE A CG2 
862  C CD1 . ILE A 136 ? 0.7207 0.3833 0.4912 -0.0096 -0.0053 0.0406  262 ILE A CD1 
863  N N   . SER A 137 ? 0.5252 0.3227 0.3595 0.0014  0.0066  0.0144  263 SER A N   
864  C CA  . SER A 137 ? 0.5300 0.3425 0.3693 -0.0083 0.0079  0.0072  263 SER A CA  
865  C C   . SER A 137 ? 0.5989 0.3757 0.4208 -0.0186 0.0053  0.0037  263 SER A C   
866  O O   . SER A 137 ? 0.5920 0.3328 0.4019 -0.0089 0.0047  0.0016  263 SER A O   
867  C CB  . SER A 137 ? 0.4873 0.3194 0.3408 0.0052  0.0101  -0.0014 263 SER A CB  
868  O OG  . SER A 137 ? 0.4976 0.3592 0.3644 0.0116  0.0116  0.0005  263 SER A OG  
869  N N   . ILE A 138 ? 0.5341 0.3210 0.3545 -0.0378 0.0033  0.0027  264 ILE A N   
870  C CA  . ILE A 138 ? 0.6021 0.3539 0.4026 -0.0521 -0.0011 -0.0017 264 ILE A CA  
871  C C   . ILE A 138 ? 0.5682 0.3410 0.3733 -0.0589 -0.0034 -0.0103 264 ILE A C   
872  O O   . ILE A 138 ? 0.5385 0.3554 0.3637 -0.0576 -0.0024 -0.0090 264 ILE A O   
873  C CB  . ILE A 138 ? 0.6229 0.3607 0.4119 -0.0767 -0.0048 0.0083  264 ILE A CB  
874  C CG1 . ILE A 138 ? 0.5883 0.3780 0.3965 -0.0933 -0.0042 0.0145  264 ILE A CG1 
875  C CG2 . ILE A 138 ? 0.6863 0.4018 0.4673 -0.0697 -0.0034 0.0190  264 ILE A CG2 
876  C CD1 . ILE A 138 ? 0.6423 0.4253 0.4416 -0.1221 -0.0070 0.0257  264 ILE A CD1 
877  N N   . LYS A 139 ? 0.6192 0.3571 0.4029 -0.0649 -0.0070 -0.0193 265 LYS A N   
878  C CA  . LYS A 139 ? 0.6422 0.3929 0.4223 -0.0764 -0.0121 -0.0268 265 LYS A CA  
879  C C   . LYS A 139 ? 0.6760 0.4072 0.4397 -0.1062 -0.0209 -0.0254 265 LYS A C   
880  O O   . LYS A 139 ? 0.6893 0.3673 0.4268 -0.1120 -0.0228 -0.0283 265 LYS A O   
881  C CB  . LYS A 139 ? 0.6555 0.3823 0.4194 -0.0610 -0.0093 -0.0398 265 LYS A CB  
882  C CG  . LYS A 139 ? 0.6251 0.3759 0.4075 -0.0355 -0.0010 -0.0400 265 LYS A CG  
883  C CD  . LYS A 139 ? 0.6767 0.4164 0.4452 -0.0243 0.0028  -0.0513 265 LYS A CD  
884  C CE  . LYS A 139 ? 0.6417 0.3996 0.4281 -0.0010 0.0117  -0.0497 265 LYS A CE  
885  N NZ  . LYS A 139 ? 0.6023 0.4044 0.4149 -0.0005 0.0104  -0.0416 265 LYS A NZ  
886  N N   . LEU A 140 ? 0.6464 0.4204 0.4261 -0.1252 -0.0267 -0.0201 266 LEU A N   
887  C CA  . LEU A 140 ? 0.6892 0.4523 0.4577 -0.1580 -0.0359 -0.0166 266 LEU A CA  
888  C C   . LEU A 140 ? 0.7291 0.4416 0.4623 -0.1690 -0.0441 -0.0301 266 LEU A C   
889  O O   . LEU A 140 ? 0.7653 0.4402 0.4767 -0.1939 -0.0513 -0.0297 266 LEU A O   
890  C CB  . LEU A 140 ? 0.6710 0.4990 0.4683 -0.1742 -0.0408 -0.0086 266 LEU A CB  
891  C CG  . LEU A 140 ? 0.6428 0.5212 0.4722 -0.1647 -0.0318 0.0036  266 LEU A CG  
892  C CD1 . LEU A 140 ? 0.6154 0.5590 0.4739 -0.1783 -0.0362 0.0105  266 LEU A CD1 
893  C CD2 . LEU A 140 ? 0.6735 0.5289 0.4950 -0.1737 -0.0268 0.0136  266 LEU A CD2 
894  N N   . SER A 141 ? 0.7675 0.4747 0.4914 -0.1516 -0.0426 -0.0422 267 SER A N   
895  C CA  . SER A 141 ? 0.7721 0.4304 0.4574 -0.1602 -0.0490 -0.0572 267 SER A CA  
896  C C   . SER A 141 ? 0.7963 0.3829 0.4504 -0.1519 -0.0441 -0.0640 267 SER A C   
897  O O   . SER A 141 ? 0.8522 0.3865 0.4686 -0.1629 -0.0498 -0.0766 267 SER A O   
898  C CB  . SER A 141 ? 0.7759 0.4485 0.4568 -0.1423 -0.0466 -0.0674 267 SER A CB  
899  O OG  . SER A 141 ? 0.7550 0.4135 0.4368 -0.1106 -0.0328 -0.0711 267 SER A OG  
900  N N   . ALA A 142 ? 0.7897 0.3712 0.4569 -0.1314 -0.0344 -0.0563 268 ALA A N   
901  C CA  . ALA A 142 ? 0.8851 0.4007 0.5262 -0.1224 -0.0311 -0.0592 268 ALA A CA  
902  C C   . ALA A 142 ? 0.8883 0.3702 0.5145 -0.1518 -0.0397 -0.0504 268 ALA A C   
903  O O   . ALA A 142 ? 0.9441 0.3574 0.5379 -0.1513 -0.0408 -0.0551 268 ALA A O   
904  C CB  . ALA A 142 ? 0.8345 0.3612 0.4965 -0.0912 -0.0201 -0.0517 268 ALA A CB  
905  N N   . LEU A 143 ? 0.8803 0.4080 0.5289 -0.1772 -0.0451 -0.0373 269 LEU A N   
906  C CA  . LEU A 143 ? 0.8903 0.3966 0.5312 -0.2054 -0.0507 -0.0243 269 LEU A CA  
907  C C   . LEU A 143 ? 0.9595 0.4542 0.5834 -0.2460 -0.0645 -0.0271 269 LEU A C   
908  O O   . LEU A 143 ? 1.0040 0.4776 0.6189 -0.2731 -0.0698 -0.0161 269 LEU A O   
909  C CB  . LEU A 143 ? 0.8319 0.3998 0.5097 -0.2067 -0.0452 -0.0058 269 LEU A CB  
910  C CG  . LEU A 143 ? 0.8297 0.4109 0.5234 -0.1700 -0.0339 -0.0029 269 LEU A CG  
911  C CD1 . LEU A 143 ? 0.7964 0.4422 0.5234 -0.1714 -0.0286 0.0116  269 LEU A CD1 
912  C CD2 . LEU A 143 ? 0.8703 0.3853 0.5384 -0.1580 -0.0324 0.0000  269 LEU A CD2 
913  N N   . HIS A 144 ? 0.9806 0.4900 0.5993 -0.2510 -0.0710 -0.0405 270 HIS A N   
914  C CA  . HIS A 144 ? 0.9799 0.4907 0.5871 -0.2868 -0.0855 -0.0428 270 HIS A CA  
915  C C   . HIS A 144 ? 1.0516 0.5276 0.6276 -0.2749 -0.0883 -0.0622 270 HIS A C   
916  O O   . HIS A 144 ? 1.0131 0.5066 0.5902 -0.2561 -0.0851 -0.0729 270 HIS A O   
917  C CB  . HIS A 144 ? 0.9589 0.5529 0.6039 -0.3062 -0.0918 -0.0339 270 HIS A CB  
918  C CG  . HIS A 144 ? 1.0313 0.6420 0.6766 -0.3451 -0.1062 -0.0287 270 HIS A CG  
919  N ND1 . HIS A 144 ? 1.0818 0.6844 0.7077 -0.3538 -0.1175 -0.0405 270 HIS A ND1 
920  C CD2 . HIS A 144 ? 1.0656 0.7065 0.7306 -0.3737 -0.1095 -0.0116 270 HIS A CD2 
921  C CE1 . HIS A 144 ? 1.0796 0.7054 0.7138 -0.3869 -0.1284 -0.0311 270 HIS A CE1 
922  N NE2 . HIS A 144 ? 1.1168 0.7675 0.7755 -0.3991 -0.1234 -0.0135 270 HIS A NE2 
923  N N   . PRO A 145 ? 1.0596 0.4876 0.6064 -0.2861 -0.0940 -0.0669 271 PRO A N   
924  C CA  . PRO A 145 ? 1.1323 0.5173 0.6454 -0.2692 -0.0928 -0.0859 271 PRO A CA  
925  C C   . PRO A 145 ? 1.1509 0.5686 0.6609 -0.2776 -0.1010 -0.0958 271 PRO A C   
926  O O   . PRO A 145 ? 1.2312 0.6190 0.7134 -0.2624 -0.0984 -0.1116 271 PRO A O   
927  C CB  . PRO A 145 ? 1.1733 0.5022 0.6576 -0.2860 -0.0991 -0.0862 271 PRO A CB  
928  C CG  . PRO A 145 ? 1.1680 0.5298 0.6722 -0.3236 -0.1093 -0.0688 271 PRO A CG  
929  C CD  . PRO A 145 ? 1.0681 0.4813 0.6108 -0.3167 -0.1018 -0.0549 271 PRO A CD  
930  N N   . ARG A 146 ? 1.0970 0.5770 0.6346 -0.3006 -0.1109 -0.0866 272 ARG A N   
931  C CA  . ARG A 146 ? 1.1257 0.6410 0.6620 -0.3067 -0.1202 -0.0938 272 ARG A CA  
932  C C   . ARG A 146 ? 1.1129 0.7051 0.6912 -0.3104 -0.1232 -0.0826 272 ARG A C   
933  O O   . ARG A 146 ? 1.1350 0.7791 0.7318 -0.3327 -0.1367 -0.0760 272 ARG A O   
934  C CB  . ARG A 146 ? 1.1726 0.6787 0.6914 -0.3388 -0.1362 -0.0953 272 ARG A CB  
935  N N   . TYR A 147 ? 1.0399 0.6410 0.6343 -0.2868 -0.1107 -0.0801 273 TYR A N   
936  C CA  . TYR A 147 ? 0.9783 0.6558 0.6205 -0.2834 -0.1091 -0.0656 273 TYR A CA  
937  C C   . TYR A 147 ? 0.9813 0.7137 0.6361 -0.2835 -0.1189 -0.0665 273 TYR A C   
938  O O   . TYR A 147 ? 0.9496 0.7484 0.6408 -0.2977 -0.1271 -0.0533 273 TYR A O   
939  C CB  . TYR A 147 ? 0.8606 0.5416 0.5213 -0.2442 -0.0895 -0.0617 273 TYR A CB  
940  C CG  . TYR A 147 ? 0.8550 0.6115 0.5662 -0.2335 -0.0839 -0.0458 273 TYR A CG  
941  C CD1 . TYR A 147 ? 0.7686 0.5613 0.5070 -0.2542 -0.0861 -0.0306 273 TYR A CD1 
942  C CD2 . TYR A 147 ? 0.7836 0.5730 0.5133 -0.2029 -0.0756 -0.0461 273 TYR A CD2 
943  C CE1 . TYR A 147 ? 0.7510 0.6104 0.5325 -0.2421 -0.0794 -0.0179 273 TYR A CE1 
944  C CE2 . TYR A 147 ? 0.7302 0.5809 0.5018 -0.1919 -0.0704 -0.0332 273 TYR A CE2 
945  C CZ  . TYR A 147 ? 0.6867 0.5721 0.4835 -0.2102 -0.0719 -0.0201 273 TYR A CZ  
946  O OH  . TYR A 147 ? 0.7304 0.6755 0.5663 -0.1973 -0.0652 -0.0089 273 TYR A OH  
947  N N   . SER A 148 ? 0.9865 0.6939 0.6117 -0.2665 -0.1176 -0.0810 274 SER A N   
948  C CA  . SER A 148 ? 1.0209 0.7757 0.6535 -0.2637 -0.1267 -0.0806 274 SER A CA  
949  C C   . SER A 148 ? 1.0822 0.8452 0.7009 -0.2953 -0.1471 -0.0824 274 SER A C   
950  O O   . SER A 148 ? 1.0849 0.9017 0.7201 -0.2987 -0.1588 -0.0764 274 SER A O   
951  C CB  . SER A 148 ? 1.0359 0.7637 0.6416 -0.2335 -0.1158 -0.0931 274 SER A CB  
952  N N   . ARG A 149 ? 1.1585 0.8737 0.7533 -0.3127 -0.1496 -0.0875 275 ARG A N   
953  C CA  . ARG A 149 ? 1.1645 0.8818 0.7450 -0.3371 -0.1658 -0.0895 275 ARG A CA  
954  C C   . ARG A 149 ? 1.1828 0.9283 0.7881 -0.3709 -0.1771 -0.0757 275 ARG A C   
955  O O   . ARG A 149 ? 1.1919 0.9467 0.7899 -0.3941 -0.1922 -0.0754 275 ARG A O   
956  C CB  . ARG A 149 ? 1.1755 0.8161 0.7045 -0.3323 -0.1617 -0.1073 275 ARG A CB  
957  N N   . ALA A 150 ? 1.2887 1.0494 0.9223 -0.3749 -0.1698 -0.0637 276 ALA A N   
958  C CA  . ALA A 150 ? 1.3505 1.1373 1.0070 -0.4065 -0.1770 -0.0492 276 ALA A CA  
959  C C   . ALA A 150 ? 1.3622 1.2443 1.0750 -0.4117 -0.1812 -0.0317 276 ALA A C   
960  O O   . ALA A 150 ? 1.2989 1.2155 1.0356 -0.3895 -0.1735 -0.0287 276 ALA A O   
961  C CB  . ALA A 150 ? 1.3796 1.1194 1.0284 -0.4085 -0.1650 -0.0455 276 ALA A CB  
962  N N   . GLN A 151 ? 1.2516 1.1770 0.9861 -0.4401 -0.1932 -0.0201 277 GLN A N   
963  C CA  . GLN A 151 ? 1.1860 1.2071 0.9779 -0.4434 -0.1959 -0.0023 277 GLN A CA  
964  C C   . GLN A 151 ? 1.2052 1.2496 1.0281 -0.4365 -0.1795 0.0093  277 GLN A C   
965  O O   . GLN A 151 ? 1.2288 1.2200 1.0316 -0.4422 -0.1699 0.0085  277 GLN A O   
966  C CB  . GLN A 151 ? 1.0901 1.1481 0.8972 -0.4761 -0.2102 0.0080  277 GLN A CB  
967  N N   . ALA A 152 ? 1.1855 1.3106 1.0573 -0.4220 -0.1760 0.0206  278 ALA A N   
968  C CA  . ALA A 152 ? 1.1503 1.3020 1.0517 -0.4109 -0.1588 0.0303  278 ALA A CA  
969  C C   . ALA A 152 ? 1.1488 1.3077 1.0620 -0.4360 -0.1523 0.0439  278 ALA A C   
970  O O   . ALA A 152 ? 1.2031 1.3477 1.1187 -0.4317 -0.1369 0.0489  278 ALA A O   
971  C CB  . ALA A 152 ? 1.1755 1.4167 1.1284 -0.3879 -0.1561 0.0399  278 ALA A CB  
972  N N   . ALA A 153 ? 1.1930 1.3738 1.1122 -0.4626 -0.1637 0.0508  279 ALA A N   
973  C CA  . ALA A 153 ? 1.2405 1.4314 1.1703 -0.4876 -0.1581 0.0648  279 ALA A CA  
974  C C   . ALA A 153 ? 1.2650 1.3616 1.1471 -0.4970 -0.1530 0.0587  279 ALA A C   
975  O O   . ALA A 153 ? 1.2638 1.3542 1.1510 -0.4964 -0.1385 0.0679  279 ALA A O   
976  C CB  . ALA A 153 ? 1.1886 1.4173 1.1308 -0.5162 -0.1737 0.0722  279 ALA A CB  
977  N N   . ARG A 154 ? 1.2182 1.2400 1.0525 -0.5031 -0.1640 0.0434  280 ARG A N   
978  C CA  . ARG A 154 ? 1.2332 1.1627 1.0215 -0.5077 -0.1596 0.0373  280 ARG A CA  
979  C C   . ARG A 154 ? 1.2132 1.1011 0.9880 -0.4766 -0.1450 0.0301  280 ARG A C   
980  O O   . ARG A 154 ? 1.2179 1.0519 0.9715 -0.4754 -0.1362 0.0326  280 ARG A O   
981  C CB  . ARG A 154 ? 1.2019 1.0652 0.9432 -0.5190 -0.1740 0.0218  280 ARG A CB  
982  N N   . VAL A 155 ? 1.2074 1.1195 0.9938 -0.4512 -0.1430 0.0220  281 VAL A N   
983  C CA  . VAL A 155 ? 1.1934 1.0687 0.9682 -0.4223 -0.1297 0.0149  281 VAL A CA  
984  C C   . VAL A 155 ? 1.2019 1.1172 1.0099 -0.4191 -0.1147 0.0314  281 VAL A C   
985  O O   . VAL A 155 ? 1.1336 1.0024 0.9250 -0.4020 -0.1020 0.0319  281 VAL A O   
986  C CB  . VAL A 155 ? 1.1681 1.0597 0.9446 -0.3973 -0.1325 0.0019  281 VAL A CB  
987  N N   . MET A 156 ? 1.2130 1.2182 1.0689 -0.4274 -0.1135 0.0457  282 MET A N   
988  C CA  . MET A 156 ? 1.1398 1.1899 1.0271 -0.4172 -0.0954 0.0614  282 MET A CA  
989  C C   . MET A 156 ? 1.1326 1.1406 0.9999 -0.4399 -0.0903 0.0722  282 MET A C   
990  O O   . MET A 156 ? 1.1244 1.1056 0.9827 -0.4268 -0.0765 0.0771  282 MET A O   
991  C CB  . MET A 156 ? 1.1559 1.3118 1.0975 -0.4229 -0.0953 0.0740  282 MET A CB  
992  C CG  . MET A 156 ? 1.1267 1.3353 1.0993 -0.4260 -0.0778 0.0923  282 MET A CG  
993  S SD  . MET A 156 ? 1.1615 1.3921 1.1502 -0.3703 -0.0545 0.0904  282 MET A SD  
994  C CE  . MET A 156 ? 0.9080 1.1678 0.9127 -0.3388 -0.0637 0.0772  282 MET A CE  
995  N N   . GLY A 157 ? 1.2510 1.2507 1.1088 -0.4678 -0.1012 0.0759  283 GLY A N   
996  C CA  . GLY A 157 ? 1.2760 1.2477 1.1198 -0.4870 -0.0967 0.0883  283 GLY A CA  
997  C C   . GLY A 157 ? 1.3525 1.2226 1.1467 -0.4797 -0.0955 0.0814  283 GLY A C   
998  O O   . GLY A 157 ? 1.3332 1.1804 1.1174 -0.4862 -0.0881 0.0933  283 GLY A O   
999  N N   . GLU A 158 ? 1.2291 1.0391 0.9918 -0.4645 -0.1024 0.0626  284 GLU A N   
1000 C CA  . GLU A 158 ? 1.2291 0.9458 0.9478 -0.4496 -0.0998 0.0550  284 GLU A CA  
1001 C C   . GLU A 158 ? 1.1449 0.8482 0.8642 -0.4160 -0.0867 0.0523  284 GLU A C   
1002 O O   . GLU A 158 ? 1.1408 0.7848 0.8351 -0.4017 -0.0807 0.0539  284 GLU A O   
1003 C CB  . GLU A 158 ? 1.2565 0.9124 0.9377 -0.4481 -0.1121 0.0354  284 GLU A CB  
1004 N N   . LEU A 159 ? 1.0804 0.8388 0.8287 -0.4029 -0.0828 0.0492  285 LEU A N   
1005 C CA  . LEU A 159 ? 1.0296 0.7863 0.7829 -0.3591 -0.0692 0.0450  285 LEU A CA  
1006 C C   . LEU A 159 ? 0.9430 0.7472 0.7230 -0.3504 -0.0545 0.0622  285 LEU A C   
1007 O O   . LEU A 159 ? 0.8871 0.6631 0.6568 -0.3244 -0.0449 0.0637  285 LEU A O   
1008 C CB  . LEU A 159 ? 0.9869 0.7842 0.7586 -0.3331 -0.0700 0.0318  285 LEU A CB  
1009 C CG  . LEU A 159 ? 0.9247 0.6988 0.6896 -0.2888 -0.0601 0.0215  285 LEU A CG  
1010 C CD1 . LEU A 159 ? 0.9668 0.6512 0.6874 -0.2847 -0.0630 0.0110  285 LEU A CD1 
1011 C CD2 . LEU A 159 ? 0.8315 0.6447 0.6123 -0.2704 -0.0625 0.0108  285 LEU A CD2 
1012 N N   . LEU A 160 ? 0.9130 0.7918 0.7274 -0.3706 -0.0526 0.0747  286 LEU A N   
1013 C CA  . LEU A 160 ? 0.8651 0.7930 0.7028 -0.3631 -0.0368 0.0902  286 LEU A CA  
1014 C C   . LEU A 160 ? 0.8735 0.7471 0.6823 -0.3709 -0.0312 0.1023  286 LEU A C   
1015 O O   . LEU A 160 ? 0.8607 0.7377 0.6699 -0.3439 -0.0191 0.1059  286 LEU A O   
1016 C CB  . LEU A 160 ? 0.8627 0.8757 0.7391 -0.3901 -0.0359 0.1029  286 LEU A CB  
1017 C CG  . LEU A 160 ? 0.8225 0.8898 0.7207 -0.3895 -0.0182 0.1202  286 LEU A CG  
1018 C CD1 . LEU A 160 ? 0.7504 0.8420 0.6609 -0.3430 -0.0044 0.1135  286 LEU A CD1 
1019 C CD2 . LEU A 160 ? 0.7404 0.8930 0.6784 -0.4166 -0.0176 0.1322  286 LEU A CD2 
1020 N N   . PRO A 161 ? 0.8818 0.7031 0.6633 -0.4035 -0.0404 0.1084  287 PRO A N   
1021 C CA  . PRO A 161 ? 0.9301 0.7010 0.6849 -0.4005 -0.0355 0.1194  287 PRO A CA  
1022 C C   . PRO A 161 ? 0.9447 0.6495 0.6717 -0.3689 -0.0336 0.1121  287 PRO A C   
1023 O O   . PRO A 161 ? 0.9097 0.5997 0.6264 -0.3562 -0.0256 0.1234  287 PRO A O   
1024 C CB  . PRO A 161 ? 0.9495 0.6782 0.6829 -0.4272 -0.0483 0.1198  287 PRO A CB  
1025 C CG  . PRO A 161 ? 1.0336 0.7605 0.7675 -0.4342 -0.0612 0.1028  287 PRO A CG  
1026 C CD  . PRO A 161 ? 0.9915 0.8023 0.7668 -0.4287 -0.0560 0.1018  287 PRO A CD  
1027 N N   . ARG A 162 ? 0.9168 0.5883 0.6336 -0.3507 -0.0406 0.0925  288 ARG A N   
1028 C CA  . ARG A 162 ? 0.9451 0.5651 0.6425 -0.3122 -0.0380 0.0833  288 ARG A CA  
1029 C C   . ARG A 162 ? 0.8826 0.5566 0.6072 -0.2765 -0.0263 0.0823  288 ARG A C   
1030 O O   . ARG A 162 ? 0.8871 0.5394 0.6020 -0.2544 -0.0211 0.0877  288 ARG A O   
1031 C CB  . ARG A 162 ? 0.9532 0.5262 0.6316 -0.3022 -0.0468 0.0619  288 ARG A CB  
1032 C CG  . ARG A 162 ? 1.0511 0.5482 0.6924 -0.3151 -0.0563 0.0584  288 ARG A CG  
1033 C CD  . ARG A 162 ? 1.1084 0.5898 0.7380 -0.3210 -0.0661 0.0387  288 ARG A CD  
1034 N NE  . ARG A 162 ? 1.1690 0.5837 0.7645 -0.3240 -0.0732 0.0323  288 ARG A NE  
1035 C CZ  . ARG A 162 ? 1.1369 0.5025 0.7079 -0.3028 -0.0750 0.0138  288 ARG A CZ  
1036 N NH1 . ARG A 162 ? 1.1342 0.5094 0.7101 -0.2769 -0.0704 -0.0003 288 ARG A NH1 
1037 N NH2 . ARG A 162 ? 1.2182 0.5250 0.7587 -0.3076 -0.0808 0.0094  288 ARG A NH2 
1038 N N   . VAL A 163 ? 0.8330 0.5757 0.5903 -0.2705 -0.0232 0.0759  289 VAL A N   
1039 C CA  . VAL A 163 ? 0.8235 0.6116 0.6034 -0.2380 -0.0128 0.0739  289 VAL A CA  
1040 C C   . VAL A 163 ? 0.7920 0.6096 0.5776 -0.2426 -0.0025 0.0911  289 VAL A C   
1041 O O   . VAL A 163 ? 0.7751 0.5938 0.5591 -0.2173 0.0041  0.0923  289 VAL A O   
1042 C CB  . VAL A 163 ? 0.7261 0.5756 0.5373 -0.2305 -0.0125 0.0642  289 VAL A CB  
1043 C CG1 . VAL A 163 ? 0.7177 0.6050 0.5479 -0.1979 -0.0023 0.0616  289 VAL A CG1 
1044 C CG2 . VAL A 163 ? 0.7872 0.6050 0.5869 -0.2264 -0.0224 0.0479  289 VAL A CG2 
1045 N N   . LYS A 164 ? 0.8043 0.6478 0.5955 -0.2762 -0.0012 0.1050  290 LYS A N   
1046 C CA  . LYS A 164 ? 0.7608 0.6317 0.5530 -0.2833 0.0102  0.1225  290 LYS A CA  
1047 C C   . LYS A 164 ? 0.8095 0.6166 0.5671 -0.2749 0.0094  0.1308  290 LYS A C   
1048 O O   . LYS A 164 ? 0.7876 0.6089 0.5428 -0.2566 0.0178  0.1364  290 LYS A O   
1049 C CB  . LYS A 164 ? 0.8767 0.7787 0.6776 -0.3259 0.0110  0.1377  290 LYS A CB  
1050 C CG  . LYS A 164 ? 0.8629 0.8375 0.6850 -0.3307 0.0275  0.1518  290 LYS A CG  
1051 C CD  . LYS A 164 ? 0.8898 0.8387 0.6847 -0.3272 0.0359  0.1662  290 LYS A CD  
1052 C CE  . LYS A 164 ? 0.9938 0.9506 0.7841 -0.3599 0.0385  0.1843  290 LYS A CE  
1053 N NZ  . LYS A 164 ? 0.9593 1.0039 0.7888 -0.3732 0.0482  0.1880  290 LYS A NZ  
1054 N N   . ALA A 165 ? 0.8114 0.5458 0.5401 -0.2875 -0.0016 0.1316  291 ALA A N   
1055 C CA  . ALA A 165 ? 0.9035 0.5735 0.5992 -0.2781 -0.0041 0.1411  291 ALA A CA  
1056 C C   . ALA A 165 ? 0.8659 0.5307 0.5639 -0.2350 -0.0027 0.1307  291 ALA A C   
1057 O O   . ALA A 165 ? 0.8484 0.5022 0.5333 -0.2216 -0.0002 0.1413  291 ALA A O   
1058 C CB  . ALA A 165 ? 0.9536 0.5438 0.6193 -0.2936 -0.0166 0.1397  291 ALA A CB  
1059 N N   . LEU A 166 ? 0.8415 0.5157 0.5554 -0.2144 -0.0049 0.1109  292 LEU A N   
1060 C CA  . LEU A 166 ? 0.8265 0.5045 0.5474 -0.1766 -0.0031 0.1013  292 LEU A CA  
1061 C C   . LEU A 166 ? 0.7649 0.5049 0.5050 -0.1659 0.0066  0.1046  292 LEU A C   
1062 O O   . LEU A 166 ? 0.7497 0.4857 0.4841 -0.1446 0.0076  0.1072  292 LEU A O   
1063 C CB  . LEU A 166 ? 0.8079 0.4856 0.5409 -0.1609 -0.0063 0.0809  292 LEU A CB  
1064 C CG  . LEU A 166 ? 0.8568 0.4708 0.5672 -0.1663 -0.0147 0.0728  292 LEU A CG  
1065 C CD1 . LEU A 166 ? 0.8128 0.4374 0.5349 -0.1512 -0.0156 0.0531  292 LEU A CD1 
1066 C CD2 . LEU A 166 ? 0.8862 0.4355 0.5705 -0.1501 -0.0184 0.0782  292 LEU A CD2 
1067 N N   . ALA A 167 ? 0.7540 0.5517 0.5165 -0.1794 0.0132  0.1040  293 ALA A N   
1068 C CA  . ALA A 167 ? 0.7042 0.5579 0.4825 -0.1670 0.0238  0.1048  293 ALA A CA  
1069 C C   . ALA A 167 ? 0.7141 0.5646 0.4723 -0.1751 0.0293  0.1224  293 ALA A C   
1070 O O   . ALA A 167 ? 0.7319 0.5980 0.4867 -0.1563 0.0342  0.1222  293 ALA A O   
1071 C CB  . ALA A 167 ? 0.6762 0.5924 0.4836 -0.1780 0.0302  0.1015  293 ALA A CB  
1072 N N   . LEU A 168 ? 0.7389 0.5658 0.4801 -0.2042 0.0278  0.1381  294 LEU A N   
1073 C CA  . LEU A 168 ? 0.7559 0.5747 0.4730 -0.2137 0.0326  0.1574  294 LEU A CA  
1074 C C   . LEU A 168 ? 0.8096 0.5775 0.5018 -0.1909 0.0245  0.1599  294 LEU A C   
1075 O O   . LEU A 168 ? 0.8000 0.5767 0.4774 -0.1834 0.0285  0.1692  294 LEU A O   
1076 C CB  . LEU A 168 ? 0.7944 0.5924 0.4971 -0.2525 0.0315  0.1751  294 LEU A CB  
1077 N N   . LEU A 169 ? 0.8072 0.5232 0.4939 -0.1792 0.0131  0.1520  295 LEU A N   
1078 C CA  . LEU A 169 ? 0.8105 0.4858 0.4806 -0.1537 0.0049  0.1539  295 LEU A CA  
1079 C C   . LEU A 169 ? 0.8045 0.5185 0.4913 -0.1251 0.0075  0.1419  295 LEU A C   
1080 O O   . LEU A 169 ? 0.7753 0.4838 0.4485 -0.1110 0.0043  0.1491  295 LEU A O   
1081 C CB  . LEU A 169 ? 0.8400 0.4566 0.5038 -0.1446 -0.0054 0.1460  295 LEU A CB  
1082 C CG  . LEU A 169 ? 0.9125 0.4648 0.5485 -0.1667 -0.0120 0.1580  295 LEU A CG  
1083 C CD1 . LEU A 169 ? 0.9304 0.4277 0.5607 -0.1490 -0.0203 0.1448  295 LEU A CD1 
1084 C CD2 . LEU A 169 ? 0.8883 0.4113 0.4955 -0.1723 -0.0149 0.1817  295 LEU A CD2 
1085 N N   . ALA A 170 ? 0.7203 0.4712 0.4349 -0.1172 0.0116  0.1241  296 ALA A N   
1086 C CA  . ALA A 170 ? 0.7180 0.5053 0.4472 -0.0942 0.0145  0.1131  296 ALA A CA  
1087 C C   . ALA A 170 ? 0.6891 0.5138 0.4105 -0.0992 0.0236  0.1207  296 ALA A C   
1088 O O   . ALA A 170 ? 0.6891 0.5210 0.4031 -0.0829 0.0222  0.1192  296 ALA A O   
1089 C CB  . ALA A 170 ? 0.6428 0.4597 0.4005 -0.0878 0.0175  0.0951  296 ALA A CB  
1090 N N   . LYS A 171 ? 0.7005 0.5509 0.4227 -0.1224 0.0333  0.1286  297 LYS A N   
1091 C CA  . LYS A 171 ? 0.7026 0.5884 0.4139 -0.1277 0.0446  0.1368  297 LYS A CA  
1092 C C   . LYS A 171 ? 0.7377 0.5909 0.4142 -0.1278 0.0394  0.1530  297 LYS A C   
1093 O O   . LYS A 171 ? 0.7381 0.6083 0.4008 -0.1168 0.0427  0.1528  297 LYS A O   
1094 C CB  . LYS A 171 ? 0.7118 0.6319 0.4317 -0.1550 0.0563  0.1457  297 LYS A CB  
1095 C CG  . LYS A 171 ? 0.7238 0.6741 0.4254 -0.1642 0.0698  0.1588  297 LYS A CG  
1096 C CD  . LYS A 171 ? 0.7566 0.7568 0.4753 -0.1884 0.0842  0.1660  297 LYS A CD  
1097 C CE  . LYS A 171 ? 0.7476 0.7847 0.4487 -0.1919 0.1010  0.1758  297 LYS A CE  
1098 N NZ  . LYS A 171 ? 0.8092 0.8915 0.5251 -0.2185 0.1149  0.1880  297 LYS A NZ  
1099 N N   . ASN A 172 ? 0.7709 0.5737 0.4299 -0.1397 0.0302  0.1669  298 ASN A N   
1100 C CA  . ASN A 172 ? 0.8161 0.5842 0.4406 -0.1393 0.0234  0.1852  298 ASN A CA  
1101 C C   . ASN A 172 ? 0.7973 0.5601 0.4183 -0.1100 0.0137  0.1779  298 ASN A C   
1102 O O   . ASN A 172 ? 0.8616 0.6231 0.4565 -0.1068 0.0113  0.1891  298 ASN A O   
1103 C CB  . ASN A 172 ? 0.8945 0.6000 0.5024 -0.1516 0.0129  0.1992  298 ASN A CB  
1104 C CG  . ASN A 172 ? 0.9732 0.6776 0.5714 -0.1871 0.0204  0.2149  298 ASN A CG  
1105 O OD1 . ASN A 172 ? 1.0397 0.7883 0.6378 -0.1995 0.0329  0.2212  298 ASN A OD1 
1106 N ND2 . ASN A 172 ? 1.0020 0.6632 0.6018 -0.1985 0.0129  0.2157  298 ASN A ND2 
1107 N N   . TYR A 173 ? 0.8016 0.5624 0.4474 -0.0901 0.0076  0.1603  299 TYR A N   
1108 C CA  . TYR A 173 ? 0.7799 0.5401 0.4280 -0.0647 -0.0023 0.1532  299 TYR A CA  
1109 C C   . TYR A 173 ? 0.7616 0.5682 0.4245 -0.0545 0.0043  0.1360  299 TYR A C   
1110 O O   . TYR A 173 ? 0.7745 0.5847 0.4376 -0.0373 -0.0041 0.1301  299 TYR A O   
1111 C CB  . TYR A 173 ? 0.7685 0.4984 0.4342 -0.0484 -0.0125 0.1456  299 TYR A CB  
1112 C CG  . TYR A 173 ? 0.7893 0.4635 0.4372 -0.0509 -0.0214 0.1610  299 TYR A CG  
1113 C CD1 . TYR A 173 ? 0.8374 0.4857 0.4632 -0.0412 -0.0328 0.1773  299 TYR A CD1 
1114 C CD2 . TYR A 173 ? 0.8407 0.4852 0.4922 -0.0618 -0.0196 0.1586  299 TYR A CD2 
1115 C CE1 . TYR A 173 ? 0.9043 0.4969 0.5128 -0.0405 -0.0413 0.1917  299 TYR A CE1 
1116 C CE2 . TYR A 173 ? 0.8863 0.4722 0.5180 -0.0629 -0.0278 0.1712  299 TYR A CE2 
1117 C CZ  . TYR A 173 ? 0.9001 0.4591 0.5108 -0.0511 -0.0381 0.1880  299 TYR A CZ  
1118 O OH  . TYR A 173 ? 0.9308 0.4327 0.5256 -0.0488 -0.0459 0.1991  299 TYR A OH  
1119 N N   . ASP A 174 ? 0.6979 0.5392 0.3733 -0.0648 0.0184  0.1282  300 ASP A N   
1120 C CA  . ASP A 174 ? 0.6384 0.5190 0.3284 -0.0536 0.0257  0.1107  300 ASP A CA  
1121 C C   . ASP A 174 ? 0.6513 0.5267 0.3649 -0.0349 0.0172  0.0950  300 ASP A C   
1122 O O   . ASP A 174 ? 0.6458 0.5297 0.3591 -0.0209 0.0128  0.0859  300 ASP A O   
1123 C CB  . ASP A 174 ? 0.6899 0.5854 0.3531 -0.0497 0.0284  0.1126  300 ASP A CB  
1124 C CG  . ASP A 174 ? 0.7240 0.6588 0.3964 -0.0425 0.0409  0.0959  300 ASP A CG  
1125 O OD1 . ASP A 174 ? 0.7089 0.6678 0.4040 -0.0475 0.0519  0.0906  300 ASP A OD1 
1126 O OD2 . ASP A 174 ? 0.7649 0.7050 0.4218 -0.0313 0.0388  0.0878  300 ASP A OD2 
1127 N N   . ILE A 175 ? 0.6166 0.4774 0.3492 -0.0364 0.0149  0.0919  301 ILE A N   
1128 C CA  . ILE A 175 ? 0.5871 0.4479 0.3434 -0.0214 0.0103  0.0773  301 ILE A CA  
1129 C C   . ILE A 175 ? 0.6078 0.4908 0.3853 -0.0269 0.0187  0.0673  301 ILE A C   
1130 O O   . ILE A 175 ? 0.5901 0.4833 0.3674 -0.0435 0.0256  0.0728  301 ILE A O   
1131 C CB  . ILE A 175 ? 0.6048 0.4282 0.3629 -0.0141 -0.0002 0.0809  301 ILE A CB  
1132 C CG1 . ILE A 175 ? 0.6443 0.4434 0.3995 -0.0288 0.0017  0.0862  301 ILE A CG1 
1133 C CG2 . ILE A 175 ? 0.6238 0.4270 0.3617 -0.0080 -0.0099 0.0940  301 ILE A CG2 
1134 C CD1 . ILE A 175 ? 0.6582 0.4177 0.4149 -0.0183 -0.0062 0.0854  301 ILE A CD1 
1135 N N   . GLY A 176 ? 0.5347 0.4269 0.3311 -0.0137 0.0172  0.0536  302 GLY A N   
1136 C CA  . GLY A 176 ? 0.5664 0.4768 0.3827 -0.0164 0.0224  0.0449  302 GLY A CA  
1137 C C   . GLY A 176 ? 0.5462 0.4333 0.3656 -0.0255 0.0189  0.0468  302 GLY A C   
1138 O O   . GLY A 176 ? 0.5322 0.3867 0.3456 -0.0201 0.0120  0.0484  302 GLY A O   
1139 N N   . LEU A 177 ? 0.5637 0.4685 0.3924 -0.0390 0.0233  0.0461  303 LEU A N   
1140 C CA  . LEU A 177 ? 0.5277 0.4127 0.3582 -0.0494 0.0192  0.0445  303 LEU A CA  
1141 C C   . LEU A 177 ? 0.5289 0.4447 0.3799 -0.0476 0.0212  0.0349  303 LEU A C   
1142 O O   . LEU A 177 ? 0.5236 0.4767 0.3859 -0.0547 0.0267  0.0368  303 LEU A O   
1143 C CB  . LEU A 177 ? 0.5626 0.4359 0.3806 -0.0739 0.0194  0.0564  303 LEU A CB  
1144 C CG  . LEU A 177 ? 0.6202 0.4640 0.4337 -0.0872 0.0132  0.0536  303 LEU A CG  
1145 C CD1 . LEU A 177 ? 0.6845 0.4829 0.4735 -0.1025 0.0091  0.0650  303 LEU A CD1 
1146 C CD2 . LEU A 177 ? 0.6772 0.5568 0.5070 -0.1042 0.0146  0.0514  303 LEU A CD2 
1147 N N   . ASN A 178 ? 0.4799 0.3825 0.3358 -0.0368 0.0171  0.0254  304 ASN A N   
1148 C CA  . ASN A 178 ? 0.4976 0.4255 0.3700 -0.0326 0.0174  0.0173  304 ASN A CA  
1149 C C   . ASN A 178 ? 0.5052 0.4197 0.3744 -0.0457 0.0123  0.0144  304 ASN A C   
1150 O O   . ASN A 178 ? 0.5374 0.4132 0.3917 -0.0463 0.0086  0.0121  304 ASN A O   
1151 C CB  . ASN A 178 ? 0.5124 0.4373 0.3903 -0.0123 0.0170  0.0094  304 ASN A CB  
1152 C CG  . ASN A 178 ? 0.4876 0.4298 0.3778 -0.0081 0.0161  0.0028  304 ASN A CG  
1153 O OD1 . ASN A 178 ? 0.5056 0.4321 0.3921 -0.0093 0.0128  -0.0016 304 ASN A OD1 
1154 N ND2 . ASN A 178 ? 0.4582 0.4312 0.3607 -0.0022 0.0194  0.0021  304 ASN A ND2 
1155 N N   . ILE A 179 ? 0.4667 0.4132 0.3489 -0.0557 0.0115  0.0144  305 ILE A N   
1156 C CA  . ILE A 179 ? 0.4755 0.4141 0.3541 -0.0687 0.0045  0.0104  305 ILE A CA  
1157 C C   . ILE A 179 ? 0.4360 0.3803 0.3205 -0.0529 0.0027  0.0016  305 ILE A C   
1158 O O   . ILE A 179 ? 0.4506 0.4299 0.3526 -0.0439 0.0042  0.0017  305 ILE A O   
1159 C CB  . ILE A 179 ? 0.4696 0.4444 0.3608 -0.0900 0.0022  0.0167  305 ILE A CB  
1160 C CG1 . ILE A 179 ? 0.5512 0.5169 0.4335 -0.1105 0.0040  0.0271  305 ILE A CG1 
1161 C CG2 . ILE A 179 ? 0.5171 0.4854 0.4033 -0.1033 -0.0078 0.0113  305 ILE A CG2 
1162 C CD1 . ILE A 179 ? 0.5585 0.5639 0.4558 -0.1352 0.0019  0.0347  305 ILE A CD1 
1163 N N   . ASP A 180 ? 0.4763 0.3849 0.3448 -0.0485 0.0002  -0.0056 306 ASP A N   
1164 C CA  . ASP A 180 ? 0.4496 0.3617 0.3199 -0.0360 -0.0006 -0.0126 306 ASP A CA  
1165 C C   . ASP A 180 ? 0.4721 0.4058 0.3454 -0.0479 -0.0079 -0.0136 306 ASP A C   
1166 O O   . ASP A 180 ? 0.4804 0.4170 0.3502 -0.0683 -0.0136 -0.0112 306 ASP A O   
1167 C CB  . ASP A 180 ? 0.4907 0.3622 0.3419 -0.0288 0.0006  -0.0200 306 ASP A CB  
1168 C CG  . ASP A 180 ? 0.5008 0.3582 0.3539 -0.0133 0.0063  -0.0184 306 ASP A CG  
1169 O OD1 . ASP A 180 ? 0.4910 0.3697 0.3581 -0.0069 0.0086  -0.0135 306 ASP A OD1 
1170 O OD2 . ASP A 180 ? 0.5535 0.3786 0.3933 -0.0068 0.0080  -0.0225 306 ASP A OD2 
1171 N N   . ALA A 181 ? 0.4355 0.3842 0.3149 -0.0361 -0.0088 -0.0160 307 ALA A N   
1172 C CA  . ALA A 181 ? 0.4698 0.4411 0.3519 -0.0440 -0.0173 -0.0157 307 ALA A CA  
1173 C C   . ALA A 181 ? 0.4926 0.4345 0.3495 -0.0463 -0.0209 -0.0239 307 ALA A C   
1174 O O   . ALA A 181 ? 0.4735 0.3959 0.3219 -0.0318 -0.0147 -0.0282 307 ALA A O   
1175 C CB  . ALA A 181 ? 0.4031 0.4083 0.3055 -0.0283 -0.0166 -0.0113 307 ALA A CB  
1176 N N   . GLU A 182 ? 0.4852 0.4254 0.3295 -0.0653 -0.0308 -0.0262 308 GLU A N   
1177 C CA  . GLU A 182 ? 0.5462 0.4564 0.3606 -0.0683 -0.0342 -0.0357 308 GLU A CA  
1178 C C   . GLU A 182 ? 0.5407 0.4781 0.3542 -0.0737 -0.0455 -0.0337 308 GLU A C   
1179 O O   . GLU A 182 ? 0.4804 0.4483 0.3129 -0.0602 -0.0453 -0.0268 308 GLU A O   
1180 C CB  . GLU A 182 ? 0.5788 0.4481 0.3675 -0.0858 -0.0369 -0.0429 308 GLU A CB  
1181 C CG  . GLU A 182 ? 0.6110 0.4499 0.3985 -0.0756 -0.0261 -0.0435 308 GLU A CG  
1182 C CD  . GLU A 182 ? 0.6590 0.4511 0.4204 -0.0909 -0.0288 -0.0491 308 GLU A CD  
1183 O OE1 . GLU A 182 ? 0.6974 0.4488 0.4290 -0.0873 -0.0273 -0.0607 308 GLU A OE1 
1184 O OE2 . GLU A 182 ? 0.6368 0.4307 0.4057 -0.1060 -0.0317 -0.0418 308 GLU A OE2 
1185 N N   . GLU A 183 ? 0.5831 0.5076 0.3726 -0.0932 -0.0565 -0.0396 309 GLU A N   
1186 C CA  . GLU A 183 ? 0.6167 0.5660 0.4014 -0.0983 -0.0692 -0.0373 309 GLU A CA  
1187 C C   . GLU A 183 ? 0.5675 0.5742 0.3895 -0.1013 -0.0779 -0.0242 309 GLU A C   
1188 O O   . GLU A 183 ? 0.5919 0.6175 0.4368 -0.1094 -0.0765 -0.0189 309 GLU A O   
1189 C CB  . GLU A 183 ? 0.6491 0.5717 0.3972 -0.1217 -0.0813 -0.0474 309 GLU A CB  
1190 C CG  . GLU A 183 ? 0.7590 0.6269 0.4646 -0.1152 -0.0728 -0.0621 309 GLU A CG  
1191 C CD  . GLU A 183 ? 0.8233 0.6479 0.5210 -0.1116 -0.0606 -0.0693 309 GLU A CD  
1192 O OE1 . GLU A 183 ? 0.7963 0.6254 0.5123 -0.1220 -0.0619 -0.0639 309 GLU A OE1 
1193 O OE2 . GLU A 183 ? 0.9061 0.6934 0.5793 -0.0975 -0.0491 -0.0794 309 GLU A OE2 
1194 N N   . ALA A 184 ? 0.6233 0.6587 0.4505 -0.0942 -0.0866 -0.0181 310 ALA A N   
1195 C CA  . ALA A 184 ? 0.5462 0.6385 0.4109 -0.0906 -0.0941 -0.0051 310 ALA A CA  
1196 C C   . ALA A 184 ? 0.5254 0.6481 0.4035 -0.1175 -0.1067 -0.0017 310 ALA A C   
1197 O O   . ALA A 184 ? 0.5115 0.6803 0.4269 -0.1161 -0.1060 0.0080  310 ALA A O   
1198 C CB  . ALA A 184 ? 0.5364 0.6475 0.3988 -0.0781 -0.1035 0.0014  310 ALA A CB  
1199 N N   . ASP A 185 ? 0.5570 0.6546 0.4046 -0.1427 -0.1176 -0.0098 311 ASP A N   
1200 C CA  . ASP A 185 ? 0.5902 0.7175 0.4489 -0.1731 -0.1328 -0.0059 311 ASP A CA  
1201 C C   . ASP A 185 ? 0.6289 0.7439 0.4958 -0.1888 -0.1243 -0.0063 311 ASP A C   
1202 O O   . ASP A 185 ? 0.6488 0.7817 0.5220 -0.2187 -0.1356 -0.0030 311 ASP A O   
1203 C CB  . ASP A 185 ? 0.6960 0.7989 0.5147 -0.1970 -0.1507 -0.0149 311 ASP A CB  
1204 C CG  . ASP A 185 ? 0.7279 0.7553 0.4971 -0.1988 -0.1422 -0.0320 311 ASP A CG  
1205 O OD1 . ASP A 185 ? 0.7918 0.7884 0.5617 -0.1871 -0.1247 -0.0356 311 ASP A OD1 
1206 O OD2 . ASP A 185 ? 0.8445 0.8441 0.5732 -0.2109 -0.1531 -0.0420 311 ASP A OD2 
1207 N N   . ARG A 186 ? 0.5921 0.6775 0.4582 -0.1709 -0.1057 -0.0090 312 ARG A N   
1208 C CA  . ARG A 186 ? 0.6243 0.6995 0.4983 -0.1824 -0.0969 -0.0067 312 ARG A CA  
1209 C C   . ARG A 186 ? 0.6092 0.7242 0.5211 -0.1629 -0.0834 0.0036  312 ARG A C   
1210 O O   . ARG A 186 ? 0.5780 0.6915 0.4978 -0.1715 -0.0753 0.0078  312 ARG A O   
1211 C CB  . ARG A 186 ? 0.6654 0.6683 0.5025 -0.1798 -0.0877 -0.0184 312 ARG A CB  
1212 C CG  . ARG A 186 ? 0.7310 0.6844 0.5239 -0.1974 -0.0983 -0.0316 312 ARG A CG  
1213 C CD  . ARG A 186 ? 0.8189 0.7665 0.6030 -0.2359 -0.1120 -0.0309 312 ARG A CD  
1214 N NE  . ARG A 186 ? 0.8148 0.8185 0.6175 -0.2543 -0.1296 -0.0239 312 ARG A NE  
1215 C CZ  . ARG A 186 ? 0.8517 0.8576 0.6452 -0.2911 -0.1468 -0.0240 312 ARG A CZ  
1216 N NH1 . ARG A 186 ? 0.9753 0.9233 0.7368 -0.3149 -0.1488 -0.0316 312 ARG A NH1 
1217 N NH2 . ARG A 186 ? 0.8421 0.9088 0.6586 -0.3048 -0.1634 -0.0158 312 ARG A NH2 
1218 N N   . LEU A 187 ? 0.5405 0.6878 0.4724 -0.1371 -0.0810 0.0076  313 LEU A N   
1219 C CA  . LEU A 187 ? 0.5250 0.7075 0.4892 -0.1167 -0.0684 0.0153  313 LEU A CA  
1220 C C   . LEU A 187 ? 0.5577 0.7922 0.5525 -0.1342 -0.0689 0.0256  313 LEU A C   
1221 O O   . LEU A 187 ? 0.5153 0.7556 0.5208 -0.1317 -0.0557 0.0292  313 LEU A O   
1222 C CB  . LEU A 187 ? 0.4983 0.7062 0.4770 -0.0893 -0.0697 0.0184  313 LEU A CB  
1223 C CG  . LEU A 187 ? 0.5140 0.7423 0.5164 -0.0613 -0.0560 0.0224  313 LEU A CG  
1224 C CD1 . LEU A 187 ? 0.4559 0.6764 0.4550 -0.0351 -0.0571 0.0219  313 LEU A CD1 
1225 C CD2 . LEU A 187 ? 0.5085 0.8013 0.5491 -0.0621 -0.0549 0.0324  313 LEU A CD2 
1226 N N   . GLU A 188 ? 0.5130 0.7887 0.5220 -0.1529 -0.0844 0.0313  314 GLU A N   
1227 C CA  . GLU A 188 ? 0.5446 0.8822 0.5894 -0.1698 -0.0850 0.0431  314 GLU A CA  
1228 C C   . GLU A 188 ? 0.5347 0.8480 0.5676 -0.1986 -0.0798 0.0440  314 GLU A C   
1229 O O   . GLU A 188 ? 0.5458 0.8955 0.6032 -0.2026 -0.0687 0.0532  314 GLU A O   
1230 C CB  . GLU A 188 ? 0.5620 0.9478 0.6233 -0.1879 -0.1058 0.0493  314 GLU A CB  
1231 C CG  . GLU A 188 ? 0.6137 1.0410 0.6973 -0.1589 -0.1114 0.0542  314 GLU A CG  
1232 C CD  . GLU A 188 ? 0.6256 1.1263 0.7591 -0.1414 -0.1020 0.0661  314 GLU A CD  
1233 O OE1 . GLU A 188 ? 0.6306 1.1611 0.7840 -0.1581 -0.0933 0.0720  314 GLU A OE1 
1234 O OE2 . GLU A 188 ? 0.6203 1.1476 0.7718 -0.1102 -0.1027 0.0698  314 GLU A OE2 
1235 N N   . LEU A 189 ? 0.5626 0.8139 0.5562 -0.2191 -0.0874 0.0351  315 LEU A N   
1236 C CA  . LEU A 189 ? 0.6021 0.8207 0.5799 -0.2462 -0.0839 0.0367  315 LEU A CA  
1237 C C   . LEU A 189 ? 0.6164 0.8102 0.5902 -0.2259 -0.0641 0.0373  315 LEU A C   
1238 O O   . LEU A 189 ? 0.5753 0.7843 0.5598 -0.2387 -0.0554 0.0468  315 LEU A O   
1239 C CB  . LEU A 189 ? 0.6650 0.8140 0.5973 -0.2670 -0.0960 0.0250  315 LEU A CB  
1240 N N   . SER A 190 ? 0.5943 0.7521 0.5524 -0.1954 -0.0571 0.0281  316 SER A N   
1241 C CA  . SER A 190 ? 0.5811 0.7169 0.5348 -0.1763 -0.0409 0.0284  316 SER A CA  
1242 C C   . SER A 190 ? 0.5722 0.7676 0.5604 -0.1625 -0.0291 0.0377  316 SER A C   
1243 O O   . SER A 190 ? 0.5572 0.7478 0.5441 -0.1603 -0.0168 0.0422  316 SER A O   
1244 C CB  . SER A 190 ? 0.5679 0.6613 0.5022 -0.1482 -0.0373 0.0174  316 SER A CB  
1245 O OG  . SER A 190 ? 0.5022 0.6301 0.4553 -0.1257 -0.0377 0.0168  316 SER A OG  
1246 N N   . LEU A 191 ? 0.5164 0.7675 0.5337 -0.1526 -0.0328 0.0408  317 LEU A N   
1247 C CA  . LEU A 191 ? 0.5324 0.8397 0.5818 -0.1347 -0.0204 0.0478  317 LEU A CA  
1248 C C   . LEU A 191 ? 0.5057 0.8577 0.5752 -0.1598 -0.0153 0.0600  317 LEU A C   
1249 O O   . LEU A 191 ? 0.4912 0.8642 0.5703 -0.1506 0.0008  0.0647  317 LEU A O   
1250 C CB  . LEU A 191 ? 0.5255 0.8769 0.6001 -0.1146 -0.0268 0.0484  317 LEU A CB  
1251 C CG  . LEU A 191 ? 0.5158 0.9042 0.6142 -0.0819 -0.0130 0.0502  317 LEU A CG  
1252 C CD1 . LEU A 191 ? 0.4290 0.7674 0.5035 -0.0607 -0.0006 0.0418  317 LEU A CD1 
1253 C CD2 . LEU A 191 ? 0.4607 0.8784 0.5775 -0.0616 -0.0225 0.0510  317 LEU A CD2 
1254 N N   . ASP A 192 ? 0.4676 0.8357 0.5423 -0.1932 -0.0287 0.0655  318 ASP A N   
1255 C CA  . ASP A 192 ? 0.5434 0.9503 0.6351 -0.2232 -0.0243 0.0785  318 ASP A CA  
1256 C C   . ASP A 192 ? 0.5660 0.9183 0.6266 -0.2368 -0.0151 0.0801  318 ASP A C   
1257 O O   . ASP A 192 ? 0.5652 0.9472 0.6371 -0.2484 -0.0028 0.0914  318 ASP A O   
1258 C CB  . ASP A 192 ? 0.5657 0.9956 0.6665 -0.2600 -0.0437 0.0835  318 ASP A CB  
1259 C CG  . ASP A 192 ? 0.5569 1.0445 0.6888 -0.2470 -0.0554 0.0842  318 ASP A CG  
1260 O OD1 . ASP A 192 ? 0.5469 1.0643 0.6988 -0.2098 -0.0460 0.0832  318 ASP A OD1 
1261 O OD2 . ASP A 192 ? 0.5953 1.0952 0.7292 -0.2739 -0.0751 0.0858  318 ASP A OD2 
1262 N N   . LEU A 193 ? 0.6029 0.8774 0.6245 -0.2337 -0.0204 0.0696  319 LEU A N   
1263 C CA  . LEU A 193 ? 0.6061 0.8241 0.5971 -0.2402 -0.0129 0.0713  319 LEU A CA  
1264 C C   . LEU A 193 ? 0.5625 0.7917 0.5577 -0.2124 0.0052  0.0730  319 LEU A C   
1265 O O   . LEU A 193 ? 0.5715 0.7981 0.5592 -0.2229 0.0152  0.0826  319 LEU A O   
1266 C CB  . LEU A 193 ? 0.6441 0.7824 0.5969 -0.2355 -0.0219 0.0586  319 LEU A CB  
1267 C CG  . LEU A 193 ? 0.7105 0.7841 0.6299 -0.2441 -0.0184 0.0609  319 LEU A CG  
1268 C CD1 . LEU A 193 ? 0.7555 0.8227 0.6679 -0.2864 -0.0251 0.0714  319 LEU A CD1 
1269 C CD2 . LEU A 193 ? 0.7302 0.7331 0.6173 -0.2286 -0.0239 0.0470  319 LEU A CD2 
1270 N N   . LEU A 194 ? 0.5402 0.7780 0.5434 -0.1778 0.0088  0.0639  320 LEU A N   
1271 C CA  . LEU A 194 ? 0.5355 0.7823 0.5401 -0.1515 0.0244  0.0633  320 LEU A CA  
1272 C C   . LEU A 194 ? 0.5393 0.8536 0.5709 -0.1557 0.0376  0.0742  320 LEU A C   
1273 O O   . LEU A 194 ? 0.5322 0.8471 0.5546 -0.1510 0.0514  0.0784  320 LEU A O   
1274 C CB  . LEU A 194 ? 0.5010 0.7450 0.5102 -0.1172 0.0239  0.0517  320 LEU A CB  
1275 C CG  . LEU A 194 ? 0.4845 0.7326 0.4925 -0.0887 0.0376  0.0480  320 LEU A CG  
1276 C CD1 . LEU A 194 ? 0.4856 0.6758 0.4617 -0.0865 0.0391  0.0451  320 LEU A CD1 
1277 C CD2 . LEU A 194 ? 0.4351 0.6926 0.4547 -0.0598 0.0357  0.0392  320 LEU A CD2 
1278 N N   . GLU A 195 ? 0.4717 0.8462 0.5366 -0.1642 0.0338  0.0793  321 GLU A N   
1279 C CA  . GLU A 195 ? 0.4675 0.9152 0.5632 -0.1658 0.0481  0.0898  321 GLU A CA  
1280 C C   . GLU A 195 ? 0.5142 0.9637 0.6010 -0.2004 0.0544  0.1036  321 GLU A C   
1281 O O   . GLU A 195 ? 0.4844 0.9628 0.5742 -0.1963 0.0725  0.1105  321 GLU A O   
1282 C CB  . GLU A 195 ? 0.4529 0.9688 0.5900 -0.1677 0.0404  0.0938  321 GLU A CB  
1283 C CG  . GLU A 195 ? 0.4307 1.0312 0.6058 -0.1632 0.0569  0.1042  321 GLU A CG  
1284 C CD  . GLU A 195 ? 0.4497 1.1229 0.6700 -0.1621 0.0478  0.1094  321 GLU A CD  
1285 O OE1 . GLU A 195 ? 0.4862 1.1476 0.7066 -0.1804 0.0264  0.1089  321 GLU A OE1 
1286 O OE2 . GLU A 195 ? 0.5024 1.2452 0.7574 -0.1418 0.0619  0.1139  321 GLU A OE2 
1287 N N   . VAL A 196 ? 0.5265 0.9423 0.5989 -0.2352 0.0399  0.1080  322 VAL A N   
1288 C CA  . VAL A 196 ? 0.5036 0.9117 0.5633 -0.2707 0.0445  0.1225  322 VAL A CA  
1289 C C   . VAL A 196 ? 0.5613 0.9167 0.5851 -0.2589 0.0554  0.1225  322 VAL A C   
1290 O O   . VAL A 196 ? 0.5741 0.9483 0.5940 -0.2707 0.0694  0.1352  322 VAL A O   
1291 C CB  . VAL A 196 ? 0.5485 0.9167 0.5933 -0.3094 0.0248  0.1249  322 VAL A CB  
1292 C CG1 . VAL A 196 ? 0.5658 0.9095 0.5899 -0.3460 0.0286  0.1404  322 VAL A CG1 
1293 C CG2 . VAL A 196 ? 0.5327 0.9633 0.6146 -0.3263 0.0130  0.1276  322 VAL A CG2 
1294 N N   . LEU A 197 ? 0.5865 0.8785 0.5837 -0.2357 0.0491  0.1091  323 LEU A N   
1295 C CA  . LEU A 197 ? 0.6101 0.8534 0.5743 -0.2238 0.0565  0.1095  323 LEU A CA  
1296 C C   . LEU A 197 ? 0.5955 0.8809 0.5680 -0.1991 0.0750  0.1095  323 LEU A C   
1297 O O   . LEU A 197 ? 0.5976 0.8746 0.5500 -0.2036 0.0856  0.1184  323 LEU A O   
1298 C CB  . LEU A 197 ? 0.6133 0.7902 0.5540 -0.2030 0.0456  0.0953  323 LEU A CB  
1299 C CG  . LEU A 197 ? 0.6276 0.7434 0.5460 -0.2236 0.0299  0.0939  323 LEU A CG  
1300 C CD1 . LEU A 197 ? 0.6572 0.7178 0.5562 -0.1974 0.0235  0.0798  323 LEU A CD1 
1301 C CD2 . LEU A 197 ? 0.6719 0.7539 0.5658 -0.2520 0.0306  0.1087  323 LEU A CD2 
1302 N N   . CYS A 198 ? 0.5647 0.8912 0.5627 -0.1720 0.0789  0.0995  324 CYS A N   
1303 C CA  . CYS A 198 ? 0.5619 0.9204 0.5631 -0.1453 0.0965  0.0963  324 CYS A CA  
1304 C C   . CYS A 198 ? 0.5426 0.9675 0.5623 -0.1597 0.1135  0.1099  324 CYS A C   
1305 O O   . CYS A 198 ? 0.5437 0.9868 0.5546 -0.1440 0.1308  0.1096  324 CYS A O   
1306 C CB  . CYS A 198 ? 0.5040 0.8806 0.5250 -0.1115 0.0951  0.0818  324 CYS A CB  
1307 S SG  . CYS A 198 ? 0.5331 0.8344 0.5284 -0.0918 0.0805  0.0667  324 CYS A SG  
1308 N N   . LEU A 199 ? 0.5426 1.0041 0.5860 -0.1908 0.1093  0.1219  325 LEU A N   
1309 C CA  . LEU A 199 ? 0.5161 1.0439 0.5792 -0.2110 0.1253  0.1379  325 LEU A CA  
1310 C C   . LEU A 199 ? 0.5487 1.0373 0.5829 -0.2450 0.1235  0.1520  325 LEU A C   
1311 O O   . LEU A 199 ? 0.5335 1.0549 0.5777 -0.2576 0.1317  0.1618  325 LEU A O   
1312 C CB  . LEU A 199 ? 0.5095 1.0983 0.6186 -0.2207 0.1175  0.1410  325 LEU A CB  
1313 C CG  . LEU A 199 ? 0.5140 1.1466 0.6550 -0.1846 0.1188  0.1294  325 LEU A CG  
1314 C CD1 . LEU A 199 ? 0.5014 1.1879 0.6844 -0.1959 0.1064  0.1341  325 LEU A CD1 
1315 C CD2 . LEU A 199 ? 0.5281 1.1869 0.6706 -0.1484 0.1400  0.1230  325 LEU A CD2 
1316 N N   . ASP A 200 ? 0.5805 0.9935 0.5783 -0.2563 0.1115  0.1520  326 ASP A N   
1317 C CA  . ASP A 200 ? 0.6169 0.9848 0.5849 -0.2870 0.1081  0.1662  326 ASP A CA  
1318 C C   . ASP A 200 ? 0.6619 1.0160 0.6010 -0.2728 0.1228  0.1701  326 ASP A C   
1319 O O   . ASP A 200 ? 0.6601 0.9888 0.5775 -0.2474 0.1262  0.1617  326 ASP A O   
1320 C CB  . ASP A 200 ? 0.6893 0.9752 0.6284 -0.2992 0.0883  0.1631  326 ASP A CB  
1321 C CG  . ASP A 200 ? 0.7642 1.0020 0.6771 -0.3332 0.0811  0.1776  326 ASP A CG  
1322 O OD1 . ASP A 200 ? 0.8083 1.0558 0.7122 -0.3380 0.0917  0.1885  326 ASP A OD1 
1323 O OD2 . ASP A 200 ? 0.8277 1.0131 0.7273 -0.3516 0.0640  0.1758  326 ASP A OD2 
1324 N N   . GLY A 201 ? 0.6748 1.0448 0.6120 -0.2899 0.1306  0.1828  327 GLY A N   
1325 C CA  . GLY A 201 ? 0.6714 1.0323 0.5805 -0.2791 0.1446  0.1877  327 GLY A CA  
1326 C C   . GLY A 201 ? 0.7411 1.0220 0.6030 -0.2834 0.1353  0.1933  327 GLY A C   
1327 O O   . GLY A 201 ? 0.7681 1.0351 0.6023 -0.2675 0.1438  0.1940  327 GLY A O   
1328 N N   . ASP A 202 ? 0.7521 0.9780 0.6029 -0.3031 0.1170  0.1967  328 ASP A N   
1329 C CA  . ASP A 202 ? 0.8099 0.9567 0.6175 -0.3026 0.1067  0.2017  328 ASP A CA  
1330 C C   . ASP A 202 ? 0.7808 0.9046 0.5714 -0.2713 0.1055  0.1898  328 ASP A C   
1331 O O   . ASP A 202 ? 0.7866 0.8573 0.5422 -0.2631 0.0998  0.1941  328 ASP A O   
1332 C CB  . ASP A 202 ? 0.8490 0.9375 0.6481 -0.3267 0.0875  0.2050  328 ASP A CB  
1333 C CG  . ASP A 202 ? 0.8835 0.9713 0.6829 -0.3594 0.0857  0.2196  328 ASP A CG  
1334 O OD1 . ASP A 202 ? 0.8832 1.0022 0.6810 -0.3636 0.0990  0.2305  328 ASP A OD1 
1335 O OD2 . ASP A 202 ? 0.9129 0.9665 0.7116 -0.3812 0.0710  0.2196  328 ASP A OD2 
1336 N N   . LEU A 203 ? 0.7457 0.9075 0.5632 -0.2495 0.1086  0.1732  329 LEU A N   
1337 C CA  . LEU A 203 ? 0.7049 0.8421 0.5155 -0.2123 0.1032  0.1549  329 LEU A CA  
1338 C C   . LEU A 203 ? 0.6660 0.8480 0.4784 -0.1873 0.1195  0.1471  329 LEU A C   
1339 O O   . LEU A 203 ? 0.6975 0.8684 0.5098 -0.1575 0.1158  0.1302  329 LEU A O   
1340 C CB  . LEU A 203 ? 0.6789 0.8109 0.5155 -0.2005 0.0910  0.1381  329 LEU A CB  
1341 C CG  . LEU A 203 ? 0.7181 0.8044 0.5502 -0.2241 0.0752  0.1423  329 LEU A CG  
1342 C CD1 . LEU A 203 ? 0.6560 0.7494 0.5139 -0.2147 0.0655  0.1261  329 LEU A CD1 
1343 C CD2 . LEU A 203 ? 0.7047 0.7153 0.5003 -0.2200 0.0645  0.1457  329 LEU A CD2 
1344 N N   . SER A 204 ? 0.7189 0.9493 0.5311 -0.1993 0.1379  0.1587  330 SER A N   
1345 C CA  . SER A 204 ? 0.6709 0.9448 0.4838 -0.1742 0.1554  0.1491  330 SER A CA  
1346 C C   . SER A 204 ? 0.6994 0.9292 0.4737 -0.1524 0.1513  0.1416  330 SER A C   
1347 O O   . SER A 204 ? 0.7482 0.9269 0.4906 -0.1624 0.1408  0.1520  330 SER A O   
1348 C CB  . SER A 204 ? 0.7033 1.0170 0.5234 -0.1848 0.1710  0.1588  330 SER A CB  
1349 N N   . GLY A 205 ? 0.6778 0.9254 0.4550 -0.1219 0.1580  0.1231  331 GLY A N   
1350 C CA  . GLY A 205 ? 0.6897 0.9018 0.4317 -0.1018 0.1538  0.1139  331 GLY A CA  
1351 C C   . GLY A 205 ? 0.7159 0.8741 0.4557 -0.0896 0.1317  0.1041  331 GLY A C   
1352 O O   . GLY A 205 ? 0.7538 0.8857 0.4688 -0.0730 0.1259  0.0954  331 GLY A O   
1353 N N   . TRP A 206 ? 0.6395 0.7822 0.4037 -0.0980 0.1194  0.1050  332 TRP A N   
1354 C CA  . TRP A 206 ? 0.6610 0.7567 0.4258 -0.0868 0.1005  0.0963  332 TRP A CA  
1355 C C   . TRP A 206 ? 0.6160 0.7297 0.4128 -0.0695 0.0990  0.0791  332 TRP A C   
1356 O O   . TRP A 206 ? 0.6125 0.7543 0.4375 -0.0781 0.1016  0.0801  332 TRP A O   
1357 C CB  . TRP A 206 ? 0.6560 0.7135 0.4181 -0.1075 0.0881  0.1092  332 TRP A CB  
1358 C CG  . TRP A 206 ? 0.6323 0.6495 0.4015 -0.0959 0.0716  0.0997  332 TRP A CG  
1359 C CD1 . TRP A 206 ? 0.6347 0.6182 0.3895 -0.0787 0.0611  0.0944  332 TRP A CD1 
1360 C CD2 . TRP A 206 ? 0.6407 0.6497 0.4322 -0.1017 0.0642  0.0952  332 TRP A CD2 
1361 N NE1 . TRP A 206 ? 0.6239 0.5811 0.3927 -0.0723 0.0497  0.0870  332 TRP A NE1 
1362 C CE2 . TRP A 206 ? 0.6211 0.5909 0.4098 -0.0859 0.0516  0.0867  332 TRP A CE2 
1363 C CE3 . TRP A 206 ? 0.6093 0.6427 0.4226 -0.1194 0.0667  0.0974  332 TRP A CE3 
1364 C CZ2 . TRP A 206 ? 0.6059 0.5576 0.4089 -0.0862 0.0433  0.0798  332 TRP A CZ2 
1365 C CZ3 . TRP A 206 ? 0.6163 0.6295 0.4423 -0.1209 0.0560  0.0903  332 TRP A CZ3 
1366 C CH2 . TRP A 206 ? 0.6228 0.5944 0.4420 -0.1036 0.0453  0.0811  332 TRP A CH2 
1367 N N   . ASN A 207 ? 0.6083 0.7055 0.3997 -0.0465 0.0936  0.0645  333 ASN A N   
1368 C CA  . ASN A 207 ? 0.5857 0.6948 0.4024 -0.0288 0.0920  0.0491  333 ASN A CA  
1369 C C   . ASN A 207 ? 0.5553 0.6279 0.3802 -0.0255 0.0756  0.0444  333 ASN A C   
1370 O O   . ASN A 207 ? 0.5627 0.6322 0.3986 -0.0088 0.0717  0.0317  333 ASN A O   
1371 C CB  . ASN A 207 ? 0.5658 0.6818 0.3705 -0.0064 0.0986  0.0353  333 ASN A CB  
1372 C CG  . ASN A 207 ? 0.5946 0.7560 0.4001 -0.0032 0.1182  0.0354  333 ASN A CG  
1373 O OD1 . ASN A 207 ? 0.5472 0.7474 0.3778 -0.0122 0.1266  0.0422  333 ASN A OD1 
1374 N ND2 . ASN A 207 ? 0.6188 0.7780 0.3966 0.0094  0.1259  0.0277  333 ASN A ND2 
1375 N N   . GLY A 208 ? 0.5509 0.5945 0.3693 -0.0408 0.0667  0.0545  334 GLY A N   
1376 C CA  . GLY A 208 ? 0.5404 0.5488 0.3631 -0.0360 0.0533  0.0501  334 GLY A CA  
1377 C C   . GLY A 208 ? 0.5122 0.5248 0.3572 -0.0423 0.0498  0.0472  334 GLY A C   
1378 O O   . GLY A 208 ? 0.5029 0.4884 0.3507 -0.0370 0.0406  0.0420  334 GLY A O   
1379 N N   . MET A 209 ? 0.4694 0.5174 0.3294 -0.0543 0.0568  0.0509  335 MET A N   
1380 C CA  . MET A 209 ? 0.4860 0.5414 0.3659 -0.0618 0.0515  0.0482  335 MET A CA  
1381 C C   . MET A 209 ? 0.4790 0.5417 0.3736 -0.0407 0.0490  0.0350  335 MET A C   
1382 O O   . MET A 209 ? 0.4560 0.5437 0.3575 -0.0250 0.0561  0.0295  335 MET A O   
1383 C CB  . MET A 209 ? 0.5263 0.6271 0.4234 -0.0793 0.0585  0.0560  335 MET A CB  
1384 C CG  . MET A 209 ? 0.5183 0.6220 0.4309 -0.0930 0.0494  0.0551  335 MET A CG  
1385 S SD  . MET A 209 ? 0.6974 0.7439 0.5852 -0.1175 0.0391  0.0624  335 MET A SD  
1386 C CE  . MET A 209 ? 0.6201 0.6421 0.5116 -0.1147 0.0264  0.0506  335 MET A CE  
1387 N N   . GLY A 210 ? 0.4476 0.4854 0.3442 -0.0402 0.0395  0.0301  336 GLY A N   
1388 C CA  . GLY A 210 ? 0.4335 0.4714 0.3400 -0.0222 0.0363  0.0196  336 GLY A CA  
1389 C C   . GLY A 210 ? 0.4148 0.4597 0.3336 -0.0296 0.0300  0.0178  336 GLY A C   
1390 O O   . GLY A 210 ? 0.4259 0.4604 0.3402 -0.0484 0.0255  0.0221  336 GLY A O   
1391 N N   . PHE A 211 ? 0.3717 0.4315 0.3033 -0.0151 0.0289  0.0115  337 PHE A N   
1392 C CA  . PHE A 211 ? 0.4127 0.4837 0.3548 -0.0213 0.0219  0.0106  337 PHE A CA  
1393 C C   . PHE A 211 ? 0.3672 0.4294 0.3113 -0.0035 0.0186  0.0036  337 PHE A C   
1394 O O   . PHE A 211 ? 0.4355 0.5045 0.3841 0.0137  0.0228  0.0007  337 PHE A O   
1395 C CB  . PHE A 211 ? 0.4172 0.5388 0.3809 -0.0274 0.0245  0.0164  337 PHE A CB  
1396 C CG  . PHE A 211 ? 0.4097 0.5462 0.3829 -0.0411 0.0146  0.0181  337 PHE A CG  
1397 C CD1 . PHE A 211 ? 0.4193 0.5476 0.3854 -0.0677 0.0092  0.0225  337 PHE A CD1 
1398 C CD2 . PHE A 211 ? 0.4121 0.5686 0.3988 -0.0286 0.0095  0.0159  337 PHE A CD2 
1399 C CE1 . PHE A 211 ? 0.4645 0.6064 0.4366 -0.0828 -0.0016 0.0233  337 PHE A CE1 
1400 C CE2 . PHE A 211 ? 0.3942 0.5669 0.3877 -0.0422 -0.0014 0.0182  337 PHE A CE2 
1401 C CZ  . PHE A 211 ? 0.4386 0.6046 0.4246 -0.0700 -0.0073 0.0212  337 PHE A CZ  
1402 N N   . VAL A 212 ? 0.4057 0.4507 0.3439 -0.0086 0.0111  0.0009  338 VAL A N   
1403 C CA  . VAL A 212 ? 0.3743 0.4107 0.3120 0.0053  0.0082  -0.0037 338 VAL A CA  
1404 C C   . VAL A 212 ? 0.3880 0.4560 0.3399 0.0064  0.0029  -0.0011 338 VAL A C   
1405 O O   . VAL A 212 ? 0.3991 0.4844 0.3553 -0.0093 -0.0027 0.0022  338 VAL A O   
1406 C CB  . VAL A 212 ? 0.4071 0.4077 0.3275 0.0013  0.0048  -0.0082 338 VAL A CB  
1407 C CG1 . VAL A 212 ? 0.4226 0.4169 0.3419 0.0142  0.0036  -0.0111 338 VAL A CG1 
1408 C CG2 . VAL A 212 ? 0.4417 0.4154 0.3517 0.0020  0.0090  -0.0090 338 VAL A CG2 
1409 N N   . VAL A 213 ? 0.3715 0.4461 0.3302 0.0243  0.0033  -0.0018 339 VAL A N   
1410 C CA  . VAL A 213 ? 0.3445 0.4425 0.3137 0.0289  -0.0039 0.0017  339 VAL A CA  
1411 C C   . VAL A 213 ? 0.3688 0.4401 0.3254 0.0380  -0.0072 -0.0004 339 VAL A C   
1412 O O   . VAL A 213 ? 0.3902 0.4383 0.3402 0.0478  -0.0020 -0.0036 339 VAL A O   
1413 C CB  . VAL A 213 ? 0.3768 0.5109 0.3673 0.0443  -0.0004 0.0053  339 VAL A CB  
1414 C CG1 . VAL A 213 ? 0.3792 0.5446 0.3841 0.0469  -0.0101 0.0115  339 VAL A CG1 
1415 C CG2 . VAL A 213 ? 0.4072 0.5663 0.4080 0.0366  0.0074  0.0072  339 VAL A CG2 
1416 N N   . GLN A 214 ? 0.3745 0.4502 0.3265 0.0327  -0.0162 0.0020  340 GLN A N   
1417 C CA  . GLN A 214 ? 0.3957 0.4469 0.3316 0.0371  -0.0190 0.0014  340 GLN A CA  
1418 C C   . GLN A 214 ? 0.4141 0.4801 0.3586 0.0522  -0.0243 0.0081  340 GLN A C   
1419 O O   . GLN A 214 ? 0.3668 0.4634 0.3225 0.0514  -0.0328 0.0138  340 GLN A O   
1420 C CB  . GLN A 214 ? 0.4302 0.4716 0.3478 0.0209  -0.0253 -0.0009 340 GLN A CB  
1421 C CG  . GLN A 214 ? 0.4142 0.4346 0.3205 0.0076  -0.0208 -0.0077 340 GLN A CG  
1422 C CD  . GLN A 214 ? 0.4473 0.4669 0.3405 -0.0116 -0.0292 -0.0101 340 GLN A CD  
1423 O OE1 . GLN A 214 ? 0.4478 0.4977 0.3524 -0.0207 -0.0380 -0.0055 340 GLN A OE1 
1424 N NE2 . GLN A 214 ? 0.4327 0.4181 0.3014 -0.0179 -0.0267 -0.0177 340 GLN A NE2 
1425 N N   . ALA A 215 ? 0.3813 0.4255 0.3210 0.0656  -0.0204 0.0084  341 ALA A N   
1426 C CA  . ALA A 215 ? 0.3956 0.4453 0.3411 0.0822  -0.0251 0.0152  341 ALA A CA  
1427 C C   . ALA A 215 ? 0.4313 0.4790 0.3642 0.0796  -0.0351 0.0224  341 ALA A C   
1428 O O   . ALA A 215 ? 0.4121 0.4686 0.3503 0.0932  -0.0420 0.0306  341 ALA A O   
1429 C CB  . ALA A 215 ? 0.4083 0.4287 0.3488 0.0945  -0.0189 0.0133  341 ALA A CB  
1430 N N   . TYR A 216 ? 0.3927 0.4280 0.3069 0.0642  -0.0361 0.0198  342 TYR A N   
1431 C CA  . TYR A 216 ? 0.4469 0.4845 0.3463 0.0615  -0.0465 0.0269  342 TYR A CA  
1432 C C   . TYR A 216 ? 0.4441 0.5186 0.3543 0.0559  -0.0590 0.0308  342 TYR A C   
1433 O O   . TYR A 216 ? 0.4537 0.5355 0.3527 0.0542  -0.0706 0.0380  342 TYR A O   
1434 C CB  . TYR A 216 ? 0.4764 0.4883 0.3477 0.0486  -0.0427 0.0223  342 TYR A CB  
1435 C CG  . TYR A 216 ? 0.4433 0.4519 0.3045 0.0320  -0.0404 0.0120  342 TYR A CG  
1436 C CD1 . TYR A 216 ? 0.4585 0.4875 0.3333 0.0234  -0.0445 0.0087  342 TYR A CD1 
1437 C CD2 . TYR A 216 ? 0.4730 0.4562 0.3100 0.0253  -0.0333 0.0059  342 TYR A CD2 
1438 C CE1 . TYR A 216 ? 0.4663 0.4838 0.3280 0.0075  -0.0431 -0.0003 342 TYR A CE1 
1439 C CE2 . TYR A 216 ? 0.4700 0.4430 0.2943 0.0129  -0.0310 -0.0044 342 TYR A CE2 
1440 C CZ  . TYR A 216 ? 0.4562 0.4427 0.2916 0.0036  -0.0365 -0.0075 342 TYR A CZ  
1441 O OH  . TYR A 216 ? 0.4691 0.4376 0.2881 -0.0095 -0.0352 -0.0173 342 TYR A OH  
1442 N N   . GLY A 217 ? 0.4023 0.5023 0.3336 0.0515  -0.0575 0.0274  343 GLY A N   
1443 C CA  . GLY A 217 ? 0.3963 0.5379 0.3428 0.0436  -0.0695 0.0323  343 GLY A CA  
1444 C C   . GLY A 217 ? 0.4502 0.6269 0.4247 0.0644  -0.0740 0.0422  343 GLY A C   
1445 O O   . GLY A 217 ? 0.4198 0.5937 0.4079 0.0821  -0.0640 0.0412  343 GLY A O   
1446 N N   . LYS A 218 ? 0.4441 0.6543 0.4263 0.0626  -0.0898 0.0514  344 LYS A N   
1447 C CA  . LYS A 218 ? 0.4507 0.6981 0.4614 0.0854  -0.0956 0.0623  344 LYS A CA  
1448 C C   . LYS A 218 ? 0.4190 0.7092 0.4651 0.0891  -0.0879 0.0610  344 LYS A C   
1449 O O   . LYS A 218 ? 0.3762 0.6929 0.4476 0.1140  -0.0861 0.0671  344 LYS A O   
1450 C CB  . LYS A 218 ? 0.4423 0.7197 0.4534 0.0812  -0.1165 0.0736  344 LYS A CB  
1451 C CG  . LYS A 218 ? 0.4867 0.7242 0.4593 0.0776  -0.1237 0.0763  344 LYS A CG  
1452 C CD  . LYS A 218 ? 0.5099 0.7793 0.4800 0.0709  -0.1460 0.0873  344 LYS A CD  
1453 C CE  . LYS A 218 ? 0.5553 0.7868 0.4853 0.0710  -0.1528 0.0926  344 LYS A CE  
1454 N NZ  . LYS A 218 ? 0.5571 0.8222 0.4830 0.0641  -0.1767 0.1040  344 LYS A NZ  
1455 N N   . ARG A 219 ? 0.4159 0.7119 0.4629 0.0658  -0.0825 0.0537  345 ARG A N   
1456 C CA  . ARG A 219 ? 0.3913 0.7289 0.4692 0.0649  -0.0739 0.0537  345 ARG A CA  
1457 C C   . ARG A 219 ? 0.4191 0.7307 0.4945 0.0777  -0.0544 0.0455  345 ARG A C   
1458 O O   . ARG A 219 ? 0.3392 0.6847 0.4386 0.0842  -0.0445 0.0460  345 ARG A O   
1459 C CB  . ARG A 219 ? 0.3856 0.7394 0.4631 0.0306  -0.0788 0.0517  345 ARG A CB  
1460 C CG  . ARG A 219 ? 0.3981 0.7931 0.4858 0.0160  -0.0995 0.0604  345 ARG A CG  
1461 C CD  . ARG A 219 ? 0.4175 0.8095 0.4927 -0.0219 -0.1060 0.0559  345 ARG A CD  
1462 N NE  . ARG A 219 ? 0.4107 0.7361 0.4422 -0.0331 -0.1033 0.0445  345 ARG A NE  
1463 C CZ  . ARG A 219 ? 0.4499 0.7515 0.4605 -0.0620 -0.1056 0.0372  345 ARG A CZ  
1464 N NH1 . ARG A 219 ? 0.4516 0.7868 0.4787 -0.0870 -0.1116 0.0405  345 ARG A NH1 
1465 N NH2 . ARG A 219 ? 0.4014 0.6433 0.3736 -0.0658 -0.1014 0.0266  345 ARG A NH2 
1466 N N   . CYS A 220 ? 0.4007 0.6564 0.4476 0.0812  -0.0490 0.0385  346 CYS A N   
1467 C CA  . CYS A 220 ? 0.3899 0.6169 0.4295 0.0880  -0.0333 0.0300  346 CYS A CA  
1468 C C   . CYS A 220 ? 0.3948 0.6461 0.4558 0.1115  -0.0231 0.0302  346 CYS A C   
1469 O O   . CYS A 220 ? 0.3740 0.6357 0.4406 0.1068  -0.0115 0.0258  346 CYS A O   
1470 C CB  . CYS A 220 ? 0.3919 0.5640 0.4039 0.0935  -0.0320 0.0257  346 CYS A CB  
1471 S SG  . CYS A 220 ? 0.4614 0.5976 0.4613 0.0949  -0.0166 0.0151  346 CYS A SG  
1472 N N   . PRO A 221 ? 0.3745 0.6339 0.4457 0.1378  -0.0260 0.0350  347 PRO A N   
1473 C CA  . PRO A 221 ? 0.3539 0.6313 0.4416 0.1627  -0.0136 0.0324  347 PRO A CA  
1474 C C   . PRO A 221 ? 0.4070 0.7486 0.5260 0.1581  -0.0081 0.0361  347 PRO A C   
1475 O O   . PRO A 221 ? 0.4181 0.7707 0.5425 0.1654  0.0073  0.0305  347 PRO A O   
1476 C CB  . PRO A 221 ? 0.4462 0.7177 0.5379 0.1919  -0.0206 0.0385  347 PRO A CB  
1477 C CG  . PRO A 221 ? 0.4206 0.6942 0.5077 0.1798  -0.0384 0.0482  347 PRO A CG  
1478 C CD  . PRO A 221 ? 0.3456 0.5951 0.4110 0.1479  -0.0398 0.0432  347 PRO A CD  
1479 N N   . PHE A 222 ? 0.3150 0.7011 0.4539 0.1446  -0.0205 0.0458  348 PHE A N   
1480 C CA  . PHE A 222 ? 0.3125 0.7658 0.4848 0.1362  -0.0163 0.0515  348 PHE A CA  
1481 C C   . PHE A 222 ? 0.3341 0.7821 0.4966 0.1051  -0.0087 0.0471  348 PHE A C   
1482 O O   . PHE A 222 ? 0.2913 0.7801 0.4732 0.1019  0.0036  0.0487  348 PHE A O   
1483 C CB  . PHE A 222 ? 0.3067 0.8071 0.5017 0.1285  -0.0352 0.0638  348 PHE A CB  
1484 C CG  . PHE A 222 ? 0.3540 0.8450 0.5491 0.1565  -0.0459 0.0693  348 PHE A CG  
1485 C CD1 . PHE A 222 ? 0.3200 0.8426 0.5414 0.1924  -0.0401 0.0735  348 PHE A CD1 
1486 C CD2 . PHE A 222 ? 0.3684 0.8141 0.5342 0.1490  -0.0601 0.0703  348 PHE A CD2 
1487 C CE1 . PHE A 222 ? 0.4201 0.9268 0.6387 0.2199  -0.0505 0.0798  348 PHE A CE1 
1488 C CE2 . PHE A 222 ? 0.3940 0.8265 0.5563 0.1741  -0.0698 0.0773  348 PHE A CE2 
1489 C CZ  . PHE A 222 ? 0.4024 0.8634 0.5908 0.2094  -0.0660 0.0826  348 PHE A CZ  
1490 N N   . VAL A 223 ? 0.3607 0.7585 0.4924 0.0833  -0.0149 0.0422  349 VAL A N   
1491 C CA  . VAL A 223 ? 0.3180 0.6966 0.4346 0.0587  -0.0072 0.0375  349 VAL A CA  
1492 C C   . VAL A 223 ? 0.3478 0.7077 0.4557 0.0743  0.0106  0.0304  349 VAL A C   
1493 O O   . VAL A 223 ? 0.3485 0.7229 0.4587 0.0623  0.0212  0.0307  349 VAL A O   
1494 C CB  . VAL A 223 ? 0.3687 0.6928 0.4529 0.0392  -0.0164 0.0326  349 VAL A CB  
1495 C CG1 . VAL A 223 ? 0.3981 0.6944 0.4648 0.0202  -0.0077 0.0278  349 VAL A CG1 
1496 C CG2 . VAL A 223 ? 0.3581 0.7003 0.4455 0.0192  -0.0338 0.0381  349 VAL A CG2 
1497 N N   . LEU A 224 ? 0.3388 0.6645 0.4338 0.0996  0.0135  0.0243  350 LEU A N   
1498 C CA  . LEU A 224 ? 0.3774 0.6826 0.4601 0.1137  0.0287  0.0160  350 LEU A CA  
1499 C C   . LEU A 224 ? 0.3415 0.6972 0.4480 0.1312  0.0419  0.0175  350 LEU A C   
1500 O O   . LEU A 224 ? 0.4026 0.7612 0.5020 0.1294  0.0559  0.0135  350 LEU A O   
1501 C CB  . LEU A 224 ? 0.3870 0.6411 0.4489 0.1333  0.0268  0.0089  350 LEU A CB  
1502 C CG  . LEU A 224 ? 0.4293 0.6345 0.4664 0.1163  0.0187  0.0063  350 LEU A CG  
1503 C CD1 . LEU A 224 ? 0.4410 0.6051 0.4630 0.1337  0.0162  0.0023  350 LEU A CD1 
1504 C CD2 . LEU A 224 ? 0.4518 0.6375 0.4729 0.1000  0.0260  0.0015  350 LEU A CD2 
1505 N N   . ASP A 225 ? 0.3327 0.7297 0.4667 0.1500  0.0384  0.0237  351 ASP A N   
1506 C CA  . ASP A 225 ? 0.3510 0.8062 0.5130 0.1674  0.0523  0.0261  351 ASP A CA  
1507 C C   . ASP A 225 ? 0.3500 0.8503 0.5263 0.1391  0.0591  0.0325  351 ASP A C   
1508 O O   . ASP A 225 ? 0.3530 0.8807 0.5348 0.1448  0.0771  0.0309  351 ASP A O   
1509 C CB  . ASP A 225 ? 0.3583 0.8600 0.5538 0.1886  0.0441  0.0350  351 ASP A CB  
1510 C CG  . ASP A 225 ? 0.4098 0.8691 0.5924 0.2211  0.0391  0.0307  351 ASP A CG  
1511 O OD1 . ASP A 225 ? 0.4685 0.8756 0.6227 0.2348  0.0481  0.0189  351 ASP A OD1 
1512 O OD2 . ASP A 225 ? 0.4074 0.8851 0.6072 0.2317  0.0249  0.0399  351 ASP A OD2 
1513 N N   . PHE A 226 ? 0.3273 0.8344 0.5075 0.1074  0.0450  0.0400  352 PHE A N   
1514 C CA  . PHE A 226 ? 0.3432 0.8887 0.5359 0.0763  0.0489  0.0477  352 PHE A CA  
1515 C C   . PHE A 226 ? 0.3390 0.8443 0.5008 0.0629  0.0606  0.0420  352 PHE A C   
1516 O O   . PHE A 226 ? 0.3831 0.9217 0.5525 0.0528  0.0744  0.0465  352 PHE A O   
1517 C CB  . PHE A 226 ? 0.3168 0.8655 0.5130 0.0447  0.0289  0.0548  352 PHE A CB  
1518 C CG  . PHE A 226 ? 0.3330 0.9006 0.5317 0.0067  0.0304  0.0617  352 PHE A CG  
1519 C CD1 . PHE A 226 ? 0.3386 0.9824 0.5751 -0.0056 0.0336  0.0734  352 PHE A CD1 
1520 C CD2 . PHE A 226 ? 0.3878 0.8971 0.5517 -0.0168 0.0285  0.0575  352 PHE A CD2 
1521 C CE1 . PHE A 226 ? 0.3787 1.0371 0.6161 -0.0440 0.0345  0.0812  352 PHE A CE1 
1522 C CE2 . PHE A 226 ? 0.4029 0.9223 0.5657 -0.0519 0.0292  0.0648  352 PHE A CE2 
1523 C CZ  . PHE A 226 ? 0.3862 0.9783 0.5846 -0.0672 0.0321  0.0768  352 PHE A CZ  
1524 N N   . ILE A 227 ? 0.3140 0.7505 0.4414 0.0624  0.0551  0.0334  353 ILE A N   
1525 C CA  . ILE A 227 ? 0.3738 0.7707 0.4716 0.0503  0.0631  0.0291  353 ILE A CA  
1526 C C   . ILE A 227 ? 0.3807 0.7804 0.4707 0.0738  0.0810  0.0225  353 ILE A C   
1527 O O   . ILE A 227 ? 0.3453 0.7512 0.4249 0.0632  0.0929  0.0243  353 ILE A O   
1528 C CB  . ILE A 227 ? 0.3443 0.6738 0.4123 0.0452  0.0518  0.0225  353 ILE A CB  
1529 C CG1 . ILE A 227 ? 0.3563 0.6793 0.4248 0.0187  0.0368  0.0276  353 ILE A CG1 
1530 C CG2 . ILE A 227 ? 0.3494 0.6385 0.3881 0.0397  0.0593  0.0180  353 ILE A CG2 
1531 C CD1 . ILE A 227 ? 0.3985 0.6621 0.4410 0.0177  0.0270  0.0209  353 ILE A CD1 
1532 N N   . ILE A 228 ? 0.3507 0.7415 0.4413 0.1054  0.0829  0.0146  354 ILE A N   
1533 C CA  . ILE A 228 ? 0.4084 0.7984 0.4879 0.1296  0.0998  0.0058  354 ILE A CA  
1534 C C   . ILE A 228 ? 0.4220 0.8791 0.5248 0.1301  0.1167  0.0123  354 ILE A C   
1535 O O   . ILE A 228 ? 0.4108 0.8697 0.4966 0.1282  0.1319  0.0096  354 ILE A O   
1536 C CB  . ILE A 228 ? 0.4200 0.7896 0.4986 0.1636  0.0976  -0.0028 354 ILE A CB  
1537 C CG1 . ILE A 228 ? 0.4286 0.7311 0.4812 0.1597  0.0831  -0.0085 354 ILE A CG1 
1538 C CG2 . ILE A 228 ? 0.4440 0.8142 0.5103 0.1905  0.1159  -0.0136 354 ILE A CG2 
1539 C CD1 . ILE A 228 ? 0.4398 0.7166 0.4903 0.1876  0.0778  -0.0139 354 ILE A CD1 
1540 N N   . ASP A 229 ? 0.3489 0.8657 0.4912 0.1317  0.1142  0.0219  355 ASP A N   
1541 C CA  . ASP A 229 ? 0.3824 0.9729 0.5530 0.1296  0.1307  0.0302  355 ASP A CA  
1542 C C   . ASP A 229 ? 0.3788 0.9771 0.5412 0.0902  0.1338  0.0395  355 ASP A C   
1543 O O   . ASP A 229 ? 0.3708 0.9967 0.5321 0.0860  0.1508  0.0425  355 ASP A O   
1544 C CB  . ASP A 229 ? 0.3816 1.0262 0.5952 0.1342  0.1213  0.0398  355 ASP A CB  
1545 C CG  . ASP A 229 ? 0.3580 1.0632 0.5978 0.1218  0.1311  0.0499  355 ASP A CG  
1546 O OD1 . ASP A 229 ? 0.4346 1.1503 0.6754 0.1441  0.1458  0.0450  355 ASP A OD1 
1547 O OD2 . ASP A 229 ? 0.3777 1.1190 0.6367 0.0885  0.1238  0.0627  355 ASP A OD2 
1548 N N   . LEU A 230 ? 0.3700 0.9336 0.5216 0.0606  0.1160  0.0439  356 LEU A N   
1549 C CA  . LEU A 230 ? 0.3809 0.9428 0.5217 0.0233  0.1172  0.0534  356 LEU A CA  
1550 C C   . LEU A 230 ? 0.3878 0.9076 0.4893 0.0243  0.1291  0.0478  356 LEU A C   
1551 O O   . LEU A 230 ? 0.4002 0.9409 0.4964 0.0062  0.1413  0.0563  356 LEU A O   
1552 C CB  . LEU A 230 ? 0.4094 0.9329 0.5416 -0.0043 0.0955  0.0565  356 LEU A CB  
1553 C CG  . LEU A 230 ? 0.3715 0.8707 0.4826 -0.0405 0.0946  0.0645  356 LEU A CG  
1554 C CD1 . LEU A 230 ? 0.3840 0.9489 0.5214 -0.0650 0.1033  0.0794  356 LEU A CD1 
1555 C CD2 . LEU A 230 ? 0.4228 0.8711 0.5183 -0.0608 0.0741  0.0633  356 LEU A CD2 
1556 N N   . ALA A 231 ? 0.3909 0.8514 0.4638 0.0433  0.1246  0.0348  357 ALA A N   
1557 C CA  . ALA A 231 ? 0.4499 0.8726 0.4853 0.0469  0.1339  0.0286  357 ALA A CA  
1558 C C   . ALA A 231 ? 0.4610 0.9251 0.4972 0.0648  0.1568  0.0261  357 ALA A C   
1559 O O   . ALA A 231 ? 0.5170 0.9841 0.5325 0.0527  0.1688  0.0305  357 ALA A O   
1560 C CB  . ALA A 231 ? 0.4305 0.7908 0.4413 0.0650  0.1237  0.0149  357 ALA A CB  
1561 N N   . ARG A 232 ? 0.4674 0.9636 0.5258 0.0948  0.1639  0.0195  358 ARG A N   
1562 C CA  A ARG A 232 ? 0.4262 0.9400 0.4807 0.1139  0.1812  0.0136  358 ARG A CA  
1563 C CA  B ARG A 232 ? 0.4257 0.9393 0.4799 0.1138  0.1812  0.0136  358 ARG A CA  
1564 C C   . ARG A 232 ? 0.4488 1.0173 0.5231 0.0929  0.1922  0.0275  358 ARG A C   
1565 O O   . ARG A 232 ? 0.4684 1.0367 0.5227 0.0918  0.2066  0.0263  358 ARG A O   
1566 C CB  A ARG A 232 ? 0.4319 0.9502 0.5052 0.1479  0.1798  0.0042  358 ARG A CB  
1567 C CB  B ARG A 232 ? 0.4336 0.9505 0.5057 0.1482  0.1801  0.0038  358 ARG A CB  
1568 C CG  A ARG A 232 ? 0.4706 0.9837 0.5292 0.1706  0.1955  -0.0068 358 ARG A CG  
1569 C CG  B ARG A 232 ? 0.4564 0.9881 0.5257 0.1675  0.1971  -0.0029 358 ARG A CG  
1570 C CD  A ARG A 232 ? 0.4634 0.9771 0.5396 0.2037  0.1935  -0.0146 358 ARG A CD  
1571 C CD  B ARG A 232 ? 0.4671 0.9771 0.5381 0.2034  0.1954  -0.0159 358 ARG A CD  
1572 N NE  A ARG A 232 ? 0.4773 0.9512 0.5507 0.2132  0.1761  -0.0189 358 ARG A NE  
1573 N NE  B ARG A 232 ? 0.5151 0.9540 0.5451 0.2148  0.1903  -0.0313 358 ARG A NE  
1574 C CZ  A ARG A 232 ? 0.5212 0.9308 0.5608 0.2263  0.1711  -0.0328 358 ARG A CZ  
1575 C CZ  B ARG A 232 ? 0.5242 0.9228 0.5487 0.2211  0.1745  -0.0354 358 ARG A CZ  
1576 N NH1 A ARG A 232 ? 0.5550 0.9312 0.5591 0.2310  0.1807  -0.0448 358 ARG A NH1 
1577 N NH1 B ARG A 232 ? 0.4964 0.9170 0.5517 0.2191  0.1623  -0.0259 358 ARG A NH1 
1578 N NH2 A ARG A 232 ? 0.5050 0.8830 0.5457 0.2331  0.1553  -0.0343 358 ARG A NH2 
1579 N NH2 B ARG A 232 ? 0.5536 0.8887 0.5403 0.2282  0.1701  -0.0490 358 ARG A NH2 
1580 N N   . ARG A 233 ? 0.3955 1.0104 0.5079 0.0746  0.1847  0.0411  359 ARG A N   
1581 C CA  . ARG A 233 ? 0.4117 1.0779 0.5441 0.0528  0.1938  0.0549  359 ARG A CA  
1582 C C   . ARG A 233 ? 0.4168 1.0674 0.5269 0.0144  0.1936  0.0667  359 ARG A C   
1583 O O   . ARG A 233 ? 0.4423 1.1174 0.5521 -0.0012 0.2052  0.0757  359 ARG A O   
1584 C CB  . ARG A 233 ? 0.4251 1.1477 0.6064 0.0467  0.1842  0.0650  359 ARG A CB  
1585 C CG  . ARG A 233 ? 0.4480 1.1694 0.6397 0.0150  0.1653  0.0751  359 ARG A CG  
1586 C CD  . ARG A 233 ? 0.4781 1.2578 0.7162 0.0083  0.1548  0.0848  359 ARG A CD  
1587 N NE  . ARG A 233 ? 0.4753 1.2598 0.7209 -0.0337 0.1389  0.0970  359 ARG A NE  
1588 C CZ  . ARG A 233 ? 0.4208 1.1934 0.6731 -0.0420 0.1195  0.0969  359 ARG A CZ  
1589 N NH1 . ARG A 233 ? 0.4237 1.1808 0.6778 -0.0108 0.1131  0.0867  359 ARG A NH1 
1590 N NH2 . ARG A 233 ? 0.5033 1.2749 0.7577 -0.0833 0.1052  0.1069  359 ARG A NH2 
1591 N N   . SER A 234 ? 0.4569 1.0647 0.5464 -0.0009 0.1812  0.0675  360 SER A N   
1592 C CA  . SER A 234 ? 0.4957 1.0800 0.5607 -0.0369 0.1795  0.0797  360 SER A CA  
1593 C C   . SER A 234 ? 0.5383 1.0765 0.5557 -0.0306 0.1882  0.0744  360 SER A C   
1594 O O   . SER A 234 ? 0.5203 1.0430 0.5158 -0.0569 0.1899  0.0862  360 SER A O   
1595 C CB  . SER A 234 ? 0.4444 0.9850 0.5045 -0.0578 0.1569  0.0822  360 SER A CB  
1596 O OG  . SER A 234 ? 0.4732 0.9457 0.5028 -0.0391 0.1471  0.0682  360 SER A OG  
1597 N N   . GLY A 235 ? 0.5240 1.0358 0.5227 0.0023  0.1915  0.0574  361 GLY A N   
1598 C CA  . GLY A 235 ? 0.5451 1.0108 0.4966 0.0072  0.1960  0.0514  361 GLY A CA  
1599 C C   . GLY A 235 ? 0.5462 0.9463 0.4702 -0.0041 0.1770  0.0509  361 GLY A C   
1600 O O   . GLY A 235 ? 0.5894 0.9518 0.4743 -0.0057 0.1773  0.0498  361 GLY A O   
1601 N N   . ARG A 236 ? 0.5010 0.8828 0.4444 -0.0115 0.1587  0.0515  362 ARG A N   
1602 C CA  . ARG A 236 ? 0.5024 0.8191 0.4250 -0.0172 0.1394  0.0485  362 ARG A CA  
1603 C C   . ARG A 236 ? 0.5209 0.8120 0.4437 0.0111  0.1321  0.0314  362 ARG A C   
1604 O O   . ARG A 236 ? 0.5406 0.8529 0.4916 0.0227  0.1292  0.0270  362 ARG A O   
1605 C CB  . ARG A 236 ? 0.5151 0.8242 0.4544 -0.0427 0.1250  0.0584  362 ARG A CB  
1606 C CG  . ARG A 236 ? 0.5776 0.9144 0.5207 -0.0743 0.1315  0.0764  362 ARG A CG  
1607 C CD  . ARG A 236 ? 0.5583 0.8550 0.4629 -0.0887 0.1319  0.0853  362 ARG A CD  
1608 N NE  . ARG A 236 ? 0.6062 0.9323 0.5120 -0.1186 0.1411  0.1039  362 ARG A NE  
1609 C CZ  . ARG A 236 ? 0.5964 0.9139 0.5096 -0.1493 0.1315  0.1160  362 ARG A CZ  
1610 N NH1 . ARG A 236 ? 0.5843 0.8630 0.5015 -0.1527 0.1129  0.1106  362 ARG A NH1 
1611 N NH2 . ARG A 236 ? 0.5873 0.9352 0.5022 -0.1781 0.1411  0.1339  362 ARG A NH2 
1612 N N   . ARG A 237 ? 0.5007 0.7460 0.3921 0.0206  0.1274  0.0230  363 ARG A N   
1613 C CA  . ARG A 237 ? 0.4708 0.6856 0.3609 0.0420  0.1181  0.0085  363 ARG A CA  
1614 C C   . ARG A 237 ? 0.4997 0.6844 0.3993 0.0313  0.1001  0.0111  363 ARG A C   
1615 O O   . ARG A 237 ? 0.5200 0.6635 0.4008 0.0254  0.0898  0.0113  363 ARG A O   
1616 C CB  . ARG A 237 ? 0.5172 0.6975 0.3714 0.0532  0.1184  -0.0013 363 ARG A CB  
1617 C CG  . ARG A 237 ? 0.5296 0.6774 0.3812 0.0718  0.1088  -0.0156 363 ARG A CG  
1618 C CD  . ARG A 237 ? 0.5480 0.6835 0.3724 0.0901  0.1162  -0.0294 363 ARG A CD  
1619 N NE  . ARG A 237 ? 0.5446 0.6486 0.3686 0.1057  0.1067  -0.0421 363 ARG A NE  
1620 C CZ  . ARG A 237 ? 0.5754 0.6380 0.3833 0.1015  0.0922  -0.0462 363 ARG A CZ  
1621 N NH1 . ARG A 237 ? 0.5541 0.6016 0.3455 0.0855  0.0849  -0.0392 363 ARG A NH1 
1622 N NH2 . ARG A 237 ? 0.5620 0.5989 0.3716 0.1135  0.0846  -0.0562 363 ARG A NH2 
1623 N N   . ILE A 238 ? 0.4289 0.6364 0.3579 0.0300  0.0964  0.0131  364 ILE A N   
1624 C CA  . ILE A 238 ? 0.4262 0.6098 0.3621 0.0177  0.0814  0.0159  364 ILE A CA  
1625 C C   . ILE A 238 ? 0.4521 0.5941 0.3777 0.0319  0.0716  0.0057  364 ILE A C   
1626 O O   . ILE A 238 ? 0.4320 0.5746 0.3605 0.0521  0.0733  -0.0034 364 ILE A O   
1627 C CB  . ILE A 238 ? 0.4348 0.6551 0.4019 0.0133  0.0786  0.0198  364 ILE A CB  
1628 C CG1 . ILE A 238 ? 0.4619 0.7299 0.4434 -0.0041 0.0880  0.0313  364 ILE A CG1 
1629 C CG2 . ILE A 238 ? 0.3892 0.5801 0.3567 0.0010  0.0632  0.0205  364 ILE A CG2 
1630 C CD1 . ILE A 238 ? 0.4126 0.7283 0.4293 -0.0076 0.0847  0.0358  364 ILE A CD1 
1631 N N   . MET A 239 ? 0.4360 0.5414 0.3493 0.0215  0.0617  0.0077  365 MET A N   
1632 C CA  . MET A 239 ? 0.3928 0.4645 0.3003 0.0318  0.0528  0.0001  365 MET A CA  
1633 C C   . MET A 239 ? 0.4237 0.4993 0.3491 0.0318  0.0462  -0.0009 365 MET A C   
1634 O O   . MET A 239 ? 0.4308 0.5082 0.3613 0.0166  0.0421  0.0048  365 MET A O   
1635 C CB  . MET A 239 ? 0.4622 0.4993 0.3526 0.0233  0.0459  0.0033  365 MET A CB  
1636 C CG  . MET A 239 ? 0.5489 0.5843 0.4202 0.0169  0.0505  0.0093  365 MET A CG  
1637 S SD  . MET A 239 ? 0.5473 0.5413 0.4009 0.0123  0.0396  0.0140  365 MET A SD  
1638 C CE  . MET A 239 ? 0.5309 0.5085 0.3964 0.0030  0.0328  0.0168  365 MET A CE  
1639 N N   . VAL A 240 ? 0.3931 0.4681 0.3249 0.0479  0.0448  -0.0076 366 VAL A N   
1640 C CA  . VAL A 240 ? 0.3580 0.4393 0.3043 0.0491  0.0385  -0.0072 366 VAL A CA  
1641 C C   . VAL A 240 ? 0.3663 0.4136 0.3043 0.0547  0.0317  -0.0119 366 VAL A C   
1642 O O   . VAL A 240 ? 0.3929 0.4276 0.3256 0.0679  0.0324  -0.0175 366 VAL A O   
1643 C CB  . VAL A 240 ? 0.3960 0.5093 0.3592 0.0638  0.0423  -0.0080 366 VAL A CB  
1644 C CG1 . VAL A 240 ? 0.3512 0.4670 0.3255 0.0644  0.0332  -0.0061 366 VAL A CG1 
1645 C CG2 . VAL A 240 ? 0.3949 0.5505 0.3708 0.0575  0.0506  -0.0021 366 VAL A CG2 
1646 N N   . ARG A 241 ? 0.3476 0.3791 0.2828 0.0440  0.0257  -0.0100 367 ARG A N   
1647 C CA  . ARG A 241 ? 0.3629 0.3689 0.2930 0.0484  0.0210  -0.0132 367 ARG A CA  
1648 C C   . ARG A 241 ? 0.3984 0.4125 0.3363 0.0528  0.0171  -0.0127 367 ARG A C   
1649 O O   . ARG A 241 ? 0.3969 0.4217 0.3384 0.0438  0.0136  -0.0099 367 ARG A O   
1650 C CB  . ARG A 241 ? 0.3969 0.3815 0.3185 0.0382  0.0184  -0.0122 367 ARG A CB  
1651 C CG  . ARG A 241 ? 0.3939 0.3589 0.3129 0.0434  0.0158  -0.0149 367 ARG A CG  
1652 C CD  . ARG A 241 ? 0.3909 0.3386 0.3029 0.0365  0.0147  -0.0149 367 ARG A CD  
1653 N NE  . ARG A 241 ? 0.4214 0.3588 0.3275 0.0325  0.0153  -0.0125 367 ARG A NE  
1654 C CZ  . ARG A 241 ? 0.4475 0.3695 0.3451 0.0248  0.0146  -0.0113 367 ARG A CZ  
1655 N NH1 . ARG A 241 ? 0.4344 0.3495 0.3272 0.0192  0.0132  -0.0140 367 ARG A NH1 
1656 N NH2 . ARG A 241 ? 0.4507 0.3610 0.3416 0.0223  0.0144  -0.0072 367 ARG A NH2 
1657 N N   . LEU A 242 ? 0.3516 0.3580 0.2896 0.0654  0.0165  -0.0150 368 LEU A N   
1658 C CA  . LEU A 242 ? 0.3509 0.3607 0.2934 0.0712  0.0119  -0.0127 368 LEU A CA  
1659 C C   . LEU A 242 ? 0.3753 0.3616 0.3085 0.0663  0.0089  -0.0127 368 LEU A C   
1660 O O   . LEU A 242 ? 0.3656 0.3326 0.2936 0.0689  0.0101  -0.0148 368 LEU A O   
1661 C CB  . LEU A 242 ? 0.3668 0.3753 0.3116 0.0880  0.0130  -0.0142 368 LEU A CB  
1662 C CG  . LEU A 242 ? 0.3644 0.3754 0.3131 0.0963  0.0072  -0.0094 368 LEU A CG  
1663 C CD1 . LEU A 242 ? 0.4005 0.4482 0.3639 0.0954  0.0046  -0.0044 368 LEU A CD1 
1664 C CD2 . LEU A 242 ? 0.3980 0.3927 0.3433 0.1138  0.0080  -0.0115 368 LEU A CD2 
1665 N N   . VAL A 243 ? 0.3630 0.3525 0.2935 0.0581  0.0054  -0.0105 369 VAL A N   
1666 C CA  . VAL A 243 ? 0.3746 0.3459 0.2947 0.0548  0.0046  -0.0104 369 VAL A CA  
1667 C C   . VAL A 243 ? 0.3845 0.3618 0.3024 0.0580  -0.0009 -0.0057 369 VAL A C   
1668 O O   . VAL A 243 ? 0.3981 0.3962 0.3238 0.0604  -0.0055 -0.0025 369 VAL A O   
1669 C CB  . VAL A 243 ? 0.3873 0.3509 0.2986 0.0436  0.0057  -0.0133 369 VAL A CB  
1670 C CG1 . VAL A 243 ? 0.3913 0.3482 0.3043 0.0416  0.0096  -0.0156 369 VAL A CG1 
1671 C CG2 . VAL A 243 ? 0.3897 0.3676 0.2992 0.0346  0.0001  -0.0122 369 VAL A CG2 
1672 N N   . LYS A 244 ? 0.3770 0.3386 0.2844 0.0575  -0.0005 -0.0039 370 LYS A N   
1673 C CA  . LYS A 244 ? 0.4103 0.3763 0.3106 0.0586  -0.0067 0.0021  370 LYS A CA  
1674 C C   . LYS A 244 ? 0.4348 0.4090 0.3253 0.0477  -0.0107 0.0005  370 LYS A C   
1675 O O   . LYS A 244 ? 0.4591 0.4506 0.3508 0.0469  -0.0193 0.0047  370 LYS A O   
1676 C CB  . LYS A 244 ? 0.4163 0.3633 0.3058 0.0602  -0.0046 0.0065  370 LYS A CB  
1677 C CG  . LYS A 244 ? 0.4376 0.3740 0.3342 0.0701  -0.0048 0.0094  370 LYS A CG  
1678 C CD  . LYS A 244 ? 0.4754 0.3908 0.3627 0.0681  -0.0028 0.0148  370 LYS A CD  
1679 C CE  . LYS A 244 ? 0.4944 0.3936 0.3868 0.0758  -0.0040 0.0147  370 LYS A CE  
1680 N NZ  . LYS A 244 ? 0.4955 0.3721 0.3806 0.0698  -0.0025 0.0199  370 LYS A NZ  
1681 N N   . GLY A 245 ? 0.4358 0.3973 0.3165 0.0395  -0.0055 -0.0060 371 GLY A N   
1682 C CA  . GLY A 245 ? 0.4350 0.3965 0.3015 0.0280  -0.0095 -0.0098 371 GLY A CA  
1683 C C   . GLY A 245 ? 0.4518 0.3917 0.2966 0.0248  -0.0032 -0.0152 371 GLY A C   
1684 O O   . GLY A 245 ? 0.4563 0.3903 0.2928 0.0292  0.0006  -0.0119 371 GLY A O   
1685 N N   . ALA A 246 ? 0.4326 0.3597 0.2662 0.0169  -0.0016 -0.0233 372 ALA A N   
1686 C CA  . ALA A 246 ? 0.4694 0.3741 0.2830 0.0177  0.0071  -0.0305 372 ALA A CA  
1687 C C   . ALA A 246 ? 0.4995 0.3942 0.2827 0.0093  0.0033  -0.0358 372 ALA A C   
1688 O O   . ALA A 246 ? 0.4864 0.3635 0.2494 0.0124  0.0125  -0.0423 372 ALA A O   
1689 C CB  . ALA A 246 ? 0.4642 0.3522 0.2799 0.0177  0.0121  -0.0371 372 ALA A CB  
1690 N N   . TYR A 247 ? 0.4959 0.4029 0.2747 -0.0011 -0.0099 -0.0336 373 TYR A N   
1691 C CA  . TYR A 247 ? 0.5362 0.4317 0.2833 -0.0132 -0.0168 -0.0404 373 TYR A CA  
1692 C C   . TYR A 247 ? 0.5543 0.4657 0.2901 -0.0145 -0.0258 -0.0327 373 TYR A C   
1693 O O   . TYR A 247 ? 0.5726 0.4870 0.2900 -0.0273 -0.0384 -0.0347 373 TYR A O   
1694 C CB  . TYR A 247 ? 0.5248 0.4209 0.2724 -0.0294 -0.0279 -0.0442 373 TYR A CB  
1695 C CG  . TYR A 247 ? 0.5651 0.4425 0.3210 -0.0296 -0.0208 -0.0494 373 TYR A CG  
1696 C CD1 . TYR A 247 ? 0.5554 0.4500 0.3431 -0.0236 -0.0181 -0.0421 373 TYR A CD1 
1697 C CD2 . TYR A 247 ? 0.6045 0.4439 0.3328 -0.0351 -0.0172 -0.0616 373 TYR A CD2 
1698 C CE1 . TYR A 247 ? 0.5625 0.4395 0.3552 -0.0238 -0.0125 -0.0449 373 TYR A CE1 
1699 C CE2 . TYR A 247 ? 0.6137 0.4329 0.3483 -0.0339 -0.0118 -0.0644 373 TYR A CE2 
1700 C CZ  . TYR A 247 ? 0.5887 0.4283 0.3557 -0.0289 -0.0100 -0.0550 373 TYR A CZ  
1701 O OH  . TYR A 247 ? 0.6160 0.4353 0.3865 -0.0281 -0.0058 -0.0559 373 TYR A OH  
1702 N N   . TRP A 248 ? 0.5674 0.4881 0.3130 -0.0027 -0.0211 -0.0231 374 TRP A N   
1703 C CA  . TRP A 248 ? 0.5693 0.5043 0.3059 -0.0027 -0.0315 -0.0125 374 TRP A CA  
1704 C C   . TRP A 248 ? 0.6439 0.5657 0.3385 -0.0121 -0.0347 -0.0180 374 TRP A C   
1705 O O   . TRP A 248 ? 0.6410 0.5745 0.3232 -0.0217 -0.0508 -0.0153 374 TRP A O   
1706 C CB  . TRP A 248 ? 0.5548 0.4915 0.3025 0.0101  -0.0244 -0.0015 374 TRP A CB  
1707 C CG  . TRP A 248 ? 0.5656 0.5144 0.3056 0.0120  -0.0368 0.0120  374 TRP A CG  
1708 C CD1 . TRP A 248 ? 0.5487 0.5190 0.3107 0.0177  -0.0496 0.0218  374 TRP A CD1 
1709 C CD2 . TRP A 248 ? 0.6138 0.5543 0.3218 0.0098  -0.0372 0.0180  374 TRP A CD2 
1710 N NE1 . TRP A 248 ? 0.5873 0.5616 0.3336 0.0202  -0.0597 0.0343  374 TRP A NE1 
1711 C CE2 . TRP A 248 ? 0.6063 0.5617 0.3176 0.0140  -0.0526 0.0326  374 TRP A CE2 
1712 C CE3 . TRP A 248 ? 0.6581 0.5810 0.3336 0.0055  -0.0253 0.0128  374 TRP A CE3 
1713 C CZ2 . TRP A 248 ? 0.6567 0.6071 0.3381 0.0128  -0.0579 0.0436  374 TRP A CZ2 
1714 C CZ3 . TRP A 248 ? 0.7136 0.6338 0.3589 0.0033  -0.0287 0.0227  374 TRP A CZ3 
1715 C CH2 . TRP A 248 ? 0.7205 0.6531 0.3678 0.0061  -0.0457 0.0386  374 TRP A CH2 
1716 N N   . ASP A 249 ? 0.6384 0.5376 0.3100 -0.0094 -0.0194 -0.0261 375 ASP A N   
1717 C CA  . ASP A 249 ? 0.7012 0.5855 0.3273 -0.0169 -0.0198 -0.0327 375 ASP A CA  
1718 C C   . ASP A 249 ? 0.6954 0.5713 0.3015 -0.0327 -0.0338 -0.0440 375 ASP A C   
1719 O O   . ASP A 249 ? 0.7692 0.6456 0.3438 -0.0432 -0.0462 -0.0442 375 ASP A O   
1720 C CB  . ASP A 249 ? 0.7620 0.6256 0.3706 -0.0091 0.0021  -0.0418 375 ASP A CB  
1721 C CG  . ASP A 249 ? 0.8144 0.6880 0.4283 -0.0003 0.0133  -0.0288 375 ASP A CG  
1722 O OD1 . ASP A 249 ? 0.8788 0.7563 0.4678 -0.0041 0.0084  -0.0202 375 ASP A OD1 
1723 O OD2 . ASP A 249 ? 0.8021 0.6798 0.4443 0.0088  0.0258  -0.0261 375 ASP A OD2 
1724 N N   . ALA A 250 ? 0.7373 0.6051 0.3602 -0.0365 -0.0334 -0.0523 376 ALA A N   
1725 C CA  . ALA A 250 ? 0.7772 0.6329 0.3808 -0.0550 -0.0468 -0.0628 376 ALA A CA  
1726 C C   . ALA A 250 ? 0.7413 0.6319 0.3626 -0.0672 -0.0691 -0.0518 376 ALA A C   
1727 O O   . ALA A 250 ? 0.7624 0.6520 0.3580 -0.0849 -0.0851 -0.0562 376 ALA A O   
1728 C CB  . ALA A 250 ? 0.7223 0.5564 0.3379 -0.0562 -0.0397 -0.0724 376 ALA A CB  
1729 N N   . GLU A 251 ? 0.6667 0.5897 0.3316 -0.0577 -0.0708 -0.0378 377 GLU A N   
1730 C CA  . GLU A 251 ? 0.6435 0.6060 0.3300 -0.0649 -0.0903 -0.0261 377 GLU A CA  
1731 C C   . GLU A 251 ? 0.7012 0.6754 0.3641 -0.0659 -0.1033 -0.0181 377 GLU A C   
1732 O O   . GLU A 251 ? 0.7199 0.7163 0.3790 -0.0802 -0.1235 -0.0147 377 GLU A O   
1733 C CB  . GLU A 251 ? 0.5726 0.5638 0.3067 -0.0495 -0.0863 -0.0140 377 GLU A CB  
1734 C CG  . GLU A 251 ? 0.5876 0.5710 0.3442 -0.0490 -0.0751 -0.0198 377 GLU A CG  
1735 C CD  . GLU A 251 ? 0.5880 0.5813 0.3511 -0.0696 -0.0854 -0.0236 377 GLU A CD  
1736 O OE1 . GLU A 251 ? 0.6832 0.6930 0.4366 -0.0855 -0.1025 -0.0221 377 GLU A OE1 
1737 O OE2 . GLU A 251 ? 0.5838 0.5688 0.3615 -0.0714 -0.0771 -0.0270 377 GLU A OE2 
1738 N N   . ILE A 252 ? 0.7067 0.6683 0.3543 -0.0520 -0.0927 -0.0135 378 ILE A N   
1739 C CA  . ILE A 252 ? 0.7595 0.7274 0.3786 -0.0530 -0.1040 -0.0044 378 ILE A CA  
1740 C C   . ILE A 252 ? 0.8201 0.7701 0.3909 -0.0725 -0.1133 -0.0173 378 ILE A C   
1741 O O   . ILE A 252 ? 0.8700 0.8385 0.4262 -0.0835 -0.1347 -0.0114 378 ILE A O   
1742 C CB  . ILE A 252 ? 0.7345 0.6869 0.3420 -0.0378 -0.0878 0.0026  378 ILE A CB  
1743 C CG1 . ILE A 252 ? 0.7288 0.6959 0.3801 -0.0207 -0.0826 0.0157  378 ILE A CG1 
1744 C CG2 . ILE A 252 ? 0.8211 0.7737 0.3891 -0.0411 -0.0981 0.0118  378 ILE A CG2 
1745 C CD1 . ILE A 252 ? 0.7124 0.7134 0.3908 -0.0161 -0.1019 0.0302  378 ILE A CD1 
1746 N N   . LYS A 253 ? 0.8058 0.7188 0.3503 -0.0764 -0.0983 -0.0356 379 LYS A N   
1747 C CA  . LYS A 253 ? 0.8938 0.7794 0.3834 -0.0926 -0.1039 -0.0509 379 LYS A CA  
1748 C C   . LYS A 253 ? 0.9053 0.7976 0.3984 -0.1148 -0.1242 -0.0576 379 LYS A C   
1749 O O   . LYS A 253 ? 1.0132 0.9047 0.4847 -0.1266 -0.1362 -0.0621 379 LYS A O   
1750 C CB  . LYS A 253 ? 0.9380 0.7812 0.4020 -0.0852 -0.0793 -0.0687 379 LYS A CB  
1751 N N   . ARG A 254 ? 0.8862 0.7894 0.4178 -0.1186 -0.1255 -0.0570 380 ARG A N   
1752 C CA  . ARG A 254 ? 0.8858 0.8036 0.4242 -0.1434 -0.1468 -0.0592 380 ARG A CA  
1753 C C   . ARG A 254 ? 0.9520 0.9241 0.5145 -0.1474 -0.1696 -0.0409 380 ARG A C   
1754 O O   . ARG A 254 ? 0.9966 0.9829 0.5583 -0.1651 -0.1870 -0.0418 380 ARG A O   
1755 C CB  . ARG A 254 ? 0.8952 0.8140 0.4729 -0.1453 -0.1393 -0.0606 380 ARG A CB  
1756 N N   . ALA A 255 ? 0.8998 0.9026 0.4949 -0.1258 -0.1660 -0.0235 381 ALA A N   
1757 C CA  . ALA A 255 ? 0.8672 0.9213 0.4860 -0.1249 -0.1877 -0.0049 381 ALA A CA  
1758 C C   . ALA A 255 ? 0.9583 1.0081 0.5394 -0.1285 -0.1998 -0.0032 381 ALA A C   
1759 O O   . ALA A 255 ? 0.9543 1.0344 0.5457 -0.1389 -0.2200 0.0025  381 ALA A O   
1760 C CB  . ALA A 255 ? 0.8181 0.8953 0.4788 -0.0965 -0.1779 0.0116  381 ALA A CB  
1761 N N   . GLN A 256 ? 0.9397 0.9540 0.4822 -0.1181 -0.1850 -0.0076 382 GLN A N   
1762 C CA  . GLN A 256 ? 0.9777 0.9873 0.4859 -0.1193 -0.1925 -0.0061 382 GLN A CA  
1763 C C   . GLN A 256 ? 1.0711 1.0647 0.5535 -0.1411 -0.2012 -0.0232 382 GLN A C   
1764 O O   . GLN A 256 ? 1.0835 1.0912 0.5515 -0.1484 -0.2183 -0.0193 382 GLN A O   
1765 C CB  . GLN A 256 ? 0.9624 0.9400 0.4366 -0.1047 -0.1714 -0.0072 382 GLN A CB  
1766 C CG  . GLN A 256 ? 0.9722 0.9607 0.4680 -0.0852 -0.1640 0.0112  382 GLN A CG  
1767 C CD  . GLN A 256 ? 0.9814 0.9454 0.4452 -0.0739 -0.1458 0.0145  382 GLN A CD  
1768 O OE1 . GLN A 256 ? 1.0930 1.0663 0.5435 -0.0685 -0.1534 0.0290  382 GLN A OE1 
1769 N NE2 . GLN A 256 ? 0.9749 0.9093 0.4279 -0.0700 -0.1212 0.0022  382 GLN A NE2 
1770 N N   . LEU A 257 ? 1.0630 1.0253 0.5386 -0.1517 -0.1905 -0.0416 383 LEU A N   
1771 C CA  . LEU A 257 ? 1.1635 1.1042 0.6135 -0.1730 -0.1987 -0.0579 383 LEU A CA  
1772 C C   . LEU A 257 ? 1.1817 1.1619 0.6630 -0.1929 -0.2238 -0.0504 383 LEU A C   
1773 O O   . LEU A 257 ? 1.1610 1.1497 0.6260 -0.2068 -0.2414 -0.0512 383 LEU A O   
1774 C CB  . LEU A 257 ? 1.1517 1.0443 0.5874 -0.1761 -0.1799 -0.0779 383 LEU A CB  
1775 N N   . ASP A 258 ? 1.1778 1.1850 0.7049 -0.1948 -0.2254 -0.0426 384 ASP A N   
1776 C CA  . ASP A 258 ? 1.1656 1.2197 0.7311 -0.2123 -0.2465 -0.0330 384 ASP A CA  
1777 C C   . ASP A 258 ? 1.1395 1.2500 0.7343 -0.1992 -0.2621 -0.0112 384 ASP A C   
1778 O O   . ASP A 258 ? 1.1285 1.2371 0.6971 -0.1914 -0.2685 -0.0071 384 ASP A O   
1779 C CB  . ASP A 258 ? 1.1807 1.2461 0.7852 -0.2184 -0.2400 -0.0320 384 ASP A CB  
1780 N N   . ALA A 261 ? 1.0600 1.3561 0.8053 -0.0930 -0.2941 0.0836  387 ALA A N   
1781 C CA  . ALA A 261 ? 1.1138 1.3637 0.8268 -0.0780 -0.2762 0.0825  387 ALA A CA  
1782 C C   . ALA A 261 ? 1.0764 1.3417 0.8281 -0.0502 -0.2665 0.0962  387 ALA A C   
1783 O O   . ALA A 261 ? 1.0750 1.3292 0.8195 -0.0279 -0.2655 0.1098  387 ALA A O   
1784 C CB  . ALA A 261 ? 1.2231 1.4484 0.8910 -0.0723 -0.2819 0.0877  387 ALA A CB  
1785 N N   . ASP A 262 ? 0.9707 1.2603 0.7625 -0.0518 -0.2593 0.0928  388 ASP A N   
1786 C CA  . ASP A 262 ? 0.8227 1.1218 0.6478 -0.0264 -0.2458 0.1012  388 ASP A CA  
1787 C C   . ASP A 262 ? 0.8277 1.0936 0.6530 -0.0350 -0.2213 0.0823  388 ASP A C   
1788 O O   . ASP A 262 ? 0.8502 1.1297 0.6861 -0.0567 -0.2228 0.0723  388 ASP A O   
1789 C CB  . ASP A 262 ? 0.8553 1.2132 0.7412 -0.0103 -0.2528 0.1132  388 ASP A CB  
1790 N N   . PHE A 263 ? 0.7742 0.9974 0.5879 -0.0193 -0.2005 0.0786  389 PHE A N   
1791 C CA  . PHE A 263 ? 0.6480 0.8358 0.4560 -0.0262 -0.1784 0.0617  389 PHE A CA  
1792 C C   . PHE A 263 ? 0.6636 0.8751 0.5201 -0.0157 -0.1675 0.0615  389 PHE A C   
1793 O O   . PHE A 263 ? 0.6284 0.8700 0.5183 0.0056  -0.1698 0.0738  389 PHE A O   
1794 C CB  . PHE A 263 ? 0.6940 0.8322 0.4726 -0.0146 -0.1610 0.0590  389 PHE A CB  
1795 C CG  . PHE A 263 ? 0.7612 0.8777 0.4901 -0.0226 -0.1689 0.0608  389 PHE A CG  
1796 C CD1 . PHE A 263 ? 0.7988 0.9294 0.5203 -0.0122 -0.1844 0.0787  389 PHE A CD1 
1797 C CD2 . PHE A 263 ? 0.8033 0.8838 0.4909 -0.0388 -0.1601 0.0450  389 PHE A CD2 
1798 C CE1 . PHE A 263 ? 0.8429 0.9537 0.5145 -0.0206 -0.1915 0.0814  389 PHE A CE1 
1799 C CE2 . PHE A 263 ? 0.7867 0.8478 0.4248 -0.0458 -0.1654 0.0457  389 PHE A CE2 
1800 C CZ  . PHE A 263 ? 0.8316 0.9086 0.4608 -0.0378 -0.1812 0.0643  389 PHE A CZ  
1801 N N   . PRO A 264 ? 0.5904 0.7881 0.4495 -0.0298 -0.1555 0.0478  390 PRO A N   
1802 C CA  . PRO A 264 ? 0.5391 0.7537 0.4377 -0.0197 -0.1423 0.0474  390 PRO A CA  
1803 C C   . PRO A 264 ? 0.5323 0.7121 0.4298 0.0013  -0.1225 0.0448  390 PRO A C   
1804 O O   . PRO A 264 ? 0.4606 0.6513 0.3866 0.0129  -0.1114 0.0446  390 PRO A O   
1805 C CB  . PRO A 264 ? 0.5703 0.7780 0.4645 -0.0461 -0.1394 0.0352  390 PRO A CB  
1806 C CG  . PRO A 264 ? 0.6457 0.8068 0.4911 -0.0608 -0.1403 0.0242  390 PRO A CG  
1807 C CD  . PRO A 264 ? 0.6458 0.8109 0.4697 -0.0552 -0.1543 0.0325  390 PRO A CD  
1808 N N   . VAL A 265 ? 0.5131 0.6537 0.3779 0.0053  -0.1180 0.0432  391 VAL A N   
1809 C CA  . VAL A 265 ? 0.4908 0.5993 0.3533 0.0217  -0.1012 0.0419  391 VAL A CA  
1810 C C   . VAL A 265 ? 0.5264 0.6279 0.3793 0.0379  -0.1068 0.0550  391 VAL A C   
1811 O O   . VAL A 265 ? 0.5267 0.6386 0.3634 0.0342  -0.1220 0.0632  391 VAL A O   
1812 C CB  . VAL A 265 ? 0.5271 0.5945 0.3617 0.0110  -0.0875 0.0289  391 VAL A CB  
1813 C CG1 . VAL A 265 ? 0.5057 0.5737 0.3501 -0.0019 -0.0818 0.0178  391 VAL A CG1 
1814 C CG2 . VAL A 265 ? 0.5221 0.5732 0.3170 -0.0016 -0.0942 0.0266  391 VAL A CG2 
1815 N N   . PHE A 266 ? 0.5037 0.5848 0.3640 0.0547  -0.0953 0.0574  392 PHE A N   
1816 C CA  . PHE A 266 ? 0.5010 0.5640 0.3467 0.0676  -0.0988 0.0699  392 PHE A CA  
1817 C C   . PHE A 266 ? 0.5661 0.6006 0.3716 0.0541  -0.0956 0.0684  392 PHE A C   
1818 O O   . PHE A 266 ? 0.5592 0.5816 0.3512 0.0398  -0.0863 0.0555  392 PHE A O   
1819 C CB  . PHE A 266 ? 0.5298 0.5718 0.3897 0.0852  -0.0873 0.0712  392 PHE A CB  
1820 C CG  . PHE A 266 ? 0.4831 0.5517 0.3781 0.1017  -0.0886 0.0719  392 PHE A CG  
1821 C CD1 . PHE A 266 ? 0.5215 0.6192 0.4319 0.1165  -0.1026 0.0840  392 PHE A CD1 
1822 C CD2 . PHE A 266 ? 0.4624 0.5300 0.3749 0.1030  -0.0756 0.0608  392 PHE A CD2 
1823 C CE1 . PHE A 266 ? 0.5236 0.6503 0.4681 0.1340  -0.1013 0.0841  392 PHE A CE1 
1824 C CE2 . PHE A 266 ? 0.4999 0.5938 0.4419 0.1184  -0.0745 0.0607  392 PHE A CE2 
1825 C CZ  . PHE A 266 ? 0.4840 0.6082 0.4429 0.1345  -0.0862 0.0719  392 PHE A CZ  
1826 N N   . THR A 267 ? 0.5615 0.5859 0.3463 0.0596  -0.1035 0.0824  393 THR A N   
1827 C CA  . THR A 267 ? 0.6258 0.6257 0.3701 0.0479  -0.0991 0.0831  393 THR A CA  
1828 C C   . THR A 267 ? 0.6092 0.5776 0.3435 0.0551  -0.0883 0.0919  393 THR A C   
1829 O O   . THR A 267 ? 0.6353 0.5855 0.3373 0.0459  -0.0818 0.0943  393 THR A O   
1830 C CB  . THR A 267 ? 0.6715 0.6845 0.3895 0.0423  -0.1179 0.0934  393 THR A CB  
1831 O OG1 . THR A 267 ? 0.6707 0.6895 0.3984 0.0597  -0.1305 0.1125  393 THR A OG1 
1832 C CG2 . THR A 267 ? 0.7020 0.7467 0.4273 0.0301  -0.1310 0.0849  393 THR A CG2 
1833 N N   . ARG A 268 ? 0.5910 0.5523 0.3503 0.0705  -0.0861 0.0970  394 ARG A N   
1834 C CA  . ARG A 268 ? 0.6111 0.5392 0.3638 0.0745  -0.0762 0.1040  394 ARG A CA  
1835 C C   . ARG A 268 ? 0.5746 0.4960 0.3515 0.0756  -0.0622 0.0907  394 ARG A C   
1836 O O   . ARG A 268 ? 0.5896 0.5264 0.3936 0.0850  -0.0643 0.0842  394 ARG A O   
1837 C CB  . ARG A 268 ? 0.6410 0.5569 0.3960 0.0920  -0.0877 0.1217  394 ARG A CB  
1838 N N   . LYS A 269 ? 0.5788 0.4809 0.3460 0.0656  -0.0479 0.0872  395 LYS A N   
1839 C CA  . LYS A 269 ? 0.6113 0.5100 0.4001 0.0649  -0.0363 0.0747  395 LYS A CA  
1840 C C   . LYS A 269 ? 0.5942 0.4811 0.4022 0.0792  -0.0397 0.0772  395 LYS A C   
1841 O O   . LYS A 269 ? 0.5743 0.4686 0.4035 0.0838  -0.0361 0.0663  395 LYS A O   
1842 C CB  . LYS A 269 ? 0.5617 0.4460 0.3396 0.0528  -0.0219 0.0735  395 LYS A CB  
1843 C CG  . LYS A 269 ? 0.5365 0.4244 0.3349 0.0502  -0.0112 0.0599  395 LYS A CG  
1844 C CD  . LYS A 269 ? 0.6162 0.4858 0.4276 0.0528  -0.0091 0.0627  395 LYS A CD  
1845 C CE  . LYS A 269 ? 0.4973 0.3733 0.3270 0.0490  0.0001  0.0501  395 LYS A CE  
1846 N NZ  . LYS A 269 ? 0.5401 0.3984 0.3810 0.0511  -0.0009 0.0509  395 LYS A NZ  
1847 N N   . ILE A 270 ? 0.6217 0.4875 0.4192 0.0871  -0.0468 0.0917  396 ILE A N   
1848 C CA  . ILE A 270 ? 0.5971 0.4427 0.4072 0.1020  -0.0494 0.0931  396 ILE A CA  
1849 C C   . ILE A 270 ? 0.5655 0.4366 0.3981 0.1197  -0.0561 0.0878  396 ILE A C   
1850 O O   . ILE A 270 ? 0.5760 0.4400 0.4238 0.1311  -0.0530 0.0804  396 ILE A O   
1851 C CB  . ILE A 270 ? 0.6900 0.5011 0.4794 0.1062  -0.0561 0.1112  396 ILE A CB  
1852 C CG1 . ILE A 270 ? 0.7458 0.5255 0.5428 0.1219  -0.0584 0.1112  396 ILE A CG1 
1853 C CG2 . ILE A 270 ? 0.7118 0.5368 0.4892 0.1138  -0.0696 0.1250  396 ILE A CG2 
1854 C CD1 . ILE A 270 ? 0.8179 0.5507 0.5947 0.1129  -0.0570 0.1220  396 ILE A CD1 
1855 N N   . HIS A 271 ? 0.5687 0.4717 0.4035 0.1214  -0.0652 0.0913  397 HIS A N   
1856 C CA  . HIS A 271 ? 0.5389 0.4760 0.3998 0.1350  -0.0704 0.0868  397 HIS A CA  
1857 C C   . HIS A 271 ? 0.5043 0.4586 0.3825 0.1271  -0.0598 0.0700  397 HIS A C   
1858 O O   . HIS A 271 ? 0.4633 0.4327 0.3632 0.1397  -0.0576 0.0643  397 HIS A O   
1859 C CB  . HIS A 271 ? 0.5174 0.4885 0.3773 0.1334  -0.0840 0.0947  397 HIS A CB  
1860 C CG  . HIS A 271 ? 0.6111 0.5688 0.4542 0.1436  -0.0969 0.1132  397 HIS A CG  
1861 N ND1 . HIS A 271 ? 0.6329 0.6145 0.4659 0.1398  -0.1116 0.1235  397 HIS A ND1 
1862 C CD2 . HIS A 271 ? 0.6590 0.5785 0.4908 0.1564  -0.0982 0.1243  397 HIS A CD2 
1863 C CE1 . HIS A 271 ? 0.6800 0.6404 0.4966 0.1513  -0.1214 0.1411  397 HIS A CE1 
1864 N NE2 . HIS A 271 ? 0.6617 0.5824 0.4772 0.1615  -0.1133 0.1422  397 HIS A NE2 
1865 N N   . THR A 272 ? 0.4774 0.4307 0.3455 0.1076  -0.0529 0.0627  398 THR A N   
1866 C CA  . THR A 272 ? 0.4374 0.3987 0.3186 0.1006  -0.0429 0.0486  398 THR A CA  
1867 C C   . THR A 272 ? 0.4689 0.4064 0.3560 0.1078  -0.0349 0.0437  398 THR A C   
1868 O O   . THR A 272 ? 0.4920 0.4402 0.3949 0.1129  -0.0304 0.0351  398 THR A O   
1869 C CB  . THR A 272 ? 0.4450 0.4030 0.3115 0.0817  -0.0370 0.0425  398 THR A CB  
1870 O OG1 . THR A 272 ? 0.4417 0.4202 0.3002 0.0740  -0.0455 0.0442  398 THR A OG1 
1871 C CG2 . THR A 272 ? 0.4731 0.4341 0.3518 0.0759  -0.0273 0.0297  398 THR A CG2 
1872 N N   . ASP A 273 ? 0.5045 0.4093 0.3772 0.1067  -0.0334 0.0493  399 ASP A N   
1873 C CA  . ASP A 273 ? 0.5349 0.4137 0.4101 0.1106  -0.0280 0.0442  399 ASP A CA  
1874 C C   . ASP A 273 ? 0.5221 0.3989 0.4073 0.1319  -0.0315 0.0430  399 ASP A C   
1875 O O   . ASP A 273 ? 0.5442 0.4176 0.4369 0.1367  -0.0260 0.0326  399 ASP A O   
1876 C CB  . ASP A 273 ? 0.5116 0.3558 0.3692 0.1027  -0.0275 0.0526  399 ASP A CB  
1877 C CG  . ASP A 273 ? 0.5669 0.4146 0.4194 0.0833  -0.0194 0.0507  399 ASP A CG  
1878 O OD1 . ASP A 273 ? 0.5944 0.4630 0.4567 0.0782  -0.0142 0.0407  399 ASP A OD1 
1879 O OD2 . ASP A 273 ? 0.6054 0.4353 0.4441 0.0737  -0.0178 0.0598  399 ASP A OD2 
1880 N N   . VAL A 274 ? 0.4742 0.3536 0.3583 0.1463  -0.0404 0.0536  400 VAL A N   
1881 C CA  . VAL A 274 ? 0.5243 0.4048 0.4199 0.1709  -0.0424 0.0524  400 VAL A CA  
1882 C C   . VAL A 274 ? 0.5180 0.4430 0.4369 0.1753  -0.0380 0.0432  400 VAL A C   
1883 O O   . VAL A 274 ? 0.5153 0.4402 0.4427 0.1886  -0.0317 0.0343  400 VAL A O   
1884 C CB  . VAL A 274 ? 0.5539 0.4310 0.4453 0.1871  -0.0541 0.0678  400 VAL A CB  
1885 C CG1 . VAL A 274 ? 0.6094 0.4950 0.5168 0.2168  -0.0553 0.0664  400 VAL A CG1 
1886 C CG2 . VAL A 274 ? 0.6316 0.4587 0.4971 0.1817  -0.0573 0.0779  400 VAL A CG2 
1887 N N   . SER A 275 ? 0.5059 0.4681 0.4331 0.1630  -0.0411 0.0453  401 SER A N   
1888 C CA  . SER A 275 ? 0.4502 0.4546 0.3984 0.1610  -0.0372 0.0383  401 SER A CA  
1889 C C   . SER A 275 ? 0.4420 0.4367 0.3899 0.1532  -0.0254 0.0254  401 SER A C   
1890 O O   . SER A 275 ? 0.4551 0.4701 0.4172 0.1614  -0.0191 0.0191  401 SER A O   
1891 C CB  . SER A 275 ? 0.4833 0.5159 0.4321 0.1422  -0.0435 0.0418  401 SER A CB  
1892 O OG  . SER A 275 ? 0.4342 0.5047 0.4016 0.1353  -0.0406 0.0364  401 SER A OG  
1893 N N   . TYR A 276 ? 0.4746 0.4413 0.4068 0.1375  -0.0221 0.0220  402 TYR A N   
1894 C CA  . TYR A 276 ? 0.4757 0.4340 0.4072 0.1302  -0.0133 0.0113  402 TYR A CA  
1895 C C   . TYR A 276 ? 0.4620 0.4019 0.3922 0.1463  -0.0092 0.0051  402 TYR A C   
1896 O O   . TYR A 276 ? 0.4666 0.4194 0.4029 0.1494  -0.0025 -0.0029 402 TYR A O   
1897 C CB  . TYR A 276 ? 0.3880 0.3222 0.3057 0.1135  -0.0115 0.0106  402 TYR A CB  
1898 C CG  . TYR A 276 ? 0.4225 0.3548 0.3415 0.1044  -0.0048 0.0015  402 TYR A CG  
1899 C CD1 . TYR A 276 ? 0.4282 0.3400 0.3431 0.1086  -0.0020 -0.0046 402 TYR A CD1 
1900 C CD2 . TYR A 276 ? 0.4056 0.3534 0.3273 0.0917  -0.0024 -0.0006 402 TYR A CD2 
1901 C CE1 . TYR A 276 ? 0.4267 0.3387 0.3416 0.1004  0.0022  -0.0115 402 TYR A CE1 
1902 C CE2 . TYR A 276 ? 0.4053 0.3501 0.3275 0.0850  0.0025  -0.0070 402 TYR A CE2 
1903 C CZ  . TYR A 276 ? 0.4045 0.3337 0.3241 0.0894  0.0044  -0.0117 402 TYR A CZ  
1904 O OH  . TYR A 276 ? 0.4115 0.3395 0.3306 0.0828  0.0073  -0.0165 402 TYR A OH  
1905 N N   . ILE A 277 ? 0.4408 0.3465 0.3590 0.1556  -0.0129 0.0086  403 ILE A N   
1906 C CA  . ILE A 277 ? 0.4864 0.3647 0.3972 0.1710  -0.0099 0.0011  403 ILE A CA  
1907 C C   . ILE A 277 ? 0.5146 0.4203 0.4397 0.1939  -0.0064 -0.0015 403 ILE A C   
1908 O O   . ILE A 277 ? 0.5391 0.4435 0.4627 0.2031  0.0014  -0.0123 403 ILE A O   
1909 C CB  . ILE A 277 ? 0.5573 0.3887 0.4504 0.1754  -0.0161 0.0072  403 ILE A CB  
1910 C CG1 . ILE A 277 ? 0.5653 0.3761 0.4472 0.1509  -0.0175 0.0103  403 ILE A CG1 
1911 C CG2 . ILE A 277 ? 0.6106 0.4070 0.4921 0.1938  -0.0140 -0.0020 403 ILE A CG2 
1912 C CD1 . ILE A 277 ? 0.5873 0.3887 0.4655 0.1384  -0.0129 -0.0008 403 ILE A CD1 
1913 N N   . ALA A 278 ? 0.5326 0.4652 0.4715 0.2044  -0.0121 0.0088  404 ALA A N   
1914 C CA  . ALA A 278 ? 0.4953 0.4650 0.4545 0.2265  -0.0084 0.0081  404 ALA A CA  
1915 C C   . ALA A 278 ? 0.5001 0.5078 0.4721 0.2169  0.0014  0.0003  404 ALA A C   
1916 O O   . ALA A 278 ? 0.4833 0.5033 0.4607 0.2323  0.0111  -0.0075 404 ALA A O   
1917 C CB  . ALA A 278 ? 0.5276 0.5308 0.5035 0.2338  -0.0185 0.0222  404 ALA A CB  
1918 N N   . CYS A 279 ? 0.4572 0.4818 0.4319 0.1918  -0.0005 0.0025  405 CYS A N   
1919 C CA  . CYS A 279 ? 0.4650 0.5223 0.4500 0.1802  0.0075  -0.0024 405 CYS A CA  
1920 C C   . CYS A 279 ? 0.4686 0.4994 0.4373 0.1770  0.0163  -0.0139 405 CYS A C   
1921 O O   . CYS A 279 ? 0.4667 0.5206 0.4407 0.1773  0.0255  -0.0187 405 CYS A O   
1922 C CB  . CYS A 279 ? 0.4283 0.5008 0.4160 0.1551  0.0018  0.0027  405 CYS A CB  
1923 S SG  . CYS A 279 ? 0.5355 0.6491 0.5424 0.1572  -0.0102 0.0155  405 CYS A SG  
1924 N N   . ALA A 280 ? 0.4639 0.4486 0.4123 0.1723  0.0132  -0.0173 406 ALA A N   
1925 C CA  . ALA A 280 ? 0.4581 0.4170 0.3897 0.1694  0.0187  -0.0280 406 ALA A CA  
1926 C C   . ALA A 280 ? 0.5499 0.5015 0.4753 0.1926  0.0259  -0.0367 406 ALA A C   
1927 O O   . ALA A 280 ? 0.5123 0.4654 0.4286 0.1926  0.0338  -0.0458 406 ALA A O   
1928 C CB  . ALA A 280 ? 0.4651 0.3803 0.3795 0.1584  0.0123  -0.0285 406 ALA A CB  
1929 N N   . ALA A 281 ? 0.5259 0.4653 0.4525 0.2135  0.0231  -0.0344 407 ALA A N   
1930 C CA  . ALA A 281 ? 0.5395 0.4713 0.4600 0.2402  0.0312  -0.0436 407 ALA A CA  
1931 C C   . ALA A 281 ? 0.5346 0.5224 0.4752 0.2488  0.0428  -0.0446 407 ALA A C   
1932 O O   . ALA A 281 ? 0.5675 0.5553 0.4985 0.2556  0.0532  -0.0547 407 ALA A O   
1933 C CB  . ALA A 281 ? 0.6156 0.5275 0.5375 0.2589  0.0246  -0.0375 407 ALA A CB  
1934 N N   . LYS A 282 ? 0.5034 0.5400 0.4713 0.2417  0.0402  -0.0330 408 LYS A N   
1935 C CA  . LYS A 282 ? 0.4636 0.5587 0.4539 0.2455  0.0508  -0.0316 408 LYS A CA  
1936 C C   . LYS A 282 ? 0.4602 0.5602 0.4394 0.2253  0.0589  -0.0374 408 LYS A C   
1937 O O   . LYS A 282 ? 0.4913 0.6163 0.4717 0.2338  0.0726  -0.0427 408 LYS A O   
1938 C CB  . LYS A 282 ? 0.4776 0.6206 0.4976 0.2363  0.0427  -0.0173 408 LYS A CB  
1939 C CG  . LYS A 282 ? 0.4871 0.6957 0.5342 0.2342  0.0521  -0.0133 408 LYS A CG  
1940 C CD  . LYS A 282 ? 0.5064 0.7568 0.5792 0.2187  0.0404  0.0004  408 LYS A CD  
1941 C CE  . LYS A 282 ? 0.5105 0.7599 0.5933 0.2377  0.0281  0.0083  408 LYS A CE  
1942 N NZ  . LYS A 282 ? 0.4963 0.7797 0.6015 0.2722  0.0349  0.0097  408 LYS A NZ  
1943 N N   . LEU A 283 ? 0.4678 0.5445 0.4353 0.1998  0.0512  -0.0357 409 LEU A N   
1944 C CA  . LEU A 283 ? 0.4804 0.5561 0.4352 0.1815  0.0565  -0.0395 409 LEU A CA  
1945 C C   . LEU A 283 ? 0.4996 0.5428 0.4269 0.1916  0.0632  -0.0527 409 LEU A C   
1946 O O   . LEU A 283 ? 0.4919 0.5500 0.4109 0.1890  0.0733  -0.0568 409 LEU A O   
1947 C CB  . LEU A 283 ? 0.4632 0.5187 0.4123 0.1570  0.0462  -0.0349 409 LEU A CB  
1948 C CG  . LEU A 283 ? 0.4423 0.5296 0.4108 0.1407  0.0416  -0.0243 409 LEU A CG  
1949 C CD1 . LEU A 283 ? 0.3950 0.4548 0.3544 0.1227  0.0324  -0.0220 409 LEU A CD1 
1950 C CD2 . LEU A 283 ? 0.4543 0.5761 0.4294 0.1296  0.0502  -0.0218 409 LEU A CD2 
1951 N N   . LEU A 284 ? 0.5342 0.5310 0.4445 0.2011  0.0571  -0.0592 410 LEU A N   
1952 C CA  . LEU A 284 ? 0.5985 0.5580 0.4781 0.2077  0.0608  -0.0732 410 LEU A CA  
1953 C C   . LEU A 284 ? 0.5727 0.5479 0.4503 0.2287  0.0738  -0.0805 410 LEU A C   
1954 O O   . LEU A 284 ? 0.5849 0.5450 0.4393 0.2268  0.0792  -0.0904 410 LEU A O   
1955 C CB  . LEU A 284 ? 0.5803 0.4848 0.4429 0.2093  0.0497  -0.0771 410 LEU A CB  
1956 C CG  . LEU A 284 ? 0.6031 0.4892 0.4631 0.1832  0.0380  -0.0716 410 LEU A CG  
1957 C CD1 . LEU A 284 ? 0.6253 0.4640 0.4734 0.1836  0.0280  -0.0722 410 LEU A CD1 
1958 C CD2 . LEU A 284 ? 0.5984 0.4791 0.4405 0.1685  0.0389  -0.0780 410 LEU A CD2 
1959 N N   . ALA A 285 ? 0.5593 0.5665 0.4627 0.2444  0.0773  -0.0740 411 ALA A N   
1960 C CA  . ALA A 285 ? 0.5999 0.6296 0.5083 0.2606  0.0896  -0.0783 411 ALA A CA  
1961 C C   . ALA A 285 ? 0.5364 0.6187 0.4552 0.2537  0.1030  -0.0756 411 ALA A C   
1962 O O   . ALA A 285 ? 0.6000 0.7034 0.5209 0.2651  0.1154  -0.0796 411 ALA A O   
1963 C CB  . ALA A 285 ? 0.5626 0.6115 0.4973 0.2802  0.0875  -0.0708 411 ALA A CB  
1964 N N   . ALA A 286 ? 0.5540 0.6569 0.4781 0.2349  0.1016  -0.0687 412 ALA A N   
1965 C CA  . ALA A 286 ? 0.5493 0.7047 0.4853 0.2244  0.1137  -0.0626 412 ALA A CA  
1966 C C   . ALA A 286 ? 0.5400 0.6770 0.4496 0.2017  0.1132  -0.0641 412 ALA A C   
1967 O O   . ALA A 286 ? 0.5046 0.6730 0.4243 0.1814  0.1157  -0.0537 412 ALA A O   
1968 C CB  . ALA A 286 ? 0.5164 0.7208 0.4902 0.2150  0.1094  -0.0474 412 ALA A CB  
1969 N N   . THR A 287 ? 0.5509 0.6350 0.4270 0.2020  0.1076  -0.0753 413 THR A N   
1970 C CA  . THR A 287 ? 0.5669 0.6319 0.4201 0.1791  0.1028  -0.0745 413 THR A CA  
1971 C C   . THR A 287 ? 0.6030 0.6945 0.4412 0.1765  0.1180  -0.0751 413 THR A C   
1972 O O   . THR A 287 ? 0.5915 0.6773 0.4150 0.1561  0.1144  -0.0699 413 THR A O   
1973 C CB  . THR A 287 ? 0.5896 0.5970 0.4123 0.1792  0.0919  -0.0860 413 THR A CB  
1974 O OG1 . THR A 287 ? 0.6358 0.6234 0.4410 0.1973  0.0978  -0.0992 413 THR A OG1 
1975 C CG2 . THR A 287 ? 0.5566 0.5392 0.3937 0.1737  0.0761  -0.0814 413 THR A CG2 
1976 N N   . ASP A 288 ? 0.5954 0.7138 0.4411 0.1923  0.1322  -0.0786 414 ASP A N   
1977 C CA  . ASP A 288 ? 0.6002 0.7505 0.4382 0.1853  0.1471  -0.0755 414 ASP A CA  
1978 C C   . ASP A 288 ? 0.5680 0.7629 0.4250 0.1658  0.1507  -0.0586 414 ASP A C   
1979 O O   . ASP A 288 ? 0.6060 0.8063 0.4434 0.1490  0.1554  -0.0529 414 ASP A O   
1980 C CB  . ASP A 288 ? 0.5984 0.7740 0.4498 0.2043  0.1609  -0.0802 414 ASP A CB  
1981 C CG  . ASP A 288 ? 0.7033 0.8322 0.5273 0.2208  0.1601  -0.0976 414 ASP A CG  
1982 O OD1 . ASP A 288 ? 0.7535 0.8380 0.5424 0.2122  0.1520  -0.1058 414 ASP A OD1 
1983 O OD2 . ASP A 288 ? 0.7487 0.8856 0.5855 0.2418  0.1671  -0.1028 414 ASP A OD2 
1984 N N   . VAL A 289 ? 0.5328 0.7549 0.4272 0.1634  0.1454  -0.0489 415 VAL A N   
1985 C CA  . VAL A 289 ? 0.5011 0.7642 0.4197 0.1393  0.1460  -0.0319 415 VAL A CA  
1986 C C   . VAL A 289 ? 0.4809 0.7188 0.4068 0.1167  0.1265  -0.0235 415 VAL A C   
1987 O O   . VAL A 289 ? 0.5109 0.7667 0.4455 0.0926  0.1250  -0.0107 415 VAL A O   
1988 C CB  . VAL A 289 ? 0.4689 0.7955 0.4275 0.1498  0.1564  -0.0256 415 VAL A CB  
1989 C CG1 . VAL A 289 ? 0.5467 0.8932 0.5006 0.1650  0.1737  -0.0316 415 VAL A CG1 
1990 C CG2 . VAL A 289 ? 0.4623 0.7818 0.4435 0.1670  0.1448  -0.0285 415 VAL A CG2 
1991 N N   . VAL A 290 ? 0.4223 0.6188 0.3438 0.1231  0.1124  -0.0300 416 VAL A N   
1992 C CA  . VAL A 290 ? 0.4318 0.6024 0.3559 0.1041  0.0962  -0.0238 416 VAL A CA  
1993 C C   . VAL A 290 ? 0.4668 0.5853 0.3636 0.1055  0.0872  -0.0321 416 VAL A C   
1994 O O   . VAL A 290 ? 0.4821 0.5809 0.3613 0.1218  0.0900  -0.0436 416 VAL A O   
1995 C CB  . VAL A 290 ? 0.4756 0.6566 0.4274 0.1066  0.0869  -0.0202 416 VAL A CB  
1996 C CG1 . VAL A 290 ? 0.4064 0.6444 0.3878 0.1017  0.0932  -0.0105 416 VAL A CG1 
1997 C CG2 . VAL A 290 ? 0.4250 0.5871 0.3762 0.1318  0.0846  -0.0299 416 VAL A CG2 
1998 N N   . PHE A 291 ? 0.4328 0.5293 0.3257 0.0877  0.0762  -0.0262 417 PHE A N   
1999 C CA  . PHE A 291 ? 0.4824 0.5369 0.3577 0.0861  0.0654  -0.0310 417 PHE A CA  
2000 C C   . PHE A 291 ? 0.4759 0.5167 0.3670 0.0860  0.0549  -0.0303 417 PHE A C   
2001 O O   . PHE A 291 ? 0.4332 0.4730 0.3331 0.0727  0.0491  -0.0230 417 PHE A O   
2002 C CB  . PHE A 291 ? 0.4778 0.5209 0.3384 0.0692  0.0616  -0.0237 417 PHE A CB  
2003 C CG  . PHE A 291 ? 0.4863 0.4943 0.3343 0.0672  0.0496  -0.0265 417 PHE A CG  
2004 C CD1 . PHE A 291 ? 0.5147 0.5035 0.3447 0.0763  0.0471  -0.0368 417 PHE A CD1 
2005 C CD2 . PHE A 291 ? 0.4553 0.4505 0.3089 0.0560  0.0408  -0.0190 417 PHE A CD2 
2006 C CE1 . PHE A 291 ? 0.5177 0.4807 0.3400 0.0720  0.0348  -0.0381 417 PHE A CE1 
2007 C CE2 . PHE A 291 ? 0.4663 0.4373 0.3133 0.0555  0.0305  -0.0205 417 PHE A CE2 
2008 C CZ  . PHE A 291 ? 0.4793 0.4372 0.3125 0.0623  0.0271  -0.0293 417 PHE A CZ  
2009 N N   . PRO A 292 ? 0.4666 0.4946 0.3593 0.1005  0.0527  -0.0376 418 PRO A N   
2010 C CA  . PRO A 292 ? 0.4408 0.4555 0.3452 0.0993  0.0434  -0.0354 418 PRO A CA  
2011 C C   . PRO A 292 ? 0.4300 0.4164 0.3256 0.0887  0.0346  -0.0350 418 PRO A C   
2012 O O   . PRO A 292 ? 0.4208 0.3880 0.3001 0.0886  0.0322  -0.0400 418 PRO A O   
2013 C CB  . PRO A 292 ? 0.4533 0.4570 0.3567 0.1180  0.0439  -0.0424 418 PRO A CB  
2014 C CG  . PRO A 292 ? 0.4806 0.5015 0.3779 0.1315  0.0556  -0.0481 418 PRO A CG  
2015 C CD  . PRO A 292 ? 0.4556 0.4786 0.3372 0.1192  0.0592  -0.0478 418 PRO A CD  
2016 N N   . GLN A 293 ? 0.4061 0.3922 0.3125 0.0800  0.0296  -0.0291 419 GLN A N   
2017 C CA  . GLN A 293 ? 0.3755 0.3415 0.2788 0.0719  0.0229  -0.0276 419 GLN A CA  
2018 C C   . GLN A 293 ? 0.3968 0.3556 0.3085 0.0739  0.0190  -0.0267 419 GLN A C   
2019 O O   . GLN A 293 ? 0.3786 0.3487 0.2988 0.0710  0.0189  -0.0228 419 GLN A O   
2020 C CB  . GLN A 293 ? 0.4458 0.4160 0.3498 0.0603  0.0227  -0.0214 419 GLN A CB  
2021 C CG  . GLN A 293 ? 0.4165 0.3920 0.3091 0.0569  0.0263  -0.0197 419 GLN A CG  
2022 C CD  . GLN A 293 ? 0.4720 0.4514 0.3649 0.0450  0.0270  -0.0120 419 GLN A CD  
2023 O OE1 . GLN A 293 ? 0.4354 0.4265 0.3380 0.0394  0.0282  -0.0093 419 GLN A OE1 
2024 N NE2 . GLN A 293 ? 0.4401 0.4073 0.3209 0.0400  0.0248  -0.0078 419 GLN A NE2 
2025 N N   . PHE A 294 ? 0.4179 0.3578 0.3251 0.0772  0.0153  -0.0299 420 PHE A N   
2026 C CA  . PHE A 294 ? 0.3941 0.3261 0.3061 0.0794  0.0125  -0.0278 420 PHE A CA  
2027 C C   . PHE A 294 ? 0.3957 0.3219 0.3111 0.0701  0.0101  -0.0241 420 PHE A C   
2028 O O   . PHE A 294 ? 0.4039 0.3188 0.3179 0.0663  0.0073  -0.0247 420 PHE A O   
2029 C CB  . PHE A 294 ? 0.4140 0.3261 0.3179 0.0873  0.0104  -0.0322 420 PHE A CB  
2030 C CG  . PHE A 294 ? 0.4474 0.3656 0.3482 0.1011  0.0148  -0.0366 420 PHE A CG  
2031 C CD1 . PHE A 294 ? 0.4882 0.4242 0.3996 0.1097  0.0166  -0.0326 420 PHE A CD1 
2032 C CD2 . PHE A 294 ? 0.4915 0.4005 0.3786 0.1062  0.0171  -0.0448 420 PHE A CD2 
2033 C CE1 . PHE A 294 ? 0.4854 0.4331 0.3981 0.1254  0.0219  -0.0362 420 PHE A CE1 
2034 C CE2 . PHE A 294 ? 0.5245 0.4411 0.4082 0.1217  0.0238  -0.0499 420 PHE A CE2 
2035 C CZ  . PHE A 294 ? 0.4840 0.4219 0.3828 0.1322  0.0267  -0.0452 420 PHE A CZ  
2036 N N   . ALA A 295 ? 0.3935 0.3292 0.3135 0.0665  0.0114  -0.0205 421 ALA A N   
2037 C CA  . ALA A 295 ? 0.3699 0.3016 0.2914 0.0603  0.0118  -0.0183 421 ALA A CA  
2038 C C   . ALA A 295 ? 0.4202 0.3456 0.3412 0.0606  0.0111  -0.0154 421 ALA A C   
2039 O O   . ALA A 295 ? 0.4514 0.3810 0.3702 0.0618  0.0106  -0.0131 421 ALA A O   
2040 C CB  . ALA A 295 ? 0.3779 0.3168 0.2982 0.0558  0.0133  -0.0175 421 ALA A CB  
2041 N N   . THR A 296 ? 0.3900 0.3071 0.3129 0.0579  0.0106  -0.0142 422 THR A N   
2042 C CA  . THR A 296 ? 0.3780 0.2890 0.2993 0.0555  0.0111  -0.0095 422 THR A CA  
2043 C C   . THR A 296 ? 0.4204 0.3314 0.3487 0.0489  0.0123  -0.0073 422 THR A C   
2044 O O   . THR A 296 ? 0.3874 0.2987 0.3207 0.0470  0.0091  -0.0097 422 THR A O   
2045 C CB  . THR A 296 ? 0.4070 0.3048 0.3224 0.0601  0.0070  -0.0081 422 THR A CB  
2046 O OG1 . THR A 296 ? 0.4363 0.3258 0.3472 0.0562  0.0072  -0.0010 422 THR A OG1 
2047 C CG2 . THR A 296 ? 0.4695 0.3536 0.3832 0.0599  0.0034  -0.0122 422 THR A CG2 
2048 N N   . HIS A 297 ? 0.4076 0.3209 0.3359 0.0447  0.0165  -0.0022 423 HIS A N   
2049 C CA  . HIS A 297 ? 0.4160 0.3355 0.3543 0.0371  0.0188  0.0021  423 HIS A CA  
2050 C C   . HIS A 297 ? 0.4487 0.3550 0.3818 0.0297  0.0167  0.0088  423 HIS A C   
2051 O O   . HIS A 297 ? 0.4434 0.3566 0.3847 0.0199  0.0191  0.0146  423 HIS A O   
2052 C CB  . HIS A 297 ? 0.4297 0.3647 0.3723 0.0380  0.0283  0.0036  423 HIS A CB  
2053 C CG  . HIS A 297 ? 0.4219 0.3616 0.3656 0.0456  0.0300  -0.0026 423 HIS A CG  
2054 N ND1 . HIS A 297 ? 0.4350 0.3716 0.3667 0.0496  0.0345  -0.0059 423 HIS A ND1 
2055 C CD2 . HIS A 297 ? 0.4321 0.3752 0.3841 0.0488  0.0266  -0.0054 423 HIS A CD2 
2056 C CE1 . HIS A 297 ? 0.4183 0.3537 0.3513 0.0544  0.0343  -0.0105 423 HIS A CE1 
2057 N NE2 . HIS A 297 ? 0.4066 0.3465 0.3520 0.0547  0.0296  -0.0095 423 HIS A NE2 
2058 N N   . ASN A 298 ? 0.4226 0.3109 0.3431 0.0342  0.0121  0.0089  424 ASN A N   
2059 C CA  . ASN A 298 ? 0.4684 0.3369 0.3792 0.0293  0.0093  0.0165  424 ASN A CA  
2060 C C   . ASN A 298 ? 0.4499 0.2968 0.3589 0.0260  0.0016  0.0134  424 ASN A C   
2061 O O   . ASN A 298 ? 0.4383 0.2751 0.3419 0.0360  -0.0025 0.0059  424 ASN A O   
2062 C CB  . ASN A 298 ? 0.4817 0.3423 0.3796 0.0393  0.0074  0.0189  424 ASN A CB  
2063 C CG  . ASN A 298 ? 0.5144 0.3498 0.3993 0.0370  0.0034  0.0286  424 ASN A CG  
2064 O OD1 . ASN A 298 ? 0.5042 0.3176 0.3867 0.0308  -0.0007 0.0300  424 ASN A OD1 
2065 N ND2 . ASN A 298 ? 0.4858 0.3214 0.3597 0.0415  0.0031  0.0357  424 ASN A ND2 
2066 N N   . ALA A 299 ? 0.5067 0.3467 0.4186 0.0111  -0.0001 0.0190  425 ALA A N   
2067 C CA  . ALA A 299 ? 0.4835 0.3003 0.3910 0.0041  -0.0090 0.0148  425 ALA A CA  
2068 C C   . ALA A 299 ? 0.5367 0.3152 0.4239 0.0133  -0.0145 0.0126  425 ALA A C   
2069 O O   . ALA A 299 ? 0.5510 0.3084 0.4291 0.0166  -0.0206 0.0032  425 ALA A O   
2070 C CB  . ALA A 299 ? 0.5095 0.3272 0.4245 -0.0174 -0.0105 0.0233  425 ALA A CB  
2071 N N   . GLN A 300 ? 0.5420 0.3104 0.4203 0.0187  -0.0125 0.0213  426 GLN A N   
2072 C CA  . GLN A 300 ? 0.5676 0.3004 0.4283 0.0316  -0.0179 0.0210  426 GLN A CA  
2073 C C   . GLN A 300 ? 0.5565 0.2998 0.4187 0.0525  -0.0170 0.0105  426 GLN A C   
2074 O O   . GLN A 300 ? 0.5829 0.3022 0.4349 0.0634  -0.0205 0.0021  426 GLN A O   
2075 C CB  . GLN A 300 ? 0.5776 0.3011 0.4290 0.0324  -0.0172 0.0355  426 GLN A CB  
2076 C CG  . GLN A 300 ? 0.6424 0.3209 0.4742 0.0434  -0.0245 0.0395  426 GLN A CG  
2077 C CD  . GLN A 300 ? 0.6674 0.3480 0.4989 0.0699  -0.0259 0.0315  426 GLN A CD  
2078 O OE1 . GLN A 300 ? 0.6707 0.3883 0.5142 0.0787  -0.0220 0.0295  426 GLN A OE1 
2079 N NE2 . GLN A 300 ? 0.7494 0.3904 0.5669 0.0822  -0.0311 0.0267  426 GLN A NE2 
2080 N N   . THR A 301 ? 0.5108 0.2900 0.3847 0.0576  -0.0116 0.0104  427 THR A N   
2081 C CA  . THR A 301 ? 0.4958 0.2915 0.3742 0.0733  -0.0100 0.0020  427 THR A CA  
2082 C C   . THR A 301 ? 0.5282 0.3216 0.4066 0.0730  -0.0103 -0.0098 427 THR A C   
2083 O O   . THR A 301 ? 0.5240 0.3092 0.3960 0.0867  -0.0104 -0.0176 427 THR A O   
2084 C CB  . THR A 301 ? 0.4766 0.3078 0.3659 0.0724  -0.0052 0.0038  427 THR A CB  
2085 O OG1 . THR A 301 ? 0.4862 0.3187 0.3710 0.0699  -0.0053 0.0144  427 THR A OG1 
2086 C CG2 . THR A 301 ? 0.4868 0.3364 0.3814 0.0861  -0.0042 -0.0018 427 THR A CG2 
2087 N N   . LEU A 302 ? 0.4730 0.2759 0.3580 0.0584  -0.0102 -0.0108 428 LEU A N   
2088 C CA  . LEU A 302 ? 0.5090 0.3106 0.3917 0.0561  -0.0125 -0.0206 428 LEU A CA  
2089 C C   . LEU A 302 ? 0.5565 0.3197 0.4204 0.0581  -0.0184 -0.0273 428 LEU A C   
2090 O O   . LEU A 302 ? 0.5615 0.3178 0.4149 0.0687  -0.0179 -0.0377 428 LEU A O   
2091 C CB  . LEU A 302 ? 0.4994 0.3175 0.3942 0.0399  -0.0138 -0.0176 428 LEU A CB  
2092 C CG  . LEU A 302 ? 0.5208 0.3470 0.4166 0.0351  -0.0178 -0.0245 428 LEU A CG  
2093 C CD1 . LEU A 302 ? 0.5006 0.3524 0.4153 0.0243  -0.0172 -0.0176 428 LEU A CD1 
2094 C CD2 . LEU A 302 ? 0.5114 0.3086 0.3917 0.0279  -0.0266 -0.0310 428 LEU A CD2 
2095 N N   . ALA A 303 ? 0.5687 0.3046 0.4259 0.0472  -0.0234 -0.0217 429 ALA A N   
2096 C CA  . ALA A 303 ? 0.5886 0.2792 0.4239 0.0466  -0.0304 -0.0289 429 ALA A CA  
2097 C C   . ALA A 303 ? 0.6418 0.3124 0.4634 0.0714  -0.0276 -0.0351 429 ALA A C   
2098 O O   . ALA A 303 ? 0.6903 0.3354 0.4935 0.0798  -0.0293 -0.0478 429 ALA A O   
2099 C CB  . ALA A 303 ? 0.6349 0.2976 0.4651 0.0292  -0.0360 -0.0188 429 ALA A CB  
2100 N N   . ALA A 304 ? 0.6141 0.2980 0.4441 0.0843  -0.0234 -0.0264 430 ALA A N   
2101 C CA  . ALA A 304 ? 0.6317 0.3047 0.4544 0.1101  -0.0210 -0.0305 430 ALA A CA  
2102 C C   . ALA A 304 ? 0.6308 0.3297 0.4570 0.1229  -0.0143 -0.0425 430 ALA A C   
2103 O O   . ALA A 304 ? 0.6875 0.3659 0.4991 0.1397  -0.0123 -0.0532 430 ALA A O   
2104 C CB  . ALA A 304 ? 0.6240 0.3149 0.4581 0.1195  -0.0198 -0.0172 430 ALA A CB  
2105 N N   . ILE A 305 ? 0.6235 0.3653 0.4668 0.1151  -0.0102 -0.0408 431 ILE A N   
2106 C CA  . ILE A 305 ? 0.5875 0.3544 0.4330 0.1242  -0.0035 -0.0497 431 ILE A CA  
2107 C C   . ILE A 305 ? 0.6174 0.3611 0.4427 0.1196  -0.0055 -0.0624 431 ILE A C   
2108 O O   . ILE A 305 ? 0.6238 0.3657 0.4373 0.1338  -0.0001 -0.0729 431 ILE A O   
2109 C CB  . ILE A 305 ? 0.5412 0.3512 0.4059 0.1145  -0.0001 -0.0439 431 ILE A CB  
2110 C CG1 . ILE A 305 ? 0.5931 0.4316 0.4733 0.1245  0.0034  -0.0364 431 ILE A CG1 
2111 C CG2 . ILE A 305 ? 0.5868 0.4140 0.4482 0.1142  0.0045  -0.0519 431 ILE A CG2 
2112 C CD1 . ILE A 305 ? 0.6161 0.4421 0.4976 0.1263  -0.0012 -0.0271 431 ILE A CD1 
2113 N N   . TYR A 306 ? 0.6282 0.3557 0.4488 0.0994  -0.0135 -0.0614 432 TYR A N   
2114 C CA  . TYR A 306 ? 0.6261 0.3335 0.4268 0.0912  -0.0185 -0.0728 432 TYR A CA  
2115 C C   . TYR A 306 ? 0.6764 0.3386 0.4487 0.1049  -0.0191 -0.0855 432 TYR A C   
2116 O O   . TYR A 306 ? 0.7266 0.3794 0.4781 0.1104  -0.0174 -0.0989 432 TYR A O   
2117 C CB  . TYR A 306 ? 0.6390 0.3399 0.4442 0.0661  -0.0286 -0.0672 432 TYR A CB  
2118 C CG  . TYR A 306 ? 0.6816 0.3558 0.4648 0.0532  -0.0384 -0.0777 432 TYR A CG  
2119 C CD1 . TYR A 306 ? 0.6490 0.3398 0.4248 0.0510  -0.0395 -0.0849 432 TYR A CD1 
2120 C CD2 . TYR A 306 ? 0.7232 0.3542 0.4909 0.0408  -0.0479 -0.0795 432 TYR A CD2 
2121 C CE1 . TYR A 306 ? 0.6983 0.3656 0.4515 0.0376  -0.0506 -0.0945 432 TYR A CE1 
2122 C CE2 . TYR A 306 ? 0.7297 0.3351 0.4754 0.0258  -0.0591 -0.0897 432 TYR A CE2 
2123 C CZ  . TYR A 306 ? 0.7534 0.3785 0.4920 0.0244  -0.0608 -0.0975 432 TYR A CZ  
2124 O OH  . TYR A 306 ? 0.7960 0.3957 0.5098 0.0082  -0.0739 -0.1078 432 TYR A OH  
2125 N N   . HIS A 307 ? 0.7384 0.3693 0.5064 0.1116  -0.0213 -0.0814 433 HIS A N   
2126 C CA  . HIS A 307 ? 0.7603 0.3449 0.5017 0.1265  -0.0217 -0.0927 433 HIS A CA  
2127 C C   . HIS A 307 ? 0.7537 0.3648 0.5049 0.1538  -0.0097 -0.0941 433 HIS A C   
2128 O O   . HIS A 307 ? 0.7725 0.3737 0.5095 0.1646  -0.0051 -0.1050 433 HIS A O   
2129 C CB  . HIS A 307 ? 0.7844 0.3277 0.5198 0.1177  -0.0302 -0.0844 433 HIS A CB  
2130 C CG  . HIS A 307 ? 0.8171 0.3327 0.5412 0.0878  -0.0424 -0.0843 433 HIS A CG  
2131 N ND1 . HIS A 307 ? 0.8624 0.3450 0.5632 0.0757  -0.0497 -0.0954 433 HIS A ND1 
2132 C CD2 . HIS A 307 ? 0.7557 0.2965 0.5009 0.0633  -0.0468 -0.0710 433 HIS A CD2 
2133 C CE1 . HIS A 307 ? 0.8700 0.3405 0.5694 0.0462  -0.0613 -0.0915 433 HIS A CE1 
2134 N NE2 . HIS A 307 ? 0.7990 0.3125 0.5301 0.0384  -0.0582 -0.0752 433 HIS A NE2 
2135 N N   . MET A 308 ? 0.7247 0.3712 0.4999 0.1643  -0.0046 -0.0834 434 MET A N   
2136 C CA  . MET A 308 ? 0.6961 0.3769 0.4853 0.1876  0.0060  -0.0837 434 MET A CA  
2137 C C   . MET A 308 ? 0.7089 0.4148 0.4931 0.1909  0.0152  -0.0948 434 MET A C   
2138 O O   . MET A 308 ? 0.7404 0.4619 0.5270 0.2088  0.0245  -0.0993 434 MET A O   
2139 C CB  . MET A 308 ? 0.7178 0.4376 0.5335 0.1929  0.0078  -0.0704 434 MET A CB  
2140 C CG  . MET A 308 ? 0.7988 0.5050 0.6213 0.2015  0.0023  -0.0584 434 MET A CG  
2141 S SD  . MET A 308 ? 0.8583 0.6113 0.7086 0.1965  0.0007  -0.0418 434 MET A SD  
2142 C CE  . MET A 308 ? 0.7167 0.5283 0.5852 0.2027  0.0121  -0.0477 434 MET A CE  
2143 N N   . ALA A 309 ? 0.7136 0.4252 0.4908 0.1741  0.0131  -0.0982 435 ALA A N   
2144 C CA  . ALA A 309 ? 0.7319 0.4682 0.5018 0.1750  0.0213  -0.1063 435 ALA A CA  
2145 C C   . ALA A 309 ? 0.7825 0.4891 0.5238 0.1758  0.0214  -0.1202 435 ALA A C   
2146 O O   . ALA A 309 ? 0.7656 0.4912 0.4975 0.1790  0.0298  -0.1271 435 ALA A O   
2147 C CB  . ALA A 309 ? 0.6447 0.4005 0.4200 0.1535  0.0166  -0.1014 435 ALA A CB  
2148 N N   . GLY A 310 ? 0.7980 0.4579 0.5235 0.1719  0.0126  -0.1242 436 GLY A N   
2149 C CA  . GLY A 310 ? 0.8362 0.4636 0.5324 0.1725  0.0120  -0.1384 436 GLY A CA  
2150 C C   . GLY A 310 ? 0.8759 0.4886 0.5494 0.1499  0.0024  -0.1457 436 GLY A C   
2151 O O   . GLY A 310 ? 0.8695 0.4953 0.5503 0.1336  -0.0047 -0.1395 436 GLY A O   
2152 N N   . LYS A 311 ? 0.9037 0.4887 0.5479 0.1496  0.0016  -0.1594 437 LYS A N   
2153 C CA  . LYS A 311 ? 0.9618 0.5312 0.5810 0.1279  -0.0096 -0.1672 437 LYS A CA  
2154 C C   . LYS A 311 ? 0.9548 0.5616 0.5687 0.1273  -0.0031 -0.1692 437 LYS A C   
2155 O O   . LYS A 311 ? 0.9825 0.5887 0.5829 0.1078  -0.0144 -0.1704 437 LYS A O   
2156 C CB  . LYS A 311 ? 0.9688 0.4912 0.5557 0.1264  -0.0142 -0.1816 437 LYS A CB  
2157 N N   . ASP A 312 ? 0.8930 0.5337 0.5174 0.1470  0.0141  -0.1682 438 ASP A N   
2158 C CA  . ASP A 312 ? 0.9002 0.5755 0.5169 0.1461  0.0222  -0.1690 438 ASP A CA  
2159 C C   . ASP A 312 ? 0.8806 0.5888 0.5184 0.1365  0.0193  -0.1554 438 ASP A C   
2160 O O   . ASP A 312 ? 0.8399 0.5707 0.5073 0.1450  0.0251  -0.1453 438 ASP A O   
2161 C CB  . ASP A 312 ? 0.9209 0.6225 0.5431 0.1687  0.0423  -0.1719 438 ASP A CB  
2162 C CG  . ASP A 312 ? 0.9589 0.7049 0.5814 0.1670  0.0530  -0.1673 438 ASP A CG  
2163 O OD1 . ASP A 312 ? 1.0259 0.7672 0.6189 0.1569  0.0510  -0.1739 438 ASP A OD1 
2164 O OD2 . ASP A 312 ? 0.9742 0.7599 0.6253 0.1746  0.0630  -0.1563 438 ASP A OD2 
2165 N N   . PHE A 313 ? 0.8336 0.5447 0.4552 0.1193  0.0097  -0.1549 439 PHE A N   
2166 C CA  . PHE A 313 ? 0.8162 0.5573 0.4543 0.1121  0.0076  -0.1422 439 PHE A CA  
2167 C C   . PHE A 313 ? 0.7979 0.5565 0.4160 0.1018  0.0058  -0.1403 439 PHE A C   
2168 O O   . PHE A 313 ? 0.8563 0.5936 0.4428 0.0932  -0.0030 -0.1497 439 PHE A O   
2169 C CB  . PHE A 313 ? 0.7484 0.4846 0.4120 0.0939  -0.0086 -0.1316 439 PHE A CB  
2170 C CG  . PHE A 313 ? 0.7096 0.4865 0.4067 0.0852  -0.0088 -0.1136 439 PHE A CG  
2171 C CD1 . PHE A 313 ? 0.6673 0.4694 0.3946 0.0941  0.0017  -0.1040 439 PHE A CD1 
2172 C CD2 . PHE A 313 ? 0.6665 0.4559 0.3623 0.0694  -0.0197 -0.1067 439 PHE A CD2 
2173 C CE1 . PHE A 313 ? 0.6199 0.4531 0.3732 0.0862  0.0016  -0.0894 439 PHE A CE1 
2174 C CE2 . PHE A 313 ? 0.6305 0.4516 0.3541 0.0644  -0.0190 -0.0911 439 PHE A CE2 
2175 C CZ  . PHE A 313 ? 0.6187 0.4592 0.3694 0.0723  -0.0081 -0.0833 439 PHE A CZ  
2176 N N   . HIS A 314 ? 0.7589 0.5581 0.3997 0.1002  0.0130  -0.1255 440 HIS A N   
2177 C CA  . HIS A 314 ? 0.7413 0.5582 0.3692 0.0883  0.0091  -0.1178 440 HIS A CA  
2178 C C   . HIS A 314 ? 0.6909 0.5399 0.3569 0.0815  0.0094  -0.0982 440 HIS A C   
2179 O O   . HIS A 314 ? 0.6665 0.5313 0.3612 0.0888  0.0187  -0.0930 440 HIS A O   
2180 C CB  . HIS A 314 ? 0.7423 0.5687 0.3374 0.0979  0.0248  -0.1246 440 HIS A CB  
2181 C CG  . HIS A 314 ? 0.7566 0.6125 0.3722 0.1135  0.0460  -0.1213 440 HIS A CG  
2182 N ND1 . HIS A 314 ? 0.7381 0.6318 0.3772 0.1082  0.0535  -0.1045 440 HIS A ND1 
2183 C CD2 . HIS A 314 ? 0.7718 0.6297 0.3984 0.1305  0.0590  -0.1294 440 HIS A CD2 
2184 C CE1 . HIS A 314 ? 0.6891 0.6072 0.3458 0.1224  0.0708  -0.1047 440 HIS A CE1 
2185 N NE2 . HIS A 314 ? 0.7547 0.6534 0.4054 0.1374  0.0745  -0.1194 440 HIS A NE2 
2186 N N   . VAL A 315 ? 0.7145 0.5712 0.3790 0.0679  -0.0019 -0.0874 441 VAL A N   
2187 C CA  . VAL A 315 ? 0.6481 0.5285 0.3437 0.0627  -0.0016 -0.0700 441 VAL A CA  
2188 C C   . VAL A 315 ? 0.6631 0.5670 0.3614 0.0687  0.0164  -0.0647 441 VAL A C   
2189 O O   . VAL A 315 ? 0.6702 0.5801 0.3408 0.0699  0.0244  -0.0664 441 VAL A O   
2190 C CB  . VAL A 315 ? 0.7496 0.6320 0.4395 0.0506  -0.0166 -0.0593 441 VAL A CB  
2191 C CG1 . VAL A 315 ? 0.6944 0.5942 0.4132 0.0477  -0.0154 -0.0425 441 VAL A CG1 
2192 C CG2 . VAL A 315 ? 0.7554 0.6221 0.4474 0.0431  -0.0347 -0.0640 441 VAL A CG2 
2193 N N   . GLY A 316 ? 0.6050 0.5239 0.3357 0.0711  0.0227  -0.0580 442 GLY A N   
2194 C CA  . GLY A 316 ? 0.6259 0.5709 0.3658 0.0750  0.0387  -0.0531 442 GLY A CA  
2195 C C   . GLY A 316 ? 0.5796 0.5321 0.3327 0.0896  0.0493  -0.0618 442 GLY A C   
2196 O O   . GLY A 316 ? 0.5853 0.5658 0.3568 0.0920  0.0604  -0.0559 442 GLY A O   
2197 N N   . LYS A 317 ? 0.6053 0.5333 0.3498 0.0989  0.0451  -0.0748 443 LYS A N   
2198 C CA  . LYS A 317 ? 0.6239 0.5546 0.3817 0.1153  0.0533  -0.0816 443 LYS A CA  
2199 C C   . LYS A 317 ? 0.5717 0.5122 0.3646 0.1124  0.0490  -0.0720 443 LYS A C   
2200 O O   . LYS A 317 ? 0.5391 0.5067 0.3528 0.1186  0.0576  -0.0671 443 LYS A O   
2201 C CB  . LYS A 317 ? 0.6383 0.5311 0.3735 0.1248  0.0484  -0.0973 443 LYS A CB  
2202 C CG  . LYS A 317 ? 0.6752 0.5666 0.4208 0.1455  0.0571  -0.1039 443 LYS A CG  
2203 C CD  . LYS A 317 ? 0.7488 0.5954 0.4667 0.1560  0.0533  -0.1202 443 LYS A CD  
2204 C CE  . LYS A 317 ? 0.8070 0.6638 0.5326 0.1756  0.0664  -0.1249 443 LYS A CE  
2205 N NZ  . LYS A 317 ? 0.8333 0.6470 0.5368 0.1806  0.0618  -0.1379 443 LYS A NZ  
2206 N N   . TYR A 318 ? 0.5176 0.4384 0.3170 0.1027  0.0356  -0.0691 444 TYR A N   
2207 C CA  . TYR A 318 ? 0.4920 0.4204 0.3193 0.0980  0.0315  -0.0600 444 TYR A CA  
2208 C C   . TYR A 318 ? 0.4993 0.4129 0.3278 0.0848  0.0191  -0.0558 444 TYR A C   
2209 O O   . TYR A 318 ? 0.4920 0.3905 0.3025 0.0800  0.0123  -0.0600 444 TYR A O   
2210 C CB  . TYR A 318 ? 0.5206 0.4400 0.3575 0.1103  0.0322  -0.0640 444 TYR A CB  
2211 C CG  . TYR A 318 ? 0.5233 0.4066 0.3493 0.1094  0.0224  -0.0703 444 TYR A CG  
2212 C CD1 . TYR A 318 ? 0.5585 0.4339 0.3975 0.0983  0.0134  -0.0637 444 TYR A CD1 
2213 C CD2 . TYR A 318 ? 0.6064 0.4627 0.4082 0.1189  0.0229  -0.0830 444 TYR A CD2 
2214 C CE1 . TYR A 318 ? 0.6002 0.4464 0.4316 0.0939  0.0048  -0.0672 444 TYR A CE1 
2215 C CE2 . TYR A 318 ? 0.6339 0.4536 0.4247 0.1140  0.0124  -0.0880 444 TYR A CE2 
2216 C CZ  . TYR A 318 ? 0.6540 0.4714 0.4617 0.1001  0.0034  -0.0788 444 TYR A CZ  
2217 O OH  . TYR A 318 ? 0.7073 0.4933 0.5079 0.0915  -0.0067 -0.0810 444 TYR A OH  
2218 N N   . GLU A 319 ? 0.4913 0.4113 0.3411 0.0793  0.0162  -0.0476 445 GLU A N   
2219 C CA  . GLU A 319 ? 0.4519 0.3622 0.3076 0.0699  0.0064  -0.0436 445 GLU A CA  
2220 C C   . GLU A 319 ? 0.4456 0.3557 0.3199 0.0696  0.0058  -0.0399 445 GLU A C   
2221 O O   . GLU A 319 ? 0.4396 0.3591 0.3221 0.0749  0.0113  -0.0384 445 GLU A O   
2222 C CB  . GLU A 319 ? 0.4596 0.3794 0.3165 0.0624  0.0043  -0.0355 445 GLU A CB  
2223 C CG  . GLU A 319 ? 0.4527 0.3864 0.3227 0.0607  0.0104  -0.0284 445 GLU A CG  
2224 C CD  . GLU A 319 ? 0.4770 0.4121 0.3437 0.0541  0.0084  -0.0202 445 GLU A CD  
2225 O OE1 . GLU A 319 ? 0.4569 0.3869 0.3103 0.0524  0.0032  -0.0192 445 GLU A OE1 
2226 O OE2 . GLU A 319 ? 0.4720 0.4105 0.3471 0.0505  0.0110  -0.0146 445 GLU A OE2 
2227 N N   . PHE A 320 ? 0.4377 0.3404 0.3187 0.0630  -0.0012 -0.0374 446 PHE A N   
2228 C CA  . PHE A 320 ? 0.4129 0.3181 0.3097 0.0611  -0.0005 -0.0323 446 PHE A CA  
2229 C C   . PHE A 320 ? 0.3943 0.3113 0.3006 0.0576  0.0007  -0.0260 446 PHE A C   
2230 O O   . PHE A 320 ? 0.3984 0.3187 0.3007 0.0558  -0.0013 -0.0241 446 PHE A O   
2231 C CB  . PHE A 320 ? 0.4326 0.3253 0.3320 0.0554  -0.0067 -0.0325 446 PHE A CB  
2232 C CG  . PHE A 320 ? 0.4673 0.3391 0.3545 0.0588  -0.0084 -0.0386 446 PHE A CG  
2233 C CD1 . PHE A 320 ? 0.4698 0.3354 0.3587 0.0654  -0.0048 -0.0372 446 PHE A CD1 
2234 C CD2 . PHE A 320 ? 0.4990 0.3542 0.3705 0.0558  -0.0146 -0.0456 446 PHE A CD2 
2235 C CE1 . PHE A 320 ? 0.4888 0.3297 0.3649 0.0711  -0.0066 -0.0423 446 PHE A CE1 
2236 C CE2 . PHE A 320 ? 0.5153 0.3435 0.3714 0.0600  -0.0161 -0.0527 446 PHE A CE2 
2237 C CZ  . PHE A 320 ? 0.5285 0.3482 0.3875 0.0688  -0.0118 -0.0508 446 PHE A CZ  
2238 N N   . GLN A 321 ? 0.3904 0.3110 0.3065 0.0572  0.0038  -0.0227 447 GLN A N   
2239 C CA  . GLN A 321 ? 0.3649 0.2902 0.2869 0.0556  0.0055  -0.0186 447 GLN A CA  
2240 C C   . GLN A 321 ? 0.3700 0.2961 0.3012 0.0548  0.0075  -0.0166 447 GLN A C   
2241 O O   . GLN A 321 ? 0.3687 0.2922 0.3003 0.0542  0.0081  -0.0168 447 GLN A O   
2242 C CB  . GLN A 321 ? 0.3672 0.2957 0.2849 0.0551  0.0095  -0.0178 447 GLN A CB  
2243 C CG  . GLN A 321 ? 0.4109 0.3429 0.3196 0.0544  0.0098  -0.0179 447 GLN A CG  
2244 C CD  . GLN A 321 ? 0.3974 0.3326 0.3033 0.0494  0.0128  -0.0145 447 GLN A CD  
2245 O OE1 . GLN A 321 ? 0.4264 0.3604 0.3353 0.0466  0.0141  -0.0140 447 GLN A OE1 
2246 N NE2 . GLN A 321 ? 0.4375 0.3751 0.3347 0.0465  0.0135  -0.0118 447 GLN A NE2 
2247 N N   . CYS A 322 ? 0.3967 0.3259 0.3343 0.0559  0.0090  -0.0140 448 CYS A N   
2248 C CA  . CYS A 322 ? 0.3571 0.2903 0.3024 0.0565  0.0138  -0.0124 448 CYS A CA  
2249 C C   . CYS A 322 ? 0.3816 0.3123 0.3266 0.0616  0.0180  -0.0123 448 CYS A C   
2250 O O   . CYS A 322 ? 0.4083 0.3329 0.3490 0.0636  0.0154  -0.0117 448 CYS A O   
2251 C CB  . CYS A 322 ? 0.3686 0.3114 0.3271 0.0535  0.0113  -0.0094 448 CYS A CB  
2252 S SG  . CYS A 322 ? 0.4278 0.3821 0.3987 0.0567  0.0056  -0.0059 448 CYS A SG  
2253 N N   . LEU A 323 ? 0.3612 0.2930 0.3070 0.0638  0.0250  -0.0131 449 LEU A N   
2254 C CA  . LEU A 323 ? 0.3851 0.3105 0.3285 0.0712  0.0305  -0.0148 449 LEU A CA  
2255 C C   . LEU A 323 ? 0.3968 0.3369 0.3586 0.0788  0.0320  -0.0110 449 LEU A C   
2256 O O   . LEU A 323 ? 0.4022 0.3609 0.3784 0.0759  0.0329  -0.0076 449 LEU A O   
2257 C CB  . LEU A 323 ? 0.3652 0.2850 0.2970 0.0712  0.0384  -0.0188 449 LEU A CB  
2258 C CG  . LEU A 323 ? 0.3965 0.3052 0.3110 0.0636  0.0354  -0.0219 449 LEU A CG  
2259 C CD1 . LEU A 323 ? 0.4119 0.3156 0.3116 0.0626  0.0415  -0.0257 449 LEU A CD1 
2260 C CD2 . LEU A 323 ? 0.3916 0.2853 0.2973 0.0619  0.0314  -0.0238 449 LEU A CD2 
2261 N N   . HIS A 324 ? 0.3868 0.3191 0.3490 0.0883  0.0319  -0.0105 450 HIS A N   
2262 C CA  . HIS A 324 ? 0.4500 0.3995 0.4323 0.0995  0.0337  -0.0063 450 HIS A CA  
2263 C C   . HIS A 324 ? 0.4228 0.3879 0.4136 0.1038  0.0459  -0.0079 450 HIS A C   
2264 O O   . HIS A 324 ? 0.4091 0.3594 0.3829 0.1058  0.0547  -0.0142 450 HIS A O   
2265 C CB  . HIS A 324 ? 0.4449 0.3760 0.4216 0.1128  0.0334  -0.0060 450 HIS A CB  
2266 C CG  . HIS A 324 ? 0.5034 0.4542 0.5027 0.1291  0.0364  -0.0015 450 HIS A CG  
2267 N ND1 . HIS A 324 ? 0.4928 0.4689 0.5145 0.1306  0.0268  0.0071  450 HIS A ND1 
2268 C CD2 . HIS A 324 ? 0.5202 0.4719 0.5241 0.1455  0.0481  -0.0045 450 HIS A CD2 
2269 C CE1 . HIS A 324 ? 0.5058 0.5017 0.5489 0.1475  0.0318  0.0106  450 HIS A CE1 
2270 N NE2 . HIS A 324 ? 0.5108 0.4919 0.5436 0.1582  0.0459  0.0033  450 HIS A NE2 
2271 N N   . GLY A 325 ? 0.4190 0.4156 0.4354 0.1039  0.0462  -0.0017 451 GLY A N   
2272 C CA  . GLY A 325 ? 0.4138 0.4327 0.4419 0.1070  0.0591  -0.0009 451 GLY A CA  
2273 C C   . GLY A 325 ? 0.4533 0.4755 0.4746 0.0913  0.0618  -0.0001 451 GLY A C   
2274 O O   . GLY A 325 ? 0.4472 0.4907 0.4780 0.0905  0.0726  0.0029  451 GLY A O   
2275 N N   . MET A 326 ? 0.4713 0.4738 0.4764 0.0798  0.0529  -0.0016 452 MET A N   
2276 C CA  . MET A 326 ? 0.4296 0.4307 0.4272 0.0665  0.0531  0.0006  452 MET A CA  
2277 C C   . MET A 326 ? 0.4401 0.4424 0.4449 0.0545  0.0411  0.0047  452 MET A C   
2278 O O   . MET A 326 ? 0.4786 0.4863 0.4866 0.0435  0.0414  0.0097  452 MET A O   
2279 C CB  . MET A 326 ? 0.4289 0.4043 0.3991 0.0652  0.0533  -0.0050 452 MET A CB  
2280 C CG  . MET A 326 ? 0.4982 0.4672 0.4539 0.0733  0.0646  -0.0104 452 MET A CG  
2281 S SD  . MET A 326 ? 0.5855 0.5319 0.5102 0.0670  0.0627  -0.0150 452 MET A SD  
2282 C CE  . MET A 326 ? 0.5308 0.4857 0.4565 0.0554  0.0611  -0.0059 452 MET A CE  
2283 N N   . GLY A 327 ? 0.4393 0.4333 0.4431 0.0558  0.0306  0.0026  453 GLY A N   
2284 C CA  . GLY A 327 ? 0.4302 0.4150 0.4295 0.0455  0.0199  0.0027  453 GLY A CA  
2285 C C   . GLY A 327 ? 0.4199 0.4202 0.4360 0.0394  0.0104  0.0065  453 GLY A C   
2286 O O   . GLY A 327 ? 0.4274 0.4194 0.4392 0.0283  0.0020  0.0062  453 GLY A O   
2287 N N   . GLU A 328 ? 0.4582 0.4800 0.4925 0.0468  0.0108  0.0098  454 GLU A N   
2288 C CA  . GLU A 328 ? 0.4015 0.4415 0.4521 0.0410  -0.0012 0.0141  454 GLU A CA  
2289 C C   . GLU A 328 ? 0.3994 0.4530 0.4625 0.0233  -0.0052 0.0187  454 GLU A C   
2290 O O   . GLU A 328 ? 0.4251 0.4719 0.4835 0.0117  -0.0187 0.0176  454 GLU A O   
2291 C CB  . GLU A 328 ? 0.4317 0.4958 0.5028 0.0551  0.0001  0.0187  454 GLU A CB  
2292 C CG  . GLU A 328 ? 0.4564 0.4984 0.5104 0.0690  -0.0003 0.0151  454 GLU A CG  
2293 C CD  . GLU A 328 ? 0.4914 0.5239 0.5398 0.0827  0.0141  0.0120  454 GLU A CD  
2294 O OE1 . GLU A 328 ? 0.4793 0.5141 0.5267 0.0801  0.0251  0.0100  454 GLU A OE1 
2295 O OE2 . GLU A 328 ? 0.5423 0.5623 0.5844 0.0955  0.0140  0.0116  454 GLU A OE2 
2296 N N   . PRO A 329 ? 0.4259 0.4946 0.5007 0.0186  0.0055  0.0236  455 PRO A N   
2297 C CA  . PRO A 329 ? 0.4341 0.5114 0.5183 -0.0024 0.0005  0.0294  455 PRO A CA  
2298 C C   . PRO A 329 ? 0.4461 0.4836 0.5033 -0.0142 -0.0080 0.0245  455 PRO A C   
2299 O O   . PRO A 329 ? 0.4674 0.5010 0.5258 -0.0311 -0.0200 0.0258  455 PRO A O   
2300 C CB  . PRO A 329 ? 0.4451 0.5420 0.5403 -0.0032 0.0170  0.0359  455 PRO A CB  
2301 C CG  . PRO A 329 ? 0.4104 0.5226 0.5129 0.0189  0.0285  0.0336  455 PRO A CG  
2302 C CD  . PRO A 329 ? 0.3960 0.4761 0.4754 0.0306  0.0226  0.0246  455 PRO A CD  
2303 N N   . LEU A 330 ? 0.3813 0.3891 0.4140 -0.0056 -0.0025 0.0188  456 LEU A N   
2304 C CA  . LEU A 330 ? 0.4207 0.3914 0.4289 -0.0116 -0.0102 0.0136  456 LEU A CA  
2305 C C   . LEU A 330 ? 0.4183 0.3775 0.4164 -0.0094 -0.0221 0.0058  456 LEU A C   
2306 O O   . LEU A 330 ? 0.4435 0.3831 0.4301 -0.0206 -0.0328 0.0024  456 LEU A O   
2307 C CB  . LEU A 330 ? 0.4530 0.4023 0.4418 -0.0007 -0.0021 0.0106  456 LEU A CB  
2308 C CG  . LEU A 330 ? 0.4404 0.3539 0.4054 0.0004  -0.0086 0.0044  456 LEU A CG  
2309 C CD1 . LEU A 330 ? 0.4973 0.3902 0.4562 -0.0150 -0.0143 0.0084  456 LEU A CD1 
2310 C CD2 . LEU A 330 ? 0.4737 0.3776 0.4260 0.0131  -0.0013 0.0029  456 LEU A CD2 
2311 N N   . TYR A 331 ? 0.4103 0.3778 0.4085 0.0043  -0.0205 0.0028  457 TYR A N   
2312 C CA  . TYR A 331 ? 0.4140 0.3685 0.3968 0.0069  -0.0299 -0.0040 457 TYR A CA  
2313 C C   . TYR A 331 ? 0.4299 0.4004 0.4227 -0.0025 -0.0432 -0.0019 457 TYR A C   
2314 O O   . TYR A 331 ? 0.4183 0.3738 0.3926 -0.0048 -0.0530 -0.0081 457 TYR A O   
2315 C CB  . TYR A 331 ? 0.3638 0.3182 0.3398 0.0222  -0.0238 -0.0063 457 TYR A CB  
2316 C CG  . TYR A 331 ? 0.4133 0.3471 0.3727 0.0278  -0.0164 -0.0109 457 TYR A CG  
2317 C CD1 . TYR A 331 ? 0.3873 0.2996 0.3267 0.0285  -0.0200 -0.0178 457 TYR A CD1 
2318 C CD2 . TYR A 331 ? 0.3885 0.3259 0.3518 0.0329  -0.0063 -0.0083 457 TYR A CD2 
2319 C CE1 . TYR A 331 ? 0.4074 0.3063 0.3358 0.0356  -0.0138 -0.0208 457 TYR A CE1 
2320 C CE2 . TYR A 331 ? 0.4015 0.3243 0.3514 0.0375  -0.0019 -0.0111 457 TYR A CE2 
2321 C CZ  . TYR A 331 ? 0.4020 0.3078 0.3370 0.0395  -0.0059 -0.0166 457 TYR A CZ  
2322 O OH  . TYR A 331 ? 0.4242 0.3212 0.3501 0.0462  -0.0022 -0.0183 457 TYR A OH  
2323 N N   . GLU A 332 ? 0.4231 0.4255 0.4441 -0.0082 -0.0439 0.0068  458 GLU A N   
2324 C CA  . GLU A 332 ? 0.4320 0.4529 0.4652 -0.0215 -0.0593 0.0100  458 GLU A CA  
2325 C C   . GLU A 332 ? 0.4519 0.4500 0.4715 -0.0425 -0.0691 0.0063  458 GLU A C   
2326 O O   . GLU A 332 ? 0.4661 0.4712 0.4874 -0.0569 -0.0850 0.0063  458 GLU A O   
2327 C CB  . GLU A 332 ? 0.4202 0.4880 0.4922 -0.0216 -0.0566 0.0214  458 GLU A CB  
2328 C CG  . GLU A 332 ? 0.4736 0.5602 0.5570 0.0002  -0.0515 0.0244  458 GLU A CG  
2329 C CD  . GLU A 332 ? 0.5656 0.6979 0.6876 0.0066  -0.0443 0.0345  458 GLU A CD  
2330 O OE1 . GLU A 332 ? 0.5151 0.6687 0.6563 -0.0065 -0.0401 0.0399  458 GLU A OE1 
2331 O OE2 . GLU A 332 ? 0.5874 0.7336 0.7198 0.0255  -0.0421 0.0375  458 GLU A OE2 
2332 N N   . GLU A 333 ? 0.4534 0.4222 0.4578 -0.0448 -0.0613 0.0034  459 GLU A N   
2333 C CA  . GLU A 333 ? 0.5010 0.4337 0.4838 -0.0608 -0.0702 -0.0020 459 GLU A CA  
2334 C C   . GLU A 333 ? 0.5143 0.4063 0.4610 -0.0501 -0.0719 -0.0153 459 GLU A C   
2335 O O   . GLU A 333 ? 0.5568 0.4108 0.4801 -0.0585 -0.0778 -0.0221 459 GLU A O   
2336 C CB  . GLU A 333 ? 0.5238 0.4450 0.5094 -0.0689 -0.0615 0.0045  459 GLU A CB  
2337 C CG  . GLU A 333 ? 0.5161 0.4804 0.5367 -0.0804 -0.0566 0.0183  459 GLU A CG  
2338 C CD  . GLU A 333 ? 0.5720 0.5610 0.6114 -0.1023 -0.0718 0.0227  459 GLU A CD  
2339 O OE1 . GLU A 333 ? 0.5951 0.5537 0.6138 -0.1175 -0.0870 0.0159  459 GLU A OE1 
2340 O OE2 . GLU A 333 ? 0.5965 0.6363 0.6713 -0.1040 -0.0690 0.0326  459 GLU A OE2 
2341 N N   . VAL A 334 ? 0.4768 0.3755 0.4183 -0.0315 -0.0660 -0.0187 460 VAL A N   
2342 C CA  . VAL A 334 ? 0.5096 0.3787 0.4211 -0.0191 -0.0634 -0.0298 460 VAL A CA  
2343 C C   . VAL A 334 ? 0.5488 0.4232 0.4473 -0.0162 -0.0712 -0.0350 460 VAL A C   
2344 O O   . VAL A 334 ? 0.5841 0.4322 0.4540 -0.0184 -0.0778 -0.0456 460 VAL A O   
2345 C CB  . VAL A 334 ? 0.5064 0.3774 0.4200 -0.0016 -0.0482 -0.0284 460 VAL A CB  
2346 C CG1 . VAL A 334 ? 0.5438 0.3959 0.4325 0.0117  -0.0448 -0.0383 460 VAL A CG1 
2347 C CG2 . VAL A 334 ? 0.5264 0.3858 0.4443 -0.0043 -0.0422 -0.0239 460 VAL A CG2 
2348 N N   . VAL A 335 ? 0.5321 0.4378 0.4483 -0.0103 -0.0704 -0.0275 461 VAL A N   
2349 C CA  . VAL A 335 ? 0.5471 0.4575 0.4490 -0.0062 -0.0771 -0.0295 461 VAL A CA  
2350 C C   . VAL A 335 ? 0.5845 0.4975 0.4809 -0.0224 -0.0958 -0.0308 461 VAL A C   
2351 O O   . VAL A 335 ? 0.5789 0.5070 0.4969 -0.0365 -0.1037 -0.0252 461 VAL A O   
2352 C CB  . VAL A 335 ? 0.5525 0.4903 0.4737 0.0051  -0.0722 -0.0195 461 VAL A CB  
2353 C CG1 . VAL A 335 ? 0.4723 0.4050 0.3952 0.0180  -0.0556 -0.0194 461 VAL A CG1 
2354 C CG2 . VAL A 335 ? 0.5588 0.5286 0.5140 0.0000  -0.0775 -0.0089 461 VAL A CG2 
2355 N N   . GLY A 336 ? 0.6223 0.5227 0.4892 -0.0219 -0.1032 -0.0377 462 GLY A N   
2356 C CA  . GLY A 336 ? 0.6500 0.5564 0.5102 -0.0376 -0.1233 -0.0381 462 GLY A CA  
2357 C C   . GLY A 336 ? 0.7012 0.5701 0.5300 -0.0517 -0.1319 -0.0523 462 GLY A C   
2358 O O   . GLY A 336 ? 0.6593 0.5008 0.4824 -0.0518 -0.1237 -0.0586 462 GLY A O   
2359 N N   . ARG A 337 ? 0.6818 0.5465 0.4877 -0.0638 -0.1499 -0.0572 463 ARG A N   
2360 C CA  . ARG A 337 ? 0.7471 0.5692 0.5138 -0.0771 -0.1596 -0.0735 463 ARG A CA  
2361 C C   . ARG A 337 ? 0.7787 0.5908 0.5602 -0.0990 -0.1687 -0.0728 463 ARG A C   
2362 O O   . ARG A 337 ? 0.8091 0.5741 0.5594 -0.1067 -0.1711 -0.0866 463 ARG A O   
2363 C CB  . ARG A 337 ? 0.7402 0.5623 0.4760 -0.0862 -0.1782 -0.0785 463 ARG A CB  
2364 N N   . GLY A 338 ? 0.7200 0.5743 0.5471 -0.1089 -0.1732 -0.0569 464 GLY A N   
2365 C CA  . GLY A 338 ? 0.6853 0.5347 0.5290 -0.1317 -0.1797 -0.0537 464 GLY A CA  
2366 C C   . GLY A 338 ? 0.6951 0.5284 0.5503 -0.1237 -0.1609 -0.0511 464 GLY A C   
2367 O O   . GLY A 338 ? 0.6931 0.5141 0.5562 -0.1427 -0.1642 -0.0480 464 GLY A O   
2368 N N   . LYS A 339 ? 0.6300 0.4622 0.4841 -0.0975 -0.1418 -0.0515 465 LYS A N   
2369 C CA  . LYS A 339 ? 0.6376 0.4573 0.5011 -0.0879 -0.1246 -0.0482 465 LYS A CA  
2370 C C   . LYS A 339 ? 0.6385 0.4114 0.4636 -0.0713 -0.1161 -0.0628 465 LYS A C   
2371 O O   . LYS A 339 ? 0.7105 0.4416 0.5014 -0.0791 -0.1250 -0.0757 465 LYS A O   
2372 C CB  . LYS A 339 ? 0.6005 0.4642 0.5003 -0.0735 -0.1110 -0.0351 465 LYS A CB  
2373 C CG  . LYS A 339 ? 0.5724 0.4852 0.5120 -0.0862 -0.1178 -0.0211 465 LYS A CG  
2374 C CD  . LYS A 339 ? 0.5937 0.5029 0.5450 -0.1113 -0.1239 -0.0160 465 LYS A CD  
2375 C CE  . LYS A 339 ? 0.6019 0.5688 0.6006 -0.1197 -0.1235 0.0002  465 LYS A CE  
2376 N NZ  . LYS A 339 ? 0.6521 0.6179 0.6639 -0.1443 -0.1242 0.0078  465 LYS A NZ  
2377 N N   . LEU A 340 ? 0.6469 0.4265 0.4763 -0.0485 -0.0992 -0.0614 466 LEU A N   
2378 C CA  . LEU A 340 ? 0.7052 0.4495 0.5052 -0.0307 -0.0896 -0.0733 466 LEU A CA  
2379 C C   . LEU A 340 ? 0.6802 0.4312 0.4609 -0.0165 -0.0859 -0.0810 466 LEU A C   
2380 O O   . LEU A 340 ? 0.6826 0.4094 0.4386 -0.0010 -0.0772 -0.0917 466 LEU A O   
2381 C CB  . LEU A 340 ? 0.6320 0.3806 0.4487 -0.0161 -0.0741 -0.0663 466 LEU A CB  
2382 C CG  . LEU A 340 ? 0.5947 0.3370 0.4280 -0.0275 -0.0741 -0.0565 466 LEU A CG  
2383 C CD1 . LEU A 340 ? 0.6380 0.3804 0.4782 -0.0098 -0.0598 -0.0517 466 LEU A CD1 
2384 C CD2 . LEU A 340 ? 0.6840 0.3794 0.4933 -0.0425 -0.0850 -0.0633 466 LEU A CD2 
2385 N N   . ASP A 341 ? 0.6905 0.4747 0.4820 -0.0205 -0.0918 -0.0746 467 ASP A N   
2386 C CA  . ASP A 341 ? 0.6644 0.4555 0.4352 -0.0104 -0.0897 -0.0792 467 ASP A CA  
2387 C C   . ASP A 341 ? 0.6461 0.4417 0.4169 0.0106  -0.0707 -0.0794 467 ASP A C   
2388 O O   . ASP A 341 ? 0.6797 0.4630 0.4231 0.0214  -0.0638 -0.0890 467 ASP A O   
2389 C CB  . ASP A 341 ? 0.7459 0.5039 0.4733 -0.0165 -0.0996 -0.0949 467 ASP A CB  
2390 C CG  . ASP A 341 ? 0.7659 0.5390 0.4739 -0.0151 -0.1043 -0.0954 467 ASP A CG  
2391 O OD1 . ASP A 341 ? 0.8090 0.6177 0.5405 -0.0127 -0.1038 -0.0815 467 ASP A OD1 
2392 O OD2 . ASP A 341 ? 0.9155 0.6621 0.5818 -0.0161 -0.1085 -0.1096 467 ASP A OD2 
2393 N N   . ARG A 342 ? 0.6251 0.4409 0.4272 0.0156  -0.0620 -0.0687 468 ARG A N   
2394 C CA  . ARG A 342 ? 0.5812 0.4086 0.3892 0.0315  -0.0467 -0.0662 468 ARG A CA  
2395 C C   . ARG A 342 ? 0.5342 0.3934 0.3677 0.0310  -0.0451 -0.0532 468 ARG A C   
2396 O O   . ARG A 342 ? 0.5558 0.4274 0.4123 0.0235  -0.0501 -0.0453 468 ARG A O   
2397 C CB  . ARG A 342 ? 0.5337 0.3489 0.3504 0.0390  -0.0381 -0.0668 468 ARG A CB  
2398 C CG  . ARG A 342 ? 0.6316 0.4088 0.4221 0.0432  -0.0391 -0.0795 468 ARG A CG  
2399 C CD  . ARG A 342 ? 0.6242 0.3970 0.3906 0.0583  -0.0302 -0.0897 468 ARG A CD  
2400 N NE  . ARG A 342 ? 0.6977 0.4308 0.4366 0.0659  -0.0300 -0.1037 468 ARG A NE  
2401 C CZ  . ARG A 342 ? 0.7441 0.4480 0.4511 0.0593  -0.0387 -0.1161 468 ARG A CZ  
2402 N NH1 . ARG A 342 ? 0.6996 0.4138 0.3987 0.0445  -0.0493 -0.1155 468 ARG A NH1 
2403 N NH2 . ARG A 342 ? 0.7537 0.4151 0.4341 0.0683  -0.0376 -0.1296 468 ARG A NH2 
2404 N N   . PRO A 343 ? 0.5051 0.3767 0.3347 0.0391  -0.0374 -0.0504 469 PRO A N   
2405 C CA  . PRO A 343 ? 0.4810 0.3744 0.3297 0.0391  -0.0369 -0.0387 469 PRO A CA  
2406 C C   . PRO A 343 ? 0.4738 0.3748 0.3453 0.0432  -0.0281 -0.0337 469 PRO A C   
2407 O O   . PRO A 343 ? 0.4656 0.3596 0.3371 0.0479  -0.0209 -0.0376 469 PRO A O   
2408 C CB  . PRO A 343 ? 0.5414 0.4388 0.3721 0.0440  -0.0315 -0.0377 469 PRO A CB  
2409 C CG  . PRO A 343 ? 0.5434 0.4306 0.3585 0.0511  -0.0216 -0.0478 469 PRO A CG  
2410 C CD  . PRO A 343 ? 0.5378 0.4038 0.3449 0.0485  -0.0281 -0.0575 469 PRO A CD  
2411 N N   . CYS A 344 ? 0.4564 0.3716 0.3462 0.0426  -0.0293 -0.0248 470 CYS A N   
2412 C CA  . CYS A 344 ? 0.4333 0.3543 0.3397 0.0464  -0.0208 -0.0209 470 CYS A CA  
2413 C C   . CYS A 344 ? 0.4433 0.3714 0.3539 0.0501  -0.0190 -0.0139 470 CYS A C   
2414 O O   . CYS A 344 ? 0.4635 0.3977 0.3780 0.0499  -0.0264 -0.0086 470 CYS A O   
2415 C CB  . CYS A 344 ? 0.4410 0.3674 0.3660 0.0423  -0.0225 -0.0184 470 CYS A CB  
2416 S SG  . CYS A 344 ? 0.4556 0.3883 0.3948 0.0474  -0.0115 -0.0144 470 CYS A SG  
2417 N N   . ARG A 345 ? 0.4007 0.3268 0.3099 0.0530  -0.0106 -0.0133 471 ARG A N   
2418 C CA  . ARG A 345 ? 0.4201 0.3448 0.3301 0.0552  -0.0088 -0.0072 471 ARG A CA  
2419 C C   . ARG A 345 ? 0.4320 0.3573 0.3563 0.0584  -0.0043 -0.0063 471 ARG A C   
2420 O O   . ARG A 345 ? 0.3863 0.3109 0.3120 0.0574  0.0014  -0.0098 471 ARG A O   
2421 C CB  . ARG A 345 ? 0.4132 0.3342 0.3100 0.0528  -0.0032 -0.0068 471 ARG A CB  
2422 C CG  . ARG A 345 ? 0.4287 0.3409 0.3209 0.0521  -0.0028 0.0003  471 ARG A CG  
2423 C CD  . ARG A 345 ? 0.4453 0.3575 0.3259 0.0454  0.0027  0.0018  471 ARG A CD  
2424 N NE  . ARG A 345 ? 0.4713 0.3922 0.3404 0.0441  0.0030  0.0002  471 ARG A NE  
2425 C CZ  . ARG A 345 ? 0.4864 0.4038 0.3407 0.0426  -0.0010 0.0056  471 ARG A CZ  
2426 N NH1 . ARG A 345 ? 0.4917 0.3970 0.3430 0.0427  -0.0065 0.0144  471 ARG A NH1 
2427 N NH2 . ARG A 345 ? 0.5111 0.4355 0.3511 0.0422  0.0003  0.0020  471 ARG A NH2 
2428 N N   . ILE A 346 ? 0.3894 0.3167 0.3230 0.0635  -0.0067 -0.0014 472 ILE A N   
2429 C CA  . ILE A 346 ? 0.3875 0.3156 0.3326 0.0691  -0.0007 -0.0015 472 ILE A CA  
2430 C C   . ILE A 346 ? 0.4112 0.3212 0.3444 0.0710  0.0041  -0.0017 472 ILE A C   
2431 O O   . ILE A 346 ? 0.4285 0.3272 0.3527 0.0721  0.0007  0.0030  472 ILE A O   
2432 C CB  . ILE A 346 ? 0.4125 0.3541 0.3753 0.0765  -0.0046 0.0038  472 ILE A CB  
2433 C CG1 . ILE A 346 ? 0.4121 0.3719 0.3866 0.0699  -0.0109 0.0041  472 ILE A CG1 
2434 C CG2 . ILE A 346 ? 0.4071 0.3494 0.3796 0.0857  0.0044  0.0030  472 ILE A CG2 
2435 C CD1 . ILE A 346 ? 0.4176 0.3974 0.4110 0.0747  -0.0189 0.0112  472 ILE A CD1 
2436 N N   . TYR A 347 ? 0.3943 0.2994 0.3246 0.0695  0.0110  -0.0066 473 TYR A N   
2437 C CA  . TYR A 347 ? 0.4243 0.3095 0.3415 0.0688  0.0145  -0.0082 473 TYR A CA  
2438 C C   . TYR A 347 ? 0.4725 0.3482 0.3935 0.0808  0.0177  -0.0079 473 TYR A C   
2439 O O   . TYR A 347 ? 0.4371 0.3246 0.3692 0.0872  0.0229  -0.0102 473 TYR A O   
2440 C CB  . TYR A 347 ? 0.4171 0.3023 0.3283 0.0624  0.0189  -0.0139 473 TYR A CB  
2441 C CG  . TYR A 347 ? 0.4566 0.3222 0.3515 0.0559  0.0195  -0.0161 473 TYR A CG  
2442 C CD1 . TYR A 347 ? 0.4931 0.3379 0.3781 0.0602  0.0234  -0.0205 473 TYR A CD1 
2443 C CD2 . TYR A 347 ? 0.4682 0.3365 0.3570 0.0446  0.0166  -0.0143 473 TYR A CD2 
2444 C CE1 . TYR A 347 ? 0.5256 0.3472 0.3920 0.0510  0.0222  -0.0234 473 TYR A CE1 
2445 C CE2 . TYR A 347 ? 0.4684 0.3208 0.3436 0.0346  0.0158  -0.0154 473 TYR A CE2 
2446 C CZ  . TYR A 347 ? 0.4874 0.3140 0.3502 0.0366  0.0176  -0.0201 473 TYR A CZ  
2447 O OH  . TYR A 347 ? 0.5574 0.3638 0.4035 0.0235  0.0151  -0.0218 473 TYR A OH  
2448 N N   . ALA A 348 ? 0.4493 0.3036 0.3608 0.0849  0.0151  -0.0042 474 ALA A N   
2449 C CA  . ALA A 348 ? 0.4661 0.3101 0.3822 0.1010  0.0172  -0.0027 474 ALA A CA  
2450 C C   . ALA A 348 ? 0.5077 0.3155 0.4032 0.1031  0.0219  -0.0081 474 ALA A C   
2451 O O   . ALA A 348 ? 0.5042 0.2841 0.3831 0.0986  0.0173  -0.0043 474 ALA A O   
2452 C CB  . ALA A 348 ? 0.4983 0.3431 0.4190 0.1070  0.0081  0.0076  474 ALA A CB  
2453 N N   . PRO A 349 ? 0.4782 0.2822 0.3705 0.1081  0.0308  -0.0171 475 PRO A N   
2454 C CA  . PRO A 349 ? 0.5358 0.2997 0.4036 0.1105  0.0346  -0.0244 475 PRO A CA  
2455 C C   . PRO A 349 ? 0.6031 0.3448 0.4708 0.1308  0.0353  -0.0213 475 PRO A C   
2456 O O   . PRO A 349 ? 0.5968 0.3626 0.4874 0.1480  0.0380  -0.0174 475 PRO A O   
2457 C CB  . PRO A 349 ? 0.5604 0.3319 0.4244 0.1125  0.0447  -0.0349 475 PRO A CB  
2458 C CG  . PRO A 349 ? 0.5152 0.3271 0.3986 0.1047  0.0440  -0.0314 475 PRO A CG  
2459 C CD  . PRO A 349 ? 0.4920 0.3250 0.3974 0.1084  0.0373  -0.0212 475 PRO A CD  
2460 N N   . VAL A 350 ? 0.6034 0.2994 0.4461 0.1281  0.0319  -0.0217 476 VAL A N   
2461 C CA  . VAL A 350 ? 0.6459 0.3104 0.4834 0.1481  0.0310  -0.0177 476 VAL A CA  
2462 C C   . VAL A 350 ? 0.7043 0.3147 0.5091 0.1503  0.0360  -0.0295 476 VAL A C   
2463 O O   . VAL A 350 ? 0.7355 0.3174 0.5156 0.1283  0.0314  -0.0325 476 VAL A O   
2464 C CB  . VAL A 350 ? 0.6659 0.3191 0.5003 0.1417  0.0190  -0.0029 476 VAL A CB  
2465 C CG1 . VAL A 350 ? 0.7267 0.3454 0.5554 0.1648  0.0166  0.0034  476 VAL A CG1 
2466 C CG2 . VAL A 350 ? 0.6434 0.3474 0.5037 0.1364  0.0134  0.0062  476 VAL A CG2 
2467 N N   . GLY A 351 ? 0.6501 0.2588 0.4606 0.1711  0.0440  -0.0355 477 GLY A N   
2468 C CA  . GLY A 351 ? 0.7640 0.3315 0.5476 0.1694  0.0472  -0.0469 477 GLY A CA  
2469 C C   . GLY A 351 ? 0.7969 0.3791 0.5911 0.1912  0.0596  -0.0561 477 GLY A C   
2470 O O   . GLY A 351 ? 0.7423 0.3699 0.5671 0.2064  0.0661  -0.0528 477 GLY A O   
2471 N N   . THR A 352 ? 0.8723 0.4145 0.6395 0.1913  0.0626  -0.0675 478 THR A N   
2472 C CA  . THR A 352 ? 0.9333 0.4819 0.7018 0.2100  0.0758  -0.0791 478 THR A CA  
2473 C C   . THR A 352 ? 0.9012 0.4822 0.6696 0.2027  0.0852  -0.0878 478 THR A C   
2474 O O   . THR A 352 ? 0.9423 0.5301 0.7028 0.1817  0.0804  -0.0873 478 THR A O   
2475 C CB  . THR A 352 ? 0.9858 0.4773 0.7190 0.2094  0.0756  -0.0905 478 THR A CB  
2476 O OG1 . THR A 352 ? 0.9940 0.4623 0.6948 0.1830  0.0718  -0.0998 478 THR A OG1 
2477 C CG2 . THR A 352 ? 0.9716 0.4238 0.6990 0.2116  0.0647  -0.0805 478 THR A CG2 
2478 N N   . HIS A 353 ? 0.9941 0.5958 0.7711 0.2205  0.0991  -0.0954 479 HIS A N   
2479 C CA  . HIS A 353 ? 0.9752 0.6054 0.7485 0.2133  0.1088  -0.1027 479 HIS A CA  
2480 C C   . HIS A 353 ? 0.9775 0.5700 0.7080 0.1930  0.1056  -0.1154 479 HIS A C   
2481 O O   . HIS A 353 ? 0.9656 0.5747 0.6881 0.1769  0.1055  -0.1172 479 HIS A O   
2482 C CB  . HIS A 353 ? 1.0178 0.6789 0.8081 0.2359  0.1256  -0.1074 479 HIS A CB  
2483 C CG  . HIS A 353 ? 1.0455 0.7562 0.8504 0.2313  0.1354  -0.1058 479 HIS A CG  
2484 N ND1 . HIS A 353 ? 1.0372 0.7503 0.8199 0.2273  0.1465  -0.1172 479 HIS A ND1 
2485 C CD2 . HIS A 353 ? 0.9979 0.7556 0.8352 0.2289  0.1353  -0.0936 479 HIS A CD2 
2486 C CE1 . HIS A 353 ? 0.9805 0.7398 0.7813 0.2225  0.1534  -0.1109 479 HIS A CE1 
2487 N NE2 . HIS A 353 ? 1.0151 0.8015 0.8496 0.2232  0.1468  -0.0969 479 HIS A NE2 
2488 N N   . GLU A 354 ? 0.9487 0.4898 0.6509 0.1925  0.1015  -0.1234 480 GLU A N   
2489 C CA  . GLU A 354 ? 0.9824 0.4873 0.6433 0.1716  0.0966  -0.1356 480 GLU A CA  
2490 C C   . GLU A 354 ? 0.9745 0.4739 0.6275 0.1429  0.0819  -0.1293 480 GLU A C   
2491 O O   . GLU A 354 ? 0.9845 0.4874 0.6189 0.1241  0.0790  -0.1351 480 GLU A O   
2492 C CB  . GLU A 354 ? 1.0291 0.4779 0.6619 0.1771  0.0950  -0.1451 480 GLU A CB  
2493 C CG  . GLU A 354 ? 1.0990 0.5122 0.6879 0.1582  0.0916  -0.1602 480 GLU A CG  
2494 C CD  . GLU A 354 ? 1.1352 0.5648 0.7125 0.1688  0.1062  -0.1737 480 GLU A CD  
2495 O OE1 . GLU A 354 ? 1.0849 0.5624 0.6902 0.1850  0.1188  -0.1698 480 GLU A OE1 
2496 O OE2 . GLU A 354 ? 1.1809 0.5755 0.7197 0.1597  0.1050  -0.1881 480 GLU A OE2 
2497 N N   . THR A 355 ? 0.9257 0.4174 0.5920 0.1391  0.0723  -0.1170 481 THR A N   
2498 C CA  . THR A 355 ? 0.9881 0.4753 0.6469 0.1118  0.0595  -0.1113 481 THR A CA  
2499 C C   . THR A 355 ? 0.9307 0.4652 0.6082 0.1060  0.0613  -0.1068 481 THR A C   
2500 O O   . THR A 355 ? 0.9478 0.4827 0.6159 0.0830  0.0522  -0.1055 481 THR A O   
2501 C CB  . THR A 355 ? 0.9935 0.4621 0.6604 0.1088  0.0500  -0.0982 481 THR A CB  
2502 O OG1 . THR A 355 ? 1.0398 0.5013 0.6958 0.0797  0.0384  -0.0939 481 THR A OG1 
2503 C CG2 . THR A 355 ? 0.9288 0.4362 0.6335 0.1283  0.0537  -0.0855 481 THR A CG2 
2504 N N   . LEU A 356 ? 0.8771 0.4519 0.5808 0.1256  0.0725  -0.1041 482 LEU A N   
2505 C CA  . LEU A 356 ? 0.8518 0.4701 0.5749 0.1217  0.0745  -0.0983 482 LEU A CA  
2506 C C   . LEU A 356 ? 0.8186 0.4575 0.5319 0.1206  0.0837  -0.1064 482 LEU A C   
2507 O O   . LEU A 356 ? 0.7227 0.3979 0.4513 0.1194  0.0872  -0.1012 482 LEU A O   
2508 C CB  . LEU A 356 ? 0.8879 0.5401 0.6495 0.1404  0.0787  -0.0865 482 LEU A CB  
2509 N N   . LEU A 357 ? 0.8376 0.4522 0.5235 0.1207  0.0874  -0.1186 483 LEU A N   
2510 C CA  . LEU A 357 ? 0.7993 0.4321 0.4720 0.1200  0.0965  -0.1258 483 LEU A CA  
2511 C C   . LEU A 357 ? 0.7891 0.4353 0.4509 0.0984  0.0883  -0.1236 483 LEU A C   
2512 O O   . LEU A 357 ? 0.7928 0.4728 0.4625 0.0999  0.0953  -0.1198 483 LEU A O   
2513 C CB  . LEU A 357 ? 0.8933 0.4910 0.5326 0.1213  0.0994  -0.1404 483 LEU A CB  
2514 C CG  . LEU A 357 ? 0.9256 0.5430 0.5598 0.1351  0.1159  -0.1477 483 LEU A CG  
2515 C CD1 . LEU A 357 ? 0.9122 0.5720 0.5865 0.1564  0.1292  -0.1385 483 LEU A CD1 
2516 C CD2 . LEU A 357 ? 0.9345 0.5120 0.5403 0.1429  0.1197  -0.1622 483 LEU A CD2 
2517 N N   . ALA A 358 ? 0.7869 0.4079 0.4308 0.0776  0.0732  -0.1250 484 ALA A N   
2518 C CA  . ALA A 358 ? 0.8173 0.4533 0.4510 0.0572  0.0637  -0.1230 484 ALA A CA  
2519 C C   . ALA A 358 ? 0.7399 0.4271 0.4178 0.0586  0.0625  -0.1062 484 ALA A C   
2520 O O   . ALA A 358 ? 0.7179 0.4362 0.4013 0.0520  0.0610  -0.1006 484 ALA A O   
2521 C CB  . ALA A 358 ? 0.8763 0.4870 0.4941 0.0325  0.0461  -0.1244 484 ALA A CB  
2522 N N   . TYR A 359 ? 0.6858 0.3792 0.3929 0.0668  0.0622  -0.0976 485 TYR A N   
2523 C CA  . TYR A 359 ? 0.6453 0.3823 0.3916 0.0694  0.0614  -0.0835 485 TYR A CA  
2524 C C   . TYR A 359 ? 0.6298 0.3947 0.3884 0.0832  0.0748  -0.0816 485 TYR A C   
2525 O O   . TYR A 359 ? 0.5817 0.3787 0.3564 0.0774  0.0731  -0.0730 485 TYR A O   
2526 C CB  . TYR A 359 ? 0.6031 0.3355 0.3707 0.0762  0.0584  -0.0765 485 TYR A CB  
2527 C CG  . TYR A 359 ? 0.5800 0.3514 0.3841 0.0794  0.0569  -0.0637 485 TYR A CG  
2528 C CD1 . TYR A 359 ? 0.5434 0.3323 0.3599 0.0652  0.0464  -0.0557 485 TYR A CD1 
2529 C CD2 . TYR A 359 ? 0.5423 0.3334 0.3681 0.0966  0.0658  -0.0600 485 TYR A CD2 
2530 C CE1 . TYR A 359 ? 0.5017 0.3201 0.3461 0.0681  0.0446  -0.0462 485 TYR A CE1 
2531 C CE2 . TYR A 359 ? 0.4996 0.3232 0.3557 0.0965  0.0623  -0.0492 485 TYR A CE2 
2532 C CZ  . TYR A 359 ? 0.4830 0.3167 0.3456 0.0824  0.0517  -0.0433 485 TYR A CZ  
2533 O OH  . TYR A 359 ? 0.4642 0.3236 0.3511 0.0825  0.0480  -0.0348 485 TYR A OH  
2534 N N   . LEU A 360 ? 0.6335 0.3866 0.3847 0.1015  0.0887  -0.0890 486 LEU A N   
2535 C CA  . LEU A 360 ? 0.6386 0.4233 0.4032 0.1133  0.1033  -0.0863 486 LEU A CA  
2536 C C   . LEU A 360 ? 0.6381 0.4302 0.3788 0.1025  0.1061  -0.0888 486 LEU A C   
2537 O O   . LEU A 360 ? 0.6519 0.4773 0.4079 0.1010  0.1114  -0.0799 486 LEU A O   
2538 C CB  . LEU A 360 ? 0.6897 0.4634 0.4521 0.1374  0.1190  -0.0941 486 LEU A CB  
2539 N N   . VAL A 361 ? 0.6808 0.4410 0.3822 0.0931  0.1012  -0.1000 487 VAL A N   
2540 C CA  . VAL A 361 ? 0.6474 0.4152 0.3239 0.0811  0.1003  -0.1008 487 VAL A CA  
2541 C C   . VAL A 361 ? 0.6470 0.4456 0.3472 0.0673  0.0878  -0.0855 487 VAL A C   
2542 O O   . VAL A 361 ? 0.6750 0.4975 0.3778 0.0652  0.0920  -0.0774 487 VAL A O   
2543 C CB  . VAL A 361 ? 0.7262 0.4549 0.3566 0.0697  0.0924  -0.1150 487 VAL A CB  
2544 C CG1 . VAL A 361 ? 0.8025 0.5440 0.4103 0.0538  0.0849  -0.1120 487 VAL A CG1 
2545 C CG2 . VAL A 361 ? 0.7535 0.4625 0.3689 0.0816  0.1032  -0.1273 487 VAL A CG2 
2546 N N   . ARG A 362 ? 0.6444 0.4419 0.3618 0.0587  0.0732  -0.0807 488 ARG A N   
2547 C CA  . ARG A 362 ? 0.6113 0.4359 0.3509 0.0492  0.0624  -0.0676 488 ARG A CA  
2548 C C   . ARG A 362 ? 0.6159 0.4677 0.3867 0.0576  0.0700  -0.0569 488 ARG A C   
2549 O O   . ARG A 362 ? 0.6187 0.4892 0.3968 0.0523  0.0667  -0.0473 488 ARG A O   
2550 C CB  . ARG A 362 ? 0.6069 0.4273 0.3586 0.0400  0.0483  -0.0654 488 ARG A CB  
2551 C CG  . ARG A 362 ? 0.6125 0.4138 0.3355 0.0251  0.0375  -0.0729 488 ARG A CG  
2552 C CD  . ARG A 362 ? 0.6289 0.4385 0.3683 0.0131  0.0238  -0.0672 488 ARG A CD  
2553 N NE  . ARG A 362 ? 0.6050 0.4024 0.3587 0.0175  0.0261  -0.0670 488 ARG A NE  
2554 C CZ  . ARG A 362 ? 0.6491 0.4136 0.3852 0.0126  0.0243  -0.0746 488 ARG A CZ  
2555 N NH1 . ARG A 362 ? 0.6760 0.4145 0.3787 0.0023  0.0205  -0.0850 488 ARG A NH1 
2556 N NH2 . ARG A 362 ? 0.6597 0.4146 0.4096 0.0168  0.0253  -0.0712 488 ARG A NH2 
2557 N N   . ARG A 363 ? 0.5541 0.4077 0.3429 0.0703  0.0791  -0.0580 489 ARG A N   
2558 C CA  . ARG A 363 ? 0.5620 0.4439 0.3804 0.0757  0.0854  -0.0481 489 ARG A CA  
2559 C C   . ARG A 363 ? 0.5635 0.4600 0.3725 0.0766  0.0982  -0.0457 489 ARG A C   
2560 O O   . ARG A 363 ? 0.5426 0.4615 0.3690 0.0721  0.0992  -0.0346 489 ARG A O   
2561 C CB  . ARG A 363 ? 0.5332 0.4184 0.3740 0.0894  0.0909  -0.0488 489 ARG A CB  
2562 C CG  . ARG A 363 ? 0.5412 0.4118 0.3899 0.0885  0.0792  -0.0490 489 ARG A CG  
2563 C CD  . ARG A 363 ? 0.5273 0.4149 0.3974 0.0793  0.0678  -0.0392 489 ARG A CD  
2564 N NE  . ARG A 363 ? 0.5126 0.3997 0.3712 0.0666  0.0597  -0.0375 489 ARG A NE  
2565 C CZ  . ARG A 363 ? 0.5437 0.4154 0.3865 0.0588  0.0516  -0.0416 489 ARG A CZ  
2566 N NH1 . ARG A 363 ? 0.4975 0.3465 0.3288 0.0601  0.0510  -0.0483 489 ARG A NH1 
2567 N NH2 . ARG A 363 ? 0.5310 0.4105 0.3705 0.0494  0.0434  -0.0379 489 ARG A NH2 
2568 N N   . LEU A 364 ? 0.6076 0.4895 0.3865 0.0818  0.1085  -0.0560 490 LEU A N   
2569 C CA  . LEU A 364 ? 0.5951 0.4903 0.3583 0.0812  0.1216  -0.0536 490 LEU A CA  
2570 C C   . LEU A 364 ? 0.6607 0.5582 0.4093 0.0655  0.1108  -0.0449 490 LEU A C   
2571 O O   . LEU A 364 ? 0.6315 0.5486 0.3867 0.0606  0.1154  -0.0330 490 LEU A O   
2572 C CB  . LEU A 364 ? 0.5974 0.4715 0.3247 0.0908  0.1346  -0.0690 490 LEU A CB  
2573 C CG  . LEU A 364 ? 0.6791 0.5621 0.3784 0.0910  0.1505  -0.0698 490 LEU A CG  
2574 C CD1 . LEU A 364 ? 0.7326 0.6557 0.4631 0.0931  0.1637  -0.0558 490 LEU A CD1 
2575 C CD2 . LEU A 364 ? 0.7228 0.5840 0.3932 0.1044  0.1636  -0.0875 490 LEU A CD2 
2576 N N   . LEU A 365 ? 0.6371 0.5153 0.3668 0.0572  0.0957  -0.0494 491 LEU A N   
2577 C CA  . LEU A 365 ? 0.6630 0.5454 0.3814 0.0451  0.0833  -0.0402 491 LEU A CA  
2578 C C   . LEU A 365 ? 0.6315 0.5314 0.3830 0.0425  0.0764  -0.0257 491 LEU A C   
2579 O O   . LEU A 365 ? 0.6706 0.5784 0.4183 0.0370  0.0745  -0.0141 491 LEU A O   
2580 C CB  . LEU A 365 ? 0.6938 0.5591 0.3938 0.0368  0.0670  -0.0471 491 LEU A CB  
2581 C CG  . LEU A 365 ? 0.7013 0.5432 0.3592 0.0356  0.0714  -0.0620 491 LEU A CG  
2582 C CD1 . LEU A 365 ? 0.7709 0.5966 0.4153 0.0241  0.0538  -0.0689 491 LEU A CD1 
2583 C CD2 . LEU A 365 ? 0.7521 0.5987 0.3786 0.0322  0.0770  -0.0584 491 LEU A CD2 
2584 N N   . GLU A 366 ? 0.5920 0.4944 0.3726 0.0463  0.0725  -0.0264 492 GLU A N   
2585 C CA  . GLU A 366 ? 0.6062 0.5205 0.4146 0.0443  0.0659  -0.0157 492 GLU A CA  
2586 C C   . GLU A 366 ? 0.6174 0.5471 0.4402 0.0446  0.0769  -0.0072 492 GLU A C   
2587 O O   . GLU A 366 ? 0.6443 0.5778 0.4712 0.0383  0.0730  0.0041  492 GLU A O   
2588 C CB  . GLU A 366 ? 0.5523 0.4645 0.3826 0.0479  0.0597  -0.0198 492 GLU A CB  
2589 C CG  . GLU A 366 ? 0.5675 0.4885 0.4222 0.0467  0.0532  -0.0116 492 GLU A CG  
2590 C CD  . GLU A 366 ? 0.5166 0.4360 0.3880 0.0499  0.0480  -0.0157 492 GLU A CD  
2591 O OE1 . GLU A 366 ? 0.5641 0.4748 0.4299 0.0531  0.0498  -0.0233 492 GLU A OE1 
2592 O OE2 . GLU A 366 ? 0.5098 0.4336 0.3967 0.0491  0.0421  -0.0112 492 GLU A OE2 
2593 N N   . ASN A 367 ? 0.5455 0.4843 0.3766 0.0519  0.0905  -0.0117 493 ASN A N   
2594 C CA  . ASN A 367 ? 0.5610 0.5222 0.4129 0.0504  0.1004  -0.0026 493 ASN A CA  
2595 C C   . ASN A 367 ? 0.5939 0.5624 0.4258 0.0445  0.1116  0.0044  493 ASN A C   
2596 O O   . ASN A 367 ? 0.6014 0.5858 0.4471 0.0364  0.1158  0.0166  493 ASN A O   
2597 C CB  . ASN A 367 ? 0.5704 0.5461 0.4434 0.0621  0.1110  -0.0081 493 ASN A CB  
2598 C CG  . ASN A 367 ? 0.5901 0.5669 0.4902 0.0646  0.0999  -0.0082 493 ASN A CG  
2599 O OD1 . ASN A 367 ? 0.6284 0.6227 0.5540 0.0595  0.0972  0.0001  493 ASN A OD1 
2600 N ND2 . ASN A 367 ? 0.5726 0.5297 0.4649 0.0704  0.0928  -0.0171 493 ASN A ND2 
2601 N N   . GLY A 368 ? 0.6151 0.5713 0.4126 0.0466  0.1161  -0.0027 494 GLY A N   
2602 C CA  . GLY A 368 ? 0.6176 0.5812 0.3909 0.0419  0.1288  0.0031  494 GLY A CA  
2603 C C   . GLY A 368 ? 0.6616 0.6139 0.4112 0.0302  0.1179  0.0141  494 GLY A C   
2604 O O   . GLY A 368 ? 0.6602 0.6177 0.3876 0.0243  0.1274  0.0221  494 GLY A O   
2605 N N   . ALA A 369 ? 0.6483 0.5863 0.4013 0.0276  0.0985  0.0157  495 ALA A N   
2606 C CA  . ALA A 369 ? 0.6548 0.5823 0.3867 0.0200  0.0864  0.0268  495 ALA A CA  
2607 C C   . ALA A 369 ? 0.6387 0.5695 0.3849 0.0122  0.0858  0.0443  495 ALA A C   
2608 O O   . ALA A 369 ? 0.6319 0.5657 0.4092 0.0121  0.0827  0.0461  495 ALA A O   
2609 C CB  . ALA A 369 ? 0.6782 0.5945 0.4131 0.0223  0.0669  0.0224  495 ALA A CB  
2610 N N   . ASN A 370 ? 0.6605 0.5874 0.3806 0.0044  0.0878  0.0576  496 ASN A N   
2611 C CA  . ASN A 370 ? 0.6627 0.5853 0.3910 -0.0054 0.0860  0.0758  496 ASN A CA  
2612 C C   . ASN A 370 ? 0.6739 0.5789 0.4191 -0.0027 0.0670  0.0793  496 ASN A C   
2613 O O   . ASN A 370 ? 0.6814 0.5789 0.4420 -0.0093 0.0648  0.0892  496 ASN A O   
2614 C CB  . ASN A 370 ? 0.7430 0.6590 0.4343 -0.0140 0.0887  0.0910  496 ASN A CB  
2615 N N   . SER A 371 ? 0.6414 0.5401 0.3842 0.0066  0.0537  0.0707  497 SER A N   
2616 C CA  . SER A 371 ? 0.6445 0.5299 0.4028 0.0121  0.0379  0.0731  497 SER A CA  
2617 C C   . SER A 371 ? 0.6143 0.5047 0.4049 0.0162  0.0383  0.0622  497 SER A C   
2618 O O   . SER A 371 ? 0.6002 0.4787 0.4036 0.0204  0.0282  0.0636  497 SER A O   
2619 C CB  . SER A 371 ? 0.6367 0.5207 0.3827 0.0199  0.0237  0.0702  497 SER A CB  
2620 O OG  . SER A 371 ? 0.6474 0.5439 0.3965 0.0229  0.0257  0.0541  497 SER A OG  
2621 N N   . SER A 372 ? 0.5900 0.4961 0.3920 0.0164  0.0495  0.0515  498 SER A N   
2622 C CA  . SER A 372 ? 0.5633 0.4742 0.3929 0.0207  0.0480  0.0420  498 SER A CA  
2623 C C   . SER A 372 ? 0.5412 0.4515 0.3897 0.0133  0.0498  0.0488  498 SER A C   
2624 O O   . SER A 372 ? 0.5084 0.4277 0.3573 0.0042  0.0599  0.0566  498 SER A O   
2625 C CB  . SER A 372 ? 0.5792 0.5041 0.4135 0.0253  0.0577  0.0295  498 SER A CB  
2626 O OG  . SER A 372 ? 0.5611 0.4815 0.3788 0.0299  0.0528  0.0212  498 SER A OG  
2627 N N   . PHE A 373 ? 0.5455 0.4462 0.4088 0.0163  0.0402  0.0455  499 PHE A N   
2628 C CA  . PHE A 373 ? 0.5375 0.4355 0.4175 0.0077  0.0393  0.0492  499 PHE A CA  
2629 C C   . PHE A 373 ? 0.4822 0.4069 0.3801 0.0022  0.0509  0.0479  499 PHE A C   
2630 O O   . PHE A 373 ? 0.5080 0.4395 0.4145 -0.0106 0.0549  0.0570  499 PHE A O   
2631 C CB  . PHE A 373 ? 0.5325 0.4195 0.4233 0.0139  0.0289  0.0410  499 PHE A CB  
2632 C CG  . PHE A 373 ? 0.5011 0.3848 0.4065 0.0038  0.0261  0.0422  499 PHE A CG  
2633 C CD1 . PHE A 373 ? 0.4768 0.3835 0.4024 0.0015  0.0298  0.0371  499 PHE A CD1 
2634 C CD2 . PHE A 373 ? 0.5453 0.4019 0.4428 -0.0041 0.0190  0.0492  499 PHE A CD2 
2635 C CE1 . PHE A 373 ? 0.5139 0.4211 0.4531 -0.0100 0.0251  0.0388  499 PHE A CE1 
2636 C CE2 . PHE A 373 ? 0.5495 0.4009 0.4578 -0.0169 0.0148  0.0497  499 PHE A CE2 
2637 C CZ  . PHE A 373 ? 0.5211 0.4004 0.4511 -0.0206 0.0173  0.0445  499 PHE A CZ  
2638 N N   . VAL A 374 ? 0.5291 0.4696 0.4339 0.0118  0.0559  0.0375  500 VAL A N   
2639 C CA  . VAL A 374 ? 0.4904 0.4576 0.4156 0.0112  0.0662  0.0362  500 VAL A CA  
2640 C C   . VAL A 374 ? 0.5220 0.5055 0.4404 0.0062  0.0812  0.0435  500 VAL A C   
2641 O O   . VAL A 374 ? 0.5135 0.5238 0.4522 0.0016  0.0907  0.0478  500 VAL A O   
2642 C CB  . VAL A 374 ? 0.5278 0.5012 0.4588 0.0248  0.0674  0.0238  500 VAL A CB  
2643 C CG1 . VAL A 374 ? 0.5175 0.4777 0.4543 0.0278  0.0540  0.0185  500 VAL A CG1 
2644 C CG2 . VAL A 374 ? 0.5352 0.5004 0.4418 0.0324  0.0725  0.0175  500 VAL A CG2 
2645 N N   . HIS A 375 ? 0.5166 0.4876 0.4066 0.0064  0.0836  0.0460  501 HIS A N   
2646 C CA  . HIS A 375 ? 0.5184 0.5036 0.3971 -0.0002 0.0985  0.0546  501 HIS A CA  
2647 C C   . HIS A 375 ? 0.5957 0.5762 0.4762 -0.0178 0.0961  0.0712  501 HIS A C   
2648 O O   . HIS A 375 ? 0.5824 0.5867 0.4750 -0.0284 0.1081  0.0803  501 HIS A O   
2649 C CB  . HIS A 375 ? 0.5960 0.5685 0.4388 0.0049  0.1009  0.0517  501 HIS A CB  
2650 C CG  . HIS A 375 ? 0.6006 0.5882 0.4262 -0.0003 0.1183  0.0587  501 HIS A CG  
2651 N ND1 . HIS A 375 ? 0.6473 0.6296 0.4575 -0.0143 0.1195  0.0754  501 HIS A ND1 
2652 C CD2 . HIS A 375 ? 0.6451 0.6521 0.4649 0.0072  0.1365  0.0514  501 HIS A CD2 
2653 C CE1 . HIS A 375 ? 0.6662 0.6671 0.4614 -0.0166 0.1381  0.0788  501 HIS A CE1 
2654 N NE2 . HIS A 375 ? 0.6702 0.6870 0.4712 -0.0026 0.1493  0.0634  501 HIS A NE2 
2655 N N   . ARG A 376 ? 0.5742 0.5237 0.4430 -0.0210 0.0808  0.0758  502 ARG A N   
2656 C CA  . ARG A 376 ? 0.5847 0.5181 0.4484 -0.0374 0.0767  0.0918  502 ARG A CA  
2657 C C   . ARG A 376 ? 0.5717 0.5173 0.4648 -0.0509 0.0760  0.0952  502 ARG A C   
2658 O O   . ARG A 376 ? 0.6065 0.5539 0.5007 -0.0696 0.0798  0.1098  502 ARG A O   
2659 C CB  . ARG A 376 ? 0.5922 0.4869 0.4383 -0.0324 0.0597  0.0936  502 ARG A CB  
2660 C CG  . ARG A 376 ? 0.6382 0.5232 0.4533 -0.0259 0.0591  0.0979  502 ARG A CG  
2661 C CD  . ARG A 376 ? 0.6818 0.5478 0.4907 -0.0110 0.0441  0.0909  502 ARG A CD  
2662 N NE  . ARG A 376 ? 0.6943 0.5315 0.5080 -0.0113 0.0317  0.0950  502 ARG A NE  
2663 C CZ  . ARG A 376 ? 0.7424 0.5501 0.5381 -0.0152 0.0244  0.1095  502 ARG A CZ  
2664 N NH1 . ARG A 376 ? 0.7781 0.5830 0.5496 -0.0210 0.0278  0.1235  502 ARG A NH1 
2665 N NH2 . ARG A 376 ? 0.7766 0.5538 0.5757 -0.0125 0.0134  0.1100  502 ARG A NH2 
2666 N N   . ILE A 377 ? 0.5956 0.5506 0.5118 -0.0436 0.0705  0.0831  503 ILE A N   
2667 C CA  . ILE A 377 ? 0.5745 0.5409 0.5174 -0.0571 0.0661  0.0856  503 ILE A CA  
2668 C C   . ILE A 377 ? 0.5963 0.6062 0.5604 -0.0683 0.0815  0.0944  503 ILE A C   
2669 O O   . ILE A 377 ? 0.6171 0.6390 0.6008 -0.0874 0.0787  0.1030  503 ILE A O   
2670 C CB  . ILE A 377 ? 0.5868 0.5563 0.5462 -0.0452 0.0570  0.0710  503 ILE A CB  
2671 C CG1 . ILE A 377 ? 0.5895 0.5612 0.5691 -0.0608 0.0467  0.0732  503 ILE A CG1 
2672 C CG2 . ILE A 377 ? 0.5645 0.5678 0.5383 -0.0306 0.0682  0.0629  503 ILE A CG2 
2673 C CD1 . ILE A 377 ? 0.6210 0.5470 0.5822 -0.0697 0.0323  0.0748  503 ILE A CD1 
2674 N N   . ASN A 378 ? 0.5597 0.5939 0.5193 -0.0574 0.0981  0.0924  504 ASN A N   
2675 C CA  . ASN A 378 ? 0.6192 0.6986 0.5970 -0.0637 0.1169  0.1003  504 ASN A CA  
2676 C C   . ASN A 378 ? 0.6248 0.7020 0.5779 -0.0760 0.1290  0.1146  504 ASN A C   
2677 O O   . ASN A 378 ? 0.6399 0.7566 0.6049 -0.0822 0.1475  0.1226  504 ASN A O   
2678 C CB  . ASN A 378 ? 0.6261 0.7328 0.6127 -0.0407 0.1297  0.0871  504 ASN A CB  
2679 C CG  . ASN A 378 ? 0.6423 0.7555 0.6547 -0.0295 0.1191  0.0761  504 ASN A CG  
2680 O OD1 . ASN A 378 ? 0.6624 0.7811 0.6975 -0.0418 0.1072  0.0803  504 ASN A OD1 
2681 N ND2 . ASN A 378 ? 0.6938 0.8037 0.7001 -0.0074 0.1222  0.0623  504 ASN A ND2 
2682 N N   . ASP A 379 ? 0.6468 0.6808 0.5659 -0.0788 0.1194  0.1191  505 ASP A N   
2683 C CA  . ASP A 379 ? 0.6931 0.7200 0.5819 -0.0887 0.1290  0.1335  505 ASP A CA  
2684 C C   . ASP A 379 ? 0.7295 0.7480 0.6230 -0.1167 0.1253  0.1533  505 ASP A C   
2685 O O   . ASP A 379 ? 0.7114 0.6883 0.5976 -0.1233 0.1067  0.1562  505 ASP A O   
2686 C CB  . ASP A 379 ? 0.7025 0.6883 0.5530 -0.0771 0.1182  0.1302  505 ASP A CB  
2687 C CG  . ASP A 379 ? 0.7869 0.7698 0.6012 -0.0823 0.1289  0.1425  505 ASP A CG  
2688 O OD1 . ASP A 379 ? 0.8158 0.8107 0.6294 -0.1018 0.1393  0.1598  505 ASP A OD1 
2689 O OD2 . ASP A 379 ? 0.8374 0.8068 0.6229 -0.0685 0.1265  0.1354  505 ASP A OD2 
2690 N N   . PRO A 380 ? 0.7622 0.8174 0.6669 -0.1339 0.1426  0.1673  506 PRO A N   
2691 C CA  . PRO A 380 ? 0.7670 0.8119 0.6748 -0.1651 0.1384  0.1879  506 PRO A CA  
2692 C C   . PRO A 380 ? 0.8488 0.8418 0.7124 -0.1741 0.1309  0.2029  506 PRO A C   
2693 O O   . PRO A 380 ? 0.8609 0.8309 0.7209 -0.1998 0.1241  0.2202  506 PRO A O   
2694 C CB  . PRO A 380 ? 0.7754 0.8820 0.7064 -0.1787 0.1626  0.1992  506 PRO A CB  
2695 C CG  . PRO A 380 ? 0.8100 0.9405 0.7262 -0.1538 0.1815  0.1883  506 PRO A CG  
2696 C CD  . PRO A 380 ? 0.7410 0.8482 0.6544 -0.1260 0.1678  0.1652  506 PRO A CD  
2697 N N   . LYS A 381 ? 0.8220 0.7947 0.6510 -0.1548 0.1308  0.1979  507 LYS A N   
2698 C CA  . LYS A 381 ? 0.8496 0.7709 0.6380 -0.1589 0.1192  0.2118  507 LYS A CA  
2699 C C   . LYS A 381 ? 0.8270 0.6978 0.6123 -0.1490 0.0944  0.2042  507 LYS A C   
2700 O O   . LYS A 381 ? 0.8389 0.6623 0.5966 -0.1539 0.0823  0.2176  507 LYS A O   
2701 C CB  . LYS A 381 ? 0.8880 0.8110 0.6398 -0.1431 0.1270  0.2103  507 LYS A CB  
2702 N N   . VAL A 382 ? 0.7968 0.6762 0.6086 -0.1342 0.0874  0.1837  508 VAL A N   
2703 C CA  . VAL A 382 ? 0.7678 0.6057 0.5766 -0.1208 0.0669  0.1735  508 VAL A CA  
2704 C C   . VAL A 382 ? 0.7881 0.6093 0.6168 -0.1378 0.0568  0.1742  508 VAL A C   
2705 O O   . VAL A 382 ? 0.7507 0.6066 0.6115 -0.1444 0.0611  0.1666  508 VAL A O   
2706 C CB  . VAL A 382 ? 0.7563 0.6114 0.5765 -0.0948 0.0651  0.1510  508 VAL A CB  
2707 C CG1 . VAL A 382 ? 0.7000 0.5169 0.5174 -0.0810 0.0462  0.1416  508 VAL A CG1 
2708 C CG2 . VAL A 382 ? 0.7367 0.6070 0.5352 -0.0810 0.0740  0.1488  508 VAL A CG2 
2709 N N   . SER A 383 ? 0.8036 0.5699 0.6119 -0.1436 0.0422  0.1825  509 SER A N   
2710 C CA  . SER A 383 ? 0.7776 0.5160 0.5960 -0.1606 0.0303  0.1820  509 SER A CA  
2711 C C   . SER A 383 ? 0.7979 0.5263 0.6280 -0.1409 0.0186  0.1593  509 SER A C   
2712 O O   . SER A 383 ? 0.7461 0.4812 0.5737 -0.1144 0.0181  0.1469  509 SER A O   
2713 C CB  . SER A 383 ? 0.8534 0.5282 0.6398 -0.1730 0.0194  0.1992  509 SER A CB  
2714 O OG  . SER A 383 ? 0.9242 0.5556 0.6895 -0.1463 0.0067  0.1918  509 SER A OG  
2715 N N   . ILE A 384 ? 0.7617 0.4741 0.6032 -0.1561 0.0087  0.1545  510 ILE A N   
2716 C CA  . ILE A 384 ? 0.8079 0.5051 0.6545 -0.1396 -0.0027 0.1339  510 ILE A CA  
2717 C C   . ILE A 384 ? 0.7815 0.4195 0.5980 -0.1202 -0.0140 0.1308  510 ILE A C   
2718 O O   . ILE A 384 ? 0.7555 0.3918 0.5724 -0.0949 -0.0177 0.1150  510 ILE A O   
2719 C CB  . ILE A 384 ? 0.8605 0.5569 0.7237 -0.1632 -0.0112 0.1295  510 ILE A CB  
2720 C CG1 . ILE A 384 ? 0.8469 0.6139 0.7476 -0.1714 -0.0006 0.1282  510 ILE A CG1 
2721 C CG2 . ILE A 384 ? 0.8026 0.4651 0.6580 -0.1489 -0.0251 0.1099  510 ILE A CG2 
2722 C CD1 . ILE A 384 ? 0.9022 0.6833 0.8233 -0.2048 -0.0062 0.1344  510 ILE A CD1 
2723 N N   . ASP A 385 ? 0.8300 0.4194 0.6205 -0.1310 -0.0193 0.1470  511 ASP A N   
2724 C CA  . ASP A 385 ? 0.8280 0.3615 0.5906 -0.1089 -0.0297 0.1460  511 ASP A CA  
2725 C C   . ASP A 385 ? 0.8172 0.3761 0.5791 -0.0786 -0.0251 0.1425  511 ASP A C   
2726 O O   . ASP A 385 ? 0.8194 0.3644 0.5781 -0.0524 -0.0314 0.1298  511 ASP A O   
2727 C CB  . ASP A 385 ? 0.9038 0.3833 0.6376 -0.1254 -0.0350 0.1679  511 ASP A CB  
2728 C CG  . ASP A 385 ? 1.0087 0.4649 0.7444 -0.1594 -0.0402 0.1715  511 ASP A CG  
2729 O OD1 . ASP A 385 ? 1.0228 0.4653 0.7650 -0.1614 -0.0484 0.1543  511 ASP A OD1 
2730 O OD2 . ASP A 385 ? 1.0220 0.4833 0.7564 -0.1823 -0.0354 0.1892  511 ASP A OD2 
2731 N N   . GLU A 386 ? 0.8172 0.4163 0.5821 -0.0827 -0.0138 0.1528  512 GLU A N   
2732 C CA  . GLU A 386 ? 0.7823 0.4091 0.5462 -0.0583 -0.0104 0.1483  512 GLU A CA  
2733 C C   . GLU A 386 ? 0.7736 0.4356 0.5619 -0.0430 -0.0082 0.1261  512 GLU A C   
2734 O O   . GLU A 386 ? 0.7253 0.3922 0.5126 -0.0195 -0.0119 0.1177  512 GLU A O   
2735 C CB  . GLU A 386 ? 0.8069 0.4677 0.5654 -0.0690 0.0022  0.1617  512 GLU A CB  
2736 C CG  . GLU A 386 ? 0.7998 0.4956 0.5584 -0.0496 0.0068  0.1543  512 GLU A CG  
2737 C CD  . GLU A 386 ? 0.8824 0.5531 0.6202 -0.0287 -0.0050 0.1591  512 GLU A CD  
2738 O OE1 . GLU A 386 ? 0.9039 0.5281 0.6237 -0.0282 -0.0150 0.1716  512 GLU A OE1 
2739 O OE2 . GLU A 386 ? 0.9470 0.6446 0.6869 -0.0127 -0.0049 0.1509  512 GLU A OE2 
2740 N N   . LEU A 387 ? 0.7310 0.4191 0.5418 -0.0566 -0.0030 0.1178  513 LEU A N   
2741 C CA  . LEU A 387 ? 0.7107 0.4303 0.5421 -0.0429 -0.0012 0.0990  513 LEU A CA  
2742 C C   . LEU A 387 ? 0.7165 0.4069 0.5451 -0.0278 -0.0121 0.0854  513 LEU A C   
2743 O O   . LEU A 387 ? 0.6792 0.3894 0.5173 -0.0106 -0.0115 0.0721  513 LEU A O   
2744 C CB  . LEU A 387 ? 0.6646 0.4210 0.5211 -0.0596 0.0060  0.0956  513 LEU A CB  
2745 C CG  . LEU A 387 ? 0.6568 0.4575 0.5221 -0.0644 0.0211  0.1019  513 LEU A CG  
2746 C CD1 . LEU A 387 ? 0.6719 0.5071 0.5641 -0.0823 0.0276  0.1028  513 LEU A CD1 
2747 C CD2 . LEU A 387 ? 0.6485 0.4729 0.5159 -0.0428 0.0255  0.0902  513 LEU A CD2 
2748 N N   . ILE A 388 ? 0.7266 0.3688 0.5406 -0.0345 -0.0214 0.0882  514 ILE A N   
2749 C CA  . ILE A 388 ? 0.7539 0.3648 0.5608 -0.0185 -0.0301 0.0738  514 ILE A CA  
2750 C C   . ILE A 388 ? 0.7771 0.3553 0.5650 0.0053  -0.0354 0.0774  514 ILE A C   
2751 O O   . ILE A 388 ? 0.7793 0.3267 0.5584 0.0214  -0.0415 0.0665  514 ILE A O   
2752 C CB  . ILE A 388 ? 0.8138 0.3862 0.6130 -0.0374 -0.0383 0.0703  514 ILE A CB  
2753 C CG1 . ILE A 388 ? 0.8455 0.3686 0.6221 -0.0518 -0.0436 0.0873  514 ILE A CG1 
2754 C CG2 . ILE A 388 ? 0.7478 0.3595 0.5703 -0.0600 -0.0351 0.0674  514 ILE A CG2 
2755 C CD1 . ILE A 388 ? 0.9224 0.3865 0.6804 -0.0637 -0.0551 0.0815  514 ILE A CD1 
2756 N N   . ALA A 389 ? 0.7698 0.3543 0.5500 0.0086  -0.0335 0.0927  515 ALA A N   
2757 C CA  . ALA A 389 ? 0.8196 0.3797 0.5847 0.0326  -0.0400 0.0984  515 ALA A CA  
2758 C C   . ALA A 389 ? 0.8174 0.4002 0.5955 0.0593  -0.0402 0.0825  515 ALA A C   
2759 O O   . ALA A 389 ? 0.7279 0.3574 0.5247 0.0595  -0.0337 0.0735  515 ALA A O   
2760 C CB  . ALA A 389 ? 0.7969 0.3737 0.5536 0.0308  -0.0381 0.1164  515 ALA A CB  
2761 N N   . ASP A 390 ? 0.8220 0.3708 0.5899 0.0818  -0.0469 0.0795  516 ASP A N   
2762 C CA  . ASP A 390 ? 0.8395 0.4134 0.6206 0.1087  -0.0460 0.0671  516 ASP A CA  
2763 C C   . ASP A 390 ? 0.8832 0.4893 0.6698 0.1221  -0.0479 0.0785  516 ASP A C   
2764 O O   . ASP A 390 ? 0.8558 0.4360 0.6275 0.1308  -0.0553 0.0937  516 ASP A O   
2765 C CB  . ASP A 390 ? 0.9198 0.4474 0.6883 0.1305  -0.0508 0.0590  516 ASP A CB  
2766 C CG  . ASP A 390 ? 0.9125 0.4707 0.6964 0.1593  -0.0477 0.0469  516 ASP A CG  
2767 O OD1 . ASP A 390 ? 0.9291 0.5425 0.7335 0.1605  -0.0434 0.0458  516 ASP A OD1 
2768 O OD2 . ASP A 390 ? 0.9950 0.5383 0.7784 0.1741  -0.0472 0.0370  516 ASP A OD2 
2769 N N   . PRO A 391 ? 0.8044 0.4640 0.6102 0.1232  -0.0430 0.0721  517 PRO A N   
2770 C CA  . PRO A 391 ? 0.8348 0.5262 0.6438 0.1312  -0.0468 0.0825  517 PRO A CA  
2771 C C   . PRO A 391 ? 0.8706 0.5517 0.6779 0.1591  -0.0560 0.0898  517 PRO A C   
2772 O O   . PRO A 391 ? 0.8826 0.5658 0.6808 0.1627  -0.0636 0.1059  517 PRO A O   
2773 C CB  . PRO A 391 ? 0.7512 0.4938 0.5814 0.1289  -0.0405 0.0697  517 PRO A CB  
2774 C CG  . PRO A 391 ? 0.7219 0.4604 0.5558 0.1117  -0.0325 0.0587  517 PRO A CG  
2775 C CD  . PRO A 391 ? 0.7662 0.4568 0.5885 0.1135  -0.0350 0.0567  517 PRO A CD  
2776 N N   . VAL A 392 ? 0.8710 0.5424 0.6861 0.1804  -0.0554 0.0787  518 VAL A N   
2777 C CA  . VAL A 392 ? 0.9258 0.5918 0.7436 0.2103  -0.0627 0.0850  518 VAL A CA  
2778 C C   . VAL A 392 ? 0.9422 0.5636 0.7417 0.2070  -0.0695 0.0991  518 VAL A C   
2779 O O   . VAL A 392 ? 0.9840 0.6141 0.7852 0.2180  -0.0777 0.1132  518 VAL A O   
2780 C CB  . VAL A 392 ? 0.9232 0.5947 0.7562 0.2275  -0.0558 0.0668  518 VAL A CB  
2781 C CG1 . VAL A 392 ? 0.9535 0.6309 0.7978 0.2523  -0.0600 0.0713  518 VAL A CG1 
2782 C CG2 . VAL A 392 ? 0.8774 0.5969 0.7292 0.2298  -0.0491 0.0556  518 VAL A CG2 
2783 N N   . GLU A 393 ? 1.0242 0.5986 0.8065 0.1901  -0.0670 0.0965  519 GLU A N   
2784 C CA  . GLU A 393 ? 1.0711 0.6015 0.8348 0.1827  -0.0730 0.1111  519 GLU A CA  
2785 C C   . GLU A 393 ? 1.0363 0.5770 0.7884 0.1704  -0.0781 0.1326  519 GLU A C   
2786 O O   . GLU A 393 ? 1.1157 0.6421 0.8599 0.1762  -0.0856 0.1483  519 GLU A O   
2787 C CB  . GLU A 393 ? 1.0888 0.5734 0.8370 0.1604  -0.0698 0.1048  519 GLU A CB  
2788 C CG  . GLU A 393 ? 1.1406 0.6013 0.8905 0.1720  -0.0673 0.0858  519 GLU A CG  
2789 C CD  . GLU A 393 ? 1.2316 0.6585 0.9684 0.1461  -0.0652 0.0769  519 GLU A CD  
2790 O OE1 . GLU A 393 ? 1.2826 0.7046 1.0116 0.1192  -0.0654 0.0875  519 GLU A OE1 
2791 O OE2 . GLU A 393 ? 1.2534 0.6615 0.9874 0.1517  -0.0633 0.0595  519 GLU A OE2 
2792 N N   . VAL A 394 ? 0.9970 0.5623 0.7459 0.1538  -0.0739 0.1336  520 VAL A N   
2793 C CA  . VAL A 394 ? 1.0249 0.5990 0.7568 0.1391  -0.0765 0.1526  520 VAL A CA  
2794 C C   . VAL A 394 ? 1.0222 0.6385 0.7615 0.1562  -0.0843 0.1593  520 VAL A C   
2795 O O   . VAL A 394 ? 1.0049 0.6448 0.7660 0.1794  -0.0877 0.1510  520 VAL A O   
2796 C CB  . VAL A 394 ? 0.9577 0.5568 0.6924 0.1094  -0.0647 0.1467  520 VAL A CB  
2797 N N   . ARG B 2   ? 0.7875 1.4591 0.7006 -0.4510 -0.2642 0.1846  26  ARG B N   
2798 C CA  . ARG B 2   ? 0.7260 1.4187 0.6724 -0.4068 -0.2510 0.1945  26  ARG B CA  
2799 C C   . ARG B 2   ? 0.7095 1.3361 0.6204 -0.3918 -0.2382 0.1652  26  ARG B C   
2800 O O   . ARG B 2   ? 0.7255 1.2926 0.6032 -0.4069 -0.2328 0.1381  26  ARG B O   
2801 C CB  . ARG B 2   ? 0.6786 1.4088 0.6784 -0.3857 -0.2395 0.2112  26  ARG B CB  
2802 N N   . PRO B 3   ? 0.6822 1.3182 0.5997 -0.3619 -0.2334 0.1715  27  PRO B N   
2803 C CA  . PRO B 3   ? 0.6682 1.2463 0.5526 -0.3469 -0.2210 0.1462  27  PRO B CA  
2804 C C   . PRO B 3   ? 0.6989 1.2459 0.5933 -0.3346 -0.2055 0.1312  27  PRO B C   
2805 O O   . PRO B 3   ? 0.6306 1.2129 0.5711 -0.3150 -0.1991 0.1475  27  PRO B O   
2806 C CB  . PRO B 3   ? 0.6417 1.2495 0.5452 -0.3141 -0.2191 0.1652  27  PRO B CB  
2807 C CG  . PRO B 3   ? 0.6679 1.3339 0.5915 -0.3233 -0.2352 0.1932  27  PRO B CG  
2808 C CD  . PRO B 3   ? 0.6757 1.3716 0.6244 -0.3437 -0.2406 0.2022  27  PRO B CD  
2809 N N   . GLN B 4   ? 0.6780 1.1577 0.5279 -0.3456 -0.1986 0.0997  28  GLN B N   
2810 C CA  . GLN B 4   ? 0.6918 1.1333 0.5438 -0.3375 -0.1847 0.0824  28  GLN B CA  
2811 C C   . GLN B 4   ? 0.6864 1.1530 0.5735 -0.3482 -0.1862 0.0944  28  GLN B C   
2812 O O   . GLN B 4   ? 0.6448 1.1137 0.5589 -0.3316 -0.1753 0.0957  28  GLN B O   
2813 C CB  . GLN B 4   ? 0.6415 1.0859 0.5108 -0.3002 -0.1720 0.0848  28  GLN B CB  
2814 C CG  . GLN B 4   ? 0.6913 1.0989 0.5192 -0.2907 -0.1667 0.0694  28  GLN B CG  
2815 C CD  . GLN B 4   ? 0.6826 1.1211 0.5035 -0.2927 -0.1780 0.0858  28  GLN B CD  
2816 O OE1 . GLN B 4   ? 0.6676 1.1565 0.5252 -0.2734 -0.1821 0.1132  28  GLN B OE1 
2817 N NE2 . GLN B 4   ? 0.6815 1.0879 0.4548 -0.3147 -0.1821 0.0692  28  GLN B NE2 
2818 N N   . SER B 5   ? 0.7215 1.2084 0.6069 -0.3771 -0.1996 0.1040  29  SER B N   
2819 C CA  . SER B 5   ? 0.6494 1.1653 0.5672 -0.3890 -0.2013 0.1187  29  SER B CA  
2820 C C   . SER B 5   ? 0.6734 1.1339 0.5791 -0.3956 -0.1909 0.0983  29  SER B C   
2821 O O   . SER B 5   ? 0.6166 1.0985 0.5581 -0.3851 -0.1828 0.1093  29  SER B O   
2822 C CB  . SER B 5   ? 0.7056 1.2420 0.6131 -0.4243 -0.2188 0.1289  29  SER B CB  
2823 N N   . THR B 6   ? 0.6894 1.0770 0.5442 -0.4113 -0.1897 0.0689  30  THR B N   
2824 C CA  . THR B 6   ? 0.7325 1.0618 0.5740 -0.4182 -0.1804 0.0504  30  THR B CA  
2825 C C   . THR B 6   ? 0.6885 1.0142 0.5535 -0.3872 -0.1647 0.0478  30  THR B C   
2826 O O   . THR B 6   ? 0.6506 0.9750 0.5387 -0.3859 -0.1578 0.0527  30  THR B O   
2827 C CB  . THR B 6   ? 0.7750 1.0239 0.5564 -0.4351 -0.1797 0.0189  30  THR B CB  
2828 O OG1 . THR B 6   ? 0.8227 1.0710 0.5832 -0.4688 -0.1948 0.0215  30  THR B OG1 
2829 C CG2 . THR B 6   ? 0.8157 0.9977 0.5840 -0.4335 -0.1672 -0.0008 30  THR B CG2 
2830 N N   . LEU B 7   ? 0.6909 1.0173 0.5503 -0.3626 -0.1591 0.0420  31  LEU B N   
2831 C CA  . LEU B 7   ? 0.6413 0.9663 0.5210 -0.3338 -0.1457 0.0398  31  LEU B CA  
2832 C C   . LEU B 7   ? 0.5680 0.9602 0.5052 -0.3130 -0.1417 0.0686  31  LEU B C   
2833 O O   . LEU B 7   ? 0.5401 0.9193 0.4978 -0.2918 -0.1248 0.0696  31  LEU B O   
2834 C CB  . LEU B 7   ? 0.6361 0.9410 0.4945 -0.3076 -0.1370 0.0296  31  LEU B CB  
2835 C CG  . LEU B 7   ? 0.6544 0.8887 0.4567 -0.3195 -0.1332 -0.0013 31  LEU B CG  
2836 C CD1 . LEU B 7   ? 0.6366 0.8706 0.4210 -0.2990 -0.1279 -0.0046 31  LEU B CD1 
2837 C CD2 . LEU B 7   ? 0.6622 0.8339 0.4600 -0.3064 -0.1143 -0.0190 31  LEU B CD2 
2838 N N   . ARG B 8   ? 0.5728 1.0285 0.5340 -0.3113 -0.1519 0.0922  32  ARG B N   
2839 C CA  . ARG B 8   ? 0.5545 1.0750 0.5697 -0.2884 -0.1461 0.1191  32  ARG B CA  
2840 C C   . ARG B 8   ? 0.5047 1.0383 0.5407 -0.3047 -0.1434 0.1282  32  ARG B C   
2841 O O   . ARG B 8   ? 0.4631 1.0180 0.5320 -0.2857 -0.1299 0.1375  32  ARG B O   
2842 C CB  . ARG B 8   ? 0.4971 1.0740 0.5310 -0.2784 -0.1548 0.1427  32  ARG B CB  
2843 C CG  . ARG B 8   ? 0.5302 1.1065 0.5575 -0.2508 -0.1534 0.1429  32  ARG B CG  
2844 C CD  . ARG B 8   ? 0.6170 1.2567 0.6804 -0.2306 -0.1566 0.1731  32  ARG B CD  
2845 N NE  . ARG B 8   ? 0.6046 1.2412 0.6557 -0.2113 -0.1594 0.1767  32  ARG B NE  
2846 C CZ  . ARG B 8   ? 0.5551 1.1924 0.6212 -0.1741 -0.1490 0.1826  32  ARG B CZ  
2847 N NH1 . ARG B 8   ? 0.6069 1.2457 0.6993 -0.1507 -0.1337 0.1827  32  ARG B NH1 
2848 N NH2 . ARG B 8   ? 0.5383 1.1711 0.5909 -0.1600 -0.1528 0.1889  32  ARG B NH2 
2849 N N   . ARG B 9   ? 0.5191 1.0381 0.5335 -0.3399 -0.1552 0.1258  33  ARG B N   
2850 C CA  . ARG B 9   ? 0.5337 1.0594 0.5621 -0.3585 -0.1540 0.1345  33  ARG B CA  
2851 C C   . ARG B 9   ? 0.5600 1.0377 0.5836 -0.3550 -0.1405 0.1201  33  ARG B C   
2852 O O   . ARG B 9   ? 0.5141 1.0132 0.5647 -0.3522 -0.1318 0.1333  33  ARG B O   
2853 C CB  . ARG B 9   ? 0.6071 1.1104 0.6038 -0.3988 -0.1701 0.1300  33  ARG B CB  
2854 N N   . ALA B 10  ? 0.5448 0.9573 0.5329 -0.3545 -0.1377 0.0937  34  ALA B N   
2855 C CA  . ALA B 10  ? 0.5222 0.8845 0.5041 -0.3514 -0.1252 0.0803  34  ALA B CA  
2856 C C   . ALA B 10  ? 0.5260 0.9110 0.5406 -0.3083 -0.1049 0.0911  34  ALA B C   
2857 O O   . ALA B 10  ? 0.4958 0.8661 0.5198 -0.3030 -0.0930 0.0940  34  ALA B O   
2858 C CB  . ALA B 10  ? 0.5436 0.8228 0.4766 -0.3470 -0.1210 0.0498  34  ALA B CB  
2859 N N   . ILE B 11  ? 0.5286 0.9457 0.5571 -0.2781 -0.1010 0.0970  35  ILE B N   
2860 C CA  . ILE B 11  ? 0.4681 0.9055 0.5245 -0.2382 -0.0824 0.1066  35  ILE B CA  
2861 C C   . ILE B 11  ? 0.4711 0.9739 0.5687 -0.2417 -0.0794 0.1313  35  ILE B C   
2862 O O   . ILE B 11  ? 0.4572 0.9525 0.5643 -0.2299 -0.0641 0.1337  35  ILE B O   
2863 C CB  . ILE B 11  ? 0.4705 0.9272 0.5321 -0.2084 -0.0810 0.1099  35  ILE B CB  
2864 C CG1 . ILE B 11  ? 0.4518 0.8447 0.4734 -0.2029 -0.0800 0.0862  35  ILE B CG1 
2865 C CG2 . ILE B 11  ? 0.4330 0.9110 0.5225 -0.1694 -0.0627 0.1204  35  ILE B CG2 
2866 C CD1 . ILE B 11  ? 0.4255 0.8359 0.4466 -0.1822 -0.0824 0.0910  35  ILE B CD1 
2867 N N   . THR B 12  ? 0.4318 1.0037 0.5547 -0.2581 -0.0938 0.1511  36  THR B N   
2868 C CA  . THR B 12  ? 0.4435 1.0691 0.5991 -0.2570 -0.0884 0.1741  36  THR B CA  
2869 C C   . THR B 12  ? 0.4679 1.0642 0.6131 -0.2830 -0.0860 0.1714  36  THR B C   
2870 O O   . THR B 12  ? 0.4826 1.1013 0.6489 -0.2715 -0.0715 0.1831  36  THR B O   
2871 C CB  . THR B 12  ? 0.4348 1.1067 0.5993 -0.2687 -0.1040 0.1910  36  THR B CB  
2872 O OG1 . THR B 12  ? 0.4400 1.1314 0.6097 -0.2453 -0.1073 0.1943  36  THR B OG1 
2873 C CG2 . THR B 12  ? 0.4577 1.1897 0.6582 -0.2615 -0.0968 0.2159  36  THR B CG2 
2874 N N   . ALA B 13  ? 0.4755 1.0171 0.5849 -0.3168 -0.0992 0.1556  37  ALA B N   
2875 C CA  . ALA B 13  ? 0.4957 1.0023 0.5922 -0.3422 -0.0987 0.1542  37  ALA B CA  
2876 C C   . ALA B 13  ? 0.5151 0.9899 0.6125 -0.3268 -0.0806 0.1484  37  ALA B C   
2877 O O   . ALA B 13  ? 0.4963 0.9693 0.5991 -0.3345 -0.0739 0.1579  37  ALA B O   
2878 C CB  . ALA B 13  ? 0.5619 1.0044 0.6146 -0.3763 -0.1147 0.1354  37  ALA B CB  
2879 N N   . ALA B 14  ? 0.5486 0.9890 0.6335 -0.2991 -0.0717 0.1323  38  ALA B N   
2880 C CA  . ALA B 14  ? 0.5227 0.9179 0.5974 -0.2747 -0.0539 0.1245  38  ALA B CA  
2881 C C   . ALA B 14  ? 0.5371 0.9837 0.6426 -0.2451 -0.0363 0.1407  38  ALA B C   
2882 O O   . ALA B 14  ? 0.4896 0.9179 0.5917 -0.2375 -0.0236 0.1426  38  ALA B O   
2883 C CB  . ALA B 14  ? 0.5007 0.8347 0.5465 -0.2505 -0.0502 0.1006  38  ALA B CB  
2884 N N   . TYR B 15  ? 0.5223 1.0296 0.6549 -0.2266 -0.0349 0.1519  39  TYR B N   
2885 C CA  . TYR B 15  ? 0.4978 1.0560 0.6595 -0.1963 -0.0166 0.1668  39  TYR B CA  
2886 C C   . TYR B 15  ? 0.5487 1.1363 0.7256 -0.2125 -0.0080 0.1833  39  TYR B C   
2887 O O   . TYR B 15  ? 0.5457 1.1277 0.7208 -0.1912 0.0106  0.1842  39  TYR B O   
2888 C CB  . TYR B 15  ? 0.4583 1.0883 0.6534 -0.1846 -0.0210 0.1828  39  TYR B CB  
2889 C CG  . TYR B 15  ? 0.4413 1.0996 0.6555 -0.1387 -0.0018 0.1888  39  TYR B CG  
2890 C CD1 . TYR B 15  ? 0.4515 1.0657 0.6468 -0.1108 0.0169  0.1761  39  TYR B CD1 
2891 C CD2 . TYR B 15  ? 0.4958 1.2100 0.7379 -0.1208 -0.0038 0.2048  39  TYR B CD2 
2892 C CE1 . TYR B 15  ? 0.4131 1.0457 0.6204 -0.0698 0.0346  0.1793  39  TYR B CE1 
2893 C CE2 . TYR B 15  ? 0.4703 1.2017 0.7268 -0.0771 0.0142  0.2093  39  TYR B CE2 
2894 C CZ  . TYR B 15  ? 0.4326 1.1297 0.6751 -0.0530 0.0347  0.1970  39  TYR B CZ  
2895 O OH  . TYR B 15  ? 0.4650 1.1706 0.7159 -0.0099 0.0525  0.1991  39  TYR B OH  
2896 N N   . ARG B 16  ? 0.7019 1.3007 0.8801 -0.2449 -0.0230 0.1918  40  ARG B N   
2897 C CA  . ARG B 16  ? 0.7155 1.3329 0.9014 -0.2570 -0.0180 0.2064  40  ARG B CA  
2898 C C   . ARG B 16  ? 0.7476 1.3042 0.9057 -0.2857 -0.0217 0.1998  40  ARG B C   
2899 O O   . ARG B 16  ? 0.7428 1.3092 0.9041 -0.2998 -0.0194 0.2123  40  ARG B O   
2900 C CB  . ARG B 16  ? 0.6952 1.3643 0.9000 -0.2751 -0.0318 0.2229  40  ARG B CB  
2901 N N   . ARG B 17  ? 0.6127 1.1060 0.7438 -0.2937 -0.0271 0.1815  41  ARG B N   
2902 C CA  . ARG B 17  ? 0.5794 1.0071 0.6823 -0.3210 -0.0332 0.1756  41  ARG B CA  
2903 C C   . ARG B 17  ? 0.5867 1.0014 0.6861 -0.3083 -0.0159 0.1826  41  ARG B C   
2904 O O   . ARG B 17  ? 0.5491 0.9649 0.6485 -0.2752 -0.0011 0.1777  41  ARG B O   
2905 C CB  . ARG B 17  ? 0.6127 0.9692 0.6844 -0.3263 -0.0423 0.1519  41  ARG B CB  
2906 C CG  . ARG B 17  ? 0.6224 0.9037 0.6639 -0.3519 -0.0485 0.1453  41  ARG B CG  
2907 C CD  . ARG B 17  ? 0.6554 0.8675 0.6633 -0.3590 -0.0603 0.1200  41  ARG B CD  
2908 N NE  . ARG B 17  ? 0.6179 0.8580 0.6268 -0.3822 -0.0762 0.1180  41  ARG B NE  
2909 C CZ  . ARG B 17  ? 0.5882 0.8284 0.5884 -0.3733 -0.0818 0.1030  41  ARG B CZ  
2910 N NH1 . ARG B 17  ? 0.5430 0.7497 0.5304 -0.3371 -0.0717 0.0861  41  ARG B NH1 
2911 N NH2 . ARG B 17  ? 0.5687 0.8373 0.5673 -0.3916 -0.0967 0.1044  41  ARG B NH2 
2912 N N   . PRO B 18  ? 0.5811 0.9778 0.6721 -0.3297 -0.0182 0.1924  42  PRO B N   
2913 C CA  . PRO B 18  ? 0.5890 0.9664 0.6703 -0.3195 -0.0038 0.1992  42  PRO B CA  
2914 C C   . PRO B 18  ? 0.6113 0.9214 0.6661 -0.3060 -0.0014 0.1835  42  PRO B C   
2915 O O   . PRO B 18  ? 0.6291 0.8841 0.6652 -0.3123 -0.0138 0.1659  42  PRO B O   
2916 C CB  . PRO B 18  ? 0.6094 0.9659 0.6819 -0.3510 -0.0127 0.2104  42  PRO B CB  
2917 C CG  . PRO B 18  ? 0.6285 1.0316 0.7197 -0.3697 -0.0249 0.2167  42  PRO B CG  
2918 C CD  . PRO B 18  ? 0.6257 1.0274 0.7170 -0.3632 -0.0335 0.2006  42  PRO B CD  
2919 N N   . GLU B 19  ? 0.6007 0.9086 0.6491 -0.2776 0.0137  0.1844  43  GLU B N   
2920 C CA  . GLU B 19  ? 0.6197 0.8654 0.6432 -0.2515 0.0143  0.1656  43  GLU B CA  
2921 C C   . GLU B 19  ? 0.6344 0.8054 0.6340 -0.2698 0.0029  0.1612  43  GLU B C   
2922 O O   . GLU B 19  ? 0.6361 0.7558 0.6209 -0.2579 -0.0031 0.1420  43  GLU B O   
2923 C CB  . GLU B 19  ? 0.5744 0.8329 0.5921 -0.2250 0.0304  0.1704  43  GLU B CB  
2924 C CG  . GLU B 19  ? 0.5827 0.7877 0.5782 -0.1983 0.0302  0.1531  43  GLU B CG  
2925 C CD  . GLU B 19  ? 0.5387 0.7624 0.5264 -0.1724 0.0450  0.1548  43  GLU B CD  
2926 O OE1 . GLU B 19  ? 0.5072 0.7851 0.5065 -0.1713 0.0578  0.1672  43  GLU B OE1 
2927 O OE2 . GLU B 19  ? 0.5330 0.7185 0.5025 -0.1537 0.0439  0.1437  43  GLU B OE2 
2928 N N   . THR B 20  ? 0.6758 0.8388 0.6715 -0.2980 0.0006  0.1797  44  THR B N   
2929 C CA  . THR B 20  ? 0.7368 0.8226 0.7090 -0.3134 -0.0098 0.1770  44  THR B CA  
2930 C C   . THR B 20  ? 0.7380 0.7862 0.7023 -0.3297 -0.0234 0.1594  44  THR B C   
2931 O O   . THR B 20  ? 0.7417 0.7186 0.6846 -0.3252 -0.0289 0.1456  44  THR B O   
2932 C CB  . THR B 20  ? 0.7301 0.8143 0.6991 -0.3436 -0.0104 0.2024  44  THR B CB  
2933 O OG1 . THR B 20  ? 0.7840 0.9112 0.7699 -0.3653 -0.0161 0.2074  44  THR B OG1 
2934 C CG2 . THR B 20  ? 0.6923 0.8130 0.6633 -0.3260 0.0043  0.2181  44  THR B CG2 
2935 N N   . GLU B 21  ? 0.6870 0.7838 0.6677 -0.3468 -0.0286 0.1593  45  GLU B N   
2936 C CA  . GLU B 21  ? 0.7240 0.7883 0.6922 -0.3654 -0.0425 0.1420  45  GLU B CA  
2937 C C   . GLU B 21  ? 0.7057 0.7496 0.6652 -0.3333 -0.0407 0.1167  45  GLU B C   
2938 O O   . GLU B 21  ? 0.7412 0.7313 0.6783 -0.3404 -0.0487 0.0978  45  GLU B O   
2939 C CB  . GLU B 21  ? 0.7041 0.8313 0.6916 -0.3887 -0.0508 0.1502  45  GLU B CB  
2940 C CG  . GLU B 21  ? 0.7415 0.8718 0.7288 -0.4152 -0.0575 0.1654  45  GLU B CG  
2941 C CD  . GLU B 21  ? 0.7785 0.9621 0.7799 -0.4349 -0.0690 0.1698  45  GLU B CD  
2942 O OE1 . GLU B 21  ? 0.7598 0.9910 0.7770 -0.4230 -0.0695 0.1656  45  GLU B OE1 
2943 O OE2 . GLU B 21  ? 0.8720 1.0499 0.8683 -0.4623 -0.0782 0.1788  45  GLU B OE2 
2944 N N   . CYS B 22  ? 0.6809 0.7655 0.6556 -0.2993 -0.0297 0.1157  46  CYS B N   
2945 C CA  . CYS B 22  ? 0.6557 0.7244 0.6236 -0.2707 -0.0277 0.0944  46  CYS B CA  
2946 C C   . CYS B 22  ? 0.6719 0.6714 0.6190 -0.2519 -0.0248 0.0812  46  CYS B C   
2947 O O   . CYS B 22  ? 0.6701 0.6442 0.6072 -0.2362 -0.0249 0.0621  46  CYS B O   
2948 C CB  . CYS B 22  ? 0.6250 0.7503 0.6131 -0.2407 -0.0169 0.0981  46  CYS B CB  
2949 S SG  . CYS B 22  ? 0.5581 0.7754 0.5786 -0.2502 -0.0162 0.1161  46  CYS B SG  
2950 N N   . LEU B 23  ? 0.7277 0.7003 0.6696 -0.2524 -0.0220 0.0928  47  LEU B N   
2951 C CA  . LEU B 23  ? 0.7175 0.6419 0.6482 -0.2271 -0.0181 0.0857  47  LEU B CA  
2952 C C   . LEU B 23  ? 0.7420 0.5935 0.6522 -0.2306 -0.0233 0.0708  47  LEU B C   
2953 O O   . LEU B 23  ? 0.7712 0.5978 0.6774 -0.2048 -0.0194 0.0564  47  LEU B O   
2954 C CB  . LEU B 23  ? 0.7247 0.6503 0.6563 -0.2251 -0.0141 0.1061  47  LEU B CB  
2955 C CG  . LEU B 23  ? 0.6981 0.6484 0.6351 -0.1944 -0.0056 0.1074  47  LEU B CG  
2956 C CD1 . LEU B 23  ? 0.7051 0.6158 0.6359 -0.1689 -0.0062 0.0921  47  LEU B CD1 
2957 C CD2 . LEU B 23  ? 0.6447 0.6571 0.5966 -0.1859 0.0009  0.1050  47  LEU B CD2 
2958 N N   . PRO B 24  ? 0.7771 0.5907 0.6735 -0.2605 -0.0310 0.0738  48  PRO B N   
2959 C CA  . PRO B 24  ? 0.8385 0.5723 0.7116 -0.2594 -0.0335 0.0590  48  PRO B CA  
2960 C C   . PRO B 24  ? 0.8533 0.5736 0.7169 -0.2443 -0.0310 0.0323  48  PRO B C   
2961 O O   . PRO B 24  ? 0.8454 0.5224 0.7015 -0.2193 -0.0251 0.0204  48  PRO B O   
2962 C CB  . PRO B 24  ? 0.9070 0.6112 0.7652 -0.3014 -0.0436 0.0657  48  PRO B CB  
2963 C CG  . PRO B 24  ? 0.8733 0.6317 0.7504 -0.3169 -0.0438 0.0933  48  PRO B CG  
2964 C CD  . PRO B 24  ? 0.8135 0.6498 0.7141 -0.2963 -0.0368 0.0934  48  PRO B CD  
2965 N N   . PRO B 25  ? 0.8354 0.5942 0.6996 -0.2575 -0.0348 0.0236  49  PRO B N   
2966 C CA  . PRO B 25  ? 0.8109 0.5571 0.6628 -0.2423 -0.0315 -0.0006 49  PRO B CA  
2967 C C   . PRO B 25  ? 0.7919 0.5590 0.6593 -0.2036 -0.0210 -0.0037 49  PRO B C   
2968 O O   . PRO B 25  ? 0.8074 0.5419 0.6645 -0.1841 -0.0145 -0.0206 49  PRO B O   
2969 C CB  . PRO B 25  ? 0.8403 0.6352 0.6932 -0.2658 -0.0399 -0.0023 49  PRO B CB  
2970 C CG  . PRO B 25  ? 0.8102 0.6628 0.6884 -0.2793 -0.0432 0.0225  49  PRO B CG  
2971 C CD  . PRO B 25  ? 0.8347 0.6488 0.7098 -0.2875 -0.0428 0.0358  49  PRO B CD  
2972 N N   . LEU B 26  ? 0.7502 0.5707 0.6413 -0.1926 -0.0184 0.0122  50  LEU B N   
2973 C CA  . LEU B 26  ? 0.7130 0.5492 0.6165 -0.1597 -0.0103 0.0102  50  LEU B CA  
2974 C C   . LEU B 26  ? 0.7333 0.5223 0.6339 -0.1416 -0.0065 0.0102  50  LEU B C   
2975 O O   . LEU B 26  ? 0.7314 0.5110 0.6345 -0.1179 -0.0006 -0.0001 50  LEU B O   
2976 C CB  . LEU B 26  ? 0.6374 0.5297 0.5603 -0.1538 -0.0084 0.0266  50  LEU B CB  
2977 C CG  . LEU B 26  ? 0.6308 0.5779 0.5634 -0.1639 -0.0103 0.0296  50  LEU B CG  
2978 C CD1 . LEU B 26  ? 0.5557 0.5503 0.5051 -0.1579 -0.0057 0.0469  50  LEU B CD1 
2979 C CD2 . LEU B 26  ? 0.5959 0.5540 0.5276 -0.1489 -0.0082 0.0151  50  LEU B CD2 
2980 N N   . VAL B 27  ? 0.7693 0.5308 0.6663 -0.1526 -0.0101 0.0240  51  VAL B N   
2981 C CA  . VAL B 27  ? 0.7509 0.4675 0.6468 -0.1347 -0.0081 0.0280  51  VAL B CA  
2982 C C   . VAL B 27  ? 0.8044 0.4672 0.6861 -0.1254 -0.0039 0.0078  51  VAL B C   
2983 O O   . VAL B 27  ? 0.8148 0.4619 0.7039 -0.0979 0.0021  0.0039  51  VAL B O   
2984 C CB  . VAL B 27  ? 0.7877 0.4817 0.6792 -0.1520 -0.0138 0.0487  51  VAL B CB  
2985 N N   . GLU B 28  ? 0.7877 0.4236 0.6483 -0.1484 -0.0067 -0.0054 52  GLU B N   
2986 C CA  . GLU B 28  ? 0.8919 0.4706 0.7314 -0.1408 -0.0010 -0.0276 52  GLU B CA  
2987 C C   . GLU B 28  ? 0.8686 0.4721 0.7138 -0.1165 0.0086  -0.0439 52  GLU B C   
2988 O O   . GLU B 28  ? 0.9008 0.4717 0.7438 -0.0920 0.0185  -0.0550 52  GLU B O   
2989 C CB  . GLU B 28  ? 0.9736 0.5211 0.7838 -0.1757 -0.0079 -0.0394 52  GLU B CB  
2990 N N   . ALA B 29  ? 0.8159 0.4779 0.6695 -0.1220 0.0066  -0.0442 53  ALA B N   
2991 C CA  . ALA B 29  ? 0.8243 0.5105 0.6826 -0.1015 0.0152  -0.0569 53  ALA B CA  
2992 C C   . ALA B 29  ? 0.7969 0.5042 0.6817 -0.0721 0.0208  -0.0468 53  ALA B C   
2993 O O   . ALA B 29  ? 0.8189 0.5291 0.7086 -0.0511 0.0301  -0.0566 53  ALA B O   
2994 C CB  . ALA B 29  ? 0.7580 0.4972 0.6173 -0.1155 0.0103  -0.0574 53  ALA B CB  
2995 N N   . ALA B 30  ? 0.7756 0.5003 0.6765 -0.0718 0.0150  -0.0267 54  ALA B N   
2996 C CA  . ALA B 30  ? 0.7388 0.4884 0.6622 -0.0488 0.0170  -0.0161 54  ALA B CA  
2997 C C   . ALA B 30  ? 0.8389 0.5519 0.7698 -0.0290 0.0199  -0.0112 54  ALA B C   
2998 O O   . ALA B 30  ? 0.8360 0.5701 0.7865 -0.0087 0.0214  -0.0043 54  ALA B O   
2999 C CB  . ALA B 30  ? 0.6664 0.4527 0.5990 -0.0570 0.0100  0.0022  54  ALA B CB  
3000 N N   . THR B 31  ? 0.8778 0.5365 0.7939 -0.0348 0.0198  -0.0133 55  THR B N   
3001 C CA  . THR B 31  ? 0.9206 0.5397 0.8443 -0.0126 0.0234  -0.0079 55  THR B CA  
3002 C C   . THR B 31  ? 0.8923 0.5047 0.8210 0.0123  0.0368  -0.0253 55  THR B C   
3003 O O   . THR B 31  ? 0.8997 0.4912 0.8072 0.0064  0.0443  -0.0467 55  THR B O   
3004 C CB  . THR B 31  ? 0.9284 0.4832 0.8312 -0.0264 0.0202  -0.0062 55  THR B CB  
3005 N N   . GLN B 32  ? 0.9120 0.5455 0.8681 0.0389  0.0397  -0.0154 56  GLN B N   
3006 C CA  . GLN B 32  ? 0.9036 0.5391 0.8711 0.0651  0.0541  -0.0278 56  GLN B CA  
3007 C C   . GLN B 32  ? 0.9173 0.5123 0.8972 0.0917  0.0593  -0.0203 56  GLN B C   
3008 O O   . GLN B 32  ? 0.9317 0.4988 0.9118 0.0894  0.0499  -0.0033 56  GLN B O   
3009 C CB  . GLN B 32  ? 0.8278 0.5285 0.8218 0.0743  0.0539  -0.0215 56  GLN B CB  
3010 N N   . SER B 33  ? 0.9348 0.5284 0.9257 0.1183  0.0755  -0.0319 57  SER B N   
3011 C CA  . SER B 33  ? 0.9282 0.4859 0.9346 0.1501  0.0840  -0.0259 57  SER B CA  
3012 C C   . SER B 33  ? 0.9105 0.5000 0.9533 0.1634  0.0710  0.0055  57  SER B C   
3013 O O   . SER B 33  ? 0.8776 0.5230 0.9352 0.1519  0.0589  0.0186  57  SER B O   
3014 C CB  . SER B 33  ? 0.9126 0.4800 0.9294 0.1780  0.1060  -0.0428 57  SER B CB  
3015 N N   . LYS B 34  ? 0.9485 0.4988 1.0034 0.1882  0.0731  0.0177  58  LYS B N   
3016 C CA  . LYS B 34  ? 0.9589 0.5403 1.0490 0.2028  0.0597  0.0497  58  LYS B CA  
3017 C C   . LYS B 34  ? 0.9160 0.5658 1.0484 0.2257  0.0646  0.0564  58  LYS B C   
3018 O O   . LYS B 34  ? 0.8670 0.5680 1.0246 0.2237  0.0490  0.0796  58  LYS B O   
3019 C CB  . LYS B 34  ? 1.0224 0.5417 1.1151 0.2249  0.0600  0.0636  58  LYS B CB  
3020 N N   . GLU B 35  ? 0.9234 0.5760 1.0627 0.2460  0.0861  0.0369  59  GLU B N   
3021 C CA  . GLU B 35  ? 0.8612 0.5847 1.0417 0.2638  0.0919  0.0435  59  GLU B CA  
3022 C C   . GLU B 35  ? 0.8154 0.5955 0.9920 0.2343  0.0824  0.0406  59  GLU B C   
3023 O O   . GLU B 35  ? 0.7990 0.6412 1.0087 0.2367  0.0742  0.0571  59  GLU B O   
3024 C CB  . GLU B 35  ? 0.8712 0.5836 1.0567 0.2921  0.1202  0.0229  59  GLU B CB  
3025 N N   . ILE B 36  ? 0.7869 0.5455 0.9235 0.2060  0.0824  0.0209  60  ILE B N   
3026 C CA  . ILE B 36  ? 0.7635 0.5683 0.8939 0.1796  0.0736  0.0185  60  ILE B CA  
3027 C C   . ILE B 36  ? 0.7286 0.5514 0.8611 0.1621  0.0507  0.0398  60  ILE B C   
3028 O O   . ILE B 36  ? 0.6569 0.5304 0.8043 0.1538  0.0411  0.0493  60  ILE B O   
3029 C CB  . ILE B 36  ? 0.7689 0.5475 0.8582 0.1574  0.0804  -0.0068 60  ILE B CB  
3030 C CG1 . ILE B 36  ? 0.7676 0.5488 0.8539 0.1709  0.1026  -0.0277 60  ILE B CG1 
3031 C CG2 . ILE B 36  ? 0.6748 0.4877 0.7535 0.1290  0.0672  -0.0047 60  ILE B CG2 
3032 C CD1 . ILE B 36  ? 0.7642 0.5380 0.8135 0.1467  0.1063  -0.0491 60  ILE B CD1 
3033 N N   . ARG B 37  ? 0.7369 0.5168 0.8515 0.1547  0.0418  0.0474  61  ARG B N   
3034 C CA  . ARG B 37  ? 0.7381 0.5348 0.8512 0.1389  0.0219  0.0681  61  ARG B CA  
3035 C C   . ARG B 37  ? 0.6686 0.5077 0.8178 0.1549  0.0116  0.0917  61  ARG B C   
3036 O O   . ARG B 37  ? 0.5902 0.4679 0.7413 0.1405  -0.0026 0.1027  61  ARG B O   
3037 C CB  . ARG B 37  ? 0.8044 0.5476 0.8948 0.1302  0.0158  0.0756  61  ARG B CB  
3038 C CG  . ARG B 37  ? 0.8495 0.5678 0.9039 0.1026  0.0179  0.0587  61  ARG B CG  
3039 C CD  . ARG B 37  ? 0.8573 0.5304 0.8914 0.0889  0.0098  0.0703  61  ARG B CD  
3040 N NE  . ARG B 37  ? 0.8898 0.5031 0.9221 0.1059  0.0168  0.0696  61  ARG B NE  
3041 C CZ  . ARG B 37  ? 0.9271 0.5202 0.9739 0.1235  0.0107  0.0920  61  ARG B CZ  
3042 N NH1 . ARG B 37  ? 0.9265 0.5567 0.9890 0.1241  -0.0039 0.1175  61  ARG B NH1 
3043 N NH2 . ARG B 37  ? 0.9310 0.4625 0.9739 0.1410  0.0191  0.0889  61  ARG B NH2 
3044 N N   . ASP B 38  ? 0.6794 0.5126 0.8569 0.1848  0.0189  0.0996  62  ASP B N   
3045 C CA  . ASP B 38  ? 0.6631 0.5428 0.8803 0.2009  0.0078  0.1251  62  ASP B CA  
3046 C C   . ASP B 38  ? 0.6057 0.5492 0.8440 0.1961  0.0083  0.1217  62  ASP B C   
3047 O O   . ASP B 38  ? 0.5534 0.5424 0.8079 0.1880  -0.0090 0.1399  62  ASP B O   
3048 C CB  . ASP B 38  ? 0.6932 0.5534 0.9398 0.2382  0.0178  0.1348  62  ASP B CB  
3049 N N   . ALA B 39  ? 0.5817 0.5278 0.8175 0.1989  0.0275  0.0989  63  ALA B N   
3050 C CA  . ALA B 39  ? 0.5073 0.5104 0.7605 0.1912  0.0287  0.0962  63  ALA B CA  
3051 C C   . ALA B 39  ? 0.5235 0.5382 0.7493 0.1581  0.0143  0.0927  63  ALA B C   
3052 O O   . ALA B 39  ? 0.4897 0.5495 0.7297 0.1472  0.0020  0.1034  63  ALA B O   
3053 C CB  . ALA B 39  ? 0.5799 0.5794 0.8317 0.2013  0.0537  0.0734  63  ALA B CB  
3054 N N   . ALA B 40  ? 0.5388 0.5127 0.7252 0.1417  0.0156  0.0783  64  ALA B N   
3055 C CA  . ALA B 40  ? 0.5329 0.5149 0.6933 0.1145  0.0040  0.0756  64  ALA B CA  
3056 C C   . ALA B 40  ? 0.4954 0.4939 0.6582 0.1066  -0.0169 0.0970  64  ALA B C   
3057 O O   . ALA B 40  ? 0.4476 0.4725 0.6033 0.0899  -0.0273 0.0988  64  ALA B O   
3058 C CB  . ALA B 40  ? 0.4952 0.4348 0.6187 0.1009  0.0090  0.0604  64  ALA B CB  
3059 N N   . ALA B 41  ? 0.5174 0.4971 0.6862 0.1176  -0.0237 0.1135  65  ALA B N   
3060 C CA  . ALA B 41  ? 0.4899 0.4857 0.6563 0.1087  -0.0445 0.1351  65  ALA B CA  
3061 C C   . ALA B 41  ? 0.5097 0.5584 0.7085 0.1126  -0.0555 0.1494  65  ALA B C   
3062 O O   . ALA B 41  ? 0.4739 0.5463 0.6624 0.0950  -0.0726 0.1582  65  ALA B O   
3063 C CB  . ALA B 41  ? 0.5196 0.4825 0.6853 0.1198  -0.0497 0.1525  65  ALA B CB  
3064 N N   . SER B 42  ? 0.4728 0.5414 0.7101 0.1349  -0.0455 0.1518  66  SER B N   
3065 C CA  . SER B 42  ? 0.4181 0.5450 0.6925 0.1375  -0.0547 0.1663  66  SER B CA  
3066 C C   . SER B 42  ? 0.4062 0.5579 0.6682 0.1132  -0.0563 0.1531  66  SER B C   
3067 O O   . SER B 42  ? 0.4276 0.6133 0.6929 0.0965  -0.0746 0.1644  66  SER B O   
3068 C CB  . SER B 42  ? 0.4289 0.5729 0.7477 0.1685  -0.0383 0.1696  66  SER B CB  
3069 O OG  . SER B 42  ? 0.5750 0.6898 0.9044 0.1932  -0.0372 0.1829  66  SER B OG  
3070 N N   . THR B 43  ? 0.3858 0.5182 0.6311 0.1099  -0.0380 0.1294  67  THR B N   
3071 C CA  . THR B 43  ? 0.4129 0.5617 0.6442 0.0881  -0.0385 0.1174  67  THR B CA  
3072 C C   . THR B 43  ? 0.3996 0.5342 0.5927 0.0638  -0.0544 0.1162  67  THR B C   
3073 O O   . THR B 43  ? 0.4099 0.5674 0.5987 0.0456  -0.0667 0.1189  67  THR B O   
3074 C CB  . THR B 43  ? 0.3856 0.5126 0.6030 0.0906  -0.0167 0.0945  67  THR B CB  
3075 O OG1 . THR B 43  ? 0.4096 0.5544 0.6603 0.1125  -0.0003 0.0945  67  THR B OG1 
3076 C CG2 . THR B 43  ? 0.3823 0.5180 0.5802 0.0682  -0.0178 0.0835  67  THR B CG2 
3077 N N   . ALA B 44  ? 0.4021 0.4980 0.5655 0.0625  -0.0537 0.1119  68  ALA B N   
3078 C CA  . ALA B 44  ? 0.4224 0.5058 0.5482 0.0422  -0.0651 0.1100  68  ALA B CA  
3079 C C   . ALA B 44  ? 0.4349 0.5413 0.5630 0.0342  -0.0872 0.1297  68  ALA B C   
3080 O O   . ALA B 44  ? 0.4257 0.5369 0.5289 0.0147  -0.0982 0.1270  68  ALA B O   
3081 C CB  . ALA B 44  ? 0.4478 0.4922 0.5464 0.0426  -0.0589 0.1049  68  ALA B CB  
3082 N N   . ARG B 45  ? 0.4377 0.5566 0.5934 0.0491  -0.0944 0.1498  69  ARG B N   
3083 C CA  . ARG B 45  ? 0.4743 0.6222 0.6357 0.0411  -0.1180 0.1715  69  ARG B CA  
3084 C C   . ARG B 45  ? 0.4730 0.6614 0.6497 0.0270  -0.1273 0.1719  69  ARG B C   
3085 O O   . ARG B 45  ? 0.4530 0.6506 0.6060 0.0047  -0.1453 0.1750  69  ARG B O   
3086 C CB  . ARG B 45  ? 0.4369 0.5958 0.6340 0.0639  -0.1231 0.1955  69  ARG B CB  
3087 C CG  . ARG B 45  ? 0.4874 0.6811 0.6929 0.0564  -0.1501 0.2222  69  ARG B CG  
3088 C CD  . ARG B 45  ? 0.5106 0.7132 0.7530 0.0825  -0.1549 0.2485  69  ARG B CD  
3089 N NE  . ARG B 45  ? 0.5568 0.7090 0.7773 0.0925  -0.1478 0.2502  69  ARG B NE  
3090 C CZ  . ARG B 45  ? 0.5782 0.7161 0.7704 0.0830  -0.1632 0.2663  69  ARG B CZ  
3091 N NH1 . ARG B 45  ? 0.5857 0.7520 0.7608 0.0624  -0.1864 0.2789  69  ARG B NH1 
3092 N NH2 . ARG B 45  ? 0.6012 0.6937 0.7789 0.0925  -0.1555 0.2701  69  ARG B NH2 
3093 N N   . LYS B 46  ? 0.4129 0.6245 0.6268 0.0383  -0.1149 0.1686  70  LYS B N   
3094 C CA  . LYS B 46  ? 0.4032 0.6558 0.6355 0.0230  -0.1227 0.1710  70  LYS B CA  
3095 C C   . LYS B 46  ? 0.4216 0.6520 0.6107 -0.0031 -0.1238 0.1516  70  LYS B C   
3096 O O   . LYS B 46  ? 0.4110 0.6586 0.5905 -0.0263 -0.1414 0.1557  70  LYS B O   
3097 C CB  . LYS B 46  ? 0.4314 0.7108 0.7083 0.0410  -0.1040 0.1697  70  LYS B CB  
3098 C CG  . LYS B 46  ? 0.4638 0.7790 0.7547 0.0221  -0.1062 0.1681  70  LYS B CG  
3099 C CD  . LYS B 46  ? 0.4279 0.7746 0.7635 0.0415  -0.0854 0.1688  70  LYS B CD  
3100 C CE  . LYS B 46  ? 0.3845 0.6893 0.7008 0.0561  -0.0588 0.1460  70  LYS B CE  
3101 N NZ  . LYS B 46  ? 0.4101 0.7441 0.7644 0.0755  -0.0366 0.1454  70  LYS B NZ  
3102 N N   . LEU B 47  ? 0.4104 0.6010 0.5723 0.0002  -0.1058 0.1309  71  LEU B N   
3103 C CA  . LEU B 47  ? 0.4404 0.6074 0.5629 -0.0198 -0.1050 0.1133  71  LEU B CA  
3104 C C   . LEU B 47  ? 0.4396 0.5896 0.5208 -0.0368 -0.1218 0.1143  71  LEU B C   
3105 O O   . LEU B 47  ? 0.4723 0.6164 0.5279 -0.0576 -0.1308 0.1074  71  LEU B O   
3106 C CB  . LEU B 47  ? 0.3684 0.5010 0.4730 -0.0106 -0.0837 0.0944  71  LEU B CB  
3107 C CG  . LEU B 47  ? 0.4149 0.5580 0.5463 0.0009  -0.0658 0.0879  71  LEU B CG  
3108 C CD1 . LEU B 47  ? 0.3708 0.4795 0.4800 0.0079  -0.0489 0.0711  71  LEU B CD1 
3109 C CD2 . LEU B 47  ? 0.3696 0.5317 0.5060 -0.0152 -0.0684 0.0860  71  LEU B CD2 
3110 N N   . ILE B 48  ? 0.4472 0.5851 0.5174 -0.0287 -0.1253 0.1224  72  ILE B N   
3111 C CA  . ILE B 48  ? 0.4909 0.6121 0.5169 -0.0437 -0.1383 0.1229  72  ILE B CA  
3112 C C   . ILE B 48  ? 0.5163 0.6675 0.5456 -0.0599 -0.1640 0.1394  72  ILE B C   
3113 O O   . ILE B 48  ? 0.5655 0.7052 0.5540 -0.0812 -0.1762 0.1333  72  ILE B O   
3114 C CB  . ILE B 48  ? 0.5359 0.6371 0.5494 -0.0319 -0.1334 0.1290  72  ILE B CB  
3115 C CG1 . ILE B 48  ? 0.5447 0.6165 0.5474 -0.0231 -0.1107 0.1113  72  ILE B CG1 
3116 C CG2 . ILE B 48  ? 0.5897 0.6814 0.5593 -0.0469 -0.1477 0.1344  72  ILE B CG2 
3117 C CD1 . ILE B 48  ? 0.5861 0.6415 0.5879 -0.0117 -0.1048 0.1191  72  ILE B CD1 
3118 N N   . GLU B 49  ? 0.5019 0.6924 0.5789 -0.0502 -0.1729 0.1603  73  GLU B N   
3119 C CA  . GLU B 49  ? 0.5224 0.7495 0.6070 -0.0675 -0.1999 0.1787  73  GLU B CA  
3120 C C   . GLU B 49  ? 0.5310 0.7704 0.6133 -0.0910 -0.2063 0.1693  73  GLU B C   
3121 O O   . GLU B 49  ? 0.5722 0.8204 0.6312 -0.1170 -0.2290 0.1736  73  GLU B O   
3122 C CB  . GLU B 49  ? 0.4732 0.7454 0.6156 -0.0485 -0.2074 0.2063  73  GLU B CB  
3123 N N   . ALA B 50  ? 0.5296 0.7677 0.6324 -0.0844 -0.1873 0.1569  74  ALA B N   
3124 C CA  . ALA B 50  ? 0.5421 0.7817 0.6361 -0.1084 -0.1914 0.1470  74  ALA B CA  
3125 C C   . ALA B 50  ? 0.6180 0.8058 0.6462 -0.1270 -0.1932 0.1260  74  ALA B C   
3126 O O   . ALA B 50  ? 0.6865 0.8703 0.6893 -0.1549 -0.2104 0.1233  74  ALA B O   
3127 C CB  . ALA B 50  ? 0.5409 0.7865 0.6661 -0.0960 -0.1687 0.1390  74  ALA B CB  
3128 N N   . LEU B 51  ? 0.5898 0.7374 0.5894 -0.1122 -0.1752 0.1109  75  LEU B N   
3129 C CA  . LEU B 51  ? 0.6593 0.7590 0.5993 -0.1241 -0.1723 0.0906  75  LEU B CA  
3130 C C   . LEU B 51  ? 0.7151 0.8084 0.6138 -0.1422 -0.1933 0.0947  75  LEU B C   
3131 O O   . LEU B 51  ? 0.8241 0.8999 0.6866 -0.1666 -0.2060 0.0858  75  LEU B O   
3132 C CB  . LEU B 51  ? 0.5962 0.6658 0.5222 -0.1030 -0.1489 0.0780  75  LEU B CB  
3133 C CG  . LEU B 51  ? 0.5798 0.6379 0.5203 -0.0918 -0.1279 0.0654  75  LEU B CG  
3134 C CD1 . LEU B 51  ? 0.5723 0.6101 0.5027 -0.0731 -0.1096 0.0581  75  LEU B CD1 
3135 C CD2 . LEU B 51  ? 0.5920 0.6218 0.5010 -0.1081 -0.1283 0.0504  75  LEU B CD2 
3136 N N   . ARG B 52  ? 0.7192 0.8230 0.6189 -0.1316 -0.1975 0.1082  76  ARG B N   
3137 C CA  . ARG B 52  ? 0.7401 0.8400 0.5975 -0.1485 -0.2175 0.1142  76  ARG B CA  
3138 C C   . ARG B 52  ? 0.8142 0.9450 0.6784 -0.1746 -0.2465 0.1268  76  ARG B C   
3139 O O   . ARG B 52  ? 0.8895 1.0097 0.7062 -0.1968 -0.2650 0.1256  76  ARG B O   
3140 C CB  . ARG B 52  ? 0.7282 0.8407 0.5949 -0.1323 -0.2187 0.1330  76  ARG B CB  
3141 C CG  . ARG B 52  ? 0.6676 0.7460 0.5084 -0.1164 -0.1956 0.1214  76  ARG B CG  
3142 C CD  . ARG B 52  ? 0.7091 0.7970 0.5538 -0.1061 -0.2001 0.1426  76  ARG B CD  
3143 N NE  . ARG B 52  ? 0.6921 0.7492 0.4978 -0.1010 -0.1830 0.1328  76  ARG B NE  
3144 C CZ  . ARG B 52  ? 0.7394 0.7960 0.5394 -0.0940 -0.1825 0.1487  76  ARG B CZ  
3145 N NH1 . ARG B 52  ? 0.6902 0.7700 0.5217 -0.0878 -0.1974 0.1754  76  ARG B NH1 
3146 N NH2 . ARG B 52  ? 0.7033 0.7362 0.4660 -0.0931 -0.1664 0.1394  76  ARG B NH2 
3147 N N   . GLY B 53  ? 0.7925 0.9629 0.7129 -0.1741 -0.2506 0.1387  77  GLY B N   
3148 C CA  . GLY B 53  ? 0.7769 0.9889 0.7149 -0.1989 -0.2792 0.1557  77  GLY B CA  
3149 C C   . GLY B 53  ? 0.8584 1.0553 0.7766 -0.2285 -0.2857 0.1412  77  GLY B C   
3150 O O   . GLY B 53  ? 0.8748 1.0876 0.7935 -0.2496 -0.3005 0.1487  77  GLY B O   
3151 N N   . LYS B 54  ? 0.8828 1.0389 0.7848 -0.2245 -0.2645 0.1185  78  LYS B N   
3152 C CA  . LYS B 54  ? 0.9363 1.0757 0.8251 -0.2510 -0.2695 0.1072  78  LYS B CA  
3153 C C   . LYS B 54  ? 1.0605 1.1278 0.8746 -0.2640 -0.2645 0.0788  78  LYS B C   
3154 O O   . LYS B 54  ? 1.1259 1.1701 0.9167 -0.2898 -0.2725 0.0706  78  LYS B O   
3155 C CB  . LYS B 54  ? 0.9027 1.0568 0.8408 -0.2364 -0.2488 0.1074  78  LYS B CB  
3156 N N   . HIS B 55  ? 1.1339 1.1630 0.9137 -0.2424 -0.2456 0.0641  79  HIS B N   
3157 C CA  . HIS B 55  ? 1.1864 1.1482 0.8982 -0.2487 -0.2365 0.0370  79  HIS B CA  
3158 C C   . HIS B 55  ? 1.2275 1.1679 0.8983 -0.2328 -0.2267 0.0295  79  HIS B C   
3159 O O   . HIS B 55  ? 1.2207 1.1919 0.8969 -0.2320 -0.2387 0.0456  79  HIS B O   
3160 C CB  . HIS B 55  ? 1.2373 1.1695 0.9582 -0.2344 -0.2123 0.0228  79  HIS B CB  
3161 N N   . GLY B 66  ? 1.5488 0.9169 0.8540 0.0328  0.0634  -0.1934 192 GLY B N   
3162 C CA  . GLY B 66  ? 1.4713 0.8685 0.8065 0.0109  0.0430  -0.1793 192 GLY B CA  
3163 C C   . GLY B 66  ? 1.4523 0.8292 0.8128 0.0121  0.0382  -0.1718 192 GLY B C   
3164 O O   . GLY B 66  ? 1.4331 0.8412 0.8309 0.0269  0.0441  -0.1601 192 GLY B O   
3165 N N   . GLU B 67  ? 1.4827 0.8078 0.8219 -0.0053 0.0269  -0.1774 193 GLU B N   
3166 C CA  . GLU B 67  ? 1.4366 0.7359 0.7949 -0.0064 0.0223  -0.1694 193 GLU B CA  
3167 C C   . GLU B 67  ? 1.3625 0.6943 0.7541 -0.0316 0.0024  -0.1549 193 GLU B C   
3168 O O   . GLU B 67  ? 1.3233 0.6404 0.7344 -0.0339 -0.0014 -0.1456 193 GLU B O   
3169 C CB  . GLU B 67  ? 1.4620 0.6970 0.7850 -0.0217 0.0151  -0.1787 193 GLU B CB  
3170 N N   . GLN B 68  ? 1.3095 0.6866 0.7093 -0.0502 -0.0104 -0.1511 194 GLN B N   
3171 C CA  . GLN B 68  ? 1.2031 0.6355 0.6558 -0.0721 -0.0286 -0.1305 194 GLN B CA  
3172 C C   . GLN B 68  ? 1.1251 0.6108 0.6383 -0.0492 -0.0172 -0.1127 194 GLN B C   
3173 O O   . GLN B 68  ? 1.0443 0.5690 0.6002 -0.0633 -0.0284 -0.0968 194 GLN B O   
3174 C CB  . GLN B 68  ? 1.1738 0.6511 0.6300 -0.0930 -0.0443 -0.1264 194 GLN B CB  
3175 C CG  . GLN B 68  ? 1.1607 0.6879 0.6350 -0.0708 -0.0310 -0.1218 194 GLN B CG  
3176 C CD  . GLN B 68  ? 1.2415 0.7377 0.6590 -0.0605 -0.0192 -0.1401 194 GLN B CD  
3177 O OE1 . GLN B 68  ? 1.3284 0.7649 0.6985 -0.0608 -0.0148 -0.1571 194 GLN B OE1 
3178 N NE2 . GLN B 68  ? 1.2215 0.7629 0.6490 -0.0513 -0.0129 -0.1342 194 GLN B NE2 
3179 N N   . PHE B 69  ? 1.1108 0.6012 0.6280 -0.0152 0.0046  -0.1149 195 PHE B N   
3180 C CA  . PHE B 69  ? 1.0296 0.5701 0.5999 0.0044  0.0138  -0.0986 195 PHE B CA  
3181 C C   . PHE B 69  ? 1.0167 0.5293 0.5964 0.0163  0.0192  -0.0928 195 PHE B C   
3182 O O   . PHE B 69  ? 0.9767 0.5305 0.5995 0.0258  0.0222  -0.0776 195 PHE B O   
3183 C CB  . PHE B 69  ? 1.0159 0.5864 0.5921 0.0325  0.0329  -0.0999 195 PHE B CB  
3184 C CG  . PHE B 69  ? 0.9897 0.5921 0.5594 0.0222  0.0288  -0.1017 195 PHE B CG  
3185 C CD1 . PHE B 69  ? 0.9564 0.6090 0.5623 0.0054  0.0152  -0.0883 195 PHE B CD1 
3186 C CD2 . PHE B 69  ? 1.0671 0.6480 0.5932 0.0309  0.0397  -0.1160 195 PHE B CD2 
3187 C CE1 . PHE B 69  ? 0.9411 0.6201 0.5410 -0.0030 0.0106  -0.0872 195 PHE B CE1 
3188 C CE2 . PHE B 69  ? 1.0808 0.6912 0.5987 0.0204  0.0353  -0.1151 195 PHE B CE2 
3189 C CZ  . PHE B 69  ? 1.0129 0.6719 0.5689 0.0034  0.0199  -0.0995 195 PHE B CZ  
3190 N N   . VAL B 70  ? 1.1037 0.5451 0.6417 0.0151  0.0197  -0.1041 196 VAL B N   
3191 C CA  . VAL B 70  ? 1.1084 0.5142 0.6502 0.0280  0.0249  -0.0973 196 VAL B CA  
3192 C C   . VAL B 70  ? 1.1280 0.5149 0.6719 -0.0058 0.0057  -0.0896 196 VAL B C   
3193 O O   . VAL B 70  ? 1.1661 0.5103 0.6735 -0.0326 -0.0070 -0.1006 196 VAL B O   
3194 C CB  . VAL B 70  ? 1.1701 0.5026 0.6640 0.0521  0.0402  -0.1137 196 VAL B CB  
3195 N N   . THR B 71  ? 1.1050 0.5245 0.6899 -0.0062 0.0034  -0.0702 197 THR B N   
3196 C CA  . THR B 71  ? 1.1192 0.5284 0.7103 -0.0380 -0.0125 -0.0598 197 THR B CA  
3197 C C   . THR B 71  ? 1.2332 0.5564 0.7830 -0.0430 -0.0141 -0.0647 197 THR B C   
3198 O O   . THR B 71  ? 1.3083 0.6026 0.8422 -0.0775 -0.0297 -0.0642 197 THR B O   
3199 C CB  . THR B 71  ? 1.0868 0.5522 0.7275 -0.0353 -0.0117 -0.0383 197 THR B CB  
3200 N N   . GLY B 72  ? 1.2117 0.4931 0.7445 -0.0096 0.0015  -0.0684 198 GLY B N   
3201 C CA  . GLY B 72  ? 1.2942 0.4869 0.7871 -0.0094 0.0018  -0.0724 198 GLY B CA  
3202 C C   . GLY B 72  ? 1.3105 0.4854 0.8026 0.0361  0.0219  -0.0722 198 GLY B C   
3203 O O   . GLY B 72  ? 1.2535 0.4730 0.7741 0.0656  0.0340  -0.0648 198 GLY B O   
3204 N N   . GLU B 73  ? 1.3348 0.4541 0.7997 0.0417  0.0251  -0.0789 199 GLU B N   
3205 C CA  . GLU B 73  ? 1.3881 0.4916 0.8549 0.0853  0.0440  -0.0778 199 GLU B CA  
3206 C C   . GLU B 73  ? 1.3504 0.4588 0.8476 0.1000  0.0445  -0.0523 199 GLU B C   
3207 O O   . GLU B 73  ? 1.3182 0.4451 0.8358 0.1389  0.0589  -0.0438 199 GLU B O   
3208 C CB  . GLU B 73  ? 1.3786 0.4166 0.8034 0.0868  0.0479  -0.0949 199 GLU B CB  
3209 N N   . THR B 74  ? 1.3454 0.4433 0.8476 0.0687  0.0286  -0.0380 200 THR B N   
3210 C CA  . THR B 74  ? 1.3032 0.4102 0.8325 0.0771  0.0269  -0.0109 200 THR B CA  
3211 C C   . THR B 74  ? 1.2698 0.4266 0.8246 0.0525  0.0162  0.0047  200 THR B C   
3212 O O   . THR B 74  ? 1.2482 0.4220 0.7991 0.0207  0.0063  -0.0044 200 THR B O   
3213 C CB  . THR B 74  ? 1.3098 0.3576 0.8220 0.0626  0.0195  -0.0036 200 THR B CB  
3214 N N   . ILE B 75  ? 1.2266 0.4166 0.8113 0.0675  0.0180  0.0293  201 ILE B N   
3215 C CA  . ILE B 75  ? 1.1541 0.4169 0.7746 0.0408  0.0082  0.0448  201 ILE B CA  
3216 C C   . ILE B 75  ? 1.2080 0.4364 0.8136 -0.0010 -0.0058 0.0527  201 ILE B C   
3217 O O   . ILE B 75  ? 1.2254 0.5095 0.8550 -0.0297 -0.0137 0.0601  201 ILE B O   
3218 C CB  . ILE B 75  ? 1.0702 0.3852 0.7254 0.0636  0.0123  0.0687  201 ILE B CB  
3219 N N   . ARG B 76  ? 1.2813 0.4320 0.8544 -0.0053 -0.0083 0.0503  202 ARG B N   
3220 C CA  . ARG B 76  ? 1.2820 0.4132 0.8472 -0.0480 -0.0220 0.0563  202 ARG B CA  
3221 C C   . ARG B 76  ? 1.3076 0.4490 0.8628 -0.0818 -0.0317 0.0377  202 ARG B C   
3222 O O   . ARG B 76  ? 1.2794 0.4571 0.8510 -0.1174 -0.0423 0.0476  202 ARG B O   
3223 C CB  . ARG B 76  ? 1.3029 0.3667 0.8452 -0.0424 -0.0216 0.0559  202 ARG B CB  
3224 N N   . GLU B 77  ? 1.4163 0.5325 0.9465 -0.0708 -0.0279 0.0118  203 GLU B N   
3225 C CA  . GLU B 77  ? 1.3967 0.5263 0.9164 -0.1017 -0.0387 -0.0046 203 GLU B CA  
3226 C C   . GLU B 77  ? 1.3691 0.5645 0.9168 -0.1073 -0.0401 -0.0020 203 GLU B C   
3227 O O   . GLU B 77  ? 1.3453 0.5759 0.9043 -0.1416 -0.0529 -0.0019 203 GLU B O   
3228 C CB  . GLU B 77  ? 1.4453 0.5339 0.9279 -0.0870 -0.0330 -0.0316 203 GLU B CB  
3229 N N   . ALA B 78  ? 1.2959 0.5390 0.8710 -0.0710 -0.0264 0.0016  204 ALA B N   
3230 C CA  . ALA B 78  ? 1.1938 0.5296 0.8118 -0.0711 -0.0256 0.0046  204 ALA B CA  
3231 C C   . ALA B 78  ? 1.1939 0.5807 0.8461 -0.0966 -0.0330 0.0255  204 ALA B C   
3232 O O   . ALA B 78  ? 1.1054 0.5487 0.7820 -0.1159 -0.0390 0.0255  204 ALA B O   
3233 C CB  . ALA B 78  ? 1.1340 0.5062 0.7721 -0.0298 -0.0104 0.0053  204 ALA B CB  
3234 N N   . LEU B 79  ? 1.1474 0.5156 0.8015 -0.0959 -0.0318 0.0446  205 LEU B N   
3235 C CA  . LEU B 79  ? 1.1291 0.5464 0.8124 -0.1197 -0.0363 0.0650  205 LEU B CA  
3236 C C   . LEU B 79  ? 1.1817 0.5874 0.8582 -0.1637 -0.0502 0.0669  205 LEU B C   
3237 O O   . LEU B 79  ? 1.1813 0.6492 0.8893 -0.1849 -0.0533 0.0771  205 LEU B O   
3238 C CB  . LEU B 79  ? 1.0892 0.4883 0.7718 -0.1090 -0.0321 0.0869  205 LEU B CB  
3239 N N   . LYS B 80  ? 1.2508 0.5786 0.8867 -0.1784 -0.0584 0.0571  206 LYS B N   
3240 C CA  . LYS B 80  ? 1.2590 0.5781 0.8882 -0.2242 -0.0742 0.0588  206 LYS B CA  
3241 C C   . LYS B 80  ? 1.2219 0.5981 0.8697 -0.2361 -0.0808 0.0467  206 LYS B C   
3242 O O   . LYS B 80  ? 1.2145 0.6452 0.8916 -0.2654 -0.0892 0.0579  206 LYS B O   
3243 C CB  . LYS B 80  ? 1.3185 0.5667 0.9092 -0.2279 -0.0794 0.0464  206 LYS B CB  
3244 N N   . ARG B 81  ? 1.2464 0.6156 0.8799 -0.2118 -0.0762 0.0256  207 ARG B N   
3245 C CA  . ARG B 81  ? 1.1681 0.5837 0.8134 -0.2203 -0.0832 0.0143  207 ARG B CA  
3246 C C   . ARG B 81  ? 1.1342 0.6455 0.8340 -0.2126 -0.0778 0.0252  207 ARG B C   
3247 O O   . ARG B 81  ? 1.0619 0.6163 0.7767 -0.2183 -0.0837 0.0194  207 ARG B O   
3248 C CB  . ARG B 81  ? 1.2101 0.5916 0.8231 -0.1936 -0.0768 -0.0092 207 ARG B CB  
3249 N N   . SER B 82  ? 1.0769 0.6199 0.8038 -0.2003 -0.0673 0.0410  208 SER B N   
3250 C CA  . SER B 82  ? 1.0027 0.6270 0.7742 -0.1886 -0.0594 0.0478  208 SER B CA  
3251 C C   . SER B 82  ? 0.9445 0.6239 0.7502 -0.2173 -0.0648 0.0639  208 SER B C   
3252 O O   . SER B 82  ? 0.8922 0.6379 0.7339 -0.2094 -0.0589 0.0670  208 SER B O   
3253 C CB  . SER B 82  ? 0.9564 0.5898 0.7363 -0.1593 -0.0447 0.0547  208 SER B CB  
3254 N N   . LYS B 83  ? 0.9887 0.6421 0.7843 -0.2501 -0.0749 0.0747  209 LYS B N   
3255 C CA  . LYS B 83  ? 0.9555 0.6666 0.7868 -0.2767 -0.0771 0.0937  209 LYS B CA  
3256 C C   . LYS B 83  ? 0.9039 0.6763 0.7666 -0.2868 -0.0845 0.0916  209 LYS B C   
3257 O O   . LYS B 83  ? 0.8539 0.6975 0.7589 -0.2856 -0.0772 0.1026  209 LYS B O   
3258 C CB  . LYS B 83  ? 0.9495 0.6164 0.7612 -0.3139 -0.0883 0.1065  209 LYS B CB  
3259 N N   . GLU B 84  ? 0.9337 0.6789 0.7750 -0.2957 -0.0987 0.0777  210 GLU B N   
3260 C CA  . GLU B 84  ? 0.9166 0.7171 0.7855 -0.3093 -0.1101 0.0790  210 GLU B CA  
3261 C C   . GLU B 84  ? 0.8375 0.7050 0.7461 -0.2790 -0.0969 0.0791  210 GLU B C   
3262 O O   . GLU B 84  ? 0.8100 0.7456 0.7632 -0.2844 -0.0939 0.0931  210 GLU B O   
3263 C CB  . GLU B 84  ? 0.9373 0.6908 0.7670 -0.3184 -0.1263 0.0617  210 GLU B CB  
3264 N N   . LEU B 85  ? 0.8207 0.6690 0.7137 -0.2467 -0.0879 0.0639  211 LEU B N   
3265 C CA  . LEU B 85  ? 0.7811 0.6844 0.7071 -0.2205 -0.0770 0.0629  211 LEU B CA  
3266 C C   . LEU B 85  ? 0.7607 0.6934 0.7091 -0.2045 -0.0585 0.0710  211 LEU B C   
3267 O O   . LEU B 85  ? 0.7102 0.6928 0.6897 -0.1883 -0.0491 0.0724  211 LEU B O   
3268 C CB  . LEU B 85  ? 0.7927 0.6691 0.6950 -0.1955 -0.0747 0.0455  211 LEU B CB  
3269 C CG  . LEU B 85  ? 0.7982 0.6611 0.6817 -0.2085 -0.0917 0.0373  211 LEU B CG  
3270 C CD1 . LEU B 85  ? 0.7667 0.6099 0.6283 -0.1829 -0.0864 0.0220  211 LEU B CD1 
3271 C CD2 . LEU B 85  ? 0.7799 0.7050 0.7024 -0.2240 -0.1030 0.0497  211 LEU B CD2 
3272 N N   . GLU B 86  ? 0.7609 0.6622 0.6921 -0.2089 -0.0532 0.0768  212 GLU B N   
3273 C CA  . GLU B 86  ? 0.7406 0.6759 0.6915 -0.1997 -0.0375 0.0870  212 GLU B CA  
3274 C C   . GLU B 86  ? 0.7405 0.7360 0.7294 -0.2192 -0.0359 0.1027  212 GLU B C   
3275 O O   . GLU B 86  ? 0.6845 0.7305 0.7012 -0.2052 -0.0219 0.1057  212 GLU B O   
3276 C CB  . GLU B 86  ? 0.7930 0.6814 0.7156 -0.2007 -0.0339 0.0928  212 GLU B CB  
3277 C CG  . GLU B 86  ? 0.7749 0.6279 0.6738 -0.1709 -0.0277 0.0812  212 GLU B CG  
3278 C CD  . GLU B 86  ? 0.8623 0.6793 0.7399 -0.1680 -0.0234 0.0912  212 GLU B CD  
3279 O OE1 . GLU B 86  ? 0.8290 0.6404 0.7054 -0.1912 -0.0258 0.1067  212 GLU B OE1 
3280 O OE2 . GLU B 86  ? 0.8357 0.6326 0.6993 -0.1429 -0.0181 0.0856  212 GLU B OE2 
3281 N N   . GLU B 87  ? 0.7693 0.7611 0.7597 -0.2517 -0.0499 0.1126  213 GLU B N   
3282 C CA  . GLU B 87  ? 0.7668 0.8250 0.7993 -0.2711 -0.0493 0.1295  213 GLU B CA  
3283 C C   . GLU B 87  ? 0.8196 0.9338 0.8882 -0.2557 -0.0485 0.1260  213 GLU B C   
3284 O O   . GLU B 87  ? 0.8563 1.0355 0.9660 -0.2532 -0.0378 0.1372  213 GLU B O   
3285 C CB  . GLU B 87  ? 0.7772 0.8201 0.8038 -0.3128 -0.0682 0.1410  213 GLU B CB  
3286 N N   . LYS B 88  ? 0.7552 0.8448 0.8086 -0.2441 -0.0585 0.1113  214 LYS B N   
3287 C CA  . LYS B 88  ? 0.7764 0.9116 0.8603 -0.2257 -0.0575 0.1087  214 LYS B CA  
3288 C C   . LYS B 88  ? 0.7634 0.9152 0.8576 -0.1913 -0.0361 0.1015  214 LYS B C   
3289 O O   . LYS B 88  ? 0.7461 0.9393 0.8706 -0.1745 -0.0311 0.1019  214 LYS B O   
3290 C CB  . LYS B 88  ? 0.7533 0.8545 0.8125 -0.2248 -0.0742 0.0963  214 LYS B CB  
3291 N N   . GLY B 89  ? 0.6867 0.8053 0.7551 -0.1810 -0.0245 0.0954  215 GLY B N   
3292 C CA  . GLY B 89  ? 0.6220 0.7529 0.6944 -0.1531 -0.0062 0.0880  215 GLY B CA  
3293 C C   . GLY B 89  ? 0.6131 0.7002 0.6550 -0.1332 -0.0057 0.0723  215 GLY B C   
3294 O O   . GLY B 89  ? 0.5524 0.6483 0.5959 -0.1126 0.0071  0.0655  215 GLY B O   
3295 N N   . PHE B 90  ? 0.5660 0.6074 0.5797 -0.1391 -0.0187 0.0661  216 PHE B N   
3296 C CA  . PHE B 90  ? 0.5784 0.5814 0.5642 -0.1203 -0.0162 0.0536  216 PHE B CA  
3297 C C   . PHE B 90  ? 0.6000 0.5789 0.5666 -0.1176 -0.0086 0.0567  216 PHE B C   
3298 O O   . PHE B 90  ? 0.5782 0.5554 0.5438 -0.1342 -0.0088 0.0681  216 PHE B O   
3299 C CB  . PHE B 90  ? 0.5845 0.5462 0.5439 -0.1256 -0.0297 0.0455  216 PHE B CB  
3300 C CG  . PHE B 90  ? 0.5797 0.5607 0.5508 -0.1251 -0.0383 0.0420  216 PHE B CG  
3301 C CD1 . PHE B 90  ? 0.6152 0.6193 0.6029 -0.1460 -0.0508 0.0505  216 PHE B CD1 
3302 C CD2 . PHE B 90  ? 0.5547 0.5316 0.5198 -0.1052 -0.0351 0.0323  216 PHE B CD2 
3303 C CE1 . PHE B 90  ? 0.5557 0.5787 0.5533 -0.1452 -0.0608 0.0498  216 PHE B CE1 
3304 C CE2 . PHE B 90  ? 0.5357 0.5283 0.5091 -0.1051 -0.0438 0.0314  216 PHE B CE2 
3305 C CZ  . PHE B 90  ? 0.5349 0.5501 0.5240 -0.1242 -0.0570 0.0404  216 PHE B CZ  
3306 N N   . SER B 91  ? 0.5452 0.5080 0.4974 -0.0974 -0.0029 0.0486  217 SER B N   
3307 C CA  . SER B 91  ? 0.5288 0.4634 0.4596 -0.0920 0.0007  0.0524  217 SER B CA  
3308 C C   . SER B 91  ? 0.6051 0.4987 0.5122 -0.0788 -0.0034 0.0430  217 SER B C   
3309 O O   . SER B 91  ? 0.5158 0.4058 0.4216 -0.0756 -0.0078 0.0334  217 SER B O   
3310 C CB  . SER B 91  ? 0.5468 0.5090 0.4846 -0.0797 0.0122  0.0539  217 SER B CB  
3311 O OG  . SER B 91  ? 0.5536 0.5278 0.4967 -0.0632 0.0152  0.0426  217 SER B OG  
3312 N N   . TYR B 92  ? 0.6056 0.4698 0.4941 -0.0702 -0.0013 0.0471  218 TYR B N   
3313 C CA  . TYR B 92  ? 0.6148 0.4403 0.4817 -0.0547 -0.0024 0.0396  218 TYR B CA  
3314 C C   . TYR B 92  ? 0.6028 0.4342 0.4690 -0.0333 0.0045  0.0431  218 TYR B C   
3315 O O   . TYR B 92  ? 0.5628 0.4117 0.4347 -0.0340 0.0075  0.0539  218 TYR B O   
3316 C CB  . TYR B 92  ? 0.6811 0.4505 0.5217 -0.0645 -0.0087 0.0415  218 TYR B CB  
3317 C CG  . TYR B 92  ? 0.7101 0.4644 0.5428 -0.0839 -0.0184 0.0337  218 TYR B CG  
3318 C CD1 . TYR B 92  ? 0.7214 0.4933 0.5671 -0.1106 -0.0253 0.0418  218 TYR B CD1 
3319 C CD2 . TYR B 92  ? 0.7195 0.4455 0.5312 -0.0766 -0.0208 0.0194  218 TYR B CD2 
3320 C CE1 . TYR B 92  ? 0.7463 0.5098 0.5864 -0.1310 -0.0370 0.0368  218 TYR B CE1 
3321 C CE2 . TYR B 92  ? 0.7313 0.4444 0.5318 -0.0970 -0.0320 0.0125  218 TYR B CE2 
3322 C CZ  . TYR B 92  ? 0.7701 0.5028 0.5858 -0.1248 -0.0413 0.0218  218 TYR B CZ  
3323 O OH  . TYR B 92  ? 0.7764 0.5018 0.5828 -0.1473 -0.0550 0.0172  218 TYR B OH  
3324 N N   . SER B 93  ? 0.5937 0.4147 0.4528 -0.0152 0.0069  0.0346  219 SER B N   
3325 C CA  . SER B 93  ? 0.6138 0.4356 0.4714 0.0064  0.0120  0.0394  219 SER B CA  
3326 C C   . SER B 93  ? 0.6631 0.4392 0.4992 0.0207  0.0137  0.0339  219 SER B C   
3327 O O   . SER B 93  ? 0.6572 0.4273 0.4867 0.0250  0.0153  0.0213  219 SER B O   
3328 C CB  . SER B 93  ? 0.5951 0.4599 0.4701 0.0159  0.0159  0.0351  219 SER B CB  
3329 O OG  . SER B 93  ? 0.6072 0.4775 0.4833 0.0353  0.0193  0.0412  219 SER B OG  
3330 N N   . TYR B 94  ? 0.6386 0.3807 0.4618 0.0293  0.0142  0.0435  220 TYR B N   
3331 C CA  . TYR B 94  ? 0.6941 0.3858 0.4942 0.0465  0.0181  0.0377  220 TYR B CA  
3332 C C   . TYR B 94  ? 0.7305 0.4424 0.5411 0.0767  0.0269  0.0407  220 TYR B C   
3333 O O   . TYR B 94  ? 0.6921 0.4445 0.5235 0.0832  0.0267  0.0535  220 TYR B O   
3334 C CB  . TYR B 94  ? 0.7419 0.3790 0.5216 0.0421  0.0146  0.0474  220 TYR B CB  
3335 C CG  . TYR B 94  ? 0.7884 0.4119 0.5613 0.0088  0.0054  0.0477  220 TYR B CG  
3336 C CD1 . TYR B 94  ? 0.8226 0.4048 0.5720 -0.0063 0.0005  0.0340  220 TYR B CD1 
3337 C CD2 . TYR B 94  ? 0.7518 0.4083 0.5418 -0.0088 0.0016  0.0620  220 TYR B CD2 
3338 C CE1 . TYR B 94  ? 0.8669 0.4441 0.6143 -0.0392 -0.0095 0.0365  220 TYR B CE1 
3339 C CE2 . TYR B 94  ? 0.7701 0.4224 0.5587 -0.0394 -0.0055 0.0644  220 TYR B CE2 
3340 C CZ  . TYR B 94  ? 0.8576 0.4722 0.6273 -0.0550 -0.0118 0.0526  220 TYR B CZ  
3341 O OH  . TYR B 94  ? 0.8914 0.5087 0.6638 -0.0875 -0.0204 0.0574  220 TYR B OH  
3342 N N   . ASP B 95  ? 0.7898 0.4759 0.5851 0.0941  0.0345  0.0289  221 ASP B N   
3343 C CA  . ASP B 95  ? 0.8365 0.5347 0.6401 0.1262  0.0451  0.0332  221 ASP B CA  
3344 C C   . ASP B 95  ? 0.9032 0.5341 0.6771 0.1456  0.0525  0.0279  221 ASP B C   
3345 O O   . ASP B 95  ? 0.9092 0.4982 0.6539 0.1394  0.0545  0.0102  221 ASP B O   
3346 C CB  . ASP B 95  ? 0.7768 0.5172 0.5926 0.1320  0.0517  0.0234  221 ASP B CB  
3347 C CG  . ASP B 95  ? 0.8499 0.6152 0.6809 0.1641  0.0635  0.0304  221 ASP B CG  
3348 O OD1 . ASP B 95  ? 0.9057 0.6402 0.7294 0.1881  0.0699  0.0369  221 ASP B OD1 
3349 O OD2 . ASP B 95  ? 0.8104 0.6274 0.6620 0.1655  0.0668  0.0305  221 ASP B OD2 
3350 N N   . MET B 96  ? 0.9853 0.6037 0.7645 0.1690  0.0560  0.0434  222 MET B N   
3351 C CA  . MET B 96  ? 1.0508 0.6074 0.8047 0.1965  0.0669  0.0386  222 MET B CA  
3352 C C   . MET B 96  ? 1.1245 0.7060 0.8840 0.2231  0.0827  0.0282  222 MET B C   
3353 O O   . MET B 96  ? 1.0846 0.7082 0.8724 0.2502  0.0902  0.0420  222 MET B O   
3354 C CB  . MET B 96  ? 1.0490 0.5894 0.8113 0.2177  0.0664  0.0615  222 MET B CB  
3355 C CG  . MET B 96  ? 1.0438 0.5696 0.8031 0.1908  0.0515  0.0761  222 MET B CG  
3356 S SD  . MET B 96  ? 1.1553 0.6003 0.8712 0.1574  0.0439  0.0607  222 MET B SD  
3357 C CE  . MET B 96  ? 1.1271 0.4787 0.8050 0.1907  0.0565  0.0517  222 MET B CE  
3358 N N   . LEU B 97  ? 1.3408 0.9016 1.0742 0.2135  0.0871  0.0056  223 LEU B N   
3359 C CA  . LEU B 97  ? 1.3959 0.9869 1.1320 0.2311  0.1018  -0.0052 223 LEU B CA  
3360 C C   . LEU B 97  ? 1.4146 1.0148 1.1648 0.2748  0.1194  0.0039  223 LEU B C   
3361 O O   . LEU B 97  ? 1.3965 0.9350 1.1179 0.2992  0.1315  -0.0041 223 LEU B O   
3362 C CB  . LEU B 97  ? 1.4104 0.9497 1.1005 0.2207  0.1058  -0.0309 223 LEU B CB  
3363 N N   . GLY B 98  ? 1.1697 0.8468 0.9646 0.2846  0.1203  0.0214  224 GLY B N   
3364 C CA  . GLY B 98  ? 1.0666 0.7722 0.8859 0.3250  0.1355  0.0345  224 GLY B CA  
3365 C C   . GLY B 98  ? 0.9634 0.7620 0.8263 0.3243  0.1365  0.0462  224 GLY B C   
3366 O O   . GLY B 98  ? 0.8811 0.7235 0.7653 0.2968  0.1205  0.0549  224 GLY B O   
3367 N N   . GLU B 99  ? 0.9114 0.7403 0.7865 0.3533  0.1561  0.0462  225 GLU B N   
3368 C CA  . GLU B 99  ? 0.7942 0.7125 0.7110 0.3500  0.1571  0.0586  225 GLU B CA  
3369 C C   . GLU B 99  ? 0.8138 0.7650 0.7491 0.3797  0.1757  0.0646  225 GLU B C   
3370 O O   . GLU B 99  ? 0.8395 0.7425 0.7475 0.3952  0.1885  0.0516  225 GLU B O   
3371 C CB  . GLU B 99  ? 0.7930 0.7280 0.6986 0.3170  0.1533  0.0434  225 GLU B CB  
3372 C CG  . GLU B 99  ? 0.8075 0.6904 0.6678 0.3189  0.1668  0.0184  225 GLU B CG  
3373 C CD  . GLU B 99  ? 0.8498 0.7512 0.7014 0.2844  0.1589  0.0080  225 GLU B CD  
3374 O OE1 . GLU B 99  ? 0.7911 0.7473 0.6611 0.2849  0.1675  0.0122  225 GLU B OE1 
3375 O OE2 . GLU B 99  ? 0.8633 0.7276 0.6926 0.2565  0.1435  -0.0018 225 GLU B OE2 
3376 N N   . ALA B 100 ? 0.7819 0.8176 0.7636 0.3806  0.1741  0.0843  226 ALA B N   
3377 C CA  . ALA B 100 ? 0.7439 0.8271 0.7498 0.3993  0.1887  0.0927  226 ALA B CA  
3378 C C   . ALA B 100 ? 0.8301 0.8805 0.8346 0.4298  0.1960  0.0985  226 ALA B C   
3379 O O   . ALA B 100 ? 0.9096 0.9252 0.8919 0.4480  0.2133  0.0851  226 ALA B O   
3380 C CB  . ALA B 100 ? 0.7926 0.8711 0.7751 0.3947  0.2048  0.0731  226 ALA B CB  
3381 N N   . ALA B 101 ? 0.7948 0.8557 0.8219 0.4344  0.1820  0.1191  227 ALA B N   
3382 C CA  . ALA B 101 ? 0.8512 0.8834 0.8808 0.4625  0.1864  0.1283  227 ALA B CA  
3383 C C   . ALA B 101 ? 0.9087 0.9894 0.9653 0.4874  0.2037  0.1364  227 ALA B C   
3384 O O   . ALA B 101 ? 0.9169 1.0805 1.0166 0.4842  0.1998  0.1563  227 ALA B O   
3385 C CB  . ALA B 101 ? 0.8346 0.8853 0.8890 0.4598  0.1663  0.1533  227 ALA B CB  
3386 N N   . THR B 102 ? 0.9933 1.0227 1.0236 0.5108  0.2224  0.1210  228 THR B N   
3387 C CA  . THR B 102 ? 0.9195 0.9895 0.9722 0.5376  0.2418  0.1269  228 THR B CA  
3388 C C   . THR B 102 ? 0.9680 1.0393 1.0449 0.5692  0.2434  0.1464  228 THR B C   
3389 O O   . THR B 102 ? 1.0063 1.1069 1.1025 0.5963  0.2607  0.1522  228 THR B O   
3390 C CB  . THR B 102 ? 1.0098 1.0281 1.0197 0.5464  0.2633  0.0983  228 THR B CB  
3391 N N   . THR B 103 ? 0.9713 1.0127 1.0481 0.5666  0.2260  0.1576  229 THR B N   
3392 C CA  . THR B 103 ? 1.0173 1.0581 1.1171 0.5952  0.2248  0.1782  229 THR B CA  
3393 C C   . THR B 103 ? 1.0129 1.0642 1.1279 0.5784  0.1984  0.1993  229 THR B C   
3394 O O   . THR B 103 ? 0.9729 1.0019 1.0673 0.5489  0.1840  0.1918  229 THR B O   
3395 C CB  . THR B 103 ? 1.1074 1.0541 1.1686 0.6204  0.2385  0.1609  229 THR B CB  
3396 N N   . ALA B 104 ? 1.0024 1.0895 1.1535 0.5978  0.1923  0.2267  230 ALA B N   
3397 C CA  . ALA B 104 ? 0.9935 1.0873 1.1560 0.5838  0.1670  0.2484  230 ALA B CA  
3398 C C   . ALA B 104 ? 1.0591 1.0527 1.1787 0.5819  0.1610  0.2375  230 ALA B C   
3399 O O   . ALA B 104 ? 1.0119 0.9917 1.1208 0.5562  0.1412  0.2431  230 ALA B O   
3400 C CB  . ALA B 104 ? 1.0032 1.1560 1.2121 0.6063  0.1618  0.2805  230 ALA B CB  
3401 N N   . ALA B 105 ? 1.1196 1.0418 1.2131 0.6074  0.1779  0.2223  231 ALA B N   
3402 C CA  . ALA B 105 ? 1.1663 0.9875 1.2149 0.6015  0.1726  0.2096  231 ALA B CA  
3403 C C   . ALA B 105 ? 1.1258 0.9082 1.1346 0.5676  0.1695  0.1842  231 ALA B C   
3404 O O   . ALA B 105 ? 1.1160 0.8415 1.0972 0.5473  0.1555  0.1818  231 ALA B O   
3405 C CB  . ALA B 105 ? 1.2433 0.9964 1.2709 0.6348  0.1920  0.1965  231 ALA B CB  
3406 N N   . ASP B 106 ? 1.1455 0.9592 1.1514 0.5604  0.1819  0.1667  232 ASP B N   
3407 C CA  . ASP B 106 ? 1.1210 0.9039 1.0917 0.5289  0.1787  0.1436  232 ASP B CA  
3408 C C   . ASP B 106 ? 1.0622 0.8809 1.0464 0.4988  0.1564  0.1576  232 ASP B C   
3409 O O   . ASP B 106 ? 1.0320 0.7999 0.9844 0.4744  0.1463  0.1471  232 ASP B O   
3410 C CB  . ASP B 106 ? 1.0996 0.9162 1.0682 0.5288  0.1960  0.1255  232 ASP B CB  
3411 N N   . ALA B 107 ? 1.0332 0.9397 1.0636 0.4989  0.1480  0.1820  233 ALA B N   
3412 C CA  . ALA B 107 ? 0.9389 0.8838 0.9819 0.4704  0.1264  0.1960  233 ALA B CA  
3413 C C   . ALA B 107 ? 0.9883 0.8821 1.0149 0.4629  0.1098  0.2081  233 ALA B C   
3414 O O   . ALA B 107 ? 0.9594 0.8263 0.9635 0.4363  0.0980  0.2035  233 ALA B O   
3415 C CB  . ALA B 107 ? 0.8660 0.9131 0.9597 0.4708  0.1194  0.2202  233 ALA B CB  
3416 N N   . GLU B 108 ? 0.9898 0.8700 1.0274 0.4861  0.1087  0.2251  234 GLU B N   
3417 C CA  . GLU B 108 ? 1.0129 0.8445 1.0350 0.4786  0.0925  0.2393  234 GLU B CA  
3418 C C   . GLU B 108 ? 1.0884 0.8213 1.0602 0.4657  0.0955  0.2167  234 GLU B C   
3419 O O   . GLU B 108 ? 1.0921 0.7913 1.0441 0.4420  0.0803  0.2229  234 GLU B O   
3420 C CB  . GLU B 108 ? 1.0906 0.9221 1.1337 0.5089  0.0922  0.2610  234 GLU B CB  
3421 N N   . ARG B 109 ? 1.1017 0.7892 1.0504 0.4782  0.1144  0.1906  235 ARG B N   
3422 C CA  . ARG B 109 ? 1.1404 0.7364 1.0392 0.4615  0.1162  0.1668  235 ARG B CA  
3423 C C   . ARG B 109 ? 1.1550 0.7559 1.0372 0.4259  0.1074  0.1562  235 ARG B C   
3424 O O   . ARG B 109 ? 1.1806 0.7301 1.0357 0.4010  0.0956  0.1554  235 ARG B O   
3425 C CB  . ARG B 109 ? 1.1931 0.7485 1.0690 0.4801  0.1379  0.1399  235 ARG B CB  
3426 N N   . TYR B 110 ? 1.0836 0.7457 0.9822 0.4223  0.1133  0.1485  236 TYR B N   
3427 C CA  . TYR B 110 ? 1.0593 0.7347 0.9484 0.3915  0.1043  0.1415  236 TYR B CA  
3428 C C   . TYR B 110 ? 0.9943 0.6894 0.8941 0.3730  0.0841  0.1662  236 TYR B C   
3429 O O   . TYR B 110 ? 1.0335 0.6941 0.9079 0.3458  0.0748  0.1620  236 TYR B O   
3430 C CB  . TYR B 110 ? 0.9978 0.7479 0.9120 0.3931  0.1120  0.1359  236 TYR B CB  
3431 C CG  . TYR B 110 ? 1.0458 0.7724 0.9379 0.3997  0.1305  0.1079  236 TYR B CG  
3432 C CD1 . TYR B 110 ? 1.0716 0.7229 0.9164 0.3832  0.1322  0.0829  236 TYR B CD1 
3433 C CD2 . TYR B 110 ? 1.0139 0.7952 0.9309 0.4197  0.1454  0.1075  236 TYR B CD2 
3434 C CE1 . TYR B 110 ? 1.1174 0.7487 0.9379 0.3865  0.1474  0.0578  236 TYR B CE1 
3435 C CE2 . TYR B 110 ? 1.0224 0.7837 0.9160 0.4243  0.1623  0.0834  236 TYR B CE2 
3436 C CZ  . TYR B 110 ? 1.1413 0.8272 0.9853 0.4078  0.1630  0.0582  236 TYR B CZ  
3437 O OH  . TYR B 110 ? 1.1694 0.8369 0.9866 0.4101  0.1783  0.0347  236 TYR B OH  
3438 N N   . TYR B 111 ? 0.9617 0.7135 0.8973 0.3856  0.0768  0.1927  237 TYR B N   
3439 C CA  . TYR B 111 ? 0.9845 0.7610 0.9275 0.3664  0.0569  0.2170  237 TYR B CA  
3440 C C   . TYR B 111 ? 1.0230 0.7201 0.9315 0.3526  0.0493  0.2202  237 TYR B C   
3441 O O   . TYR B 111 ? 0.9945 0.6829 0.8861 0.3238  0.0382  0.2248  237 TYR B O   
3442 C CB  . TYR B 111 ? 0.9635 0.8084 0.9468 0.3821  0.0495  0.2440  237 TYR B CB  
3443 C CG  . TYR B 111 ? 0.9467 0.8106 0.9317 0.3630  0.0285  0.2697  237 TYR B CG  
3444 C CD1 . TYR B 111 ? 0.8670 0.7838 0.8565 0.3355  0.0163  0.2752  237 TYR B CD1 
3445 C CD2 . TYR B 111 ? 1.0305 0.8593 1.0103 0.3716  0.0209  0.2884  237 TYR B CD2 
3446 C CE1 . TYR B 111 ? 0.8522 0.7871 0.8376 0.3155  -0.0019 0.2968  237 TYR B CE1 
3447 C CE2 . TYR B 111 ? 1.0069 0.8541 0.9844 0.3522  0.0017  0.3122  237 TYR B CE2 
3448 C CZ  . TYR B 111 ? 0.9296 0.8305 0.9085 0.3235  -0.0089 0.3154  237 TYR B CZ  
3449 O OH  . TYR B 111 ? 0.9737 0.8941 0.9451 0.3020  -0.0267 0.3366  237 TYR B OH  
3450 N N   . ARG B 112 ? 1.0376 0.6759 0.9343 0.3714  0.0557  0.2176  238 ARG B N   
3451 C CA  . ARG B 112 ? 1.0635 0.6247 0.9287 0.3563  0.0477  0.2216  238 ARG B CA  
3452 C C   . ARG B 112 ? 1.1080 0.6131 0.9344 0.3274  0.0496  0.1973  238 ARG B C   
3453 O O   . ARG B 112 ? 1.1130 0.5850 0.9185 0.2989  0.0384  0.2045  238 ARG B O   
3454 C CB  . ARG B 112 ? 1.1294 0.6386 0.9909 0.3840  0.0547  0.2224  238 ARG B CB  
3455 N N   . ASP B 113 ? 1.1012 0.5985 0.9175 0.3321  0.0631  0.1693  239 ASP B N   
3456 C CA  . ASP B 113 ? 1.0665 0.5182 0.8474 0.3025  0.0628  0.1461  239 ASP B CA  
3457 C C   . ASP B 113 ? 1.0611 0.5627 0.8506 0.2709  0.0516  0.1513  239 ASP B C   
3458 O O   . ASP B 113 ? 1.0819 0.5565 0.8509 0.2348  0.0428  0.1445  239 ASP B O   
3459 C CB  . ASP B 113 ? 1.0903 0.5317 0.8589 0.3134  0.0786  0.1158  239 ASP B CB  
3460 N N   . TYR B 114 ? 1.0066 0.5952 0.8328 0.2758  0.0501  0.1596  240 TYR B N   
3461 C CA  . TYR B 114 ? 0.9413 0.5901 0.7814 0.2404  0.0382  0.1612  240 TYR B CA  
3462 C C   . TYR B 114 ? 0.9250 0.5688 0.7607 0.2231  0.0247  0.1850  240 TYR B C   
3463 O O   . TYR B 114 ? 0.8801 0.5276 0.7060 0.1878  0.0172  0.1809  240 TYR B O   
3464 C CB  . TYR B 114 ? 0.8894 0.6248 0.7660 0.2502  0.0390  0.1660  240 TYR B CB  
3465 C CG  . TYR B 114 ? 0.8070 0.5656 0.6885 0.2489  0.0490  0.1412  240 TYR B CG  
3466 C CD1 . TYR B 114 ? 0.8733 0.6092 0.7342 0.2210  0.0488  0.1178  240 TYR B CD1 
3467 C CD2 . TYR B 114 ? 0.8301 0.6381 0.7383 0.2742  0.0579  0.1438  240 TYR B CD2 
3468 C CE1 . TYR B 114 ? 0.8373 0.5943 0.7008 0.2190  0.0567  0.0978  240 TYR B CE1 
3469 C CE2 . TYR B 114 ? 0.7862 0.6159 0.6972 0.2711  0.0673  0.1234  240 TYR B CE2 
3470 C CZ  . TYR B 114 ? 0.8202 0.6222 0.7072 0.2435  0.0663  0.1005  240 TYR B CZ  
3471 O OH  . TYR B 114 ? 0.8503 0.6718 0.7374 0.2394  0.0743  0.0825  240 TYR B OH  
3472 N N   . GLU B 115 ? 0.9505 0.5889 0.7940 0.2484  0.0220  0.2116  241 GLU B N   
3473 C CA  . GLU B 115 ? 0.9831 0.6133 0.8188 0.2335  0.0093  0.2374  241 GLU B CA  
3474 C C   . GLU B 115 ? 0.9955 0.5490 0.7961 0.2089  0.0076  0.2314  241 GLU B C   
3475 O O   . GLU B 115 ? 0.9304 0.4953 0.7230 0.1739  -0.0004 0.2350  241 GLU B O   
3476 C CB  . GLU B 115 ? 0.9771 0.6072 0.8269 0.2689  0.0069  0.2670  241 GLU B CB  
3477 C CG  . GLU B 115 ? 1.0071 0.6111 0.8443 0.2549  -0.0057 0.2912  241 GLU B CG  
3478 C CD  . GLU B 115 ? 1.0564 0.6452 0.9078 0.2839  -0.0081 0.3059  241 GLU B CD  
3479 O OE1 . GLU B 115 ? 1.1204 0.6548 0.9655 0.3033  0.0025  0.2906  241 GLU B OE1 
3480 O OE2 . GLU B 115 ? 1.0395 0.6721 0.9074 0.2873  -0.0203 0.3318  241 GLU B OE2 
3481 N N   . SER B 116 ? 1.0473 0.5221 0.8256 0.2258  0.0157  0.2216  242 SER B N   
3482 C CA  . SER B 116 ? 1.0845 0.4823 0.8276 0.1993  0.0125  0.2157  242 SER B CA  
3483 C C   . SER B 116 ? 1.0364 0.4521 0.7736 0.1601  0.0107  0.1911  242 SER B C   
3484 O O   . SER B 116 ? 1.0348 0.4271 0.7559 0.1257  0.0034  0.1944  242 SER B O   
3485 C CB  . SER B 116 ? 1.1496 0.4803 0.8793 0.2166  0.0197  0.1992  242 SER B CB  
3486 N N   . ALA B 117 ? 0.9935 0.4537 0.7453 0.1646  0.0173  0.1688  243 ALA B N   
3487 C CA  . ALA B 117 ? 0.9648 0.4464 0.7145 0.1304  0.0150  0.1479  243 ALA B CA  
3488 C C   . ALA B 117 ? 0.8878 0.4303 0.6545 0.1028  0.0068  0.1601  243 ALA B C   
3489 O O   . ALA B 117 ? 0.9037 0.4436 0.6630 0.0698  0.0025  0.1546  243 ALA B O   
3490 C CB  . ALA B 117 ? 0.9763 0.4923 0.7378 0.1430  0.0236  0.1247  243 ALA B CB  
3491 N N   . ILE B 118 ? 0.8998 0.4992 0.6886 0.1154  0.0049  0.1765  244 ILE B N   
3492 C CA  . ILE B 118 ? 0.8299 0.4829 0.6283 0.0901  -0.0014 0.1865  244 ILE B CA  
3493 C C   . ILE B 118 ? 0.8547 0.4723 0.6342 0.0680  -0.0074 0.2051  244 ILE B C   
3494 O O   . ILE B 118 ? 0.8285 0.4667 0.6065 0.0373  -0.0091 0.2033  244 ILE B O   
3495 C CB  . ILE B 118 ? 0.7838 0.4991 0.6037 0.1065  -0.0043 0.2011  244 ILE B CB  
3496 C CG1 . ILE B 118 ? 0.7481 0.5088 0.5884 0.1167  0.0011  0.1816  244 ILE B CG1 
3497 C CG2 . ILE B 118 ? 0.7531 0.5101 0.5722 0.0815  -0.0110 0.2146  244 ILE B CG2 
3498 C CD1 . ILE B 118 ? 0.7511 0.5711 0.6137 0.1332  -0.0027 0.1954  244 ILE B CD1 
3499 N N   . HIS B 119 ? 0.8903 0.4536 0.6555 0.0836  -0.0097 0.2240  245 HIS B N   
3500 C CA  . HIS B 119 ? 0.9156 0.4366 0.6600 0.0607  -0.0155 0.2430  245 HIS B CA  
3501 C C   . HIS B 119 ? 0.9590 0.4435 0.6883 0.0292  -0.0151 0.2255  245 HIS B C   
3502 O O   . HIS B 119 ? 0.9299 0.4226 0.6543 -0.0035 -0.0186 0.2349  245 HIS B O   
3503 C CB  . HIS B 119 ? 0.9864 0.4420 0.7158 0.0857  -0.0177 0.2645  245 HIS B CB  
3504 C CG  . HIS B 119 ? 0.9979 0.4907 0.7404 0.1073  -0.0228 0.2935  245 HIS B CG  
3505 N ND1 . HIS B 119 ? 1.0014 0.5407 0.7450 0.0865  -0.0300 0.3148  245 HIS B ND1 
3506 C CD2 . HIS B 119 ? 1.0060 0.4988 0.7607 0.1476  -0.0221 0.3062  245 HIS B CD2 
3507 C CE1 . HIS B 119 ? 0.9825 0.5483 0.7365 0.1110  -0.0357 0.3393  245 HIS B CE1 
3508 N NE2 . HIS B 119 ? 1.0070 0.5482 0.7712 0.1488  -0.0314 0.3355  245 HIS B NE2 
3509 N N   . ALA B 120 ? 0.9381 0.3845 0.6594 0.0379  -0.0109 0.2013  246 ALA B N   
3510 C CA  . ALA B 120 ? 0.9786 0.3899 0.6841 0.0068  -0.0132 0.1852  246 ALA B CA  
3511 C C   . ALA B 120 ? 0.8809 0.3613 0.6073 -0.0173 -0.0129 0.1722  246 ALA B C   
3512 O O   . ALA B 120 ? 0.8834 0.3654 0.6073 -0.0513 -0.0170 0.1739  246 ALA B O   
3513 C CB  . ALA B 120 ? 1.0187 0.3684 0.7040 0.0229  -0.0092 0.1622  246 ALA B CB  
3514 N N   . ILE B 121 ? 0.8334 0.3718 0.5817 -0.0001 -0.0078 0.1607  247 ILE B N   
3515 C CA  . ILE B 121 ? 0.8257 0.4272 0.5941 -0.0190 -0.0066 0.1493  247 ILE B CA  
3516 C C   . ILE B 121 ? 0.7899 0.4353 0.5671 -0.0372 -0.0074 0.1678  247 ILE B C   
3517 O O   . ILE B 121 ? 0.7449 0.4202 0.5307 -0.0627 -0.0067 0.1645  247 ILE B O   
3518 C CB  . ILE B 121 ? 0.7743 0.4198 0.5608 0.0035  -0.0012 0.1337  247 ILE B CB  
3519 C CG1 . ILE B 121 ? 0.7881 0.3927 0.5631 0.0206  0.0018  0.1152  247 ILE B CG1 
3520 C CG2 . ILE B 121 ? 0.7088 0.4127 0.5146 -0.0140 0.0003  0.1227  247 ILE B CG2 
3521 C CD1 . ILE B 121 ? 0.7411 0.3828 0.5323 0.0477  0.0081  0.1066  247 ILE B CD1 
3522 N N   . GLY B 122 ? 0.8015 0.4534 0.5762 -0.0238 -0.0086 0.1884  248 GLY B N   
3523 C CA  . GLY B 122 ? 0.7580 0.4500 0.5345 -0.0411 -0.0088 0.2062  248 GLY B CA  
3524 C C   . GLY B 122 ? 0.7907 0.4550 0.5542 -0.0714 -0.0110 0.2203  248 GLY B C   
3525 O O   . GLY B 122 ? 0.7941 0.4995 0.5640 -0.0946 -0.0073 0.2242  248 GLY B O   
3526 N N   . LYS B 123 ? 0.8427 0.4362 0.5872 -0.0718 -0.0160 0.2282  249 LYS B N   
3527 C CA  . LYS B 123 ? 0.8931 0.4550 0.6244 -0.1048 -0.0196 0.2420  249 LYS B CA  
3528 C C   . LYS B 123 ? 0.8608 0.4415 0.6035 -0.1316 -0.0186 0.2240  249 LYS B C   
3529 O O   . LYS B 123 ? 0.8666 0.4764 0.6158 -0.1613 -0.0172 0.2345  249 LYS B O   
3530 C CB  . LYS B 123 ? 0.9654 0.4375 0.6703 -0.0991 -0.0259 0.2521  249 LYS B CB  
3531 N N   . ALA B 124 ? 0.8946 0.4639 0.6411 -0.1213 -0.0190 0.1985  250 ALA B N   
3532 C CA  . ALA B 124 ? 0.8755 0.4669 0.6346 -0.1454 -0.0202 0.1831  250 ALA B CA  
3533 C C   . ALA B 124 ? 0.8289 0.5039 0.6165 -0.1513 -0.0126 0.1813  250 ALA B C   
3534 O O   . ALA B 124 ? 0.8611 0.5664 0.6625 -0.1782 -0.0120 0.1840  250 ALA B O   
3535 C CB  . ALA B 124 ? 0.8766 0.4418 0.6308 -0.1306 -0.0223 0.1571  250 ALA B CB  
3536 N N   . SER B 125 ? 0.7645 0.4776 0.5614 -0.1263 -0.0063 0.1768  251 SER B N   
3537 C CA  . SER B 125 ? 0.7385 0.5224 0.5566 -0.1297 0.0021  0.1728  251 SER B CA  
3538 C C   . SER B 125 ? 0.7624 0.5727 0.5812 -0.1543 0.0067  0.1929  251 SER B C   
3539 O O   . SER B 125 ? 0.7078 0.5669 0.5455 -0.1679 0.0140  0.1892  251 SER B O   
3540 C CB  . SER B 125 ? 0.7358 0.5462 0.5560 -0.1029 0.0059  0.1681  251 SER B CB  
3541 O OG  . SER B 125 ? 0.6810 0.5504 0.5136 -0.1076 0.0145  0.1652  251 SER B OG  
3542 N N   . ALA B 126 ? 0.7213 0.5002 0.5198 -0.1591 0.0033  0.2157  252 ALA B N   
3543 C CA  . ALA B 126 ? 0.8038 0.6009 0.5982 -0.1852 0.0073  0.2387  252 ALA B CA  
3544 C C   . ALA B 126 ? 0.7888 0.6579 0.5949 -0.1857 0.0204  0.2368  252 ALA B C   
3545 O O   . ALA B 126 ? 0.8300 0.7356 0.6459 -0.2079 0.0288  0.2445  252 ALA B O   
3546 C CB  . ALA B 126 ? 0.8467 0.6286 0.6472 -0.2171 0.0037  0.2430  252 ALA B CB  
3547 N N   . GLY B 127 ? 0.7687 0.6585 0.5731 -0.1613 0.0228  0.2261  253 GLY B N   
3548 C CA  . GLY B 127 ? 0.7261 0.6741 0.5328 -0.1608 0.0349  0.2226  253 GLY B CA  
3549 C C   . GLY B 127 ? 0.6794 0.6689 0.5106 -0.1589 0.0447  0.1992  253 GLY B C   
3550 O O   . GLY B 127 ? 0.7096 0.7448 0.5420 -0.1617 0.0579  0.1960  253 GLY B O   
3551 N N   . ARG B 128 ? 0.6797 0.6534 0.5282 -0.1532 0.0393  0.1829  254 ARG B N   
3552 C CA  . ARG B 128 ? 0.6335 0.6455 0.5062 -0.1488 0.0474  0.1630  254 ARG B CA  
3553 C C   . ARG B 128 ? 0.6173 0.6486 0.4875 -0.1272 0.0518  0.1459  254 ARG B C   
3554 O O   . ARG B 128 ? 0.6361 0.6981 0.5231 -0.1222 0.0605  0.1303  254 ARG B O   
3555 C CB  . ARG B 128 ? 0.6416 0.6318 0.5303 -0.1503 0.0385  0.1522  254 ARG B CB  
3556 C CG  . ARG B 128 ? 0.6774 0.6655 0.5766 -0.1774 0.0355  0.1646  254 ARG B CG  
3557 C CD  . ARG B 128 ? 0.6702 0.6314 0.5778 -0.1798 0.0235  0.1529  254 ARG B CD  
3558 N NE  . ARG B 128 ? 0.7129 0.6082 0.5948 -0.1778 0.0113  0.1550  254 ARG B NE  
3559 C CZ  . ARG B 128 ? 0.7625 0.6216 0.6395 -0.1763 0.0010  0.1427  254 ARG B CZ  
3560 N NH1 . ARG B 128 ? 0.7095 0.5931 0.6059 -0.1770 -0.0009 0.1289  254 ARG B NH1 
3561 N NH2 . ARG B 128 ? 0.7898 0.5851 0.6398 -0.1729 -0.0072 0.1445  254 ARG B NH2 
3562 N N   . GLY B 129 ? 0.6157 0.6301 0.4667 -0.1148 0.0455  0.1494  255 GLY B N   
3563 C CA  . GLY B 129 ? 0.5915 0.6253 0.4391 -0.0991 0.0478  0.1347  255 GLY B CA  
3564 C C   . GLY B 129 ? 0.5828 0.6015 0.4429 -0.0830 0.0411  0.1180  255 GLY B C   
3565 O O   . GLY B 129 ? 0.5752 0.5688 0.4454 -0.0824 0.0355  0.1152  255 GLY B O   
3566 N N   . ILE B 130 ? 0.5649 0.5997 0.4218 -0.0716 0.0417  0.1065  256 ILE B N   
3567 C CA  . ILE B 130 ? 0.5256 0.5489 0.3920 -0.0567 0.0353  0.0942  256 ILE B CA  
3568 C C   . ILE B 130 ? 0.4947 0.5242 0.3806 -0.0555 0.0398  0.0768  256 ILE B C   
3569 O O   . ILE B 130 ? 0.5372 0.5538 0.4309 -0.0455 0.0346  0.0683  256 ILE B O   
3570 C CB  . ILE B 130 ? 0.5547 0.5944 0.4116 -0.0484 0.0323  0.0907  256 ILE B CB  
3571 C CG1 . ILE B 130 ? 0.5632 0.6299 0.4168 -0.0538 0.0419  0.0760  256 ILE B CG1 
3572 C CG2 . ILE B 130 ? 0.5298 0.5683 0.3684 -0.0493 0.0258  0.1111  256 ILE B CG2 
3573 C CD1 . ILE B 130 ? 0.5817 0.6635 0.4202 -0.0521 0.0377  0.0721  256 ILE B CD1 
3574 N N   . TYR B 131 ? 0.5093 0.5604 0.4040 -0.0642 0.0497  0.0728  257 TYR B N   
3575 C CA  . TYR B 131 ? 0.5086 0.5689 0.4244 -0.0610 0.0533  0.0590  257 TYR B CA  
3576 C C   . TYR B 131 ? 0.4578 0.5115 0.3892 -0.0707 0.0500  0.0650  257 TYR B C   
3577 O O   . TYR B 131 ? 0.5243 0.5681 0.4673 -0.0669 0.0440  0.0578  257 TYR B O   
3578 C CB  . TYR B 131 ? 0.5002 0.5904 0.4192 -0.0604 0.0674  0.0498  257 TYR B CB  
3579 C CG  . TYR B 131 ? 0.4966 0.5902 0.3957 -0.0546 0.0693  0.0412  257 TYR B CG  
3580 C CD1 . TYR B 131 ? 0.4672 0.5484 0.3649 -0.0458 0.0609  0.0327  257 TYR B CD1 
3581 C CD2 . TYR B 131 ? 0.5032 0.6137 0.3829 -0.0603 0.0791  0.0421  257 TYR B CD2 
3582 C CE1 . TYR B 131 ? 0.4872 0.5730 0.3670 -0.0448 0.0603  0.0259  257 TYR B CE1 
3583 C CE2 . TYR B 131 ? 0.5140 0.6259 0.3710 -0.0586 0.0786  0.0335  257 TYR B CE2 
3584 C CZ  . TYR B 131 ? 0.4997 0.5994 0.3580 -0.0518 0.0682  0.0256  257 TYR B CZ  
3585 O OH  . TYR B 131 ? 0.5327 0.6354 0.3691 -0.0541 0.0654  0.0181  257 TYR B OH  
3586 N N   . GLU B 132 ? 0.5113 0.5716 0.4419 -0.0855 0.0531  0.0789  258 GLU B N   
3587 C CA  . GLU B 132 ? 0.5397 0.5971 0.4853 -0.0999 0.0485  0.0860  258 GLU B CA  
3588 C C   . GLU B 132 ? 0.5864 0.5984 0.5167 -0.1061 0.0353  0.0936  258 GLU B C   
3589 O O   . GLU B 132 ? 0.6060 0.6037 0.5433 -0.1163 0.0271  0.0936  258 GLU B O   
3590 C CB  . GLU B 132 ? 0.4981 0.5875 0.4524 -0.1159 0.0589  0.0990  258 GLU B CB  
3591 N N   . GLY B 133 ? 0.5857 0.5734 0.4939 -0.0996 0.0326  0.1000  259 GLY B N   
3592 C CA  . GLY B 133 ? 0.5854 0.5254 0.4769 -0.1027 0.0225  0.1086  259 GLY B CA  
3593 C C   . GLY B 133 ? 0.5686 0.4807 0.4523 -0.0826 0.0169  0.0975  259 GLY B C   
3594 O O   . GLY B 133 ? 0.5604 0.4929 0.4517 -0.0683 0.0199  0.0853  259 GLY B O   
3595 N N   . PRO B 134 ? 0.6042 0.4678 0.4716 -0.0814 0.0096  0.1016  260 PRO B N   
3596 C CA  . PRO B 134 ? 0.5916 0.4292 0.4515 -0.0608 0.0068  0.0906  260 PRO B CA  
3597 C C   . PRO B 134 ? 0.6207 0.4709 0.4787 -0.0400 0.0096  0.0947  260 PRO B C   
3598 O O   . PRO B 134 ? 0.6331 0.4983 0.4879 -0.0418 0.0108  0.1084  260 PRO B O   
3599 C CB  . PRO B 134 ? 0.6693 0.4468 0.5079 -0.0655 0.0004  0.0949  260 PRO B CB  
3600 C CG  . PRO B 134 ? 0.6403 0.4112 0.4736 -0.0853 -0.0010 0.1134  260 PRO B CG  
3601 C CD  . PRO B 134 ? 0.6473 0.4748 0.5017 -0.1001 0.0043  0.1151  260 PRO B CD  
3602 N N   . GLY B 135 ? 0.5766 0.4242 0.4368 -0.0214 0.0100  0.0834  261 GLY B N   
3603 C CA  . GLY B 135 ? 0.6190 0.4802 0.4808 -0.0015 0.0110  0.0880  261 GLY B CA  
3604 C C   . GLY B 135 ? 0.6166 0.4459 0.4717 0.0190  0.0112  0.0837  261 GLY B C   
3605 O O   . GLY B 135 ? 0.5766 0.3687 0.4206 0.0168  0.0107  0.0750  261 GLY B O   
3606 N N   . ILE B 136 ? 0.6011 0.4472 0.4622 0.0387  0.0122  0.0902  262 ILE B N   
3607 C CA  . ILE B 136 ? 0.5932 0.4181 0.4519 0.0627  0.0157  0.0873  262 ILE B CA  
3608 C C   . ILE B 136 ? 0.5786 0.4485 0.4553 0.0727  0.0187  0.0807  262 ILE B C   
3609 O O   . ILE B 136 ? 0.5235 0.4361 0.4122 0.0642  0.0161  0.0832  262 ILE B O   
3610 C CB  . ILE B 136 ? 0.6084 0.4095 0.4607 0.0809  0.0145  0.1062  262 ILE B CB  
3611 C CG1 . ILE B 136 ? 0.6441 0.4020 0.4862 0.1050  0.0209  0.1002  262 ILE B CG1 
3612 C CG2 . ILE B 136 ? 0.6271 0.4780 0.4964 0.0903  0.0115  0.1213  262 ILE B CG2 
3613 C CD1 . ILE B 136 ? 0.7225 0.4556 0.5614 0.1294  0.0214  0.1193  262 ILE B CD1 
3614 N N   . SER B 137 ? 0.5430 0.4007 0.4186 0.0886  0.0246  0.0712  263 SER B N   
3615 C CA  . SER B 137 ? 0.5090 0.4069 0.4016 0.0997  0.0286  0.0677  263 SER B CA  
3616 C C   . SER B 137 ? 0.5913 0.4791 0.4856 0.1290  0.0355  0.0742  263 SER B C   
3617 O O   . SER B 137 ? 0.6070 0.4446 0.4823 0.1401  0.0402  0.0705  263 SER B O   
3618 C CB  . SER B 137 ? 0.5281 0.4285 0.4191 0.0902  0.0315  0.0498  263 SER B CB  
3619 O OG  . SER B 137 ? 0.5343 0.4442 0.4269 0.0670  0.0262  0.0452  263 SER B OG  
3620 N N   . ILE B 138 ? 0.5433 0.4784 0.4599 0.1414  0.0365  0.0840  264 ILE B N   
3621 C CA  . ILE B 138 ? 0.6082 0.5457 0.5338 0.1726  0.0443  0.0934  264 ILE B CA  
3622 C C   . ILE B 138 ? 0.5335 0.5211 0.4804 0.1790  0.0504  0.0907  264 ILE B C   
3623 O O   . ILE B 138 ? 0.4839 0.5113 0.4428 0.1592  0.0446  0.0886  264 ILE B O   
3624 C CB  . ILE B 138 ? 0.5936 0.5451 0.5307 0.1846  0.0376  0.1177  264 ILE B CB  
3625 C CG1 . ILE B 138 ? 0.5391 0.5566 0.4987 0.1711  0.0276  0.1286  264 ILE B CG1 
3626 C CG2 . ILE B 138 ? 0.6336 0.5375 0.5486 0.1734  0.0309  0.1229  264 ILE B CG2 
3627 C CD1 . ILE B 138 ? 0.5079 0.5488 0.4800 0.1829  0.0190  0.1550  264 ILE B CD1 
3628 N N   . LYS B 139 ? 0.5288 0.5113 0.4785 0.2063  0.0633  0.0904  265 LYS B N   
3629 C CA  . LYS B 139 ? 0.5328 0.5688 0.5064 0.2155  0.0710  0.0927  265 LYS B CA  
3630 C C   . LYS B 139 ? 0.5558 0.6316 0.5584 0.2407  0.0716  0.1162  265 LYS B C   
3631 O O   . LYS B 139 ? 0.6156 0.6601 0.6134 0.2686  0.0783  0.1234  265 LYS B O   
3632 C CB  . LYS B 139 ? 0.6098 0.6203 0.5666 0.2284  0.0874  0.0759  265 LYS B CB  
3633 C CG  . LYS B 139 ? 0.6168 0.5901 0.5450 0.2029  0.0843  0.0549  265 LYS B CG  
3634 C CD  . LYS B 139 ? 0.6286 0.5793 0.5355 0.2134  0.0993  0.0388  265 LYS B CD  
3635 C CE  . LYS B 139 ? 0.6432 0.5543 0.5202 0.1880  0.0928  0.0208  265 LYS B CE  
3636 N NZ  . LYS B 139 ? 0.6088 0.5522 0.5006 0.1587  0.0797  0.0222  265 LYS B NZ  
3637 N N   . LEU B 140 ? 0.5220 0.6651 0.5540 0.2302  0.0635  0.1292  266 LEU B N   
3638 C CA  . LEU B 140 ? 0.4974 0.6892 0.5613 0.2510  0.0605  0.1549  266 LEU B CA  
3639 C C   . LEU B 140 ? 0.5824 0.7853 0.6628 0.2899  0.0797  0.1604  266 LEU B C   
3640 O O   . LEU B 140 ? 0.5645 0.7906 0.6682 0.3172  0.0802  0.1823  266 LEU B O   
3641 C CB  . LEU B 140 ? 0.5071 0.7705 0.5971 0.2271  0.0471  0.1658  266 LEU B CB  
3642 C CG  . LEU B 140 ? 0.4900 0.7465 0.5636 0.1921  0.0292  0.1619  266 LEU B CG  
3643 C CD1 . LEU B 140 ? 0.4827 0.8025 0.5763 0.1673  0.0173  0.1683  266 LEU B CD1 
3644 C CD2 . LEU B 140 ? 0.5077 0.7443 0.5728 0.1987  0.0193  0.1770  266 LEU B CD2 
3645 N N   . SER B 141 ? 0.5893 0.7773 0.6578 0.2946  0.0963  0.1420  267 SER B N   
3646 C CA  . SER B 141 ? 0.5738 0.7704 0.6537 0.3333  0.1182  0.1448  267 SER B CA  
3647 C C   . SER B 141 ? 0.6418 0.7671 0.6974 0.3653  0.1283  0.1413  267 SER B C   
3648 O O   . SER B 141 ? 0.6964 0.8201 0.7563 0.3891  0.1427  0.1424  267 SER B O   
3649 C CB  . SER B 141 ? 0.5954 0.7934 0.6626 0.3270  0.1336  0.1254  267 SER B CB  
3650 O OG  . SER B 141 ? 0.6165 0.7386 0.6371 0.3153  0.1352  0.1006  267 SER B OG  
3651 N N   . ALA B 142 ? 0.7009 0.7606 0.7237 0.3496  0.1172  0.1327  268 ALA B N   
3652 C CA  . ALA B 142 ? 0.7775 0.7641 0.7757 0.3753  0.1235  0.1319  268 ALA B CA  
3653 C C   . ALA B 142 ? 0.7463 0.7517 0.7687 0.3884  0.1135  0.1588  268 ALA B C   
3654 O O   . ALA B 142 ? 0.8036 0.7637 0.8148 0.4088  0.1200  0.1598  268 ALA B O   
3655 C CB  . ALA B 142 ? 0.7787 0.6918 0.7338 0.3463  0.1135  0.1140  268 ALA B CB  
3656 N N   . LEU B 143 ? 0.6846 0.7551 0.7376 0.3746  0.0967  0.1799  269 LEU B N   
3657 C CA  . LEU B 143 ? 0.7039 0.7890 0.7731 0.3790  0.0826  0.2055  269 LEU B CA  
3658 C C   . LEU B 143 ? 0.7101 0.8686 0.8219 0.3931  0.0837  0.2248  269 LEU B C   
3659 O O   . LEU B 143 ? 0.6896 0.8634 0.8165 0.3992  0.0726  0.2469  269 LEU B O   
3660 C CB  . LEU B 143 ? 0.6560 0.7591 0.7222 0.3473  0.0602  0.2154  269 LEU B CB  
3661 C CG  . LEU B 143 ? 0.7142 0.7435 0.7366 0.3208  0.0561  0.1955  269 LEU B CG  
3662 C CD1 . LEU B 143 ? 0.6587 0.7140 0.6774 0.2811  0.0366  0.1991  269 LEU B CD1 
3663 C CD2 . LEU B 143 ? 0.7785 0.7346 0.7790 0.3429  0.0592  0.2027  269 LEU B CD2 
3664 N N   . HIS B 144 ? 0.6882 0.8929 0.8190 0.3971  0.0966  0.2184  270 HIS B N   
3665 C CA  . HIS B 144 ? 0.7075 0.9795 0.8780 0.4110  0.0995  0.2374  270 HIS B CA  
3666 C C   . HIS B 144 ? 0.7429 1.0088 0.9126 0.4340  0.1248  0.2240  270 HIS B C   
3667 O O   . HIS B 144 ? 0.7293 0.9860 0.8827 0.4246  0.1354  0.2036  270 HIS B O   
3668 C CB  . HIS B 144 ? 0.6628 1.0221 0.8654 0.3834  0.0843  0.2514  270 HIS B CB  
3669 C CG  . HIS B 144 ? 0.6770 1.1045 0.9198 0.3932  0.0815  0.2759  270 HIS B CG  
3670 N ND1 . HIS B 144 ? 0.7143 1.1822 0.9797 0.4075  0.0981  0.2774  270 HIS B ND1 
3671 C CD2 . HIS B 144 ? 0.7050 1.1666 0.9682 0.3913  0.0642  0.3009  270 HIS B CD2 
3672 C CE1 . HIS B 144 ? 0.6985 1.2243 0.9991 0.4145  0.0912  0.3029  270 HIS B CE1 
3673 N NE2 . HIS B 144 ? 0.6819 1.2049 0.9816 0.4046  0.0702  0.3172  270 HIS B NE2 
3674 N N   . PRO B 145 ? 0.7552 1.0259 0.9407 0.4643  0.1352  0.2350  271 PRO B N   
3675 C CA  . PRO B 145 ? 0.7892 1.0616 0.9750 0.4864  0.1599  0.2237  271 PRO B CA  
3676 C C   . PRO B 145 ? 0.7585 1.1169 0.9766 0.4720  0.1618  0.2312  271 PRO B C   
3677 O O   . PRO B 145 ? 0.7559 1.1843 1.0095 0.4581  0.1462  0.2539  271 PRO B O   
3678 C CB  . PRO B 145 ? 0.8210 1.0866 1.0225 0.5219  0.1667  0.2391  271 PRO B CB  
3679 C CG  . PRO B 145 ? 0.7921 1.1004 1.0224 0.5123  0.1430  0.2674  271 PRO B CG  
3680 C CD  . PRO B 145 ? 0.7476 1.0287 0.9536 0.4796  0.1245  0.2600  271 PRO B CD  
3681 N N   . ARG B 146 ? 0.7691 1.1200 0.9719 0.4728  0.1800  0.2119  272 ARG B N   
3682 C CA  . ARG B 146 ? 0.8221 1.2457 1.0492 0.4548  0.1824  0.2164  272 ARG B CA  
3683 C C   . ARG B 146 ? 0.7837 1.2515 1.0260 0.4169  0.1583  0.2262  272 ARG B C   
3684 O O   . ARG B 146 ? 0.7492 1.2919 1.0283 0.4031  0.1478  0.2469  272 ARG B O   
3685 C CB  . ARG B 146 ? 0.8258 1.3138 1.0927 0.4758  0.1923  0.2370  272 ARG B CB  
3686 N N   . TYR B 147 ? 0.7706 1.1894 0.9829 0.3993  0.1490  0.2107  273 TYR B N   
3687 C CA  . TYR B 147 ? 0.7074 1.1597 0.9293 0.3642  0.1266  0.2170  273 TYR B CA  
3688 C C   . TYR B 147 ? 0.7133 1.2274 0.9542 0.3389  0.1266  0.2182  273 TYR B C   
3689 O O   . TYR B 147 ? 0.6696 1.2415 0.9357 0.3134  0.1086  0.2339  273 TYR B O   
3690 C CB  . TYR B 147 ? 0.6399 1.0258 0.8246 0.3535  0.1211  0.1978  273 TYR B CB  
3691 C CG  . TYR B 147 ? 0.5810 0.9943 0.7703 0.3181  0.1011  0.1990  273 TYR B CG  
3692 C CD1 . TYR B 147 ? 0.5919 1.0367 0.7972 0.3032  0.0783  0.2178  273 TYR B CD1 
3693 C CD2 . TYR B 147 ? 0.5570 0.9577 0.7283 0.2959  0.1042  0.1793  273 TYR B CD2 
3694 C CE1 . TYR B 147 ? 0.5140 0.9721 0.7132 0.2649  0.0593  0.2140  273 TYR B CE1 
3695 C CE2 . TYR B 147 ? 0.5156 0.9210 0.6785 0.2537  0.0843  0.1742  273 TYR B CE2 
3696 C CZ  . TYR B 147 ? 0.5097 0.9428 0.6856 0.2386  0.0630  0.1902  273 TYR B CZ  
3697 O OH  . TYR B 147 ? 0.4672 0.9004 0.6302 0.1982  0.0455  0.1826  273 TYR B OH  
3698 N N   . SER B 148 ? 0.7821 1.2826 1.0082 0.3434  0.1457  0.2020  274 SER B N   
3699 C CA  . SER B 148 ? 0.7701 1.3218 1.0101 0.3186  0.1469  0.2030  274 SER B CA  
3700 C C   . SER B 148 ? 0.8285 1.4492 1.1055 0.3250  0.1518  0.2239  274 SER B C   
3701 O O   . SER B 148 ? 0.8235 1.4902 1.1145 0.3024  0.1514  0.2281  274 SER B O   
3702 C CB  . SER B 148 ? 0.7941 1.3030 1.0004 0.3194  0.1650  0.1785  274 SER B CB  
3703 N N   . ARG B 149 ? 0.8908 1.5199 1.1846 0.3543  0.1561  0.2381  275 ARG B N   
3704 C CA  . ARG B 149 ? 0.9029 1.5968 1.2326 0.3659  0.1639  0.2581  275 ARG B CA  
3705 C C   . ARG B 149 ? 0.9268 1.6742 1.2923 0.3628  0.1453  0.2861  275 ARG B C   
3706 O O   . ARG B 149 ? 0.8890 1.7077 1.2873 0.3488  0.1400  0.3051  275 ARG B O   
3707 C CB  . ARG B 149 ? 0.9092 1.5718 1.2293 0.4083  0.1906  0.2505  275 ARG B CB  
3708 N N   . ALA B 150 ? 0.8856 1.6004 1.2445 0.3740  0.1347  0.2901  276 ALA B N   
3709 C CA  . ALA B 150 ? 0.8523 1.6160 1.2419 0.3701  0.1159  0.3170  276 ALA B CA  
3710 C C   . ALA B 150 ? 0.8905 1.6927 1.2858 0.3235  0.0897  0.3235  276 ALA B C   
3711 O O   . ALA B 150 ? 0.8907 1.6684 1.2632 0.2977  0.0846  0.3058  276 ALA B O   
3712 C CB  . ALA B 150 ? 0.7911 1.5041 1.1684 0.3941  0.1117  0.3196  276 ALA B CB  
3713 N N   . GLN B 151 ? 0.9479 1.8096 1.3728 0.3126  0.0727  0.3489  277 GLN B N   
3714 C CA  . GLN B 151 ? 0.9740 1.8747 1.4030 0.2665  0.0472  0.3558  277 GLN B CA  
3715 C C   . GLN B 151 ? 0.9914 1.8459 1.3909 0.2493  0.0293  0.3454  277 GLN B C   
3716 O O   . GLN B 151 ? 1.0145 1.8134 1.3952 0.2735  0.0343  0.3379  277 GLN B O   
3717 C CB  . GLN B 151 ? 0.8942 1.8682 1.3595 0.2600  0.0337  0.3860  277 GLN B CB  
3718 N N   . ALA B 152 ? 0.7902 1.6665 1.1837 0.2056  0.0080  0.3446  278 ALA B N   
3719 C CA  . ALA B 152 ? 0.7545 1.5952 1.1198 0.1847  -0.0107 0.3356  278 ALA B CA  
3720 C C   . ALA B 152 ? 0.7245 1.5822 1.0954 0.1844  -0.0290 0.3558  278 ALA B C   
3721 O O   . ALA B 152 ? 0.7197 1.5429 1.0647 0.1737  -0.0425 0.3500  278 ALA B O   
3722 C CB  . ALA B 152 ? 0.6851 1.5359 1.0366 0.1373  -0.0254 0.3239  278 ALA B CB  
3723 N N   . ALA B 153 ? 0.6596 1.5708 1.0631 0.1954  -0.0300 0.3801  279 ALA B N   
3724 C CA  . ALA B 153 ? 0.6957 1.6234 1.1069 0.2002  -0.0458 0.4014  279 ALA B CA  
3725 C C   . ALA B 153 ? 0.7294 1.5984 1.1277 0.2389  -0.0358 0.3990  279 ALA B C   
3726 O O   . ALA B 153 ? 0.7236 1.5556 1.0958 0.2309  -0.0489 0.3959  279 ALA B O   
3727 C CB  . ALA B 153 ? 0.5319 1.5322 0.9850 0.2078  -0.0467 0.4291  279 ALA B CB  
3728 N N   . ARG B 154 ? 0.7677 1.6242 1.1808 0.2799  -0.0122 0.3997  280 ARG B N   
3729 C CA  . ARG B 154 ? 0.7920 1.5859 1.1910 0.3175  -0.0013 0.3966  280 ARG B CA  
3730 C C   . ARG B 154 ? 0.7871 1.5055 1.1461 0.3152  0.0052  0.3691  280 ARG B C   
3731 O O   . ARG B 154 ? 0.8045 1.4634 1.1425 0.3343  0.0069  0.3662  280 ARG B O   
3732 C CB  . ARG B 154 ? 0.8085 1.6067 1.2309 0.3608  0.0231  0.4023  280 ARG B CB  
3733 N N   . VAL B 155 ? 0.8586 1.5773 1.2064 0.2918  0.0084  0.3500  281 VAL B N   
3734 C CA  . VAL B 155 ? 0.9209 1.5747 1.2320 0.2855  0.0113  0.3258  281 VAL B CA  
3735 C C   . VAL B 155 ? 0.9453 1.5837 1.2342 0.2601  -0.0123 0.3283  281 VAL B C   
3736 O O   . VAL B 155 ? 0.9594 1.5400 1.2234 0.2722  -0.0128 0.3247  281 VAL B O   
3737 C CB  . VAL B 155 ? 0.9043 1.5678 1.2116 0.2656  0.0190  0.3068  281 VAL B CB  
3738 N N   . MET B 156 ? 0.8573 1.5445 1.1512 0.2227  -0.0321 0.3345  282 MET B N   
3739 C CA  . MET B 156 ? 0.8184 1.4931 1.0864 0.1957  -0.0543 0.3357  282 MET B CA  
3740 C C   . MET B 156 ? 0.8317 1.4914 1.0980 0.2149  -0.0610 0.3548  282 MET B C   
3741 O O   . MET B 156 ? 0.8596 1.4714 1.0953 0.2124  -0.0673 0.3512  282 MET B O   
3742 C CB  . MET B 156 ? 0.8224 1.5527 1.0955 0.1532  -0.0735 0.3397  282 MET B CB  
3743 C CG  . MET B 156 ? 0.8421 1.5506 1.0773 0.1169  -0.0916 0.3276  282 MET B CG  
3744 S SD  . MET B 156 ? 0.8503 1.5166 1.0592 0.1029  -0.0835 0.2965  282 MET B SD  
3745 C CE  . MET B 156 ? 0.6747 1.3403 0.8457 0.0519  -0.1073 0.2858  282 MET B CE  
3746 N N   . GLY B 157 ? 0.7571 1.4567 1.0560 0.2346  -0.0593 0.3765  283 GLY B N   
3747 C CA  . GLY B 157 ? 0.7994 1.4921 1.1001 0.2507  -0.0683 0.3977  283 GLY B CA  
3748 C C   . GLY B 157 ? 0.7773 1.3976 1.0619 0.2862  -0.0548 0.3942  283 GLY B C   
3749 O O   . GLY B 157 ? 0.7714 1.3691 1.0453 0.2929  -0.0650 0.4084  283 GLY B O   
3750 N N   . GLU B 158 ? 0.7487 1.3297 1.0291 0.3077  -0.0324 0.3756  284 GLU B N   
3751 C CA  . GLU B 158 ? 0.7656 1.2684 1.0248 0.3379  -0.0190 0.3685  284 GLU B CA  
3752 C C   . GLU B 158 ? 0.7699 1.2102 0.9911 0.3263  -0.0140 0.3437  284 GLU B C   
3753 O O   . GLU B 158 ? 0.7785 1.1507 0.9722 0.3367  -0.0121 0.3406  284 GLU B O   
3754 C CB  . GLU B 158 ? 0.7991 1.2952 1.0785 0.3771  0.0051  0.3665  284 GLU B CB  
3755 N N   . LEU B 159 ? 0.7359 1.1970 0.9547 0.3041  -0.0124 0.3272  285 LEU B N   
3756 C CA  . LEU B 159 ? 0.7481 1.1549 0.9326 0.2926  -0.0090 0.3054  285 LEU B CA  
3757 C C   . LEU B 159 ? 0.6710 1.0706 0.8295 0.2613  -0.0300 0.3091  285 LEU B C   
3758 O O   . LEU B 159 ? 0.6842 1.0224 0.8105 0.2611  -0.0295 0.3032  285 LEU B O   
3759 C CB  . LEU B 159 ? 0.6906 1.1213 0.8823 0.2817  0.0005  0.2870  285 LEU B CB  
3760 C CG  . LEU B 159 ? 0.6151 0.9917 0.7759 0.2747  0.0087  0.2619  285 LEU B CG  
3761 C CD1 . LEU B 159 ? 0.6166 0.9118 0.7510 0.3000  0.0215  0.2543  285 LEU B CD1 
3762 C CD2 . LEU B 159 ? 0.5516 0.9522 0.7256 0.2730  0.0234  0.2460  285 LEU B CD2 
3763 N N   . LEU B 160 ? 0.6324 1.0918 0.8008 0.2325  -0.0479 0.3181  286 LEU B N   
3764 C CA  . LEU B 160 ? 0.6525 1.1060 0.7905 0.1999  -0.0665 0.3185  286 LEU B CA  
3765 C C   . LEU B 160 ? 0.6914 1.0991 0.8073 0.2089  -0.0712 0.3314  286 LEU B C   
3766 O O   . LEU B 160 ? 0.6761 1.0413 0.7563 0.1937  -0.0737 0.3233  286 LEU B O   
3767 C CB  . LEU B 160 ? 0.6629 1.1838 0.8128 0.1691  -0.0846 0.3265  286 LEU B CB  
3768 N N   . PRO B 161 ? 0.6393 1.0518 0.7733 0.2322  -0.0722 0.3518  287 PRO B N   
3769 C CA  . PRO B 161 ? 0.6894 1.0482 0.8000 0.2415  -0.0755 0.3634  287 PRO B CA  
3770 C C   . PRO B 161 ? 0.7094 0.9884 0.7957 0.2570  -0.0598 0.3493  287 PRO B C   
3771 O O   . PRO B 161 ? 0.6911 0.9217 0.7456 0.2477  -0.0642 0.3525  287 PRO B O   
3772 C CB  . PRO B 161 ? 0.7180 1.0989 0.8592 0.2693  -0.0767 0.3864  287 PRO B CB  
3773 C CG  . PRO B 161 ? 0.6595 1.1223 0.8338 0.2582  -0.0833 0.3919  287 PRO B CG  
3774 C CD  . PRO B 161 ? 0.6568 1.1276 0.8319 0.2468  -0.0729 0.3680  287 PRO B CD  
3775 N N   . ARG B 162 ? 0.7115 0.9745 0.8093 0.2779  -0.0412 0.3334  288 ARG B N   
3776 C CA  . ARG B 162 ? 0.6553 0.8378 0.7272 0.2917  -0.0262 0.3183  288 ARG B CA  
3777 C C   . ARG B 162 ? 0.6942 0.8521 0.7351 0.2628  -0.0271 0.3002  288 ARG B C   
3778 O O   . ARG B 162 ? 0.6817 0.7744 0.6910 0.2543  -0.0243 0.2924  288 ARG B O   
3779 C CB  . ARG B 162 ? 0.7618 0.9338 0.8508 0.3216  -0.0050 0.3042  288 ARG B CB  
3780 N N   . VAL B 163 ? 0.6238 0.8283 0.6723 0.2378  -0.0295 0.2843  289 VAL B N   
3781 C CA  . VAL B 163 ? 0.6463 0.8261 0.6666 0.2025  -0.0284 0.2571  289 VAL B CA  
3782 C C   . VAL B 163 ? 0.6381 0.8219 0.6355 0.1749  -0.0434 0.2664  289 VAL B C   
3783 O O   . VAL B 163 ? 0.5690 0.7136 0.5382 0.1536  -0.0406 0.2511  289 VAL B O   
3784 C CB  . VAL B 163 ? 0.5992 0.8212 0.6336 0.1867  -0.0256 0.2381  289 VAL B CB  
3785 C CG1 . VAL B 163 ? 0.5423 0.7388 0.5498 0.1537  -0.0241 0.2115  289 VAL B CG1 
3786 C CG2 . VAL B 163 ? 0.5783 0.7964 0.6319 0.2139  -0.0086 0.2296  289 VAL B CG2 
3787 N N   . LYS B 164 ? 0.5876 0.8212 0.5962 0.1743  -0.0593 0.2925  290 LYS B N   
3788 C CA  . LYS B 164 ? 0.5639 0.7993 0.5448 0.1485  -0.0727 0.3019  290 LYS B CA  
3789 C C   . LYS B 164 ? 0.6076 0.7814 0.5653 0.1561  -0.0695 0.3125  290 LYS B C   
3790 O O   . LYS B 164 ? 0.6359 0.7845 0.5632 0.1309  -0.0695 0.3045  290 LYS B O   
3791 C CB  . LYS B 164 ? 0.6390 0.9381 0.6340 0.1446  -0.0917 0.3272  290 LYS B CB  
3792 C CG  . LYS B 164 ? 0.6413 0.9408 0.6028 0.1151  -0.1037 0.3321  290 LYS B CG  
3793 C CD  . LYS B 164 ? 0.6250 0.9769 0.5988 0.1066  -0.1201 0.3473  290 LYS B CD  
3794 C CE  . LYS B 164 ? 0.6840 1.0226 0.6239 0.0881  -0.1296 0.3579  290 LYS B CE  
3795 N NZ  . LYS B 164 ? 0.6908 1.0830 0.6363 0.0731  -0.1467 0.3692  290 LYS B NZ  
3796 N N   . ALA B 165 ? 0.6338 0.7817 0.6053 0.1908  -0.0658 0.3310  291 ALA B N   
3797 C CA  . ALA B 165 ? 0.6913 0.7707 0.6393 0.1977  -0.0624 0.3406  291 ALA B CA  
3798 C C   . ALA B 165 ? 0.7017 0.7243 0.6266 0.1806  -0.0488 0.3098  291 ALA B C   
3799 O O   . ALA B 165 ? 0.7092 0.6966 0.6065 0.1601  -0.0499 0.3108  291 ALA B O   
3800 C CB  . ALA B 165 ? 0.7331 0.7834 0.7000 0.2344  -0.0569 0.3502  291 ALA B CB  
3801 N N   . LEU B 166 ? 0.6858 0.7026 0.6223 0.1880  -0.0362 0.2840  292 LEU B N   
3802 C CA  . LEU B 166 ? 0.6895 0.6612 0.6065 0.1703  -0.0256 0.2552  292 LEU B CA  
3803 C C   . LEU B 166 ? 0.6693 0.6642 0.5717 0.1330  -0.0300 0.2435  292 LEU B C   
3804 O O   . LEU B 166 ? 0.6497 0.6084 0.5305 0.1139  -0.0268 0.2357  292 LEU B O   
3805 C CB  . LEU B 166 ? 0.6554 0.6278 0.5872 0.1837  -0.0131 0.2316  292 LEU B CB  
3806 C CG  . LEU B 166 ? 0.7360 0.6753 0.6766 0.2224  -0.0034 0.2372  292 LEU B CG  
3807 C CD1 . LEU B 166 ? 0.6857 0.6250 0.6345 0.2326  0.0107  0.2124  292 LEU B CD1 
3808 C CD2 . LEU B 166 ? 0.7932 0.6532 0.7066 0.2272  -0.0010 0.2418  292 LEU B CD2 
3809 N N   . ALA B 167 ? 0.6047 0.6600 0.5182 0.1221  -0.0368 0.2421  293 ALA B N   
3810 C CA  . ALA B 167 ? 0.6612 0.7364 0.5580 0.0895  -0.0394 0.2294  293 ALA B CA  
3811 C C   . ALA B 167 ? 0.6451 0.7108 0.5172 0.0748  -0.0459 0.2475  293 ALA B C   
3812 O O   . ALA B 167 ? 0.6410 0.6966 0.4934 0.0513  -0.0413 0.2360  293 ALA B O   
3813 C CB  . ALA B 167 ? 0.6533 0.7888 0.5625 0.0806  -0.0470 0.2259  293 ALA B CB  
3814 N N   . LEU B 168 ? 0.6444 0.7144 0.5178 0.0893  -0.0559 0.2778  294 LEU B N   
3815 C CA  . LEU B 168 ? 0.6906 0.7488 0.5381 0.0751  -0.0621 0.2982  294 LEU B CA  
3816 C C   . LEU B 168 ? 0.7160 0.7113 0.5477 0.0703  -0.0523 0.2945  294 LEU B C   
3817 O O   . LEU B 168 ? 0.7443 0.7332 0.5538 0.0452  -0.0497 0.2930  294 LEU B O   
3818 C CB  . LEU B 168 ? 0.6962 0.7708 0.5499 0.0937  -0.0762 0.3345  294 LEU B CB  
3819 C CG  . LEU B 168 ? 0.6982 0.8401 0.5535 0.0823  -0.0911 0.3438  294 LEU B CG  
3820 C CD1 . LEU B 168 ? 0.7506 0.9080 0.6262 0.1032  -0.1026 0.3670  294 LEU B CD1 
3821 C CD2 . LEU B 168 ? 0.7547 0.9047 0.5742 0.0484  -0.0936 0.3400  294 LEU B CD2 
3822 N N   . LEU B 169 ? 0.7267 0.6759 0.5687 0.0929  -0.0461 0.2922  295 LEU B N   
3823 C CA  . LEU B 169 ? 0.7119 0.5978 0.5373 0.0850  -0.0387 0.2875  295 LEU B CA  
3824 C C   . LEU B 169 ? 0.7181 0.6082 0.5375 0.0579  -0.0301 0.2596  295 LEU B C   
3825 O O   . LEU B 169 ? 0.7354 0.6061 0.5378 0.0354  -0.0277 0.2619  295 LEU B O   
3826 C CB  . LEU B 169 ? 0.7461 0.5796 0.5793 0.1134  -0.0327 0.2837  295 LEU B CB  
3827 C CG  . LEU B 169 ? 0.8357 0.6487 0.6754 0.1468  -0.0376 0.3113  295 LEU B CG  
3828 C CD1 . LEU B 169 ? 0.8664 0.6260 0.7101 0.1741  -0.0267 0.2974  295 LEU B CD1 
3829 C CD2 . LEU B 169 ? 0.8417 0.6206 0.6596 0.1394  -0.0457 0.3421  295 LEU B CD2 
3830 N N   . ALA B 170 ? 0.6944 0.6123 0.5298 0.0599  -0.0254 0.2351  296 ALA B N   
3831 C CA  . ALA B 170 ? 0.6519 0.5768 0.4848 0.0376  -0.0177 0.2102  296 ALA B CA  
3832 C C   . ALA B 170 ? 0.6343 0.5932 0.4535 0.0132  -0.0186 0.2137  296 ALA B C   
3833 O O   . ALA B 170 ? 0.6153 0.5661 0.4258 -0.0066 -0.0119 0.2062  296 ALA B O   
3834 C CB  . ALA B 170 ? 0.6047 0.5536 0.4562 0.0452  -0.0136 0.1868  296 ALA B CB  
3835 N N   . LYS B 171 ? 0.6371 0.6360 0.4532 0.0139  -0.0266 0.2255  297 LYS B N   
3836 C CA  . LYS B 171 ? 0.6417 0.6684 0.4367 -0.0087 -0.0270 0.2297  297 LYS B CA  
3837 C C   . LYS B 171 ? 0.6989 0.6985 0.4745 -0.0202 -0.0259 0.2504  297 LYS B C   
3838 O O   . LYS B 171 ? 0.6943 0.7022 0.4554 -0.0417 -0.0180 0.2457  297 LYS B O   
3839 C CB  . LYS B 171 ? 0.6489 0.7189 0.4390 -0.0072 -0.0391 0.2420  297 LYS B CB  
3840 C CG  . LYS B 171 ? 0.6359 0.7269 0.3950 -0.0292 -0.0409 0.2525  297 LYS B CG  
3841 C CD  . LYS B 171 ? 0.6485 0.7841 0.3976 -0.0327 -0.0548 0.2620  297 LYS B CD  
3842 C CE  . LYS B 171 ? 0.7397 0.8898 0.4510 -0.0543 -0.0565 0.2754  297 LYS B CE  
3843 N NZ  . LYS B 171 ? 0.7556 0.9422 0.4569 -0.0606 -0.0702 0.2775  297 LYS B NZ  
3844 N N   . ASN B 172 ? 0.6820 0.6489 0.4574 -0.0056 -0.0331 0.2744  298 ASN B N   
3845 C CA  . ASN B 172 ? 0.7182 0.6539 0.4740 -0.0178 -0.0334 0.2973  298 ASN B CA  
3846 C C   . ASN B 172 ? 0.7156 0.6220 0.4704 -0.0354 -0.0222 0.2832  298 ASN B C   
3847 O O   . ASN B 172 ? 0.7497 0.6522 0.4883 -0.0572 -0.0186 0.2954  298 ASN B O   
3848 C CB  . ASN B 172 ? 0.7778 0.6727 0.5351 0.0048  -0.0424 0.3235  298 ASN B CB  
3849 C CG  . ASN B 172 ? 0.8048 0.7347 0.5648 0.0213  -0.0557 0.3461  298 ASN B CG  
3850 O OD1 . ASN B 172 ? 0.8162 0.7983 0.5682 0.0091  -0.0605 0.3465  298 ASN B OD1 
3851 N ND2 . ASN B 172 ? 0.8474 0.7473 0.6170 0.0489  -0.0622 0.3662  298 ASN B ND2 
3852 N N   . TYR B 173 ? 0.6906 0.5784 0.4627 -0.0275 -0.0173 0.2598  299 TYR B N   
3853 C CA  . TYR B 173 ? 0.7056 0.5704 0.4796 -0.0449 -0.0094 0.2467  299 TYR B CA  
3854 C C   . TYR B 173 ? 0.6758 0.5827 0.4601 -0.0573 0.0000  0.2219  299 TYR B C   
3855 O O   . TYR B 173 ? 0.7115 0.6110 0.5015 -0.0725 0.0064  0.2122  299 TYR B O   
3856 C CB  . TYR B 173 ? 0.7606 0.5743 0.5425 -0.0302 -0.0105 0.2365  299 TYR B CB  
3857 C CG  . TYR B 173 ? 0.7680 0.5238 0.5362 -0.0205 -0.0169 0.2590  299 TYR B CG  
3858 C CD1 . TYR B 173 ? 0.8016 0.5195 0.5538 -0.0423 -0.0177 0.2740  299 TYR B CD1 
3859 C CD2 . TYR B 173 ? 0.7911 0.5294 0.5635 0.0108  -0.0214 0.2663  299 TYR B CD2 
3860 C CE1 . TYR B 173 ? 0.8647 0.5209 0.6014 -0.0339 -0.0237 0.2950  299 TYR B CE1 
3861 C CE2 . TYR B 173 ? 0.8367 0.5162 0.5961 0.0234  -0.0260 0.2870  299 TYR B CE2 
3862 C CZ  . TYR B 173 ? 0.8831 0.5182 0.6229 0.0006  -0.0275 0.3010  299 TYR B CZ  
3863 O OH  . TYR B 173 ? 0.9514 0.5204 0.6757 0.0125  -0.0323 0.3215  299 TYR B OH  
3864 N N   . ASP B 174 ? 0.6670 0.6167 0.4538 -0.0514 0.0002  0.2126  300 ASP B N   
3865 C CA  . ASP B 174 ? 0.5830 0.5672 0.3785 -0.0585 0.0091  0.1877  300 ASP B CA  
3866 C C   . ASP B 174 ? 0.6161 0.5839 0.4318 -0.0531 0.0125  0.1667  300 ASP B C   
3867 O O   . ASP B 174 ? 0.6417 0.6179 0.4655 -0.0651 0.0206  0.1545  300 ASP B O   
3868 C CB  . ASP B 174 ? 0.6469 0.6542 0.4312 -0.0804 0.0196  0.1894  300 ASP B CB  
3869 C CG  . ASP B 174 ? 0.6827 0.7283 0.4682 -0.0830 0.0286  0.1670  300 ASP B CG  
3870 O OD1 . ASP B 174 ? 0.6421 0.6998 0.4288 -0.0720 0.0233  0.1567  300 ASP B OD1 
3871 O OD2 . ASP B 174 ? 0.6302 0.6932 0.4159 -0.0957 0.0414  0.1603  300 ASP B OD2 
3872 N N   . ILE B 175 ? 0.6036 0.5515 0.4279 -0.0340 0.0066  0.1633  301 ILE B N   
3873 C CA  . ILE B 175 ? 0.5762 0.5096 0.4152 -0.0279 0.0090  0.1436  301 ILE B CA  
3874 C C   . ILE B 175 ? 0.5473 0.5058 0.3974 -0.0133 0.0080  0.1309  301 ILE B C   
3875 O O   . ILE B 175 ? 0.5159 0.4953 0.3638 -0.0054 0.0031  0.1398  301 ILE B O   
3876 C CB  . ILE B 175 ? 0.6154 0.4964 0.4507 -0.0197 0.0053  0.1483  301 ILE B CB  
3877 C CG1 . ILE B 175 ? 0.6380 0.5064 0.4716 0.0046  0.0001  0.1599  301 ILE B CG1 
3878 C CG2 . ILE B 175 ? 0.6563 0.5086 0.4789 -0.0383 0.0046  0.1631  301 ILE B CG2 
3879 C CD1 . ILE B 175 ? 0.6781 0.4947 0.5084 0.0201  0.0000  0.1559  301 ILE B CD1 
3880 N N   . GLY B 176 ? 0.5430 0.5007 0.4053 -0.0113 0.0116  0.1117  302 GLY B N   
3881 C CA  . GLY B 176 ? 0.4953 0.4730 0.3684 0.0006  0.0109  0.1008  302 GLY B CA  
3882 C C   . GLY B 176 ? 0.5223 0.4844 0.3991 0.0215  0.0071  0.1078  302 GLY B C   
3883 O O   . GLY B 176 ? 0.5343 0.4577 0.4053 0.0290  0.0072  0.1123  302 GLY B O   
3884 N N   . LEU B 177 ? 0.4935 0.4861 0.3795 0.0309  0.0044  0.1087  303 LEU B N   
3885 C CA  . LEU B 177 ? 0.4884 0.4786 0.3843 0.0533  0.0033  0.1146  303 LEU B CA  
3886 C C   . LEU B 177 ? 0.4607 0.4837 0.3711 0.0539  0.0045  0.1023  303 LEU B C   
3887 O O   . LEU B 177 ? 0.4649 0.5239 0.3784 0.0452  -0.0003 0.1041  303 LEU B O   
3888 C CB  . LEU B 177 ? 0.5245 0.5266 0.4207 0.0647  -0.0037 0.1381  303 LEU B CB  
3889 C CG  . LEU B 177 ? 0.6057 0.5987 0.5138 0.0932  -0.0022 0.1469  303 LEU B CG  
3890 C CD1 . LEU B 177 ? 0.5915 0.5777 0.4962 0.1054  -0.0087 0.1732  303 LEU B CD1 
3891 C CD2 . LEU B 177 ? 0.5868 0.6252 0.5166 0.1019  -0.0023 0.1441  303 LEU B CD2 
3892 N N   . ASN B 178 ? 0.4505 0.4590 0.3663 0.0618  0.0104  0.0899  304 ASN B N   
3893 C CA  . ASN B 178 ? 0.4109 0.4455 0.3389 0.0603  0.0123  0.0788  304 ASN B CA  
3894 C C   . ASN B 178 ? 0.4287 0.4758 0.3702 0.0815  0.0152  0.0850  304 ASN B C   
3895 O O   . ASN B 178 ? 0.4628 0.4806 0.3999 0.0990  0.0207  0.0866  304 ASN B O   
3896 C CB  . ASN B 178 ? 0.4631 0.4773 0.3871 0.0520  0.0172  0.0613  304 ASN B CB  
3897 C CG  . ASN B 178 ? 0.4325 0.4660 0.3672 0.0536  0.0199  0.0527  304 ASN B CG  
3898 O OD1 . ASN B 178 ? 0.4929 0.5206 0.4305 0.0677  0.0248  0.0515  304 ASN B OD1 
3899 N ND2 . ASN B 178 ? 0.4071 0.4623 0.3459 0.0393  0.0175  0.0469  304 ASN B ND2 
3900 N N   . ILE B 179 ? 0.4339 0.5237 0.3908 0.0795  0.0124  0.0879  305 ILE B N   
3901 C CA  . ILE B 179 ? 0.3670 0.4801 0.3420 0.0983  0.0167  0.0947  305 ILE B CA  
3902 C C   . ILE B 179 ? 0.3957 0.5054 0.3719 0.0949  0.0243  0.0791  305 ILE B C   
3903 O O   . ILE B 179 ? 0.3712 0.4985 0.3502 0.0766  0.0212  0.0717  305 ILE B O   
3904 C CB  . ILE B 179 ? 0.4035 0.5708 0.3971 0.0949  0.0078  0.1096  305 ILE B CB  
3905 C CG1 . ILE B 179 ? 0.4280 0.5993 0.4185 0.0994  -0.0010 0.1280  305 ILE B CG1 
3906 C CG2 . ILE B 179 ? 0.4094 0.6090 0.4269 0.1129  0.0140  0.1171  305 ILE B CG2 
3907 C CD1 . ILE B 179 ? 0.4317 0.6558 0.4329 0.0868  -0.0144 0.1417  305 ILE B CD1 
3908 N N   . ASP B 180 ? 0.4338 0.5164 0.4040 0.1121  0.0343  0.0738  306 ASP B N   
3909 C CA  . ASP B 180 ? 0.4157 0.4958 0.3837 0.1101  0.0418  0.0611  306 ASP B CA  
3910 C C   . ASP B 180 ? 0.4061 0.5370 0.3968 0.1119  0.0440  0.0686  306 ASP B C   
3911 O O   . ASP B 180 ? 0.4086 0.5741 0.4184 0.1235  0.0428  0.0840  306 ASP B O   
3912 C CB  . ASP B 180 ? 0.4489 0.4887 0.4002 0.1288  0.0525  0.0539  306 ASP B CB  
3913 C CG  . ASP B 180 ? 0.4888 0.4766 0.4158 0.1202  0.0490  0.0449  306 ASP B CG  
3914 O OD1 . ASP B 180 ? 0.4727 0.4611 0.3985 0.0993  0.0408  0.0419  306 ASP B OD1 
3915 O OD2 . ASP B 180 ? 0.5598 0.5064 0.4687 0.1340  0.0548  0.0409  306 ASP B OD2 
3916 N N   . ALA B 181 ? 0.3963 0.5335 0.3863 0.0998  0.0465  0.0595  307 ALA B N   
3917 C CA  . ALA B 181 ? 0.3839 0.5673 0.3941 0.0974  0.0492  0.0667  307 ALA B CA  
3918 C C   . ALA B 181 ? 0.4282 0.6111 0.4369 0.1166  0.0647  0.0649  307 ALA B C   
3919 O O   . ALA B 181 ? 0.3997 0.5440 0.3856 0.1186  0.0706  0.0519  307 ALA B O   
3920 C CB  . ALA B 181 ? 0.3138 0.5027 0.3226 0.0702  0.0423  0.0599  307 ALA B CB  
3921 N N   . GLU B 182 ? 0.3640 0.5928 0.3966 0.1306  0.0715  0.0786  308 GLU B N   
3922 C CA  . GLU B 182 ? 0.4166 0.6493 0.4479 0.1525  0.0897  0.0775  308 GLU B CA  
3923 C C   . GLU B 182 ? 0.3977 0.6815 0.4483 0.1411  0.0940  0.0850  308 GLU B C   
3924 O O   . GLU B 182 ? 0.4280 0.7116 0.4745 0.1138  0.0853  0.0808  308 GLU B O   
3925 C CB  . GLU B 182 ? 0.4567 0.6951 0.4990 0.1858  0.0985  0.0878  308 GLU B CB  
3926 C CG  . GLU B 182 ? 0.4406 0.6213 0.4600 0.1919  0.0925  0.0812  308 GLU B CG  
3927 C CD  . GLU B 182 ? 0.4869 0.6571 0.5108 0.2268  0.1017  0.0903  308 GLU B CD  
3928 O OE1 . GLU B 182 ? 0.5141 0.6642 0.5260 0.2512  0.1196  0.0832  308 GLU B OE1 
3929 O OE2 . GLU B 182 ? 0.5066 0.6858 0.5436 0.2303  0.0912  0.1044  308 GLU B OE2 
3930 N N   . GLU B 183 ? 0.4281 0.7550 0.5001 0.1616  0.1082  0.0968  309 GLU B N   
3931 C CA  . GLU B 183 ? 0.3928 0.7692 0.4824 0.1486  0.1138  0.1052  309 GLU B CA  
3932 C C   . GLU B 183 ? 0.3700 0.7878 0.4841 0.1186  0.0952  0.1174  309 GLU B C   
3933 O O   . GLU B 183 ? 0.3580 0.7828 0.4822 0.1153  0.0813  0.1236  309 GLU B O   
3934 C CB  . GLU B 183 ? 0.4243 0.8464 0.5359 0.1783  0.1347  0.1172  309 GLU B CB  
3935 C CG  . GLU B 183 ? 0.5063 0.8862 0.5863 0.2038  0.1561  0.1020  309 GLU B CG  
3936 C CD  . GLU B 183 ? 0.5706 0.9032 0.6353 0.2336  0.1601  0.0948  309 GLU B CD  
3937 O OE1 . GLU B 183 ? 0.5291 0.8629 0.6086 0.2337  0.1456  0.1033  309 GLU B OE1 
3938 O OE2 . GLU B 183 ? 0.6413 0.9332 0.6765 0.2560  0.1774  0.0810  309 GLU B OE2 
3939 N N   . ALA B 184 ? 0.3825 0.8259 0.5029 0.0949  0.0948  0.1212  310 ALA B N   
3940 C CA  . ALA B 184 ? 0.3537 0.8253 0.4898 0.0618  0.0764  0.1297  310 ALA B CA  
3941 C C   . ALA B 184 ? 0.3643 0.9032 0.5391 0.0652  0.0705  0.1512  310 ALA B C   
3942 O O   . ALA B 184 ? 0.3009 0.8532 0.4824 0.0422  0.0513  0.1560  310 ALA B O   
3943 C CB  . ALA B 184 ? 0.3524 0.8345 0.4870 0.0355  0.0777  0.1314  310 ALA B CB  
3944 N N   . ASP B 185 ? 0.3572 0.9395 0.5567 0.0941  0.0866  0.1644  311 ASP B N   
3945 C CA  . ASP B 185 ? 0.3058 0.9598 0.5473 0.0975  0.0794  0.1883  311 ASP B CA  
3946 C C   . ASP B 185 ? 0.3653 1.0048 0.6067 0.1141  0.0683  0.1910  311 ASP B C   
3947 O O   . ASP B 185 ? 0.3450 1.0368 0.6158 0.1142  0.0573  0.2111  311 ASP B O   
3948 C CB  . ASP B 185 ? 0.4045 1.0940 0.6645 0.1206  0.0966  0.2002  311 ASP B CB  
3949 C CG  . ASP B 185 ? 0.4348 1.0902 0.6825 0.1656  0.1162  0.1928  311 ASP B CG  
3950 O OD1 . ASP B 185 ? 0.4482 1.0509 0.6715 0.1792  0.1188  0.1778  311 ASP B OD1 
3951 O OD2 . ASP B 185 ? 0.5369 1.2166 0.7983 0.1868  0.1294  0.2019  311 ASP B OD2 
3952 N N   . ARG B 186 ? 0.3370 0.9040 0.5429 0.1249  0.0690  0.1723  312 ARG B N   
3953 C CA  . ARG B 186 ? 0.3796 0.9258 0.5800 0.1363  0.0580  0.1750  312 ARG B CA  
3954 C C   . ARG B 186 ? 0.3713 0.8879 0.5489 0.1029  0.0369  0.1652  312 ARG B C   
3955 O O   . ARG B 186 ? 0.3873 0.8848 0.5557 0.1075  0.0269  0.1671  312 ARG B O   
3956 C CB  . ARG B 186 ? 0.4429 0.9270 0.6181 0.1688  0.0725  0.1622  312 ARG B CB  
3957 C CG  . ARG B 186 ? 0.4683 0.9607 0.6514 0.2029  0.0978  0.1631  312 ARG B CG  
3958 C CD  . ARG B 186 ? 0.4807 1.0285 0.7026 0.2332  0.1030  0.1873  312 ARG B CD  
3959 N NE  . ARG B 186 ? 0.5391 1.1544 0.7909 0.2142  0.0981  0.2035  312 ARG B NE  
3960 C CZ  . ARG B 186 ? 0.5346 1.1967 0.8146 0.2176  0.0892  0.2253  312 ARG B CZ  
3961 N NH1 . ARG B 186 ? 0.5689 1.2193 0.8519 0.2381  0.0834  0.2347  312 ARG B NH1 
3962 N NH2 . ARG B 186 ? 0.4943 1.2152 0.7988 0.1986  0.0855  0.2392  312 ARG B NH2 
3963 N N   . LEU B 187 ? 0.3012 0.8114 0.4680 0.0704  0.0311  0.1553  313 LEU B N   
3964 C CA  . LEU B 187 ? 0.3262 0.7995 0.4667 0.0424  0.0152  0.1422  313 LEU B CA  
3965 C C   . LEU B 187 ? 0.3078 0.8199 0.4600 0.0269  -0.0043 0.1563  313 LEU B C   
3966 O O   . LEU B 187 ? 0.3728 0.8575 0.5050 0.0232  -0.0140 0.1512  313 LEU B O   
3967 C CB  . LEU B 187 ? 0.3804 0.8368 0.5081 0.0137  0.0142  0.1300  313 LEU B CB  
3968 C CG  . LEU B 187 ? 0.3548 0.7631 0.4522 -0.0114 0.0029  0.1124  313 LEU B CG  
3969 C CD1 . LEU B 187 ? 0.3627 0.7381 0.4457 -0.0238 0.0090  0.0996  313 LEU B CD1 
3970 C CD2 . LEU B 187 ? 0.4306 0.8658 0.5303 -0.0408 -0.0157 0.1180  313 LEU B CD2 
3971 N N   . GLU B 188 ? 0.2866 0.8661 0.4709 0.0169  -0.0104 0.1754  314 GLU B N   
3972 C CA  . GLU B 188 ? 0.2974 0.9181 0.4905 -0.0051 -0.0325 0.1891  314 GLU B CA  
3973 C C   . GLU B 188 ? 0.3236 0.9504 0.5200 0.0184  -0.0382 0.2016  314 GLU B C   
3974 O O   . GLU B 188 ? 0.3377 0.9538 0.5140 0.0016  -0.0546 0.2002  314 GLU B O   
3975 C CB  . GLU B 188 ? 0.3209 1.0205 0.5536 -0.0190 -0.0378 0.2107  314 GLU B CB  
3976 N N   . LEU B 189 ? 0.2977 0.9413 0.5179 0.0574  -0.0244 0.2149  315 LEU B N   
3977 C CA  . LEU B 189 ? 0.3111 0.9577 0.5353 0.0811  -0.0303 0.2298  315 LEU B CA  
3978 C C   . LEU B 189 ? 0.3178 0.8878 0.4994 0.0825  -0.0299 0.2111  315 LEU B C   
3979 O O   . LEU B 189 ? 0.3677 0.9339 0.5376 0.0788  -0.0437 0.2190  315 LEU B O   
3980 C CB  . LEU B 189 ? 0.3196 0.9917 0.5763 0.1261  -0.0132 0.2466  315 LEU B CB  
3981 N N   . SER B 190 ? 0.3342 0.8460 0.4923 0.0859  -0.0149 0.1878  316 SER B N   
3982 C CA  . SER B 190 ? 0.3689 0.8140 0.4902 0.0840  -0.0146 0.1710  316 SER B CA  
3983 C C   . SER B 190 ? 0.4041 0.8415 0.5019 0.0485  -0.0307 0.1621  316 SER B C   
3984 O O   . SER B 190 ? 0.4165 0.8229 0.4906 0.0460  -0.0358 0.1588  316 SER B O   
3985 C CB  . SER B 190 ? 0.3619 0.7546 0.4655 0.0910  0.0023  0.1493  316 SER B CB  
3986 O OG  . SER B 190 ? 0.4278 0.8187 0.5243 0.0640  0.0011  0.1354  316 SER B OG  
3987 N N   . LEU B 191 ? 0.4167 0.8802 0.5186 0.0206  -0.0379 0.1582  317 LEU B N   
3988 C CA  . LEU B 191 ? 0.3634 0.8132 0.4381 -0.0126 -0.0516 0.1467  317 LEU B CA  
3989 C C   . LEU B 191 ? 0.4175 0.9064 0.4933 -0.0223 -0.0705 0.1646  317 LEU B C   
3990 O O   . LEU B 191 ? 0.4397 0.9049 0.4848 -0.0362 -0.0784 0.1573  317 LEU B O   
3991 C CB  . LEU B 191 ? 0.4200 0.8768 0.4949 -0.0405 -0.0539 0.1366  317 LEU B CB  
3992 C CG  . LEU B 191 ? 0.4868 0.9077 0.5260 -0.0712 -0.0620 0.1167  317 LEU B CG  
3993 C CD1 . LEU B 191 ? 0.4013 0.7629 0.4117 -0.0606 -0.0524 0.0991  317 LEU B CD1 
3994 C CD2 . LEU B 191 ? 0.4117 0.8250 0.4506 -0.0930 -0.0605 0.1060  317 LEU B CD2 
3995 N N   . ASP B 192 ? 0.4021 0.9541 0.5132 -0.0149 -0.0777 0.1894  318 ASP B N   
3996 C CA  . ASP B 192 ? 0.3846 0.9775 0.4989 -0.0208 -0.0972 0.2106  318 ASP B CA  
3997 C C   . ASP B 192 ? 0.4112 0.9720 0.5103 0.0031  -0.0946 0.2164  318 ASP B C   
3998 O O   . ASP B 192 ? 0.4194 0.9802 0.4952 -0.0108 -0.1090 0.2215  318 ASP B O   
3999 C CB  . ASP B 192 ? 0.3872 1.0593 0.5499 -0.0114 -0.1041 0.2399  318 ASP B CB  
4000 C CG  . ASP B 192 ? 0.4575 1.1601 0.6336 -0.0404 -0.1068 0.2360  318 ASP B CG  
4001 O OD1 . ASP B 192 ? 0.4649 1.1387 0.6115 -0.0727 -0.1128 0.2152  318 ASP B OD1 
4002 O OD2 . ASP B 192 ? 0.4243 1.1696 0.6352 -0.0309 -0.1003 0.2521  318 ASP B OD2 
4003 N N   . LEU B 193 ? 0.3757 0.9070 0.4845 0.0374  -0.0763 0.2159  319 LEU B N   
4004 C CA  . LEU B 193 ? 0.4218 0.9145 0.5151 0.0590  -0.0728 0.2213  319 LEU B CA  
4005 C C   . LEU B 193 ? 0.4412 0.8821 0.4907 0.0376  -0.0740 0.2010  319 LEU B C   
4006 O O   . LEU B 193 ? 0.4472 0.8810 0.4773 0.0342  -0.0830 0.2105  319 LEU B O   
4007 C CB  . LEU B 193 ? 0.4215 0.8806 0.5262 0.0946  -0.0520 0.2180  319 LEU B CB  
4008 C CG  . LEU B 193 ? 0.5152 0.9238 0.6010 0.1149  -0.0477 0.2221  319 LEU B CG  
4009 C CD1 . LEU B 193 ? 0.5696 1.0137 0.6713 0.1303  -0.0606 0.2542  319 LEU B CD1 
4010 C CD2 . LEU B 193 ? 0.5619 0.9245 0.6486 0.1434  -0.0272 0.2118  319 LEU B CD2 
4011 N N   . LEU B 194 ? 0.4030 0.8094 0.4374 0.0241  -0.0639 0.1746  320 LEU B N   
4012 C CA  . LEU B 194 ? 0.4594 0.8213 0.4564 0.0055  -0.0624 0.1547  320 LEU B CA  
4013 C C   . LEU B 194 ? 0.4820 0.8658 0.4571 -0.0224 -0.0792 0.1571  320 LEU B C   
4014 O O   . LEU B 194 ? 0.4439 0.8067 0.3907 -0.0284 -0.0812 0.1559  320 LEU B O   
4015 C CB  . LEU B 194 ? 0.4445 0.7762 0.4349 -0.0045 -0.0511 0.1290  320 LEU B CB  
4016 C CG  . LEU B 194 ? 0.4498 0.7399 0.4064 -0.0214 -0.0474 0.1080  320 LEU B CG  
4017 C CD1 . LEU B 194 ? 0.4310 0.6812 0.3781 -0.0051 -0.0370 0.1060  320 LEU B CD1 
4018 C CD2 . LEU B 194 ? 0.3936 0.6660 0.3463 -0.0355 -0.0414 0.0865  320 LEU B CD2 
4019 N N   . GLU B 195 ? 0.4684 0.8951 0.4540 -0.0415 -0.0916 0.1612  321 GLU B N   
4020 C CA  . GLU B 195 ? 0.4241 0.8694 0.3833 -0.0718 -0.1092 0.1614  321 GLU B CA  
4021 C C   . GLU B 195 ? 0.4876 0.9566 0.4420 -0.0646 -0.1219 0.1865  321 GLU B C   
4022 O O   . GLU B 195 ? 0.5024 0.9562 0.4193 -0.0802 -0.1275 0.1821  321 GLU B O   
4023 C CB  . GLU B 195 ? 0.4264 0.9165 0.4009 -0.0953 -0.1227 0.1645  321 GLU B CB  
4024 C CG  . GLU B 195 ? 0.4465 0.9577 0.3908 -0.1292 -0.1440 0.1658  321 GLU B CG  
4025 C CD  . GLU B 195 ? 0.5213 1.0658 0.4776 -0.1575 -0.1561 0.1656  321 GLU B CD  
4026 O OE1 . GLU B 195 ? 0.5120 1.0976 0.5130 -0.1466 -0.1554 0.1824  321 GLU B OE1 
4027 O OE2 . GLU B 195 ? 0.6277 1.1507 0.5482 -0.1897 -0.1627 0.1478  321 GLU B OE2 
4028 N N   . VAL B 196 ? 0.4667 0.9730 0.4582 -0.0396 -0.1257 0.2141  322 VAL B N   
4029 C CA  . VAL B 196 ? 0.4518 0.9796 0.4428 -0.0305 -0.1380 0.2410  322 VAL B CA  
4030 C C   . VAL B 196 ? 0.5016 0.9786 0.4623 -0.0200 -0.1295 0.2386  322 VAL B C   
4031 O O   . VAL B 196 ? 0.5505 1.0250 0.4861 -0.0308 -0.1382 0.2463  322 VAL B O   
4032 C CB  . VAL B 196 ? 0.4830 1.0468 0.5239 0.0002  -0.1359 0.2662  322 VAL B CB  
4033 C CG1 . VAL B 196 ? 0.5274 1.0922 0.5687 0.0147  -0.1419 0.2892  322 VAL B CG1 
4034 C CG2 . VAL B 196 ? 0.4870 1.1043 0.5569 -0.0159 -0.1433 0.2703  322 VAL B CG2 
4035 N N   . LEU B 197 ? 0.5208 0.9486 0.4843 -0.0017 -0.1090 0.2233  323 LEU B N   
4036 C CA  . LEU B 197 ? 0.5335 0.9117 0.4716 0.0056  -0.0999 0.2209  323 LEU B CA  
4037 C C   . LEU B 197 ? 0.5614 0.9173 0.4571 -0.0236 -0.0987 0.1999  323 LEU B C   
4038 O O   . LEU B 197 ? 0.5544 0.8961 0.4231 -0.0286 -0.1004 0.2074  323 LEU B O   
4039 C CB  . LEU B 197 ? 0.5470 0.8800 0.4979 0.0287  -0.0802 0.2091  323 LEU B CB  
4040 C CG  . LEU B 197 ? 0.5188 0.8575 0.5038 0.0634  -0.0755 0.2266  323 LEU B CG  
4041 C CD1 . LEU B 197 ? 0.5953 0.8885 0.5846 0.0780  -0.0563 0.2069  323 LEU B CD1 
4042 C CD2 . LEU B 197 ? 0.6079 0.9393 0.5900 0.0809  -0.0818 0.2542  323 LEU B CD2 
4043 N N   . CYS B 198 ? 0.5141 0.8653 0.4028 -0.0421 -0.0944 0.1742  324 CYS B N   
4044 C CA  . CYS B 198 ? 0.5768 0.9037 0.4257 -0.0659 -0.0900 0.1518  324 CYS B CA  
4045 C C   . CYS B 198 ? 0.5913 0.9456 0.4088 -0.0897 -0.1068 0.1595  324 CYS B C   
4046 O O   . CYS B 198 ? 0.5808 0.9147 0.3593 -0.1045 -0.1019 0.1473  324 CYS B O   
4047 C CB  . CYS B 198 ? 0.5208 0.8323 0.3706 -0.0772 -0.0817 0.1239  324 CYS B CB  
4048 S SG  . CYS B 198 ? 0.5451 0.8133 0.4145 -0.0554 -0.0602 0.1096  324 CYS B SG  
4049 N N   . LEU B 199 ? 0.5852 0.9878 0.4181 -0.0941 -0.1262 0.1798  325 LEU B N   
4050 C CA  . LEU B 199 ? 0.5855 1.0074 0.3967 -0.1158 -0.1403 0.1846  325 LEU B CA  
4051 C C   . LEU B 199 ? 0.6206 1.0507 0.4353 -0.1018 -0.1460 0.2120  325 LEU B C   
4052 O O   . LEU B 199 ? 0.6387 1.0783 0.4310 -0.1186 -0.1555 0.2158  325 LEU B O   
4053 C CB  . LEU B 199 ? 0.5637 1.0260 0.3972 -0.1309 -0.1548 0.1875  325 LEU B CB  
4054 C CG  . LEU B 199 ? 0.5879 1.0404 0.4159 -0.1500 -0.1519 0.1616  325 LEU B CG  
4055 C CD1 . LEU B 199 ? 0.5596 1.0556 0.4169 -0.1639 -0.1658 0.1705  325 LEU B CD1 
4056 C CD2 . LEU B 199 ? 0.6229 1.0357 0.3983 -0.1750 -0.1464 0.1321  325 LEU B CD2 
4057 N N   . ASP B 200 ? 0.5909 1.0136 0.4310 -0.0716 -0.1401 0.2306  326 ASP B N   
4058 C CA  . ASP B 200 ? 0.6326 1.0543 0.4759 -0.0562 -0.1445 0.2571  326 ASP B CA  
4059 C C   . ASP B 200 ? 0.6387 1.0253 0.4383 -0.0678 -0.1372 0.2504  326 ASP B C   
4060 O O   . ASP B 200 ? 0.6686 1.0199 0.4543 -0.0646 -0.1217 0.2378  326 ASP B O   
4061 C CB  . ASP B 200 ? 0.6236 1.0348 0.5022 -0.0202 -0.1374 0.2747  326 ASP B CB  
4062 C CG  . ASP B 200 ? 0.6781 1.0899 0.5672 -0.0016 -0.1437 0.3038  326 ASP B CG  
4063 O OD1 . ASP B 200 ? 0.6782 1.0775 0.5373 -0.0135 -0.1476 0.3100  326 ASP B OD1 
4064 O OD2 . ASP B 200 ? 0.7581 1.1824 0.6855 0.0261  -0.1438 0.3206  326 ASP B OD2 
4065 N N   . GLY B 201 ? 0.6730 1.0722 0.4517 -0.0820 -0.1475 0.2596  327 GLY B N   
4066 C CA  . GLY B 201 ? 0.7406 1.1119 0.4789 -0.0929 -0.1398 0.2553  327 GLY B CA  
4067 C C   . GLY B 201 ? 0.7230 1.0622 0.4652 -0.0724 -0.1303 0.2723  327 GLY B C   
4068 O O   . GLY B 201 ? 0.7030 1.0141 0.4162 -0.0808 -0.1177 0.2644  327 GLY B O   
4069 N N   . ASP B 202 ? 0.6757 1.0169 0.4534 -0.0457 -0.1349 0.2953  328 ASP B N   
4070 C CA  . ASP B 202 ? 0.7031 1.0052 0.4823 -0.0268 -0.1266 0.3116  328 ASP B CA  
4071 C C   . ASP B 202 ? 0.7137 0.9790 0.4849 -0.0267 -0.1083 0.2936  328 ASP B C   
4072 O O   . ASP B 202 ? 0.7305 0.9588 0.4918 -0.0220 -0.0996 0.3022  328 ASP B O   
4073 C CB  . ASP B 202 ? 0.7271 1.0317 0.5459 0.0051  -0.1326 0.3356  328 ASP B CB  
4074 C CG  . ASP B 202 ? 0.7440 1.0776 0.5704 0.0087  -0.1494 0.3608  328 ASP B CG  
4075 O OD1 . ASP B 202 ? 0.7629 1.1090 0.5599 -0.0137 -0.1569 0.3625  328 ASP B OD1 
4076 O OD2 . ASP B 202 ? 0.7578 1.1014 0.6196 0.0353  -0.1540 0.3790  328 ASP B OD2 
4077 N N   . LEU B 203 ? 0.6688 0.9436 0.4437 -0.0338 -0.1027 0.2695  329 LEU B N   
4078 C CA  . LEU B 203 ? 0.6090 0.8500 0.3835 -0.0335 -0.0841 0.2467  329 LEU B CA  
4079 C C   . LEU B 203 ? 0.6302 0.8686 0.3719 -0.0592 -0.0740 0.2209  329 LEU B C   
4080 O O   . LEU B 203 ? 0.6869 0.9015 0.4344 -0.0598 -0.0580 0.1961  329 LEU B O   
4081 C CB  . LEU B 203 ? 0.6597 0.9023 0.4701 -0.0188 -0.0803 0.2311  329 LEU B CB  
4082 C CG  . LEU B 203 ? 0.6543 0.8958 0.4990 0.0112  -0.0844 0.2517  329 LEU B CG  
4083 C CD1 . LEU B 203 ? 0.6022 0.8527 0.4775 0.0216  -0.0790 0.2344  329 LEU B CD1 
4084 C CD2 . LEU B 203 ? 0.6674 0.8585 0.5107 0.0262  -0.0748 0.2605  329 LEU B CD2 
4085 N N   . SER B 204 ? 0.7368 0.9956 0.4482 -0.0781 -0.0815 0.2228  330 SER B N   
4086 C CA  . SER B 204 ? 0.7037 0.9579 0.3826 -0.0995 -0.0699 0.1958  330 SER B CA  
4087 C C   . SER B 204 ? 0.7253 0.9515 0.3926 -0.1004 -0.0502 0.1917  330 SER B C   
4088 O O   . SER B 204 ? 0.7257 0.9368 0.3973 -0.0929 -0.0493 0.2137  330 SER B O   
4089 C CB  . SER B 204 ? 0.7484 1.0204 0.4001 -0.1161 -0.0796 0.1976  330 SER B CB  
4090 O OG  . SER B 204 ? 0.8132 1.0789 0.4554 -0.1136 -0.0809 0.2210  330 SER B OG  
4091 N N   . GLY B 205 ? 0.6417 0.8597 0.2972 -0.1094 -0.0339 0.1631  331 GLY B N   
4092 C CA  . GLY B 205 ? 0.6670 0.8656 0.3173 -0.1114 -0.0136 0.1561  331 GLY B CA  
4093 C C   . GLY B 205 ? 0.6895 0.8627 0.3783 -0.0960 -0.0051 0.1523  331 GLY B C   
4094 O O   . GLY B 205 ? 0.7604 0.9212 0.4506 -0.0988 0.0105  0.1474  331 GLY B O   
4095 N N   . TRP B 206 ? 0.6248 0.7925 0.3440 -0.0807 -0.0148 0.1547  332 TRP B N   
4096 C CA  . TRP B 206 ? 0.5775 0.7192 0.3286 -0.0666 -0.0082 0.1493  332 TRP B CA  
4097 C C   . TRP B 206 ? 0.5674 0.7114 0.3361 -0.0623 -0.0058 0.1245  332 TRP B C   
4098 O O   . TRP B 206 ? 0.5940 0.7558 0.3670 -0.0606 -0.0169 0.1239  332 TRP B O   
4099 C CB  . TRP B 206 ? 0.5948 0.7231 0.3626 -0.0503 -0.0190 0.1738  332 TRP B CB  
4100 C CG  . TRP B 206 ? 0.5975 0.6987 0.3942 -0.0342 -0.0151 0.1667  332 TRP B CG  
4101 C CD1 . TRP B 206 ? 0.5820 0.6535 0.3856 -0.0347 -0.0051 0.1608  332 TRP B CD1 
4102 C CD2 . TRP B 206 ? 0.5742 0.6770 0.3942 -0.0163 -0.0215 0.1663  332 TRP B CD2 
4103 N NE1 . TRP B 206 ? 0.5626 0.6133 0.3875 -0.0190 -0.0056 0.1553  332 TRP B NE1 
4104 C CE2 . TRP B 206 ? 0.5770 0.6466 0.4126 -0.0062 -0.0140 0.1579  332 TRP B CE2 
4105 C CE3 . TRP B 206 ? 0.5950 0.7278 0.4247 -0.0089 -0.0327 0.1726  332 TRP B CE3 
4106 C CZ2 . TRP B 206 ? 0.5773 0.6400 0.4339 0.0124  -0.0151 0.1543  332 TRP B CZ2 
4107 C CZ3 . TRP B 206 ? 0.5601 0.6906 0.4162 0.0100  -0.0333 0.1707  332 TRP B CZ3 
4108 C CH2 . TRP B 206 ? 0.5497 0.6442 0.4174 0.0212  -0.0235 0.1608  332 TRP B CH2 
4109 N N   . ASN B 207 ? 0.5467 0.6757 0.3260 -0.0620 0.0078  0.1059  333 ASN B N   
4110 C CA  . ASN B 207 ? 0.5477 0.6746 0.3431 -0.0578 0.0106  0.0842  333 ASN B CA  
4111 C C   . ASN B 207 ? 0.5199 0.6274 0.3445 -0.0433 0.0108  0.0843  333 ASN B C   
4112 O O   . ASN B 207 ? 0.4852 0.5864 0.3236 -0.0405 0.0160  0.0674  333 ASN B O   
4113 C CB  . ASN B 207 ? 0.5601 0.6856 0.3458 -0.0661 0.0255  0.0625  333 ASN B CB  
4114 C CG  . ASN B 207 ? 0.6039 0.7442 0.3559 -0.0797 0.0262  0.0552  333 ASN B CG  
4115 O OD1 . ASN B 207 ? 0.6266 0.7802 0.3667 -0.0851 0.0126  0.0600  333 ASN B OD1 
4116 N ND2 . ASN B 207 ? 0.6644 0.8043 0.3997 -0.0858 0.0421  0.0438  333 ASN B ND2 
4117 N N   . GLY B 208 ? 0.5002 0.5952 0.3316 -0.0340 0.0052  0.1030  334 GLY B N   
4118 C CA  . GLY B 208 ? 0.5000 0.5715 0.3518 -0.0210 0.0065  0.1008  334 GLY B CA  
4119 C C   . GLY B 208 ? 0.4298 0.5079 0.2978 -0.0072 0.0005  0.0993  334 GLY B C   
4120 O O   . GLY B 208 ? 0.4599 0.5182 0.3410 0.0042  0.0029  0.0957  334 GLY B O   
4121 N N   . MET B 209 ? 0.4952 0.6025 0.3618 -0.0089 -0.0074 0.1032  335 MET B N   
4122 C CA  . MET B 209 ? 0.4496 0.5717 0.3354 0.0028  -0.0124 0.1043  335 MET B CA  
4123 C C   . MET B 209 ? 0.4314 0.5488 0.3269 0.0001  -0.0059 0.0833  335 MET B C   
4124 O O   . MET B 209 ? 0.4340 0.5572 0.3204 -0.0142 -0.0037 0.0692  335 MET B O   
4125 C CB  . MET B 209 ? 0.4824 0.6428 0.3651 -0.0039 -0.0243 0.1142  335 MET B CB  
4126 C CG  . MET B 209 ? 0.5477 0.7322 0.4550 0.0079  -0.0296 0.1204  335 MET B CG  
4127 S SD  . MET B 209 ? 0.6431 0.8258 0.5664 0.0356  -0.0327 0.1469  335 MET B SD  
4128 C CE  . MET B 209 ? 0.5602 0.7117 0.4995 0.0552  -0.0193 0.1348  335 MET B CE  
4129 N N   . GLY B 210 ? 0.4068 0.5120 0.3183 0.0145  -0.0024 0.0815  336 GLY B N   
4130 C CA  . GLY B 210 ? 0.4048 0.5049 0.3248 0.0126  0.0029  0.0648  336 GLY B CA  
4131 C C   . GLY B 210 ? 0.3867 0.5062 0.3237 0.0220  0.0012  0.0676  336 GLY B C   
4132 O O   . GLY B 210 ? 0.3765 0.5097 0.3229 0.0358  -0.0019 0.0825  336 GLY B O   
4133 N N   . PHE B 211 ? 0.3304 0.4534 0.2730 0.0154  0.0037  0.0551  337 PHE B N   
4134 C CA  . PHE B 211 ? 0.3585 0.5052 0.3175 0.0205  0.0029  0.0587  337 PHE B CA  
4135 C C   . PHE B 211 ? 0.3439 0.4749 0.3050 0.0181  0.0093  0.0453  337 PHE B C   
4136 O O   . PHE B 211 ? 0.3531 0.4692 0.3058 0.0061  0.0103  0.0333  337 PHE B O   
4137 C CB  . PHE B 211 ? 0.3677 0.5499 0.3291 0.0054  -0.0068 0.0636  337 PHE B CB  
4138 C CG  . PHE B 211 ? 0.3620 0.5796 0.3450 0.0091  -0.0091 0.0732  337 PHE B CG  
4139 C CD1 . PHE B 211 ? 0.3764 0.6213 0.3760 0.0260  -0.0113 0.0918  337 PHE B CD1 
4140 C CD2 . PHE B 211 ? 0.3249 0.5509 0.3129 -0.0044 -0.0091 0.0656  337 PHE B CD2 
4141 C CE1 . PHE B 211 ? 0.3696 0.6553 0.3934 0.0303  -0.0120 0.1025  337 PHE B CE1 
4142 C CE2 . PHE B 211 ? 0.3457 0.6098 0.3557 -0.0033 -0.0105 0.0765  337 PHE B CE2 
4143 C CZ  . PHE B 211 ? 0.3636 0.6611 0.3929 0.0143  -0.0115 0.0951  337 PHE B CZ  
4144 N N   . VAL B 212 ? 0.3329 0.4673 0.3044 0.0311  0.0145  0.0481  338 VAL B N   
4145 C CA  . VAL B 212 ? 0.3075 0.4294 0.2788 0.0284  0.0197  0.0380  338 VAL B CA  
4146 C C   . VAL B 212 ? 0.3361 0.4866 0.3183 0.0170  0.0171  0.0400  338 VAL B C   
4147 O O   . VAL B 212 ? 0.3174 0.5025 0.3136 0.0200  0.0149  0.0518  338 VAL B O   
4148 C CB  . VAL B 212 ? 0.3422 0.4489 0.3122 0.0465  0.0279  0.0382  338 VAL B CB  
4149 C CG1 . VAL B 212 ? 0.3367 0.4338 0.3034 0.0414  0.0317  0.0296  338 VAL B CG1 
4150 C CG2 . VAL B 212 ? 0.3894 0.4619 0.3458 0.0536  0.0287  0.0362  338 VAL B CG2 
4151 N N   . VAL B 213 ? 0.3292 0.4663 0.3068 0.0043  0.0172  0.0304  339 VAL B N   
4152 C CA  . VAL B 213 ? 0.3207 0.4771 0.3067 -0.0074 0.0157  0.0329  339 VAL B CA  
4153 C C   . VAL B 213 ? 0.3454 0.4839 0.3286 -0.0048 0.0219  0.0285  339 VAL B C   
4154 O O   . VAL B 213 ? 0.3269 0.4351 0.3000 -0.0036 0.0230  0.0198  339 VAL B O   
4155 C CB  . VAL B 213 ? 0.3590 0.5137 0.3384 -0.0293 0.0079  0.0273  339 VAL B CB  
4156 C CG1 . VAL B 213 ? 0.3928 0.5717 0.3823 -0.0444 0.0043  0.0338  339 VAL B CG1 
4157 C CG2 . VAL B 213 ? 0.3664 0.5335 0.3405 -0.0331 0.0012  0.0298  339 VAL B CG2 
4158 N N   . GLN B 214 ? 0.3580 0.5194 0.3511 -0.0045 0.0256  0.0364  340 GLN B N   
4159 C CA  . GLN B 214 ? 0.3161 0.4661 0.3041 -0.0006 0.0324  0.0352  340 GLN B CA  
4160 C C   . GLN B 214 ? 0.3599 0.5069 0.3480 -0.0202 0.0285  0.0357  340 GLN B C   
4161 O O   . GLN B 214 ? 0.3284 0.5030 0.3275 -0.0330 0.0261  0.0440  340 GLN B O   
4162 C CB  . GLN B 214 ? 0.3362 0.5137 0.3324 0.0142  0.0421  0.0441  340 GLN B CB  
4163 C CG  . GLN B 214 ? 0.3573 0.5306 0.3517 0.0358  0.0466  0.0440  340 GLN B CG  
4164 C CD  . GLN B 214 ? 0.3490 0.5615 0.3605 0.0511  0.0548  0.0562  340 GLN B CD  
4165 O OE1 . GLN B 214 ? 0.3736 0.6268 0.4058 0.0434  0.0504  0.0675  340 GLN B OE1 
4166 N NE2 . GLN B 214 ? 0.3421 0.5428 0.3448 0.0732  0.0667  0.0539  340 GLN B NE2 
4167 N N   . ALA B 215 ? 0.3414 0.4550 0.3181 -0.0229 0.0273  0.0284  341 ALA B N   
4168 C CA  . ALA B 215 ? 0.3725 0.4734 0.3474 -0.0396 0.0232  0.0291  341 ALA B CA  
4169 C C   . ALA B 215 ? 0.3883 0.5057 0.3661 -0.0457 0.0271  0.0402  341 ALA B C   
4170 O O   . ALA B 215 ? 0.3811 0.4922 0.3590 -0.0630 0.0231  0.0444  341 ALA B O   
4171 C CB  . ALA B 215 ? 0.3843 0.4481 0.3499 -0.0369 0.0212  0.0212  341 ALA B CB  
4172 N N   . TYR B 216 ? 0.3548 0.4914 0.3329 -0.0326 0.0357  0.0453  342 TYR B N   
4173 C CA  . TYR B 216 ? 0.3787 0.5370 0.3596 -0.0401 0.0412  0.0571  342 TYR B CA  
4174 C C   . TYR B 216 ? 0.3485 0.5501 0.3494 -0.0512 0.0411  0.0679  342 TYR B C   
4175 O O   . TYR B 216 ? 0.3838 0.6098 0.3909 -0.0615 0.0454  0.0801  342 TYR B O   
4176 C CB  . TYR B 216 ? 0.3605 0.5239 0.3304 -0.0228 0.0527  0.0579  342 TYR B CB  
4177 C CG  . TYR B 216 ? 0.3754 0.5596 0.3497 -0.0016 0.0624  0.0565  342 TYR B CG  
4178 C CD1 . TYR B 216 ? 0.3553 0.5654 0.3490 0.0020  0.0607  0.0597  342 TYR B CD1 
4179 C CD2 . TYR B 216 ? 0.3832 0.5586 0.3396 0.0153  0.0731  0.0523  342 TYR B CD2 
4180 C CE1 . TYR B 216 ? 0.3518 0.5777 0.3503 0.0245  0.0698  0.0604  342 TYR B CE1 
4181 C CE2 . TYR B 216 ? 0.4028 0.5889 0.3602 0.0371  0.0834  0.0501  342 TYR B CE2 
4182 C CZ  . TYR B 216 ? 0.3537 0.5654 0.3344 0.0430  0.0820  0.0551  342 TYR B CZ  
4183 O OH  . TYR B 216 ? 0.3762 0.5959 0.3590 0.0678  0.0926  0.0549  342 TYR B OH  
4184 N N   . GLY B 217 ? 0.3662 0.5805 0.3773 -0.0514 0.0353  0.0656  343 GLY B N   
4185 C CA  . GLY B 217 ? 0.3585 0.6187 0.3902 -0.0643 0.0321  0.0776  343 GLY B CA  
4186 C C   . GLY B 217 ? 0.4038 0.6510 0.4324 -0.0946 0.0199  0.0775  343 GLY B C   
4187 O O   . GLY B 217 ? 0.3895 0.5953 0.4027 -0.1002 0.0128  0.0647  343 GLY B O   
4188 N N   . LYS B 218 ? 0.3996 0.6820 0.4425 -0.1145 0.0185  0.0920  344 LYS B N   
4189 C CA  . LYS B 218 ? 0.3846 0.6554 0.4237 -0.1473 0.0055  0.0927  344 LYS B CA  
4190 C C   . LYS B 218 ? 0.4446 0.7122 0.4797 -0.1550 -0.0066 0.0836  344 LYS B C   
4191 O O   . LYS B 218 ? 0.4655 0.6970 0.4833 -0.1765 -0.0166 0.0743  344 LYS B O   
4192 C CB  . LYS B 218 ? 0.4256 0.7470 0.4855 -0.1691 0.0052  0.1128  344 LYS B CB  
4193 C CG  . LYS B 218 ? 0.4361 0.7651 0.4973 -0.1633 0.0186  0.1235  344 LYS B CG  
4194 C CD  . LYS B 218 ? 0.4607 0.8493 0.5461 -0.1841 0.0206  0.1458  344 LYS B CD  
4195 C CE  . LYS B 218 ? 0.4702 0.8535 0.5482 -0.1879 0.0316  0.1562  344 LYS B CE  
4196 N NZ  . LYS B 218 ? 0.4801 0.9333 0.5850 -0.2011 0.0395  0.1797  344 LYS B NZ  
4197 N N   . ARG B 219 ? 0.4070 0.7101 0.4553 -0.1381 -0.0058 0.0867  345 ARG B N   
4198 C CA  . ARG B 219 ? 0.3821 0.6895 0.4256 -0.1476 -0.0184 0.0815  345 ARG B CA  
4199 C C   . ARG B 219 ? 0.4022 0.6571 0.4204 -0.1363 -0.0183 0.0619  345 ARG B C   
4200 O O   . ARG B 219 ? 0.4135 0.6633 0.4198 -0.1463 -0.0279 0.0551  345 ARG B O   
4201 C CB  . ARG B 219 ? 0.3879 0.7552 0.4567 -0.1330 -0.0185 0.0960  345 ARG B CB  
4202 C CG  . ARG B 219 ? 0.4089 0.8408 0.5084 -0.1454 -0.0194 0.1177  345 ARG B CG  
4203 C CD  . ARG B 219 ? 0.4110 0.9007 0.5388 -0.1216 -0.0162 0.1329  345 ARG B CD  
4204 N NE  . ARG B 219 ? 0.3915 0.8734 0.5222 -0.0846 0.0028  0.1314  345 ARG B NE  
4205 C CZ  . ARG B 219 ? 0.4204 0.9401 0.5727 -0.0559 0.0108  0.1427  345 ARG B CZ  
4206 N NH1 . ARG B 219 ? 0.3394 0.9140 0.5172 -0.0574 0.0010  0.1593  345 ARG B NH1 
4207 N NH2 . ARG B 219 ? 0.3647 0.8653 0.5117 -0.0247 0.0285  0.1377  345 ARG B NH2 
4208 N N   . CYS B 220 ? 0.4133 0.6320 0.4225 -0.1177 -0.0081 0.0537  346 CYS B N   
4209 C CA  . CYS B 220 ? 0.4001 0.5814 0.3928 -0.1026 -0.0058 0.0388  346 CYS B CA  
4210 C C   . CYS B 220 ? 0.4265 0.5753 0.3980 -0.1192 -0.0135 0.0248  346 CYS B C   
4211 O O   . CYS B 220 ? 0.4309 0.5809 0.3944 -0.1143 -0.0158 0.0191  346 CYS B O   
4212 C CB  . CYS B 220 ? 0.3844 0.5337 0.3716 -0.0865 0.0035  0.0338  346 CYS B CB  
4213 S SG  . CYS B 220 ? 0.4303 0.5466 0.4050 -0.0665 0.0073  0.0199  346 CYS B SG  
4214 N N   . PRO B 221 ? 0.4287 0.5454 0.3877 -0.1380 -0.0167 0.0185  347 PRO B N   
4215 C CA  . PRO B 221 ? 0.4892 0.5677 0.4229 -0.1495 -0.0209 0.0016  347 PRO B CA  
4216 C C   . PRO B 221 ? 0.4981 0.6018 0.4243 -0.1683 -0.0322 0.0018  347 PRO B C   
4217 O O   . PRO B 221 ? 0.5141 0.5989 0.4185 -0.1697 -0.0335 -0.0116 347 PRO B O   
4218 C CB  . PRO B 221 ? 0.5443 0.5819 0.4673 -0.1656 -0.0220 -0.0024 347 PRO B CB  
4219 C CG  . PRO B 221 ? 0.5420 0.6108 0.4848 -0.1743 -0.0235 0.0159  347 PRO B CG  
4220 C CD  . PRO B 221 ? 0.4253 0.5377 0.3899 -0.1512 -0.0166 0.0271  347 PRO B CD  
4221 N N   . PHE B 222 ? 0.4323 0.5833 0.3767 -0.1823 -0.0402 0.0182  348 PHE B N   
4222 C CA  . PHE B 222 ? 0.4526 0.6352 0.3925 -0.2027 -0.0541 0.0218  348 PHE B CA  
4223 C C   . PHE B 222 ? 0.4314 0.6517 0.3821 -0.1826 -0.0541 0.0297  348 PHE B C   
4224 O O   . PHE B 222 ? 0.4408 0.6728 0.3772 -0.1939 -0.0645 0.0279  348 PHE B O   
4225 C CB  . PHE B 222 ? 0.4441 0.6659 0.4028 -0.2281 -0.0636 0.0386  348 PHE B CB  
4226 C CG  . PHE B 222 ? 0.4848 0.6657 0.4335 -0.2467 -0.0627 0.0339  348 PHE B CG  
4227 C CD1 . PHE B 222 ? 0.5509 0.6808 0.4662 -0.2722 -0.0705 0.0173  348 PHE B CD1 
4228 C CD2 . PHE B 222 ? 0.5141 0.7019 0.4829 -0.2372 -0.0531 0.0455  348 PHE B CD2 
4229 C CE1 . PHE B 222 ? 0.5892 0.6739 0.4939 -0.2881 -0.0697 0.0140  348 PHE B CE1 
4230 C CE2 . PHE B 222 ? 0.5691 0.7167 0.5274 -0.2545 -0.0529 0.0439  348 PHE B CE2 
4231 C CZ  . PHE B 222 ? 0.5900 0.6846 0.5174 -0.2795 -0.0614 0.0288  348 PHE B CZ  
4232 N N   . VAL B 223 ? 0.3963 0.6330 0.3689 -0.1539 -0.0432 0.0388  349 VAL B N   
4233 C CA  . VAL B 223 ? 0.4073 0.6616 0.3844 -0.1318 -0.0412 0.0436  349 VAL B CA  
4234 C C   . VAL B 223 ? 0.4415 0.6511 0.3900 -0.1270 -0.0376 0.0257  349 VAL B C   
4235 O O   . VAL B 223 ? 0.4242 0.6428 0.3617 -0.1262 -0.0425 0.0262  349 VAL B O   
4236 C CB  . VAL B 223 ? 0.3689 0.6380 0.3696 -0.1027 -0.0289 0.0538  349 VAL B CB  
4237 C CG1 . VAL B 223 ? 0.3302 0.6025 0.3311 -0.0793 -0.0259 0.0571  349 VAL B CG1 
4238 C CG2 . VAL B 223 ? 0.3602 0.6829 0.3905 -0.1058 -0.0304 0.0731  349 VAL B CG2 
4239 N N   . LEU B 224 ? 0.4537 0.6175 0.3903 -0.1243 -0.0289 0.0110  350 LEU B N   
4240 C CA  . LEU B 224 ? 0.4565 0.5831 0.3697 -0.1188 -0.0234 -0.0052 350 LEU B CA  
4241 C C   . LEU B 224 ? 0.4760 0.5923 0.3601 -0.1416 -0.0317 -0.0162 350 LEU B C   
4242 O O   . LEU B 224 ? 0.5156 0.6276 0.3819 -0.1381 -0.0304 -0.0221 350 LEU B O   
4243 C CB  . LEU B 224 ? 0.4391 0.5241 0.3501 -0.1099 -0.0130 -0.0161 350 LEU B CB  
4244 C CG  . LEU B 224 ? 0.4676 0.5592 0.3991 -0.0872 -0.0051 -0.0077 350 LEU B CG  
4245 C CD1 . LEU B 224 ? 0.4801 0.5357 0.4096 -0.0804 0.0022  -0.0160 350 LEU B CD1 
4246 C CD2 . LEU B 224 ? 0.4890 0.5902 0.4212 -0.0711 -0.0019 -0.0051 350 LEU B CD2 
4247 N N   . ASP B 225 ? 0.4901 0.6013 0.3660 -0.1670 -0.0407 -0.0190 351 ASP B N   
4248 C CA  . ASP B 225 ? 0.5197 0.6185 0.3622 -0.1922 -0.0503 -0.0308 351 ASP B CA  
4249 C C   . ASP B 225 ? 0.5262 0.6710 0.3680 -0.1967 -0.0616 -0.0188 351 ASP B C   
4250 O O   . ASP B 225 ? 0.5603 0.6945 0.3701 -0.2057 -0.0648 -0.0291 351 ASP B O   
4251 C CB  . ASP B 225 ? 0.5566 0.6460 0.3922 -0.2229 -0.0612 -0.0324 351 ASP B CB  
4252 C CG  . ASP B 225 ? 0.6199 0.6524 0.4465 -0.2219 -0.0517 -0.0459 351 ASP B CG  
4253 O OD1 . ASP B 225 ? 0.6578 0.6545 0.4754 -0.2007 -0.0378 -0.0588 351 ASP B OD1 
4254 O OD2 . ASP B 225 ? 0.6723 0.6975 0.5022 -0.2428 -0.0585 -0.0417 351 ASP B OD2 
4255 N N   . PHE B 226 ? 0.5079 0.7048 0.3838 -0.1901 -0.0674 0.0041  352 PHE B N   
4256 C CA  . PHE B 226 ? 0.4800 0.7243 0.3604 -0.1915 -0.0793 0.0200  352 PHE B CA  
4257 C C   . PHE B 226 ? 0.4732 0.7083 0.3451 -0.1680 -0.0705 0.0190  352 PHE B C   
4258 O O   . PHE B 226 ? 0.4913 0.7389 0.3432 -0.1751 -0.0787 0.0216  352 PHE B O   
4259 C CB  . PHE B 226 ? 0.4642 0.7664 0.3877 -0.1844 -0.0844 0.0456  352 PHE B CB  
4260 C CG  . PHE B 226 ? 0.4796 0.8329 0.4146 -0.1793 -0.0958 0.0659  352 PHE B CG  
4261 C CD1 . PHE B 226 ? 0.4922 0.8850 0.4234 -0.2072 -0.1163 0.0760  352 PHE B CD1 
4262 C CD2 . PHE B 226 ? 0.4574 0.8176 0.4060 -0.1476 -0.0873 0.0761  352 PHE B CD2 
4263 C CE1 . PHE B 226 ? 0.5508 0.9936 0.4944 -0.2011 -0.1282 0.0977  352 PHE B CE1 
4264 C CE2 . PHE B 226 ? 0.4918 0.8950 0.4507 -0.1409 -0.0980 0.0969  352 PHE B CE2 
4265 C CZ  . PHE B 226 ? 0.4825 0.9293 0.4405 -0.1663 -0.1185 0.1087  352 PHE B CZ  
4266 N N   . ILE B 227 ? 0.4868 0.6995 0.3715 -0.1424 -0.0547 0.0159  353 ILE B N   
4267 C CA  . ILE B 227 ? 0.4857 0.6903 0.3651 -0.1222 -0.0467 0.0172  353 ILE B CA  
4268 C C   . ILE B 227 ? 0.5249 0.6941 0.3671 -0.1306 -0.0412 -0.0024 353 ILE B C   
4269 O O   . ILE B 227 ? 0.4850 0.6603 0.3101 -0.1293 -0.0422 0.0006  353 ILE B O   
4270 C CB  . ILE B 227 ? 0.4256 0.6165 0.3278 -0.0964 -0.0332 0.0194  353 ILE B CB  
4271 C CG1 . ILE B 227 ? 0.4041 0.6319 0.3383 -0.0834 -0.0360 0.0394  353 ILE B CG1 
4272 C CG2 . ILE B 227 ? 0.4237 0.5962 0.3164 -0.0809 -0.0243 0.0173  353 ILE B CG2 
4273 C CD1 . ILE B 227 ? 0.4318 0.6417 0.3821 -0.0616 -0.0230 0.0385  353 ILE B CD1 
4274 N N   . ILE B 228 ? 0.5140 0.6453 0.3429 -0.1376 -0.0341 -0.0218 354 ILE B N   
4275 C CA  . ILE B 228 ? 0.5717 0.6692 0.3646 -0.1436 -0.0264 -0.0420 354 ILE B CA  
4276 C C   . ILE B 228 ? 0.6096 0.7200 0.3694 -0.1674 -0.0393 -0.0441 354 ILE B C   
4277 O O   . ILE B 228 ? 0.6342 0.7409 0.3668 -0.1676 -0.0353 -0.0493 354 ILE B O   
4278 C CB  . ILE B 228 ? 0.5900 0.6429 0.3754 -0.1458 -0.0174 -0.0612 354 ILE B CB  
4279 C CG1 . ILE B 228 ? 0.5394 0.5827 0.3552 -0.1220 -0.0057 -0.0574 354 ILE B CG1 
4280 C CG2 . ILE B 228 ? 0.6177 0.6354 0.3635 -0.1503 -0.0076 -0.0835 354 ILE B CG2 
4281 C CD1 . ILE B 228 ? 0.5457 0.5526 0.3629 -0.1234 -0.0008 -0.0685 354 ILE B CD1 
4282 N N   . ASP B 229 ? 0.5990 0.7286 0.3603 -0.1895 -0.0559 -0.0383 355 ASP B N   
4283 C CA  . ASP B 229 ? 0.6125 0.7587 0.3417 -0.2157 -0.0719 -0.0385 355 ASP B CA  
4284 C C   . ASP B 229 ? 0.5719 0.7617 0.3075 -0.2072 -0.0793 -0.0170 355 ASP B C   
4285 O O   . ASP B 229 ? 0.6060 0.7961 0.3052 -0.2180 -0.0832 -0.0211 355 ASP B O   
4286 C CB  . ASP B 229 ? 0.6018 0.7667 0.3372 -0.2434 -0.0903 -0.0330 355 ASP B CB  
4287 C CG  . ASP B 229 ? 0.6588 0.8458 0.3610 -0.2740 -0.1105 -0.0315 355 ASP B CG  
4288 O OD1 . ASP B 229 ? 0.7338 0.8787 0.3897 -0.2909 -0.1084 -0.0544 355 ASP B OD1 
4289 O OD2 . ASP B 229 ? 0.6910 0.9358 0.4154 -0.2777 -0.1269 -0.0062 355 ASP B OD2 
4290 N N   . LEU B 230 ? 0.5544 0.7777 0.3333 -0.1866 -0.0801 0.0059  356 LEU B N   
4291 C CA  . LEU B 230 ? 0.5357 0.7933 0.3225 -0.1742 -0.0857 0.0281  356 LEU B CA  
4292 C C   . LEU B 230 ? 0.5385 0.7689 0.3006 -0.1626 -0.0719 0.0200  356 LEU B C   
4293 O O   . LEU B 230 ? 0.5932 0.8399 0.3346 -0.1670 -0.0786 0.0301  356 LEU B O   
4294 C CB  . LEU B 230 ? 0.5073 0.7921 0.3428 -0.1491 -0.0839 0.0498  356 LEU B CB  
4295 C CG  . LEU B 230 ? 0.4852 0.7941 0.3313 -0.1299 -0.0867 0.0731  356 LEU B CG  
4296 C CD1 . LEU B 230 ? 0.5119 0.8663 0.3495 -0.1460 -0.1084 0.0921  356 LEU B CD1 
4297 C CD2 . LEU B 230 ? 0.4443 0.7646 0.3336 -0.1017 -0.0796 0.0878  356 LEU B CD2 
4298 N N   . ALA B 231 ? 0.5758 0.7679 0.3403 -0.1491 -0.0529 0.0036  357 ALA B N   
4299 C CA  . ALA B 231 ? 0.5931 0.7635 0.3383 -0.1393 -0.0380 -0.0038 357 ALA B CA  
4300 C C   . ALA B 231 ? 0.6277 0.7867 0.3230 -0.1594 -0.0382 -0.0192 357 ALA B C   
4301 O O   . ALA B 231 ? 0.6380 0.8011 0.3116 -0.1580 -0.0336 -0.0149 357 ALA B O   
4302 C CB  . ALA B 231 ? 0.5370 0.6740 0.2975 -0.1235 -0.0197 -0.0182 357 ALA B CB  
4303 N N   . ARG B 232 ? 0.6509 0.7929 0.3239 -0.1794 -0.0429 -0.0376 358 ARG B N   
4304 C CA  . ARG B 232 ? 0.6797 0.8029 0.2980 -0.1994 -0.0418 -0.0568 358 ARG B CA  
4305 C C   . ARG B 232 ? 0.6940 0.8537 0.2916 -0.2168 -0.0613 -0.0401 358 ARG B C   
4306 O O   . ARG B 232 ? 0.7266 0.8820 0.2978 -0.2171 -0.0554 -0.0419 358 ARG B O   
4307 C CB  . ARG B 232 ? 0.6999 0.7875 0.2979 -0.2174 -0.0430 -0.0810 358 ARG B CB  
4308 C CG  . ARG B 232 ? 0.6827 0.7327 0.3036 -0.1987 -0.0248 -0.0949 358 ARG B CG  
4309 C CD  . ARG B 232 ? 0.7295 0.7304 0.3173 -0.2148 -0.0217 -0.1224 358 ARG B CD  
4310 N NE  . ARG B 232 ? 0.7560 0.7243 0.3700 -0.1976 -0.0083 -0.1305 358 ARG B NE  
4311 C CZ  . ARG B 232 ? 0.7865 0.7275 0.4025 -0.1746 0.0140  -0.1427 358 ARG B CZ  
4312 N NH1 . ARG B 232 ? 0.8433 0.7859 0.4376 -0.1655 0.0282  -0.1492 358 ARG B NH1 
4313 N NH2 . ARG B 232 ? 0.8043 0.7195 0.4460 -0.1606 0.0222  -0.1464 358 ARG B NH2 
4314 N N   . ARG B 233 ? 0.6817 0.8776 0.3044 -0.2261 -0.0826 -0.0208 359 ARG B N   
4315 C CA  . ARG B 233 ? 0.6938 0.9219 0.3112 -0.2383 -0.0998 -0.0030 359 ARG B CA  
4316 C C   . ARG B 233 ? 0.6688 0.9293 0.3036 -0.2200 -0.1023 0.0252  359 ARG B C   
4317 O O   . ARG B 233 ? 0.6844 0.9638 0.3070 -0.2273 -0.1123 0.0380  359 ARG B O   
4318 C CB  . ARG B 233 ? 0.7218 0.9791 0.3618 -0.2564 -0.1206 0.0078  359 ARG B CB  
4319 C CG  . ARG B 233 ? 0.6383 0.9334 0.3293 -0.2422 -0.1272 0.0301  359 ARG B CG  
4320 C CD  . ARG B 233 ? 0.6976 1.0136 0.4089 -0.2628 -0.1420 0.0344  359 ARG B CD  
4321 N NE  . ARG B 233 ? 0.6092 0.9509 0.3667 -0.2483 -0.1420 0.0477  359 ARG B NE  
4322 C CZ  . ARG B 233 ? 0.6044 0.9992 0.4054 -0.2331 -0.1502 0.0776  359 ARG B CZ  
4323 N NH1 . ARG B 233 ? 0.6230 1.0510 0.4293 -0.2314 -0.1606 0.0984  359 ARG B NH1 
4324 N NH2 . ARG B 233 ? 0.5666 0.9774 0.4092 -0.2161 -0.1447 0.0864  359 ARG B NH2 
4325 N N   . SER B 234 ? 0.6636 0.9279 0.3244 -0.1969 -0.0936 0.0354  360 SER B N   
4326 C CA  . SER B 234 ? 0.6788 0.9628 0.3526 -0.1787 -0.0941 0.0616  360 SER B CA  
4327 C C   . SER B 234 ? 0.6972 0.9539 0.3433 -0.1723 -0.0756 0.0534  360 SER B C   
4328 O O   . SER B 234 ? 0.6793 0.9476 0.3253 -0.1646 -0.0775 0.0741  360 SER B O   
4329 C CB  . SER B 234 ? 0.6158 0.9074 0.3426 -0.1517 -0.0903 0.0775  360 SER B CB  
4330 O OG  . SER B 234 ? 0.6122 0.8654 0.3498 -0.1386 -0.0695 0.0579  360 SER B OG  
4331 N N   . GLY B 235 ? 0.7004 0.9209 0.3288 -0.1734 -0.0565 0.0252  361 GLY B N   
4332 C CA  . GLY B 235 ? 0.7324 0.9332 0.3434 -0.1649 -0.0360 0.0188  361 GLY B CA  
4333 C C   . GLY B 235 ? 0.6956 0.8896 0.3469 -0.1403 -0.0244 0.0307  361 GLY B C   
4334 O O   . GLY B 235 ? 0.7508 0.9349 0.3929 -0.1347 -0.0090 0.0306  361 GLY B O   
4335 N N   . ARG B 236 ? 0.6616 0.8616 0.3554 -0.1271 -0.0313 0.0411  362 ARG B N   
4336 C CA  . ARG B 236 ? 0.6229 0.8099 0.3515 -0.1056 -0.0210 0.0481  362 ARG B CA  
4337 C C   . ARG B 236 ? 0.6207 0.7818 0.3629 -0.0998 -0.0068 0.0250  362 ARG B C   
4338 O O   . ARG B 236 ? 0.6252 0.7817 0.3684 -0.1067 -0.0102 0.0111  362 ARG B O   
4339 C CB  . ARG B 236 ? 0.5642 0.7685 0.3278 -0.0923 -0.0339 0.0697  362 ARG B CB  
4340 C CG  . ARG B 236 ? 0.6449 0.8789 0.4003 -0.0957 -0.0507 0.0955  362 ARG B CG  
4341 C CD  . ARG B 236 ? 0.6493 0.8745 0.3939 -0.0895 -0.0456 0.1116  362 ARG B CD  
4342 N NE  . ARG B 236 ? 0.6550 0.9075 0.3825 -0.0963 -0.0620 0.1357  362 ARG B NE  
4343 C CZ  . ARG B 236 ? 0.6373 0.9127 0.3884 -0.0845 -0.0771 0.1608  362 ARG B CZ  
4344 N NH1 . ARG B 236 ? 0.6317 0.9041 0.4222 -0.0645 -0.0755 0.1640  362 ARG B NH1 
4345 N NH2 . ARG B 236 ? 0.6998 1.0035 0.4342 -0.0921 -0.0936 0.1837  362 ARG B NH2 
4346 N N   . ARG B 237 ? 0.6294 0.7748 0.3847 -0.0878 0.0077  0.0237  363 ARG B N   
4347 C CA  . ARG B 237 ? 0.5242 0.6489 0.2985 -0.0795 0.0194  0.0069  363 ARG B CA  
4348 C C   . ARG B 237 ? 0.5304 0.6529 0.3405 -0.0655 0.0145  0.0167  363 ARG B C   
4349 O O   . ARG B 237 ? 0.5763 0.6898 0.4024 -0.0552 0.0201  0.0234  363 ARG B O   
4350 C CB  . ARG B 237 ? 0.5525 0.6670 0.3227 -0.0757 0.0373  -0.0001 363 ARG B CB  
4351 C CG  . ARG B 237 ? 0.5153 0.6126 0.3060 -0.0667 0.0477  -0.0155 363 ARG B CG  
4352 C CD  . ARG B 237 ? 0.5261 0.6198 0.3145 -0.0629 0.0665  -0.0243 363 ARG B CD  
4353 N NE  . ARG B 237 ? 0.5229 0.6018 0.3322 -0.0531 0.0735  -0.0377 363 ARG B NE  
4354 C CZ  . ARG B 237 ? 0.5055 0.5851 0.3419 -0.0432 0.0813  -0.0349 363 ARG B CZ  
4355 N NH1 . ARG B 237 ? 0.4939 0.5863 0.3400 -0.0434 0.0838  -0.0205 363 ARG B NH1 
4356 N NH2 . ARG B 237 ? 0.4984 0.5656 0.3520 -0.0343 0.0855  -0.0454 363 ARG B NH2 
4357 N N   . ILE B 238 ? 0.4756 0.6054 0.2961 -0.0669 0.0046  0.0162  364 ILE B N   
4358 C CA  . ILE B 238 ? 0.4349 0.5681 0.2847 -0.0536 0.0000  0.0272  364 ILE B CA  
4359 C C   . ILE B 238 ? 0.4649 0.5756 0.3315 -0.0435 0.0105  0.0180  364 ILE B C   
4360 O O   . ILE B 238 ? 0.4559 0.5540 0.3213 -0.0470 0.0168  0.0022  364 ILE B O   
4361 C CB  . ILE B 238 ? 0.4269 0.5791 0.2849 -0.0596 -0.0111 0.0289  364 ILE B CB  
4362 C CG1 . ILE B 238 ? 0.5001 0.6779 0.3387 -0.0740 -0.0238 0.0374  364 ILE B CG1 
4363 C CG2 . ILE B 238 ? 0.4234 0.5852 0.3105 -0.0435 -0.0138 0.0424  364 ILE B CG2 
4364 C CD1 . ILE B 238 ? 0.5135 0.7151 0.3594 -0.0860 -0.0365 0.0393  364 ILE B CD1 
4365 N N   . MET B 239 ? 0.4520 0.5555 0.3325 -0.0313 0.0118  0.0284  365 MET B N   
4366 C CA  . MET B 239 ? 0.4228 0.5080 0.3186 -0.0234 0.0182  0.0216  365 MET B CA  
4367 C C   . MET B 239 ? 0.4441 0.5331 0.3540 -0.0184 0.0142  0.0203  365 MET B C   
4368 O O   . MET B 239 ? 0.4215 0.5234 0.3385 -0.0117 0.0085  0.0317  365 MET B O   
4369 C CB  . MET B 239 ? 0.4265 0.4981 0.3267 -0.0156 0.0197  0.0318  365 MET B CB  
4370 C CG  . MET B 239 ? 0.4708 0.5444 0.3568 -0.0218 0.0212  0.0404  365 MET B CG  
4371 S SD  . MET B 239 ? 0.5219 0.5721 0.4115 -0.0178 0.0229  0.0514  365 MET B SD  
4372 C CE  . MET B 239 ? 0.5326 0.5683 0.4322 -0.0014 0.0169  0.0569  365 MET B CE  
4373 N N   . VAL B 240 ? 0.3996 0.4795 0.3143 -0.0209 0.0180  0.0080  366 VAL B N   
4374 C CA  . VAL B 240 ? 0.3869 0.4712 0.3126 -0.0196 0.0151  0.0071  366 VAL B CA  
4375 C C   . VAL B 240 ? 0.3494 0.4165 0.2848 -0.0112 0.0197  0.0040  366 VAL B C   
4376 O O   . VAL B 240 ? 0.3982 0.4518 0.3340 -0.0131 0.0239  -0.0045 366 VAL B O   
4377 C CB  . VAL B 240 ? 0.4009 0.4861 0.3201 -0.0328 0.0134  -0.0028 366 VAL B CB  
4378 C CG1 . VAL B 240 ? 0.3641 0.4552 0.2958 -0.0334 0.0106  -0.0006 366 VAL B CG1 
4379 C CG2 . VAL B 240 ? 0.3799 0.4820 0.2844 -0.0444 0.0068  -0.0004 366 VAL B CG2 
4380 N N   . ARG B 241 ? 0.3273 0.3950 0.2694 -0.0010 0.0190  0.0113  367 ARG B N   
4381 C CA  . ARG B 241 ? 0.3308 0.3822 0.2768 0.0049  0.0218  0.0079  367 ARG B CA  
4382 C C   . ARG B 241 ? 0.3718 0.4305 0.3238 0.0030  0.0216  0.0063  367 ARG B C   
4383 O O   . ARG B 241 ? 0.3588 0.4347 0.3158 0.0067  0.0211  0.0129  367 ARG B O   
4384 C CB  . ARG B 241 ? 0.3755 0.4162 0.3189 0.0165  0.0228  0.0139  367 ARG B CB  
4385 C CG  . ARG B 241 ? 0.3503 0.3725 0.2914 0.0194  0.0245  0.0087  367 ARG B CG  
4386 C CD  . ARG B 241 ? 0.4086 0.4169 0.3420 0.0318  0.0268  0.0118  367 ARG B CD  
4387 N NE  . ARG B 241 ? 0.4477 0.4391 0.3737 0.0337  0.0257  0.0159  367 ARG B NE  
4388 C CZ  . ARG B 241 ? 0.4607 0.4394 0.3801 0.0466  0.0277  0.0216  367 ARG B CZ  
4389 N NH1 . ARG B 241 ? 0.4668 0.4516 0.3876 0.0608  0.0327  0.0231  367 ARG B NH1 
4390 N NH2 . ARG B 241 ? 0.5026 0.4621 0.4143 0.0459  0.0257  0.0270  367 ARG B NH2 
4391 N N   . LEU B 242 ? 0.3540 0.4014 0.3070 -0.0023 0.0224  -0.0005 368 LEU B N   
4392 C CA  . LEU B 242 ? 0.3540 0.4038 0.3108 -0.0058 0.0219  -0.0003 368 LEU B CA  
4393 C C   . LEU B 242 ? 0.3345 0.3753 0.2901 0.0019  0.0236  0.0015  368 LEU B C   
4394 O O   . LEU B 242 ? 0.3582 0.3836 0.3118 0.0034  0.0230  -0.0017 368 LEU B O   
4395 C CB  . LEU B 242 ? 0.3554 0.3923 0.3117 -0.0141 0.0216  -0.0073 368 LEU B CB  
4396 C CG  . LEU B 242 ? 0.3293 0.3647 0.2877 -0.0210 0.0200  -0.0051 368 LEU B CG  
4397 C CD1 . LEU B 242 ? 0.3923 0.4496 0.3518 -0.0303 0.0172  -0.0004 368 LEU B CD1 
4398 C CD2 . LEU B 242 ? 0.3981 0.4111 0.3545 -0.0256 0.0204  -0.0122 368 LEU B CD2 
4399 N N   . VAL B 243 ? 0.3377 0.3906 0.2938 0.0066  0.0260  0.0069  369 VAL B N   
4400 C CA  . VAL B 243 ? 0.3455 0.3895 0.2943 0.0127  0.0288  0.0073  369 VAL B CA  
4401 C C   . VAL B 243 ? 0.3371 0.3924 0.2888 0.0063  0.0300  0.0117  369 VAL B C   
4402 O O   . VAL B 243 ? 0.3660 0.4375 0.3266 -0.0024 0.0287  0.0153  369 VAL B O   
4403 C CB  . VAL B 243 ? 0.3637 0.4077 0.3058 0.0266  0.0342  0.0091  369 VAL B CB  
4404 C CG1 . VAL B 243 ? 0.3696 0.3994 0.3080 0.0307  0.0322  0.0073  369 VAL B CG1 
4405 C CG2 . VAL B 243 ? 0.3570 0.4311 0.3098 0.0317  0.0387  0.0171  369 VAL B CG2 
4406 N N   . LYS B 244 ? 0.3478 0.3935 0.2898 0.0079  0.0314  0.0122  370 LYS B N   
4407 C CA  . LYS B 244 ? 0.3459 0.4057 0.2892 0.0020  0.0341  0.0193  370 LYS B CA  
4408 C C   . LYS B 244 ? 0.3731 0.4590 0.3191 0.0103  0.0430  0.0246  370 LYS B C   
4409 O O   . LYS B 244 ? 0.4249 0.5367 0.3830 0.0028  0.0447  0.0327  370 LYS B O   
4410 C CB  . LYS B 244 ? 0.3686 0.4125 0.2990 -0.0005 0.0322  0.0205  370 LYS B CB  
4411 C CG  . LYS B 244 ? 0.3757 0.4013 0.3118 -0.0070 0.0237  0.0185  370 LYS B CG  
4412 C CD  . LYS B 244 ? 0.3721 0.3844 0.2997 -0.0095 0.0187  0.0228  370 LYS B CD  
4413 C CE  . LYS B 244 ? 0.3827 0.3803 0.3215 -0.0108 0.0117  0.0216  370 LYS B CE  
4414 N NZ  . LYS B 244 ? 0.4396 0.4282 0.3720 -0.0114 0.0046  0.0288  370 LYS B NZ  
4415 N N   . GLY B 245 ? 0.3873 0.4671 0.3235 0.0255  0.0490  0.0209  371 GLY B N   
4416 C CA  . GLY B 245 ? 0.3824 0.4876 0.3239 0.0387  0.0597  0.0262  371 GLY B CA  
4417 C C   . GLY B 245 ? 0.4137 0.5050 0.3330 0.0528  0.0702  0.0214  371 GLY B C   
4418 O O   . GLY B 245 ? 0.4325 0.5127 0.3348 0.0466  0.0707  0.0196  371 GLY B O   
4419 N N   . ALA B 246 ? 0.4055 0.4957 0.3222 0.0723  0.0790  0.0196  372 ALA B N   
4420 C CA  . ALA B 246 ? 0.4164 0.4808 0.3046 0.0873  0.0895  0.0107  372 ALA B CA  
4421 C C   . ALA B 246 ? 0.4618 0.5538 0.3491 0.1019  0.1076  0.0153  372 ALA B C   
4422 O O   . ALA B 246 ? 0.4925 0.5612 0.3502 0.1141  0.1186  0.0059  372 ALA B O   
4423 C CB  . ALA B 246 ? 0.4922 0.5269 0.3726 0.1021  0.0899  0.0044  372 ALA B CB  
4424 N N   . TYR B 247 ? 0.4355 0.5769 0.3527 0.0999  0.1113  0.0291  373 TYR B N   
4425 C CA  . TYR B 247 ? 0.4250 0.6028 0.3500 0.1174  0.1305  0.0363  373 TYR B CA  
4426 C C   . TYR B 247 ? 0.4415 0.6542 0.3721 0.1018  0.1350  0.0463  373 TYR B C   
4427 O O   . TYR B 247 ? 0.4464 0.7080 0.3981 0.1092  0.1481  0.0586  373 TYR B O   
4428 C CB  . TYR B 247 ? 0.4108 0.6277 0.3717 0.1309  0.1325  0.0486  373 TYR B CB  
4429 C CG  . TYR B 247 ? 0.4565 0.6417 0.4137 0.1471  0.1285  0.0429  373 TYR B CG  
4430 C CD1 . TYR B 247 ? 0.4207 0.5896 0.3835 0.1322  0.1101  0.0422  373 TYR B CD1 
4431 C CD2 . TYR B 247 ? 0.5176 0.6878 0.4646 0.1782  0.1443  0.0390  373 TYR B CD2 
4432 C CE1 . TYR B 247 ? 0.4729 0.6134 0.4314 0.1450  0.1064  0.0396  373 TYR B CE1 
4433 C CE2 . TYR B 247 ? 0.5308 0.6669 0.4732 0.1922  0.1399  0.0359  373 TYR B CE2 
4434 C CZ  . TYR B 247 ? 0.4814 0.6048 0.4303 0.1742  0.1204  0.0374  373 TYR B CZ  
4435 O OH  . TYR B 247 ? 0.5102 0.6006 0.4535 0.1854  0.1157  0.0366  373 TYR B OH  
4436 N N   . TRP B 248 ? 0.4752 0.6653 0.3882 0.0804  0.1247  0.0433  374 TRP B N   
4437 C CA  . TRP B 248 ? 0.4790 0.6992 0.4000 0.0613  0.1254  0.0561  374 TRP B CA  
4438 C C   . TRP B 248 ? 0.4873 0.7376 0.3998 0.0729  0.1473  0.0616  374 TRP B C   
4439 O O   . TRP B 248 ? 0.4562 0.7574 0.3939 0.0665  0.1546  0.0776  374 TRP B O   
4440 C CB  . TRP B 248 ? 0.4862 0.6713 0.3868 0.0409  0.1113  0.0529  374 TRP B CB  
4441 C CG  . TRP B 248 ? 0.4744 0.6843 0.3834 0.0203  0.1104  0.0679  374 TRP B CG  
4442 C CD1 . TRP B 248 ? 0.4669 0.6913 0.4011 0.0006  0.0994  0.0780  374 TRP B CD1 
4443 C CD2 . TRP B 248 ? 0.5007 0.7203 0.3894 0.0155  0.1206  0.0752  374 TRP B CD2 
4444 N NE1 . TRP B 248 ? 0.4049 0.6461 0.3380 -0.0169 0.1018  0.0921  374 TRP B NE1 
4445 C CE2 . TRP B 248 ? 0.4628 0.7035 0.3689 -0.0081 0.1148  0.0917  374 TRP B CE2 
4446 C CE3 . TRP B 248 ? 0.5217 0.7328 0.3758 0.0277  0.1345  0.0691  374 TRP B CE3 
4447 C CZ2 . TRP B 248 ? 0.4950 0.7504 0.3875 -0.0201 0.1222  0.1049  374 TRP B CZ2 
4448 C CZ3 . TRP B 248 ? 0.5632 0.7909 0.4019 0.0165  0.1424  0.0808  374 TRP B CZ3 
4449 C CH2 . TRP B 248 ? 0.5483 0.7993 0.4075 -0.0072 0.1362  0.0998  374 TRP B CH2 
4450 N N   . ASP B 249 ? 0.5378 0.7582 0.4131 0.0886  0.1587  0.0485  375 ASP B N   
4451 C CA  . ASP B 249 ? 0.5516 0.7983 0.4126 0.1009  0.1824  0.0517  375 ASP B CA  
4452 C C   . ASP B 249 ? 0.4926 0.7885 0.3870 0.1241  0.2001  0.0603  375 ASP B C   
4453 O O   . ASP B 249 ? 0.5436 0.8866 0.4548 0.1232  0.2131  0.0731  375 ASP B O   
4454 C CB  . ASP B 249 ? 0.6552 0.8532 0.4635 0.1139  0.1908  0.0324  375 ASP B CB  
4455 C CG  . ASP B 249 ? 0.6971 0.8620 0.4727 0.0900  0.1754  0.0294  375 ASP B CG  
4456 O OD1 . ASP B 249 ? 0.7428 0.9320 0.5152 0.0742  0.1778  0.0423  375 ASP B OD1 
4457 O OD2 . ASP B 249 ? 0.7597 0.8768 0.5150 0.0863  0.1602  0.0162  375 ASP B OD2 
4458 N N   . ALA B 250 ? 0.5439 0.8267 0.4520 0.1423  0.1968  0.0544  376 ALA B N   
4459 C CA  . ALA B 250 ? 0.5331 0.8611 0.4769 0.1660  0.2099  0.0645  376 ALA B CA  
4460 C C   . ALA B 250 ? 0.4697 0.8621 0.4624 0.1468  0.2013  0.0871  376 ALA B C   
4461 O O   . ALA B 250 ? 0.4963 0.9350 0.5161 0.1517  0.2096  0.0995  376 ALA B O   
4462 C CB  . ALA B 250 ? 0.5219 0.8171 0.4665 0.1884  0.2061  0.0557  376 ALA B CB  
4463 N N   . GLU B 251 ? 0.4643 0.8479 0.4666 0.1197  0.1784  0.0901  377 GLU B N   
4464 C CA  . GLU B 251 ? 0.4619 0.8989 0.5040 0.0963  0.1678  0.1094  377 GLU B CA  
4465 C C   . GLU B 251 ? 0.4256 0.9024 0.4724 0.0789  0.1774  0.1232  377 GLU B C   
4466 O O   . GLU B 251 ? 0.4200 0.9480 0.5017 0.0709  0.1760  0.1393  377 GLU B O   
4467 C CB  . GLU B 251 ? 0.3725 0.7756 0.4125 0.0692  0.1415  0.1048  377 GLU B CB  
4468 C CG  . GLU B 251 ? 0.3981 0.7703 0.4378 0.0812  0.1305  0.0949  377 GLU B CG  
4469 C CD  . GLU B 251 ? 0.4094 0.8304 0.4871 0.0908  0.1284  0.1087  377 GLU B CD  
4470 O OE1 . GLU B 251 ? 0.4109 0.8948 0.5190 0.0902  0.1361  0.1262  377 GLU B OE1 
4471 O OE2 . GLU B 251 ? 0.4578 0.8567 0.5355 0.0980  0.1182  0.1037  377 GLU B OE2 
4472 N N   . ILE B 252 ? 0.4381 0.8802 0.4481 0.0689  0.1801  0.1160  378 ILE B N   
4473 C CA  . ILE B 252 ? 0.4606 0.9288 0.4703 0.0516  0.1867  0.1282  378 ILE B CA  
4474 C C   . ILE B 252 ? 0.4801 0.9823 0.5027 0.0738  0.2054  0.1312  378 ILE B C   
4475 O O   . ILE B 252 ? 0.4759 1.0261 0.5260 0.0618  0.2073  0.1478  378 ILE B O   
4476 C CB  . ILE B 252 ? 0.4789 0.9034 0.4420 0.0413  0.1876  0.1208  378 ILE B CB  
4477 C CG1 . ILE B 252 ? 0.4912 0.8719 0.4477 0.0167  0.1619  0.1175  378 ILE B CG1 
4478 C CG2 . ILE B 252 ? 0.5282 0.9756 0.4872 0.0272  0.1962  0.1328  378 ILE B CG2 
4479 C CD1 . ILE B 252 ? 0.5228 0.9304 0.5150 -0.0100 0.1469  0.1324  378 ILE B CD1 
4480 N N   . LYS B 253 ? 0.4802 0.9563 0.4826 0.1061  0.2191  0.1154  379 LYS B N   
4481 C CA  . LYS B 253 ? 0.5210 1.0229 0.5304 0.1293  0.2394  0.1164  379 LYS B CA  
4482 C C   . LYS B 253 ? 0.5180 1.0742 0.5788 0.1397  0.2375  0.1320  379 LYS B C   
4483 O O   . LYS B 253 ? 0.5543 1.1574 0.6373 0.1447  0.2491  0.1441  379 LYS B O   
4484 C CB  . LYS B 253 ? 0.5896 1.0395 0.5592 0.1592  0.2531  0.0935  379 LYS B CB  
4485 N N   . ARG B 254 ? 0.5357 1.0889 0.6157 0.1421  0.2225  0.1333  380 ARG B N   
4486 C CA  . ARG B 254 ? 0.5236 1.1286 0.6505 0.1497  0.2170  0.1501  380 ARG B CA  
4487 C C   . ARG B 254 ? 0.4676 1.1280 0.6271 0.1163  0.2049  0.1713  380 ARG B C   
4488 O O   . ARG B 254 ? 0.4728 1.1880 0.6656 0.1207  0.2083  0.1878  380 ARG B O   
4489 C CB  . ARG B 254 ? 0.5757 1.1593 0.7089 0.1578  0.2027  0.1460  380 ARG B CB  
4490 C CG  . ARG B 254 ? 0.5615 1.1975 0.7403 0.1588  0.1910  0.1653  380 ARG B CG  
4491 C CD  . ARG B 254 ? 0.6350 1.2441 0.8137 0.1687  0.1787  0.1602  380 ARG B CD  
4492 N NE  . ARG B 254 ? 0.7118 1.2808 0.8723 0.2075  0.1928  0.1482  380 ARG B NE  
4493 C CZ  . ARG B 254 ? 0.6538 1.1968 0.8137 0.2238  0.1858  0.1453  380 ARG B CZ  
4494 N NH1 . ARG B 254 ? 0.5847 1.1411 0.7613 0.2060  0.1656  0.1529  380 ARG B NH1 
4495 N NH2 . ARG B 254 ? 0.7034 1.2043 0.8439 0.2576  0.1991  0.1347  380 ARG B NH2 
4496 N N   . ALA B 255 ? 0.5046 1.1492 0.6536 0.0820  0.1901  0.1715  381 ALA B N   
4497 C CA  . ALA B 255 ? 0.4828 1.1681 0.6567 0.0461  0.1765  0.1899  381 ALA B CA  
4498 C C   . ALA B 255 ? 0.5037 1.2231 0.6823 0.0423  0.1909  0.2007  381 ALA B C   
4499 O O   . ALA B 255 ? 0.4768 1.2505 0.6886 0.0295  0.1863  0.2194  381 ALA B O   
4500 C CB  . ALA B 255 ? 0.4418 1.0901 0.5962 0.0122  0.1603  0.1857  381 ALA B CB  
4501 N N   . GLN B 256 ? 0.5226 1.2118 0.6663 0.0520  0.2081  0.1897  382 GLN B N   
4502 C CA  . GLN B 256 ? 0.4947 1.2162 0.6398 0.0506  0.2246  0.1991  382 GLN B CA  
4503 C C   . GLN B 256 ? 0.5168 1.2842 0.6892 0.0818  0.2409  0.2052  382 GLN B C   
4504 O O   . GLN B 256 ? 0.5330 1.3562 0.7330 0.0739  0.2458  0.2232  382 GLN B O   
4505 C CB  . GLN B 256 ? 0.5856 1.2605 0.6814 0.0543  0.2387  0.1846  382 GLN B CB  
4506 C CG  . GLN B 256 ? 0.5807 1.2136 0.6502 0.0232  0.2227  0.1828  382 GLN B CG  
4507 C CD  . GLN B 256 ? 0.6646 1.2474 0.6813 0.0290  0.2333  0.1680  382 GLN B CD  
4508 O OE1 . GLN B 256 ? 0.6473 1.2030 0.6393 0.0577  0.2463  0.1501  382 GLN B OE1 
4509 N NE2 . GLN B 256 ? 0.6948 1.2622 0.6919 0.0006  0.2264  0.1759  382 GLN B NE2 
4510 N N   . LEU B 257 ? 0.5221 1.2662 0.6875 0.1174  0.2494  0.1914  383 LEU B N   
4511 C CA  . LEU B 257 ? 0.5490 1.3322 0.7399 0.1498  0.2653  0.1978  383 LEU B CA  
4512 C C   . LEU B 257 ? 0.5293 1.3689 0.7705 0.1447  0.2494  0.2193  383 LEU B C   
4513 O O   . LEU B 257 ? 0.5523 1.4475 0.8246 0.1575  0.2595  0.2347  383 LEU B O   
4514 C CB  . LEU B 257 ? 0.5915 1.3250 0.7567 0.1891  0.2783  0.1769  383 LEU B CB  
4515 N N   . ASP B 258 ? 0.4911 1.3192 0.7400 0.1256  0.2248  0.2210  384 ASP B N   
4516 C CA  . ASP B 258 ? 0.4759 1.3575 0.7673 0.1124  0.2063  0.2420  384 ASP B CA  
4517 C C   . ASP B 258 ? 0.4781 1.4067 0.7891 0.0741  0.1969  0.2608  384 ASP B C   
4518 O O   . ASP B 258 ? 0.4741 1.4517 0.8188 0.0596  0.1815  0.2797  384 ASP B O   
4519 C CB  . ASP B 258 ? 0.4917 1.3445 0.7806 0.1010  0.1830  0.2367  384 ASP B CB  
4520 C CG  . ASP B 258 ? 0.4832 1.3084 0.7676 0.1391  0.1879  0.2270  384 ASP B CG  
4521 O OD1 . ASP B 258 ? 0.5248 1.3523 0.8092 0.1744  0.2086  0.2248  384 ASP B OD1 
4522 O OD2 . ASP B 258 ? 0.6153 1.4140 0.8945 0.1331  0.1716  0.2214  384 ASP B OD2 
4523 N N   . GLY B 259 ? 0.4887 1.4016 0.7770 0.0559  0.2047  0.2569  385 GLY B N   
4524 C CA  . GLY B 259 ? 0.4988 1.4509 0.8022 0.0199  0.1977  0.2751  385 GLY B CA  
4525 C C   . GLY B 259 ? 0.4766 1.4088 0.7754 -0.0238 0.1706  0.2777  385 GLY B C   
4526 O O   . GLY B 259 ? 0.4887 1.4530 0.8026 -0.0566 0.1603  0.2944  385 GLY B O   
4527 N N   . LEU B 260 ? 0.4495 1.3282 0.7269 -0.0257 0.1591  0.2617  386 LEU B N   
4528 C CA  . LEU B 260 ? 0.4663 1.3211 0.7375 -0.0655 0.1341  0.2620  386 LEU B CA  
4529 C C   . LEU B 260 ? 0.4925 1.3204 0.7403 -0.0948 0.1344  0.2630  386 LEU B C   
4530 O O   . LEU B 260 ? 0.5332 1.3383 0.7567 -0.0817 0.1523  0.2558  386 LEU B O   
4531 C CB  . LEU B 260 ? 0.4925 1.2964 0.7453 -0.0574 0.1253  0.2439  386 LEU B CB  
4532 C CG  . LEU B 260 ? 0.4701 1.2882 0.7388 -0.0236 0.1270  0.2412  386 LEU B CG  
4533 C CD1 . LEU B 260 ? 0.4152 1.1859 0.6667 -0.0229 0.1155  0.2255  386 LEU B CD1 
4534 C CD2 . LEU B 260 ? 0.4298 1.3095 0.7360 -0.0308 0.1154  0.2613  386 LEU B CD2 
4535 N N   . ALA B 261 ? 0.4727 1.3003 0.7252 -0.1356 0.1136  0.2724  387 ALA B N   
4536 C CA  . ALA B 261 ? 0.5047 1.2972 0.7338 -0.1667 0.1095  0.2744  387 ALA B CA  
4537 C C   . ALA B 261 ? 0.5504 1.2719 0.7486 -0.1779 0.0984  0.2584  387 ALA B C   
4538 O O   . ALA B 261 ? 0.6134 1.2950 0.7867 -0.1959 0.0977  0.2584  387 ALA B O   
4539 C CB  . ALA B 261 ? 0.4969 1.3193 0.7438 -0.2060 0.0931  0.2930  387 ALA B CB  
4540 N N   . ASP B 262 ? 0.4821 1.1876 0.6815 -0.1673 0.0898  0.2462  388 ASP B N   
4541 C CA  . ASP B 262 ? 0.5175 1.1596 0.6902 -0.1763 0.0800  0.2311  388 ASP B CA  
4542 C C   . ASP B 262 ? 0.5321 1.1670 0.7042 -0.1437 0.0854  0.2167  388 ASP B C   
4543 O O   . ASP B 262 ? 0.5134 1.1862 0.7099 -0.1296 0.0828  0.2195  388 ASP B O   
4544 C CB  . ASP B 262 ? 0.5964 1.2179 0.7689 -0.2153 0.0551  0.2322  388 ASP B CB  
4545 C CG  . ASP B 262 ? 0.6892 1.2672 0.8397 -0.2472 0.0484  0.2365  388 ASP B CG  
4546 O OD1 . ASP B 262 ? 0.7822 1.3237 0.9090 -0.2389 0.0588  0.2328  388 ASP B OD1 
4547 O OD2 . ASP B 262 ? 0.6377 1.2151 0.7921 -0.2804 0.0321  0.2440  388 ASP B OD2 
4548 N N   . PHE B 263 ? 0.4955 1.0798 0.6384 -0.1332 0.0912  0.2028  389 PHE B N   
4549 C CA  . PHE B 263 ? 0.4492 1.0190 0.5842 -0.1005 0.0995  0.1884  389 PHE B CA  
4550 C C   . PHE B 263 ? 0.3944 0.9373 0.5298 -0.1073 0.0803  0.1773  389 PHE B C   
4551 O O   . PHE B 263 ? 0.4208 0.9389 0.5508 -0.1384 0.0626  0.1765  389 PHE B O   
4552 C CB  . PHE B 263 ? 0.4752 0.9912 0.5715 -0.0876 0.1089  0.1757  389 PHE B CB  
4553 C CG  . PHE B 263 ? 0.4837 1.0152 0.5699 -0.0824 0.1261  0.1836  389 PHE B CG  
4554 C CD1 . PHE B 263 ? 0.4558 1.0039 0.5392 -0.0484 0.1454  0.1782  389 PHE B CD1 
4555 C CD2 . PHE B 263 ? 0.5186 1.0384 0.5943 -0.1108 0.1214  0.1943  389 PHE B CD2 
4556 C CE1 . PHE B 263 ? 0.5069 1.0633 0.5766 -0.0437 0.1606  0.1823  389 PHE B CE1 
4557 C CE2 . PHE B 263 ? 0.5255 1.0564 0.5893 -0.1061 0.1358  0.2006  389 PHE B CE2 
4558 C CZ  . PHE B 263 ? 0.5566 1.1073 0.6169 -0.0730 0.1559  0.1941  389 PHE B CZ  
4559 N N   . PRO B 264 ? 0.3724 0.9111 0.5097 -0.0774 0.0826  0.1667  390 PRO B N   
4560 C CA  . PRO B 264 ? 0.3729 0.8765 0.5031 -0.0812 0.0644  0.1536  390 PRO B CA  
4561 C C   . PRO B 264 ? 0.3893 0.8161 0.4835 -0.0776 0.0598  0.1330  390 PRO B C   
4562 O O   . PRO B 264 ? 0.3918 0.7854 0.4768 -0.0847 0.0457  0.1217  390 PRO B O   
4563 C CB  . PRO B 264 ? 0.4093 0.9438 0.5576 -0.0494 0.0705  0.1549  390 PRO B CB  
4564 C CG  . PRO B 264 ? 0.3964 0.9432 0.5421 -0.0196 0.0945  0.1563  390 PRO B CG  
4565 C CD  . PRO B 264 ? 0.3352 0.9108 0.4859 -0.0405 0.1022  0.1700  390 PRO B CD  
4566 N N   . VAL B 265 ? 0.3923 0.7938 0.4660 -0.0670 0.0714  0.1288  391 VAL B N   
4567 C CA  . VAL B 265 ? 0.4239 0.7609 0.4669 -0.0620 0.0675  0.1124  391 VAL B CA  
4568 C C   . VAL B 265 ? 0.4000 0.7159 0.4285 -0.0824 0.0661  0.1182  391 VAL B C   
4569 O O   . VAL B 265 ? 0.4017 0.7525 0.4395 -0.0954 0.0728  0.1342  391 VAL B O   
4570 C CB  . VAL B 265 ? 0.4092 0.7303 0.4362 -0.0302 0.0801  0.1019  391 VAL B CB  
4571 C CG1 . VAL B 265 ? 0.3474 0.6807 0.3871 -0.0098 0.0804  0.0975  391 VAL B CG1 
4572 C CG2 . VAL B 265 ? 0.4197 0.7706 0.4439 -0.0202 0.0989  0.1109  391 VAL B CG2 
4573 N N   . PHE B 266 ? 0.4208 0.6810 0.4278 -0.0848 0.0575  0.1070  392 PHE B N   
4574 C CA  . PHE B 266 ? 0.4298 0.6639 0.4210 -0.0996 0.0555  0.1135  392 PHE B CA  
4575 C C   . PHE B 266 ? 0.4676 0.7117 0.4433 -0.0862 0.0697  0.1184  392 PHE B C   
4576 O O   . PHE B 266 ? 0.4761 0.7268 0.4451 -0.0623 0.0795  0.1099  392 PHE B O   
4577 C CB  . PHE B 266 ? 0.4551 0.6307 0.4306 -0.1006 0.0435  0.1015  392 PHE B CB  
4578 C CG  . PHE B 266 ? 0.4379 0.5973 0.4213 -0.1142 0.0316  0.0947  392 PHE B CG  
4579 C CD1 . PHE B 266 ? 0.4961 0.6585 0.4856 -0.1420 0.0249  0.1040  392 PHE B CD1 
4580 C CD2 . PHE B 266 ? 0.4152 0.5549 0.3967 -0.1012 0.0273  0.0789  392 PHE B CD2 
4581 C CE1 . PHE B 266 ? 0.5007 0.6434 0.4907 -0.1560 0.0138  0.0951  392 PHE B CE1 
4582 C CE2 . PHE B 266 ? 0.4585 0.5826 0.4419 -0.1138 0.0178  0.0711  392 PHE B CE2 
4583 C CZ  . PHE B 266 ? 0.4777 0.6018 0.4635 -0.1409 0.0110  0.0781  392 PHE B CZ  
4584 N N   . THR B 267 ? 0.4523 0.6948 0.4190 -0.1030 0.0707  0.1323  393 THR B N   
4585 C CA  . THR B 267 ? 0.4515 0.7026 0.3976 -0.0944 0.0838  0.1382  393 THR B CA  
4586 C C   . THR B 267 ? 0.4903 0.6931 0.4085 -0.0965 0.0753  0.1370  393 THR B C   
4587 O O   . THR B 267 ? 0.5236 0.7274 0.4176 -0.0890 0.0836  0.1394  393 THR B O   
4588 C CB  . THR B 267 ? 0.5190 0.8169 0.4752 -0.1116 0.0944  0.1596  393 THR B CB  
4589 O OG1 . THR B 267 ? 0.5450 0.8246 0.5048 -0.1419 0.0815  0.1726  393 THR B OG1 
4590 C CG2 . THR B 267 ? 0.5167 0.8735 0.5049 -0.1062 0.1039  0.1635  393 THR B CG2 
4591 N N   . ARG B 268 ? 0.5292 0.6911 0.4491 -0.1058 0.0592  0.1339  394 ARG B N   
4592 C CA  . ARG B 268 ? 0.4953 0.6141 0.3946 -0.1038 0.0497  0.1338  394 ARG B CA  
4593 C C   . ARG B 268 ? 0.4789 0.5712 0.3795 -0.0868 0.0422  0.1147  394 ARG B C   
4594 O O   . ARG B 268 ? 0.5147 0.6001 0.4323 -0.0875 0.0371  0.1058  394 ARG B O   
4595 C CB  . ARG B 268 ? 0.5605 0.6510 0.4613 -0.1254 0.0388  0.1477  394 ARG B CB  
4596 N N   . LYS B 269 ? 0.5473 0.6270 0.4284 -0.0733 0.0415  0.1090  395 LYS B N   
4597 C CA  . LYS B 269 ? 0.5193 0.5809 0.4022 -0.0584 0.0357  0.0922  395 LYS B CA  
4598 C C   . LYS B 269 ? 0.5104 0.5425 0.4077 -0.0620 0.0233  0.0900  395 LYS B C   
4599 O O   . LYS B 269 ? 0.4956 0.5218 0.4047 -0.0545 0.0212  0.0771  395 LYS B O   
4600 C CB  . LYS B 269 ? 0.5068 0.5583 0.3638 -0.0492 0.0343  0.0889  395 LYS B CB  
4601 C CG  . LYS B 269 ? 0.4839 0.5233 0.3409 -0.0356 0.0308  0.0719  395 LYS B CG  
4602 C CD  . LYS B 269 ? 0.4882 0.5031 0.3534 -0.0359 0.0160  0.0714  395 LYS B CD  
4603 C CE  . LYS B 269 ? 0.4935 0.5006 0.3591 -0.0256 0.0129  0.0568  395 LYS B CE  
4604 N NZ  . LYS B 269 ? 0.4800 0.4724 0.3633 -0.0249 0.0014  0.0569  395 LYS B NZ  
4605 N N   . ILE B 270 ? 0.5387 0.5506 0.4337 -0.0726 0.0161  0.1031  396 ILE B N   
4606 C CA  . ILE B 270 ? 0.5304 0.5102 0.4377 -0.0725 0.0068  0.1004  396 ILE B CA  
4607 C C   . ILE B 270 ? 0.5137 0.4927 0.4354 -0.0812 0.0087  0.0931  396 ILE B C   
4608 O O   . ILE B 270 ? 0.5303 0.4861 0.4603 -0.0773 0.0046  0.0833  396 ILE B O   
4609 C CB  . ILE B 270 ? 0.5914 0.5458 0.4917 -0.0798 -0.0010 0.1181  396 ILE B CB  
4610 C CG1 . ILE B 270 ? 0.6674 0.5861 0.5797 -0.0721 -0.0092 0.1146  396 ILE B CG1 
4611 C CG2 . ILE B 270 ? 0.6134 0.5712 0.5110 -0.1003 0.0022  0.1323  396 ILE B CG2 
4612 C CD1 . ILE B 270 ? 0.7218 0.6138 0.6287 -0.0729 -0.0182 0.1338  396 ILE B CD1 
4613 N N   . HIS B 271 ? 0.5083 0.5145 0.4328 -0.0939 0.0149  0.0983  397 HIS B N   
4614 C CA  . HIS B 271 ? 0.5117 0.5224 0.4487 -0.1045 0.0143  0.0915  397 HIS B CA  
4615 C C   . HIS B 271 ? 0.4714 0.4935 0.4157 -0.0898 0.0163  0.0748  397 HIS B C   
4616 O O   . HIS B 271 ? 0.4521 0.4600 0.4014 -0.0925 0.0124  0.0644  397 HIS B O   
4617 C CB  . HIS B 271 ? 0.5153 0.5627 0.4579 -0.1218 0.0196  0.1037  397 HIS B CB  
4618 C CG  . HIS B 271 ? 0.5770 0.6109 0.5134 -0.1426 0.0168  0.1216  397 HIS B CG  
4619 N ND1 . HIS B 271 ? 0.5645 0.6332 0.5067 -0.1619 0.0216  0.1368  397 HIS B ND1 
4620 C CD2 . HIS B 271 ? 0.5565 0.5461 0.4824 -0.1473 0.0095  0.1287  397 HIS B CD2 
4621 C CE1 . HIS B 271 ? 0.6277 0.6719 0.5609 -0.1799 0.0172  0.1525  397 HIS B CE1 
4622 N NE2 . HIS B 271 ? 0.6408 0.6345 0.5634 -0.1705 0.0095  0.1479  397 HIS B NE2 
4623 N N   . THR B 272 ? 0.4571 0.5015 0.3986 -0.0747 0.0225  0.0719  398 THR B N   
4624 C CA  . THR B 272 ? 0.4141 0.4633 0.3604 -0.0605 0.0237  0.0581  398 THR B CA  
4625 C C   . THR B 272 ? 0.4474 0.4643 0.3926 -0.0529 0.0173  0.0488  398 THR B C   
4626 O O   . THR B 272 ? 0.4336 0.4474 0.3848 -0.0489 0.0165  0.0381  398 THR B O   
4627 C CB  . THR B 272 ? 0.4008 0.4704 0.3399 -0.0460 0.0318  0.0570  398 THR B CB  
4628 O OG1 . THR B 272 ? 0.4046 0.5107 0.3503 -0.0498 0.0403  0.0652  398 THR B OG1 
4629 C CG2 . THR B 272 ? 0.3765 0.4434 0.3181 -0.0319 0.0319  0.0442  398 THR B CG2 
4630 N N   . ASP B 273 ? 0.4768 0.4728 0.4154 -0.0509 0.0130  0.0544  399 ASP B N   
4631 C CA  . ASP B 273 ? 0.4712 0.4435 0.4143 -0.0418 0.0077  0.0483  399 ASP B CA  
4632 C C   . ASP B 273 ? 0.4867 0.4360 0.4365 -0.0471 0.0062  0.0430  399 ASP B C   
4633 O O   . ASP B 273 ? 0.4949 0.4360 0.4507 -0.0390 0.0069  0.0320  399 ASP B O   
4634 C CB  . ASP B 273 ? 0.4824 0.4423 0.4195 -0.0383 0.0017  0.0591  399 ASP B CB  
4635 C CG  . ASP B 273 ? 0.4912 0.4665 0.4164 -0.0320 0.0015  0.0593  399 ASP B CG  
4636 O OD1 . ASP B 273 ? 0.5168 0.5044 0.4410 -0.0264 0.0059  0.0489  399 ASP B OD1 
4637 O OD2 . ASP B 273 ? 0.5250 0.4968 0.4389 -0.0334 -0.0037 0.0702  399 ASP B OD2 
4638 N N   . VAL B 274 ? 0.5106 0.4472 0.4570 -0.0616 0.0047  0.0505  400 VAL B N   
4639 C CA  . VAL B 274 ? 0.5045 0.4124 0.4508 -0.0692 0.0035  0.0431  400 VAL B CA  
4640 C C   . VAL B 274 ? 0.4939 0.4187 0.4412 -0.0744 0.0059  0.0305  400 VAL B C   
4641 O O   . VAL B 274 ? 0.5082 0.4142 0.4532 -0.0718 0.0068  0.0175  400 VAL B O   
4642 C CB  . VAL B 274 ? 0.5336 0.4212 0.4732 -0.0879 0.0001  0.0548  400 VAL B CB  
4643 C CG1 . VAL B 274 ? 0.5858 0.4362 0.5192 -0.0977 -0.0014 0.0441  400 VAL B CG1 
4644 C CG2 . VAL B 274 ? 0.5847 0.4533 0.5220 -0.0818 -0.0035 0.0696  400 VAL B CG2 
4645 N N   . SER B 275 ? 0.4843 0.4458 0.4343 -0.0815 0.0075  0.0352  401 SER B N   
4646 C CA  . SER B 275 ? 0.4661 0.4499 0.4189 -0.0853 0.0080  0.0272  401 SER B CA  
4647 C C   . SER B 275 ? 0.4579 0.4400 0.4117 -0.0685 0.0105  0.0152  401 SER B C   
4648 O O   . SER B 275 ? 0.4617 0.4385 0.4116 -0.0715 0.0099  0.0047  401 SER B O   
4649 C CB  . SER B 275 ? 0.4606 0.4892 0.4213 -0.0880 0.0109  0.0374  401 SER B CB  
4650 O OG  . SER B 275 ? 0.4374 0.4923 0.4038 -0.0901 0.0101  0.0334  401 SER B OG  
4651 N N   . TYR B 276 ? 0.4621 0.4478 0.4186 -0.0527 0.0128  0.0169  402 TYR B N   
4652 C CA  . TYR B 276 ? 0.4390 0.4250 0.3975 -0.0394 0.0147  0.0080  402 TYR B CA  
4653 C C   . TYR B 276 ? 0.4696 0.4287 0.4278 -0.0363 0.0153  -0.0009 402 TYR B C   
4654 O O   . TYR B 276 ? 0.4171 0.3775 0.3739 -0.0337 0.0180  -0.0104 402 TYR B O   
4655 C CB  . TYR B 276 ? 0.3842 0.3757 0.3432 -0.0277 0.0151  0.0124  402 TYR B CB  
4656 C CG  . TYR B 276 ? 0.3744 0.3706 0.3355 -0.0177 0.0165  0.0056  402 TYR B CG  
4657 C CD1 . TYR B 276 ? 0.3964 0.3806 0.3631 -0.0121 0.0162  0.0008  402 TYR B CD1 
4658 C CD2 . TYR B 276 ? 0.3809 0.3935 0.3389 -0.0134 0.0188  0.0057  402 TYR B CD2 
4659 C CE1 . TYR B 276 ? 0.3956 0.3866 0.3648 -0.0061 0.0174  -0.0030 402 TYR B CE1 
4660 C CE2 . TYR B 276 ? 0.3472 0.3595 0.3051 -0.0066 0.0193  0.0014  402 TYR B CE2 
4661 C CZ  . TYR B 276 ? 0.3803 0.3828 0.3435 -0.0048 0.0183  -0.0026 402 TYR B CZ  
4662 O OH  . TYR B 276 ? 0.3842 0.3887 0.3479 -0.0010 0.0188  -0.0050 402 TYR B OH  
4663 N N   . ILE B 277 ? 0.4449 0.3796 0.4040 -0.0349 0.0138  0.0028  403 ILE B N   
4664 C CA  . ILE B 277 ? 0.4724 0.3807 0.4330 -0.0272 0.0169  -0.0056 403 ILE B CA  
4665 C C   . ILE B 277 ? 0.5152 0.4051 0.4629 -0.0387 0.0189  -0.0172 403 ILE B C   
4666 O O   . ILE B 277 ? 0.5325 0.4115 0.4761 -0.0326 0.0246  -0.0296 403 ILE B O   
4667 C CB  . ILE B 277 ? 0.5370 0.4221 0.5030 -0.0207 0.0143  0.0036  403 ILE B CB  
4668 C CG1 . ILE B 277 ? 0.4885 0.3939 0.4635 -0.0120 0.0101  0.0145  403 ILE B CG1 
4669 C CG2 . ILE B 277 ? 0.5370 0.3953 0.5073 -0.0082 0.0198  -0.0047 403 ILE B CG2 
4670 C CD1 . ILE B 277 ? 0.4866 0.4080 0.4724 0.0000  0.0126  0.0092  403 ILE B CD1 
4671 N N   . ALA B 278 ? 0.5128 0.3992 0.4522 -0.0570 0.0142  -0.0131 404 ALA B N   
4672 C CA  . ALA B 278 ? 0.5454 0.4156 0.4689 -0.0732 0.0132  -0.0240 404 ALA B CA  
4673 C C   . ALA B 278 ? 0.5201 0.4178 0.4399 -0.0744 0.0143  -0.0321 404 ALA B C   
4674 O O   . ALA B 278 ? 0.5542 0.4356 0.4586 -0.0785 0.0166  -0.0460 404 ALA B O   
4675 C CB  . ALA B 278 ? 0.5706 0.4417 0.4896 -0.0963 0.0061  -0.0145 404 ALA B CB  
4676 N N   . CYS B 279 ? 0.5017 0.4387 0.4329 -0.0704 0.0130  -0.0234 405 CYS B N   
4677 C CA  . CYS B 279 ? 0.4491 0.4110 0.3772 -0.0706 0.0130  -0.0277 405 CYS B CA  
4678 C C   . CYS B 279 ? 0.4941 0.4489 0.4210 -0.0552 0.0201  -0.0367 405 CYS B C   
4679 O O   . CYS B 279 ? 0.5192 0.4765 0.4342 -0.0585 0.0217  -0.0453 405 CYS B O   
4680 C CB  . CYS B 279 ? 0.4316 0.4323 0.3724 -0.0678 0.0109  -0.0151 405 CYS B CB  
4681 S SG  . CYS B 279 ? 0.5438 0.5668 0.4877 -0.0895 0.0038  -0.0045 405 CYS B SG  
4682 N N   . ALA B 280 ? 0.4676 0.4160 0.4063 -0.0401 0.0239  -0.0337 406 ALA B N   
4683 C CA  . ALA B 280 ? 0.4754 0.4212 0.4173 -0.0269 0.0310  -0.0401 406 ALA B CA  
4684 C C   . ALA B 280 ? 0.5452 0.4637 0.4738 -0.0270 0.0379  -0.0543 406 ALA B C   
4685 O O   . ALA B 280 ? 0.5087 0.4318 0.4309 -0.0228 0.0449  -0.0625 406 ALA B O   
4686 C CB  . ALA B 280 ? 0.4365 0.3826 0.3954 -0.0136 0.0314  -0.0325 406 ALA B CB  
4687 N N   . ALA B 281 ? 0.5541 0.4413 0.4761 -0.0317 0.0369  -0.0573 407 ALA B N   
4688 C CA  . ALA B 281 ? 0.5673 0.4194 0.4709 -0.0315 0.0444  -0.0732 407 ALA B CA  
4689 C C   . ALA B 281 ? 0.5871 0.4428 0.4655 -0.0480 0.0431  -0.0844 407 ALA B C   
4690 O O   . ALA B 281 ? 0.6347 0.4777 0.4959 -0.0443 0.0525  -0.0990 407 ALA B O   
4691 C CB  . ALA B 281 ? 0.6466 0.4580 0.5446 -0.0364 0.0416  -0.0729 407 ALA B CB  
4692 N N   . LYS B 282 ? 0.5853 0.4611 0.4607 -0.0663 0.0318  -0.0770 408 LYS B N   
4693 C CA  . LYS B 282 ? 0.5841 0.4705 0.4375 -0.0836 0.0271  -0.0840 408 LYS B CA  
4694 C C   . LYS B 282 ? 0.5519 0.4661 0.4056 -0.0739 0.0323  -0.0844 408 LYS B C   
4695 O O   . LYS B 282 ? 0.6209 0.5287 0.4502 -0.0790 0.0364  -0.0966 408 LYS B O   
4696 C CB  . LYS B 282 ? 0.6050 0.5180 0.4645 -0.1024 0.0135  -0.0710 408 LYS B CB  
4697 C CG  . LYS B 282 ? 0.6335 0.5657 0.4743 -0.1225 0.0047  -0.0737 408 LYS B CG  
4698 C CD  . LYS B 282 ? 0.6104 0.5829 0.4692 -0.1352 -0.0073 -0.0557 408 LYS B CD  
4699 C CE  . LYS B 282 ? 0.5949 0.5505 0.4569 -0.1510 -0.0125 -0.0515 408 LYS B CE  
4700 N NZ  . LYS B 282 ? 0.6959 0.6145 0.5274 -0.1756 -0.0182 -0.0656 408 LYS B NZ  
4701 N N   . LEU B 283 ? 0.5341 0.4759 0.4120 -0.0608 0.0325  -0.0711 409 LEU B N   
4702 C CA  . LEU B 283 ? 0.5590 0.5243 0.4386 -0.0528 0.0367  -0.0685 409 LEU B CA  
4703 C C   . LEU B 283 ? 0.5570 0.5080 0.4311 -0.0410 0.0507  -0.0796 409 LEU B C   
4704 O O   . LEU B 283 ? 0.5275 0.4889 0.3875 -0.0422 0.0558  -0.0837 409 LEU B O   
4705 C CB  . LEU B 283 ? 0.4737 0.4616 0.3777 -0.0424 0.0339  -0.0533 409 LEU B CB  
4706 C CG  . LEU B 283 ? 0.4365 0.4491 0.3453 -0.0495 0.0239  -0.0414 409 LEU B CG  
4707 C CD1 . LEU B 283 ? 0.4358 0.4588 0.3640 -0.0376 0.0234  -0.0301 409 LEU B CD1 
4708 C CD2 . LEU B 283 ? 0.4446 0.4776 0.3411 -0.0553 0.0206  -0.0389 409 LEU B CD2 
4709 N N   . LEU B 284 ? 0.5761 0.5069 0.4626 -0.0286 0.0574  -0.0826 410 LEU B N   
4710 C CA  . LEU B 284 ? 0.5485 0.4737 0.4377 -0.0135 0.0724  -0.0903 410 LEU B CA  
4711 C C   . LEU B 284 ? 0.6137 0.5132 0.4711 -0.0172 0.0823  -0.1097 410 LEU B C   
4712 O O   . LEU B 284 ? 0.6534 0.5552 0.5073 -0.0059 0.0974  -0.1172 410 LEU B O   
4713 C CB  . LEU B 284 ? 0.5491 0.4634 0.4637 0.0025  0.0754  -0.0854 410 LEU B CB  
4714 C CG  . LEU B 284 ? 0.5270 0.4703 0.4697 0.0084  0.0694  -0.0687 410 LEU B CG  
4715 C CD1 . LEU B 284 ? 0.5352 0.4682 0.4991 0.0188  0.0662  -0.0608 410 LEU B CD1 
4716 C CD2 . LEU B 284 ? 0.4984 0.4680 0.4506 0.0152  0.0780  -0.0664 410 LEU B CD2 
4717 N N   . ALA B 285 ? 0.6051 0.4812 0.4375 -0.0343 0.0746  -0.1180 411 ALA B N   
4718 C CA  . ALA B 285 ? 0.6799 0.5263 0.4734 -0.0426 0.0816  -0.1385 411 ALA B CA  
4719 C C   . ALA B 285 ? 0.6399 0.5102 0.4080 -0.0589 0.0768  -0.1399 411 ALA B C   
4720 O O   . ALA B 285 ? 0.7172 0.5663 0.4467 -0.0684 0.0820  -0.1575 411 ALA B O   
4721 C CB  . ALA B 285 ? 0.7098 0.5143 0.4863 -0.0570 0.0735  -0.1465 411 ALA B CB  
4722 N N   . ALA B 286 ? 0.6113 0.5230 0.3979 -0.0615 0.0674  -0.1218 412 ALA B N   
4723 C CA  . ALA B 286 ? 0.6386 0.5762 0.4053 -0.0759 0.0599  -0.1177 412 ALA B CA  
4724 C C   . ALA B 286 ? 0.6113 0.5808 0.3925 -0.0646 0.0660  -0.1054 412 ALA B C   
4725 O O   . ALA B 286 ? 0.5902 0.5863 0.3668 -0.0730 0.0566  -0.0934 412 ALA B O   
4726 C CB  . ALA B 286 ? 0.6488 0.6052 0.4224 -0.0923 0.0399  -0.1044 412 ALA B CB  
4727 N N   . THR B 287 ? 0.5794 0.5478 0.3794 -0.0463 0.0805  -0.1061 413 THR B N   
4728 C CA  . THR B 287 ? 0.5958 0.5940 0.4116 -0.0393 0.0846  -0.0923 413 THR B CA  
4729 C C   . THR B 287 ? 0.5839 0.5951 0.3697 -0.0472 0.0907  -0.0945 413 THR B C   
4730 O O   . THR B 287 ? 0.5745 0.6100 0.3693 -0.0460 0.0914  -0.0801 413 THR B O   
4731 C CB  . THR B 287 ? 0.5521 0.5521 0.3968 -0.0210 0.0977  -0.0911 413 THR B CB  
4732 O OG1 . THR B 287 ? 0.6142 0.5962 0.4447 -0.0124 0.1154  -0.1085 413 THR B OG1 
4733 C CG2 . THR B 287 ? 0.5466 0.5391 0.4209 -0.0142 0.0890  -0.0840 413 THR B CG2 
4734 N N   . ASP B 288 ? 0.6158 0.6091 0.3631 -0.0568 0.0949  -0.1118 414 ASP B N   
4735 C CA  . ASP B 288 ? 0.6330 0.6403 0.3455 -0.0680 0.0973  -0.1124 414 ASP B CA  
4736 C C   . ASP B 288 ? 0.6348 0.6665 0.3454 -0.0820 0.0767  -0.0935 414 ASP B C   
4737 O O   . ASP B 288 ? 0.6826 0.7356 0.3804 -0.0865 0.0769  -0.0824 414 ASP B O   
4738 C CB  . ASP B 288 ? 0.6990 0.6771 0.3643 -0.0775 0.1045  -0.1373 414 ASP B CB  
4739 C CG  . ASP B 288 ? 0.7625 0.7156 0.4164 -0.0921 0.0882  -0.1456 414 ASP B CG  
4740 O OD1 . ASP B 288 ? 0.7691 0.7130 0.4552 -0.0852 0.0827  -0.1410 414 ASP B OD1 
4741 O OD2 . ASP B 288 ? 0.8785 0.8217 0.4896 -0.1125 0.0805  -0.1561 414 ASP B OD2 
4742 N N   . VAL B 289 ? 0.6080 0.6387 0.3317 -0.0882 0.0594  -0.0879 415 VAL B N   
4743 C CA  . VAL B 289 ? 0.6081 0.6651 0.3318 -0.0991 0.0405  -0.0696 415 VAL B CA  
4744 C C   . VAL B 289 ? 0.5466 0.6176 0.3114 -0.0885 0.0319  -0.0510 415 VAL B C   
4745 O O   . VAL B 289 ? 0.5526 0.6471 0.3231 -0.0913 0.0189  -0.0331 415 VAL B O   
4746 C CB  . VAL B 289 ? 0.6423 0.6960 0.3389 -0.1206 0.0258  -0.0770 415 VAL B CB  
4747 C CG1 . VAL B 289 ? 0.7068 0.7451 0.3530 -0.1334 0.0333  -0.0958 415 VAL B CG1 
4748 C CG2 . VAL B 289 ? 0.6205 0.6528 0.3321 -0.1222 0.0223  -0.0860 415 VAL B CG2 
4749 N N   . VAL B 290 ? 0.5050 0.5624 0.2971 -0.0754 0.0386  -0.0541 416 VAL B N   
4750 C CA  . VAL B 290 ? 0.4918 0.5596 0.3166 -0.0647 0.0329  -0.0382 416 VAL B CA  
4751 C C   . VAL B 290 ? 0.4514 0.5112 0.2949 -0.0509 0.0451  -0.0386 416 VAL B C   
4752 O O   . VAL B 290 ? 0.4770 0.5249 0.3163 -0.0472 0.0577  -0.0511 416 VAL B O   
4753 C CB  . VAL B 290 ? 0.5246 0.5897 0.3651 -0.0664 0.0239  -0.0377 416 VAL B CB  
4754 C CG1 . VAL B 290 ? 0.4864 0.5684 0.3135 -0.0824 0.0100  -0.0335 416 VAL B CG1 
4755 C CG2 . VAL B 290 ? 0.4869 0.5246 0.3286 -0.0650 0.0314  -0.0536 416 VAL B CG2 
4756 N N   . PHE B 291 ? 0.4301 0.4975 0.2939 -0.0432 0.0411  -0.0242 417 PHE B N   
4757 C CA  . PHE B 291 ? 0.4251 0.4875 0.3082 -0.0337 0.0483  -0.0219 417 PHE B CA  
4758 C C   . PHE B 291 ? 0.4417 0.4959 0.3450 -0.0271 0.0430  -0.0207 417 PHE B C   
4759 O O   . PHE B 291 ? 0.3993 0.4564 0.3099 -0.0237 0.0358  -0.0101 417 PHE B O   
4760 C CB  . PHE B 291 ? 0.4507 0.5213 0.3346 -0.0334 0.0473  -0.0070 417 PHE B CB  
4761 C CG  . PHE B 291 ? 0.4262 0.4926 0.3294 -0.0284 0.0517  -0.0032 417 PHE B CG  
4762 C CD1 . PHE B 291 ? 0.4194 0.4896 0.3304 -0.0269 0.0630  -0.0105 417 PHE B CD1 
4763 C CD2 . PHE B 291 ? 0.3983 0.4574 0.3109 -0.0253 0.0445  0.0077  417 PHE B CD2 
4764 C CE1 . PHE B 291 ? 0.3882 0.4611 0.3196 -0.0248 0.0649  -0.0049 417 PHE B CE1 
4765 C CE2 . PHE B 291 ? 0.4252 0.4794 0.3520 -0.0249 0.0461  0.0107  417 PHE B CE2 
4766 C CZ  . PHE B 291 ? 0.3980 0.4622 0.3360 -0.0259 0.0552  0.0055  417 PHE B CZ  
4767 N N   . PRO B 292 ? 0.4144 0.4571 0.3255 -0.0239 0.0470  -0.0306 418 PRO B N   
4768 C CA  . PRO B 292 ? 0.4082 0.4441 0.3345 -0.0194 0.0413  -0.0280 418 PRO B CA  
4769 C C   . PRO B 292 ? 0.3855 0.4217 0.3268 -0.0129 0.0405  -0.0202 418 PRO B C   
4770 O O   . PRO B 292 ? 0.3777 0.4164 0.3265 -0.0110 0.0461  -0.0199 418 PRO B O   
4771 C CB  . PRO B 292 ? 0.4392 0.4597 0.3669 -0.0182 0.0460  -0.0392 418 PRO B CB  
4772 C CG  . PRO B 292 ? 0.4350 0.4514 0.3419 -0.0237 0.0531  -0.0504 418 PRO B CG  
4773 C CD  . PRO B 292 ? 0.4264 0.4593 0.3297 -0.0236 0.0572  -0.0443 418 PRO B CD  
4774 N N   . GLN B 293 ? 0.3555 0.3901 0.3004 -0.0104 0.0338  -0.0138 419 GLN B N   
4775 C CA  . GLN B 293 ? 0.3553 0.3841 0.3069 -0.0063 0.0312  -0.0079 419 GLN B CA  
4776 C C   . GLN B 293 ? 0.3584 0.3807 0.3153 -0.0032 0.0279  -0.0091 419 GLN B C   
4777 O O   . GLN B 293 ? 0.3464 0.3711 0.3000 -0.0017 0.0256  -0.0071 419 GLN B O   
4778 C CB  . GLN B 293 ? 0.3828 0.4109 0.3268 -0.0045 0.0282  0.0003  419 GLN B CB  
4779 C CG  . GLN B 293 ? 0.3719 0.4063 0.3087 -0.0092 0.0308  0.0043  419 GLN B CG  
4780 C CD  . GLN B 293 ? 0.3946 0.4266 0.3235 -0.0059 0.0269  0.0148  419 GLN B CD  
4781 O OE1 . GLN B 293 ? 0.4188 0.4574 0.3467 -0.0010 0.0235  0.0179  419 GLN B OE1 
4782 N NE2 . GLN B 293 ? 0.4041 0.4268 0.3289 -0.0084 0.0272  0.0220  419 GLN B NE2 
4783 N N   . PHE B 294 ? 0.3328 0.3508 0.2991 -0.0023 0.0280  -0.0108 420 PHE B N   
4784 C CA  . PHE B 294 ? 0.3792 0.3913 0.3486 -0.0005 0.0245  -0.0105 420 PHE B CA  
4785 C C   . PHE B 294 ? 0.3648 0.3708 0.3300 0.0006  0.0196  -0.0064 420 PHE B C   
4786 O O   . PHE B 294 ? 0.3572 0.3616 0.3277 -0.0012 0.0162  -0.0045 420 PHE B O   
4787 C CB  . PHE B 294 ? 0.3601 0.3701 0.3411 0.0014  0.0263  -0.0128 420 PHE B CB  
4788 C CG  . PHE B 294 ? 0.3673 0.3747 0.3457 0.0007  0.0325  -0.0199 420 PHE B CG  
4789 C CD1 . PHE B 294 ? 0.4015 0.4030 0.3702 -0.0043 0.0312  -0.0226 420 PHE B CD1 
4790 C CD2 . PHE B 294 ? 0.3500 0.3613 0.3334 0.0036  0.0399  -0.0242 420 PHE B CD2 
4791 C CE1 . PHE B 294 ? 0.4008 0.3944 0.3611 -0.0081 0.0356  -0.0312 420 PHE B CE1 
4792 C CE2 . PHE B 294 ? 0.3968 0.4003 0.3709 0.0030  0.0469  -0.0337 420 PHE B CE2 
4793 C CZ  . PHE B 294 ? 0.4044 0.3963 0.3650 -0.0039 0.0437  -0.0380 420 PHE B CZ  
4794 N N   . ALA B 295 ? 0.3459 0.3495 0.3010 0.0032  0.0194  -0.0051 421 ALA B N   
4795 C CA  . ALA B 295 ? 0.3744 0.3663 0.3182 0.0055  0.0168  -0.0040 421 ALA B CA  
4796 C C   . ALA B 295 ? 0.4233 0.4134 0.3646 0.0047  0.0141  -0.0032 421 ALA B C   
4797 O O   . ALA B 295 ? 0.4512 0.4476 0.3908 0.0065  0.0170  -0.0018 421 ALA B O   
4798 C CB  . ALA B 295 ? 0.3791 0.3694 0.3131 0.0127  0.0206  -0.0028 421 ALA B CB  
4799 N N   . THR B 296 ? 0.3720 0.3565 0.3133 0.0007  0.0079  -0.0022 422 THR B N   
4800 C CA  . THR B 296 ? 0.3748 0.3573 0.3101 -0.0007 0.0038  0.0007  422 THR B CA  
4801 C C   . THR B 296 ? 0.4107 0.3861 0.3388 -0.0068 -0.0054 0.0018  422 THR B C   
4802 O O   . THR B 296 ? 0.3926 0.3703 0.3301 -0.0111 -0.0089 0.0022  422 THR B O   
4803 C CB  . THR B 296 ? 0.3938 0.3838 0.3448 -0.0007 0.0035  0.0046  422 THR B CB  
4804 O OG1 . THR B 296 ? 0.4121 0.3992 0.3551 -0.0026 -0.0013 0.0104  422 THR B OG1 
4805 C CG2 . THR B 296 ? 0.4336 0.4294 0.4044 -0.0005 0.0014  0.0057  422 THR B CG2 
4806 N N   . HIS B 297 ? 0.4315 0.3996 0.3408 -0.0090 -0.0095 0.0028  423 HIS B N   
4807 C CA  . HIS B 297 ? 0.4401 0.4041 0.3409 -0.0181 -0.0216 0.0053  423 HIS B CA  
4808 C C   . HIS B 297 ? 0.4506 0.4260 0.3597 -0.0196 -0.0289 0.0150  423 HIS B C   
4809 O O   . HIS B 297 ? 0.4684 0.4435 0.3665 -0.0277 -0.0406 0.0194  423 HIS B O   
4810 C CB  . HIS B 297 ? 0.5006 0.4427 0.3655 -0.0213 -0.0223 -0.0019 423 HIS B CB  
4811 C CG  . HIS B 297 ? 0.5223 0.4478 0.3773 -0.0159 -0.0138 -0.0102 423 HIS B CG  
4812 N ND1 . HIS B 297 ? 0.5540 0.4712 0.3934 -0.0045 -0.0018 -0.0153 423 HIS B ND1 
4813 C CD2 . HIS B 297 ? 0.5103 0.4280 0.3713 -0.0193 -0.0150 -0.0121 423 HIS B CD2 
4814 C CE1 . HIS B 297 ? 0.5530 0.4559 0.3893 0.0007  0.0032  -0.0197 423 HIS B CE1 
4815 N NE2 . HIS B 297 ? 0.5513 0.4519 0.3985 -0.0092 -0.0049 -0.0178 423 HIS B NE2 
4816 N N   . ASN B 298 ? 0.4523 0.4352 0.3777 -0.0131 -0.0231 0.0191  424 ASN B N   
4817 C CA  . ASN B 298 ? 0.4325 0.4201 0.3645 -0.0128 -0.0288 0.0300  424 ASN B CA  
4818 C C   . ASN B 298 ? 0.4065 0.4057 0.3698 -0.0089 -0.0330 0.0360  424 ASN B C   
4819 O O   . ASN B 298 ? 0.4018 0.4024 0.3825 -0.0027 -0.0244 0.0318  424 ASN B O   
4820 C CB  . ASN B 298 ? 0.4212 0.4051 0.3504 -0.0096 -0.0200 0.0313  424 ASN B CB  
4821 C CG  . ASN B 298 ? 0.4365 0.4192 0.3706 -0.0101 -0.0258 0.0444  424 ASN B CG  
4822 O OD1 . ASN B 298 ? 0.4513 0.4374 0.4036 -0.0071 -0.0334 0.0520  424 ASN B OD1 
4823 N ND2 . ASN B 298 ? 0.4430 0.4221 0.3627 -0.0133 -0.0216 0.0488  424 ASN B ND2 
4824 N N   . ALA B 299 ? 0.4228 0.4323 0.3928 -0.0123 -0.0460 0.0462  425 ALA B N   
4825 C CA  . ALA B 299 ? 0.4203 0.4476 0.4245 -0.0063 -0.0490 0.0535  425 ALA B CA  
4826 C C   . ALA B 299 ? 0.3920 0.4141 0.4143 0.0065  -0.0422 0.0582  425 ALA B C   
4827 O O   . ALA B 299 ? 0.4065 0.4370 0.4552 0.0164  -0.0363 0.0581  425 ALA B O   
4828 C CB  . ALA B 299 ? 0.4414 0.4866 0.4512 -0.0132 -0.0666 0.0667  425 ALA B CB  
4829 N N   . GLN B 300 ? 0.3984 0.4046 0.4050 0.0061  -0.0422 0.0622  426 GLN B N   
4830 C CA  . GLN B 300 ? 0.4099 0.4022 0.4289 0.0157  -0.0366 0.0664  426 GLN B CA  
4831 C C   . GLN B 300 ? 0.4147 0.3954 0.4333 0.0177  -0.0222 0.0515  426 GLN B C   
4832 O O   . GLN B 300 ? 0.4388 0.4115 0.4734 0.0273  -0.0152 0.0485  426 GLN B O   
4833 C CB  . GLN B 300 ? 0.4367 0.4149 0.4369 0.0107  -0.0415 0.0770  426 GLN B CB  
4834 C CG  . GLN B 300 ? 0.4929 0.4518 0.5057 0.0195  -0.0402 0.0867  426 GLN B CG  
4835 C CD  . GLN B 300 ? 0.5140 0.4513 0.5250 0.0198  -0.0270 0.0740  426 GLN B CD  
4836 O OE1 . GLN B 300 ? 0.5405 0.4765 0.5340 0.0093  -0.0215 0.0655  426 GLN B OE1 
4837 N NE2 . GLN B 300 ? 0.5514 0.4723 0.5799 0.0321  -0.0219 0.0730  426 GLN B NE2 
4838 N N   . THR B 301 ? 0.4251 0.4044 0.4240 0.0092  -0.0177 0.0421  427 THR B N   
4839 C CA  . THR B 301 ? 0.3997 0.3741 0.3978 0.0092  -0.0068 0.0296  427 THR B CA  
4840 C C   . THR B 301 ? 0.3878 0.3723 0.4024 0.0152  -0.0021 0.0230  427 THR B C   
4841 O O   . THR B 301 ? 0.4105 0.3879 0.4310 0.0198  0.0066  0.0156  427 THR B O   
4842 C CB  . THR B 301 ? 0.4031 0.3816 0.3818 0.0017  -0.0041 0.0239  427 THR B CB  
4843 O OG1 . THR B 301 ? 0.3794 0.3543 0.3431 -0.0035 -0.0067 0.0312  427 THR B OG1 
4844 C CG2 . THR B 301 ? 0.4047 0.3817 0.3828 0.0003  0.0047  0.0143  427 THR B CG2 
4845 N N   . LEU B 302 ? 0.3557 0.3562 0.3747 0.0133  -0.0074 0.0253  428 LEU B N   
4846 C CA  . LEU B 302 ? 0.3697 0.3846 0.4046 0.0162  -0.0026 0.0215  428 LEU B CA  
4847 C C   . LEU B 302 ? 0.3547 0.3752 0.4151 0.0288  0.0015  0.0255  428 LEU B C   
4848 O O   . LEU B 302 ? 0.4116 0.4329 0.4793 0.0350  0.0132  0.0177  428 LEU B O   
4849 C CB  . LEU B 302 ? 0.3935 0.4229 0.4280 0.0079  -0.0116 0.0257  428 LEU B CB  
4850 C CG  . LEU B 302 ? 0.4037 0.4504 0.4511 0.0046  -0.0091 0.0246  428 LEU B CG  
4851 C CD1 . LEU B 302 ? 0.4748 0.5245 0.5118 -0.0086 -0.0215 0.0286  428 LEU B CD1 
4852 C CD2 . LEU B 302 ? 0.3491 0.4185 0.4288 0.0137  -0.0055 0.0310  428 LEU B CD2 
4853 N N   . ALA B 303 ? 0.4023 0.4268 0.4753 0.0339  -0.0073 0.0383  429 ALA B N   
4854 C CA  . ALA B 303 ? 0.3961 0.4251 0.4961 0.0503  -0.0026 0.0440  429 ALA B CA  
4855 C C   . ALA B 303 ? 0.3796 0.3785 0.4718 0.0585  0.0102  0.0334  429 ALA B C   
4856 O O   . ALA B 303 ? 0.4256 0.4244 0.5316 0.0715  0.0225  0.0276  429 ALA B O   
4857 C CB  . ALA B 303 ? 0.3923 0.4272 0.5044 0.0548  -0.0162 0.0622  429 ALA B CB  
4858 N N   . ALA B 304 ? 0.4230 0.3962 0.4914 0.0500  0.0080  0.0306  430 ALA B N   
4859 C CA  . ALA B 304 ? 0.4327 0.3737 0.4904 0.0529  0.0172  0.0211  430 ALA B CA  
4860 C C   . ALA B 304 ? 0.4384 0.3800 0.4888 0.0515  0.0297  0.0041  430 ALA B C   
4861 O O   . ALA B 304 ? 0.4765 0.4010 0.5282 0.0616  0.0408  -0.0050 430 ALA B O   
4862 C CB  . ALA B 304 ? 0.4509 0.3722 0.4859 0.0389  0.0114  0.0232  430 ALA B CB  
4863 N N   . ILE B 305 ? 0.4280 0.3871 0.4680 0.0398  0.0282  -0.0002 431 ILE B N   
4864 C CA  . ILE B 305 ? 0.4648 0.4274 0.4958 0.0371  0.0382  -0.0134 431 ILE B CA  
4865 C C   . ILE B 305 ? 0.4458 0.4260 0.4960 0.0493  0.0477  -0.0149 431 ILE B C   
4866 O O   . ILE B 305 ? 0.4861 0.4588 0.5304 0.0543  0.0605  -0.0265 431 ILE B O   
4867 C CB  . ILE B 305 ? 0.4583 0.4357 0.4767 0.0244  0.0334  -0.0137 431 ILE B CB  
4868 C CG1 . ILE B 305 ? 0.4989 0.4627 0.4990 0.0139  0.0291  -0.0149 431 ILE B CG1 
4869 C CG2 . ILE B 305 ? 0.4410 0.4307 0.4558 0.0230  0.0416  -0.0215 431 ILE B CG2 
4870 C CD1 . ILE B 305 ? 0.4705 0.4483 0.4622 0.0066  0.0244  -0.0119 431 ILE B CD1 
4871 N N   . TYR B 306 ? 0.4146 0.4210 0.4868 0.0525  0.0419  -0.0029 432 TYR B N   
4872 C CA  . TYR B 306 ? 0.3937 0.4267 0.4903 0.0628  0.0504  -0.0003 432 TYR B CA  
4873 C C   . TYR B 306 ? 0.4367 0.4562 0.5433 0.0822  0.0644  -0.0059 432 TYR B C   
4874 O O   . TYR B 306 ? 0.4606 0.4876 0.5687 0.0894  0.0801  -0.0150 432 TYR B O   
4875 C CB  . TYR B 306 ? 0.3796 0.4413 0.5003 0.0615  0.0377  0.0165  432 TYR B CB  
4876 C CG  . TYR B 306 ? 0.4351 0.5323 0.5900 0.0724  0.0444  0.0243  432 TYR B CG  
4877 C CD1 . TYR B 306 ? 0.3952 0.5165 0.5549 0.0674  0.0539  0.0211  432 TYR B CD1 
4878 C CD2 . TYR B 306 ? 0.4223 0.5332 0.6071 0.0876  0.0409  0.0376  432 TYR B CD2 
4879 C CE1 . TYR B 306 ? 0.4190 0.5803 0.6139 0.0768  0.0615  0.0304  432 TYR B CE1 
4880 C CE2 . TYR B 306 ? 0.3913 0.5427 0.6133 0.0992  0.0476  0.0471  432 TYR B CE2 
4881 C CZ  . TYR B 306 ? 0.4124 0.5906 0.6400 0.0931  0.0584  0.0433  432 TYR B CZ  
4882 O OH  . TYR B 306 ? 0.4273 0.6524 0.6955 0.1040  0.0661  0.0548  432 TYR B OH  
4883 N N   . HIS B 307 ? 0.4341 0.4299 0.5442 0.0913  0.0601  -0.0010 433 HIS B N   
4884 C CA  . HIS B 307 ? 0.4709 0.4457 0.5890 0.1125  0.0739  -0.0064 433 HIS B CA  
4885 C C   . HIS B 307 ? 0.5303 0.4616 0.6137 0.1079  0.0834  -0.0263 433 HIS B C   
4886 O O   . HIS B 307 ? 0.5522 0.4651 0.6324 0.1230  0.1000  -0.0383 433 HIS B O   
4887 C CB  . HIS B 307 ? 0.5183 0.4821 0.6547 0.1253  0.0648  0.0095  433 HIS B CB  
4888 C CG  . HIS B 307 ? 0.5031 0.5128 0.6766 0.1325  0.0561  0.0295  433 HIS B CG  
4889 N ND1 . HIS B 307 ? 0.4817 0.5208 0.6903 0.1541  0.0674  0.0352  433 HIS B ND1 
4890 C CD2 . HIS B 307 ? 0.4527 0.4867 0.6329 0.1195  0.0370  0.0451  433 HIS B CD2 
4891 C CE1 . HIS B 307 ? 0.4634 0.5461 0.7019 0.1523  0.0535  0.0554  433 HIS B CE1 
4892 N NE2 . HIS B 307 ? 0.4206 0.4981 0.6395 0.1305  0.0345  0.0606  433 HIS B NE2 
4893 N N   . MET B 308 ? 0.5283 0.4443 0.5851 0.0869  0.0736  -0.0301 434 MET B N   
4894 C CA  . MET B 308 ? 0.5683 0.4488 0.5919 0.0775  0.0796  -0.0478 434 MET B CA  
4895 C C   . MET B 308 ? 0.5930 0.4863 0.6042 0.0762  0.0929  -0.0623 434 MET B C   
4896 O O   . MET B 308 ? 0.6461 0.5094 0.6330 0.0769  0.1037  -0.0794 434 MET B O   
4897 C CB  . MET B 308 ? 0.5276 0.4019 0.5320 0.0548  0.0656  -0.0452 434 MET B CB  
4898 C CG  . MET B 308 ? 0.6402 0.4839 0.6122 0.0401  0.0679  -0.0606 434 MET B CG  
4899 S SD  . MET B 308 ? 0.7997 0.6556 0.7599 0.0152  0.0521  -0.0528 434 MET B SD  
4900 C CE  . MET B 308 ? 0.6042 0.4715 0.5879 0.0222  0.0421  -0.0318 434 MET B CE  
4901 N N   . ALA B 309 ? 0.5542 0.4889 0.5781 0.0727  0.0920  -0.0558 435 ALA B N   
4902 C CA  . ALA B 309 ? 0.5848 0.5344 0.5953 0.0691  0.1036  -0.0662 435 ALA B CA  
4903 C C   . ALA B 309 ? 0.5861 0.5382 0.6051 0.0892  0.1243  -0.0742 435 ALA B C   
4904 O O   . ALA B 309 ? 0.5996 0.5584 0.6007 0.0867  0.1370  -0.0853 435 ALA B O   
4905 C CB  . ALA B 309 ? 0.5176 0.5066 0.5398 0.0592  0.0963  -0.0543 435 ALA B CB  
4906 N N   . GLY B 310 ? 0.6299 0.5787 0.6756 0.1100  0.1288  -0.0680 436 GLY B N   
4907 C CA  . GLY B 310 ? 0.6124 0.5685 0.6717 0.1337  0.1508  -0.0739 436 GLY B CA  
4908 C C   . GLY B 310 ? 0.5354 0.5508 0.6317 0.1395  0.1552  -0.0591 436 GLY B C   
4909 O O   . GLY B 310 ? 0.5472 0.5935 0.6574 0.1244  0.1398  -0.0444 436 GLY B O   
4910 N N   . LYS B 311 ? 0.6159 0.6466 0.7272 0.1615  0.1778  -0.0635 437 LYS B N   
4911 C CA  . LYS B 311 ? 0.5926 0.6849 0.7445 0.1682  0.1846  -0.0478 437 LYS B CA  
4912 C C   . LYS B 311 ? 0.5760 0.6958 0.7118 0.1538  0.1957  -0.0530 437 LYS B C   
4913 O O   . LYS B 311 ? 0.5377 0.7102 0.7038 0.1497  0.1966  -0.0373 437 LYS B O   
4914 C CB  . LYS B 311 ? 0.5798 0.6843 0.7650 0.2029  0.2049  -0.0456 437 LYS B CB  
4915 N N   . ASP B 312 ? 0.5872 0.6738 0.6755 0.1443  0.2031  -0.0730 438 ASP B N   
4916 C CA  . ASP B 312 ? 0.5826 0.6939 0.6517 0.1295  0.2121  -0.0758 438 ASP B CA  
4917 C C   . ASP B 312 ? 0.5642 0.6833 0.6259 0.1014  0.1882  -0.0641 438 ASP B C   
4918 O O   . ASP B 312 ? 0.6152 0.7001 0.6539 0.0897  0.1716  -0.0689 438 ASP B O   
4919 C CB  . ASP B 312 ? 0.6703 0.7443 0.6884 0.1295  0.2282  -0.1010 438 ASP B CB  
4920 N N   . PHE B 313 ? 0.5114 0.6748 0.5933 0.0909  0.1866  -0.0481 439 PHE B N   
4921 C CA  . PHE B 313 ? 0.4323 0.5966 0.5041 0.0664  0.1658  -0.0380 439 PHE B CA  
4922 C C   . PHE B 313 ? 0.4804 0.6790 0.5508 0.0529  0.1730  -0.0287 439 PHE B C   
4923 O O   . PHE B 313 ? 0.4101 0.6480 0.5069 0.0598  0.1881  -0.0210 439 PHE B O   
4924 C CB  . PHE B 313 ? 0.4351 0.6071 0.5364 0.0622  0.1448  -0.0223 439 PHE B CB  
4925 C CG  . PHE B 313 ? 0.4054 0.5699 0.4912 0.0400  0.1258  -0.0151 439 PHE B CG  
4926 C CD1 . PHE B 313 ? 0.4053 0.5339 0.4631 0.0339  0.1141  -0.0229 439 PHE B CD1 
4927 C CD2 . PHE B 313 ? 0.3816 0.5741 0.4801 0.0255  0.1208  -0.0003 439 PHE B CD2 
4928 C CE1 . PHE B 313 ? 0.3843 0.5061 0.4288 0.0180  0.0994  -0.0165 439 PHE B CE1 
4929 C CE2 . PHE B 313 ? 0.3935 0.5713 0.4747 0.0078  0.1051  0.0051  439 PHE B CE2 
4930 C CZ  . PHE B 313 ? 0.3750 0.5177 0.4295 0.0062  0.0954  -0.0034 439 PHE B CZ  
4931 N N   . HIS B 314 ? 0.4596 0.6448 0.5011 0.0335  0.1616  -0.0271 440 HIS B N   
4932 C CA  . HIS B 314 ? 0.4286 0.6395 0.4675 0.0169  0.1626  -0.0138 440 HIS B CA  
4933 C C   . HIS B 314 ? 0.4126 0.6014 0.4360 0.0000  0.1400  -0.0067 440 HIS B C   
4934 O O   . HIS B 314 ? 0.4343 0.5916 0.4386 0.0011  0.1296  -0.0158 440 HIS B O   
4935 C CB  . HIS B 314 ? 0.4470 0.6635 0.4544 0.0153  0.1820  -0.0220 440 HIS B CB  
4936 C CG  . HIS B 314 ? 0.5049 0.6837 0.4678 0.0120  0.1775  -0.0379 440 HIS B CG  
4937 N ND1 . HIS B 314 ? 0.5453 0.6981 0.4911 0.0253  0.1865  -0.0585 440 HIS B ND1 
4938 C CD2 . HIS B 314 ? 0.5185 0.6815 0.4520 -0.0037 0.1634  -0.0348 440 HIS B CD2 
4939 C CE1 . HIS B 314 ? 0.5545 0.6795 0.4618 0.0146  0.1769  -0.0675 440 HIS B CE1 
4940 N NE2 . HIS B 314 ? 0.5304 0.6643 0.4318 -0.0018 0.1629  -0.0526 440 HIS B NE2 
4941 N N   . VAL B 315 ? 0.4258 0.6306 0.4580 -0.0154 0.1330  0.0101  441 VAL B N   
4942 C CA  . VAL B 315 ? 0.4324 0.6118 0.4471 -0.0285 0.1141  0.0163  441 VAL B CA  
4943 C C   . VAL B 315 ? 0.4039 0.5658 0.3807 -0.0312 0.1158  0.0097  441 VAL B C   
4944 O O   . VAL B 315 ? 0.4797 0.6561 0.4407 -0.0347 0.1292  0.0099  441 VAL B O   
4945 C CB  . VAL B 315 ? 0.4876 0.6802 0.5135 -0.0459 0.1074  0.0350  441 VAL B CB  
4946 N N   . GLY B 316 ? 0.4257 0.5603 0.3881 -0.0304 0.1021  0.0052  442 GLY B N   
4947 C CA  . GLY B 316 ? 0.4541 0.5752 0.3846 -0.0323 0.1003  -0.0011 442 GLY B CA  
4948 C C   . GLY B 316 ? 0.4763 0.5830 0.3986 -0.0234 0.1021  -0.0187 442 GLY B C   
4949 O O   . GLY B 316 ? 0.4785 0.5730 0.3768 -0.0274 0.0957  -0.0235 442 GLY B O   
4950 N N   . LYS B 317 ? 0.4779 0.5858 0.4198 -0.0122 0.1099  -0.0269 443 LYS B N   
4951 C CA  . LYS B 317 ? 0.4838 0.5702 0.4169 -0.0046 0.1107  -0.0426 443 LYS B CA  
4952 C C   . LYS B 317 ? 0.4474 0.5163 0.3837 -0.0068 0.0931  -0.0400 443 LYS B C   
4953 O O   . LYS B 317 ? 0.4808 0.5359 0.3967 -0.0121 0.0866  -0.0458 443 LYS B O   
4954 C CB  . LYS B 317 ? 0.4522 0.5421 0.4071 0.0107  0.1238  -0.0494 443 LYS B CB  
4955 C CG  . LYS B 317 ? 0.4819 0.5419 0.4301 0.0183  0.1223  -0.0629 443 LYS B CG  
4956 C CD  . LYS B 317 ? 0.5332 0.5889 0.4885 0.0355  0.1408  -0.0741 443 LYS B CD  
4957 C CE  . LYS B 317 ? 0.5719 0.5887 0.5159 0.0411  0.1381  -0.0871 443 LYS B CE  
4958 N NZ  . LYS B 317 ? 0.6991 0.7011 0.6372 0.0585  0.1592  -0.1025 443 LYS B NZ  
4959 N N   . TYR B 318 ? 0.4042 0.4762 0.3653 -0.0039 0.0855  -0.0308 444 TYR B N   
4960 C CA  . TYR B 318 ? 0.3972 0.4560 0.3605 -0.0056 0.0709  -0.0269 444 TYR B CA  
4961 C C   . TYR B 318 ? 0.3809 0.4475 0.3630 -0.0071 0.0644  -0.0151 444 TYR B C   
4962 O O   . TYR B 318 ? 0.3548 0.4386 0.3513 -0.0079 0.0701  -0.0097 444 TYR B O   
4963 C CB  . TYR B 318 ? 0.3827 0.4249 0.3494 0.0009  0.0693  -0.0354 444 TYR B CB  
4964 C CG  . TYR B 318 ? 0.3662 0.4114 0.3578 0.0112  0.0724  -0.0338 444 TYR B CG  
4965 C CD1 . TYR B 318 ? 0.3995 0.4468 0.4072 0.0114  0.0618  -0.0243 444 TYR B CD1 
4966 C CD2 . TYR B 318 ? 0.4581 0.5035 0.4558 0.0216  0.0858  -0.0415 444 TYR B CD2 
4967 C CE1 . TYR B 318 ? 0.4589 0.5128 0.4899 0.0199  0.0618  -0.0200 444 TYR B CE1 
4968 C CE2 . TYR B 318 ? 0.4636 0.5155 0.4884 0.0336  0.0879  -0.0369 444 TYR B CE2 
4969 C CZ  . TYR B 318 ? 0.4692 0.5272 0.5115 0.0318  0.0745  -0.0250 444 TYR B CZ  
4970 O OH  . TYR B 318 ? 0.5403 0.6085 0.6101 0.0429  0.0738  -0.0178 444 TYR B OH  
4971 N N   . GLU B 319 ? 0.3532 0.4078 0.3339 -0.0085 0.0527  -0.0112 445 GLU B N   
4972 C CA  . GLU B 319 ? 0.3682 0.4235 0.3611 -0.0114 0.0454  -0.0030 445 GLU B CA  
4973 C C   . GLU B 319 ? 0.3454 0.3866 0.3376 -0.0081 0.0364  -0.0042 445 GLU B C   
4974 O O   . GLU B 319 ? 0.3344 0.3670 0.3172 -0.0049 0.0357  -0.0090 445 GLU B O   
4975 C CB  . GLU B 319 ? 0.3724 0.4234 0.3550 -0.0198 0.0415  0.0054  445 GLU B CB  
4976 C CG  . GLU B 319 ? 0.3838 0.4182 0.3482 -0.0178 0.0360  0.0057  445 GLU B CG  
4977 C CD  . GLU B 319 ? 0.4104 0.4356 0.3633 -0.0231 0.0334  0.0151  445 GLU B CD  
4978 O OE1 . GLU B 319 ? 0.4079 0.4401 0.3648 -0.0315 0.0360  0.0213  445 GLU B OE1 
4979 O OE2 . GLU B 319 ? 0.4534 0.4651 0.3946 -0.0184 0.0292  0.0176  445 GLU B OE2 
4980 N N   . PHE B 320 ? 0.3188 0.3598 0.3199 -0.0109 0.0292  0.0009  446 PHE B N   
4981 C CA  . PHE B 320 ? 0.3138 0.3401 0.3071 -0.0099 0.0206  0.0007  446 PHE B CA  
4982 C C   . PHE B 320 ? 0.3616 0.3719 0.3376 -0.0146 0.0161  0.0029  446 PHE B C   
4983 O O   . PHE B 320 ? 0.3797 0.3895 0.3530 -0.0203 0.0172  0.0068  446 PHE B O   
4984 C CB  . PHE B 320 ? 0.3615 0.3944 0.3692 -0.0109 0.0137  0.0049  446 PHE B CB  
4985 C CG  . PHE B 320 ? 0.3389 0.3822 0.3640 -0.0023 0.0183  0.0041  446 PHE B CG  
4986 C CD1 . PHE B 320 ? 0.3609 0.3921 0.3801 0.0035  0.0183  0.0007  446 PHE B CD1 
4987 C CD2 . PHE B 320 ? 0.3511 0.4157 0.3990 0.0007  0.0236  0.0076  446 PHE B CD2 
4988 C CE1 . PHE B 320 ? 0.3702 0.4024 0.4027 0.0121  0.0227  0.0000  446 PHE B CE1 
4989 C CE2 . PHE B 320 ? 0.3542 0.4234 0.4175 0.0126  0.0295  0.0064  446 PHE B CE2 
4990 C CZ  . PHE B 320 ? 0.3669 0.4160 0.4207 0.0183  0.0287  0.0021  446 PHE B CZ  
4991 N N   . GLN B 321 ? 0.3735 0.3691 0.3364 -0.0110 0.0123  0.0007  447 GLN B N   
4992 C CA  . GLN B 321 ? 0.3809 0.3553 0.3251 -0.0116 0.0096  0.0011  447 GLN B CA  
4993 C C   . GLN B 321 ? 0.4058 0.3662 0.3374 -0.0114 0.0042  -0.0018 447 GLN B C   
4994 O O   . GLN B 321 ? 0.4042 0.3727 0.3399 -0.0083 0.0037  -0.0028 447 GLN B O   
4995 C CB  . GLN B 321 ? 0.3766 0.3483 0.3123 -0.0030 0.0149  0.0013  447 GLN B CB  
4996 C CG  . GLN B 321 ? 0.3847 0.3688 0.3259 -0.0048 0.0189  0.0049  447 GLN B CG  
4997 C CD  . GLN B 321 ? 0.4117 0.3929 0.3438 0.0026  0.0207  0.0088  447 GLN B CD  
4998 O OE1 . GLN B 321 ? 0.4523 0.4288 0.3793 0.0115  0.0211  0.0081  447 GLN B OE1 
4999 N NE2 . GLN B 321 ? 0.4266 0.4134 0.3572 -0.0003 0.0221  0.0145  447 GLN B NE2 
5000 N N   . CYS B 322 ? 0.4241 0.3600 0.3369 -0.0155 0.0002  -0.0033 448 CYS B N   
5001 C CA  . CYS B 322 ? 0.4504 0.3684 0.3430 -0.0163 -0.0042 -0.0081 448 CYS B CA  
5002 C C   . CYS B 322 ? 0.5296 0.4128 0.3951 -0.0121 -0.0017 -0.0128 448 CYS B C   
5003 O O   . CYS B 322 ? 0.5334 0.4047 0.3979 -0.0122 0.0000  -0.0099 448 CYS B O   
5004 C CB  . CYS B 322 ? 0.4502 0.3717 0.3454 -0.0311 -0.0160 -0.0060 448 CYS B CB  
5005 S SG  . CYS B 322 ? 0.5255 0.4294 0.4144 -0.0484 -0.0237 -0.0037 448 CYS B SG  
5006 N N   . LEU B 323 ? 0.5189 0.3842 0.3607 -0.0074 -0.0006 -0.0196 449 LEU B N   
5007 C CA  . LEU B 323 ? 0.5696 0.3946 0.3806 -0.0013 0.0032  -0.0267 449 LEU B CA  
5008 C C   . LEU B 323 ? 0.6273 0.4212 0.4153 -0.0199 -0.0084 -0.0314 449 LEU B C   
5009 O O   . LEU B 323 ? 0.6351 0.4391 0.4214 -0.0335 -0.0184 -0.0318 449 LEU B O   
5010 C CB  . LEU B 323 ? 0.5902 0.4106 0.3830 0.0141  0.0129  -0.0331 449 LEU B CB  
5011 C CG  . LEU B 323 ? 0.5628 0.4166 0.3779 0.0300  0.0236  -0.0272 449 LEU B CG  
5012 C CD1 . LEU B 323 ? 0.6366 0.4927 0.4358 0.0423  0.0338  -0.0316 449 LEU B CD1 
5013 C CD2 . LEU B 323 ? 0.5609 0.4127 0.3866 0.0413  0.0290  -0.0220 449 LEU B CD2 
5014 N N   . HIS B 324 ? 0.6759 0.4318 0.4464 -0.0218 -0.0084 -0.0336 450 HIS B N   
5015 C CA  . HIS B 324 ? 0.7074 0.4249 0.4494 -0.0420 -0.0199 -0.0395 450 HIS B CA  
5016 C C   . HIS B 324 ? 0.7864 0.4845 0.4938 -0.0433 -0.0218 -0.0520 450 HIS B C   
5017 O O   . HIS B 324 ? 0.7649 0.4553 0.4569 -0.0229 -0.0089 -0.0590 450 HIS B O   
5018 C CB  . HIS B 324 ? 0.7833 0.4505 0.5038 -0.0393 -0.0165 -0.0415 450 HIS B CB  
5019 C CG  . HIS B 324 ? 0.8866 0.5002 0.5669 -0.0593 -0.0270 -0.0513 450 HIS B CG  
5020 N ND1 . HIS B 324 ? 0.8872 0.5045 0.5720 -0.0905 -0.0438 -0.0460 450 HIS B ND1 
5021 C CD2 . HIS B 324 ? 0.9524 0.5065 0.5855 -0.0536 -0.0231 -0.0664 450 HIS B CD2 
5022 C CE1 . HIS B 324 ? 0.9302 0.4913 0.5711 -0.1064 -0.0520 -0.0574 450 HIS B CE1 
5023 N NE2 . HIS B 324 ? 1.0016 0.5200 0.6080 -0.0837 -0.0390 -0.0712 450 HIS B NE2 
5024 N N   . GLY B 325 ? 0.8204 0.5143 0.5156 -0.0682 -0.0380 -0.0534 451 GLY B N   
5025 C CA  . GLY B 325 ? 0.8170 0.4939 0.4750 -0.0742 -0.0428 -0.0643 451 GLY B CA  
5026 C C   . GLY B 325 ? 0.7964 0.5198 0.4722 -0.0700 -0.0438 -0.0583 451 GLY B C   
5027 O O   . GLY B 325 ? 0.8743 0.5897 0.5198 -0.0782 -0.0503 -0.0643 451 GLY B O   
5028 N N   . MET B 326 ? 0.7585 0.5262 0.4784 -0.0585 -0.0378 -0.0467 452 MET B N   
5029 C CA  . MET B 326 ? 0.7115 0.5195 0.4512 -0.0549 -0.0389 -0.0390 452 MET B CA  
5030 C C   . MET B 326 ? 0.6588 0.5077 0.4426 -0.0635 -0.0484 -0.0250 452 MET B C   
5031 O O   . MET B 326 ? 0.6304 0.5026 0.4229 -0.0708 -0.0588 -0.0177 452 MET B O   
5032 C CB  . MET B 326 ? 0.7077 0.5294 0.4575 -0.0314 -0.0210 -0.0388 452 MET B CB  
5033 C CG  . MET B 326 ? 0.7819 0.5748 0.4937 -0.0180 -0.0081 -0.0505 452 MET B CG  
5034 S SD  . MET B 326 ? 0.8106 0.6367 0.5422 0.0042  0.0099  -0.0451 452 MET B SD  
5035 C CE  . MET B 326 ? 0.6890 0.5468 0.4300 -0.0081 -0.0006 -0.0352 452 MET B CE  
5036 N N   . GLY B 327 ? 0.6359 0.4947 0.4473 -0.0614 -0.0443 -0.0202 453 GLY B N   
5037 C CA  . GLY B 327 ? 0.5839 0.4837 0.4378 -0.0623 -0.0467 -0.0085 453 GLY B CA  
5038 C C   . GLY B 327 ? 0.5605 0.4757 0.4325 -0.0812 -0.0595 -0.0004 453 GLY B C   
5039 O O   . GLY B 327 ? 0.5626 0.5155 0.4698 -0.0808 -0.0621 0.0099  453 GLY B O   
5040 N N   . GLU B 328 ? 0.5758 0.4629 0.4255 -0.0976 -0.0671 -0.0043 454 GLU B N   
5041 C CA  . GLU B 328 ? 0.5999 0.5063 0.4707 -0.1184 -0.0786 0.0056  454 GLU B CA  
5042 C C   . GLU B 328 ? 0.5857 0.5293 0.4763 -0.1296 -0.0940 0.0160  454 GLU B C   
5043 O O   . GLU B 328 ? 0.5617 0.5458 0.4918 -0.1354 -0.0972 0.0289  454 GLU B O   
5044 C CB  . GLU B 328 ? 0.6533 0.5158 0.4912 -0.1382 -0.0860 -0.0003 454 GLU B CB  
5045 C CG  . GLU B 328 ? 0.6698 0.5016 0.4983 -0.1276 -0.0720 -0.0045 454 GLU B CG  
5046 C CD  . GLU B 328 ? 0.7335 0.5153 0.5196 -0.1127 -0.0637 -0.0194 454 GLU B CD  
5047 O OE1 . GLU B 328 ? 0.7493 0.5314 0.5206 -0.1033 -0.0624 -0.0262 454 GLU B OE1 
5048 O OE2 . GLU B 328 ? 0.7631 0.5055 0.5306 -0.1098 -0.0578 -0.0230 454 GLU B OE2 
5049 N N   . PRO B 329 ? 0.5868 0.5224 0.4534 -0.1324 -0.1037 0.0129  455 PRO B N   
5050 C CA  . PRO B 329 ? 0.5696 0.5468 0.4607 -0.1405 -0.1192 0.0270  455 PRO B CA  
5051 C C   . PRO B 329 ? 0.5535 0.5715 0.4899 -0.1193 -0.1097 0.0378  455 PRO B C   
5052 O O   . PRO B 329 ? 0.5275 0.5882 0.5043 -0.1224 -0.1162 0.0524  455 PRO B O   
5053 C CB  . PRO B 329 ? 0.5754 0.5290 0.4227 -0.1453 -0.1287 0.0203  455 PRO B CB  
5054 C CG  . PRO B 329 ? 0.5959 0.4939 0.3939 -0.1529 -0.1250 0.0024  455 PRO B CG  
5055 C CD  . PRO B 329 ? 0.6060 0.4937 0.4185 -0.1342 -0.1042 -0.0022 455 PRO B CD  
5056 N N   . LEU B 330 ? 0.5187 0.5244 0.4497 -0.0978 -0.0940 0.0311  456 LEU B N   
5057 C CA  . LEU B 330 ? 0.4790 0.5137 0.4470 -0.0791 -0.0847 0.0390  456 LEU B CA  
5058 C C   . LEU B 330 ? 0.4440 0.5006 0.4463 -0.0757 -0.0752 0.0425  456 LEU B C   
5059 O O   . LEU B 330 ? 0.4466 0.5390 0.4870 -0.0696 -0.0751 0.0537  456 LEU B O   
5060 C CB  . LEU B 330 ? 0.4618 0.4765 0.4143 -0.0618 -0.0707 0.0307  456 LEU B CB  
5061 C CG  . LEU B 330 ? 0.4305 0.4643 0.4151 -0.0443 -0.0600 0.0357  456 LEU B CG  
5062 C CD1 . LEU B 330 ? 0.4643 0.5212 0.4700 -0.0410 -0.0703 0.0500  456 LEU B CD1 
5063 C CD2 . LEU B 330 ? 0.4630 0.4771 0.4319 -0.0324 -0.0466 0.0270  456 LEU B CD2 
5064 N N   . TYR B 331 ? 0.4300 0.4660 0.4189 -0.0788 -0.0665 0.0340  457 TYR B N   
5065 C CA  . TYR B 331 ? 0.4516 0.5082 0.4685 -0.0751 -0.0554 0.0374  457 TYR B CA  
5066 C C   . TYR B 331 ? 0.4362 0.5192 0.4743 -0.0937 -0.0643 0.0483  457 TYR B C   
5067 O O   . TYR B 331 ? 0.4040 0.5166 0.4723 -0.0900 -0.0547 0.0546  457 TYR B O   
5068 C CB  . TYR B 331 ? 0.4303 0.4582 0.4261 -0.0699 -0.0429 0.0274  457 TYR B CB  
5069 C CG  . TYR B 331 ? 0.4376 0.4588 0.4294 -0.0507 -0.0318 0.0209  457 TYR B CG  
5070 C CD1 . TYR B 331 ? 0.4174 0.4593 0.4332 -0.0383 -0.0209 0.0223  457 TYR B CD1 
5071 C CD2 . TYR B 331 ? 0.4418 0.4366 0.4051 -0.0460 -0.0321 0.0135  457 TYR B CD2 
5072 C CE1 . TYR B 331 ? 0.3854 0.4189 0.3958 -0.0251 -0.0127 0.0165  457 TYR B CE1 
5073 C CE2 . TYR B 331 ? 0.4099 0.4032 0.3723 -0.0318 -0.0229 0.0098  457 TYR B CE2 
5074 C CZ  . TYR B 331 ? 0.3880 0.3994 0.3735 -0.0231 -0.0145 0.0114  457 TYR B CZ  
5075 O OH  . TYR B 331 ? 0.3928 0.4002 0.3756 -0.0132 -0.0071 0.0077  457 TYR B OH  
5076 N N   . GLU B 332 ? 0.4729 0.5486 0.4957 -0.1146 -0.0823 0.0511  458 GLU B N   
5077 C CA  . GLU B 332 ? 0.4489 0.5627 0.5005 -0.1338 -0.0942 0.0656  458 GLU B CA  
5078 C C   . GLU B 332 ? 0.4646 0.6315 0.5632 -0.1200 -0.0935 0.0795  458 GLU B C   
5079 O O   . GLU B 332 ? 0.4230 0.6349 0.5596 -0.1276 -0.0954 0.0935  458 GLU B O   
5080 C CB  . GLU B 332 ? 0.4969 0.5935 0.5206 -0.1606 -0.1171 0.0659  458 GLU B CB  
5081 N N   . GLU B 333 ? 0.3959 0.5587 0.4939 -0.0992 -0.0900 0.0772  459 GLU B N   
5082 C CA  . GLU B 333 ? 0.4119 0.6160 0.5524 -0.0813 -0.0874 0.0899  459 GLU B CA  
5083 C C   . GLU B 333 ? 0.3664 0.5735 0.5246 -0.0574 -0.0636 0.0843  459 GLU B C   
5084 O O   . GLU B 333 ? 0.3535 0.5830 0.5413 -0.0375 -0.0574 0.0912  459 GLU B O   
5085 C CB  . GLU B 333 ? 0.4157 0.6106 0.5442 -0.0742 -0.0987 0.0932  459 GLU B CB  
5086 C CG  . GLU B 333 ? 0.4429 0.6269 0.5414 -0.0988 -0.1217 0.0950  459 GLU B CG  
5087 C CD  . GLU B 333 ? 0.4944 0.7243 0.6226 -0.1188 -0.1400 0.1125  459 GLU B CD  
5088 O OE1 . GLU B 333 ? 0.4346 0.7135 0.6142 -0.1078 -0.1354 0.1273  459 GLU B OE1 
5089 O OE2 . GLU B 333 ? 0.5471 0.7644 0.6467 -0.1460 -0.1587 0.1113  459 GLU B OE2 
5090 N N   . VAL B 334 ? 0.3743 0.5573 0.5127 -0.0589 -0.0505 0.0721  460 VAL B N   
5091 C CA  . VAL B 334 ? 0.3430 0.5214 0.4864 -0.0396 -0.0293 0.0638  460 VAL B CA  
5092 C C   . VAL B 334 ? 0.3306 0.5278 0.4863 -0.0457 -0.0176 0.0652  460 VAL B C   
5093 O O   . VAL B 334 ? 0.3486 0.5731 0.5309 -0.0320 -0.0026 0.0677  460 VAL B O   
5094 C CB  . VAL B 334 ? 0.3560 0.4894 0.4614 -0.0340 -0.0242 0.0488  460 VAL B CB  
5095 C CG1 . VAL B 334 ? 0.3340 0.4634 0.4408 -0.0198 -0.0048 0.0402  460 VAL B CG1 
5096 C CG2 . VAL B 334 ? 0.3821 0.5017 0.4781 -0.0266 -0.0323 0.0492  460 VAL B CG2 
5097 N N   . VAL B 335 ? 0.3624 0.5442 0.4977 -0.0661 -0.0237 0.0645  461 VAL B N   
5098 C CA  . VAL B 335 ? 0.3669 0.5595 0.5063 -0.0752 -0.0135 0.0671  461 VAL B CA  
5099 C C   . VAL B 335 ? 0.3941 0.6392 0.5737 -0.0858 -0.0160 0.0838  461 VAL B C   
5100 O O   . VAL B 335 ? 0.4380 0.6989 0.6292 -0.1000 -0.0340 0.0936  461 VAL B O   
5101 C CB  . VAL B 335 ? 0.4639 0.6154 0.5663 -0.0935 -0.0209 0.0626  461 VAL B CB  
5102 C CG1 . VAL B 335 ? 0.4822 0.6432 0.5876 -0.1055 -0.0122 0.0689  461 VAL B CG1 
5103 C CG2 . VAL B 335 ? 0.4220 0.5311 0.4913 -0.0801 -0.0166 0.0484  461 VAL B CG2 
5104 N N   . GLY B 336 ? 0.3725 0.6480 0.5733 -0.0799 0.0019  0.0877  462 GLY B N   
5105 C CA  . GLY B 336 ? 0.3991 0.7307 0.6410 -0.0914 0.0007  0.1056  462 GLY B CA  
5106 C C   . GLY B 336 ? 0.3780 0.7562 0.6627 -0.0658 0.0143  0.1112  462 GLY B C   
5107 O O   . GLY B 336 ? 0.3551 0.7212 0.6411 -0.0440 0.0144  0.1051  462 GLY B O   
5108 N N   . ARG B 337 ? 0.3556 0.7881 0.6768 -0.0682 0.0266  0.1244  463 ARG B N   
5109 C CA  . ARG B 337 ? 0.3255 0.8050 0.6896 -0.0403 0.0444  0.1299  463 ARG B CA  
5110 C C   . ARG B 337 ? 0.3337 0.8360 0.7291 -0.0302 0.0285  0.1410  463 ARG B C   
5111 O O   . ARG B 337 ? 0.3701 0.8775 0.7830 0.0009  0.0396  0.1383  463 ARG B O   
5112 C CB  . ARG B 337 ? 0.3065 0.8480 0.7067 -0.0481 0.0596  0.1452  463 ARG B CB  
5113 N N   . GLY B 338 ? 0.2888 0.8022 0.6890 -0.0567 0.0016  0.1538  464 GLY B N   
5114 C CA  . GLY B 338 ? 0.3162 0.8553 0.7446 -0.0499 -0.0165 0.1673  464 GLY B CA  
5115 C C   . GLY B 338 ? 0.3142 0.8005 0.7116 -0.0335 -0.0237 0.1545  464 GLY B C   
5116 O O   . GLY B 338 ? 0.3420 0.8472 0.7642 -0.0173 -0.0320 0.1652  464 GLY B O   
5117 N N   . LYS B 339 ? 0.3141 0.7375 0.6597 -0.0371 -0.0207 0.1340  465 LYS B N   
5118 C CA  . LYS B 339 ? 0.3228 0.6969 0.6367 -0.0253 -0.0268 0.1224  465 LYS B CA  
5119 C C   . LYS B 339 ? 0.3291 0.6793 0.6366 0.0039  -0.0031 0.1081  465 LYS B C   
5120 O O   . LYS B 339 ? 0.3309 0.7108 0.6732 0.0272  0.0118  0.1135  465 LYS B O   
5121 C CB  . LYS B 339 ? 0.3379 0.6615 0.6004 -0.0485 -0.0395 0.1104  465 LYS B CB  
5122 C CG  . LYS B 339 ? 0.3741 0.7119 0.6353 -0.0792 -0.0638 0.1217  465 LYS B CG  
5123 C CD  . LYS B 339 ? 0.3302 0.7013 0.6183 -0.0759 -0.0817 0.1382  465 LYS B CD  
5124 C CE  . LYS B 339 ? 0.4814 0.8802 0.7762 -0.1092 -0.1067 0.1525  465 LYS B CE  
5125 N NZ  . LYS B 339 ? 0.5388 0.8828 0.7776 -0.1357 -0.1187 0.1383  465 LYS B NZ  
5126 N N   . LEU B 340 ? 0.2900 0.5871 0.5533 0.0030  0.0009  0.0900  466 LEU B N   
5127 C CA  . LEU B 340 ? 0.3501 0.6210 0.6016 0.0251  0.0209  0.0754  466 LEU B CA  
5128 C C   . LEU B 340 ? 0.3627 0.6351 0.6050 0.0237  0.0404  0.0659  466 LEU B C   
5129 O O   . LEU B 340 ? 0.3610 0.6171 0.5945 0.0409  0.0581  0.0536  466 LEU B O   
5130 C CB  . LEU B 340 ? 0.3477 0.5665 0.5592 0.0247  0.0145  0.0630  466 LEU B CB  
5131 C CG  . LEU B 340 ? 0.3124 0.5213 0.5228 0.0264  -0.0029 0.0707  466 LEU B CG  
5132 C CD1 . LEU B 340 ? 0.3700 0.5322 0.5462 0.0312  -0.0009 0.0581  466 LEU B CD1 
5133 C CD2 . LEU B 340 ? 0.3582 0.5981 0.6097 0.0454  -0.0028 0.0854  466 LEU B CD2 
5134 N N   . ASP B 341 ? 0.3458 0.6340 0.5863 0.0019  0.0367  0.0715  467 ASP B N   
5135 C CA  . ASP B 341 ? 0.3269 0.6224 0.5599 -0.0019 0.0543  0.0669  467 ASP B CA  
5136 C C   . ASP B 341 ? 0.3489 0.5971 0.5389 0.0010  0.0609  0.0492  467 ASP B C   
5137 O O   . ASP B 341 ? 0.3415 0.5884 0.5224 0.0101  0.0794  0.0403  467 ASP B O   
5138 C CB  . ASP B 341 ? 0.3728 0.7106 0.6403 0.0170  0.0760  0.0707  467 ASP B CB  
5139 C CG  . ASP B 341 ? 0.3729 0.7308 0.6365 0.0075  0.0924  0.0715  467 ASP B CG  
5140 O OD1 . ASP B 341 ? 0.3767 0.7228 0.6198 -0.0169 0.0826  0.0748  467 ASP B OD1 
5141 O OD2 . ASP B 341 ? 0.3701 0.7530 0.6487 0.0248  0.1155  0.0690  467 ASP B OD2 
5142 N N   . ARG B 342 ? 0.3496 0.5611 0.5129 -0.0068 0.0457  0.0443  468 ARG B N   
5143 C CA  . ARG B 342 ? 0.3473 0.5206 0.4738 -0.0062 0.0491  0.0310  468 ARG B CA  
5144 C C   . ARG B 342 ? 0.3491 0.5023 0.4524 -0.0251 0.0367  0.0334  468 ARG B C   
5145 O O   . ARG B 342 ? 0.3420 0.4936 0.4479 -0.0362 0.0215  0.0400  468 ARG B O   
5146 C CB  . ARG B 342 ? 0.3589 0.5048 0.4743 0.0067  0.0463  0.0221  468 ARG B CB  
5147 C CG  . ARG B 342 ? 0.3780 0.5305 0.5104 0.0268  0.0589  0.0180  468 ARG B CG  
5148 C CD  . ARG B 342 ? 0.3659 0.5163 0.4859 0.0331  0.0784  0.0067  468 ARG B CD  
5149 N NE  . ARG B 342 ? 0.3764 0.5266 0.5090 0.0540  0.0926  0.0005  468 ARG B NE  
5150 C CZ  . ARG B 342 ? 0.4050 0.5879 0.5670 0.0665  0.1060  0.0057  468 ARG B CZ  
5151 N NH1 . ARG B 342 ? 0.4023 0.6260 0.5868 0.0574  0.1062  0.0187  468 ARG B NH1 
5152 N NH2 . ARG B 342 ? 0.4341 0.6081 0.6032 0.0888  0.1206  -0.0020 468 ARG B NH2 
5153 N N   . PRO B 343 ? 0.3605 0.4971 0.4396 -0.0290 0.0425  0.0285  469 PRO B N   
5154 C CA  . PRO B 343 ? 0.3711 0.4844 0.4283 -0.0435 0.0324  0.0316  469 PRO B CA  
5155 C C   . PRO B 343 ? 0.3565 0.4367 0.3922 -0.0396 0.0227  0.0246  469 PRO B C   
5156 O O   . PRO B 343 ? 0.3473 0.4208 0.3801 -0.0275 0.0249  0.0171  469 PRO B O   
5157 C CB  . PRO B 343 ? 0.3643 0.4748 0.4053 -0.0451 0.0431  0.0310  469 PRO B CB  
5158 C CG  . PRO B 343 ? 0.3906 0.5068 0.4311 -0.0299 0.0551  0.0208  469 PRO B CG  
5159 C CD  . PRO B 343 ? 0.3873 0.5266 0.4572 -0.0208 0.0587  0.0212  469 PRO B CD  
5160 N N   . CYS B 344 ? 0.3951 0.4530 0.4143 -0.0507 0.0126  0.0273  470 CYS B N   
5161 C CA  . CYS B 344 ? 0.3801 0.4072 0.3767 -0.0461 0.0061  0.0207  470 CYS B CA  
5162 C C   . CYS B 344 ? 0.4313 0.4299 0.4046 -0.0523 0.0040  0.0222  470 CYS B C   
5163 O O   . CYS B 344 ? 0.4665 0.4590 0.4380 -0.0672 -0.0013 0.0287  470 CYS B O   
5164 C CB  . CYS B 344 ? 0.3979 0.4213 0.3955 -0.0508 -0.0059 0.0208  470 CYS B CB  
5165 S SG  . CYS B 344 ? 0.4610 0.4461 0.4253 -0.0456 -0.0107 0.0123  470 CYS B SG  
5166 N N   . ARG B 345 ? 0.4095 0.3910 0.3662 -0.0410 0.0077  0.0177  471 ARG B N   
5167 C CA  . ARG B 345 ? 0.4255 0.3766 0.3604 -0.0413 0.0062  0.0199  471 ARG B CA  
5168 C C   . ARG B 345 ? 0.4618 0.3835 0.3779 -0.0369 0.0008  0.0132  471 ARG B C   
5169 O O   . ARG B 345 ? 0.4733 0.3994 0.3885 -0.0258 0.0029  0.0073  471 ARG B O   
5170 C CB  . ARG B 345 ? 0.4206 0.3763 0.3512 -0.0303 0.0134  0.0216  471 ARG B CB  
5171 C CG  . ARG B 345 ? 0.4943 0.4207 0.4060 -0.0263 0.0122  0.0271  471 ARG B CG  
5172 C CD  . ARG B 345 ? 0.4379 0.3785 0.3491 -0.0173 0.0171  0.0323  471 ARG B CD  
5173 N NE  . ARG B 345 ? 0.4283 0.3976 0.3496 -0.0253 0.0216  0.0349  471 ARG B NE  
5174 C CZ  . ARG B 345 ? 0.4801 0.4516 0.3986 -0.0356 0.0232  0.0446  471 ARG B CZ  
5175 N NH1 . ARG B 345 ? 0.4932 0.4368 0.3993 -0.0401 0.0190  0.0543  471 ARG B NH1 
5176 N NH2 . ARG B 345 ? 0.4795 0.4795 0.4061 -0.0416 0.0300  0.0447  471 ARG B NH2 
5177 N N   . ILE B 346 ? 0.4981 0.3888 0.3970 -0.0471 -0.0056 0.0139  472 ILE B N   
5178 C CA  . ILE B 346 ? 0.5406 0.3964 0.4138 -0.0435 -0.0093 0.0053  472 ILE B CA  
5179 C C   . ILE B 346 ? 0.5986 0.4282 0.4549 -0.0261 -0.0020 0.0044  472 ILE B C   
5180 O O   . ILE B 346 ? 0.5877 0.4005 0.4389 -0.0271 -0.0010 0.0117  472 ILE B O   
5181 C CB  . ILE B 346 ? 0.6146 0.4431 0.4721 -0.0642 -0.0204 0.0048  472 ILE B CB  
5182 C CG1 . ILE B 346 ? 0.5625 0.4259 0.4423 -0.0800 -0.0289 0.0085  472 ILE B CG1 
5183 C CG2 . ILE B 346 ? 0.6362 0.4200 0.4581 -0.0598 -0.0224 -0.0067 472 ILE B CG2 
5184 C CD1 . ILE B 346 ? 0.6387 0.4871 0.5105 -0.1064 -0.0419 0.0123  472 ILE B CD1 
5185 N N   . TYR B 347 ? 0.6158 0.4450 0.4654 -0.0097 0.0034  -0.0023 473 TYR B N   
5186 C CA  . TYR B 347 ? 0.6103 0.4176 0.4458 0.0098  0.0111  -0.0028 473 TYR B CA  
5187 C C   . TYR B 347 ? 0.6136 0.3670 0.4156 0.0089  0.0094  -0.0106 473 TYR B C   
5188 O O   . TYR B 347 ? 0.6705 0.4109 0.4554 0.0025  0.0061  -0.0208 473 TYR B O   
5189 C CB  . TYR B 347 ? 0.6069 0.4394 0.4499 0.0260  0.0185  -0.0060 473 TYR B CB  
5190 C CG  . TYR B 347 ? 0.6098 0.4406 0.4520 0.0483  0.0276  -0.0019 473 TYR B CG  
5191 C CD1 . TYR B 347 ? 0.6338 0.4289 0.4525 0.0638  0.0342  -0.0077 473 TYR B CD1 
5192 C CD2 . TYR B 347 ? 0.6057 0.4724 0.4704 0.0545  0.0296  0.0078  473 TYR B CD2 
5193 C CE1 . TYR B 347 ? 0.7128 0.5120 0.5363 0.0881  0.0437  -0.0016 473 TYR B CE1 
5194 C CE2 . TYR B 347 ? 0.5845 0.4578 0.4534 0.0749  0.0362  0.0148  473 TYR B CE2 
5195 C CZ  . TYR B 347 ? 0.6468 0.4888 0.4981 0.0930  0.0436  0.0112  473 TYR B CZ  
5196 O OH  . TYR B 347 ? 0.6874 0.5425 0.5487 0.1162  0.0509  0.0206  473 TYR B OH  
5197 N N   . ALA B 348 ? 0.6643 0.3830 0.4538 0.0149  0.0113  -0.0058 474 ALA B N   
5198 C CA  . ALA B 348 ? 0.7493 0.4058 0.5029 0.0119  0.0094  -0.0137 474 ALA B CA  
5199 C C   . ALA B 348 ? 0.7690 0.3958 0.5076 0.0416  0.0215  -0.0154 474 ALA B C   
5200 O O   . ALA B 348 ? 0.7802 0.3996 0.5260 0.0529  0.0242  -0.0031 474 ALA B O   
5201 C CB  . ALA B 348 ? 0.8046 0.4368 0.5542 -0.0102 0.0000  -0.0050 474 ALA B CB  
5202 N N   . PRO B 349 ? 0.7880 0.4003 0.5067 0.0563  0.0297  -0.0287 475 PRO B N   
5203 C CA  . PRO B 349 ? 0.8569 0.4383 0.5607 0.0874  0.0436  -0.0309 475 PRO B CA  
5204 C C   . PRO B 349 ? 0.9408 0.4451 0.6082 0.0854  0.0418  -0.0357 475 PRO B C   
5205 O O   . PRO B 349 ? 0.9840 0.4495 0.6224 0.0612  0.0323  -0.0467 475 PRO B O   
5206 C CB  . PRO B 349 ? 0.8366 0.4250 0.5254 0.0991  0.0537  -0.0455 475 PRO B CB  
5207 C CG  . PRO B 349 ? 0.8156 0.4502 0.5207 0.0761  0.0440  -0.0461 475 PRO B CG  
5208 C CD  . PRO B 349 ? 0.8137 0.4429 0.5248 0.0474  0.0280  -0.0406 475 PRO B CD  
5209 N N   . VAL B 350 ? 0.9703 0.4519 0.6392 0.1103  0.0498  -0.0262 476 VAL B N   
5210 C CA  . VAL B 350 ? 1.0865 0.4878 0.7208 0.1131  0.0497  -0.0284 476 VAL B CA  
5211 C C   . VAL B 350 ? 1.1219 0.4916 0.7403 0.1542  0.0686  -0.0349 476 VAL B C   
5212 O O   . VAL B 350 ? 1.1577 0.5741 0.8079 0.1825  0.0786  -0.0228 476 VAL B O   
5213 C CB  . VAL B 350 ? 1.0542 0.4523 0.7055 0.1049  0.0410  -0.0063 476 VAL B CB  
5214 N N   . GLY B 351 ? 1.1507 0.4437 0.7202 0.1574  0.0737  -0.0539 477 GLY B N   
5215 C CA  . GLY B 351 ? 1.2305 0.5066 0.7920 0.1941  0.0921  -0.0594 477 GLY B CA  
5216 C C   . GLY B 351 ? 1.3394 0.5709 0.8568 0.1855  0.0956  -0.0840 477 GLY B C   
5217 O O   . GLY B 351 ? 1.3521 0.5616 0.8422 0.1510  0.0824  -0.0965 477 GLY B O   
5218 N N   . THR B 352 ? 1.3850 0.6060 0.8967 0.2177  0.1133  -0.0894 478 THR B N   
5219 C CA  . THR B 352 ? 1.4590 0.6376 0.9274 0.2162  0.1206  -0.1126 478 THR B CA  
5220 C C   . THR B 352 ? 1.4923 0.7184 0.9599 0.2220  0.1313  -0.1237 478 THR B C   
5221 O O   . THR B 352 ? 1.4543 0.7285 0.9400 0.2080  0.1245  -0.1193 478 THR B O   
5222 C CB  . THR B 352 ? 1.4502 0.5900 0.9115 0.2488  0.1356  -0.1132 478 THR B CB  
5223 N N   . HIS B 353 ? 1.5723 0.7849 1.0186 0.2424  0.1486  -0.1376 479 HIS B N   
5224 C CA  . HIS B 353 ? 1.5193 0.7778 0.9641 0.2479  0.1602  -0.1465 479 HIS B CA  
5225 C C   . HIS B 353 ? 1.4760 0.8051 0.9689 0.2819  0.1773  -0.1306 479 HIS B C   
5226 O O   . HIS B 353 ? 1.3993 0.7867 0.9086 0.2788  0.1806  -0.1285 479 HIS B O   
5227 C CB  . HIS B 353 ? 1.5028 0.7163 0.8998 0.2514  0.1711  -0.1692 479 HIS B CB  
5228 N N   . GLU B 354 ? 1.6908 1.0188 1.2082 0.3126  0.1870  -0.1178 480 GLU B N   
5229 C CA  . GLU B 354 ? 1.6484 1.0496 1.2164 0.3426  0.2005  -0.0993 480 GLU B CA  
5230 C C   . GLU B 354 ? 1.6167 1.0715 1.2253 0.3312  0.1872  -0.0797 480 GLU B C   
5231 O O   . GLU B 354 ? 1.6154 1.0431 1.2238 0.3149  0.1707  -0.0730 480 GLU B O   
5232 C CB  . GLU B 354 ? 1.6937 1.0788 1.2772 0.3775  0.2120  -0.0891 480 GLU B CB  
5233 N N   . THR B 355 ? 1.4572 0.9888 1.1001 0.3389  0.1948  -0.0706 481 THR B N   
5234 C CA  . THR B 355 ? 1.3446 0.9360 1.0247 0.3275  0.1846  -0.0548 481 THR B CA  
5235 C C   . THR B 355 ? 1.2806 0.8591 0.9348 0.2926  0.1713  -0.0680 481 THR B C   
5236 O O   . THR B 355 ? 1.2207 0.8539 0.8971 0.2830  0.1687  -0.0620 481 THR B O   
5237 C CB  . THR B 355 ? 1.3087 0.9018 1.0180 0.3334  0.1734  -0.0340 481 THR B CB  
5238 N N   . LEU B 356 ? 1.2677 0.7761 0.8759 0.2719  0.1620  -0.0851 482 LEU B N   
5239 C CA  . LEU B 356 ? 1.1652 0.6641 0.7485 0.2374  0.1480  -0.0970 482 LEU B CA  
5240 C C   . LEU B 356 ? 1.1080 0.6386 0.6786 0.2344  0.1574  -0.1074 482 LEU B C   
5241 O O   . LEU B 356 ? 1.0253 0.5878 0.5987 0.2147  0.1498  -0.1073 482 LEU B O   
5242 C CB  . LEU B 356 ? 1.2431 0.6656 0.7830 0.2128  0.1338  -0.1104 482 LEU B CB  
5243 N N   . LEU B 357 ? 1.0874 0.6097 0.6434 0.2539  0.1744  -0.1154 483 LEU B N   
5244 C CA  . LEU B 357 ? 0.9938 0.5467 0.5369 0.2519  0.1850  -0.1237 483 LEU B CA  
5245 C C   . LEU B 357 ? 0.9791 0.6137 0.5661 0.2557  0.1898  -0.1073 483 LEU B C   
5246 O O   . LEU B 357 ? 0.9571 0.6182 0.5351 0.2375  0.1870  -0.1102 483 LEU B O   
5247 C CB  . LEU B 357 ? 1.0621 0.5977 0.5889 0.2777  0.2056  -0.1328 483 LEU B CB  
5248 N N   . ALA B 358 ? 0.9349 0.6112 0.5694 0.2773  0.1955  -0.0884 484 ALA B N   
5249 C CA  . ALA B 358 ? 0.8962 0.6519 0.5751 0.2772  0.1976  -0.0711 484 ALA B CA  
5250 C C   . ALA B 358 ? 0.8329 0.6007 0.5184 0.2452  0.1767  -0.0676 484 ALA B C   
5251 O O   . ALA B 358 ? 0.8102 0.6294 0.5141 0.2290  0.1731  -0.0603 484 ALA B O   
5252 C CB  . ALA B 358 ? 0.9104 0.7083 0.6397 0.3026  0.2031  -0.0501 484 ALA B CB  
5253 N N   . TYR B 359 ? 0.8409 0.5685 0.5211 0.2295  0.1583  -0.0687 485 TYR B N   
5254 C CA  . TYR B 359 ? 0.8088 0.5485 0.4993 0.1932  0.1347  -0.0650 485 TYR B CA  
5255 C C   . TYR B 359 ? 0.8243 0.5449 0.4765 0.1711  0.1295  -0.0795 485 TYR B C   
5256 O O   . TYR B 359 ? 0.7484 0.5069 0.4161 0.1500  0.1191  -0.0733 485 TYR B O   
5257 C CB  . TYR B 359 ? 0.8013 0.5013 0.4914 0.1829  0.1194  -0.0629 485 TYR B CB  
5258 C CG  . TYR B 359 ? 0.7758 0.4849 0.4763 0.1480  0.0970  -0.0593 485 TYR B CG  
5259 C CD1 . TYR B 359 ? 0.7357 0.4955 0.4797 0.1390  0.0881  -0.0434 485 TYR B CD1 
5260 C CD2 . TYR B 359 ? 0.7639 0.4307 0.4300 0.1244  0.0851  -0.0719 485 TYR B CD2 
5261 C CE1 . TYR B 359 ? 0.6974 0.4651 0.4512 0.1111  0.0707  -0.0407 485 TYR B CE1 
5262 C CE2 . TYR B 359 ? 0.7973 0.4781 0.4777 0.0956  0.0661  -0.0667 485 TYR B CE2 
5263 C CZ  . TYR B 359 ? 0.7557 0.4865 0.4804 0.0908  0.0604  -0.0515 485 TYR B CZ  
5264 O OH  . TYR B 359 ? 0.7509 0.4953 0.4898 0.0656  0.0445  -0.0471 485 TYR B OH  
5265 N N   . LEU B 360 ? 0.8448 0.5050 0.4446 0.1763  0.1364  -0.0986 486 LEU B N   
5266 C CA  . LEU B 360 ? 0.8614 0.5006 0.4185 0.1537  0.1294  -0.1126 486 LEU B CA  
5267 C C   . LEU B 360 ? 0.8535 0.5418 0.4130 0.1570  0.1412  -0.1093 486 LEU B C   
5268 O O   . LEU B 360 ? 0.8545 0.5569 0.4043 0.1323  0.1287  -0.1088 486 LEU B O   
5269 C CB  . LEU B 360 ? 0.9534 0.5163 0.4521 0.1577  0.1344  -0.1342 486 LEU B CB  
5270 N N   . VAL B 361 ? 0.8221 0.5398 0.3966 0.1870  0.1650  -0.1048 487 VAL B N   
5271 C CA  . VAL B 361 ? 0.7947 0.5665 0.3773 0.1885  0.1771  -0.0979 487 VAL B CA  
5272 C C   . VAL B 361 ? 0.7875 0.6152 0.4165 0.1653  0.1597  -0.0784 487 VAL B C   
5273 O O   . VAL B 361 ? 0.7488 0.5971 0.3700 0.1465  0.1541  -0.0752 487 VAL B O   
5274 C CB  . VAL B 361 ? 0.8032 0.6112 0.4149 0.2184  0.1996  -0.0904 487 VAL B CB  
5275 C CG1 . VAL B 361 ? 0.8175 0.6917 0.4495 0.2152  0.2098  -0.0780 487 VAL B CG1 
5276 C CG2 . VAL B 361 ? 0.8797 0.6403 0.4556 0.2322  0.2111  -0.1076 487 VAL B CG2 
5277 N N   . ARG B 362 ? 0.7652 0.6147 0.4402 0.1663  0.1508  -0.0653 488 ARG B N   
5278 C CA  . ARG B 362 ? 0.6529 0.5457 0.3665 0.1440  0.1344  -0.0500 488 ARG B CA  
5279 C C   . ARG B 362 ? 0.6852 0.5532 0.3810 0.1154  0.1131  -0.0549 488 ARG B C   
5280 O O   . ARG B 362 ? 0.7094 0.6053 0.4176 0.0977  0.1041  -0.0464 488 ARG B O   
5281 C CB  . ARG B 362 ? 0.6720 0.5879 0.4304 0.1496  0.1288  -0.0372 488 ARG B CB  
5282 C CG  . ARG B 362 ? 0.6542 0.6116 0.4395 0.1754  0.1472  -0.0267 488 ARG B CG  
5283 C CD  . ARG B 362 ? 0.6135 0.6079 0.4451 0.1735  0.1378  -0.0105 488 ARG B CD  
5284 N NE  . ARG B 362 ? 0.6526 0.6098 0.4820 0.1747  0.1271  -0.0129 488 ARG B NE  
5285 C CZ  . ARG B 362 ? 0.6558 0.5942 0.4852 0.1995  0.1352  -0.0117 488 ARG B CZ  
5286 N NH1 . ARG B 362 ? 0.6763 0.6300 0.5092 0.2286  0.1554  -0.0093 488 ARG B NH1 
5287 N NH2 . ARG B 362 ? 0.7006 0.6053 0.5275 0.1958  0.1236  -0.0113 488 ARG B NH2 
5288 N N   . ARG B 363 ? 0.7336 0.5489 0.3998 0.1103  0.1048  -0.0677 489 ARG B N   
5289 C CA  . ARG B 363 ? 0.7563 0.5533 0.4059 0.0828  0.0844  -0.0711 489 ARG B CA  
5290 C C   . ARG B 363 ? 0.7980 0.5932 0.4107 0.0742  0.0861  -0.0768 489 ARG B C   
5291 O O   . ARG B 363 ? 0.7631 0.5728 0.3789 0.0532  0.0706  -0.0702 489 ARG B O   
5292 C CB  . ARG B 363 ? 0.7911 0.5338 0.4164 0.0760  0.0746  -0.0824 489 ARG B CB  
5293 C CG  . ARG B 363 ? 0.7895 0.5320 0.4480 0.0802  0.0703  -0.0746 489 ARG B CG  
5294 C CD  . ARG B 363 ? 0.7093 0.4896 0.4092 0.0622  0.0545  -0.0608 489 ARG B CD  
5295 N NE  . ARG B 363 ? 0.6414 0.4739 0.3753 0.0671  0.0596  -0.0489 489 ARG B NE  
5296 C CZ  . ARG B 363 ? 0.7004 0.5591 0.4596 0.0843  0.0708  -0.0413 489 ARG B CZ  
5297 N NH1 . ARG B 363 ? 0.6845 0.5244 0.4405 0.1033  0.0799  -0.0431 489 ARG B NH1 
5298 N NH2 . ARG B 363 ? 0.6979 0.6023 0.4866 0.0818  0.0717  -0.0304 489 ARG B NH2 
5299 N N   . LEU B 364 ? 0.8073 0.5844 0.3836 0.0912  0.1055  -0.0884 490 LEU B N   
5300 C CA  . LEU B 364 ? 0.8285 0.6062 0.3653 0.0832  0.1091  -0.0932 490 LEU B CA  
5301 C C   . LEU B 364 ? 0.8332 0.6692 0.4010 0.0789  0.1116  -0.0748 490 LEU B C   
5302 O O   . LEU B 364 ? 0.8215 0.6666 0.3757 0.0596  0.1002  -0.0694 490 LEU B O   
5303 C CB  . LEU B 364 ? 0.8357 0.5832 0.3260 0.1055  0.1337  -0.1104 490 LEU B CB  
5304 C CG  . LEU B 364 ? 0.8615 0.6111 0.3079 0.0955  0.1377  -0.1157 490 LEU B CG  
5305 C CD1 . LEU B 364 ? 0.9699 0.6928 0.3841 0.0638  0.1108  -0.1194 490 LEU B CD1 
5306 C CD2 . LEU B 364 ? 0.9250 0.6527 0.3463 0.1126  0.1565  -0.1317 490 LEU B CD2 
5307 N N   . LEU B 365 ? 0.7970 0.6726 0.4056 0.0955  0.1256  -0.0638 491 LEU B N   
5308 C CA  . LEU B 365 ? 0.7706 0.6984 0.4081 0.0879  0.1270  -0.0457 491 LEU B CA  
5309 C C   . LEU B 365 ? 0.7406 0.6782 0.4061 0.0648  0.1028  -0.0342 491 LEU B C   
5310 O O   . LEU B 365 ? 0.7915 0.7525 0.4627 0.0508  0.0973  -0.0219 491 LEU B O   
5311 C CB  . LEU B 365 ? 0.7324 0.7024 0.4100 0.1073  0.1442  -0.0355 491 LEU B CB  
5312 C CG  . LEU B 365 ? 0.7482 0.7219 0.4049 0.1339  0.1724  -0.0428 491 LEU B CG  
5313 C CD1 . LEU B 365 ? 0.7960 0.8151 0.5011 0.1532  0.1852  -0.0300 491 LEU B CD1 
5314 C CD2 . LEU B 365 ? 0.7932 0.7849 0.4208 0.1275  0.1839  -0.0403 491 LEU B CD2 
5315 N N   . GLU B 366 ? 0.7081 0.6260 0.3891 0.0611  0.0890  -0.0377 492 GLU B N   
5316 C CA  . GLU B 366 ? 0.7222 0.6479 0.4296 0.0427  0.0684  -0.0285 492 GLU B CA  
5317 C C   . GLU B 366 ? 0.7316 0.6361 0.4101 0.0247  0.0521  -0.0312 492 GLU B C   
5318 O O   . GLU B 366 ? 0.7462 0.6676 0.4368 0.0115  0.0406  -0.0193 492 GLU B O   
5319 C CB  . GLU B 366 ? 0.6843 0.6006 0.4174 0.0457  0.0619  -0.0305 492 GLU B CB  
5320 C CG  . GLU B 366 ? 0.6504 0.5759 0.4121 0.0304  0.0445  -0.0225 492 GLU B CG  
5321 C CD  . GLU B 366 ? 0.6628 0.5778 0.4426 0.0330  0.0404  -0.0253 492 GLU B CD  
5322 O OE1 . GLU B 366 ? 0.6763 0.5733 0.4451 0.0461  0.0492  -0.0323 492 GLU B OE1 
5323 O OE2 . GLU B 366 ? 0.6548 0.5787 0.4589 0.0232  0.0292  -0.0198 492 GLU B OE2 
5324 N N   . ASN B 367 ? 0.7528 0.6191 0.3926 0.0235  0.0499  -0.0460 493 ASN B N   
5325 C CA  . ASN B 367 ? 0.8209 0.6693 0.4342 0.0033  0.0307  -0.0478 493 ASN B CA  
5326 C C   . ASN B 367 ? 0.8184 0.6720 0.3950 -0.0031 0.0327  -0.0457 493 ASN B C   
5327 O O   . ASN B 367 ? 0.8675 0.7191 0.4295 -0.0215 0.0141  -0.0405 493 ASN B O   
5328 C CB  . ASN B 367 ? 0.8448 0.6472 0.4267 -0.0005 0.0253  -0.0646 493 ASN B CB  
5329 C CG  . ASN B 367 ? 0.8704 0.6700 0.4876 -0.0053 0.0141  -0.0616 493 ASN B CG  
5330 O OD1 . ASN B 367 ? 0.9034 0.7069 0.5309 -0.0237 -0.0056 -0.0558 493 ASN B OD1 
5331 N ND2 . ASN B 367 ? 0.8200 0.6166 0.4570 0.0116  0.0266  -0.0636 493 ASN B ND2 
5332 N N   . GLY B 368 ? 0.8336 0.6974 0.3956 0.0113  0.0547  -0.0476 494 GLY B N   
5333 C CA  . GLY B 368 ? 0.8653 0.7321 0.3850 0.0057  0.0599  -0.0468 494 GLY B CA  
5334 C C   . GLY B 368 ? 0.8570 0.7664 0.3998 0.0026  0.0638  -0.0260 494 GLY B C   
5335 O O   . GLY B 368 ? 0.8371 0.7524 0.3469 -0.0060 0.0648  -0.0205 494 GLY B O   
5336 N N   . ALA B 369 ? 0.8011 0.7382 0.3973 0.0073  0.0654  -0.0139 495 ALA B N   
5337 C CA  . ALA B 369 ? 0.7849 0.7580 0.4031 0.0025  0.0694  0.0057  495 ALA B CA  
5338 C C   . ALA B 369 ? 0.7481 0.7225 0.3712 -0.0166 0.0469  0.0212  495 ALA B C   
5339 O O   . ALA B 369 ? 0.7170 0.6798 0.3587 -0.0225 0.0284  0.0214  495 ALA B O   
5340 C CB  . ALA B 369 ? 0.7466 0.7448 0.4164 0.0110  0.0764  0.0122  495 ALA B CB  
5341 N N   . ASN B 370 ? 0.7786 0.7695 0.3874 -0.0251 0.0495  0.0363  496 ASN B N   
5342 C CA  . ASN B 370 ? 0.7513 0.7421 0.3607 -0.0411 0.0287  0.0539  496 ASN B CA  
5343 C C   . ASN B 370 ? 0.7233 0.7204 0.3851 -0.0430 0.0171  0.0658  496 ASN B C   
5344 O O   . ASN B 370 ? 0.7281 0.7193 0.3985 -0.0512 -0.0024 0.0771  496 ASN B O   
5345 C CB  . ASN B 370 ? 0.7943 0.8014 0.3778 -0.0495 0.0360  0.0702  496 ASN B CB  
5346 N N   . SER B 371 ? 0.7133 0.7224 0.4093 -0.0349 0.0286  0.0632  497 SER B N   
5347 C CA  . SER B 371 ? 0.6431 0.6540 0.3832 -0.0365 0.0200  0.0706  497 SER B CA  
5348 C C   . SER B 371 ? 0.6217 0.6194 0.3811 -0.0300 0.0119  0.0574  497 SER B C   
5349 O O   . SER B 371 ? 0.6148 0.6105 0.4057 -0.0310 0.0033  0.0621  497 SER B O   
5350 C CB  . SER B 371 ? 0.6032 0.6354 0.3674 -0.0352 0.0346  0.0753  497 SER B CB  
5351 O OG  . SER B 371 ? 0.6198 0.6608 0.3868 -0.0224 0.0488  0.0609  497 SER B OG  
5352 N N   . SER B 372 ? 0.6026 0.5891 0.3423 -0.0237 0.0153  0.0411  498 SER B N   
5353 C CA  . SER B 372 ? 0.5984 0.5730 0.3554 -0.0196 0.0085  0.0303  498 SER B CA  
5354 C C   . SER B 372 ? 0.5970 0.5637 0.3583 -0.0284 -0.0118 0.0355  498 SER B C   
5355 O O   . SER B 372 ? 0.5941 0.5555 0.3277 -0.0368 -0.0217 0.0393  498 SER B O   
5356 C CB  . SER B 372 ? 0.6813 0.6405 0.4128 -0.0116 0.0176  0.0129  498 SER B CB  
5357 O OG  . SER B 372 ? 0.6689 0.6407 0.4082 0.0008  0.0363  0.0097  498 SER B OG  
5358 N N   . PHE B 373 ? 0.5659 0.5349 0.3625 -0.0263 -0.0178 0.0363  499 PHE B N   
5359 C CA  . PHE B 373 ? 0.5701 0.5388 0.3794 -0.0319 -0.0353 0.0420  499 PHE B CA  
5360 C C   . PHE B 373 ? 0.6065 0.5636 0.3872 -0.0398 -0.0446 0.0336  499 PHE B C   
5361 O O   . PHE B 373 ? 0.6188 0.5792 0.3907 -0.0495 -0.0609 0.0422  499 PHE B O   
5362 C CB  . PHE B 373 ? 0.5272 0.5006 0.3753 -0.0261 -0.0347 0.0399  499 PHE B CB  
5363 C CG  . PHE B 373 ? 0.4986 0.4785 0.3655 -0.0297 -0.0498 0.0459  499 PHE B CG  
5364 C CD1 . PHE B 373 ? 0.5278 0.5172 0.4178 -0.0275 -0.0579 0.0610  499 PHE B CD1 
5365 C CD2 . PHE B 373 ? 0.5183 0.4956 0.3817 -0.0350 -0.0555 0.0378  499 PHE B CD2 
5366 C CE1 . PHE B 373 ? 0.5312 0.5340 0.4443 -0.0282 -0.0708 0.0688  499 PHE B CE1 
5367 C CE2 . PHE B 373 ? 0.5346 0.5259 0.4199 -0.0398 -0.0693 0.0456  499 PHE B CE2 
5368 C CZ  . PHE B 373 ? 0.5376 0.5450 0.4498 -0.0351 -0.0764 0.0614  499 PHE B CZ  
5369 N N   . VAL B 374 ? 0.6192 0.5613 0.3851 -0.0365 -0.0358 0.0175  500 VAL B N   
5370 C CA  . VAL B 374 ? 0.6781 0.6012 0.4144 -0.0464 -0.0453 0.0078  500 VAL B CA  
5371 C C   . VAL B 374 ? 0.7314 0.6437 0.4194 -0.0543 -0.0483 0.0061  500 VAL B C   
5372 O O   . VAL B 374 ? 0.8109 0.7102 0.4717 -0.0684 -0.0628 0.0021  500 VAL B O   
5373 C CB  . VAL B 374 ? 0.6751 0.5771 0.4047 -0.0398 -0.0344 -0.0083 500 VAL B CB  
5374 C CG1 . VAL B 374 ? 0.6322 0.5471 0.4062 -0.0342 -0.0325 -0.0051 500 VAL B CG1 
5375 C CG2 . VAL B 374 ? 0.6994 0.5924 0.4069 -0.0261 -0.0141 -0.0169 500 VAL B CG2 
5376 N N   . HIS B 375 ? 0.7207 0.6397 0.3955 -0.0477 -0.0354 0.0098  501 HIS B N   
5377 C CA  . HIS B 375 ? 0.7544 0.6682 0.3833 -0.0561 -0.0381 0.0114  501 HIS B CA  
5378 C C   . HIS B 375 ? 0.7334 0.6661 0.3731 -0.0671 -0.0573 0.0327  501 HIS B C   
5379 O O   . HIS B 375 ? 0.7594 0.6878 0.3679 -0.0812 -0.0736 0.0357  501 HIS B O   
5380 C CB  . HIS B 375 ? 0.7871 0.7054 0.3986 -0.0450 -0.0151 0.0091  501 HIS B CB  
5381 C CG  . HIS B 375 ? 0.8273 0.7414 0.3868 -0.0529 -0.0140 0.0103  501 HIS B CG  
5382 N ND1 . HIS B 375 ? 0.8524 0.7860 0.4103 -0.0607 -0.0201 0.0305  501 HIS B ND1 
5383 C CD2 . HIS B 375 ? 0.9056 0.7955 0.4088 -0.0543 -0.0070 -0.0066 501 HIS B CD2 
5384 C CE1 . HIS B 375 ? 0.9244 0.8501 0.4276 -0.0676 -0.0171 0.0271  501 HIS B CE1 
5385 N NE2 . HIS B 375 ? 0.9551 0.8537 0.4230 -0.0635 -0.0086 0.0034  501 HIS B NE2 
5386 N N   . ARG B 376 ? 0.7249 0.6765 0.4076 -0.0608 -0.0565 0.0480  502 ARG B N   
5387 C CA  . ARG B 376 ? 0.6581 0.6243 0.3541 -0.0670 -0.0730 0.0704  502 ARG B CA  
5388 C C   . ARG B 376 ? 0.6609 0.6334 0.3718 -0.0751 -0.0957 0.0758  502 ARG B C   
5389 O O   . ARG B 376 ? 0.7079 0.6905 0.4102 -0.0843 -0.1138 0.0921  502 ARG B O   
5390 C CB  . ARG B 376 ? 0.6168 0.5930 0.3548 -0.0574 -0.0658 0.0826  502 ARG B CB  
5391 C CG  . ARG B 376 ? 0.6517 0.6291 0.3763 -0.0548 -0.0473 0.0838  502 ARG B CG  
5392 C CD  . ARG B 376 ? 0.6553 0.6372 0.4193 -0.0474 -0.0377 0.0877  502 ARG B CD  
5393 N NE  . ARG B 376 ? 0.6358 0.6171 0.4298 -0.0469 -0.0498 0.1044  502 ARG B NE  
5394 C CZ  . ARG B 376 ? 0.7532 0.7336 0.5432 -0.0519 -0.0549 0.1246  502 ARG B CZ  
5395 N NH1 . ARG B 376 ? 0.7786 0.7627 0.5341 -0.0602 -0.0505 0.1318  502 ARG B NH1 
5396 N NH2 . ARG B 376 ? 0.7273 0.7014 0.5473 -0.0476 -0.0637 0.1383  502 ARG B NH2 
5397 N N   . ILE B 377 ? 0.6732 0.6434 0.4069 -0.0727 -0.0956 0.0643  503 ILE B N   
5398 C CA  . ILE B 377 ? 0.7010 0.6843 0.4532 -0.0820 -0.1166 0.0714  503 ILE B CA  
5399 C C   . ILE B 377 ? 0.7545 0.7298 0.4594 -0.1014 -0.1331 0.0682  503 ILE B C   
5400 O O   . ILE B 377 ? 0.7150 0.7091 0.4285 -0.1133 -0.1559 0.0822  503 ILE B O   
5401 C CB  . ILE B 377 ? 0.6916 0.6753 0.4761 -0.0774 -0.1113 0.0608  503 ILE B CB  
5402 C CG1 . ILE B 377 ? 0.6934 0.7024 0.5115 -0.0845 -0.1308 0.0738  503 ILE B CG1 
5403 C CG2 . ILE B 377 ? 0.7050 0.6614 0.4548 -0.0831 -0.1038 0.0388  503 ILE B CG2 
5404 C CD1 . ILE B 377 ? 0.6729 0.6955 0.5405 -0.0729 -0.1226 0.0740  503 ILE B CD1 
5405 N N   . ASN B 378 ? 0.7675 0.7161 0.4208 -0.1049 -0.1222 0.0506  504 ASN B N   
5406 C CA  . ASN B 378 ? 0.8332 0.7670 0.4309 -0.1243 -0.1362 0.0442  504 ASN B CA  
5407 C C   . ASN B 378 ? 0.8547 0.7919 0.4139 -0.1284 -0.1378 0.0547  504 ASN B C   
5408 O O   . ASN B 378 ? 0.9142 0.8373 0.4183 -0.1449 -0.1479 0.0482  504 ASN B O   
5409 C CB  . ASN B 378 ? 0.8920 0.7868 0.4484 -0.1255 -0.1228 0.0162  504 ASN B CB  
5410 C CG  . ASN B 378 ? 0.9023 0.7897 0.4884 -0.1266 -0.1247 0.0073  504 ASN B CG  
5411 O OD1 . ASN B 378 ? 0.9331 0.8371 0.5425 -0.1408 -0.1454 0.0167  504 ASN B OD1 
5412 N ND2 . ASN B 378 ? 0.9180 0.7837 0.5049 -0.1117 -0.1030 -0.0085 504 ASN B ND2 
5413 N N   . ASP B 379 ? 0.8558 0.8092 0.4387 -0.1159 -0.1284 0.0706  505 ASP B N   
5414 C CA  . ASP B 379 ? 0.8718 0.8290 0.4179 -0.1207 -0.1283 0.0830  505 ASP B CA  
5415 C C   . ASP B 379 ? 0.9303 0.9112 0.4902 -0.1305 -0.1557 0.1112  505 ASP B C   
5416 O O   . ASP B 379 ? 0.8600 0.8591 0.4754 -0.1207 -0.1613 0.1286  505 ASP B O   
5417 C CB  . ASP B 379 ? 0.8863 0.8476 0.4483 -0.1053 -0.1046 0.0879  505 ASP B CB  
5418 C CG  . ASP B 379 ? 0.9645 0.9305 0.4867 -0.1116 -0.1014 0.1015  505 ASP B CG  
5419 O OD1 . ASP B 379 ? 0.9702 0.9345 0.4479 -0.1268 -0.1169 0.1058  505 ASP B OD1 
5420 O OD2 . ASP B 379 ? 1.0450 1.0174 0.5794 -0.1030 -0.0837 0.1088  505 ASP B OD2 
5421 N N   . PRO B 380 ? 0.9585 0.9400 0.4748 -0.1468 -0.1709 0.1154  506 PRO B N   
5422 C CA  . PRO B 380 ? 1.0060 1.0138 0.5474 -0.1519 -0.1943 0.1424  506 PRO B CA  
5423 C C   . PRO B 380 ? 0.9925 1.0122 0.5570 -0.1407 -0.1908 0.1690  506 PRO B C   
5424 O O   . PRO B 380 ? 1.0585 1.0988 0.6629 -0.1371 -0.2081 0.1935  506 PRO B O   
5425 C CB  . PRO B 380 ? 0.9973 0.9982 0.4887 -0.1680 -0.2016 0.1341  506 PRO B CB  
5426 C CG  . PRO B 380 ? 1.0251 0.9957 0.4646 -0.1656 -0.1759 0.1065  506 PRO B CG  
5427 C CD  . PRO B 380 ? 1.0168 0.9743 0.4757 -0.1558 -0.1628 0.0908  506 PRO B CD  
5428 N N   . LYS B 381 ? 1.0025 1.0099 0.5450 -0.1348 -0.1684 0.1658  507 LYS B N   
5429 C CA  . LYS B 381 ? 0.9556 0.9697 0.5173 -0.1276 -0.1648 0.1914  507 LYS B CA  
5430 C C   . LYS B 381 ? 0.9032 0.9186 0.5205 -0.1131 -0.1613 0.2016  507 LYS B C   
5431 O O   . LYS B 381 ? 0.8572 0.8739 0.4970 -0.1073 -0.1634 0.2256  507 LYS B O   
5432 C CB  . LYS B 381 ? 1.0253 1.0301 0.5479 -0.1283 -0.1406 0.1851  507 LYS B CB  
5433 N N   . VAL B 382 ? 0.8305 0.8419 0.4769 -0.1045 -0.1524 0.1797  508 VAL B N   
5434 C CA  . VAL B 382 ? 0.7819 0.7920 0.4854 -0.0879 -0.1431 0.1806  508 VAL B CA  
5435 C C   . VAL B 382 ? 0.7594 0.7855 0.5065 -0.0825 -0.1629 0.1921  508 VAL B C   
5436 O O   . VAL B 382 ? 0.7879 0.8234 0.5360 -0.0886 -0.1727 0.1812  508 VAL B O   
5437 C CB  . VAL B 382 ? 0.7713 0.7707 0.4810 -0.0810 -0.1207 0.1520  508 VAL B CB  
5438 C CG1 . VAL B 382 ? 0.6591 0.6569 0.4224 -0.0662 -0.1124 0.1523  508 VAL B CG1 
5439 C CG2 . VAL B 382 ? 0.7972 0.7881 0.4684 -0.0839 -0.1001 0.1425  508 VAL B CG2 
5440 N N   . SER B 383 ? 0.7285 0.7572 0.5133 -0.0706 -0.1676 0.2142  509 SER B N   
5441 C CA  . SER B 383 ? 0.6630 0.7111 0.4941 -0.0610 -0.1840 0.2284  509 SER B CA  
5442 C C   . SER B 383 ? 0.6578 0.7042 0.5326 -0.0465 -0.1696 0.2111  509 SER B C   
5443 O O   . SER B 383 ? 0.6078 0.6348 0.4825 -0.0415 -0.1486 0.1941  509 SER B O   
5444 C CB  . SER B 383 ? 0.6523 0.6999 0.5039 -0.0508 -0.1942 0.2606  509 SER B CB  
5445 O OG  . SER B 383 ? 0.6991 0.7216 0.5737 -0.0365 -0.1756 0.2583  509 SER B OG  
5446 N N   . ILE B 384 ? 0.6445 0.7154 0.5577 -0.0402 -0.1818 0.2177  510 ILE B N   
5447 C CA  . ILE B 384 ? 0.6019 0.6752 0.5588 -0.0249 -0.1685 0.2054  510 ILE B CA  
5448 C C   . ILE B 384 ? 0.5490 0.5993 0.5290 -0.0061 -0.1541 0.2107  510 ILE B C   
5449 O O   . ILE B 384 ? 0.5559 0.5930 0.5518 0.0029  -0.1358 0.1930  510 ILE B O   
5450 C CB  . ILE B 384 ? 0.5958 0.7071 0.5922 -0.0217 -0.1847 0.2169  510 ILE B CB  
5451 C CG1 . ILE B 384 ? 0.6374 0.7549 0.6740 -0.0083 -0.1689 0.2022  510 ILE B CG1 
5452 C CG2 . ILE B 384 ? 0.5870 0.7157 0.6083 -0.0106 -0.2023 0.2503  510 ILE B CG2 
5453 C CD1 . ILE B 384 ? 0.6203 0.7812 0.6927 -0.0102 -0.1825 0.2105  510 ILE B CD1 
5454 N N   . ASP B 385 ? 0.5859 0.6277 0.5640 -0.0016 -0.1628 0.2351  511 ASP B N   
5455 C CA  . ASP B 385 ? 0.5906 0.6010 0.5826 0.0128  -0.1505 0.2407  511 ASP B CA  
5456 C C   . ASP B 385 ? 0.5838 0.5677 0.5505 0.0043  -0.1303 0.2190  511 ASP B C   
5457 O O   . ASP B 385 ? 0.5925 0.5565 0.5768 0.0140  -0.1150 0.2069  511 ASP B O   
5458 C CB  . ASP B 385 ? 0.5986 0.5992 0.5808 0.0133  -0.1643 0.2720  511 ASP B CB  
5459 C CG  . ASP B 385 ? 0.6213 0.6540 0.6264 0.0203  -0.1879 0.2985  511 ASP B CG  
5460 O OD1 . ASP B 385 ? 0.6787 0.7459 0.6820 0.0101  -0.2000 0.2945  511 ASP B OD1 
5461 O OD2 . ASP B 385 ? 0.6562 0.6789 0.6792 0.0347  -0.1959 0.3254  511 ASP B OD2 
5462 N N   . GLU B 386 ? 0.6191 0.6037 0.5434 -0.0139 -0.1301 0.2147  512 GLU B N   
5463 C CA  . GLU B 386 ? 0.6039 0.5713 0.5077 -0.0214 -0.1111 0.1972  512 GLU B CA  
5464 C C   . GLU B 386 ? 0.5836 0.5562 0.4987 -0.0183 -0.0985 0.1700  512 GLU B C   
5465 O O   . GLU B 386 ? 0.6111 0.5698 0.5295 -0.0173 -0.0829 0.1569  512 GLU B O   
5466 C CB  . GLU B 386 ? 0.6937 0.6657 0.5506 -0.0385 -0.1114 0.1992  512 GLU B CB  
5467 N N   . LEU B 387 ? 0.5796 0.5725 0.5008 -0.0186 -0.1063 0.1630  513 LEU B N   
5468 C CA  . LEU B 387 ? 0.5704 0.5675 0.4988 -0.0176 -0.0956 0.1394  513 LEU B CA  
5469 C C   . LEU B 387 ? 0.5470 0.5400 0.5140 -0.0028 -0.0866 0.1338  513 LEU B C   
5470 O O   . LEU B 387 ? 0.5147 0.5025 0.4839 -0.0018 -0.0730 0.1154  513 LEU B O   
5471 C CB  . LEU B 387 ? 0.5586 0.5753 0.4801 -0.0256 -0.1081 0.1356  513 LEU B CB  
5472 C CG  . LEU B 387 ? 0.6017 0.6152 0.4749 -0.0413 -0.1120 0.1306  513 LEU B CG  
5473 C CD1 . LEU B 387 ? 0.5944 0.6225 0.4592 -0.0525 -0.1281 0.1282  513 LEU B CD1 
5474 C CD2 . LEU B 387 ? 0.5923 0.5909 0.4448 -0.0421 -0.0924 0.1101  513 LEU B CD2 
5475 N N   . ILE B 388 ? 0.5194 0.5148 0.5159 0.0099  -0.0934 0.1496  514 ILE B N   
5476 C CA  . ILE B 388 ? 0.5253 0.5136 0.5549 0.0262  -0.0824 0.1431  514 ILE B CA  
5477 C C   . ILE B 388 ? 0.5561 0.5093 0.5833 0.0316  -0.0729 0.1449  514 ILE B C   
5478 O O   . ILE B 388 ? 0.5570 0.4955 0.6056 0.0455  -0.0633 0.1393  514 ILE B O   
5479 C CB  . ILE B 388 ? 0.5533 0.5654 0.6205 0.0408  -0.0918 0.1574  514 ILE B CB  
5480 C CG1 . ILE B 388 ? 0.5859 0.5901 0.6611 0.0500  -0.1033 0.1836  514 ILE B CG1 
5481 C CG2 . ILE B 388 ? 0.5428 0.5905 0.6100 0.0295  -0.1051 0.1587  514 ILE B CG2 
5482 C CD1 . ILE B 388 ? 0.5917 0.6181 0.7124 0.0714  -0.1088 0.1991  514 ILE B CD1 
5483 N N   . ALA B 389 ? 0.5518 0.4902 0.5512 0.0194  -0.0749 0.1527  515 ALA B N   
5484 C CA  . ALA B 389 ? 0.5700 0.4737 0.5646 0.0191  -0.0678 0.1563  515 ALA B CA  
5485 C C   . ALA B 389 ? 0.5862 0.4769 0.5805 0.0167  -0.0519 0.1334  515 ALA B C   
5486 O O   . ALA B 389 ? 0.5769 0.4842 0.5598 0.0079  -0.0462 0.1185  515 ALA B O   
5487 C CB  . ALA B 389 ? 0.6258 0.5243 0.5893 0.0025  -0.0720 0.1695  515 ALA B CB  
5488 N N   . ASP B 390 ? 0.5812 0.4402 0.5864 0.0249  -0.0452 0.1309  516 ASP B N   
5489 C CA  . ASP B 390 ? 0.6366 0.4817 0.6386 0.0208  -0.0320 0.1095  516 ASP B CA  
5490 C C   . ASP B 390 ? 0.6865 0.5200 0.6650 0.0000  -0.0294 0.1099  516 ASP B C   
5491 O O   . ASP B 390 ? 0.6651 0.4699 0.6361 -0.0059 -0.0325 0.1234  516 ASP B O   
5492 C CB  . ASP B 390 ? 0.6956 0.5071 0.7125 0.0365  -0.0251 0.1041  516 ASP B CB  
5493 C CG  . ASP B 390 ? 0.7473 0.5342 0.7512 0.0267  -0.0140 0.0842  516 ASP B CG  
5494 O OD1 . ASP B 390 ? 0.7504 0.5601 0.7470 0.0164  -0.0096 0.0701  516 ASP B OD1 
5495 O OD2 . ASP B 390 ? 0.8597 0.6023 0.8593 0.0290  -0.0104 0.0830  516 ASP B OD2 
5496 N N   . PRO B 391 ? 0.6698 0.5253 0.6380 -0.0114 -0.0238 0.0971  517 PRO B N   
5497 C CA  . PRO B 391 ? 0.7122 0.5663 0.6634 -0.0309 -0.0207 0.0998  517 PRO B CA  
5498 C C   . PRO B 391 ? 0.7604 0.5798 0.7098 -0.0398 -0.0170 0.0954  517 PRO B C   
5499 O O   . PRO B 391 ? 0.7927 0.6048 0.7304 -0.0579 -0.0176 0.1049  517 PRO B O   
5500 C CB  . PRO B 391 ? 0.6783 0.5663 0.6253 -0.0347 -0.0146 0.0861  517 PRO B CB  
5501 C CG  . PRO B 391 ? 0.6399 0.5334 0.6008 -0.0206 -0.0129 0.0722  517 PRO B CG  
5502 C CD  . PRO B 391 ? 0.6156 0.4997 0.5888 -0.0068 -0.0200 0.0820  517 PRO B CD  
5503 N N   . VAL B 392 ? 0.7943 0.5918 0.7525 -0.0295 -0.0129 0.0812  518 VAL B N   
5504 C CA  . VAL B 392 ? 0.8320 0.5878 0.7821 -0.0392 -0.0101 0.0749  518 VAL B CA  
5505 C C   . VAL B 392 ? 0.8657 0.5815 0.8108 -0.0414 -0.0159 0.0938  518 VAL B C   
5506 O O   . VAL B 392 ? 0.9316 0.6186 0.8631 -0.0611 -0.0170 0.0975  518 VAL B O   
5507 C CB  . VAL B 392 ? 0.8226 0.5597 0.7785 -0.0247 -0.0026 0.0547  518 VAL B CB  
5508 N N   . GLU B 393 ? 0.8925 0.6069 0.8488 -0.0228 -0.0211 0.1081  519 GLU B N   
5509 C CA  . GLU B 393 ? 0.9382 0.6131 0.8911 -0.0217 -0.0276 0.1291  519 GLU B CA  
5510 C C   . GLU B 393 ? 0.9717 0.6615 0.9101 -0.0420 -0.0345 0.1508  519 GLU B C   
5511 O O   . GLU B 393 ? 1.0429 0.6963 0.9699 -0.0547 -0.0381 0.1661  519 GLU B O   
5512 C CB  . GLU B 393 ? 0.9210 0.5942 0.8944 0.0071  -0.0317 0.1394  519 GLU B CB  
5513 N N   . VAL B 394 ? 0.8904 0.6309 0.8266 -0.0458 -0.0354 0.1523  520 VAL B N   
5514 C CA  . VAL B 394 ? 0.9036 0.6618 0.8231 -0.0633 -0.0392 0.1718  520 VAL B CA  
5515 C C   . VAL B 394 ? 0.9126 0.6750 0.8209 -0.0891 -0.0327 0.1683  520 VAL B C   
5516 O O   . VAL B 394 ? 0.9293 0.6880 0.8246 -0.1074 -0.0345 0.1876  520 VAL B O   
5517 C CB  . VAL B 394 ? 0.8591 0.6649 0.7750 -0.0574 -0.0412 0.1726  520 VAL B CB  
5518 N N   . VAL B 395 ? 0.9131 0.6865 0.8271 -0.0920 -0.0256 0.1462  521 VAL B N   
5519 C CA  . VAL B 395 ? 0.9032 0.6860 0.8113 -0.1170 -0.0212 0.1436  521 VAL B CA  
5520 C C   . VAL B 395 ? 0.9071 0.6359 0.8087 -0.1327 -0.0247 0.1475  521 VAL B C   
5521 O O   . VAL B 395 ? 0.9484 0.6672 0.8404 -0.1541 -0.0274 0.1664  521 VAL B O   
5522 C CB  . VAL B 395 ? 0.7946 0.6072 0.7107 -0.1148 -0.0148 0.1207  521 VAL B CB  
# 
