data_8Y54
# 
_entry.id   8Y54 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8Y54         pdb_00008y54 10.2210/pdb8y54/pdb 
WWPDB D_1300044668 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Y54 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ycy21th@sdu.edu.cn 
_pdbx_contact_author.name_first         Yang 
_pdbx_contact_author.name_last          Chuyu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4202-9325 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, Y.'  1 0000-0001-9838-0512 
'Yang, C.' 2 0000-0002-4202-9325 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Cystathionine beta-lyase(PatB)of Lactobacillus lactobacillus delbrueckii at 1.78 ?' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, Y.'  1 ? 
primary 'Yang, C.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'cysteine-S-conjugate beta-lyase' 44058.172 2   4.4.1.13 'V311E, N326D' ? ? 
2 water   nat water                             18.015    342 ?        ?              ? ? 
# 
_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       
;MAEKQYDFTHVPKRQGNSIKWGGLKEKELPMWIAEMDFRIAPEIMTSMEEKLKVAAFGYESVPAEYYKAVADWEEIEHRA
RPKEDWCVFASGVVPAISAMVRQFTSPGDQILVQEPVYNMFYSVIEGNGRRVISSDLIYENSKYSVNWADLEEKLATPSV
RMMVFCNPHNPIGYAWSEEEVKRIAELCAKHQVLLISDEIHGDLVLTDEDITPAFTVDWDAKNWVVSLISPSKTFNLAAL
HAACAIIPNPDLRARAEESFFLAGIGEPNLLAIPAAIAAYEEGHNWLRELKQVLRDNFAYAREFLAKEVPEVKVLDSNAS
YLAWVDISALGMNAEDFCKYLREKTGLIISAGNGYRGNGHEFVRINLACPKELVIDGMQRLKQGVLNLNN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAEKQYDFTHVPKRQGNSIKWGGLKEKELPMWIAEMDFRIAPEIMTSMEEKLKVAAFGYESVPAEYYKAVADWEEIEHRA
RPKEDWCVFASGVVPAISAMVRQFTSPGDQILVQEPVYNMFYSVIEGNGRRVISSDLIYENSKYSVNWADLEEKLATPSV
RMMVFCNPHNPIGYAWSEEEVKRIAELCAKHQVLLISDEIHGDLVLTDEDITPAFTVDWDAKNWVVSLISPSKTFNLAAL
HAACAIIPNPDLRARAEESFFLAGIGEPNLLAIPAAIAAYEEGHNWLRELKQVLRDNFAYAREFLAKEVPEVKVLDSNAS
YLAWVDISALGMNAEDFCKYLREKTGLIISAGNGYRGNGHEFVRINLACPKELVIDGMQRLKQGVLNLNN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   GLU n 
1 4   LYS n 
1 5   GLN n 
1 6   TYR n 
1 7   ASP n 
1 8   PHE n 
1 9   THR n 
1 10  HIS n 
1 11  VAL n 
1 12  PRO n 
1 13  LYS n 
1 14  ARG n 
1 15  GLN n 
1 16  GLY n 
1 17  ASN n 
1 18  SER n 
1 19  ILE n 
1 20  LYS n 
1 21  TRP n 
1 22  GLY n 
1 23  GLY n 
1 24  LEU n 
1 25  LYS n 
1 26  GLU n 
1 27  LYS n 
1 28  GLU n 
1 29  LEU n 
1 30  PRO n 
1 31  MET n 
1 32  TRP n 
1 33  ILE n 
1 34  ALA n 
1 35  GLU n 
1 36  MET n 
1 37  ASP n 
1 38  PHE n 
1 39  ARG n 
1 40  ILE n 
1 41  ALA n 
1 42  PRO n 
1 43  GLU n 
1 44  ILE n 
1 45  MET n 
1 46  THR n 
1 47  SER n 
1 48  MET n 
1 49  GLU n 
1 50  GLU n 
1 51  LYS n 
1 52  LEU n 
1 53  LYS n 
1 54  VAL n 
1 55  ALA n 
1 56  ALA n 
1 57  PHE n 
1 58  GLY n 
1 59  TYR n 
1 60  GLU n 
1 61  SER n 
1 62  VAL n 
1 63  PRO n 
1 64  ALA n 
1 65  GLU n 
1 66  TYR n 
1 67  TYR n 
1 68  LYS n 
1 69  ALA n 
1 70  VAL n 
1 71  ALA n 
1 72  ASP n 
1 73  TRP n 
1 74  GLU n 
1 75  GLU n 
1 76  ILE n 
1 77  GLU n 
1 78  HIS n 
1 79  ARG n 
1 80  ALA n 
1 81  ARG n 
1 82  PRO n 
1 83  LYS n 
1 84  GLU n 
1 85  ASP n 
1 86  TRP n 
1 87  CYS n 
1 88  VAL n 
1 89  PHE n 
1 90  ALA n 
1 91  SER n 
1 92  GLY n 
1 93  VAL n 
1 94  VAL n 
1 95  PRO n 
1 96  ALA n 
1 97  ILE n 
1 98  SER n 
1 99  ALA n 
1 100 MET n 
1 101 VAL n 
1 102 ARG n 
1 103 GLN n 
1 104 PHE n 
1 105 THR n 
1 106 SER n 
1 107 PRO n 
1 108 GLY n 
1 109 ASP n 
1 110 GLN n 
1 111 ILE n 
1 112 LEU n 
1 113 VAL n 
1 114 GLN n 
1 115 GLU n 
1 116 PRO n 
1 117 VAL n 
1 118 TYR n 
1 119 ASN n 
1 120 MET n 
1 121 PHE n 
1 122 TYR n 
1 123 SER n 
1 124 VAL n 
1 125 ILE n 
1 126 GLU n 
1 127 GLY n 
1 128 ASN n 
1 129 GLY n 
1 130 ARG n 
1 131 ARG n 
1 132 VAL n 
1 133 ILE n 
1 134 SER n 
1 135 SER n 
1 136 ASP n 
1 137 LEU n 
1 138 ILE n 
1 139 TYR n 
1 140 GLU n 
1 141 ASN n 
1 142 SER n 
1 143 LYS n 
1 144 TYR n 
1 145 SER n 
1 146 VAL n 
1 147 ASN n 
1 148 TRP n 
1 149 ALA n 
1 150 ASP n 
1 151 LEU n 
1 152 GLU n 
1 153 GLU n 
1 154 LYS n 
1 155 LEU n 
1 156 ALA n 
1 157 THR n 
1 158 PRO n 
1 159 SER n 
1 160 VAL n 
1 161 ARG n 
1 162 MET n 
1 163 MET n 
1 164 VAL n 
1 165 PHE n 
1 166 CYS n 
1 167 ASN n 
1 168 PRO n 
1 169 HIS n 
1 170 ASN n 
1 171 PRO n 
1 172 ILE n 
1 173 GLY n 
1 174 TYR n 
1 175 ALA n 
1 176 TRP n 
1 177 SER n 
1 178 GLU n 
1 179 GLU n 
1 180 GLU n 
1 181 VAL n 
1 182 LYS n 
1 183 ARG n 
1 184 ILE n 
1 185 ALA n 
1 186 GLU n 
1 187 LEU n 
1 188 CYS n 
1 189 ALA n 
1 190 LYS n 
1 191 HIS n 
1 192 GLN n 
1 193 VAL n 
1 194 LEU n 
1 195 LEU n 
1 196 ILE n 
1 197 SER n 
1 198 ASP n 
1 199 GLU n 
1 200 ILE n 
1 201 HIS n 
1 202 GLY n 
1 203 ASP n 
1 204 LEU n 
1 205 VAL n 
1 206 LEU n 
1 207 THR n 
1 208 ASP n 
1 209 GLU n 
1 210 ASP n 
1 211 ILE n 
1 212 THR n 
1 213 PRO n 
1 214 ALA n 
1 215 PHE n 
1 216 THR n 
1 217 VAL n 
1 218 ASP n 
1 219 TRP n 
1 220 ASP n 
1 221 ALA n 
1 222 LYS n 
1 223 ASN n 
1 224 TRP n 
1 225 VAL n 
1 226 VAL n 
1 227 SER n 
1 228 LEU n 
1 229 ILE n 
1 230 SER n 
1 231 PRO n 
1 232 SER n 
1 233 LYS n 
1 234 THR n 
1 235 PHE n 
1 236 ASN n 
1 237 LEU n 
1 238 ALA n 
1 239 ALA n 
1 240 LEU n 
1 241 HIS n 
1 242 ALA n 
1 243 ALA n 
1 244 CYS n 
1 245 ALA n 
1 246 ILE n 
1 247 ILE n 
1 248 PRO n 
1 249 ASN n 
1 250 PRO n 
1 251 ASP n 
1 252 LEU n 
1 253 ARG n 
1 254 ALA n 
1 255 ARG n 
1 256 ALA n 
1 257 GLU n 
1 258 GLU n 
1 259 SER n 
1 260 PHE n 
1 261 PHE n 
1 262 LEU n 
1 263 ALA n 
1 264 GLY n 
1 265 ILE n 
1 266 GLY n 
1 267 GLU n 
1 268 PRO n 
1 269 ASN n 
1 270 LEU n 
1 271 LEU n 
1 272 ALA n 
1 273 ILE n 
1 274 PRO n 
1 275 ALA n 
1 276 ALA n 
1 277 ILE n 
1 278 ALA n 
1 279 ALA n 
1 280 TYR n 
1 281 GLU n 
1 282 GLU n 
1 283 GLY n 
1 284 HIS n 
1 285 ASN n 
1 286 TRP n 
1 287 LEU n 
1 288 ARG n 
1 289 GLU n 
1 290 LEU n 
1 291 LYS n 
1 292 GLN n 
1 293 VAL n 
1 294 LEU n 
1 295 ARG n 
1 296 ASP n 
1 297 ASN n 
1 298 PHE n 
1 299 ALA n 
1 300 TYR n 
1 301 ALA n 
1 302 ARG n 
1 303 GLU n 
1 304 PHE n 
1 305 LEU n 
1 306 ALA n 
1 307 LYS n 
1 308 GLU n 
1 309 VAL n 
1 310 PRO n 
1 311 GLU n 
1 312 VAL n 
1 313 LYS n 
1 314 VAL n 
1 315 LEU n 
1 316 ASP n 
1 317 SER n 
1 318 ASN n 
1 319 ALA n 
1 320 SER n 
1 321 TYR n 
1 322 LEU n 
1 323 ALA n 
1 324 TRP n 
1 325 VAL n 
1 326 ASP n 
1 327 ILE n 
1 328 SER n 
1 329 ALA n 
1 330 LEU n 
1 331 GLY n 
1 332 MET n 
1 333 ASN n 
1 334 ALA n 
1 335 GLU n 
1 336 ASP n 
1 337 PHE n 
1 338 CYS n 
1 339 LYS n 
1 340 TYR n 
1 341 LEU n 
1 342 ARG n 
1 343 GLU n 
1 344 LYS n 
1 345 THR n 
1 346 GLY n 
1 347 LEU n 
1 348 ILE n 
1 349 ILE n 
1 350 SER n 
1 351 ALA n 
1 352 GLY n 
1 353 ASN n 
1 354 GLY n 
1 355 TYR n 
1 356 ARG n 
1 357 GLY n 
1 358 ASN n 
1 359 GLY n 
1 360 HIS n 
1 361 GLU n 
1 362 PHE n 
1 363 VAL n 
1 364 ARG n 
1 365 ILE n 
1 366 ASN n 
1 367 LEU n 
1 368 ALA n 
1 369 CYS n 
1 370 PRO n 
1 371 LYS n 
1 372 GLU n 
1 373 LEU n 
1 374 VAL n 
1 375 ILE n 
1 376 ASP n 
1 377 GLY n 
1 378 MET n 
1 379 GLN n 
1 380 ARG n 
1 381 LEU n 
1 382 LYS n 
1 383 GLN n 
1 384 GLY n 
1 385 VAL n 
1 386 LEU n 
1 387 ASN n 
1 388 LEU n 
1 389 ASN n 
1 390 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   390 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 LDL72_07215 
_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      'Lactobacillus delbrueckii subsp. lactis DSM 20072' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     888027 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   ASP 7   7   7   ASP ASP A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  TRP 21  21  21  TRP TRP A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  MET 31  31  31  MET MET A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  MET 36  36  36  MET MET A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  MET 45  45  45  MET MET A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  MET 48  48  48  MET MET A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  TYR 66  66  66  TYR TYR A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  TRP 73  73  73  TRP TRP A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  ILE 76  76  76  ILE ILE A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  TRP 86  86  86  TRP TRP A . n 
A 1 87  CYS 87  87  87  CYS CYS A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 PHE 104 104 104 PHE PHE A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 PRO 107 107 107 PRO PRO A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 MET 120 120 120 MET MET A . n 
A 1 121 PHE 121 121 121 PHE PHE A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 ASN 141 141 141 ASN ASN A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 TRP 148 148 148 TRP TRP A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 MET 163 163 163 MET MET A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 CYS 166 166 166 CYS CYS A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 HIS 169 169 169 HIS HIS A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 PRO 171 171 171 PRO PRO A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 TYR 174 174 174 TYR TYR A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 TRP 176 176 176 TRP TRP A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 LYS 182 182 182 LYS LYS A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 CYS 188 188 188 CYS CYS A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 HIS 191 191 191 HIS HIS A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 HIS 201 201 201 HIS HIS A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 GLU 209 209 209 GLU GLU A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 THR 212 212 212 THR THR A . n 
A 1 213 PRO 213 213 213 PRO PRO A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 PHE 215 215 215 PHE PHE A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 TRP 219 219 219 TRP TRP A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 ASN 223 223 223 ASN ASN A . n 
A 1 224 TRP 224 224 224 TRP TRP A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 SER 227 227 227 SER SER A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 THR 234 234 234 THR THR A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 ASN 236 236 236 ASN ASN A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 HIS 241 241 241 HIS HIS A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 CYS 244 244 244 CYS CYS A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 ILE 265 265 265 ILE ILE A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 PRO 268 268 268 PRO PRO A . n 
A 1 269 ASN 269 269 269 ASN ASN A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 PRO 274 274 274 PRO PRO A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 ILE 277 277 277 ILE ILE A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 TYR 280 280 280 TYR TYR A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 HIS 284 284 284 HIS HIS A . n 
A 1 285 ASN 285 285 285 ASN ASN A . n 
A 1 286 TRP 286 286 286 TRP TRP A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 GLN 292 292 292 GLN GLN A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 ASP 296 296 296 ASP ASP A . n 
A 1 297 ASN 297 297 297 ASN ASN A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 TYR 300 300 300 TYR TYR A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 ASP 316 316 316 ASP ASP A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 ASN 318 318 318 ASN ASN A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 SER 320 320 320 SER SER A . n 
A 1 321 TYR 321 321 321 TYR TYR A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 TRP 324 324 324 TRP TRP A . n 
A 1 325 VAL 325 325 325 VAL VAL A . n 
A 1 326 ASP 326 326 326 ASP ASP A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 SER 328 328 328 SER SER A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 MET 332 332 332 MET MET A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 GLU 335 335 335 GLU GLU A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 CYS 338 338 338 CYS CYS A . n 
A 1 339 LYS 339 339 339 LYS LYS A . n 
A 1 340 TYR 340 340 340 TYR TYR A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 ARG 342 342 342 ARG ARG A . n 
A 1 343 GLU 343 343 343 GLU GLU A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 THR 345 345 345 THR THR A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 ILE 348 348 348 ILE ILE A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 SER 350 350 350 SER SER A . n 
A 1 351 ALA 351 351 351 ALA ALA A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 ASN 353 353 353 ASN ASN A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 TYR 355 355 355 TYR TYR A . n 
A 1 356 ARG 356 356 356 ARG ARG A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 ASN 358 358 358 ASN ASN A . n 
A 1 359 GLY 359 359 359 GLY GLY A . n 
A 1 360 HIS 360 360 360 HIS HIS A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 PHE 362 362 362 PHE PHE A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ARG 364 364 364 ARG ARG A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 ASN 366 366 366 ASN ASN A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 ALA 368 368 368 ALA ALA A . n 
A 1 369 CYS 369 369 369 CYS CYS A . n 
A 1 370 PRO 370 370 370 PRO PRO A . n 
A 1 371 LYS 371 371 371 LYS LYS A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 ILE 375 375 375 ILE ILE A . n 
A 1 376 ASP 376 376 376 ASP ASP A . n 
A 1 377 GLY 377 377 377 GLY GLY A . n 
A 1 378 MET 378 378 378 MET MET A . n 
A 1 379 GLN 379 379 379 GLN GLN A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 LYS 382 382 382 LYS LYS A . n 
A 1 383 GLN 383 383 383 GLN GLN A . n 
A 1 384 GLY 384 384 384 GLY GLY A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 ASN 387 387 387 ASN ASN A . n 
A 1 388 LEU 388 388 388 LEU LEU A . n 
A 1 389 ASN 389 389 389 ASN ASN A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   ?   ?   ?   B . n 
B 1 3   GLU 3   3   3   GLU GLU B . n 
B 1 4   LYS 4   4   4   LYS LYS B . n 
B 1 5   GLN 5   5   5   GLN GLN B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   ASP 7   7   7   ASP ASP B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   THR 9   9   9   THR THR B . n 
B 1 10  HIS 10  10  10  HIS HIS B . n 
B 1 11  VAL 11  11  11  VAL VAL B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  LYS 13  13  13  LYS LYS B . n 
B 1 14  ARG 14  14  14  ARG ARG B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ASN 17  17  17  ASN ASN B . n 
B 1 18  SER 18  18  18  SER SER B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  TRP 21  21  21  TRP TRP B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  LYS 25  25  ?   ?   ?   B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  GLU 28  28  28  GLU GLU B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  MET 31  31  31  MET MET B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  MET 36  36  36  MET MET B . n 
B 1 37  ASP 37  37  37  ASP ASP B . n 
B 1 38  PHE 38  38  38  PHE PHE B . n 
B 1 39  ARG 39  39  39  ARG ARG B . n 
B 1 40  ILE 40  40  40  ILE ILE B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  MET 45  45  45  MET MET B . n 
B 1 46  THR 46  46  46  THR THR B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  MET 48  48  48  MET MET B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  GLU 50  50  50  GLU GLU B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  VAL 54  54  54  VAL VAL B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  PHE 57  57  57  PHE PHE B . n 
B 1 58  GLY 58  58  58  GLY GLY B . n 
B 1 59  TYR 59  59  59  TYR TYR B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  SER 61  61  61  SER SER B . n 
B 1 62  VAL 62  62  62  VAL VAL B . n 
B 1 63  PRO 63  63  63  PRO PRO B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  TYR 66  66  66  TYR TYR B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  TRP 73  73  73  TRP TRP B . n 
B 1 74  GLU 74  74  74  GLU GLU B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  ILE 76  76  76  ILE ILE B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  HIS 78  78  78  HIS HIS B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  PRO 82  82  82  PRO PRO B . n 
B 1 83  LYS 83  83  83  LYS LYS B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  TRP 86  86  86  TRP TRP B . n 
B 1 87  CYS 87  87  87  CYS CYS B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  SER 91  91  91  SER SER B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  PRO 95  95  95  PRO PRO B . n 
B 1 96  ALA 96  96  96  ALA ALA B . n 
B 1 97  ILE 97  97  97  ILE ILE B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 MET 100 100 100 MET MET B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 ARG 102 102 102 ARG ARG B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 PHE 104 104 104 PHE PHE B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 PRO 107 107 107 PRO PRO B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 ILE 111 111 111 ILE ILE B . n 
B 1 112 LEU 112 112 112 LEU LEU B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 GLN 114 114 114 GLN GLN B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 PRO 116 116 116 PRO PRO B . n 
B 1 117 VAL 117 117 117 VAL VAL B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 MET 120 120 120 MET MET B . n 
B 1 121 PHE 121 121 121 PHE PHE B . n 
B 1 122 TYR 122 122 122 TYR TYR B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 ASN 128 128 128 ASN ASN B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 ARG 130 130 130 ARG ARG B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 ILE 133 133 133 ILE ILE B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 SER 135 135 135 SER SER B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 ILE 138 138 138 ILE ILE B . n 
B 1 139 TYR 139 139 139 TYR TYR B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 ASN 141 141 141 ASN ASN B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 TYR 144 144 144 TYR TYR B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 ASN 147 147 147 ASN ASN B . n 
B 1 148 TRP 148 148 148 TRP TRP B . n 
B 1 149 ALA 149 149 149 ALA ALA B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 LYS 154 154 154 LYS LYS B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 ALA 156 156 156 ALA ALA B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 PRO 158 158 158 PRO PRO B . n 
B 1 159 SER 159 159 159 SER SER B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 MET 163 163 163 MET MET B . n 
B 1 164 VAL 164 164 164 VAL VAL B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 CYS 166 166 166 CYS CYS B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 HIS 169 169 169 HIS HIS B . n 
B 1 170 ASN 170 170 170 ASN ASN B . n 
B 1 171 PRO 171 171 171 PRO PRO B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 TYR 174 174 174 TYR TYR B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 TRP 176 176 176 TRP TRP B . n 
B 1 177 SER 177 177 177 SER SER B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLU 179 179 179 GLU GLU B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 VAL 181 181 181 VAL VAL B . n 
B 1 182 LYS 182 182 182 LYS LYS B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 ILE 184 184 184 ILE ILE B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 CYS 188 188 188 CYS CYS B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 LYS 190 190 190 LYS LYS B . n 
B 1 191 HIS 191 191 191 HIS HIS B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 LEU 194 194 194 LEU LEU B . n 
B 1 195 LEU 195 195 195 LEU LEU B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 ASP 198 198 198 ASP ASP B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 HIS 201 201 201 HIS HIS B . n 
B 1 202 GLY 202 202 202 GLY GLY B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 VAL 205 205 205 VAL VAL B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 THR 207 207 207 THR THR B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 GLU 209 209 209 GLU GLU B . n 
B 1 210 ASP 210 210 210 ASP ASP B . n 
B 1 211 ILE 211 211 211 ILE ILE B . n 
B 1 212 THR 212 212 212 THR THR B . n 
B 1 213 PRO 213 213 213 PRO PRO B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 PHE 215 215 215 PHE PHE B . n 
B 1 216 THR 216 216 216 THR THR B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 ASP 218 218 218 ASP ASP B . n 
B 1 219 TRP 219 219 219 TRP TRP B . n 
B 1 220 ASP 220 220 ?   ?   ?   B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 LYS 222 222 222 LYS LYS B . n 
B 1 223 ASN 223 223 223 ASN ASN B . n 
B 1 224 TRP 224 224 224 TRP TRP B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 SER 227 227 227 SER SER B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 PRO 231 231 231 PRO PRO B . n 
B 1 232 SER 232 232 232 SER SER B . n 
B 1 233 LYS 233 233 233 LYS LYS B . n 
B 1 234 THR 234 234 234 THR THR B . n 
B 1 235 PHE 235 235 235 PHE PHE B . n 
B 1 236 ASN 236 236 236 ASN ASN B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 ALA 238 238 238 ALA ALA B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 HIS 241 241 241 HIS HIS B . n 
B 1 242 ALA 242 242 242 ALA ALA B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 CYS 244 244 244 CYS CYS B . n 
B 1 245 ALA 245 245 245 ALA ALA B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 ILE 247 247 247 ILE ILE B . n 
B 1 248 PRO 248 248 248 PRO PRO B . n 
B 1 249 ASN 249 249 249 ASN ASN B . n 
B 1 250 PRO 250 250 250 PRO PRO B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 LEU 252 252 252 LEU LEU B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 ALA 254 254 254 ALA ALA B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 ALA 256 256 256 ALA ALA B . n 
B 1 257 GLU 257 257 257 GLU GLU B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 SER 259 259 259 SER SER B . n 
B 1 260 PHE 260 260 260 PHE PHE B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 ILE 265 265 265 ILE ILE B . n 
B 1 266 GLY 266 266 266 GLY GLY B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 PRO 268 268 268 PRO PRO B . n 
B 1 269 ASN 269 269 269 ASN ASN B . n 
B 1 270 LEU 270 270 270 LEU LEU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 ALA 272 272 272 ALA ALA B . n 
B 1 273 ILE 273 273 273 ILE ILE B . n 
B 1 274 PRO 274 274 274 PRO PRO B . n 
B 1 275 ALA 275 275 275 ALA ALA B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 ILE 277 277 277 ILE ILE B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 ALA 279 279 279 ALA ALA B . n 
B 1 280 TYR 280 280 280 TYR TYR B . n 
B 1 281 GLU 281 281 281 GLU GLU B . n 
B 1 282 GLU 282 282 282 GLU GLU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 HIS 284 284 284 HIS HIS B . n 
B 1 285 ASN 285 285 285 ASN ASN B . n 
B 1 286 TRP 286 286 286 TRP TRP B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 ARG 288 288 288 ARG ARG B . n 
B 1 289 GLU 289 289 289 GLU GLU B . n 
B 1 290 LEU 290 290 290 LEU LEU B . n 
B 1 291 LYS 291 291 291 LYS LYS B . n 
B 1 292 GLN 292 292 292 GLN GLN B . n 
B 1 293 VAL 293 293 293 VAL VAL B . n 
B 1 294 LEU 294 294 294 LEU LEU B . n 
B 1 295 ARG 295 295 295 ARG ARG B . n 
B 1 296 ASP 296 296 296 ASP ASP B . n 
B 1 297 ASN 297 297 297 ASN ASN B . n 
B 1 298 PHE 298 298 298 PHE PHE B . n 
B 1 299 ALA 299 299 299 ALA ALA B . n 
B 1 300 TYR 300 300 300 TYR TYR B . n 
B 1 301 ALA 301 301 301 ALA ALA B . n 
B 1 302 ARG 302 302 302 ARG ARG B . n 
B 1 303 GLU 303 303 303 GLU GLU B . n 
B 1 304 PHE 304 304 304 PHE PHE B . n 
B 1 305 LEU 305 305 305 LEU LEU B . n 
B 1 306 ALA 306 306 306 ALA ALA B . n 
B 1 307 LYS 307 307 307 LYS LYS B . n 
B 1 308 GLU 308 308 308 GLU GLU B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 PRO 310 310 310 PRO PRO B . n 
B 1 311 GLU 311 311 311 GLU GLU B . n 
B 1 312 VAL 312 312 312 VAL VAL B . n 
B 1 313 LYS 313 313 313 LYS LYS B . n 
B 1 314 VAL 314 314 314 VAL VAL B . n 
B 1 315 LEU 315 315 315 LEU LEU B . n 
B 1 316 ASP 316 316 316 ASP ASP B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 ASN 318 318 318 ASN ASN B . n 
B 1 319 ALA 319 319 319 ALA ALA B . n 
B 1 320 SER 320 320 320 SER SER B . n 
B 1 321 TYR 321 321 321 TYR TYR B . n 
B 1 322 LEU 322 322 322 LEU LEU B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 TRP 324 324 324 TRP TRP B . n 
B 1 325 VAL 325 325 325 VAL VAL B . n 
B 1 326 ASP 326 326 326 ASP ASP B . n 
B 1 327 ILE 327 327 327 ILE ILE B . n 
B 1 328 SER 328 328 328 SER SER B . n 
B 1 329 ALA 329 329 329 ALA ALA B . n 
B 1 330 LEU 330 330 330 LEU LEU B . n 
B 1 331 GLY 331 331 331 GLY GLY B . n 
B 1 332 MET 332 332 332 MET MET B . n 
B 1 333 ASN 333 333 333 ASN ASN B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 GLU 335 335 335 GLU GLU B . n 
B 1 336 ASP 336 336 336 ASP ASP B . n 
B 1 337 PHE 337 337 337 PHE PHE B . n 
B 1 338 CYS 338 338 338 CYS CYS B . n 
B 1 339 LYS 339 339 339 LYS LYS B . n 
B 1 340 TYR 340 340 340 TYR TYR B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 ARG 342 342 342 ARG ARG B . n 
B 1 343 GLU 343 343 343 GLU GLU B . n 
B 1 344 LYS 344 344 344 LYS LYS B . n 
B 1 345 THR 345 345 345 THR THR B . n 
B 1 346 GLY 346 346 346 GLY GLY B . n 
B 1 347 LEU 347 347 347 LEU LEU B . n 
B 1 348 ILE 348 348 348 ILE ILE B . n 
B 1 349 ILE 349 349 349 ILE ILE B . n 
B 1 350 SER 350 350 350 SER SER B . n 
B 1 351 ALA 351 351 351 ALA ALA B . n 
B 1 352 GLY 352 352 352 GLY GLY B . n 
B 1 353 ASN 353 353 353 ASN ASN B . n 
B 1 354 GLY 354 354 354 GLY GLY B . n 
B 1 355 TYR 355 355 355 TYR TYR B . n 
B 1 356 ARG 356 356 356 ARG ARG B . n 
B 1 357 GLY 357 357 357 GLY GLY B . n 
B 1 358 ASN 358 358 358 ASN ASN B . n 
B 1 359 GLY 359 359 359 GLY GLY B . n 
B 1 360 HIS 360 360 360 HIS HIS B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 PHE 362 362 362 PHE PHE B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 ARG 364 364 364 ARG ARG B . n 
B 1 365 ILE 365 365 365 ILE ILE B . n 
B 1 366 ASN 366 366 366 ASN ASN B . n 
B 1 367 LEU 367 367 367 LEU LEU B . n 
B 1 368 ALA 368 368 368 ALA ALA B . n 
B 1 369 CYS 369 369 369 CYS CYS B . n 
B 1 370 PRO 370 370 370 PRO PRO B . n 
B 1 371 LYS 371 371 371 LYS LYS B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 VAL 374 374 374 VAL VAL B . n 
B 1 375 ILE 375 375 375 ILE ILE B . n 
B 1 376 ASP 376 376 376 ASP ASP B . n 
B 1 377 GLY 377 377 377 GLY GLY B . n 
B 1 378 MET 378 378 378 MET MET B . n 
B 1 379 GLN 379 379 379 GLN GLN B . n 
B 1 380 ARG 380 380 380 ARG ARG B . n 
B 1 381 LEU 381 381 381 LEU LEU B . n 
B 1 382 LYS 382 382 382 LYS LYS B . n 
B 1 383 GLN 383 383 383 GLN GLN B . n 
B 1 384 GLY 384 384 384 GLY GLY B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 ASN 387 387 387 ASN ASN B . n 
B 1 388 LEU 388 388 388 LEU LEU B . n 
B 1 389 ASN 389 389 389 ASN ASN B . n 
B 1 390 ASN 390 390 390 ASN ASN B . n 
# 
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 HOH 1   401 293 HOH HOH A . 
C 2 HOH 2   402 245 HOH HOH A . 
C 2 HOH 3   403 375 HOH HOH A . 
C 2 HOH 4   404 45  HOH HOH A . 
C 2 HOH 5   405 214 HOH HOH A . 
C 2 HOH 6   406 151 HOH HOH A . 
C 2 HOH 7   407 110 HOH HOH A . 
C 2 HOH 8   408 270 HOH HOH A . 
C 2 HOH 9   409 123 HOH HOH A . 
C 2 HOH 10  410 103 HOH HOH A . 
C 2 HOH 11  411 355 HOH HOH A . 
C 2 HOH 12  412 8   HOH HOH A . 
C 2 HOH 13  413 234 HOH HOH A . 
C 2 HOH 14  414 128 HOH HOH A . 
C 2 HOH 15  415 134 HOH HOH A . 
C 2 HOH 16  416 31  HOH HOH A . 
C 2 HOH 17  417 241 HOH HOH A . 
C 2 HOH 18  418 272 HOH HOH A . 
C 2 HOH 19  419 67  HOH HOH A . 
C 2 HOH 20  420 56  HOH HOH A . 
C 2 HOH 21  421 193 HOH HOH A . 
C 2 HOH 22  422 60  HOH HOH A . 
C 2 HOH 23  423 76  HOH HOH A . 
C 2 HOH 24  424 86  HOH HOH A . 
C 2 HOH 25  425 109 HOH HOH A . 
C 2 HOH 26  426 62  HOH HOH A . 
C 2 HOH 27  427 81  HOH HOH A . 
C 2 HOH 28  428 127 HOH HOH A . 
C 2 HOH 29  429 59  HOH HOH A . 
C 2 HOH 30  430 133 HOH HOH A . 
C 2 HOH 31  431 77  HOH HOH A . 
C 2 HOH 32  432 170 HOH HOH A . 
C 2 HOH 33  433 299 HOH HOH A . 
C 2 HOH 34  434 199 HOH HOH A . 
C 2 HOH 35  435 154 HOH HOH A . 
C 2 HOH 36  436 120 HOH HOH A . 
C 2 HOH 37  437 251 HOH HOH A . 
C 2 HOH 38  438 308 HOH HOH A . 
C 2 HOH 39  439 249 HOH HOH A . 
C 2 HOH 40  440 82  HOH HOH A . 
C 2 HOH 41  441 150 HOH HOH A . 
C 2 HOH 42  442 342 HOH HOH A . 
C 2 HOH 43  443 71  HOH HOH A . 
C 2 HOH 44  444 247 HOH HOH A . 
C 2 HOH 45  445 237 HOH HOH A . 
C 2 HOH 46  446 42  HOH HOH A . 
C 2 HOH 47  447 30  HOH HOH A . 
C 2 HOH 48  448 265 HOH HOH A . 
C 2 HOH 49  449 169 HOH HOH A . 
C 2 HOH 50  450 183 HOH HOH A . 
C 2 HOH 51  451 21  HOH HOH A . 
C 2 HOH 52  452 11  HOH HOH A . 
C 2 HOH 53  453 188 HOH HOH A . 
C 2 HOH 54  454 367 HOH HOH A . 
C 2 HOH 55  455 5   HOH HOH A . 
C 2 HOH 56  456 304 HOH HOH A . 
C 2 HOH 57  457 79  HOH HOH A . 
C 2 HOH 58  458 57  HOH HOH A . 
C 2 HOH 59  459 138 HOH HOH A . 
C 2 HOH 60  460 93  HOH HOH A . 
C 2 HOH 61  461 13  HOH HOH A . 
C 2 HOH 62  462 39  HOH HOH A . 
C 2 HOH 63  463 164 HOH HOH A . 
C 2 HOH 64  464 35  HOH HOH A . 
C 2 HOH 65  465 236 HOH HOH A . 
C 2 HOH 66  466 315 HOH HOH A . 
C 2 HOH 67  467 63  HOH HOH A . 
C 2 HOH 68  468 357 HOH HOH A . 
C 2 HOH 69  469 70  HOH HOH A . 
C 2 HOH 70  470 331 HOH HOH A . 
C 2 HOH 71  471 48  HOH HOH A . 
C 2 HOH 72  472 246 HOH HOH A . 
C 2 HOH 73  473 373 HOH HOH A . 
C 2 HOH 74  474 69  HOH HOH A . 
C 2 HOH 75  475 264 HOH HOH A . 
C 2 HOH 76  476 4   HOH HOH A . 
C 2 HOH 77  477 369 HOH HOH A . 
C 2 HOH 78  478 14  HOH HOH A . 
C 2 HOH 79  479 352 HOH HOH A . 
C 2 HOH 80  480 111 HOH HOH A . 
C 2 HOH 81  481 238 HOH HOH A . 
C 2 HOH 82  482 371 HOH HOH A . 
C 2 HOH 83  483 140 HOH HOH A . 
C 2 HOH 84  484 50  HOH HOH A . 
C 2 HOH 85  485 198 HOH HOH A . 
C 2 HOH 86  486 233 HOH HOH A . 
C 2 HOH 87  487 126 HOH HOH A . 
C 2 HOH 88  488 232 HOH HOH A . 
C 2 HOH 89  489 139 HOH HOH A . 
C 2 HOH 90  490 142 HOH HOH A . 
C 2 HOH 91  491 26  HOH HOH A . 
C 2 HOH 92  492 316 HOH HOH A . 
C 2 HOH 93  493 157 HOH HOH A . 
C 2 HOH 94  494 94  HOH HOH A . 
C 2 HOH 95  495 113 HOH HOH A . 
C 2 HOH 96  496 3   HOH HOH A . 
C 2 HOH 97  497 223 HOH HOH A . 
C 2 HOH 98  498 184 HOH HOH A . 
C 2 HOH 99  499 95  HOH HOH A . 
C 2 HOH 100 500 190 HOH HOH A . 
C 2 HOH 101 501 281 HOH HOH A . 
C 2 HOH 102 502 182 HOH HOH A . 
C 2 HOH 103 503 189 HOH HOH A . 
C 2 HOH 104 504 275 HOH HOH A . 
C 2 HOH 105 505 260 HOH HOH A . 
C 2 HOH 106 506 353 HOH HOH A . 
C 2 HOH 107 507 136 HOH HOH A . 
C 2 HOH 108 508 155 HOH HOH A . 
C 2 HOH 109 509 38  HOH HOH A . 
C 2 HOH 110 510 179 HOH HOH A . 
C 2 HOH 111 511 268 HOH HOH A . 
C 2 HOH 112 512 174 HOH HOH A . 
C 2 HOH 113 513 65  HOH HOH A . 
C 2 HOH 114 514 132 HOH HOH A . 
C 2 HOH 115 515 161 HOH HOH A . 
C 2 HOH 116 516 171 HOH HOH A . 
C 2 HOH 117 517 280 HOH HOH A . 
C 2 HOH 118 518 72  HOH HOH A . 
C 2 HOH 119 519 321 HOH HOH A . 
C 2 HOH 120 520 121 HOH HOH A . 
C 2 HOH 121 521 162 HOH HOH A . 
C 2 HOH 122 522 273 HOH HOH A . 
C 2 HOH 123 523 257 HOH HOH A . 
C 2 HOH 124 524 242 HOH HOH A . 
C 2 HOH 125 525 303 HOH HOH A . 
C 2 HOH 126 526 259 HOH HOH A . 
C 2 HOH 127 527 318 HOH HOH A . 
C 2 HOH 128 528 102 HOH HOH A . 
C 2 HOH 129 529 178 HOH HOH A . 
C 2 HOH 130 530 180 HOH HOH A . 
C 2 HOH 131 531 300 HOH HOH A . 
C 2 HOH 132 532 294 HOH HOH A . 
C 2 HOH 133 533 250 HOH HOH A . 
C 2 HOH 134 534 358 HOH HOH A . 
C 2 HOH 135 535 163 HOH HOH A . 
C 2 HOH 136 536 298 HOH HOH A . 
C 2 HOH 137 537 87  HOH HOH A . 
C 2 HOH 138 538 229 HOH HOH A . 
C 2 HOH 139 539 202 HOH HOH A . 
C 2 HOH 140 540 215 HOH HOH A . 
C 2 HOH 141 541 92  HOH HOH A . 
C 2 HOH 142 542 219 HOH HOH A . 
C 2 HOH 143 543 22  HOH HOH A . 
C 2 HOH 144 544 368 HOH HOH A . 
C 2 HOH 145 545 340 HOH HOH A . 
C 2 HOH 146 546 327 HOH HOH A . 
C 2 HOH 147 547 118 HOH HOH A . 
C 2 HOH 148 548 374 HOH HOH A . 
C 2 HOH 149 549 302 HOH HOH A . 
C 2 HOH 150 550 289 HOH HOH A . 
C 2 HOH 151 551 256 HOH HOH A . 
C 2 HOH 152 552 195 HOH HOH A . 
C 2 HOH 153 553 376 HOH HOH A . 
C 2 HOH 154 554 350 HOH HOH A . 
C 2 HOH 155 555 359 HOH HOH A . 
C 2 HOH 156 556 341 HOH HOH A . 
C 2 HOH 157 557 119 HOH HOH A . 
C 2 HOH 158 558 328 HOH HOH A . 
C 2 HOH 159 559 220 HOH HOH A . 
C 2 HOH 160 560 370 HOH HOH A . 
C 2 HOH 161 561 307 HOH HOH A . 
C 2 HOH 162 562 323 HOH HOH A . 
C 2 HOH 163 563 166 HOH HOH A . 
C 2 HOH 164 564 158 HOH HOH A . 
C 2 HOH 165 565 263 HOH HOH A . 
D 2 HOH 1   401 12  HOH HOH B . 
D 2 HOH 2   402 344 HOH HOH B . 
D 2 HOH 3   403 172 HOH HOH B . 
D 2 HOH 4   404 23  HOH HOH B . 
D 2 HOH 5   405 274 HOH HOH B . 
D 2 HOH 6   406 148 HOH HOH B . 
D 2 HOH 7   407 144 HOH HOH B . 
D 2 HOH 8   408 129 HOH HOH B . 
D 2 HOH 9   409 2   HOH HOH B . 
D 2 HOH 10  410 292 HOH HOH B . 
D 2 HOH 11  411 309 HOH HOH B . 
D 2 HOH 12  412 288 HOH HOH B . 
D 2 HOH 13  413 345 HOH HOH B . 
D 2 HOH 14  414 200 HOH HOH B . 
D 2 HOH 15  415 108 HOH HOH B . 
D 2 HOH 16  416 290 HOH HOH B . 
D 2 HOH 17  417 61  HOH HOH B . 
D 2 HOH 18  418 29  HOH HOH B . 
D 2 HOH 19  419 145 HOH HOH B . 
D 2 HOH 20  420 52  HOH HOH B . 
D 2 HOH 21  421 267 HOH HOH B . 
D 2 HOH 22  422 301 HOH HOH B . 
D 2 HOH 23  423 32  HOH HOH B . 
D 2 HOH 24  424 141 HOH HOH B . 
D 2 HOH 25  425 104 HOH HOH B . 
D 2 HOH 26  426 107 HOH HOH B . 
D 2 HOH 27  427 217 HOH HOH B . 
D 2 HOH 28  428 130 HOH HOH B . 
D 2 HOH 29  429 279 HOH HOH B . 
D 2 HOH 30  430 282 HOH HOH B . 
D 2 HOH 31  431 262 HOH HOH B . 
D 2 HOH 32  432 131 HOH HOH B . 
D 2 HOH 33  433 225 HOH HOH B . 
D 2 HOH 34  434 191 HOH HOH B . 
D 2 HOH 35  435 207 HOH HOH B . 
D 2 HOH 36  436 201 HOH HOH B . 
D 2 HOH 37  437 9   HOH HOH B . 
D 2 HOH 38  438 6   HOH HOH B . 
D 2 HOH 39  439 51  HOH HOH B . 
D 2 HOH 40  440 176 HOH HOH B . 
D 2 HOH 41  441 173 HOH HOH B . 
D 2 HOH 42  442 33  HOH HOH B . 
D 2 HOH 43  443 80  HOH HOH B . 
D 2 HOH 44  444 25  HOH HOH B . 
D 2 HOH 45  445 337 HOH HOH B . 
D 2 HOH 46  446 112 HOH HOH B . 
D 2 HOH 47  447 41  HOH HOH B . 
D 2 HOH 48  448 335 HOH HOH B . 
D 2 HOH 49  449 96  HOH HOH B . 
D 2 HOH 50  450 1   HOH HOH B . 
D 2 HOH 51  451 98  HOH HOH B . 
D 2 HOH 52  452 19  HOH HOH B . 
D 2 HOH 53  453 49  HOH HOH B . 
D 2 HOH 54  454 106 HOH HOH B . 
D 2 HOH 55  455 15  HOH HOH B . 
D 2 HOH 56  456 73  HOH HOH B . 
D 2 HOH 57  457 24  HOH HOH B . 
D 2 HOH 58  458 167 HOH HOH B . 
D 2 HOH 59  459 68  HOH HOH B . 
D 2 HOH 60  460 55  HOH HOH B . 
D 2 HOH 61  461 27  HOH HOH B . 
D 2 HOH 62  462 101 HOH HOH B . 
D 2 HOH 63  463 47  HOH HOH B . 
D 2 HOH 64  464 53  HOH HOH B . 
D 2 HOH 65  465 224 HOH HOH B . 
D 2 HOH 66  466 147 HOH HOH B . 
D 2 HOH 67  467 78  HOH HOH B . 
D 2 HOH 68  468 286 HOH HOH B . 
D 2 HOH 69  469 66  HOH HOH B . 
D 2 HOH 70  470 135 HOH HOH B . 
D 2 HOH 71  471 196 HOH HOH B . 
D 2 HOH 72  472 209 HOH HOH B . 
D 2 HOH 73  473 216 HOH HOH B . 
D 2 HOH 74  474 74  HOH HOH B . 
D 2 HOH 75  475 7   HOH HOH B . 
D 2 HOH 76  476 248 HOH HOH B . 
D 2 HOH 77  477 43  HOH HOH B . 
D 2 HOH 78  478 10  HOH HOH B . 
D 2 HOH 79  479 18  HOH HOH B . 
D 2 HOH 80  480 16  HOH HOH B . 
D 2 HOH 81  481 287 HOH HOH B . 
D 2 HOH 82  482 291 HOH HOH B . 
D 2 HOH 83  483 258 HOH HOH B . 
D 2 HOH 84  484 230 HOH HOH B . 
D 2 HOH 85  485 362 HOH HOH B . 
D 2 HOH 86  486 203 HOH HOH B . 
D 2 HOH 87  487 156 HOH HOH B . 
D 2 HOH 88  488 146 HOH HOH B . 
D 2 HOH 89  489 44  HOH HOH B . 
D 2 HOH 90  490 349 HOH HOH B . 
D 2 HOH 91  491 252 HOH HOH B . 
D 2 HOH 92  492 64  HOH HOH B . 
D 2 HOH 93  493 324 HOH HOH B . 
D 2 HOH 94  494 338 HOH HOH B . 
D 2 HOH 95  495 34  HOH HOH B . 
D 2 HOH 96  496 114 HOH HOH B . 
D 2 HOH 97  497 75  HOH HOH B . 
D 2 HOH 98  498 210 HOH HOH B . 
D 2 HOH 99  499 168 HOH HOH B . 
D 2 HOH 100 500 152 HOH HOH B . 
D 2 HOH 101 501 58  HOH HOH B . 
D 2 HOH 102 502 54  HOH HOH B . 
D 2 HOH 103 503 194 HOH HOH B . 
D 2 HOH 104 504 363 HOH HOH B . 
D 2 HOH 105 505 187 HOH HOH B . 
D 2 HOH 106 506 346 HOH HOH B . 
D 2 HOH 107 507 269 HOH HOH B . 
D 2 HOH 108 508 185 HOH HOH B . 
D 2 HOH 109 509 235 HOH HOH B . 
D 2 HOH 110 510 221 HOH HOH B . 
D 2 HOH 111 511 20  HOH HOH B . 
D 2 HOH 112 512 305 HOH HOH B . 
D 2 HOH 113 513 218 HOH HOH B . 
D 2 HOH 114 514 313 HOH HOH B . 
D 2 HOH 115 515 36  HOH HOH B . 
D 2 HOH 116 516 181 HOH HOH B . 
D 2 HOH 117 517 311 HOH HOH B . 
D 2 HOH 118 518 329 HOH HOH B . 
D 2 HOH 119 519 283 HOH HOH B . 
D 2 HOH 120 520 356 HOH HOH B . 
D 2 HOH 121 521 266 HOH HOH B . 
D 2 HOH 122 522 276 HOH HOH B . 
D 2 HOH 123 523 28  HOH HOH B . 
D 2 HOH 124 524 326 HOH HOH B . 
D 2 HOH 125 525 17  HOH HOH B . 
D 2 HOH 126 526 333 HOH HOH B . 
D 2 HOH 127 527 222 HOH HOH B . 
D 2 HOH 128 528 84  HOH HOH B . 
D 2 HOH 129 529 125 HOH HOH B . 
D 2 HOH 130 530 115 HOH HOH B . 
D 2 HOH 131 531 239 HOH HOH B . 
D 2 HOH 132 532 192 HOH HOH B . 
D 2 HOH 133 533 254 HOH HOH B . 
D 2 HOH 134 534 285 HOH HOH B . 
D 2 HOH 135 535 37  HOH HOH B . 
D 2 HOH 136 536 153 HOH HOH B . 
D 2 HOH 137 537 46  HOH HOH B . 
D 2 HOH 138 538 347 HOH HOH B . 
D 2 HOH 139 539 100 HOH HOH B . 
D 2 HOH 140 540 261 HOH HOH B . 
D 2 HOH 141 541 240 HOH HOH B . 
D 2 HOH 142 542 149 HOH HOH B . 
D 2 HOH 143 543 348 HOH HOH B . 
D 2 HOH 144 544 366 HOH HOH B . 
D 2 HOH 145 545 278 HOH HOH B . 
D 2 HOH 146 546 334 HOH HOH B . 
D 2 HOH 147 547 213 HOH HOH B . 
D 2 HOH 148 548 319 HOH HOH B . 
D 2 HOH 149 549 226 HOH HOH B . 
D 2 HOH 150 550 243 HOH HOH B . 
D 2 HOH 151 551 314 HOH HOH B . 
D 2 HOH 152 552 297 HOH HOH B . 
D 2 HOH 153 553 330 HOH HOH B . 
D 2 HOH 154 554 377 HOH HOH B . 
D 2 HOH 155 555 165 HOH HOH B . 
D 2 HOH 156 556 116 HOH HOH B . 
D 2 HOH 157 557 177 HOH HOH B . 
D 2 HOH 158 558 343 HOH HOH B . 
D 2 HOH 159 559 351 HOH HOH B . 
D 2 HOH 160 560 143 HOH HOH B . 
D 2 HOH 161 561 228 HOH HOH B . 
D 2 HOH 162 562 339 HOH HOH B . 
D 2 HOH 163 563 284 HOH HOH B . 
D 2 HOH 164 564 320 HOH HOH B . 
D 2 HOH 165 565 296 HOH HOH B . 
D 2 HOH 166 566 211 HOH HOH B . 
D 2 HOH 167 567 244 HOH HOH B . 
D 2 HOH 168 568 271 HOH HOH B . 
D 2 HOH 169 569 312 HOH HOH B . 
D 2 HOH 170 570 332 HOH HOH B . 
D 2 HOH 171 571 372 HOH HOH B . 
D 2 HOH 172 572 378 HOH HOH B . 
D 2 HOH 173 573 231 HOH HOH B . 
D 2 HOH 174 574 361 HOH HOH B . 
D 2 HOH 175 575 364 HOH HOH B . 
D 2 HOH 176 576 306 HOH HOH B . 
D 2 HOH 177 577 204 HOH HOH B . 
# 
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   ? ? ? v1.16 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .     2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .     3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .     4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   125.27 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y54 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     112.470 
_cell.length_a_esd                 ? 
_cell.length_b                     91.060 
_cell.length_b_esd                 ? 
_cell.length_c                     80.870 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Y54 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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                   8Y54 
_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             1.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.89 
_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, HANGING 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    'Magnesium formate dihydrate, Polyethylene glycol 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             'oxford cryosystems 700' 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-30 
_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   0.978610 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978610 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Y54 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               38.95 
_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                                     63450 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.079 
_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                                    1.78 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4699 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.170 
_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                                 8Y54 
_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                            1.78 
_refine.ls_d_res_low                             38.95 
_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                     63450 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2319 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2075 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        38.95 
_refine_hist.number_atoms_solvent             342 
_refine_hist.number_atoms_total               6490 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        6148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.R_factor_R_free                  0.2319 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2057 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.d_res_high                       1.78 
_refine_ls_shell.d_res_low                        1.84 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                6129 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.percent_reflns_obs               99.5 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
# 
_struct.entry_id                     8Y54 
_struct.title                        
'Three-dimensional structure of homo-dimer of cystathione beta lyase from lactobacillus delbrueckii(LdPatB)' 
_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        8Y54 
_struct_keywords.text            'C-S cleavage reaction, L-cysteine-S-conjugate, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
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 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0AAC9VP02_LACDL 
_struct_ref.pdbx_db_accession          A0AAC9VP02 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAEKQYDFTHVPKRQGNSIKWGGLKEKELPMWIAEMDFRIAPEIMTSMEEKLKVAAFGYESVPAEYYKAVADWEEIEHRA
RPKEDWCVFASGVVPAISAMVRQFTSPGDQILVQEPVYNMFYSVIEGNGRRVISSDLIYENSKYSVNWADLEEKLATPSV
RMMVFCNPHNPIGYAWSEEEVKRIAELCAKHQVLLISDEIHGDLVLTDEDITPAFTVDWDAKNWVVSLISPSKTFNLAAL
HAACAIIPNPDLRARAEESFFLAGIGEPNLLAIPAAIAAYEEGHNWLRELKQVLRDNFAYAREFLAKEVPVVKVLDSNAS
YLAWVNISALGMNAEDFCKYLREKTGLIISAGNGYRGNGHEFVRINLACPKELVIDGMQRLKQGVLNLNN
;
_struct_ref.pdbx_align_begin           1 
# 
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 8Y54 A 1 ? 390 ? A0AAC9VP02 1 ? 390 ? 1 390 
2 1 8Y54 B 1 ? 390 ? A0AAC9VP02 1 ? 390 ? 1 390 
# 
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 8Y54 GLU A 311 ? UNP A0AAC9VP02 VAL 311 'engineered mutation' 311 1 
1 8Y54 ASP A 326 ? UNP A0AAC9VP02 ASN 326 'engineered mutation' 326 2 
2 8Y54 GLU B 311 ? UNP A0AAC9VP02 VAL 311 'engineered mutation' 311 3 
2 8Y54 ASP B 326 ? UNP A0AAC9VP02 ASN 326 'engineered mutation' 326 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4490  ? 
1 MORE         -31   ? 
1 'SSA (A^2)'  27930 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ALA A 41  ? LYS A 53  ? ALA A 41  LYS A 53  1 ? 13 
HELX_P HELX_P2  AA2 PRO A 63  ? ARG A 79  ? PRO A 63  ARG A 79  1 ? 17 
HELX_P HELX_P3  AA3 LYS A 83  ? ASP A 85  ? LYS A 83  ASP A 85  5 ? 3  
HELX_P HELX_P4  AA4 GLY A 92  ? THR A 105 ? GLY A 92  THR A 105 1 ? 14 
HELX_P HELX_P5  AA5 TYR A 118 ? ASN A 128 ? TYR A 118 ASN A 128 1 ? 11 
HELX_P HELX_P6  AA6 ASN A 147 ? ALA A 156 ? ASN A 147 ALA A 156 1 ? 10 
HELX_P HELX_P7  AA7 SER A 177 ? HIS A 191 ? SER A 177 HIS A 191 1 ? 15 
HELX_P HELX_P8  AA8 HIS A 201 ? VAL A 205 ? HIS A 201 VAL A 205 5 ? 5  
HELX_P HELX_P9  AA9 PRO A 213 ? VAL A 217 ? PRO A 213 VAL A 217 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 220 ? ASN A 223 ? ASP A 220 ASN A 223 5 ? 4  
HELX_P HELX_P11 AB2 SER A 230 ? ASN A 236 ? SER A 230 ASN A 236 1 ? 7  
HELX_P HELX_P12 AB3 ASN A 249 ? GLY A 264 ? ASN A 249 GLY A 264 1 ? 16 
HELX_P HELX_P13 AB4 LEU A 271 ? GLY A 283 ? LEU A 271 GLY A 283 1 ? 13 
HELX_P HELX_P14 AB5 GLY A 283 ? VAL A 309 ? GLY A 283 VAL A 309 1 ? 27 
HELX_P HELX_P15 AB6 SER A 328 ? GLY A 331 ? SER A 328 GLY A 331 5 ? 4  
HELX_P HELX_P16 AB7 ASN A 333 ? GLY A 346 ? ASN A 333 GLY A 346 1 ? 14 
HELX_P HELX_P17 AB8 ASN A 353 ? ARG A 356 ? ASN A 353 ARG A 356 5 ? 4  
HELX_P HELX_P18 AB9 ASN A 358 ? HIS A 360 ? ASN A 358 HIS A 360 5 ? 3  
HELX_P HELX_P19 AC1 PRO A 370 ? ASN A 389 ? PRO A 370 ASN A 389 1 ? 20 
HELX_P HELX_P20 AC2 ALA B 41  ? LYS B 53  ? ALA B 41  LYS B 53  1 ? 13 
HELX_P HELX_P21 AC3 PRO B 63  ? ARG B 79  ? PRO B 63  ARG B 79  1 ? 17 
HELX_P HELX_P22 AC4 LYS B 83  ? ASP B 85  ? LYS B 83  ASP B 85  5 ? 3  
HELX_P HELX_P23 AC5 GLY B 92  ? THR B 105 ? GLY B 92  THR B 105 1 ? 14 
HELX_P HELX_P24 AC6 TYR B 118 ? ASN B 128 ? TYR B 118 ASN B 128 1 ? 11 
HELX_P HELX_P25 AC7 ASN B 147 ? ALA B 156 ? ASN B 147 ALA B 156 1 ? 10 
HELX_P HELX_P26 AC8 SER B 177 ? HIS B 191 ? SER B 177 HIS B 191 1 ? 15 
HELX_P HELX_P27 AC9 HIS B 201 ? VAL B 205 ? HIS B 201 VAL B 205 5 ? 5  
HELX_P HELX_P28 AD1 PRO B 213 ? VAL B 217 ? PRO B 213 VAL B 217 5 ? 5  
HELX_P HELX_P29 AD2 ASP B 218 ? TRP B 219 ? ASP B 218 TRP B 219 5 ? 2  
HELX_P HELX_P30 AD3 ALA B 221 ? ASN B 223 ? ALA B 221 ASN B 223 5 ? 3  
HELX_P HELX_P31 AD4 PRO B 231 ? ASN B 236 ? PRO B 231 ASN B 236 1 ? 6  
HELX_P HELX_P32 AD5 LEU B 237 ? HIS B 241 ? LEU B 237 HIS B 241 5 ? 5  
HELX_P HELX_P33 AD6 ASN B 249 ? GLY B 264 ? ASN B 249 GLY B 264 1 ? 16 
HELX_P HELX_P34 AD7 LEU B 271 ? GLY B 283 ? LEU B 271 GLY B 283 1 ? 13 
HELX_P HELX_P35 AD8 GLY B 283 ? VAL B 309 ? GLY B 283 VAL B 309 1 ? 27 
HELX_P HELX_P36 AD9 SER B 328 ? GLY B 331 ? SER B 328 GLY B 331 5 ? 4  
HELX_P HELX_P37 AE1 ASN B 333 ? GLY B 346 ? ASN B 333 GLY B 346 1 ? 14 
HELX_P HELX_P38 AE2 ASN B 353 ? ARG B 356 ? ASN B 353 ARG B 356 5 ? 4  
HELX_P HELX_P39 AE3 ASN B 358 ? HIS B 360 ? ASN B 358 HIS B 360 5 ? 3  
HELX_P HELX_P40 AE4 PRO B 370 ? ASN B 389 ? PRO B 370 ASN B 389 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 115 A . ? GLU 115 A PRO 116 A ? PRO 116 A 1 -2.00 
2 ASN 167 A . ? ASN 167 A PRO 168 A ? PRO 168 A 1 2.22  
3 ASN 170 A . ? ASN 170 A PRO 171 A ? PRO 171 A 1 17.14 
4 GLU 115 B . ? GLU 115 B PRO 116 B ? PRO 116 B 1 -8.26 
5 ASN 167 B . ? ASN 167 B PRO 168 B ? PRO 168 B 1 1.55  
6 ASN 170 B . ? ASN 170 B PRO 171 B ? PRO 171 B 1 15.21 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 7 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
AA5 ? 7 ? 
AA6 ? 2 ? 
AA7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 29  ? PRO A 30  ? LEU A 29  PRO A 30  
AA1 2 LEU A 347 ? ILE A 348 ? LEU A 347 ILE A 348 
AA2 1 CYS A 87  ? ALA A 90  ? CYS A 87  ALA A 90  
AA2 2 ALA A 243 ? ILE A 246 ? ALA A 243 ILE A 246 
AA2 3 VAL A 225 ? ILE A 229 ? VAL A 225 ILE A 229 
AA2 4 LEU A 194 ? ASP A 198 ? LEU A 194 ASP A 198 
AA2 5 VAL A 160 ? CYS A 166 ? VAL A 160 CYS A 166 
AA2 6 GLN A 110 ? VAL A 113 ? GLN A 110 VAL A 113 
AA2 7 ARG A 131 ? SER A 134 ? ARG A 131 SER A 134 
AA3 1 LYS A 313 ? VAL A 314 ? LYS A 313 VAL A 314 
AA3 2 LEU A 322 ? ASP A 326 ? LEU A 322 ASP A 326 
AA3 3 PHE A 362 ? ASN A 366 ? PHE A 362 ASN A 366 
AA3 4 SER A 350 ? ALA A 351 ? SER A 350 ALA A 351 
AA4 1 LEU B 29  ? PRO B 30  ? LEU B 29  PRO B 30  
AA4 2 LEU B 347 ? ILE B 348 ? LEU B 347 ILE B 348 
AA5 1 CYS B 87  ? ALA B 90  ? CYS B 87  ALA B 90  
AA5 2 ALA B 243 ? ILE B 246 ? ALA B 243 ILE B 246 
AA5 3 VAL B 225 ? ILE B 229 ? VAL B 225 ILE B 229 
AA5 4 LEU B 194 ? ASP B 198 ? LEU B 194 ASP B 198 
AA5 5 VAL B 160 ? CYS B 166 ? VAL B 160 CYS B 166 
AA5 6 GLN B 110 ? VAL B 113 ? GLN B 110 VAL B 113 
AA5 7 ARG B 131 ? SER B 134 ? ARG B 131 SER B 134 
AA6 1 ILE B 138 ? GLU B 140 ? ILE B 138 GLU B 140 
AA6 2 LYS B 143 ? SER B 145 ? LYS B 143 SER B 145 
AA7 1 LYS B 313 ? VAL B 314 ? LYS B 313 VAL B 314 
AA7 2 LEU B 322 ? ASP B 326 ? LEU B 322 ASP B 326 
AA7 3 PHE B 362 ? ASN B 366 ? PHE B 362 ASN B 366 
AA7 4 SER B 350 ? ALA B 351 ? SER B 350 ALA B 351 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 29  ? N LEU A 29  O ILE A 348 ? O ILE A 348 
AA2 1 2 N VAL A 88  ? N VAL A 88  O ALA A 245 ? O ALA A 245 
AA2 2 3 O ILE A 246 ? O ILE A 246 N SER A 227 ? N SER A 227 
AA2 3 4 O VAL A 226 ? O VAL A 226 N SER A 197 ? N SER A 197 
AA2 4 5 O ASP A 198 ? O ASP A 198 N PHE A 165 ? N PHE A 165 
AA2 5 6 O MET A 162 ? O MET A 162 N LEU A 112 ? N LEU A 112 
AA2 6 7 N ILE A 111 ? N ILE A 111 O ARG A 131 ? O ARG A 131 
AA3 1 2 N LYS A 313 ? N LYS A 313 O ASP A 326 ? O ASP A 326 
AA3 2 3 N ALA A 323 ? N ALA A 323 O ILE A 365 ? O ILE A 365 
AA3 3 4 O ARG A 364 ? O ARG A 364 N SER A 350 ? N SER A 350 
AA4 1 2 N LEU B 29  ? N LEU B 29  O ILE B 348 ? O ILE B 348 
AA5 1 2 N VAL B 88  ? N VAL B 88  O ALA B 245 ? O ALA B 245 
AA5 2 3 O ILE B 246 ? O ILE B 246 N SER B 227 ? N SER B 227 
AA5 3 4 O VAL B 226 ? O VAL B 226 N SER B 197 ? N SER B 197 
AA5 4 5 O ILE B 196 ? O ILE B 196 N MET B 163 ? N MET B 163 
AA5 5 6 O MET B 162 ? O MET B 162 N LEU B 112 ? N LEU B 112 
AA5 6 7 N ILE B 111 ? N ILE B 111 O ARG B 131 ? O ARG B 131 
AA6 1 2 N ILE B 138 ? N ILE B 138 O SER B 145 ? O SER B 145 
AA7 1 2 N LYS B 313 ? N LYS B 313 O ASP B 326 ? O ASP B 326 
AA7 2 3 N VAL B 325 ? N VAL B 325 O VAL B 363 ? O VAL B 363 
AA7 3 4 O ARG B 364 ? O ARG B 364 N SER B 350 ? N SER B 350 
# 
_pdbx_entry_details.entry_id                   8Y54 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 17  ? ? -94.23  38.35   
2  1 TRP A 32  ? ? -116.19 -71.39  
3  1 ASP A 37  ? ? -106.62 44.76   
4  1 TYR A 118 ? ? -37.81  127.26  
5  1 ASN A 141 ? ? -103.56 -123.95 
6  1 SER A 142 ? ? -108.91 44.86   
7  1 TRP A 219 ? ? -57.46  171.12  
8  1 ASP A 220 ? ? 76.64   -67.94  
9  1 SER A 320 ? ? 84.06   166.87  
10 1 ARG A 356 ? ? 57.48   -144.95 
11 1 TRP B 32  ? ? -109.05 -74.08  
12 1 ASP B 37  ? ? -109.05 41.52   
13 1 TYR B 118 ? ? -31.40  127.04  
14 1 SER B 142 ? ? 59.92   12.22   
15 1 SER B 320 ? ? 79.94   162.25  
16 1 ARG B 356 ? ? 57.83   -146.55 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 557 ? C HOH . 
2 1 A HOH 564 ? C HOH . 
3 1 B HOH 482 ? D HOH . 
4 1 B HOH 577 ? D HOH . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       565 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.20 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A ALA 2   ? A ALA 2   
3 1 Y 1 A GLU 3   ? A GLU 3   
4 1 Y 1 B MET 1   ? B MET 1   
5 1 Y 1 B ALA 2   ? B ALA 2   
6 1 Y 1 B LYS 25  ? B LYS 25  
7 1 Y 1 B ASP 220 ? B ASP 220 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           'Project no. 42077214' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      SwissModel 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Y54 
_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]   0.008891 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006288 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010982 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.015146 
_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 
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   . LYS A 1 4   ? 45.441  14.683  25.432  1.00 69.57 ?  4   LYS A N   1 
ATOM   2    C CA  . LYS A 1 4   ? 43.976  14.769  25.575  1.00 64.56 ?  4   LYS A CA  1 
ATOM   3    C C   . LYS A 1 4   ? 43.414  14.461  26.948  1.00 59.82 ?  4   LYS A C   1 
ATOM   4    O O   . LYS A 1 4   ? 44.165  14.128  27.874  1.00 64.81 ?  4   LYS A O   1 
ATOM   5    C CB  . LYS A 1 4   ? 43.233  13.997  24.474  1.00 63.15 ?  4   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 4   ? 43.380  14.566  23.070  1.00 63.33 ?  4   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 4   ? 42.654  13.768  22.004  1.00 58.06 ?  4   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 4   ? 42.797  14.368  20.623  1.00 59.63 ?  4   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 4   ? 42.102  13.565  19.587  1.00 60.76 1  4   LYS A NZ  1 
ATOM   10   N N   . GLN A 1 5   ? 42.108  14.525  27.003  1.00 53.33 ?  5   GLN A N   1 
ATOM   11   C CA  . GLN A 1 5   ? 41.308  14.269  28.207  1.00 50.56 ?  5   GLN A CA  1 
ATOM   12   C C   . GLN A 1 5   ? 40.556  12.972  27.848  1.00 45.08 ?  5   GLN A C   1 
ATOM   13   O O   . GLN A 1 5   ? 39.986  12.371  28.761  1.00 42.98 ?  5   GLN A O   1 
ATOM   14   C CB  . GLN A 1 5   ? 40.428  15.493  28.419  1.00 46.45 ?  5   GLN A CB  1 
ATOM   15   C CG  . GLN A 1 5   ? 39.689  15.504  29.744  1.00 49.63 ?  5   GLN A CG  1 
ATOM   16   C CD  . GLN A 1 5   ? 38.561  16.503  29.721  1.00 49.62 ?  5   GLN A CD  1 
ATOM   17   O OE1 . GLN A 1 5   ? 38.759  17.683  29.442  1.00 52.68 ?  5   GLN A OE1 1 
ATOM   18   N NE2 . GLN A 1 5   ? 37.364  16.031  30.015  1.00 51.36 ?  5   GLN A NE2 1 
ATOM   19   N N   . TYR A 1 6   ? 40.667  12.515  26.581  1.00 43.15 ?  6   TYR A N   1 
ATOM   20   C CA  . TYR A 1 6   ? 39.885  11.378  26.113  1.00 38.16 ?  6   TYR A CA  1 
ATOM   21   C C   . TYR A 1 6   ? 40.733  10.442  25.255  1.00 39.29 ?  6   TYR A C   1 
ATOM   22   O O   . TYR A 1 6   ? 41.650  10.876  24.551  1.00 39.09 ?  6   TYR A O   1 
ATOM   23   C CB  . TYR A 1 6   ? 38.682  11.847  25.294  1.00 32.57 ?  6   TYR A CB  1 
ATOM   24   C CG  . TYR A 1 6   ? 37.770  12.822  25.998  1.00 28.71 ?  6   TYR A CG  1 
ATOM   25   C CD1 . TYR A 1 6   ? 36.930  12.400  27.014  1.00 31.27 ?  6   TYR A CD1 1 
ATOM   26   C CD2 . TYR A 1 6   ? 37.705  14.145  25.607  1.00 28.76 ?  6   TYR A CD2 1 
ATOM   27   C CE1 . TYR A 1 6   ? 36.073  13.273  27.637  1.00 28.27 ?  6   TYR A CE1 1 
ATOM   28   C CE2 . TYR A 1 6   ? 36.849  15.036  26.234  1.00 28.58 ?  6   TYR A CE2 1 
ATOM   29   C CZ  . TYR A 1 6   ? 36.028  14.581  27.243  1.00 30.09 ?  6   TYR A CZ  1 
ATOM   30   O OH  . TYR A 1 6   ? 35.162  15.424  27.895  1.00 33.59 ?  6   TYR A OH  1 
ATOM   31   N N   . ASP A 1 7   ? 40.384  9.156   25.286  1.00 36.55 ?  7   ASP A N   1 
ATOM   32   C CA  . ASP A 1 7   ? 41.116  8.115   24.563  1.00 37.34 ?  7   ASP A CA  1 
ATOM   33   C C   . ASP A 1 7   ? 40.742  8.130   23.089  1.00 33.83 ?  7   ASP A C   1 
ATOM   34   O O   . ASP A 1 7   ? 39.617  7.766   22.726  1.00 32.83 ?  7   ASP A O   1 
ATOM   35   C CB  . ASP A 1 7   ? 40.814  6.740   25.150  1.00 36.10 ?  7   ASP A CB  1 
ATOM   36   C CG  . ASP A 1 7   ? 41.731  5.651   24.608  1.00 39.19 ?  7   ASP A CG  1 
ATOM   37   O OD1 . ASP A 1 7   ? 42.259  5.793   23.486  1.00 36.41 ?  7   ASP A OD1 1 
ATOM   38   O OD2 . ASP A 1 7   ? 41.946  4.647   25.321  1.00 46.93 -1 7   ASP A OD2 1 
ATOM   39   N N   . PHE A 1 8   ? 41.699  8.485   22.229  1.00 27.68 ?  8   PHE A N   1 
ATOM   40   C CA  . PHE A 1 8   ? 41.549  8.299   20.788  1.00 28.75 ?  8   PHE A CA  1 
ATOM   41   C C   . PHE A 1 8   ? 42.661  7.419   20.218  1.00 32.13 ?  8   PHE A C   1 
ATOM   42   O O   . PHE A 1 8   ? 43.051  7.560   19.054  1.00 31.98 ?  8   PHE A O   1 
ATOM   43   C CB  . PHE A 1 8   ? 41.494  9.644   20.076  1.00 30.56 ?  8   PHE A CB  1 
ATOM   44   C CG  . PHE A 1 8   ? 40.260  10.440  20.405  1.00 34.06 ?  8   PHE A CG  1 
ATOM   45   C CD1 . PHE A 1 8   ? 39.073  10.207  19.726  1.00 27.34 ?  8   PHE A CD1 1 
ATOM   46   C CD2 . PHE A 1 8   ? 40.281  11.400  21.413  1.00 32.61 ?  8   PHE A CD2 1 
ATOM   47   C CE1 . PHE A 1 8   ? 37.938  10.931  20.019  1.00 30.65 ?  8   PHE A CE1 1 
ATOM   48   C CE2 . PHE A 1 8   ? 39.145  12.124  21.720  1.00 28.73 ?  8   PHE A CE2 1 
ATOM   49   C CZ  . PHE A 1 8   ? 37.972  11.896  21.021  1.00 29.80 ?  8   PHE A CZ  1 
ATOM   50   N N   . THR A 1 9   ? 43.144  6.472   21.019  1.00 33.80 ?  9   THR A N   1 
ATOM   51   C CA  . THR A 1 9   ? 44.317  5.673   20.673  1.00 34.27 ?  9   THR A CA  1 
ATOM   52   C C   . THR A 1 9   ? 43.998  4.186   20.631  1.00 35.11 ?  9   THR A C   1 
ATOM   53   O O   . THR A 1 9   ? 44.526  3.453   19.789  1.00 35.41 ?  9   THR A O   1 
ATOM   54   C CB  . THR A 1 9   ? 45.444  5.941   21.677  1.00 31.38 ?  9   THR A CB  1 
ATOM   55   O OG1 . THR A 1 9   ? 45.863  7.305   21.571  1.00 36.95 ?  9   THR A OG1 1 
ATOM   56   C CG2 . THR A 1 9   ? 46.640  5.027   21.430  1.00 40.45 ?  9   THR A CG2 1 
ATOM   57   N N   . HIS A 1 10  ? 43.149  3.730   21.539  1.00 34.75 ?  10  HIS A N   1 
ATOM   58   C CA  . HIS A 1 10  ? 42.907  2.309   21.720  1.00 33.37 ?  10  HIS A CA  1 
ATOM   59   C C   . HIS A 1 10  ? 41.571  1.915   21.105  1.00 31.57 ?  10  HIS A C   1 
ATOM   60   O O   . HIS A 1 10  ? 40.544  2.544   21.372  1.00 32.71 ?  10  HIS A O   1 
ATOM   61   C CB  . HIS A 1 10  ? 42.968  1.963   23.206  1.00 35.55 ?  10  HIS A CB  1 
ATOM   62   C CG  . HIS A 1 10  ? 44.299  2.269   23.815  1.00 34.90 ?  10  HIS A CG  1 
ATOM   63   N ND1 . HIS A 1 10  ? 44.545  3.419   24.534  1.00 37.67 ?  10  HIS A ND1 1 
ATOM   64   C CD2 . HIS A 1 10  ? 45.469  1.589   23.780  1.00 34.68 ?  10  HIS A CD2 1 
ATOM   65   C CE1 . HIS A 1 10  ? 45.805  3.427   24.931  1.00 33.67 ?  10  HIS A CE1 1 
ATOM   66   N NE2 . HIS A 1 10  ? 46.387  2.327   24.488  1.00 37.59 ?  10  HIS A NE2 1 
ATOM   67   N N   . VAL A 1 11  ? 41.601  0.896   20.262  1.00 30.46 ?  11  VAL A N   1 
ATOM   68   C CA  . VAL A 1 11  ? 40.390  0.444   19.576  1.00 32.06 ?  11  VAL A CA  1 
ATOM   69   C C   . VAL A 1 11  ? 39.573  -0.407  20.544  1.00 32.49 ?  11  VAL A C   1 
ATOM   70   O O   . VAL A 1 11  ? 40.125  -1.331  21.159  1.00 32.74 ?  11  VAL A O   1 
ATOM   71   C CB  . VAL A 1 11  ? 40.752  -0.342  18.319  1.00 34.65 ?  11  VAL A CB  1 
ATOM   72   C CG1 . VAL A 1 11  ? 39.504  -0.931  17.656  1.00 29.90 ?  11  VAL A CG1 1 
ATOM   73   C CG2 . VAL A 1 11  ? 41.510  0.554   17.353  1.00 32.90 ?  11  VAL A CG2 1 
ATOM   74   N N   . PRO A 1 12  ? 38.287  -0.123  20.719  1.00 31.26 ?  12  PRO A N   1 
ATOM   75   C CA  . PRO A 1 12  ? 37.465  -0.944  21.618  1.00 32.01 ?  12  PRO A CA  1 
ATOM   76   C C   . PRO A 1 12  ? 37.438  -2.394  21.176  1.00 32.98 ?  12  PRO A C   1 
ATOM   77   O O   . PRO A 1 12  ? 37.427  -2.697  19.981  1.00 30.82 ?  12  PRO A O   1 
ATOM   78   C CB  . PRO A 1 12  ? 36.077  -0.302  21.514  1.00 31.89 ?  12  PRO A CB  1 
ATOM   79   C CG  . PRO A 1 12  ? 36.364  1.117   21.060  1.00 30.82 ?  12  PRO A CG  1 
ATOM   80   C CD  . PRO A 1 12  ? 37.539  1.010   20.151  1.00 30.78 ?  12  PRO A CD  1 
ATOM   81   N N   . LYS A 1 13  ? 37.415  -3.297  22.154  1.00 29.25 ?  13  LYS A N   1 
ATOM   82   C CA  . LYS A 1 13  ? 37.339  -4.725  21.873  1.00 30.91 ?  13  LYS A CA  1 
ATOM   83   C C   . LYS A 1 13  ? 35.867  -5.123  21.841  1.00 30.12 ?  13  LYS A C   1 
ATOM   84   O O   . LYS A 1 13  ? 35.199  -5.138  22.879  1.00 27.90 ?  13  LYS A O   1 
ATOM   85   C CB  . LYS A 1 13  ? 38.123  -5.518  22.911  1.00 34.55 ?  13  LYS A CB  1 
ATOM   86   C CG  . LYS A 1 13  ? 39.547  -5.023  23.082  1.00 41.23 ?  13  LYS A CG  1 
ATOM   87   C CD  . LYS A 1 13  ? 39.829  -4.572  24.508  1.00 42.66 ?  13  LYS A CD  1 
ATOM   88   C CE  . LYS A 1 13  ? 41.286  -4.184  24.679  1.00 44.66 ?  13  LYS A CE  1 
ATOM   89   N NZ  . LYS A 1 13  ? 41.700  -4.270  26.105  1.00 45.00 1  13  LYS A NZ  1 
ATOM   90   N N   . ARG A 1 14  ? 35.358  -5.411  20.642  1.00 29.29 ?  14  ARG A N   1 
ATOM   91   C CA  . ARG A 1 14  ? 33.949  -5.726  20.473  1.00 30.43 ?  14  ARG A CA  1 
ATOM   92   C C   . ARG A 1 14  ? 33.677  -7.182  20.826  1.00 28.54 ?  14  ARG A C   1 
ATOM   93   O O   . ARG A 1 14  ? 34.581  -8.023  20.887  1.00 25.36 ?  14  ARG A O   1 
ATOM   94   C CB  . ARG A 1 14  ? 33.479  -5.482  19.035  1.00 29.51 ?  14  ARG A CB  1 
ATOM   95   C CG  . ARG A 1 14  ? 34.119  -4.325  18.299  1.00 35.38 ?  14  ARG A CG  1 
ATOM   96   C CD  . ARG A 1 14  ? 33.810  -2.995  18.938  1.00 34.65 ?  14  ARG A CD  1 
ATOM   97   N NE  . ARG A 1 14  ? 33.467  -1.984  17.932  1.00 37.38 ?  14  ARG A NE  1 
ATOM   98   C CZ  . ARG A 1 14  ? 34.351  -1.208  17.308  1.00 34.61 ?  14  ARG A CZ  1 
ATOM   99   N NH1 . ARG A 1 14  ? 35.650  -1.315  17.584  1.00 33.52 1  14  ARG A NH1 1 
ATOM   100  N NH2 . ARG A 1 14  ? 33.923  -0.314  16.421  1.00 30.13 ?  14  ARG A NH2 1 
ATOM   101  N N   . GLN A 1 15  ? 32.404  -7.473  21.051  1.00 27.10 ?  15  GLN A N   1 
ATOM   102  C CA  . GLN A 1 15  ? 31.961  -8.850  21.114  1.00 24.36 ?  15  GLN A CA  1 
ATOM   103  C C   . GLN A 1 15  ? 31.872  -9.393  19.688  1.00 30.20 ?  15  GLN A C   1 
ATOM   104  O O   . GLN A 1 15  ? 32.105  -8.676  18.706  1.00 27.50 ?  15  GLN A O   1 
ATOM   105  C CB  . GLN A 1 15  ? 30.642  -8.938  21.880  1.00 26.08 ?  15  GLN A CB  1 
ATOM   106  C CG  . GLN A 1 15  ? 30.783  -8.489  23.343  1.00 29.75 ?  15  GLN A CG  1 
ATOM   107  C CD  . GLN A 1 15  ? 29.625  -8.926  24.210  1.00 26.81 ?  15  GLN A CD  1 
ATOM   108  O OE1 . GLN A 1 15  ? 28.597  -9.379  23.697  1.00 26.66 ?  15  GLN A OE1 1 
ATOM   109  N NE2 . GLN A 1 15  ? 29.782  -8.804  25.536  1.00 25.43 ?  15  GLN A NE2 1 
ATOM   110  N N   . GLY A 1 16  ? 31.533  -10.678 19.566  1.00 28.62 ?  16  GLY A N   1 
ATOM   111  C CA  . GLY A 1 16  ? 31.737  -11.371 18.305  1.00 27.54 ?  16  GLY A CA  1 
ATOM   112  C C   . GLY A 1 16  ? 30.796  -10.945 17.201  1.00 33.74 ?  16  GLY A C   1 
ATOM   113  O O   . GLY A 1 16  ? 31.115  -11.115 16.015  1.00 29.11 ?  16  GLY A O   1 
ATOM   114  N N   . ASN A 1 17  ? 29.638  -10.384 17.560  1.00 26.96 ?  17  ASN A N   1 
ATOM   115  C CA  . ASN A 1 17  ? 28.588  -10.074 16.586  1.00 28.62 ?  17  ASN A CA  1 
ATOM   116  C C   . ASN A 1 17  ? 28.663  -8.643  16.078  1.00 32.04 ?  17  ASN A C   1 
ATOM   117  O O   . ASN A 1 17  ? 27.633  -7.994  15.867  1.00 29.19 ?  17  ASN A O   1 
ATOM   118  C CB  . ASN A 1 17  ? 27.215  -10.364 17.186  1.00 25.65 ?  17  ASN A CB  1 
ATOM   119  C CG  . ASN A 1 17  ? 26.826  -9.379  18.276  1.00 30.47 ?  17  ASN A CG  1 
ATOM   120  O OD1 . ASN A 1 17  ? 27.620  -9.080  19.175  1.00 28.54 ?  17  ASN A OD1 1 
ATOM   121  N ND2 . ASN A 1 17  ? 25.598  -8.849  18.187  1.00 25.21 ?  17  ASN A ND2 1 
ATOM   122  N N   . SER A 1 18  ? 29.871  -8.130  15.867  1.00 30.36 ?  18  SER A N   1 
ATOM   123  C CA  . SER A 1 18  ? 30.049  -6.803  15.292  1.00 32.07 ?  18  SER A CA  1 
ATOM   124  C C   . SER A 1 18  ? 30.018  -6.875  13.766  1.00 31.06 ?  18  SER A C   1 
ATOM   125  O O   . SER A 1 18  ? 30.609  -7.775  13.166  1.00 33.68 ?  18  SER A O   1 
ATOM   126  C CB  . SER A 1 18  ? 31.374  -6.204  15.771  1.00 30.67 ?  18  SER A CB  1 
ATOM   127  O OG  . SER A 1 18  ? 31.785  -5.150  14.923  1.00 29.19 ?  18  SER A OG  1 
ATOM   128  N N   . ILE A 1 19  ? 29.307  -5.932  13.139  1.00 31.20 ?  19  ILE A N   1 
ATOM   129  C CA  . ILE A 1 19  ? 29.306  -5.856  11.677  1.00 29.77 ?  19  ILE A CA  1 
ATOM   130  C C   . ILE A 1 19  ? 30.670  -5.402  11.163  1.00 32.98 ?  19  ILE A C   1 
ATOM   131  O O   . ILE A 1 19  ? 31.194  -5.942  10.181  1.00 29.85 ?  19  ILE A O   1 
ATOM   132  C CB  . ILE A 1 19  ? 28.185  -4.923  11.181  1.00 32.35 ?  19  ILE A CB  1 
ATOM   133  C CG1 . ILE A 1 19  ? 26.806  -5.459  11.590  1.00 29.46 ?  19  ILE A CG1 1 
ATOM   134  C CG2 . ILE A 1 19  ? 28.265  -4.741  9.665   1.00 33.49 ?  19  ILE A CG2 1 
ATOM   135  C CD1 . ILE A 1 19  ? 26.201  -6.404  10.605  1.00 36.18 ?  19  ILE A CD1 1 
ATOM   136  N N   . LYS A 1 20  ? 31.265  -4.402  11.805  1.00 31.27 ?  20  LYS A N   1 
ATOM   137  C CA  . LYS A 1 20  ? 32.533  -3.885  11.304  1.00 31.17 ?  20  LYS A CA  1 
ATOM   138  C C   . LYS A 1 20  ? 33.655  -4.900  11.497  1.00 31.77 ?  20  LYS A C   1 
ATOM   139  O O   . LYS A 1 20  ? 34.420  -5.172  10.565  1.00 36.68 ?  20  LYS A O   1 
ATOM   140  C CB  . LYS A 1 20  ? 32.877  -2.553  11.985  1.00 28.04 ?  20  LYS A CB  1 
ATOM   141  C CG  . LYS A 1 20  ? 34.109  -1.882  11.397  1.00 31.04 ?  20  LYS A CG  1 
ATOM   142  C CD  . LYS A 1 20  ? 34.449  -0.554  12.089  1.00 33.58 ?  20  LYS A CD  1 
ATOM   143  C CE  . LYS A 1 20  ? 35.196  0.364   11.116  1.00 31.12 ?  20  LYS A CE  1 
ATOM   144  N NZ  . LYS A 1 20  ? 35.612  1.669   11.696  1.00 28.46 1  20  LYS A NZ  1 
ATOM   145  N N   . TRP A 1 21  ? 33.755  -5.492  12.688  1.00 33.64 ?  21  TRP A N   1 
ATOM   146  C CA  . TRP A 1 21  ? 34.904  -6.310  13.053  1.00 35.10 ?  21  TRP A CA  1 
ATOM   147  C C   . TRP A 1 21  ? 34.598  -7.799  13.152  1.00 39.54 ?  21  TRP A C   1 
ATOM   148  O O   . TRP A 1 21  ? 35.506  -8.587  13.438  1.00 35.40 ?  21  TRP A O   1 
ATOM   149  C CB  . TRP A 1 21  ? 35.485  -5.824  14.383  1.00 34.49 ?  21  TRP A CB  1 
ATOM   150  C CG  . TRP A 1 21  ? 36.212  -4.533  14.260  1.00 33.77 ?  21  TRP A CG  1 
ATOM   151  C CD1 . TRP A 1 21  ? 35.693  -3.281  14.417  1.00 32.11 ?  21  TRP A CD1 1 
ATOM   152  C CD2 . TRP A 1 21  ? 37.597  -4.359  13.930  1.00 35.42 ?  21  TRP A CD2 1 
ATOM   153  N NE1 . TRP A 1 21  ? 36.673  -2.335  14.213  1.00 32.44 ?  21  TRP A NE1 1 
ATOM   154  C CE2 . TRP A 1 21  ? 37.851  -2.972  13.913  1.00 33.64 ?  21  TRP A CE2 1 
ATOM   155  C CE3 . TRP A 1 21  ? 38.649  -5.242  13.656  1.00 35.12 ?  21  TRP A CE3 1 
ATOM   156  C CZ2 . TRP A 1 21  ? 39.116  -2.446  13.636  1.00 37.74 ?  21  TRP A CZ2 1 
ATOM   157  C CZ3 . TRP A 1 21  ? 39.904  -4.721  13.383  1.00 35.08 ?  21  TRP A CZ3 1 
ATOM   158  C CH2 . TRP A 1 21  ? 40.127  -3.334  13.376  1.00 37.12 ?  21  TRP A CH2 1 
ATOM   159  N N   . GLY A 1 22  ? 33.353  -8.209  12.932  1.00 39.50 ?  22  GLY A N   1 
ATOM   160  C CA  . GLY A 1 22  ? 32.980  -9.602  13.098  1.00 38.59 ?  22  GLY A CA  1 
ATOM   161  C C   . GLY A 1 22  ? 33.185  -10.385 11.814  1.00 41.05 ?  22  GLY A C   1 
ATOM   162  O O   . GLY A 1 22  ? 32.909  -9.899  10.717  1.00 40.31 ?  22  GLY A O   1 
ATOM   163  N N   . GLY A 1 23  ? 33.682  -11.609 11.968  1.00 43.28 ?  23  GLY A N   1 
ATOM   164  C CA  . GLY A 1 23  ? 33.912  -12.469 10.828  1.00 43.74 ?  23  GLY A CA  1 
ATOM   165  C C   . GLY A 1 23  ? 35.175  -12.180 10.052  1.00 44.25 ?  23  GLY A C   1 
ATOM   166  O O   . GLY A 1 23  ? 35.293  -12.615 8.903   1.00 45.62 ?  23  GLY A O   1 
ATOM   167  N N   . LEU A 1 24  ? 36.132  -11.475 10.642  1.00 37.79 ?  24  LEU A N   1 
ATOM   168  C CA  . LEU A 1 24  ? 37.303  -11.029 9.907   1.00 42.21 ?  24  LEU A CA  1 
ATOM   169  C C   . LEU A 1 24  ? 38.403  -12.084 9.906   1.00 42.02 ?  24  LEU A C   1 
ATOM   170  O O   . LEU A 1 24  ? 38.604  -12.815 10.881  1.00 39.89 ?  24  LEU A O   1 
ATOM   171  C CB  . LEU A 1 24  ? 37.836  -9.719  10.494  1.00 39.00 ?  24  LEU A CB  1 
ATOM   172  C CG  . LEU A 1 24  ? 36.961  -8.504  10.177  1.00 42.09 ?  24  LEU A CG  1 
ATOM   173  C CD1 . LEU A 1 24  ? 37.611  -7.212  10.665  1.00 38.94 ?  24  LEU A CD1 1 
ATOM   174  C CD2 . LEU A 1 24  ? 36.662  -8.430  8.676   1.00 38.75 ?  24  LEU A CD2 1 
ATOM   175  N N   . LYS A 1 25  ? 39.119  -12.153 8.789   1.00 37.96 ?  25  LYS A N   1 
ATOM   176  C CA  . LYS A 1 25  ? 40.355  -12.912 8.747   1.00 42.62 ?  25  LYS A CA  1 
ATOM   177  C C   . LYS A 1 25  ? 41.441  -12.185 9.531   1.00 41.00 ?  25  LYS A C   1 
ATOM   178  O O   . LYS A 1 25  ? 41.356  -10.982 9.804   1.00 41.19 ?  25  LYS A O   1 
ATOM   179  C CB  . LYS A 1 25  ? 40.804  -13.126 7.301   1.00 38.85 ?  25  LYS A CB  1 
ATOM   180  C CG  . LYS A 1 25  ? 39.667  -13.437 6.351   1.00 42.63 ?  25  LYS A CG  1 
ATOM   181  C CD  . LYS A 1 25  ? 40.155  -13.522 4.918   1.00 44.58 ?  25  LYS A CD  1 
ATOM   182  C CE  . LYS A 1 25  ? 39.014  -13.921 4.001   1.00 46.68 ?  25  LYS A CE  1 
ATOM   183  N NZ  . LYS A 1 25  ? 39.398  -13.955 2.566   1.00 47.76 1  25  LYS A NZ  1 
ATOM   184  N N   . GLU A 1 26  ? 42.475  -12.938 9.896   1.00 44.43 ?  26  GLU A N   1 
ATOM   185  C CA  . GLU A 1 26  ? 43.570  -12.377 10.673  1.00 45.96 ?  26  GLU A CA  1 
ATOM   186  C C   . GLU A 1 26  ? 44.214  -11.219 9.918   1.00 45.98 ?  26  GLU A C   1 
ATOM   187  O O   . GLU A 1 26  ? 44.519  -11.331 8.726   1.00 45.00 ?  26  GLU A O   1 
ATOM   188  C CB  . GLU A 1 26  ? 44.602  -13.464 10.981  1.00 46.86 ?  26  GLU A CB  1 
ATOM   189  C CG  . GLU A 1 26  ? 45.922  -12.940 11.525  1.00 50.17 ?  26  GLU A CG  1 
ATOM   190  C CD  . GLU A 1 26  ? 46.867  -14.052 11.943  1.00 57.47 ?  26  GLU A CD  1 
ATOM   191  O OE1 . GLU A 1 26  ? 46.472  -14.887 12.786  1.00 66.00 ?  26  GLU A OE1 1 
ATOM   192  O OE2 . GLU A 1 26  ? 48.008  -14.088 11.432  1.00 57.22 -1 26  GLU A OE2 1 
ATOM   193  N N   . LYS A 1 27  ? 44.371  -10.092 10.608  1.00 43.74 ?  27  LYS A N   1 
ATOM   194  C CA  . LYS A 1 27  ? 45.046  -8.868  10.169  1.00 42.53 ?  27  LYS A CA  1 
ATOM   195  C C   . LYS A 1 27  ? 44.218  -8.043  9.191   1.00 42.55 ?  27  LYS A C   1 
ATOM   196  O O   . LYS A 1 27  ? 44.738  -7.052  8.654   1.00 37.21 ?  27  LYS A O   1 
ATOM   197  C CB  . LYS A 1 27  ? 46.421  -9.142  9.537   1.00 46.01 ?  27  LYS A CB  1 
ATOM   198  C CG  . LYS A 1 27  ? 47.438  -9.722  10.499  1.00 41.24 ?  27  LYS A CG  1 
ATOM   199  C CD  . LYS A 1 27  ? 48.023  -8.638  11.394  1.00 51.77 ?  27  LYS A CD  1 
ATOM   200  C CE  . LYS A 1 27  ? 48.453  -9.203  12.740  1.00 49.87 ?  27  LYS A CE  1 
ATOM   201  N NZ  . LYS A 1 27  ? 47.424  -8.976  13.799  1.00 48.82 1  27  LYS A NZ  1 
ATOM   202  N N   . GLU A 1 28  ? 42.967  -8.408  8.921   1.00 40.50 ?  28  GLU A N   1 
ATOM   203  C CA  . GLU A 1 28  ? 42.131  -7.553  8.096   1.00 37.88 ?  28  GLU A CA  1 
ATOM   204  C C   . GLU A 1 28  ? 41.809  -6.265  8.842   1.00 34.08 ?  28  GLU A C   1 
ATOM   205  O O   . GLU A 1 28  ? 41.614  -6.259  10.061  1.00 35.09 ?  28  GLU A O   1 
ATOM   206  C CB  . GLU A 1 28  ? 40.849  -8.276  7.692   1.00 38.71 ?  28  GLU A CB  1 
ATOM   207  C CG  . GLU A 1 28  ? 41.093  -9.428  6.730   1.00 42.03 ?  28  GLU A CG  1 
ATOM   208  C CD  . GLU A 1 28  ? 39.864  -9.771  5.916   1.00 42.13 ?  28  GLU A CD  1 
ATOM   209  O OE1 . GLU A 1 28  ? 39.913  -9.639  4.673   1.00 40.08 ?  28  GLU A OE1 1 
ATOM   210  O OE2 . GLU A 1 28  ? 38.845  -10.163 6.528   1.00 42.36 -1 28  GLU A OE2 1 
ATOM   211  N N   . LEU A 1 29  ? 41.772  -5.166  8.100   1.00 35.86 ?  29  LEU A N   1 
ATOM   212  C CA  . LEU A 1 29  ? 41.569  -3.836  8.677   1.00 35.00 ?  29  LEU A CA  1 
ATOM   213  C C   . LEU A 1 29  ? 40.339  -3.207  8.051   1.00 31.98 ?  29  LEU A C   1 
ATOM   214  O O   . LEU A 1 29  ? 40.392  -2.754  6.893   1.00 32.93 ?  29  LEU A O   1 
ATOM   215  C CB  . LEU A 1 29  ? 42.797  -2.960  8.448   1.00 35.29 ?  29  LEU A CB  1 
ATOM   216  C CG  . LEU A 1 29  ? 42.705  -1.517  8.930   1.00 35.62 ?  29  LEU A CG  1 
ATOM   217  C CD1 . LEU A 1 29  ? 42.461  -1.490  10.426  1.00 36.15 ?  29  LEU A CD1 1 
ATOM   218  C CD2 . LEU A 1 29  ? 44.006  -0.804  8.590   1.00 37.22 ?  29  LEU A CD2 1 
ATOM   219  N N   . PRO A 1 30  ? 39.207  -3.170  8.760   1.00 32.12 ?  30  PRO A N   1 
ATOM   220  C CA  . PRO A 1 30  ? 37.980  -2.609  8.177   1.00 30.11 ?  30  PRO A CA  1 
ATOM   221  C C   . PRO A 1 30  ? 37.984  -1.091  8.272   1.00 32.57 ?  30  PRO A C   1 
ATOM   222  O O   . PRO A 1 30  ? 38.177  -0.526  9.348   1.00 29.79 ?  30  PRO A O   1 
ATOM   223  C CB  . PRO A 1 30  ? 36.868  -3.221  9.039   1.00 28.89 ?  30  PRO A CB  1 
ATOM   224  C CG  . PRO A 1 30  ? 37.509  -3.426  10.373  1.00 31.01 ?  30  PRO A CG  1 
ATOM   225  C CD  . PRO A 1 30  ? 38.978  -3.719  10.110  1.00 34.08 ?  30  PRO A CD  1 
ATOM   226  N N   . MET A 1 31  ? 37.802  -0.420  7.137   1.00 29.73 ?  31  MET A N   1 
ATOM   227  C CA  . MET A 1 31  ? 37.701  1.062   7.104   1.00 32.42 ?  31  MET A CA  1 
ATOM   228  C C   . MET A 1 31  ? 36.553  1.418   6.150   1.00 30.58 ?  31  MET A C   1 
ATOM   229  O O   . MET A 1 31  ? 36.690  2.354   5.382   1.00 29.47 ?  31  MET A O   1 
ATOM   230  C CB  . MET A 1 31  ? 39.035  1.708   6.697   1.00 29.75 ?  31  MET A CB  1 
ATOM   231  C CG  . MET A 1 31  ? 40.184  1.396   7.622   1.00 29.79 ?  31  MET A CG  1 
ATOM   232  S SD  . MET A 1 31  ? 41.743  2.138   7.104   1.00 34.99 ?  31  MET A SD  1 
ATOM   233  C CE  . MET A 1 31  ? 41.555  3.790   7.763   1.00 29.77 ?  31  MET A CE  1 
ATOM   234  N N   . TRP A 1 32  ? 35.435  0.701   6.262   1.00 30.76 ?  32  TRP A N   1 
ATOM   235  C CA  . TRP A 1 32  ? 34.304  0.873   5.317   1.00 31.56 ?  32  TRP A CA  1 
ATOM   236  C C   . TRP A 1 32  ? 33.040  1.395   6.015   1.00 33.75 ?  32  TRP A C   1 
ATOM   237  O O   . TRP A 1 32  ? 32.696  2.547   5.814   1.00 31.81 ?  32  TRP A O   1 
ATOM   238  C CB  . TRP A 1 32  ? 34.035  -0.458  4.592   1.00 30.46 ?  32  TRP A CB  1 
ATOM   239  C CG  . TRP A 1 32  ? 33.688  -1.624  5.467   1.00 34.33 ?  32  TRP A CG  1 
ATOM   240  C CD1 . TRP A 1 32  ? 34.498  -2.267  6.354   1.00 32.61 ?  32  TRP A CD1 1 
ATOM   241  C CD2 . TRP A 1 32  ? 32.401  -2.257  5.571   1.00 30.84 ?  32  TRP A CD2 1 
ATOM   242  N NE1 . TRP A 1 32  ? 33.808  -3.255  6.995   1.00 31.39 ?  32  TRP A NE1 1 
ATOM   243  C CE2 . TRP A 1 32  ? 32.520  -3.273  6.538   1.00 30.22 ?  32  TRP A CE2 1 
ATOM   244  C CE3 . TRP A 1 32  ? 31.164  -2.050  4.957   1.00 32.64 ?  32  TRP A CE3 1 
ATOM   245  C CZ2 . TRP A 1 32  ? 31.450  -4.090  6.892   1.00 33.56 ?  32  TRP A CZ2 1 
ATOM   246  C CZ3 . TRP A 1 32  ? 30.109  -2.861  5.304   1.00 37.01 ?  32  TRP A CZ3 1 
ATOM   247  C CH2 . TRP A 1 32  ? 30.254  -3.867  6.257   1.00 30.42 ?  32  TRP A CH2 1 
ATOM   248  N N   . ILE A 1 33  ? 32.391  0.562   6.820   1.00 30.12 ?  33  ILE A N   1 
ATOM   249  C CA  . ILE A 1 33  ? 31.094  0.953   7.438   1.00 27.10 ?  33  ILE A CA  1 
ATOM   250  C C   . ILE A 1 33  ? 31.292  2.167   8.344   1.00 28.47 ?  33  ILE A C   1 
ATOM   251  O O   . ILE A 1 33  ? 32.305  2.241   9.007   1.00 30.04 ?  33  ILE A O   1 
ATOM   252  C CB  . ILE A 1 33  ? 30.390  -0.236  8.124   1.00 31.79 ?  33  ILE A CB  1 
ATOM   253  C CG1 . ILE A 1 33  ? 28.896  0.022   8.328   1.00 34.05 ?  33  ILE A CG1 1 
ATOM   254  C CG2 . ILE A 1 33  ? 31.074  -0.647  9.411   1.00 30.21 ?  33  ILE A CG2 1 
ATOM   255  C CD1 . ILE A 1 33  ? 28.113  -1.204  8.701   1.00 33.11 ?  33  ILE A CD1 1 
ATOM   256  N N   . ALA A 1 34  ? 30.305  3.044   8.372   1.00 28.81 ?  34  ALA A N   1 
ATOM   257  C CA  . ALA A 1 34  ? 30.441  4.295   9.118   1.00 26.91 ?  34  ALA A CA  1 
ATOM   258  C C   . ALA A 1 34  ? 30.114  4.059   10.591  1.00 29.73 ?  34  ALA A C   1 
ATOM   259  O O   . ALA A 1 34  ? 29.015  4.339   11.075  1.00 27.95 ?  34  ALA A O   1 
ATOM   260  C CB  . ALA A 1 34  ? 29.556  5.378   8.513   1.00 32.21 ?  34  ALA A CB  1 
ATOM   261  N N   . GLU A 1 35  ? 31.104  3.517   11.303  1.00 27.64 ?  35  GLU A N   1 
ATOM   262  C CA  . GLU A 1 35  ? 31.175  3.565   12.758  1.00 28.94 ?  35  GLU A CA  1 
ATOM   263  C C   . GLU A 1 35  ? 32.639  3.739   13.131  1.00 26.83 ?  35  GLU A C   1 
ATOM   264  O O   . GLU A 1 35  ? 33.538  3.429   12.345  1.00 27.02 ?  35  GLU A O   1 
ATOM   265  C CB  . GLU A 1 35  ? 30.586  2.305   13.423  1.00 26.43 ?  35  GLU A CB  1 
ATOM   266  C CG  . GLU A 1 35  ? 31.440  1.048   13.258  1.00 29.74 ?  35  GLU A CG  1 
ATOM   267  C CD  . GLU A 1 35  ? 30.793  -0.221  13.816  1.00 26.54 ?  35  GLU A CD  1 
ATOM   268  O OE1 . GLU A 1 35  ? 31.260  -0.745  14.847  1.00 28.32 ?  35  GLU A OE1 1 
ATOM   269  O OE2 . GLU A 1 35  ? 29.822  -0.702  13.203  1.00 29.67 -1 35  GLU A OE2 1 
ATOM   270  N N   . MET A 1 36  ? 32.880  4.229   14.347  1.00 28.14 ?  36  MET A N   1 
ATOM   271  C CA  . MET A 1 36  ? 34.229  4.583   14.764  1.00 28.61 ?  36  MET A CA  1 
ATOM   272  C C   . MET A 1 36  ? 34.923  3.443   15.495  1.00 27.42 ?  36  MET A C   1 
ATOM   273  O O   . MET A 1 36  ? 34.294  2.564   16.079  1.00 24.47 ?  36  MET A O   1 
ATOM   274  C CB  . MET A 1 36  ? 34.219  5.784   15.693  1.00 21.12 ?  36  MET A CB  1 
ATOM   275  C CG  . MET A 1 36  ? 33.357  6.906   15.246  1.00 22.25 ?  36  MET A CG  1 
ATOM   276  S SD  . MET A 1 36  ? 33.717  8.326   16.291  1.00 25.01 ?  36  MET A SD  1 
ATOM   277  C CE  . MET A 1 36  ? 32.376  9.406   15.818  1.00 25.21 ?  36  MET A CE  1 
ATOM   278  N N   . ASP A 1 37  ? 36.246  3.499   15.484  1.00 24.46 ?  37  ASP A N   1 
ATOM   279  C CA  . ASP A 1 37  ? 37.077  2.649   16.323  1.00 24.76 ?  37  ASP A CA  1 
ATOM   280  C C   . ASP A 1 37  ? 37.681  3.461   17.460  1.00 25.90 ?  37  ASP A C   1 
ATOM   281  O O   . ASP A 1 37  ? 38.872  3.365   17.771  1.00 27.88 ?  37  ASP A O   1 
ATOM   282  C CB  . ASP A 1 37  ? 38.125  1.948   15.474  1.00 29.42 ?  37  ASP A CB  1 
ATOM   283  C CG  . ASP A 1 37  ? 37.490  0.952   14.526  1.00 33.71 ?  37  ASP A CG  1 
ATOM   284  O OD1 . ASP A 1 37  ? 36.654  0.144   15.009  1.00 30.98 ?  37  ASP A OD1 1 
ATOM   285  O OD2 . ASP A 1 37  ? 37.782  1.000   13.312  1.00 33.46 -1 37  ASP A OD2 1 
ATOM   286  N N   . PHE A 1 38  ? 36.833  4.283   18.074  1.00 23.09 ?  38  PHE A N   1 
ATOM   287  C CA  . PHE A 1 38  ? 37.120  5.034   19.284  1.00 24.22 ?  38  PHE A CA  1 
ATOM   288  C C   . PHE A 1 38  ? 36.104  4.653   20.350  1.00 27.13 ?  38  PHE A C   1 
ATOM   289  O O   . PHE A 1 38  ? 34.934  4.407   20.043  1.00 25.41 ?  38  PHE A O   1 
ATOM   290  C CB  . PHE A 1 38  ? 37.004  6.548   19.079  1.00 26.89 ?  38  PHE A CB  1 
ATOM   291  C CG  . PHE A 1 38  ? 37.946  7.120   18.060  1.00 23.50 ?  38  PHE A CG  1 
ATOM   292  C CD1 . PHE A 1 38  ? 39.300  6.821   18.100  1.00 27.41 ?  38  PHE A CD1 1 
ATOM   293  C CD2 . PHE A 1 38  ? 37.474  7.982   17.081  1.00 24.84 ?  38  PHE A CD2 1 
ATOM   294  C CE1 . PHE A 1 38  ? 40.166  7.362   17.175  1.00 28.12 ?  38  PHE A CE1 1 
ATOM   295  C CE2 . PHE A 1 38  ? 38.337  8.533   16.153  1.00 28.31 ?  38  PHE A CE2 1 
ATOM   296  C CZ  . PHE A 1 38  ? 39.687  8.222   16.206  1.00 27.35 ?  38  PHE A CZ  1 
ATOM   297  N N   . ARG A 1 39  ? 36.541  4.634   21.604  1.00 23.94 ?  39  ARG A N   1 
ATOM   298  C CA  . ARG A 1 39  ? 35.586  4.487   22.691  1.00 29.12 ?  39  ARG A CA  1 
ATOM   299  C C   . ARG A 1 39  ? 34.697  5.721   22.752  1.00 26.31 ?  39  ARG A C   1 
ATOM   300  O O   . ARG A 1 39  ? 35.098  6.820   22.365  1.00 26.32 ?  39  ARG A O   1 
ATOM   301  C CB  . ARG A 1 39  ? 36.301  4.285   24.032  1.00 29.97 ?  39  ARG A CB  1 
ATOM   302  C CG  . ARG A 1 39  ? 37.294  3.118   24.059  1.00 37.88 ?  39  ARG A CG  1 
ATOM   303  C CD  . ARG A 1 39  ? 38.289  3.251   25.216  1.00 44.99 ?  39  ARG A CD  1 
ATOM   304  N NE  . ARG A 1 39  ? 37.646  3.731   26.440  1.00 44.78 ?  39  ARG A NE  1 
ATOM   305  C CZ  . ARG A 1 39  ? 37.125  2.936   27.371  1.00 43.74 ?  39  ARG A CZ  1 
ATOM   306  N NH1 . ARG A 1 39  ? 37.176  1.619   27.224  1.00 42.44 1  39  ARG A NH1 1 
ATOM   307  N NH2 . ARG A 1 39  ? 36.551  3.456   28.450  1.00 43.42 ?  39  ARG A NH2 1 
ATOM   308  N N   . ILE A 1 40  ? 33.471  5.535   23.238  1.00 21.29 ?  40  ILE A N   1 
ATOM   309  C CA  . ILE A 1 40  ? 32.552  6.660   23.337  1.00 20.42 ?  40  ILE A CA  1 
ATOM   310  C C   . ILE A 1 40  ? 32.934  7.574   24.495  1.00 23.75 ?  40  ILE A C   1 
ATOM   311  O O   . ILE A 1 40  ? 33.734  7.206   25.371  1.00 23.94 ?  40  ILE A O   1 
ATOM   312  C CB  . ILE A 1 40  ? 31.095  6.186   23.499  1.00 22.51 ?  40  ILE A CB  1 
ATOM   313  C CG1 . ILE A 1 40  ? 30.946  5.486   24.842  1.00 23.46 ?  40  ILE A CG1 1 
ATOM   314  C CG2 . ILE A 1 40  ? 30.701  5.271   22.345  1.00 23.10 ?  40  ILE A CG2 1 
ATOM   315  C CD1 . ILE A 1 40  ? 29.517  5.210   25.272  1.00 24.14 ?  40  ILE A CD1 1 
ATOM   316  N N   . ALA A 1 41  ? 32.327  8.761   24.505  1.00 22.79 ?  41  ALA A N   1 
ATOM   317  C CA  . ALA A 1 41  ? 32.531  9.749   25.548  1.00 24.29 ?  41  ALA A CA  1 
ATOM   318  C C   . ALA A 1 41  ? 32.229  9.144   26.915  1.00 26.34 ?  41  ALA A C   1 
ATOM   319  O O   . ALA A 1 41  ? 31.183  8.498   27.087  1.00 24.64 ?  41  ALA A O   1 
ATOM   320  C CB  . ALA A 1 41  ? 31.633  10.965  25.313  1.00 22.97 ?  41  ALA A CB  1 
ATOM   321  N N   . PRO A 1 42  ? 33.115  9.312   27.898  1.00 24.10 ?  42  PRO A N   1 
ATOM   322  C CA  . PRO A 1 42  ? 32.817  8.801   29.241  1.00 25.04 ?  42  PRO A CA  1 
ATOM   323  C C   . PRO A 1 42  ? 31.549  9.380   29.830  1.00 24.42 ?  42  PRO A C   1 
ATOM   324  O O   . PRO A 1 42  ? 30.848  8.682   30.571  1.00 25.70 ?  42  PRO A O   1 
ATOM   325  C CB  . PRO A 1 42  ? 34.063  9.198   30.062  1.00 24.76 ?  42  PRO A CB  1 
ATOM   326  C CG  . PRO A 1 42  ? 34.906  10.044  29.161  1.00 28.81 ?  42  PRO A CG  1 
ATOM   327  C CD  . PRO A 1 42  ? 34.501  9.783   27.759  1.00 25.97 ?  42  PRO A CD  1 
ATOM   328  N N   . GLU A 1 43  ? 31.218  10.631  29.518  1.00 22.45 ?  43  GLU A N   1 
ATOM   329  C CA  . GLU A 1 43  ? 29.976  11.196  30.027  1.00 22.99 ?  43  GLU A CA  1 
ATOM   330  C C   . GLU A 1 43  ? 28.761  10.434  29.505  1.00 26.75 ?  43  GLU A C   1 
ATOM   331  O O   . GLU A 1 43  ? 27.740  10.342  30.196  1.00 24.63 ?  43  GLU A O   1 
ATOM   332  C CB  . GLU A 1 43  ? 29.867  12.671  29.647  1.00 26.89 ?  43  GLU A CB  1 
ATOM   333  C CG  . GLU A 1 43  ? 30.977  13.544  30.224  1.00 28.87 ?  43  GLU A CG  1 
ATOM   334  C CD  . GLU A 1 43  ? 32.189  13.641  29.311  1.00 28.89 ?  43  GLU A CD  1 
ATOM   335  O OE1 . GLU A 1 43  ? 33.003  14.568  29.500  1.00 33.85 ?  43  GLU A OE1 1 
ATOM   336  O OE2 . GLU A 1 43  ? 32.341  12.792  28.403  1.00 24.89 -1 43  GLU A OE2 1 
ATOM   337  N N   . ILE A 1 44  ? 28.849  9.887   28.294  1.00 22.81 ?  44  ILE A N   1 
ATOM   338  C CA  . ILE A 1 44  ? 27.761  9.049   27.799  1.00 24.30 ?  44  ILE A CA  1 
ATOM   339  C C   . ILE A 1 44  ? 27.781  7.705   28.499  1.00 26.64 ?  44  ILE A C   1 
ATOM   340  O O   . ILE A 1 44  ? 26.747  7.215   28.975  1.00 22.99 ?  44  ILE A O   1 
ATOM   341  C CB  . ILE A 1 44  ? 27.854  8.893   26.273  1.00 21.09 ?  44  ILE A CB  1 
ATOM   342  C CG1 . ILE A 1 44  ? 27.764  10.283  25.623  1.00 25.18 ?  44  ILE A CG1 1 
ATOM   343  C CG2 . ILE A 1 44  ? 26.748  7.951   25.765  1.00 22.79 ?  44  ILE A CG2 1 
ATOM   344  C CD1 . ILE A 1 44  ? 28.105  10.335  24.158  1.00 20.83 ?  44  ILE A CD1 1 
ATOM   345  N N   . MET A 1 45  ? 28.968  7.096   28.578  1.00 25.57 ?  45  MET A N   1 
ATOM   346  C CA  . MET A 1 45  ? 29.130  5.820   29.268  1.00 27.36 ?  45  MET A CA  1 
ATOM   347  C C   . MET A 1 45  ? 28.547  5.871   30.675  1.00 28.14 ?  45  MET A C   1 
ATOM   348  O O   . MET A 1 45  ? 27.811  4.966   31.086  1.00 24.73 ?  45  MET A O   1 
ATOM   349  C CB  . MET A 1 45  ? 30.619  5.450   29.298  1.00 23.69 ?  45  MET A CB  1 
ATOM   350  C CG  . MET A 1 45  ? 30.921  4.029   29.641  1.00 34.42 ?  45  MET A CG  1 
ATOM   351  S SD  . MET A 1 45  ? 30.447  2.892   28.330  1.00 38.84 ?  45  MET A SD  1 
ATOM   352  C CE  . MET A 1 45  ? 29.358  1.885   29.317  1.00 33.21 ?  45  MET A CE  1 
ATOM   353  N N   . THR A 1 46  ? 28.849  6.941   31.426  1.00 25.89 ?  46  THR A N   1 
ATOM   354  C CA  . THR A 1 46  ? 28.330  7.071   32.789  1.00 26.23 ?  46  THR A CA  1 
ATOM   355  C C   . THR A 1 46  ? 26.804  7.026   32.826  1.00 27.48 ?  46  THR A C   1 
ATOM   356  O O   . THR A 1 46  ? 26.212  6.416   33.727  1.00 27.06 ?  46  THR A O   1 
ATOM   357  C CB  . THR A 1 46  ? 28.829  8.368   33.421  1.00 28.15 ?  46  THR A CB  1 
ATOM   358  O OG1 . THR A 1 46  ? 30.265  8.362   33.433  1.00 30.00 ?  46  THR A OG1 1 
ATOM   359  C CG2 . THR A 1 46  ? 28.326  8.476   34.847  1.00 34.01 ?  46  THR A CG2 1 
ATOM   360  N N   . SER A 1 47  ? 26.143  7.625   31.844  1.00 26.15 ?  47  SER A N   1 
ATOM   361  C CA  . SER A 1 47  ? 24.662  7.672   31.856  1.00 24.61 ?  47  SER A CA  1 
ATOM   362  C C   . SER A 1 47  ? 24.102  6.271   31.600  1.00 25.70 ?  47  SER A C   1 
ATOM   363  O O   . SER A 1 47  ? 23.084  5.929   32.159  1.00 26.49 ?  47  SER A O   1 
ATOM   364  C CB  . SER A 1 47  ? 24.147  8.643   30.849  1.00 26.62 ?  47  SER A CB  1 
ATOM   365  O OG  . SER A 1 47  ? 24.410  8.199   29.537  1.00 29.89 ?  47  SER A OG  1 
ATOM   366  N N   . MET A 1 48  ? 24.800  5.499   30.780  1.00 24.19 ?  48  MET A N   1 
ATOM   367  C CA  . MET A 1 48  ? 24.347  4.127   30.479  1.00 22.50 ?  48  MET A CA  1 
ATOM   368  C C   . MET A 1 48  ? 24.531  3.225   31.707  1.00 28.08 ?  48  MET A C   1 
ATOM   369  O O   . MET A 1 48  ? 23.616  2.482   32.026  1.00 24.32 ?  48  MET A O   1 
ATOM   370  C CB  . MET A 1 48  ? 25.084  3.578   29.262  1.00 25.59 ?  48  MET A CB  1 
ATOM   371  C CG  . MET A 1 48  ? 24.732  4.274   27.979  1.00 25.43 ?  48  MET A CG  1 
ATOM   372  S SD  . MET A 1 48  ? 25.581  3.423   26.649  1.00 27.80 ?  48  MET A SD  1 
ATOM   373  C CE  . MET A 1 48  ? 27.250  3.603   27.229  1.00 37.84 ?  48  MET A CE  1 
ATOM   374  N N   . GLU A 1 49  ? 25.683  3.325   32.367  1.00 26.96 ?  49  GLU A N   1 
ATOM   375  C CA  . GLU A 1 49  ? 25.922  2.515   33.584  1.00 26.12 ?  49  GLU A CA  1 
ATOM   376  C C   . GLU A 1 49  ? 24.908  2.944   34.650  1.00 24.10 ?  49  GLU A C   1 
ATOM   377  O O   . GLU A 1 49  ? 24.412  2.088   35.365  1.00 28.24 ?  49  GLU A O   1 
ATOM   378  C CB  . GLU A 1 49  ? 27.369  2.648   34.064  1.00 29.20 ?  49  GLU A CB  1 
ATOM   379  C CG  . GLU A 1 49  ? 28.404  2.124   33.094  1.00 32.07 ?  49  GLU A CG  1 
ATOM   380  C CD  . GLU A 1 49  ? 29.823  2.579   33.391  1.00 33.51 ?  49  GLU A CD  1 
ATOM   381  O OE1 . GLU A 1 49  ? 30.746  2.068   32.753  1.00 42.71 ?  49  GLU A OE1 1 
ATOM   382  O OE2 . GLU A 1 49  ? 29.998  3.439   34.263  1.00 40.16 -1 49  GLU A OE2 1 
ATOM   383  N N   . GLU A 1 50  ? 24.627  4.239   34.730  1.00 26.85 ?  50  GLU A N   1 
ATOM   384  C CA  . GLU A 1 50  ? 23.663  4.735   35.699  1.00 26.41 ?  50  GLU A CA  1 
ATOM   385  C C   . GLU A 1 50  ? 22.267  4.185   35.424  1.00 28.55 ?  50  GLU A C   1 
ATOM   386  O O   . GLU A 1 50  ? 21.554  3.754   36.343  1.00 24.67 ?  50  GLU A O   1 
ATOM   387  C CB  . GLU A 1 50  ? 23.653  6.256   35.656  1.00 29.77 ?  50  GLU A CB  1 
ATOM   388  C CG  . GLU A 1 50  ? 22.454  6.802   36.331  1.00 38.09 ?  50  GLU A CG  1 
ATOM   389  C CD  . GLU A 1 50  ? 22.599  6.679   37.794  1.00 44.27 ?  50  GLU A CD  1 
ATOM   390  O OE1 . GLU A 1 50  ? 21.591  6.819   38.515  1.00 48.99 ?  50  GLU A OE1 1 
ATOM   391  O OE2 . GLU A 1 50  ? 23.758  6.502   38.248  1.00 45.37 -1 50  GLU A OE2 1 
ATOM   392  N N   . LYS A 1 51  ? 21.848  4.230   34.161  1.00 23.70 ?  51  LYS A N   1 
ATOM   393  C CA  . LYS A 1 51  ? 20.529  3.716   33.792  1.00 26.11 ?  51  LYS A CA  1 
ATOM   394  C C   . LYS A 1 51  ? 20.388  2.233   34.127  1.00 21.96 ?  51  LYS A C   1 
ATOM   395  O O   . LYS A 1 51  ? 19.347  1.804   34.641  1.00 23.51 ?  51  LYS A O   1 
ATOM   396  C CB  . LYS A 1 51  ? 20.287  3.968   32.298  1.00 19.34 ?  51  LYS A CB  1 
ATOM   397  C CG  . LYS A 1 51  ? 18.918  3.495   31.790  1.00 24.52 ?  51  LYS A CG  1 
ATOM   398  C CD  . LYS A 1 51  ? 17.787  4.084   32.618  1.00 22.68 ?  51  LYS A CD  1 
ATOM   399  C CE  . LYS A 1 51  ? 16.415  3.582   32.151  1.00 22.44 ?  51  LYS A CE  1 
ATOM   400  N NZ  . LYS A 1 51  ? 16.038  4.062   30.748  1.00 24.72 1  51  LYS A NZ  1 
ATOM   401  N N   . LEU A 1 52  ? 21.413  1.432   33.831  1.00 23.98 ?  52  LEU A N   1 
ATOM   402  C CA  . LEU A 1 52  ? 21.346  -0.001  34.104  1.00 23.59 ?  52  LEU A CA  1 
ATOM   403  C C   . LEU A 1 52  ? 21.064  -0.292  35.573  1.00 25.89 ?  52  LEU A C   1 
ATOM   404  O O   . LEU A 1 52  ? 20.425  -1.297  35.893  1.00 24.01 ?  52  LEU A O   1 
ATOM   405  C CB  . LEU A 1 52  ? 22.648  -0.684  33.689  1.00 22.10 ?  52  LEU A CB  1 
ATOM   406  C CG  . LEU A 1 52  ? 22.917  -0.998  32.226  1.00 31.59 ?  52  LEU A CG  1 
ATOM   407  C CD1 . LEU A 1 52  ? 24.025  -2.029  32.141  1.00 32.80 ?  52  LEU A CD1 1 
ATOM   408  C CD2 . LEU A 1 52  ? 21.647  -1.479  31.496  1.00 30.05 ?  52  LEU A CD2 1 
ATOM   409  N N   . LYS A 1 53  ? 21.530  0.566   36.481  1.00 28.35 ?  53  LYS A N   1 
ATOM   410  C CA  . LYS A 1 53  ? 21.321  0.296   37.901  1.00 27.70 ?  53  LYS A CA  1 
ATOM   411  C C   . LYS A 1 53  ? 19.851  0.353   38.311  1.00 26.73 ?  53  LYS A C   1 
ATOM   412  O O   . LYS A 1 53  ? 19.511  -0.150  39.387  1.00 27.30 ?  53  LYS A O   1 
ATOM   413  C CB  . LYS A 1 53  ? 22.162  1.270   38.733  1.00 29.45 ?  53  LYS A CB  1 
ATOM   414  C CG  . LYS A 1 53  ? 23.638  0.913   38.704  1.00 31.90 ?  53  LYS A CG  1 
ATOM   415  C CD  . LYS A 1 53  ? 23.867  -0.417  39.413  1.00 40.38 ?  53  LYS A CD  1 
ATOM   416  C CE  . LYS A 1 53  ? 25.059  -1.174  38.839  1.00 47.63 ?  53  LYS A CE  1 
ATOM   417  N NZ  . LYS A 1 53  ? 26.294  -0.345  38.886  1.00 46.77 1  53  LYS A NZ  1 
ATOM   418  N N   . VAL A 1 54  ? 18.968  0.884   37.470  1.00 25.67 ?  54  VAL A N   1 
ATOM   419  C CA  . VAL A 1 54  ? 17.507  0.847   37.767  1.00 24.07 ?  54  VAL A CA  1 
ATOM   420  C C   . VAL A 1 54  ? 17.140  -0.627  37.940  1.00 21.72 ?  54  VAL A C   1 
ATOM   421  O O   . VAL A 1 54  ? 16.303  -0.931  38.769  1.00 27.80 ?  54  VAL A O   1 
ATOM   422  C CB  . VAL A 1 54  ? 16.687  1.549   36.668  1.00 25.15 ?  54  VAL A CB  1 
ATOM   423  C CG1 . VAL A 1 54  ? 15.195  1.354   36.868  1.00 23.71 ?  54  VAL A CG1 1 
ATOM   424  C CG2 . VAL A 1 54  ? 17.013  3.028   36.589  1.00 24.65 ?  54  VAL A CG2 1 
ATOM   425  N N   . ALA A 1 55  ? 17.799  -1.524  37.200  1.00 25.45 ?  55  ALA A N   1 
ATOM   426  C CA  . ALA A 1 55  ? 17.635  -3.003  37.318  1.00 25.91 ?  55  ALA A CA  1 
ATOM   427  C C   . ALA A 1 55  ? 16.208  -3.418  36.953  1.00 25.08 ?  55  ALA A C   1 
ATOM   428  O O   . ALA A 1 55  ? 15.802  -4.478  37.381  1.00 23.91 ?  55  ALA A O   1 
ATOM   429  C CB  . ALA A 1 55  ? 18.093  -3.477  38.664  1.00 27.21 ?  55  ALA A CB  1 
ATOM   430  N N   . ALA A 1 56  ? 15.509  -2.590  36.190  1.00 24.64 ?  56  ALA A N   1 
ATOM   431  C CA  . ALA A 1 56  ? 14.163  -2.929  35.694  1.00 24.54 ?  56  ALA A CA  1 
ATOM   432  C C   . ALA A 1 56  ? 13.957  -2.044  34.475  1.00 23.83 ?  56  ALA A C   1 
ATOM   433  O O   . ALA A 1 56  ? 14.264  -0.869  34.566  1.00 24.60 ?  56  ALA A O   1 
ATOM   434  C CB  . ALA A 1 56  ? 13.095  -2.737  36.706  1.00 24.17 ?  56  ALA A CB  1 
ATOM   435  N N   . PHE A 1 57  ? 13.421  -2.607  33.406  1.00 21.91 ?  57  PHE A N   1 
ATOM   436  C CA  . PHE A 1 57  ? 13.406  -1.887  32.140  1.00 20.53 ?  57  PHE A CA  1 
ATOM   437  C C   . PHE A 1 57  ? 12.022  -2.003  31.505  1.00 21.39 ?  57  PHE A C   1 
ATOM   438  O O   . PHE A 1 57  ? 11.829  -2.622  30.455  1.00 22.80 ?  57  PHE A O   1 
ATOM   439  C CB  . PHE A 1 57  ? 14.559  -2.375  31.263  1.00 21.62 ?  57  PHE A CB  1 
ATOM   440  C CG  . PHE A 1 57  ? 15.891  -2.254  31.973  1.00 21.08 ?  57  PHE A CG  1 
ATOM   441  C CD1 . PHE A 1 57  ? 16.422  -1.006  32.231  1.00 23.31 ?  57  PHE A CD1 1 
ATOM   442  C CD2 . PHE A 1 57  ? 16.537  -3.367  32.471  1.00 21.84 ?  57  PHE A CD2 1 
ATOM   443  C CE1 . PHE A 1 57  ? 17.607  -0.865  32.950  1.00 24.78 ?  57  PHE A CE1 1 
ATOM   444  C CE2 . PHE A 1 57  ? 17.732  -3.246  33.173  1.00 23.57 ?  57  PHE A CE2 1 
ATOM   445  C CZ  . PHE A 1 57  ? 18.260  -1.985  33.417  1.00 23.57 ?  57  PHE A CZ  1 
ATOM   446  N N   . GLY A 1 58  ? 11.056  -1.343  32.149  1.00 23.20 ?  58  GLY A N   1 
ATOM   447  C CA  . GLY A 1 58  ? 9.713   -1.230  31.621  1.00 23.54 ?  58  GLY A CA  1 
ATOM   448  C C   . GLY A 1 58  ? 9.622   -0.155  30.558  1.00 24.77 ?  58  GLY A C   1 
ATOM   449  O O   . GLY A 1 58  ? 10.628  0.340   30.046  1.00 23.68 ?  58  GLY A O   1 
ATOM   450  N N   . TYR A 1 59  ? 8.386   0.220   30.241  1.00 23.71 ?  59  TYR A N   1 
ATOM   451  C CA  . TYR A 1 59  ? 8.125   1.113   29.122  1.00 24.64 ?  59  TYR A CA  1 
ATOM   452  C C   . TYR A 1 59  ? 8.595   2.527   29.433  1.00 22.25 ?  59  TYR A C   1 
ATOM   453  O O   . TYR A 1 59  ? 8.494   3.002   30.567  1.00 25.70 ?  59  TYR A O   1 
ATOM   454  C CB  . TYR A 1 59  ? 6.636   1.117   28.785  1.00 23.38 ?  59  TYR A CB  1 
ATOM   455  C CG  . TYR A 1 59  ? 6.108   -0.226  28.287  1.00 23.15 ?  59  TYR A CG  1 
ATOM   456  C CD1 . TYR A 1 59  ? 6.186   -0.573  26.947  1.00 21.07 ?  59  TYR A CD1 1 
ATOM   457  C CD2 . TYR A 1 59  ? 5.522   -1.133  29.164  1.00 23.09 ?  59  TYR A CD2 1 
ATOM   458  C CE1 . TYR A 1 59  ? 5.697   -1.777  26.488  1.00 24.01 ?  59  TYR A CE1 1 
ATOM   459  C CE2 . TYR A 1 59  ? 5.031   -2.347  28.714  1.00 23.67 ?  59  TYR A CE2 1 
ATOM   460  C CZ  . TYR A 1 59  ? 5.115   -2.663  27.377  1.00 25.30 ?  59  TYR A CZ  1 
ATOM   461  O OH  . TYR A 1 59  ? 4.628   -3.876  26.927  1.00 29.09 ?  59  TYR A OH  1 
ATOM   462  N N   . GLU A 1 60  ? 9.106   3.199   28.412  1.00 23.25 ?  60  GLU A N   1 
ATOM   463  C CA  . GLU A 1 60  ? 9.675   4.527   28.557  1.00 24.51 ?  60  GLU A CA  1 
ATOM   464  C C   . GLU A 1 60  ? 8.911   5.532   27.726  1.00 23.35 ?  60  GLU A C   1 
ATOM   465  O O   . GLU A 1 60  ? 8.480   5.227   26.612  1.00 23.61 ?  60  GLU A O   1 
ATOM   466  C CB  . GLU A 1 60  ? 11.133  4.516   28.153  1.00 24.85 ?  60  GLU A CB  1 
ATOM   467  C CG  . GLU A 1 60  ? 11.869  3.677   29.131  1.00 29.85 ?  60  GLU A CG  1 
ATOM   468  C CD  . GLU A 1 60  ? 13.292  4.077   29.308  1.00 26.78 ?  60  GLU A CD  1 
ATOM   469  O OE1 . GLU A 1 60  ? 14.034  3.226   29.822  1.00 29.05 ?  60  GLU A OE1 1 
ATOM   470  O OE2 . GLU A 1 60  ? 13.651  5.217   28.936  1.00 22.26 -1 60  GLU A OE2 1 
ATOM   471  N N   . SER A 1 61  ? 8.714   6.711   28.305  1.00 23.79 ?  61  SER A N   1 
ATOM   472  C CA  . SER A 1 61  ? 8.233   7.878   27.592  1.00 24.99 ?  61  SER A CA  1 
ATOM   473  C C   . SER A 1 61  ? 9.429   8.706   27.143  1.00 25.50 ?  61  SER A C   1 
ATOM   474  O O   . SER A 1 61  ? 10.565  8.505   27.584  1.00 24.49 ?  61  SER A O   1 
ATOM   475  C CB  . SER A 1 61  ? 7.305   8.708   28.482  1.00 29.11 ?  61  SER A CB  1 
ATOM   476  O OG  . SER A 1 61  ? 8.006   9.204   29.617  1.00 28.59 ?  61  SER A OG  1 
ATOM   477  N N   . VAL A 1 62  ? 9.178   9.637   26.231  1.00 26.45 ?  62  VAL A N   1 
ATOM   478  C CA  . VAL A 1 62  ? 10.177  10.618  25.826  1.00 24.98 ?  62  VAL A CA  1 
ATOM   479  C C   . VAL A 1 62  ? 9.963   11.862  26.690  1.00 23.94 ?  62  VAL A C   1 
ATOM   480  O O   . VAL A 1 62  ? 8.915   12.504  26.564  1.00 23.24 ?  62  VAL A O   1 
ATOM   481  C CB  . VAL A 1 62  ? 10.070  10.947  24.333  1.00 27.75 ?  62  VAL A CB  1 
ATOM   482  C CG1 . VAL A 1 62  ? 11.198  11.892  23.925  1.00 27.50 ?  62  VAL A CG1 1 
ATOM   483  C CG2 . VAL A 1 62  ? 10.131  9.659   23.523  1.00 25.35 ?  62  VAL A CG2 1 
ATOM   484  N N   . PRO A 1 63  ? 10.887  12.197  27.589  1.00 25.76 ?  63  PRO A N   1 
ATOM   485  C CA  . PRO A 1 63  ? 10.673  13.337  28.489  1.00 24.12 ?  63  PRO A CA  1 
ATOM   486  C C   . PRO A 1 63  ? 10.977  14.644  27.779  1.00 25.47 ?  63  PRO A C   1 
ATOM   487  O O   . PRO A 1 63  ? 11.646  14.679  26.752  1.00 25.41 ?  63  PRO A O   1 
ATOM   488  C CB  . PRO A 1 63  ? 11.683  13.083  29.616  1.00 25.21 ?  63  PRO A CB  1 
ATOM   489  C CG  . PRO A 1 63  ? 12.841  12.410  28.895  1.00 20.56 ?  63  PRO A CG  1 
ATOM   490  C CD  . PRO A 1 63  ? 12.181  11.535  27.819  1.00 23.23 ?  63  PRO A CD  1 
ATOM   491  N N   . ALA A 1 64  ? 10.492  15.753  28.344  1.00 27.98 ?  64  ALA A N   1 
ATOM   492  C CA  . ALA A 1 64  ? 10.834  16.992  27.650  1.00 31.96 ?  64  ALA A CA  1 
ATOM   493  C C   . ALA A 1 64  ? 12.303  17.323  27.772  1.00 27.59 ?  64  ALA A C   1 
ATOM   494  O O   . ALA A 1 64  ? 12.807  18.081  26.942  1.00 30.77 ?  64  ALA A O   1 
ATOM   495  C CB  . ALA A 1 64  ? 10.050  18.187  28.146  1.00 39.21 ?  64  ALA A CB  1 
ATOM   496  N N   . GLU A 1 65  ? 12.994  16.770  28.777  1.00 28.72 ?  65  GLU A N   1 
ATOM   497  C CA  . GLU A 1 65  ? 14.438  16.946  28.861  1.00 30.07 ?  65  GLU A CA  1 
ATOM   498  C C   . GLU A 1 65  ? 15.125  16.492  27.581  1.00 28.97 ?  65  GLU A C   1 
ATOM   499  O O   . GLU A 1 65  ? 16.167  17.041  27.205  1.00 27.17 ?  65  GLU A O   1 
ATOM   500  C CB  . GLU A 1 65  ? 15.002  16.166  30.049  1.00 30.33 ?  65  GLU A CB  1 
ATOM   501  C CG  . GLU A 1 65  ? 14.776  16.812  31.402  1.00 39.12 ?  65  GLU A CG  1 
ATOM   502  C CD  . GLU A 1 65  ? 13.528  16.309  32.087  1.00 38.27 ?  65  GLU A CD  1 
ATOM   503  O OE1 . GLU A 1 65  ? 12.647  15.749  31.403  1.00 33.62 ?  65  GLU A OE1 1 
ATOM   504  O OE2 . GLU A 1 65  ? 13.413  16.493  33.313  1.00 45.97 -1 65  GLU A OE2 1 
ATOM   505  N N   . TYR A 1 66  ? 14.575  15.469  26.923  1.00 26.74 ?  66  TYR A N   1 
ATOM   506  C CA  . TYR A 1 66  ? 15.137  15.002  25.662  1.00 26.81 ?  66  TYR A CA  1 
ATOM   507  C C   . TYR A 1 66  ? 15.067  16.082  24.601  1.00 24.90 ?  66  TYR A C   1 
ATOM   508  O O   . TYR A 1 66  ? 16.049  16.351  23.902  1.00 24.72 ?  66  TYR A O   1 
ATOM   509  C CB  . TYR A 1 66  ? 14.387  13.763  25.187  1.00 26.24 ?  66  TYR A CB  1 
ATOM   510  C CG  . TYR A 1 66  ? 14.949  13.161  23.929  1.00 25.84 ?  66  TYR A CG  1 
ATOM   511  C CD1 . TYR A 1 66  ? 16.100  12.404  23.967  1.00 26.56 ?  66  TYR A CD1 1 
ATOM   512  C CD2 . TYR A 1 66  ? 14.321  13.341  22.697  1.00 24.52 ?  66  TYR A CD2 1 
ATOM   513  C CE1 . TYR A 1 66  ? 16.622  11.845  22.839  1.00 26.37 ?  66  TYR A CE1 1 
ATOM   514  C CE2 . TYR A 1 66  ? 14.846  12.778  21.552  1.00 22.65 ?  66  TYR A CE2 1 
ATOM   515  C CZ  . TYR A 1 66  ? 15.993  12.029  21.628  1.00 27.59 ?  66  TYR A CZ  1 
ATOM   516  O OH  . TYR A 1 66  ? 16.532  11.447  20.502  1.00 26.71 ?  66  TYR A OH  1 
ATOM   517  N N   . TYR A 1 67  ? 13.890  16.693  24.446  1.00 26.41 ?  67  TYR A N   1 
ATOM   518  C CA  . TYR A 1 67  ? 13.723  17.739  23.452  1.00 24.29 ?  67  TYR A CA  1 
ATOM   519  C C   . TYR A 1 67  ? 14.529  18.977  23.822  1.00 22.95 ?  67  TYR A C   1 
ATOM   520  O O   . TYR A 1 67  ? 15.093  19.643  22.946  1.00 24.74 ?  67  TYR A O   1 
ATOM   521  C CB  . TYR A 1 67  ? 12.238  18.075  23.314  1.00 29.13 ?  67  TYR A CB  1 
ATOM   522  C CG  . TYR A 1 67  ? 11.408  16.876  22.908  1.00 26.20 ?  67  TYR A CG  1 
ATOM   523  C CD1 . TYR A 1 67  ? 11.868  15.999  21.948  1.00 28.75 ?  67  TYR A CD1 1 
ATOM   524  C CD2 . TYR A 1 67  ? 10.193  16.600  23.517  1.00 34.08 ?  67  TYR A CD2 1 
ATOM   525  C CE1 . TYR A 1 67  ? 11.132  14.903  21.570  1.00 30.94 ?  67  TYR A CE1 1 
ATOM   526  C CE2 . TYR A 1 67  ? 9.448   15.496  23.144  1.00 29.84 ?  67  TYR A CE2 1 
ATOM   527  C CZ  . TYR A 1 67  ? 9.928   14.659  22.177  1.00 31.53 ?  67  TYR A CZ  1 
ATOM   528  O OH  . TYR A 1 67  ? 9.206   13.560  21.775  1.00 40.48 ?  67  TYR A OH  1 
ATOM   529  N N   . LYS A 1 68  ? 14.611  19.288  25.117  1.00 25.49 ?  68  LYS A N   1 
ATOM   530  C CA  . LYS A 1 68  ? 15.431  20.426  25.536  1.00 23.64 ?  68  LYS A CA  1 
ATOM   531  C C   . LYS A 1 68  ? 16.905  20.166  25.253  1.00 26.15 ?  68  LYS A C   1 
ATOM   532  O O   . LYS A 1 68  ? 17.627  21.071  24.810  1.00 27.76 ?  68  LYS A O   1 
ATOM   533  C CB  . LYS A 1 68  ? 15.210  20.733  27.017  1.00 29.61 ?  68  LYS A CB  1 
ATOM   534  C CG  . LYS A 1 68  ? 15.956  21.991  27.453  1.00 29.94 ?  68  LYS A CG  1 
ATOM   535  C CD  . LYS A 1 68  ? 15.967  22.203  28.946  1.00 39.05 ?  68  LYS A CD  1 
ATOM   536  C CE  . LYS A 1 68  ? 16.938  23.340  29.273  1.00 36.08 ?  68  LYS A CE  1 
ATOM   537  N NZ  . LYS A 1 68  ? 16.992  24.275  28.120  1.00 38.49 1  68  LYS A NZ  1 
ATOM   538  N N   . ALA A 1 69  ? 17.366  18.930  25.486  1.00 25.11 ?  69  ALA A N   1 
ATOM   539  C CA  . ALA A 1 69  ? 18.754  18.587  25.182  1.00 27.97 ?  69  ALA A CA  1 
ATOM   540  C C   . ALA A 1 69  ? 19.040  18.716  23.693  1.00 25.19 ?  69  ALA A C   1 
ATOM   541  O O   . ALA A 1 69  ? 20.083  19.252  23.297  1.00 24.84 ?  69  ALA A O   1 
ATOM   542  C CB  . ALA A 1 69  ? 19.074  17.176  25.670  1.00 28.78 ?  69  ALA A CB  1 
ATOM   543  N N   . VAL A 1 70  ? 18.125  18.224  22.848  1.00 23.25 ?  70  VAL A N   1 
ATOM   544  C CA  . VAL A 1 70  ? 18.244  18.426  21.400  1.00 23.14 ?  70  VAL A CA  1 
ATOM   545  C C   . VAL A 1 70  ? 18.336  19.912  21.057  1.00 21.16 ?  70  VAL A C   1 
ATOM   546  O O   . VAL A 1 70  ? 19.205  20.334  20.281  1.00 23.55 ?  70  VAL A O   1 
ATOM   547  C CB  . VAL A 1 70  ? 17.068  17.744  20.674  1.00 22.03 ?  70  VAL A CB  1 
ATOM   548  C CG1 . VAL A 1 70  ? 16.894  18.293  19.265  1.00 21.33 ?  70  VAL A CG1 1 
ATOM   549  C CG2 . VAL A 1 70  ? 17.293  16.225  20.659  1.00 22.43 ?  70  VAL A CG2 1 
ATOM   550  N N   . ALA A 1 71  ? 17.445  20.729  21.619  1.00 21.91 ?  71  ALA A N   1 
ATOM   551  C CA  . ALA A 1 71  ? 17.439  22.153  21.276  1.00 24.35 ?  71  ALA A CA  1 
ATOM   552  C C   . ALA A 1 71  ? 18.724  22.828  21.730  1.00 23.60 ?  71  ALA A C   1 
ATOM   553  O O   . ALA A 1 71  ? 19.318  23.624  20.988  1.00 26.66 ?  71  ALA A O   1 
ATOM   554  C CB  . ALA A 1 71  ? 16.229  22.856  21.894  1.00 25.22 ?  71  ALA A CB  1 
ATOM   555  N N   . ASP A 1 72  ? 19.149  22.540  22.959  1.00 23.84 ?  72  ASP A N   1 
ATOM   556  C CA  . ASP A 1 72  ? 20.369  23.139  23.498  1.00 25.09 ?  72  ASP A CA  1 
ATOM   557  C C   . ASP A 1 72  ? 21.573  22.767  22.645  1.00 23.34 ?  72  ASP A C   1 
ATOM   558  O O   . ASP A 1 72  ? 22.432  23.609  22.355  1.00 25.49 ?  72  ASP A O   1 
ATOM   559  C CB  . ASP A 1 72  ? 20.594  22.675  24.936  1.00 28.48 ?  72  ASP A CB  1 
ATOM   560  C CG  . ASP A 1 72  ? 19.577  23.226  25.917  1.00 30.75 ?  72  ASP A CG  1 
ATOM   561  O OD1 . ASP A 1 72  ? 18.875  24.206  25.607  1.00 30.82 ?  72  ASP A OD1 1 
ATOM   562  O OD2 . ASP A 1 72  ? 19.498  22.669  27.035  1.00 37.37 -1 72  ASP A OD2 1 
ATOM   563  N N   . TRP A 1 73  ? 21.646  21.501  22.238  1.00 22.68 ?  73  TRP A N   1 
ATOM   564  C CA  . TRP A 1 73  ? 22.773  21.015  21.448  1.00 23.79 ?  73  TRP A CA  1 
ATOM   565  C C   . TRP A 1 73  ? 22.839  21.724  20.108  1.00 27.59 ?  73  TRP A C   1 
ATOM   566  O O   . TRP A 1 73  ? 23.898  22.217  19.697  1.00 25.55 ?  73  TRP A O   1 
ATOM   567  C CB  . TRP A 1 73  ? 22.643  19.511  21.244  1.00 22.87 ?  73  TRP A CB  1 
ATOM   568  C CG  . TRP A 1 73  ? 23.655  18.959  20.316  1.00 24.89 ?  73  TRP A CG  1 
ATOM   569  C CD1 . TRP A 1 73  ? 23.494  18.712  18.992  1.00 23.78 ?  73  TRP A CD1 1 
ATOM   570  C CD2 . TRP A 1 73  ? 25.004  18.594  20.637  1.00 22.51 ?  73  TRP A CD2 1 
ATOM   571  N NE1 . TRP A 1 73  ? 24.653  18.198  18.461  1.00 27.31 ?  73  TRP A NE1 1 
ATOM   572  C CE2 . TRP A 1 73  ? 25.597  18.118  19.453  1.00 25.45 ?  73  TRP A CE2 1 
ATOM   573  C CE3 . TRP A 1 73  ? 25.758  18.610  21.811  1.00 24.90 ?  73  TRP A CE3 1 
ATOM   574  C CZ2 . TRP A 1 73  ? 26.914  17.664  19.403  1.00 25.53 ?  73  TRP A CZ2 1 
ATOM   575  C CZ3 . TRP A 1 73  ? 27.070  18.161  21.761  1.00 27.32 ?  73  TRP A CZ3 1 
ATOM   576  C CH2 . TRP A 1 73  ? 27.632  17.690  20.559  1.00 23.05 ?  73  TRP A CH2 1 
ATOM   577  N N   . GLU A 1 74  ? 21.700  21.791  19.419  1.00 22.81 ?  74  GLU A N   1 
ATOM   578  C CA  . GLU A 1 74  ? 21.645  22.440  18.117  1.00 25.35 ?  74  GLU A CA  1 
ATOM   579  C C   . GLU A 1 74  ? 22.091  23.889  18.214  1.00 25.47 ?  74  GLU A C   1 
ATOM   580  O O   . GLU A 1 74  ? 22.822  24.385  17.352  1.00 26.89 ?  74  GLU A O   1 
ATOM   581  C CB  . GLU A 1 74  ? 20.226  22.354  17.563  1.00 25.58 ?  74  GLU A CB  1 
ATOM   582  C CG  . GLU A 1 74  ? 19.833  20.950  17.158  1.00 25.29 ?  74  GLU A CG  1 
ATOM   583  C CD  . GLU A 1 74  ? 20.554  20.493  15.912  1.00 26.88 ?  74  GLU A CD  1 
ATOM   584  O OE1 . GLU A 1 74  ? 21.676  19.941  16.022  1.00 28.67 ?  74  GLU A OE1 1 
ATOM   585  O OE2 . GLU A 1 74  ? 19.989  20.673  14.818  1.00 29.41 -1 74  GLU A OE2 1 
ATOM   586  N N   . GLU A 1 75  ? 21.661  24.586  19.262  1.00 24.57 ?  75  GLU A N   1 
ATOM   587  C CA  . GLU A 1 75  ? 22.060  25.982  19.402  1.00 26.72 ?  75  GLU A CA  1 
ATOM   588  C C   . GLU A 1 75  ? 23.553  26.126  19.692  1.00 27.20 ?  75  GLU A C   1 
ATOM   589  O O   . GLU A 1 75  ? 24.213  26.997  19.115  1.00 28.58 ?  75  GLU A O   1 
ATOM   590  C CB  . GLU A 1 75  ? 21.245  26.665  20.492  1.00 31.59 ?  75  GLU A CB  1 
ATOM   591  C CG  . GLU A 1 75  ? 21.760  28.079  20.781  1.00 31.79 ?  75  GLU A CG  1 
ATOM   592  C CD  . GLU A 1 75  ? 21.168  28.678  22.040  1.00 35.06 ?  75  GLU A CD  1 
ATOM   593  O OE1 . GLU A 1 75  ? 21.677  29.718  22.512  1.00 40.42 ?  75  GLU A OE1 1 
ATOM   594  O OE2 . GLU A 1 75  ? 20.169  28.133  22.542  1.00 31.71 -1 75  GLU A OE2 1 
ATOM   595  N N   . ILE A 1 76  ? 24.105  25.297  20.578  1.00 28.90 ?  76  ILE A N   1 
ATOM   596  C CA  . ILE A 1 76  ? 25.505  25.466  20.972  1.00 28.53 ?  76  ILE A CA  1 
ATOM   597  C C   . ILE A 1 76  ? 26.435  25.077  19.831  1.00 30.22 ?  76  ILE A C   1 
ATOM   598  O O   . ILE A 1 76  ? 27.408  25.780  19.531  1.00 31.21 ?  76  ILE A O   1 
ATOM   599  C CB  . ILE A 1 76  ? 25.814  24.657  22.246  1.00 28.17 ?  76  ILE A CB  1 
ATOM   600  C CG1 . ILE A 1 76  ? 25.034  25.216  23.438  1.00 29.58 ?  76  ILE A CG1 1 
ATOM   601  C CG2 . ILE A 1 76  ? 27.324  24.675  22.552  1.00 32.92 ?  76  ILE A CG2 1 
ATOM   602  C CD1 . ILE A 1 76  ? 25.150  24.358  24.695  1.00 33.83 ?  76  ILE A CD1 1 
ATOM   603  N N   . GLU A 1 77  ? 26.136  23.963  19.205  1.00 30.72 ?  77  GLU A N   1 
ATOM   604  C CA  . GLU A 1 77  ? 26.999  23.474  18.119  1.00 33.24 ?  77  GLU A CA  1 
ATOM   605  C C   . GLU A 1 77  ? 26.680  24.146  16.794  1.00 32.76 ?  77  GLU A C   1 
ATOM   606  O O   . GLU A 1 77  ? 27.625  24.331  16.066  1.00 33.39 ?  77  GLU A O   1 
ATOM   607  C CB  . GLU A 1 77  ? 26.852  21.960  18.007  1.00 32.49 ?  77  GLU A CB  1 
ATOM   608  C CG  . GLU A 1 77  ? 27.483  21.232  19.174  1.00 34.41 ?  77  GLU A CG  1 
ATOM   609  C CD  . GLU A 1 77  ? 28.986  21.366  19.341  1.00 31.81 ?  77  GLU A CD  1 
ATOM   610  O OE1 . GLU A 1 77  ? 29.439  21.409  20.483  1.00 35.71 ?  77  GLU A OE1 1 
ATOM   611  O OE2 . GLU A 1 77  ? 29.699  21.421  18.333  1.00 35.45 -1 77  GLU A OE2 1 
ATOM   612  N N   . HIS A 1 78  ? 25.429  24.511  16.528  1.00 30.47 ?  78  HIS A N   1 
ATOM   613  C CA  . HIS A 1 78  ? 25.032  25.010  15.185  1.00 30.91 ?  78  HIS A CA  1 
ATOM   614  C C   . HIS A 1 78  ? 24.477  26.439  15.149  1.00 33.03 ?  78  HIS A C   1 
ATOM   615  O O   . HIS A 1 78  ? 24.217  26.906  14.058  1.00 30.09 ?  78  HIS A O   1 
ATOM   616  C CB  . HIS A 1 78  ? 24.151  23.970  14.466  1.00 33.94 ?  78  HIS A CB  1 
ATOM   617  C CG  . HIS A 1 78  ? 24.700  22.595  14.542  1.00 35.11 ?  78  HIS A CG  1 
ATOM   618  N ND1 . HIS A 1 78  ? 25.973  22.296  14.138  1.00 37.10 ?  78  HIS A ND1 1 
ATOM   619  C CD2 . HIS A 1 78  ? 24.170  21.452  15.005  1.00 32.87 ?  78  HIS A CD2 1 
ATOM   620  C CE1 . HIS A 1 78  ? 26.209  21.027  14.345  1.00 36.54 ?  78  HIS A CE1 1 
ATOM   621  N NE2 . HIS A 1 78  ? 25.118  20.493  14.865  1.00 35.43 ?  78  HIS A NE2 1 
ATOM   622  N N   . ARG A 1 79  ? 24.313  27.082  16.300  1.00 30.97 ?  79  ARG A N   1 
ATOM   623  C CA  . ARG A 1 79  ? 23.716  28.436  16.342  1.00 27.48 ?  79  ARG A CA  1 
ATOM   624  C C   . ARG A 1 79  ? 22.339  28.360  15.679  1.00 31.98 ?  79  ARG A C   1 
ATOM   625  O O   . ARG A 1 79  ? 21.978  29.273  14.957  1.00 26.02 ?  79  ARG A O   1 
ATOM   626  C CB  . ARG A 1 79  ? 24.724  29.445  15.782  1.00 30.68 ?  79  ARG A CB  1 
ATOM   627  C CG  . ARG A 1 79  ? 26.051  29.473  16.526  1.00 39.25 ?  79  ARG A CG  1 
ATOM   628  C CD  . ARG A 1 79  ? 27.210  29.961  15.679  1.00 47.68 ?  79  ARG A CD  1 
ATOM   629  N NE  . ARG A 1 79  ? 26.777  30.895  14.652  1.00 51.48 ?  79  ARG A NE  1 
ATOM   630  C CZ  . ARG A 1 79  ? 27.517  31.880  14.151  1.00 43.19 ?  79  ARG A CZ  1 
ATOM   631  N NH1 . ARG A 1 79  ? 28.752  32.070  14.579  1.00 53.79 1  79  ARG A NH1 1 
ATOM   632  N NH2 . ARG A 1 79  ? 27.014  32.674  13.225  1.00 34.03 ?  79  ARG A NH2 1 
ATOM   633  N N   . ALA A 1 80  ? 21.632  27.259  15.930  1.00 28.34 ?  80  ALA A N   1 
ATOM   634  C CA  . ALA A 1 80  ? 20.283  27.042  15.368  1.00 28.69 ?  80  ALA A CA  1 
ATOM   635  C C   . ALA A 1 80  ? 19.488  26.401  16.484  1.00 28.04 ?  80  ALA A C   1 
ATOM   636  O O   . ALA A 1 80  ? 19.963  25.463  17.042  1.00 31.64 ?  80  ALA A O   1 
ATOM   637  C CB  . ALA A 1 80  ? 20.346  26.112  14.198  1.00 27.05 ?  80  ALA A CB  1 
ATOM   638  N N   . ARG A 1 81  ? 18.315  26.902  16.769  1.00 27.60 ?  81  ARG A N   1 
ATOM   639  C CA  . ARG A 1 81  ? 17.538  26.374  17.884  1.00 27.44 ?  81  ARG A CA  1 
ATOM   640  C C   . ARG A 1 81  ? 16.127  26.025  17.454  1.00 29.19 ?  81  ARG A C   1 
ATOM   641  O O   . ARG A 1 81  ? 15.321  26.939  17.192  1.00 24.77 ?  81  ARG A O   1 
ATOM   642  C CB  . ARG A 1 81  ? 17.488  27.338  19.061  1.00 26.43 ?  81  ARG A CB  1 
ATOM   643  C CG  . ARG A 1 81  ? 17.006  26.588  20.312  1.00 28.67 ?  81  ARG A CG  1 
ATOM   644  C CD  . ARG A 1 81  ? 16.845  27.457  21.534  1.00 26.41 ?  81  ARG A CD  1 
ATOM   645  N NE  . ARG A 1 81  ? 16.253  26.689  22.633  1.00 30.90 ?  81  ARG A NE  1 
ATOM   646  C CZ  . ARG A 1 81  ? 16.948  25.925  23.469  1.00 27.02 ?  81  ARG A CZ  1 
ATOM   647  N NH1 . ARG A 1 81  ? 18.264  25.834  23.334  1.00 29.08 1  81  ARG A NH1 1 
ATOM   648  N NH2 . ARG A 1 81  ? 16.331  25.247  24.441  1.00 29.50 ?  81  ARG A NH2 1 
ATOM   649  N N   . PRO A 1 82  ? 15.774  24.746  17.410  1.00 29.16 ?  82  PRO A N   1 
ATOM   650  C CA  . PRO A 1 82  ? 14.383  24.380  17.152  1.00 24.69 ?  82  PRO A CA  1 
ATOM   651  C C   . PRO A 1 82  ? 13.524  24.628  18.376  1.00 26.03 ?  82  PRO A C   1 
ATOM   652  O O   . PRO A 1 82  ? 13.998  24.602  19.520  1.00 25.95 ?  82  PRO A O   1 
ATOM   653  C CB  . PRO A 1 82  ? 14.468  22.881  16.849  1.00 25.74 ?  82  PRO A CB  1 
ATOM   654  C CG  . PRO A 1 82  ? 15.596  22.422  17.750  1.00 21.78 ?  82  PRO A CG  1 
ATOM   655  C CD  . PRO A 1 82  ? 16.604  23.572  17.739  1.00 22.93 ?  82  PRO A CD  1 
ATOM   656  N N   . LYS A 1 83  ? 12.244  24.878  18.113  1.00 23.40 ?  83  LYS A N   1 
ATOM   657  C CA  . LYS A 1 83  ? 11.217  24.772  19.139  1.00 24.87 ?  83  LYS A CA  1 
ATOM   658  C C   . LYS A 1 83  ? 11.183  23.352  19.661  1.00 22.26 ?  83  LYS A C   1 
ATOM   659  O O   . LYS A 1 83  ? 11.153  22.406  18.869  1.00 24.99 ?  83  LYS A O   1 
ATOM   660  C CB  . LYS A 1 83  ? 9.850   25.092  18.545  1.00 28.36 ?  83  LYS A CB  1 
ATOM   661  C CG  . LYS A 1 83  ? 9.281   26.418  18.840  1.00 31.72 ?  83  LYS A CG  1 
ATOM   662  C CD  . LYS A 1 83  ? 7.829   26.450  18.364  1.00 30.64 ?  83  LYS A CD  1 
ATOM   663  C CE  . LYS A 1 83  ? 6.846   26.195  19.495  1.00 29.74 ?  83  LYS A CE  1 
ATOM   664  N NZ  . LYS A 1 83  ? 5.435   26.375  19.025  1.00 30.13 1  83  LYS A NZ  1 
ATOM   665  N N   . GLU A 1 84  ? 11.157  23.190  20.986  1.00 25.08 ?  84  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84  ? 11.078  21.835  21.522  1.00 26.82 ?  84  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84  ? 9.856   21.103  20.992  1.00 22.61 ?  84  GLU A C   1 
ATOM   668  O O   . GLU A 1 84  ? 9.895   19.878  20.822  1.00 24.28 ?  84  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84  ? 11.047  21.861  23.047  1.00 28.17 ?  84  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84  ? 12.406  22.164  23.656  1.00 26.55 ?  84  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84  ? 12.627  23.657  23.851  1.00 31.41 ?  84  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84  ? 13.512  24.018  24.650  1.00 31.01 ?  84  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84  ? 11.916  24.469  23.204  1.00 28.75 -1 84  GLU A OE2 1 
ATOM   674  N N   . ASP A 1 85  ? 8.763   21.831  20.739  1.00 23.00 ?  85  ASP A N   1 
ATOM   675  C CA  . ASP A 1 85  ? 7.537   21.216  20.232  1.00 23.76 ?  85  ASP A CA  1 
ATOM   676  C C   . ASP A 1 85  ? 7.721   20.572  18.872  1.00 25.66 ?  85  ASP A C   1 
ATOM   677  O O   . ASP A 1 85  ? 6.962   19.662  18.528  1.00 24.99 ?  85  ASP A O   1 
ATOM   678  C CB  . ASP A 1 85  ? 6.419   22.244  20.102  1.00 24.75 ?  85  ASP A CB  1 
ATOM   679  C CG  . ASP A 1 85  ? 6.181   22.997  21.370  1.00 29.69 ?  85  ASP A CG  1 
ATOM   680  O OD1 . ASP A 1 85  ? 7.136   23.656  21.857  1.00 26.56 ?  85  ASP A OD1 1 
ATOM   681  O OD2 . ASP A 1 85  ? 5.035   22.921  21.870  1.00 30.32 -1 85  ASP A OD2 1 
ATOM   682  N N   . TRP A 1 86  ? 8.674   21.054  18.080  1.00 23.92 ?  86  TRP A N   1 
ATOM   683  C CA  . TRP A 1 86  ? 8.901   20.499  16.754  1.00 22.48 ?  86  TRP A CA  1 
ATOM   684  C C   . TRP A 1 86  ? 9.501   19.111  16.808  1.00 23.94 ?  86  TRP A C   1 
ATOM   685  O O   . TRP A 1 86  ? 9.514   18.416  15.788  1.00 24.14 ?  86  TRP A O   1 
ATOM   686  C CB  . TRP A 1 86  ? 9.845   21.394  15.956  1.00 21.25 ?  86  TRP A CB  1 
ATOM   687  C CG  . TRP A 1 86  ? 9.323   22.745  15.710  1.00 20.71 ?  86  TRP A CG  1 
ATOM   688  C CD1 . TRP A 1 86  ? 8.045   23.186  15.907  1.00 23.78 ?  86  TRP A CD1 1 
ATOM   689  C CD2 . TRP A 1 86  ? 10.062  23.854  15.199  1.00 21.17 ?  86  TRP A CD2 1 
ATOM   690  N NE1 . TRP A 1 86  ? 7.949   24.515  15.552  1.00 21.90 ?  86  TRP A NE1 1 
ATOM   691  C CE2 . TRP A 1 86  ? 9.173   24.945  15.111  1.00 25.78 ?  86  TRP A CE2 1 
ATOM   692  C CE3 . TRP A 1 86  ? 11.394  24.034  14.812  1.00 24.36 ?  86  TRP A CE3 1 
ATOM   693  C CZ2 . TRP A 1 86  ? 9.575   26.197  14.657  1.00 28.94 ?  86  TRP A CZ2 1 
ATOM   694  C CZ3 . TRP A 1 86  ? 11.789  25.276  14.354  1.00 27.52 ?  86  TRP A CZ3 1 
ATOM   695  C CH2 . TRP A 1 86  ? 10.879  26.344  14.279  1.00 26.68 ?  86  TRP A CH2 1 
ATOM   696  N N   . CYS A 1 87  ? 10.018  18.708  17.958  1.00 23.94 ?  87  CYS A N   1 
ATOM   697  C CA  . CYS A 1 87  ? 10.907  17.563  18.040  1.00 23.17 ?  87  CYS A CA  1 
ATOM   698  C C   . CYS A 1 87  ? 10.115  16.303  18.347  1.00 20.47 ?  87  CYS A C   1 
ATOM   699  O O   . CYS A 1 87  ? 9.248   16.298  19.231  1.00 22.55 ?  87  CYS A O   1 
ATOM   700  C CB  . CYS A 1 87  ? 11.970  17.794  19.116  1.00 22.66 ?  87  CYS A CB  1 
ATOM   701  S SG  . CYS A 1 87  ? 13.064  19.202  18.819  1.00 23.98 ?  87  CYS A SG  1 
ATOM   702  N N   . VAL A 1 88  ? 10.439  15.224  17.635  1.00 21.95 ?  88  VAL A N   1 
ATOM   703  C CA  . VAL A 1 88  ? 9.767   13.932  17.805  1.00 21.98 ?  88  VAL A CA  1 
ATOM   704  C C   . VAL A 1 88  ? 10.818  12.840  17.844  1.00 23.32 ?  88  VAL A C   1 
ATOM   705  O O   . VAL A 1 88  ? 11.657  12.754  16.946  1.00 21.17 ?  88  VAL A O   1 
ATOM   706  C CB  . VAL A 1 88  ? 8.771   13.628  16.669  1.00 23.31 ?  88  VAL A CB  1 
ATOM   707  C CG1 . VAL A 1 88  ? 8.131   12.246  16.890  1.00 22.28 ?  88  VAL A CG1 1 
ATOM   708  C CG2 . VAL A 1 88  ? 7.701   14.692  16.578  1.00 22.16 ?  88  VAL A CG2 1 
ATOM   709  N N   . PHE A 1 89  ? 10.765  11.995  18.871  1.00 23.51 ?  89  PHE A N   1 
ATOM   710  C CA  . PHE A 1 89  ? 11.717  10.903  18.963  1.00 21.96 ?  89  PHE A CA  1 
ATOM   711  C C   . PHE A 1 89  ? 11.464  9.869   17.868  1.00 23.82 ?  89  PHE A C   1 
ATOM   712  O O   . PHE A 1 89  ? 10.314  9.504   17.576  1.00 20.31 ?  89  PHE A O   1 
ATOM   713  C CB  . PHE A 1 89  ? 11.641  10.227  20.340  1.00 24.15 ?  89  PHE A CB  1 
ATOM   714  C CG  . PHE A 1 89  ? 12.521  9.014   20.457  1.00 22.25 ?  89  PHE A CG  1 
ATOM   715  C CD1 . PHE A 1 89  ? 12.057  7.755   20.091  1.00 21.38 ?  89  PHE A CD1 1 
ATOM   716  C CD2 . PHE A 1 89  ? 13.825  9.137   20.922  1.00 23.04 ?  89  PHE A CD2 1 
ATOM   717  C CE1 . PHE A 1 89  ? 12.890  6.645   20.176  1.00 20.54 ?  89  PHE A CE1 1 
ATOM   718  C CE2 . PHE A 1 89  ? 14.662  8.033   21.019  1.00 21.72 ?  89  PHE A CE2 1 
ATOM   719  C CZ  . PHE A 1 89  ? 14.207  6.789   20.665  1.00 20.39 ?  89  PHE A CZ  1 
ATOM   720  N N   . ALA A 1 90  ? 12.555  9.405   17.262  1.00 19.60 ?  90  ALA A N   1 
ATOM   721  C CA  . ALA A 1 90  ? 12.557  8.226   16.402  1.00 25.03 ?  90  ALA A CA  1 
ATOM   722  C C   . ALA A 1 90  ? 13.772  7.379   16.745  1.00 21.75 ?  90  ALA A C   1 
ATOM   723  O O   . ALA A 1 90  ? 14.817  7.902   17.147  1.00 22.90 ?  90  ALA A O   1 
ATOM   724  C CB  . ALA A 1 90  ? 12.597  8.605   14.920  1.00 19.74 ?  90  ALA A CB  1 
ATOM   725  N N   . SER A 1 91  ? 13.643  6.064   16.598  1.00 21.61 ?  91  SER A N   1 
ATOM   726  C CA  . SER A 1 91  ? 14.781  5.239   16.993  1.00 20.61 ?  91  SER A CA  1 
ATOM   727  C C   . SER A 1 91  ? 15.899  5.245   15.956  1.00 22.85 ?  91  SER A C   1 
ATOM   728  O O   . SER A 1 91  ? 16.983  4.732   16.228  1.00 23.28 ?  91  SER A O   1 
ATOM   729  C CB  . SER A 1 91  ? 14.320  3.805   17.282  1.00 23.66 ?  91  SER A CB  1 
ATOM   730  O OG  . SER A 1 91  ? 13.821  3.193   16.110  1.00 22.11 ?  91  SER A OG  1 
ATOM   731  N N   . GLY A 1 92  ? 15.682  5.813   14.773  1.00 22.89 ?  92  GLY A N   1 
ATOM   732  C CA  . GLY A 1 92  ? 16.774  5.873   13.828  1.00 19.13 ?  92  GLY A CA  1 
ATOM   733  C C   . GLY A 1 92  ? 16.457  6.767   12.655  1.00 21.47 ?  92  GLY A C   1 
ATOM   734  O O   . GLY A 1 92  ? 15.284  6.970   12.312  1.00 20.20 ?  92  GLY A O   1 
ATOM   735  N N   . VAL A 1 93  ? 17.499  7.328   12.045  1.00 20.73 ?  93  VAL A N   1 
ATOM   736  C CA  . VAL A 1 93  ? 17.284  8.277   10.959  1.00 22.26 ?  93  VAL A CA  1 
ATOM   737  C C   . VAL A 1 93  ? 16.722  7.573   9.729   1.00 22.94 ?  93  VAL A C   1 
ATOM   738  O O   . VAL A 1 93  ? 15.749  8.034   9.120   1.00 21.75 ?  93  VAL A O   1 
ATOM   739  C CB  . VAL A 1 93  ? 18.587  9.030   10.642  1.00 21.78 ?  93  VAL A CB  1 
ATOM   740  C CG1 . VAL A 1 93  ? 18.500  9.655   9.270   1.00 25.28 ?  93  VAL A CG1 1 
ATOM   741  C CG2 . VAL A 1 93  ? 18.818  10.116  11.695  1.00 24.78 ?  93  VAL A CG2 1 
ATOM   742  N N   . VAL A 1 94  ? 17.368  6.487   9.333   1.00 23.35 ?  94  VAL A N   1 
ATOM   743  C CA  . VAL A 1 94  ? 16.950  5.750   8.115   1.00 22.95 ?  94  VAL A CA  1 
ATOM   744  C C   . VAL A 1 94  ? 15.538  5.186   8.295   1.00 23.34 ?  94  VAL A C   1 
ATOM   745  O O   . VAL A 1 94  ? 14.715  5.401   7.412   1.00 22.11 ?  94  VAL A O   1 
ATOM   746  C CB  . VAL A 1 94  ? 18.012  4.742   7.651   1.00 23.53 ?  94  VAL A CB  1 
ATOM   747  C CG1 . VAL A 1 94  ? 17.496  3.779   6.604   1.00 24.39 ?  94  VAL A CG1 1 
ATOM   748  C CG2 . VAL A 1 94  ? 19.263  5.449   7.162   1.00 23.00 ?  94  VAL A CG2 1 
ATOM   749  N N   . PRO A 1 95  ? 15.201  4.511   9.411   1.00 23.26 ?  95  PRO A N   1 
ATOM   750  C CA  . PRO A 1 95  ? 13.824  4.087   9.617   1.00 21.80 ?  95  PRO A CA  1 
ATOM   751  C C   . PRO A 1 95  ? 12.811  5.249   9.620   1.00 22.18 ?  95  PRO A C   1 
ATOM   752  O O   . PRO A 1 95  ? 11.707  5.052   9.233   1.00 20.86 ?  95  PRO A O   1 
ATOM   753  C CB  . PRO A 1 95  ? 13.850  3.370   10.972  1.00 22.51 ?  95  PRO A CB  1 
ATOM   754  C CG  . PRO A 1 95  ? 15.272  2.936   11.163  1.00 24.48 ?  95  PRO A CG  1 
ATOM   755  C CD  . PRO A 1 95  ? 16.095  3.971   10.441  1.00 22.23 ?  95  PRO A CD  1 
ATOM   756  N N   . ALA A 1 96  ? 13.235  6.436   10.041  1.00 20.71 ?  96  ALA A N   1 
ATOM   757  C CA  . ALA A 1 96  ? 12.329  7.599   10.001  1.00 21.50 ?  96  ALA A CA  1 
ATOM   758  C C   . ALA A 1 96  ? 12.045  7.974   8.542   1.00 23.71 ?  96  ALA A C   1 
ATOM   759  O O   . ALA A 1 96  ? 10.909  8.247   8.224   1.00 19.65 ?  96  ALA A O   1 
ATOM   760  C CB  . ALA A 1 96  ? 12.884  8.752   10.791  1.00 19.89 ?  96  ALA A CB  1 
ATOM   761  N N   . ILE A 1 97  ? 13.096  7.959   7.728   1.00 22.97 ?  97  ILE A N   1 
ATOM   762  C CA  . ILE A 1 97  ? 12.894  8.234   6.311   1.00 21.18 ?  97  ILE A CA  1 
ATOM   763  C C   . ILE A 1 97  ? 11.947  7.204   5.711   1.00 23.49 ?  97  ILE A C   1 
ATOM   764  O O   . ILE A 1 97  ? 10.998  7.544   4.990   1.00 21.70 ?  97  ILE A O   1 
ATOM   765  C CB  . ILE A 1 97  ? 14.244  8.247   5.573   1.00 19.81 ?  97  ILE A CB  1 
ATOM   766  C CG1 . ILE A 1 97  ? 15.150  9.342   6.126   1.00 21.65 ?  97  ILE A CG1 1 
ATOM   767  C CG2 . ILE A 1 97  ? 14.032  8.443   4.043   1.00 22.66 ?  97  ILE A CG2 1 
ATOM   768  C CD1 . ILE A 1 97  ? 16.592  9.298   5.564   1.00 21.07 ?  97  ILE A CD1 1 
ATOM   769  N N   . SER A 1 98  ? 12.200  5.929   5.999   1.00 20.09 ?  98  SER A N   1 
ATOM   770  C CA  . SER A 1 98  ? 11.326  4.861   5.531   1.00 22.14 ?  98  SER A CA  1 
ATOM   771  C C   . SER A 1 98  ? 9.870   5.133   5.897   1.00 23.11 ?  98  SER A C   1 
ATOM   772  O O   . SER A 1 98  ? 8.981   5.051   5.044   1.00 21.07 ?  98  SER A O   1 
ATOM   773  C CB  . SER A 1 98  ? 11.796  3.524   6.106   1.00 19.33 ?  98  SER A CB  1 
ATOM   774  O OG  . SER A 1 98  ? 11.166  2.427   5.482   1.00 21.60 ?  98  SER A OG  1 
ATOM   775  N N   . ALA A 1 99  ? 9.604   5.461   7.161   1.00 19.34 ?  99  ALA A N   1 
ATOM   776  C CA  . ALA A 1 99  ? 8.223   5.680   7.585   1.00 20.80 ?  99  ALA A CA  1 
ATOM   777  C C   . ALA A 1 99  ? 7.611   6.886   6.886   1.00 18.64 ?  99  ALA A C   1 
ATOM   778  O O   . ALA A 1 99  ? 6.427   6.873   6.533   1.00 21.09 ?  99  ALA A O   1 
ATOM   779  C CB  . ALA A 1 99  ? 8.149   5.854   9.109   1.00 21.44 ?  99  ALA A CB  1 
ATOM   780  N N   . MET A 1 100 ? 8.397   7.946   6.681   1.00 19.91 ?  100 MET A N   1 
ATOM   781  C CA  . MET A 1 100 ? 7.841   9.136   6.045   1.00 18.71 ?  100 MET A CA  1 
ATOM   782  C C   . MET A 1 100 ? 7.659   8.943   4.554   1.00 20.49 ?  100 MET A C   1 
ATOM   783  O O   . MET A 1 100 ? 6.797   9.592   3.960   1.00 18.35 ?  100 MET A O   1 
ATOM   784  C CB  . MET A 1 100 ? 8.722   10.349  6.352   1.00 20.83 ?  100 MET A CB  1 
ATOM   785  C CG  . MET A 1 100 ? 8.607   10.751  7.838   1.00 20.78 ?  100 MET A CG  1 
ATOM   786  S SD  . MET A 1 100 ? 9.561   12.235  8.196   1.00 23.40 ?  100 MET A SD  1 
ATOM   787  C CE  . MET A 1 100 ? 11.212  11.709  7.697   1.00 20.50 ?  100 MET A CE  1 
ATOM   788  N N   . VAL A 1 101 ? 8.464   8.078   3.935   1.00 21.12 ?  101 VAL A N   1 
ATOM   789  C CA  . VAL A 1 101 ? 8.195   7.663   2.560   1.00 21.56 ?  101 VAL A CA  1 
ATOM   790  C C   . VAL A 1 101 ? 6.813   7.023   2.469   1.00 23.41 ?  101 VAL A C   1 
ATOM   791  O O   . VAL A 1 101 ? 6.017   7.332   1.576   1.00 22.38 ?  101 VAL A O   1 
ATOM   792  C CB  . VAL A 1 101 ? 9.287   6.697   2.071   1.00 18.21 ?  101 VAL A CB  1 
ATOM   793  C CG1 . VAL A 1 101 ? 8.821   5.975   0.814   1.00 22.41 ?  101 VAL A CG1 1 
ATOM   794  C CG2 . VAL A 1 101 ? 10.603  7.436   1.812   1.00 21.52 ?  101 VAL A CG2 1 
ATOM   795  N N   . ARG A 1 102 ? 6.502   6.128   3.404   1.00 20.60 ?  102 ARG A N   1 
ATOM   796  C CA  . ARG A 1 102 ? 5.207   5.459   3.347   1.00 21.98 ?  102 ARG A CA  1 
ATOM   797  C C   . ARG A 1 102 ? 4.053   6.396   3.669   1.00 24.98 ?  102 ARG A C   1 
ATOM   798  O O   . ARG A 1 102 ? 2.951   6.230   3.127   1.00 26.19 ?  102 ARG A O   1 
ATOM   799  C CB  . ARG A 1 102 ? 5.187   4.276   4.307   1.00 20.06 ?  102 ARG A CB  1 
ATOM   800  C CG  . ARG A 1 102 ? 6.069   3.140   3.860   1.00 21.63 ?  102 ARG A CG  1 
ATOM   801  C CD  . ARG A 1 102 ? 5.770   1.906   4.704   1.00 20.02 ?  102 ARG A CD  1 
ATOM   802  N NE  . ARG A 1 102 ? 6.062   2.126   6.123   1.00 20.23 ?  102 ARG A NE  1 
ATOM   803  C CZ  . ARG A 1 102 ? 7.281   2.027   6.654   1.00 25.30 ?  102 ARG A CZ  1 
ATOM   804  N NH1 . ARG A 1 102 ? 8.327   1.705   5.888   1.00 22.12 1  102 ARG A NH1 1 
ATOM   805  N NH2 . ARG A 1 102 ? 7.459   2.253   7.945   1.00 22.61 ?  102 ARG A NH2 1 
ATOM   806  N N   . GLN A 1 103 ? 4.277   7.375   4.539   1.00 20.89 ?  103 GLN A N   1 
ATOM   807  C CA  . GLN A 1 103 ? 3.207   8.253   4.995   1.00 22.41 ?  103 GLN A CA  1 
ATOM   808  C C   . GLN A 1 103 ? 2.961   9.440   4.078   1.00 21.25 ?  103 GLN A C   1 
ATOM   809  O O   . GLN A 1 103 ? 1.819   9.899   3.965   1.00 26.36 ?  103 GLN A O   1 
ATOM   810  C CB  . GLN A 1 103 ? 3.519   8.781   6.399   1.00 24.93 ?  103 GLN A CB  1 
ATOM   811  C CG  . GLN A 1 103 ? 2.327   9.423   7.053   1.00 27.16 ?  103 GLN A CG  1 
ATOM   812  C CD  . GLN A 1 103 ? 1.367   8.384   7.539   1.00 30.06 ?  103 GLN A CD  1 
ATOM   813  O OE1 . GLN A 1 103 ? 1.777   7.440   8.210   1.00 30.71 ?  103 GLN A OE1 1 
ATOM   814  N NE2 . GLN A 1 103 ? 0.094   8.523   7.189   1.00 26.65 ?  103 GLN A NE2 1 
ATOM   815  N N   . PHE A 1 104 ? 3.994   9.958   3.427   1.00 18.77 ?  104 PHE A N   1 
ATOM   816  C CA  . PHE A 1 104 ? 3.871   11.226  2.719   1.00 21.04 ?  104 PHE A CA  1 
ATOM   817  C C   . PHE A 1 104 ? 3.993   11.101  1.208   1.00 22.54 ?  104 PHE A C   1 
ATOM   818  O O   . PHE A 1 104 ? 4.004   12.126  0.515   1.00 22.63 ?  104 PHE A O   1 
ATOM   819  C CB  . PHE A 1 104 ? 4.918   12.213  3.244   1.00 20.99 ?  104 PHE A CB  1 
ATOM   820  C CG  . PHE A 1 104 ? 4.765   12.528  4.704   1.00 21.82 ?  104 PHE A CG  1 
ATOM   821  C CD1 . PHE A 1 104 ? 3.504   12.686  5.260   1.00 26.53 ?  104 PHE A CD1 1 
ATOM   822  C CD2 . PHE A 1 104 ? 5.874   12.659  5.519   1.00 24.99 ?  104 PHE A CD2 1 
ATOM   823  C CE1 . PHE A 1 104 ? 3.348   12.971  6.608   1.00 26.24 ?  104 PHE A CE1 1 
ATOM   824  C CE2 . PHE A 1 104 ? 5.732   12.947  6.872   1.00 21.99 ?  104 PHE A CE2 1 
ATOM   825  C CZ  . PHE A 1 104 ? 4.471   13.100  7.419   1.00 22.12 ?  104 PHE A CZ  1 
ATOM   826  N N   . THR A 1 105 ? 4.113   9.886   0.678   1.00 24.54 ?  105 THR A N   1 
ATOM   827  C CA  . THR A 1 105 ? 4.087   9.643   -0.763  1.00 20.88 ?  105 THR A CA  1 
ATOM   828  C C   . THR A 1 105 ? 3.268   8.382   -1.010  1.00 21.98 ?  105 THR A C   1 
ATOM   829  O O   . THR A 1 105 ? 2.944   7.640   -0.077  1.00 24.22 ?  105 THR A O   1 
ATOM   830  C CB  . THR A 1 105 ? 5.493   9.456   -1.352  1.00 21.55 ?  105 THR A CB  1 
ATOM   831  O OG1 . THR A 1 105 ? 6.001   8.191   -0.923  1.00 20.73 ?  105 THR A OG1 1 
ATOM   832  C CG2 . THR A 1 105 ? 6.468   10.588  -0.900  1.00 17.82 ?  105 THR A CG2 1 
ATOM   833  N N   . SER A 1 106 ? 2.955   8.119   -2.303  1.00 23.99 ?  106 SER A N   1 
ATOM   834  C CA  . SER A 1 106 ? 2.212   6.927   -2.683  1.00 19.75 ?  106 SER A CA  1 
ATOM   835  C C   . SER A 1 106 ? 3.094   5.932   -3.434  1.00 20.78 ?  106 SER A C   1 
ATOM   836  O O   . SER A 1 106 ? 4.073   6.323   -4.078  1.00 21.17 ?  106 SER A O   1 
ATOM   837  C CB  . SER A 1 106 ? 0.999   7.279   -3.562  1.00 22.68 ?  106 SER A CB  1 
ATOM   838  O OG  . SER A 1 106 ? 0.194   8.268   -2.944  1.00 27.81 ?  106 SER A OG  1 
ATOM   839  N N   . PRO A 1 107 ? 2.764   4.639   -3.394  1.00 19.73 ?  107 PRO A N   1 
ATOM   840  C CA  . PRO A 1 107 ? 3.487   3.681   -4.237  1.00 24.63 ?  107 PRO A CA  1 
ATOM   841  C C   . PRO A 1 107 ? 3.546   4.165   -5.686  1.00 24.04 ?  107 PRO A C   1 
ATOM   842  O O   . PRO A 1 107 ? 2.539   4.576   -6.268  1.00 23.96 ?  107 PRO A O   1 
ATOM   843  C CB  . PRO A 1 107 ? 2.666   2.392   -4.094  1.00 23.16 ?  107 PRO A CB  1 
ATOM   844  C CG  . PRO A 1 107 ? 2.040   2.517   -2.716  1.00 21.15 ?  107 PRO A CG  1 
ATOM   845  C CD  . PRO A 1 107 ? 1.693   3.987   -2.614  1.00 22.42 ?  107 PRO A CD  1 
ATOM   846  N N   . GLY A 1 108 ? 4.753   4.170   -6.247  1.00 21.19 ?  108 GLY A N   1 
ATOM   847  C CA  . GLY A 1 108 ? 4.978   4.613   -7.607  1.00 23.00 ?  108 GLY A CA  1 
ATOM   848  C C   . GLY A 1 108 ? 5.410   6.064   -7.729  1.00 26.75 ?  108 GLY A C   1 
ATOM   849  O O   . GLY A 1 108 ? 5.913   6.464   -8.794  1.00 24.79 ?  108 GLY A O   1 
ATOM   850  N N   . ASP A 1 109 ? 5.207   6.868   -6.686  1.00 23.71 ?  109 ASP A N   1 
ATOM   851  C CA  . ASP A 1 109 ? 5.681   8.242   -6.730  1.00 20.94 ?  109 ASP A CA  1 
ATOM   852  C C   . ASP A 1 109 ? 7.198   8.266   -6.841  1.00 23.79 ?  109 ASP A C   1 
ATOM   853  O O   . ASP A 1 109 ? 7.896   7.316   -6.460  1.00 24.62 ?  109 ASP A O   1 
ATOM   854  C CB  . ASP A 1 109 ? 5.249   9.020   -5.490  1.00 21.98 ?  109 ASP A CB  1 
ATOM   855  C CG  . ASP A 1 109 ? 3.793   9.366   -5.503  1.00 23.53 ?  109 ASP A CG  1 
ATOM   856  O OD1 . ASP A 1 109 ? 3.169   9.247   -6.567  1.00 26.39 ?  109 ASP A OD1 1 
ATOM   857  O OD2 . ASP A 1 109 ? 3.277   9.767   -4.447  1.00 23.26 -1 109 ASP A OD2 1 
ATOM   858  N N   . GLN A 1 110 ? 7.708   9.381   -7.354  1.00 23.23 ?  110 GLN A N   1 
ATOM   859  C CA  . GLN A 1 110 ? 9.134   9.599   -7.496  1.00 20.71 ?  110 GLN A CA  1 
ATOM   860  C C   . GLN A 1 110 ? 9.625   10.398  -6.298  1.00 23.33 ?  110 GLN A C   1 
ATOM   861  O O   . GLN A 1 110 ? 8.902   11.242  -5.761  1.00 20.52 ?  110 GLN A O   1 
ATOM   862  C CB  . GLN A 1 110 ? 9.452   10.339  -8.803  1.00 25.33 ?  110 GLN A CB  1 
ATOM   863  C CG  . GLN A 1 110 ? 9.216   9.492   -10.057 1.00 25.68 ?  110 GLN A CG  1 
ATOM   864  C CD  . GLN A 1 110 ? 9.735   10.163  -11.309 1.00 22.88 ?  110 GLN A CD  1 
ATOM   865  O OE1 . GLN A 1 110 ? 9.203   11.177  -11.746 1.00 27.00 ?  110 GLN A OE1 1 
ATOM   866  N NE2 . GLN A 1 110 ? 10.796  9.611   -11.879 1.00 25.57 ?  110 GLN A NE2 1 
ATOM   867  N N   . ILE A 1 111 ? 10.831  10.050  -5.874  1.00 23.04 ?  111 ILE A N   1 
ATOM   868  C CA  . ILE A 1 111 ? 11.479  10.748  -4.729  1.00 22.79 ?  111 ILE A CA  1 
ATOM   869  C C   . ILE A 1 111 ? 12.861  11.207  -5.185  1.00 20.73 ?  111 ILE A C   1 
ATOM   870  O O   . ILE A 1 111 ? 13.604  10.393  -5.715  1.00 21.88 ?  111 ILE A O   1 
ATOM   871  C CB  . ILE A 1 111 ? 11.482  9.885   -3.451  1.00 22.74 ?  111 ILE A CB  1 
ATOM   872  C CG1 . ILE A 1 111 ? 10.070  9.429   -3.075  1.00 21.43 ?  111 ILE A CG1 1 
ATOM   873  C CG2 . ILE A 1 111 ? 12.147  10.622  -2.307  1.00 23.80 ?  111 ILE A CG2 1 
ATOM   874  C CD1 . ILE A 1 111 ? 9.980   8.722   -1.753  1.00 20.80 ?  111 ILE A CD1 1 
ATOM   875  N N   . LEU A 1 112 ? 13.113  12.503  -5.053  1.00 22.64 ?  112 LEU A N   1 
ATOM   876  C CA  . LEU A 1 112 ? 14.356  13.086  -5.592  1.00 24.00 ?  112 LEU A CA  1 
ATOM   877  C C   . LEU A 1 112 ? 15.545  13.008  -4.645  1.00 24.21 ?  112 LEU A C   1 
ATOM   878  O O   . LEU A 1 112 ? 15.414  13.365  -3.489  1.00 24.95 ?  112 LEU A O   1 
ATOM   879  C CB  . LEU A 1 112 ? 14.124  14.529  -6.046  1.00 21.67 ?  112 LEU A CB  1 
ATOM   880  C CG  . LEU A 1 112 ? 15.224  15.123  -6.925  1.00 25.93 ?  112 LEU A CG  1 
ATOM   881  C CD1 . LEU A 1 112 ? 14.636  16.019  -7.987  1.00 23.06 ?  112 LEU A CD1 1 
ATOM   882  C CD2 . LEU A 1 112 ? 16.222  15.904  -6.096  1.00 26.86 ?  112 LEU A CD2 1 
ATOM   883  N N   . VAL A 1 113 ? 16.660  12.573  -5.191  1.00 22.16 ?  113 VAL A N   1 
ATOM   884  C CA  . VAL A 1 113 ? 17.922  12.528  -4.440  1.00 26.18 ?  113 VAL A CA  1 
ATOM   885  C C   . VAL A 1 113 ? 18.954  13.248  -5.316  1.00 25.58 ?  113 VAL A C   1 
ATOM   886  O O   . VAL A 1 113 ? 18.636  13.574  -6.441  1.00 25.61 ?  113 VAL A O   1 
ATOM   887  C CB  . VAL A 1 113 ? 18.365  11.084  -4.134  1.00 27.68 ?  113 VAL A CB  1 
ATOM   888  C CG1 . VAL A 1 113 ? 17.348  10.314  -3.315  1.00 28.84 ?  113 VAL A CG1 1 
ATOM   889  C CG2 . VAL A 1 113 ? 18.751  10.328  -5.391  1.00 29.25 ?  113 VAL A CG2 1 
ATOM   890  N N   . GLN A 1 114 ? 20.123  13.509  -4.753  1.00 28.73 ?  114 GLN A N   1 
ATOM   891  C CA  . GLN A 1 114 ? 21.220  14.147  -5.478  1.00 27.26 ?  114 GLN A CA  1 
ATOM   892  C C   . GLN A 1 114 ? 22.368  13.145  -5.556  1.00 27.24 ?  114 GLN A C   1 
ATOM   893  O O   . GLN A 1 114 ? 23.180  13.059  -4.636  1.00 26.79 ?  114 GLN A O   1 
ATOM   894  C CB  . GLN A 1 114 ? 21.642  15.439  -4.792  1.00 26.57 ?  114 GLN A CB  1 
ATOM   895  C CG  . GLN A 1 114 ? 20.513  16.429  -4.672  1.00 26.93 ?  114 GLN A CG  1 
ATOM   896  C CD  . GLN A 1 114 ? 20.905  17.637  -3.896  1.00 29.41 ?  114 GLN A CD  1 
ATOM   897  O OE1 . GLN A 1 114 ? 21.023  17.582  -2.665  1.00 29.04 ?  114 GLN A OE1 1 
ATOM   898  N NE2 . GLN A 1 114 ? 21.107  18.754  -4.599  1.00 30.19 ?  114 GLN A NE2 1 
ATOM   899  N N   . GLU A 1 115 ? 22.446  12.397  -6.659  1.00 27.75 ?  115 GLU A N   1 
ATOM   900  C CA  . GLU A 1 115 ? 23.502  11.403  -6.781  1.00 24.80 ?  115 GLU A CA  1 
ATOM   901  C C   . GLU A 1 115 ? 24.854  12.082  -7.005  1.00 28.66 ?  115 GLU A C   1 
ATOM   902  O O   . GLU A 1 115 ? 24.923  13.172  -7.584  1.00 27.74 ?  115 GLU A O   1 
ATOM   903  C CB  . GLU A 1 115 ? 23.207  10.436  -7.920  1.00 28.59 ?  115 GLU A CB  1 
ATOM   904  C CG  . GLU A 1 115 ? 22.067  9.494   -7.625  1.00 28.52 ?  115 GLU A CG  1 
ATOM   905  C CD  . GLU A 1 115 ? 21.814  8.562   -8.784  1.00 33.16 ?  115 GLU A CD  1 
ATOM   906  O OE1 . GLU A 1 115 ? 20.778  7.873   -8.799  1.00 31.00 ?  115 GLU A OE1 1 
ATOM   907  O OE2 . GLU A 1 115 ? 22.676  8.520   -9.676  1.00 30.81 -1 115 GLU A OE2 1 
ATOM   908  N N   . PRO A 1 116 ? 25.949  11.480  -6.511  1.00 26.62 ?  116 PRO A N   1 
ATOM   909  C CA  . PRO A 1 116 ? 26.034  10.240  -5.726  1.00 27.64 ?  116 PRO A CA  1 
ATOM   910  C C   . PRO A 1 116 ? 25.635  10.466  -4.272  1.00 29.17 ?  116 PRO A C   1 
ATOM   911  O O   . PRO A 1 116 ? 26.058  11.459  -3.701  1.00 26.32 ?  116 PRO A O   1 
ATOM   912  C CB  . PRO A 1 116 ? 27.513  9.876   -5.820  1.00 28.11 ?  116 PRO A CB  1 
ATOM   913  C CG  . PRO A 1 116 ? 28.200  11.216  -5.887  1.00 27.70 ?  116 PRO A CG  1 
ATOM   914  C CD  . PRO A 1 116 ? 27.272  12.122  -6.664  1.00 30.89 ?  116 PRO A CD  1 
ATOM   915  N N   . VAL A 1 117 ? 24.733  9.625   -3.835  1.00 28.18 ?  117 VAL A N   1 
ATOM   916  C CA  . VAL A 1 117 ? 24.240  9.832   -2.475  1.00 28.77 ?  117 VAL A CA  1 
ATOM   917  C C   . VAL A 1 117 ? 24.243  8.492   -1.814  1.00 29.22 ?  117 VAL A C   1 
ATOM   918  O O   . VAL A 1 117 ? 24.207  7.446   -2.411  1.00 25.93 ?  117 VAL A O   1 
ATOM   919  C CB  . VAL A 1 117 ? 22.861  10.511  -2.390  1.00 26.77 ?  117 VAL A CB  1 
ATOM   920  C CG1 . VAL A 1 117 ? 21.709  9.559   -2.619  1.00 28.47 ?  117 VAL A CG1 1 
ATOM   921  C CG2 . VAL A 1 117 ? 22.680  11.290  -1.098  1.00 27.47 ?  117 VAL A CG2 1 
ATOM   922  N N   . TYR A 1 118 ? 24.260  8.552   -0.466  1.00 28.07 ?  118 TYR A N   1 
ATOM   923  C CA  . TYR A 1 118 ? 24.190  7.386   0.454   1.00 27.61 ?  118 TYR A CA  1 
ATOM   924  C C   . TYR A 1 118 ? 23.254  6.281   -0.022  1.00 30.33 ?  118 TYR A C   1 
ATOM   925  O O   . TYR A 1 118 ? 22.081  6.558   -0.199  1.00 24.98 ?  118 TYR A O   1 
ATOM   926  C CB  . TYR A 1 118 ? 23.636  7.897   1.785   1.00 29.02 ?  118 TYR A CB  1 
ATOM   927  C CG  . TYR A 1 118 ? 23.476  6.953   2.948   1.00 28.24 ?  118 TYR A CG  1 
ATOM   928  C CD1 . TYR A 1 118 ? 24.386  5.951   3.228   1.00 28.66 ?  118 TYR A CD1 1 
ATOM   929  C CD2 . TYR A 1 118 ? 22.423  7.127   3.825   1.00 26.17 ?  118 TYR A CD2 1 
ATOM   930  C CE1 . TYR A 1 118 ? 24.225  5.121   4.324   1.00 30.01 ?  118 TYR A CE1 1 
ATOM   931  C CE2 . TYR A 1 118 ? 22.251  6.314   4.928   1.00 28.11 ?  118 TYR A CE2 1 
ATOM   932  C CZ  . TYR A 1 118 ? 23.159  5.308   5.183   1.00 30.10 ?  118 TYR A CZ  1 
ATOM   933  O OH  . TYR A 1 118 ? 22.975  4.511   6.273   1.00 35.52 ?  118 TYR A OH  1 
ATOM   934  N N   . ASN A 1 119 ? 23.767  5.069   -0.081  1.00 25.45 ?  119 ASN A N   1 
ATOM   935  C CA  . ASN A 1 119 ? 22.998  3.904   -0.584  1.00 28.08 ?  119 ASN A CA  1 
ATOM   936  C C   . ASN A 1 119 ? 21.667  3.634   0.115   1.00 29.74 ?  119 ASN A C   1 
ATOM   937  O O   . ASN A 1 119 ? 20.752  3.157   -0.551  1.00 26.49 ?  119 ASN A O   1 
ATOM   938  C CB  . ASN A 1 119 ? 23.886  2.670   -0.583  1.00 30.29 ?  119 ASN A CB  1 
ATOM   939  C CG  . ASN A 1 119 ? 24.532  2.421   0.762   1.00 30.25 ?  119 ASN A CG  1 
ATOM   940  O OD1 . ASN A 1 119 ? 25.403  3.169   1.177   1.00 36.08 ?  119 ASN A OD1 1 
ATOM   941  N ND2 . ASN A 1 119 ? 24.109  1.383   1.458   1.00 32.33 ?  119 ASN A ND2 1 
ATOM   942  N N   . MET A 1 120 ? 21.578  3.898   1.410   1.00 29.64 ?  120 MET A N   1 
ATOM   943  C CA  . MET A 1 120 ? 20.327  3.536   2.122   1.00 24.61 ?  120 MET A CA  1 
ATOM   944  C C   . MET A 1 120 ? 19.180  4.430   1.650   1.00 26.93 ?  120 MET A C   1 
ATOM   945  O O   . MET A 1 120 ? 18.050  4.040   1.847   1.00 25.97 ?  120 MET A O   1 
ATOM   946  C CB  . MET A 1 120 ? 20.506  3.539   3.637   1.00 32.02 ?  120 MET A CB  1 
ATOM   947  C CG  . MET A 1 120 ? 21.371  2.399   4.104   1.00 26.21 ?  120 MET A CG  1 
ATOM   948  S SD  . MET A 1 120 ? 20.523  0.828   3.873   1.00 36.69 ?  120 MET A SD  1 
ATOM   949  C CE  . MET A 1 120 ? 21.920  -0.253  3.601   1.00 37.12 ?  120 MET A CE  1 
ATOM   950  N N   . PHE A 1 121 ? 19.490  5.606   1.101   1.00 24.39 ?  121 PHE A N   1 
ATOM   951  C CA  . PHE A 1 121 ? 18.430  6.379   0.459   1.00 25.86 ?  121 PHE A CA  1 
ATOM   952  C C   . PHE A 1 121 ? 17.724  5.539   -0.599  1.00 24.48 ?  121 PHE A C   1 
ATOM   953  O O   . PHE A 1 121 ? 16.489  5.475   -0.638  1.00 25.26 ?  121 PHE A O   1 
ATOM   954  C CB  . PHE A 1 121 ? 18.999  7.658   -0.177  1.00 23.45 ?  121 PHE A CB  1 
ATOM   955  C CG  . PHE A 1 121 ? 19.306  8.767   0.810   1.00 27.18 ?  121 PHE A CG  1 
ATOM   956  C CD1 . PHE A 1 121 ? 19.386  8.513   2.167   1.00 27.03 ?  121 PHE A CD1 1 
ATOM   957  C CD2 . PHE A 1 121 ? 19.541  10.058  0.362   1.00 25.57 ?  121 PHE A CD2 1 
ATOM   958  C CE1 . PHE A 1 121 ? 19.679  9.533   3.071   1.00 26.82 ?  121 PHE A CE1 1 
ATOM   959  C CE2 . PHE A 1 121 ? 19.849  11.086  1.264   1.00 25.66 ?  121 PHE A CE2 1 
ATOM   960  C CZ  . PHE A 1 121 ? 19.916  10.820  2.611   1.00 26.06 ?  121 PHE A CZ  1 
ATOM   961  N N   . TYR A 1 122 ? 18.498  4.873   -1.458  1.00 24.29 ?  122 TYR A N   1 
ATOM   962  C CA  . TYR A 1 122 ? 17.896  4.033   -2.488  1.00 28.31 ?  122 TYR A CA  1 
ATOM   963  C C   . TYR A 1 122 ? 17.155  2.856   -1.875  1.00 28.17 ?  122 TYR A C   1 
ATOM   964  O O   . TYR A 1 122 ? 16.073  2.483   -2.342  1.00 27.07 ?  122 TYR A O   1 
ATOM   965  C CB  . TYR A 1 122 ? 18.957  3.523   -3.460  1.00 23.60 ?  122 TYR A CB  1 
ATOM   966  C CG  . TYR A 1 122 ? 19.909  4.591   -3.909  1.00 27.22 ?  122 TYR A CG  1 
ATOM   967  C CD1 . TYR A 1 122 ? 19.448  5.730   -4.558  1.00 27.66 ?  122 TYR A CD1 1 
ATOM   968  C CD2 . TYR A 1 122 ? 21.268  4.460   -3.695  1.00 25.48 ?  122 TYR A CD2 1 
ATOM   969  C CE1 . TYR A 1 122 ? 20.326  6.718   -4.971  1.00 25.46 ?  122 TYR A CE1 1 
ATOM   970  C CE2 . TYR A 1 122 ? 22.157  5.444   -4.100  1.00 27.03 ?  122 TYR A CE2 1 
ATOM   971  C CZ  . TYR A 1 122 ? 21.682  6.562   -4.744  1.00 25.72 ?  122 TYR A CZ  1 
ATOM   972  O OH  . TYR A 1 122 ? 22.575  7.525   -5.143  1.00 26.69 ?  122 TYR A OH  1 
ATOM   973  N N   . SER A 1 123 ? 17.729  2.251   -0.840  1.00 27.26 ?  123 SER A N   1 
ATOM   974  C CA  . SER A 1 123 ? 17.100  1.083   -0.242  1.00 28.09 ?  123 SER A CA  1 
ATOM   975  C C   . SER A 1 123 ? 15.741  1.428   0.358   1.00 25.22 ?  123 SER A C   1 
ATOM   976  O O   . SER A 1 123 ? 14.790  0.644   0.239   1.00 26.36 ?  123 SER A O   1 
ATOM   977  C CB  . SER A 1 123 ? 18.038  0.471   0.814   1.00 26.27 ?  123 SER A CB  1 
ATOM   978  O OG  . SER A 1 123 ? 17.303  -0.280  1.762   1.00 37.65 ?  123 SER A OG  1 
ATOM   979  N N   . VAL A 1 124 ? 15.617  2.590   1.005   1.00 24.30 ?  124 VAL A N   1 
ATOM   980  C CA  . VAL A 1 124 ? 14.328  2.899   1.621   1.00 24.87 ?  124 VAL A CA  1 
ATOM   981  C C   . VAL A 1 124 ? 13.331  3.434   0.607   1.00 24.48 ?  124 VAL A C   1 
ATOM   982  O O   . VAL A 1 124 ? 12.125  3.263   0.790   1.00 24.84 ?  124 VAL A O   1 
ATOM   983  C CB  . VAL A 1 124 ? 14.454  3.876   2.804   1.00 25.18 ?  124 VAL A CB  1 
ATOM   984  C CG1 . VAL A 1 124 ? 15.379  3.298   3.857   1.00 22.83 ?  124 VAL A CG1 1 
ATOM   985  C CG2 . VAL A 1 124 ? 14.893  5.266   2.342   1.00 28.52 ?  124 VAL A CG2 1 
ATOM   986  N N   . ILE A 1 125 ? 13.790  4.117   -0.440  1.00 22.97 ?  125 ILE A N   1 
ATOM   987  C CA  . ILE A 1 125 ? 12.873  4.586   -1.479  1.00 24.46 ?  125 ILE A CA  1 
ATOM   988  C C   . ILE A 1 125 ? 12.382  3.408   -2.310  1.00 23.55 ?  125 ILE A C   1 
ATOM   989  O O   . ILE A 1 125 ? 11.174  3.148   -2.421  1.00 23.56 ?  125 ILE A O   1 
ATOM   990  C CB  . ILE A 1 125 ? 13.564  5.646   -2.357  1.00 22.28 ?  125 ILE A CB  1 
ATOM   991  C CG1 . ILE A 1 125 ? 13.836  6.902   -1.530  1.00 24.61 ?  125 ILE A CG1 1 
ATOM   992  C CG2 . ILE A 1 125 ? 12.716  5.987   -3.591  1.00 18.56 ?  125 ILE A CG2 1 
ATOM   993  C CD1 . ILE A 1 125 ? 14.702  7.913   -2.229  1.00 26.46 ?  125 ILE A CD1 1 
ATOM   994  N N   . GLU A 1 126 ? 13.321  2.667   -2.891  1.00 22.56 ?  126 GLU A N   1 
ATOM   995  C CA  . GLU A 1 126 ? 12.962  1.550   -3.759  1.00 24.51 ?  126 GLU A CA  1 
ATOM   996  C C   . GLU A 1 126 ? 12.368  0.391   -2.969  1.00 21.97 ?  126 GLU A C   1 
ATOM   997  O O   . GLU A 1 126 ? 11.419  -0.255  -3.428  1.00 23.55 ?  126 GLU A O   1 
ATOM   998  C CB  . GLU A 1 126 ? 14.191  1.106   -4.556  1.00 27.11 ?  126 GLU A CB  1 
ATOM   999  C CG  . GLU A 1 126 ? 14.667  2.179   -5.530  1.00 28.20 ?  126 GLU A CG  1 
ATOM   1000 C CD  . GLU A 1 126 ? 15.979  1.852   -6.197  1.00 26.98 ?  126 GLU A CD  1 
ATOM   1001 O OE1 . GLU A 1 126 ? 16.334  2.529   -7.188  1.00 30.16 ?  126 GLU A OE1 1 
ATOM   1002 O OE2 . GLU A 1 126 ? 16.661  0.917   -5.739  1.00 30.11 -1 126 GLU A OE2 1 
ATOM   1003 N N   . GLY A 1 127 ? 12.899  0.114   -1.778  1.00 21.86 ?  127 GLY A N   1 
ATOM   1004 C CA  . GLY A 1 127 ? 12.349  -0.964  -0.973  1.00 24.37 ?  127 GLY A CA  1 
ATOM   1005 C C   . GLY A 1 127 ? 10.893  -0.760  -0.627  1.00 21.74 ?  127 GLY A C   1 
ATOM   1006 O O   . GLY A 1 127 ? 10.154  -1.734  -0.435  1.00 20.74 ?  127 GLY A O   1 
ATOM   1007 N N   . ASN A 1 128 ? 10.464  0.503   -0.520  1.00 22.34 ?  128 ASN A N   1 
ATOM   1008 C CA  . ASN A 1 128 ? 9.070   0.822   -0.249  1.00 21.99 ?  128 ASN A CA  1 
ATOM   1009 C C   . ASN A 1 128 ? 8.260   1.017   -1.515  1.00 19.67 ?  128 ASN A C   1 
ATOM   1010 O O   . ASN A 1 128 ? 7.095   1.410   -1.423  1.00 20.63 ?  128 ASN A O   1 
ATOM   1011 C CB  . ASN A 1 128 ? 8.948   2.088   0.603   1.00 18.42 ?  128 ASN A CB  1 
ATOM   1012 C CG  . ASN A 1 128 ? 9.242   1.833   2.071   1.00 20.78 ?  128 ASN A CG  1 
ATOM   1013 O OD1 . ASN A 1 128 ? 8.580   1.027   2.715   1.00 19.14 ?  128 ASN A OD1 1 
ATOM   1014 N ND2 . ASN A 1 128 ? 10.239  2.518   2.602   1.00 22.26 ?  128 ASN A ND2 1 
ATOM   1015 N N   . GLY A 1 129 ? 8.854   0.801   -2.681  1.00 20.39 ?  129 GLY A N   1 
ATOM   1016 C CA  . GLY A 1 129 ? 8.080   0.886   -3.904  1.00 21.44 ?  129 GLY A CA  1 
ATOM   1017 C C   . GLY A 1 129 ? 7.881   2.291   -4.412  1.00 24.74 ?  129 GLY A C   1 
ATOM   1018 O O   . GLY A 1 129 ? 6.915   2.559   -5.138  1.00 22.93 ?  129 GLY A O   1 
ATOM   1019 N N   . ARG A 1 130 ? 8.768   3.203   -4.048  1.00 18.49 ?  130 ARG A N   1 
ATOM   1020 C CA  . ARG A 1 130 ? 8.837   4.501   -4.688  1.00 19.18 ?  130 ARG A CA  1 
ATOM   1021 C C   . ARG A 1 130 ? 10.018  4.489   -5.648  1.00 21.79 ?  130 ARG A C   1 
ATOM   1022 O O   . ARG A 1 130 ? 10.823  3.555   -5.655  1.00 20.91 ?  130 ARG A O   1 
ATOM   1023 C CB  . ARG A 1 130 ? 8.934   5.625   -3.655  1.00 21.55 ?  130 ARG A CB  1 
ATOM   1024 C CG  . ARG A 1 130 ? 7.586   6.048   -3.072  1.00 21.89 ?  130 ARG A CG  1 
ATOM   1025 C CD  . ARG A 1 130 ? 6.934   4.950   -2.212  1.00 22.31 ?  130 ARG A CD  1 
ATOM   1026 N NE  . ARG A 1 130 ? 5.780   5.405   -1.430  1.00 20.05 ?  130 ARG A NE  1 
ATOM   1027 C CZ  . ARG A 1 130 ? 5.029   4.598   -0.683  1.00 21.69 ?  130 ARG A CZ  1 
ATOM   1028 N NH1 . ARG A 1 130 ? 5.307   3.306   -0.640  1.00 20.39 1  130 ARG A NH1 1 
ATOM   1029 N NH2 . ARG A 1 130 ? 3.999   5.072   0.021   1.00 19.92 ?  130 ARG A NH2 1 
ATOM   1030 N N   . ARG A 1 131 ? 10.050  5.466   -6.556  1.00 23.58 ?  131 ARG A N   1 
ATOM   1031 C CA  . ARG A 1 131 ? 11.020  5.456   -7.641  1.00 21.02 ?  131 ARG A CA  1 
ATOM   1032 C C   . ARG A 1 131 ? 12.035  6.567   -7.421  1.00 22.97 ?  131 ARG A C   1 
ATOM   1033 O O   . ARG A 1 131 ? 11.658  7.724   -7.216  1.00 22.38 ?  131 ARG A O   1 
ATOM   1034 C CB  . ARG A 1 131 ? 10.333  5.612   -9.007  1.00 24.94 ?  131 ARG A CB  1 
ATOM   1035 C CG  . ARG A 1 131 ? 9.391   4.451   -9.335  1.00 29.14 ?  131 ARG A CG  1 
ATOM   1036 C CD  . ARG A 1 131 ? 8.731   4.614   -10.701 1.00 33.04 ?  131 ARG A CD  1 
ATOM   1037 N NE  . ARG A 1 131 ? 7.656   5.598   -10.656 1.00 33.65 ?  131 ARG A NE  1 
ATOM   1038 C CZ  . ARG A 1 131 ? 6.769   5.779   -11.628 1.00 38.87 ?  131 ARG A CZ  1 
ATOM   1039 N NH1 . ARG A 1 131 ? 6.833   5.044   -12.731 1.00 41.91 1  131 ARG A NH1 1 
ATOM   1040 N NH2 . ARG A 1 131 ? 5.824   6.705   -11.499 1.00 41.89 ?  131 ARG A NH2 1 
ATOM   1041 N N   . VAL A 1 132 ? 13.320  6.212   -7.455  1.00 24.80 ?  132 VAL A N   1 
ATOM   1042 C CA  . VAL A 1 132 ? 14.366  7.219   -7.342  1.00 22.15 ?  132 VAL A CA  1 
ATOM   1043 C C   . VAL A 1 132 ? 14.469  8.009   -8.641  1.00 26.50 ?  132 VAL A C   1 
ATOM   1044 O O   . VAL A 1 132 ? 14.480  7.438   -9.742  1.00 24.14 ?  132 VAL A O   1 
ATOM   1045 C CB  . VAL A 1 132 ? 15.718  6.579   -7.006  1.00 27.36 ?  132 VAL A CB  1 
ATOM   1046 C CG1 . VAL A 1 132 ? 16.785  7.683   -6.921  1.00 23.10 ?  132 VAL A CG1 1 
ATOM   1047 C CG2 . VAL A 1 132 ? 15.632  5.763   -5.710  1.00 25.07 ?  132 VAL A CG2 1 
ATOM   1048 N N   . ILE A 1 133 ? 14.524  9.330   -8.512  1.00 25.99 ?  133 ILE A N   1 
ATOM   1049 C CA  . ILE A 1 133 ? 14.915  10.232  -9.585  1.00 26.72 ?  133 ILE A CA  1 
ATOM   1050 C C   . ILE A 1 133 ? 16.009  11.125  -9.019  1.00 27.04 ?  133 ILE A C   1 
ATOM   1051 O O   . ILE A 1 133 ? 15.938  11.548  -7.859  1.00 27.03 ?  133 ILE A O   1 
ATOM   1052 C CB  . ILE A 1 133 ? 13.717  11.051  -10.121 1.00 27.08 ?  133 ILE A CB  1 
ATOM   1053 C CG1 . ILE A 1 133 ? 14.165  12.016  -11.216 1.00 29.66 ?  133 ILE A CG1 1 
ATOM   1054 C CG2 . ILE A 1 133 ? 13.006  11.812  -8.995  1.00 28.70 ?  133 ILE A CG2 1 
ATOM   1055 C CD1 . ILE A 1 133 ? 13.026  12.771  -11.865 1.00 26.47 ?  133 ILE A CD1 1 
ATOM   1056 N N   . SER A 1 134 ? 17.055  11.359  -9.801  1.00 26.62 ?  134 SER A N   1 
ATOM   1057 C CA  . SER A 1 134 ? 18.181  12.134  -9.312  1.00 26.14 ?  134 SER A CA  1 
ATOM   1058 C C   . SER A 1 134 ? 18.368  13.383  -10.159 1.00 31.64 ?  134 SER A C   1 
ATOM   1059 O O   . SER A 1 134 ? 18.226  13.346  -11.384 1.00 25.01 ?  134 SER A O   1 
ATOM   1060 C CB  . SER A 1 134 ? 19.467  11.313  -9.316  1.00 28.95 ?  134 SER A CB  1 
ATOM   1061 O OG  . SER A 1 134 ? 20.587  12.148  -9.034  1.00 30.36 ?  134 SER A OG  1 
ATOM   1062 N N   . SER A 1 135 ? 18.671  14.495  -9.497  1.00 27.82 ?  135 SER A N   1 
ATOM   1063 C CA  . SER A 1 135 ? 19.304  15.633  -10.160 1.00 29.42 ?  135 SER A CA  1 
ATOM   1064 C C   . SER A 1 135 ? 20.767  15.494  -9.753  1.00 32.10 ?  135 SER A C   1 
ATOM   1065 O O   . SER A 1 135 ? 21.171  15.888  -8.654  1.00 29.18 ?  135 SER A O   1 
ATOM   1066 C CB  . SER A 1 135 ? 18.674  16.961  -9.744  1.00 30.66 ?  135 SER A CB  1 
ATOM   1067 O OG  . SER A 1 135 ? 19.411  18.087  -10.206 1.00 30.71 ?  135 SER A OG  1 
ATOM   1068 N N   . ASP A 1 136 ? 21.547  14.851  -10.622 1.00 33.20 ?  136 ASP A N   1 
ATOM   1069 C CA  . ASP A 1 136 ? 22.915  14.511  -10.267 1.00 33.35 ?  136 ASP A CA  1 
ATOM   1070 C C   . ASP A 1 136 ? 23.684  15.771  -9.908  1.00 35.91 ?  136 ASP A C   1 
ATOM   1071 O O   . ASP A 1 136 ? 23.529  16.818  -10.543 1.00 32.10 ?  136 ASP A O   1 
ATOM   1072 C CB  . ASP A 1 136 ? 23.625  13.788  -11.422 1.00 32.84 ?  136 ASP A CB  1 
ATOM   1073 C CG  . ASP A 1 136 ? 23.102  12.387  -11.656 1.00 33.85 ?  136 ASP A CG  1 
ATOM   1074 O OD1 . ASP A 1 136 ? 22.047  12.026  -11.100 1.00 34.41 ?  136 ASP A OD1 1 
ATOM   1075 O OD2 . ASP A 1 136 ? 23.740  11.636  -12.426 1.00 40.47 -1 136 ASP A OD2 1 
ATOM   1076 N N   . LEU A 1 137 ? 24.517  15.638  -8.887  1.00 33.97 ?  137 LEU A N   1 
ATOM   1077 C CA  . LEU A 1 137 ? 25.436  16.728  -8.584  1.00 31.81 ?  137 LEU A CA  1 
ATOM   1078 C C   . LEU A 1 137 ? 26.483  16.717  -9.705  1.00 39.26 ?  137 LEU A C   1 
ATOM   1079 O O   . LEU A 1 137 ? 26.930  15.640  -10.095 1.00 39.84 ?  137 LEU A O   1 
ATOM   1080 C CB  . LEU A 1 137 ? 26.025  16.487  -7.199  1.00 36.85 ?  137 LEU A CB  1 
ATOM   1081 C CG  . LEU A 1 137 ? 25.040  16.539  -6.041  1.00 29.55 ?  137 LEU A CG  1 
ATOM   1082 C CD1 . LEU A 1 137 ? 25.720  16.137  -4.747  1.00 32.56 ?  137 LEU A CD1 1 
ATOM   1083 C CD2 . LEU A 1 137 ? 24.434  17.924  -5.924  1.00 31.38 ?  137 LEU A CD2 1 
ATOM   1084 N N   . ILE A 1 138 ? 26.815  17.891  -10.229 1.00 42.82 ?  138 ILE A N   1 
ATOM   1085 C CA  . ILE A 1 138 ? 27.783  18.028  -11.345 1.00 44.00 ?  138 ILE A CA  1 
ATOM   1086 C C   . ILE A 1 138 ? 29.202  17.861  -10.820 1.00 49.02 ?  138 ILE A C   1 
ATOM   1087 O O   . ILE A 1 138 ? 29.598  18.679  -9.988  1.00 50.32 ?  138 ILE A O   1 
ATOM   1088 C CB  . ILE A 1 138 ? 27.617  19.424  -11.972 1.00 47.82 ?  138 ILE A CB  1 
ATOM   1089 C CG1 . ILE A 1 138 ? 26.148  19.755  -12.247 1.00 45.50 ?  138 ILE A CG1 1 
ATOM   1090 C CG2 . ILE A 1 138 ? 28.459  19.549  -13.228 1.00 51.72 ?  138 ILE A CG2 1 
ATOM   1091 C CD1 . ILE A 1 138 ? 25.914  21.198  -12.607 1.00 45.15 ?  138 ILE A CD1 1 
ATOM   1092 N N   . TYR A 1 139 ? 29.922  16.846  -11.301 1.00 49.95 ?  139 TYR A N   1 
ATOM   1093 C CA  . TYR A 1 139 ? 31.355  16.667  -10.938 1.00 55.28 ?  139 TYR A CA  1 
ATOM   1094 C C   . TYR A 1 139 ? 32.205  17.266  -12.070 1.00 59.68 ?  139 TYR A C   1 
ATOM   1095 O O   . TYR A 1 139 ? 32.924  16.534  -12.756 1.00 61.75 ?  139 TYR A O   1 
ATOM   1096 C CB  . TYR A 1 139 ? 31.706  15.212  -10.618 1.00 51.19 ?  139 TYR A CB  1 
ATOM   1097 C CG  . TYR A 1 139 ? 33.089  15.007  -10.054 1.00 50.41 ?  139 TYR A CG  1 
ATOM   1098 C CD1 . TYR A 1 139 ? 33.491  15.643  -8.895  1.00 52.01 ?  139 TYR A CD1 1 
ATOM   1099 C CD2 . TYR A 1 139 ? 34.010  14.192  -10.689 1.00 50.58 ?  139 TYR A CD2 1 
ATOM   1100 C CE1 . TYR A 1 139 ? 34.759  15.469  -8.373  1.00 51.64 ?  139 TYR A CE1 1 
ATOM   1101 C CE2 . TYR A 1 139 ? 35.284  14.006  -10.184 1.00 47.01 ?  139 TYR A CE2 1 
ATOM   1102 C CZ  . TYR A 1 139 ? 35.661  14.646  -9.018  1.00 52.66 ?  139 TYR A CZ  1 
ATOM   1103 O OH  . TYR A 1 139 ? 36.913  14.472  -8.505  1.00 54.82 ?  139 TYR A OH  1 
ATOM   1104 N N   . GLU A 1 140 ? 32.344  18.598  -12.036 1.00 61.00 ?  140 GLU A N   1 
ATOM   1105 C CA  . GLU A 1 140 ? 33.057  19.364  -13.099 1.00 63.26 ?  140 GLU A CA  1 
ATOM   1106 C C   . GLU A 1 140 ? 34.486  19.722  -12.699 1.00 68.78 ?  140 GLU A C   1 
ATOM   1107 O O   . GLU A 1 140 ? 35.365  19.695  -13.598 1.00 67.50 ?  140 GLU A O   1 
ATOM   1108 C CB  . GLU A 1 140 ? 32.370  20.706  -13.321 1.00 57.89 ?  140 GLU A CB  1 
ATOM   1109 C CG  . GLU A 1 140 ? 31.716  20.883  -14.680 1.00 60.35 ?  140 GLU A CG  1 
ATOM   1110 C CD  . GLU A 1 140 ? 31.231  22.302  -14.943 1.00 54.70 ?  140 GLU A CD  1 
ATOM   1111 O OE1 . GLU A 1 140 ? 31.229  22.720  -16.115 1.00 55.85 ?  140 GLU A OE1 1 
ATOM   1112 O OE2 . GLU A 1 140 ? 30.864  22.989  -13.973 1.00 55.35 -1 140 GLU A OE2 1 
ATOM   1113 N N   . ASN A 1 141 ? 34.722  20.144  -11.458 1.00 66.05 ?  141 ASN A N   1 
ATOM   1114 C CA  . ASN A 1 141 ? 36.145  20.378  -11.108 1.00 68.40 ?  141 ASN A CA  1 
ATOM   1115 C C   . ASN A 1 141 ? 36.597  19.205  -10.255 1.00 66.18 ?  141 ASN A C   1 
ATOM   1116 O O   . ASN A 1 141 ? 36.570  18.063  -10.757 1.00 65.35 ?  141 ASN A O   1 
ATOM   1117 C CB  . ASN A 1 141 ? 36.340  21.659  -10.314 1.00 64.02 ?  141 ASN A CB  1 
ATOM   1118 C CG  . ASN A 1 141 ? 35.693  22.859  -10.963 1.00 64.76 ?  141 ASN A CG  1 
ATOM   1119 O OD1 . ASN A 1 141 ? 35.805  23.054  -12.171 1.00 63.31 ?  141 ASN A OD1 1 
ATOM   1120 N ND2 . ASN A 1 141 ? 35.017  23.669  -10.166 1.00 77.68 ?  141 ASN A ND2 1 
ATOM   1121 N N   . SER A 1 142 ? 37.095  19.495  -9.071  1.00 63.35 ?  142 SER A N   1 
ATOM   1122 C CA  . SER A 1 142 ? 37.423  18.448  -8.085  1.00 63.91 ?  142 SER A CA  1 
ATOM   1123 C C   . SER A 1 142 ? 36.303  18.736  -7.108  1.00 61.60 ?  142 SER A C   1 
ATOM   1124 O O   . SER A 1 142 ? 36.529  18.741  -5.896  1.00 58.43 ?  142 SER A O   1 
ATOM   1125 C CB  . SER A 1 142 ? 38.781  18.713  -7.507  1.00 62.27 ?  142 SER A CB  1 
ATOM   1126 O OG  . SER A 1 142 ? 39.001  17.968  -6.321  1.00 62.66 ?  142 SER A OG  1 
ATOM   1127 N N   . LYS A 1 143 ? 35.113  18.928  -7.667  1.00 58.63 ?  143 LYS A N   1 
ATOM   1128 C CA  . LYS A 1 143 ? 34.014  19.447  -6.869  1.00 58.62 ?  143 LYS A CA  1 
ATOM   1129 C C   . LYS A 1 143 ? 32.681  18.952  -7.412  1.00 57.10 ?  143 LYS A C   1 
ATOM   1130 O O   . LYS A 1 143 ? 32.558  18.566  -8.579  1.00 57.04 ?  143 LYS A O   1 
ATOM   1131 C CB  . LYS A 1 143 ? 34.012  20.980  -6.851  1.00 61.65 ?  143 LYS A CB  1 
ATOM   1132 C CG  . LYS A 1 143 ? 35.065  21.611  -5.953  1.00 62.86 ?  143 LYS A CG  1 
ATOM   1133 C CD  . LYS A 1 143 ? 35.316  23.057  -6.347  1.00 65.00 ?  143 LYS A CD  1 
ATOM   1134 C CE  . LYS A 1 143 ? 36.799  23.323  -6.539  1.00 58.58 ?  143 LYS A CE  1 
ATOM   1135 N NZ  . LYS A 1 143 ? 37.424  22.361  -7.490  1.00 60.18 1  143 LYS A NZ  1 
ATOM   1136 N N   . TYR A 1 144 ? 31.676  18.999  -6.539  1.00 50.64 ?  144 TYR A N   1 
ATOM   1137 C CA  . TYR A 1 144 ? 30.293  18.692  -6.871  1.00 47.48 ?  144 TYR A CA  1 
ATOM   1138 C C   . TYR A 1 144 ? 29.454  19.952  -6.716  1.00 49.46 ?  144 TYR A C   1 
ATOM   1139 O O   . TYR A 1 144 ? 29.622  20.707  -5.750  1.00 40.44 ?  144 TYR A O   1 
ATOM   1140 C CB  . TYR A 1 144 ? 29.731  17.591  -5.962  1.00 44.29 ?  144 TYR A CB  1 
ATOM   1141 C CG  . TYR A 1 144 ? 30.294  16.214  -6.206  1.00 40.79 ?  144 TYR A CG  1 
ATOM   1142 C CD1 . TYR A 1 144 ? 31.443  15.785  -5.549  1.00 42.62 ?  144 TYR A CD1 1 
ATOM   1143 C CD2 . TYR A 1 144 ? 29.673  15.333  -7.082  1.00 42.78 ?  144 TYR A CD2 1 
ATOM   1144 C CE1 . TYR A 1 144 ? 31.956  14.523  -5.765  1.00 38.65 ?  144 TYR A CE1 1 
ATOM   1145 C CE2 . TYR A 1 144 ? 30.181  14.068  -7.298  1.00 41.23 ?  144 TYR A CE2 1 
ATOM   1146 C CZ  . TYR A 1 144 ? 31.325  13.671  -6.641  1.00 39.10 ?  144 TYR A CZ  1 
ATOM   1147 O OH  . TYR A 1 144 ? 31.832  12.414  -6.860  1.00 40.14 ?  144 TYR A OH  1 
ATOM   1148 N N   . SER A 1 145 ? 28.543  20.177  -7.658  1.00 41.50 ?  145 SER A N   1 
ATOM   1149 C CA  . SER A 1 145 ? 27.653  21.323  -7.550  1.00 44.17 ?  145 SER A CA  1 
ATOM   1150 C C   . SER A 1 145 ? 26.287  20.969  -8.123  1.00 36.33 ?  145 SER A C   1 
ATOM   1151 O O   . SER A 1 145 ? 26.118  19.971  -8.828  1.00 40.68 ?  145 SER A O   1 
ATOM   1152 C CB  . SER A 1 145 ? 28.237  22.554  -8.248  1.00 43.50 ?  145 SER A CB  1 
ATOM   1153 O OG  . SER A 1 145 ? 27.886  22.572  -9.619  1.00 46.72 ?  145 SER A OG  1 
ATOM   1154 N N   . VAL A 1 146 ? 25.314  21.821  -7.810  1.00 37.06 ?  146 VAL A N   1 
ATOM   1155 C CA  . VAL A 1 146 ? 23.902  21.599  -8.114  1.00 36.52 ?  146 VAL A CA  1 
ATOM   1156 C C   . VAL A 1 146 ? 23.559  22.248  -9.446  1.00 36.54 ?  146 VAL A C   1 
ATOM   1157 O O   . VAL A 1 146 ? 23.880  23.421  -9.670  1.00 40.51 ?  146 VAL A O   1 
ATOM   1158 C CB  . VAL A 1 146 ? 23.012  22.176  -6.999  1.00 36.42 ?  146 VAL A CB  1 
ATOM   1159 C CG1 . VAL A 1 146 ? 21.528  22.040  -7.349  1.00 34.53 ?  146 VAL A CG1 1 
ATOM   1160 C CG2 . VAL A 1 146 ? 23.334  21.524  -5.673  1.00 31.60 ?  146 VAL A CG2 1 
ATOM   1161 N N   . ASN A 1 147 ? 22.882  21.499  -10.316 1.00 38.44 ?  147 ASN A N   1 
ATOM   1162 C CA  . ASN A 1 147 ? 22.244  22.048  -11.514 1.00 37.05 ?  147 ASN A CA  1 
ATOM   1163 C C   . ASN A 1 147 ? 20.877  22.579  -11.096 1.00 34.98 ?  147 ASN A C   1 
ATOM   1164 O O   . ASN A 1 147 ? 19.882  21.853  -11.060 1.00 31.93 ?  147 ASN A O   1 
ATOM   1165 C CB  . ASN A 1 147 ? 22.130  20.985  -12.602 1.00 37.54 ?  147 ASN A CB  1 
ATOM   1166 C CG  . ASN A 1 147 ? 21.689  21.558  -13.937 1.00 39.02 ?  147 ASN A CG  1 
ATOM   1167 O OD1 . ASN A 1 147 ? 21.014  22.588  -13.999 1.00 40.04 ?  147 ASN A OD1 1 
ATOM   1168 N ND2 . ASN A 1 147 ? 22.057  20.879  -15.016 1.00 40.32 ?  147 ASN A ND2 1 
ATOM   1169 N N   . TRP A 1 148 ? 20.829  23.870  -10.769 1.00 32.87 ?  148 TRP A N   1 
ATOM   1170 C CA  . TRP A 1 148 ? 19.596  24.439  -10.239 1.00 35.12 ?  148 TRP A CA  1 
ATOM   1171 C C   . TRP A 1 148 ? 18.465  24.376  -11.255 1.00 35.70 ?  148 TRP A C   1 
ATOM   1172 O O   . TRP A 1 148 ? 17.302  24.201  -10.873 1.00 33.65 ?  148 TRP A O   1 
ATOM   1173 C CB  . TRP A 1 148 ? 19.848  25.868  -9.765  1.00 35.00 ?  148 TRP A CB  1 
ATOM   1174 C CG  . TRP A 1 148 ? 20.848  25.891  -8.639  1.00 37.38 ?  148 TRP A CG  1 
ATOM   1175 C CD1 . TRP A 1 148 ? 22.170  26.229  -8.717  1.00 39.84 ?  148 TRP A CD1 1 
ATOM   1176 C CD2 . TRP A 1 148 ? 20.610  25.513  -7.272  1.00 35.09 ?  148 TRP A CD2 1 
ATOM   1177 N NE1 . TRP A 1 148 ? 22.765  26.097  -7.481  1.00 35.47 ?  148 TRP A NE1 1 
ATOM   1178 C CE2 . TRP A 1 148 ? 21.829  25.661  -6.578  1.00 34.85 ?  148 TRP A CE2 1 
ATOM   1179 C CE3 . TRP A 1 148 ? 19.485  25.071  -6.570  1.00 35.83 ?  148 TRP A CE3 1 
ATOM   1180 C CZ2 . TRP A 1 148 ? 21.951  25.377  -5.218  1.00 36.89 ?  148 TRP A CZ2 1 
ATOM   1181 C CZ3 . TRP A 1 148 ? 19.606  24.797  -5.218  1.00 32.91 ?  148 TRP A CZ3 1 
ATOM   1182 C CH2 . TRP A 1 148 ? 20.828  24.956  -4.556  1.00 33.00 ?  148 TRP A CH2 1 
ATOM   1183 N N   . ALA A 1 149 ? 18.781  24.492  -12.547 1.00 33.64 ?  149 ALA A N   1 
ATOM   1184 C CA  . ALA A 1 149 ? 17.744  24.347  -13.561 1.00 34.23 ?  149 ALA A CA  1 
ATOM   1185 C C   . ALA A 1 149 ? 17.195  22.930  -13.566 1.00 35.54 ?  149 ALA A C   1 
ATOM   1186 O O   . ALA A 1 149 ? 15.976  22.721  -13.537 1.00 32.26 ?  149 ALA A O   1 
ATOM   1187 C CB  . ALA A 1 149 ? 18.292  24.715  -14.944 1.00 34.56 ?  149 ALA A CB  1 
ATOM   1188 N N   . ASP A 1 150 ? 18.089  21.943  -13.607 1.00 34.56 ?  150 ASP A N   1 
ATOM   1189 C CA  . ASP A 1 150 ? 17.658  20.554  -13.636 1.00 34.25 ?  150 ASP A CA  1 
ATOM   1190 C C   . ASP A 1 150 ? 16.937  20.174  -12.349 1.00 33.14 ?  150 ASP A C   1 
ATOM   1191 O O   . ASP A 1 150 ? 15.921  19.469  -12.381 1.00 32.36 ?  150 ASP A O   1 
ATOM   1192 C CB  . ASP A 1 150 ? 18.866  19.656  -13.871 1.00 29.14 ?  150 ASP A CB  1 
ATOM   1193 C CG  . ASP A 1 150 ? 18.501  18.205  -13.925 1.00 37.48 ?  150 ASP A CG  1 
ATOM   1194 O OD1 . ASP A 1 150 ? 17.817  17.813  -14.901 1.00 33.04 ?  150 ASP A OD1 1 
ATOM   1195 O OD2 . ASP A 1 150 ? 18.896  17.468  -12.990 1.00 33.37 -1 150 ASP A OD2 1 
ATOM   1196 N N   . LEU A 1 151 ? 17.436  20.641  -11.210 1.00 31.84 ?  151 LEU A N   1 
ATOM   1197 C CA  . LEU A 1 151 ? 16.779  20.317  -9.949  1.00 34.25 ?  151 LEU A CA  1 
ATOM   1198 C C   . LEU A 1 151 ? 15.338  20.827  -9.933  1.00 29.94 ?  151 LEU A C   1 
ATOM   1199 O O   . LEU A 1 151 ? 14.414  20.090  -9.576  1.00 26.54 ?  151 LEU A O   1 
ATOM   1200 C CB  . LEU A 1 151 ? 17.584  20.881  -8.781  1.00 30.98 ?  151 LEU A CB  1 
ATOM   1201 C CG  . LEU A 1 151 ? 16.993  20.742  -7.374  1.00 30.22 ?  151 LEU A CG  1 
ATOM   1202 C CD1 . LEU A 1 151 ? 16.872  19.281  -6.933  1.00 25.66 ?  151 LEU A CD1 1 
ATOM   1203 C CD2 . LEU A 1 151 ? 17.810  21.541  -6.366  1.00 29.38 ?  151 LEU A CD2 1 
ATOM   1204 N N   . GLU A 1 152 ? 15.117  22.076  -10.354 1.00 29.77 ?  152 GLU A N   1 
ATOM   1205 C CA  . GLU A 1 152 ? 13.775  22.645  -10.248 1.00 28.92 ?  152 GLU A CA  1 
ATOM   1206 C C   . GLU A 1 152 ? 12.783  21.933  -11.151 1.00 30.27 ?  152 GLU A C   1 
ATOM   1207 O O   . GLU A 1 152 ? 11.630  21.698  -10.764 1.00 29.45 ?  152 GLU A O   1 
ATOM   1208 C CB  . GLU A 1 152 ? 13.790  24.134  -10.583 1.00 34.13 ?  152 GLU A CB  1 
ATOM   1209 C CG  . GLU A 1 152 ? 12.389  24.703  -10.724 1.00 36.64 ?  152 GLU A CG  1 
ATOM   1210 C CD  . GLU A 1 152 ? 12.311  26.170  -10.389 1.00 35.47 ?  152 GLU A CD  1 
ATOM   1211 O OE1 . GLU A 1 152 ? 11.260  26.610  -9.873  1.00 36.26 ?  152 GLU A OE1 1 
ATOM   1212 O OE2 . GLU A 1 152 ? 13.298  26.884  -10.651 1.00 38.64 -1 152 GLU A OE2 1 
ATOM   1213 N N   . GLU A 1 153 ? 13.199  21.612  -12.372 1.00 29.40 ?  153 GLU A N   1 
ATOM   1214 C CA  . GLU A 1 153 ? 12.285  20.985  -13.316 1.00 31.16 ?  153 GLU A CA  1 
ATOM   1215 C C   . GLU A 1 153 ? 11.898  19.596  -12.852 1.00 30.65 ?  153 GLU A C   1 
ATOM   1216 O O   . GLU A 1 153 ? 10.767  19.153  -13.073 1.00 29.95 ?  153 GLU A O   1 
ATOM   1217 C CB  . GLU A 1 153 ? 12.934  20.910  -14.691 1.00 38.16 ?  153 GLU A CB  1 
ATOM   1218 C CG  . GLU A 1 153 ? 13.262  22.258  -15.233 1.00 46.49 ?  153 GLU A CG  1 
ATOM   1219 C CD  . GLU A 1 153 ? 14.135  22.172  -16.417 1.00 54.29 ?  153 GLU A CD  1 
ATOM   1220 O OE1 . GLU A 1 153 ? 14.732  21.093  -16.680 1.00 64.41 ?  153 GLU A OE1 1 
ATOM   1221 O OE2 . GLU A 1 153 ? 14.243  23.202  -17.157 1.00 56.79 -1 153 GLU A OE2 1 
ATOM   1222 N N   . LYS A 1 154 ? 12.825  18.891  -12.200 1.00 27.59 ?  154 LYS A N   1 
ATOM   1223 C CA  . LYS A 1 154 ? 12.464  17.602  -11.629 1.00 28.28 ?  154 LYS A CA  1 
ATOM   1224 C C   . LYS A 1 154 ? 11.574  17.788  -10.411 1.00 29.14 ?  154 LYS A C   1 
ATOM   1225 O O   . LYS A 1 154 ? 10.549  17.107  -10.285 1.00 28.83 ?  154 LYS A O   1 
ATOM   1226 C CB  . LYS A 1 154 ? 13.723  16.799  -11.312 1.00 31.53 ?  154 LYS A CB  1 
ATOM   1227 C CG  . LYS A 1 154 ? 14.386  16.272  -12.588 1.00 33.53 ?  154 LYS A CG  1 
ATOM   1228 C CD  . LYS A 1 154 ? 15.807  15.756  -12.369 1.00 30.22 ?  154 LYS A CD  1 
ATOM   1229 C CE  . LYS A 1 154 ? 16.336  15.114  -13.659 1.00 34.77 ?  154 LYS A CE  1 
ATOM   1230 N NZ  . LYS A 1 154 ? 17.782  14.748  -13.548 1.00 34.72 1  154 LYS A NZ  1 
ATOM   1231 N N   . LEU A 1 155 ? 11.900  18.760  -9.543  1.00 26.58 ?  155 LEU A N   1 
ATOM   1232 C CA  . LEU A 1 155 ? 11.031  19.039  -8.404  1.00 30.14 ?  155 LEU A CA  1 
ATOM   1233 C C   . LEU A 1 155 ? 9.632   19.414  -8.861  1.00 32.76 ?  155 LEU A C   1 
ATOM   1234 O O   . LEU A 1 155 ? 8.646   19.054  -8.202  1.00 27.91 ?  155 LEU A O   1 
ATOM   1235 C CB  . LEU A 1 155 ? 11.614  20.161  -7.537  1.00 26.23 ?  155 LEU A CB  1 
ATOM   1236 C CG  . LEU A 1 155 ? 12.866  19.797  -6.732  1.00 25.77 ?  155 LEU A CG  1 
ATOM   1237 C CD1 . LEU A 1 155 ? 13.428  21.029  -6.033  1.00 29.01 ?  155 LEU A CD1 1 
ATOM   1238 C CD2 . LEU A 1 155 ? 12.575  18.669  -5.727  1.00 23.60 ?  155 LEU A CD2 1 
ATOM   1239 N N   . ALA A 1 156 ? 9.530   20.119  -9.995  1.00 29.90 ?  156 ALA A N   1 
ATOM   1240 C CA  . ALA A 1 156 ? 8.259   20.561  -10.551 1.00 31.16 ?  156 ALA A CA  1 
ATOM   1241 C C   . ALA A 1 156 ? 7.486   19.446  -11.230 1.00 27.43 ?  156 ALA A C   1 
ATOM   1242 O O   . ALA A 1 156 ? 6.310   19.650  -11.557 1.00 30.12 ?  156 ALA A O   1 
ATOM   1243 C CB  . ALA A 1 156 ? 8.476   21.694  -11.559 1.00 28.53 ?  156 ALA A CB  1 
ATOM   1244 N N   . THR A 1 157 ? 8.115   18.306  -11.477 1.00 25.43 ?  157 THR A N   1 
ATOM   1245 C CA  . THR A 1 157 ? 7.400   17.177  -12.052 1.00 30.44 ?  157 THR A CA  1 
ATOM   1246 C C   . THR A 1 157 ? 6.318   16.725  -11.078 1.00 29.52 ?  157 THR A C   1 
ATOM   1247 O O   . THR A 1 157 ? 6.609   16.538  -9.885  1.00 25.38 ?  157 THR A O   1 
ATOM   1248 C CB  . THR A 1 157 ? 8.361   16.031  -12.350 1.00 30.41 ?  157 THR A CB  1 
ATOM   1249 O OG1 . THR A 1 157 ? 9.421   16.512  -13.190 1.00 35.40 ?  157 THR A OG1 1 
ATOM   1250 C CG2 . THR A 1 157 ? 7.634   14.912  -13.054 1.00 31.65 ?  157 THR A CG2 1 
ATOM   1251 N N   . PRO A 1 158 ? 5.066   16.570  -11.527 1.00 25.70 ?  158 PRO A N   1 
ATOM   1252 C CA  . PRO A 1 158 ? 3.990   16.280  -10.569 1.00 26.95 ?  158 PRO A CA  1 
ATOM   1253 C C   . PRO A 1 158 ? 4.207   15.004  -9.778  1.00 26.81 ?  158 PRO A C   1 
ATOM   1254 O O   . PRO A 1 158 ? 3.829   14.962  -8.602  1.00 25.74 ?  158 PRO A O   1 
ATOM   1255 C CB  . PRO A 1 158 ? 2.744   16.190  -11.459 1.00 25.19 ?  158 PRO A CB  1 
ATOM   1256 C CG  . PRO A 1 158 ? 3.075   17.026  -12.654 1.00 27.67 ?  158 PRO A CG  1 
ATOM   1257 C CD  . PRO A 1 158 ? 4.543   16.813  -12.886 1.00 29.71 ?  158 PRO A CD  1 
ATOM   1258 N N   . SER A 1 159 ? 4.780   13.958  -10.390 1.00 22.53 ?  159 SER A N   1 
ATOM   1259 C CA  . SER A 1 159 ? 4.993   12.700  -9.685  1.00 24.92 ?  159 SER A CA  1 
ATOM   1260 C C   . SER A 1 159 ? 6.149   12.769  -8.691  1.00 24.82 ?  159 SER A C   1 
ATOM   1261 O O   . SER A 1 159 ? 6.293   11.856  -7.872  1.00 22.31 ?  159 SER A O   1 
ATOM   1262 C CB  . SER A 1 159 ? 5.231   11.560  -10.685 1.00 24.50 ?  159 SER A CB  1 
ATOM   1263 O OG  . SER A 1 159 ? 6.340   11.849  -11.528 1.00 27.23 ?  159 SER A OG  1 
ATOM   1264 N N   . VAL A 1 160 ? 6.968   13.816  -8.732  1.00 24.36 ?  160 VAL A N   1 
ATOM   1265 C CA  . VAL A 1 160 ? 8.031   13.990  -7.743  1.00 22.02 ?  160 VAL A CA  1 
ATOM   1266 C C   . VAL A 1 160 ? 7.420   14.623  -6.494  1.00 24.61 ?  160 VAL A C   1 
ATOM   1267 O O   . VAL A 1 160 ? 6.998   15.783  -6.505  1.00 24.02 ?  160 VAL A O   1 
ATOM   1268 C CB  . VAL A 1 160 ? 9.179   14.832  -8.300  1.00 23.90 ?  160 VAL A CB  1 
ATOM   1269 C CG1 . VAL A 1 160 ? 10.193  15.115  -7.214  1.00 22.86 ?  160 VAL A CG1 1 
ATOM   1270 C CG2 . VAL A 1 160 ? 9.833   14.086  -9.456  1.00 21.80 ?  160 VAL A CG2 1 
ATOM   1271 N N   . ARG A 1 161 ? 7.345   13.850  -5.411  1.00 24.25 ?  161 ARG A N   1 
ATOM   1272 C CA  . ARG A 1 161 ? 6.577   14.256  -4.249  1.00 24.39 ?  161 ARG A CA  1 
ATOM   1273 C C   . ARG A 1 161 ? 7.435   14.576  -3.040  1.00 23.57 ?  161 ARG A C   1 
ATOM   1274 O O   . ARG A 1 161 ? 6.928   15.159  -2.079  1.00 21.20 ?  161 ARG A O   1 
ATOM   1275 C CB  . ARG A 1 161 ? 5.578   13.157  -3.854  1.00 25.86 ?  161 ARG A CB  1 
ATOM   1276 C CG  . ARG A 1 161 ? 4.591   12.745  -4.929  1.00 26.30 ?  161 ARG A CG  1 
ATOM   1277 C CD  . ARG A 1 161 ? 3.838   13.918  -5.517  1.00 29.99 ?  161 ARG A CD  1 
ATOM   1278 N NE  . ARG A 1 161 ? 3.238   14.797  -4.517  1.00 35.15 ?  161 ARG A NE  1 
ATOM   1279 C CZ  . ARG A 1 161 ? 3.489   16.105  -4.433  1.00 35.20 ?  161 ARG A CZ  1 
ATOM   1280 N NH1 . ARG A 1 161 ? 4.337   16.678  -5.278  1.00 36.55 1  161 ARG A NH1 1 
ATOM   1281 N NH2 . ARG A 1 161 ? 2.898   16.842  -3.503  1.00 44.00 ?  161 ARG A NH2 1 
ATOM   1282 N N   . MET A 1 162 ? 8.704   14.192  -3.052  1.00 20.45 ?  162 MET A N   1 
ATOM   1283 C CA  . MET A 1 162 ? 9.541   14.281  -1.867  1.00 20.09 ?  162 MET A CA  1 
ATOM   1284 C C   . MET A 1 162 ? 10.970  14.391  -2.352  1.00 21.67 ?  162 MET A C   1 
ATOM   1285 O O   . MET A 1 162 ? 11.322  13.842  -3.400  1.00 19.69 ?  162 MET A O   1 
ATOM   1286 C CB  . MET A 1 162 ? 9.357   13.047  -0.960  1.00 20.18 ?  162 MET A CB  1 
ATOM   1287 C CG  . MET A 1 162 ? 10.271  13.017  0.270   1.00 21.84 ?  162 MET A CG  1 
ATOM   1288 S SD  . MET A 1 162 ? 10.064  11.508  1.251   1.00 21.47 ?  162 MET A SD  1 
ATOM   1289 C CE  . MET A 1 162 ? 8.540   11.937  2.106   1.00 19.18 ?  162 MET A CE  1 
ATOM   1290 N N   . MET A 1 163 ? 11.778  15.128  -1.602  1.00 24.70 ?  163 MET A N   1 
ATOM   1291 C CA  . MET A 1 163 ? 13.214  15.164  -1.810  1.00 22.92 ?  163 MET A CA  1 
ATOM   1292 C C   . MET A 1 163 ? 13.893  14.689  -0.535  1.00 23.70 ?  163 MET A C   1 
ATOM   1293 O O   . MET A 1 163 ? 13.580  15.177  0.558   1.00 22.77 ?  163 MET A O   1 
ATOM   1294 C CB  . MET A 1 163 ? 13.677  16.575  -2.182  1.00 21.95 ?  163 MET A CB  1 
ATOM   1295 C CG  . MET A 1 163 ? 15.179  16.741  -2.234  1.00 20.86 ?  163 MET A CG  1 
ATOM   1296 S SD  . MET A 1 163 ? 15.661  18.353  -2.907  1.00 26.40 ?  163 MET A SD  1 
ATOM   1297 C CE  . MET A 1 163 ? 17.430  18.098  -3.048  1.00 25.78 ?  163 MET A CE  1 
ATOM   1298 N N   . VAL A 1 164 ? 14.761  13.688  -0.667  1.00 21.24 ?  164 VAL A N   1 
ATOM   1299 C CA  . VAL A 1 164 ? 15.544  13.199  0.455   1.00 21.63 ?  164 VAL A CA  1 
ATOM   1300 C C   . VAL A 1 164 ? 16.928  13.791  0.285   1.00 25.05 ?  164 VAL A C   1 
ATOM   1301 O O   . VAL A 1 164 ? 17.641  13.479  -0.680  1.00 24.50 ?  164 VAL A O   1 
ATOM   1302 C CB  . VAL A 1 164 ? 15.578  11.669  0.544   1.00 21.05 ?  164 VAL A CB  1 
ATOM   1303 C CG1 . VAL A 1 164 ? 16.395  11.267  1.798   1.00 22.30 ?  164 VAL A CG1 1 
ATOM   1304 C CG2 . VAL A 1 164 ? 14.149  11.113  0.655   1.00 18.32 ?  164 VAL A CG2 1 
ATOM   1305 N N   . PHE A 1 165 ? 17.274  14.655  1.238   1.00 22.11 ?  165 PHE A N   1 
ATOM   1306 C CA  . PHE A 1 165 ? 18.377  15.598  1.163   1.00 22.45 ?  165 PHE A CA  1 
ATOM   1307 C C   . PHE A 1 165 ? 19.376  15.212  2.239   1.00 23.22 ?  165 PHE A C   1 
ATOM   1308 O O   . PHE A 1 165 ? 18.996  15.026  3.399   1.00 29.24 ?  165 PHE A O   1 
ATOM   1309 C CB  . PHE A 1 165 ? 17.848  17.014  1.386   1.00 22.37 ?  165 PHE A CB  1 
ATOM   1310 C CG  . PHE A 1 165 ? 18.887  18.106  1.295   1.00 25.17 ?  165 PHE A CG  1 
ATOM   1311 C CD1 . PHE A 1 165 ? 19.797  18.146  0.253   1.00 25.40 ?  165 PHE A CD1 1 
ATOM   1312 C CD2 . PHE A 1 165 ? 18.907  19.126  2.238   1.00 24.24 ?  165 PHE A CD2 1 
ATOM   1313 C CE1 . PHE A 1 165 ? 20.733  19.172  0.165   1.00 26.01 ?  165 PHE A CE1 1 
ATOM   1314 C CE2 . PHE A 1 165 ? 19.843  20.166  2.146   1.00 25.91 ?  165 PHE A CE2 1 
ATOM   1315 C CZ  . PHE A 1 165 ? 20.752  20.177  1.104   1.00 24.31 ?  165 PHE A CZ  1 
ATOM   1316 N N   . CYS A 1 166 ? 20.638  15.074  1.852   1.00 26.47 ?  166 CYS A N   1 
ATOM   1317 C CA  . CYS A 1 166 ? 21.700  14.670  2.769   1.00 23.39 ?  166 CYS A CA  1 
ATOM   1318 C C   . CYS A 1 166 ? 22.504  15.914  3.108   1.00 25.01 ?  166 CYS A C   1 
ATOM   1319 O O   . CYS A 1 166 ? 23.230  16.439  2.259   1.00 25.81 ?  166 CYS A O   1 
ATOM   1320 C CB  . CYS A 1 166 ? 22.581  13.591  2.150   1.00 24.62 ?  166 CYS A CB  1 
ATOM   1321 S SG  . CYS A 1 166 ? 23.395  12.636  3.411   1.00 26.72 ?  166 CYS A SG  1 
ATOM   1322 N N   . ASN A 1 167 ? 22.392  16.370  4.354   1.00 25.04 ?  167 ASN A N   1 
ATOM   1323 C CA  . ASN A 1 167 ? 22.879  17.691  4.746   1.00 22.44 ?  167 ASN A CA  1 
ATOM   1324 C C   . ASN A 1 167 ? 23.554  17.611  6.109   1.00 21.28 ?  167 ASN A C   1 
ATOM   1325 O O   . ASN A 1 167 ? 22.881  17.730  7.142   1.00 23.57 ?  167 ASN A O   1 
ATOM   1326 C CB  . ASN A 1 167 ? 21.717  18.679  4.766   1.00 22.10 ?  167 ASN A CB  1 
ATOM   1327 C CG  . ASN A 1 167 ? 22.105  20.039  5.302   1.00 26.54 ?  167 ASN A CG  1 
ATOM   1328 O OD1 . ASN A 1 167 ? 23.236  20.495  5.135   1.00 26.56 ?  167 ASN A OD1 1 
ATOM   1329 N ND2 . ASN A 1 167 ? 21.146  20.712  5.920   1.00 23.83 ?  167 ASN A ND2 1 
ATOM   1330 N N   . PRO A 1 168 ? 24.888  17.471  6.158   1.00 24.87 ?  168 PRO A N   1 
ATOM   1331 C CA  . PRO A 1 168 ? 25.894  17.416  5.090   1.00 23.60 ?  168 PRO A CA  1 
ATOM   1332 C C   . PRO A 1 168 ? 25.788  16.171  4.235   1.00 27.88 ?  168 PRO A C   1 
ATOM   1333 O O   . PRO A 1 168 ? 25.221  15.157  4.652   1.00 26.28 ?  168 PRO A O   1 
ATOM   1334 C CB  . PRO A 1 168 ? 27.236  17.419  5.858   1.00 27.08 ?  168 PRO A CB  1 
ATOM   1335 C CG  . PRO A 1 168 ? 26.900  17.900  7.235   1.00 28.01 ?  168 PRO A CG  1 
ATOM   1336 C CD  . PRO A 1 168 ? 25.512  17.407  7.488   1.00 25.88 ?  168 PRO A CD  1 
ATOM   1337 N N   . HIS A 1 169 ? 26.377  16.293  3.053   1.00 26.17 ?  169 HIS A N   1 
ATOM   1338 C CA  . HIS A 1 169 ? 26.196  15.260  2.025   1.00 26.39 ?  169 HIS A CA  1 
ATOM   1339 C C   . HIS A 1 169 ? 27.157  14.109  2.177   1.00 29.24 ?  169 HIS A C   1 
ATOM   1340 O O   . HIS A 1 169 ? 28.342  14.340  2.153   1.00 31.26 ?  169 HIS A O   1 
ATOM   1341 C CB  . HIS A 1 169 ? 26.250  15.890  0.638   1.00 28.61 ?  169 HIS A CB  1 
ATOM   1342 C CG  . HIS A 1 169 ? 25.722  14.999  -0.427  1.00 28.98 ?  169 HIS A CG  1 
ATOM   1343 N ND1 . HIS A 1 169 ? 24.454  15.126  -0.903  1.00 27.42 ?  169 HIS A ND1 1 
ATOM   1344 C CD2 . HIS A 1 169 ? 26.272  13.969  -1.096  1.00 28.82 ?  169 HIS A CD2 1 
ATOM   1345 C CE1 . HIS A 1 169 ? 24.244  14.232  -1.837  1.00 28.38 ?  169 HIS A CE1 1 
ATOM   1346 N NE2 . HIS A 1 169 ? 25.335  13.512  -1.968  1.00 27.32 ?  169 HIS A NE2 1 
ATOM   1347 N N   . ASN A 1 170 ? 26.597  12.929  2.297   1.00 29.00 ?  170 ASN A N   1 
ATOM   1348 C CA  . ASN A 1 170 ? 27.377  11.683  2.398   1.00 26.20 ?  170 ASN A CA  1 
ATOM   1349 C C   . ASN A 1 170 ? 27.108  10.915  1.090   1.00 30.49 ?  170 ASN A C   1 
ATOM   1350 O O   . ASN A 1 170 ? 25.909  10.809  0.784   1.00 28.18 ?  170 ASN A O   1 
ATOM   1351 C CB  . ASN A 1 170 ? 26.899  10.865  3.592   1.00 29.89 ?  170 ASN A CB  1 
ATOM   1352 C CG  . ASN A 1 170 ? 27.204  9.380   3.574   1.00 30.40 ?  170 ASN A CG  1 
ATOM   1353 O OD1 . ASN A 1 170 ? 28.293  8.954   3.226   1.00 31.42 ?  170 ASN A OD1 1 
ATOM   1354 N ND2 . ASN A 1 170 ? 26.256  8.577   4.020   1.00 29.99 ?  170 ASN A ND2 1 
ATOM   1355 N N   . PRO A 1 171 ? 28.111  10.406  0.309   1.00 31.19 ?  171 PRO A N   1 
ATOM   1356 C CA  . PRO A 1 171 ? 29.501  10.191  0.740   1.00 30.05 ?  171 PRO A CA  1 
ATOM   1357 C C   . PRO A 1 171 ? 30.518  11.302  0.482   1.00 30.64 ?  171 PRO A C   1 
ATOM   1358 O O   . PRO A 1 171 ? 31.680  11.100  0.851   1.00 32.57 ?  171 PRO A O   1 
ATOM   1359 C CB  . PRO A 1 171 ? 29.890  8.954   -0.065  1.00 32.55 ?  171 PRO A CB  1 
ATOM   1360 C CG  . PRO A 1 171 ? 29.159  9.146   -1.380  1.00 30.96 ?  171 PRO A CG  1 
ATOM   1361 C CD  . PRO A 1 171 ? 27.876  9.890   -1.054  1.00 29.50 ?  171 PRO A CD  1 
ATOM   1362 N N   . ILE A 1 172 ? 30.137  12.408  -0.142  1.00 31.82 ?  172 ILE A N   1 
ATOM   1363 C CA  . ILE A 1 172 ? 31.132  13.432  -0.593  1.00 32.94 ?  172 ILE A CA  1 
ATOM   1364 C C   . ILE A 1 172 ? 31.626  14.310  0.554   1.00 33.80 ?  172 ILE A C   1 
ATOM   1365 O O   . ILE A 1 172 ? 32.600  15.039  0.356   1.00 34.56 ?  172 ILE A O   1 
ATOM   1366 C CB  . ILE A 1 172 ? 30.555  14.263  -1.755  1.00 30.86 ?  172 ILE A CB  1 
ATOM   1367 C CG1 . ILE A 1 172 ? 29.553  15.313  -1.270  1.00 31.49 ?  172 ILE A CG1 1 
ATOM   1368 C CG2 . ILE A 1 172 ? 29.942  13.356  -2.807  1.00 35.23 ?  172 ILE A CG2 1 
ATOM   1369 C CD1 . ILE A 1 172 ? 29.023  16.213  -2.357  1.00 32.98 ?  172 ILE A CD1 1 
ATOM   1370 N N   . GLY A 1 173 ? 30.928  14.285  1.678   1.00 33.46 ?  173 GLY A N   1 
ATOM   1371 C CA  . GLY A 1 173 ? 31.365  15.039  2.842   1.00 32.71 ?  173 GLY A CA  1 
ATOM   1372 C C   . GLY A 1 173 ? 31.272  16.549  2.730   1.00 36.30 ?  173 GLY A C   1 
ATOM   1373 O O   . GLY A 1 173 ? 32.223  17.251  3.088   1.00 36.85 ?  173 GLY A O   1 
ATOM   1374 N N   . TYR A 1 174 ? 30.133  17.062  2.262   1.00 29.39 ?  174 TYR A N   1 
ATOM   1375 C CA  . TYR A 1 174 ? 29.956  18.483  1.991   1.00 34.24 ?  174 TYR A CA  1 
ATOM   1376 C C   . TYR A 1 174 ? 28.781  19.030  2.788   1.00 33.04 ?  174 TYR A C   1 
ATOM   1377 O O   . TYR A 1 174 ? 27.636  18.601  2.590   1.00 30.82 ?  174 TYR A O   1 
ATOM   1378 C CB  . TYR A 1 174 ? 29.728  18.742  0.503   1.00 29.04 ?  174 TYR A CB  1 
ATOM   1379 C CG  . TYR A 1 174 ? 29.446  20.187  0.196   1.00 33.12 ?  174 TYR A CG  1 
ATOM   1380 C CD1 . TYR A 1 174 ? 30.405  21.166  0.434   1.00 33.41 ?  174 TYR A CD1 1 
ATOM   1381 C CD2 . TYR A 1 174 ? 28.211  20.587  -0.303  1.00 30.63 ?  174 TYR A CD2 1 
ATOM   1382 C CE1 . TYR A 1 174 ? 30.151  22.496  0.168   1.00 33.11 ?  174 TYR A CE1 1 
ATOM   1383 C CE2 . TYR A 1 174 ? 27.953  21.920  -0.577  1.00 30.53 ?  174 TYR A CE2 1 
ATOM   1384 C CZ  . TYR A 1 174 ? 28.922  22.870  -0.344  1.00 33.40 ?  174 TYR A CZ  1 
ATOM   1385 O OH  . TYR A 1 174 ? 28.658  24.202  -0.620  1.00 32.52 ?  174 TYR A OH  1 
ATOM   1386 N N   . ALA A 1 175 ? 29.063  20.003  3.656   1.00 29.94 ?  175 ALA A N   1 
ATOM   1387 C CA  . ALA A 1 175 ? 28.035  20.738  4.388   1.00 27.62 ?  175 ALA A CA  1 
ATOM   1388 C C   . ALA A 1 175 ? 27.577  21.922  3.545   1.00 31.16 ?  175 ALA A C   1 
ATOM   1389 O O   . ALA A 1 175 ? 28.287  22.927  3.440   1.00 30.08 ?  175 ALA A O   1 
ATOM   1390 C CB  . ALA A 1 175 ? 28.566  21.203  5.743   1.00 27.97 ?  175 ALA A CB  1 
ATOM   1391 N N   . TRP A 1 176 ? 26.380  21.806  2.966   1.00 31.21 ?  176 TRP A N   1 
ATOM   1392 C CA  . TRP A 1 176 ? 25.821  22.841  2.104   1.00 28.89 ?  176 TRP A CA  1 
ATOM   1393 C C   . TRP A 1 176 ? 25.865  24.217  2.759   1.00 28.52 ?  176 TRP A C   1 
ATOM   1394 O O   . TRP A 1 176 ? 25.801  24.357  3.985   1.00 31.37 ?  176 TRP A O   1 
ATOM   1395 C CB  . TRP A 1 176 ? 24.377  22.486  1.747   1.00 27.16 ?  176 TRP A CB  1 
ATOM   1396 C CG  . TRP A 1 176 ? 24.261  21.114  1.178   1.00 27.85 ?  176 TRP A CG  1 
ATOM   1397 C CD1 . TRP A 1 176 ? 23.998  19.959  1.858   1.00 26.96 ?  176 TRP A CD1 1 
ATOM   1398 C CD2 . TRP A 1 176 ? 24.440  20.744  -0.190  1.00 26.23 ?  176 TRP A CD2 1 
ATOM   1399 N NE1 . TRP A 1 176 ? 23.987  18.894  0.992   1.00 29.53 ?  176 TRP A NE1 1 
ATOM   1400 C CE2 . TRP A 1 176 ? 24.262  19.348  -0.272  1.00 27.48 ?  176 TRP A CE2 1 
ATOM   1401 C CE3 . TRP A 1 176 ? 24.733  21.460  -1.356  1.00 31.09 ?  176 TRP A CE3 1 
ATOM   1402 C CZ2 . TRP A 1 176 ? 24.350  18.648  -1.481  1.00 28.18 ?  176 TRP A CZ2 1 
ATOM   1403 C CZ3 . TRP A 1 176 ? 24.828  20.763  -2.559  1.00 30.28 ?  176 TRP A CZ3 1 
ATOM   1404 C CH2 . TRP A 1 176 ? 24.641  19.372  -2.609  1.00 30.68 ?  176 TRP A CH2 1 
ATOM   1405 N N   . SER A 1 177 ? 25.965  25.242  1.917   1.00 30.38 ?  177 SER A N   1 
ATOM   1406 C CA  . SER A 1 177 ? 25.963  26.617  2.387   1.00 32.54 ?  177 SER A CA  1 
ATOM   1407 C C   . SER A 1 177 ? 24.555  27.041  2.781   1.00 32.71 ?  177 SER A C   1 
ATOM   1408 O O   . SER A 1 177 ? 23.560  26.438  2.371   1.00 28.48 ?  177 SER A O   1 
ATOM   1409 C CB  . SER A 1 177 ? 26.478  27.555  1.301   1.00 30.32 ?  177 SER A CB  1 
ATOM   1410 O OG  . SER A 1 177 ? 25.414  27.927  0.437   1.00 33.70 ?  177 SER A OG  1 
ATOM   1411 N N   . GLU A 1 178 ? 24.481  28.116  3.569   1.00 33.29 ?  178 GLU A N   1 
ATOM   1412 C CA  . GLU A 1 178 ? 23.184  28.617  4.008   1.00 29.77 ?  178 GLU A CA  1 
ATOM   1413 C C   . GLU A 1 178 ? 22.296  28.971  2.822   1.00 33.48 ?  178 GLU A C   1 
ATOM   1414 O O   . GLU A 1 178 ? 21.093  28.685  2.835   1.00 25.45 ?  178 GLU A O   1 
ATOM   1415 C CB  . GLU A 1 178 ? 23.367  29.826  4.922   1.00 34.90 ?  178 GLU A CB  1 
ATOM   1416 C CG  . GLU A 1 178 ? 22.055  30.343  5.489   1.00 37.53 ?  178 GLU A CG  1 
ATOM   1417 C CD  . GLU A 1 178 ? 22.191  31.712  6.103   1.00 40.45 ?  178 GLU A CD  1 
ATOM   1418 O OE1 . GLU A 1 178 ? 21.177  32.431  6.199   1.00 39.27 ?  178 GLU A OE1 1 
ATOM   1419 O OE2 . GLU A 1 178 ? 23.320  32.077  6.481   1.00 45.42 -1 178 GLU A OE2 1 
ATOM   1420 N N   . GLU A 1 179 ? 22.877  29.590  1.786   1.00 33.65 ?  179 GLU A N   1 
ATOM   1421 C CA  . GLU A 1 179 ? 22.121  29.905  0.578   1.00 32.30 ?  179 GLU A CA  1 
ATOM   1422 C C   . GLU A 1 179 ? 21.640  28.640  -0.115  1.00 33.16 ?  179 GLU A C   1 
ATOM   1423 O O   . GLU A 1 179 ? 20.527  28.607  -0.654  1.00 28.30 ?  179 GLU A O   1 
ATOM   1424 C CB  . GLU A 1 179 ? 22.970  30.731  -0.393  1.00 34.70 ?  179 GLU A CB  1 
ATOM   1425 C CG  . GLU A 1 179 ? 22.233  31.108  -1.691  1.00 44.37 ?  179 GLU A CG  1 
ATOM   1426 C CD  . GLU A 1 179 ? 23.126  31.096  -2.935  1.00 58.08 ?  179 GLU A CD  1 
ATOM   1427 O OE1 . GLU A 1 179 ? 23.151  30.059  -3.647  1.00 56.90 ?  179 GLU A OE1 1 
ATOM   1428 O OE2 . GLU A 1 179 ? 23.782  32.129  -3.210  1.00 57.79 -1 179 GLU A OE2 1 
ATOM   1429 N N   . GLU A 1 180 ? 22.473  27.593  -0.119  1.00 29.48 ?  180 GLU A N   1 
ATOM   1430 C CA  . GLU A 1 180 ? 22.125  26.362  -0.825  1.00 30.89 ?  180 GLU A CA  1 
ATOM   1431 C C   . GLU A 1 180 ? 20.970  25.649  -0.135  1.00 28.75 ?  180 GLU A C   1 
ATOM   1432 O O   . GLU A 1 180 ? 20.003  25.236  -0.786  1.00 26.74 ?  180 GLU A O   1 
ATOM   1433 C CB  . GLU A 1 180 ? 23.350  25.445  -0.927  1.00 30.71 ?  180 GLU A CB  1 
ATOM   1434 C CG  . GLU A 1 180 ? 24.402  25.908  -1.939  1.00 32.55 ?  180 GLU A CG  1 
ATOM   1435 C CD  . GLU A 1 180 ? 25.777  25.245  -1.753  1.00 33.16 ?  180 GLU A CD  1 
ATOM   1436 O OE1 . GLU A 1 180 ? 26.462  24.996  -2.768  1.00 42.89 ?  180 GLU A OE1 1 
ATOM   1437 O OE2 . GLU A 1 180 ? 26.181  24.971  -0.607  1.00 34.95 -1 180 GLU A OE2 1 
ATOM   1438 N N   . VAL A 1 181 ? 21.040  25.523  1.191   1.00 29.44 ?  181 VAL A N   1 
ATOM   1439 C CA  . VAL A 1 181 ? 19.970  24.841  1.917   1.00 28.63 ?  181 VAL A CA  1 
ATOM   1440 C C   . VAL A 1 181 ? 18.671  25.618  1.777   1.00 25.81 ?  181 VAL A C   1 
ATOM   1441 O O   . VAL A 1 181 ? 17.605  25.035  1.553   1.00 29.00 ?  181 VAL A O   1 
ATOM   1442 C CB  . VAL A 1 181 ? 20.360  24.650  3.397   1.00 28.37 ?  181 VAL A CB  1 
ATOM   1443 C CG1 . VAL A 1 181 ? 19.155  24.254  4.240   1.00 26.86 ?  181 VAL A CG1 1 
ATOM   1444 C CG2 . VAL A 1 181 ? 21.470  23.627  3.530   1.00 26.76 ?  181 VAL A CG2 1 
ATOM   1445 N N   . LYS A 1 182 ? 18.741  26.948  1.900   1.00 27.45 ?  182 LYS A N   1 
ATOM   1446 C CA  . LYS A 1 182 ? 17.537  27.766  1.816   1.00 26.31 ?  182 LYS A CA  1 
ATOM   1447 C C   . LYS A 1 182 ? 16.957  27.747  0.410   1.00 28.77 ?  182 LYS A C   1 
ATOM   1448 O O   . LYS A 1 182 ? 15.735  27.744  0.241   1.00 25.80 ?  182 LYS A O   1 
ATOM   1449 C CB  . LYS A 1 182 ? 17.830  29.203  2.255   1.00 28.29 ?  182 LYS A CB  1 
ATOM   1450 C CG  . LYS A 1 182 ? 17.927  29.380  3.768   1.00 30.18 ?  182 LYS A CG  1 
ATOM   1451 C CD  . LYS A 1 182 ? 18.328  30.814  4.141   1.00 33.89 ?  182 LYS A CD  1 
ATOM   1452 C CE  . LYS A 1 182 ? 18.228  31.031  5.650   1.00 32.24 ?  182 LYS A CE  1 
ATOM   1453 N NZ  . LYS A 1 182 ? 18.384  32.469  6.009   1.00 40.64 1  182 LYS A NZ  1 
ATOM   1454 N N   . ARG A 1 183 ? 17.816  27.734  -0.613  1.00 27.79 ?  183 ARG A N   1 
ATOM   1455 C CA  . ARG A 1 183 ? 17.309  27.690  -1.977  1.00 29.42 ?  183 ARG A CA  1 
ATOM   1456 C C   . ARG A 1 183 ? 16.643  26.357  -2.264  1.00 29.51 ?  183 ARG A C   1 
ATOM   1457 O O   . ARG A 1 183 ? 15.607  26.302  -2.937  1.00 28.18 ?  183 ARG A O   1 
ATOM   1458 C CB  . ARG A 1 183 ? 18.433  27.937  -2.974  1.00 30.97 ?  183 ARG A CB  1 
ATOM   1459 C CG  . ARG A 1 183 ? 17.920  28.055  -4.392  1.00 33.96 ?  183 ARG A CG  1 
ATOM   1460 C CD  . ARG A 1 183 ? 19.030  28.276  -5.390  1.00 41.58 ?  183 ARG A CD  1 
ATOM   1461 N NE  . ARG A 1 183 ? 18.494  28.680  -6.685  1.00 40.55 ?  183 ARG A NE  1 
ATOM   1462 C CZ  . ARG A 1 183 ? 19.240  29.121  -7.690  1.00 43.36 ?  183 ARG A CZ  1 
ATOM   1463 N NH1 . ARG A 1 183 ? 20.555  29.205  -7.541  1.00 42.96 1  183 ARG A NH1 1 
ATOM   1464 N NH2 . ARG A 1 183 ? 18.670  29.479  -8.837  1.00 44.59 ?  183 ARG A NH2 1 
ATOM   1465 N N   . ILE A 1 184 ? 17.224  25.269  -1.763  1.00 27.31 ?  184 ILE A N   1 
ATOM   1466 C CA  . ILE A 1 184 ? 16.610  23.962  -1.962  1.00 25.76 ?  184 ILE A CA  1 
ATOM   1467 C C   . ILE A 1 184 ? 15.256  23.912  -1.266  1.00 27.23 ?  184 ILE A C   1 
ATOM   1468 O O   . ILE A 1 184 ? 14.250  23.500  -1.857  1.00 26.60 ?  184 ILE A O   1 
ATOM   1469 C CB  . ILE A 1 184 ? 17.563  22.852  -1.491  1.00 28.35 ?  184 ILE A CB  1 
ATOM   1470 C CG1 . ILE A 1 184 ? 18.680  22.696  -2.529  1.00 26.73 ?  184 ILE A CG1 1 
ATOM   1471 C CG2 . ILE A 1 184 ? 16.808  21.531  -1.285  1.00 25.79 ?  184 ILE A CG2 1 
ATOM   1472 C CD1 . ILE A 1 184 ? 19.900  21.883  -2.062  1.00 28.01 ?  184 ILE A CD1 1 
ATOM   1473 N N   . ALA A 1 185 ? 15.189  24.403  -0.027  1.00 24.76 ?  185 ALA A N   1 
ATOM   1474 C CA  . ALA A 1 185 ? 13.925  24.330  0.702   1.00 26.95 ?  185 ALA A CA  1 
ATOM   1475 C C   . ALA A 1 185 ? 12.871  25.243  0.089   1.00 27.15 ?  185 ALA A C   1 
ATOM   1476 O O   . ALA A 1 185 ? 11.685  24.892  0.066   1.00 24.67 ?  185 ALA A O   1 
ATOM   1477 C CB  . ALA A 1 185 ? 14.144  24.666  2.174   1.00 27.22 ?  185 ALA A CB  1 
ATOM   1478 N N   . GLU A 1 186 ? 13.279  26.413  -0.420  1.00 28.52 ?  186 GLU A N   1 
ATOM   1479 C CA  . GLU A 1 186 ? 12.344  27.275  -1.140  1.00 28.38 ?  186 GLU A CA  1 
ATOM   1480 C C   . GLU A 1 186 ? 11.823  26.606  -2.412  1.00 27.48 ?  186 GLU A C   1 
ATOM   1481 O O   . GLU A 1 186 ? 10.630  26.696  -2.714  1.00 26.90 ?  186 GLU A O   1 
ATOM   1482 C CB  . GLU A 1 186 ? 13.009  28.617  -1.461  1.00 30.93 ?  186 GLU A CB  1 
ATOM   1483 C CG  . GLU A 1 186 ? 13.259  29.490  -0.221  1.00 34.46 ?  186 GLU A CG  1 
ATOM   1484 C CD  . GLU A 1 186 ? 14.378  30.500  -0.426  1.00 37.22 ?  186 GLU A CD  1 
ATOM   1485 O OE1 . GLU A 1 186 ? 15.007  30.916  0.573   1.00 37.39 ?  186 GLU A OE1 1 
ATOM   1486 O OE2 . GLU A 1 186 ? 14.631  30.881  -1.589  1.00 39.56 -1 186 GLU A OE2 1 
ATOM   1487 N N   . LEU A 1 187 ? 12.693  25.928  -3.166  1.00 28.63 ?  187 LEU A N   1 
ATOM   1488 C CA  . LEU A 1 187 ? 12.242  25.262  -4.389  1.00 27.84 ?  187 LEU A CA  1 
ATOM   1489 C C   . LEU A 1 187 ? 11.286  24.117  -4.079  1.00 28.02 ?  187 LEU A C   1 
ATOM   1490 O O   . LEU A 1 187 ? 10.304  23.909  -4.800  1.00 28.63 ?  187 LEU A O   1 
ATOM   1491 C CB  . LEU A 1 187 ? 13.439  24.741  -5.189  1.00 29.71 ?  187 LEU A CB  1 
ATOM   1492 C CG  . LEU A 1 187 ? 14.281  25.778  -5.952  1.00 34.09 ?  187 LEU A CG  1 
ATOM   1493 C CD1 . LEU A 1 187 ? 15.398  25.097  -6.725  1.00 32.64 ?  187 LEU A CD1 1 
ATOM   1494 C CD2 . LEU A 1 187 ? 13.409  26.604  -6.893  1.00 35.87 ?  187 LEU A CD2 1 
ATOM   1495 N N   . CYS A 1 188 ? 11.564  23.355  -3.015  1.00 29.40 ?  188 CYS A N   1 
ATOM   1496 C CA  . CYS A 1 188 ? 10.651  22.293  -2.605  1.00 25.38 ?  188 CYS A CA  1 
ATOM   1497 C C   . CYS A 1 188 ? 9.301   22.863  -2.200  1.00 25.23 ?  188 CYS A C   1 
ATOM   1498 O O   . CYS A 1 188 ? 8.247   22.360  -2.608  1.00 27.27 ?  188 CYS A O   1 
ATOM   1499 C CB  . CYS A 1 188 ? 11.260  21.500  -1.446  1.00 24.06 ?  188 CYS A CB  1 
ATOM   1500 S SG  . CYS A 1 188 ? 12.607  20.428  -1.941  1.00 24.48 ?  188 CYS A SG  1 
ATOM   1501 N N   . ALA A 1 189 ? 9.317   23.917  -1.389  1.00 29.24 ?  189 ALA A N   1 
ATOM   1502 C CA  . ALA A 1 189 ? 8.072   24.555  -0.979  1.00 26.58 ?  189 ALA A CA  1 
ATOM   1503 C C   . ALA A 1 189 ? 7.302   25.066  -2.190  1.00 29.25 ?  189 ALA A C   1 
ATOM   1504 O O   . ALA A 1 189 ? 6.081   24.893  -2.284  1.00 25.18 ?  189 ALA A O   1 
ATOM   1505 C CB  . ALA A 1 189 ? 8.381   25.696  -0.008  1.00 27.50 ?  189 ALA A CB  1 
ATOM   1506 N N   . LYS A 1 190 ? 8.014   25.690  -3.130  1.00 30.98 ?  190 LYS A N   1 
ATOM   1507 C CA  . LYS A 1 190 ? 7.388   26.290  -4.305  1.00 26.86 ?  190 LYS A CA  1 
ATOM   1508 C C   . LYS A 1 190 ? 6.649   25.251  -5.130  1.00 33.13 ?  190 LYS A C   1 
ATOM   1509 O O   . LYS A 1 190 ? 5.632   25.557  -5.763  1.00 32.29 ?  190 LYS A O   1 
ATOM   1510 C CB  . LYS A 1 190 ? 8.470   26.982  -5.136  1.00 26.15 ?  190 LYS A CB  1 
ATOM   1511 C CG  . LYS A 1 190 ? 8.063   27.394  -6.533  1.00 35.92 ?  190 LYS A CG  1 
ATOM   1512 C CD  . LYS A 1 190 ? 9.291   27.841  -7.321  1.00 33.69 ?  190 LYS A CD  1 
ATOM   1513 C CE  . LYS A 1 190 ? 8.902   28.586  -8.584  1.00 40.73 ?  190 LYS A CE  1 
ATOM   1514 N NZ  . LYS A 1 190 ? 10.118  29.100  -9.275  1.00 43.01 1  190 LYS A NZ  1 
ATOM   1515 N N   . HIS A 1 191 ? 7.138   24.016  -5.129  1.00 27.08 ?  191 HIS A N   1 
ATOM   1516 C CA  . HIS A 1 191 ? 6.533   22.940  -5.892  1.00 27.85 ?  191 HIS A CA  1 
ATOM   1517 C C   . HIS A 1 191 ? 5.827   21.923  -5.007  1.00 29.30 ?  191 HIS A C   1 
ATOM   1518 O O   . HIS A 1 191 ? 5.476   20.837  -5.480  1.00 27.55 ?  191 HIS A O   1 
ATOM   1519 C CB  . HIS A 1 191 ? 7.612   22.305  -6.766  1.00 28.00 ?  191 HIS A CB  1 
ATOM   1520 C CG  . HIS A 1 191 ? 8.172   23.266  -7.769  1.00 30.27 ?  191 HIS A CG  1 
ATOM   1521 N ND1 . HIS A 1 191 ? 7.378   23.902  -8.698  1.00 29.46 ?  191 HIS A ND1 1 
ATOM   1522 C CD2 . HIS A 1 191 ? 9.425   23.741  -7.958  1.00 31.03 ?  191 HIS A CD2 1 
ATOM   1523 C CE1 . HIS A 1 191 ? 8.120   24.713  -9.431  1.00 35.18 ?  191 HIS A CE1 1 
ATOM   1524 N NE2 . HIS A 1 191 ? 9.368   24.638  -9.000  1.00 33.59 ?  191 HIS A NE2 1 
ATOM   1525 N N   . GLN A 1 192 ? 5.595   22.268  -3.733  1.00 26.97 ?  192 GLN A N   1 
ATOM   1526 C CA  . GLN A 1 192 ? 4.866   21.415  -2.798  1.00 29.85 ?  192 GLN A CA  1 
ATOM   1527 C C   . GLN A 1 192 ? 5.505   20.034  -2.709  1.00 27.24 ?  192 GLN A C   1 
ATOM   1528 O O   . GLN A 1 192 ? 4.825   19.007  -2.703  1.00 24.52 ?  192 GLN A O   1 
ATOM   1529 C CB  . GLN A 1 192 ? 3.382   21.325  -3.168  1.00 29.66 ?  192 GLN A CB  1 
ATOM   1530 C CG  . GLN A 1 192 ? 2.660   22.647  -2.949  1.00 33.03 ?  192 GLN A CG  1 
ATOM   1531 C CD  . GLN A 1 192 ? 2.171   23.256  -4.227  1.00 44.26 ?  192 GLN A CD  1 
ATOM   1532 O OE1 . GLN A 1 192 ? 1.221   22.762  -4.832  1.00 47.48 ?  192 GLN A OE1 1 
ATOM   1533 N NE2 . GLN A 1 192 ? 2.820   24.333  -4.661  1.00 47.25 ?  192 GLN A NE2 1 
ATOM   1534 N N   . VAL A 1 193 ? 6.834   20.030  -2.628  1.00 26.17 ?  193 VAL A N   1 
ATOM   1535 C CA  . VAL A 1 193 ? 7.644   18.842  -2.410  1.00 24.38 ?  193 VAL A CA  1 
ATOM   1536 C C   . VAL A 1 193 ? 8.123   18.853  -0.960  1.00 26.67 ?  193 VAL A C   1 
ATOM   1537 O O   . VAL A 1 193 ? 8.602   19.879  -0.463  1.00 23.48 ?  193 VAL A O   1 
ATOM   1538 C CB  . VAL A 1 193 ? 8.832   18.803  -3.386  1.00 25.49 ?  193 VAL A CB  1 
ATOM   1539 C CG1 . VAL A 1 193 ? 9.816   17.698  -3.012  1.00 24.39 ?  193 VAL A CG1 1 
ATOM   1540 C CG2 . VAL A 1 193 ? 8.329   18.638  -4.833  1.00 24.57 ?  193 VAL A CG2 1 
ATOM   1541 N N   . LEU A 1 194 ? 7.993   17.718  -0.276  1.00 21.34 ?  194 LEU A N   1 
ATOM   1542 C CA  . LEU A 1 194 ? 8.490   17.615  1.091   1.00 25.61 ?  194 LEU A CA  1 
ATOM   1543 C C   . LEU A 1 194 ? 9.999   17.436  1.077   1.00 22.83 ?  194 LEU A C   1 
ATOM   1544 O O   . LEU A 1 194 ? 10.513  16.533  0.406   1.00 23.91 ?  194 LEU A O   1 
ATOM   1545 C CB  . LEU A 1 194 ? 7.843   16.435  1.811   1.00 25.26 ?  194 LEU A CB  1 
ATOM   1546 C CG  . LEU A 1 194 ? 6.465   16.612  2.441   1.00 28.89 ?  194 LEU A CG  1 
ATOM   1547 C CD1 . LEU A 1 194 ? 6.231   15.493  3.464   1.00 31.06 ?  194 LEU A CD1 1 
ATOM   1548 C CD2 . LEU A 1 194 ? 6.327   17.982  3.090   1.00 33.54 ?  194 LEU A CD2 1 
ATOM   1549 N N   . LEU A 1 195 ? 10.705  18.263  1.862   1.00 24.75 ?  195 LEU A N   1 
ATOM   1550 C CA  . LEU A 1 195 ? 12.159  18.184  1.986   1.00 23.89 ?  195 LEU A CA  1 
ATOM   1551 C C   . LEU A 1 195 ? 12.505  17.438  3.274   1.00 20.73 ?  195 LEU A C   1 
ATOM   1552 O O   . LEU A 1 195 ? 12.257  17.937  4.375   1.00 21.77 ?  195 LEU A O   1 
ATOM   1553 C CB  . LEU A 1 195 ? 12.794  19.576  1.983   1.00 22.83 ?  195 LEU A CB  1 
ATOM   1554 C CG  . LEU A 1 195 ? 14.319  19.579  2.172   1.00 21.43 ?  195 LEU A CG  1 
ATOM   1555 C CD1 . LEU A 1 195 ? 14.960  18.936  0.958   1.00 22.31 ?  195 LEU A CD1 1 
ATOM   1556 C CD2 . LEU A 1 195 ? 14.886  21.000  2.401   1.00 22.57 ?  195 LEU A CD2 1 
ATOM   1557 N N   . ILE A 1 196 ? 13.043  16.235  3.127   1.00 18.90 ?  196 ILE A N   1 
ATOM   1558 C CA  . ILE A 1 196 ? 13.516  15.424  4.240   1.00 23.16 ?  196 ILE A CA  1 
ATOM   1559 C C   . ILE A 1 196 ? 15.026  15.611  4.298   1.00 24.44 ?  196 ILE A C   1 
ATOM   1560 O O   . ILE A 1 196 ? 15.754  15.131  3.422   1.00 22.49 ?  196 ILE A O   1 
ATOM   1561 C CB  . ILE A 1 196 ? 13.130  13.949  4.062   1.00 22.60 ?  196 ILE A CB  1 
ATOM   1562 C CG1 . ILE A 1 196 ? 11.625  13.820  3.799   1.00 20.69 ?  196 ILE A CG1 1 
ATOM   1563 C CG2 . ILE A 1 196 ? 13.533  13.128  5.296   1.00 20.49 ?  196 ILE A CG2 1 
ATOM   1564 C CD1 . ILE A 1 196 ? 10.734  14.561  4.792   1.00 21.87 ?  196 ILE A CD1 1 
ATOM   1565 N N   . SER A 1 197 ? 15.505  16.306  5.330   1.00 23.85 ?  197 SER A N   1 
ATOM   1566 C CA  . SER A 1 197 ? 16.908  16.701  5.410   1.00 22.11 ?  197 SER A CA  1 
ATOM   1567 C C   . SER A 1 197 ? 17.599  15.792  6.421   1.00 22.19 ?  197 SER A C   1 
ATOM   1568 O O   . SER A 1 197 ? 17.376  15.905  7.631   1.00 24.13 ?  197 SER A O   1 
ATOM   1569 C CB  . SER A 1 197 ? 17.044  18.168  5.787   1.00 21.94 ?  197 SER A CB  1 
ATOM   1570 O OG  . SER A 1 197 ? 18.421  18.546  5.825   1.00 26.79 ?  197 SER A OG  1 
ATOM   1571 N N   . ASP A 1 198 ? 18.405  14.874  5.910   1.00 21.58 ?  198 ASP A N   1 
ATOM   1572 C CA  . ASP A 1 198 ? 19.138  13.915  6.723   1.00 22.18 ?  198 ASP A CA  1 
ATOM   1573 C C   . ASP A 1 198 ? 20.379  14.637  7.224   1.00 20.96 ?  198 ASP A C   1 
ATOM   1574 O O   . ASP A 1 198 ? 21.344  14.827  6.481   1.00 23.21 ?  198 ASP A O   1 
ATOM   1575 C CB  . ASP A 1 198 ? 19.470  12.673  5.896   1.00 22.63 ?  198 ASP A CB  1 
ATOM   1576 C CG  . ASP A 1 198 ? 20.332  11.667  6.647   1.00 25.51 ?  198 ASP A CG  1 
ATOM   1577 O OD1 . ASP A 1 198 ? 20.833  12.000  7.747   1.00 22.98 ?  198 ASP A OD1 1 
ATOM   1578 O OD2 . ASP A 1 198 ? 20.509  10.534  6.145   1.00 23.62 -1 198 ASP A OD2 1 
ATOM   1579 N N   . GLU A 1 199 ? 20.361  15.026  8.498   1.00 22.99 ?  199 GLU A N   1 
ATOM   1580 C CA  . GLU A 1 199 ? 21.476  15.825  9.071   1.00 22.70 ?  199 GLU A CA  1 
ATOM   1581 C C   . GLU A 1 199 ? 22.293  14.996  10.059  1.00 24.75 ?  199 GLU A C   1 
ATOM   1582 O O   . GLU A 1 199 ? 22.830  15.558  10.995  1.00 23.71 ?  199 GLU A O   1 
ATOM   1583 C CB  . GLU A 1 199 ? 20.914  17.087  9.701   1.00 22.17 ?  199 GLU A CB  1 
ATOM   1584 C CG  . GLU A 1 199 ? 20.116  17.893  8.696   1.00 20.80 ?  199 GLU A CG  1 
ATOM   1585 C CD  . GLU A 1 199 ? 19.264  19.019  9.228   1.00 23.58 ?  199 GLU A CD  1 
ATOM   1586 O OE1 . GLU A 1 199 ? 18.558  19.624  8.426   1.00 26.47 ?  199 GLU A OE1 1 
ATOM   1587 O OE2 . GLU A 1 199 ? 19.308  19.275  10.430  1.00 26.79 -1 199 GLU A OE2 1 
ATOM   1588 N N   . ILE A 1 200 ? 22.395  13.712  9.780   1.00 23.87 ?  200 ILE A N   1 
ATOM   1589 C CA  . ILE A 1 200 ? 23.045  12.819  10.721  1.00 22.44 ?  200 ILE A CA  1 
ATOM   1590 C C   . ILE A 1 200 ? 24.545  13.080  10.770  1.00 25.70 ?  200 ILE A C   1 
ATOM   1591 O O   . ILE A 1 200 ? 25.193  12.754  11.767  1.00 23.53 ?  200 ILE A O   1 
ATOM   1592 C CB  . ILE A 1 200 ? 22.699  11.340  10.389  1.00 24.05 ?  200 ILE A CB  1 
ATOM   1593 C CG1 . ILE A 1 200 ? 22.923  10.432  11.611  1.00 23.52 ?  200 ILE A CG1 1 
ATOM   1594 C CG2 . ILE A 1 200 ? 23.491  10.822  9.183   1.00 24.86 ?  200 ILE A CG2 1 
ATOM   1595 C CD1 . ILE A 1 200 ? 22.368  9.013   11.449  1.00 23.46 ?  200 ILE A CD1 1 
ATOM   1596 N N   . HIS A 1 201 ? 25.110  13.714  9.745   1.00 25.33 ?  201 HIS A N   1 
ATOM   1597 C CA  . HIS A 1 201 ? 26.528  14.056  9.752   1.00 28.37 ?  201 HIS A CA  1 
ATOM   1598 C C   . HIS A 1 201 ? 26.766  15.494  10.175  1.00 25.39 ?  201 HIS A C   1 
ATOM   1599 O O   . HIS A 1 201 ? 27.909  15.967  10.121  1.00 27.34 ?  201 HIS A O   1 
ATOM   1600 C CB  . HIS A 1 201 ? 27.149  13.783  8.380   1.00 24.75 ?  201 HIS A CB  1 
ATOM   1601 C CG  . HIS A 1 201 ? 27.221  12.327  8.048   1.00 27.19 ?  201 HIS A CG  1 
ATOM   1602 N ND1 . HIS A 1 201 ? 26.229  11.673  7.350   1.00 31.25 ?  201 HIS A ND1 1 
ATOM   1603 C CD2 . HIS A 1 201 ? 28.149  11.389  8.353   1.00 26.78 ?  201 HIS A CD2 1 
ATOM   1604 C CE1 . HIS A 1 201 ? 26.545  10.395  7.233   1.00 29.63 ?  201 HIS A CE1 1 
ATOM   1605 N NE2 . HIS A 1 201 ? 27.704  10.196  7.838   1.00 30.91 ?  201 HIS A NE2 1 
ATOM   1606 N N   . GLY A 1 202 ? 25.719  16.174  10.655  1.00 23.36 ?  202 GLY A N   1 
ATOM   1607 C CA  . GLY A 1 202 ? 25.768  17.605  10.882  1.00 26.80 ?  202 GLY A CA  1 
ATOM   1608 C C   . GLY A 1 202 ? 26.650  18.037  12.031  1.00 26.63 ?  202 GLY A C   1 
ATOM   1609 O O   . GLY A 1 202 ? 27.091  19.192  12.049  1.00 27.16 ?  202 GLY A O   1 
ATOM   1610 N N   . ASP A 1 203 ? 26.897  17.154  13.001  1.00 21.21 ?  203 ASP A N   1 
ATOM   1611 C CA  . ASP A 1 203 ? 27.798  17.479  14.098  1.00 26.17 ?  203 ASP A CA  1 
ATOM   1612 C C   . ASP A 1 203 ? 29.254  17.286  13.710  1.00 26.91 ?  203 ASP A C   1 
ATOM   1613 O O   . ASP A 1 203 ? 30.136  17.566  14.526  1.00 25.72 ?  203 ASP A O   1 
ATOM   1614 C CB  . ASP A 1 203 ? 27.498  16.621  15.332  1.00 24.76 ?  203 ASP A CB  1 
ATOM   1615 C CG  . ASP A 1 203 ? 26.094  16.810  15.857  1.00 27.36 ?  203 ASP A CG  1 
ATOM   1616 O OD1 . ASP A 1 203 ? 25.537  17.913  15.713  1.00 25.87 ?  203 ASP A OD1 1 
ATOM   1617 O OD2 . ASP A 1 203 ? 25.550  15.847  16.436  1.00 24.21 -1 203 ASP A OD2 1 
ATOM   1618 N N   . LEU A 1 204 ? 29.485  16.809  12.487  1.00 26.43 ?  204 LEU A N   1 
ATOM   1619 C CA  . LEU A 1 204 ? 30.845  16.435  12.072  1.00 24.87 ?  204 LEU A CA  1 
ATOM   1620 C C   . LEU A 1 204 ? 31.424  17.368  11.012  1.00 26.66 ?  204 LEU A C   1 
ATOM   1621 O O   . LEU A 1 204 ? 32.185  16.905  10.190  1.00 29.62 ?  204 LEU A O   1 
ATOM   1622 C CB  . LEU A 1 204 ? 30.845  14.970  11.644  1.00 29.66 ?  204 LEU A CB  1 
ATOM   1623 C CG  . LEU A 1 204 ? 30.603  13.974  12.777  1.00 28.41 ?  204 LEU A CG  1 
ATOM   1624 C CD1 . LEU A 1 204 ? 30.265  12.597  12.232  1.00 27.62 ?  204 LEU A CD1 1 
ATOM   1625 C CD2 . LEU A 1 204 ? 31.801  13.909  13.710  1.00 24.36 ?  204 LEU A CD2 1 
ATOM   1626 N N   . VAL A 1 205 ? 31.038  18.632  11.042  1.00 29.42 ?  205 VAL A N   1 
ATOM   1627 C CA  . VAL A 1 205 ? 31.721  19.606  10.152  1.00 32.00 ?  205 VAL A CA  1 
ATOM   1628 C C   . VAL A 1 205 ? 33.103  19.856  10.757  1.00 34.22 ?  205 VAL A C   1 
ATOM   1629 O O   . VAL A 1 205 ? 33.179  19.966  11.980  1.00 35.69 ?  205 VAL A O   1 
ATOM   1630 C CB  . VAL A 1 205 ? 30.892  20.869  9.931   1.00 35.68 ?  205 VAL A CB  1 
ATOM   1631 C CG1 . VAL A 1 205 ? 31.594  21.798  8.971   1.00 40.99 ?  205 VAL A CG1 1 
ATOM   1632 C CG2 . VAL A 1 205 ? 29.525  20.514  9.407   1.00 31.15 ?  205 VAL A CG2 1 
ATOM   1633 N N   . LEU A 1 206 ? 34.143  19.856  9.929   1.00 38.50 ?  206 LEU A N   1 
ATOM   1634 C CA  . LEU A 1 206 ? 35.533  19.946  10.418  1.00 35.43 ?  206 LEU A CA  1 
ATOM   1635 C C   . LEU A 1 206 ? 36.026  21.366  10.189  1.00 44.03 ?  206 LEU A C   1 
ATOM   1636 O O   . LEU A 1 206 ? 37.077  21.728  10.689  1.00 42.30 ?  206 LEU A O   1 
ATOM   1637 C CB  . LEU A 1 206 ? 36.343  18.878  9.693   1.00 32.27 ?  206 LEU A CB  1 
ATOM   1638 C CG  . LEU A 1 206 ? 35.844  17.449  9.896   1.00 33.04 ?  206 LEU A CG  1 
ATOM   1639 C CD1 . LEU A 1 206 ? 36.777  16.446  9.246   1.00 34.79 ?  206 LEU A CD1 1 
ATOM   1640 C CD2 . LEU A 1 206 ? 35.682  17.137  11.373  1.00 32.17 ?  206 LEU A CD2 1 
ATOM   1641 N N   . THR A 1 207 ? 35.320  22.111  9.374   1.00 42.22 ?  207 THR A N   1 
ATOM   1642 C CA  . THR A 1 207 ? 35.585  23.532  9.257   1.00 47.34 ?  207 THR A CA  1 
ATOM   1643 C C   . THR A 1 207 ? 34.643  24.303  10.177  1.00 48.62 ?  207 THR A C   1 
ATOM   1644 O O   . THR A 1 207 ? 33.642  23.777  10.671  1.00 52.02 ?  207 THR A O   1 
ATOM   1645 C CB  . THR A 1 207 ? 35.409  23.984  7.809   1.00 43.11 ?  207 THR A CB  1 
ATOM   1646 O OG1 . THR A 1 207 ? 34.053  23.753  7.415   1.00 45.80 ?  207 THR A OG1 1 
ATOM   1647 C CG2 . THR A 1 207 ? 36.328  23.190  6.888   1.00 40.90 ?  207 THR A CG2 1 
ATOM   1648 N N   . ASP A 1 208 ? 34.979  25.570  10.407  1.00 47.12 ?  208 ASP A N   1 
ATOM   1649 C CA  . ASP A 1 208 ? 34.097  26.446  11.165  1.00 44.01 ?  208 ASP A CA  1 
ATOM   1650 C C   . ASP A 1 208 ? 32.847  26.835  10.381  1.00 47.49 ?  208 ASP A C   1 
ATOM   1651 O O   . ASP A 1 208 ? 31.971  27.497  10.946  1.00 48.30 ?  208 ASP A O   1 
ATOM   1652 C CB  . ASP A 1 208 ? 34.872  27.696  11.595  1.00 44.65 ?  208 ASP A CB  1 
ATOM   1653 C CG  . ASP A 1 208 ? 34.344  28.315  12.876  1.00 46.43 ?  208 ASP A CG  1 
ATOM   1654 O OD1 . ASP A 1 208 ? 33.893  27.572  13.776  1.00 46.11 ?  208 ASP A OD1 1 
ATOM   1655 O OD2 . ASP A 1 208 ? 34.399  29.560  12.987  1.00 51.83 -1 208 ASP A OD2 1 
ATOM   1656 N N   . GLU A 1 209 ? 32.741  26.371  9.133   1.00 49.37 ?  209 GLU A N   1 
ATOM   1657 C CA  . GLU A 1 209 ? 31.528  26.620  8.292   1.00 53.02 ?  209 GLU A CA  1 
ATOM   1658 C C   . GLU A 1 209 ? 30.392  25.726  8.785   1.00 50.37 ?  209 GLU A C   1 
ATOM   1659 O O   . GLU A 1 209 ? 30.232  24.652  8.200   1.00 54.18 ?  209 GLU A O   1 
ATOM   1660 C CB  . GLU A 1 209 ? 31.753  26.273  6.822   1.00 48.87 ?  209 GLU A CB  1 
ATOM   1661 C CG  . GLU A 1 209 ? 33.114  26.642  6.261   1.00 49.74 ?  209 GLU A CG  1 
ATOM   1662 C CD  . GLU A 1 209 ? 33.396  26.042  4.892   1.00 52.00 ?  209 GLU A CD  1 
ATOM   1663 O OE1 . GLU A 1 209 ? 33.032  26.670  3.886   1.00 56.60 ?  209 GLU A OE1 1 
ATOM   1664 O OE2 . GLU A 1 209 ? 33.976  24.949  4.830   1.00 52.50 -1 209 GLU A OE2 1 
ATOM   1665 N N   . ASP A 1 210 ? 29.596  26.175  9.752   1.00 45.35 ?  210 ASP A N   1 
ATOM   1666 C CA  . ASP A 1 210 ? 28.610  25.230  10.327  1.00 42.78 ?  210 ASP A CA  1 
ATOM   1667 C C   . ASP A 1 210 ? 27.457  24.910  9.398   1.00 41.45 ?  210 ASP A C   1 
ATOM   1668 O O   . ASP A 1 210 ? 27.235  25.617  8.417   1.00 41.94 ?  210 ASP A O   1 
ATOM   1669 C CB  . ASP A 1 210 ? 27.897  25.704  11.576  1.00 43.00 ?  210 ASP A CB  1 
ATOM   1670 C CG  . ASP A 1 210 ? 27.646  24.587  12.579  1.00 43.87 ?  210 ASP A CG  1 
ATOM   1671 O OD1 . ASP A 1 210 ? 27.832  23.414  12.237  1.00 45.55 ?  210 ASP A OD1 1 
ATOM   1672 O OD2 . ASP A 1 210 ? 27.478  24.955  13.664  1.00 47.17 -1 210 ASP A OD2 1 
ATOM   1673 N N   . ILE A 1 211 ? 26.691  23.925  9.816   1.00 40.92 ?  211 ILE A N   1 
ATOM   1674 C CA  . ILE A 1 211 ? 25.595  23.436  8.952   1.00 35.01 ?  211 ILE A CA  1 
ATOM   1675 C C   . ILE A 1 211 ? 24.402  24.370  9.048   1.00 33.57 ?  211 ILE A C   1 
ATOM   1676 O O   . ILE A 1 211 ? 24.285  25.073  10.055  1.00 34.60 ?  211 ILE A O   1 
ATOM   1677 C CB  . ILE A 1 211 ? 25.176  22.008  9.353   1.00 34.46 ?  211 ILE A CB  1 
ATOM   1678 C CG1 . ILE A 1 211 ? 24.769  21.874  10.817  1.00 36.82 ?  211 ILE A CG1 1 
ATOM   1679 C CG2 . ILE A 1 211 ? 26.206  20.985  8.954   1.00 37.43 ?  211 ILE A CG2 1 
ATOM   1680 C CD1 . ILE A 1 211 ? 23.678  20.863  11.011  1.00 36.48 ?  211 ILE A CD1 1 
ATOM   1681 N N   . THR A 1 212 ? 23.623  24.449  7.979   1.00 27.95 ?  212 THR A N   1 
ATOM   1682 C CA  . THR A 1 212 ? 22.349  25.143  8.052   1.00 26.52 ?  212 THR A CA  1 
ATOM   1683 C C   . THR A 1 212 ? 21.283  24.070  8.138   1.00 27.81 ?  212 THR A C   1 
ATOM   1684 O O   . THR A 1 212 ? 20.954  23.442  7.121   1.00 28.55 ?  212 THR A O   1 
ATOM   1685 C CB  . THR A 1 212 ? 22.139  26.028  6.823   1.00 27.79 ?  212 THR A CB  1 
ATOM   1686 O OG1 . THR A 1 212 ? 23.209  26.980  6.762   1.00 29.26 ?  212 THR A OG1 1 
ATOM   1687 C CG2 . THR A 1 212 ? 20.784  26.749  6.888   1.00 25.22 ?  212 THR A CG2 1 
ATOM   1688 N N   . PRO A 1 213 ? 20.758  23.781  9.320   1.00 25.80 ?  213 PRO A N   1 
ATOM   1689 C CA  . PRO A 1 213 ? 19.690  22.780  9.417   1.00 25.78 ?  213 PRO A CA  1 
ATOM   1690 C C   . PRO A 1 213 ? 18.450  23.232  8.654   1.00 26.85 ?  213 PRO A C   1 
ATOM   1691 O O   . PRO A 1 213 ? 18.103  24.419  8.626   1.00 25.75 ?  213 PRO A O   1 
ATOM   1692 C CB  . PRO A 1 213 ? 19.436  22.678  10.925  1.00 25.89 ?  213 PRO A CB  1 
ATOM   1693 C CG  . PRO A 1 213 ? 20.739  23.146  11.574  1.00 27.23 ?  213 PRO A CG  1 
ATOM   1694 C CD  . PRO A 1 213 ? 21.217  24.249  10.642  1.00 27.71 ?  213 PRO A CD  1 
ATOM   1695 N N   . ALA A 1 214 ? 17.772  22.265  8.029   1.00 25.15 ?  214 ALA A N   1 
ATOM   1696 C CA  . ALA A 1 214 ? 16.600  22.604  7.228   1.00 24.01 ?  214 ALA A CA  1 
ATOM   1697 C C   . ALA A 1 214 ? 15.553  23.338  8.053   1.00 26.96 ?  214 ALA A C   1 
ATOM   1698 O O   . ALA A 1 214 ? 14.909  24.269  7.554   1.00 25.60 ?  214 ALA A O   1 
ATOM   1699 C CB  . ALA A 1 214 ? 16.002  21.344  6.604   1.00 24.73 ?  214 ALA A CB  1 
ATOM   1700 N N   . PHE A 1 215 ? 15.389  22.972  9.330   1.00 21.95 ?  215 PHE A N   1 
ATOM   1701 C CA  . PHE A 1 215 ? 14.380  23.670  10.125  1.00 23.94 ?  215 PHE A CA  1 
ATOM   1702 C C   . PHE A 1 215 ? 14.679  25.153  10.338  1.00 28.20 ?  215 PHE A C   1 
ATOM   1703 O O   . PHE A 1 215 ? 13.827  25.850  10.907  1.00 26.95 ?  215 PHE A O   1 
ATOM   1704 C CB  . PHE A 1 215 ? 14.178  23.006  11.490  1.00 25.24 ?  215 PHE A CB  1 
ATOM   1705 C CG  . PHE A 1 215 ? 15.330  23.174  12.452  1.00 26.27 ?  215 PHE A CG  1 
ATOM   1706 C CD1 . PHE A 1 215 ? 15.437  24.311  13.255  1.00 29.00 ?  215 PHE A CD1 1 
ATOM   1707 C CD2 . PHE A 1 215 ? 16.266  22.168  12.604  1.00 24.10 ?  215 PHE A CD2 1 
ATOM   1708 C CE1 . PHE A 1 215 ? 16.480  24.458  14.160  1.00 26.64 ?  215 PHE A CE1 1 
ATOM   1709 C CE2 . PHE A 1 215 ? 17.306  22.299  13.523  1.00 29.96 ?  215 PHE A CE2 1 
ATOM   1710 C CZ  . PHE A 1 215 ? 17.421  23.455  14.289  1.00 28.27 ?  215 PHE A CZ  1 
ATOM   1711 N N   . THR A 1 216 ? 15.835  25.654  9.910   1.00 25.94 ?  216 THR A N   1 
ATOM   1712 C CA  . THR A 1 216 ? 16.174  27.100  10.074  1.00 27.30 ?  216 THR A CA  1 
ATOM   1713 C C   . THR A 1 216 ? 15.517  27.985  9.010   1.00 30.58 ?  216 THR A C   1 
ATOM   1714 O O   . THR A 1 216 ? 15.477  29.192  9.217   1.00 28.08 ?  216 THR A O   1 
ATOM   1715 C CB  . THR A 1 216 ? 17.683  27.374  10.030  1.00 30.20 ?  216 THR A CB  1 
ATOM   1716 O OG1 . THR A 1 216 ? 18.226  27.041  8.760   1.00 26.25 ?  216 THR A OG1 1 
ATOM   1717 C CG2 . THR A 1 216 ? 18.406  26.672  11.155  1.00 29.74 ?  216 THR A CG2 1 
ATOM   1718 N N   . VAL A 1 217 ? 15.120  27.386  7.879   1.00 28.36 ?  217 VAL A N   1 
ATOM   1719 C CA  . VAL A 1 217 ? 14.530  28.145  6.741   1.00 27.73 ?  217 VAL A CA  1 
ATOM   1720 C C   . VAL A 1 217 ? 13.338  28.927  7.245   1.00 29.59 ?  217 VAL A C   1 
ATOM   1721 O O   . VAL A 1 217 ? 12.637  28.426  8.108   1.00 31.28 ?  217 VAL A O   1 
ATOM   1722 C CB  . VAL A 1 217 ? 14.227  27.279  5.509   1.00 27.56 ?  217 VAL A CB  1 
ATOM   1723 C CG1 . VAL A 1 217 ? 15.491  26.609  4.999   1.00 30.38 ?  217 VAL A CG1 1 
ATOM   1724 C CG2 . VAL A 1 217 ? 13.141  26.253  5.753   1.00 33.46 ?  217 VAL A CG2 1 
ATOM   1725 N N   . ASP A 1 218 ? 13.141  30.116  6.701   1.00 30.00 ?  218 ASP A N   1 
ATOM   1726 C CA  . ASP A 1 218 ? 12.119  30.996  7.304   1.00 30.00 ?  218 ASP A CA  1 
ATOM   1727 C C   . ASP A 1 218 ? 10.745  30.414  7.151   1.00 30.00 ?  218 ASP A C   1 
ATOM   1728 O O   . ASP A 1 218 ? 10.494  29.713  6.160   1.00 30.00 ?  218 ASP A O   1 
ATOM   1729 C CB  . ASP A 1 218 ? 12.132  32.457  6.864   1.00 30.00 ?  218 ASP A CB  1 
ATOM   1730 C CG  . ASP A 1 218 ? 11.451  33.413  7.832   1.00 30.00 ?  218 ASP A CG  1 
ATOM   1731 O OD1 . ASP A 1 218 ? 11.210  33.014  8.984   1.00 30.00 ?  218 ASP A OD1 1 
ATOM   1732 O OD2 . ASP A 1 218 ? 11.156  34.544  7.422   1.00 30.00 -1 218 ASP A OD2 1 
ATOM   1733 N N   . TRP A 1 219 ? 9.750   30.911  7.853   1.00 30.00 ?  219 TRP A N   1 
ATOM   1734 C CA  . TRP A 1 219 ? 8.393   30.338  7.779   1.00 30.00 ?  219 TRP A CA  1 
ATOM   1735 C C   . TRP A 1 219 ? 7.768   30.294  6.403   1.00 30.00 ?  219 TRP A C   1 
ATOM   1736 O O   . TRP A 1 219 ? 8.217   31.028  5.499   1.00 30.00 ?  219 TRP A O   1 
ATOM   1737 C CB  . TRP A 1 219 ? 7.422   30.920  8.809   1.00 30.00 ?  219 TRP A CB  1 
ATOM   1738 C CG  . TRP A 1 219 ? 7.542   30.267  10.146  1.00 30.00 ?  219 TRP A CG  1 
ATOM   1739 C CD1 . TRP A 1 219 ? 8.124   30.784  11.263  1.00 30.00 ?  219 TRP A CD1 1 
ATOM   1740 C CD2 . TRP A 1 219 ? 7.064   28.961  10.504  1.00 30.00 ?  219 TRP A CD2 1 
ATOM   1741 N NE1 . TRP A 1 219 ? 8.043   29.889  12.293  1.00 30.00 ?  219 TRP A NE1 1 
ATOM   1742 C CE2 . TRP A 1 219 ? 7.389   28.767  11.861  1.00 30.00 ?  219 TRP A CE2 1 
ATOM   1743 C CE3 . TRP A 1 219 ? 6.389   27.947  9.818   1.00 30.00 ?  219 TRP A CE3 1 
ATOM   1744 C CZ2 . TRP A 1 219 ? 7.068   27.595  12.539  1.00 30.00 ?  219 TRP A CZ2 1 
ATOM   1745 C CZ3 . TRP A 1 219 ? 6.080   26.789  10.491  1.00 30.00 ?  219 TRP A CZ3 1 
ATOM   1746 C CH2 . TRP A 1 219 ? 6.412   26.618  11.832  1.00 30.00 ?  219 TRP A CH2 1 
ATOM   1747 N N   . ASP A 1 220 ? 6.639   29.605  6.372   1.00 30.00 ?  220 ASP A N   1 
ATOM   1748 C CA  . ASP A 1 220 ? 5.946   29.309  5.116   1.00 30.00 ?  220 ASP A CA  1 
ATOM   1749 C C   . ASP A 1 220 ? 6.774   28.134  4.450   1.00 30.00 ?  220 ASP A C   1 
ATOM   1750 O O   . ASP A 1 220 ? 6.228   27.052  4.379   1.00 30.00 ?  220 ASP A O   1 
ATOM   1751 C CB  . ASP A 1 220 ? 5.764   30.430  4.102   1.00 30.00 ?  220 ASP A CB  1 
ATOM   1752 C CG  . ASP A 1 220 ? 5.085   31.643  4.714   1.00 30.00 ?  220 ASP A CG  1 
ATOM   1753 O OD1 . ASP A 1 220 ? 4.324   31.450  5.680   1.00 30.00 ?  220 ASP A OD1 1 
ATOM   1754 O OD2 . ASP A 1 220 ? 5.352   32.768  4.241   1.00 30.00 -1 220 ASP A OD2 1 
ATOM   1755 N N   . ALA A 1 221 ? 8.034   28.290  3.969   1.00 37.39 ?  221 ALA A N   1 
ATOM   1756 C CA  . ALA A 1 221 ? 8.863   27.160  3.423   1.00 34.57 ?  221 ALA A CA  1 
ATOM   1757 C C   . ALA A 1 221 ? 9.240   26.172  4.528   1.00 31.18 ?  221 ALA A C   1 
ATOM   1758 O O   . ALA A 1 221 ? 9.427   25.008  4.244   1.00 31.37 ?  221 ALA A O   1 
ATOM   1759 C CB  . ALA A 1 221 ? 10.123  27.643  2.766   1.00 32.96 ?  221 ALA A CB  1 
ATOM   1760 N N   . LYS A 1 222 ? 9.480   26.672  5.710   1.00 29.22 ?  222 LYS A N   1 
ATOM   1761 C CA  . LYS A 1 222 ? 9.679   25.856  6.930   1.00 32.42 ?  222 LYS A CA  1 
ATOM   1762 C C   . LYS A 1 222 ? 8.545   24.822  7.046   1.00 29.32 ?  222 LYS A C   1 
ATOM   1763 O O   . LYS A 1 222 ? 8.783   23.762  7.606   1.00 29.03 ?  222 LYS A O   1 
ATOM   1764 C CB  . LYS A 1 222 ? 9.796   26.725  8.180   1.00 28.40 ?  222 LYS A CB  1 
ATOM   1765 C CG  . LYS A 1 222 ? 10.625  26.166  9.317   1.00 30.00 ?  222 LYS A CG  1 
ATOM   1766 C CD  . LYS A 1 222 ? 10.304  26.823  10.637  1.00 32.91 ?  222 LYS A CD  1 
ATOM   1767 C CE  . LYS A 1 222 ? 10.813  28.237  10.780  1.00 30.20 ?  222 LYS A CE  1 
ATOM   1768 N NZ  . LYS A 1 222 ? 12.280  28.270  10.949  1.00 28.90 1  222 LYS A NZ  1 
ATOM   1769 N N   . ASN A 1 223 ? 7.371   25.137  6.504   1.00 29.39 ?  223 ASN A N   1 
ATOM   1770 C CA  . ASN A 1 223 ? 6.281   24.161  6.572   1.00 28.85 ?  223 ASN A CA  1 
ATOM   1771 C C   . ASN A 1 223 ? 6.502   22.948  5.686   1.00 27.34 ?  223 ASN A C   1 
ATOM   1772 O O   . ASN A 1 223 ? 5.672   22.020  5.727   1.00 28.20 ?  223 ASN A O   1 
ATOM   1773 C CB  . ASN A 1 223 ? 4.955   24.816  6.185   1.00 29.20 ?  223 ASN A CB  1 
ATOM   1774 C CG  . ASN A 1 223 ? 4.407   25.689  7.283   1.00 33.29 ?  223 ASN A CG  1 
ATOM   1775 O OD1 . ASN A 1 223 ? 4.347   25.278  8.443   1.00 34.11 ?  223 ASN A OD1 1 
ATOM   1776 N ND2 . ASN A 1 223 ? 4.026   26.906  6.931   1.00 30.47 ?  223 ASN A ND2 1 
ATOM   1777 N N   . TRP A 1 224 ? 7.573   22.918  4.891   1.00 24.71 ?  224 TRP A N   1 
ATOM   1778 C CA  . TRP A 1 224 ? 7.820   21.812  3.974   1.00 25.13 ?  224 TRP A CA  1 
ATOM   1779 C C   . TRP A 1 224 ? 9.085   21.031  4.300   1.00 23.96 ?  224 TRP A C   1 
ATOM   1780 O O   . TRP A 1 224 ? 9.515   20.220  3.478   1.00 23.88 ?  224 TRP A O   1 
ATOM   1781 C CB  . TRP A 1 224 ? 7.878   22.338  2.535   1.00 24.83 ?  224 TRP A CB  1 
ATOM   1782 C CG  . TRP A 1 224 ? 6.549   22.850  2.104   1.00 22.91 ?  224 TRP A CG  1 
ATOM   1783 C CD1 . TRP A 1 224 ? 6.071   24.126  2.233   1.00 28.14 ?  224 TRP A CD1 1 
ATOM   1784 C CD2 . TRP A 1 224 ? 5.500   22.085  1.509   1.00 27.58 ?  224 TRP A CD2 1 
ATOM   1785 N NE1 . TRP A 1 224 ? 4.790   24.201  1.735   1.00 29.05 ?  224 TRP A NE1 1 
ATOM   1786 C CE2 . TRP A 1 224 ? 4.420   22.960  1.282   1.00 29.05 ?  224 TRP A CE2 1 
ATOM   1787 C CE3 . TRP A 1 224 ? 5.377   20.746  1.123   1.00 30.14 ?  224 TRP A CE3 1 
ATOM   1788 C CZ2 . TRP A 1 224 ? 3.232   22.537  0.711   1.00 26.02 ?  224 TRP A CZ2 1 
ATOM   1789 C CZ3 . TRP A 1 224 ? 4.188   20.330  0.547   1.00 28.35 ?  224 TRP A CZ3 1 
ATOM   1790 C CH2 . TRP A 1 224 ? 3.134   21.226  0.350   1.00 25.86 ?  224 TRP A CH2 1 
ATOM   1791 N N   . VAL A 1 225 ? 9.694   21.237  5.476   1.00 22.67 ?  225 VAL A N   1 
ATOM   1792 C CA  . VAL A 1 225 ? 10.955  20.579  5.787   1.00 25.86 ?  225 VAL A CA  1 
ATOM   1793 C C   . VAL A 1 225 ? 10.800  19.687  7.009   1.00 20.87 ?  225 VAL A C   1 
ATOM   1794 O O   . VAL A 1 225 ? 9.974   19.924  7.905   1.00 22.01 ?  225 VAL A O   1 
ATOM   1795 C CB  . VAL A 1 225 ? 12.115  21.576  6.019   1.00 24.36 ?  225 VAL A CB  1 
ATOM   1796 C CG1 . VAL A 1 225 ? 12.252  22.531  4.842   1.00 26.65 ?  225 VAL A CG1 1 
ATOM   1797 C CG2 . VAL A 1 225 ? 11.920  22.318  7.333   1.00 27.65 ?  225 VAL A CG2 1 
ATOM   1798 N N   . VAL A 1 226 ? 11.620  18.641  7.021   1.00 20.53 ?  226 VAL A N   1 
ATOM   1799 C CA  . VAL A 1 226 ? 11.897  17.823  8.198   1.00 24.21 ?  226 VAL A CA  1 
ATOM   1800 C C   . VAL A 1 226 ? 13.411  17.750  8.336   1.00 21.13 ?  226 VAL A C   1 
ATOM   1801 O O   . VAL A 1 226 ? 14.111  17.470  7.357   1.00 22.46 ?  226 VAL A O   1 
ATOM   1802 C CB  . VAL A 1 226 ? 11.302  16.406  8.060   1.00 23.27 ?  226 VAL A CB  1 
ATOM   1803 C CG1 . VAL A 1 226 ? 11.766  15.490  9.211   1.00 22.29 ?  226 VAL A CG1 1 
ATOM   1804 C CG2 . VAL A 1 226 ? 9.757   16.455  7.963   1.00 21.87 ?  226 VAL A CG2 1 
ATOM   1805 N N   . SER A 1 227 ? 13.922  18.016  9.534   1.00 20.67 ?  227 SER A N   1 
ATOM   1806 C CA  . SER A 1 227 ? 15.317  17.746  9.843   1.00 18.78 ?  227 SER A CA  1 
ATOM   1807 C C   . SER A 1 227 ? 15.409  16.473  10.677  1.00 20.86 ?  227 SER A C   1 
ATOM   1808 O O   . SER A 1 227 ? 14.618  16.273  11.602  1.00 23.23 ?  227 SER A O   1 
ATOM   1809 C CB  . SER A 1 227 ? 15.960  18.912  10.621  1.00 24.12 ?  227 SER A CB  1 
ATOM   1810 O OG  . SER A 1 227 ? 16.225  20.028  9.790   1.00 23.98 ?  227 SER A OG  1 
ATOM   1811 N N   . LEU A 1 228 ? 16.373  15.614  10.353  1.00 21.07 ?  228 LEU A N   1 
ATOM   1812 C CA  . LEU A 1 228 ? 16.594  14.373  11.091  1.00 21.41 ?  228 LEU A CA  1 
ATOM   1813 C C   . LEU A 1 228 ? 18.014  14.362  11.637  1.00 20.84 ?  228 LEU A C   1 
ATOM   1814 O O   . LEU A 1 228 ? 18.968  14.503  10.871  1.00 20.10 ?  228 LEU A O   1 
ATOM   1815 C CB  . LEU A 1 228 ? 16.380  13.140  10.207  1.00 22.47 ?  228 LEU A CB  1 
ATOM   1816 C CG  . LEU A 1 228 ? 15.040  13.006  9.493   1.00 23.71 ?  228 LEU A CG  1 
ATOM   1817 C CD1 . LEU A 1 228 ? 15.147  11.889  8.467   1.00 21.43 ?  228 LEU A CD1 1 
ATOM   1818 C CD2 . LEU A 1 228 ? 13.907  12.777  10.486  1.00 22.66 ?  228 LEU A CD2 1 
ATOM   1819 N N   . ILE A 1 229 ? 18.155  14.178  12.951  1.00 20.59 ?  229 ILE A N   1 
ATOM   1820 C CA  . ILE A 1 229 ? 19.460  14.135  13.598  1.00 19.57 ?  229 ILE A CA  1 
ATOM   1821 C C   . ILE A 1 229 ? 19.516  12.911  14.497  1.00 24.34 ?  229 ILE A C   1 
ATOM   1822 O O   . ILE A 1 229 ? 18.499  12.281  14.799  1.00 23.31 ?  229 ILE A O   1 
ATOM   1823 C CB  . ILE A 1 229 ? 19.761  15.407  14.430  1.00 24.63 ?  229 ILE A CB  1 
ATOM   1824 C CG1 . ILE A 1 229 ? 18.854  15.471  15.664  1.00 20.70 ?  229 ILE A CG1 1 
ATOM   1825 C CG2 . ILE A 1 229 ? 19.631  16.669  13.558  1.00 23.58 ?  229 ILE A CG2 1 
ATOM   1826 C CD1 . ILE A 1 229 ? 19.213  16.603  16.649  1.00 23.90 ?  229 ILE A CD1 1 
ATOM   1827 N N   . SER A 1 230 ? 20.734  12.590  14.937  1.00 21.85 ?  230 SER A N   1 
ATOM   1828 C CA  . SER A 1 230 ? 20.947  11.479  15.851  1.00 19.97 ?  230 SER A CA  1 
ATOM   1829 C C   . SER A 1 230 ? 22.313  11.654  16.498  1.00 23.16 ?  230 SER A C   1 
ATOM   1830 O O   . SER A 1 230 ? 23.210  12.240  15.888  1.00 21.48 ?  230 SER A O   1 
ATOM   1831 C CB  . SER A 1 230 ? 20.877  10.135  15.111  1.00 21.70 ?  230 SER A CB  1 
ATOM   1832 O OG  . SER A 1 230 ? 21.295  9.054   15.937  1.00 22.97 ?  230 SER A OG  1 
ATOM   1833 N N   . PRO A 1 231 ? 22.506  11.154  17.717  1.00 23.00 ?  231 PRO A N   1 
ATOM   1834 C CA  . PRO A 1 231 ? 23.862  11.082  18.274  1.00 23.66 ?  231 PRO A CA  1 
ATOM   1835 C C   . PRO A 1 231 ? 24.694  9.945   17.700  1.00 23.54 ?  231 PRO A C   1 
ATOM   1836 O O   . PRO A 1 231 ? 25.883  9.862   18.019  1.00 25.29 ?  231 PRO A O   1 
ATOM   1837 C CB  . PRO A 1 231 ? 23.600  10.870  19.773  1.00 25.03 ?  231 PRO A CB  1 
ATOM   1838 C CG  . PRO A 1 231 ? 22.303  10.156  19.817  1.00 25.14 ?  231 PRO A CG  1 
ATOM   1839 C CD  . PRO A 1 231 ? 21.483  10.754  18.695  1.00 19.63 ?  231 PRO A CD  1 
ATOM   1840 N N   . SER A 1 232 ? 24.119  9.112   16.825  1.00 24.08 ?  232 SER A N   1 
ATOM   1841 C CA  . SER A 1 232 ? 24.731  7.826   16.473  1.00 24.26 ?  232 SER A CA  1 
ATOM   1842 C C   . SER A 1 232 ? 26.043  7.989   15.708  1.00 22.86 ?  232 SER A C   1 
ATOM   1843 O O   . SER A 1 232 ? 27.042  7.340   16.042  1.00 25.78 ?  232 SER A O   1 
ATOM   1844 C CB  . SER A 1 232 ? 23.749  6.980   15.653  1.00 23.40 ?  232 SER A CB  1 
ATOM   1845 O OG  . SER A 1 232 ? 23.579  7.526   14.361  1.00 28.35 ?  232 SER A OG  1 
ATOM   1846 N N   . LYS A 1 233 ? 26.056  8.808   14.644  1.00 21.31 ?  233 LYS A N   1 
ATOM   1847 C CA  . LYS A 1 233 ? 27.306  9.008   13.905  1.00 24.55 ?  233 LYS A CA  1 
ATOM   1848 C C   . LYS A 1 233 ? 28.274  9.870   14.706  1.00 24.98 ?  233 LYS A C   1 
ATOM   1849 O O   . LYS A 1 233 ? 29.477  9.581   14.782  1.00 24.44 ?  233 LYS A O   1 
ATOM   1850 C CB  . LYS A 1 233 ? 27.031  9.654   12.537  1.00 26.24 ?  233 LYS A CB  1 
ATOM   1851 C CG  . LYS A 1 233 ? 26.489  8.719   11.465  1.00 32.86 ?  233 LYS A CG  1 
ATOM   1852 C CD  . LYS A 1 233 ? 27.410  7.546   11.180  1.00 32.42 ?  233 LYS A CD  1 
ATOM   1853 C CE  . LYS A 1 233 ? 26.633  6.376   10.574  1.00 36.56 ?  233 LYS A CE  1 
ATOM   1854 N NZ  . LYS A 1 233 ? 25.780  6.812   9.448   1.00 40.76 1  233 LYS A NZ  1 
ATOM   1855 N N   . THR A 1 234 ? 27.759  10.934  15.309  1.00 20.32 ?  234 THR A N   1 
ATOM   1856 C CA  . THR A 1 234 ? 28.600  11.855  16.069  1.00 24.85 ?  234 THR A CA  1 
ATOM   1857 C C   . THR A 1 234 ? 29.361  11.153  17.185  1.00 23.93 ?  234 THR A C   1 
ATOM   1858 O O   . THR A 1 234 ? 30.549  11.426  17.394  1.00 23.13 ?  234 THR A O   1 
ATOM   1859 C CB  . THR A 1 234 ? 27.740  12.954  16.667  1.00 21.44 ?  234 THR A CB  1 
ATOM   1860 O OG1 . THR A 1 234 ? 27.024  13.603  15.624  1.00 25.11 ?  234 THR A OG1 1 
ATOM   1861 C CG2 . THR A 1 234 ? 28.618  13.967  17.450  1.00 24.28 ?  234 THR A CG2 1 
ATOM   1862 N N   . PHE A 1 235 ? 28.696  10.270  17.936  1.00 21.60 ?  235 PHE A N   1 
ATOM   1863 C CA  . PHE A 1 235 ? 29.280  9.740   19.163  1.00 19.93 ?  235 PHE A CA  1 
ATOM   1864 C C   . PHE A 1 235 ? 29.567  8.247   19.118  1.00 22.60 ?  235 PHE A C   1 
ATOM   1865 O O   . PHE A 1 235 ? 29.857  7.670   20.169  1.00 21.05 ?  235 PHE A O   1 
ATOM   1866 C CB  . PHE A 1 235 ? 28.379  10.041  20.362  1.00 21.78 ?  235 PHE A CB  1 
ATOM   1867 C CG  . PHE A 1 235 ? 28.222  11.506  20.644  1.00 21.21 ?  235 PHE A CG  1 
ATOM   1868 C CD1 . PHE A 1 235 ? 29.211  12.208  21.336  1.00 22.96 ?  235 PHE A CD1 1 
ATOM   1869 C CD2 . PHE A 1 235 ? 27.082  12.184  20.219  1.00 22.27 ?  235 PHE A CD2 1 
ATOM   1870 C CE1 . PHE A 1 235 ? 29.063  13.572  21.602  1.00 26.22 ?  235 PHE A CE1 1 
ATOM   1871 C CE2 . PHE A 1 235 ? 26.920  13.546  20.482  1.00 22.92 ?  235 PHE A CE2 1 
ATOM   1872 C CZ  . PHE A 1 235 ? 27.917  14.243  21.177  1.00 25.93 ?  235 PHE A CZ  1 
ATOM   1873 N N   . ASN A 1 236 ? 29.502  7.614   17.940  1.00 18.73 ?  236 ASN A N   1 
ATOM   1874 C CA  . ASN A 1 236 ? 29.775  6.171   17.782  1.00 23.14 ?  236 ASN A CA  1 
ATOM   1875 C C   . ASN A 1 236 ? 28.726  5.312   18.494  1.00 23.36 ?  236 ASN A C   1 
ATOM   1876 O O   . ASN A 1 236 ? 29.055  4.380   19.234  1.00 20.22 ?  236 ASN A O   1 
ATOM   1877 C CB  . ASN A 1 236 ? 31.185  5.789   18.258  1.00 22.38 ?  236 ASN A CB  1 
ATOM   1878 C CG  . ASN A 1 236 ? 31.660  4.504   17.636  1.00 23.97 ?  236 ASN A CG  1 
ATOM   1879 O OD1 . ASN A 1 236 ? 31.105  4.067   16.620  1.00 25.50 ?  236 ASN A OD1 1 
ATOM   1880 N ND2 . ASN A 1 236 ? 32.678  3.882   18.227  1.00 23.93 ?  236 ASN A ND2 1 
ATOM   1881 N N   . LEU A 1 237 ? 27.453  5.619   18.243  1.00 20.92 ?  237 LEU A N   1 
ATOM   1882 C CA  . LEU A 1 237 ? 26.312  5.016   18.931  1.00 18.27 ?  237 LEU A CA  1 
ATOM   1883 C C   . LEU A 1 237 ? 25.295  4.461   17.941  1.00 20.83 ?  237 LEU A C   1 
ATOM   1884 O O   . LEU A 1 237 ? 24.087  4.604   18.132  1.00 19.66 ?  237 LEU A O   1 
ATOM   1885 C CB  . LEU A 1 237 ? 25.630  6.033   19.837  1.00 21.30 ?  237 LEU A CB  1 
ATOM   1886 C CG  . LEU A 1 237 ? 26.503  6.518   20.996  1.00 23.26 ?  237 LEU A CG  1 
ATOM   1887 C CD1 . LEU A 1 237 ? 25.862  7.707   21.675  1.00 21.54 ?  237 LEU A CD1 1 
ATOM   1888 C CD2 . LEU A 1 237 ? 26.744  5.360   21.974  1.00 22.37 ?  237 LEU A CD2 1 
ATOM   1889 N N   . ALA A 1 238 ? 25.773  3.820   16.873  1.00 21.12 ?  238 ALA A N   1 
ATOM   1890 C CA  . ALA A 1 238 ? 24.876  3.229   15.878  1.00 22.51 ?  238 ALA A CA  1 
ATOM   1891 C C   . ALA A 1 238 ? 23.871  2.273   16.506  1.00 21.93 ?  238 ALA A C   1 
ATOM   1892 O O   . ALA A 1 238 ? 22.724  2.196   16.054  1.00 24.87 ?  238 ALA A O   1 
ATOM   1893 C CB  . ALA A 1 238 ? 25.686  2.494   14.812  1.00 22.85 ?  238 ALA A CB  1 
ATOM   1894 N N   . ALA A 1 239 ? 24.269  1.528   17.529  1.00 19.45 ?  239 ALA A N   1 
ATOM   1895 C CA  . ALA A 1 239 ? 23.367  0.550   18.122  1.00 16.98 ?  239 ALA A CA  1 
ATOM   1896 C C   . ALA A 1 239 ? 22.590  1.110   19.300  1.00 19.59 ?  239 ALA A C   1 
ATOM   1897 O O   . ALA A 1 239 ? 21.866  0.353   19.958  1.00 20.16 ?  239 ALA A O   1 
ATOM   1898 C CB  . ALA A 1 239 ? 24.129  -0.714  18.539  1.00 16.61 ?  239 ALA A CB  1 
ATOM   1899 N N   . LEU A 1 240 ? 22.694  2.418   19.561  1.00 20.64 ?  240 LEU A N   1 
ATOM   1900 C CA  . LEU A 1 240 ? 21.885  3.027   20.612  1.00 20.62 ?  240 LEU A CA  1 
ATOM   1901 C C   . LEU A 1 240 ? 20.429  3.139   20.190  1.00 21.21 ?  240 LEU A C   1 
ATOM   1902 O O   . LEU A 1 240 ? 19.520  2.973   21.015  1.00 22.89 ?  240 LEU A O   1 
ATOM   1903 C CB  . LEU A 1 240 ? 22.416  4.416   20.965  1.00 20.77 ?  240 LEU A CB  1 
ATOM   1904 C CG  . LEU A 1 240 ? 21.585  5.147   22.028  1.00 23.96 ?  240 LEU A CG  1 
ATOM   1905 C CD1 . LEU A 1 240 ? 21.478  4.278   23.283  1.00 22.28 ?  240 LEU A CD1 1 
ATOM   1906 C CD2 . LEU A 1 240 ? 22.162  6.528   22.381  1.00 22.03 ?  240 LEU A CD2 1 
ATOM   1907 N N   . HIS A 1 241 ? 20.196  3.472   18.921  1.00 20.54 ?  241 HIS A N   1 
ATOM   1908 C CA  . HIS A 1 241 ? 18.846  3.608   18.364  1.00 22.78 ?  241 HIS A CA  1 
ATOM   1909 C C   . HIS A 1 241 ? 18.118  4.795   18.997  1.00 21.70 ?  241 HIS A C   1 
ATOM   1910 O O   . HIS A 1 241 ? 16.981  4.688   19.458  1.00 22.68 ?  241 HIS A O   1 
ATOM   1911 C CB  . HIS A 1 241 ? 18.044  2.312   18.505  1.00 18.64 ?  241 HIS A CB  1 
ATOM   1912 C CG  . HIS A 1 241 ? 18.603  1.178   17.703  1.00 19.28 ?  241 HIS A CG  1 
ATOM   1913 N ND1 . HIS A 1 241 ? 18.095  -0.101  17.761  1.00 21.80 ?  241 HIS A ND1 1 
ATOM   1914 C CD2 . HIS A 1 241 ? 19.645  1.130   16.839  1.00 20.62 ?  241 HIS A CD2 1 
ATOM   1915 C CE1 . HIS A 1 241 ? 18.797  -0.888  16.964  1.00 18.39 ?  241 HIS A CE1 1 
ATOM   1916 N NE2 . HIS A 1 241 ? 19.748  -0.168  16.397  1.00 20.02 ?  241 HIS A NE2 1 
ATOM   1917 N N   . ALA A 1 242 ? 18.794  5.942   18.998  1.00 19.51 ?  242 ALA A N   1 
ATOM   1918 C CA  . ALA A 1 242 ? 18.215  7.218   19.372  1.00 21.01 ?  242 ALA A CA  1 
ATOM   1919 C C   . ALA A 1 242 ? 18.357  8.198   18.220  1.00 23.09 ?  242 ALA A C   1 
ATOM   1920 O O   . ALA A 1 242 ? 19.433  8.308   17.614  1.00 24.42 ?  242 ALA A O   1 
ATOM   1921 C CB  . ALA A 1 242 ? 18.902  7.801   20.609  1.00 20.67 ?  242 ALA A CB  1 
ATOM   1922 N N   . ALA A 1 243 ? 17.282  8.920   17.927  1.00 19.62 ?  243 ALA A N   1 
ATOM   1923 C CA  . ALA A 1 243 ? 17.314  9.929   16.879  1.00 19.12 ?  243 ALA A CA  1 
ATOM   1924 C C   . ALA A 1 243 ? 16.190  10.915  17.147  1.00 21.30 ?  243 ALA A C   1 
ATOM   1925 O O   . ALA A 1 243 ? 15.421  10.774  18.103  1.00 20.05 ?  243 ALA A O   1 
ATOM   1926 C CB  . ALA A 1 243 ? 17.212  9.287   15.485  1.00 20.09 ?  243 ALA A CB  1 
ATOM   1927 N N   . CYS A 1 244 ? 16.099  11.934  16.306  1.00 20.71 ?  244 CYS A N   1 
ATOM   1928 C CA  . CYS A 1 244 ? 15.072  12.931  16.558  1.00 23.06 ?  244 CYS A CA  1 
ATOM   1929 C C   . CYS A 1 244 ? 14.678  13.547  15.234  1.00 18.64 ?  244 CYS A C   1 
ATOM   1930 O O   . CYS A 1 244 ? 15.544  13.886  14.425  1.00 23.30 ?  244 CYS A O   1 
ATOM   1931 C CB  . CYS A 1 244 ? 15.565  14.014  17.525  1.00 24.28 ?  244 CYS A CB  1 
ATOM   1932 S SG  . CYS A 1 244 ? 14.240  15.105  18.057  1.00 22.33 ?  244 CYS A SG  1 
ATOM   1933 N N   . ALA A 1 245 ? 13.376  13.631  14.996  1.00 18.57 ?  245 ALA A N   1 
ATOM   1934 C CA  . ALA A 1 245 ? 12.853  14.369  13.860  1.00 22.70 ?  245 ALA A CA  1 
ATOM   1935 C C   . ALA A 1 245 ? 12.478  15.760  14.344  1.00 21.08 ?  245 ALA A C   1 
ATOM   1936 O O   . ALA A 1 245 ? 11.953  15.917  15.447  1.00 24.58 ?  245 ALA A O   1 
ATOM   1937 C CB  . ALA A 1 245 ? 11.637  13.661  13.244  1.00 21.00 ?  245 ALA A CB  1 
ATOM   1938 N N   . ILE A 1 246 ? 12.797  16.769  13.545  1.00 21.43 ?  246 ILE A N   1 
ATOM   1939 C CA  . ILE A 1 246 ? 12.465  18.159  13.862  1.00 20.76 ?  246 ILE A CA  1 
ATOM   1940 C C   . ILE A 1 246 ? 11.568  18.649  12.741  1.00 21.78 ?  246 ILE A C   1 
ATOM   1941 O O   . ILE A 1 246 ? 12.025  18.825  11.604  1.00 20.35 ?  246 ILE A O   1 
ATOM   1942 C CB  . ILE A 1 246 ? 13.712  19.041  14.013  1.00 23.51 ?  246 ILE A CB  1 
ATOM   1943 C CG1 . ILE A 1 246 ? 14.617  18.453  15.107  1.00 27.15 ?  246 ILE A CG1 1 
ATOM   1944 C CG2 . ILE A 1 246 ? 13.298  20.492  14.362  1.00 20.66 ?  246 ILE A CG2 1 
ATOM   1945 C CD1 . ILE A 1 246 ? 15.932  19.201  15.351  1.00 25.44 ?  246 ILE A CD1 1 
ATOM   1946 N N   . ILE A 1 247 ? 10.287  18.840  13.054  1.00 20.57 ?  247 ILE A N   1 
ATOM   1947 C CA  . ILE A 1 247 ? 9.263   19.063  12.035  1.00 21.58 ?  247 ILE A CA  1 
ATOM   1948 C C   . ILE A 1 247 ? 8.458   20.297  12.403  1.00 22.17 ?  247 ILE A C   1 
ATOM   1949 O O   . ILE A 1 247 ? 7.506   20.198  13.191  1.00 20.86 ?  247 ILE A O   1 
ATOM   1950 C CB  . ILE A 1 247 ? 8.338   17.845  11.893  1.00 20.01 ?  247 ILE A CB  1 
ATOM   1951 C CG1 . ILE A 1 247 ? 9.168   16.568  11.739  1.00 22.41 ?  247 ILE A CG1 1 
ATOM   1952 C CG2 . ILE A 1 247 ? 7.406   18.021  10.681  1.00 21.64 ?  247 ILE A CG2 1 
ATOM   1953 C CD1 . ILE A 1 247 ? 8.352   15.294  11.864  1.00 20.85 ?  247 ILE A CD1 1 
ATOM   1954 N N   . PRO A 1 248 ? 8.806   21.495  11.867  1.00 23.82 ?  248 PRO A N   1 
ATOM   1955 C CA  . PRO A 1 248 ? 8.087   22.694  12.255  1.00 23.69 ?  248 PRO A CA  1 
ATOM   1956 C C   . PRO A 1 248 ? 6.581   22.638  12.001  1.00 26.48 ?  248 PRO A C   1 
ATOM   1957 O O   . PRO A 1 248 ? 5.849   23.102  12.826  1.00 24.53 ?  248 PRO A O   1 
ATOM   1958 C CB  . PRO A 1 248 ? 8.772   23.783  11.435  1.00 22.08 ?  248 PRO A CB  1 
ATOM   1959 C CG  . PRO A 1 248 ? 10.178  23.299  11.333  1.00 22.93 ?  248 PRO A CG  1 
ATOM   1960 C CD  . PRO A 1 248 ? 9.948   21.860  10.976  1.00 24.25 ?  248 PRO A CD  1 
ATOM   1961 N N   . ASN A 1 249 ? 6.191   22.111  10.847  1.00 26.36 ?  249 ASN A N   1 
ATOM   1962 C CA  . ASN A 1 249 ? 4.779   22.016  10.483  1.00 26.60 ?  249 ASN A CA  1 
ATOM   1963 C C   . ASN A 1 249 ? 4.091   21.030  11.422  1.00 26.00 ?  249 ASN A C   1 
ATOM   1964 O O   . ASN A 1 249 ? 4.469   19.853  11.451  1.00 28.48 ?  249 ASN A O   1 
ATOM   1965 C CB  . ASN A 1 249 ? 4.672   21.570  9.021   1.00 24.87 ?  249 ASN A CB  1 
ATOM   1966 C CG  . ASN A 1 249 ? 3.247   21.528  8.506   1.00 30.51 ?  249 ASN A CG  1 
ATOM   1967 O OD1 . ASN A 1 249 ? 2.334   21.048  9.177   1.00 28.16 ?  249 ASN A OD1 1 
ATOM   1968 N ND2 . ASN A 1 249 ? 3.058   21.996  7.273   1.00 35.51 ?  249 ASN A ND2 1 
ATOM   1969 N N   . PRO A 1 250 ? 3.094   21.447  12.204  1.00 25.71 ?  250 PRO A N   1 
ATOM   1970 C CA  . PRO A 1 250 ? 2.563   20.542  13.234  1.00 25.91 ?  250 PRO A CA  1 
ATOM   1971 C C   . PRO A 1 250 ? 1.593   19.510  12.708  1.00 25.19 ?  250 PRO A C   1 
ATOM   1972 O O   . PRO A 1 250 ? 1.408   18.481  13.367  1.00 26.10 ?  250 PRO A O   1 
ATOM   1973 C CB  . PRO A 1 250 ? 1.869   21.491  14.212  1.00 33.19 ?  250 PRO A CB  1 
ATOM   1974 C CG  . PRO A 1 250 ? 1.433   22.613  13.365  1.00 38.31 ?  250 PRO A CG  1 
ATOM   1975 C CD  . PRO A 1 250 ? 2.472   22.781  12.274  1.00 34.40 ?  250 PRO A CD  1 
ATOM   1976 N N   . ASP A 1 251 ? 0.925   19.767  11.577  1.00 25.50 ?  251 ASP A N   1 
ATOM   1977 C CA  . ASP A 1 251 ? 0.153   18.709  10.940  1.00 28.00 ?  251 ASP A CA  1 
ATOM   1978 C C   . ASP A 1 251 ? 1.078   17.602  10.462  1.00 25.42 ?  251 ASP A C   1 
ATOM   1979 O O   . ASP A 1 251 ? 0.883   16.429  10.783  1.00 24.99 ?  251 ASP A O   1 
ATOM   1980 C CB  . ASP A 1 251 ? -0.657  19.274  9.774   1.00 29.48 ?  251 ASP A CB  1 
ATOM   1981 C CG  . ASP A 1 251 ? -1.877  20.051  10.237  1.00 39.79 ?  251 ASP A CG  1 
ATOM   1982 O OD1 . ASP A 1 251 ? -2.027  20.251  11.459  1.00 36.17 ?  251 ASP A OD1 1 
ATOM   1983 O OD2 . ASP A 1 251 ? -2.683  20.471  9.371   1.00 42.88 -1 251 ASP A OD2 1 
ATOM   1984 N N   . LEU A 1 252 ? 2.101   17.973  9.697   1.00 24.50 ?  252 LEU A N   1 
ATOM   1985 C CA  . LEU A 1 252 ? 3.109   17.016  9.263   1.00 23.81 ?  252 LEU A CA  1 
ATOM   1986 C C   . LEU A 1 252 ? 3.742   16.316  10.451  1.00 25.01 ?  252 LEU A C   1 
ATOM   1987 O O   . LEU A 1 252 ? 4.010   15.108  10.412  1.00 23.82 ?  252 LEU A O   1 
ATOM   1988 C CB  . LEU A 1 252 ? 4.178   17.748  8.462   1.00 29.70 ?  252 LEU A CB  1 
ATOM   1989 C CG  . LEU A 1 252 ? 4.856   17.013  7.321   1.00 34.94 ?  252 LEU A CG  1 
ATOM   1990 C CD1 . LEU A 1 252 ? 3.804   16.433  6.375   1.00 29.49 ?  252 LEU A CD1 1 
ATOM   1991 C CD2 . LEU A 1 252 ? 5.737   18.029  6.614   1.00 34.26 ?  252 LEU A CD2 1 
ATOM   1992 N N   . ARG A 1 253 ? 3.992   17.067  11.521  1.00 22.67 ?  253 ARG A N   1 
ATOM   1993 C CA  . ARG A 1 253 ? 4.640   16.479  12.689  1.00 21.13 ?  253 ARG A CA  1 
ATOM   1994 C C   . ARG A 1 253 ? 3.757   15.421  13.328  1.00 21.95 ?  253 ARG A C   1 
ATOM   1995 O O   . ARG A 1 253 ? 4.217   14.327  13.664  1.00 22.13 ?  253 ARG A O   1 
ATOM   1996 C CB  . ARG A 1 253 ? 4.977   17.581  13.694  1.00 21.16 ?  253 ARG A CB  1 
ATOM   1997 C CG  . ARG A 1 253 ? 5.726   17.079  14.928  1.00 22.57 ?  253 ARG A CG  1 
ATOM   1998 C CD  . ARG A 1 253 ? 6.231   18.246  15.769  1.00 24.17 ?  253 ARG A CD  1 
ATOM   1999 N NE  . ARG A 1 253 ? 5.149   18.971  16.429  1.00 28.35 ?  253 ARG A NE  1 
ATOM   2000 C CZ  . ARG A 1 253 ? 4.860   20.257  16.228  1.00 26.21 ?  253 ARG A CZ  1 
ATOM   2001 N NH1 . ARG A 1 253 ? 5.558   20.983  15.366  1.00 24.99 1  253 ARG A NH1 1 
ATOM   2002 N NH2 . ARG A 1 253 ? 3.864   20.825  16.898  1.00 26.44 ?  253 ARG A NH2 1 
ATOM   2003 N N   . ALA A 1 254 ? 2.473   15.726  13.501  1.00 22.32 ?  254 ALA A N   1 
ATOM   2004 C CA  . ALA A 1 254 ? 1.584   14.731  14.084  1.00 25.45 ?  254 ALA A CA  1 
ATOM   2005 C C   . ALA A 1 254 ? 1.496   13.485  13.205  1.00 25.17 ?  254 ALA A C   1 
ATOM   2006 O O   . ALA A 1 254 ? 1.458   12.361  13.716  1.00 25.03 ?  254 ALA A O   1 
ATOM   2007 C CB  . ALA A 1 254 ? 0.198   15.333  14.314  1.00 25.29 ?  254 ALA A CB  1 
ATOM   2008 N N   . ARG A 1 255 ? 1.502   13.655  11.877  1.00 22.64 ?  255 ARG A N   1 
ATOM   2009 C CA  . ARG A 1 255 ? 1.418   12.482  11.009  1.00 23.83 ?  255 ARG A CA  1 
ATOM   2010 C C   . ARG A 1 255 ? 2.706   11.664  11.046  1.00 26.58 ?  255 ARG A C   1 
ATOM   2011 O O   . ARG A 1 255 ? 2.659   10.428  11.073  1.00 22.99 ?  255 ARG A O   1 
ATOM   2012 C CB  . ARG A 1 255 ? 1.074   12.910  9.584   1.00 27.15 ?  255 ARG A CB  1 
ATOM   2013 C CG  . ARG A 1 255 ? -0.314  13.548  9.498   1.00 26.34 ?  255 ARG A CG  1 
ATOM   2014 C CD  . ARG A 1 255 ? -0.440  14.391  8.258   1.00 28.50 ?  255 ARG A CD  1 
ATOM   2015 N NE  . ARG A 1 255 ? -0.367  13.571  7.055   1.00 29.05 ?  255 ARG A NE  1 
ATOM   2016 C CZ  . ARG A 1 255 ? -0.035  14.032  5.851   1.00 31.40 ?  255 ARG A CZ  1 
ATOM   2017 N NH1 . ARG A 1 255 ? 0.266   15.317  5.686   1.00 29.19 1  255 ARG A NH1 1 
ATOM   2018 N NH2 . ARG A 1 255 ? -0.006  13.204  4.808   1.00 30.79 ?  255 ARG A NH2 1 
ATOM   2019 N N   . ALA A 1 256 ? 3.869   12.324  11.075  1.00 23.45 ?  256 ALA A N   1 
ATOM   2020 C CA  . ALA A 1 256 ? 5.107   11.555  11.142  1.00 23.85 ?  256 ALA A CA  1 
ATOM   2021 C C   . ALA A 1 256 ? 5.221   10.818  12.470  1.00 23.60 ?  256 ALA A C   1 
ATOM   2022 O O   . ALA A 1 256 ? 5.707   9.682   12.506  1.00 23.98 ?  256 ALA A O   1 
ATOM   2023 C CB  . ALA A 1 256 ? 6.319   12.461  10.928  1.00 22.69 ?  256 ALA A CB  1 
ATOM   2024 N N   . GLU A 1 257 ? 4.776   11.448  13.567  1.00 21.81 ?  257 GLU A N   1 
ATOM   2025 C CA  . GLU A 1 257 ? 4.837   10.800  14.877  1.00 25.20 ?  257 GLU A CA  1 
ATOM   2026 C C   . GLU A 1 257 ? 4.014   9.520   14.886  1.00 26.32 ?  257 GLU A C   1 
ATOM   2027 O O   . GLU A 1 257 ? 4.435   8.504   15.440  1.00 23.63 ?  257 GLU A O   1 
ATOM   2028 C CB  . GLU A 1 257 ? 4.337   11.747  15.968  1.00 26.78 ?  257 GLU A CB  1 
ATOM   2029 C CG  . GLU A 1 257 ? 4.452   11.149  17.354  1.00 25.18 ?  257 GLU A CG  1 
ATOM   2030 C CD  . GLU A 1 257 ? 3.843   12.016  18.423  1.00 35.70 ?  257 GLU A CD  1 
ATOM   2031 O OE1 . GLU A 1 257 ? 4.098   11.733  19.609  1.00 34.03 ?  257 GLU A OE1 1 
ATOM   2032 O OE2 . GLU A 1 257 ? 3.104   12.969  18.082  1.00 31.31 -1 257 GLU A OE2 1 
ATOM   2033 N N   . GLU A 1 258 ? 2.838   9.552   14.259  1.00 25.68 ?  258 GLU A N   1 
ATOM   2034 C CA  . GLU A 1 258 ? 2.033   8.340   14.140  1.00 27.04 ?  258 GLU A CA  1 
ATOM   2035 C C   . GLU A 1 258 ? 2.711   7.309   13.242  1.00 25.16 ?  258 GLU A C   1 
ATOM   2036 O O   . GLU A 1 258 ? 2.697   6.116   13.556  1.00 27.71 ?  258 GLU A O   1 
ATOM   2037 C CB  . GLU A 1 258 ? 0.644   8.691   13.607  1.00 28.13 ?  258 GLU A CB  1 
ATOM   2038 C CG  . GLU A 1 258 ? -0.251  7.488   13.416  1.00 32.57 ?  258 GLU A CG  1 
ATOM   2039 C CD  . GLU A 1 258 ? -1.059  7.196   14.652  1.00 36.96 ?  258 GLU A CD  1 
ATOM   2040 O OE1 . GLU A 1 258 ? -2.003  6.379   14.575  1.00 44.93 ?  258 GLU A OE1 1 
ATOM   2041 O OE2 . GLU A 1 258 ? -0.755  7.795   15.705  1.00 41.83 -1 258 GLU A OE2 1 
ATOM   2042 N N   . SER A 1 259 ? 3.298   7.744   12.116  1.00 26.15 ?  259 SER A N   1 
ATOM   2043 C CA  . SER A 1 259 ? 4.036   6.807   11.267  1.00 24.82 ?  259 SER A CA  1 
ATOM   2044 C C   . SER A 1 259 ? 5.163   6.133   12.047  1.00 22.00 ?  259 SER A C   1 
ATOM   2045 O O   . SER A 1 259 ? 5.371   4.914   11.925  1.00 22.10 ?  259 SER A O   1 
ATOM   2046 C CB  . SER A 1 259 ? 4.561   7.509   10.004  1.00 23.69 ?  259 SER A CB  1 
ATOM   2047 O OG  . SER A 1 259 ? 5.788   8.221   10.226  1.00 27.67 ?  259 SER A OG  1 
ATOM   2048 N N   . PHE A 1 260 ? 5.867   6.892   12.897  1.00 20.39 ?  260 PHE A N   1 
ATOM   2049 C CA  . PHE A 1 260 ? 6.930   6.291   13.706  1.00 20.37 ?  260 PHE A CA  1 
ATOM   2050 C C   . PHE A 1 260 ? 6.358   5.264   14.671  1.00 21.55 ?  260 PHE A C   1 
ATOM   2051 O O   . PHE A 1 260 ? 6.917   4.178   14.839  1.00 20.97 ?  260 PHE A O   1 
ATOM   2052 C CB  . PHE A 1 260 ? 7.694   7.362   14.502  1.00 20.26 ?  260 PHE A CB  1 
ATOM   2053 C CG  . PHE A 1 260 ? 8.377   8.403   13.656  1.00 21.58 ?  260 PHE A CG  1 
ATOM   2054 C CD1 . PHE A 1 260 ? 8.564   8.217   12.299  1.00 24.69 ?  260 PHE A CD1 1 
ATOM   2055 C CD2 . PHE A 1 260 ? 8.826   9.583   14.239  1.00 22.11 ?  260 PHE A CD2 1 
ATOM   2056 C CE1 . PHE A 1 260 ? 9.191   9.193   11.528  1.00 23.98 ?  260 PHE A CE1 1 
ATOM   2057 C CE2 . PHE A 1 260 ? 9.448   10.558  13.484  1.00 23.45 ?  260 PHE A CE2 1 
ATOM   2058 C CZ  . PHE A 1 260 ? 9.636   10.358  12.124  1.00 25.87 ?  260 PHE A CZ  1 
ATOM   2059 N N   . PHE A 1 261 ? 5.266   5.616   15.353  1.00 20.69 ?  261 PHE A N   1 
ATOM   2060 C CA  . PHE A 1 261 ? 4.620   4.679   16.273  1.00 27.05 ?  261 PHE A CA  1 
ATOM   2061 C C   . PHE A 1 261 ? 4.266   3.369   15.572  1.00 28.28 ?  261 PHE A C   1 
ATOM   2062 O O   . PHE A 1 261 ? 4.539   2.276   16.084  1.00 29.48 ?  261 PHE A O   1 
ATOM   2063 C CB  . PHE A 1 261 ? 3.374   5.346   16.870  1.00 29.30 ?  261 PHE A CB  1 
ATOM   2064 C CG  . PHE A 1 261 ? 2.664   4.528   17.915  1.00 39.21 ?  261 PHE A CG  1 
ATOM   2065 C CD1 . PHE A 1 261 ? 1.908   3.420   17.570  1.00 44.47 ?  261 PHE A CD1 1 
ATOM   2066 C CD2 . PHE A 1 261 ? 2.722   4.898   19.243  1.00 44.83 ?  261 PHE A CD2 1 
ATOM   2067 C CE1 . PHE A 1 261 ? 1.253   2.682   18.539  1.00 46.47 ?  261 PHE A CE1 1 
ATOM   2068 C CE2 . PHE A 1 261 ? 2.064   4.170   20.212  1.00 46.92 ?  261 PHE A CE2 1 
ATOM   2069 C CZ  . PHE A 1 261 ? 1.326   3.066   19.858  1.00 42.84 ?  261 PHE A CZ  1 
ATOM   2070 N N   . LEU A 1 262 ? 3.653   3.461   14.391  1.00 24.04 ?  262 LEU A N   1 
ATOM   2071 C CA  . LEU A 1 262 ? 3.217   2.260   13.681  1.00 23.55 ?  262 LEU A CA  1 
ATOM   2072 C C   . LEU A 1 262 ? 4.379   1.463   13.111  1.00 26.54 ?  262 LEU A C   1 
ATOM   2073 O O   . LEU A 1 262 ? 4.264   0.241   12.941  1.00 27.99 ?  262 LEU A O   1 
ATOM   2074 C CB  . LEU A 1 262 ? 2.251   2.641   12.556  1.00 29.62 ?  262 LEU A CB  1 
ATOM   2075 C CG  . LEU A 1 262 ? 0.845   3.014   13.015  1.00 29.88 ?  262 LEU A CG  1 
ATOM   2076 C CD1 . LEU A 1 262 ? 0.184   3.918   11.994  1.00 30.89 ?  262 LEU A CD1 1 
ATOM   2077 C CD2 . LEU A 1 262 ? 0.023   1.749   13.258  1.00 29.89 ?  262 LEU A CD2 1 
ATOM   2078 N N   . ALA A 1 263 ? 5.496   2.096   12.794  1.00 19.75 ?  263 ALA A N   1 
ATOM   2079 C CA  . ALA A 1 263 ? 6.671   1.348   12.308  1.00 20.67 ?  263 ALA A CA  1 
ATOM   2080 C C   . ALA A 1 263 ? 7.344   0.614   13.467  1.00 21.95 ?  263 ALA A C   1 
ATOM   2081 O O   . ALA A 1 263 ? 8.087   -0.316  13.224  1.00 24.05 ?  263 ALA A O   1 
ATOM   2082 C CB  . ALA A 1 263 ? 7.640   2.278   11.654  1.00 23.69 ?  263 ALA A CB  1 
ATOM   2083 N N   . GLY A 1 264 ? 7.082   1.061   14.679  1.00 24.51 ?  264 GLY A N   1 
ATOM   2084 C CA  . GLY A 1 264 ? 7.734   0.480   15.861  1.00 22.50 ?  264 GLY A CA  1 
ATOM   2085 C C   . GLY A 1 264 ? 9.040   1.184   16.173  1.00 21.59 ?  264 GLY A C   1 
ATOM   2086 O O   . GLY A 1 264 ? 9.917   0.567   16.772  1.00 23.04 ?  264 GLY A O   1 
ATOM   2087 N N   . ILE A 1 265 ? 9.146   2.438   15.760  1.00 22.27 ?  265 ILE A N   1 
ATOM   2088 C CA  . ILE A 1 265 ? 10.391  3.219   15.953  1.00 21.47 ?  265 ILE A CA  1 
ATOM   2089 C C   . ILE A 1 265 ? 10.097  4.468   16.785  1.00 18.49 ?  265 ILE A C   1 
ATOM   2090 O O   . ILE A 1 265 ? 10.943  5.320   16.843  1.00 23.30 ?  265 ILE A O   1 
ATOM   2091 C CB  . ILE A 1 265 ? 11.012  3.569   14.588  1.00 21.08 ?  265 ILE A CB  1 
ATOM   2092 C CG1 . ILE A 1 265 ? 10.080  4.433   13.743  1.00 20.41 ?  265 ILE A CG1 1 
ATOM   2093 C CG2 . ILE A 1 265 ? 11.434  2.321   13.835  1.00 22.98 ?  265 ILE A CG2 1 
ATOM   2094 C CD1 . ILE A 1 265 ? 10.747  5.056   12.558  1.00 25.52 ?  265 ILE A CD1 1 
ATOM   2095 N N   . GLY A 1 266 ? 8.946   4.508   17.434  1.00 19.20 ?  266 GLY A N   1 
ATOM   2096 C CA  . GLY A 1 266 ? 8.573   5.705   18.162  1.00 20.67 ?  266 GLY A CA  1 
ATOM   2097 C C   . GLY A 1 266 ? 8.792   5.632   19.657  1.00 23.22 ?  266 GLY A C   1 
ATOM   2098 O O   . GLY A 1 266 ? 8.617   6.635   20.349  1.00 22.38 ?  266 GLY A O   1 
ATOM   2099 N N   . GLU A 1 267 ? 9.176   4.458   20.163  1.00 20.04 ?  267 GLU A N   1 
ATOM   2100 C CA  . GLU A 1 267 ? 9.326   4.220   21.594  1.00 23.90 ?  267 GLU A CA  1 
ATOM   2101 C C   . GLU A 1 267 ? 10.788  4.006   21.922  1.00 21.62 ?  267 GLU A C   1 
ATOM   2102 O O   . GLU A 1 267 ? 11.427  3.150   21.295  1.00 21.75 ?  267 GLU A O   1 
ATOM   2103 C CB  . GLU A 1 267 ? 8.519   2.986   22.028  1.00 24.89 ?  267 GLU A CB  1 
ATOM   2104 C CG  . GLU A 1 267 ? 8.791   2.529   23.484  1.00 24.84 ?  267 GLU A CG  1 
ATOM   2105 C CD  . GLU A 1 267 ? 8.058   1.252   23.831  1.00 31.77 ?  267 GLU A CD  1 
ATOM   2106 O OE1 . GLU A 1 267 ? 8.704   0.268   24.287  1.00 25.84 ?  267 GLU A OE1 1 
ATOM   2107 O OE2 . GLU A 1 267 ? 6.824   1.237   23.621  1.00 30.22 -1 267 GLU A OE2 1 
ATOM   2108 N N   . PRO A 1 268 ? 11.361  4.738   22.876  1.00 21.02 ?  268 PRO A N   1 
ATOM   2109 C CA  . PRO A 1 268 ? 12.791  4.557   23.153  1.00 24.51 ?  268 PRO A CA  1 
ATOM   2110 C C   . PRO A 1 268 ? 13.058  3.239   23.854  1.00 23.09 ?  268 PRO A C   1 
ATOM   2111 O O   . PRO A 1 268 ? 12.241  2.757   24.644  1.00 21.45 ?  268 PRO A O   1 
ATOM   2112 C CB  . PRO A 1 268 ? 13.149  5.758   24.037  1.00 24.38 ?  268 PRO A CB  1 
ATOM   2113 C CG  . PRO A 1 268 ? 11.849  6.255   24.588  1.00 25.96 ?  268 PRO A CG  1 
ATOM   2114 C CD  . PRO A 1 268 ? 10.780  5.887   23.588  1.00 20.52 ?  268 PRO A CD  1 
ATOM   2115 N N   . ASN A 1 269 ? 14.202  2.635   23.525  1.00 21.56 ?  269 ASN A N   1 
ATOM   2116 C CA  . ASN A 1 269 ? 14.661  1.453   24.237  1.00 20.16 ?  269 ASN A CA  1 
ATOM   2117 C C   . ASN A 1 269 ? 15.242  1.894   25.583  1.00 22.62 ?  269 ASN A C   1 
ATOM   2118 O O   . ASN A 1 269 ? 15.167  3.064   25.970  1.00 22.05 ?  269 ASN A O   1 
ATOM   2119 C CB  . ASN A 1 269 ? 15.636  0.635   23.373  1.00 20.17 ?  269 ASN A CB  1 
ATOM   2120 C CG  . ASN A 1 269 ? 16.957  1.350   23.102  1.00 24.62 ?  269 ASN A CG  1 
ATOM   2121 O OD1 . ASN A 1 269 ? 17.492  2.047   23.961  1.00 22.96 ?  269 ASN A OD1 1 
ATOM   2122 N ND2 . ASN A 1 269 ? 17.501  1.157   21.897  1.00 20.24 ?  269 ASN A ND2 1 
ATOM   2123 N N   . LEU A 1 270 ? 15.839  0.950   26.303  1.00 21.19 ?  270 LEU A N   1 
ATOM   2124 C CA  . LEU A 1 270 ? 16.300  1.187   27.700  1.00 24.08 ?  270 LEU A CA  1 
ATOM   2125 C C   . LEU A 1 270 ? 17.435  2.204   27.877  1.00 21.80 ?  270 LEU A C   1 
ATOM   2126 O O   . LEU A 1 270 ? 17.619  2.629   28.996  1.00 23.21 ?  270 LEU A O   1 
ATOM   2127 C CB  . LEU A 1 270 ? 16.613  -0.157  28.373  1.00 21.14 ?  270 LEU A CB  1 
ATOM   2128 C CG  . LEU A 1 270 ? 17.913  -0.881  28.016  1.00 24.00 ?  270 LEU A CG  1 
ATOM   2129 C CD1 . LEU A 1 270 ? 18.019  -2.163  28.818  1.00 22.15 ?  270 LEU A CD1 1 
ATOM   2130 C CD2 . LEU A 1 270 ? 18.031  -1.207  26.534  1.00 24.17 ?  270 LEU A CD2 1 
ATOM   2131 N N   . LEU A 1 271 ? 18.176  2.531   26.833  1.00 21.41 ?  271 LEU A N   1 
ATOM   2132 C CA  . LEU A 1 271 ? 19.338  3.442   27.024  1.00 21.38 ?  271 LEU A CA  1 
ATOM   2133 C C   . LEU A 1 271 ? 19.194  4.697   26.167  1.00 22.21 ?  271 LEU A C   1 
ATOM   2134 O O   . LEU A 1 271 ? 19.844  5.666   26.457  1.00 20.68 ?  271 LEU A O   1 
ATOM   2135 C CB  . LEU A 1 271 ? 20.618  2.693   26.660  1.00 20.74 ?  271 LEU A CB  1 
ATOM   2136 C CG  . LEU A 1 271 ? 21.081  1.633   27.652  1.00 23.27 ?  271 LEU A CG  1 
ATOM   2137 C CD1 . LEU A 1 271 ? 22.412  1.047   27.224  1.00 23.85 ?  271 LEU A CD1 1 
ATOM   2138 C CD2 . LEU A 1 271 ? 21.187  2.213   29.046  1.00 22.70 ?  271 LEU A CD2 1 
ATOM   2139 N N   . ALA A 1 272 ? 18.309  4.659   25.173  1.00 21.35 ?  272 ALA A N   1 
ATOM   2140 C CA  . ALA A 1 272 ? 18.198  5.772   24.211  1.00 17.81 ?  272 ALA A CA  1 
ATOM   2141 C C   . ALA A 1 272 ? 18.056  7.137   24.887  1.00 22.86 ?  272 ALA A C   1 
ATOM   2142 O O   . ALA A 1 272 ? 18.773  8.045   24.509  1.00 20.97 ?  272 ALA A O   1 
ATOM   2143 C CB  . ALA A 1 272 ? 17.073  5.531   23.252  1.00 19.60 ?  272 ALA A CB  1 
ATOM   2144 N N   . ILE A 1 273 ? 17.148  7.252   25.834  1.00 21.47 ?  273 ILE A N   1 
ATOM   2145 C CA  . ILE A 1 273 ? 16.882  8.577   26.402  1.00 21.52 ?  273 ILE A CA  1 
ATOM   2146 C C   . ILE A 1 273 ? 18.061  9.062   27.250  1.00 20.52 ?  273 ILE A C   1 
ATOM   2147 O O   . ILE A 1 273 ? 18.626  10.125  26.940  1.00 24.12 ?  273 ILE A O   1 
ATOM   2148 C CB  . ILE A 1 273 ? 15.565  8.603   27.202  1.00 20.15 ?  273 ILE A CB  1 
ATOM   2149 C CG1 . ILE A 1 273 ? 14.368  8.325   26.281  1.00 21.94 ?  273 ILE A CG1 1 
ATOM   2150 C CG2 . ILE A 1 273 ? 15.380  9.946   27.880  1.00 20.57 ?  273 ILE A CG2 1 
ATOM   2151 C CD1 . ILE A 1 273 ? 14.182  9.336   25.145  1.00 21.22 ?  273 ILE A CD1 1 
ATOM   2152 N N   . PRO A 1 274 ? 18.478  8.366   28.319  1.00 23.32 ?  274 PRO A N   1 
ATOM   2153 C CA  . PRO A 1 274 ? 19.564  8.945   29.140  1.00 23.01 ?  274 PRO A CA  1 
ATOM   2154 C C   . PRO A 1 274 ? 20.861  9.103   28.371  1.00 22.33 ?  274 PRO A C   1 
ATOM   2155 O O   . PRO A 1 274 ? 21.566  10.104  28.556  1.00 25.79 ?  274 PRO A O   1 
ATOM   2156 C CB  . PRO A 1 274 ? 19.699  7.964   30.317  1.00 21.48 ?  274 PRO A CB  1 
ATOM   2157 C CG  . PRO A 1 274 ? 19.018  6.703   29.867  1.00 23.78 ?  274 PRO A CG  1 
ATOM   2158 C CD  . PRO A 1 274 ? 17.986  7.088   28.873  1.00 22.11 ?  274 PRO A CD  1 
ATOM   2159 N N   . ALA A 1 275 ? 21.184  8.162   27.482  1.00 24.05 ?  275 ALA A N   1 
ATOM   2160 C CA  . ALA A 1 275 ? 22.447  8.254   26.756  1.00 23.64 ?  275 ALA A CA  1 
ATOM   2161 C C   . ALA A 1 275 ? 22.439  9.404   25.764  1.00 23.96 ?  275 ALA A C   1 
ATOM   2162 O O   . ALA A 1 275 ? 23.420  10.156  25.679  1.00 21.69 ?  275 ALA A O   1 
ATOM   2163 C CB  . ALA A 1 275 ? 22.755  6.945   26.030  1.00 22.70 ?  275 ALA A CB  1 
ATOM   2164 N N   . ALA A 1 276 ? 21.343  9.565   25.000  1.00 18.68 ?  276 ALA A N   1 
ATOM   2165 C CA  . ALA A 1 276 ? 21.271  10.700  24.081  1.00 24.44 ?  276 ALA A CA  1 
ATOM   2166 C C   . ALA A 1 276 ? 21.276  12.026  24.839  1.00 20.64 ?  276 ALA A C   1 
ATOM   2167 O O   . ALA A 1 276 ? 21.926  12.990  24.415  1.00 24.25 ?  276 ALA A O   1 
ATOM   2168 C CB  . ALA A 1 276 ? 20.033  10.590  23.187  1.00 22.30 ?  276 ALA A CB  1 
ATOM   2169 N N   . ILE A 1 277 ? 20.571  12.098  25.971  1.00 24.59 ?  277 ILE A N   1 
ATOM   2170 C CA  . ILE A 1 277 ? 20.587  13.337  26.754  1.00 23.13 ?  277 ILE A CA  1 
ATOM   2171 C C   . ILE A 1 277 ? 22.006  13.678  27.197  1.00 22.37 ?  277 ILE A C   1 
ATOM   2172 O O   . ILE A 1 277 ? 22.431  14.832  27.092  1.00 21.30 ?  277 ILE A O   1 
ATOM   2173 C CB  . ILE A 1 277 ? 19.620  13.245  27.949  1.00 24.41 ?  277 ILE A CB  1 
ATOM   2174 C CG1 . ILE A 1 277 ? 18.176  13.331  27.434  1.00 26.08 ?  277 ILE A CG1 1 
ATOM   2175 C CG2 . ILE A 1 277 ? 19.907  14.364  28.985  1.00 24.54 ?  277 ILE A CG2 1 
ATOM   2176 C CD1 . ILE A 1 277 ? 17.125  13.288  28.521  1.00 25.95 ?  277 ILE A CD1 1 
ATOM   2177 N N   . ALA A 1 278 ? 22.770  12.672  27.653  1.00 24.79 ?  278 ALA A N   1 
ATOM   2178 C CA  . ALA A 1 278 ? 24.149  12.886  28.089  1.00 24.34 ?  278 ALA A CA  1 
ATOM   2179 C C   . ALA A 1 278 ? 25.026  13.338  26.936  1.00 23.94 ?  278 ALA A C   1 
ATOM   2180 O O   . ALA A 1 278 ? 25.857  14.248  27.083  1.00 24.75 ?  278 ALA A O   1 
ATOM   2181 C CB  . ALA A 1 278 ? 24.713  11.594  28.687  1.00 23.40 ?  278 ALA A CB  1 
ATOM   2182 N N   . ALA A 1 279 ? 24.870  12.684  25.782  1.00 24.32 ?  279 ALA A N   1 
ATOM   2183 C CA  . ALA A 1 279 ? 25.591  13.081  24.582  1.00 22.17 ?  279 ALA A CA  1 
ATOM   2184 C C   . ALA A 1 279 ? 25.342  14.550  24.255  1.00 25.35 ?  279 ALA A C   1 
ATOM   2185 O O   . ALA A 1 279 ? 26.287  15.323  24.045  1.00 23.82 ?  279 ALA A O   1 
ATOM   2186 C CB  . ALA A 1 279 ? 25.179  12.169  23.425  1.00 24.44 ?  279 ALA A CB  1 
ATOM   2187 N N   . TYR A 1 280 ? 24.072  14.969  24.268  1.00 23.24 ?  280 TYR A N   1 
ATOM   2188 C CA  . TYR A 1 280 ? 23.716  16.315  23.836  1.00 20.89 ?  280 TYR A CA  1 
ATOM   2189 C C   . TYR A 1 280 ? 23.969  17.369  24.912  1.00 27.77 ?  280 TYR A C   1 
ATOM   2190 O O   . TYR A 1 280 ? 24.185  18.542  24.583  1.00 29.89 ?  280 TYR A O   1 
ATOM   2191 C CB  . TYR A 1 280 ? 22.244  16.335  23.388  1.00 24.46 ?  280 TYR A CB  1 
ATOM   2192 C CG  . TYR A 1 280 ? 22.022  15.722  22.011  1.00 25.83 ?  280 TYR A CG  1 
ATOM   2193 C CD1 . TYR A 1 280 ? 23.014  15.778  21.039  1.00 22.79 ?  280 TYR A CD1 1 
ATOM   2194 C CD2 . TYR A 1 280 ? 20.826  15.081  21.684  1.00 26.14 ?  280 TYR A CD2 1 
ATOM   2195 C CE1 . TYR A 1 280 ? 22.831  15.235  19.782  1.00 25.95 ?  280 TYR A CE1 1 
ATOM   2196 C CE2 . TYR A 1 280 ? 20.632  14.534  20.419  1.00 25.75 ?  280 TYR A CE2 1 
ATOM   2197 C CZ  . TYR A 1 280 ? 21.637  14.618  19.473  1.00 24.98 ?  280 TYR A CZ  1 
ATOM   2198 O OH  . TYR A 1 280 ? 21.457  14.087  18.223  1.00 25.75 ?  280 TYR A OH  1 
ATOM   2199 N N   . GLU A 1 281 ? 23.936  16.990  26.191  1.00 24.71 ?  281 GLU A N   1 
ATOM   2200 C CA  . GLU A 1 281 ? 24.239  17.958  27.237  1.00 27.55 ?  281 GLU A CA  1 
ATOM   2201 C C   . GLU A 1 281 ? 25.726  18.001  27.562  1.00 26.27 ?  281 GLU A C   1 
ATOM   2202 O O   . GLU A 1 281 ? 26.266  19.068  27.885  1.00 25.37 ?  281 GLU A O   1 
ATOM   2203 C CB  . GLU A 1 281 ? 23.442  17.644  28.503  1.00 27.97 ?  281 GLU A CB  1 
ATOM   2204 C CG  . GLU A 1 281 ? 21.939  17.693  28.316  1.00 33.74 ?  281 GLU A CG  1 
ATOM   2205 C CD  . GLU A 1 281 ? 21.382  19.099  28.435  1.00 39.33 ?  281 GLU A CD  1 
ATOM   2206 O OE1 . GLU A 1 281 ? 20.186  19.302  28.127  1.00 47.52 ?  281 GLU A OE1 1 
ATOM   2207 O OE2 . GLU A 1 281 ? 22.142  20.010  28.834  1.00 44.55 -1 281 GLU A OE2 1 
ATOM   2208 N N   . GLU A 1 282 ? 26.413  16.869  27.469  1.00 25.83 ?  282 GLU A N   1 
ATOM   2209 C CA  . GLU A 1 282 ? 27.762  16.763  27.997  1.00 25.67 ?  282 GLU A CA  1 
ATOM   2210 C C   . GLU A 1 282 ? 28.803  16.357  26.963  1.00 29.41 ?  282 GLU A C   1 
ATOM   2211 O O   . GLU A 1 282 ? 29.992  16.315  27.296  1.00 29.28 ?  282 GLU A O   1 
ATOM   2212 C CB  . GLU A 1 282 ? 27.778  15.779  29.171  1.00 28.72 ?  282 GLU A CB  1 
ATOM   2213 C CG  . GLU A 1 282 ? 26.832  16.197  30.283  1.00 31.87 ?  282 GLU A CG  1 
ATOM   2214 C CD  . GLU A 1 282 ? 27.121  15.520  31.599  1.00 43.33 ?  282 GLU A CD  1 
ATOM   2215 O OE1 . GLU A 1 282 ? 28.306  15.448  31.999  1.00 44.91 ?  282 GLU A OE1 1 
ATOM   2216 O OE2 . GLU A 1 282 ? 26.155  15.056  32.242  1.00 54.27 -1 282 GLU A OE2 1 
ATOM   2217 N N   . GLY A 1 283 ? 28.407  16.083  25.719  1.00 25.44 ?  283 GLY A N   1 
ATOM   2218 C CA  . GLY A 1 283 ? 29.356  15.563  24.765  1.00 26.12 ?  283 GLY A CA  1 
ATOM   2219 C C   . GLY A 1 283 ? 30.146  16.595  24.004  1.00 24.87 ?  283 GLY A C   1 
ATOM   2220 O O   . GLY A 1 283 ? 30.931  16.219  23.128  1.00 26.27 ?  283 GLY A O   1 
ATOM   2221 N N   . HIS A 1 284 ? 29.967  17.883  24.322  1.00 23.48 ?  284 HIS A N   1 
ATOM   2222 C CA  . HIS A 1 284 ? 30.626  18.953  23.576  1.00 25.64 ?  284 HIS A CA  1 
ATOM   2223 C C   . HIS A 1 284 ? 32.142  18.802  23.579  1.00 26.63 ?  284 HIS A C   1 
ATOM   2224 O O   . HIS A 1 284 ? 32.805  18.978  22.544  1.00 28.79 ?  284 HIS A O   1 
ATOM   2225 C CB  . HIS A 1 284 ? 30.249  20.304  24.178  1.00 29.04 ?  284 HIS A CB  1 
ATOM   2226 C CG  . HIS A 1 284 ? 28.785  20.602  24.140  1.00 28.32 ?  284 HIS A CG  1 
ATOM   2227 N ND1 . HIS A 1 284 ? 28.155  21.077  23.012  1.00 31.27 ?  284 HIS A ND1 1 
ATOM   2228 C CD2 . HIS A 1 284 ? 27.831  20.515  25.097  1.00 31.98 ?  284 HIS A CD2 1 
ATOM   2229 C CE1 . HIS A 1 284 ? 26.873  21.261  23.272  1.00 31.09 ?  284 HIS A CE1 1 
ATOM   2230 N NE2 . HIS A 1 284 ? 26.652  20.933  24.532  1.00 30.09 ?  284 HIS A NE2 1 
ATOM   2231 N N   . ASN A 1 285 ? 32.714  18.531  24.747  1.00 26.34 ?  285 ASN A N   1 
ATOM   2232 C CA  . ASN A 1 285 ? 34.170  18.501  24.847  1.00 26.06 ?  285 ASN A CA  1 
ATOM   2233 C C   . ASN A 1 285 ? 34.751  17.295  24.125  1.00 28.17 ?  285 ASN A C   1 
ATOM   2234 O O   . ASN A 1 285 ? 35.761  17.417  23.420  1.00 27.64 ?  285 ASN A O   1 
ATOM   2235 C CB  . ASN A 1 285 ? 34.586  18.522  26.313  1.00 30.96 ?  285 ASN A CB  1 
ATOM   2236 C CG  . ASN A 1 285 ? 34.428  19.896  26.925  1.00 33.53 ?  285 ASN A CG  1 
ATOM   2237 O OD1 . ASN A 1 285 ? 33.785  20.050  27.956  1.00 39.15 ?  285 ASN A OD1 1 
ATOM   2238 N ND2 . ASN A 1 285 ? 35.017  20.903  26.289  1.00 40.85 ?  285 ASN A ND2 1 
ATOM   2239 N N   . TRP A 1 286 ? 34.112  16.129  24.263  1.00 23.54 ?  286 TRP A N   1 
ATOM   2240 C CA  . TRP A 1 286 ? 34.591  14.945  23.552  1.00 24.29 ?  286 TRP A CA  1 
ATOM   2241 C C   . TRP A 1 286 ? 34.506  15.140  22.043  1.00 26.51 ?  286 TRP A C   1 
ATOM   2242 O O   . TRP A 1 286 ? 35.404  14.716  21.303  1.00 27.55 ?  286 TRP A O   1 
ATOM   2243 C CB  . TRP A 1 286 ? 33.794  13.708  23.981  1.00 24.41 ?  286 TRP A CB  1 
ATOM   2244 C CG  . TRP A 1 286 ? 34.258  12.429  23.335  1.00 25.54 ?  286 TRP A CG  1 
ATOM   2245 C CD1 . TRP A 1 286 ? 35.162  11.524  23.835  1.00 26.56 ?  286 TRP A CD1 1 
ATOM   2246 C CD2 . TRP A 1 286 ? 33.821  11.904  22.081  1.00 24.59 ?  286 TRP A CD2 1 
ATOM   2247 N NE1 . TRP A 1 286 ? 35.324  10.475  22.948  1.00 24.79 ?  286 TRP A NE1 1 
ATOM   2248 C CE2 . TRP A 1 286 ? 34.507  10.687  21.867  1.00 25.18 ?  286 TRP A CE2 1 
ATOM   2249 C CE3 . TRP A 1 286 ? 32.922  12.352  21.107  1.00 26.51 ?  286 TRP A CE3 1 
ATOM   2250 C CZ2 . TRP A 1 286 ? 34.316  9.913   20.716  1.00 24.24 ?  286 TRP A CZ2 1 
ATOM   2251 C CZ3 . TRP A 1 286 ? 32.734  11.585  19.972  1.00 22.15 ?  286 TRP A CZ3 1 
ATOM   2252 C CH2 . TRP A 1 286 ? 33.424  10.380  19.782  1.00 24.17 ?  286 TRP A CH2 1 
ATOM   2253 N N   . LEU A 1 287 ? 33.495  15.836  21.553  1.00 23.61 ?  287 LEU A N   1 
ATOM   2254 C CA  . LEU A 1 287 ? 33.355  16.016  20.082  1.00 26.07 ?  287 LEU A CA  1 
ATOM   2255 C C   . LEU A 1 287 ? 34.427  16.985  19.570  1.00 25.00 ?  287 LEU A C   1 
ATOM   2256 O O   . LEU A 1 287 ? 34.927  16.793  18.488  1.00 26.98 ?  287 LEU A O   1 
ATOM   2257 C CB  . LEU A 1 287 ? 31.951  16.533  19.756  1.00 26.00 ?  287 LEU A CB  1 
ATOM   2258 C CG  . LEU A 1 287 ? 31.696  16.904  18.297  1.00 24.88 ?  287 LEU A CG  1 
ATOM   2259 C CD1 . LEU A 1 287 ? 31.847  15.704  17.378  1.00 23.05 ?  287 LEU A CD1 1 
ATOM   2260 C CD2 . LEU A 1 287 ? 30.340  17.559  18.119  1.00 22.95 ?  287 LEU A CD2 1 
ATOM   2261 N N   . ARG A 1 288 ? 34.750  17.993  20.366  1.00 27.69 ?  288 ARG A N   1 
ATOM   2262 C CA  . ARG A 1 288 ? 35.778  18.987  19.977  1.00 30.78 ?  288 ARG A CA  1 
ATOM   2263 C C   . ARG A 1 288 ? 37.101  18.249  19.733  1.00 29.82 ?  288 ARG A C   1 
ATOM   2264 O O   . ARG A 1 288 ? 37.734  18.501  18.729  1.00 31.30 ?  288 ARG A O   1 
ATOM   2265 C CB  . ARG A 1 288 ? 35.857  20.022  21.097  1.00 29.08 ?  288 ARG A CB  1 
ATOM   2266 C CG  . ARG A 1 288 ? 36.689  21.251  20.770  1.00 36.77 ?  288 ARG A CG  1 
ATOM   2267 C CD  . ARG A 1 288 ? 36.864  22.183  21.954  1.00 40.42 ?  288 ARG A CD  1 
ATOM   2268 N NE  . ARG A 1 288 ? 35.611  22.523  22.608  1.00 47.16 ?  288 ARG A NE  1 
ATOM   2269 C CZ  . ARG A 1 288 ? 35.516  23.201  23.747  1.00 47.33 ?  288 ARG A CZ  1 
ATOM   2270 N NH1 . ARG A 1 288 ? 36.607  23.617  24.366  1.00 41.20 1  288 ARG A NH1 1 
ATOM   2271 N NH2 . ARG A 1 288 ? 34.330  23.464  24.263  1.00 46.90 ?  288 ARG A NH2 1 
ATOM   2272 N N   . GLU A 1 289 ? 37.435  17.335  20.634  1.00 31.10 ?  289 GLU A N   1 
ATOM   2273 C CA  . GLU A 1 289 ? 38.672  16.539  20.501  1.00 35.36 ?  289 GLU A CA  1 
ATOM   2274 C C   . GLU A 1 289 ? 38.538  15.527  19.369  1.00 33.18 ?  289 GLU A C   1 
ATOM   2275 O O   . GLU A 1 289 ? 39.546  15.219  18.761  1.00 34.71 ?  289 GLU A O   1 
ATOM   2276 C CB  . GLU A 1 289 ? 38.987  15.785  21.786  1.00 33.81 ?  289 GLU A CB  1 
ATOM   2277 C CG  . GLU A 1 289 ? 39.365  16.673  22.950  1.00 41.94 ?  289 GLU A CG  1 
ATOM   2278 C CD  . GLU A 1 289 ? 40.665  17.445  22.818  1.00 47.50 ?  289 GLU A CD  1 
ATOM   2279 O OE1 . GLU A 1 289 ? 41.450  17.146  21.909  1.00 52.47 ?  289 GLU A OE1 1 
ATOM   2280 O OE2 . GLU A 1 289 ? 40.885  18.355  23.635  1.00 51.18 -1 289 GLU A OE2 1 
ATOM   2281 N N   . LEU A 1 290 ? 37.332  14.995  19.169  1.00 30.56 ?  290 LEU A N   1 
ATOM   2282 C CA  . LEU A 1 290 ? 37.150  14.078  18.048  1.00 31.81 ?  290 LEU A CA  1 
ATOM   2283 C C   . LEU A 1 290 ? 37.483  14.741  16.714  1.00 29.19 ?  290 LEU A C   1 
ATOM   2284 O O   . LEU A 1 290 ? 38.246  14.192  15.914  1.00 33.06 ?  290 LEU A O   1 
ATOM   2285 C CB  . LEU A 1 290 ? 35.712  13.555  18.029  1.00 26.69 ?  290 LEU A CB  1 
ATOM   2286 C CG  . LEU A 1 290 ? 35.422  12.740  16.767  1.00 27.13 ?  290 LEU A CG  1 
ATOM   2287 C CD1 . LEU A 1 290 ? 36.283  11.481  16.754  1.00 27.06 ?  290 LEU A CD1 1 
ATOM   2288 C CD2 . LEU A 1 290 ? 33.954  12.415  16.685  1.00 26.85 ?  290 LEU A CD2 1 
ATOM   2289 N N   . LYS A 1 291 ? 36.882  15.904  16.435  1.00 31.12 ?  291 LYS A N   1 
ATOM   2290 C CA  . LYS A 1 291 ? 37.122  16.583  15.162  1.00 30.61 ?  291 LYS A CA  1 
ATOM   2291 C C   . LYS A 1 291 ? 38.601  16.861  14.981  1.00 35.03 ?  291 LYS A C   1 
ATOM   2292 O O   . LYS A 1 291 ? 39.137  16.796  13.867  1.00 34.50 ?  291 LYS A O   1 
ATOM   2293 C CB  . LYS A 1 291 ? 36.351  17.892  15.121  1.00 33.67 ?  291 LYS A CB  1 
ATOM   2294 C CG  . LYS A 1 291 ? 34.879  17.744  15.365  1.00 33.35 ?  291 LYS A CG  1 
ATOM   2295 C CD  . LYS A 1 291 ? 34.196  19.068  15.189  1.00 36.48 ?  291 LYS A CD  1 
ATOM   2296 C CE  . LYS A 1 291 ? 32.717  18.871  15.265  1.00 30.91 ?  291 LYS A CE  1 
ATOM   2297 N NZ  . LYS A 1 291 ? 32.001  19.984  14.627  1.00 37.71 1  291 LYS A NZ  1 
ATOM   2298 N N   . GLN A 1 292 ? 39.264  17.174  16.089  1.00 33.58 ?  292 GLN A N   1 
ATOM   2299 C CA  . GLN A 1 292 ? 40.704  17.342  16.114  1.00 38.10 ?  292 GLN A CA  1 
ATOM   2300 C C   . GLN A 1 292 ? 41.424  16.103  15.611  1.00 39.84 ?  292 GLN A C   1 
ATOM   2301 O O   . GLN A 1 292 ? 42.293  16.196  14.741  1.00 35.49 ?  292 GLN A O   1 
ATOM   2302 C CB  . GLN A 1 292 ? 41.148  17.663  17.534  1.00 41.81 ?  292 GLN A CB  1 
ATOM   2303 C CG  . GLN A 1 292 ? 42.502  18.265  17.535  1.00 45.98 ?  292 GLN A CG  1 
ATOM   2304 C CD  . GLN A 1 292 ? 42.828  18.999  16.215  1.00 54.04 ?  292 GLN A CD  1 
ATOM   2305 O OE1 . GLN A 1 292 ? 42.263  20.011  15.850  1.00 56.44 ?  292 GLN A OE1 1 
ATOM   2306 N NE2 . GLN A 1 292 ? 43.815  18.434  15.490  1.00 49.57 ?  292 GLN A NE2 1 
ATOM   2307 N N   . VAL A 1 293 ? 41.101  14.939  16.174  1.00 34.29 ?  293 VAL A N   1 
ATOM   2308 C CA  . VAL A 1 293 ? 41.736  13.673  15.699  1.00 34.05 ?  293 VAL A CA  1 
ATOM   2309 C C   . VAL A 1 293 ? 41.344  13.417  14.242  1.00 27.71 ?  293 VAL A C   1 
ATOM   2310 O O   . VAL A 1 293 ? 42.181  12.952  13.498  1.00 29.30 ?  293 VAL A O   1 
ATOM   2311 C CB  . VAL A 1 293 ? 41.487  12.450  16.609  1.00 35.41 ?  293 VAL A CB  1 
ATOM   2312 C CG1 . VAL A 1 293 ? 40.152  11.785  16.378  1.00 32.73 ?  293 VAL A CG1 1 
ATOM   2313 C CG2 . VAL A 1 293 ? 42.590  11.415  16.483  1.00 30.00 ?  293 VAL A CG2 1 
ATOM   2314 N N   . LEU A 1 294 ? 40.113  13.764  13.874  1.00 28.07 ?  294 LEU A N   1 
ATOM   2315 C CA  . LEU A 1 294 ? 39.679  13.584  12.493  1.00 28.56 ?  294 LEU A CA  1 
ATOM   2316 C C   . LEU A 1 294 ? 40.472  14.473  11.546  1.00 34.02 ?  294 LEU A C   1 
ATOM   2317 O O   . LEU A 1 294 ? 40.969  14.012  10.511  1.00 30.86 ?  294 LEU A O   1 
ATOM   2318 C CB  . LEU A 1 294 ? 38.188  13.895  12.364  1.00 29.15 ?  294 LEU A CB  1 
ATOM   2319 C CG  . LEU A 1 294 ? 37.271  12.952  13.134  1.00 24.81 ?  294 LEU A CG  1 
ATOM   2320 C CD1 . LEU A 1 294 ? 35.804  13.256  12.820  1.00 28.43 ?  294 LEU A CD1 1 
ATOM   2321 C CD2 . LEU A 1 294 ? 37.635  11.521  12.787  1.00 24.67 ?  294 LEU A CD2 1 
ATOM   2322 N N   . ARG A 1 295 ? 40.706  15.703  11.962  1.00 32.84 ?  295 ARG A N   1 
ATOM   2323 C CA  . ARG A 1 295 ? 41.441  16.649  11.104  1.00 37.03 ?  295 ARG A CA  1 
ATOM   2324 C C   . ARG A 1 295 ? 42.891  16.176  10.926  1.00 36.29 ?  295 ARG A C   1 
ATOM   2325 O O   . ARG A 1 295 ? 43.473  16.428  9.878   1.00 36.90 ?  295 ARG A O   1 
ATOM   2326 C CB  . ARG A 1 295 ? 41.278  18.058  11.664  1.00 38.33 ?  295 ARG A CB  1 
ATOM   2327 C CG  . ARG A 1 295 ? 39.950  18.713  11.321  1.00 38.42 ?  295 ARG A CG  1 
ATOM   2328 C CD  . ARG A 1 295 ? 39.920  20.171  11.727  1.00 40.50 ?  295 ARG A CD  1 
ATOM   2329 N NE  . ARG A 1 295 ? 39.889  20.296  13.170  1.00 43.34 ?  295 ARG A NE  1 
ATOM   2330 C CZ  . ARG A 1 295 ? 38.806  20.571  13.876  1.00 38.22 ?  295 ARG A CZ  1 
ATOM   2331 N NH1 . ARG A 1 295 ? 37.655  20.781  13.269  1.00 36.76 1  295 ARG A NH1 1 
ATOM   2332 N NH2 . ARG A 1 295 ? 38.880  20.653  15.187  1.00 37.33 ?  295 ARG A NH2 1 
ATOM   2333 N N   . ASP A 1 296 ? 43.459  15.545  11.936  1.00 33.92 ?  296 ASP A N   1 
ATOM   2334 C CA  . ASP A 1 296 ? 44.853  15.035  11.836  1.00 37.58 ?  296 ASP A CA  1 
ATOM   2335 C C   . ASP A 1 296 ? 44.907  13.817  10.906  1.00 37.44 ?  296 ASP A C   1 
ATOM   2336 O O   . ASP A 1 296 ? 45.853  13.708  10.141  1.00 35.11 ?  296 ASP A O   1 
ATOM   2337 C CB  . ASP A 1 296 ? 45.417  14.689  13.204  1.00 37.26 ?  296 ASP A CB  1 
ATOM   2338 C CG  . ASP A 1 296 ? 45.492  15.868  14.157  1.00 48.05 ?  296 ASP A CG  1 
ATOM   2339 O OD1 . ASP A 1 296 ? 45.354  17.002  13.683  1.00 50.13 ?  296 ASP A OD1 1 
ATOM   2340 O OD2 . ASP A 1 296 ? 45.680  15.637  15.368  1.00 46.96 -1 296 ASP A OD2 1 
ATOM   2341 N N   . ASN A 1 297 ? 43.912  12.929  11.011  1.00 35.35 ?  297 ASN A N   1 
ATOM   2342 C CA  . ASN A 1 297 ? 43.880  11.710  10.179  1.00 35.04 ?  297 ASN A CA  1 
ATOM   2343 C C   . ASN A 1 297 ? 43.674  12.107  8.719   1.00 34.72 ?  297 ASN A C   1 
ATOM   2344 O O   . ASN A 1 297 ? 44.293  11.492  7.879   1.00 35.47 ?  297 ASN A O   1 
ATOM   2345 C CB  . ASN A 1 297 ? 42.795  10.751  10.663  1.00 31.81 ?  297 ASN A CB  1 
ATOM   2346 C CG  . ASN A 1 297 ? 43.091  10.172  12.028  1.00 34.56 ?  297 ASN A CG  1 
ATOM   2347 O OD1 . ASN A 1 297 ? 44.183  10.342  12.552  1.00 34.51 ?  297 ASN A OD1 1 
ATOM   2348 N ND2 . ASN A 1 297 ? 42.125  9.481   12.608  1.00 28.98 ?  297 ASN A ND2 1 
ATOM   2349 N N   . PHE A 1 298 ? 42.780  13.048  8.460   1.00 34.51 ?  298 PHE A N   1 
ATOM   2350 C CA  . PHE A 1 298 ? 42.591  13.572  7.108   1.00 34.94 ?  298 PHE A CA  1 
ATOM   2351 C C   . PHE A 1 298 ? 43.866  14.226  6.586   1.00 39.55 ?  298 PHE A C   1 
ATOM   2352 O O   . PHE A 1 298 ? 44.230  14.050  5.417   1.00 38.53 ?  298 PHE A O   1 
ATOM   2353 C CB  . PHE A 1 298 ? 41.445  14.583  7.081   1.00 33.77 ?  298 PHE A CB  1 
ATOM   2354 C CG  . PHE A 1 298 ? 40.110  13.986  6.737   1.00 36.24 ?  298 PHE A CG  1 
ATOM   2355 C CD1 . PHE A 1 298 ? 39.767  13.726  5.416   1.00 36.50 ?  298 PHE A CD1 1 
ATOM   2356 C CD2 . PHE A 1 298 ? 39.184  13.714  7.725   1.00 34.26 ?  298 PHE A CD2 1 
ATOM   2357 C CE1 . PHE A 1 298 ? 38.533  13.194  5.091   1.00 38.89 ?  298 PHE A CE1 1 
ATOM   2358 C CE2 . PHE A 1 298 ? 37.942  13.167  7.399   1.00 32.92 ?  298 PHE A CE2 1 
ATOM   2359 C CZ  . PHE A 1 298 ? 37.624  12.912  6.088   1.00 34.39 ?  298 PHE A CZ  1 
ATOM   2360 N N   . ALA A 1 299 ? 44.540  15.009  7.434   1.00 39.48 ?  299 ALA A N   1 
ATOM   2361 C CA  . ALA A 1 299 ? 45.787  15.649  7.028   1.00 40.90 ?  299 ALA A CA  1 
ATOM   2362 C C   . ALA A 1 299 ? 46.850  14.609  6.698   1.00 40.29 ?  299 ALA A C   1 
ATOM   2363 O O   . ALA A 1 299 ? 47.509  14.692  5.653   1.00 43.10 ?  299 ALA A O   1 
ATOM   2364 C CB  . ALA A 1 299 ? 46.276  16.593  8.125   1.00 36.92 ?  299 ALA A CB  1 
ATOM   2365 N N   . TYR A 1 300 ? 47.034  13.620  7.584   1.00 37.62 ?  300 TYR A N   1 
ATOM   2366 C CA  . TYR A 1 300 ? 47.932  12.515  7.265   1.00 36.93 ?  300 TYR A CA  1 
ATOM   2367 C C   . TYR A 1 300 ? 47.482  11.793  6.003   1.00 41.23 ?  300 TYR A C   1 
ATOM   2368 O O   . TYR A 1 300 ? 48.307  11.476  5.138   1.00 39.07 ?  300 TYR A O   1 
ATOM   2369 C CB  . TYR A 1 300 ? 48.023  11.528  8.433   1.00 37.98 ?  300 TYR A CB  1 
ATOM   2370 C CG  . TYR A 1 300 ? 48.965  10.361  8.172   1.00 41.81 ?  300 TYR A CG  1 
ATOM   2371 C CD1 . TYR A 1 300 ? 48.538  9.239   7.459   1.00 39.41 ?  300 TYR A CD1 1 
ATOM   2372 C CD2 . TYR A 1 300 ? 50.281  10.378  8.647   1.00 39.34 ?  300 TYR A CD2 1 
ATOM   2373 C CE1 . TYR A 1 300 ? 49.392  8.174   7.212   1.00 37.12 ?  300 TYR A CE1 1 
ATOM   2374 C CE2 . TYR A 1 300 ? 51.143  9.319   8.399   1.00 42.03 ?  300 TYR A CE2 1 
ATOM   2375 C CZ  . TYR A 1 300 ? 50.692  8.221   7.678   1.00 40.76 ?  300 TYR A CZ  1 
ATOM   2376 O OH  . TYR A 1 300 ? 51.531  7.160   7.423   1.00 44.17 ?  300 TYR A OH  1 
ATOM   2377 N N   . ALA A 1 301 ? 46.177  11.518  5.886   1.00 38.15 ?  301 ALA A N   1 
ATOM   2378 C CA  . ALA A 1 301 ? 45.666  10.782  4.733   1.00 41.13 ?  301 ALA A CA  1 
ATOM   2379 C C   . ALA A 1 301 ? 45.962  11.521  3.438   1.00 42.64 ?  301 ALA A C   1 
ATOM   2380 O O   . ALA A 1 301 ? 46.558  10.959  2.513   1.00 40.84 ?  301 ALA A O   1 
ATOM   2381 C CB  . ALA A 1 301 ? 44.160  10.551  4.871   1.00 40.82 ?  301 ALA A CB  1 
ATOM   2382 N N   . ARG A 1 302 ? 45.688  12.810  3.440   1.00 39.45 ?  302 ARG A N   1 
ATOM   2383 C CA  . ARG A 1 302 ? 45.838  13.588  2.201   1.00 43.05 ?  302 ARG A CA  1 
ATOM   2384 C C   . ARG A 1 302 ? 47.313  13.688  1.822   1.00 43.61 ?  302 ARG A C   1 
ATOM   2385 O O   . ARG A 1 302 ? 47.603  13.561  0.640   1.00 42.23 ?  302 ARG A O   1 
ATOM   2386 C CB  . ARG A 1 302 ? 45.167  14.947  2.388   1.00 41.59 ?  302 ARG A CB  1 
ATOM   2387 C CG  . ARG A 1 302 ? 43.656  14.913  2.266   1.00 44.16 ?  302 ARG A CG  1 
ATOM   2388 C CD  . ARG A 1 302 ? 43.111  16.279  2.583   1.00 43.96 ?  302 ARG A CD  1 
ATOM   2389 N NE  . ARG A 1 302 ? 41.756  16.383  2.090   1.00 48.07 ?  302 ARG A NE  1 
ATOM   2390 C CZ  . ARG A 1 302 ? 40.705  16.548  2.869   1.00 44.33 ?  302 ARG A CZ  1 
ATOM   2391 N NH1 . ARG A 1 302 ? 40.850  16.635  4.177   1.00 46.86 1  302 ARG A NH1 1 
ATOM   2392 N NH2 . ARG A 1 302 ? 39.509  16.635  2.340   1.00 52.20 ?  302 ARG A NH2 1 
ATOM   2393 N N   . GLU A 1 303 ? 48.186  13.862  2.806   1.00 43.62 ?  303 GLU A N   1 
ATOM   2394 C CA  . GLU A 1 303 ? 49.623  14.083  2.528   1.00 44.77 ?  303 GLU A CA  1 
ATOM   2395 C C   . GLU A 1 303 ? 50.234  12.780  2.012   1.00 45.83 ?  303 GLU A C   1 
ATOM   2396 O O   . GLU A 1 303 ? 50.916  12.823  0.986   1.00 44.14 ?  303 GLU A O   1 
ATOM   2397 C CB  . GLU A 1 303 ? 50.299  14.590  3.797   1.00 46.43 ?  303 GLU A CB  1 
ATOM   2398 C CG  . GLU A 1 303 ? 51.587  15.339  3.542   1.00 51.87 ?  303 GLU A CG  1 
ATOM   2399 C CD  . GLU A 1 303 ? 52.533  15.344  4.724   1.00 52.84 ?  303 GLU A CD  1 
ATOM   2400 O OE1 . GLU A 1 303 ? 52.133  15.810  5.799   1.00 59.96 ?  303 GLU A OE1 1 
ATOM   2401 O OE2 . GLU A 1 303 ? 53.673  14.883  4.562   1.00 57.43 -1 303 GLU A OE2 1 
ATOM   2402 N N   . PHE A 1 304 ? 49.997  11.675  2.721   1.00 43.34 ?  304 PHE A N   1 
ATOM   2403 C CA  . PHE A 1 304 ? 50.532  10.361  2.289   1.00 42.98 ?  304 PHE A CA  1 
ATOM   2404 C C   . PHE A 1 304 ? 50.065  10.089  0.863   1.00 41.45 ?  304 PHE A C   1 
ATOM   2405 O O   . PHE A 1 304 ? 50.881  9.722   0.043   1.00 42.86 ?  304 PHE A O   1 
ATOM   2406 C CB  . PHE A 1 304 ? 50.101  9.257   3.255   1.00 41.10 ?  304 PHE A CB  1 
ATOM   2407 C CG  . PHE A 1 304 ? 50.563  7.864   2.922   1.00 40.44 ?  304 PHE A CG  1 
ATOM   2408 C CD1 . PHE A 1 304 ? 49.912  7.103   1.968   1.00 41.67 ?  304 PHE A CD1 1 
ATOM   2409 C CD2 . PHE A 1 304 ? 51.636  7.303   3.589   1.00 41.27 ?  304 PHE A CD2 1 
ATOM   2410 C CE1 . PHE A 1 304 ? 50.355  5.832   1.657   1.00 43.01 ?  304 PHE A CE1 1 
ATOM   2411 C CE2 . PHE A 1 304 ? 52.059  6.018   3.296   1.00 46.32 ?  304 PHE A CE2 1 
ATOM   2412 C CZ  . PHE A 1 304 ? 51.416  5.286   2.331   1.00 39.11 ?  304 PHE A CZ  1 
ATOM   2413 N N   . LEU A 1 305 ? 48.778  10.282  0.597   1.00 36.52 ?  305 LEU A N   1 
ATOM   2414 C CA  . LEU A 1 305 ? 48.296  9.933   -0.734  1.00 42.67 ?  305 LEU A CA  1 
ATOM   2415 C C   . LEU A 1 305 ? 48.786  10.919  -1.786  1.00 43.31 ?  305 LEU A C   1 
ATOM   2416 O O   . LEU A 1 305 ? 48.974  10.538  -2.943  1.00 40.80 ?  305 LEU A O   1 
ATOM   2417 C CB  . LEU A 1 305 ? 46.766  9.847   -0.743  1.00 39.44 ?  305 LEU A CB  1 
ATOM   2418 C CG  . LEU A 1 305 ? 46.187  8.667   0.048   1.00 43.45 ?  305 LEU A CG  1 
ATOM   2419 C CD1 . LEU A 1 305 ? 44.668  8.631   -0.042  1.00 37.82 ?  305 LEU A CD1 1 
ATOM   2420 C CD2 . LEU A 1 305 ? 46.786  7.345   -0.427  1.00 43.25 ?  305 LEU A CD2 1 
ATOM   2421 N N   . ALA A 1 306 ? 49.009  12.183  -1.419  1.00 44.32 ?  306 ALA A N   1 
ATOM   2422 C CA  . ALA A 1 306 ? 49.525  13.125  -2.409  1.00 45.00 ?  306 ALA A CA  1 
ATOM   2423 C C   . ALA A 1 306 ? 50.970  12.801  -2.768  1.00 43.74 ?  306 ALA A C   1 
ATOM   2424 O O   . ALA A 1 306 ? 51.357  12.867  -3.941  1.00 48.32 ?  306 ALA A O   1 
ATOM   2425 C CB  . ALA A 1 306 ? 49.396  14.556  -1.898  1.00 43.22 ?  306 ALA A CB  1 
ATOM   2426 N N   . LYS A 1 307 ? 51.749  12.356  -1.790  1.00 41.05 ?  307 LYS A N   1 
ATOM   2427 C CA  . LYS A 1 307 ? 53.189  12.076  -1.995  1.00 46.76 ?  307 LYS A CA  1 
ATOM   2428 C C   . LYS A 1 307 ? 53.455  10.641  -2.453  1.00 48.58 ?  307 LYS A C   1 
ATOM   2429 O O   . LYS A 1 307 ? 54.455  10.433  -3.136  1.00 48.76 ?  307 LYS A O   1 
ATOM   2430 C CB  . LYS A 1 307 ? 53.925  12.238  -0.666  1.00 44.47 ?  307 LYS A CB  1 
ATOM   2431 C CG  . LYS A 1 307 ? 53.983  13.657  -0.126  1.00 45.79 ?  307 LYS A CG  1 
ATOM   2432 C CD  . LYS A 1 307 ? 54.277  13.737  1.352   1.00 50.82 ?  307 LYS A CD  1 
ATOM   2433 C CE  . LYS A 1 307 ? 54.623  12.409  1.988   1.00 50.27 ?  307 LYS A CE  1 
ATOM   2434 N NZ  . LYS A 1 307 ? 55.416  12.603  3.224   1.00 53.10 1  307 LYS A NZ  1 
ATOM   2435 N N   . GLU A 1 308 ? 52.601  9.693   -2.089  1.00 45.03 ?  308 GLU A N   1 
ATOM   2436 C CA  . GLU A 1 308 ? 52.936  8.278   -2.368  1.00 47.89 ?  308 GLU A CA  1 
ATOM   2437 C C   . GLU A 1 308 ? 51.951  7.632   -3.342  1.00 42.26 ?  308 GLU A C   1 
ATOM   2438 O O   . GLU A 1 308 ? 52.339  6.679   -3.986  1.00 46.59 ?  308 GLU A O   1 
ATOM   2439 C CB  . GLU A 1 308 ? 53.109  7.531   -1.046  1.00 46.34 ?  308 GLU A CB  1 
ATOM   2440 C CG  . GLU A 1 308 ? 54.088  8.151   -0.073  1.00 48.95 ?  308 GLU A CG  1 
ATOM   2441 C CD  . GLU A 1 308 ? 54.614  7.180   0.968   1.00 54.60 ?  308 GLU A CD  1 
ATOM   2442 O OE1 . GLU A 1 308 ? 55.119  7.638   2.005   1.00 56.43 ?  308 GLU A OE1 1 
ATOM   2443 O OE2 . GLU A 1 308 ? 54.507  5.965   0.742   1.00 59.23 -1 308 GLU A OE2 1 
ATOM   2444 N N   . VAL A 1 309 ? 50.726  8.137   -3.435  1.00 44.96 ?  309 VAL A N   1 
ATOM   2445 C CA  . VAL A 1 309 ? 49.721  7.604   -4.405  1.00 46.07 ?  309 VAL A CA  1 
ATOM   2446 C C   . VAL A 1 309 ? 49.170  8.785   -5.215  1.00 47.52 ?  309 VAL A C   1 
ATOM   2447 O O   . VAL A 1 309 ? 47.964  9.036   -5.149  1.00 48.10 ?  309 VAL A O   1 
ATOM   2448 C CB  . VAL A 1 309 ? 48.638  6.696   -3.793  1.00 46.66 ?  309 VAL A CB  1 
ATOM   2449 C CG1 . VAL A 1 309 ? 47.987  5.808   -4.835  1.00 48.62 ?  309 VAL A CG1 1 
ATOM   2450 C CG2 . VAL A 1 309 ? 49.180  5.852   -2.661  1.00 47.37 ?  309 VAL A CG2 1 
ATOM   2451 N N   . PRO A 1 310 ? 49.982  9.581   -5.951  1.00 46.81 ?  310 PRO A N   1 
ATOM   2452 C CA  . PRO A 1 310 ? 49.449  10.771  -6.637  1.00 48.86 ?  310 PRO A CA  1 
ATOM   2453 C C   . PRO A 1 310 ? 48.402  10.439  -7.691  1.00 47.09 ?  310 PRO A C   1 
ATOM   2454 O O   . PRO A 1 310 ? 47.702  11.350  -8.151  1.00 48.29 ?  310 PRO A O   1 
ATOM   2455 C CB  . PRO A 1 310 ? 50.697  11.407  -7.262  1.00 47.12 ?  310 PRO A CB  1 
ATOM   2456 C CG  . PRO A 1 310 ? 51.653  10.262  -7.432  1.00 47.92 ?  310 PRO A CG  1 
ATOM   2457 C CD  . PRO A 1 310 ? 51.400  9.339   -6.275  1.00 48.14 ?  310 PRO A CD  1 
ATOM   2458 N N   . GLU A 1 311 ? 48.273  9.165   -8.068  1.00 51.11 ?  311 GLU A N   1 
ATOM   2459 C CA  . GLU A 1 311 ? 47.265  8.701   -9.012  1.00 50.76 ?  311 GLU A CA  1 
ATOM   2460 C C   . GLU A 1 311 ? 45.852  8.721   -8.433  1.00 51.25 ?  311 GLU A C   1 
ATOM   2461 O O   . GLU A 1 311 ? 44.888  8.578   -9.194  1.00 47.89 ?  311 GLU A O   1 
ATOM   2462 C CB  . GLU A 1 311 ? 47.629  7.289   -9.479  1.00 52.26 ?  311 GLU A CB  1 
ATOM   2463 C CG  . GLU A 1 311 ? 49.113  7.112   -9.828  1.00 54.35 ?  311 GLU A CG  1 
ATOM   2464 C CD  . GLU A 1 311 ? 49.896  6.355   -8.763  1.00 56.67 ?  311 GLU A CD  1 
ATOM   2465 O OE1 . GLU A 1 311 ? 50.766  5.530   -9.121  1.00 63.36 ?  311 GLU A OE1 1 
ATOM   2466 O OE2 . GLU A 1 311 ? 49.650  6.589   -7.564  1.00 53.92 -1 311 GLU A OE2 1 
ATOM   2467 N N   . VAL A 1 312 ? 45.704  8.888   -7.121  1.00 48.36 ?  312 VAL A N   1 
ATOM   2468 C CA  . VAL A 1 312 ? 44.400  9.054   -6.493  1.00 44.29 ?  312 VAL A CA  1 
ATOM   2469 C C   . VAL A 1 312 ? 44.298  10.481  -5.970  1.00 48.71 ?  312 VAL A C   1 
ATOM   2470 O O   . VAL A 1 312 ? 45.298  11.188  -5.807  1.00 47.20 ?  312 VAL A O   1 
ATOM   2471 C CB  . VAL A 1 312 ? 44.159  8.033   -5.360  1.00 47.64 ?  312 VAL A CB  1 
ATOM   2472 C CG1 . VAL A 1 312 ? 44.376  6.615   -5.870  1.00 44.49 ?  312 VAL A CG1 1 
ATOM   2473 C CG2 . VAL A 1 312 ? 45.069  8.330   -4.168  1.00 43.31 ?  312 VAL A CG2 1 
ATOM   2474 N N   . LYS A 1 313 ? 43.066  10.942  -5.720  1.00 44.19 ?  313 LYS A N   1 
ATOM   2475 C CA  . LYS A 1 313 ? 42.838  12.302  -5.172  1.00 45.35 ?  313 LYS A CA  1 
ATOM   2476 C C   . LYS A 1 313 ? 41.810  12.313  -4.030  1.00 43.79 ?  313 LYS A C   1 
ATOM   2477 O O   . LYS A 1 313 ? 40.640  12.097  -4.322  1.00 42.50 ?  313 LYS A O   1 
ATOM   2478 C CB  . LYS A 1 313 ? 42.346  13.220  -6.287  1.00 46.49 ?  313 LYS A CB  1 
ATOM   2479 C CG  . LYS A 1 313 ? 41.997  14.647  -5.880  1.00 51.25 ?  313 LYS A CG  1 
ATOM   2480 C CD  . LYS A 1 313 ? 43.151  15.407  -5.256  1.00 51.62 ?  313 LYS A CD  1 
ATOM   2481 C CE  . LYS A 1 313 ? 42.729  16.697  -4.589  1.00 50.13 ?  313 LYS A CE  1 
ATOM   2482 N NZ  . LYS A 1 313 ? 41.628  17.355  -5.327  1.00 52.47 1  313 LYS A NZ  1 
ATOM   2483 N N   . VAL A 1 314 ? 42.223  12.622  -2.793  1.00 43.49 ?  314 VAL A N   1 
ATOM   2484 C CA  . VAL A 1 314 ? 41.249  12.775  -1.674  1.00 43.13 ?  314 VAL A CA  1 
ATOM   2485 C C   . VAL A 1 314 ? 40.520  14.088  -1.901  1.00 47.53 ?  314 VAL A C   1 
ATOM   2486 O O   . VAL A 1 314 ? 41.166  15.136  -1.851  1.00 49.07 ?  314 VAL A O   1 
ATOM   2487 C CB  . VAL A 1 314 ? 41.888  12.755  -0.276  1.00 43.12 ?  314 VAL A CB  1 
ATOM   2488 C CG1 . VAL A 1 314 ? 40.845  12.711  0.826   1.00 41.64 ?  314 VAL A CG1 1 
ATOM   2489 C CG2 . VAL A 1 314 ? 42.888  11.634  -0.125  1.00 43.08 ?  314 VAL A CG2 1 
ATOM   2490 N N   . LEU A 1 315 ? 39.214  14.034  -2.121  1.00 44.06 ?  315 LEU A N   1 
ATOM   2491 C CA  . LEU A 1 315 ? 38.510  15.282  -2.472  1.00 45.56 ?  315 LEU A CA  1 
ATOM   2492 C C   . LEU A 1 315 ? 38.483  16.243  -1.302  1.00 44.40 ?  315 LEU A C   1 
ATOM   2493 O O   . LEU A 1 315 ? 38.501  15.788  -0.159  1.00 44.84 ?  315 LEU A O   1 
ATOM   2494 C CB  . LEU A 1 315 ? 37.072  14.978  -2.889  1.00 47.42 ?  315 LEU A CB  1 
ATOM   2495 C CG  . LEU A 1 315 ? 36.851  14.519  -4.327  1.00 46.73 ?  315 LEU A CG  1 
ATOM   2496 C CD1 . LEU A 1 315 ? 35.495  14.983  -4.817  1.00 45.09 ?  315 LEU A CD1 1 
ATOM   2497 C CD2 . LEU A 1 315 ? 37.951  15.029  -5.243  1.00 53.58 ?  315 LEU A CD2 1 
ATOM   2498 N N   . ASP A 1 316 ? 38.412  17.530  -1.611  1.00 46.29 ?  316 ASP A N   1 
ATOM   2499 C CA  . ASP A 1 316 ? 38.232  18.528  -0.538  1.00 47.37 ?  316 ASP A CA  1 
ATOM   2500 C C   . ASP A 1 316 ? 36.907  18.212  0.151   1.00 45.58 ?  316 ASP A C   1 
ATOM   2501 O O   . ASP A 1 316 ? 35.899  18.138  -0.526  1.00 50.74 ?  316 ASP A O   1 
ATOM   2502 C CB  . ASP A 1 316 ? 38.335  19.960  -1.055  1.00 47.76 ?  316 ASP A CB  1 
ATOM   2503 C CG  . ASP A 1 316 ? 39.759  20.360  -1.404  1.00 55.04 ?  316 ASP A CG  1 
ATOM   2504 O OD1 . ASP A 1 316 ? 40.689  19.652  -0.973  1.00 52.05 ?  316 ASP A OD1 1 
ATOM   2505 O OD2 . ASP A 1 316 ? 39.925  21.377  -2.101  1.00 54.81 -1 316 ASP A OD2 1 
ATOM   2506 N N   . SER A 1 317 ? 36.949  17.982  1.441   1.00 50.43 ?  317 SER A N   1 
ATOM   2507 C CA  . SER A 1 317 ? 35.775  17.659  2.243   1.00 46.02 ?  317 SER A CA  1 
ATOM   2508 C C   . SER A 1 317 ? 35.739  18.573  3.457   1.00 42.94 ?  317 SER A C   1 
ATOM   2509 O O   . SER A 1 317 ? 36.783  18.876  4.043   1.00 44.66 ?  317 SER A O   1 
ATOM   2510 C CB  . SER A 1 317 ? 35.787  16.188  2.693   1.00 39.80 ?  317 SER A CB  1 
ATOM   2511 O OG  . SER A 1 317 ? 37.101  15.760  3.020   1.00 49.65 ?  317 SER A OG  1 
ATOM   2512 N N   . ASN A 1 318 ? 34.541  19.021  3.832   1.00 38.31 ?  318 ASN A N   1 
ATOM   2513 C CA  . ASN A 1 318 ? 34.391  19.889  4.994   1.00 37.55 ?  318 ASN A CA  1 
ATOM   2514 C C   . ASN A 1 318 ? 33.509  19.282  6.078   1.00 36.74 ?  318 ASN A C   1 
ATOM   2515 O O   . ASN A 1 318 ? 33.227  19.961  7.072   1.00 35.59 ?  318 ASN A O   1 
ATOM   2516 C CB  . ASN A 1 318 ? 33.863  21.275  4.577   1.00 41.44 ?  318 ASN A CB  1 
ATOM   2517 C CG  . ASN A 1 318 ? 32.382  21.275  4.167   1.00 35.29 ?  318 ASN A CG  1 
ATOM   2518 O OD1 . ASN A 1 318 ? 31.738  20.237  4.083   1.00 30.11 ?  318 ASN A OD1 1 
ATOM   2519 N ND2 . ASN A 1 318 ? 31.850  22.464  3.899   1.00 36.26 ?  318 ASN A ND2 1 
ATOM   2520 N N   . ALA A 1 319 ? 33.073  18.029  5.919   1.00 35.23 ?  319 ALA A N   1 
ATOM   2521 C CA  . ALA A 1 319 ? 32.216  17.397  6.913   1.00 33.78 ?  319 ALA A CA  1 
ATOM   2522 C C   . ALA A 1 319 ? 32.308  15.881  6.788   1.00 35.39 ?  319 ALA A C   1 
ATOM   2523 O O   . ALA A 1 319 ? 32.641  15.353  5.722   1.00 32.84 ?  319 ALA A O   1 
ATOM   2524 C CB  . ALA A 1 319 ? 30.761  17.864  6.776   1.00 31.64 ?  319 ALA A CB  1 
ATOM   2525 N N   . SER A 1 320 ? 32.036  15.204  7.912   1.00 32.33 ?  320 SER A N   1 
ATOM   2526 C CA  . SER A 1 320 ? 32.042  13.748  8.056   1.00 27.49 ?  320 SER A CA  1 
ATOM   2527 C C   . SER A 1 320 ? 33.442  13.207  8.325   1.00 31.48 ?  320 SER A C   1 
ATOM   2528 O O   . SER A 1 320 ? 34.449  13.891  8.103   1.00 34.78 ?  320 SER A O   1 
ATOM   2529 C CB  . SER A 1 320 ? 31.443  13.071  6.815   1.00 28.55 ?  320 SER A CB  1 
ATOM   2530 O OG  . SER A 1 320 ? 32.473  12.709  5.906   1.00 32.34 ?  320 SER A OG  1 
ATOM   2531 N N   . TYR A 1 321 ? 33.526  11.946  8.736   1.00 28.95 ?  321 TYR A N   1 
ATOM   2532 C CA  . TYR A 1 321 ? 34.835  11.288  8.947   1.00 29.56 ?  321 TYR A CA  1 
ATOM   2533 C C   . TYR A 1 321 ? 35.100  10.328  7.786   1.00 32.24 ?  321 TYR A C   1 
ATOM   2534 O O   . TYR A 1 321 ? 35.969  9.476   7.878   1.00 31.72 ?  321 TYR A O   1 
ATOM   2535 C CB  . TYR A 1 321 ? 34.892  10.604  10.307  1.00 30.47 ?  321 TYR A CB  1 
ATOM   2536 C CG  . TYR A 1 321 ? 33.811  9.607   10.646  1.00 26.76 ?  321 TYR A CG  1 
ATOM   2537 C CD1 . TYR A 1 321 ? 33.687  8.399   9.979   1.00 30.31 ?  321 TYR A CD1 1 
ATOM   2538 C CD2 . TYR A 1 321 ? 32.958  9.837   11.708  1.00 27.89 ?  321 TYR A CD2 1 
ATOM   2539 C CE1 . TYR A 1 321 ? 32.717  7.473   10.322  1.00 31.36 ?  321 TYR A CE1 1 
ATOM   2540 C CE2 . TYR A 1 321 ? 31.984  8.924   12.068  1.00 27.99 ?  321 TYR A CE2 1 
ATOM   2541 C CZ  . TYR A 1 321 ? 31.861  7.738   11.374  1.00 30.65 ?  321 TYR A CZ  1 
ATOM   2542 O OH  . TYR A 1 321 ? 30.906  6.842   11.739  1.00 25.81 ?  321 TYR A OH  1 
ATOM   2543 N N   . LEU A 1 322 ? 34.335  10.500  6.714   1.00 33.29 ?  322 LEU A N   1 
ATOM   2544 C CA  . LEU A 1 322 ? 34.494  9.616   5.536   1.00 33.59 ?  322 LEU A CA  1 
ATOM   2545 C C   . LEU A 1 322 ? 35.235  10.342  4.405   1.00 31.59 ?  322 LEU A C   1 
ATOM   2546 O O   . LEU A 1 322 ? 34.732  11.372  3.951   1.00 33.07 ?  322 LEU A O   1 
ATOM   2547 C CB  . LEU A 1 322 ? 33.101  9.132   5.133   1.00 32.72 ?  322 LEU A CB  1 
ATOM   2548 C CG  . LEU A 1 322 ? 32.317  8.535   6.297   1.00 34.26 ?  322 LEU A CG  1 
ATOM   2549 C CD1 . LEU A 1 322 ? 30.818  8.657   6.098   1.00 29.11 ?  322 LEU A CD1 1 
ATOM   2550 C CD2 . LEU A 1 322 ? 32.738  7.099   6.547   1.00 31.39 ?  322 LEU A CD2 1 
ATOM   2551 N N   . ALA A 1 323 ? 36.380  9.804   3.998   1.00 30.44 ?  323 ALA A N   1 
ATOM   2552 C CA  . ALA A 1 323 ? 37.166  10.373  2.881   1.00 32.47 ?  323 ALA A CA  1 
ATOM   2553 C C   . ALA A 1 323 ? 36.627  9.876   1.538   1.00 32.02 ?  323 ALA A C   1 
ATOM   2554 O O   . ALA A 1 323 ? 36.504  8.687   1.388   1.00 32.42 ?  323 ALA A O   1 
ATOM   2555 C CB  . ALA A 1 323 ? 38.599  10.003  3.052   1.00 32.68 ?  323 ALA A CB  1 
ATOM   2556 N N   . TRP A 1 324 ? 36.339  10.789  0.615   1.00 35.23 ?  324 TRP A N   1 
ATOM   2557 C CA  . TRP A 1 324 ? 35.800  10.457  -0.726  1.00 33.43 ?  324 TRP A CA  1 
ATOM   2558 C C   . TRP A 1 324 ? 36.986  10.598  -1.658  1.00 35.24 ?  324 TRP A C   1 
ATOM   2559 O O   . TRP A 1 324 ? 37.367  11.726  -1.933  1.00 34.93 ?  324 TRP A O   1 
ATOM   2560 C CB  . TRP A 1 324 ? 34.667  11.415  -1.082  1.00 33.16 ?  324 TRP A CB  1 
ATOM   2561 C CG  . TRP A 1 324 ? 33.778  11.083  -2.244  1.00 37.22 ?  324 TRP A CG  1 
ATOM   2562 C CD1 . TRP A 1 324 ? 33.398  11.956  -3.219  1.00 37.22 ?  324 TRP A CD1 1 
ATOM   2563 C CD2 . TRP A 1 324 ? 33.087  9.850   -2.531  1.00 35.48 ?  324 TRP A CD2 1 
ATOM   2564 N NE1 . TRP A 1 324 ? 32.552  11.352  -4.104  1.00 36.97 ?  324 TRP A NE1 1 
ATOM   2565 C CE2 . TRP A 1 324 ? 32.340  10.061  -3.710  1.00 36.26 ?  324 TRP A CE2 1 
ATOM   2566 C CE3 . TRP A 1 324 ? 33.039  8.586   -1.938  1.00 34.47 ?  324 TRP A CE3 1 
ATOM   2567 C CZ2 . TRP A 1 324 ? 31.556  9.067   -4.292  1.00 34.67 ?  324 TRP A CZ2 1 
ATOM   2568 C CZ3 . TRP A 1 324 ? 32.273  7.601   -2.517  1.00 37.34 ?  324 TRP A CZ3 1 
ATOM   2569 C CH2 . TRP A 1 324 ? 31.542  7.838   -3.680  1.00 31.59 ?  324 TRP A CH2 1 
ATOM   2570 N N   . VAL A 1 325 ? 37.519  9.478   -2.105  1.00 35.41 ?  325 VAL A N   1 
ATOM   2571 C CA  . VAL A 1 325 ? 38.778  9.480   -2.847  1.00 36.06 ?  325 VAL A CA  1 
ATOM   2572 C C   . VAL A 1 325 ? 38.505  9.152   -4.309  1.00 38.23 ?  325 VAL A C   1 
ATOM   2573 O O   . VAL A 1 325 ? 37.905  8.118   -4.623  1.00 33.65 ?  325 VAL A O   1 
ATOM   2574 C CB  . VAL A 1 325 ? 39.782  8.484   -2.245  1.00 29.29 ?  325 VAL A CB  1 
ATOM   2575 C CG1 . VAL A 1 325 ? 41.105  8.522   -3.008  1.00 35.47 ?  325 VAL A CG1 1 
ATOM   2576 C CG2 . VAL A 1 325 ? 40.001  8.778   -0.768  1.00 35.56 ?  325 VAL A CG2 1 
ATOM   2577 N N   . ASP A 1 326 ? 38.960  10.024  -5.202  1.00 34.12 ?  326 ASP A N   1 
ATOM   2578 C CA  . ASP A 1 326 ? 38.866  9.777   -6.636  1.00 36.56 ?  326 ASP A CA  1 
ATOM   2579 C C   . ASP A 1 326 ? 39.950  8.779   -7.035  1.00 36.11 ?  326 ASP A C   1 
ATOM   2580 O O   . ASP A 1 326 ? 41.143  9.091   -6.970  1.00 37.67 ?  326 ASP A O   1 
ATOM   2581 C CB  . ASP A 1 326 ? 39.002  11.100  -7.387  1.00 37.03 ?  326 ASP A CB  1 
ATOM   2582 C CG  . ASP A 1 326 ? 38.645  10.983  -8.847  1.00 39.12 ?  326 ASP A CG  1 
ATOM   2583 O OD1 . ASP A 1 326 ? 38.860  9.900   -9.420  1.00 40.72 ?  326 ASP A OD1 1 
ATOM   2584 O OD2 . ASP A 1 326 ? 38.139  11.977  -9.415  1.00 41.40 -1 326 ASP A OD2 1 
ATOM   2585 N N   . ILE A 1 327 ? 39.539  7.601   -7.497  1.00 34.27 ?  327 ILE A N   1 
ATOM   2586 C CA  . ILE A 1 327 ? 40.504  6.566   -7.977  1.00 34.42 ?  327 ILE A CA  1 
ATOM   2587 C C   . ILE A 1 327 ? 40.388  6.422   -9.504  1.00 35.80 ?  327 ILE A C   1 
ATOM   2588 O O   . ILE A 1 327 ? 40.863  5.427   -10.013 1.00 34.48 ?  327 ILE A O   1 
ATOM   2589 C CB  . ILE A 1 327 ? 40.239  5.240   -7.248  1.00 35.25 ?  327 ILE A CB  1 
ATOM   2590 C CG1 . ILE A 1 327 ? 38.778  4.811   -7.382  1.00 38.81 ?  327 ILE A CG1 1 
ATOM   2591 C CG2 . ILE A 1 327 ? 40.666  5.314   -5.795  1.00 33.18 ?  327 ILE A CG2 1 
ATOM   2592 C CD1 . ILE A 1 327 ? 38.611  3.330   -7.549  1.00 35.57 ?  327 ILE A CD1 1 
ATOM   2593 N N   . SER A 1 328 ? 39.758  7.387   -10.181 1.00 38.02 ?  328 SER A N   1 
ATOM   2594 C CA  . SER A 1 328 ? 39.484  7.306   -11.645 1.00 40.96 ?  328 SER A CA  1 
ATOM   2595 C C   . SER A 1 328 ? 40.766  7.134   -12.446 1.00 40.74 ?  328 SER A C   1 
ATOM   2596 O O   . SER A 1 328 ? 40.742  6.390   -13.414 1.00 43.17 ?  328 SER A O   1 
ATOM   2597 C CB  . SER A 1 328 ? 38.761  8.513   -12.124 1.00 41.41 ?  328 SER A CB  1 
ATOM   2598 O OG  . SER A 1 328 ? 39.550  9.678   -11.996 1.00 39.74 ?  328 SER A OG  1 
ATOM   2599 N N   . ALA A 1 329 ? 41.822  7.821   -12.030 1.00 38.06 ?  329 ALA A N   1 
ATOM   2600 C CA  . ALA A 1 329 ? 43.112  7.757   -12.746 1.00 42.08 ?  329 ALA A CA  1 
ATOM   2601 C C   . ALA A 1 329 ? 43.752  6.385   -12.552 1.00 40.41 ?  329 ALA A C   1 
ATOM   2602 O O   . ALA A 1 329 ? 44.644  6.054   -13.333 1.00 40.48 ?  329 ALA A O   1 
ATOM   2603 C CB  . ALA A 1 329 ? 44.004  8.868   -12.267 1.00 40.14 ?  329 ALA A CB  1 
ATOM   2604 N N   . LEU A 1 330 ? 43.286  5.580   -11.603 1.00 38.69 ?  330 LEU A N   1 
ATOM   2605 C CA  . LEU A 1 330 ? 43.842  4.206   -11.478 1.00 39.89 ?  330 LEU A CA  1 
ATOM   2606 C C   . LEU A 1 330 ? 43.238  3.343   -12.579 1.00 40.65 ?  330 LEU A C   1 
ATOM   2607 O O   . LEU A 1 330 ? 43.782  2.278   -12.831 1.00 38.45 ?  330 LEU A O   1 
ATOM   2608 C CB  . LEU A 1 330 ? 43.560  3.626   -10.098 1.00 40.26 ?  330 LEU A CB  1 
ATOM   2609 C CG  . LEU A 1 330 ? 44.301  4.255   -8.926  1.00 45.35 ?  330 LEU A CG  1 
ATOM   2610 C CD1 . LEU A 1 330 ? 43.857  3.587   -7.640  1.00 43.29 ?  330 LEU A CD1 1 
ATOM   2611 C CD2 . LEU A 1 330 ? 45.799  4.104   -9.104  1.00 46.98 ?  330 LEU A CD2 1 
ATOM   2612 N N   . GLY A 1 331 ? 42.144  3.813   -13.175 1.00 40.47 ?  331 GLY A N   1 
ATOM   2613 C CA  . GLY A 1 331 ? 41.502  3.123   -14.307 1.00 40.78 ?  331 GLY A CA  1 
ATOM   2614 C C   . GLY A 1 331 ? 40.749  1.880   -13.911 1.00 41.96 ?  331 GLY A C   1 
ATOM   2615 O O   . GLY A 1 331 ? 40.434  1.096   -14.797 1.00 42.71 ?  331 GLY A O   1 
ATOM   2616 N N   . MET A 1 332 ? 40.480  1.714   -12.622 1.00 39.53 ?  332 MET A N   1 
ATOM   2617 C CA  . MET A 1 332 ? 39.837  0.487   -12.127 1.00 38.87 ?  332 MET A CA  1 
ATOM   2618 C C   . MET A 1 332 ? 38.495  0.850   -11.518 1.00 43.69 ?  332 MET A C   1 
ATOM   2619 O O   . MET A 1 332 ? 38.390  1.899   -10.868 1.00 39.59 ?  332 MET A O   1 
ATOM   2620 C CB  . MET A 1 332 ? 40.670  -0.178  -11.041 1.00 40.28 ?  332 MET A CB  1 
ATOM   2621 C CG  . MET A 1 332 ? 40.365  -1.630  -10.830 1.00 43.45 ?  332 MET A CG  1 
ATOM   2622 S SD  . MET A 1 332 ? 41.693  -2.365  -9.870  1.00 48.64 ?  332 MET A SD  1 
ATOM   2623 C CE  . MET A 1 332 ? 41.121  -4.056  -9.761  1.00 42.18 ?  332 MET A CE  1 
ATOM   2624 N N   . ASN A 1 333 ? 37.495  0.054   -11.833 1.00 41.04 ?  333 ASN A N   1 
ATOM   2625 C CA  . ASN A 1 333 ? 36.200  0.230   -11.187 1.00 39.73 ?  333 ASN A CA  1 
ATOM   2626 C C   . ASN A 1 333 ? 36.363  0.121   -9.672  1.00 39.42 ?  333 ASN A C   1 
ATOM   2627 O O   . ASN A 1 333 ? 37.189  -0.648  -9.173  1.00 40.96 ?  333 ASN A O   1 
ATOM   2628 C CB  . ASN A 1 333 ? 35.198  -0.812  -11.698 1.00 40.65 ?  333 ASN A CB  1 
ATOM   2629 C CG  . ASN A 1 333 ? 33.925  -0.862  -10.869 1.00 43.71 ?  333 ASN A CG  1 
ATOM   2630 O OD1 . ASN A 1 333 ? 33.137  0.080   -10.879 1.00 40.36 ?  333 ASN A OD1 1 
ATOM   2631 N ND2 . ASN A 1 333 ? 33.718  -1.965  -10.152 1.00 45.37 ?  333 ASN A ND2 1 
ATOM   2632 N N   . ALA A 1 334 ? 35.652  0.960   -8.935  1.00 38.68 ?  334 ALA A N   1 
ATOM   2633 C CA  . ALA A 1 334 ? 35.812  1.012   -7.464  1.00 38.48 ?  334 ALA A CA  1 
ATOM   2634 C C   . ALA A 1 334 ? 35.595  -0.347  -6.790  1.00 36.83 ?  334 ALA A C   1 
ATOM   2635 O O   . ALA A 1 334 ? 36.389  -0.681  -5.923  1.00 34.40 ?  334 ALA A O   1 
ATOM   2636 C CB  . ALA A 1 334 ? 34.863  2.026   -6.924  1.00 31.31 ?  334 ALA A CB  1 
ATOM   2637 N N   . GLU A 1 335 ? 34.536  -1.056  -7.151  1.00 38.47 ?  335 GLU A N   1 
ATOM   2638 C CA  . GLU A 1 335 ? 34.285  -2.330  -6.481  1.00 38.52 ?  335 GLU A CA  1 
ATOM   2639 C C   . GLU A 1 335 ? 35.400  -3.328  -6.764  1.00 40.36 ?  335 GLU A C   1 
ATOM   2640 O O   . GLU A 1 335 ? 35.899  -3.997  -5.849  1.00 39.42 ?  335 GLU A O   1 
ATOM   2641 C CB  . GLU A 1 335 ? 32.936  -2.895  -6.914  1.00 45.25 ?  335 GLU A CB  1 
ATOM   2642 C CG  . GLU A 1 335 ? 32.465  -4.056  -6.064  1.00 46.98 ?  335 GLU A CG  1 
ATOM   2643 C CD  . GLU A 1 335 ? 32.843  -5.400  -6.653  1.00 54.94 ?  335 GLU A CD  1 
ATOM   2644 O OE1 . GLU A 1 335 ? 32.632  -6.422  -5.967  1.00 56.08 ?  335 GLU A OE1 1 
ATOM   2645 O OE2 . GLU A 1 335 ? 33.347  -5.433  -7.800  1.00 57.36 -1 335 GLU A OE2 1 
ATOM   2646 N N   . ASP A 1 336 ? 35.788  -3.457  -8.035  1.00 39.06 ?  336 ASP A N   1 
ATOM   2647 C CA  . ASP A 1 336 ? 36.921  -4.307  -8.377  1.00 40.86 ?  336 ASP A CA  1 
ATOM   2648 C C   . ASP A 1 336 ? 38.149  -3.909  -7.575  1.00 37.24 ?  336 ASP A C   1 
ATOM   2649 O O   . ASP A 1 336 ? 38.850  -4.763  -7.026  1.00 38.36 ?  336 ASP A O   1 
ATOM   2650 C CB  . ASP A 1 336 ? 37.216  -4.213  -9.875  1.00 39.35 ?  336 ASP A CB  1 
ATOM   2651 C CG  . ASP A 1 336 ? 36.073  -4.723  -10.736 1.00 43.10 ?  336 ASP A CG  1 
ATOM   2652 O OD1 . ASP A 1 336 ? 35.053  -4.008  -10.891 1.00 40.99 ?  336 ASP A OD1 1 
ATOM   2653 O OD2 . ASP A 1 336 ? 36.203  -5.843  -11.268 1.00 44.10 -1 336 ASP A OD2 1 
ATOM   2654 N N   . PHE A 1 337 ? 38.416  -2.605  -7.494  1.00 40.15 ?  337 PHE A N   1 
ATOM   2655 C CA  . PHE A 1 337 ? 39.574  -2.124  -6.754  1.00 36.06 ?  337 PHE A CA  1 
ATOM   2656 C C   . PHE A 1 337 ? 39.463  -2.469  -5.275  1.00 38.19 ?  337 PHE A C   1 
ATOM   2657 O O   . PHE A 1 337 ? 40.425  -2.951  -4.666  1.00 34.58 ?  337 PHE A O   1 
ATOM   2658 C CB  . PHE A 1 337 ? 39.721  -0.616  -6.960  1.00 36.92 ?  337 PHE A CB  1 
ATOM   2659 C CG  . PHE A 1 337 ? 40.894  -0.020  -6.237  1.00 35.52 ?  337 PHE A CG  1 
ATOM   2660 C CD1 . PHE A 1 337 ? 42.185  -0.343  -6.617  1.00 39.17 ?  337 PHE A CD1 1 
ATOM   2661 C CD2 . PHE A 1 337 ? 40.710  0.858   -5.183  1.00 39.25 ?  337 PHE A CD2 1 
ATOM   2662 C CE1 . PHE A 1 337 ? 43.269  0.187   -5.959  1.00 36.77 ?  337 PHE A CE1 1 
ATOM   2663 C CE2 . PHE A 1 337 ? 41.797  1.399   -4.521  1.00 31.85 ?  337 PHE A CE2 1 
ATOM   2664 C CZ  . PHE A 1 337 ? 43.075  1.064   -4.913  1.00 38.18 ?  337 PHE A CZ  1 
ATOM   2665 N N   . CYS A 1 338 ? 38.280  -2.266  -4.695  1.00 36.87 ?  338 CYS A N   1 
ATOM   2666 C CA  . CYS A 1 338 ? 38.090  -2.559  -3.281  1.00 39.48 ?  338 CYS A CA  1 
ATOM   2667 C C   . CYS A 1 338 ? 38.240  -4.054  -3.005  1.00 39.35 ?  338 CYS A C   1 
ATOM   2668 O O   . CYS A 1 338 ? 38.848  -4.456  -2.002  1.00 35.85 ?  338 CYS A O   1 
ATOM   2669 C CB  . CYS A 1 338 ? 36.717  -2.043  -2.861  1.00 34.90 ?  338 CYS A CB  1 
ATOM   2670 S SG  . CYS A 1 338 ? 36.730  -0.252  -2.724  1.00 34.12 ?  338 CYS A SG  1 
ATOM   2671 N N   . LYS A 1 339 ? 37.718  -4.898  -3.904  1.00 37.19 ?  339 LYS A N   1 
ATOM   2672 C CA  . LYS A 1 339 ? 37.889  -6.343  -3.749  1.00 40.43 ?  339 LYS A CA  1 
ATOM   2673 C C   . LYS A 1 339 ? 39.357  -6.729  -3.829  1.00 38.08 ?  339 LYS A C   1 
ATOM   2674 O O   . LYS A 1 339 ? 39.876  -7.446  -2.964  1.00 39.06 ?  339 LYS A O   1 
ATOM   2675 C CB  . LYS A 1 339 ? 37.101  -7.087  -4.824  1.00 39.66 ?  339 LYS A CB  1 
ATOM   2676 C CG  . LYS A 1 339 ? 35.757  -7.590  -4.376  1.00 45.79 ?  339 LYS A CG  1 
ATOM   2677 C CD  . LYS A 1 339 ? 35.004  -8.142  -5.567  1.00 46.67 ?  339 LYS A CD  1 
ATOM   2678 C CE  . LYS A 1 339 ? 35.732  -9.319  -6.195  1.00 52.22 ?  339 LYS A CE  1 
ATOM   2679 N NZ  . LYS A 1 339 ? 34.778  -10.245 -6.887  1.00 47.07 1  339 LYS A NZ  1 
ATOM   2680 N N   . TYR A 1 340 ? 40.038  -6.255  -4.875  1.00 39.16 ?  340 TYR A N   1 
ATOM   2681 C CA  . TYR A 1 340 ? 41.467  -6.501  -5.027  1.00 41.30 ?  340 TYR A CA  1 
ATOM   2682 C C   . TYR A 1 340 ? 42.238  -6.053  -3.792  1.00 39.82 ?  340 TYR A C   1 
ATOM   2683 O O   . TYR A 1 340 ? 43.160  -6.744  -3.340  1.00 40.89 ?  340 TYR A O   1 
ATOM   2684 C CB  . TYR A 1 340 ? 41.975  -5.778  -6.278  1.00 41.51 ?  340 TYR A CB  1 
ATOM   2685 C CG  . TYR A 1 340 ? 43.477  -5.788  -6.425  1.00 39.93 ?  340 TYR A CG  1 
ATOM   2686 C CD1 . TYR A 1 340 ? 44.122  -6.833  -7.070  1.00 44.76 ?  340 TYR A CD1 1 
ATOM   2687 C CD2 . TYR A 1 340 ? 44.248  -4.750  -5.922  1.00 45.90 ?  340 TYR A CD2 1 
ATOM   2688 C CE1 . TYR A 1 340 ? 45.497  -6.846  -7.207  1.00 52.10 ?  340 TYR A CE1 1 
ATOM   2689 C CE2 . TYR A 1 340 ? 45.622  -4.755  -6.048  1.00 49.83 ?  340 TYR A CE2 1 
ATOM   2690 C CZ  . TYR A 1 340 ? 46.242  -5.801  -6.691  1.00 51.42 ?  340 TYR A CZ  1 
ATOM   2691 O OH  . TYR A 1 340 ? 47.616  -5.796  -6.812  1.00 57.21 ?  340 TYR A OH  1 
ATOM   2692 N N   . LEU A 1 341 ? 41.868  -4.895  -3.235  1.00 36.37 ?  341 LEU A N   1 
ATOM   2693 C CA  . LEU A 1 341 ? 42.534  -4.379  -2.045  1.00 39.66 ?  341 LEU A CA  1 
ATOM   2694 C C   . LEU A 1 341 ? 42.418  -5.349  -0.874  1.00 38.00 ?  341 LEU A C   1 
ATOM   2695 O O   . LEU A 1 341 ? 43.423  -5.700  -0.244  1.00 38.26 ?  341 LEU A O   1 
ATOM   2696 C CB  . LEU A 1 341 ? 41.938  -3.020  -1.678  1.00 39.64 ?  341 LEU A CB  1 
ATOM   2697 C CG  . LEU A 1 341 ? 42.887  -1.862  -1.391  1.00 44.96 ?  341 LEU A CG  1 
ATOM   2698 C CD1 . LEU A 1 341 ? 44.002  -1.800  -2.423  1.00 46.21 ?  341 LEU A CD1 1 
ATOM   2699 C CD2 . LEU A 1 341 ? 42.099  -0.562  -1.377  1.00 41.49 ?  341 LEU A CD2 1 
ATOM   2700 N N   . ARG A 1 342 ? 41.195  -5.784  -0.553  1.00 37.35 ?  342 ARG A N   1 
ATOM   2701 C CA  . ARG A 1 342 ? 41.029  -6.720  0.557   1.00 35.58 ?  342 ARG A CA  1 
ATOM   2702 C C   . ARG A 1 342 ? 41.789  -8.015  0.302   1.00 39.02 ?  342 ARG A C   1 
ATOM   2703 O O   . ARG A 1 342 ? 42.404  -8.572  1.217   1.00 36.39 ?  342 ARG A O   1 
ATOM   2704 C CB  . ARG A 1 342 ? 39.551  -7.028  0.800   1.00 35.25 ?  342 ARG A CB  1 
ATOM   2705 C CG  . ARG A 1 342 ? 39.364  -8.156  1.807   1.00 38.66 ?  342 ARG A CG  1 
ATOM   2706 C CD  . ARG A 1 342 ? 37.903  -8.436  2.169   1.00 41.37 ?  342 ARG A CD  1 
ATOM   2707 N NE  . ARG A 1 342 ? 37.788  -9.131  3.457   1.00 39.19 ?  342 ARG A NE  1 
ATOM   2708 C CZ  . ARG A 1 342 ? 36.630  -9.394  4.059   1.00 42.18 ?  342 ARG A CZ  1 
ATOM   2709 N NH1 . ARG A 1 342 ? 35.496  -9.034  3.478   1.00 33.92 1  342 ARG A NH1 1 
ATOM   2710 N NH2 . ARG A 1 342 ? 36.598  -10.017 5.232   1.00 38.54 ?  342 ARG A NH2 1 
ATOM   2711 N N   . GLU A 1 343 ? 41.760  -8.511  -0.939  1.00 39.29 ?  343 GLU A N   1 
ATOM   2712 C CA  . GLU A 1 343 ? 42.404  -9.785  -1.238  1.00 39.72 ?  343 GLU A CA  1 
ATOM   2713 C C   . GLU A 1 343 ? 43.914  -9.697  -1.072  1.00 37.70 ?  343 GLU A C   1 
ATOM   2714 O O   . GLU A 1 343 ? 44.539  -10.594 -0.494  1.00 40.51 ?  343 GLU A O   1 
ATOM   2715 C CB  . GLU A 1 343 ? 42.042  -10.233 -2.653  1.00 37.07 ?  343 GLU A CB  1 
ATOM   2716 C CG  . GLU A 1 343 ? 40.641  -10.778 -2.750  1.00 36.57 ?  343 GLU A CG  1 
ATOM   2717 C CD  . GLU A 1 343 ? 40.244  -11.121 -4.165  1.00 42.41 ?  343 GLU A CD  1 
ATOM   2718 O OE1 . GLU A 1 343 ? 41.139  -11.207 -5.033  1.00 41.03 ?  343 GLU A OE1 1 
ATOM   2719 O OE2 . GLU A 1 343 ? 39.031  -11.311 -4.404  1.00 38.77 -1 343 GLU A OE2 1 
ATOM   2720 N N   . LYS A 1 344 ? 44.521  -8.617  -1.567  1.00 38.03 ?  344 LYS A N   1 
ATOM   2721 C CA  . LYS A 1 344 ? 45.978  -8.517  -1.519  1.00 43.17 ?  344 LYS A CA  1 
ATOM   2722 C C   . LYS A 1 344 ? 46.483  -8.034  -0.164  1.00 39.93 ?  344 LYS A C   1 
ATOM   2723 O O   . LYS A 1 344 ? 47.496  -8.535  0.332   1.00 43.32 ?  344 LYS A O   1 
ATOM   2724 C CB  . LYS A 1 344 ? 46.482  -7.586  -2.623  1.00 42.73 ?  344 LYS A CB  1 
ATOM   2725 C CG  . LYS A 1 344 ? 46.712  -8.267  -3.962  1.00 48.81 ?  344 LYS A CG  1 
ATOM   2726 C CD  . LYS A 1 344 ? 47.734  -9.399  -3.863  1.00 48.27 ?  344 LYS A CD  1 
ATOM   2727 C CE  . LYS A 1 344 ? 49.088  -8.897  -3.365  1.00 53.08 ?  344 LYS A CE  1 
ATOM   2728 N NZ  . LYS A 1 344 ? 50.219  -9.462  -4.158  1.00 54.95 1  344 LYS A NZ  1 
ATOM   2729 N N   . THR A 1 345 ? 45.799  -7.062  0.446   1.00 38.47 ?  345 THR A N   1 
ATOM   2730 C CA  . THR A 1 345 ? 46.317  -6.365  1.617   1.00 36.98 ?  345 THR A CA  1 
ATOM   2731 C C   . THR A 1 345 ? 45.471  -6.520  2.867   1.00 39.71 ?  345 THR A C   1 
ATOM   2732 O O   . THR A 1 345 ? 45.944  -6.161  3.954   1.00 36.40 ?  345 THR A O   1 
ATOM   2733 C CB  . THR A 1 345 ? 46.443  -4.861  1.341   1.00 37.96 ?  345 THR A CB  1 
ATOM   2734 O OG1 . THR A 1 345 ? 45.133  -4.280  1.323   1.00 35.72 ?  345 THR A OG1 1 
ATOM   2735 C CG2 . THR A 1 345 ? 47.121  -4.606  -0.004  1.00 42.42 ?  345 THR A CG2 1 
ATOM   2736 N N   . GLY A 1 346 ? 44.237  -7.001  2.749   1.00 38.63 ?  346 GLY A N   1 
ATOM   2737 C CA  . GLY A 1 346 ? 43.340  -7.065  3.877   1.00 38.12 ?  346 GLY A CA  1 
ATOM   2738 C C   . GLY A 1 346 ? 42.664  -5.756  4.230   1.00 38.80 ?  346 GLY A C   1 
ATOM   2739 O O   . GLY A 1 346 ? 41.923  -5.712  5.222   1.00 39.82 ?  346 GLY A O   1 
ATOM   2740 N N   . LEU A 1 347 ? 42.898  -4.693  3.462   1.00 34.23 ?  347 LEU A N   1 
ATOM   2741 C CA  . LEU A 1 347 ? 42.231  -3.415  3.690   1.00 36.90 ?  347 LEU A CA  1 
ATOM   2742 C C   . LEU A 1 347 ? 40.844  -3.448  3.069   1.00 39.65 ?  347 LEU A C   1 
ATOM   2743 O O   . LEU A 1 347 ? 40.695  -3.759  1.883   1.00 34.81 ?  347 LEU A O   1 
ATOM   2744 C CB  . LEU A 1 347 ? 43.036  -2.262  3.090   1.00 36.97 ?  347 LEU A CB  1 
ATOM   2745 C CG  . LEU A 1 347 ? 42.368  -0.882  3.219   1.00 34.93 ?  347 LEU A CG  1 
ATOM   2746 C CD1 . LEU A 1 347 ? 42.366  -0.442  4.683   1.00 33.79 ?  347 LEU A CD1 1 
ATOM   2747 C CD2 . LEU A 1 347 ? 43.044  0.158   2.340   1.00 33.10 ?  347 LEU A CD2 1 
ATOM   2748 N N   . ILE A 1 348 ? 39.833  -3.117  3.867   1.00 33.76 ?  348 ILE A N   1 
ATOM   2749 C CA  . ILE A 1 348 ? 38.439  -3.173  3.445   1.00 32.25 ?  348 ILE A CA  1 
ATOM   2750 C C   . ILE A 1 348 ? 37.909  -1.753  3.481   1.00 33.46 ?  348 ILE A C   1 
ATOM   2751 O O   . ILE A 1 348 ? 37.736  -1.179  4.562   1.00 31.42 ?  348 ILE A O   1 
ATOM   2752 C CB  . ILE A 1 348 ? 37.597  -4.094  4.344   1.00 32.53 ?  348 ILE A CB  1 
ATOM   2753 C CG1 . ILE A 1 348 ? 38.189  -5.502  4.397   1.00 33.14 ?  348 ILE A CG1 1 
ATOM   2754 C CG2 . ILE A 1 348 ? 36.162  -4.115  3.867   1.00 31.54 ?  348 ILE A CG2 1 
ATOM   2755 C CD1 . ILE A 1 348 ? 37.652  -6.360  5.552   1.00 37.43 ?  348 ILE A CD1 1 
ATOM   2756 N N   . ILE A 1 349 ? 37.659  -1.176  2.304   1.00 30.91 ?  349 ILE A N   1 
ATOM   2757 C CA  . ILE A 1 349 ? 37.066  0.149   2.200   1.00 31.90 ?  349 ILE A CA  1 
ATOM   2758 C C   . ILE A 1 349 ? 35.824  0.066   1.322   1.00 32.98 ?  349 ILE A C   1 
ATOM   2759 O O   . ILE A 1 349 ? 35.561  -0.943  0.667   1.00 38.56 ?  349 ILE A O   1 
ATOM   2760 C CB  . ILE A 1 349 ? 38.058  1.194   1.647   1.00 31.82 ?  349 ILE A CB  1 
ATOM   2761 C CG1 . ILE A 1 349 ? 38.605  0.749   0.283   1.00 31.73 ?  349 ILE A CG1 1 
ATOM   2762 C CG2 . ILE A 1 349 ? 39.177  1.430   2.655   1.00 29.70 ?  349 ILE A CG2 1 
ATOM   2763 C CD1 . ILE A 1 349 ? 39.591  1.750   -0.310  1.00 32.22 ?  349 ILE A CD1 1 
ATOM   2764 N N   . SER A 1 350 ? 35.052  1.149   1.322   1.00 33.40 ?  350 SER A N   1 
ATOM   2765 C CA  . SER A 1 350 ? 33.747  1.171   0.675   1.00 28.47 ?  350 SER A CA  1 
ATOM   2766 C C   . SER A 1 350 ? 33.909  1.576   -0.787  1.00 34.34 ?  350 SER A C   1 
ATOM   2767 O O   . SER A 1 350 ? 34.463  2.640   -1.091  1.00 32.65 ?  350 SER A O   1 
ATOM   2768 C CB  . SER A 1 350 ? 32.796  2.130   1.389   1.00 33.27 ?  350 SER A CB  1 
ATOM   2769 O OG  . SER A 1 350 ? 32.469  1.669   2.689   1.00 38.58 ?  350 SER A OG  1 
ATOM   2770 N N   . ALA A 1 351 ? 33.426  0.724   -1.684  1.00 30.85 ?  351 ALA A N   1 
ATOM   2771 C CA  . ALA A 1 351 ? 33.365  1.069   -3.092  1.00 31.73 ?  351 ALA A CA  1 
ATOM   2772 C C   . ALA A 1 351 ? 32.302  2.130   -3.313  1.00 30.86 ?  351 ALA A C   1 
ATOM   2773 O O   . ALA A 1 351 ? 31.270  2.146   -2.643  1.00 31.77 ?  351 ALA A O   1 
ATOM   2774 C CB  . ALA A 1 351 ? 33.049  -0.167  -3.925  1.00 30.52 ?  351 ALA A CB  1 
ATOM   2775 N N   . GLY A 1 352 ? 32.558  3.031   -4.257  1.00 31.49 ?  352 GLY A N   1 
ATOM   2776 C CA  . GLY A 1 352 ? 31.593  4.096   -4.472  1.00 30.38 ?  352 GLY A CA  1 
ATOM   2777 C C   . GLY A 1 352 ? 30.368  3.693   -5.256  1.00 29.88 ?  352 GLY A C   1 
ATOM   2778 O O   . GLY A 1 352 ? 29.395  4.453   -5.310  1.00 29.29 ?  352 GLY A O   1 
ATOM   2779 N N   . ASN A 1 353 ? 30.397  2.503   -5.859  1.00 32.79 ?  353 ASN A N   1 
ATOM   2780 C CA  . ASN A 1 353 ? 29.352  2.113   -6.803  1.00 31.49 ?  353 ASN A CA  1 
ATOM   2781 C C   . ASN A 1 353 ? 27.967  2.205   -6.181  1.00 30.26 ?  353 ASN A C   1 
ATOM   2782 O O   . ASN A 1 353 ? 27.016  2.654   -6.832  1.00 31.03 ?  353 ASN A O   1 
ATOM   2783 C CB  . ASN A 1 353 ? 29.613  0.696   -7.300  1.00 35.16 ?  353 ASN A CB  1 
ATOM   2784 C CG  . ASN A 1 353 ? 30.917  0.584   -8.038  1.00 37.91 ?  353 ASN A CG  1 
ATOM   2785 O OD1 . ASN A 1 353 ? 31.989  0.712   -7.447  1.00 38.33 ?  353 ASN A OD1 1 
ATOM   2786 N ND2 . ASN A 1 353 ? 30.838  0.364   -9.344  1.00 38.18 ?  353 ASN A ND2 1 
ATOM   2787 N N   . GLY A 1 354 ? 27.840  1.804   -4.917  1.00 32.29 ?  354 GLY A N   1 
ATOM   2788 C CA  . GLY A 1 354 ? 26.535  1.741   -4.288  1.00 33.16 ?  354 GLY A CA  1 
ATOM   2789 C C   . GLY A 1 354 ? 25.903  3.088   -4.034  1.00 30.35 ?  354 GLY A C   1 
ATOM   2790 O O   . GLY A 1 354 ? 24.714  3.145   -3.717  1.00 29.04 ?  354 GLY A O   1 
ATOM   2791 N N   . TYR A 1 355 ? 26.691  4.158   -4.130  1.00 26.79 ?  355 TYR A N   1 
ATOM   2792 C CA  . TYR A 1 355 ? 26.175  5.532   -3.915  1.00 26.82 ?  355 TYR A CA  1 
ATOM   2793 C C   . TYR A 1 355 ? 25.697  6.036   -5.262  1.00 28.87 ?  355 TYR A C   1 
ATOM   2794 O O   . TYR A 1 355 ? 25.176  7.143   -5.339  1.00 27.63 ?  355 TYR A O   1 
ATOM   2795 C CB  . TYR A 1 355 ? 27.280  6.392   -3.306  1.00 28.10 ?  355 TYR A CB  1 
ATOM   2796 C CG  . TYR A 1 355 ? 27.861  5.782   -2.062  1.00 27.09 ?  355 TYR A CG  1 
ATOM   2797 C CD1 . TYR A 1 355 ? 27.137  5.753   -0.889  1.00 32.19 ?  355 TYR A CD1 1 
ATOM   2798 C CD2 . TYR A 1 355 ? 29.113  5.201   -2.066  1.00 29.41 ?  355 TYR A CD2 1 
ATOM   2799 C CE1 . TYR A 1 355 ? 27.653  5.190   0.261   1.00 27.68 ?  355 TYR A CE1 1 
ATOM   2800 C CE2 . TYR A 1 355 ? 29.644  4.625   -0.929  1.00 28.88 ?  355 TYR A CE2 1 
ATOM   2801 C CZ  . TYR A 1 355 ? 28.906  4.612   0.237   1.00 30.17 ?  355 TYR A CZ  1 
ATOM   2802 O OH  . TYR A 1 355 ? 29.420  4.042   1.358   1.00 27.79 ?  355 TYR A OH  1 
ATOM   2803 N N   . ARG A 1 356 ? 25.912  5.213   -6.275  1.00 28.33 ?  356 ARG A N   1 
ATOM   2804 C CA  . ARG A 1 356 ? 25.524  5.537   -7.657  1.00 29.72 ?  356 ARG A CA  1 
ATOM   2805 C C   . ARG A 1 356 ? 26.181  6.846   -8.121  1.00 30.63 ?  356 ARG A C   1 
ATOM   2806 O O   . ARG A 1 356 ? 27.307  7.102   -7.733  1.00 29.91 ?  356 ARG A O   1 
ATOM   2807 C CB  . ARG A 1 356 ? 23.999  5.586   -7.792  1.00 29.05 ?  356 ARG A CB  1 
ATOM   2808 C CG  . ARG A 1 356 ? 23.320  4.250   -7.520  1.00 28.68 ?  356 ARG A CG  1 
ATOM   2809 C CD  . ARG A 1 356 ? 21.805  4.256   -7.611  1.00 28.65 ?  356 ARG A CD  1 
ATOM   2810 N NE  . ARG A 1 356 ? 21.223  3.042   -7.058  1.00 25.62 ?  356 ARG A NE  1 
ATOM   2811 C CZ  . ARG A 1 356 ? 19.925  2.774   -7.002  1.00 25.98 ?  356 ARG A CZ  1 
ATOM   2812 N NH1 . ARG A 1 356 ? 19.044  3.641   -7.461  1.00 29.62 1  356 ARG A NH1 1 
ATOM   2813 N NH2 . ARG A 1 356 ? 19.506  1.640   -6.473  1.00 28.36 ?  356 ARG A NH2 1 
ATOM   2814 N N   . GLY A 1 357 ? 25.489  7.640   -8.936  1.00 29.55 ?  357 GLY A N   1 
ATOM   2815 C CA  . GLY A 1 357 ? 26.139  8.822   -9.533  1.00 31.87 ?  357 GLY A CA  1 
ATOM   2816 C C   . GLY A 1 357 ? 27.410  8.377   -10.220 1.00 32.34 ?  357 GLY A C   1 
ATOM   2817 O O   . GLY A 1 357 ? 27.354  7.379   -10.926 1.00 35.16 ?  357 GLY A O   1 
ATOM   2818 N N   . ASN A 1 358 ? 28.515  9.082   -10.010 1.00 35.88 ?  358 ASN A N   1 
ATOM   2819 C CA  . ASN A 1 358 ? 29.806  8.650   -10.536 1.00 37.51 ?  358 ASN A CA  1 
ATOM   2820 C C   . ASN A 1 358 ? 30.603  7.836   -9.522  1.00 37.41 ?  358 ASN A C   1 
ATOM   2821 O O   . ASN A 1 358 ? 31.837  7.885   -9.528  1.00 35.49 ?  358 ASN A O   1 
ATOM   2822 C CB  . ASN A 1 358 ? 30.619  9.861   -10.996 1.00 39.67 ?  358 ASN A CB  1 
ATOM   2823 C CG  . ASN A 1 358 ? 30.772  10.906  -9.907  1.00 40.39 ?  358 ASN A CG  1 
ATOM   2824 O OD1 . ASN A 1 358 ? 29.986  10.953  -8.960  1.00 39.28 ?  358 ASN A OD1 1 
ATOM   2825 N ND2 . ASN A 1 358 ? 31.778  11.762  -10.045 1.00 44.09 ?  358 ASN A ND2 1 
ATOM   2826 N N   . GLY A 1 359 ? 29.932  7.119   -8.637  1.00 38.00 ?  359 GLY A N   1 
ATOM   2827 C CA  . GLY A 1 359 ? 30.649  6.418   -7.561  1.00 32.23 ?  359 GLY A CA  1 
ATOM   2828 C C   . GLY A 1 359 ? 31.566  5.313   -8.033  1.00 32.63 ?  359 GLY A C   1 
ATOM   2829 O O   . GLY A 1 359 ? 32.458  4.956   -7.288  1.00 29.66 ?  359 GLY A O   1 
ATOM   2830 N N   . HIS A 1 360 ? 31.413  4.861   -9.278  1.00 36.16 ?  360 HIS A N   1 
ATOM   2831 C CA  . HIS A 1 360 ? 32.334  3.828   -9.810  1.00 34.31 ?  360 HIS A CA  1 
ATOM   2832 C C   . HIS A 1 360 ? 33.773  4.356   -9.840  1.00 32.59 ?  360 HIS A C   1 
ATOM   2833 O O   . HIS A 1 360 ? 34.681  3.538   -9.885  1.00 36.25 ?  360 HIS A O   1 
ATOM   2834 C CB  . HIS A 1 360 ? 31.853  3.316   -11.168 1.00 36.06 ?  360 HIS A CB  1 
ATOM   2835 C CG  . HIS A 1 360 ? 31.791  4.344   -12.241 1.00 39.64 ?  360 HIS A CG  1 
ATOM   2836 N ND1 . HIS A 1 360 ? 30.790  5.282   -12.304 1.00 42.51 ?  360 HIS A ND1 1 
ATOM   2837 C CD2 . HIS A 1 360 ? 32.583  4.561   -13.310 1.00 41.28 ?  360 HIS A CD2 1 
ATOM   2838 C CE1 . HIS A 1 360 ? 30.976  6.051   -13.353 1.00 42.03 ?  360 HIS A CE1 1 
ATOM   2839 N NE2 . HIS A 1 360 ? 32.069  5.629   -13.984 1.00 42.37 ?  360 HIS A NE2 1 
ATOM   2840 N N   . GLU A 1 361 ? 33.947  5.675   -9.830  1.00 31.11 ?  361 GLU A N   1 
ATOM   2841 C CA  . GLU A 1 361 ? 35.295  6.298   -9.866  1.00 37.93 ?  361 GLU A CA  1 
ATOM   2842 C C   . GLU A 1 361 ? 35.726  6.751   -8.462  1.00 35.08 ?  361 GLU A C   1 
ATOM   2843 O O   . GLU A 1 361 ? 36.679  7.528   -8.387  1.00 31.71 ?  361 GLU A O   1 
ATOM   2844 C CB  . GLU A 1 361 ? 35.282  7.524   -10.778 1.00 38.72 ?  361 GLU A CB  1 
ATOM   2845 C CG  . GLU A 1 361 ? 34.229  7.498   -11.863 1.00 42.09 ?  361 GLU A CG  1 
ATOM   2846 C CD  . GLU A 1 361 ? 34.323  8.653   -12.843 1.00 49.24 ?  361 GLU A CD  1 
ATOM   2847 O OE1 . GLU A 1 361 ? 34.789  8.423   -13.964 1.00 56.01 ?  361 GLU A OE1 1 
ATOM   2848 O OE2 . GLU A 1 361 ? 33.932  9.774   -12.479 1.00 45.74 -1 361 GLU A OE2 1 
ATOM   2849 N N   . PHE A 1 362 ? 35.082  6.243   -7.400  1.00 33.08 ?  362 PHE A N   1 
ATOM   2850 C CA  . PHE A 1 362 ? 35.417  6.743   -6.072  1.00 34.96 ?  362 PHE A CA  1 
ATOM   2851 C C   . PHE A 1 362 ? 35.439  5.617   -5.047  1.00 36.40 ?  362 PHE A C   1 
ATOM   2852 O O   . PHE A 1 362 ? 34.724  4.622   -5.182  1.00 33.98 ?  362 PHE A O   1 
ATOM   2853 C CB  . PHE A 1 362 ? 34.408  7.802   -5.617  1.00 36.15 ?  362 PHE A CB  1 
ATOM   2854 C CG  . PHE A 1 362 ? 34.560  9.125   -6.301  1.00 37.30 ?  362 PHE A CG  1 
ATOM   2855 C CD1 . PHE A 1 362 ? 33.880  9.397   -7.478  1.00 32.95 ?  362 PHE A CD1 1 
ATOM   2856 C CD2 . PHE A 1 362 ? 35.379  10.111  -5.755  1.00 35.99 ?  362 PHE A CD2 1 
ATOM   2857 C CE1 . PHE A 1 362 ? 34.022  10.620  -8.106  1.00 38.70 ?  362 PHE A CE1 1 
ATOM   2858 C CE2 . PHE A 1 362 ? 35.520  11.335  -6.373  1.00 37.00 ?  362 PHE A CE2 1 
ATOM   2859 C CZ  . PHE A 1 362 ? 34.842  11.595  -7.548  1.00 40.22 ?  362 PHE A CZ  1 
ATOM   2860 N N   . VAL A 1 363 ? 36.251  5.798   -4.000  1.00 31.89 ?  363 VAL A N   1 
ATOM   2861 C CA  . VAL A 1 363 ? 36.176  4.977   -2.799  1.00 33.91 ?  363 VAL A CA  1 
ATOM   2862 C C   . VAL A 1 363 ? 35.884  5.893   -1.615  1.00 33.07 ?  363 VAL A C   1 
ATOM   2863 O O   . VAL A 1 363 ? 36.148  7.097   -1.650  1.00 33.09 ?  363 VAL A O   1 
ATOM   2864 C CB  . VAL A 1 363 ? 37.460  4.158   -2.537  1.00 34.63 ?  363 VAL A CB  1 
ATOM   2865 C CG1 . VAL A 1 363 ? 37.545  2.994   -3.502  1.00 34.15 ?  363 VAL A CG1 1 
ATOM   2866 C CG2 . VAL A 1 363 ? 38.700  5.034   -2.641  1.00 32.84 ?  363 VAL A CG2 1 
ATOM   2867 N N   . ARG A 1 364 ? 35.332  5.300   -0.557  1.00 35.63 ?  364 ARG A N   1 
ATOM   2868 C CA  . ARG A 1 364 ? 35.028  6.002   0.686   1.00 33.57 ?  364 ARG A CA  1 
ATOM   2869 C C   . ARG A 1 364 ? 35.787  5.315   1.814   1.00 30.78 ?  364 ARG A C   1 
ATOM   2870 O O   . ARG A 1 364 ? 35.626  4.110   2.037   1.00 27.05 ?  364 ARG A O   1 
ATOM   2871 C CB  . ARG A 1 364 ? 33.518  6.020   0.957   1.00 34.65 ?  364 ARG A CB  1 
ATOM   2872 C CG  . ARG A 1 364 ? 33.041  7.215   1.790   1.00 33.26 ?  364 ARG A CG  1 
ATOM   2873 C CD  . ARG A 1 364 ? 31.650  6.999   2.357   1.00 32.01 ?  364 ARG A CD  1 
ATOM   2874 N NE  . ARG A 1 364 ? 31.609  5.851   3.261   1.00 32.18 ?  364 ARG A NE  1 
ATOM   2875 C CZ  . ARG A 1 364 ? 30.520  5.440   3.903   1.00 35.11 ?  364 ARG A CZ  1 
ATOM   2876 N NH1 . ARG A 1 364 ? 29.371  6.080   3.737   1.00 30.46 1  364 ARG A NH1 1 
ATOM   2877 N NH2 . ARG A 1 364 ? 30.583  4.379   4.704   1.00 33.82 ?  364 ARG A NH2 1 
ATOM   2878 N N   . ILE A 1 365 ? 36.630  6.071   2.511   1.00 33.10 ?  365 ILE A N   1 
ATOM   2879 C CA  . ILE A 1 365 ? 37.508  5.522   3.535   1.00 27.20 ?  365 ILE A CA  1 
ATOM   2880 C C   . ILE A 1 365 ? 37.123  6.126   4.878   1.00 32.60 ?  365 ILE A C   1 
ATOM   2881 O O   . ILE A 1 365 ? 37.027  7.349   5.009   1.00 30.29 ?  365 ILE A O   1 
ATOM   2882 C CB  . ILE A 1 365 ? 38.984  5.797   3.196   1.00 33.59 ?  365 ILE A CB  1 
ATOM   2883 C CG1 . ILE A 1 365 ? 39.306  5.235   1.805   1.00 27.60 ?  365 ILE A CG1 1 
ATOM   2884 C CG2 . ILE A 1 365 ? 39.904  5.191   4.247   1.00 28.89 ?  365 ILE A CG2 1 
ATOM   2885 C CD1 . ILE A 1 365 ? 40.792  5.226   1.462   1.00 35.55 ?  365 ILE A CD1 1 
ATOM   2886 N N   . ASN A 1 366 ? 36.905  5.264   5.870   1.00 27.37 ?  366 ASN A N   1 
ATOM   2887 C CA  . ASN A 1 366 ? 36.525  5.669   7.223   1.00 30.93 ?  366 ASN A CA  1 
ATOM   2888 C C   . ASN A 1 366 ? 37.786  5.998   8.022   1.00 27.56 ?  366 ASN A C   1 
ATOM   2889 O O   . ASN A 1 366 ? 38.576  5.105   8.344   1.00 27.44 ?  366 ASN A O   1 
ATOM   2890 C CB  . ASN A 1 366 ? 35.722  4.540   7.878   1.00 28.67 ?  366 ASN A CB  1 
ATOM   2891 C CG  . ASN A 1 366 ? 35.208  4.896   9.271   1.00 34.92 ?  366 ASN A CG  1 
ATOM   2892 O OD1 . ASN A 1 366 ? 35.669  5.853   9.894   1.00 31.38 ?  366 ASN A OD1 1 
ATOM   2893 N ND2 . ASN A 1 366 ? 34.267  4.091   9.779   1.00 27.53 ?  366 ASN A ND2 1 
ATOM   2894 N N   . LEU A 1 367 ? 37.968  7.277   8.364   1.00 30.83 ?  367 LEU A N   1 
ATOM   2895 C CA  . LEU A 1 367 ? 39.131  7.729   9.124   1.00 28.60 ?  367 LEU A CA  1 
ATOM   2896 C C   . LEU A 1 367 ? 38.846  7.913   10.611  1.00 32.31 ?  367 LEU A C   1 
ATOM   2897 O O   . LEU A 1 367 ? 39.715  8.400   11.344  1.00 28.48 ?  367 LEU A O   1 
ATOM   2898 C CB  . LEU A 1 367 ? 39.667  9.044   8.543   1.00 31.23 ?  367 LEU A CB  1 
ATOM   2899 C CG  . LEU A 1 367 ? 40.129  8.967   7.079   1.00 30.56 ?  367 LEU A CG  1 
ATOM   2900 C CD1 . LEU A 1 367 ? 40.583  10.339  6.620   1.00 28.54 ?  367 LEU A CD1 1 
ATOM   2901 C CD2 . LEU A 1 367 ? 41.263  7.951   6.940   1.00 29.66 ?  367 LEU A CD2 1 
ATOM   2902 N N   . ALA A 1 368 ? 37.654  7.545   11.076  1.00 29.78 ?  368 ALA A N   1 
ATOM   2903 C CA  . ALA A 1 368 ? 37.338  7.619   12.501  1.00 32.99 ?  368 ALA A CA  1 
ATOM   2904 C C   . ALA A 1 368 ? 37.970  6.437   13.235  1.00 28.02 ?  368 ALA A C   1 
ATOM   2905 O O   . ALA A 1 368 ? 37.282  5.565   13.761  1.00 27.68 ?  368 ALA A O   1 
ATOM   2906 C CB  . ALA A 1 368 ? 35.827  7.645   12.707  1.00 27.98 ?  368 ALA A CB  1 
ATOM   2907 N N   . CYS A 1 369 ? 39.302  6.391   13.214  1.00 28.83 ?  369 CYS A N   1 
ATOM   2908 C CA  . CYS A 1 369 ? 40.055  5.346   13.889  1.00 26.73 ?  369 CYS A CA  1 
ATOM   2909 C C   . CYS A 1 369 ? 41.336  5.970   14.423  1.00 27.48 ?  369 CYS A C   1 
ATOM   2910 O O   . CYS A 1 369 ? 41.723  7.066   14.006  1.00 31.56 ?  369 CYS A O   1 
ATOM   2911 C CB  . CYS A 1 369 ? 40.384  4.164   12.966  1.00 33.09 ?  369 CYS A CB  1 
ATOM   2912 S SG  . CYS A 1 369 ? 41.072  4.617   11.378  1.00 33.55 ?  369 CYS A SG  1 
ATOM   2913 N N   . PRO A 1 370 ? 42.008  5.313   15.359  1.00 28.97 ?  370 PRO A N   1 
ATOM   2914 C CA  . PRO A 1 370 ? 43.299  5.820   15.834  1.00 31.14 ?  370 PRO A CA  1 
ATOM   2915 C C   . PRO A 1 370 ? 44.277  6.009   14.682  1.00 32.12 ?  370 PRO A C   1 
ATOM   2916 O O   . PRO A 1 370 ? 44.238  5.290   13.681  1.00 30.96 ?  370 PRO A O   1 
ATOM   2917 C CB  . PRO A 1 370 ? 43.763  4.727   16.800  1.00 35.47 ?  370 PRO A CB  1 
ATOM   2918 C CG  . PRO A 1 370 ? 42.470  4.061   17.253  1.00 30.30 ?  370 PRO A CG  1 
ATOM   2919 C CD  . PRO A 1 370 ? 41.618  4.065   16.031  1.00 32.08 ?  370 PRO A CD  1 
ATOM   2920 N N   . LYS A 1 371 ? 45.156  7.001   14.835  1.00 34.20 ?  371 LYS A N   1 
ATOM   2921 C CA  . LYS A 1 371 ? 46.077  7.342   13.757  1.00 35.00 ?  371 LYS A CA  1 
ATOM   2922 C C   . LYS A 1 371 ? 46.857  6.126   13.278  1.00 34.63 ?  371 LYS A C   1 
ATOM   2923 O O   . LYS A 1 371 ? 47.152  6.006   12.082  1.00 33.86 ?  371 LYS A O   1 
ATOM   2924 C CB  . LYS A 1 371 ? 47.040  8.448   14.207  1.00 36.69 ?  371 LYS A CB  1 
ATOM   2925 C CG  . LYS A 1 371 ? 47.835  9.074   13.052  1.00 35.44 ?  371 LYS A CG  1 
ATOM   2926 C CD  . LYS A 1 371 ? 48.406  10.442  13.421  1.00 41.72 ?  371 LYS A CD  1 
ATOM   2927 C CE  . LYS A 1 371 ? 49.200  11.039  12.268  1.00 48.50 ?  371 LYS A CE  1 
ATOM   2928 N NZ  . LYS A 1 371 ? 49.697  12.411  12.568  1.00 47.39 1  371 LYS A NZ  1 
ATOM   2929 N N   . GLU A 1 372 ? 47.195  5.215   14.178  1.00 34.71 ?  372 GLU A N   1 
ATOM   2930 C CA  . GLU A 1 372 ? 47.977  4.000   13.827  1.00 38.06 ?  372 GLU A CA  1 
ATOM   2931 C C   . GLU A 1 372 ? 47.235  3.134   12.807  1.00 36.61 ?  372 GLU A C   1 
ATOM   2932 O O   . GLU A 1 372 ? 47.884  2.577   11.945  1.00 37.54 ?  372 GLU A O   1 
ATOM   2933 C CB  . GLU A 1 372 ? 48.379  3.242   15.089  1.00 37.40 ?  372 GLU A CB  1 
ATOM   2934 C CG  . GLU A 1 372 ? 49.043  4.117   16.138  1.00 45.90 ?  372 GLU A CG  1 
ATOM   2935 C CD  . GLU A 1 372 ? 50.213  4.988   15.707  1.00 51.51 ?  372 GLU A CD  1 
ATOM   2936 O OE1 . GLU A 1 372 ? 51.133  4.465   15.041  1.00 47.43 ?  372 GLU A OE1 1 
ATOM   2937 O OE2 . GLU A 1 372 ? 50.222  6.184   16.073  1.00 52.63 -1 372 GLU A OE2 1 
ATOM   2938 N N   . LEU A 1 373 ? 45.911  3.072   12.910  1.00 33.41 ?  373 LEU A N   1 
ATOM   2939 C CA  . LEU A 1 373 ? 45.157  2.331   11.906  1.00 35.14 ?  373 LEU A CA  1 
ATOM   2940 C C   . LEU A 1 373 ? 45.062  3.102   10.591  1.00 37.58 ?  373 LEU A C   1 
ATOM   2941 O O   . LEU A 1 373 ? 44.932  2.486   9.528   1.00 34.38 ?  373 LEU A O   1 
ATOM   2942 C CB  . LEU A 1 373 ? 43.758  1.973   12.440  1.00 35.18 ?  373 LEU A CB  1 
ATOM   2943 C CG  . LEU A 1 373 ? 43.682  0.727   13.349  1.00 37.34 ?  373 LEU A CG  1 
ATOM   2944 C CD1 . LEU A 1 373 ? 44.455  0.913   14.661  1.00 33.87 ?  373 LEU A CD1 1 
ATOM   2945 C CD2 . LEU A 1 373 ? 42.234  0.308   13.635  1.00 37.55 ?  373 LEU A CD2 1 
ATOM   2946 N N   . VAL A 1 374 ? 45.129  4.438   10.632  1.00 33.18 ?  374 VAL A N   1 
ATOM   2947 C CA  . VAL A 1 374 ? 45.223  5.195   9.386   1.00 31.63 ?  374 VAL A CA  1 
ATOM   2948 C C   . VAL A 1 374 ? 46.561  4.927   8.706   1.00 35.35 ?  374 VAL A C   1 
ATOM   2949 O O   . VAL A 1 374 ? 46.626  4.750   7.483   1.00 35.10 ?  374 VAL A O   1 
ATOM   2950 C CB  . VAL A 1 374 ? 45.011  6.700   9.637   1.00 32.25 ?  374 VAL A CB  1 
ATOM   2951 C CG1 . VAL A 1 374 ? 45.095  7.479   8.319   1.00 33.73 ?  374 VAL A CG1 1 
ATOM   2952 C CG2 . VAL A 1 374 ? 43.670  6.950   10.308  1.00 32.15 ?  374 VAL A CG2 1 
ATOM   2953 N N   . ILE A 1 375 ? 47.644  4.899   9.485   1.00 35.13 ?  375 ILE A N   1 
ATOM   2954 C CA  . ILE A 1 375 ? 48.965  4.604   8.938   1.00 35.42 ?  375 ILE A CA  1 
ATOM   2955 C C   . ILE A 1 375 ? 48.967  3.232   8.271   1.00 40.77 ?  375 ILE A C   1 
ATOM   2956 O O   . ILE A 1 375 ? 49.413  3.077   7.128   1.00 39.71 ?  375 ILE A O   1 
ATOM   2957 C CB  . ILE A 1 375 ? 50.031  4.698   10.046  1.00 36.59 ?  375 ILE A CB  1 
ATOM   2958 C CG1 . ILE A 1 375 ? 50.194  6.154   10.498  1.00 38.35 ?  375 ILE A CG1 1 
ATOM   2959 C CG2 . ILE A 1 375 ? 51.344  4.098   9.570   1.00 34.50 ?  375 ILE A CG2 1 
ATOM   2960 C CD1 . ILE A 1 375 ? 51.166  6.351   11.649  1.00 31.17 ?  375 ILE A CD1 1 
ATOM   2961 N N   . ASP A 1 376 ? 48.461  2.220   8.981   1.00 36.13 ?  376 ASP A N   1 
ATOM   2962 C CA  . ASP A 1 376 ? 48.296  0.888   8.406   1.00 37.24 ?  376 ASP A CA  1 
ATOM   2963 C C   . ASP A 1 376 ? 47.491  0.937   7.109   1.00 40.97 ?  376 ASP A C   1 
ATOM   2964 O O   . ASP A 1 376 ? 47.958  0.497   6.051   1.00 38.88 ?  376 ASP A O   1 
ATOM   2965 C CB  . ASP A 1 376 ? 47.617  -0.016  9.436   1.00 39.77 ?  376 ASP A CB  1 
ATOM   2966 C CG  . ASP A 1 376 ? 47.775  -1.486  9.126   1.00 39.30 ?  376 ASP A CG  1 
ATOM   2967 O OD1 . ASP A 1 376 ? 48.415  -1.822  8.108   1.00 37.66 ?  376 ASP A OD1 1 
ATOM   2968 O OD2 . ASP A 1 376 ? 47.265  -2.307  9.917   1.00 38.49 -1 376 ASP A OD2 1 
ATOM   2969 N N   . GLY A 1 377 ? 46.268  1.473   7.177   1.00 36.18 ?  377 GLY A N   1 
ATOM   2970 C CA  . GLY A 1 377 ? 45.403  1.485   6.008   1.00 36.50 ?  377 GLY A CA  1 
ATOM   2971 C C   . GLY A 1 377 ? 46.003  2.233   4.832   1.00 38.27 ?  377 GLY A C   1 
ATOM   2972 O O   . GLY A 1 377 ? 45.871  1.809   3.680   1.00 37.49 ?  377 GLY A O   1 
ATOM   2973 N N   . MET A 1 378 ? 46.672  3.354   5.100   1.00 33.29 ?  378 MET A N   1 
ATOM   2974 C CA  . MET A 1 378 ? 47.299  4.092   4.007   1.00 36.78 ?  378 MET A CA  1 
ATOM   2975 C C   . MET A 1 378 ? 48.463  3.306   3.404   1.00 39.67 ?  378 MET A C   1 
ATOM   2976 O O   . MET A 1 378 ? 48.652  3.307   2.181   1.00 44.02 ?  378 MET A O   1 
ATOM   2977 C CB  . MET A 1 378 ? 47.757  5.466   4.496   1.00 37.14 ?  378 MET A CB  1 
ATOM   2978 C CG  . MET A 1 378 ? 46.611  6.441   4.722   1.00 34.84 ?  378 MET A CG  1 
ATOM   2979 S SD  . MET A 1 378 ? 45.658  6.808   3.238   1.00 40.35 ?  378 MET A SD  1 
ATOM   2980 C CE  . MET A 1 378 ? 44.009  6.324   3.737   1.00 37.49 ?  378 MET A CE  1 
ATOM   2981 N N   . GLN A 1 379 ? 49.239  2.613   4.242   1.00 38.06 ?  379 GLN A N   1 
ATOM   2982 C CA  . GLN A 1 379 ? 50.309  1.759   3.728   1.00 43.16 ?  379 GLN A CA  1 
ATOM   2983 C C   . GLN A 1 379 ? 49.758  0.619   2.875   1.00 42.13 ?  379 GLN A C   1 
ATOM   2984 O O   . GLN A 1 379 ? 50.338  0.275   1.837   1.00 41.57 ?  379 GLN A O   1 
ATOM   2985 C CB  . GLN A 1 379 ? 51.137  1.195   4.882   1.00 39.69 ?  379 GLN A CB  1 
ATOM   2986 C CG  . GLN A 1 379 ? 52.155  2.161   5.461   1.00 46.03 ?  379 GLN A CG  1 
ATOM   2987 C CD  . GLN A 1 379 ? 52.701  1.690   6.798   1.00 48.73 ?  379 GLN A CD  1 
ATOM   2988 O OE1 . GLN A 1 379 ? 52.374  0.597   7.263   1.00 52.85 ?  379 GLN A OE1 1 
ATOM   2989 N NE2 . GLN A 1 379 ? 53.534  2.516   7.424   1.00 50.74 ?  379 GLN A NE2 1 
ATOM   2990 N N   . ARG A 1 380 ? 48.646  0.011   3.306   1.00 40.58 ?  380 ARG A N   1 
ATOM   2991 C CA  . ARG A 1 380 ? 48.047  -1.084  2.546   1.00 37.36 ?  380 ARG A CA  1 
ATOM   2992 C C   . ARG A 1 380 ? 47.503  -0.598  1.208   1.00 42.71 ?  380 ARG A C   1 
ATOM   2993 O O   . ARG A 1 380 ? 47.655  -1.279  0.186   1.00 43.53 ?  380 ARG A O   1 
ATOM   2994 C CB  . ARG A 1 380 ? 46.931  -1.741  3.360   1.00 36.16 ?  380 ARG A CB  1 
ATOM   2995 C CG  . ARG A 1 380 ? 47.378  -2.305  4.691   1.00 38.04 ?  380 ARG A CG  1 
ATOM   2996 C CD  . ARG A 1 380 ? 46.278  -3.147  5.300   1.00 37.90 ?  380 ARG A CD  1 
ATOM   2997 N NE  . ARG A 1 380 ? 46.587  -3.531  6.668   1.00 33.86 ?  380 ARG A NE  1 
ATOM   2998 C CZ  . ARG A 1 380 ? 46.146  -4.647  7.236   1.00 40.25 ?  380 ARG A CZ  1 
ATOM   2999 N NH1 . ARG A 1 380 ? 45.382  -5.483  6.538   1.00 35.05 1  380 ARG A NH1 1 
ATOM   3000 N NH2 . ARG A 1 380 ? 46.473  -4.930  8.495   1.00 37.79 ?  380 ARG A NH2 1 
ATOM   3001 N N   . LEU A 1 381 ? 46.954  0.603   1.168   1.00 38.71 ?  381 LEU A N   1 
ATOM   3002 C CA  . LEU A 1 381 ? 46.396  1.138   -0.100  1.00 43.00 ?  381 LEU A CA  1 
ATOM   3003 C C   . LEU A 1 381 ? 47.545  1.263   -1.097  1.00 45.00 ?  381 LEU A C   1 
ATOM   3004 O O   . LEU A 1 381 ? 47.400  0.831   -2.226  1.00 44.15 ?  381 LEU A O   1 
ATOM   3005 C CB  . LEU A 1 381 ? 45.742  2.496   0.157   1.00 40.26 ?  381 LEU A CB  1 
ATOM   3006 C CG  . LEU A 1 381 ? 44.863  3.065   -0.956  1.00 45.56 ?  381 LEU A CG  1 
ATOM   3007 C CD1 . LEU A 1 381 ? 43.788  3.954   -0.362  1.00 43.53 ?  381 LEU A CD1 1 
ATOM   3008 C CD2 . LEU A 1 381 ? 45.678  3.873   -1.953  1.00 49.06 ?  381 LEU A CD2 1 
ATOM   3009 N N   . LYS A 1 382 ? 48.650  1.821   -0.640  1.00 45.96 ?  382 LYS A N   1 
ATOM   3010 C CA  . LYS A 1 382 ? 49.799  2.065   -1.536  1.00 47.34 ?  382 LYS A CA  1 
ATOM   3011 C C   . LYS A 1 382 ? 50.372  0.736   -2.007  1.00 47.39 ?  382 LYS A C   1 
ATOM   3012 O O   . LYS A 1 382 ? 50.687  0.634   -3.190  1.00 44.62 ?  382 LYS A O   1 
ATOM   3013 C CB  . LYS A 1 382 ? 50.817  2.919   -0.783  1.00 47.86 ?  382 LYS A CB  1 
ATOM   3014 C CG  . LYS A 1 382 ? 51.896  3.541   -1.655  1.00 54.08 ?  382 LYS A CG  1 
ATOM   3015 C CD  . LYS A 1 382 ? 53.277  3.390   -1.084  1.00 57.14 ?  382 LYS A CD  1 
ATOM   3016 C CE  . LYS A 1 382 ? 54.358  3.835   -2.044  1.00 59.53 ?  382 LYS A CE  1 
ATOM   3017 N NZ  . LYS A 1 382 ? 55.693  3.401   -1.577  1.00 58.82 1  382 LYS A NZ  1 
ATOM   3018 N N   . GLN A 1 383 ? 50.471  -0.228  -1.094  1.00 45.20 ?  383 GLN A N   1 
ATOM   3019 C CA  . GLN A 1 383 ? 51.027  -1.553  -1.443  1.00 47.48 ?  383 GLN A CA  1 
ATOM   3020 C C   . GLN A 1 383 ? 50.145  -2.158  -2.528  1.00 48.51 ?  383 GLN A C   1 
ATOM   3021 O O   . GLN A 1 383 ? 50.690  -2.757  -3.465  1.00 47.54 ?  383 GLN A O   1 
ATOM   3022 C CB  . GLN A 1 383 ? 51.178  -2.449  -0.214  1.00 48.29 ?  383 GLN A CB  1 
ATOM   3023 C CG  . GLN A 1 383 ? 52.328  -3.440  -0.310  1.00 52.04 ?  383 GLN A CG  1 
ATOM   3024 C CD  . GLN A 1 383 ? 53.656  -2.791  -0.617  1.00 54.22 ?  383 GLN A CD  1 
ATOM   3025 O OE1 . GLN A 1 383 ? 54.075  -1.842  0.041   1.00 55.06 ?  383 GLN A OE1 1 
ATOM   3026 N NE2 . GLN A 1 383 ? 54.339  -3.311  -1.624  1.00 51.47 ?  383 GLN A NE2 1 
ATOM   3027 N N   . GLY A 1 384 ? 48.842  -1.944  -2.412  1.00 42.43 ?  384 GLY A N   1 
ATOM   3028 C CA  . GLY A 1 384 ? 47.934  -2.490  -3.404  1.00 45.15 ?  384 GLY A CA  1 
ATOM   3029 C C   . GLY A 1 384 ? 47.999  -1.761  -4.727  1.00 48.34 ?  384 GLY A C   1 
ATOM   3030 O O   . GLY A 1 384 ? 47.831  -2.374  -5.787  1.00 49.62 ?  384 GLY A O   1 
ATOM   3031 N N   . VAL A 1 385 ? 48.246  -0.450  -4.691  1.00 47.30 ?  385 VAL A N   1 
ATOM   3032 C CA  . VAL A 1 385 ? 48.408  0.305   -5.928  1.00 49.27 ?  385 VAL A CA  1 
ATOM   3033 C C   . VAL A 1 385 ? 49.718  -0.069  -6.607  1.00 48.45 ?  385 VAL A C   1 
ATOM   3034 O O   . VAL A 1 385 ? 49.800  -0.135  -7.841  1.00 50.91 ?  385 VAL A O   1 
ATOM   3035 C CB  . VAL A 1 385 ? 48.322  1.818   -5.646  1.00 48.91 ?  385 VAL A CB  1 
ATOM   3036 C CG1 . VAL A 1 385 ? 48.977  2.626   -6.769  1.00 50.53 ?  385 VAL A CG1 1 
ATOM   3037 C CG2 . VAL A 1 385 ? 46.874  2.246   -5.459  1.00 44.32 ?  385 VAL A CG2 1 
ATOM   3038 N N   . LEU A 1 386 ? 50.756  -0.344  -5.817  1.00 45.90 ?  386 LEU A N   1 
ATOM   3039 C CA  . LEU A 1 386 ? 52.059  -0.637  -6.399  1.00 47.93 ?  386 LEU A CA  1 
ATOM   3040 C C   . LEU A 1 386 ? 52.071  -1.998  -7.084  1.00 51.06 ?  386 LEU A C   1 
ATOM   3041 O O   . LEU A 1 386 ? 52.699  -2.159  -8.137  1.00 52.16 ?  386 LEU A O   1 
ATOM   3042 C CB  . LEU A 1 386 ? 53.141  -0.562  -5.326  1.00 49.24 ?  386 LEU A CB  1 
ATOM   3043 C CG  . LEU A 1 386 ? 54.119  0.602   -5.501  1.00 51.50 ?  386 LEU A CG  1 
ATOM   3044 C CD1 . LEU A 1 386 ? 55.070  0.678   -4.323  1.00 50.65 ?  386 LEU A CD1 1 
ATOM   3045 C CD2 . LEU A 1 386 ? 54.887  0.449   -6.809  1.00 53.41 ?  386 LEU A CD2 1 
ATOM   3046 N N   . ASN A 1 387 ? 51.385  -2.990  -6.511  1.00 49.89 ?  387 ASN A N   1 
ATOM   3047 C CA  . ASN A 1 387 ? 51.391  -4.313  -7.127  1.00 51.28 ?  387 ASN A CA  1 
ATOM   3048 C C   . ASN A 1 387 ? 50.593  -4.335  -8.423  1.00 49.97 ?  387 ASN A C   1 
ATOM   3049 O O   . ASN A 1 387 ? 50.846  -5.183  -9.286  1.00 51.12 ?  387 ASN A O   1 
ATOM   3050 C CB  . ASN A 1 387 ? 50.856  -5.368  -6.157  1.00 51.14 ?  387 ASN A CB  1 
ATOM   3051 C CG  . ASN A 1 387 ? 50.958  -6.778  -6.720  1.00 55.36 ?  387 ASN A CG  1 
ATOM   3052 O OD1 . ASN A 1 387 ? 51.992  -7.430  -6.603  1.00 56.63 ?  387 ASN A OD1 1 
ATOM   3053 N ND2 . ASN A 1 387 ? 49.875  -7.258  -7.321  1.00 60.85 ?  387 ASN A ND2 1 
ATOM   3054 N N   . LEU A 1 388 ? 49.629  -3.425  -8.585  1.00 48.19 ?  388 LEU A N   1 
ATOM   3055 C CA  . LEU A 1 388 ? 48.979  -3.290  -9.882  1.00 48.35 ?  388 LEU A CA  1 
ATOM   3056 C C   . LEU A 1 388 ? 49.971  -2.889  -10.962 1.00 50.40 ?  388 LEU A C   1 
ATOM   3057 O O   . LEU A 1 388 ? 49.726  -3.141  -12.145 1.00 47.53 ?  388 LEU A O   1 
ATOM   3058 C CB  . LEU A 1 388 ? 47.846  -2.265  -9.809  1.00 48.15 ?  388 LEU A CB  1 
ATOM   3059 C CG  . LEU A 1 388 ? 46.558  -2.715  -9.123  1.00 43.75 ?  388 LEU A CG  1 
ATOM   3060 C CD1 . LEU A 1 388 ? 45.618  -1.535  -8.922  1.00 41.52 ?  388 LEU A CD1 1 
ATOM   3061 C CD2 . LEU A 1 388 ? 45.885  -3.822  -9.937  1.00 45.29 ?  388 LEU A CD2 1 
ATOM   3062 N N   . ASN A 1 389 ? 51.087  -2.282  -10.574 1.00 53.89 ?  389 ASN A N   1 
ATOM   3063 C CA  . ASN A 1 389 ? 52.124  -1.856  -11.498 1.00 52.23 ?  389 ASN A CA  1 
ATOM   3064 C C   . ASN A 1 389 ? 53.274  -2.850  -11.585 1.00 51.97 ?  389 ASN A C   1 
ATOM   3065 O O   . ASN A 1 389 ? 54.241  -2.590  -12.307 1.00 55.57 ?  389 ASN A O   1 
ATOM   3066 C CB  . ASN A 1 389 ? 52.657  -0.483  -11.083 1.00 52.85 ?  389 ASN A CB  1 
ATOM   3067 C CG  . ASN A 1 389 ? 51.558  0.568   -10.977 1.00 57.00 ?  389 ASN A CG  1 
ATOM   3068 O OD1 . ASN A 1 389 ? 50.410  0.309   -11.337 1.00 57.48 ?  389 ASN A OD1 1 
ATOM   3069 N ND2 . ASN A 1 389 ? 51.900  1.751   -10.466 1.00 55.75 ?  389 ASN A ND2 1 
ATOM   3070 N N   . ASN A 1 390 ? 53.189  -3.976  -10.875 1.00 51.66 ?  390 ASN A N   1 
ATOM   3071 C CA  . ASN A 1 390 ? 54.240  -4.993  -10.882 1.00 51.30 ?  390 ASN A CA  1 
ATOM   3072 C C   . ASN A 1 390 ? 53.733  -6.424  -11.017 1.00 49.91 ?  390 ASN A C   1 
ATOM   3073 O O   . ASN A 1 390 ? 52.606  -6.767  -10.669 1.00 52.15 ?  390 ASN A O   1 
ATOM   3074 C CB  . ASN A 1 390 ? 55.069  -4.892  -9.609  1.00 54.83 ?  390 ASN A CB  1 
ATOM   3075 C CG  . ASN A 1 390 ? 56.100  -3.797  -9.679  1.00 57.85 ?  390 ASN A CG  1 
ATOM   3076 O OD1 . ASN A 1 390 ? 56.353  -3.234  -10.743 1.00 55.28 ?  390 ASN A OD1 1 
ATOM   3077 N ND2 . ASN A 1 390 ? 56.711  -3.490  -8.542  1.00 55.64 ?  390 ASN A ND2 1 
ATOM   3078 O OXT . ASN A 1 390 ? 54.472  -7.301  -11.470 1.00 60.16 -1 390 ASN A OXT 1 
ATOM   3079 N N   . GLU B 1 3   ? 14.002  -19.978 51.526  1.00 76.53 ?  3   GLU B N   1 
ATOM   3080 C CA  . GLU B 1 3   ? 14.564  -18.676 51.184  1.00 72.82 ?  3   GLU B CA  1 
ATOM   3081 C C   . GLU B 1 3   ? 14.673  -18.491 49.675  1.00 69.39 ?  3   GLU B C   1 
ATOM   3082 O O   . GLU B 1 3   ? 14.939  -19.438 48.928  1.00 67.51 ?  3   GLU B O   1 
ATOM   3083 C CB  . GLU B 1 3   ? 15.938  -18.502 51.834  1.00 73.24 ?  3   GLU B CB  1 
ATOM   3084 C CG  . GLU B 1 3   ? 16.261  -17.064 52.224  1.00 67.22 ?  3   GLU B CG  1 
ATOM   3085 C CD  . GLU B 1 3   ? 17.078  -16.987 53.497  1.00 65.73 ?  3   GLU B CD  1 
ATOM   3086 O OE1 . GLU B 1 3   ? 18.266  -17.377 53.468  1.00 63.50 ?  3   GLU B OE1 1 
ATOM   3087 O OE2 . GLU B 1 3   ? 16.528  -16.548 54.530  1.00 65.17 -1 3   GLU B OE2 1 
ATOM   3088 N N   . LYS B 1 4   ? 14.364  -17.269 49.213  1.00 67.38 ?  4   LYS B N   1 
ATOM   3089 C CA  . LYS B 1 4   ? 14.438  -16.925 47.769  1.00 62.66 ?  4   LYS B CA  1 
ATOM   3090 C C   . LYS B 1 4   ? 15.849  -16.432 47.435  1.00 59.78 ?  4   LYS B C   1 
ATOM   3091 O O   . LYS B 1 4   ? 16.384  -15.628 48.204  1.00 60.80 ?  4   LYS B O   1 
ATOM   3092 C CB  . LYS B 1 4   ? 13.481  -15.767 47.452  1.00 60.56 ?  4   LYS B CB  1 
ATOM   3093 C CG  . LYS B 1 4   ? 12.000  -16.129 47.430  1.00 62.76 ?  4   LYS B CG  1 
ATOM   3094 C CD  . LYS B 1 4   ? 11.081  -14.955 47.149  1.00 58.11 ?  4   LYS B CD  1 
ATOM   3095 C CE  . LYS B 1 4   ? 10.934  -14.001 48.317  1.00 57.31 ?  4   LYS B CE  1 
ATOM   3096 N NZ  . LYS B 1 4   ? 9.641   -13.276 48.289  1.00 57.82 1  4   LYS B NZ  1 
ATOM   3097 N N   . GLN B 1 5   ? 16.402  -16.858 46.298  1.00 53.62 ?  5   GLN B N   1 
ATOM   3098 C CA  . GLN B 1 5   ? 17.804  -16.490 45.969  1.00 51.74 ?  5   GLN B CA  1 
ATOM   3099 C C   . GLN B 1 5   ? 17.769  -15.069 45.417  1.00 52.09 ?  5   GLN B C   1 
ATOM   3100 O O   . GLN B 1 5   ? 18.772  -14.348 45.520  1.00 52.78 ?  5   GLN B O   1 
ATOM   3101 C CB  . GLN B 1 5   ? 18.331  -17.495 44.945  1.00 48.62 ?  5   GLN B CB  1 
ATOM   3102 C CG  . GLN B 1 5   ? 19.751  -17.251 44.455  1.00 49.93 ?  5   GLN B CG  1 
ATOM   3103 C CD  . GLN B 1 5   ? 20.127  -18.221 43.361  1.00 53.91 ?  5   GLN B CD  1 
ATOM   3104 O OE1 . GLN B 1 5   ? 19.604  -19.330 43.281  1.00 56.80 ?  5   GLN B OE1 1 
ATOM   3105 N NE2 . GLN B 1 5   ? 21.044  -17.808 42.502  1.00 53.76 ?  5   GLN B NE2 1 
ATOM   3106 N N   . TYR B 1 6   ? 16.597  -14.682 44.945  1.00 48.85 ?  6   TYR B N   1 
ATOM   3107 C CA  . TYR B 1 6   ? 16.470  -13.392 44.257  1.00 41.67 ?  6   TYR B CA  1 
ATOM   3108 C C   . TYR B 1 6   ? 15.573  -12.455 45.063  1.00 38.54 ?  6   TYR B C   1 
ATOM   3109 O O   . TYR B 1 6   ? 14.862  -12.921 45.940  1.00 39.82 ?  6   TYR B O   1 
ATOM   3110 C CB  . TYR B 1 6   ? 15.956  -13.703 42.851  1.00 31.94 ?  6   TYR B CB  1 
ATOM   3111 C CG  . TYR B 1 6   ? 16.742  -14.710 42.055  1.00 32.51 ?  6   TYR B CG  1 
ATOM   3112 C CD1 . TYR B 1 6   ? 17.954  -14.373 41.487  1.00 34.18 ?  6   TYR B CD1 1 
ATOM   3113 C CD2 . TYR B 1 6   ? 16.258  -15.985 41.829  1.00 31.81 ?  6   TYR B CD2 1 
ATOM   3114 C CE1 . TYR B 1 6   ? 18.674  -15.275 40.726  1.00 33.50 ?  6   TYR B CE1 1 
ATOM   3115 C CE2 . TYR B 1 6   ? 16.967  -16.902 41.077  1.00 34.05 ?  6   TYR B CE2 1 
ATOM   3116 C CZ  . TYR B 1 6   ? 18.176  -16.543 40.514  1.00 33.25 ?  6   TYR B CZ  1 
ATOM   3117 O OH  . TYR B 1 6   ? 18.878  -17.432 39.765  1.00 27.46 ?  6   TYR B OH  1 
ATOM   3118 N N   . ASP B 1 7   ? 15.575  -11.188 44.704  1.00 34.47 ?  7   ASP B N   1 
ATOM   3119 C CA  . ASP B 1 7   ? 14.824  -10.152 45.412  1.00 31.86 ?  7   ASP B CA  1 
ATOM   3120 C C   . ASP B 1 7   ? 13.524  -9.886  44.667  1.00 34.85 ?  7   ASP B C   1 
ATOM   3121 O O   . ASP B 1 7   ? 13.535  -9.348  43.553  1.00 30.87 ?  7   ASP B O   1 
ATOM   3122 C CB  . ASP B 1 7   ? 15.647  -8.869  45.545  1.00 34.11 ?  7   ASP B CB  1 
ATOM   3123 C CG  . ASP B 1 7   ? 14.880  -7.710  46.214  1.00 38.32 ?  7   ASP B CG  1 
ATOM   3124 O OD1 . ASP B 1 7   ? 13.634  -7.724  46.334  1.00 40.99 ?  7   ASP B OD1 1 
ATOM   3125 O OD2 . ASP B 1 7   ? 15.554  -6.747  46.636  1.00 47.76 -1 7   ASP B OD2 1 
ATOM   3126 N N   . PHE B 1 8   ? 12.406  -10.246 45.296  1.00 30.78 ?  8   PHE B N   1 
ATOM   3127 C CA  . PHE B 1 8   ? 11.080  -9.871  44.817  1.00 27.28 ?  8   PHE B CA  1 
ATOM   3128 C C   . PHE B 1 8   ? 10.381  -8.964  45.819  1.00 29.78 ?  8   PHE B C   1 
ATOM   3129 O O   . PHE B 1 8   ? 9.150   -8.893  45.836  1.00 30.62 ?  8   PHE B O   1 
ATOM   3130 C CB  . PHE B 1 8   ? 10.239  -11.119 44.531  1.00 26.31 ?  8   PHE B CB  1 
ATOM   3131 C CG  . PHE B 1 8   ? 10.813  -11.995 43.463  1.00 27.34 ?  8   PHE B CG  1 
ATOM   3132 C CD1 . PHE B 1 8   ? 10.548  -11.743 42.117  1.00 28.06 ?  8   PHE B CD1 1 
ATOM   3133 C CD2 . PHE B 1 8   ? 11.624  -13.076 43.790  1.00 30.53 ?  8   PHE B CD2 1 
ATOM   3134 C CE1 . PHE B 1 8   ? 11.087  -12.554 41.128  1.00 25.19 ?  8   PHE B CE1 1 
ATOM   3135 C CE2 . PHE B 1 8   ? 12.151  -13.895 42.802  1.00 28.55 ?  8   PHE B CE2 1 
ATOM   3136 C CZ  . PHE B 1 8   ? 11.885  -13.630 41.466  1.00 28.35 ?  8   PHE B CZ  1 
ATOM   3137 N N   . THR B 1 9   ? 11.152  -8.272  46.659  1.00 28.59 ?  9   THR B N   1 
ATOM   3138 C CA  . THR B 1 9   ? 10.618  -7.415  47.712  1.00 32.55 ?  9   THR B CA  1 
ATOM   3139 C C   . THR B 1 9   ? 10.815  -5.937  47.442  1.00 33.32 ?  9   THR B C   1 
ATOM   3140 O O   . THR B 1 9   ? 9.976   -5.131  47.836  1.00 30.28 ?  9   THR B O   1 
ATOM   3141 C CB  . THR B 1 9   ? 11.268  -7.757  49.065  1.00 33.86 ?  9   THR B CB  1 
ATOM   3142 O OG1 . THR B 1 9   ? 12.682  -7.529  48.994  1.00 39.14 ?  9   THR B OG1 1 
ATOM   3143 C CG2 . THR B 1 9   ? 11.018  -9.201  49.418  1.00 34.44 ?  9   THR B CG2 1 
ATOM   3144 N N   . HIS B 1 10  ? 11.895  -5.555  46.768  1.00 30.62 ?  10  HIS B N   1 
ATOM   3145 C CA  . HIS B 1 10  ? 12.258  -4.154  46.641  1.00 32.21 ?  10  HIS B CA  1 
ATOM   3146 C C   . HIS B 1 10  ? 11.849  -3.624  45.272  1.00 30.45 ?  10  HIS B C   1 
ATOM   3147 O O   . HIS B 1 10  ? 12.207  -4.203  44.243  1.00 32.66 ?  10  HIS B O   1 
ATOM   3148 C CB  . HIS B 1 10  ? 13.756  -3.972  46.873  1.00 38.19 ?  10  HIS B CB  1 
ATOM   3149 C CG  . HIS B 1 10  ? 14.183  -4.280  48.278  1.00 36.55 ?  10  HIS B CG  1 
ATOM   3150 N ND1 . HIS B 1 10  ? 14.531  -5.549  48.689  1.00 39.36 ?  10  HIS B ND1 1 
ATOM   3151 C CD2 . HIS B 1 10  ? 14.287  -3.490  49.373  1.00 40.07 ?  10  HIS B CD2 1 
ATOM   3152 C CE1 . HIS B 1 10  ? 14.853  -5.524  49.970  1.00 41.23 ?  10  HIS B CE1 1 
ATOM   3153 N NE2 . HIS B 1 10  ? 14.714  -4.286  50.409  1.00 42.84 ?  10  HIS B NE2 1 
ATOM   3154 N N   . VAL B 1 11  ? 11.103  -2.532  45.269  1.00 29.90 ?  11  VAL B N   1 
ATOM   3155 C CA  . VAL B 1 11  ? 10.699  -1.915  44.001  1.00 31.17 ?  11  VAL B CA  1 
ATOM   3156 C C   . VAL B 1 11  ? 11.919  -1.255  43.365  1.00 32.77 ?  11  VAL B C   1 
ATOM   3157 O O   . VAL B 1 11  ? 12.694  -0.582  44.067  1.00 31.79 ?  11  VAL B O   1 
ATOM   3158 C CB  . VAL B 1 11  ? 9.578   -0.897  44.239  1.00 30.82 ?  11  VAL B CB  1 
ATOM   3159 C CG1 . VAL B 1 11  ? 9.118   -0.276  42.915  1.00 33.22 ?  11  VAL B CG1 1 
ATOM   3160 C CG2 . VAL B 1 11  ? 8.401   -1.556  44.955  1.00 31.08 ?  11  VAL B CG2 1 
ATOM   3161 N N   . PRO B 1 12  ? 12.168  -1.444  42.048  1.00 28.23 ?  12  PRO B N   1 
ATOM   3162 C CA  . PRO B 1 12  ? 13.226  -0.715  41.400  1.00 28.58 ?  12  PRO B CA  1 
ATOM   3163 C C   . PRO B 1 12  ? 13.069  0.805   41.479  1.00 33.13 ?  12  PRO B C   1 
ATOM   3164 O O   . PRO B 1 12  ? 11.973  1.293   41.406  1.00 33.42 ?  12  PRO B O   1 
ATOM   3165 C CB  . PRO B 1 12  ? 13.118  -1.146  39.939  1.00 29.32 ?  12  PRO B CB  1 
ATOM   3166 C CG  . PRO B 1 12  ? 12.666  -2.554  40.055  1.00 27.86 ?  12  PRO B CG  1 
ATOM   3167 C CD  . PRO B 1 12  ? 11.580  -2.415  41.083  1.00 27.50 ?  12  PRO B CD  1 
ATOM   3168 N N   . LYS B 1 13  ? 14.211  1.478   41.581  1.00 26.86 ?  13  LYS B N   1 
ATOM   3169 C CA  . LYS B 1 13  ? 14.230  2.955   41.641  1.00 31.44 ?  13  LYS B CA  1 
ATOM   3170 C C   . LYS B 1 13  ? 14.326  3.463   40.213  1.00 25.16 ?  13  LYS B C   1 
ATOM   3171 O O   . LYS B 1 13  ? 15.418  3.578   39.687  1.00 26.66 ?  13  LYS B O   1 
ATOM   3172 C CB  . LYS B 1 13  ? 15.342  3.464   42.555  1.00 28.74 ?  13  LYS B CB  1 
ATOM   3173 C CG  . LYS B 1 13  ? 15.174  3.147   44.036  1.00 33.52 ?  13  LYS B CG  1 
ATOM   3174 C CD  . LYS B 1 13  ? 16.310  3.646   44.911  1.00 41.40 ?  13  LYS B CD  1 
ATOM   3175 C CE  . LYS B 1 13  ? 16.114  3.344   46.381  1.00 45.53 ?  13  LYS B CE  1 
ATOM   3176 N NZ  . LYS B 1 13  ? 17.251  3.824   47.202  1.00 46.72 1  13  LYS B NZ  1 
ATOM   3177 N N   . ARG B 1 14  ? 13.191  3.803   39.665  1.00 27.35 ?  14  ARG B N   1 
ATOM   3178 C CA  . ARG B 1 14  ? 13.126  4.201   38.248  1.00 28.19 ?  14  ARG B CA  1 
ATOM   3179 C C   . ARG B 1 14  ? 13.477  5.657   37.985  1.00 31.34 ?  14  ARG B C   1 
ATOM   3180 O O   . ARG B 1 14  ? 13.362  6.487   38.888  1.00 31.88 ?  14  ARG B O   1 
ATOM   3181 C CB  . ARG B 1 14  ? 11.736  3.901   37.701  1.00 32.34 ?  14  ARG B CB  1 
ATOM   3182 C CG  . ARG B 1 14  ? 11.492  2.440   37.372  1.00 31.79 ?  14  ARG B CG  1 
ATOM   3183 C CD  . ARG B 1 14  ? 9.999   2.277   37.416  1.00 33.57 ?  14  ARG B CD  1 
ATOM   3184 N NE  . ARG B 1 14  ? 9.499   1.125   36.697  1.00 31.89 ?  14  ARG B NE  1 
ATOM   3185 C CZ  . ARG B 1 14  ? 9.122   0.007   37.289  1.00 30.46 ?  14  ARG B CZ  1 
ATOM   3186 N NH1 . ARG B 1 14  ? 9.220   -0.103  38.601  1.00 30.30 1  14  ARG B NH1 1 
ATOM   3187 N NH2 . ARG B 1 14  ? 8.652   -0.991  36.568  1.00 26.33 ?  14  ARG B NH2 1 
ATOM   3188 N N   . GLN B 1 15  ? 13.871  5.922   36.753  1.00 25.99 ?  15  GLN B N   1 
ATOM   3189 C CA  . GLN B 1 15  ? 14.120  7.287   36.334  1.00 26.49 ?  15  GLN B CA  1 
ATOM   3190 C C   . GLN B 1 15  ? 12.795  7.959   35.974  1.00 30.04 ?  15  GLN B C   1 
ATOM   3191 O O   . GLN B 1 15  ? 11.736  7.323   35.919  1.00 30.94 ?  15  GLN B O   1 
ATOM   3192 C CB  . GLN B 1 15  ? 15.130  7.313   35.180  1.00 28.17 ?  15  GLN B CB  1 
ATOM   3193 C CG  . GLN B 1 15  ? 16.553  7.002   35.675  1.00 26.02 ?  15  GLN B CG  1 
ATOM   3194 C CD  . GLN B 1 15  ? 17.641  7.180   34.624  1.00 26.61 ?  15  GLN B CD  1 
ATOM   3195 O OE1 . GLN B 1 15  ? 17.396  7.662   33.522  1.00 21.58 ?  15  GLN B OE1 1 
ATOM   3196 N NE2 . GLN B 1 15  ? 18.861  6.789   34.975  1.00 26.59 ?  15  GLN B NE2 1 
ATOM   3197 N N   . GLY B 1 16  ? 12.854  9.268   35.744  1.00 26.04 ?  16  GLY B N   1 
ATOM   3198 C CA  . GLY B 1 16  ? 11.636  10.056  35.645  1.00 24.12 ?  16  GLY B CA  1 
ATOM   3199 C C   . GLY B 1 16  ? 10.741  9.748   34.454  1.00 29.99 ?  16  GLY B C   1 
ATOM   3200 O O   . GLY B 1 16  ? 9.535   10.009  34.525  1.00 29.65 ?  16  GLY B O   1 
ATOM   3201 N N   . ASN B 1 17  ? 11.295  9.223   33.354  1.00 26.56 ?  17  ASN B N   1 
ATOM   3202 C CA  . ASN B 1 17  ? 10.522  9.015   32.133  1.00 26.43 ?  17  ASN B CA  1 
ATOM   3203 C C   . ASN B 1 17  ? 9.866   7.635   32.068  1.00 27.40 ?  17  ASN B C   1 
ATOM   3204 O O   . ASN B 1 17  ? 9.536   7.161   30.976  1.00 27.42 ?  17  ASN B O   1 
ATOM   3205 C CB  . ASN B 1 17  ? 11.397  9.242   30.895  1.00 26.35 ?  17  ASN B CB  1 
ATOM   3206 C CG  . ASN B 1 17  ? 12.440  8.157   30.707  1.00 26.40 ?  17  ASN B CG  1 
ATOM   3207 O OD1 . ASN B 1 17  ? 13.065  7.727   31.670  1.00 23.97 ?  17  ASN B OD1 1 
ATOM   3208 N ND2 . ASN B 1 17  ? 12.636  7.713   29.454  1.00 22.90 ?  17  ASN B ND2 1 
ATOM   3209 N N   . SER B 1 18  ? 9.664   6.992   33.212  1.00 24.84 ?  18  SER B N   1 
ATOM   3210 C CA  . SER B 1 18  ? 8.949   5.723   33.263  1.00 26.09 ?  18  SER B CA  1 
ATOM   3211 C C   . SER B 1 18  ? 7.471   5.916   32.943  1.00 26.77 ?  18  SER B C   1 
ATOM   3212 O O   . SER B 1 18  ? 6.817   6.804   33.497  1.00 29.80 ?  18  SER B O   1 
ATOM   3213 C CB  . SER B 1 18  ? 9.097   5.108   34.649  1.00 25.62 ?  18  SER B CB  1 
ATOM   3214 O OG  . SER B 1 18  ? 8.223   3.997   34.789  1.00 30.04 ?  18  SER B OG  1 
ATOM   3215 N N   . ILE B 1 19  ? 6.925   5.075   32.060  1.00 27.94 ?  19  ILE B N   1 
ATOM   3216 C CA  . ILE B 1 19  ? 5.500   5.208   31.762  1.00 29.78 ?  19  ILE B CA  1 
ATOM   3217 C C   . ILE B 1 19  ? 4.662   4.803   32.968  1.00 28.14 ?  19  ILE B C   1 
ATOM   3218 O O   . ILE B 1 19  ? 3.641   5.430   33.272  1.00 25.55 ?  19  ILE B O   1 
ATOM   3219 C CB  . ILE B 1 19  ? 5.104   4.390   30.522  1.00 29.96 ?  19  ILE B CB  1 
ATOM   3220 C CG1 . ILE B 1 19  ? 5.800   4.931   29.273  1.00 28.10 ?  19  ILE B CG1 1 
ATOM   3221 C CG2 . ILE B 1 19  ? 3.589   4.417   30.356  1.00 25.34 ?  19  ILE B CG2 1 
ATOM   3222 C CD1 . ILE B 1 19  ? 5.012   5.966   28.535  1.00 36.56 ?  19  ILE B CD1 1 
ATOM   3223 N N   . LYS B 1 20  ? 5.061   3.737   33.661  1.00 25.31 ?  20  LYS B N   1 
ATOM   3224 C CA  . LYS B 1 20  ? 4.259   3.254   34.784  1.00 23.97 ?  20  LYS B CA  1 
ATOM   3225 C C   . LYS B 1 20  ? 4.364   4.176   35.993  1.00 30.96 ?  20  LYS B C   1 
ATOM   3226 O O   . LYS B 1 20  ? 3.362   4.425   36.675  1.00 31.95 ?  20  LYS B O   1 
ATOM   3227 C CB  . LYS B 1 20  ? 4.686   1.832   35.172  1.00 25.87 ?  20  LYS B CB  1 
ATOM   3228 C CG  . LYS B 1 20  ? 3.727   1.140   36.149  1.00 25.93 ?  20  LYS B CG  1 
ATOM   3229 C CD  . LYS B 1 20  ? 4.125   -0.306  36.394  1.00 23.15 ?  20  LYS B CD  1 
ATOM   3230 C CE  . LYS B 1 20  ? 3.078   -1.047  37.233  1.00 25.26 ?  20  LYS B CE  1 
ATOM   3231 N NZ  . LYS B 1 20  ? 3.546   -2.397  37.654  1.00 23.75 1  20  LYS B NZ  1 
ATOM   3232 N N   . TRP B 1 21  ? 5.561   4.676   36.294  1.00 28.89 ?  21  TRP B N   1 
ATOM   3233 C CA  . TRP B 1 21  ? 5.790   5.414   37.530  1.00 30.82 ?  21  TRP B CA  1 
ATOM   3234 C C   . TRP B 1 21  ? 6.151   6.877   37.326  1.00 32.88 ?  21  TRP B C   1 
ATOM   3235 O O   . TRP B 1 21  ? 6.339   7.594   38.315  1.00 35.31 ?  21  TRP B O   1 
ATOM   3236 C CB  . TRP B 1 21  ? 6.891   4.738   38.353  1.00 31.49 ?  21  TRP B CB  1 
ATOM   3237 C CG  . TRP B 1 21  ? 6.442   3.471   38.977  1.00 29.81 ?  21  TRP B CG  1 
ATOM   3238 C CD1 . TRP B 1 21  ? 6.492   2.227   38.422  1.00 31.34 ?  21  TRP B CD1 1 
ATOM   3239 C CD2 . TRP B 1 21  ? 5.861   3.313   40.272  1.00 29.19 ?  21  TRP B CD2 1 
ATOM   3240 N NE1 . TRP B 1 21  ? 5.978   1.299   39.293  1.00 27.73 ?  21  TRP B NE1 1 
ATOM   3241 C CE2 . TRP B 1 21  ? 5.580   1.942   40.437  1.00 31.06 ?  21  TRP B CE2 1 
ATOM   3242 C CE3 . TRP B 1 21  ? 5.543   4.195   41.306  1.00 27.31 ?  21  TRP B CE3 1 
ATOM   3243 C CZ2 . TRP B 1 21  ? 5.012   1.433   41.600  1.00 29.16 ?  21  TRP B CZ2 1 
ATOM   3244 C CZ3 . TRP B 1 21  ? 4.975   3.686   42.465  1.00 31.13 ?  21  TRP B CZ3 1 
ATOM   3245 C CH2 . TRP B 1 21  ? 4.713   2.324   42.600  1.00 28.49 ?  21  TRP B CH2 1 
ATOM   3246 N N   . GLY B 1 22  ? 6.269   7.340   36.086  1.00 34.46 ?  22  GLY B N   1 
ATOM   3247 C CA  . GLY B 1 22  ? 6.621   8.729   35.855  1.00 36.76 ?  22  GLY B CA  1 
ATOM   3248 C C   . GLY B 1 22  ? 5.404   9.629   35.955  1.00 38.46 ?  22  GLY B C   1 
ATOM   3249 O O   . GLY B 1 22  ? 4.290   9.263   35.571  1.00 38.90 ?  22  GLY B O   1 
ATOM   3250 N N   . GLY B 1 23  ? 5.524   10.865  36.391  1.00 40.00 ?  23  GLY B N   1 
ATOM   3251 C CA  . GLY B 1 23  ? 4.365   11.785  36.307  1.00 45.57 ?  23  GLY B CA  1 
ATOM   3252 C C   . GLY B 1 23  ? 3.232   11.451  37.248  1.00 44.33 ?  23  GLY B C   1 
ATOM   3253 O O   . GLY B 1 23  ? 2.079   11.731  36.925  1.00 47.60 ?  23  GLY B O   1 
ATOM   3254 N N   . LEU B 1 24  ? 3.571   10.924  38.406  1.00 49.06 ?  24  LEU B N   1 
ATOM   3255 C CA  . LEU B 1 24  ? 2.550   10.513  39.391  1.00 47.78 ?  24  LEU B CA  1 
ATOM   3256 C C   . LEU B 1 24  ? 2.421   11.539  40.519  1.00 50.30 ?  24  LEU B C   1 
ATOM   3257 O O   . LEU B 1 24  ? 3.379   12.267  40.776  1.00 58.02 ?  24  LEU B O   1 
ATOM   3258 C CB  . LEU B 1 24  ? 3.044   9.214   40.038  1.00 45.73 ?  24  LEU B CB  1 
ATOM   3259 C CG  . LEU B 1 24  ? 2.934   7.933   39.215  1.00 39.14 ?  24  LEU B CG  1 
ATOM   3260 C CD1 . LEU B 1 24  ? 2.815   6.728   40.123  1.00 44.79 ?  24  LEU B CD1 1 
ATOM   3261 C CD2 . LEU B 1 24  ? 1.728   7.997   38.304  1.00 35.09 ?  24  LEU B CD2 1 
ATOM   3262 N N   . GLU B 1 26  ? 1.794   12.104  44.713  1.00 49.42 ?  26  GLU B N   1 
ATOM   3263 C CA  . GLU B 1 26  ? 2.350   11.434  45.898  1.00 46.79 ?  26  GLU B CA  1 
ATOM   3264 C C   . GLU B 1 26  ? 1.484   10.255  46.302  1.00 38.26 ?  26  GLU B C   1 
ATOM   3265 O O   . GLU B 1 26  ? 0.262   10.429  46.277  1.00 40.80 ?  26  GLU B O   1 
ATOM   3266 C CB  . GLU B 1 26  ? 2.442   12.490  46.999  1.00 48.00 ?  26  GLU B CB  1 
ATOM   3267 C CG  . GLU B 1 26  ? 1.274   13.465  47.024  1.00 53.42 ?  26  GLU B CG  1 
ATOM   3268 C CD  . GLU B 1 26  ? 1.385   14.739  46.198  1.00 55.74 ?  26  GLU B CD  1 
ATOM   3269 O OE1 . GLU B 1 26  ? 2.290   14.819  45.337  1.00 53.59 ?  26  GLU B OE1 1 
ATOM   3270 O OE2 . GLU B 1 26  ? 0.539   15.635  46.394  1.00 52.58 -1 26  GLU B OE2 1 
ATOM   3271 N N   . LYS B 1 27  ? 2.114   9.113   46.592  1.00 38.87 ?  27  LYS B N   1 
ATOM   3272 C CA  . LYS B 1 27  ? 1.389   7.967   47.106  1.00 38.56 ?  27  LYS B CA  1 
ATOM   3273 C C   . LYS B 1 27  ? 0.495   7.342   46.053  1.00 34.89 ?  27  LYS B C   1 
ATOM   3274 O O   . LYS B 1 27  ? -0.241  6.416   46.369  1.00 33.16 ?  27  LYS B O   1 
ATOM   3275 C CB  . LYS B 1 27  ? 0.560   8.300   48.353  1.00 40.21 ?  27  LYS B CB  1 
ATOM   3276 C CG  . LYS B 1 27  ? 1.258   9.130   49.428  1.00 44.83 ?  27  LYS B CG  1 
ATOM   3277 C CD  . LYS B 1 27  ? 0.259   9.609   50.494  1.00 46.71 ?  27  LYS B CD  1 
ATOM   3278 C CE  . LYS B 1 27  ? 0.641   9.146   51.895  1.00 48.35 ?  27  LYS B CE  1 
ATOM   3279 N NZ  . LYS B 1 27  ? 0.314   10.178  52.925  1.00 48.49 1  27  LYS B NZ  1 
ATOM   3280 N N   . GLU B 1 28  ? 0.518   7.814   44.812  1.00 32.94 ?  28  GLU B N   1 
ATOM   3281 C CA  . GLU B 1 28  ? -0.277  7.126   43.805  1.00 32.58 ?  28  GLU B CA  1 
ATOM   3282 C C   . GLU B 1 28  ? 0.355   5.774   43.500  1.00 26.46 ?  28  GLU B C   1 
ATOM   3283 O O   . GLU B 1 28  ? 1.571   5.587   43.606  1.00 25.21 ?  28  GLU B O   1 
ATOM   3284 C CB  . GLU B 1 28  ? -0.430  7.973   42.539  1.00 33.05 ?  28  GLU B CB  1 
ATOM   3285 C CG  . GLU B 1 28  ? -1.660  8.895   42.600  1.00 33.99 ?  28  GLU B CG  1 
ATOM   3286 C CD  . GLU B 1 28  ? -1.977  9.580   41.280  1.00 32.25 ?  28  GLU B CD  1 
ATOM   3287 O OE1 . GLU B 1 28  ? -3.169  9.864   41.017  1.00 30.52 ?  28  GLU B OE1 1 
ATOM   3288 O OE2 . GLU B 1 28  ? -1.031  9.854   40.516  1.00 32.57 -1 28  GLU B OE2 1 
ATOM   3289 N N   . LEU B 1 29  ? -0.498  4.807   43.176  1.00 27.22 ?  29  LEU B N   1 
ATOM   3290 C CA  . LEU B 1 29  ? -0.078  3.418   43.005  1.00 23.52 ?  29  LEU B CA  1 
ATOM   3291 C C   . LEU B 1 29  ? -0.479  2.941   41.615  1.00 25.19 ?  29  LEU B C   1 
ATOM   3292 O O   . LEU B 1 29  ? -1.659  2.630   41.376  1.00 24.42 ?  29  LEU B O   1 
ATOM   3293 C CB  . LEU B 1 29  ? -0.692  2.524   44.091  1.00 23.02 ?  29  LEU B CB  1 
ATOM   3294 C CG  . LEU B 1 29  ? -0.367  1.028   43.996  1.00 26.17 ?  29  LEU B CG  1 
ATOM   3295 C CD1 . LEU B 1 29  ? 1.132   0.836   43.781  1.00 28.90 ?  29  LEU B CD1 1 
ATOM   3296 C CD2 . LEU B 1 29  ? -0.812  0.287   45.259  1.00 26.13 ?  29  LEU B CD2 1 
ATOM   3297 N N   . PRO B 1 30  ? 0.454   2.876   40.663  1.00 23.17 ?  30  PRO B N   1 
ATOM   3298 C CA  . PRO B 1 30  ? 0.101   2.425   39.314  1.00 24.18 ?  30  PRO B CA  1 
ATOM   3299 C C   . PRO B 1 30  ? 0.114   0.906   39.262  1.00 24.28 ?  30  PRO B C   1 
ATOM   3300 O O   . PRO B 1 30  ? 1.125   0.278   39.575  1.00 23.24 ?  30  PRO B O   1 
ATOM   3301 C CB  . PRO B 1 30  ? 1.211   3.020   38.447  1.00 25.98 ?  30  PRO B CB  1 
ATOM   3302 C CG  . PRO B 1 30  ? 2.427   2.896   39.353  1.00 22.55 ?  30  PRO B CG  1 
ATOM   3303 C CD  . PRO B 1 30  ? 1.903   3.103   40.794  1.00 26.33 ?  30  PRO B CD  1 
ATOM   3304 N N   . MET B 1 31  ? -1.008  0.320   38.852  1.00 25.61 ?  31  MET B N   1 
ATOM   3305 C CA  . MET B 1 31  ? -1.116  -1.118  38.607  1.00 24.65 ?  31  MET B CA  1 
ATOM   3306 C C   . MET B 1 31  ? -1.764  -1.382  37.259  1.00 22.68 ?  31  MET B C   1 
ATOM   3307 O O   . MET B 1 31  ? -2.587  -2.292  37.109  1.00 24.85 ?  31  MET B O   1 
ATOM   3308 C CB  . MET B 1 31  ? -1.899  -1.806  39.721  1.00 23.68 ?  31  MET B CB  1 
ATOM   3309 C CG  . MET B 1 31  ? -1.402  -1.454  41.114  1.00 24.48 ?  31  MET B CG  1 
ATOM   3310 S SD  . MET B 1 31  ? -2.275  -2.357  42.405  1.00 27.40 ?  31  MET B SD  1 
ATOM   3311 C CE  . MET B 1 31  ? -1.309  -3.850  42.493  1.00 22.80 ?  31  MET B CE  1 
ATOM   3312 N N   . TRP B 1 32  ? -1.403  -0.592  36.247  1.00 23.09 ?  32  TRP B N   1 
ATOM   3313 C CA  . TRP B 1 32  ? -2.135  -0.650  34.989  1.00 20.36 ?  32  TRP B CA  1 
ATOM   3314 C C   . TRP B 1 32  ? -1.284  -1.299  33.901  1.00 25.56 ?  32  TRP B C   1 
ATOM   3315 O O   . TRP B 1 32  ? -1.498  -2.475  33.575  1.00 24.26 ?  32  TRP B O   1 
ATOM   3316 C CB  . TRP B 1 32  ? -2.649  0.745   34.576  1.00 23.26 ?  32  TRP B CB  1 
ATOM   3317 C CG  . TRP B 1 32  ? -1.628  1.830   34.448  1.00 23.65 ?  32  TRP B CG  1 
ATOM   3318 C CD1 . TRP B 1 32  ? -0.946  2.453   35.461  1.00 25.62 ?  32  TRP B CD1 1 
ATOM   3319 C CD2 . TRP B 1 32  ? -1.178  2.437   33.230  1.00 23.45 ?  32  TRP B CD2 1 
ATOM   3320 N NE1 . TRP B 1 32  ? -0.103  3.411   34.942  1.00 26.83 ?  32  TRP B NE1 1 
ATOM   3321 C CE2 . TRP B 1 32  ? -0.225  3.418   33.576  1.00 24.02 ?  32  TRP B CE2 1 
ATOM   3322 C CE3 . TRP B 1 32  ? -1.487  2.240   31.879  1.00 25.65 ?  32  TRP B CE3 1 
ATOM   3323 C CZ2 . TRP B 1 32  ? 0.427   4.200   32.614  1.00 26.16 ?  32  TRP B CZ2 1 
ATOM   3324 C CZ3 . TRP B 1 32  ? -0.837  3.016   30.923  1.00 25.84 ?  32  TRP B CZ3 1 
ATOM   3325 C CH2 . TRP B 1 32  ? 0.107   3.982   31.297  1.00 24.43 ?  32  TRP B CH2 1 
ATOM   3326 N N   . ILE B 1 33  ? -0.286  -0.575  33.389  1.00 24.09 ?  33  ILE B N   1 
ATOM   3327 C CA  . ILE B 1 33  ? 0.497   -1.045  32.250  1.00 23.60 ?  33  ILE B CA  1 
ATOM   3328 C C   . ILE B 1 33  ? 1.304   -2.290  32.621  1.00 24.77 ?  33  ILE B C   1 
ATOM   3329 O O   . ILE B 1 33  ? 1.791   -2.436  33.753  1.00 21.62 ?  33  ILE B O   1 
ATOM   3330 C CB  . ILE B 1 33  ? 1.408   0.089   31.739  1.00 23.12 ?  33  ILE B CB  1 
ATOM   3331 C CG1 . ILE B 1 33  ? 1.959   -0.249  30.346  1.00 30.45 ?  33  ILE B CG1 1 
ATOM   3332 C CG2 . ILE B 1 33  ? 2.518   0.389   32.761  1.00 26.02 ?  33  ILE B CG2 1 
ATOM   3333 C CD1 . ILE B 1 33  ? 2.642   0.926   29.638  1.00 30.05 ?  33  ILE B CD1 1 
ATOM   3334 N N   . ALA B 1 34  ? 1.470   -3.187  31.648  1.00 21.42 ?  34  ALA B N   1 
ATOM   3335 C CA  . ALA B 1 34  ? 2.031   -4.525  31.886  1.00 22.29 ?  34  ALA B CA  1 
ATOM   3336 C C   . ALA B 1 34  ? 3.559   -4.487  31.888  1.00 22.60 ?  34  ALA B C   1 
ATOM   3337 O O   . ALA B 1 34  ? 4.233   -4.923  30.946  1.00 19.93 ?  34  ALA B O   1 
ATOM   3338 C CB  . ALA B 1 34  ? 1.504   -5.505  30.844  1.00 23.46 ?  34  ALA B CB  1 
ATOM   3339 N N   . GLU B 1 35  ? 4.111   -3.969  32.986  1.00 21.70 ?  35  GLU B N   1 
ATOM   3340 C CA  . GLU B 1 35  ? 5.507   -4.165  33.358  1.00 21.01 ?  35  GLU B CA  1 
ATOM   3341 C C   . GLU B 1 35  ? 5.546   -4.446  34.850  1.00 22.72 ?  35  GLU B C   1 
ATOM   3342 O O   . GLU B 1 35  ? 4.635   -4.069  35.589  1.00 21.46 ?  35  GLU B O   1 
ATOM   3343 C CB  . GLU B 1 35  ? 6.395   -2.947  33.033  1.00 22.96 ?  35  GLU B CB  1 
ATOM   3344 C CG  . GLU B 1 35  ? 6.029   -1.695  33.812  1.00 20.42 ?  35  GLU B CG  1 
ATOM   3345 C CD  . GLU B 1 35  ? 6.734   -0.459  33.302  1.00 24.89 ?  35  GLU B CD  1 
ATOM   3346 O OE1 . GLU B 1 35  ? 7.640   0.039   34.003  1.00 23.83 ?  35  GLU B OE1 1 
ATOM   3347 O OE2 . GLU B 1 35  ? 6.396   0.003   32.192  1.00 23.42 -1 35  GLU B OE2 1 
ATOM   3348 N N   . MET B 1 36  ? 6.610   -5.119  35.290  1.00 19.38 ?  36  MET B N   1 
ATOM   3349 C CA  . MET B 1 36  ? 6.678   -5.543  36.680  1.00 22.18 ?  36  MET B CA  1 
ATOM   3350 C C   . MET B 1 36  ? 7.372   -4.504  37.555  1.00 25.29 ?  36  MET B C   1 
ATOM   3351 O O   . MET B 1 36  ? 8.122   -3.641  37.085  1.00 24.24 ?  36  MET B O   1 
ATOM   3352 C CB  . MET B 1 36  ? 7.417   -6.877  36.811  1.00 19.69 ?  36  MET B CB  1 
ATOM   3353 C CG  . MET B 1 36  ? 7.073   -7.923  35.763  1.00 25.98 ?  36  MET B CG  1 
ATOM   3354 S SD  . MET B 1 36  ? 7.864   -9.467  36.312  1.00 30.25 ?  36  MET B SD  1 
ATOM   3355 C CE  . MET B 1 36  ? 7.916   -10.425 34.842  1.00 27.30 ?  36  MET B CE  1 
ATOM   3356 N N   . ASP B 1 37  ? 7.139   -4.626  38.856  1.00 25.06 ?  37  ASP B N   1 
ATOM   3357 C CA  . ASP B 1 37  ? 7.855   -3.835  39.847  1.00 23.83 ?  37  ASP B CA  1 
ATOM   3358 C C   . ASP B 1 37  ? 8.826   -4.700  40.635  1.00 25.96 ?  37  ASP B C   1 
ATOM   3359 O O   . ASP B 1 37  ? 8.963   -4.565  41.853  1.00 26.50 ?  37  ASP B O   1 
ATOM   3360 C CB  . ASP B 1 37  ? 6.867   -3.107  40.745  1.00 21.63 ?  37  ASP B CB  1 
ATOM   3361 C CG  . ASP B 1 37  ? 6.118   -2.029  39.975  1.00 28.82 ?  37  ASP B CG  1 
ATOM   3362 O OD1 . ASP B 1 37  ? 6.797   -1.229  39.290  1.00 31.74 ?  37  ASP B OD1 1 
ATOM   3363 O OD2 . ASP B 1 37  ? 4.874   -2.002  40.004  1.00 25.83 -1 37  ASP B OD2 1 
ATOM   3364 N N   . PHE B 1 38  ? 9.514   -5.597  39.924  1.00 23.55 ?  38  PHE B N   1 
ATOM   3365 C CA  . PHE B 1 38  ? 10.595  -6.402  40.463  1.00 26.29 ?  38  PHE B CA  1 
ATOM   3366 C C   . PHE B 1 38  ? 11.883  -6.071  39.729  1.00 27.43 ?  38  PHE B C   1 
ATOM   3367 O O   . PHE B 1 38  ? 11.862  -5.703  38.551  1.00 24.13 ?  38  PHE B O   1 
ATOM   3368 C CB  . PHE B 1 38  ? 10.318  -7.904  40.303  1.00 24.33 ?  38  PHE B CB  1 
ATOM   3369 C CG  . PHE B 1 38  ? 9.050   -8.356  40.946  1.00 23.17 ?  38  PHE B CG  1 
ATOM   3370 C CD1 . PHE B 1 38  ? 8.816   -8.103  42.285  1.00 21.51 ?  38  PHE B CD1 1 
ATOM   3371 C CD2 . PHE B 1 38  ? 8.094   -9.050  40.215  1.00 25.30 ?  38  PHE B CD2 1 
ATOM   3372 C CE1 . PHE B 1 38  ? 7.643   -8.523  42.871  1.00 25.24 ?  38  PHE B CE1 1 
ATOM   3373 C CE2 . PHE B 1 38  ? 6.915   -9.472  40.805  1.00 21.99 ?  38  PHE B CE2 1 
ATOM   3374 C CZ  . PHE B 1 38  ? 6.693   -9.203  42.128  1.00 21.52 ?  38  PHE B CZ  1 
ATOM   3375 N N   . ARG B 1 39  ? 13.001  -6.223  40.432  1.00 28.50 ?  39  ARG B N   1 
ATOM   3376 C CA  . ARG B 1 39  ? 14.308  -6.207  39.793  1.00 23.47 ?  39  ARG B CA  1 
ATOM   3377 C C   . ARG B 1 39  ? 14.468  -7.405  38.867  1.00 26.96 ?  39  ARG B C   1 
ATOM   3378 O O   . ARG B 1 39  ? 13.910  -8.482  39.107  1.00 26.46 ?  39  ARG B O   1 
ATOM   3379 C CB  . ARG B 1 39  ? 15.409  -6.262  40.844  1.00 27.91 ?  39  ARG B CB  1 
ATOM   3380 C CG  . ARG B 1 39  ? 15.808  -4.949  41.431  1.00 35.88 ?  39  ARG B CG  1 
ATOM   3381 C CD  . ARG B 1 39  ? 17.023  -5.202  42.317  1.00 39.15 ?  39  ARG B CD  1 
ATOM   3382 N NE  . ARG B 1 39  ? 17.541  -3.995  42.947  1.00 51.36 ?  39  ARG B NE  1 
ATOM   3383 C CZ  . ARG B 1 39  ? 17.672  -3.840  44.261  1.00 53.76 ?  39  ARG B CZ  1 
ATOM   3384 N NH1 . ARG B 1 39  ? 17.319  -4.817  45.089  1.00 51.03 1  39  ARG B NH1 1 
ATOM   3385 N NH2 . ARG B 1 39  ? 18.166  -2.713  44.749  1.00 60.71 ?  39  ARG B NH2 1 
ATOM   3386 N N   . ILE B 1 40  ? 15.266  -7.225  37.813  1.00 22.36 ?  40  ILE B N   1 
ATOM   3387 C CA  . ILE B 1 40  ? 15.456  -8.321  36.866  1.00 23.88 ?  40  ILE B CA  1 
ATOM   3388 C C   . ILE B 1 40  ? 16.471  -9.313  37.413  1.00 23.82 ?  40  ILE B C   1 
ATOM   3389 O O   . ILE B 1 40  ? 17.170  -9.028  38.394  1.00 27.07 ?  40  ILE B O   1 
ATOM   3390 C CB  . ILE B 1 40  ? 15.878  -7.804  35.478  1.00 24.76 ?  40  ILE B CB  1 
ATOM   3391 C CG1 . ILE B 1 40  ? 17.311  -7.239  35.499  1.00 22.70 ?  40  ILE B CG1 1 
ATOM   3392 C CG2 . ILE B 1 40  ? 14.871  -6.781  34.963  1.00 19.85 ?  40  ILE B CG2 1 
ATOM   3393 C CD1 . ILE B 1 40  ? 17.874  -7.033  34.089  1.00 24.30 ?  40  ILE B CD1 1 
ATOM   3394 N N   . ALA B 1 41  ? 16.536  -10.489 36.790  1.00 24.99 ?  41  ALA B N   1 
ATOM   3395 C CA  . ALA B 1 41  ? 17.451  -11.535 37.220  1.00 25.54 ?  41  ALA B CA  1 
ATOM   3396 C C   . ALA B 1 41  ? 18.890  -11.028 37.171  1.00 27.91 ?  41  ALA B C   1 
ATOM   3397 O O   . ALA B 1 41  ? 19.291  -10.425 36.173  1.00 25.46 ?  41  ALA B O   1 
ATOM   3398 C CB  . ALA B 1 41  ? 17.293  -12.760 36.319  1.00 23.82 ?  41  ALA B CB  1 
ATOM   3399 N N   . PRO B 1 42  ? 19.695  -11.259 38.215  1.00 26.75 ?  42  PRO B N   1 
ATOM   3400 C CA  . PRO B 1 42  ? 21.079  -10.745 38.190  1.00 22.00 ?  42  PRO B CA  1 
ATOM   3401 C C   . PRO B 1 42  ? 21.930  -11.368 37.097  1.00 22.58 ?  42  PRO B C   1 
ATOM   3402 O O   . PRO B 1 42  ? 22.899  -10.734 36.658  1.00 25.73 ?  42  PRO B O   1 
ATOM   3403 C CB  . PRO B 1 42  ? 21.617  -11.077 39.599  1.00 28.52 ?  42  PRO B CB  1 
ATOM   3404 C CG  . PRO B 1 42  ? 20.664  -12.084 40.179  1.00 29.56 ?  42  PRO B CG  1 
ATOM   3405 C CD  . PRO B 1 42  ? 19.323  -11.834 39.518  1.00 29.16 ?  42  PRO B CD  1 
ATOM   3406 N N   . GLU B 1 43  ? 21.595  -12.580 36.633  1.00 23.43 ?  43  GLU B N   1 
ATOM   3407 C CA  . GLU B 1 43  ? 22.293  -13.153 35.485  1.00 24.52 ?  43  GLU B CA  1 
ATOM   3408 C C   . GLU B 1 43  ? 22.107  -12.300 34.236  1.00 25.20 ?  43  GLU B C   1 
ATOM   3409 O O   . GLU B 1 43  ? 23.004  -12.243 33.389  1.00 25.25 ?  43  GLU B O   1 
ATOM   3410 C CB  . GLU B 1 43  ? 21.806  -14.572 35.211  1.00 28.65 ?  43  GLU B CB  1 
ATOM   3411 C CG  . GLU B 1 43  ? 21.992  -15.543 36.365  1.00 27.77 ?  43  GLU B CG  1 
ATOM   3412 C CD  . GLU B 1 43  ? 20.846  -15.528 37.362  1.00 28.61 ?  43  GLU B CD  1 
ATOM   3413 O OE1 . GLU B 1 43  ? 20.757  -16.488 38.155  1.00 33.01 ?  43  GLU B OE1 1 
ATOM   3414 O OE2 . GLU B 1 43  ? 20.057  -14.558 37.387  1.00 27.36 -1 43  GLU B OE2 1 
ATOM   3415 N N   . ILE B 1 44  ? 20.951  -11.646 34.092  1.00 24.31 ?  44  ILE B N   1 
ATOM   3416 C CA  . ILE B 1 44  ? 20.769  -10.752 32.950  1.00 22.24 ?  44  ILE B CA  1 
ATOM   3417 C C   . ILE B 1 44  ? 21.563  -9.471  33.157  1.00 23.42 ?  44  ILE B C   1 
ATOM   3418 O O   . ILE B 1 44  ? 22.232  -8.983  32.235  1.00 23.00 ?  44  ILE B O   1 
ATOM   3419 C CB  . ILE B 1 44  ? 19.274  -10.448 32.712  1.00 24.99 ?  44  ILE B CB  1 
ATOM   3420 C CG1 . ILE B 1 44  ? 18.474  -11.720 32.459  1.00 25.54 ?  44  ILE B CG1 1 
ATOM   3421 C CG2 . ILE B 1 44  ? 19.123  -9.475  31.552  1.00 19.88 ?  44  ILE B CG2 1 
ATOM   3422 C CD1 . ILE B 1 44  ? 16.971  -11.501 32.590  1.00 23.23 ?  44  ILE B CD1 1 
ATOM   3423 N N   . MET B 1 45  ? 21.539  -8.933  34.372  1.00 21.44 ?  45  MET B N   1 
ATOM   3424 C CA  . MET B 1 45  ? 22.273  -7.670  34.674  1.00 21.39 ?  45  MET B CA  1 
ATOM   3425 C C   . MET B 1 45  ? 23.770  -7.882  34.414  1.00 26.28 ?  45  MET B C   1 
ATOM   3426 O O   . MET B 1 45  ? 24.389  -7.027  33.811  1.00 27.80 ?  45  MET B O   1 
ATOM   3427 C CB  . MET B 1 45  ? 22.017  -7.209  36.119  1.00 26.96 ?  45  MET B CB  1 
ATOM   3428 C CG  . MET B 1 45  ? 22.718  -5.929  36.495  1.00 31.58 ?  45  MET B CG  1 
ATOM   3429 S SD  . MET B 1 45  ? 21.883  -4.468  35.843  1.00 42.57 ?  45  MET B SD  1 
ATOM   3430 C CE  . MET B 1 45  ? 20.186  -5.014  35.921  1.00 21.43 ?  45  MET B CE  1 
ATOM   3431 N N   . THR B 1 46  ? 24.291  -9.034  34.822  1.00 24.48 ?  46  THR B N   1 
ATOM   3432 C CA  . THR B 1 46  ? 25.691  -9.341  34.551  1.00 26.75 ?  46  THR B CA  1 
ATOM   3433 C C   . THR B 1 46  ? 26.002  -9.269  33.062  1.00 23.77 ?  46  THR B C   1 
ATOM   3434 O O   . THR B 1 46  ? 27.038  -8.727  32.662  1.00 24.87 ?  46  THR B O   1 
ATOM   3435 C CB  . THR B 1 46  ? 26.022  -10.719 35.111  1.00 25.38 ?  46  THR B CB  1 
ATOM   3436 O OG1 . THR B 1 46  ? 25.906  -10.658 36.541  1.00 26.81 ?  46  THR B OG1 1 
ATOM   3437 C CG2 . THR B 1 46  ? 27.447  -11.162 34.713  1.00 25.25 ?  46  THR B CG2 1 
ATOM   3438 N N   . SER B 1 47  ? 25.111  -9.793  32.225  1.00 23.56 ?  47  SER B N   1 
ATOM   3439 C CA  . SER B 1 47  ? 25.380  -9.802  30.794  1.00 25.55 ?  47  SER B CA  1 
ATOM   3440 C C   . SER B 1 47  ? 25.353  -8.394  30.226  1.00 18.71 ?  47  SER B C   1 
ATOM   3441 O O   . SER B 1 47  ? 26.124  -8.068  29.314  1.00 24.78 ?  47  SER B O   1 
ATOM   3442 C CB  . SER B 1 47  ? 24.362  -10.679 30.072  1.00 26.24 ?  47  SER B CB  1 
ATOM   3443 O OG  . SER B 1 47  ? 23.135  -9.967  29.961  1.00 28.98 ?  47  SER B OG  1 
ATOM   3444 N N   . MET B 1 48  ? 24.458  -7.548  30.745  1.00 21.23 ?  48  MET B N   1 
ATOM   3445 C CA  . MET B 1 48  ? 24.367  -6.174  30.270  1.00 21.16 ?  48  MET B CA  1 
ATOM   3446 C C   . MET B 1 48  ? 25.602  -5.382  30.654  1.00 21.70 ?  48  MET B C   1 
ATOM   3447 O O   . MET B 1 48  ? 26.150  -4.636  29.839  1.00 21.25 ?  48  MET B O   1 
ATOM   3448 C CB  . MET B 1 48  ? 23.120  -5.504  30.842  1.00 22.80 ?  48  MET B CB  1 
ATOM   3449 C CG  . MET B 1 48  ? 21.820  -5.940  30.174  1.00 24.83 ?  48  MET B CG  1 
ATOM   3450 S SD  . MET B 1 48  ? 20.435  -5.200  31.038  1.00 33.11 ?  48  MET B SD  1 
ATOM   3451 C CE  . MET B 1 48  ? 19.084  -5.778  30.019  1.00 29.67 ?  48  MET B CE  1 
ATOM   3452 N N   . GLU B 1 49  ? 26.057  -5.544  31.893  1.00 24.24 ?  49  GLU B N   1 
ATOM   3453 C CA  . GLU B 1 49  ? 27.216  -4.791  32.343  1.00 24.83 ?  49  GLU B CA  1 
ATOM   3454 C C   . GLU B 1 49  ? 28.471  -5.235  31.607  1.00 23.57 ?  49  GLU B C   1 
ATOM   3455 O O   . GLU B 1 49  ? 29.350  -4.413  31.342  1.00 28.19 ?  49  GLU B O   1 
ATOM   3456 C CB  . GLU B 1 49  ? 27.344  -4.932  33.862  1.00 26.39 ?  49  GLU B CB  1 
ATOM   3457 C CG  . GLU B 1 49  ? 26.279  -4.086  34.562  1.00 30.67 ?  49  GLU B CG  1 
ATOM   3458 C CD  . GLU B 1 49  ? 26.141  -4.357  36.044  1.00 38.48 ?  49  GLU B CD  1 
ATOM   3459 O OE1 . GLU B 1 49  ? 25.494  -3.534  36.726  1.00 44.50 ?  49  GLU B OE1 1 
ATOM   3460 O OE2 . GLU B 1 49  ? 26.666  -5.385  36.522  1.00 44.46 -1 49  GLU B OE2 1 
ATOM   3461 N N   . GLU B 1 50  ? 28.553  -6.509  31.231  1.00 23.08 ?  50  GLU B N   1 
ATOM   3462 C CA  . GLU B 1 50  ? 29.698  -6.975  30.448  1.00 26.26 ?  50  GLU B CA  1 
ATOM   3463 C C   . GLU B 1 50  ? 29.699  -6.379  29.044  1.00 27.09 ?  50  GLU B C   1 
ATOM   3464 O O   . GLU B 1 50  ? 30.756  -6.013  28.517  1.00 25.65 ?  50  GLU B O   1 
ATOM   3465 C CB  . GLU B 1 50  ? 29.711  -8.502  30.361  1.00 29.01 ?  50  GLU B CB  1 
ATOM   3466 C CG  . GLU B 1 50  ? 30.904  -9.055  29.587  1.00 32.38 ?  50  GLU B CG  1 
ATOM   3467 C CD  . GLU B 1 50  ? 32.198  -9.035  30.401  1.00 37.81 ?  50  GLU B CD  1 
ATOM   3468 O OE1 . GLU B 1 50  ? 33.051  -9.910  30.168  1.00 51.30 ?  50  GLU B OE1 1 
ATOM   3469 O OE2 . GLU B 1 50  ? 32.363  -8.160  31.279  1.00 41.11 -1 50  GLU B OE2 1 
ATOM   3470 N N   . LYS B 1 51  ? 28.527  -6.291  28.414  1.00 23.24 ?  51  LYS B N   1 
ATOM   3471 C CA  . LYS B 1 51  ? 28.458  -5.706  27.086  1.00 21.85 ?  51  LYS B CA  1 
ATOM   3472 C C   . LYS B 1 51  ? 28.842  -4.232  27.121  1.00 24.02 ?  51  LYS B C   1 
ATOM   3473 O O   . LYS B 1 51  ? 29.449  -3.715  26.174  1.00 23.56 ?  51  LYS B O   1 
ATOM   3474 C CB  . LYS B 1 51  ? 27.043  -5.900  26.518  1.00 21.19 ?  51  LYS B CB  1 
ATOM   3475 C CG  . LYS B 1 51  ? 26.798  -5.244  25.154  1.00 22.01 ?  51  LYS B CG  1 
ATOM   3476 C CD  . LYS B 1 51  ? 27.800  -5.711  24.104  1.00 24.12 ?  51  LYS B CD  1 
ATOM   3477 C CE  . LYS B 1 51  ? 27.530  -5.112  22.720  1.00 21.06 ?  51  LYS B CE  1 
ATOM   3478 N NZ  . LYS B 1 51  ? 26.254  -5.625  22.100  1.00 22.17 1  51  LYS B NZ  1 
ATOM   3479 N N   . LEU B 1 52  ? 28.520  -3.543  28.214  1.00 22.33 ?  52  LEU B N   1 
ATOM   3480 C CA  . LEU B 1 52  ? 28.801  -2.115  28.279  1.00 22.79 ?  52  LEU B CA  1 
ATOM   3481 C C   . LEU B 1 52  ? 30.294  -1.818  28.295  1.00 24.60 ?  52  LEU B C   1 
ATOM   3482 O O   . LEU B 1 52  ? 30.696  -0.735  27.870  1.00 25.98 ?  52  LEU B O   1 
ATOM   3483 C CB  . LEU B 1 52  ? 28.140  -1.511  29.509  1.00 23.60 ?  52  LEU B CB  1 
ATOM   3484 C CG  . LEU B 1 52  ? 26.703  -1.038  29.354  1.00 26.51 ?  52  LEU B CG  1 
ATOM   3485 C CD1 . LEU B 1 52  ? 26.389  0.011   30.405  1.00 24.26 ?  52  LEU B CD1 1 
ATOM   3486 C CD2 . LEU B 1 52  ? 26.468  -0.498  27.945  1.00 25.33 ?  52  LEU B CD2 1 
ATOM   3487 N N   . LYS B 1 53  ? 31.120  -2.769  28.744  1.00 28.14 ?  53  LYS B N   1 
ATOM   3488 C CA  . LYS B 1 53  ? 32.569  -2.598  28.747  1.00 27.93 ?  53  LYS B CA  1 
ATOM   3489 C C   . LYS B 1 53  ? 33.162  -2.431  27.359  1.00 28.96 ?  53  LYS B C   1 
ATOM   3490 O O   . LYS B 1 53  ? 34.265  -1.880  27.238  1.00 25.71 ?  53  LYS B O   1 
ATOM   3491 C CB  . LYS B 1 53  ? 33.215  -3.798  29.422  1.00 30.47 ?  53  LYS B CB  1 
ATOM   3492 C CG  . LYS B 1 53  ? 32.791  -3.869  30.833  1.00 34.32 ?  53  LYS B CG  1 
ATOM   3493 C CD  . LYS B 1 53  ? 33.213  -5.135  31.466  1.00 39.49 ?  53  LYS B CD  1 
ATOM   3494 C CE  . LYS B 1 53  ? 34.325  -5.868  30.787  1.00 38.36 ?  53  LYS B CE  1 
ATOM   3495 N NZ  . LYS B 1 53  ? 34.565  -6.995  31.733  1.00 40.49 1  53  LYS B NZ  1 
ATOM   3496 N N   . VAL B 1 54  ? 32.479  -2.905  26.310  1.00 28.07 ?  54  VAL B N   1 
ATOM   3497 C CA  . VAL B 1 54  ? 32.968  -2.652  24.959  1.00 25.70 ?  54  VAL B CA  1 
ATOM   3498 C C   . VAL B 1 54  ? 33.212  -1.164  24.772  1.00 21.87 ?  54  VAL B C   1 
ATOM   3499 O O   . VAL B 1 54  ? 34.208  -0.753  24.164  1.00 26.66 ?  54  VAL B O   1 
ATOM   3500 C CB  . VAL B 1 54  ? 31.981  -3.192  23.906  1.00 26.22 ?  54  VAL B CB  1 
ATOM   3501 C CG1 . VAL B 1 54  ? 32.460  -2.819  22.499  1.00 25.73 ?  54  VAL B CG1 1 
ATOM   3502 C CG2 . VAL B 1 54  ? 31.820  -4.703  24.041  1.00 25.61 ?  54  VAL B CG2 1 
ATOM   3503 N N   . ALA B 1 55  ? 32.312  -0.334  25.313  1.00 23.46 ?  55  ALA B N   1 
ATOM   3504 C CA  . ALA B 1 55  ? 32.449  1.121   25.322  1.00 25.47 ?  55  ALA B CA  1 
ATOM   3505 C C   . ALA B 1 55  ? 32.482  1.689   23.910  1.00 24.40 ?  55  ALA B C   1 
ATOM   3506 O O   . ALA B 1 55  ? 33.038  2.761   23.679  1.00 24.57 ?  55  ALA B O   1 
ATOM   3507 C CB  . ALA B 1 55  ? 33.685  1.568   26.123  1.00 26.61 ?  55  ALA B CB  1 
ATOM   3508 N N   . ALA B 1 56  ? 31.891  0.961   22.968  1.00 22.63 ?  56  ALA B N   1 
ATOM   3509 C CA  . ALA B 1 56  ? 31.683  1.416   21.601  1.00 23.26 ?  56  ALA B CA  1 
ATOM   3510 C C   . ALA B 1 56  ? 30.553  0.573   21.042  1.00 24.28 ?  56  ALA B C   1 
ATOM   3511 O O   . ALA B 1 56  ? 30.560  -0.653  21.188  1.00 25.42 ?  56  ALA B O   1 
ATOM   3512 C CB  . ALA B 1 56  ? 32.944  1.270   20.756  1.00 22.97 ?  56  ALA B CB  1 
ATOM   3513 N N   . PHE B 1 57  ? 29.563  1.218   20.452  1.00 25.34 ?  57  PHE B N   1 
ATOM   3514 C CA  . PHE B 1 57  ? 28.327  0.528   20.113  1.00 25.84 ?  57  PHE B CA  1 
ATOM   3515 C C   . PHE B 1 57  ? 27.981  0.783   18.650  1.00 22.66 ?  57  PHE B C   1 
ATOM   3516 O O   . PHE B 1 57  ? 27.021  1.476   18.308  1.00 25.37 ?  57  PHE B O   1 
ATOM   3517 C CB  . PHE B 1 57  ? 27.254  0.930   21.103  1.00 22.57 ?  57  PHE B CB  1 
ATOM   3518 C CG  . PHE B 1 57  ? 27.692  0.675   22.514  1.00 26.63 ?  57  PHE B CG  1 
ATOM   3519 C CD1 . PHE B 1 57  ? 27.882  -0.633  22.960  1.00 21.68 ?  57  PHE B CD1 1 
ATOM   3520 C CD2 . PHE B 1 57  ? 28.037  1.726   23.352  1.00 25.09 ?  57  PHE B CD2 1 
ATOM   3521 C CE1 . PHE B 1 57  ? 28.341  -0.884  24.241  1.00 25.74 ?  57  PHE B CE1 1 
ATOM   3522 C CE2 . PHE B 1 57  ? 28.503  1.483   24.621  1.00 28.15 ?  57  PHE B CE2 1 
ATOM   3523 C CZ  . PHE B 1 57  ? 28.646  0.181   25.081  1.00 24.28 ?  57  PHE B CZ  1 
ATOM   3524 N N   . GLY B 1 58  ? 28.792  0.180   17.781  1.00 23.53 ?  58  GLY B N   1 
ATOM   3525 C CA  . GLY B 1 58  ? 28.551  0.170   16.357  1.00 21.04 ?  58  GLY B CA  1 
ATOM   3526 C C   . GLY B 1 58  ? 27.529  -0.883  15.989  1.00 23.49 ?  58  GLY B C   1 
ATOM   3527 O O   . GLY B 1 58  ? 26.795  -1.402  16.831  1.00 21.24 ?  58  GLY B O   1 
ATOM   3528 N N   . TYR B 1 59  ? 27.501  -1.219  14.707  1.00 25.56 ?  59  TYR B N   1 
ATOM   3529 C CA  . TYR B 1 59  ? 26.408  -2.021  14.179  1.00 23.65 ?  59  TYR B CA  1 
ATOM   3530 C C   . TYR B 1 59  ? 26.555  -3.475  14.604  1.00 23.25 ?  59  TYR B C   1 
ATOM   3531 O O   . TYR B 1 59  ? 27.657  -4.017  14.623  1.00 24.02 ?  59  TYR B O   1 
ATOM   3532 C CB  . TYR B 1 59  ? 26.371  -1.910  12.658  1.00 26.90 ?  59  TYR B CB  1 
ATOM   3533 C CG  . TYR B 1 59  ? 26.003  -0.533  12.153  1.00 28.70 ?  59  TYR B CG  1 
ATOM   3534 C CD1 . TYR B 1 59  ? 24.671  -0.148  12.031  1.00 29.28 ?  59  TYR B CD1 1 
ATOM   3535 C CD2 . TYR B 1 59  ? 26.987  0.382   11.798  1.00 27.46 ?  59  TYR B CD2 1 
ATOM   3536 C CE1 . TYR B 1 59  ? 24.334  1.102   11.577  1.00 30.40 ?  59  TYR B CE1 1 
ATOM   3537 C CE2 . TYR B 1 59  ? 26.658  1.639   11.340  1.00 30.77 ?  59  TYR B CE2 1 
ATOM   3538 C CZ  . TYR B 1 59  ? 25.332  1.997   11.225  1.00 36.16 ?  59  TYR B CZ  1 
ATOM   3539 O OH  . TYR B 1 59  ? 25.007  3.252   10.760  1.00 33.82 ?  59  TYR B OH  1 
ATOM   3540 N N   . GLU B 1 60  ? 25.427  -4.117  14.915  1.00 25.33 ?  60  GLU B N   1 
ATOM   3541 C CA  . GLU B 1 60  ? 25.401  -5.489  15.408  1.00 26.59 ?  60  GLU B CA  1 
ATOM   3542 C C   . GLU B 1 60  ? 24.777  -6.452  14.406  1.00 27.82 ?  60  GLU B C   1 
ATOM   3543 O O   . GLU B 1 60  ? 23.761  -6.134  13.786  1.00 28.47 ?  60  GLU B O   1 
ATOM   3544 C CB  . GLU B 1 60  ? 24.588  -5.576  16.689  1.00 25.03 ?  60  GLU B CB  1 
ATOM   3545 C CG  . GLU B 1 60  ? 24.937  -4.553  17.714  1.00 27.83 ?  60  GLU B CG  1 
ATOM   3546 C CD  . GLU B 1 60  ? 25.241  -5.207  19.039  1.00 27.94 ?  60  GLU B CD  1 
ATOM   3547 O OE1 . GLU B 1 60  ? 25.824  -4.510  19.890  1.00 24.54 ?  60  GLU B OE1 1 
ATOM   3548 O OE2 . GLU B 1 60  ? 24.891  -6.412  19.215  1.00 26.62 -1 60  GLU B OE2 1 
ATOM   3549 N N   . SER B 1 61  ? 25.365  -7.646  14.286  1.00 26.11 ?  61  SER B N   1 
ATOM   3550 C CA  . SER B 1 61  ? 24.733  -8.774  13.617  1.00 25.44 ?  61  SER B CA  1 
ATOM   3551 C C   . SER B 1 61  ? 23.933  -9.591  14.636  1.00 24.20 ?  61  SER B C   1 
ATOM   3552 O O   . SER B 1 61  ? 24.039  -9.393  15.851  1.00 24.75 ?  61  SER B O   1 
ATOM   3553 C CB  . SER B 1 61  ? 25.791  -9.635  12.911  1.00 28.84 ?  61  SER B CB  1 
ATOM   3554 O OG  . SER B 1 61  ? 26.550  -10.401 13.832  1.00 30.61 ?  61  SER B OG  1 
ATOM   3555 N N   . VAL B 1 62  ? 23.104  -10.498 14.136  1.00 24.56 ?  62  VAL B N   1 
ATOM   3556 C CA  . VAL B 1 62  ? 22.381  -11.444 15.000  1.00 24.22 ?  62  VAL B CA  1 
ATOM   3557 C C   . VAL B 1 62  ? 23.111  -12.723 14.976  1.00 25.74 ?  62  VAL B C   1 
ATOM   3558 O O   . VAL B 1 62  ? 23.183  -13.415 13.919  1.00 24.84 ?  62  VAL B O   1 
ATOM   3559 C CB  . VAL B 1 62  ? 20.918  -11.625 14.563  1.00 26.27 ?  62  VAL B CB  1 
ATOM   3560 C CG1 . VAL B 1 62  ? 20.259  -12.541 15.570  1.00 24.53 ?  62  VAL B CG1 1 
ATOM   3561 C CG2 . VAL B 1 62  ? 20.184  -10.303 14.502  1.00 25.71 ?  62  VAL B CG2 1 
ATOM   3562 N N   . PRO B 1 63  ? 23.722  -13.195 16.075  1.00 24.34 ?  63  PRO B N   1 
ATOM   3563 C CA  . PRO B 1 63  ? 24.516  -14.400 16.084  1.00 23.85 ?  63  PRO B CA  1 
ATOM   3564 C C   . PRO B 1 63  ? 23.654  -15.647 16.249  1.00 27.30 ?  63  PRO B C   1 
ATOM   3565 O O   . PRO B 1 63  ? 22.534  -15.605 16.766  1.00 25.29 ?  63  PRO B O   1 
ATOM   3566 C CB  . PRO B 1 63  ? 25.443  -14.211 17.285  1.00 24.66 ?  63  PRO B CB  1 
ATOM   3567 C CG  . PRO B 1 63  ? 24.623  -13.381 18.250  1.00 23.33 ?  63  PRO B CG  1 
ATOM   3568 C CD  . PRO B 1 63  ? 23.672  -12.528 17.405  1.00 21.24 ?  63  PRO B CD  1 
ATOM   3569 N N   . ALA B 1 64  ? 24.211  -16.768 15.788  1.00 27.00 ?  64  ALA B N   1 
ATOM   3570 C CA  . ALA B 1 64  ? 23.540  -18.060 15.917  1.00 29.92 ?  64  ALA B CA  1 
ATOM   3571 C C   . ALA B 1 64  ? 23.201  -18.384 17.365  1.00 27.64 ?  64  ALA B C   1 
ATOM   3572 O O   . ALA B 1 64  ? 22.192  -19.056 17.634  1.00 26.64 ?  64  ALA B O   1 
ATOM   3573 C CB  . ALA B 1 64  ? 24.419  -19.158 15.315  1.00 30.78 ?  64  ALA B CB  1 
ATOM   3574 N N   . GLU B 1 65  ? 24.023  -17.908 18.312  1.00 25.27 ?  65  GLU B N   1 
ATOM   3575 C CA  . GLU B 1 65  ? 23.772  -18.165 19.727  1.00 26.74 ?  65  GLU B CA  1 
ATOM   3576 C C   . GLU B 1 65  ? 22.457  -17.553 20.192  1.00 25.84 ?  65  GLU B C   1 
ATOM   3577 O O   . GLU B 1 65  ? 21.859  -18.043 21.157  1.00 26.33 ?  65  GLU B O   1 
ATOM   3578 C CB  . GLU B 1 65  ? 24.927  -17.628 20.574  1.00 29.04 ?  65  GLU B CB  1 
ATOM   3579 C CG  . GLU B 1 65  ? 26.278  -18.264 20.262  1.00 31.05 ?  65  GLU B CG  1 
ATOM   3580 C CD  . GLU B 1 65  ? 27.059  -17.509 19.191  1.00 37.09 ?  65  GLU B CD  1 
ATOM   3581 O OE1 . GLU B 1 65  ? 28.249  -17.204 19.422  1.00 47.08 ?  65  GLU B OE1 1 
ATOM   3582 O OE2 . GLU B 1 65  ? 26.487  -17.216 18.121  1.00 33.83 -1 65  GLU B OE2 1 
ATOM   3583 N N   . TYR B 1 66  ? 21.996  -16.484 19.532  1.00 24.29 ?  66  TYR B N   1 
ATOM   3584 C CA  . TYR B 1 66  ? 20.692  -15.912 19.874  1.00 22.95 ?  66  TYR B CA  1 
ATOM   3585 C C   . TYR B 1 66  ? 19.581  -16.912 19.589  1.00 23.13 ?  66  TYR B C   1 
ATOM   3586 O O   . TYR B 1 66  ? 18.728  -17.179 20.445  1.00 25.77 ?  66  TYR B O   1 
ATOM   3587 C CB  . TYR B 1 66  ? 20.465  -14.617 19.089  1.00 22.53 ?  66  TYR B CB  1 
ATOM   3588 C CG  . TYR B 1 66  ? 19.164  -13.908 19.426  1.00 17.52 ?  66  TYR B CG  1 
ATOM   3589 C CD1 . TYR B 1 66  ? 19.060  -13.108 20.558  1.00 25.98 ?  66  TYR B CD1 1 
ATOM   3590 C CD2 . TYR B 1 66  ? 18.049  -14.048 18.620  1.00 23.78 ?  66  TYR B CD2 1 
ATOM   3591 C CE1 . TYR B 1 66  ? 17.879  -12.452 20.864  1.00 26.67 ?  66  TYR B CE1 1 
ATOM   3592 C CE2 . TYR B 1 66  ? 16.860  -13.408 18.926  1.00 21.29 ?  66  TYR B CE2 1 
ATOM   3593 C CZ  . TYR B 1 66  ? 16.778  -12.624 20.049  1.00 24.21 ?  66  TYR B CZ  1 
ATOM   3594 O OH  . TYR B 1 66  ? 15.592  -11.975 20.341  1.00 27.85 ?  66  TYR B OH  1 
ATOM   3595 N N   . TYR B 1 67  ? 19.594  -17.496 18.390  1.00 21.76 ?  67  TYR B N   1 
ATOM   3596 C CA  . TYR B 1 67  ? 18.553  -18.440 18.012  1.00 21.96 ?  67  TYR B CA  1 
ATOM   3597 C C   . TYR B 1 67  ? 18.669  -19.748 18.779  1.00 25.15 ?  67  TYR B C   1 
ATOM   3598 O O   . TYR B 1 67  ? 17.646  -20.368 19.090  1.00 22.85 ?  67  TYR B O   1 
ATOM   3599 C CB  . TYR B 1 67  ? 18.606  -18.681 16.512  1.00 25.07 ?  67  TYR B CB  1 
ATOM   3600 C CG  . TYR B 1 67  ? 18.398  -17.377 15.737  1.00 26.62 ?  67  TYR B CG  1 
ATOM   3601 C CD1 . TYR B 1 67  ? 17.403  -16.479 16.119  1.00 24.24 ?  67  TYR B CD1 1 
ATOM   3602 C CD2 . TYR B 1 67  ? 19.204  -17.033 14.661  1.00 30.42 ?  67  TYR B CD2 1 
ATOM   3603 C CE1 . TYR B 1 67  ? 17.199  -15.286 15.444  1.00 23.75 ?  67  TYR B CE1 1 
ATOM   3604 C CE2 . TYR B 1 67  ? 19.000  -15.836 13.974  1.00 30.37 ?  67  TYR B CE2 1 
ATOM   3605 C CZ  . TYR B 1 67  ? 17.992  -14.970 14.378  1.00 27.30 ?  67  TYR B CZ  1 
ATOM   3606 O OH  . TYR B 1 67  ? 17.773  -13.776 13.706  1.00 26.57 ?  67  TYR B OH  1 
ATOM   3607 N N   . LYS B 1 68  ? 19.894  -20.194 19.067  1.00 24.03 ?  68  LYS B N   1 
ATOM   3608 C CA  . LYS B 1 68  ? 20.046  -21.381 19.904  1.00 28.28 ?  68  LYS B CA  1 
ATOM   3609 C C   . LYS B 1 68  ? 19.484  -21.141 21.297  1.00 26.83 ?  68  LYS B C   1 
ATOM   3610 O O   . LYS B 1 68  ? 18.840  -22.026 21.871  1.00 27.16 ?  68  LYS B O   1 
ATOM   3611 C CB  . LYS B 1 68  ? 21.505  -21.813 20.004  1.00 29.98 ?  68  LYS B CB  1 
ATOM   3612 C CG  . LYS B 1 68  ? 21.610  -23.163 20.733  1.00 35.14 ?  68  LYS B CG  1 
ATOM   3613 C CD  . LYS B 1 68  ? 22.986  -23.479 21.275  1.00 41.68 ?  68  LYS B CD  1 
ATOM   3614 C CE  . LYS B 1 68  ? 23.073  -24.972 21.626  1.00 44.92 ?  68  LYS B CE  1 
ATOM   3615 N NZ  . LYS B 1 68  ? 23.213  -25.158 23.095  1.00 40.11 1  68  LYS B NZ  1 
ATOM   3616 N N   . ALA B 1 69  ? 19.694  -19.949 21.845  1.00 25.36 ?  69  ALA B N   1 
ATOM   3617 C CA  . ALA B 1 69  ? 19.144  -19.609 23.174  1.00 25.01 ?  69  ALA B CA  1 
ATOM   3618 C C   . ALA B 1 69  ? 17.611  -19.673 23.134  1.00 24.74 ?  69  ALA B C   1 
ATOM   3619 O O   . ALA B 1 69  ? 17.014  -20.276 24.005  1.00 22.82 ?  69  ALA B O   1 
ATOM   3620 C CB  . ALA B 1 69  ? 19.648  -18.278 23.634  1.00 23.08 ?  69  ALA B CB  1 
ATOM   3621 N N   . VAL B 1 70  ? 17.027  -19.072 22.109  1.00 21.86 ?  70  VAL B N   1 
ATOM   3622 C CA  . VAL B 1 70  ? 15.549  -19.081 21.970  1.00 23.48 ?  70  VAL B CA  1 
ATOM   3623 C C   . VAL B 1 70  ? 15.052  -20.526 21.870  1.00 22.82 ?  70  VAL B C   1 
ATOM   3624 O O   . VAL B 1 70  ? 14.142  -20.878 22.599  1.00 24.77 ?  70  VAL B O   1 
ATOM   3625 C CB  . VAL B 1 70  ? 15.118  -18.215 20.774  1.00 23.65 ?  70  VAL B CB  1 
ATOM   3626 C CG1 . VAL B 1 70  ? 13.684  -18.457 20.353  1.00 21.60 ?  70  VAL B CG1 1 
ATOM   3627 C CG2 . VAL B 1 70  ? 15.394  -16.741 21.002  1.00 22.20 ?  70  VAL B CG2 1 
ATOM   3628 N N   . ALA B 1 71  ? 15.663  -21.322 21.009  1.00 22.77 ?  71  ALA B N   1 
ATOM   3629 C CA  . ALA B 1 71  ? 15.262  -22.729 20.818  1.00 22.05 ?  71  ALA B CA  1 
ATOM   3630 C C   . ALA B 1 71  ? 15.419  -23.534 22.112  1.00 26.14 ?  71  ALA B C   1 
ATOM   3631 O O   . ALA B 1 71  ? 14.527  -24.299 22.430  1.00 25.41 ?  71  ALA B O   1 
ATOM   3632 C CB  . ALA B 1 71  ? 16.066  -23.327 19.718  1.00 26.68 ?  71  ALA B CB  1 
ATOM   3633 N N   . ASP B 1 72  ? 16.558  -23.369 22.784  1.00 24.86 ?  72  ASP B N   1 
ATOM   3634 C CA  . ASP B 1 72  ? 16.754  -24.064 24.056  1.00 28.13 ?  72  ASP B CA  1 
ATOM   3635 C C   . ASP B 1 72  ? 15.676  -23.689 25.062  1.00 28.67 ?  72  ASP B C   1 
ATOM   3636 O O   . ASP B 1 72  ? 15.104  -24.554 25.739  1.00 27.15 ?  72  ASP B O   1 
ATOM   3637 C CB  . ASP B 1 72  ? 18.130  -23.726 24.630  1.00 25.11 ?  72  ASP B CB  1 
ATOM   3638 C CG  . ASP B 1 72  ? 19.254  -24.473 23.946  1.00 31.19 ?  72  ASP B CG  1 
ATOM   3639 O OD1 . ASP B 1 72  ? 18.971  -25.334 23.100  1.00 32.59 ?  72  ASP B OD1 1 
ATOM   3640 O OD2 . ASP B 1 72  ? 20.428  -24.187 24.268  1.00 34.49 -1 72  ASP B OD2 1 
ATOM   3641 N N   . TRP B 1 73  ? 15.416  -22.400 25.188  1.00 24.83 ?  73  TRP B N   1 
ATOM   3642 C CA  . TRP B 1 73  ? 14.394  -21.944 26.152  1.00 22.79 ?  73  TRP B CA  1 
ATOM   3643 C C   . TRP B 1 73  ? 13.044  -22.591 25.839  1.00 24.03 ?  73  TRP B C   1 
ATOM   3644 O O   . TRP B 1 73  ? 12.438  -23.138 26.742  1.00 26.67 ?  73  TRP B O   1 
ATOM   3645 C CB  . TRP B 1 73  ? 14.301  -20.428 26.108  1.00 20.75 ?  73  TRP B CB  1 
ATOM   3646 C CG  . TRP B 1 73  ? 13.204  -19.878 26.962  1.00 24.19 ?  73  TRP B CG  1 
ATOM   3647 C CD1 . TRP B 1 73  ? 11.938  -19.558 26.571  1.00 25.91 ?  73  TRP B CD1 1 
ATOM   3648 C CD2 . TRP B 1 73  ? 13.282  -19.566 28.360  1.00 25.11 ?  73  TRP B CD2 1 
ATOM   3649 N NE1 . TRP B 1 73  ? 11.224  -19.079 27.631  1.00 26.76 ?  73  TRP B NE1 1 
ATOM   3650 C CE2 . TRP B 1 73  ? 12.023  -19.065 28.741  1.00 24.05 ?  73  TRP B CE2 1 
ATOM   3651 C CE3 . TRP B 1 73  ? 14.289  -19.653 29.324  1.00 24.55 ?  73  TRP B CE3 1 
ATOM   3652 C CZ2 . TRP B 1 73  ? 11.749  -18.667 30.045  1.00 27.48 ?  73  TRP B CZ2 1 
ATOM   3653 C CZ3 . TRP B 1 73  ? 14.016  -19.260 30.612  1.00 25.62 ?  73  TRP B CZ3 1 
ATOM   3654 C CH2 . TRP B 1 73  ? 12.760  -18.780 30.968  1.00 26.06 ?  73  TRP B CH2 1 
ATOM   3655 N N   . GLU B 1 74  ? 12.613  -22.507 24.586  1.00 24.38 ?  74  GLU B N   1 
ATOM   3656 C CA  . GLU B 1 74  ? 11.279  -23.021 24.202  1.00 25.87 ?  74  GLU B CA  1 
ATOM   3657 C C   . GLU B 1 74  ? 11.194  -24.524 24.483  1.00 27.87 ?  74  GLU B C   1 
ATOM   3658 O O   . GLU B 1 74  ? 10.132  -25.010 24.822  1.00 28.55 ?  74  GLU B O   1 
ATOM   3659 C CB  . GLU B 1 74  ? 11.064  -22.725 22.723  1.00 24.21 ?  74  GLU B CB  1 
ATOM   3660 C CG  . GLU B 1 74  ? 10.839  -21.267 22.399  1.00 23.28 ?  74  GLU B CG  1 
ATOM   3661 C CD  . GLU B 1 74  ? 9.480   -20.768 22.842  1.00 28.04 ?  74  GLU B CD  1 
ATOM   3662 O OE1 . GLU B 1 74  ? 9.373   -20.341 23.989  1.00 25.77 ?  74  GLU B OE1 1 
ATOM   3663 O OE2 . GLU B 1 74  ? 8.544   -20.826 22.036  1.00 23.21 -1 74  GLU B OE2 1 
ATOM   3664 N N   . GLU B 1 75  ? 12.305  -25.216 24.323  1.00 25.23 ?  75  GLU B N   1 
ATOM   3665 C CA  . GLU B 1 75  ? 12.320  -26.676 24.559  1.00 26.67 ?  75  GLU B CA  1 
ATOM   3666 C C   . GLU B 1 75  ? 12.221  -26.967 26.055  1.00 29.03 ?  75  GLU B C   1 
ATOM   3667 O O   . GLU B 1 75  ? 11.430  -27.799 26.432  1.00 31.38 ?  75  GLU B O   1 
ATOM   3668 C CB  . GLU B 1 75  ? 13.615  -27.260 24.029  1.00 31.34 ?  75  GLU B CB  1 
ATOM   3669 C CG  . GLU B 1 75  ? 13.831  -28.723 24.327  1.00 33.55 ?  75  GLU B CG  1 
ATOM   3670 C CD  . GLU B 1 75  ? 14.923  -29.300 23.450  1.00 34.11 ?  75  GLU B CD  1 
ATOM   3671 O OE1 . GLU B 1 75  ? 14.620  -30.197 22.662  1.00 43.39 ?  75  GLU B OE1 1 
ATOM   3672 O OE2 . GLU B 1 75  ? 16.058  -28.816 23.534  1.00 36.77 -1 75  GLU B OE2 1 
ATOM   3673 N N   . ILE B 1 76  ? 12.991  -26.267 26.863  1.00 29.42 ?  76  ILE B N   1 
ATOM   3674 C CA  . ILE B 1 76  ? 13.045  -26.596 28.313  1.00 29.08 ?  76  ILE B CA  1 
ATOM   3675 C C   . ILE B 1 76  ? 11.811  -26.091 29.041  1.00 34.41 ?  76  ILE B C   1 
ATOM   3676 O O   . ILE B 1 76  ? 11.251  -26.846 29.827  1.00 34.05 ?  76  ILE B O   1 
ATOM   3677 C CB  . ILE B 1 76  ? 14.334  -26.030 28.942  1.00 28.54 ?  76  ILE B CB  1 
ATOM   3678 C CG1 . ILE B 1 76  ? 15.581  -26.690 28.352  1.00 29.63 ?  76  ILE B CG1 1 
ATOM   3679 C CG2 . ILE B 1 76  ? 14.312  -26.124 30.459  1.00 30.78 ?  76  ILE B CG2 1 
ATOM   3680 C CD1 . ILE B 1 76  ? 16.866  -25.994 28.713  1.00 31.28 ?  76  ILE B CD1 1 
ATOM   3681 N N   . GLU B 1 77  ? 11.320  -24.919 28.690  1.00 29.53 ?  77  GLU B N   1 
ATOM   3682 C CA  . GLU B 1 77  ? 10.168  -24.379 29.435  1.00 33.63 ?  77  GLU B CA  1 
ATOM   3683 C C   . GLU B 1 77  ? 8.851   -24.899 28.867  1.00 35.88 ?  77  GLU B C   1 
ATOM   3684 O O   . GLU B 1 77  ? 7.978   -25.166 29.674  1.00 36.43 ?  77  GLU B O   1 
ATOM   3685 C CB  . GLU B 1 77  ? 10.233  -22.856 29.434  1.00 30.94 ?  77  GLU B CB  1 
ATOM   3686 C CG  . GLU B 1 77  ? 11.375  -22.323 30.267  1.00 31.11 ?  77  GLU B CG  1 
ATOM   3687 C CD  . GLU B 1 77  ? 11.179  -22.466 31.763  1.00 33.04 ?  77  GLU B CD  1 
ATOM   3688 O OE1 . GLU B 1 77  ? 12.178  -22.621 32.464  1.00 34.77 ?  77  GLU B OE1 1 
ATOM   3689 O OE2 . GLU B 1 77  ? 10.029  -22.421 32.216  1.00 33.74 -1 77  GLU B OE2 1 
ATOM   3690 N N   . HIS B 1 78  ? 8.745   -25.064 27.548  1.00 37.30 ?  78  HIS B N   1 
ATOM   3691 C CA  . HIS B 1 78  ? 7.446   -25.413 26.924  1.00 39.96 ?  78  HIS B CA  1 
ATOM   3692 C C   . HIS B 1 78  ? 7.426   -26.750 26.182  1.00 41.94 ?  78  HIS B C   1 
ATOM   3693 O O   . HIS B 1 78  ? 6.397   -27.016 25.580  1.00 40.73 ?  78  HIS B O   1 
ATOM   3694 C CB  . HIS B 1 78  ? 6.994   -24.241 26.051  1.00 35.98 ?  78  HIS B CB  1 
ATOM   3695 C CG  . HIS B 1 78  ? 7.036   -22.970 26.810  1.00 35.72 ?  78  HIS B CG  1 
ATOM   3696 N ND1 . HIS B 1 78  ? 6.352   -22.819 27.989  1.00 38.20 ?  78  HIS B ND1 1 
ATOM   3697 C CD2 . HIS B 1 78  ? 7.732   -21.838 26.620  1.00 32.33 ?  78  HIS B CD2 1 
ATOM   3698 C CE1 . HIS B 1 78  ? 6.588   -21.629 28.478  1.00 36.60 ?  78  HIS B CE1 1 
ATOM   3699 N NE2 . HIS B 1 78  ? 7.428   -21.021 27.660  1.00 33.19 ?  78  HIS B NE2 1 
ATOM   3700 N N   . ARG B 1 79  ? 8.528   -27.500 26.178  1.00 30.00 ?  79  ARG B N   1 
ATOM   3701 C CA  . ARG B 1 79  ? 8.579   -28.847 25.552  1.00 30.00 ?  79  ARG B CA  1 
ATOM   3702 C C   . ARG B 1 79  ? 8.358   -28.720 24.054  1.00 30.00 ?  79  ARG B C   1 
ATOM   3703 O O   . ARG B 1 79  ? 7.733   -29.605 23.490  1.00 30.00 ?  79  ARG B O   1 
ATOM   3704 C CB  . ARG B 1 79  ? 7.637   -29.812 26.272  1.00 30.00 ?  79  ARG B CB  1 
ATOM   3705 C CG  . ARG B 1 79  ? 8.139   -30.243 27.641  1.00 30.00 ?  79  ARG B CG  1 
ATOM   3706 C CD  . ARG B 1 79  ? 7.148   -29.916 28.735  1.00 30.00 ?  79  ARG B CD  1 
ATOM   3707 N NE  . ARG B 1 79  ? 7.803   -29.337 29.896  1.00 30.00 ?  79  ARG B NE  1 
ATOM   3708 C CZ  . ARG B 1 79  ? 7.769   -29.854 31.118  1.00 30.00 ?  79  ARG B CZ  1 
ATOM   3709 N NH1 . ARG B 1 79  ? 7.107   -30.975 31.347  1.00 30.00 1  79  ARG B NH1 1 
ATOM   3710 N NH2 . ARG B 1 79  ? 8.398   -29.248 32.108  1.00 30.00 ?  79  ARG B NH2 1 
ATOM   3711 N N   . ALA B 1 80  ? 8.907   -27.657 23.466  1.00 44.11 ?  80  ALA B N   1 
ATOM   3712 C CA  . ALA B 1 80  ? 8.698   -27.370 22.037  1.00 39.36 ?  80  ALA B CA  1 
ATOM   3713 C C   . ALA B 1 80  ? 9.924   -26.687 21.458  1.00 33.39 ?  80  ALA B C   1 
ATOM   3714 O O   . ALA B 1 80  ? 10.071  -25.508 21.649  1.00 37.27 ?  80  ALA B O   1 
ATOM   3715 C CB  . ALA B 1 80  ? 7.514   -26.467 21.929  1.00 40.13 ?  80  ALA B CB  1 
ATOM   3716 N N   . ARG B 1 81  ? 10.767  -27.446 20.787  1.00 29.27 ?  81  ARG B N   1 
ATOM   3717 C CA  . ARG B 1 81  ? 12.004  -26.841 20.293  1.00 31.81 ?  81  ARG B CA  1 
ATOM   3718 C C   . ARG B 1 81  ? 11.805  -26.376 18.851  1.00 31.70 ?  81  ARG B C   1 
ATOM   3719 O O   . ARG B 1 81  ? 11.662  -27.241 18.004  1.00 29.76 ?  81  ARG B O   1 
ATOM   3720 C CB  . ARG B 1 81  ? 13.212  -27.754 20.425  1.00 30.04 ?  81  ARG B CB  1 
ATOM   3721 C CG  . ARG B 1 81  ? 14.514  -27.071 20.041  1.00 30.17 ?  81  ARG B CG  1 
ATOM   3722 C CD  . ARG B 1 81  ? 15.689  -28.012 19.883  1.00 31.86 ?  81  ARG B CD  1 
ATOM   3723 N NE  . ARG B 1 81  ? 16.880  -27.226 19.623  1.00 30.61 ?  81  ARG B NE  1 
ATOM   3724 C CZ  . ARG B 1 81  ? 17.582  -26.638 20.570  1.00 30.17 ?  81  ARG B CZ  1 
ATOM   3725 N NH1 . ARG B 1 81  ? 17.219  -26.787 21.829  1.00 33.81 1  81  ARG B NH1 1 
ATOM   3726 N NH2 . ARG B 1 81  ? 18.647  -25.925 20.270  1.00 35.07 ?  81  ARG B NH2 1 
ATOM   3727 N N   . PRO B 1 82  ? 11.788  -25.059 18.528  1.00 28.11 ?  82  PRO B N   1 
ATOM   3728 C CA  . PRO B 1 82  ? 11.758  -24.631 17.167  1.00 25.77 ?  82  PRO B CA  1 
ATOM   3729 C C   . PRO B 1 82  ? 13.098  -24.905 16.476  1.00 28.94 ?  82  PRO B C   1 
ATOM   3730 O O   . PRO B 1 82  ? 14.102  -25.014 17.102  1.00 27.08 ?  82  PRO B O   1 
ATOM   3731 C CB  . PRO B 1 82  ? 11.680  -23.113 17.239  1.00 26.96 ?  82  PRO B CB  1 
ATOM   3732 C CG  . PRO B 1 82  ? 12.291  -22.743 18.540  1.00 26.32 ?  82  PRO B CG  1 
ATOM   3733 C CD  . PRO B 1 82  ? 11.837  -23.870 19.427  1.00 25.83 ?  82  PRO B CD  1 
ATOM   3734 N N   . LYS B 1 83  ? 13.027  -25.055 15.169  1.00 26.18 ?  83  LYS B N   1 
ATOM   3735 C CA  . LYS B 1 83  ? 14.282  -25.138 14.424  1.00 31.91 ?  83  LYS B CA  1 
ATOM   3736 C C   . LYS B 1 83  ? 14.873  -23.733 14.494  1.00 30.67 ?  83  LYS B C   1 
ATOM   3737 O O   . LYS B 1 83  ? 14.137  -22.779 14.373  1.00 30.11 ?  83  LYS B O   1 
ATOM   3738 C CB  . LYS B 1 83  ? 14.028  -25.639 13.007  1.00 29.32 ?  83  LYS B CB  1 
ATOM   3739 C CG  . LYS B 1 83  ? 13.699  -27.119 12.898  1.00 32.37 ?  83  LYS B CG  1 
ATOM   3740 C CD  . LYS B 1 83  ? 13.282  -27.546 11.511  1.00 37.19 ?  83  LYS B CD  1 
ATOM   3741 C CE  . LYS B 1 83  ? 14.409  -28.123 10.685  1.00 43.38 ?  83  LYS B CE  1 
ATOM   3742 N NZ  . LYS B 1 83  ? 13.894  -28.825 9.485   1.00 48.13 1  83  LYS B NZ  1 
ATOM   3743 N N   . GLU B 1 84  ? 16.176  -23.635 14.716  1.00 30.11 ?  84  GLU B N   1 
ATOM   3744 C CA  . GLU B 1 84  ? 16.832  -22.310 14.790  1.00 31.10 ?  84  GLU B CA  1 
ATOM   3745 C C   . GLU B 1 84  ? 16.692  -21.536 13.466  1.00 32.10 ?  84  GLU B C   1 
ATOM   3746 O O   . GLU B 1 84  ? 16.665  -20.326 13.511  1.00 28.75 ?  84  GLU B O   1 
ATOM   3747 C CB  . GLU B 1 84  ? 18.290  -22.487 15.204  1.00 32.17 ?  84  GLU B CB  1 
ATOM   3748 C CG  . GLU B 1 84  ? 18.436  -22.789 16.681  1.00 29.89 ?  84  GLU B CG  1 
ATOM   3749 C CD  . GLU B 1 84  ? 19.604  -23.669 17.080  1.00 39.69 ?  84  GLU B CD  1 
ATOM   3750 O OE1 . GLU B 1 84  ? 19.374  -24.662 17.785  1.00 36.90 ?  84  GLU B OE1 1 
ATOM   3751 O OE2 . GLU B 1 84  ? 20.739  -23.347 16.703  1.00 41.85 -1 84  GLU B OE2 1 
ATOM   3752 N N   . ASP B 1 85  ? 16.637  -22.243 12.338  1.00 35.20 ?  85  ASP B N   1 
ATOM   3753 C CA  . ASP B 1 85  ? 16.468  -21.589 11.017  1.00 37.57 ?  85  ASP B CA  1 
ATOM   3754 C C   . ASP B 1 85  ? 15.126  -20.844 10.941  1.00 29.02 ?  85  ASP B C   1 
ATOM   3755 O O   . ASP B 1 85  ? 15.033  -19.927 10.166  1.00 28.37 ?  85  ASP B O   1 
ATOM   3756 C CB  . ASP B 1 85  ? 16.696  -22.561 9.851   1.00 43.81 ?  85  ASP B CB  1 
ATOM   3757 C CG  . ASP B 1 85  ? 16.019  -23.910 9.980   1.00 52.28 ?  85  ASP B CG  1 
ATOM   3758 O OD1 . ASP B 1 85  ? 16.369  -24.649 10.910  1.00 57.38 ?  85  ASP B OD1 1 
ATOM   3759 O OD2 . ASP B 1 85  ? 15.181  -24.221 9.126   1.00 58.11 -1 85  ASP B OD2 1 
ATOM   3760 N N   . TRP B 1 86  ? 14.125  -21.278 11.690  1.00 26.01 ?  86  TRP B N   1 
ATOM   3761 C CA  . TRP B 1 86  ? 12.781  -20.642 11.654  1.00 24.54 ?  86  TRP B CA  1 
ATOM   3762 C C   . TRP B 1 86  ? 12.778  -19.299 12.378  1.00 23.89 ?  86  TRP B C   1 
ATOM   3763 O O   . TRP B 1 86  ? 11.784  -18.593 12.264  1.00 22.57 ?  86  TRP B O   1 
ATOM   3764 C CB  . TRP B 1 86  ? 11.803  -21.533 12.404  1.00 25.02 ?  86  TRP B CB  1 
ATOM   3765 C CG  . TRP B 1 86  ? 11.506  -22.868 11.813  1.00 27.65 ?  86  TRP B CG  1 
ATOM   3766 C CD1 . TRP B 1 86  ? 11.894  -23.365 10.606  1.00 28.31 ?  86  TRP B CD1 1 
ATOM   3767 C CD2 . TRP B 1 86  ? 10.725  -23.891 12.444  1.00 27.75 ?  86  TRP B CD2 1 
ATOM   3768 N NE1 . TRP B 1 86  ? 11.402  -24.630 10.444  1.00 26.18 ?  86  TRP B NE1 1 
ATOM   3769 C CE2 . TRP B 1 86  ? 10.683  -24.980 11.554  1.00 28.01 ?  86  TRP B CE2 1 
ATOM   3770 C CE3 . TRP B 1 86  ? 10.062  -23.987 13.669  1.00 25.35 ?  86  TRP B CE3 1 
ATOM   3771 C CZ2 . TRP B 1 86  ? 10.000  -26.153 11.858  1.00 27.72 ?  86  TRP B CZ2 1 
ATOM   3772 C CZ3 . TRP B 1 86  ? 9.386   -25.146 13.967  1.00 28.84 ?  86  TRP B CZ3 1 
ATOM   3773 C CH2 . TRP B 1 86  ? 9.359   -26.213 13.072  1.00 28.10 ?  86  TRP B CH2 1 
ATOM   3774 N N   . CYS B 1 87  ? 13.874  -18.931 13.020  1.00 27.10 ?  87  CYS B N   1 
ATOM   3775 C CA  . CYS B 1 87  ? 13.898  -17.827 13.969  1.00 23.74 ?  87  CYS B CA  1 
ATOM   3776 C C   . CYS B 1 87  ? 14.476  -16.581 13.315  1.00 28.02 ?  87  CYS B C   1 
ATOM   3777 O O   . CYS B 1 87  ? 15.489  -16.647 12.612  1.00 26.77 ?  87  CYS B O   1 
ATOM   3778 C CB  . CYS B 1 87  ? 14.721  -18.199 15.205  1.00 23.85 ?  87  CYS B CB  1 
ATOM   3779 S SG  . CYS B 1 87  ? 13.998  -19.520 16.253  1.00 24.39 ?  87  CYS B SG  1 
ATOM   3780 N N   . VAL B 1 88  ? 13.825  -15.446 13.552  1.00 20.99 ?  88  VAL B N   1 
ATOM   3781 C CA  . VAL B 1 88  ? 14.248  -14.158 13.009  1.00 25.65 ?  88  VAL B CA  1 
ATOM   3782 C C   . VAL B 1 88  ? 14.158  -13.130 14.121  1.00 22.24 ?  88  VAL B C   1 
ATOM   3783 O O   . VAL B 1 88  ? 13.089  -12.962 14.714  1.00 23.57 ?  88  VAL B O   1 
ATOM   3784 C CB  . VAL B 1 88  ? 13.366  -13.697 11.828  1.00 23.07 ?  88  VAL B CB  1 
ATOM   3785 C CG1 . VAL B 1 88  ? 13.817  -12.309 11.331  1.00 23.49 ?  88  VAL B CG1 1 
ATOM   3786 C CG2 . VAL B 1 88  ? 13.382  -14.711 10.706  1.00 26.66 ?  88  VAL B CG2 1 
ATOM   3787 N N   . PHE B 1 89  ? 15.256  -12.418 14.378  1.00 20.77 ?  89  PHE B N   1 
ATOM   3788 C CA  . PHE B 1 89  ? 15.225  -11.320 15.345  1.00 23.13 ?  89  PHE B CA  1 
ATOM   3789 C C   . PHE B 1 89  ? 14.298  -10.190 14.901  1.00 22.07 ?  89  PHE B C   1 
ATOM   3790 O O   . PHE B 1 89  ? 14.272  -9.798  13.730  1.00 20.45 ?  89  PHE B O   1 
ATOM   3791 C CB  . PHE B 1 89  ? 16.634  -10.753 15.566  1.00 20.69 ?  89  PHE B CB  1 
ATOM   3792 C CG  . PHE B 1 89  ? 16.671  -9.606  16.548  1.00 23.98 ?  89  PHE B CG  1 
ATOM   3793 C CD1 . PHE B 1 89  ? 16.494  -8.294  16.119  1.00 21.52 ?  89  PHE B CD1 1 
ATOM   3794 C CD2 . PHE B 1 89  ? 16.841  -9.844  17.897  1.00 22.09 ?  89  PHE B CD2 1 
ATOM   3795 C CE1 . PHE B 1 89  ? 16.506  -7.232  17.023  1.00 19.88 ?  89  PHE B CE1 1 
ATOM   3796 C CE2 . PHE B 1 89  ? 16.854  -8.792  18.807  1.00 21.98 ?  89  PHE B CE2 1 
ATOM   3797 C CZ  . PHE B 1 89  ? 16.683  -7.485  18.367  1.00 22.00 ?  89  PHE B CZ  1 
ATOM   3798 N N   . ALA B 1 90  ? 13.556  -9.636  15.861  1.00 17.35 ?  90  ALA B N   1 
ATOM   3799 C CA  . ALA B 1 90  ? 12.799  -8.400  15.663  1.00 17.04 ?  90  ALA B CA  1 
ATOM   3800 C C   . ALA B 1 90  ? 12.910  -7.566  16.928  1.00 20.86 ?  90  ALA B C   1 
ATOM   3801 O O   . ALA B 1 90  ? 13.017  -8.115  18.021  1.00 18.82 ?  90  ALA B O   1 
ATOM   3802 C CB  . ALA B 1 90  ? 11.310  -8.650  15.354  1.00 20.45 ?  90  ALA B CB  1 
ATOM   3803 N N   . SER B 1 91  ? 12.865  -6.235  16.782  1.00 20.35 ?  91  SER B N   1 
ATOM   3804 C CA  . SER B 1 91  ? 13.058  -5.382  17.954  1.00 19.59 ?  91  SER B CA  1 
ATOM   3805 C C   . SER B 1 91  ? 11.849  -5.336  18.882  1.00 22.92 ?  91  SER B C   1 
ATOM   3806 O O   . SER B 1 91  ? 11.928  -4.732  19.959  1.00 26.24 ?  91  SER B O   1 
ATOM   3807 C CB  . SER B 1 91  ? 13.443  -3.965  17.521  1.00 22.68 ?  91  SER B CB  1 
ATOM   3808 O OG  . SER B 1 91  ? 14.788  -3.960  17.078  1.00 26.62 ?  91  SER B OG  1 
ATOM   3809 N N   . GLY B 1 92  ? 10.748  -5.970  18.533  1.00 22.16 ?  92  GLY B N   1 
ATOM   3810 C CA  . GLY B 1 92  ? 9.611   -5.986  19.431  1.00 20.57 ?  92  GLY B CA  1 
ATOM   3811 C C   . GLY B 1 92  ? 8.488   -6.780  18.812  1.00 23.41 ?  92  GLY B C   1 
ATOM   3812 O O   . GLY B 1 92  ? 8.409   -6.931  17.586  1.00 18.73 ?  92  GLY B O   1 
ATOM   3813 N N   . VAL B 1 93  ? 7.618   -7.289  19.687  1.00 20.68 ?  93  VAL B N   1 
ATOM   3814 C CA  . VAL B 1 93  ? 6.498   -8.107  19.230  1.00 20.92 ?  93  VAL B CA  1 
ATOM   3815 C C   . VAL B 1 93  ? 5.488   -7.253  18.461  1.00 22.83 ?  93  VAL B C   1 
ATOM   3816 O O   . VAL B 1 93  ? 5.163   -7.533  17.299  1.00 21.26 ?  93  VAL B O   1 
ATOM   3817 C CB  . VAL B 1 93  ? 5.856   -8.848  20.416  1.00 20.22 ?  93  VAL B CB  1 
ATOM   3818 C CG1 . VAL B 1 93  ? 4.489   -9.384  20.043  1.00 19.21 ?  93  VAL B CG1 1 
ATOM   3819 C CG2 . VAL B 1 93  ? 6.744   -10.019 20.814  1.00 20.29 ?  93  VAL B CG2 1 
ATOM   3820 N N   . VAL B 1 94  ? 4.999   -6.178  19.092  1.00 21.21 ?  94  VAL B N   1 
ATOM   3821 C CA  . VAL B 1 94  ? 4.021   -5.358  18.396  1.00 24.13 ?  94  VAL B CA  1 
ATOM   3822 C C   . VAL B 1 94  ? 4.554   -4.730  17.124  1.00 21.02 ?  94  VAL B C   1 
ATOM   3823 O O   . VAL B 1 94  ? 3.853   -4.782  16.103  1.00 21.00 ?  94  VAL B O   1 
ATOM   3824 C CB  . VAL B 1 94  ? 3.461   -4.257  19.423  1.00 26.70 ?  94  VAL B CB  1 
ATOM   3825 C CG1 . VAL B 1 94  ? 2.629   -3.241  18.629  1.00 26.49 ?  94  VAL B CG1 1 
ATOM   3826 C CG2 . VAL B 1 94  ? 2.651   -4.956  20.494  1.00 26.11 ?  94  VAL B CG2 1 
ATOM   3827 N N   . PRO B 1 95  ? 5.788   -4.152  17.075  1.00 23.37 ?  95  PRO B N   1 
ATOM   3828 C CA  . PRO B 1 95  ? 6.371   -3.710  15.788  1.00 23.29 ?  95  PRO B CA  1 
ATOM   3829 C C   . PRO B 1 95  ? 6.396   -4.859  14.764  1.00 22.22 ?  95  PRO B C   1 
ATOM   3830 O O   . PRO B 1 95  ? 6.144   -4.607  13.626  1.00 19.91 ?  95  PRO B O   1 
ATOM   3831 C CB  . PRO B 1 95  ? 7.773   -3.231  16.179  1.00 25.00 ?  95  PRO B CB  1 
ATOM   3832 C CG  . PRO B 1 95  ? 7.614   -2.692  17.553  1.00 26.62 ?  95  PRO B CG  1 
ATOM   3833 C CD  . PRO B 1 95  ? 6.676   -3.685  18.181  1.00 22.04 ?  95  PRO B CD  1 
ATOM   3834 N N   . ALA B 1 96  ? 6.704   -6.082  15.217  1.00 19.68 ?  96  ALA B N   1 
ATOM   3835 C CA  . ALA B 1 96  ? 6.706   -7.217  14.294  1.00 21.66 ?  96  ALA B CA  1 
ATOM   3836 C C   . ALA B 1 96  ? 5.311   -7.478  13.733  1.00 20.01 ?  96  ALA B C   1 
ATOM   3837 O O   . ALA B 1 96  ? 5.154   -7.696  12.531  1.00 19.78 ?  96  ALA B O   1 
ATOM   3838 C CB  . ALA B 1 96  ? 7.254   -8.469  14.985  1.00 20.49 ?  96  ALA B CB  1 
ATOM   3839 N N   . ILE B 1 97  ? 4.283   -7.467  14.587  1.00 18.59 ?  97  ILE B N   1 
ATOM   3840 C CA  . ILE B 1 97  ? 2.911   -7.565  14.091  1.00 18.68 ?  97  ILE B CA  1 
ATOM   3841 C C   . ILE B 1 97  ? 2.655   -6.486  13.045  1.00 22.64 ?  97  ILE B C   1 
ATOM   3842 O O   . ILE B 1 97  ? 2.221   -6.771  11.924  1.00 20.34 ?  97  ILE B O   1 
ATOM   3843 C CB  . ILE B 1 97  ? 1.906   -7.461  15.253  1.00 21.92 ?  97  ILE B CB  1 
ATOM   3844 C CG1 . ILE B 1 97  ? 2.096   -8.625  16.230  1.00 23.11 ?  97  ILE B CG1 1 
ATOM   3845 C CG2 . ILE B 1 97  ? 0.464   -7.425  14.724  1.00 21.88 ?  97  ILE B CG2 1 
ATOM   3846 C CD1 . ILE B 1 97  ? 1.237   -8.502  17.472  1.00 21.95 ?  97  ILE B CD1 1 
ATOM   3847 N N   . SER B 1 98  ? 2.975   -5.236  13.384  1.00 21.16 ?  98  SER B N   1 
ATOM   3848 C CA  . SER B 1 98  ? 2.673   -4.115  12.499  1.00 20.70 ?  98  SER B CA  1 
ATOM   3849 C C   . SER B 1 98  ? 3.367   -4.276  11.143  1.00 21.66 ?  98  SER B C   1 
ATOM   3850 O O   . SER B 1 98  ? 2.756   -4.032  10.093  1.00 22.67 ?  98  SER B O   1 
ATOM   3851 C CB  . SER B 1 98  ? 3.069   -2.814  13.201  1.00 21.01 ?  98  SER B CB  1 
ATOM   3852 O OG  . SER B 1 98  ? 2.841   -1.677  12.395  1.00 23.79 ?  98  SER B OG  1 
ATOM   3853 N N   . ALA B 1 99  ? 4.617   -4.761  11.139  1.00 18.40 ?  99  ALA B N   1 
ATOM   3854 C CA  . ALA B 1 99  ? 5.339   -4.945  9.882   1.00 20.69 ?  99  ALA B CA  1 
ATOM   3855 C C   . ALA B 1 99  ? 4.709   -6.046  9.042   1.00 22.49 ?  99  ALA B C   1 
ATOM   3856 O O   . ALA B 1 99  ? 4.673   -5.962  7.803   1.00 22.54 ?  99  ALA B O   1 
ATOM   3857 C CB  . ALA B 1 99  ? 6.815   -5.259  10.157  1.00 21.76 ?  99  ALA B CB  1 
ATOM   3858 N N   . MET B 1 100 ? 4.201   -7.082  9.698   1.00 19.29 ?  100 MET B N   1 
ATOM   3859 C CA  . MET B 1 100 ? 3.610   -8.182  8.952   1.00 21.22 ?  100 MET B CA  1 
ATOM   3860 C C   . MET B 1 100 ? 2.217   -7.841  8.457   1.00 20.90 ?  100 MET B C   1 
ATOM   3861 O O   . MET B 1 100 ? 1.794   -8.363  7.424   1.00 21.67 ?  100 MET B O   1 
ATOM   3862 C CB  . MET B 1 100 ? 3.603   -9.438  9.818   1.00 22.55 ?  100 MET B CB  1 
ATOM   3863 C CG  . MET B 1 100 ? 5.018   -9.865  10.176  1.00 20.64 ?  100 MET B CG  1 
ATOM   3864 S SD  . MET B 1 100 ? 5.196   -11.516 10.920  1.00 23.73 ?  100 MET B SD  1 
ATOM   3865 C CE  . MET B 1 100 ? 4.647   -11.196 12.604  1.00 20.21 ?  100 MET B CE  1 
ATOM   3866 N N   . VAL B 1 101 ? 1.493   -6.975  9.168   1.00 20.68 ?  101 VAL B N   1 
ATOM   3867 C CA  . VAL B 1 101 ? 0.264   -6.417  8.615   1.00 21.77 ?  101 VAL B CA  1 
ATOM   3868 C C   . VAL B 1 101 ? 0.556   -5.736  7.287   1.00 22.07 ?  101 VAL B C   1 
ATOM   3869 O O   . VAL B 1 101 ? -0.116  -5.979  6.278   1.00 20.87 ?  101 VAL B O   1 
ATOM   3870 C CB  . VAL B 1 101 ? -0.378  -5.439  9.619   1.00 23.07 ?  101 VAL B CB  1 
ATOM   3871 C CG1 . VAL B 1 101 ? -1.481  -4.628  8.949   1.00 21.38 ?  101 VAL B CG1 1 
ATOM   3872 C CG2 . VAL B 1 101 ? -0.914  -6.201  10.851  1.00 19.69 ?  101 VAL B CG2 1 
ATOM   3873 N N   . ARG B 1 102 ? 1.589   -4.892  7.254   1.00 21.63 ?  102 ARG B N   1 
ATOM   3874 C CA  . ARG B 1 102 ? 1.884   -4.169  6.023   1.00 22.21 ?  102 ARG B CA  1 
ATOM   3875 C C   . ARG B 1 102 ? 2.392   -5.114  4.943   1.00 23.40 ?  102 ARG B C   1 
ATOM   3876 O O   . ARG B 1 102 ? 2.063   -4.954  3.763   1.00 22.42 ?  102 ARG B O   1 
ATOM   3877 C CB  . ARG B 1 102 ? 2.907   -3.058  6.291   1.00 22.64 ?  102 ARG B CB  1 
ATOM   3878 C CG  . ARG B 1 102 ? 2.343   -1.858  7.058   1.00 19.89 ?  102 ARG B CG  1 
ATOM   3879 C CD  . ARG B 1 102 ? 3.318   -0.673  7.081   1.00 22.61 ?  102 ARG B CD  1 
ATOM   3880 N NE  . ARG B 1 102 ? 4.617   -1.086  7.575   1.00 24.19 ?  102 ARG B NE  1 
ATOM   3881 C CZ  . ARG B 1 102 ? 4.924   -1.178  8.867   1.00 27.83 ?  102 ARG B CZ  1 
ATOM   3882 N NH1 . ARG B 1 102 ? 4.031   -0.843  9.799   1.00 22.27 1  102 ARG B NH1 1 
ATOM   3883 N NH2 . ARG B 1 102 ? 6.132   -1.592  9.226   1.00 22.04 ?  102 ARG B NH2 1 
ATOM   3884 N N   . GLN B 1 103 ? 3.180   -6.116  5.325   1.00 18.66 ?  103 GLN B N   1 
ATOM   3885 C CA  . GLN B 1 103 ? 3.840   -6.945  4.322   1.00 20.04 ?  103 GLN B CA  1 
ATOM   3886 C C   . GLN B 1 103 ? 2.912   -8.015  3.762   1.00 24.18 ?  103 GLN B C   1 
ATOM   3887 O O   . GLN B 1 103 ? 2.983   -8.337  2.565   1.00 21.53 ?  103 GLN B O   1 
ATOM   3888 C CB  . GLN B 1 103 ? 5.093   -7.600  4.913   1.00 24.89 ?  103 GLN B CB  1 
ATOM   3889 C CG  . GLN B 1 103 ? 5.888   -8.439  3.912   1.00 25.52 ?  103 GLN B CG  1 
ATOM   3890 C CD  . GLN B 1 103 ? 6.642   -7.610  2.868   1.00 29.86 ?  103 GLN B CD  1 
ATOM   3891 O OE1 . GLN B 1 103 ? 6.045   -6.850  2.116   1.00 34.61 ?  103 GLN B OE1 1 
ATOM   3892 N NE2 . GLN B 1 103 ? 7.960   -7.794  2.799   1.00 35.26 ?  103 GLN B NE2 1 
ATOM   3893 N N   . PHE B 1 104 ? 2.046   -8.578  4.603   1.00 22.07 ?  104 PHE B N   1 
ATOM   3894 C CA  . PHE B 1 104 ? 1.300   -9.777  4.250   1.00 21.72 ?  104 PHE B CA  1 
ATOM   3895 C C   . PHE B 1 104 ? -0.191  -9.545  4.056   1.00 21.28 ?  104 PHE B C   1 
ATOM   3896 O O   . PHE B 1 104 ? -0.928  -10.514 3.831   1.00 23.48 ?  104 PHE B O   1 
ATOM   3897 C CB  . PHE B 1 104 ? 1.500   -10.857 5.319   1.00 19.81 ?  104 PHE B CB  1 
ATOM   3898 C CG  . PHE B 1 104 ? 2.931   -11.282 5.500   1.00 23.23 ?  104 PHE B CG  1 
ATOM   3899 C CD1 . PHE B 1 104 ? 3.723   -11.597 4.409   1.00 27.58 ?  104 PHE B CD1 1 
ATOM   3900 C CD2 . PHE B 1 104 ? 3.478   -11.384 6.772   1.00 26.00 ?  104 PHE B CD2 1 
ATOM   3901 C CE1 . PHE B 1 104 ? 5.039   -11.995 4.585   1.00 29.52 ?  104 PHE B CE1 1 
ATOM   3902 C CE2 . PHE B 1 104 ? 4.789   -11.779 6.949   1.00 29.53 ?  104 PHE B CE2 1 
ATOM   3903 C CZ  . PHE B 1 104 ? 5.566   -12.089 5.854   1.00 27.32 ?  104 PHE B CZ  1 
ATOM   3904 N N   . THR B 1 105 ? -0.663  -8.306  4.147   1.00 21.90 ?  105 THR B N   1 
ATOM   3905 C CA  . THR B 1 105 ? -2.039  -7.970  3.812   1.00 23.34 ?  105 THR B CA  1 
ATOM   3906 C C   . THR B 1 105 ? -2.028  -6.712  2.961   1.00 23.30 ?  105 THR B C   1 
ATOM   3907 O O   . THR B 1 105 ? -1.004  -6.036  2.837   1.00 20.09 ?  105 THR B O   1 
ATOM   3908 C CB  . THR B 1 105 ? -2.919  -7.734  5.053   1.00 23.82 ?  105 THR B CB  1 
ATOM   3909 O OG1 . THR B 1 105 ? -2.525  -6.513  5.688   1.00 22.23 ?  105 THR B OG1 1 
ATOM   3910 C CG2 . THR B 1 105 ? -2.834  -8.912  6.069   1.00 19.01 ?  105 THR B CG2 1 
ATOM   3911 N N   . SER B 1 106 ? -3.200  -6.392  2.379   1.00 20.51 ?  106 SER B N   1 
ATOM   3912 C CA  . SER B 1 106 ? -3.315  -5.190  1.579   1.00 19.91 ?  106 SER B CA  1 
ATOM   3913 C C   . SER B 1 106 ? -4.102  -4.133  2.344   1.00 20.78 ?  106 SER B C   1 
ATOM   3914 O O   . SER B 1 106 ? -4.933  -4.477  3.191   1.00 18.85 ?  106 SER B O   1 
ATOM   3915 C CB  . SER B 1 106 ? -4.042  -5.483  0.258   1.00 22.02 ?  106 SER B CB  1 
ATOM   3916 O OG  . SER B 1 106 ? -3.275  -6.336  -0.574  1.00 25.79 ?  106 SER B OG  1 
ATOM   3917 N N   . PRO B 1 107 ? -3.873  -2.849  2.074   1.00 21.39 ?  107 PRO B N   1 
ATOM   3918 C CA  . PRO B 1 107 ? -4.767  -1.817  2.624   1.00 21.93 ?  107 PRO B CA  1 
ATOM   3919 C C   . PRO B 1 107 ? -6.226  -2.163  2.345   1.00 21.56 ?  107 PRO B C   1 
ATOM   3920 O O   . PRO B 1 107 ? -6.604  -2.483  1.223   1.00 20.71 ?  107 PRO B O   1 
ATOM   3921 C CB  . PRO B 1 107 ? -4.332  -0.544  1.894   1.00 21.56 ?  107 PRO B CB  1 
ATOM   3922 C CG  . PRO B 1 107 ? -2.900  -0.814  1.470   1.00 22.14 ?  107 PRO B CG  1 
ATOM   3923 C CD  . PRO B 1 107 ? -2.835  -2.287  1.192   1.00 22.70 ?  107 PRO B CD  1 
ATOM   3924 N N   . GLY B 1 108 ? -7.049  -2.138  3.391   1.00 19.72 ?  108 GLY B N   1 
ATOM   3925 C CA  . GLY B 1 108 ? -8.451  -2.476  3.267   1.00 20.91 ?  108 GLY B CA  1 
ATOM   3926 C C   . GLY B 1 108 ? -8.784  -3.897  3.652   1.00 21.76 ?  108 GLY B C   1 
ATOM   3927 O O   . GLY B 1 108 ? -9.949  -4.185  3.966   1.00 26.38 ?  108 GLY B O   1 
ATOM   3928 N N   . ASP B 1 109 ? -7.801  -4.774  3.647   1.00 18.79 ?  109 ASP B N   1 
ATOM   3929 C CA  . ASP B 1 109 ? -8.036  -6.154  4.119   1.00 19.95 ?  109 ASP B CA  1 
ATOM   3930 C C   . ASP B 1 109 ? -8.473  -6.131  5.574   1.00 22.95 ?  109 ASP B C   1 
ATOM   3931 O O   . ASP B 1 109 ? -8.122  -5.224  6.302   1.00 23.05 ?  109 ASP B O   1 
ATOM   3932 C CB  . ASP B 1 109 ? -6.759  -6.959  3.939   1.00 24.17 ?  109 ASP B CB  1 
ATOM   3933 C CG  . ASP B 1 109 ? -6.548  -7.424  2.517   1.00 23.54 ?  109 ASP B CG  1 
ATOM   3934 O OD1 . ASP B 1 109 ? -7.474  -7.291  1.714   1.00 22.95 ?  109 ASP B OD1 1 
ATOM   3935 O OD2 . ASP B 1 109 ? -5.461  -7.925  2.251   1.00 22.78 -1 109 ASP B OD2 1 
ATOM   3936 N N   . GLN B 1 110 ? -9.262  -7.116  5.932   1.00 22.06 ?  110 GLN B N   1 
ATOM   3937 C CA  . GLN B 1 110 ? -9.654  -7.274  7.316   1.00 19.34 ?  110 GLN B CA  1 
ATOM   3938 C C   . GLN B 1 110 ? -8.668  -8.179  8.037   1.00 20.29 ?  110 GLN B C   1 
ATOM   3939 O O   . GLN B 1 110 ? -8.079  -9.091  7.453   1.00 19.72 ?  110 GLN B O   1 
ATOM   3940 C CB  . GLN B 1 110 ? -11.072 -7.836  7.393   1.00 22.52 ?  110 GLN B CB  1 
ATOM   3941 C CG  . GLN B 1 110 ? -12.087 -6.934  6.691   1.00 21.81 ?  110 GLN B CG  1 
ATOM   3942 C CD  . GLN B 1 110 ? -13.494 -7.409  6.920   1.00 30.12 ?  110 GLN B CD  1 
ATOM   3943 O OE1 . GLN B 1 110 ? -14.139 -7.014  7.891   1.00 26.58 ?  110 GLN B OE1 1 
ATOM   3944 N NE2 . GLN B 1 110 ? -13.978 -8.274  6.039   1.00 27.17 ?  110 GLN B NE2 1 
ATOM   3945 N N   . ILE B 1 111 ? -8.461  -7.893  9.315   1.00 21.28 ?  111 ILE B N   1 
ATOM   3946 C CA  . ILE B 1 111 ? -7.567  -8.677  10.154  1.00 20.77 ?  111 ILE B CA  1 
ATOM   3947 C C   . ILE B 1 111 ? -8.348  -9.067  11.396  1.00 20.54 ?  111 ILE B C   1 
ATOM   3948 O O   . ILE B 1 111 ? -8.996  -8.216  12.017  1.00 23.52 ?  111 ILE B O   1 
ATOM   3949 C CB  . ILE B 1 111 ? -6.287  -7.888  10.485  1.00 19.56 ?  111 ILE B CB  1 
ATOM   3950 C CG1 . ILE B 1 111 ? -5.513  -7.640  9.180   1.00 22.31 ?  111 ILE B CG1 1 
ATOM   3951 C CG2 . ILE B 1 111 ? -5.406  -8.619  11.517  1.00 17.69 ?  111 ILE B CG2 1 
ATOM   3952 C CD1 . ILE B 1 111 ? -4.211  -6.885  9.338   1.00 22.58 ?  111 ILE B CD1 1 
ATOM   3953 N N   . LEU B 1 112 ? -8.337  -10.359 11.691  1.00 19.37 ?  112 LEU B N   1 
ATOM   3954 C CA  . LEU B 1 112 ? -9.216  -10.880 12.744  1.00 20.59 ?  112 LEU B CA  1 
ATOM   3955 C C   . LEU B 1 112 ? -8.572  -10.917 14.110  1.00 19.50 ?  112 LEU B C   1 
ATOM   3956 O O   . LEU B 1 112 ? -7.437  -11.334 14.220  1.00 20.09 ?  112 LEU B O   1 
ATOM   3957 C CB  . LEU B 1 112 ? -9.769  -12.256 12.371  1.00 18.52 ?  112 LEU B CB  1 
ATOM   3958 C CG  . LEU B 1 112 ? -10.922 -12.782 13.223  1.00 20.08 ?  112 LEU B CG  1 
ATOM   3959 C CD1 . LEU B 1 112 ? -11.973 -13.433 12.353  1.00 24.42 ?  112 LEU B CD1 1 
ATOM   3960 C CD2 . LEU B 1 112 ? -10.424 -13.769 14.260  1.00 24.63 ?  112 LEU B CD2 1 
ATOM   3961 N N   . VAL B 1 113 ? -9.339  -10.460 15.074  1.00 20.06 ?  113 VAL B N   1 
ATOM   3962 C CA  . VAL B 1 113 ? -8.946  -10.565 16.468  1.00 20.62 ?  113 VAL B CA  1 
ATOM   3963 C C   . VAL B 1 113 ? -10.142 -11.118 17.224  1.00 22.37 ?  113 VAL B C   1 
ATOM   3964 O O   . VAL B 1 113 ? -11.235 -11.251 16.675  1.00 21.83 ?  113 VAL B O   1 
ATOM   3965 C CB  . VAL B 1 113 ? -8.497  -9.208  17.042  1.00 20.29 ?  113 VAL B CB  1 
ATOM   3966 C CG1 . VAL B 1 113 ? -7.300  -8.666  16.226  1.00 18.59 ?  113 VAL B CG1 1 
ATOM   3967 C CG2 . VAL B 1 113 ? -9.635  -8.226  16.987  1.00 21.49 ?  113 VAL B CG2 1 
ATOM   3968 N N   . GLN B 1 114 ? -9.925  -11.439 18.500  1.00 20.31 ?  114 GLN B N   1 
ATOM   3969 C CA  . GLN B 1 114 ? -10.966 -11.984 19.367  1.00 23.29 ?  114 GLN B CA  1 
ATOM   3970 C C   . GLN B 1 114 ? -11.172 -11.034 20.544  1.00 19.43 ?  114 GLN B C   1 
ATOM   3971 O O   . GLN B 1 114 ? -10.461 -11.123 21.548  1.00 21.51 ?  114 GLN B O   1 
ATOM   3972 C CB  . GLN B 1 114 ? -10.595 -13.383 19.847  1.00 21.60 ?  114 GLN B CB  1 
ATOM   3973 C CG  . GLN B 1 114 ? -10.470 -14.388 18.716  1.00 23.10 ?  114 GLN B CG  1 
ATOM   3974 C CD  . GLN B 1 114 ? -9.870  -15.691 19.173  1.00 27.89 ?  114 GLN B CD  1 
ATOM   3975 O OE1 . GLN B 1 114 ? -8.683  -15.766 19.508  1.00 26.57 ?  114 GLN B OE1 1 
ATOM   3976 N NE2 . GLN B 1 114 ? -10.695 -16.741 19.199  1.00 28.77 ?  114 GLN B NE2 1 
ATOM   3977 N N   . GLU B 1 115 ? -12.135 -10.126 20.392  1.00 20.47 ?  115 GLU B N   1 
ATOM   3978 C CA  . GLU B 1 115 ? -12.435 -9.076  21.388  1.00 19.69 ?  115 GLU B CA  1 
ATOM   3979 C C   . GLU B 1 115 ? -12.987 -9.750  22.654  1.00 22.41 ?  115 GLU B C   1 
ATOM   3980 O O   . GLU B 1 115 ? -13.724 -10.728 22.451  1.00 21.27 ?  115 GLU B O   1 
ATOM   3981 C CB  . GLU B 1 115 ? -13.432 -8.080  20.830  1.00 22.33 ?  115 GLU B CB  1 
ATOM   3982 C CG  . GLU B 1 115 ? -12.804 -7.015  19.982  1.00 20.67 ?  115 GLU B CG  1 
ATOM   3983 C CD  . GLU B 1 115 ? -13.855 -6.070  19.448  1.00 26.10 ?  115 GLU B CD  1 
ATOM   3984 O OE1 . GLU B 1 115 ? -13.655 -5.552  18.365  1.00 28.24 ?  115 GLU B OE1 1 
ATOM   3985 O OE2 . GLU B 1 115 ? -14.872 -5.888  20.120  1.00 27.31 -1 115 GLU B OE2 1 
ATOM   3986 N N   . PRO B 1 116 ? -12.720 -9.262  23.910  1.00 21.73 ?  116 PRO B N   1 
ATOM   3987 C CA  . PRO B 1 116 ? -11.776 -8.190  24.232  1.00 20.03 ?  116 PRO B CA  1 
ATOM   3988 C C   . PRO B 1 116 ? -10.344 -8.653  24.133  1.00 22.35 ?  116 PRO B C   1 
ATOM   3989 O O   . PRO B 1 116 ? -10.033 -9.768  24.549  1.00 19.87 ?  116 PRO B O   1 
ATOM   3990 C CB  . PRO B 1 116 ? -12.108 -7.848  25.690  1.00 18.88 ?  116 PRO B CB  1 
ATOM   3991 C CG  . PRO B 1 116 ? -12.602 -9.156  26.266  1.00 23.77 ?  116 PRO B CG  1 
ATOM   3992 C CD  . PRO B 1 116 ? -13.356 -9.812  25.127  1.00 21.75 ?  116 PRO B CD  1 
ATOM   3993 N N   . VAL B 1 117 ? -9.468  -7.796  23.618  1.00 20.75 ?  117 VAL B N   1 
ATOM   3994 C CA  . VAL B 1 117 ? -8.069  -8.157  23.449  1.00 19.91 ?  117 VAL B CA  1 
ATOM   3995 C C   . VAL B 1 117 ? -7.245  -6.873  23.499  1.00 20.67 ?  117 VAL B C   1 
ATOM   3996 O O   . VAL B 1 117 ? -7.770  -5.767  23.348  1.00 22.99 ?  117 VAL B O   1 
ATOM   3997 C CB  . VAL B 1 117 ? -7.862  -8.949  22.128  1.00 19.16 ?  117 VAL B CB  1 
ATOM   3998 C CG1 . VAL B 1 117 ? -8.089  -8.083  20.901  1.00 19.92 ?  117 VAL B CG1 1 
ATOM   3999 C CG2 . VAL B 1 117 ? -6.478  -9.645  22.094  1.00 18.88 ?  117 VAL B CG2 1 
ATOM   4000 N N   . TYR B 1 118 ? -5.958  -7.048  23.760  1.00 19.92 ?  118 TYR B N   1 
ATOM   4001 C CA  . TYR B 1 118 ? -4.968  -5.947  23.814  1.00 19.76 ?  118 TYR B CA  1 
ATOM   4002 C C   . TYR B 1 118 ? -5.278  -4.781  22.872  1.00 24.04 ?  118 TYR B C   1 
ATOM   4003 O O   . TYR B 1 118 ? -5.364  -4.990  21.664  1.00 25.61 ?  118 TYR B O   1 
ATOM   4004 C CB  . TYR B 1 118 ? -3.585  -6.549  23.557  1.00 20.46 ?  118 TYR B CB  1 
ATOM   4005 C CG  . TYR B 1 118 ? -2.397  -5.674  23.854  1.00 20.87 ?  118 TYR B CG  1 
ATOM   4006 C CD1 . TYR B 1 118 ? -2.463  -4.638  24.768  1.00 21.94 ?  118 TYR B CD1 1 
ATOM   4007 C CD2 . TYR B 1 118 ? -1.188  -5.907  23.226  1.00 28.25 ?  118 TYR B CD2 1 
ATOM   4008 C CE1 . TYR B 1 118 ? -1.363  -3.842  25.035  1.00 24.46 ?  118 TYR B CE1 1 
ATOM   4009 C CE2 . TYR B 1 118 ? -0.078  -5.126  23.485  1.00 26.82 ?  118 TYR B CE2 1 
ATOM   4010 C CZ  . TYR B 1 118 ? -0.163  -4.095  24.399  1.00 26.20 ?  118 TYR B CZ  1 
ATOM   4011 O OH  . TYR B 1 118 ? 0.931   -3.319  24.645  1.00 33.83 ?  118 TYR B OH  1 
ATOM   4012 N N   . ASN B 1 119 ? -5.308  -3.576  23.443  1.00 21.71 ?  119 ASN B N   1 
ATOM   4013 C CA  . ASN B 1 119 ? -5.680  -2.395  22.661  1.00 23.45 ?  119 ASN B CA  1 
ATOM   4014 C C   . ASN B 1 119 ? -4.724  -2.141  21.503  1.00 25.16 ?  119 ASN B C   1 
ATOM   4015 O O   . ASN B 1 119 ? -5.135  -1.632  20.445  1.00 23.61 ?  119 ASN B O   1 
ATOM   4016 C CB  . ASN B 1 119 ? -5.723  -1.160  23.567  1.00 24.48 ?  119 ASN B CB  1 
ATOM   4017 C CG  . ASN B 1 119 ? -4.532  -1.090  24.516  1.00 25.60 ?  119 ASN B CG  1 
ATOM   4018 O OD1 . ASN B 1 119 ? -4.406  -1.909  25.416  1.00 28.46 ?  119 ASN B OD1 1 
ATOM   4019 N ND2 . ASN B 1 119 ? -3.664  -0.094  24.332  1.00 28.43 ?  119 ASN B ND2 1 
ATOM   4020 N N   . MET B 1 120 ? -3.451  -2.476  21.683  1.00 20.06 ?  120 MET B N   1 
ATOM   4021 C CA  . MET B 1 120 ? -2.452  -2.207  20.658  1.00 25.14 ?  120 MET B CA  1 
ATOM   4022 C C   . MET B 1 120 ? -2.712  -2.996  19.385  1.00 23.74 ?  120 MET B C   1 
ATOM   4023 O O   . MET B 1 120 ? -2.258  -2.575  18.314  1.00 23.24 ?  120 MET B O   1 
ATOM   4024 C CB  . MET B 1 120 ? -1.050  -2.508  21.196  1.00 22.92 ?  120 MET B CB  1 
ATOM   4025 C CG  . MET B 1 120 ? -0.535  -1.465  22.173  1.00 26.23 ?  120 MET B CG  1 
ATOM   4026 S SD  . MET B 1 120 ? -0.211  0.087   21.307  1.00 38.34 ?  120 MET B SD  1 
ATOM   4027 C CE  . MET B 1 120 ? -1.610  1.029   21.878  1.00 35.59 ?  120 MET B CE  1 
ATOM   4028 N N   . PHE B 1 121 ? -3.439  -4.121  19.469  1.00 20.96 ?  121 PHE B N   1 
ATOM   4029 C CA  . PHE B 1 121 ? -3.842  -4.817  18.251  1.00 21.11 ?  121 PHE B CA  1 
ATOM   4030 C C   . PHE B 1 121 ? -4.687  -3.904  17.364  1.00 22.76 ?  121 PHE B C   1 
ATOM   4031 O O   . PHE B 1 121 ? -4.525  -3.889  16.139  1.00 24.01 ?  121 PHE B O   1 
ATOM   4032 C CB  . PHE B 1 121 ? -4.636  -6.092  18.567  1.00 21.01 ?  121 PHE B CB  1 
ATOM   4033 C CG  . PHE B 1 121 ? -3.800  -7.254  19.070  1.00 23.87 ?  121 PHE B CG  1 
ATOM   4034 C CD1 . PHE B 1 121 ? -2.452  -7.105  19.343  1.00 22.30 ?  121 PHE B CD1 1 
ATOM   4035 C CD2 . PHE B 1 121 ? -4.390  -8.500  19.275  1.00 22.41 ?  121 PHE B CD2 1 
ATOM   4036 C CE1 . PHE B 1 121 ? -1.693  -8.185  19.819  1.00 22.44 ?  121 PHE B CE1 1 
ATOM   4037 C CE2 . PHE B 1 121 ? -3.639  -9.585  19.752  1.00 25.03 ?  121 PHE B CE2 1 
ATOM   4038 C CZ  . PHE B 1 121 ? -2.291  -9.422  20.030  1.00 21.67 ?  121 PHE B CZ  1 
ATOM   4039 N N   . TYR B 1 122 ? -5.573  -3.134  17.953  1.00 21.54 ?  122 TYR B N   1 
ATOM   4040 C CA  . TYR B 1 122 ? -6.435  -2.277  17.121  1.00 21.60 ?  122 TYR B CA  1 
ATOM   4041 C C   . TYR B 1 122 ? -5.572  -1.178  16.509  1.00 22.90 ?  122 TYR B C   1 
ATOM   4042 O O   . TYR B 1 122 ? -5.731  -0.903  15.345  1.00 23.27 ?  122 TYR B O   1 
ATOM   4043 C CB  . TYR B 1 122 ? -7.584  -1.733  17.950  1.00 21.41 ?  122 TYR B CB  1 
ATOM   4044 C CG  . TYR B 1 122 ? -8.285  -2.768  18.785  1.00 23.93 ?  122 TYR B CG  1 
ATOM   4045 C CD1 . TYR B 1 122 ? -8.859  -3.882  18.201  1.00 21.26 ?  122 TYR B CD1 1 
ATOM   4046 C CD2 . TYR B 1 122 ? -8.375  -2.633  20.156  1.00 22.23 ?  122 TYR B CD2 1 
ATOM   4047 C CE1 . TYR B 1 122 ? -9.507  -4.840  18.957  1.00 22.81 ?  122 TYR B CE1 1 
ATOM   4048 C CE2 . TYR B 1 122 ? -9.011  -3.585  20.928  1.00 22.09 ?  122 TYR B CE2 1 
ATOM   4049 C CZ  . TYR B 1 122 ? -9.581  -4.689  20.327  1.00 22.72 ?  122 TYR B CZ  1 
ATOM   4050 O OH  . TYR B 1 122 ? -10.212 -5.618  21.090  1.00 21.52 ?  122 TYR B OH  1 
ATOM   4051 N N   . SER B 1 123 ? -4.640  -0.633  17.288  1.00 23.67 ?  123 SER B N   1 
ATOM   4052 C CA  . SER B 1 123 ? -3.838  0.484   16.810  1.00 22.87 ?  123 SER B CA  1 
ATOM   4053 C C   . SER B 1 123 ? -3.018  0.084   15.596  1.00 22.34 ?  123 SER B C   1 
ATOM   4054 O O   . SER B 1 123 ? -2.946  0.831   14.616  1.00 25.50 ?  123 SER B O   1 
ATOM   4055 C CB  . SER B 1 123 ? -2.926  1.000   17.931  1.00 27.89 ?  123 SER B CB  1 
ATOM   4056 O OG  . SER B 1 123 ? -3.663  1.148   19.122  1.00 25.01 ?  123 SER B OG  1 
ATOM   4057 N N   . VAL B 1 124 ? -2.367  -1.082  15.645  1.00 26.41 ?  124 VAL B N   1 
ATOM   4058 C CA  . VAL B 1 124 ? -1.504  -1.422  14.519  1.00 24.15 ?  124 VAL B CA  1 
ATOM   4059 C C   . VAL B 1 124 ? -2.336  -1.862  13.331  1.00 26.06 ?  124 VAL B C   1 
ATOM   4060 O O   . VAL B 1 124 ? -1.943  -1.633  12.185  1.00 26.92 ?  124 VAL B O   1 
ATOM   4061 C CB  . VAL B 1 124 ? -0.433  -2.471  14.885  1.00 25.93 ?  124 VAL B CB  1 
ATOM   4062 C CG1 . VAL B 1 124 ? 0.379   -1.988  16.083  1.00 22.66 ?  124 VAL B CG1 1 
ATOM   4063 C CG2 . VAL B 1 124 ? -1.036  -3.847  15.157  1.00 27.31 ?  124 VAL B CG2 1 
ATOM   4064 N N   . ILE B 1 125 ? -3.500  -2.470  13.563  1.00 20.83 ?  125 ILE B N   1 
ATOM   4065 C CA  . ILE B 1 125 ? -4.354  -2.819  12.437  1.00 20.71 ?  125 ILE B CA  1 
ATOM   4066 C C   . ILE B 1 125 ? -4.935  -1.552  11.821  1.00 21.85 ?  125 ILE B C   1 
ATOM   4067 O O   . ILE B 1 125 ? -4.719  -1.255  10.644  1.00 21.94 ?  125 ILE B O   1 
ATOM   4068 C CB  . ILE B 1 125 ? -5.453  -3.803  12.863  1.00 19.80 ?  125 ILE B CB  1 
ATOM   4069 C CG1 . ILE B 1 125 ? -4.837  -5.160  13.235  1.00 22.03 ?  125 ILE B CG1 1 
ATOM   4070 C CG2 . ILE B 1 125 ? -6.505  -3.964  11.710  1.00 17.82 ?  125 ILE B CG2 1 
ATOM   4071 C CD1 . ILE B 1 125 ? -5.785  -6.053  14.046  1.00 20.29 ?  125 ILE B CD1 1 
ATOM   4072 N N   . GLU B 1 126 ? -5.614  -0.750  12.636  1.00 21.08 ?  126 GLU B N   1 
ATOM   4073 C CA  . GLU B 1 126 ? -6.363  0.381   12.104  1.00 24.43 ?  126 GLU B CA  1 
ATOM   4074 C C   . GLU B 1 126 ? -5.440  1.477   11.596  1.00 25.56 ?  126 GLU B C   1 
ATOM   4075 O O   . GLU B 1 126 ? -5.700  2.075   10.545  1.00 22.80 ?  126 GLU B O   1 
ATOM   4076 C CB  . GLU B 1 126 ? -7.321  0.900   13.179  1.00 24.40 ?  126 GLU B CB  1 
ATOM   4077 C CG  . GLU B 1 126 ? -8.358  -0.177  13.516  1.00 25.68 ?  126 GLU B CG  1 
ATOM   4078 C CD  . GLU B 1 126 ? -9.418  0.272   14.498  1.00 30.26 ?  126 GLU B CD  1 
ATOM   4079 O OE1 . GLU B 1 126 ? -10.538 -0.296  14.443  1.00 28.51 ?  126 GLU B OE1 1 
ATOM   4080 O OE2 . GLU B 1 126 ? -9.134  1.186   15.307  1.00 24.75 -1 126 GLU B OE2 1 
ATOM   4081 N N   . GLY B 1 127 ? -4.356  1.755   12.323  1.00 25.04 ?  127 GLY B N   1 
ATOM   4082 C CA  . GLY B 1 127 ? -3.465  2.824   11.904  1.00 21.07 ?  127 GLY B CA  1 
ATOM   4083 C C   . GLY B 1 127 ? -2.732  2.500   10.620  1.00 22.74 ?  127 GLY B C   1 
ATOM   4084 O O   . GLY B 1 127 ? -2.387  3.410   9.858   1.00 21.36 ?  127 GLY B O   1 
ATOM   4085 N N   . ASN B 1 128 ? -2.488  1.208   10.355  1.00 21.11 ?  128 ASN B N   1 
ATOM   4086 C CA  . ASN B 1 128 ? -1.913  0.769   9.090   1.00 19.23 ?  128 ASN B CA  1 
ATOM   4087 C C   . ASN B 1 128 ? -2.930  0.719   7.949   1.00 23.46 ?  128 ASN B C   1 
ATOM   4088 O O   . ASN B 1 128 ? -2.560  0.362   6.830   1.00 25.81 ?  128 ASN B O   1 
ATOM   4089 C CB  . ASN B 1 128 ? -1.260  -0.610  9.245   1.00 22.68 ?  128 ASN B CB  1 
ATOM   4090 C CG  . ASN B 1 128 ? 0.126   -0.540  9.858   1.00 25.28 ?  128 ASN B CG  1 
ATOM   4091 O OD1 . ASN B 1 128 ? 1.027   0.143   9.343   1.00 20.91 ?  128 ASN B OD1 1 
ATOM   4092 N ND2 . ASN B 1 128 ? 0.312   -1.263  10.965  1.00 23.56 ?  128 ASN B ND2 1 
ATOM   4093 N N   . GLY B 1 129 ? -4.188  1.082   8.176   1.00 19.21 ?  129 GLY B N   1 
ATOM   4094 C CA  . GLY B 1 129 ? -5.126  1.054   7.071   1.00 23.29 ?  129 GLY B CA  1 
ATOM   4095 C C   . GLY B 1 129 ? -5.657  -0.325  6.779   1.00 22.74 ?  129 GLY B C   1 
ATOM   4096 O O   . GLY B 1 129 ? -6.014  -0.629  5.634   1.00 19.51 ?  129 GLY B O   1 
ATOM   4097 N N   . ARG B 1 130 ? -5.685  -1.187  7.782   1.00 20.53 ?  130 ARG B N   1 
ATOM   4098 C CA  . ARG B 1 130 ? -6.451  -2.417  7.701   1.00 21.19 ?  130 ARG B CA  1 
ATOM   4099 C C   . ARG B 1 130 ? -7.641  -2.303  8.650   1.00 20.60 ?  130 ARG B C   1 
ATOM   4100 O O   . ARG B 1 130 ? -7.749  -1.371  9.452   1.00 22.71 ?  130 ARG B O   1 
ATOM   4101 C CB  . ARG B 1 130 ? -5.565  -3.634  8.003   1.00 19.39 ?  130 ARG B CB  1 
ATOM   4102 C CG  . ARG B 1 130 ? -4.687  -4.129  6.811   1.00 20.68 ?  130 ARG B CG  1 
ATOM   4103 C CD  . ARG B 1 130 ? -3.590  -3.104  6.408   1.00 20.43 ?  130 ARG B CD  1 
ATOM   4104 N NE  . ARG B 1 130 ? -2.600  -3.622  5.459   1.00 19.33 ?  130 ARG B NE  1 
ATOM   4105 C CZ  . ARG B 1 130 ? -1.725  -2.852  4.810   1.00 18.37 ?  130 ARG B CZ  1 
ATOM   4106 N NH1 . ARG B 1 130 ? -1.718  -1.544  5.017   1.00 23.06 1  130 ARG B NH1 1 
ATOM   4107 N NH2 . ARG B 1 130 ? -0.849  -3.376  3.964   1.00 20.92 ?  130 ARG B NH2 1 
ATOM   4108 N N   . ARG B 1 131 ? -8.580  -3.225  8.516   1.00 20.47 ?  131 ARG B N   1 
ATOM   4109 C CA  . ARG B 1 131 ? -9.847  -3.141  9.220   1.00 21.38 ?  131 ARG B CA  1 
ATOM   4110 C C   . ARG B 1 131 ? -9.922  -4.259  10.245  1.00 21.85 ?  131 ARG B C   1 
ATOM   4111 O O   . ARG B 1 131 ? -9.720  -5.431  9.909   1.00 22.98 ?  131 ARG B O   1 
ATOM   4112 C CB  . ARG B 1 131 ? -11.027 -3.216  8.242   1.00 24.22 ?  131 ARG B CB  1 
ATOM   4113 C CG  . ARG B 1 131 ? -11.086 -2.028  7.307   1.00 25.00 ?  131 ARG B CG  1 
ATOM   4114 C CD  . ARG B 1 131 ? -12.315 -2.096  6.409   1.00 26.01 ?  131 ARG B CD  1 
ATOM   4115 N NE  . ARG B 1 131 ? -12.103 -3.047  5.332   1.00 24.42 ?  131 ARG B NE  1 
ATOM   4116 C CZ  . ARG B 1 131 ? -13.079 -3.631  4.637   1.00 32.87 ?  131 ARG B CZ  1 
ATOM   4117 N NH1 . ARG B 1 131 ? -14.351 -3.361  4.910   1.00 32.19 1  131 ARG B NH1 1 
ATOM   4118 N NH2 . ARG B 1 131 ? -12.781 -4.480  3.661   1.00 25.30 ?  131 ARG B NH2 1 
ATOM   4119 N N   . VAL B 1 132 ? -10.186 -3.894  11.498  1.00 20.35 ?  132 VAL B N   1 
ATOM   4120 C CA  . VAL B 1 132 ? -10.404 -4.903  12.521  1.00 22.73 ?  132 VAL B CA  1 
ATOM   4121 C C   . VAL B 1 132 ? -11.718 -5.619  12.249  1.00 22.16 ?  132 VAL B C   1 
ATOM   4122 O O   . VAL B 1 132 ? -12.758 -4.984  12.034  1.00 22.33 ?  132 VAL B O   1 
ATOM   4123 C CB  . VAL B 1 132 ? -10.399 -4.262  13.921  1.00 22.16 ?  132 VAL B CB  1 
ATOM   4124 C CG1 . VAL B 1 132 ? -10.793 -5.280  14.971  1.00 21.55 ?  132 VAL B CG1 1 
ATOM   4125 C CG2 . VAL B 1 132 ? -9.024  -3.697  14.223  1.00 19.87 ?  132 VAL B CG2 1 
ATOM   4126 N N   . ILE B 1 133 ? -11.656 -6.951  12.307  1.00 20.19 ?  133 ILE B N   1 
ATOM   4127 C CA  . ILE B 1 133 ? -12.896 -7.763  12.352  1.00 23.78 ?  133 ILE B CA  1 
ATOM   4128 C C   . ILE B 1 133 ? -12.723 -8.654  13.605  1.00 23.52 ?  133 ILE B C   1 
ATOM   4129 O O   . ILE B 1 133 ? -11.653 -9.196  13.789  1.00 23.30 ?  133 ILE B O   1 
ATOM   4130 C CB  . ILE B 1 133 ? -13.212 -8.552  11.069  1.00 20.14 ?  133 ILE B CB  1 
ATOM   4131 C CG1 . ILE B 1 133 ? -14.570 -9.247  11.159  1.00 23.50 ?  133 ILE B CG1 1 
ATOM   4132 C CG2 . ILE B 1 133 ? -12.106 -9.520  10.691  1.00 20.77 ?  133 ILE B CG2 1 
ATOM   4133 C CD1 . ILE B 1 133 ? -15.036 -9.835  9.856   1.00 25.38 ?  133 ILE B CD1 1 
ATOM   4134 N N   . SER B 1 134 ? -13.721 -8.725  14.469  1.00 26.15 ?  134 SER B N   1 
ATOM   4135 C CA  . SER B 1 134 ? -13.628 -9.526  15.684  1.00 21.00 ?  134 SER B CA  1 
ATOM   4136 C C   . SER B 1 134 ? -14.591 -10.697 15.615  1.00 24.85 ?  134 SER B C   1 
ATOM   4137 O O   . SER B 1 134 ? -15.756 -10.531 15.228  1.00 26.52 ?  134 SER B O   1 
ATOM   4138 C CB  . SER B 1 134 ? -13.931 -8.691  16.935  1.00 22.61 ?  134 SER B CB  1 
ATOM   4139 O OG  . SER B 1 134 ? -14.043 -9.526  18.088  1.00 23.83 ?  134 SER B OG  1 
ATOM   4140 N N   . SER B 1 135 ? -14.106 -11.873 15.985  1.00 24.27 ?  135 SER B N   1 
ATOM   4141 C CA  . SER B 1 135 ? -14.991 -12.947 16.423  1.00 24.32 ?  135 SER B CA  1 
ATOM   4142 C C   . SER B 1 135 ? -14.990 -12.840 17.941  1.00 26.43 ?  135 SER B C   1 
ATOM   4143 O O   . SER B 1 135 ? -14.088 -13.345 18.620  1.00 22.84 ?  135 SER B O   1 
ATOM   4144 C CB  . SER B 1 135 ? -14.515 -14.303 15.913  1.00 23.03 ?  135 SER B CB  1 
ATOM   4145 O OG  . SER B 1 135 ? -15.318 -15.376 16.404  1.00 28.23 ?  135 SER B OG  1 
ATOM   4146 N N   . ASP B 1 136 ? -15.990 -12.143 18.474  1.00 25.54 ?  136 ASP B N   1 
ATOM   4147 C CA  . ASP B 1 136 ? -16.008 -11.853 19.907  1.00 25.85 ?  136 ASP B CA  1 
ATOM   4148 C C   . ASP B 1 136 ? -15.977 -13.143 20.708  1.00 28.20 ?  136 ASP B C   1 
ATOM   4149 O O   . ASP B 1 136 ? -16.679 -14.101 20.390  1.00 25.85 ?  136 ASP B O   1 
ATOM   4150 C CB  . ASP B 1 136 ? -17.271 -11.069 20.298  1.00 26.08 ?  136 ASP B CB  1 
ATOM   4151 C CG  . ASP B 1 136 ? -17.282 -9.642  19.791  1.00 27.46 ?  136 ASP B CG  1 
ATOM   4152 O OD1 . ASP B 1 136 ? -16.330 -9.198  19.115  1.00 26.44 ?  136 ASP B OD1 1 
ATOM   4153 O OD2 . ASP B 1 136 ? -18.267 -8.943  20.090  1.00 29.68 -1 136 ASP B OD2 1 
ATOM   4154 N N   . LEU B 1 137 ? -15.156 -13.167 21.750  1.00 28.24 ?  137 LEU B N   1 
ATOM   4155 C CA  . LEU B 1 137 ? -15.282 -14.215 22.752  1.00 30.24 ?  137 LEU B CA  1 
ATOM   4156 C C   . LEU B 1 137 ? -16.635 -14.090 23.434  1.00 27.56 ?  137 LEU B C   1 
ATOM   4157 O O   . LEU B 1 137 ? -17.085 -12.990 23.754  1.00 30.42 ?  137 LEU B O   1 
ATOM   4158 C CB  . LEU B 1 137 ? -14.152 -14.109 23.778  1.00 24.00 ?  137 LEU B CB  1 
ATOM   4159 C CG  . LEU B 1 137 ? -12.751 -14.243 23.181  1.00 23.77 ?  137 LEU B CG  1 
ATOM   4160 C CD1 . LEU B 1 137 ? -11.696 -14.052 24.283  1.00 24.10 ?  137 LEU B CD1 1 
ATOM   4161 C CD2 . LEU B 1 137 ? -12.575 -15.605 22.515  1.00 29.60 ?  137 LEU B CD2 1 
ATOM   4162 N N   . ILE B 1 138 ? -17.265 -15.224 23.657  1.00 30.19 ?  138 ILE B N   1 
ATOM   4163 C CA  . ILE B 1 138 ? -18.587 -15.211 24.348  1.00 30.72 ?  138 ILE B CA  1 
ATOM   4164 C C   . ILE B 1 138 ? -18.379 -15.222 25.866  1.00 29.37 ?  138 ILE B C   1 
ATOM   4165 O O   . ILE B 1 138 ? -17.706 -16.103 26.350  1.00 29.46 ?  138 ILE B O   1 
ATOM   4166 C CB  . ILE B 1 138 ? -19.486 -16.354 23.849  1.00 33.98 ?  138 ILE B CB  1 
ATOM   4167 C CG1 . ILE B 1 138 ? -19.586 -16.369 22.323  1.00 34.08 ?  138 ILE B CG1 1 
ATOM   4168 C CG2 . ILE B 1 138 ? -20.855 -16.294 24.504  1.00 41.17 ?  138 ILE B CG2 1 
ATOM   4169 C CD1 . ILE B 1 138 ? -20.103 -15.084 21.724  1.00 37.80 ?  138 ILE B CD1 1 
ATOM   4170 N N   . TYR B 1 139 ? -18.951 -14.245 26.542  1.00 32.94 ?  139 TYR B N   1 
ATOM   4171 C CA  . TYR B 1 139 ? -18.873 -14.144 28.014  1.00 33.50 ?  139 TYR B CA  1 
ATOM   4172 C C   . TYR B 1 139 ? -20.160 -14.670 28.652  1.00 37.54 ?  139 TYR B C   1 
ATOM   4173 O O   . TYR B 1 139 ? -21.144 -13.941 28.689  1.00 37.58 ?  139 TYR B O   1 
ATOM   4174 C CB  . TYR B 1 139 ? -18.662 -12.696 28.452  1.00 31.44 ?  139 TYR B CB  1 
ATOM   4175 C CG  . TYR B 1 139 ? -18.448 -12.514 29.927  1.00 32.44 ?  139 TYR B CG  1 
ATOM   4176 C CD1 . TYR B 1 139 ? -17.412 -13.150 30.578  1.00 32.02 ?  139 TYR B CD1 1 
ATOM   4177 C CD2 . TYR B 1 139 ? -19.292 -11.714 30.670  1.00 33.08 ?  139 TYR B CD2 1 
ATOM   4178 C CE1 . TYR B 1 139 ? -17.215 -12.980 31.933  1.00 33.11 ?  139 TYR B CE1 1 
ATOM   4179 C CE2 . TYR B 1 139 ? -19.108 -11.534 32.026  1.00 32.01 ?  139 TYR B CE2 1 
ATOM   4180 C CZ  . TYR B 1 139 ? -18.063 -12.171 32.661  1.00 32.96 ?  139 TYR B CZ  1 
ATOM   4181 O OH  . TYR B 1 139 ? -17.879 -11.993 33.996  1.00 33.20 ?  139 TYR B OH  1 
ATOM   4182 N N   . GLU B 1 140 ? -20.109 -15.899 29.138  1.00 39.88 ?  140 GLU B N   1 
ATOM   4183 C CA  . GLU B 1 140 ? -21.247 -16.517 29.850  1.00 41.36 ?  140 GLU B CA  1 
ATOM   4184 C C   . GLU B 1 140 ? -20.623 -17.347 30.967  1.00 42.18 ?  140 GLU B C   1 
ATOM   4185 O O   . GLU B 1 140 ? -19.588 -17.974 30.701  1.00 41.10 ?  140 GLU B O   1 
ATOM   4186 C CB  . GLU B 1 140 ? -22.122 -17.338 28.907  1.00 44.40 ?  140 GLU B CB  1 
ATOM   4187 C CG  . GLU B 1 140 ? -21.340 -18.110 27.864  1.00 45.18 ?  140 GLU B CG  1 
ATOM   4188 C CD  . GLU B 1 140 ? -22.092 -19.255 27.212  1.00 58.09 ?  140 GLU B CD  1 
ATOM   4189 O OE1 . GLU B 1 140 ? -21.768 -20.419 27.517  1.00 64.38 ?  140 GLU B OE1 1 
ATOM   4190 O OE2 . GLU B 1 140 ? -22.989 -18.978 26.391  1.00 58.28 -1 140 GLU B OE2 1 
ATOM   4191 N N   . ASN B 1 141 ? -21.214 -17.305 32.158  1.00 43.29 ?  141 ASN B N   1 
ATOM   4192 C CA  . ASN B 1 141 ? -20.660 -17.967 33.345  1.00 49.06 ?  141 ASN B CA  1 
ATOM   4193 C C   . ASN B 1 141 ? -19.305 -17.467 33.751  1.00 43.72 ?  141 ASN B C   1 
ATOM   4194 O O   . ASN B 1 141 ? -18.470 -18.267 34.180  1.00 49.66 ?  141 ASN B O   1 
ATOM   4195 C CB  . ASN B 1 141 ? -20.551 -19.463 33.187  1.00 53.35 ?  141 ASN B CB  1 
ATOM   4196 C CG  . ASN B 1 141 ? -21.856 -20.111 33.291  1.00 59.86 ?  141 ASN B CG  1 
ATOM   4197 O OD1 . ASN B 1 141 ? -22.618 -19.850 34.217  1.00 62.80 ?  141 ASN B OD1 1 
ATOM   4198 N ND2 . ASN B 1 141 ? -22.154 -20.998 32.319  1.00 59.46 ?  141 ASN B ND2 1 
ATOM   4199 N N   . SER B 1 142 ? -19.067 -16.169 33.643  1.00 41.90 ?  142 SER B N   1 
ATOM   4200 C CA  . SER B 1 142 ? -17.811 -15.637 34.140  1.00 37.45 ?  142 SER B CA  1 
ATOM   4201 C C   . SER B 1 142 ? -16.636 -16.281 33.424  1.00 41.17 ?  142 SER B C   1 
ATOM   4202 O O   . SER B 1 142 ? -15.508 -16.266 33.926  1.00 37.74 ?  142 SER B O   1 
ATOM   4203 C CB  . SER B 1 142 ? -17.723 -15.832 35.659  1.00 41.88 ?  142 SER B CB  1 
ATOM   4204 O OG  . SER B 1 142 ? -19.004 -15.644 36.245  1.00 41.61 ?  142 SER B OG  1 
ATOM   4205 N N   . LYS B 1 143 ? -16.912 -17.061 32.240  1.00 38.00 ?  143 LYS B N   1 
ATOM   4206 C CA  . LYS B 1 143 ? -15.906 -17.630 31.363  1.00 40.07 ?  143 LYS B CA  1 
ATOM   4207 C C   . LYS B 1 143 ? -16.047 -16.991 29.991  1.00 36.49 ?  143 LYS B C   1 
ATOM   4208 O O   . LYS B 1 143 ? -17.156 -16.620 29.565  1.00 32.39 ?  143 LYS B O   1 
ATOM   4209 C CB  . LYS B 1 143 ? -16.037 -19.169 31.258  1.00 36.55 ?  143 LYS B CB  1 
ATOM   4210 C CG  . LYS B 1 143 ? -15.796 -19.922 32.565  1.00 46.11 ?  143 LYS B CG  1 
ATOM   4211 C CD  . LYS B 1 143 ? -14.341 -19.829 33.008  1.00 44.03 ?  143 LYS B CD  1 
ATOM   4212 C CE  . LYS B 1 143 ? -14.094 -20.664 34.259  1.00 43.05 ?  143 LYS B CE  1 
ATOM   4213 N NZ  . LYS B 1 143 ? -14.726 -20.070 35.472  1.00 51.15 1  143 LYS B NZ  1 
ATOM   4214 N N   . TYR B 1 144 ? -14.911 -16.896 29.308  1.00 33.01 ?  144 TYR B N   1 
ATOM   4215 C CA  . TYR B 1 144 ? -14.968 -16.509 27.888  1.00 30.28 ?  144 TYR B CA  1 
ATOM   4216 C C   . TYR B 1 144 ? -14.827 -17.798 27.068  1.00 32.68 ?  144 TYR B C   1 
ATOM   4217 O O   . TYR B 1 144 ? -14.077 -18.700 27.453  1.00 32.13 ?  144 TYR B O   1 
ATOM   4218 C CB  . TYR B 1 144 ? -13.878 -15.515 27.517  1.00 26.18 ?  144 TYR B CB  1 
ATOM   4219 C CG  . TYR B 1 144 ? -14.123 -14.103 27.958  1.00 22.67 ?  144 TYR B CG  1 
ATOM   4220 C CD1 . TYR B 1 144 ? -14.864 -13.227 27.189  1.00 27.16 ?  144 TYR B CD1 1 
ATOM   4221 C CD2 . TYR B 1 144 ? -13.585 -13.640 29.140  1.00 28.47 ?  144 TYR B CD2 1 
ATOM   4222 C CE1 . TYR B 1 144 ? -15.069 -11.920 27.587  1.00 28.04 ?  144 TYR B CE1 1 
ATOM   4223 C CE2 . TYR B 1 144 ? -13.782 -12.337 29.551  1.00 24.84 ?  144 TYR B CE2 1 
ATOM   4224 C CZ  . TYR B 1 144 ? -14.522 -11.474 28.775  1.00 26.89 ?  144 TYR B CZ  1 
ATOM   4225 O OH  . TYR B 1 144 ? -14.703 -10.200 29.205  1.00 23.99 ?  144 TYR B OH  1 
ATOM   4226 N N   . SER B 1 145 ? -15.541 -17.853 25.951  1.00 32.71 ?  145 SER B N   1 
ATOM   4227 C CA  . SER B 1 145 ? -15.471 -19.027 25.069  1.00 34.47 ?  145 SER B CA  1 
ATOM   4228 C C   . SER B 1 145 ? -15.267 -18.556 23.627  1.00 32.40 ?  145 SER B C   1 
ATOM   4229 O O   . SER B 1 145 ? -15.699 -17.479 23.292  1.00 29.39 ?  145 SER B O   1 
ATOM   4230 C CB  . SER B 1 145 ? -16.728 -19.865 25.206  1.00 33.98 ?  145 SER B CB  1 
ATOM   4231 O OG  . SER B 1 145 ? -17.828 -19.080 25.623  1.00 40.88 ?  145 SER B OG  1 
ATOM   4232 N N   . VAL B 1 146 ? -14.654 -19.392 22.810  1.00 36.32 ?  146 VAL B N   1 
ATOM   4233 C CA  . VAL B 1 146 ? -14.524 -19.058 21.364  1.00 35.27 ?  146 VAL B CA  1 
ATOM   4234 C C   . VAL B 1 146 ? -15.820 -19.419 20.637  1.00 40.13 ?  146 VAL B C   1 
ATOM   4235 O O   . VAL B 1 146 ? -16.343 -20.510 20.898  1.00 37.82 ?  146 VAL B O   1 
ATOM   4236 C CB  . VAL B 1 146 ? -13.337 -19.790 20.719  1.00 35.30 ?  146 VAL B CB  1 
ATOM   4237 C CG1 . VAL B 1 146 ? -13.256 -19.557 19.222  1.00 37.63 ?  146 VAL B CG1 1 
ATOM   4238 C CG2 . VAL B 1 146 ? -12.022 -19.428 21.361  1.00 36.77 ?  146 VAL B CG2 1 
ATOM   4239 N N   . ASN B 1 147 ? -16.339 -18.509 19.800  1.00 38.69 ?  147 ASN B N   1 
ATOM   4240 C CA  . ASN B 1 147 ? -17.474 -18.858 18.915  1.00 37.17 ?  147 ASN B CA  1 
ATOM   4241 C C   . ASN B 1 147 ? -16.820 -19.454 17.673  1.00 33.26 ?  147 ASN B C   1 
ATOM   4242 O O   . ASN B 1 147 ? -16.479 -18.697 16.788  1.00 31.51 ?  147 ASN B O   1 
ATOM   4243 C CB  . ASN B 1 147 ? -18.364 -17.667 18.567  1.00 36.00 ?  147 ASN B CB  1 
ATOM   4244 C CG  . ASN B 1 147 ? -19.639 -18.044 17.845  1.00 36.62 ?  147 ASN B CG  1 
ATOM   4245 O OD1 . ASN B 1 147 ? -19.673 -18.998 17.080  1.00 35.78 ?  147 ASN B OD1 1 
ATOM   4246 N ND2 . ASN B 1 147 ? -20.690 -17.271 18.057  1.00 44.49 ?  147 ASN B ND2 1 
ATOM   4247 N N   . TRP B 1 148 ? -16.645 -20.762 17.655  1.00 35.05 ?  148 TRP B N   1 
ATOM   4248 C CA  . TRP B 1 148 ? -15.974 -21.434 16.548  1.00 34.10 ?  148 TRP B CA  1 
ATOM   4249 C C   . TRP B 1 148 ? -16.713 -21.227 15.237  1.00 31.43 ?  148 TRP B C   1 
ATOM   4250 O O   . TRP B 1 148 ? -16.082 -21.010 14.197  1.00 32.15 ?  148 TRP B O   1 
ATOM   4251 C CB  . TRP B 1 148 ? -15.815 -22.926 16.853  1.00 37.25 ?  148 TRP B CB  1 
ATOM   4252 C CG  . TRP B 1 148 ? -14.880 -23.182 17.985  1.00 38.19 ?  148 TRP B CG  1 
ATOM   4253 C CD1 . TRP B 1 148 ? -15.215 -23.537 19.258  1.00 38.62 ?  148 TRP B CD1 1 
ATOM   4254 C CD2 . TRP B 1 148 ? -13.451 -23.091 17.959  1.00 34.62 ?  148 TRP B CD2 1 
ATOM   4255 N NE1 . TRP B 1 148 ? -14.093 -23.661 20.028  1.00 35.83 ?  148 TRP B NE1 1 
ATOM   4256 C CE2 . TRP B 1 148 ? -12.993 -23.398 19.255  1.00 38.93 ?  148 TRP B CE2 1 
ATOM   4257 C CE3 . TRP B 1 148 ? -12.516 -22.784 16.966  1.00 34.70 ?  148 TRP B CE3 1 
ATOM   4258 C CZ2 . TRP B 1 148 ? -11.638 -23.410 19.587  1.00 39.54 ?  148 TRP B CZ2 1 
ATOM   4259 C CZ3 . TRP B 1 148 ? -11.167 -22.801 17.297  1.00 34.96 ?  148 TRP B CZ3 1 
ATOM   4260 C CH2 . TRP B 1 148 ? -10.744 -23.107 18.597  1.00 36.50 ?  148 TRP B CH2 1 
ATOM   4261 N N   . ALA B 1 149 ? -18.046 -21.271 15.261  1.00 32.46 ?  149 ALA B N   1 
ATOM   4262 C CA  . ALA B 1 149 ? -18.808 -21.076 14.028  1.00 32.19 ?  149 ALA B CA  1 
ATOM   4263 C C   . ALA B 1 149 ? -18.608 -19.670 13.477  1.00 32.19 ?  149 ALA B C   1 
ATOM   4264 O O   . ALA B 1 149 ? -18.420 -19.475 12.265  1.00 29.83 ?  149 ALA B O   1 
ATOM   4265 C CB  . ALA B 1 149 ? -20.291 -21.346 14.286  1.00 34.80 ?  149 ALA B CB  1 
ATOM   4266 N N   . ASP B 1 150 ? -18.673 -18.668 14.358  1.00 32.34 ?  150 ASP B N   1 
ATOM   4267 C CA  . ASP B 1 150 ? -18.446 -17.291 13.931  1.00 32.45 ?  150 ASP B CA  1 
ATOM   4268 C C   . ASP B 1 150 ? -17.009 -17.109 13.470  1.00 30.31 ?  150 ASP B C   1 
ATOM   4269 O O   . ASP B 1 150 ? -16.744 -16.441 12.460  1.00 27.40 ?  150 ASP B O   1 
ATOM   4270 C CB  . ASP B 1 150 ? -18.777 -16.337 15.080  1.00 31.76 ?  150 ASP B CB  1 
ATOM   4271 C CG  . ASP B 1 150 ? -18.566 -14.891 14.723  1.00 34.03 ?  150 ASP B CG  1 
ATOM   4272 O OD1 . ASP B 1 150 ? -19.367 -14.356 13.941  1.00 33.88 ?  150 ASP B OD1 1 
ATOM   4273 O OD2 . ASP B 1 150 ? -17.593 -14.283 15.228  1.00 33.19 -1 150 ASP B OD2 1 
ATOM   4274 N N   . LEU B 1 151 ? -16.070 -17.722 14.193  1.00 28.60 ?  151 LEU B N   1 
ATOM   4275 C CA  . LEU B 1 151 ? -14.669 -17.675 13.797  1.00 28.04 ?  151 LEU B CA  1 
ATOM   4276 C C   . LEU B 1 151 ? -14.479 -18.219 12.390  1.00 28.95 ?  151 LEU B C   1 
ATOM   4277 O O   . LEU B 1 151 ? -13.827 -17.584 11.552  1.00 28.62 ?  151 LEU B O   1 
ATOM   4278 C CB  . LEU B 1 151 ? -13.822 -18.462 14.792  1.00 27.58 ?  151 LEU B CB  1 
ATOM   4279 C CG  . LEU B 1 151 ? -12.330 -18.461 14.475  1.00 30.67 ?  151 LEU B CG  1 
ATOM   4280 C CD1 . LEU B 1 151 ? -11.827 -17.029 14.283  1.00 25.00 ?  151 LEU B CD1 1 
ATOM   4281 C CD2 . LEU B 1 151 ? -11.548 -19.183 15.551  1.00 30.82 ?  151 LEU B CD2 1 
ATOM   4282 N N   . GLU B 1 152 ? -15.056 -19.393 12.098  1.00 27.72 ?  152 GLU B N   1 
ATOM   4283 C CA  . GLU B 1 152 ? -14.835 -19.972 10.771  1.00 31.14 ?  152 GLU B CA  1 
ATOM   4284 C C   . GLU B 1 152 ? -15.480 -19.136 9.674   1.00 25.84 ?  152 GLU B C   1 
ATOM   4285 O O   . GLU B 1 152 ? -14.881 -18.944 8.610   1.00 31.88 ?  152 GLU B O   1 
ATOM   4286 C CB  . GLU B 1 152 ? -15.341 -21.410 10.683  1.00 36.29 ?  152 GLU B CB  1 
ATOM   4287 C CG  . GLU B 1 152 ? -14.532 -22.195 9.632   1.00 39.63 ?  152 GLU B CG  1 
ATOM   4288 C CD  . GLU B 1 152 ? -15.282 -23.317 8.976   1.00 46.01 ?  152 GLU B CD  1 
ATOM   4289 O OE1 . GLU B 1 152 ? -14.886 -24.478 9.196   1.00 51.76 ?  152 GLU B OE1 1 
ATOM   4290 O OE2 . GLU B 1 152 ? -16.239 -23.045 8.217   1.00 49.33 -1 152 GLU B OE2 1 
ATOM   4291 N N   . GLU B 1 153 ? -16.705 -18.653 9.890   1.00 29.10 ?  153 GLU B N   1 
ATOM   4292 C CA  . GLU B 1 153 ? -17.347 -17.840 8.862   1.00 29.18 ?  153 GLU B CA  1 
ATOM   4293 C C   . GLU B 1 153 ? -16.540 -16.585 8.567   1.00 28.55 ?  153 GLU B C   1 
ATOM   4294 O O   . GLU B 1 153 ? -16.476 -16.126 7.418   1.00 27.26 ?  153 GLU B O   1 
ATOM   4295 C CB  . GLU B 1 153 ? -18.762 -17.456 9.282   1.00 33.49 ?  153 GLU B CB  1 
ATOM   4296 C CG  . GLU B 1 153 ? -19.545 -16.819 8.151   1.00 40.80 ?  153 GLU B CG  1 
ATOM   4297 C CD  . GLU B 1 153 ? -20.743 -16.029 8.626   1.00 48.62 ?  153 GLU B CD  1 
ATOM   4298 O OE1 . GLU B 1 153 ? -20.625 -15.333 9.656   1.00 50.00 ?  153 GLU B OE1 1 
ATOM   4299 O OE2 . GLU B 1 153 ? -21.799 -16.098 7.956   1.00 54.88 -1 153 GLU B OE2 1 
ATOM   4300 N N   . LYS B 1 154 ? -15.920 -16.011 9.588   1.00 25.56 ?  154 LYS B N   1 
ATOM   4301 C CA  . LYS B 1 154 ? -15.172 -14.787 9.345   1.00 27.79 ?  154 LYS B CA  1 
ATOM   4302 C C   . LYS B 1 154 ? -13.827 -15.086 8.700   1.00 23.44 ?  154 LYS B C   1 
ATOM   4303 O O   . LYS B 1 154 ? -13.454 -14.430 7.718   1.00 26.10 ?  154 LYS B O   1 
ATOM   4304 C CB  . LYS B 1 154 ? -15.039 -14.006 10.645  1.00 28.15 ?  154 LYS B CB  1 
ATOM   4305 C CG  . LYS B 1 154 ? -16.378 -13.445 11.082  1.00 25.39 ?  154 LYS B CG  1 
ATOM   4306 C CD  . LYS B 1 154 ? -16.326 -12.768 12.434  1.00 25.82 ?  154 LYS B CD  1 
ATOM   4307 C CE  . LYS B 1 154 ? -17.510 -11.804 12.604  1.00 24.44 ?  154 LYS B CE  1 
ATOM   4308 N NZ  . LYS B 1 154 ? -17.956 -11.674 14.033  1.00 28.12 1  154 LYS B NZ  1 
ATOM   4309 N N   . LEU B 1 155 ? -13.123 -16.121 9.182   1.00 25.16 ?  155 LEU B N   1 
ATOM   4310 C CA  . LEU B 1 155 ? -11.892 -16.540 8.522   1.00 24.38 ?  155 LEU B CA  1 
ATOM   4311 C C   . LEU B 1 155 ? -12.132 -16.907 7.057   1.00 27.53 ?  155 LEU B C   1 
ATOM   4312 O O   . LEU B 1 155 ? -11.250 -16.699 6.212   1.00 26.62 ?  155 LEU B O   1 
ATOM   4313 C CB  . LEU B 1 155 ? -11.269 -17.713 9.277   1.00 24.84 ?  155 LEU B CB  1 
ATOM   4314 C CG  . LEU B 1 155 ? -10.655 -17.386 10.653  1.00 29.24 ?  155 LEU B CG  1 
ATOM   4315 C CD1 . LEU B 1 155 ? -10.201 -18.668 11.360  1.00 26.93 ?  155 LEU B CD1 1 
ATOM   4316 C CD2 . LEU B 1 155 ? -9.495  -16.388 10.572  1.00 22.97 ?  155 LEU B CD2 1 
ATOM   4317 N N   . ALA B 1 156 ? -13.322 -17.425 6.736   1.00 24.31 ?  156 ALA B N   1 
ATOM   4318 C CA  . ALA B 1 156 ? -13.661 -17.771 5.357   1.00 29.06 ?  156 ALA B CA  1 
ATOM   4319 C C   . ALA B 1 156 ? -13.889 -16.555 4.469   1.00 29.23 ?  156 ALA B C   1 
ATOM   4320 O O   . ALA B 1 156 ? -13.918 -16.704 3.239   1.00 26.70 ?  156 ALA B O   1 
ATOM   4321 C CB  . ALA B 1 156 ? -14.922 -18.637 5.328   1.00 29.95 ?  156 ALA B CB  1 
ATOM   4322 N N   . THR B 1 157 ? -14.084 -15.375 5.053   1.00 26.14 ?  157 THR B N   1 
ATOM   4323 C CA  . THR B 1 157 ? -14.348 -14.176 4.262   1.00 25.72 ?  157 THR B CA  1 
ATOM   4324 C C   . THR B 1 157 ? -13.129 -13.853 3.408   1.00 25.75 ?  157 THR B C   1 
ATOM   4325 O O   . THR B 1 157 ? -12.003 -13.872 3.923   1.00 29.26 ?  157 THR B O   1 
ATOM   4326 C CB  . THR B 1 157 ? -14.676 -13.003 5.182   1.00 30.10 ?  157 THR B CB  1 
ATOM   4327 O OG1 . THR B 1 157 ? -15.812 -13.351 5.978   1.00 32.30 ?  157 THR B OG1 1 
ATOM   4328 C CG2 . THR B 1 157 ? -14.984 -11.731 4.385   1.00 26.82 ?  157 THR B CG2 1 
ATOM   4329 N N   . PRO B 1 158 ? -13.299 -13.603 2.104   1.00 28.22 ?  158 PRO B N   1 
ATOM   4330 C CA  . PRO B 1 158 ? -12.122 -13.347 1.257   1.00 28.40 ?  158 PRO B CA  1 
ATOM   4331 C C   . PRO B 1 158 ? -11.256 -12.189 1.737   1.00 24.38 ?  158 PRO B C   1 
ATOM   4332 O O   . PRO B 1 158 ? -10.027 -12.307 1.699   1.00 26.60 ?  158 PRO B O   1 
ATOM   4333 C CB  . PRO B 1 158 ? -12.742 -13.067 -0.124  1.00 29.79 ?  158 PRO B CB  1 
ATOM   4334 C CG  . PRO B 1 158 ? -14.061 -13.822 -0.089  1.00 27.45 ?  158 PRO B CG  1 
ATOM   4335 C CD  . PRO B 1 158 ? -14.548 -13.690 1.317   1.00 26.81 ?  158 PRO B CD  1 
ATOM   4336 N N   . SER B 1 159 ? -11.850 -11.079 2.191   1.00 23.80 ?  159 SER B N   1 
ATOM   4337 C CA  . SER B 1 159 ? -11.054 -9.938  2.635   1.00 24.03 ?  159 SER B CA  1 
ATOM   4338 C C   . SER B 1 159 ? -10.379 -10.166 3.989   1.00 22.15 ?  159 SER B C   1 
ATOM   4339 O O   . SER B 1 159 ? -9.544  -9.346  4.389   1.00 23.35 ?  159 SER B O   1 
ATOM   4340 C CB  . SER B 1 159 ? -11.927 -8.676  2.713   1.00 25.67 ?  159 SER B CB  1 
ATOM   4341 O OG  . SER B 1 159 ? -13.053 -8.912  3.551   1.00 30.01 ?  159 SER B OG  1 
ATOM   4342 N N   . VAL B 1 160 ? -10.747 -11.219 4.709   1.00 20.46 ?  160 VAL B N   1 
ATOM   4343 C CA  . VAL B 1 160 ? -10.054 -11.531 5.996   1.00 23.14 ?  160 VAL B CA  1 
ATOM   4344 C C   . VAL B 1 160 ? -8.765  -12.297 5.660   1.00 26.83 ?  160 VAL B C   1 
ATOM   4345 O O   . VAL B 1 160 ? -8.865  -13.422 5.248   1.00 24.64 ?  160 VAL B O   1 
ATOM   4346 C CB  . VAL B 1 160 ? -10.968 -12.229 7.022   1.00 25.34 ?  160 VAL B CB  1 
ATOM   4347 C CG1 . VAL B 1 160 ? -10.222 -12.634 8.280   1.00 21.61 ?  160 VAL B CG1 1 
ATOM   4348 C CG2 . VAL B 1 160 ? -12.179 -11.380 7.359   1.00 21.90 ?  160 VAL B CG2 1 
ATOM   4349 N N   . ARG B 1 161 ? -7.599  -11.683 5.857   1.00 22.96 ?  161 ARG B N   1 
ATOM   4350 C CA  . ARG B 1 161 ? -6.323  -12.275 5.377   1.00 20.70 ?  161 ARG B CA  1 
ATOM   4351 C C   . ARG B 1 161 ? -5.345  -12.644 6.492   1.00 19.87 ?  161 ARG B C   1 
ATOM   4352 O O   . ARG B 1 161 ? -4.351  -13.295 6.201   1.00 20.39 ?  161 ARG B O   1 
ATOM   4353 C CB  . ARG B 1 161 ? -5.632  -11.207 4.536   1.00 23.86 ?  161 ARG B CB  1 
ATOM   4354 C CG  . ARG B 1 161 ? -6.315  -10.930 3.209   1.00 29.36 ?  161 ARG B CG  1 
ATOM   4355 C CD  . ARG B 1 161 ? -5.656  -11.747 2.124   1.00 36.72 ?  161 ARG B CD  1 
ATOM   4356 N NE  . ARG B 1 161 ? -6.366  -12.998 2.002   1.00 33.56 ?  161 ARG B NE  1 
ATOM   4357 C CZ  . ARG B 1 161 ? -5.799  -14.190 2.093   1.00 42.70 ?  161 ARG B CZ  1 
ATOM   4358 N NH1 . ARG B 1 161 ? -4.496  -14.287 2.292   1.00 41.15 1  161 ARG B NH1 1 
ATOM   4359 N NH2 . ARG B 1 161 ? -6.537  -15.277 1.975   1.00 43.30 ?  161 ARG B NH2 1 
ATOM   4360 N N   . MET B 1 162 ? -5.647  -12.209 7.710   1.00 20.22 ?  162 MET B N   1 
ATOM   4361 C CA  . MET B 1 162 ? -4.714  -12.432 8.826   1.00 21.18 ?  162 MET B CA  1 
ATOM   4362 C C   . MET B 1 162 ? -5.482  -12.476 10.128  1.00 21.21 ?  162 MET B C   1 
ATOM   4363 O O   . MET B 1 162 ? -6.500  -11.821 10.217  1.00 22.99 ?  162 MET B O   1 
ATOM   4364 C CB  . MET B 1 162 ? -3.645  -11.333 8.903   1.00 19.95 ?  162 MET B CB  1 
ATOM   4365 C CG  . MET B 1 162 ? -2.779  -11.326 10.139  1.00 18.69 ?  162 MET B CG  1 
ATOM   4366 S SD  . MET B 1 162 ? -1.516  -10.034 10.074  1.00 21.49 ?  162 MET B SD  1 
ATOM   4367 C CE  . MET B 1 162 ? -0.505  -10.647 8.731   1.00 22.34 ?  162 MET B CE  1 
ATOM   4368 N N   . MET B 1 163 ? -5.083  -13.370 11.001  1.00 21.60 ?  163 MET B N   1 
ATOM   4369 C CA  . MET B 1 163 ? -5.613  -13.397 12.354  1.00 18.94 ?  163 MET B CA  1 
ATOM   4370 C C   . MET B 1 163 ? -4.468  -13.064 13.295  1.00 20.99 ?  163 MET B C   1 
ATOM   4371 O O   . MET B 1 163 ? -3.402  -13.679 13.216  1.00 22.11 ?  163 MET B O   1 
ATOM   4372 C CB  . MET B 1 163 ? -6.215  -14.761 12.701  1.00 19.08 ?  163 MET B CB  1 
ATOM   4373 C CG  . MET B 1 163 ? -6.516  -14.943 14.179  1.00 20.64 ?  163 MET B CG  1 
ATOM   4374 S SD  . MET B 1 163 ? -7.487  -16.445 14.388  1.00 25.36 ?  163 MET B SD  1 
ATOM   4375 C CE  . MET B 1 163 ? -7.975  -16.298 16.108  1.00 24.54 ?  163 MET B CE  1 
ATOM   4376 N N   . VAL B 1 164 ? -4.669  -12.059 14.143  1.00 20.43 ?  164 VAL B N   1 
ATOM   4377 C CA  . VAL B 1 164 ? -3.735  -11.746 15.214  1.00 20.28 ?  164 VAL B CA  1 
ATOM   4378 C C   . VAL B 1 164 ? -4.299  -12.378 16.475  1.00 20.56 ?  164 VAL B C   1 
ATOM   4379 O O   . VAL B 1 164 ? -5.311  -11.920 17.019  1.00 21.06 ?  164 VAL B O   1 
ATOM   4380 C CB  . VAL B 1 164 ? -3.513  -10.240 15.382  1.00 20.88 ?  164 VAL B CB  1 
ATOM   4381 C CG1 . VAL B 1 164 ? -2.480  -10.009 16.467  1.00 22.26 ?  164 VAL B CG1 1 
ATOM   4382 C CG2 . VAL B 1 164 ? -3.023  -9.637  14.069  1.00 23.67 ?  164 VAL B CG2 1 
ATOM   4383 N N   . PHE B 1 165 ? -3.626  -13.446 16.885  1.00 19.79 ?  165 PHE B N   1 
ATOM   4384 C CA  . PHE B 1 165 ? -4.070  -14.298 17.999  1.00 21.30 ?  165 PHE B CA  1 
ATOM   4385 C C   . PHE B 1 165 ? -3.170  -14.034 19.200  1.00 21.52 ?  165 PHE B C   1 
ATOM   4386 O O   . PHE B 1 165 ? -1.967  -14.025 19.057  1.00 22.77 ?  165 PHE B O   1 
ATOM   4387 C CB  . PHE B 1 165 ? -3.857  -15.732 17.524  1.00 20.05 ?  165 PHE B CB  1 
ATOM   4388 C CG  . PHE B 1 165 ? -4.188  -16.879 18.438  1.00 22.75 ?  165 PHE B CG  1 
ATOM   4389 C CD1 . PHE B 1 165 ? -5.396  -16.943 19.103  1.00 21.18 ?  165 PHE B CD1 1 
ATOM   4390 C CD2 . PHE B 1 165 ? -3.309  -17.941 18.564  1.00 22.39 ?  165 PHE B CD2 1 
ATOM   4391 C CE1 . PHE B 1 165 ? -5.689  -18.019 19.921  1.00 23.48 ?  165 PHE B CE1 1 
ATOM   4392 C CE2 . PHE B 1 165 ? -3.611  -19.020 19.375  1.00 23.74 ?  165 PHE B CE2 1 
ATOM   4393 C CZ  . PHE B 1 165 ? -4.801  -19.057 20.051  1.00 23.50 ?  165 PHE B CZ  1 
ATOM   4394 N N   . CYS B 1 166 ? -3.796  -13.800 20.325  1.00 19.78 ?  166 CYS B N   1 
ATOM   4395 C CA  . CYS B 1 166 ? -3.070  -13.554 21.598  1.00 20.27 ?  166 CYS B CA  1 
ATOM   4396 C C   . CYS B 1 166 ? -3.014  -14.871 22.375  1.00 21.52 ?  166 CYS B C   1 
ATOM   4397 O O   . CYS B 1 166 ? -4.039  -15.289 22.844  1.00 20.72 ?  166 CYS B O   1 
ATOM   4398 C CB  . CYS B 1 166 ? -3.687  -12.416 22.396  1.00 22.18 ?  166 CYS B CB  1 
ATOM   4399 S SG  . CYS B 1 166 ? -2.521  -11.532 23.458  1.00 22.11 ?  166 CYS B SG  1 
ATOM   4400 N N   . ASN B 1 167 ? -1.834  -15.477 22.466  1.00 19.75 ?  167 ASN B N   1 
ATOM   4401 C CA  . ASN B 1 167 ? -1.682  -16.816 23.075  1.00 18.66 ?  167 ASN B CA  1 
ATOM   4402 C C   . ASN B 1 167 ? -0.484  -16.838 24.027  1.00 19.41 ?  167 ASN B C   1 
ATOM   4403 O O   . ASN B 1 167 ? 0.586   -17.064 23.571  1.00 23.39 ?  167 ASN B O   1 
ATOM   4404 C CB  . ASN B 1 167 ? -1.445  -17.824 21.953  1.00 20.84 ?  167 ASN B CB  1 
ATOM   4405 C CG  . ASN B 1 167 ? -1.186  -19.233 22.427  1.00 21.38 ?  167 ASN B CG  1 
ATOM   4406 O OD1 . ASN B 1 167 ? -1.694  -19.643 23.459  1.00 24.14 ?  167 ASN B OD1 1 
ATOM   4407 N ND2 . ASN B 1 167 ? -0.381  -19.959 21.676  1.00 24.19 ?  167 ASN B ND2 1 
ATOM   4408 N N   . PRO B 1 168 ? -0.642  -16.667 25.346  1.00 21.18 ?  168 PRO B N   1 
ATOM   4409 C CA  . PRO B 1 168 ? -1.927  -16.482 25.994  1.00 19.80 ?  168 PRO B CA  1 
ATOM   4410 C C   . PRO B 1 168 ? -2.666  -15.165 25.731  1.00 21.41 ?  168 PRO B C   1 
ATOM   4411 O O   . PRO B 1 168 ? -2.017  -14.217 25.399  1.00 22.20 ?  168 PRO B O   1 
ATOM   4412 C CB  . PRO B 1 168 ? -1.546  -16.531 27.471  1.00 21.34 ?  168 PRO B CB  1 
ATOM   4413 C CG  . PRO B 1 168 ? -0.281  -17.317 27.496  1.00 25.16 ?  168 PRO B CG  1 
ATOM   4414 C CD  . PRO B 1 168 ? 0.432   -16.734 26.307  1.00 22.63 ?  168 PRO B CD  1 
ATOM   4415 N N   . HIS B 1 169 ? -3.965  -15.123 25.998  1.00 20.56 ?  169 HIS B N   1 
ATOM   4416 C CA  . HIS B 1 169 ? -4.793  -13.976 25.628  1.00 19.87 ?  169 HIS B CA  1 
ATOM   4417 C C   . HIS B 1 169 ? -4.803  -12.947 26.751  1.00 21.48 ?  169 HIS B C   1 
ATOM   4418 O O   . HIS B 1 169 ? -5.135  -13.261 27.905  1.00 24.27 ?  169 HIS B O   1 
ATOM   4419 C CB  . HIS B 1 169 ? -6.206  -14.462 25.285  1.00 21.49 ?  169 HIS B CB  1 
ATOM   4420 C CG  . HIS B 1 169 ? -7.082  -13.429 24.635  1.00 19.49 ?  169 HIS B CG  1 
ATOM   4421 N ND1 . HIS B 1 169 ? -7.360  -13.433 23.284  1.00 20.65 ?  169 HIS B ND1 1 
ATOM   4422 C CD2 . HIS B 1 169 ? -7.783  -12.395 25.161  1.00 20.89 ?  169 HIS B CD2 1 
ATOM   4423 C CE1 . HIS B 1 169 ? -8.180  -12.435 23.000  1.00 21.19 ?  169 HIS B CE1 1 
ATOM   4424 N NE2 . HIS B 1 169 ? -8.455  -11.790 24.122  1.00 21.22 ?  169 HIS B NE2 1 
ATOM   4425 N N   . ASN B 1 170 ? -4.384  -11.734 26.417  1.00 19.16 ?  170 ASN B N   1 
ATOM   4426 C CA  . ASN B 1 170 ? -4.414  -10.475 27.153  1.00 19.57 ?  170 ASN B CA  1 
ATOM   4427 C C   . ASN B 1 170 ? -5.642  -9.715  26.689  1.00 20.99 ?  170 ASN B C   1 
ATOM   4428 O O   . ASN B 1 170 ? -5.773  -9.489  25.483  1.00 21.37 ?  170 ASN B O   1 
ATOM   4429 C CB  . ASN B 1 170 ? -3.125  -9.702  26.842  1.00 21.26 ?  170 ASN B CB  1 
ATOM   4430 C CG  . ASN B 1 170 ? -3.102  -8.280  27.358  1.00 22.12 ?  170 ASN B CG  1 
ATOM   4431 O OD1 . ASN B 1 170 ? -3.907  -7.868  28.197  1.00 24.99 ?  170 ASN B OD1 1 
ATOM   4432 N ND2 . ASN B 1 170 ? -2.128  -7.512  26.861  1.00 20.04 ?  170 ASN B ND2 1 
ATOM   4433 N N   . PRO B 1 171 ? -6.565  -9.283  27.571  1.00 22.57 ?  171 PRO B N   1 
ATOM   4434 C CA  . PRO B 1 171 ? -6.462  -9.160  29.033  1.00 19.84 ?  171 PRO B CA  1 
ATOM   4435 C C   . PRO B 1 171 ? -7.127  -10.230 29.899  1.00 23.72 ?  171 PRO B C   1 
ATOM   4436 O O   . PRO B 1 171 ? -7.082  -10.097 31.125  1.00 22.34 ?  171 PRO B O   1 
ATOM   4437 C CB  . PRO B 1 171 ? -7.145  -7.816  29.282  1.00 21.00 ?  171 PRO B CB  1 
ATOM   4438 C CG  . PRO B 1 171 ? -8.285  -7.824  28.260  1.00 22.34 ?  171 PRO B CG  1 
ATOM   4439 C CD  . PRO B 1 171 ? -7.755  -8.580  27.050  1.00 21.99 ?  171 PRO B CD  1 
ATOM   4440 N N   . ILE B 1 172 ? -7.741  -11.250 29.300  1.00 22.56 ?  172 ILE B N   1 
ATOM   4441 C CA  . ILE B 1 172 ? -8.479  -12.228 30.097  1.00 22.98 ?  172 ILE B CA  1 
ATOM   4442 C C   . ILE B 1 172 ? -7.577  -13.259 30.762  1.00 25.34 ?  172 ILE B C   1 
ATOM   4443 O O   . ILE B 1 172 ? -8.041  -13.998 31.641  1.00 24.24 ?  172 ILE B O   1 
ATOM   4444 C CB  . ILE B 1 172 ? -9.539  -12.921 29.221  1.00 19.34 ?  172 ILE B CB  1 
ATOM   4445 C CG1 . ILE B 1 172 ? -8.858  -13.871 28.245  1.00 21.15 ?  172 ILE B CG1 1 
ATOM   4446 C CG2 . ILE B 1 172 ? -10.386 -11.860 28.432  1.00 20.90 ?  172 ILE B CG2 1 
ATOM   4447 C CD1 . ILE B 1 172 ? -9.806  -14.580 27.345  1.00 23.17 ?  172 ILE B CD1 1 
ATOM   4448 N N   . GLY B 1 173 ? -6.307  -13.340 30.377  1.00 23.32 ?  173 GLY B N   1 
ATOM   4449 C CA  . GLY B 1 173 ? -5.382  -14.197 31.103  1.00 25.45 ?  173 GLY B CA  1 
ATOM   4450 C C   . GLY B 1 173 ? -5.555  -15.675 30.827  1.00 29.22 ?  173 GLY B C   1 
ATOM   4451 O O   . GLY B 1 173 ? -5.478  -16.493 31.754  1.00 26.52 ?  173 GLY B O   1 
ATOM   4452 N N   . TYR B 1 174 ? -5.781  -16.045 29.572  1.00 24.12 ?  174 TYR B N   1 
ATOM   4453 C CA  . TYR B 1 174 ? -6.110  -17.419 29.239  1.00 25.02 ?  174 TYR B CA  1 
ATOM   4454 C C   . TYR B 1 174 ? -5.052  -18.007 28.325  1.00 24.58 ?  174 TYR B C   1 
ATOM   4455 O O   . TYR B 1 174 ? -4.875  -17.537 27.195  1.00 22.87 ?  174 TYR B O   1 
ATOM   4456 C CB  . TYR B 1 174 ? -7.474  -17.494 28.565  1.00 26.43 ?  174 TYR B CB  1 
ATOM   4457 C CG  . TYR B 1 174 ? -7.871  -18.900 28.365  1.00 32.13 ?  174 TYR B CG  1 
ATOM   4458 C CD1 . TYR B 1 174 ? -7.927  -19.770 29.444  1.00 36.96 ?  174 TYR B CD1 1 
ATOM   4459 C CD2 . TYR B 1 174 ? -8.165  -19.383 27.102  1.00 34.96 ?  174 TYR B CD2 1 
ATOM   4460 C CE1 . TYR B 1 174 ? -8.282  -21.076 29.274  1.00 35.18 ?  174 TYR B CE1 1 
ATOM   4461 C CE2 . TYR B 1 174 ? -8.525  -20.690 26.920  1.00 35.01 ?  174 TYR B CE2 1 
ATOM   4462 C CZ  . TYR B 1 174 ? -8.581  -21.526 28.011  1.00 40.07 ?  174 TYR B CZ  1 
ATOM   4463 O OH  . TYR B 1 174 ? -8.942  -22.823 27.830  1.00 44.31 ?  174 TYR B OH  1 
ATOM   4464 N N   . ALA B 1 175 ? -4.367  -19.040 28.805  1.00 24.94 ?  175 ALA B N   1 
ATOM   4465 C CA  . ALA B 1 175 ? -3.519  -19.865 27.950  1.00 25.14 ?  175 ALA B CA  1 
ATOM   4466 C C   . ALA B 1 175 ? -4.382  -20.954 27.317  1.00 28.60 ?  175 ALA B C   1 
ATOM   4467 O O   . ALA B 1 175 ? -4.833  -21.880 27.994  1.00 31.30 ?  175 ALA B O   1 
ATOM   4468 C CB  . ALA B 1 175 ? -2.356  -20.469 28.733  1.00 24.80 ?  175 ALA B CB  1 
ATOM   4469 N N   . TRP B 1 176 ? -4.494  -20.779 26.007  1.00 28.44 ?  176 TRP B N   1 
ATOM   4470 C CA  . TRP B 1 176 ? -5.249  -21.710 25.164  1.00 35.01 ?  176 TRP B CA  1 
ATOM   4471 C C   . TRP B 1 176 ? -4.686  -23.125 25.253  1.00 39.32 ?  176 TRP B C   1 
ATOM   4472 O O   . TRP B 1 176 ? -3.497  -23.297 25.432  1.00 36.58 ?  176 TRP B O   1 
ATOM   4473 C CB  . TRP B 1 176 ? -5.286  -21.206 23.712  1.00 36.27 ?  176 TRP B CB  1 
ATOM   4474 C CG  . TRP B 1 176 ? -5.710  -19.782 23.569  1.00 27.70 ?  176 TRP B CG  1 
ATOM   4475 C CD1 . TRP B 1 176 ? -4.890  -18.700 23.489  1.00 25.91 ?  176 TRP B CD1 1 
ATOM   4476 C CD2 . TRP B 1 176 ? -7.052  -19.274 23.476  1.00 32.16 ?  176 TRP B CD2 1 
ATOM   4477 N NE1 . TRP B 1 176 ? -5.628  -17.561 23.359  1.00 23.55 ?  176 TRP B NE1 1 
ATOM   4478 C CE2 . TRP B 1 176 ? -6.954  -17.876 23.347  1.00 24.84 ?  176 TRP B CE2 1 
ATOM   4479 C CE3 . TRP B 1 176 ? -8.320  -19.852 23.486  1.00 34.14 ?  176 TRP B CE3 1 
ATOM   4480 C CZ2 . TRP B 1 176 ? -8.068  -17.051 23.237  1.00 29.16 ?  176 TRP B CZ2 1 
ATOM   4481 C CZ3 . TRP B 1 176 ? -9.422  -19.034 23.401  1.00 39.57 ?  176 TRP B CZ3 1 
ATOM   4482 C CH2 . TRP B 1 176 ? -9.300  -17.653 23.265  1.00 32.17 ?  176 TRP B CH2 1 
ATOM   4483 N N   . SER B 1 177 ? -5.587  -24.089 25.081  1.00 54.77 ?  177 SER B N   1 
ATOM   4484 C CA  . SER B 1 177 ? -5.224  -25.519 25.134  1.00 61.81 ?  177 SER B CA  1 
ATOM   4485 C C   . SER B 1 177 ? -4.522  -25.896 23.849  1.00 62.75 ?  177 SER B C   1 
ATOM   4486 O O   . SER B 1 177 ? -4.692  -25.197 22.844  1.00 62.46 ?  177 SER B O   1 
ATOM   4487 C CB  . SER B 1 177 ? -6.460  -26.390 25.251  1.00 71.85 ?  177 SER B CB  1 
ATOM   4488 O OG  . SER B 1 177 ? -7.101  -26.540 24.002  1.00 67.28 ?  177 SER B OG  1 
ATOM   4489 N N   . GLU B 1 178 ? -3.834  -27.025 23.907  1.00 63.84 ?  178 GLU B N   1 
ATOM   4490 C CA  . GLU B 1 178 ? -3.197  -27.530 22.662  1.00 63.82 ?  178 GLU B CA  1 
ATOM   4491 C C   . GLU B 1 178 ? -4.227  -27.657 21.533  1.00 65.67 ?  178 GLU B C   1 
ATOM   4492 O O   . GLU B 1 178 ? -3.955  -27.204 20.430  1.00 70.26 ?  178 GLU B O   1 
ATOM   4493 C CB  . GLU B 1 178 ? -2.464  -28.847 22.940  1.00 63.74 ?  178 GLU B CB  1 
ATOM   4494 C CG  . GLU B 1 178 ? -1.759  -29.445 21.740  1.00 60.43 ?  178 GLU B CG  1 
ATOM   4495 C CD  . GLU B 1 178 ? -1.043  -30.748 22.049  1.00 54.75 ?  178 GLU B CD  1 
ATOM   4496 O OE1 . GLU B 1 178 ? -0.524  -31.369 21.117  1.00 59.07 ?  178 GLU B OE1 1 
ATOM   4497 O OE2 . GLU B 1 178 ? -1.013  -31.136 23.224  1.00 65.18 -1 178 GLU B OE2 1 
ATOM   4498 N N   . GLU B 1 179 ? -5.368  -28.252 21.830  1.00 62.79 ?  179 GLU B N   1 
ATOM   4499 C CA  . GLU B 1 179 ? -6.434  -28.423 20.828  1.00 60.52 ?  179 GLU B CA  1 
ATOM   4500 C C   . GLU B 1 179 ? -6.839  -27.071 20.251  1.00 53.10 ?  179 GLU B C   1 
ATOM   4501 O O   . GLU B 1 179 ? -6.904  -26.966 19.074  1.00 50.49 ?  179 GLU B O   1 
ATOM   4502 C CB  . GLU B 1 179 ? -7.659  -29.040 21.499  1.00 60.99 ?  179 GLU B CB  1 
ATOM   4503 C CG  . GLU B 1 179 ? -8.461  -29.955 20.604  1.00 62.25 ?  179 GLU B CG  1 
ATOM   4504 C CD  . GLU B 1 179 ? -9.541  -30.709 21.358  1.00 64.12 ?  179 GLU B CD  1 
ATOM   4505 O OE1 . GLU B 1 179 ? -9.232  -31.779 21.912  1.00 64.67 ?  179 GLU B OE1 1 
ATOM   4506 O OE2 . GLU B 1 179 ? -10.677 -30.211 21.408  1.00 64.10 -1 179 GLU B OE2 1 
ATOM   4507 N N   . GLU B 1 180 ? -7.030  -26.070 21.084  1.00 49.12 ?  180 GLU B N   1 
ATOM   4508 C CA  . GLU B 1 180 ? -7.526  -24.768 20.584  1.00 44.11 ?  180 GLU B CA  1 
ATOM   4509 C C   . GLU B 1 180 ? -6.507  -24.138 19.633  1.00 37.40 ?  180 GLU B C   1 
ATOM   4510 O O   . GLU B 1 180 ? -6.904  -23.662 18.581  1.00 34.87 ?  180 GLU B O   1 
ATOM   4511 C CB  . GLU B 1 180 ? -7.852  -23.880 21.773  1.00 47.81 ?  180 GLU B CB  1 
ATOM   4512 C CG  . GLU B 1 180 ? -9.099  -24.298 22.522  1.00 53.82 ?  180 GLU B CG  1 
ATOM   4513 C CD  . GLU B 1 180 ? -9.235  -23.685 23.904  1.00 50.95 ?  180 GLU B CD  1 
ATOM   4514 O OE1 . GLU B 1 180 ? -10.360 -23.571 24.385  1.00 54.28 ?  180 GLU B OE1 1 
ATOM   4515 O OE2 . GLU B 1 180 ? -8.214  -23.311 24.477  1.00 46.24 -1 180 GLU B OE2 1 
ATOM   4516 N N   . VAL B 1 181 ? -5.248  -24.147 20.029  1.00 36.34 ?  181 VAL B N   1 
ATOM   4517 C CA  . VAL B 1 181 ? -4.192  -23.527 19.182  1.00 37.68 ?  181 VAL B CA  1 
ATOM   4518 C C   . VAL B 1 181 ? -4.173  -24.233 17.823  1.00 37.43 ?  181 VAL B C   1 
ATOM   4519 O O   . VAL B 1 181 ? -4.262  -23.545 16.813  1.00 36.87 ?  181 VAL B O   1 
ATOM   4520 C CB  . VAL B 1 181 ? -2.809  -23.513 19.867  1.00 35.88 ?  181 VAL B CB  1 
ATOM   4521 C CG1 . VAL B 1 181 ? -1.732  -22.938 18.967  1.00 30.32 ?  181 VAL B CG1 1 
ATOM   4522 C CG2 . VAL B 1 181 ? -2.845  -22.770 21.191  1.00 33.91 ?  181 VAL B CG2 1 
ATOM   4523 N N   . LYS B 1 182 ? -4.137  -25.564 17.825  1.00 40.49 ?  182 LYS B N   1 
ATOM   4524 C CA  . LYS B 1 182 ? -4.017  -26.329 16.558  1.00 37.18 ?  182 LYS B CA  1 
ATOM   4525 C C   . LYS B 1 182 ? -5.260  -26.121 15.702  1.00 33.46 ?  182 LYS B C   1 
ATOM   4526 O O   . LYS B 1 182 ? -5.111  -25.901 14.521  1.00 30.95 ?  182 LYS B O   1 
ATOM   4527 C CB  . LYS B 1 182 ? -3.667  -27.780 16.885  1.00 43.19 ?  182 LYS B CB  1 
ATOM   4528 C CG  . LYS B 1 182 ? -2.328  -27.951 17.590  1.00 44.32 ?  182 LYS B CG  1 
ATOM   4529 C CD  . LYS B 1 182 ? -1.779  -29.353 17.574  1.00 47.10 ?  182 LYS B CD  1 
ATOM   4530 C CE  . LYS B 1 182 ? -0.333  -29.415 18.014  1.00 41.55 ?  182 LYS B CE  1 
ATOM   4531 N NZ  . LYS B 1 182 ? 0.068   -30.787 18.400  1.00 48.35 1  182 LYS B NZ  1 
ATOM   4532 N N   . ARG B 1 183 ? -6.434  -26.114 16.328  1.00 28.74 ?  183 ARG B N   1 
ATOM   4533 C CA  . ARG B 1 183 ? -7.702  -25.894 15.594  1.00 32.91 ?  183 ARG B CA  1 
ATOM   4534 C C   . ARG B 1 183 ? -7.685  -24.508 14.946  1.00 31.52 ?  183 ARG B C   1 
ATOM   4535 O O   . ARG B 1 183 ? -8.070  -24.385 13.808  1.00 26.95 ?  183 ARG B O   1 
ATOM   4536 C CB  . ARG B 1 183 ? -8.875  -26.012 16.559  1.00 37.13 ?  183 ARG B CB  1 
ATOM   4537 C CG  . ARG B 1 183 ? -9.805  -27.186 16.302  1.00 44.56 ?  183 ARG B CG  1 
ATOM   4538 C CD  . ARG B 1 183 ? -9.926  -28.194 17.429  1.00 48.66 ?  183 ARG B CD  1 
ATOM   4539 N NE  . ARG B 1 183 ? -10.908 -27.877 18.454  1.00 53.43 ?  183 ARG B NE  1 
ATOM   4540 C CZ  . ARG B 1 183 ? -11.849 -28.710 18.895  1.00 54.11 ?  183 ARG B CZ  1 
ATOM   4541 N NH1 . ARG B 1 183 ? -11.934 -29.933 18.403  1.00 48.16 1  183 ARG B NH1 1 
ATOM   4542 N NH2 . ARG B 1 183 ? -12.672 -28.322 19.852  1.00 55.56 ?  183 ARG B NH2 1 
ATOM   4543 N N   . ILE B 1 184 ? -7.227  -23.513 15.692  1.00 31.86 ?  184 ILE B N   1 
ATOM   4544 C CA  . ILE B 1 184 ? -7.216  -22.120 15.170  1.00 27.91 ?  184 ILE B CA  1 
ATOM   4545 C C   . ILE B 1 184 ? -6.224  -22.049 14.008  1.00 29.38 ?  184 ILE B C   1 
ATOM   4546 O O   . ILE B 1 184 ? -6.547  -21.443 12.984  1.00 28.95 ?  184 ILE B O   1 
ATOM   4547 C CB  . ILE B 1 184 ? -6.947  -21.093 16.287  1.00 31.05 ?  184 ILE B CB  1 
ATOM   4548 C CG1 . ILE B 1 184 ? -8.247  -20.731 17.007  1.00 28.47 ?  184 ILE B CG1 1 
ATOM   4549 C CG2 . ILE B 1 184 ? -6.249  -19.854 15.766  1.00 27.22 ?  184 ILE B CG2 1 
ATOM   4550 C CD1 . ILE B 1 184 ? -8.077  -20.342 18.446  1.00 33.05 ?  184 ILE B CD1 1 
ATOM   4551 N N   . ALA B 1 185 ? -5.091  -22.707 14.154  1.00 28.36 ?  185 ALA B N   1 
ATOM   4552 C CA  . ALA B 1 185 ? -4.128  -22.726 13.059  1.00 29.16 ?  185 ALA B CA  1 
ATOM   4553 C C   . ALA B 1 185 ? -4.669  -23.478 11.849  1.00 29.89 ?  185 ALA B C   1 
ATOM   4554 O O   . ALA B 1 185 ? -4.510  -23.030 10.708  1.00 30.87 ?  185 ALA B O   1 
ATOM   4555 C CB  . ALA B 1 185 ? -2.823  -23.353 13.533  1.00 29.13 ?  185 ALA B CB  1 
ATOM   4556 N N   . GLU B 1 186 ? -5.315  -24.627 12.070  1.00 29.27 ?  186 GLU B N   1 
ATOM   4557 C CA  . GLU B 1 186 ? -5.846  -25.368 10.930  1.00 28.46 ?  186 GLU B CA  1 
ATOM   4558 C C   . GLU B 1 186 ? -6.966  -24.603 10.234  1.00 30.53 ?  186 GLU B C   1 
ATOM   4559 O O   . GLU B 1 186 ? -7.065  -24.632 9.002   1.00 27.41 ?  186 GLU B O   1 
ATOM   4560 C CB  . GLU B 1 186 ? -6.319  -26.756 11.361  1.00 34.85 ?  186 GLU B CB  1 
ATOM   4561 C CG  . GLU B 1 186 ? -5.207  -27.613 11.958  1.00 34.51 ?  186 GLU B CG  1 
ATOM   4562 C CD  . GLU B 1 186 ? -4.473  -28.444 10.923  1.00 45.22 ?  186 GLU B CD  1 
ATOM   4563 O OE1 . GLU B 1 186 ? -3.631  -29.284 11.315  1.00 46.86 ?  186 GLU B OE1 1 
ATOM   4564 O OE2 . GLU B 1 186 ? -4.741  -28.262 9.715   1.00 47.82 -1 186 GLU B OE2 1 
ATOM   4565 N N   . LEU B 1 187 ? -7.803  -23.907 10.980  1.00 28.89 ?  187 LEU B N   1 
ATOM   4566 C CA  . LEU B 1 187 ? -8.867  -23.083 10.348  1.00 28.79 ?  187 LEU B CA  1 
ATOM   4567 C C   . LEU B 1 187 ? -8.219  -21.964 9.512   1.00 29.14 ?  187 LEU B C   1 
ATOM   4568 O O   . LEU B 1 187 ? -8.691  -21.697 8.416   1.00 26.97 ?  187 LEU B O   1 
ATOM   4569 C CB  . LEU B 1 187 ? -9.748  -22.484 11.444  1.00 31.24 ?  187 LEU B CB  1 
ATOM   4570 C CG  . LEU B 1 187 ? -10.781 -23.425 12.052  1.00 39.01 ?  187 LEU B CG  1 
ATOM   4571 C CD1 . LEU B 1 187 ? -11.705 -22.674 12.993  1.00 33.69 ?  187 LEU B CD1 1 
ATOM   4572 C CD2 . LEU B 1 187 ? -11.574 -24.122 10.962  1.00 37.09 ?  187 LEU B CD2 1 
ATOM   4573 N N   . CYS B 1 188 ? -7.181  -21.344 10.057  1.00 26.39 ?  188 CYS B N   1 
ATOM   4574 C CA  . CYS B 1 188 ? -6.523  -20.283 9.305   1.00 23.76 ?  188 CYS B CA  1 
ATOM   4575 C C   . CYS B 1 188 ? -5.898  -20.835 8.032   1.00 22.77 ?  188 CYS B C   1 
ATOM   4576 O O   . CYS B 1 188 ? -6.088  -20.281 6.943   1.00 24.45 ?  188 CYS B O   1 
ATOM   4577 C CB  . CYS B 1 188 ? -5.454  -19.604 10.168  1.00 25.60 ?  188 CYS B CB  1 
ATOM   4578 S SG  . CYS B 1 188 ? -6.106  -18.473 11.427  1.00 24.38 ?  188 CYS B SG  1 
ATOM   4579 N N   . ALA B 1 189 ? -5.127  -21.919 8.160   1.00 27.04 ?  189 ALA B N   1 
ATOM   4580 C CA  . ALA B 1 189 ? -4.456  -22.498 7.002   1.00 26.84 ?  189 ALA B CA  1 
ATOM   4581 C C   . ALA B 1 189 ? -5.465  -22.950 5.955   1.00 29.47 ?  189 ALA B C   1 
ATOM   4582 O O   . ALA B 1 189 ? -5.264  -22.732 4.755   1.00 26.45 ?  189 ALA B O   1 
ATOM   4583 C CB  . ALA B 1 189 ? -3.574  -23.664 7.443   1.00 31.31 ?  189 ALA B CB  1 
ATOM   4584 N N   . LYS B 1 190 ? -6.565  -23.566 6.401   1.00 28.74 ?  190 LYS B N   1 
ATOM   4585 C CA  . LYS B 1 190 ? -7.632  -24.006 5.507   1.00 27.57 ?  190 LYS B CA  1 
ATOM   4586 C C   . LYS B 1 190 ? -8.129  -22.872 4.625   1.00 29.19 ?  190 LYS B C   1 
ATOM   4587 O O   . LYS B 1 190 ? -8.429  -23.070 3.439   1.00 28.09 ?  190 LYS B O   1 
ATOM   4588 C CB  . LYS B 1 190 ? -8.784  -24.566 6.344   1.00 29.62 ?  190 LYS B CB  1 
ATOM   4589 C CG  . LYS B 1 190 ? -9.676  -25.537 5.622   1.00 39.40 ?  190 LYS B CG  1 
ATOM   4590 C CD  . LYS B 1 190 ? -10.947 -24.858 5.126   1.00 38.75 ?  190 LYS B CD  1 
ATOM   4591 C CE  . LYS B 1 190 ? -11.684 -25.762 4.129   1.00 37.41 ?  190 LYS B CE  1 
ATOM   4592 N NZ  . LYS B 1 190 ? -13.003 -25.196 3.751   1.00 43.12 1  190 LYS B NZ  1 
ATOM   4593 N N   . HIS B 1 191 ? -8.253  -21.682 5.195   1.00 26.98 ?  191 HIS B N   1 
ATOM   4594 C CA  . HIS B 1 191 ? -8.760  -20.517 4.495   1.00 28.43 ?  191 HIS B CA  1 
ATOM   4595 C C   . HIS B 1 191 ? -7.645  -19.618 3.990   1.00 25.66 ?  191 HIS B C   1 
ATOM   4596 O O   . HIS B 1 191 ? -7.910  -18.474 3.625   1.00 24.12 ?  191 HIS B O   1 
ATOM   4597 C CB  . HIS B 1 191 ? -9.707  -19.736 5.410   1.00 26.51 ?  191 HIS B CB  1 
ATOM   4598 C CG  . HIS B 1 191 ? -10.933 -20.507 5.795   1.00 31.44 ?  191 HIS B CG  1 
ATOM   4599 N ND1 . HIS B 1 191 ? -11.875 -20.912 4.870   1.00 31.68 ?  191 HIS B ND1 1 
ATOM   4600 C CD2 . HIS B 1 191 ? -11.358 -20.972 6.993   1.00 33.45 ?  191 HIS B CD2 1 
ATOM   4601 C CE1 . HIS B 1 191 ? -12.839 -21.572 5.488   1.00 34.08 ?  191 HIS B CE1 1 
ATOM   4602 N NE2 . HIS B 1 191 ? -12.548 -21.627 6.774   1.00 35.20 ?  191 HIS B NE2 1 
ATOM   4603 N N   . GLN B 1 192 ? -6.399  -20.103 3.989   1.00 21.74 ?  192 GLN B N   1 
ATOM   4604 C CA  . GLN B 1 192 ? -5.270  -19.327 3.471   1.00 23.00 ?  192 GLN B CA  1 
ATOM   4605 C C   . GLN B 1 192 ? -5.143  -17.992 4.206   1.00 23.22 ?  192 GLN B C   1 
ATOM   4606 O O   . GLN B 1 192 ? -4.845  -16.954 3.612   1.00 25.73 ?  192 GLN B O   1 
ATOM   4607 C CB  . GLN B 1 192 ? -5.396  -19.139 1.947   1.00 27.39 ?  192 GLN B CB  1 
ATOM   4608 C CG  . GLN B 1 192 ? -5.095  -20.437 1.193   1.00 28.56 ?  192 GLN B CG  1 
ATOM   4609 C CD  . GLN B 1 192 ? -5.431  -20.371 -0.283  1.00 30.96 ?  192 GLN B CD  1 
ATOM   4610 O OE1 . GLN B 1 192 ? -6.446  -20.914 -0.725  1.00 32.53 ?  192 GLN B OE1 1 
ATOM   4611 N NE2 . GLN B 1 192 ? -4.587  -19.709 -1.050  1.00 30.76 ?  192 GLN B NE2 1 
ATOM   4612 N N   . VAL B 1 193 ? -5.391  -18.032 5.520   1.00 21.57 ?  193 VAL B N   1 
ATOM   4613 C CA  . VAL B 1 193 ? -5.268  -16.891 6.422   1.00 22.45 ?  193 VAL B CA  1 
ATOM   4614 C C   . VAL B 1 193 ? -4.009  -17.088 7.257   1.00 25.94 ?  193 VAL B C   1 
ATOM   4615 O O   . VAL B 1 193 ? -3.763  -18.188 7.760   1.00 23.14 ?  193 VAL B O   1 
ATOM   4616 C CB  . VAL B 1 193 ? -6.511  -16.759 7.325   1.00 26.30 ?  193 VAL B CB  1 
ATOM   4617 C CG1 . VAL B 1 193 ? -6.304  -15.667 8.409   1.00 23.55 ?  193 VAL B CG1 1 
ATOM   4618 C CG2 . VAL B 1 193 ? -7.750  -16.484 6.495   1.00 25.16 ?  193 VAL B CG2 1 
ATOM   4619 N N   . LEU B 1 194 ? -3.200  -16.037 7.381   1.00 22.98 ?  194 LEU B N   1 
ATOM   4620 C CA  . LEU B 1 194 ? -1.993  -16.095 8.191   1.00 22.23 ?  194 LEU B CA  1 
ATOM   4621 C C   . LEU B 1 194 ? -2.346  -15.978 9.662   1.00 22.55 ?  194 LEU B C   1 
ATOM   4622 O O   . LEU B 1 194 ? -3.022  -15.034 10.068  1.00 23.71 ?  194 LEU B O   1 
ATOM   4623 C CB  . LEU B 1 194 ? -1.047  -14.950 7.842   1.00 25.70 ?  194 LEU B CB  1 
ATOM   4624 C CG  . LEU B 1 194 ? -0.169  -14.956 6.607   1.00 33.05 ?  194 LEU B CG  1 
ATOM   4625 C CD1 . LEU B 1 194 ? 0.989   -13.973 6.870   1.00 30.97 ?  194 LEU B CD1 1 
ATOM   4626 C CD2 . LEU B 1 194 ? 0.334   -16.346 6.360   1.00 27.02 ?  194 LEU B CD2 1 
ATOM   4627 N N   . LEU B 1 195 ? -1.855  -16.898 10.465  1.00 22.57 ?  195 LEU B N   1 
ATOM   4628 C CA  . LEU B 1 195 ? -2.040  -16.816 11.906  1.00 20.44 ?  195 LEU B CA  1 
ATOM   4629 C C   . LEU B 1 195 ? -0.802  -16.169 12.513  1.00 19.19 ?  195 LEU B C   1 
ATOM   4630 O O   . LEU B 1 195 ? 0.303   -16.715 12.407  1.00 22.54 ?  195 LEU B O   1 
ATOM   4631 C CB  . LEU B 1 195 ? -2.280  -18.197 12.506  1.00 24.05 ?  195 LEU B CB  1 
ATOM   4632 C CG  . LEU B 1 195 ? -2.341  -18.193 14.034  1.00 22.91 ?  195 LEU B CG  1 
ATOM   4633 C CD1 . LEU B 1 195 ? -3.529  -17.351 14.474  1.00 23.90 ?  195 LEU B CD1 1 
ATOM   4634 C CD2 . LEU B 1 195 ? -2.452  -19.604 14.557  1.00 22.81 ?  195 LEU B CD2 1 
ATOM   4635 N N   . ILE B 1 196 ? -0.977  -14.996 13.106  1.00 20.18 ?  196 ILE B N   1 
ATOM   4636 C CA  . ILE B 1 196 ? 0.082   -14.326 13.862  1.00 21.69 ?  196 ILE B CA  1 
ATOM   4637 C C   . ILE B 1 196 ? -0.183  -14.573 15.339  1.00 21.84 ?  196 ILE B C   1 
ATOM   4638 O O   . ILE B 1 196 ? -1.122  -14.007 15.916  1.00 21.32 ?  196 ILE B O   1 
ATOM   4639 C CB  . ILE B 1 196 ? 0.137   -12.821 13.566  1.00 18.65 ?  196 ILE B CB  1 
ATOM   4640 C CG1 . ILE B 1 196 ? 0.351   -12.552 12.069  1.00 17.93 ?  196 ILE B CG1 1 
ATOM   4641 C CG2 . ILE B 1 196 ? 1.286   -12.177 14.359  1.00 20.63 ?  196 ILE B CG2 1 
ATOM   4642 C CD1 . ILE B 1 196 ? 1.530   -13.281 11.485  1.00 19.93 ?  196 ILE B CD1 1 
ATOM   4643 N N   . SER B 1 197 ? 0.654   -15.398 15.966  1.00 19.87 ?  197 SER B N   1 
ATOM   4644 C CA  . SER B 1 197 ? 0.406   -15.869 17.323  1.00 21.92 ?  197 SER B CA  1 
ATOM   4645 C C   . SER B 1 197 ? 1.343   -15.086 18.241  1.00 20.66 ?  197 SER B C   1 
ATOM   4646 O O   . SER B 1 197 ? 2.551   -15.341 18.284  1.00 20.18 ?  197 SER B O   1 
ATOM   4647 C CB  . SER B 1 197 ? 0.624   -17.377 17.415  1.00 21.16 ?  197 SER B CB  1 
ATOM   4648 O OG  . SER B 1 197 ? 0.408   -17.835 18.735  1.00 22.47 ?  197 SER B OG  1 
ATOM   4649 N N   . ASP B 1 198 ? 0.789   -14.083 18.923  1.00 18.75 ?  198 ASP B N   1 
ATOM   4650 C CA  . ASP B 1 198 ? 1.542   -13.265 19.873  1.00 18.45 ?  198 ASP B CA  1 
ATOM   4651 C C   . ASP B 1 198 ? 1.632   -14.041 21.178  1.00 21.07 ?  198 ASP B C   1 
ATOM   4652 O O   . ASP B 1 198 ? 0.644   -14.144 21.910  1.00 18.74 ?  198 ASP B O   1 
ATOM   4653 C CB  . ASP B 1 198 ? 0.844   -11.912 20.058  1.00 19.06 ?  198 ASP B CB  1 
ATOM   4654 C CG  . ASP B 1 198 ? 1.438   -11.058 21.189  1.00 21.52 ?  198 ASP B CG  1 
ATOM   4655 O OD1 . ASP B 1 198 ? 2.277   -11.526 21.976  1.00 21.64 ?  198 ASP B OD1 1 
ATOM   4656 O OD2 . ASP B 1 198 ? 1.045   -9.880  21.292  1.00 21.85 -1 198 ASP B OD2 1 
ATOM   4657 N N   . GLU B 1 199 ? 2.801   -14.624 21.440  1.00 18.95 ?  199 GLU B N   1 
ATOM   4658 C CA  . GLU B 1 199 ? 3.002   -15.510 22.618  1.00 20.45 ?  199 GLU B CA  1 
ATOM   4659 C C   . GLU B 1 199 ? 3.886   -14.822 23.654  1.00 21.34 ?  199 GLU B C   1 
ATOM   4660 O O   . GLU B 1 199 ? 4.654   -15.509 24.322  1.00 21.95 ?  199 GLU B O   1 
ATOM   4661 C CB  . GLU B 1 199 ? 3.647   -16.792 22.122  1.00 25.06 ?  199 GLU B CB  1 
ATOM   4662 C CG  . GLU B 1 199 ? 2.728   -17.548 21.193  1.00 21.89 ?  199 GLU B CG  1 
ATOM   4663 C CD  . GLU B 1 199 ? 3.324   -18.680 20.389  1.00 22.19 ?  199 GLU B CD  1 
ATOM   4664 O OE1 . GLU B 1 199 ? 2.622   -19.179 19.512  1.00 24.66 ?  199 GLU B OE1 1 
ATOM   4665 O OE2 . GLU B 1 199 ? 4.469   -19.045 20.636  1.00 22.47 -1 199 GLU B OE2 1 
ATOM   4666 N N   . ILE B 1 200 ? 3.699   -13.522 23.814  1.00 17.58 ?  200 ILE B N   1 
ATOM   4667 C CA  . ILE B 1 200 ? 4.556   -12.751 24.708  1.00 19.82 ?  200 ILE B CA  1 
ATOM   4668 C C   . ILE B 1 200 ? 4.285   -13.052 26.172  1.00 21.83 ?  200 ILE B C   1 
ATOM   4669 O O   . ILE B 1 200 ? 5.170   -12.835 27.015  1.00 20.03 ?  200 ILE B O   1 
ATOM   4670 C CB  . ILE B 1 200 ? 4.413   -11.247 24.412  1.00 20.98 ?  200 ILE B CB  1 
ATOM   4671 C CG1 . ILE B 1 200 ? 5.629   -10.476 24.939  1.00 21.51 ?  200 ILE B CG1 1 
ATOM   4672 C CG2 . ILE B 1 200 ? 3.097   -10.680 24.952  1.00 20.39 ?  200 ILE B CG2 1 
ATOM   4673 C CD1 . ILE B 1 200 ? 5.602   -8.986  24.540  1.00 21.96 ?  200 ILE B CD1 1 
ATOM   4674 N N   . HIS B 1 201 ? 3.098   -13.560 26.510  1.00 20.84 ?  201 HIS B N   1 
ATOM   4675 C CA  . HIS B 1 201 ? 2.808   -13.951 27.883  1.00 22.62 ?  201 HIS B CA  1 
ATOM   4676 C C   . HIS B 1 201 ? 3.004   -15.447 28.109  1.00 20.52 ?  201 HIS B C   1 
ATOM   4677 O O   . HIS B 1 201 ? 2.602   -15.960 29.157  1.00 21.23 ?  201 HIS B O   1 
ATOM   4678 C CB  . HIS B 1 201 ? 1.379   -13.553 28.276  1.00 22.44 ?  201 HIS B CB  1 
ATOM   4679 C CG  . HIS B 1 201 ? 1.095   -12.087 28.167  1.00 20.82 ?  201 HIS B CG  1 
ATOM   4680 N ND1 . HIS B 1 201 ? 1.246   -11.214 29.224  1.00 18.54 ?  201 HIS B ND1 1 
ATOM   4681 C CD2 . HIS B 1 201 ? 0.596   -11.352 27.142  1.00 21.69 ?  201 HIS B CD2 1 
ATOM   4682 C CE1 . HIS B 1 201 ? 0.893   -9.998  28.841  1.00 23.90 ?  201 HIS B CE1 1 
ATOM   4683 N NE2 . HIS B 1 201 ? 0.491   -10.055 27.581  1.00 21.49 ?  201 HIS B NE2 1 
ATOM   4684 N N   . GLY B 1 202 ? 3.642   -16.128 27.157  1.00 20.50 ?  202 GLY B N   1 
ATOM   4685 C CA  . GLY B 1 202 ? 3.715   -17.598 27.176  1.00 20.15 ?  202 GLY B CA  1 
ATOM   4686 C C   . GLY B 1 202 ? 4.480   -18.210 28.321  1.00 24.45 ?  202 GLY B C   1 
ATOM   4687 O O   . GLY B 1 202 ? 4.161   -19.328 28.703  1.00 22.11 ?  202 GLY B O   1 
ATOM   4688 N N   . ASP B 1 203 ? 5.518   -17.526 28.762  1.00 22.61 ?  203 ASP B N   1 
ATOM   4689 C CA  . ASP B 1 203 ? 6.305   -17.995 29.894  1.00 23.14 ?  203 ASP B CA  1 
ATOM   4690 C C   . ASP B 1 203 ? 5.618   -17.749 31.218  1.00 24.79 ?  203 ASP B C   1 
ATOM   4691 O O   . ASP B 1 203 ? 6.176   -18.085 32.267  1.00 23.74 ?  203 ASP B O   1 
ATOM   4692 C CB  . ASP B 1 203 ? 7.679   -17.312 29.941  1.00 22.38 ?  203 ASP B CB  1 
ATOM   4693 C CG  . ASP B 1 203 ? 8.475   -17.490 28.672  1.00 27.20 ?  203 ASP B CG  1 
ATOM   4694 O OD1 . ASP B 1 203 ? 8.354   -18.544 28.015  1.00 24.33 ?  203 ASP B OD1 1 
ATOM   4695 O OD2 . ASP B 1 203 ? 9.245   -16.567 28.334  1.00 23.65 -1 203 ASP B OD2 1 
ATOM   4696 N N   . LEU B 1 204 ? 4.460   -17.111 31.210  1.00 21.92 ?  204 LEU B N   1 
ATOM   4697 C CA  . LEU B 1 204 ? 3.829   -16.661 32.437  1.00 21.76 ?  204 LEU B CA  1 
ATOM   4698 C C   . LEU B 1 204 ? 2.518   -17.387 32.674  1.00 21.41 ?  204 LEU B C   1 
ATOM   4699 O O   . LEU B 1 204 ? 1.565   -16.794 33.180  1.00 24.43 ?  204 LEU B O   1 
ATOM   4700 C CB  . LEU B 1 204 ? 3.607   -15.145 32.413  1.00 20.02 ?  204 LEU B CB  1 
ATOM   4701 C CG  . LEU B 1 204 ? 4.904   -14.336 32.494  1.00 20.10 ?  204 LEU B CG  1 
ATOM   4702 C CD1 . LEU B 1 204 ? 4.623   -12.856 32.235  1.00 21.02 ?  204 LEU B CD1 1 
ATOM   4703 C CD2 . LEU B 1 204 ? 5.591   -14.543 33.850  1.00 23.83 ?  204 LEU B CD2 1 
ATOM   4704 N N   . VAL B 1 205 ? 2.472   -18.654 32.284  1.00 23.58 ?  205 VAL B N   1 
ATOM   4705 C CA  . VAL B 1 205 ? 1.290   -19.473 32.686  1.00 28.69 ?  205 VAL B CA  1 
ATOM   4706 C C   . VAL B 1 205 ? 1.539   -19.816 34.158  1.00 28.82 ?  205 VAL B C   1 
ATOM   4707 O O   . VAL B 1 205 ? 2.535   -20.447 34.450  1.00 29.06 ?  205 VAL B O   1 
ATOM   4708 C CB  . VAL B 1 205 ? 1.035   -20.693 31.779  1.00 29.57 ?  205 VAL B CB  1 
ATOM   4709 C CG1 . VAL B 1 205 ? -0.319  -21.304 32.087  1.00 31.28 ?  205 VAL B CG1 1 
ATOM   4710 C CG2 . VAL B 1 205 ? 1.125   -20.332 30.307  1.00 24.25 ?  205 VAL B CG2 1 
ATOM   4711 N N   . LEU B 1 206 ? 0.661   -19.372 35.042  1.00 29.99 ?  206 LEU B N   1 
ATOM   4712 C CA  . LEU B 1 206 ? 0.928   -19.503 36.491  1.00 34.53 ?  206 LEU B CA  1 
ATOM   4713 C C   . LEU B 1 206 ? 0.533   -20.872 37.029  1.00 38.99 ?  206 LEU B C   1 
ATOM   4714 O O   . LEU B 1 206 ? 0.629   -21.060 38.206  1.00 43.47 ?  206 LEU B O   1 
ATOM   4715 C CB  . LEU B 1 206 ? 0.278   -18.323 37.196  1.00 30.90 ?  206 LEU B CB  1 
ATOM   4716 C CG  . LEU B 1 206 ? 0.847   -16.970 36.785  1.00 31.43 ?  206 LEU B CG  1 
ATOM   4717 C CD1 . LEU B 1 206 ? 0.296   -15.859 37.658  1.00 35.69 ?  206 LEU B CD1 1 
ATOM   4718 C CD2 . LEU B 1 206 ? 2.363   -16.999 36.849  1.00 31.24 ?  206 LEU B CD2 1 
ATOM   4719 N N   . THR B 1 207 ? 0.179   -21.805 36.165  1.00 45.05 ?  207 THR B N   1 
ATOM   4720 C CA  . THR B 1 207 ? -0.087  -23.202 36.565  1.00 45.76 ?  207 THR B CA  1 
ATOM   4721 C C   . THR B 1 207 ? 0.921   -24.112 35.811  1.00 52.11 ?  207 THR B C   1 
ATOM   4722 O O   . THR B 1 207 ? 1.806   -23.543 35.162  1.00 47.88 ?  207 THR B O   1 
ATOM   4723 C CB  . THR B 1 207 ? -1.581  -23.405 36.296  1.00 47.25 ?  207 THR B CB  1 
ATOM   4724 O OG1 . THR B 1 207 ? -1.740  -23.017 34.934  1.00 42.35 ?  207 THR B OG1 1 
ATOM   4725 C CG2 . THR B 1 207 ? -2.480  -22.553 37.162  1.00 44.15 ?  207 THR B CG2 1 
ATOM   4726 N N   . ASP B 1 208 ? 0.880   -25.463 35.955  1.00 54.84 ?  208 ASP B N   1 
ATOM   4727 C CA  . ASP B 1 208 ? 1.690   -26.366 35.132  1.00 55.72 ?  208 ASP B CA  1 
ATOM   4728 C C   . ASP B 1 208 ? 1.177   -26.409 33.710  1.00 54.01 ?  208 ASP B C   1 
ATOM   4729 O O   . ASP B 1 208 ? 1.972   -26.613 32.783  1.00 58.32 ?  208 ASP B O   1 
ATOM   4730 C CB  . ASP B 1 208 ? 1.723   -27.799 35.681  1.00 59.15 ?  208 ASP B CB  1 
ATOM   4731 C CG  . ASP B 1 208 ? 2.985   -28.108 36.479  1.00 62.00 ?  208 ASP B CG  1 
ATOM   4732 O OD1 . ASP B 1 208 ? 3.958   -27.333 36.384  1.00 64.12 ?  208 ASP B OD1 1 
ATOM   4733 O OD2 . ASP B 1 208 ? 3.004   -29.137 37.200  1.00 61.83 -1 208 ASP B OD2 1 
ATOM   4734 N N   . GLU B 1 209 ? -0.097  -25.998 33.578  1.00 52.99 ?  209 GLU B N   1 
ATOM   4735 C CA  . GLU B 1 209 ? -0.771  -25.961 32.265  1.00 50.42 ?  209 GLU B CA  1 
ATOM   4736 C C   . GLU B 1 209 ? 0.189   -25.223 31.356  1.00 47.66 ?  209 GLU B C   1 
ATOM   4737 O O   . GLU B 1 209 ? 0.652   -24.161 31.732  1.00 48.08 ?  209 GLU B O   1 
ATOM   4738 C CB  . GLU B 1 209 ? -2.104  -25.245 32.425  1.00 47.56 ?  209 GLU B CB  1 
ATOM   4739 C CG  . GLU B 1 209 ? -2.966  -25.725 33.571  1.00 45.17 ?  209 GLU B CG  1 
ATOM   4740 C CD  . GLU B 1 209 ? -4.279  -24.964 33.660  1.00 44.75 ?  209 GLU B CD  1 
ATOM   4741 O OE1 . GLU B 1 209 ? -5.245  -25.384 33.015  1.00 49.16 ?  209 GLU B OE1 1 
ATOM   4742 O OE2 . GLU B 1 209 ? -4.326  -23.946 34.360  1.00 45.42 -1 209 GLU B OE2 1 
ATOM   4743 N N   . ASP B 1 210 ? 0.593   -25.841 30.269  1.00 41.86 ?  210 ASP B N   1 
ATOM   4744 C CA  . ASP B 1 210 ? 1.612   -25.093 29.510  1.00 43.32 ?  210 ASP B CA  1 
ATOM   4745 C C   . ASP B 1 210 ? 1.028   -24.471 28.263  1.00 37.37 ?  210 ASP B C   1 
ATOM   4746 O O   . ASP B 1 210 ? -0.088  -24.814 27.893  1.00 41.66 ?  210 ASP B O   1 
ATOM   4747 C CB  . ASP B 1 210 ? 2.855   -25.894 29.163  1.00 45.69 ?  210 ASP B CB  1 
ATOM   4748 C CG  . ASP B 1 210 ? 4.122   -25.081 29.284  1.00 41.53 ?  210 ASP B CG  1 
ATOM   4749 O OD1 . ASP B 1 210 ? 4.019   -23.872 29.546  1.00 42.90 ?  210 ASP B OD1 1 
ATOM   4750 O OD2 . ASP B 1 210 ? 5.183   -25.675 29.155  1.00 47.17 -1 210 ASP B OD2 1 
ATOM   4751 N N   . ILE B 1 211 ? 1.834   -23.620 27.654  1.00 37.11 ?  211 ILE B N   1 
ATOM   4752 C CA  . ILE B 1 211 ? 1.405   -22.926 26.424  1.00 33.96 ?  211 ILE B CA  1 
ATOM   4753 C C   . ILE B 1 211 ? 1.676   -23.868 25.264  1.00 35.27 ?  211 ILE B C   1 
ATOM   4754 O O   . ILE B 1 211 ? 2.555   -24.728 25.379  1.00 30.09 ?  211 ILE B O   1 
ATOM   4755 C CB  . ILE B 1 211 ? 2.198   -21.620 26.305  1.00 34.46 ?  211 ILE B CB  1 
ATOM   4756 C CG1 . ILE B 1 211 ? 1.953   -20.884 24.996  1.00 31.91 ?  211 ILE B CG1 1 
ATOM   4757 C CG2 . ILE B 1 211 ? 3.671   -21.892 26.441  1.00 33.02 ?  211 ILE B CG2 1 
ATOM   4758 C CD1 . ILE B 1 211 ? 0.936   -19.854 25.150  1.00 33.44 ?  211 ILE B CD1 1 
ATOM   4759 N N   . THR B 1 212 ? 0.882   -23.731 24.225  1.00 28.20 ?  212 THR B N   1 
ATOM   4760 C CA  . THR B 1 212 ? 1.144   -24.484 22.993  1.00 26.47 ?  212 THR B CA  1 
ATOM   4761 C C   . THR B 1 212 ? 1.586   -23.439 21.953  1.00 23.75 ?  212 THR B C   1 
ATOM   4762 O O   . THR B 1 212 ? 0.712   -22.710 21.522  1.00 26.03 ?  212 THR B O   1 
ATOM   4763 C CB  . THR B 1 212 ? -0.046  -25.388 22.647  1.00 34.59 ?  212 THR B CB  1 
ATOM   4764 O OG1 . THR B 1 212 ? -0.199  -26.376 23.660  1.00 29.66 ?  212 THR B OG1 1 
ATOM   4765 C CG2 . THR B 1 212 ? 0.098   -26.032 21.284  1.00 31.12 ?  212 THR B CG2 1 
ATOM   4766 N N   . PRO B 1 213 ? 2.895   -23.243 21.628  1.00 26.28 ?  213 PRO B N   1 
ATOM   4767 C CA  . PRO B 1 213 ? 3.269   -22.330 20.568  1.00 23.06 ?  213 PRO B CA  1 
ATOM   4768 C C   . PRO B 1 213 ? 2.646   -22.734 19.228  1.00 25.90 ?  213 PRO B C   1 
ATOM   4769 O O   . PRO B 1 213 ? 2.548   -23.893 18.930  1.00 24.28 ?  213 PRO B O   1 
ATOM   4770 C CB  . PRO B 1 213 ? 4.756   -22.591 20.434  1.00 23.82 ?  213 PRO B CB  1 
ATOM   4771 C CG  . PRO B 1 213 ? 5.204   -22.867 21.819  1.00 27.76 ?  213 PRO B CG  1 
ATOM   4772 C CD  . PRO B 1 213 ? 4.131   -23.828 22.243  1.00 26.67 ?  213 PRO B CD  1 
ATOM   4773 N N   . ALA B 1 214 ? 2.287   -21.744 18.428  1.00 23.00 ?  214 ALA B N   1 
ATOM   4774 C CA  . ALA B 1 214 ? 1.661   -22.006 17.120  1.00 22.21 ?  214 ALA B CA  1 
ATOM   4775 C C   . ALA B 1 214 ? 2.620   -22.795 16.219  1.00 22.38 ?  214 ALA B C   1 
ATOM   4776 O O   . ALA B 1 214 ? 2.154   -23.543 15.402  1.00 25.48 ?  214 ALA B O   1 
ATOM   4777 C CB  . ALA B 1 214 ? 1.211   -20.714 16.502  1.00 20.37 ?  214 ALA B CB  1 
ATOM   4778 N N   . PHE B 1 215 ? 3.914   -22.624 16.408  1.00 20.71 ?  215 PHE B N   1 
ATOM   4779 C CA  . PHE B 1 215 ? 4.907   -23.328 15.564  1.00 25.20 ?  215 PHE B CA  1 
ATOM   4780 C C   . PHE B 1 215 ? 4.799   -24.864 15.694  1.00 24.20 ?  215 PHE B C   1 
ATOM   4781 O O   . PHE B 1 215 ? 5.393   -25.531 14.869  1.00 24.37 ?  215 PHE B O   1 
ATOM   4782 C CB  . PHE B 1 215 ? 6.318   -22.750 15.752  1.00 24.38 ?  215 PHE B CB  1 
ATOM   4783 C CG  . PHE B 1 215 ? 7.005   -23.043 17.059  1.00 25.31 ?  215 PHE B CG  1 
ATOM   4784 C CD1 . PHE B 1 215 ? 7.462   -24.313 17.360  1.00 24.88 ?  215 PHE B CD1 1 
ATOM   4785 C CD2 . PHE B 1 215 ? 7.243   -22.032 17.971  1.00 24.74 ?  215 PHE B CD2 1 
ATOM   4786 C CE1 . PHE B 1 215 ? 8.090   -24.576 18.563  1.00 26.46 ?  215 PHE B CE1 1 
ATOM   4787 C CE2 . PHE B 1 215 ? 7.895   -22.291 19.163  1.00 25.67 ?  215 PHE B CE2 1 
ATOM   4788 C CZ  . PHE B 1 215 ? 8.305   -23.565 19.462  1.00 27.57 ?  215 PHE B CZ  1 
ATOM   4789 N N   . THR B 1 216 ? 4.112   -25.370 16.724  1.00 26.43 ?  216 THR B N   1 
ATOM   4790 C CA  . THR B 1 216 ? 4.043   -26.819 16.936  1.00 28.77 ?  216 THR B CA  1 
ATOM   4791 C C   . THR B 1 216 ? 2.900   -27.479 16.176  1.00 32.40 ?  216 THR B C   1 
ATOM   4792 O O   . THR B 1 216 ? 2.798   -28.714 16.194  1.00 27.58 ?  216 THR B O   1 
ATOM   4793 C CB  . THR B 1 216 ? 3.903   -27.183 18.433  1.00 25.42 ?  216 THR B CB  1 
ATOM   4794 O OG1 . THR B 1 216 ? 2.642   -26.733 18.950  1.00 23.68 ?  216 THR B OG1 1 
ATOM   4795 C CG2 . THR B 1 216 ? 5.032   -26.589 19.268  1.00 27.13 ?  216 THR B CG2 1 
ATOM   4796 N N   . VAL B 1 217 ? 2.057   -26.683 15.538  1.00 26.36 ?  217 VAL B N   1 
ATOM   4797 C CA  . VAL B 1 217 ? 0.960   -27.256 14.724  1.00 27.91 ?  217 VAL B CA  1 
ATOM   4798 C C   . VAL B 1 217 ? 1.516   -28.163 13.631  1.00 31.97 ?  217 VAL B C   1 
ATOM   4799 O O   . VAL B 1 217 ? 2.611   -27.941 13.172  1.00 30.50 ?  217 VAL B O   1 
ATOM   4800 C CB  . VAL B 1 217 ? 0.027   -26.171 14.172  1.00 27.41 ?  217 VAL B CB  1 
ATOM   4801 C CG1 . VAL B 1 217 ? -0.494  -25.304 15.303  1.00 33.30 ?  217 VAL B CG1 1 
ATOM   4802 C CG2 . VAL B 1 217 ? 0.677   -25.332 13.099  1.00 26.63 ?  217 VAL B CG2 1 
ATOM   4803 N N   . ASP B 1 218 ? 0.739   -29.172 13.282  1.00 33.39 ?  218 ASP B N   1 
ATOM   4804 C CA  . ASP B 1 218 ? 1.141   -30.141 12.244  1.00 35.80 ?  218 ASP B CA  1 
ATOM   4805 C C   . ASP B 1 218 ? 1.461   -29.460 10.924  1.00 35.41 ?  218 ASP B C   1 
ATOM   4806 O O   . ASP B 1 218 ? 0.776   -28.508 10.576  1.00 35.90 ?  218 ASP B O   1 
ATOM   4807 C CB  . ASP B 1 218 ? 0.112   -31.262 12.107  1.00 38.45 ?  218 ASP B CB  1 
ATOM   4808 C CG  . ASP B 1 218 ? 0.198   -32.271 13.230  1.00 44.79 ?  218 ASP B CG  1 
ATOM   4809 O OD1 . ASP B 1 218 ? 1.274   -32.357 13.847  1.00 45.84 ?  218 ASP B OD1 1 
ATOM   4810 O OD2 . ASP B 1 218 ? -0.812  -32.952 13.476  1.00 47.11 -1 218 ASP B OD2 1 
ATOM   4811 N N   . TRP B 1 219 ? 2.386   -30.039 10.186  1.00 30.00 ?  219 TRP B N   1 
ATOM   4812 C CA  . TRP B 1 219 ? 2.936   -29.471 8.939   1.00 30.00 ?  219 TRP B CA  1 
ATOM   4813 C C   . TRP B 1 219 ? 2.001   -28.842 7.952   1.00 30.00 ?  219 TRP B C   1 
ATOM   4814 O O   . TRP B 1 219 ? 2.434   -27.858 7.377   1.00 30.00 ?  219 TRP B O   1 
ATOM   4815 C CB  . TRP B 1 219 ? 3.793   -30.490 8.224   1.00 30.00 ?  219 TRP B CB  1 
ATOM   4816 C CG  . TRP B 1 219 ? 5.082   -30.665 8.928   1.00 30.00 ?  219 TRP B CG  1 
ATOM   4817 C CD1 . TRP B 1 219 ? 5.471   -31.723 9.692   1.00 30.00 ?  219 TRP B CD1 1 
ATOM   4818 C CD2 . TRP B 1 219 ? 6.139   -29.707 8.953   1.00 30.00 ?  219 TRP B CD2 1 
ATOM   4819 N NE1 . TRP B 1 219 ? 6.726   -31.500 10.177  1.00 30.00 ?  219 TRP B NE1 1 
ATOM   4820 C CE2 . TRP B 1 219 ? 7.147   -30.272 9.747   1.00 30.00 ?  219 TRP B CE2 1 
ATOM   4821 C CE3 . TRP B 1 219 ? 6.333   -28.446 8.378   1.00 30.00 ?  219 TRP B CE3 1 
ATOM   4822 C CZ2 . TRP B 1 219 ? 8.352   -29.611 9.969   1.00 30.00 ?  219 TRP B CZ2 1 
ATOM   4823 C CZ3 . TRP B 1 219 ? 7.518   -27.787 8.610   1.00 30.00 ?  219 TRP B CZ3 1 
ATOM   4824 C CH2 . TRP B 1 219 ? 8.513   -28.372 9.390   1.00 30.00 ?  219 TRP B CH2 1 
ATOM   4825 N N   . ALA B 1 221 ? -0.644  -27.102 8.272   1.00 33.05 ?  221 ALA B N   1 
ATOM   4826 C CA  . ALA B 1 221 ? -0.976  -25.767 8.806   1.00 31.95 ?  221 ALA B CA  1 
ATOM   4827 C C   . ALA B 1 221 ? 0.248   -24.986 9.285   1.00 26.85 ?  221 ALA B C   1 
ATOM   4828 O O   . ALA B 1 221 ? 0.155   -23.782 9.402   1.00 25.79 ?  221 ALA B O   1 
ATOM   4829 C CB  . ALA B 1 221 ? -1.917  -26.000 9.930   1.00 31.85 ?  221 ALA B CB  1 
ATOM   4830 N N   . LYS B 1 222 ? 1.327   -25.689 9.581   1.00 30.90 ?  222 LYS B N   1 
ATOM   4831 C CA  . LYS B 1 222 ? 2.499   -24.994 10.108  1.00 28.16 ?  222 LYS B CA  1 
ATOM   4832 C C   . LYS B 1 222 ? 3.030   -23.949 9.146   1.00 29.71 ?  222 LYS B C   1 
ATOM   4833 O O   . LYS B 1 222 ? 3.729   -23.023 9.577   1.00 25.06 ?  222 LYS B O   1 
ATOM   4834 C CB  . LYS B 1 222 ? 3.614   -25.990 10.447  1.00 30.01 ?  222 LYS B CB  1 
ATOM   4835 C CG  . LYS B 1 222 ? 4.496   -25.525 11.612  1.00 26.24 ?  222 LYS B CG  1 
ATOM   4836 C CD  . LYS B 1 222 ? 5.847   -26.241 11.646  1.00 30.64 ?  222 LYS B CD  1 
ATOM   4837 C CE  . LYS B 1 222 ? 5.668   -27.728 11.922  1.00 31.31 ?  222 LYS B CE  1 
ATOM   4838 N NZ  . LYS B 1 222 ? 5.259   -27.980 13.333  1.00 30.35 1  222 LYS B NZ  1 
ATOM   4839 N N   . ASN B 1 223 ? 2.717   -24.066 7.857   1.00 28.18 ?  223 ASN B N   1 
ATOM   4840 C CA  . ASN B 1 223 ? 3.189   -23.086 6.885   1.00 29.52 ?  223 ASN B CA  1 
ATOM   4841 C C   . ASN B 1 223 ? 2.429   -21.776 6.941   1.00 26.28 ?  223 ASN B C   1 
ATOM   4842 O O   . ASN B 1 223 ? 2.774   -20.848 6.206   1.00 28.31 ?  223 ASN B O   1 
ATOM   4843 C CB  . ASN B 1 223 ? 3.102   -23.660 5.472   1.00 29.27 ?  223 ASN B CB  1 
ATOM   4844 C CG  . ASN B 1 223 ? 4.251   -24.594 5.172   1.00 32.55 ?  223 ASN B CG  1 
ATOM   4845 O OD1 . ASN B 1 223 ? 5.415   -24.190 5.219   1.00 29.72 ?  223 ASN B OD1 1 
ATOM   4846 N ND2 . ASN B 1 223 ? 3.940   -25.843 4.878   1.00 37.21 ?  223 ASN B ND2 1 
ATOM   4847 N N   . TRP B 1 224 ? 1.400   -21.684 7.773   1.00 23.58 ?  224 TRP B N   1 
ATOM   4848 C CA  . TRP B 1 224 ? 0.561   -20.500 7.832   1.00 23.99 ?  224 TRP B CA  1 
ATOM   4849 C C   . TRP B 1 224 ? 0.657   -19.787 9.176   1.00 22.25 ?  224 TRP B C   1 
ATOM   4850 O O   . TRP B 1 224 ? -0.165  -18.913 9.457   1.00 26.21 ?  224 TRP B O   1 
ATOM   4851 C CB  . TRP B 1 224 ? -0.890  -20.882 7.521   1.00 23.85 ?  224 TRP B CB  1 
ATOM   4852 C CG  . TRP B 1 224 ? -1.043  -21.323 6.094   1.00 25.48 ?  224 TRP B CG  1 
ATOM   4853 C CD1 . TRP B 1 224 ? -0.869  -22.588 5.598   1.00 30.48 ?  224 TRP B CD1 1 
ATOM   4854 C CD2 . TRP B 1 224 ? -1.335  -20.486 4.974   1.00 28.21 ?  224 TRP B CD2 1 
ATOM   4855 N NE1 . TRP B 1 224 ? -1.057  -22.587 4.230   1.00 26.10 ?  224 TRP B NE1 1 
ATOM   4856 C CE2 . TRP B 1 224 ? -1.339  -21.304 3.827   1.00 26.02 ?  224 TRP B CE2 1 
ATOM   4857 C CE3 . TRP B 1 224 ? -1.594  -19.116 4.829   1.00 23.68 ?  224 TRP B CE3 1 
ATOM   4858 C CZ2 . TRP B 1 224 ? -1.604  -20.799 2.560   1.00 27.57 ?  224 TRP B CZ2 1 
ATOM   4859 C CZ3 . TRP B 1 224 ? -1.845  -18.617 3.579   1.00 27.68 ?  224 TRP B CZ3 1 
ATOM   4860 C CH2 . TRP B 1 224 ? -1.855  -19.453 2.456   1.00 27.33 ?  224 TRP B CH2 1 
ATOM   4861 N N   . VAL B 1 225 ? 1.641   -20.147 9.975   1.00 22.44 ?  225 VAL B N   1 
ATOM   4862 C CA  . VAL B 1 225 ? 1.732   -19.590 11.348  1.00 21.68 ?  225 VAL B CA  1 
ATOM   4863 C C   . VAL B 1 225 ? 3.015   -18.802 11.599  1.00 20.48 ?  225 VAL B C   1 
ATOM   4864 O O   . VAL B 1 225 ? 4.023   -19.051 10.945  1.00 19.15 ?  225 VAL B O   1 
ATOM   4865 C CB  . VAL B 1 225 ? 1.563   -20.694 12.415  1.00 22.27 ?  225 VAL B CB  1 
ATOM   4866 C CG1 . VAL B 1 225 ? 0.373   -21.592 12.144  1.00 19.62 ?  225 VAL B CG1 1 
ATOM   4867 C CG2 . VAL B 1 225 ? 2.829   -21.515 12.596  1.00 22.99 ?  225 VAL B CG2 1 
ATOM   4868 N N   . VAL B 1 226 ? 2.921   -17.870 12.530  1.00 18.82 ?  226 VAL B N   1 
ATOM   4869 C CA  . VAL B 1 226 ? 4.108   -17.121 13.011  1.00 20.32 ?  226 VAL B CA  1 
ATOM   4870 C C   . VAL B 1 226 ? 3.943   -17.052 14.529  1.00 20.47 ?  226 VAL B C   1 
ATOM   4871 O O   . VAL B 1 226 ? 2.886   -16.649 14.972  1.00 22.57 ?  226 VAL B O   1 
ATOM   4872 C CB  . VAL B 1 226 ? 4.260   -15.701 12.447  1.00 20.74 ?  226 VAL B CB  1 
ATOM   4873 C CG1 . VAL B 1 226 ? 5.415   -14.973 13.106  1.00 21.23 ?  226 VAL B CG1 1 
ATOM   4874 C CG2 . VAL B 1 226 ? 4.408   -15.675 10.938  1.00 17.93 ?  226 VAL B CG2 1 
ATOM   4875 N N   . SER B 1 227 ? 4.937   -17.525 15.264  1.00 21.37 ?  227 SER B N   1 
ATOM   4876 C CA  . SER B 1 227 ? 4.934   -17.392 16.736  1.00 20.31 ?  227 SER B CA  1 
ATOM   4877 C C   . SER B 1 227 ? 5.841   -16.205 17.089  1.00 19.04 ?  227 SER B C   1 
ATOM   4878 O O   . SER B 1 227 ? 6.933   -16.133 16.563  1.00 21.22 ?  227 SER B O   1 
ATOM   4879 C CB  . SER B 1 227 ? 5.363   -18.682 17.413  1.00 19.92 ?  227 SER B CB  1 
ATOM   4880 O OG  . SER B 1 227 ? 4.357   -19.670 17.346  1.00 23.07 ?  227 SER B OG  1 
ATOM   4881 N N   . LEU B 1 228 ? 5.353   -15.306 17.935  1.00 19.65 ?  228 LEU B N   1 
ATOM   4882 C CA  . LEU B 1 228 ? 6.145   -14.156 18.367  1.00 19.92 ?  228 LEU B CA  1 
ATOM   4883 C C   . LEU B 1 228 ? 6.379   -14.262 19.864  1.00 20.06 ?  228 LEU B C   1 
ATOM   4884 O O   . LEU B 1 228 ? 5.420   -14.353 20.640  1.00 21.94 ?  228 LEU B O   1 
ATOM   4885 C CB  . LEU B 1 228 ? 5.469   -12.819 18.040  1.00 16.56 ?  228 LEU B CB  1 
ATOM   4886 C CG  . LEU B 1 228 ? 5.213   -12.535 16.559  1.00 20.56 ?  228 LEU B CG  1 
ATOM   4887 C CD1 . LEU B 1 228 ? 4.419   -11.244 16.420  1.00 19.88 ?  228 LEU B CD1 1 
ATOM   4888 C CD2 . LEU B 1 228 ? 6.500   -12.466 15.754  1.00 21.14 ?  228 LEU B CD2 1 
ATOM   4889 N N   . ILE B 1 229 ? 7.657   -14.235 20.221  1.00 20.33 ?  229 ILE B N   1 
ATOM   4890 C CA  . ILE B 1 229 ? 8.064   -14.318 21.650  1.00 20.43 ?  229 ILE B CA  1 
ATOM   4891 C C   . ILE B 1 229 ? 9.090   -13.218 21.946  1.00 21.31 ?  229 ILE B C   1 
ATOM   4892 O O   . ILE B 1 229 ? 9.631   -12.654 21.003  1.00 21.09 ?  229 ILE B O   1 
ATOM   4893 C CB  . ILE B 1 229 ? 8.644   -15.706 21.990  1.00 22.05 ?  229 ILE B CB  1 
ATOM   4894 C CG1 . ILE B 1 229 ? 10.005  -15.949 21.340  1.00 22.77 ?  229 ILE B CG1 1 
ATOM   4895 C CG2 . ILE B 1 229 ? 7.665   -16.823 21.672  1.00 20.47 ?  229 ILE B CG2 1 
ATOM   4896 C CD1 . ILE B 1 229 ? 10.739  -17.118 21.931  1.00 24.28 ?  229 ILE B CD1 1 
ATOM   4897 N N   . SER B 1 230 ? 9.325   -12.973 23.226  1.00 19.37 ?  230 SER B N   1 
ATOM   4898 C CA  . SER B 1 230 ? 10.294  -11.983 23.676  1.00 20.37 ?  230 SER B CA  1 
ATOM   4899 C C   . SER B 1 230 ? 10.589  -12.267 25.145  1.00 21.83 ?  230 SER B C   1 
ATOM   4900 O O   . SER B 1 230 ? 9.756   -12.874 25.829  1.00 20.44 ?  230 SER B O   1 
ATOM   4901 C CB  . SER B 1 230 ? 9.725   -10.563 23.488  1.00 22.72 ?  230 SER B CB  1 
ATOM   4902 O OG  . SER B 1 230 ? 10.513  -9.552  24.089  1.00 20.31 ?  230 SER B OG  1 
ATOM   4903 N N   . PRO B 1 231 ? 11.762  -11.882 25.652  1.00 21.36 ?  231 PRO B N   1 
ATOM   4904 C CA  . PRO B 1 231 ? 11.980  -11.949 27.104  1.00 23.78 ?  231 PRO B CA  1 
ATOM   4905 C C   . PRO B 1 231 ? 11.304  -10.824 27.863  1.00 20.66 ?  231 PRO B C   1 
ATOM   4906 O O   . PRO B 1 231 ? 11.380  -10.793 29.095  1.00 23.97 ?  231 PRO B O   1 
ATOM   4907 C CB  . PRO B 1 231 ? 13.512  -11.867 27.233  1.00 24.01 ?  231 PRO B CB  1 
ATOM   4908 C CG  . PRO B 1 231 ? 13.962  -11.102 26.016  1.00 20.50 ?  231 PRO B CG  1 
ATOM   4909 C CD  . PRO B 1 231 ? 12.970  -11.471 24.911  1.00 20.46 ?  231 PRO B CD  1 
ATOM   4910 N N   . SER B 1 232 ? 10.613  -9.917  27.165  1.00 22.71 ?  232 SER B N   1 
ATOM   4911 C CA  . SER B 1 232 ? 10.253  -8.644  27.778  1.00 20.19 ?  232 SER B CA  1 
ATOM   4912 C C   . SER B 1 232 ? 9.233   -8.821  28.894  1.00 20.64 ?  232 SER B C   1 
ATOM   4913 O O   . SER B 1 232 ? 9.416   -8.299  29.997  1.00 20.18 ?  232 SER B O   1 
ATOM   4914 C CB  . SER B 1 232 ? 9.726   -7.685  26.720  1.00 24.39 ?  232 SER B CB  1 
ATOM   4915 O OG  . SER B 1 232 ? 8.478   -8.145  26.233  1.00 27.21 ?  232 SER B OG  1 
ATOM   4916 N N   . LYS B 1 233 ? 8.135   -9.528  28.627  1.00 19.15 ?  233 LYS B N   1 
ATOM   4917 C CA  . LYS B 1 233 ? 7.134   -9.673  29.676  1.00 21.65 ?  233 LYS B CA  1 
ATOM   4918 C C   . LYS B 1 233 ? 7.628   -10.605 30.771  1.00 22.27 ?  233 LYS B C   1 
ATOM   4919 O O   . LYS B 1 233 ? 7.409   -10.348 31.960  1.00 22.59 ?  233 LYS B O   1 
ATOM   4920 C CB  . LYS B 1 233 ? 5.815   -10.182 29.081  1.00 24.55 ?  233 LYS B CB  1 
ATOM   4921 C CG  . LYS B 1 233 ? 4.562   -9.703  29.815  1.00 27.99 ?  233 LYS B CG  1 
ATOM   4922 C CD  . LYS B 1 233 ? 4.246   -8.229  29.546  1.00 21.64 ?  233 LYS B CD  1 
ATOM   4923 C CE  . LYS B 1 233 ? 4.259   -7.896  28.061  1.00 23.90 ?  233 LYS B CE  1 
ATOM   4924 N NZ  . LYS B 1 233 ? 3.738   -6.505  27.851  1.00 25.01 1  233 LYS B NZ  1 
ATOM   4925 N N   . THR B 1 234 ? 8.299   -11.691 30.374  1.00 19.83 ?  234 THR B N   1 
ATOM   4926 C CA  . THR B 1 234 ? 8.789   -12.697 31.315  1.00 19.09 ?  234 THR B CA  1 
ATOM   4927 C C   . THR B 1 234 ? 9.803   -12.125 32.302  1.00 20.91 ?  234 THR B C   1 
ATOM   4928 O O   . THR B 1 234 ? 9.775   -12.458 33.489  1.00 22.77 ?  234 THR B O   1 
ATOM   4929 C CB  . THR B 1 234 ? 9.425   -13.828 30.527  1.00 22.14 ?  234 THR B CB  1 
ATOM   4930 O OG1 . THR B 1 234 ? 8.487   -14.273 29.528  1.00 20.11 ?  234 THR B OG1 1 
ATOM   4931 C CG2 . THR B 1 234 ? 9.847   -14.978 31.456  1.00 21.53 ?  234 THR B CG2 1 
ATOM   4932 N N   . PHE B 1 235 ? 10.734  -11.306 31.823  1.00 20.28 ?  235 PHE B N   1 
ATOM   4933 C CA  . PHE B 1 235 ? 11.864  -10.872 32.635  1.00 19.12 ?  235 PHE B CA  1 
ATOM   4934 C C   . PHE B 1 235 ? 11.847  -9.382  32.962  1.00 22.05 ?  235 PHE B C   1 
ATOM   4935 O O   . PHE B 1 235 ? 12.815  -8.881  33.527  1.00 20.38 ?  235 PHE B O   1 
ATOM   4936 C CB  . PHE B 1 235 ? 13.165  -11.261 31.943  1.00 20.86 ?  235 PHE B CB  1 
ATOM   4937 C CG  . PHE B 1 235 ? 13.347  -12.759 31.795  1.00 22.15 ?  235 PHE B CG  1 
ATOM   4938 C CD1 . PHE B 1 235 ? 13.761  -13.528 32.875  1.00 22.54 ?  235 PHE B CD1 1 
ATOM   4939 C CD2 . PHE B 1 235 ? 13.100  -13.391 30.591  1.00 23.31 ?  235 PHE B CD2 1 
ATOM   4940 C CE1 . PHE B 1 235 ? 13.924  -14.894 32.750  1.00 23.03 ?  235 PHE B CE1 1 
ATOM   4941 C CE2 . PHE B 1 235 ? 13.267  -14.774 30.463  1.00 26.06 ?  235 PHE B CE2 1 
ATOM   4942 C CZ  . PHE B 1 235 ? 13.678  -15.520 31.552  1.00 20.12 ?  235 PHE B CZ  1 
ATOM   4943 N N   . ASN B 1 236 ? 10.757  -8.680  32.664  1.00 18.16 ?  236 ASN B N   1 
ATOM   4944 C CA  . ASN B 1 236 ? 10.610  -7.242  32.936  1.00 20.13 ?  236 ASN B CA  1 
ATOM   4945 C C   . ASN B 1 236 ? 11.612  -6.418  32.122  1.00 21.88 ?  236 ASN B C   1 
ATOM   4946 O O   . ASN B 1 236 ? 12.326  -5.554  32.651  1.00 19.53 ?  236 ASN B O   1 
ATOM   4947 C CB  . ASN B 1 236 ? 10.727  -6.928  34.429  1.00 20.18 ?  236 ASN B CB  1 
ATOM   4948 C CG  . ASN B 1 236 ? 10.079  -5.613  34.791  1.00 20.36 ?  236 ASN B CG  1 
ATOM   4949 O OD1 . ASN B 1 236 ? 9.216   -5.119  34.074  1.00 19.41 ?  236 ASN B OD1 1 
ATOM   4950 N ND2 . ASN B 1 236 ? 10.494  -5.034  35.917  1.00 22.21 ?  236 ASN B ND2 1 
ATOM   4951 N N   . LEU B 1 237 ? 11.630  -6.668  30.813  1.00 20.90 ?  237 LEU B N   1 
ATOM   4952 C CA  . LEU B 1 237 ? 12.549  -6.038  29.867  1.00 20.28 ?  237 LEU B CA  1 
ATOM   4953 C C   . LEU B 1 237 ? 11.802  -5.441  28.681  1.00 18.37 ?  237 LEU B C   1 
ATOM   4954 O O   . LEU B 1 237 ? 12.252  -5.551  27.541  1.00 21.56 ?  237 LEU B O   1 
ATOM   4955 C CB  . LEU B 1 237 ? 13.587  -7.049  29.368  1.00 19.87 ?  237 LEU B CB  1 
ATOM   4956 C CG  . LEU B 1 237 ? 14.455  -7.719  30.433  1.00 20.96 ?  237 LEU B CG  1 
ATOM   4957 C CD1 . LEU B 1 237 ? 15.251  -8.842  29.781  1.00 20.09 ?  237 LEU B CD1 1 
ATOM   4958 C CD2 . LEU B 1 237 ? 15.380  -6.710  31.100  1.00 18.53 ?  237 LEU B CD2 1 
ATOM   4959 N N   . ALA B 1 238 ? 10.684  -4.771  28.917  1.00 19.17 ?  238 ALA B N   1 
ATOM   4960 C CA  . ALA B 1 238 ? 9.914   -4.155  27.821  1.00 19.03 ?  238 ALA B CA  1 
ATOM   4961 C C   . ALA B 1 238 ? 10.812  -3.267  26.964  1.00 22.69 ?  238 ALA B C   1 
ATOM   4962 O O   . ALA B 1 238 ? 10.745  -3.351  25.750  1.00 22.70 ?  238 ALA B O   1 
ATOM   4963 C CB  . ALA B 1 238 ? 8.792   -3.335  28.362  1.00 20.05 ?  238 ALA B CB  1 
ATOM   4964 N N   . ALA B 1 239 ? 11.605  -2.439  27.618  1.00 21.73 ?  239 ALA B N   1 
ATOM   4965 C CA  . ALA B 1 239 ? 12.417  -1.492  26.869  1.00 19.60 ?  239 ALA B CA  1 
ATOM   4966 C C   . ALA B 1 239 ? 13.684  -2.121  26.313  1.00 20.21 ?  239 ALA B C   1 
ATOM   4967 O O   . ALA B 1 239 ? 14.458  -1.424  25.659  1.00 21.68 ?  239 ALA B O   1 
ATOM   4968 C CB  . ALA B 1 239 ? 12.762  -0.283  27.738  1.00 21.98 ?  239 ALA B CB  1 
ATOM   4969 N N   . LEU B 1 240 ? 13.924  -3.414  26.541  1.00 20.00 ?  240 LEU B N   1 
ATOM   4970 C CA  . LEU B 1 240 ? 15.089  -4.021  25.910  1.00 20.00 ?  240 LEU B CA  1 
ATOM   4971 C C   . LEU B 1 240 ? 14.936  -4.064  24.397  1.00 18.42 ?  240 LEU B C   1 
ATOM   4972 O O   . LEU B 1 240 ? 15.938  -4.035  23.674  1.00 20.27 ?  240 LEU B O   1 
ATOM   4973 C CB  . LEU B 1 240 ? 15.320  -5.430  26.435  1.00 19.10 ?  240 LEU B CB  1 
ATOM   4974 C CG  . LEU B 1 240 ? 16.519  -6.131  25.815  1.00 19.87 ?  240 LEU B CG  1 
ATOM   4975 C CD1 . LEU B 1 240 ? 17.809  -5.392  26.182  1.00 20.02 ?  240 LEU B CD1 1 
ATOM   4976 C CD2 . LEU B 1 240 ? 16.538  -7.583  26.285  1.00 20.79 ?  240 LEU B CD2 1 
ATOM   4977 N N   . HIS B 1 241 ? 13.700  -4.131  23.910  1.00 18.58 ?  241 HIS B N   1 
ATOM   4978 C CA  . HIS B 1 241 ? 13.415  -4.214  22.478  1.00 18.77 ?  241 HIS B CA  1 
ATOM   4979 C C   . HIS B 1 241 ? 14.148  -5.391  21.839  1.00 19.94 ?  241 HIS B C   1 
ATOM   4980 O O   . HIS B 1 241 ? 14.876  -5.254  20.850  1.00 21.24 ?  241 HIS B O   1 
ATOM   4981 C CB  . HIS B 1 241 ? 13.741  -2.902  21.766  1.00 22.26 ?  241 HIS B CB  1 
ATOM   4982 C CG  . HIS B 1 241 ? 12.815  -1.781  22.131  1.00 20.94 ?  241 HIS B CG  1 
ATOM   4983 N ND1 . HIS B 1 241 ? 12.896  -0.530  21.559  1.00 21.25 ?  241 HIS B ND1 1 
ATOM   4984 C CD2 . HIS B 1 241 ? 11.789  -1.725  23.015  1.00 24.86 ?  241 HIS B CD2 1 
ATOM   4985 C CE1 . HIS B 1 241 ? 11.966  0.253   22.079  1.00 21.33 ?  241 HIS B CE1 1 
ATOM   4986 N NE2 . HIS B 1 241 ? 11.280  -0.447  22.968  1.00 22.98 ?  241 HIS B NE2 1 
ATOM   4987 N N   . ALA B 1 242 ? 13.920  -6.567  22.407  1.00 21.82 ?  242 ALA B N   1 
ATOM   4988 C CA  . ALA B 1 242 ? 14.399  -7.826  21.863  1.00 23.27 ?  242 ALA B CA  1 
ATOM   4989 C C   . ALA B 1 242 ? 13.209  -8.758  21.707  1.00 20.32 ?  242 ALA B C   1 
ATOM   4990 O O   . ALA B 1 242 ? 12.419  -8.918  22.646  1.00 22.45 ?  242 ALA B O   1 
ATOM   4991 C CB  . ALA B 1 242 ? 15.446  -8.464  22.779  1.00 19.28 ?  242 ALA B CB  1 
ATOM   4992 N N   . ALA B 1 243 ? 13.086  -9.367  20.535  1.00 19.80 ?  243 ALA B N   1 
ATOM   4993 C CA  . ALA B 1 243 ? 11.983  -10.280 20.269  1.00 20.65 ?  243 ALA B CA  1 
ATOM   4994 C C   . ALA B 1 243 ? 12.447  -11.299 19.243  1.00 20.75 ?  243 ALA B C   1 
ATOM   4995 O O   . ALA B 1 243 ? 13.567  -11.234 18.731  1.00 20.09 ?  243 ALA B O   1 
ATOM   4996 C CB  . ALA B 1 243 ? 10.732  -9.515  19.817  1.00 22.10 ?  243 ALA B CB  1 
ATOM   4997 N N   . CYS B 1 244 ? 11.596  -12.276 18.963  1.00 18.85 ?  244 CYS B N   1 
ATOM   4998 C CA  . CYS B 1 244 ? 11.981  -13.280 17.985  1.00 21.16 ?  244 CYS B CA  1 
ATOM   4999 C C   . CYS B 1 244 ? 10.720  -13.763 17.298  1.00 22.32 ?  244 CYS B C   1 
ATOM   5000 O O   . CYS B 1 244 ? 9.743   -14.088 17.975  1.00 21.41 ?  244 CYS B O   1 
ATOM   5001 C CB  . CYS B 1 244 ? 12.735  -14.442 18.648  1.00 22.50 ?  244 CYS B CB  1 
ATOM   5002 S SG  . CYS B 1 244 ? 13.513  -15.531 17.427  1.00 23.21 ?  244 CYS B SG  1 
ATOM   5003 N N   . ALA B 1 245 ? 10.726  -13.753 15.964  1.00 19.94 ?  245 ALA B N   1 
ATOM   5004 C CA  . ALA B 1 245 ? 9.659   -14.364 15.185  1.00 22.39 ?  245 ALA B CA  1 
ATOM   5005 C C   . ALA B 1 245 ? 10.093  -15.778 14.844  1.00 20.73 ?  245 ALA B C   1 
ATOM   5006 O O   . ALA B 1 245 ? 11.241  -16.001 14.453  1.00 23.29 ?  245 ALA B O   1 
ATOM   5007 C CB  . ALA B 1 245 ? 9.358   -13.568 13.903  1.00 19.24 ?  245 ALA B CB  1 
ATOM   5008 N N   . ILE B 1 246 ? 9.189   -16.731 15.020  1.00 18.73 ?  246 ILE B N   1 
ATOM   5009 C CA  . ILE B 1 246 ? 9.455   -18.124 14.686  1.00 19.37 ?  246 ILE B CA  1 
ATOM   5010 C C   . ILE B 1 246 ? 8.532   -18.463 13.536  1.00 18.04 ?  246 ILE B C   1 
ATOM   5011 O O   . ILE B 1 246 ? 7.305   -18.497 13.701  1.00 19.89 ?  246 ILE B O   1 
ATOM   5012 C CB  . ILE B 1 246 ? 9.244   -19.053 15.892  1.00 17.82 ?  246 ILE B CB  1 
ATOM   5013 C CG1 . ILE B 1 246 ? 10.189  -18.627 17.021  1.00 22.74 ?  246 ILE B CG1 1 
ATOM   5014 C CG2 . ILE B 1 246 ? 9.487   -20.502 15.491  1.00 22.85 ?  246 ILE B CG2 1 
ATOM   5015 C CD1 . ILE B 1 246 ? 9.812   -19.151 18.386  1.00 20.70 ?  246 ILE B CD1 1 
ATOM   5016 N N   . ILE B 1 247 ? 9.117   -18.645 12.357  1.00 20.16 ?  247 ILE B N   1 
ATOM   5017 C CA  . ILE B 1 247 ? 8.353   -18.746 11.118  1.00 20.34 ?  247 ILE B CA  1 
ATOM   5018 C C   . ILE B 1 247 ? 8.827   -19.978 10.360  1.00 21.62 ?  247 ILE B C   1 
ATOM   5019 O O   . ILE B 1 247 ? 9.846   -19.913 9.661   1.00 22.28 ?  247 ILE B O   1 
ATOM   5020 C CB  . ILE B 1 247 ? 8.517   -17.492 10.248  1.00 22.29 ?  247 ILE B CB  1 
ATOM   5021 C CG1 . ILE B 1 247 ? 8.287   -16.224 11.071  1.00 20.78 ?  247 ILE B CG1 1 
ATOM   5022 C CG2 . ILE B 1 247 ? 7.594   -17.577 9.024   1.00 22.53 ?  247 ILE B CG2 1 
ATOM   5023 C CD1 . ILE B 1 247 ? 8.360   -14.944 10.256  1.00 20.34 ?  247 ILE B CD1 1 
ATOM   5024 N N   . PRO B 1 248 ? 8.120   -21.106 10.459  1.00 21.11 ?  248 PRO B N   1 
ATOM   5025 C CA  . PRO B 1 248 ? 8.592   -22.324 9.784   1.00 22.39 ?  248 PRO B CA  1 
ATOM   5026 C C   . PRO B 1 248 ? 8.590   -22.242 8.261   1.00 23.07 ?  248 PRO B C   1 
ATOM   5027 O O   . PRO B 1 248 ? 9.432   -22.893 7.626   1.00 25.06 ?  248 PRO B O   1 
ATOM   5028 C CB  . PRO B 1 248 ? 7.616   -23.400 10.286  1.00 24.76 ?  248 PRO B CB  1 
ATOM   5029 C CG  . PRO B 1 248 ? 7.120   -22.872 11.619  1.00 23.34 ?  248 PRO B CG  1 
ATOM   5030 C CD  . PRO B 1 248 ? 7.048   -21.375 11.441  1.00 21.06 ?  248 PRO B CD  1 
ATOM   5031 N N   . ASN B 1 249 ? 7.662   -21.502 7.658   1.00 20.28 ?  249 ASN B N   1 
ATOM   5032 C CA  . ASN B 1 249 ? 7.631   -21.351 6.195   1.00 24.36 ?  249 ASN B CA  1 
ATOM   5033 C C   . ASN B 1 249 ? 8.835   -20.527 5.761   1.00 25.83 ?  249 ASN B C   1 
ATOM   5034 O O   . ASN B 1 249 ? 8.925   -19.347 6.123   1.00 23.17 ?  249 ASN B O   1 
ATOM   5035 C CB  . ASN B 1 249 ? 6.323   -20.682 5.769   1.00 20.28 ?  249 ASN B CB  1 
ATOM   5036 C CG  . ASN B 1 249 ? 6.179   -20.504 4.257   1.00 26.85 ?  249 ASN B CG  1 
ATOM   5037 O OD1 . ASN B 1 249 ? 7.090   -20.056 3.552   1.00 22.93 ?  249 ASN B OD1 1 
ATOM   5038 N ND2 . ASN B 1 249 ? 4.979   -20.778 3.770   1.00 29.90 ?  249 ASN B ND2 1 
ATOM   5039 N N   . PRO B 1 250 ? 9.779   -21.095 5.004   1.00 22.67 ?  250 PRO B N   1 
ATOM   5040 C CA  . PRO B 1 250 ? 11.012  -20.350 4.698   1.00 24.17 ?  250 PRO B CA  1 
ATOM   5041 C C   . PRO B 1 250 ? 10.788  -19.119 3.824   1.00 26.86 ?  250 PRO B C   1 
ATOM   5042 O O   . PRO B 1 250 ? 11.495  -18.122 3.991   1.00 25.91 ?  250 PRO B O   1 
ATOM   5043 C CB  . PRO B 1 250 ? 11.889  -21.402 4.002   1.00 22.90 ?  250 PRO B CB  1 
ATOM   5044 C CG  . PRO B 1 250 ? 10.904  -22.428 3.488   1.00 30.23 ?  250 PRO B CG  1 
ATOM   5045 C CD  . PRO B 1 250 ? 9.841   -22.487 4.532   1.00 26.31 ?  250 PRO B CD  1 
ATOM   5046 N N   . ASP B 1 251 ? 9.825   -19.132 2.908   1.00 28.11 ?  251 ASP B N   1 
ATOM   5047 C CA  . ASP B 1 251 ? 9.632   -17.943 2.087   1.00 26.35 ?  251 ASP B CA  1 
ATOM   5048 C C   . ASP B 1 251 ? 8.943   -16.839 2.879   1.00 27.09 ?  251 ASP B C   1 
ATOM   5049 O O   . ASP B 1 251 ? 9.358   -15.674 2.833   1.00 27.53 ?  251 ASP B O   1 
ATOM   5050 C CB  . ASP B 1 251 ? 8.851   -18.291 0.824   1.00 29.97 ?  251 ASP B CB  1 
ATOM   5051 C CG  . ASP B 1 251 ? 8.672   -17.095 -0.085  1.00 36.55 ?  251 ASP B CG  1 
ATOM   5052 O OD1 . ASP B 1 251 ? 9.654   -16.718 -0.760  1.00 39.35 ?  251 ASP B OD1 1 
ATOM   5053 O OD2 . ASP B 1 251 ? 7.552   -16.531 -0.125  1.00 36.58 -1 251 ASP B OD2 1 
ATOM   5054 N N   . LEU B 1 252 ? 7.892   -17.192 3.623   1.00 25.44 ?  252 LEU B N   1 
ATOM   5055 C CA  . LEU B 1 252 ? 7.264   -16.253 4.552   1.00 26.55 ?  252 LEU B CA  1 
ATOM   5056 C C   . LEU B 1 252 ? 8.283   -15.671 5.526   1.00 23.58 ?  252 LEU B C   1 
ATOM   5057 O O   . LEU B 1 252 ? 8.253   -14.480 5.854   1.00 24.26 ?  252 LEU B O   1 
ATOM   5058 C CB  . LEU B 1 252 ? 6.167   -16.985 5.320   1.00 23.93 ?  252 LEU B CB  1 
ATOM   5059 C CG  . LEU B 1 252 ? 5.169   -16.150 6.091   1.00 28.26 ?  252 LEU B CG  1 
ATOM   5060 C CD1 . LEU B 1 252 ? 4.308   -15.332 5.119   1.00 29.02 ?  252 LEU B CD1 1 
ATOM   5061 C CD2 . LEU B 1 252 ? 4.307   -17.063 6.951   1.00 30.17 ?  252 LEU B CD2 1 
ATOM   5062 N N   . ARG B 1 253 ? 9.197   -16.505 5.992   1.00 20.96 ?  253 ARG B N   1 
ATOM   5063 C CA  . ARG B 1 253 ? 10.178  -16.061 6.971   1.00 21.24 ?  253 ARG B CA  1 
ATOM   5064 C C   . ARG B 1 253 ? 11.106  -15.002 6.389   1.00 22.83 ?  253 ARG B C   1 
ATOM   5065 O O   . ARG B 1 253 ? 11.386  -13.990 7.041   1.00 20.69 ?  253 ARG B O   1 
ATOM   5066 C CB  . ARG B 1 253 ? 10.969  -17.262 7.466   1.00 21.09 ?  253 ARG B CB  1 
ATOM   5067 C CG  . ARG B 1 253 ? 12.053  -16.930 8.478   1.00 24.77 ?  253 ARG B CG  1 
ATOM   5068 C CD  . ARG B 1 253 ? 12.603  -18.225 9.035   1.00 28.03 ?  253 ARG B CD  1 
ATOM   5069 N NE  . ARG B 1 253 ? 13.446  -18.956 8.087   1.00 27.69 ?  253 ARG B NE  1 
ATOM   5070 C CZ  . ARG B 1 253 ? 13.180  -20.177 7.615   1.00 29.75 ?  253 ARG B CZ  1 
ATOM   5071 N NH1 . ARG B 1 253 ? 12.065  -20.822 7.969   1.00 26.35 1  253 ARG B NH1 1 
ATOM   5072 N NH2 . ARG B 1 253 ? 14.033  -20.763 6.782   1.00 26.69 ?  253 ARG B NH2 1 
ATOM   5073 N N   . ALA B 1 254 ? 11.575  -15.195 5.168   1.00 21.12 ?  254 ALA B N   1 
ATOM   5074 C CA  . ALA B 1 254 ? 12.533  -14.227 4.575   1.00 25.06 ?  254 ALA B CA  1 
ATOM   5075 C C   . ALA B 1 254 ? 11.837  -12.892 4.269   1.00 23.81 ?  254 ALA B C   1 
ATOM   5076 O O   . ALA B 1 254 ? 12.464  -11.852 4.341   1.00 25.60 ?  254 ALA B O   1 
ATOM   5077 C CB  . ALA B 1 254 ? 13.152  -14.826 3.348   1.00 28.07 ?  254 ALA B CB  1 
ATOM   5078 N N   . ARG B 1 255 ? 10.560  -12.952 3.940   1.00 23.36 ?  255 ARG B N   1 
ATOM   5079 C CA  . ARG B 1 255 ? 9.786   -11.744 3.598   1.00 26.14 ?  255 ARG B CA  1 
ATOM   5080 C C   . ARG B 1 255 ? 9.547   -10.947 4.868   1.00 24.73 ?  255 ARG B C   1 
ATOM   5081 O O   . ARG B 1 255 ? 9.684   -9.746  4.831   1.00 23.94 ?  255 ARG B O   1 
ATOM   5082 C CB  . ARG B 1 255 ? 8.474   -12.194 2.970   1.00 27.81 ?  255 ARG B CB  1 
ATOM   5083 C CG  . ARG B 1 255 ? 8.606   -12.634 1.519   1.00 29.56 ?  255 ARG B CG  1 
ATOM   5084 C CD  . ARG B 1 255 ? 7.296   -13.123 0.932   1.00 34.86 ?  255 ARG B CD  1 
ATOM   5085 N NE  . ARG B 1 255 ? 6.263   -12.101 0.862   1.00 40.72 ?  255 ARG B NE  1 
ATOM   5086 C CZ  . ARG B 1 255 ? 4.961   -12.327 1.010   1.00 36.72 ?  255 ARG B CZ  1 
ATOM   5087 N NH1 . ARG B 1 255 ? 4.519   -13.551 1.227   1.00 32.90 1  255 ARG B NH1 1 
ATOM   5088 N NH2 . ARG B 1 255 ? 4.100   -11.332 0.925   1.00 34.13 ?  255 ARG B NH2 1 
ATOM   5089 N N   . ALA B 1 256 ? 9.190   -11.643 5.936   1.00 27.25 ?  256 ALA B N   1 
ATOM   5090 C CA  . ALA B 1 256 ? 9.003   -10.969 7.228   1.00 22.10 ?  256 ALA B CA  1 
ATOM   5091 C C   . ALA B 1 256 ? 10.308  -10.266 7.608   1.00 24.38 ?  256 ALA B C   1 
ATOM   5092 O O   . ALA B 1 256 ? 10.281  -9.111  7.970   1.00 22.67 ?  256 ALA B O   1 
ATOM   5093 C CB  . ALA B 1 256 ? 8.604   -11.986 8.257   1.00 23.31 ?  256 ALA B CB  1 
ATOM   5094 N N   . GLU B 1 257 ? 11.409  -10.996 7.509   1.00 21.74 ?  257 GLU B N   1 
ATOM   5095 C CA  . GLU B 1 257 ? 12.682  -10.401 7.889   1.00 22.89 ?  257 GLU B CA  1 
ATOM   5096 C C   . GLU B 1 257 ? 12.998  -9.184  7.036   1.00 28.20 ?  257 GLU B C   1 
ATOM   5097 O O   . GLU B 1 257 ? 13.505  -8.174  7.543   1.00 23.99 ?  257 GLU B O   1 
ATOM   5098 C CB  . GLU B 1 257 ? 13.799  -11.433 7.767   1.00 27.14 ?  257 GLU B CB  1 
ATOM   5099 C CG  . GLU B 1 257 ? 15.177  -10.851 7.943   1.00 28.79 ?  257 GLU B CG  1 
ATOM   5100 C CD  . GLU B 1 257 ? 16.263  -11.835 7.562   1.00 35.79 ?  257 GLU B CD  1 
ATOM   5101 O OE1 . GLU B 1 257 ? 17.283  -11.889 8.272   1.00 38.09 ?  257 GLU B OE1 1 
ATOM   5102 O OE2 . GLU B 1 257 ? 16.090  -12.554 6.559   1.00 37.18 -1 257 GLU B OE2 1 
ATOM   5103 N N   . GLU B 1 258 ? 12.737  -9.272  5.728   1.00 23.58 ?  258 GLU B N   1 
ATOM   5104 C CA  . GLU B 1 258 ? 12.920  -8.104  4.877   1.00 26.37 ?  258 GLU B CA  1 
ATOM   5105 C C   . GLU B 1 258 ? 12.043  -6.954  5.348   1.00 27.19 ?  258 GLU B C   1 
ATOM   5106 O O   . GLU B 1 258 ? 12.487  -5.802  5.386   1.00 23.19 ?  258 GLU B O   1 
ATOM   5107 C CB  . GLU B 1 258 ? 12.615  -8.457  3.420   1.00 24.33 ?  258 GLU B CB  1 
ATOM   5108 C CG  . GLU B 1 258 ? 12.819  -7.316  2.451   1.00 33.68 ?  258 GLU B CG  1 
ATOM   5109 C CD  . GLU B 1 258 ? 13.429  -7.772  1.138   1.00 41.37 ?  258 GLU B CD  1 
ATOM   5110 O OE1 . GLU B 1 258 ? 13.791  -6.898  0.322   1.00 43.90 ?  258 GLU B OE1 1 
ATOM   5111 O OE2 . GLU B 1 258 ? 13.545  -9.005  0.926   1.00 40.13 -1 258 GLU B OE2 1 
ATOM   5112 N N   . SER B 1 259 ? 10.800  -7.254  5.742   1.00 21.37 ?  259 SER B N   1 
ATOM   5113 C CA  . SER B 1 259 ? 9.925   -6.199  6.244   1.00 21.71 ?  259 SER B CA  1 
ATOM   5114 C C   . SER B 1 259 ? 10.458  -5.600  7.543   1.00 21.98 ?  259 SER B C   1 
ATOM   5115 O O   . SER B 1 259 ? 10.379  -4.382  7.742   1.00 22.69 ?  259 SER B O   1 
ATOM   5116 C CB  . SER B 1 259 ? 8.515   -6.737  6.450   1.00 24.55 ?  259 SER B CB  1 
ATOM   5117 O OG  . SER B 1 259 ? 7.607   -5.680  6.704   1.00 32.88 ?  259 SER B OG  1 
ATOM   5118 N N   . PHE B 1 260 ? 11.007  -6.431  8.437   1.00 20.46 ?  260 PHE B N   1 
ATOM   5119 C CA  . PHE B 1 260 ? 11.604  -5.898  9.664   1.00 18.59 ?  260 PHE B CA  1 
ATOM   5120 C C   . PHE B 1 260 ? 12.734  -4.930  9.342   1.00 22.74 ?  260 PHE B C   1 
ATOM   5121 O O   . PHE B 1 260 ? 12.854  -3.859  9.954   1.00 24.76 ?  260 PHE B O   1 
ATOM   5122 C CB  . PHE B 1 260 ? 12.141  -7.034  10.562  1.00 20.55 ?  260 PHE B CB  1 
ATOM   5123 C CG  . PHE B 1 260 ? 11.098  -8.030  11.020  1.00 22.26 ?  260 PHE B CG  1 
ATOM   5124 C CD1 . PHE B 1 260 ? 9.749   -7.752  10.932  1.00 19.88 ?  260 PHE B CD1 1 
ATOM   5125 C CD2 . PHE B 1 260 ? 11.492  -9.271  11.530  1.00 20.83 ?  260 PHE B CD2 1 
ATOM   5126 C CE1 . PHE B 1 260 ? 8.797   -8.689  11.329  1.00 21.53 ?  260 PHE B CE1 1 
ATOM   5127 C CE2 . PHE B 1 260 ? 10.558  -10.202 11.933  1.00 22.68 ?  260 PHE B CE2 1 
ATOM   5128 C CZ  . PHE B 1 260 ? 9.202   -9.917  11.833  1.00 21.32 ?  260 PHE B CZ  1 
ATOM   5129 N N   . PHE B 1 261 ? 13.604  -5.305  8.404   1.00 22.29 ?  261 PHE B N   1 
ATOM   5130 C CA  . PHE B 1 261 ? 14.743  -4.451  8.102   1.00 23.45 ?  261 PHE B CA  1 
ATOM   5131 C C   . PHE B 1 261 ? 14.294  -3.125  7.520   1.00 27.71 ?  261 PHE B C   1 
ATOM   5132 O O   . PHE B 1 261 ? 14.787  -2.066  7.927   1.00 24.82 ?  261 PHE B O   1 
ATOM   5133 C CB  . PHE B 1 261 ? 15.698  -5.171  7.162   1.00 25.64 ?  261 PHE B CB  1 
ATOM   5134 C CG  . PHE B 1 261 ? 16.679  -6.001  7.893   1.00 35.90 ?  261 PHE B CG  1 
ATOM   5135 C CD1 . PHE B 1 261 ? 17.759  -5.409  8.527   1.00 34.19 ?  261 PHE B CD1 1 
ATOM   5136 C CD2 . PHE B 1 261 ? 16.476  -7.361  8.040   1.00 34.58 ?  261 PHE B CD2 1 
ATOM   5137 C CE1 . PHE B 1 261 ? 18.649  -6.170  9.241   1.00 37.18 ?  261 PHE B CE1 1 
ATOM   5138 C CE2 . PHE B 1 261 ? 17.358  -8.124  8.747   1.00 32.35 ?  261 PHE B CE2 1 
ATOM   5139 C CZ  . PHE B 1 261 ? 18.453  -7.528  9.348   1.00 34.78 ?  261 PHE B CZ  1 
ATOM   5140 N N   . LEU B 1 262 ? 13.342  -3.175  6.579   1.00 24.92 ?  262 LEU B N   1 
ATOM   5141 C CA  . LEU B 1 262 ? 12.820  -1.979  5.930   1.00 24.41 ?  262 LEU B CA  1 
ATOM   5142 C C   . LEU B 1 262 ? 12.181  -1.034  6.937   1.00 23.10 ?  262 LEU B C   1 
ATOM   5143 O O   . LEU B 1 262 ? 12.302  0.189   6.816   1.00 24.99 ?  262 LEU B O   1 
ATOM   5144 C CB  . LEU B 1 262 ? 11.789  -2.379  4.868   1.00 21.58 ?  262 LEU B CB  1 
ATOM   5145 C CG  . LEU B 1 262 ? 12.057  -2.126  3.389   1.00 34.12 ?  262 LEU B CG  1 
ATOM   5146 C CD1 . LEU B 1 262 ? 10.737  -2.164  2.605   1.00 26.13 ?  262 LEU B CD1 1 
ATOM   5147 C CD2 . LEU B 1 262 ? 12.768  -0.795  3.200   1.00 25.34 ?  262 LEU B CD2 1 
ATOM   5148 N N   . ALA B 1 263 ? 11.485  -1.586  7.930   1.00 21.54 ?  263 ALA B N   1 
ATOM   5149 C CA  . ALA B 1 263 ? 10.798  -0.779  8.934   1.00 24.33 ?  263 ALA B CA  1 
ATOM   5150 C C   . ALA B 1 263 ? 11.749  -0.177  9.967   1.00 25.25 ?  263 ALA B C   1 
ATOM   5151 O O   . ALA B 1 263 ? 11.387  0.801   10.636  1.00 21.83 ?  263 ALA B O   1 
ATOM   5152 C CB  . ALA B 1 263 ? 9.757   -1.634  9.652   1.00 19.07 ?  263 ALA B CB  1 
ATOM   5153 N N   . GLY B 1 264 ? 12.940  -0.744  10.125  1.00 23.91 ?  264 GLY B N   1 
ATOM   5154 C CA  . GLY B 1 264 ? 13.836  -0.318  11.181  1.00 26.40 ?  264 GLY B CA  1 
ATOM   5155 C C   . GLY B 1 264 ? 13.770  -1.127  12.457  1.00 26.29 ?  264 GLY B C   1 
ATOM   5156 O O   . GLY B 1 264 ? 14.141  -0.613  13.523  1.00 23.03 ?  264 GLY B O   1 
ATOM   5157 N N   . ILE B 1 265 ? 13.303  -2.374  12.399  1.00 20.59 ?  265 ILE B N   1 
ATOM   5158 C CA  . ILE B 1 265 ? 13.150  -3.170  13.618  1.00 19.18 ?  265 ILE B CA  1 
ATOM   5159 C C   . ILE B 1 265 ? 13.855  -4.511  13.439  1.00 20.07 ?  265 ILE B C   1 
ATOM   5160 O O   . ILE B 1 265 ? 13.613  -5.457  14.197  1.00 21.00 ?  265 ILE B O   1 
ATOM   5161 C CB  . ILE B 1 265 ? 11.665  -3.366  13.976  1.00 21.77 ?  265 ILE B CB  1 
ATOM   5162 C CG1 . ILE B 1 265 ? 10.913  -4.034  12.810  1.00 20.45 ?  265 ILE B CG1 1 
ATOM   5163 C CG2 . ILE B 1 265 ? 10.998  -2.028  14.311  1.00 21.06 ?  265 ILE B CG2 1 
ATOM   5164 C CD1 . ILE B 1 265 ? 9.593   -4.709  13.239  1.00 19.43 ?  265 ILE B CD1 1 
ATOM   5165 N N   . GLY B 1 266 ? 14.731  -4.605  12.443  1.00 20.70 ?  266 GLY B N   1 
ATOM   5166 C CA  . GLY B 1 266 ? 15.454  -5.844  12.212  1.00 21.77 ?  266 GLY B CA  1 
ATOM   5167 C C   . GLY B 1 266 ? 16.853  -5.909  12.809  1.00 25.83 ?  266 GLY B C   1 
ATOM   5168 O O   . GLY B 1 266 ? 17.471  -6.979  12.800  1.00 23.60 ?  266 GLY B O   1 
ATOM   5169 N N   . GLU B 1 267 ? 17.377  -4.773  13.313  1.00 22.37 ?  267 GLU B N   1 
ATOM   5170 C CA  . GLU B 1 267 ? 18.746  -4.692  13.846  1.00 24.55 ?  267 GLU B CA  1 
ATOM   5171 C C   . GLU B 1 267 ? 18.718  -4.599  15.365  1.00 21.46 ?  267 GLU B C   1 
ATOM   5172 O O   . GLU B 1 267 ? 17.979  -3.764  15.912  1.00 19.60 ?  267 GLU B O   1 
ATOM   5173 C CB  . GLU B 1 267 ? 19.486  -3.476  13.286  1.00 25.91 ?  267 GLU B CB  1 
ATOM   5174 C CG  . GLU B 1 267 ? 19.646  -3.475  11.761  1.00 30.90 ?  267 GLU B CG  1 
ATOM   5175 C CD  . GLU B 1 267 ? 20.698  -2.474  11.290  1.00 38.10 ?  267 GLU B CD  1 
ATOM   5176 O OE1 . GLU B 1 267 ? 21.204  -2.634  10.156  1.00 42.84 ?  267 GLU B OE1 1 
ATOM   5177 O OE2 . GLU B 1 267 ? 21.027  -1.538  12.058  1.00 39.99 -1 267 GLU B OE2 1 
ATOM   5178 N N   . PRO B 1 268 ? 19.505  -5.396  16.082  1.00 20.84 ?  268 PRO B N   1 
ATOM   5179 C CA  . PRO B 1 268 ? 19.482  -5.304  17.544  1.00 20.03 ?  268 PRO B CA  1 
ATOM   5180 C C   . PRO B 1 268 ? 20.177  -4.045  18.016  1.00 21.77 ?  268 PRO B C   1 
ATOM   5181 O O   . PRO B 1 268 ? 21.179  -3.605  17.437  1.00 19.77 ?  268 PRO B O   1 
ATOM   5182 C CB  . PRO B 1 268 ? 20.231  -6.562  18.003  1.00 24.12 ?  268 PRO B CB  1 
ATOM   5183 C CG  . PRO B 1 268 ? 21.010  -7.024  16.823  1.00 25.50 ?  268 PRO B CG  1 
ATOM   5184 C CD  . PRO B 1 268 ? 20.323  -6.518  15.592  1.00 23.79 ?  268 PRO B CD  1 
ATOM   5185 N N   . ASN B 1 269 ? 19.644  -3.476  19.095  1.00 20.65 ?  269 ASN B N   1 
ATOM   5186 C CA  . ASN B 1 269 ? 20.358  -2.418  19.787  1.00 20.99 ?  269 ASN B CA  1 
ATOM   5187 C C   . ASN B 1 269 ? 21.518  -3.023  20.581  1.00 19.75 ?  269 ASN B C   1 
ATOM   5188 O O   . ASN B 1 269 ? 21.766  -4.233  20.560  1.00 20.99 ?  269 ASN B O   1 
ATOM   5189 C CB  . ASN B 1 269 ? 19.416  -1.607  20.685  1.00 22.44 ?  269 ASN B CB  1 
ATOM   5190 C CG  . ASN B 1 269 ? 18.827  -2.418  21.839  1.00 22.65 ?  269 ASN B CG  1 
ATOM   5191 O OD1 . ASN B 1 269 ? 19.549  -3.061  22.608  1.00 22.12 ?  269 ASN B OD1 1 
ATOM   5192 N ND2 . ASN B 1 269 ? 17.501  -2.359  21.980  1.00 20.94 ?  269 ASN B ND2 1 
ATOM   5193 N N   . LEU B 1 270 ? 22.265  -2.150  21.243  1.00 18.73 ?  270 LEU B N   1 
ATOM   5194 C CA  . LEU B 1 270 ? 23.529  -2.497  21.945  1.00 23.81 ?  270 LEU B CA  1 
ATOM   5195 C C   . LEU B 1 270 ? 23.412  -3.504  23.099  1.00 25.01 ?  270 LEU B C   1 
ATOM   5196 O O   . LEU B 1 270 ? 24.442  -4.002  23.516  1.00 24.25 ?  270 LEU B O   1 
ATOM   5197 C CB  . LEU B 1 270 ? 24.160  -1.178  22.412  1.00 21.10 ?  270 LEU B CB  1 
ATOM   5198 C CG  . LEU B 1 270 ? 23.590  -0.463  23.646  1.00 26.33 ?  270 LEU B CG  1 
ATOM   5199 C CD1 . LEU B 1 270 ? 24.377  0.801   23.921  1.00 28.67 ?  270 LEU B CD1 1 
ATOM   5200 C CD2 . LEU B 1 270 ? 22.119  -0.090  23.521  1.00 25.65 ?  270 LEU B CD2 1 
ATOM   5201 N N   . LEU B 1 271 ? 22.216  -3.729  23.611  1.00 20.54 ?  271 LEU B N   1 
ATOM   5202 C CA  . LEU B 1 271 ? 22.066  -4.707  24.683  1.00 19.95 ?  271 LEU B CA  1 
ATOM   5203 C C   . LEU B 1 271 ? 21.166  -5.884  24.320  1.00 19.56 ?  271 LEU B C   1 
ATOM   5204 O O   . LEU B 1 271 ? 21.146  -6.871  25.061  1.00 18.71 ?  271 LEU B O   1 
ATOM   5205 C CB  . LEU B 1 271 ? 21.518  -4.034  25.955  1.00 23.97 ?  271 LEU B CB  1 
ATOM   5206 C CG  . LEU B 1 271 ? 22.421  -3.020  26.660  1.00 25.28 ?  271 LEU B CG  1 
ATOM   5207 C CD1 . LEU B 1 271 ? 21.706  -2.418  27.878  1.00 25.45 ?  271 LEU B CD1 1 
ATOM   5208 C CD2 . LEU B 1 271 ? 23.750  -3.670  27.062  1.00 25.08 ?  271 LEU B CD2 1 
ATOM   5209 N N   . ALA B 1 272 ? 20.445  -5.820  23.196  1.00 19.81 ?  272 ALA B N   1 
ATOM   5210 C CA  . ALA B 1 272 ? 19.393  -6.794  22.914  1.00 16.82 ?  272 ALA B CA  1 
ATOM   5211 C C   . ALA B 1 272 ? 19.923  -8.225  22.877  1.00 18.93 ?  272 ALA B C   1 
ATOM   5212 O O   . ALA B 1 272 ? 19.318  -9.134  23.453  1.00 19.81 ?  272 ALA B O   1 
ATOM   5213 C CB  . ALA B 1 272 ? 18.709  -6.445  21.581  1.00 18.32 ?  272 ALA B CB  1 
ATOM   5214 N N   . ILE B 1 273 ? 21.027  -8.456  22.169  1.00 20.21 ?  273 ILE B N   1 
ATOM   5215 C CA  . ILE B 1 273 ? 21.551  -9.815  21.974  1.00 21.74 ?  273 ILE B CA  1 
ATOM   5216 C C   . ILE B 1 273 ? 22.090  -10.405 23.283  1.00 22.03 ?  273 ILE B C   1 
ATOM   5217 O O   . ILE B 1 273 ? 21.571  -11.439 23.742  1.00 19.93 ?  273 ILE B O   1 
ATOM   5218 C CB  . ILE B 1 273 ? 22.623  -9.831  20.867  1.00 22.47 ?  273 ILE B CB  1 
ATOM   5219 C CG1 . ILE B 1 273 ? 22.018  -9.431  19.514  1.00 22.21 ?  273 ILE B CG1 1 
ATOM   5220 C CG2 . ILE B 1 273 ? 23.320  -11.196 20.801  1.00 24.16 ?  273 ILE B CG2 1 
ATOM   5221 C CD1 . ILE B 1 273 ? 20.769  -10.249 19.106  1.00 24.39 ?  273 ILE B CD1 1 
ATOM   5222 N N   . PRO B 1 274 ? 23.111  -9.825  23.932  1.00 22.55 ?  274 PRO B N   1 
ATOM   5223 C CA  . PRO B 1 274 ? 23.612  -10.483 25.155  1.00 22.16 ?  274 PRO B CA  1 
ATOM   5224 C C   . PRO B 1 274 ? 22.557  -10.611 26.246  1.00 21.99 ?  274 PRO B C   1 
ATOM   5225 O O   . PRO B 1 274 ? 22.530  -11.621 26.959  1.00 23.57 ?  274 PRO B O   1 
ATOM   5226 C CB  . PRO B 1 274 ? 24.792  -9.589  25.585  1.00 24.76 ?  274 PRO B CB  1 
ATOM   5227 C CG  . PRO B 1 274 ? 24.575  -8.286  24.926  1.00 21.60 ?  274 PRO B CG  1 
ATOM   5228 C CD  . PRO B 1 274 ? 23.887  -8.608  23.616  1.00 20.63 ?  274 PRO B CD  1 
ATOM   5229 N N   . ALA B 1 275 ? 21.669  -9.620  26.387  1.00 21.41 ?  275 ALA B N   1 
ATOM   5230 C CA  . ALA B 1 275 ? 20.682  -9.661  27.465  1.00 20.88 ?  275 ALA B CA  1 
ATOM   5231 C C   . ALA B 1 275 ? 19.636  -10.744 27.224  1.00 21.93 ?  275 ALA B C   1 
ATOM   5232 O O   . ALA B 1 275 ? 19.260  -11.476 28.148  1.00 22.77 ?  275 ALA B O   1 
ATOM   5233 C CB  . ALA B 1 275 ? 20.013  -8.290  27.615  1.00 20.15 ?  275 ALA B CB  1 
ATOM   5234 N N   . ALA B 1 276 ? 19.131  -10.839 25.991  1.00 18.93 ?  276 ALA B N   1 
ATOM   5235 C CA  . ALA B 1 276 ? 18.192  -11.903 25.651  1.00 20.84 ?  276 ALA B CA  1 
ATOM   5236 C C   . ALA B 1 276 ? 18.831  -13.276 25.787  1.00 23.51 ?  276 ALA B C   1 
ATOM   5237 O O   . ALA B 1 276 ? 18.170  -14.239 26.194  1.00 21.44 ?  276 ALA B O   1 
ATOM   5238 C CB  . ALA B 1 276 ? 17.672  -11.716 24.227  1.00 20.95 ?  276 ALA B CB  1 
ATOM   5239 N N   . ILE B 1 277 ? 20.096  -13.408 25.392  1.00 22.92 ?  277 ILE B N   1 
ATOM   5240 C CA  . ILE B 1 277 ? 20.753  -14.709 25.517  1.00 24.09 ?  277 ILE B CA  1 
ATOM   5241 C C   . ILE B 1 277 ? 20.870  -15.097 26.984  1.00 22.46 ?  277 ILE B C   1 
ATOM   5242 O O   . ILE B 1 277 ? 20.553  -16.230 27.368  1.00 25.09 ?  277 ILE B O   1 
ATOM   5243 C CB  . ILE B 1 277 ? 22.118  -14.696 24.809  1.00 23.31 ?  277 ILE B CB  1 
ATOM   5244 C CG1 . ILE B 1 277 ? 21.901  -14.700 23.295  1.00 21.68 ?  277 ILE B CG1 1 
ATOM   5245 C CG2 . ILE B 1 277 ? 22.928  -15.931 25.179  1.00 23.12 ?  277 ILE B CG2 1 
ATOM   5246 C CD1 . ILE B 1 277 ? 23.170  -14.504 22.485  1.00 23.94 ?  277 ILE B CD1 1 
ATOM   5247 N N   . ALA B 1 278 ? 21.301  -14.156 27.832  1.00 22.51 ?  278 ALA B N   1 
ATOM   5248 C CA  . ALA B 1 278 ? 21.390  -14.438 29.264  1.00 23.95 ?  278 ALA B CA  1 
ATOM   5249 C C   . ALA B 1 278 ? 20.029  -14.786 29.851  1.00 24.65 ?  278 ALA B C   1 
ATOM   5250 O O   . ALA B 1 278 ? 19.907  -15.739 30.627  1.00 24.38 ?  278 ALA B O   1 
ATOM   5251 C CB  . ALA B 1 278 ? 21.990  -13.248 30.010  1.00 23.03 ?  278 ALA B CB  1 
ATOM   5252 N N   . ALA B 1 279 ? 18.992  -14.022 29.494  1.00 21.54 ?  279 ALA B N   1 
ATOM   5253 C CA  . ALA B 1 279 ? 17.658  -14.320 30.004  1.00 23.73 ?  279 ALA B CA  1 
ATOM   5254 C C   . ALA B 1 279 ? 17.242  -15.742 29.645  1.00 24.99 ?  279 ALA B C   1 
ATOM   5255 O O   . ALA B 1 279 ? 16.801  -16.507 30.510  1.00 24.56 ?  279 ALA B O   1 
ATOM   5256 C CB  . ALA B 1 279 ? 16.648  -13.298 29.467  1.00 23.14 ?  279 ALA B CB  1 
ATOM   5257 N N   . TYR B 1 280 ? 17.436  -16.136 28.386  1.00 21.21 ?  280 TYR B N   1 
ATOM   5258 C CA  . TYR B 1 280 ? 16.953  -17.424 27.915  1.00 23.88 ?  280 TYR B CA  1 
ATOM   5259 C C   . TYR B 1 280 ? 17.876  -18.582 28.273  1.00 25.58 ?  280 TYR B C   1 
ATOM   5260 O O   . TYR B 1 280 ? 17.452  -19.738 28.201  1.00 26.96 ?  280 TYR B O   1 
ATOM   5261 C CB  . TYR B 1 280 ? 16.765  -17.382 26.397  1.00 22.76 ?  280 TYR B CB  1 
ATOM   5262 C CG  . TYR B 1 280 ? 15.501  -16.689 25.906  1.00 22.96 ?  280 TYR B CG  1 
ATOM   5263 C CD1 . TYR B 1 280 ? 14.307  -16.777 26.610  1.00 20.81 ?  280 TYR B CD1 1 
ATOM   5264 C CD2 . TYR B 1 280 ? 15.500  -15.971 24.714  1.00 26.67 ?  280 TYR B CD2 1 
ATOM   5265 C CE1 . TYR B 1 280 ? 13.151  -16.159 26.144  1.00 23.63 ?  280 TYR B CE1 1 
ATOM   5266 C CE2 . TYR B 1 280 ? 14.354  -15.357 24.245  1.00 24.67 ?  280 TYR B CE2 1 
ATOM   5267 C CZ  . TYR B 1 280 ? 13.180  -15.455 24.963  1.00 25.06 ?  280 TYR B CZ  1 
ATOM   5268 O OH  . TYR B 1 280 ? 12.031  -14.849 24.481  1.00 21.69 ?  280 TYR B OH  1 
ATOM   5269 N N   . GLU B 1 281 ? 19.130  -18.309 28.617  1.00 25.59 ?  281 GLU B N   1 
ATOM   5270 C CA  . GLU B 1 281 ? 20.035  -19.377 29.017  1.00 27.24 ?  281 GLU B CA  1 
ATOM   5271 C C   . GLU B 1 281 ? 20.094  -19.557 30.520  1.00 28.54 ?  281 GLU B C   1 
ATOM   5272 O O   . GLU B 1 281 ? 20.270  -20.687 31.001  1.00 31.11 ?  281 GLU B O   1 
ATOM   5273 C CB  . GLU B 1 281 ? 21.443  -19.102 28.486  1.00 25.83 ?  281 GLU B CB  1 
ATOM   5274 C CG  . GLU B 1 281 ? 21.501  -19.139 26.985  1.00 27.62 ?  281 GLU B CG  1 
ATOM   5275 C CD  . GLU B 1 281 ? 22.871  -19.439 26.446  1.00 33.85 ?  281 GLU B CD  1 
ATOM   5276 O OE1 . GLU B 1 281 ? 23.862  -18.993 27.059  1.00 40.73 ?  281 GLU B OE1 1 
ATOM   5277 O OE2 . GLU B 1 281 ? 22.950  -20.113 25.397  1.00 45.53 -1 281 GLU B OE2 1 
ATOM   5278 N N   . GLU B 1 282 ? 19.944  -18.474 31.277  1.00 25.44 ?  282 GLU B N   1 
ATOM   5279 C CA  . GLU B 1 282 ? 20.175  -18.523 32.714  1.00 26.39 ?  282 GLU B CA  1 
ATOM   5280 C C   . GLU B 1 282 ? 18.997  -18.002 33.517  1.00 25.65 ?  282 GLU B C   1 
ATOM   5281 O O   . GLU B 1 282 ? 19.146  -17.788 34.718  1.00 25.84 ?  282 GLU B O   1 
ATOM   5282 C CB  . GLU B 1 282 ? 21.429  -17.733 33.103  1.00 29.25 ?  282 GLU B CB  1 
ATOM   5283 C CG  . GLU B 1 282 ? 22.595  -17.858 32.140  1.00 31.27 ?  282 GLU B CG  1 
ATOM   5284 C CD  . GLU B 1 282 ? 23.750  -16.973 32.551  1.00 38.80 ?  282 GLU B CD  1 
ATOM   5285 O OE1 . GLU B 1 282 ? 24.200  -17.078 33.718  1.00 41.40 ?  282 GLU B OE1 1 
ATOM   5286 O OE2 . GLU B 1 282 ? 24.193  -16.149 31.717  1.00 41.36 -1 282 GLU B OE2 1 
ATOM   5287 N N   . GLY B 1 283 ? 17.842  -17.766 32.886  1.00 23.74 ?  283 GLY B N   1 
ATOM   5288 C CA  . GLY B 1 283 ? 16.703  -17.196 33.578  1.00 25.91 ?  283 GLY B CA  1 
ATOM   5289 C C   . GLY B 1 283 ? 15.723  -18.191 34.170  1.00 26.95 ?  283 GLY B C   1 
ATOM   5290 O O   . GLY B 1 283 ? 14.740  -17.776 34.793  1.00 24.85 ?  283 GLY B O   1 
ATOM   5291 N N   . HIS B 1 284 ? 15.966  -19.497 34.019  1.00 29.12 ?  284 HIS B N   1 
ATOM   5292 C CA  . HIS B 1 284 ? 14.980  -20.492 34.436  1.00 27.87 ?  284 HIS B CA  1 
ATOM   5293 C C   . HIS B 1 284 ? 14.689  -20.404 35.930  1.00 26.35 ?  284 HIS B C   1 
ATOM   5294 O O   . HIS B 1 284 ? 13.524  -20.383 36.348  1.00 28.55 ?  284 HIS B O   1 
ATOM   5295 C CB  . HIS B 1 284 ? 15.461  -21.898 34.080  1.00 31.05 ?  284 HIS B CB  1 
ATOM   5296 C CG  . HIS B 1 284 ? 15.843  -22.069 32.644  1.00 31.78 ?  284 HIS B CG  1 
ATOM   5297 N ND1 . HIS B 1 284 ? 14.952  -22.505 31.685  1.00 31.05 ?  284 HIS B ND1 1 
ATOM   5298 C CD2 . HIS B 1 284 ? 17.024  -21.884 32.006  1.00 31.11 ?  284 HIS B CD2 1 
ATOM   5299 C CE1 . HIS B 1 284 ? 15.568  -22.580 30.518  1.00 30.28 ?  284 HIS B CE1 1 
ATOM   5300 N NE2 . HIS B 1 284 ? 16.824  -22.208 30.686  1.00 29.51 ?  284 HIS B NE2 1 
ATOM   5301 N N   . ASN B 1 285 ? 15.737  -20.387 36.754  1.00 27.39 ?  285 ASN B N   1 
ATOM   5302 C CA  . ASN B 1 285 ? 15.541  -20.364 38.202  1.00 30.97 ?  285 ASN B CA  1 
ATOM   5303 C C   . ASN B 1 285 ? 14.777  -19.121 38.639  1.00 29.93 ?  285 ASN B C   1 
ATOM   5304 O O   . ASN B 1 285 ? 13.853  -19.202 39.455  1.00 27.00 ?  285 ASN B O   1 
ATOM   5305 C CB  . ASN B 1 285 ? 16.888  -20.442 38.913  1.00 29.37 ?  285 ASN B CB  1 
ATOM   5306 C CG  . ASN B 1 285 ? 17.575  -21.765 38.696  1.00 40.54 ?  285 ASN B CG  1 
ATOM   5307 O OD1 . ASN B 1 285 ? 16.920  -22.811 38.618  1.00 38.45 ?  285 ASN B OD1 1 
ATOM   5308 N ND2 . ASN B 1 285 ? 18.902  -21.733 38.587  1.00 44.78 ?  285 ASN B ND2 1 
ATOM   5309 N N   . TRP B 1 286 ? 15.158  -17.953 38.111  1.00 22.68 ?  286 TRP B N   1 
ATOM   5310 C CA  . TRP B 1 286 ? 14.485  -16.718 38.491  1.00 24.39 ?  286 TRP B CA  1 
ATOM   5311 C C   . TRP B 1 286 ? 13.006  -16.757 38.126  1.00 28.95 ?  286 TRP B C   1 
ATOM   5312 O O   . TRP B 1 286 ? 12.148  -16.368 38.932  1.00 27.75 ?  286 TRP B O   1 
ATOM   5313 C CB  . TRP B 1 286 ? 15.179  -15.529 37.824  1.00 22.34 ?  286 TRP B CB  1 
ATOM   5314 C CG  . TRP B 1 286 ? 14.615  -14.200 38.201  1.00 21.82 ?  286 TRP B CG  1 
ATOM   5315 C CD1 . TRP B 1 286 ? 15.002  -13.406 39.241  1.00 24.65 ?  286 TRP B CD1 1 
ATOM   5316 C CD2 . TRP B 1 286 ? 13.568  -13.496 37.522  1.00 22.66 ?  286 TRP B CD2 1 
ATOM   5317 N NE1 . TRP B 1 286 ? 14.246  -12.255 39.262  1.00 23.30 ?  286 TRP B NE1 1 
ATOM   5318 C CE2 . TRP B 1 286 ? 13.358  -12.286 38.216  1.00 22.68 ?  286 TRP B CE2 1 
ATOM   5319 C CE3 . TRP B 1 286 ? 12.778  -13.779 36.401  1.00 24.36 ?  286 TRP B CE3 1 
ATOM   5320 C CZ2 . TRP B 1 286 ? 12.392  -11.349 37.824  1.00 25.94 ?  286 TRP B CZ2 1 
ATOM   5321 C CZ3 . TRP B 1 286 ? 11.817  -12.847 36.015  1.00 24.15 ?  286 TRP B CZ3 1 
ATOM   5322 C CH2 . TRP B 1 286 ? 11.636  -11.650 36.718  1.00 24.03 ?  286 TRP B CH2 1 
ATOM   5323 N N   . LEU B 1 287 ? 12.689  -17.234 36.917  1.00 26.77 ?  287 LEU B N   1 
ATOM   5324 C CA  . LEU B 1 287 ? 11.294  -17.351 36.498  1.00 24.65 ?  287 LEU B CA  1 
ATOM   5325 C C   . LEU B 1 287 ? 10.506  -18.270 37.428  1.00 25.89 ?  287 LEU B C   1 
ATOM   5326 O O   . LEU B 1 287 ? 9.347   -17.988 37.758  1.00 25.28 ?  287 LEU B O   1 
ATOM   5327 C CB  . LEU B 1 287 ? 11.222  -17.852 35.052  1.00 24.61 ?  287 LEU B CB  1 
ATOM   5328 C CG  . LEU B 1 287 ? 9.814   -18.139 34.523  1.00 25.17 ?  287 LEU B CG  1 
ATOM   5329 C CD1 . LEU B 1 287 ? 8.947   -16.889 34.635  1.00 25.20 ?  287 LEU B CD1 1 
ATOM   5330 C CD2 . LEU B 1 287 ? 9.839   -18.629 33.076  1.00 25.79 ?  287 LEU B CD2 1 
ATOM   5331 N N   . ARG B 1 288 ? 11.119  -19.367 37.882  1.00 29.85 ?  288 ARG B N   1 
ATOM   5332 C CA  . ARG B 1 288 ? 10.386  -20.280 38.752  1.00 29.84 ?  288 ARG B CA  1 
ATOM   5333 C C   . ARG B 1 288 ? 10.022  -19.611 40.071  1.00 25.64 ?  288 ARG B C   1 
ATOM   5334 O O   . ARG B 1 288 ? 8.904   -19.777 40.572  1.00 27.60 ?  288 ARG B O   1 
ATOM   5335 C CB  . ARG B 1 288 ? 11.193  -21.548 38.998  1.00 34.10 ?  288 ARG B CB  1 
ATOM   5336 C CG  . ARG B 1 288 ? 10.397  -22.593 39.760  1.00 37.15 ?  288 ARG B CG  1 
ATOM   5337 C CD  . ARG B 1 288 ? 11.269  -23.749 40.156  1.00 42.03 ?  288 ARG B CD  1 
ATOM   5338 N NE  . ARG B 1 288 ? 12.572  -23.257 40.563  1.00 48.06 ?  288 ARG B NE  1 
ATOM   5339 C CZ  . ARG B 1 288 ? 13.710  -23.581 39.962  1.00 52.48 ?  288 ARG B CZ  1 
ATOM   5340 N NH1 . ARG B 1 288 ? 13.697  -24.405 38.924  1.00 51.83 1  288 ARG B NH1 1 
ATOM   5341 N NH2 . ARG B 1 288 ? 14.857  -23.080 40.398  1.00 51.55 ?  288 ARG B NH2 1 
ATOM   5342 N N   . GLU B 1 289 ? 10.955  -18.835 40.642  1.00 26.97 ?  289 GLU B N   1 
ATOM   5343 C CA  . GLU B 1 289 ? 10.656  -18.062 41.844  1.00 25.90 ?  289 GLU B CA  1 
ATOM   5344 C C   . GLU B 1 289 ? 9.610   -16.987 41.565  1.00 29.47 ?  289 GLU B C   1 
ATOM   5345 O O   . GLU B 1 289 ? 8.709   -16.764 42.381  1.00 24.09 ?  289 GLU B O   1 
ATOM   5346 C CB  . GLU B 1 289 ? 11.930  -17.417 42.377  1.00 35.08 ?  289 GLU B CB  1 
ATOM   5347 C CG  . GLU B 1 289 ? 12.966  -18.410 42.837  1.00 34.35 ?  289 GLU B CG  1 
ATOM   5348 C CD  . GLU B 1 289 ? 13.785  -17.890 44.000  1.00 45.42 ?  289 GLU B CD  1 
ATOM   5349 O OE1 . GLU B 1 289 ? 14.708  -18.613 44.429  1.00 45.10 ?  289 GLU B OE1 1 
ATOM   5350 O OE2 . GLU B 1 289 ? 13.514  -16.759 44.473  1.00 47.17 -1 289 GLU B OE2 1 
ATOM   5351 N N   . LEU B 1 290 ? 9.732   -16.289 40.431  1.00 26.33 ?  290 LEU B N   1 
ATOM   5352 C CA  . LEU B 1 290 ? 8.735   -15.280 40.079  1.00 23.35 ?  290 LEU B CA  1 
ATOM   5353 C C   . LEU B 1 290 ? 7.332   -15.861 40.106  1.00 22.19 ?  290 LEU B C   1 
ATOM   5354 O O   . LEU B 1 290 ? 6.397   -15.231 40.618  1.00 24.01 ?  290 LEU B O   1 
ATOM   5355 C CB  . LEU B 1 290 ? 9.028   -14.695 38.689  1.00 21.06 ?  290 LEU B CB  1 
ATOM   5356 C CG  . LEU B 1 290 ? 7.946   -13.759 38.132  1.00 25.58 ?  290 LEU B CG  1 
ATOM   5357 C CD1 . LEU B 1 290 ? 7.789   -12.511 38.969  1.00 24.43 ?  290 LEU B CD1 1 
ATOM   5358 C CD2 . LEU B 1 290 ? 8.243   -13.421 36.668  1.00 19.96 ?  290 LEU B CD2 1 
ATOM   5359 N N   . LYS B 1 291 ? 7.156   -17.048 39.546  1.00 22.45 ?  291 LYS B N   1 
ATOM   5360 C CA  . LYS B 1 291 ? 5.801   -17.638 39.441  1.00 24.33 ?  291 LYS B CA  1 
ATOM   5361 C C   . LYS B 1 291 ? 5.282   -17.985 40.836  1.00 25.84 ?  291 LYS B C   1 
ATOM   5362 O O   . LYS B 1 291 ? 4.090   -17.890 41.039  1.00 24.27 ?  291 LYS B O   1 
ATOM   5363 C CB  . LYS B 1 291 ? 5.782   -18.805 38.456  1.00 24.76 ?  291 LYS B CB  1 
ATOM   5364 C CG  . LYS B 1 291 ? 6.115   -18.433 37.024  1.00 28.35 ?  291 LYS B CG  1 
ATOM   5365 C CD  . LYS B 1 291 ? 6.416   -19.632 36.181  1.00 26.39 ?  291 LYS B CD  1 
ATOM   5366 C CE  . LYS B 1 291 ? 5.600   -19.630 34.916  1.00 28.02 ?  291 LYS B CE  1 
ATOM   5367 N NZ  . LYS B 1 291 ? 5.840   -20.831 34.088  1.00 32.70 1  291 LYS B NZ  1 
ATOM   5368 N N   . GLN B 1 292 ? 6.163   -18.392 41.740  1.00 22.11 ?  292 GLN B N   1 
ATOM   5369 C CA  . GLN B 1 292 ? 5.726   -18.606 43.117  1.00 24.75 ?  292 GLN B CA  1 
ATOM   5370 C C   . GLN B 1 292 ? 5.260   -17.294 43.746  1.00 22.13 ?  292 GLN B C   1 
ATOM   5371 O O   . GLN B 1 292 ? 4.220   -17.254 44.412  1.00 26.14 ?  292 GLN B O   1 
ATOM   5372 C CB  . GLN B 1 292 ? 6.858   -19.246 43.937  1.00 25.67 ?  292 GLN B CB  1 
ATOM   5373 C CG  . GLN B 1 292 ? 7.377   -20.572 43.363  1.00 30.64 ?  292 GLN B CG  1 
ATOM   5374 C CD  . GLN B 1 292 ? 8.674   -21.037 44.012  1.00 34.26 ?  292 GLN B CD  1 
ATOM   5375 O OE1 . GLN B 1 292 ? 9.264   -20.328 44.819  1.00 34.27 ?  292 GLN B OE1 1 
ATOM   5376 N NE2 . GLN B 1 292 ? 9.120   -22.234 43.656  1.00 38.25 ?  292 GLN B NE2 1 
ATOM   5377 N N   . VAL B 1 293 ? 5.988   -16.201 43.508  1.00 24.05 ?  293 VAL B N   1 
ATOM   5378 C CA  . VAL B 1 293 ? 5.563   -14.891 44.017  1.00 22.67 ?  293 VAL B CA  1 
ATOM   5379 C C   . VAL B 1 293 ? 4.241   -14.469 43.387  1.00 24.82 ?  293 VAL B C   1 
ATOM   5380 O O   . VAL B 1 293 ? 3.356   -13.911 44.054  1.00 25.74 ?  293 VAL B O   1 
ATOM   5381 C CB  . VAL B 1 293 ? 6.663   -13.840 43.759  1.00 22.27 ?  293 VAL B CB  1 
ATOM   5382 C CG1 . VAL B 1 293 ? 6.190   -12.459 44.159  1.00 24.96 ?  293 VAL B CG1 1 
ATOM   5383 C CG2 . VAL B 1 293 ? 7.947   -14.194 44.503  1.00 25.03 ?  293 VAL B CG2 1 
ATOM   5384 N N   . LEU B 1 294 ? 4.088   -14.709 42.087  1.00 24.34 ?  294 LEU B N   1 
ATOM   5385 C CA  . LEU B 1 294 ? 2.874   -14.276 41.403  1.00 25.23 ?  294 LEU B CA  1 
ATOM   5386 C C   . LEU B 1 294 ? 1.665   -15.072 41.878  1.00 25.78 ?  294 LEU B C   1 
ATOM   5387 O O   . LEU B 1 294 ? 0.579   -14.512 42.078  1.00 24.04 ?  294 LEU B O   1 
ATOM   5388 C CB  . LEU B 1 294 ? 3.055   -14.424 39.893  1.00 23.57 ?  294 LEU B CB  1 
ATOM   5389 C CG  . LEU B 1 294 ? 4.043   -13.450 39.250  1.00 28.15 ?  294 LEU B CG  1 
ATOM   5390 C CD1 . LEU B 1 294 ? 4.154   -13.728 37.752  1.00 22.16 ?  294 LEU B CD1 1 
ATOM   5391 C CD2 . LEU B 1 294 ? 3.608   -12.009 39.494  1.00 21.28 ?  294 LEU B CD2 1 
ATOM   5392 N N   . ARG B 1 295 ? 1.862   -16.367 42.073  1.00 25.21 ?  295 ARG B N   1 
ATOM   5393 C CA  . ARG B 1 295 ? 0.751   -17.195 42.599  1.00 26.07 ?  295 ARG B CA  1 
ATOM   5394 C C   . ARG B 1 295 ? 0.372   -16.720 44.000  1.00 27.62 ?  295 ARG B C   1 
ATOM   5395 O O   . ARG B 1 295 ? -0.815  -16.672 44.291  1.00 28.39 ?  295 ARG B O   1 
ATOM   5396 C CB  . ARG B 1 295 ? 1.130   -18.670 42.542  1.00 26.14 ?  295 ARG B CB  1 
ATOM   5397 C CG  . ARG B 1 295 ? 0.990   -19.280 41.159  1.00 21.53 ?  295 ARG B CG  1 
ATOM   5398 C CD  . ARG B 1 295 ? 1.197   -20.773 41.269  1.00 26.18 ?  295 ARG B CD  1 
ATOM   5399 N NE  . ARG B 1 295 ? 2.541   -21.121 41.691  1.00 28.93 ?  295 ARG B NE  1 
ATOM   5400 C CZ  . ARG B 1 295 ? 3.539   -21.399 40.870  1.00 27.74 ?  295 ARG B CZ  1 
ATOM   5401 N NH1 . ARG B 1 295 ? 3.357   -21.370 39.563  1.00 26.68 1  295 ARG B NH1 1 
ATOM   5402 N NH2 . ARG B 1 295 ? 4.719   -21.714 41.361  1.00 26.70 ?  295 ARG B NH2 1 
ATOM   5403 N N   . ASP B 1 296 ? 1.360   -16.346 44.793  1.00 22.60 ?  296 ASP B N   1 
ATOM   5404 C CA  . ASP B 1 296 ? 1.076   -15.817 46.123  1.00 26.38 ?  296 ASP B CA  1 
ATOM   5405 C C   . ASP B 1 296 ? 0.307   -14.507 46.039  1.00 26.37 ?  296 ASP B C   1 
ATOM   5406 O O   . ASP B 1 296 ? -0.673  -14.308 46.766  1.00 26.40 ?  296 ASP B O   1 
ATOM   5407 C CB  . ASP B 1 296 ? 2.378   -15.636 46.904  1.00 25.41 ?  296 ASP B CB  1 
ATOM   5408 C CG  . ASP B 1 296 ? 2.138   -15.368 48.373  1.00 30.47 ?  296 ASP B CG  1 
ATOM   5409 O OD1 . ASP B 1 296 ? 2.006   -16.343 49.138  1.00 34.48 ?  296 ASP B OD1 1 
ATOM   5410 O OD2 . ASP B 1 296 ? 2.057   -14.185 48.761  1.00 32.70 -1 296 ASP B OD2 1 
ATOM   5411 N N   . ASN B 1 297 ? 0.714   -13.610 45.138  1.00 23.74 ?  297 ASN B N   1 
ATOM   5412 C CA  . ASN B 1 297 ? -0.011  -12.354 44.971  1.00 23.67 ?  297 ASN B CA  1 
ATOM   5413 C C   . ASN B 1 297 ? -1.452  -12.596 44.524  1.00 26.55 ?  297 ASN B C   1 
ATOM   5414 O O   . ASN B 1 297 ? -2.392  -11.988 45.052  1.00 24.85 ?  297 ASN B O   1 
ATOM   5415 C CB  . ASN B 1 297 ? 0.717   -11.463 43.960  1.00 23.57 ?  297 ASN B CB  1 
ATOM   5416 C CG  . ASN B 1 297 ? 2.004   -10.911 44.516  1.00 26.49 ?  297 ASN B CG  1 
ATOM   5417 O OD1 . ASN B 1 297 ? 2.280   -11.061 45.703  1.00 26.90 ?  297 ASN B OD1 1 
ATOM   5418 N ND2 . ASN B 1 297 ? 2.797   -10.265 43.672  1.00 24.68 ?  297 ASN B ND2 1 
ATOM   5419 N N   . PHE B 1 298 ? -1.641  -13.466 43.531  1.00 22.87 ?  298 PHE B N   1 
ATOM   5420 C CA  . PHE B 1 298 ? -2.989  -13.756 43.049  1.00 25.91 ?  298 PHE B CA  1 
ATOM   5421 C C   . PHE B 1 298 ? -3.830  -14.435 44.124  1.00 26.47 ?  298 PHE B C   1 
ATOM   5422 O O   . PHE B 1 298 ? -5.031  -14.173 44.236  1.00 23.99 ?  298 PHE B O   1 
ATOM   5423 C CB  . PHE B 1 298 ? -2.917  -14.633 41.796  1.00 26.30 ?  298 PHE B CB  1 
ATOM   5424 C CG  . PHE B 1 298 ? -2.925  -13.853 40.509  1.00 24.76 ?  298 PHE B CG  1 
ATOM   5425 C CD1 . PHE B 1 298 ? -1.745  -13.347 39.985  1.00 26.38 ?  298 PHE B CD1 1 
ATOM   5426 C CD2 . PHE B 1 298 ? -4.106  -13.636 39.819  1.00 22.81 ?  298 PHE B CD2 1 
ATOM   5427 C CE1 . PHE B 1 298 ? -1.748  -12.627 38.788  1.00 25.50 ?  298 PHE B CE1 1 
ATOM   5428 C CE2 . PHE B 1 298 ? -4.116  -12.917 38.634  1.00 25.57 ?  298 PHE B CE2 1 
ATOM   5429 C CZ  . PHE B 1 298 ? -2.937  -12.416 38.114  1.00 22.10 ?  298 PHE B CZ  1 
ATOM   5430 N N   . ALA B 1 299 ? -3.231  -15.341 44.898  1.00 25.17 ?  299 ALA B N   1 
ATOM   5431 C CA  . ALA B 1 299 ? -3.985  -15.968 45.984  1.00 28.47 ?  299 ALA B CA  1 
ATOM   5432 C C   . ALA B 1 299 ? -4.521  -14.914 46.946  1.00 26.15 ?  299 ALA B C   1 
ATOM   5433 O O   . ALA B 1 299 ? -5.720  -14.897 47.263  1.00 24.53 ?  299 ALA B O   1 
ATOM   5434 C CB  . ALA B 1 299 ? -3.115  -16.987 46.721  1.00 26.77 ?  299 ALA B CB  1 
ATOM   5435 N N   . TYR B 1 300 ? -3.646  -14.019 47.417  1.00 26.09 ?  300 TYR B N   1 
ATOM   5436 C CA  . TYR B 1 300 ? -4.088  -12.946 48.303  1.00 30.71 ?  300 TYR B CA  1 
ATOM   5437 C C   . TYR B 1 300 ? -5.152  -12.086 47.635  1.00 28.13 ?  300 TYR B C   1 
ATOM   5438 O O   . TYR B 1 300 ? -6.209  -11.822 48.219  1.00 25.80 ?  300 TYR B O   1 
ATOM   5439 C CB  . TYR B 1 300 ? -2.917  -12.051 48.725  1.00 25.90 ?  300 TYR B CB  1 
ATOM   5440 C CG  . TYR B 1 300 ? -3.410  -10.824 49.463  1.00 29.17 ?  300 TYR B CG  1 
ATOM   5441 C CD1 . TYR B 1 300 ? -3.623  -10.866 50.829  1.00 31.77 ?  300 TYR B CD1 1 
ATOM   5442 C CD2 . TYR B 1 300 ? -3.708  -9.640  48.789  1.00 25.84 ?  300 TYR B CD2 1 
ATOM   5443 C CE1 . TYR B 1 300 ? -4.092  -9.761  51.520  1.00 35.94 ?  300 TYR B CE1 1 
ATOM   5444 C CE2 . TYR B 1 300 ? -4.194  -8.533  49.469  1.00 28.58 ?  300 TYR B CE2 1 
ATOM   5445 C CZ  . TYR B 1 300 ? -4.380  -8.599  50.830  1.00 30.40 ?  300 TYR B CZ  1 
ATOM   5446 O OH  . TYR B 1 300 ? -4.847  -7.512  51.521  1.00 36.52 ?  300 TYR B OH  1 
ATOM   5447 N N   . ALA B 1 301 ? -4.917  -11.633 46.418  1.00 24.38 ?  301 ALA B N   1 
ATOM   5448 C CA  . ALA B 1 301 ? -5.856  -10.687 45.780  1.00 26.23 ?  301 ALA B CA  1 
ATOM   5449 C C   . ALA B 1 301 ? -7.221  -11.340 45.533  1.00 28.15 ?  301 ALA B C   1 
ATOM   5450 O O   . ALA B 1 301 ? -8.220  -10.732 45.815  1.00 25.09 ?  301 ALA B O   1 
ATOM   5451 C CB  . ALA B 1 301 ? -5.264  -10.184 44.507  1.00 23.09 ?  301 ALA B CB  1 
ATOM   5452 N N   . ARG B 1 302 ? -7.207  -12.551 44.987  1.00 28.90 ?  302 ARG B N   1 
ATOM   5453 C CA  . ARG B 1 302 ? -8.472  -13.252 44.684  1.00 30.62 ?  302 ARG B CA  1 
ATOM   5454 C C   . ARG B 1 302 ? -9.246  -13.477 45.979  1.00 31.52 ?  302 ARG B C   1 
ATOM   5455 O O   . ARG B 1 302 ? -10.435 -13.219 46.024  1.00 30.16 ?  302 ARG B O   1 
ATOM   5456 C CB  . ARG B 1 302 ? -8.193  -14.559 43.944  1.00 26.51 ?  302 ARG B CB  1 
ATOM   5457 C CG  . ARG B 1 302 ? -7.646  -14.354 42.537  1.00 29.16 ?  302 ARG B CG  1 
ATOM   5458 C CD  . ARG B 1 302 ? -7.709  -15.606 41.692  1.00 29.15 ?  302 ARG B CD  1 
ATOM   5459 N NE  . ARG B 1 302 ? -9.118  -15.935 41.597  1.00 39.26 ?  302 ARG B NE  1 
ATOM   5460 C CZ  . ARG B 1 302 ? -9.850  -15.753 40.514  1.00 36.80 ?  302 ARG B CZ  1 
ATOM   5461 N NH1 . ARG B 1 302 ? -9.282  -15.287 39.416  1.00 43.26 1  302 ARG B NH1 1 
ATOM   5462 N NH2 . ARG B 1 302 ? -11.133 -16.064 40.523  1.00 39.94 ?  302 ARG B NH2 1 
ATOM   5463 N N   . GLU B 1 303 ? -8.551  -13.959 46.996  1.00 29.27 ?  303 GLU B N   1 
ATOM   5464 C CA  . GLU B 1 303 ? -9.227  -14.198 48.285  1.00 28.35 ?  303 GLU B CA  1 
ATOM   5465 C C   . GLU B 1 303 ? -9.708  -12.848 48.802  1.00 31.21 ?  303 GLU B C   1 
ATOM   5466 O O   . GLU B 1 303 ? -10.864 -12.770 49.186  1.00 30.62 ?  303 GLU B O   1 
ATOM   5467 C CB  . GLU B 1 303 ? -8.298  -14.854 49.294  1.00 24.42 ?  303 GLU B CB  1 
ATOM   5468 C CG  . GLU B 1 303 ? -8.909  -15.013 50.664  1.00 25.24 ?  303 GLU B CG  1 
ATOM   5469 C CD  . GLU B 1 303 ? -8.043  -15.835 51.591  1.00 31.27 ?  303 GLU B CD  1 
ATOM   5470 O OE1 . GLU B 1 303 ? -7.601  -15.296 52.611  1.00 37.35 ?  303 GLU B OE1 1 
ATOM   5471 O OE2 . GLU B 1 303 ? -7.812  -17.006 51.276  1.00 28.34 -1 303 GLU B OE2 1 
ATOM   5472 N N   . PHE B 1 304 ? -8.832  -11.838 48.776  1.00 29.05 ?  304 PHE B N   1 
ATOM   5473 C CA  . PHE B 1 304 ? -9.293  -10.580 49.367  1.00 30.37 ?  304 PHE B CA  1 
ATOM   5474 C C   . PHE B 1 304 ? -10.464 -9.991  48.587  1.00 31.94 ?  304 PHE B C   1 
ATOM   5475 O O   . PHE B 1 304 ? -11.531 -9.724  49.156  1.00 28.85 ?  304 PHE B O   1 
ATOM   5476 C CB  . PHE B 1 304 ? -8.167  -9.544  49.449  1.00 28.49 ?  304 PHE B CB  1 
ATOM   5477 C CG  . PHE B 1 304 ? -8.662  -8.167  49.856  1.00 29.76 ?  304 PHE B CG  1 
ATOM   5478 C CD1 . PHE B 1 304 ? -9.114  -7.248  48.907  1.00 26.86 ?  304 PHE B CD1 1 
ATOM   5479 C CD2 . PHE B 1 304 ? -8.699  -7.807  51.186  1.00 33.21 ?  304 PHE B CD2 1 
ATOM   5480 C CE1 . PHE B 1 304 ? -9.589  -5.987  49.294  1.00 26.25 ?  304 PHE B CE1 1 
ATOM   5481 C CE2 . PHE B 1 304 ? -9.158  -6.554  51.576  1.00 33.21 ?  304 PHE B CE2 1 
ATOM   5482 C CZ  . PHE B 1 304 ? -9.603  -5.645  50.626  1.00 27.87 ?  304 PHE B CZ  1 
ATOM   5483 N N   . LEU B 1 305 ? -10.457 -10.017 47.268  1.00 31.04 ?  305 LEU B N   1 
ATOM   5484 C CA  . LEU B 1 305 ? -11.658 -9.485  46.579  1.00 32.04 ?  305 LEU B CA  1 
ATOM   5485 C C   . LEU B 1 305 ? -12.891 -10.386 46.776  1.00 34.49 ?  305 LEU B C   1 
ATOM   5486 O O   . LEU B 1 305 ? -13.971 -9.850  46.848  1.00 31.22 ?  305 LEU B O   1 
ATOM   5487 C CB  . LEU B 1 305 ? -11.334 -9.185  45.113  1.00 28.73 ?  305 LEU B CB  1 
ATOM   5488 C CG  . LEU B 1 305 ? -10.255 -8.137  44.870  1.00 32.05 ?  305 LEU B CG  1 
ATOM   5489 C CD1 . LEU B 1 305 ? -9.995  -7.968  43.383  1.00 26.47 ?  305 LEU B CD1 1 
ATOM   5490 C CD2 . LEU B 1 305 ? -10.638 -6.809  45.490  1.00 26.10 ?  305 LEU B CD2 1 
ATOM   5491 N N   . ALA B 1 306 ? -12.731 -11.703 46.914  1.00 37.86 ?  306 ALA B N   1 
ATOM   5492 C CA  . ALA B 1 306 ? -13.916 -12.586 47.015  1.00 32.57 ?  306 ALA B CA  1 
ATOM   5493 C C   . ALA B 1 306 ? -14.598 -12.409 48.369  1.00 42.30 ?  306 ALA B C   1 
ATOM   5494 O O   . ALA B 1 306 ? -15.826 -12.430 48.419  1.00 52.78 ?  306 ALA B O   1 
ATOM   5495 C CB  . ALA B 1 306 ? -13.509 -14.016 46.819  1.00 40.55 ?  306 ALA B CB  1 
ATOM   5496 N N   . LYS B 1 307 ? -13.803 -12.222 49.404  1.00 41.35 ?  307 LYS B N   1 
ATOM   5497 C CA  . LYS B 1 307 ? -14.328 -12.098 50.779  1.00 39.34 ?  307 LYS B CA  1 
ATOM   5498 C C   . LYS B 1 307 ? -14.737 -10.656 51.084  1.00 39.02 ?  307 LYS B C   1 
ATOM   5499 O O   . LYS B 1 307 ? -15.735 -10.493 51.772  1.00 38.25 ?  307 LYS B O   1 
ATOM   5500 C CB  . LYS B 1 307 ? -13.229 -12.529 51.755  1.00 34.74 ?  307 LYS B CB  1 
ATOM   5501 C CG  . LYS B 1 307 ? -13.700 -12.959 53.135  1.00 39.72 ?  307 LYS B CG  1 
ATOM   5502 C CD  . LYS B 1 307 ? -12.592 -12.979 54.165  1.00 41.65 ?  307 LYS B CD  1 
ATOM   5503 C CE  . LYS B 1 307 ? -11.267 -13.436 53.596  1.00 44.04 ?  307 LYS B CE  1 
ATOM   5504 N NZ  . LYS B 1 307 ? -10.542 -14.346 54.516  1.00 43.15 1  307 LYS B NZ  1 
ATOM   5505 N N   . GLU B 1 308 ? -14.060 -9.668  50.510  1.00 32.80 ?  308 GLU B N   1 
ATOM   5506 C CA  . GLU B 1 308 ? -14.283 -8.263  50.933  1.00 34.12 ?  308 GLU B CA  1 
ATOM   5507 C C   . GLU B 1 308 ? -14.948 -7.371  49.879  1.00 33.64 ?  308 GLU B C   1 
ATOM   5508 O O   . GLU B 1 308 ? -15.475 -6.349  50.273  1.00 33.73 ?  308 GLU B O   1 
ATOM   5509 C CB  . GLU B 1 308 ? -12.958 -7.650  51.376  1.00 32.32 ?  308 GLU B CB  1 
ATOM   5510 C CG  . GLU B 1 308 ? -12.257 -8.439  52.457  1.00 29.87 ?  308 GLU B CG  1 
ATOM   5511 C CD  . GLU B 1 308 ? -12.947 -8.402  53.806  1.00 34.22 ?  308 GLU B CD  1 
ATOM   5512 O OE1 . GLU B 1 308 ? -12.680 -9.293  54.618  1.00 38.49 ?  308 GLU B OE1 1 
ATOM   5513 O OE2 . GLU B 1 308 ? -13.744 -7.490  54.037  1.00 30.19 -1 308 GLU B OE2 1 
ATOM   5514 N N   . VAL B 1 309 ? -14.841 -7.714  48.597  1.00 32.24 ?  309 VAL B N   1 
ATOM   5515 C CA  . VAL B 1 309 ? -15.481 -6.876  47.592  1.00 28.49 ?  309 VAL B CA  1 
ATOM   5516 C C   . VAL B 1 309 ? -16.382 -7.775  46.757  1.00 31.13 ?  309 VAL B C   1 
ATOM   5517 O O   . VAL B 1 309 ? -16.060 -8.071  45.596  1.00 29.04 ?  309 VAL B O   1 
ATOM   5518 C CB  . VAL B 1 309 ? -14.433 -6.165  46.728  1.00 30.52 ?  309 VAL B CB  1 
ATOM   5519 C CG1 . VAL B 1 309 ? -15.091 -5.116  45.865  1.00 28.33 ?  309 VAL B CG1 1 
ATOM   5520 C CG2 . VAL B 1 309 ? -13.348 -5.548  47.616  1.00 26.88 ?  309 VAL B CG2 1 
ATOM   5521 N N   . PRO B 1 310 ? -17.510 -8.241  47.299  1.00 31.12 ?  310 PRO B N   1 
ATOM   5522 C CA  . PRO B 1 310 ? -18.392 -9.112  46.507  1.00 34.64 ?  310 PRO B CA  1 
ATOM   5523 C C   . PRO B 1 310 ? -19.022 -8.408  45.317  1.00 33.59 ?  310 PRO B C   1 
ATOM   5524 O O   . PRO B 1 310 ? -19.608 -9.083  44.461  1.00 34.09 ?  310 PRO B O   1 
ATOM   5525 C CB  . PRO B 1 310 ? -19.451 -9.558  47.526  1.00 35.99 ?  310 PRO B CB  1 
ATOM   5526 C CG  . PRO B 1 310 ? -19.459 -8.464  48.565  1.00 32.04 ?  310 PRO B CG  1 
ATOM   5527 C CD  . PRO B 1 310 ? -18.018 -8.030  48.668  1.00 31.76 ?  310 PRO B CD  1 
ATOM   5528 N N   . GLU B 1 311 ? -18.908 -7.081  45.231  1.00 33.59 ?  311 GLU B N   1 
ATOM   5529 C CA  . GLU B 1 311 ? -19.427 -6.323  44.101  1.00 32.96 ?  311 GLU B CA  1 
ATOM   5530 C C   . GLU B 1 311 ? -18.619 -6.529  42.829  1.00 31.90 ?  311 GLU B C   1 
ATOM   5531 O O   . GLU B 1 311 ? -19.073 -6.116  41.758  1.00 31.75 ?  311 GLU B O   1 
ATOM   5532 C CB  . GLU B 1 311 ? -19.457 -4.828  44.430  1.00 33.30 ?  311 GLU B CB  1 
ATOM   5533 C CG  . GLU B 1 311 ? -20.353 -4.462  45.595  1.00 38.56 ?  311 GLU B CG  1 
ATOM   5534 C CD  . GLU B 1 311 ? -19.649 -4.575  46.935  1.00 37.07 ?  311 GLU B CD  1 
ATOM   5535 O OE1 . GLU B 1 311 ? -20.297 -4.284  47.960  1.00 42.68 ?  311 GLU B OE1 1 
ATOM   5536 O OE2 . GLU B 1 311 ? -18.455 -4.952  46.968  1.00 36.84 -1 311 GLU B OE2 1 
ATOM   5537 N N   . VAL B 1 312 ? -17.424 -7.110  42.913  1.00 28.75 ?  312 VAL B N   1 
ATOM   5538 C CA  . VAL B 1 312 ? -16.640 -7.388  41.719  1.00 27.41 ?  312 VAL B CA  1 
ATOM   5539 C C   . VAL B 1 312 ? -16.427 -8.887  41.638  1.00 28.79 ?  312 VAL B C   1 
ATOM   5540 O O   . VAL B 1 312 ? -16.564 -9.609  42.624  1.00 27.84 ?  312 VAL B O   1 
ATOM   5541 C CB  . VAL B 1 312 ? -15.294 -6.642  41.701  1.00 27.02 ?  312 VAL B CB  1 
ATOM   5542 C CG1 . VAL B 1 312 ? -15.519 -5.159  41.945  1.00 26.57 ?  312 VAL B CG1 1 
ATOM   5543 C CG2 . VAL B 1 312 ? -14.342 -7.233  42.767  1.00 25.97 ?  312 VAL B CG2 1 
ATOM   5544 N N   . LYS B 1 313 ? -16.120 -9.354  40.428  1.00 30.54 ?  313 LYS B N   1 
ATOM   5545 C CA  . LYS B 1 313 ? -15.839 -10.765 40.185  1.00 29.85 ?  313 LYS B CA  1 
ATOM   5546 C C   . LYS B 1 313 ? -14.557 -10.869 39.373  1.00 29.45 ?  313 LYS B C   1 
ATOM   5547 O O   . LYS B 1 313 ? -14.535 -10.509 38.189  1.00 28.71 ?  313 LYS B O   1 
ATOM   5548 C CB  . LYS B 1 313 ? -17.005 -11.453 39.468  1.00 30.89 ?  313 LYS B CB  1 
ATOM   5549 C CG  . LYS B 1 313 ? -16.715 -12.919 39.092  1.00 36.68 ?  313 LYS B CG  1 
ATOM   5550 C CD  . LYS B 1 313 ? -16.376 -13.770 40.334  1.00 42.08 ?  313 LYS B CD  1 
ATOM   5551 C CE  . LYS B 1 313 ? -15.829 -15.159 39.957  1.00 45.84 ?  313 LYS B CE  1 
ATOM   5552 N NZ  . LYS B 1 313 ? -14.752 -15.637 40.881  1.00 48.40 1  313 LYS B NZ  1 
ATOM   5553 N N   . VAL B 1 314 ? -13.486 -11.335 40.011  1.00 31.39 ?  314 VAL B N   1 
ATOM   5554 C CA  . VAL B 1 314 ? -12.251 -11.596 39.285  1.00 28.66 ?  314 VAL B CA  1 
ATOM   5555 C C   . VAL B 1 314 ? -12.457 -12.861 38.464  1.00 30.69 ?  314 VAL B C   1 
ATOM   5556 O O   . VAL B 1 314 ? -12.859 -13.907 38.985  1.00 31.76 ?  314 VAL B O   1 
ATOM   5557 C CB  . VAL B 1 314 ? -11.060 -11.728 40.248  1.00 30.44 ?  314 VAL B CB  1 
ATOM   5558 C CG1 . VAL B 1 314 ? -9.724  -11.687 39.483  1.00 27.82 ?  314 VAL B CG1 1 
ATOM   5559 C CG2 . VAL B 1 314 ? -11.101 -10.639 41.326  1.00 28.61 ?  314 VAL B CG2 1 
ATOM   5560 N N   . LEU B 1 315 ? -12.209 -12.754 37.185  1.00 29.85 ?  315 LEU B N   1 
ATOM   5561 C CA  . LEU B 1 315 ? -12.446 -13.919 36.331  1.00 28.52 ?  315 LEU B CA  1 
ATOM   5562 C C   . LEU B 1 315 ? -11.342 -14.941 36.530  1.00 33.38 ?  315 LEU B C   1 
ATOM   5563 O O   . LEU B 1 315 ? -10.213 -14.552 36.805  1.00 28.85 ?  315 LEU B O   1 
ATOM   5564 C CB  . LEU B 1 315 ? -12.520 -13.499 34.877  1.00 29.85 ?  315 LEU B CB  1 
ATOM   5565 C CG  . LEU B 1 315 ? -13.935 -13.451 34.317  1.00 35.99 ?  315 LEU B CG  1 
ATOM   5566 C CD1 . LEU B 1 315 ? -14.882 -12.718 35.252  1.00 31.19 ?  315 LEU B CD1 1 
ATOM   5567 C CD2 . LEU B 1 315 ? -13.933 -12.820 32.949  1.00 34.22 ?  315 LEU B CD2 1 
ATOM   5568 N N   . ASP B 1 316 ? -11.710 -16.203 36.401  1.00 30.98 ?  316 ASP B N   1 
ATOM   5569 C CA  . ASP B 1 316 ? -10.737 -17.282 36.472  1.00 32.53 ?  316 ASP B CA  1 
ATOM   5570 C C   . ASP B 1 316 ? -9.777  -17.162 35.300  1.00 31.62 ?  316 ASP B C   1 
ATOM   5571 O O   . ASP B 1 316 ? -10.195 -16.954 34.161  1.00 31.03 ?  316 ASP B O   1 
ATOM   5572 C CB  . ASP B 1 316 ? -11.452 -18.635 36.448  1.00 36.23 ?  316 ASP B CB  1 
ATOM   5573 C CG  . ASP B 1 316 ? -10.495 -19.806 36.567  1.00 38.14 ?  316 ASP B CG  1 
ATOM   5574 O OD1 . ASP B 1 316 ? -9.618  -19.786 37.457  1.00 45.75 ?  316 ASP B OD1 1 
ATOM   5575 O OD2 . ASP B 1 316 ? -10.627 -20.759 35.781  1.00 41.55 -1 316 ASP B OD2 1 
ATOM   5576 N N   . SER B 1 317 ? -8.486  -17.253 35.590  1.00 33.35 ?  317 SER B N   1 
ATOM   5577 C CA  . SER B 1 317 ? -7.465  -17.136 34.563  1.00 31.70 ?  317 SER B CA  1 
ATOM   5578 C C   . SER B 1 317 ? -6.320  -18.049 34.956  1.00 28.60 ?  317 SER B C   1 
ATOM   5579 O O   . SER B 1 317 ? -6.186  -18.421 36.119  1.00 31.47 ?  317 SER B O   1 
ATOM   5580 C CB  . SER B 1 317 ? -6.985  -15.689 34.415  1.00 28.74 ?  317 SER B CB  1 
ATOM   5581 O OG  . SER B 1 317 ? -6.386  -15.244 35.614  1.00 33.71 ?  317 SER B OG  1 
ATOM   5582 N N   . ASN B 1 318 ? -5.502  -18.429 33.978  1.00 28.19 ?  318 ASN B N   1 
ATOM   5583 C CA  . ASN B 1 318 ? -4.351  -19.264 34.276  1.00 31.09 ?  318 ASN B CA  1 
ATOM   5584 C C   . ASN B 1 318 ? -3.031  -18.688 33.793  1.00 31.52 ?  318 ASN B C   1 
ATOM   5585 O O   . ASN B 1 318 ? -1.996  -19.344 33.971  1.00 29.21 ?  318 ASN B O   1 
ATOM   5586 C CB  . ASN B 1 318 ? -4.532  -20.683 33.706  1.00 29.53 ?  318 ASN B CB  1 
ATOM   5587 C CG  . ASN B 1 318 ? -4.757  -20.706 32.202  1.00 29.37 ?  318 ASN B CG  1 
ATOM   5588 O OD1 . ASN B 1 318 ? -4.668  -19.690 31.520  1.00 28.01 ?  318 ASN B OD1 1 
ATOM   5589 N ND2 . ASN B 1 318 ? -5.042  -21.888 31.677  1.00 32.43 ?  318 ASN B ND2 1 
ATOM   5590 N N   . ALA B 1 319 ? -3.086  -17.518 33.169  1.00 29.41 ?  319 ALA B N   1 
ATOM   5591 C CA  . ALA B 1 319 ? -1.870  -16.989 32.529  1.00 25.21 ?  319 ALA B CA  1 
ATOM   5592 C C   . ALA B 1 319 ? -1.791  -15.474 32.633  1.00 22.43 ?  319 ALA B C   1 
ATOM   5593 O O   . ALA B 1 319 ? -2.824  -14.878 32.827  1.00 24.72 ?  319 ALA B O   1 
ATOM   5594 C CB  . ALA B 1 319 ? -1.844  -17.438 31.104  1.00 23.79 ?  319 ALA B CB  1 
ATOM   5595 N N   . SER B 1 320 ? -0.583  -14.930 32.523  1.00 22.88 ?  320 SER B N   1 
ATOM   5596 C CA  . SER B 1 320 ? -0.337  -13.476 32.673  1.00 24.73 ?  320 SER B CA  1 
ATOM   5597 C C   . SER B 1 320 ? -0.285  -13.085 34.151  1.00 22.09 ?  320 SER B C   1 
ATOM   5598 O O   . SER B 1 320 ? -0.798  -13.836 34.976  1.00 21.38 ?  320 SER B O   1 
ATOM   5599 C CB  . SER B 1 320 ? -1.319  -12.590 31.928  1.00 21.45 ?  320 SER B CB  1 
ATOM   5600 O OG  . SER B 1 320 ? -2.414  -12.219 32.738  1.00 23.11 ?  320 SER B OG  1 
ATOM   5601 N N   . TYR B 1 321 ? 0.279   -11.919 34.420  1.00 18.83 ?  321 TYR B N   1 
ATOM   5602 C CA  . TYR B 1 321 ? 0.274   -11.376 35.796  1.00 20.95 ?  321 TYR B CA  1 
ATOM   5603 C C   . TYR B 1 321 ? -0.828  -10.314 35.887  1.00 22.21 ?  321 TYR B C   1 
ATOM   5604 O O   . TYR B 1 321 ? -0.809  -9.530  36.819  1.00 20.62 ?  321 TYR B O   1 
ATOM   5605 C CB  . TYR B 1 321 ? 1.666   -10.886 36.173  1.00 20.59 ?  321 TYR B CB  1 
ATOM   5606 C CG  . TYR B 1 321 ? 2.369   -9.946  35.235  1.00 17.60 ?  321 TYR B CG  1 
ATOM   5607 C CD1 . TYR B 1 321 ? 1.879   -8.678  34.983  1.00 22.88 ?  321 TYR B CD1 1 
ATOM   5608 C CD2 . TYR B 1 321 ? 3.584   -10.291 34.677  1.00 19.04 ?  321 TYR B CD2 1 
ATOM   5609 C CE1 . TYR B 1 321 ? 2.550   -7.795  34.160  1.00 20.92 ?  321 TYR B CE1 1 
ATOM   5610 C CE2 . TYR B 1 321 ? 4.267   -9.424  33.846  1.00 20.82 ?  321 TYR B CE2 1 
ATOM   5611 C CZ  . TYR B 1 321 ? 3.750   -8.168  33.594  1.00 21.12 ?  321 TYR B CZ  1 
ATOM   5612 O OH  . TYR B 1 321 ? 4.408   -7.302  32.787  1.00 22.30 ?  321 TYR B OH  1 
ATOM   5613 N N   . LEU B 1 322 ? -1.754  -10.342 34.927  1.00 21.63 ?  322 LEU B N   1 
ATOM   5614 C CA  . LEU B 1 322 ? -2.840  -9.375  34.890  1.00 22.61 ?  322 LEU B CA  1 
ATOM   5615 C C   . LEU B 1 322 ? -4.136  -10.063 35.278  1.00 23.82 ?  322 LEU B C   1 
ATOM   5616 O O   . LEU B 1 322 ? -4.398  -11.196 34.862  1.00 24.08 ?  322 LEU B O   1 
ATOM   5617 C CB  . LEU B 1 322 ? -2.978  -8.759  33.491  1.00 22.87 ?  322 LEU B CB  1 
ATOM   5618 C CG  . LEU B 1 322 ? -1.612  -8.330  32.942  1.00 23.11 ?  322 LEU B CG  1 
ATOM   5619 C CD1 . LEU B 1 322 ? -1.662  -8.232  31.435  1.00 23.29 ?  322 LEU B CD1 1 
ATOM   5620 C CD2 . LEU B 1 322 ? -1.181  -7.011  33.556  1.00 20.30 ?  322 LEU B CD2 1 
ATOM   5621 N N   . ALA B 1 323 ? -4.931  -9.379  36.089  1.00 22.41 ?  323 ALA B N   1 
ATOM   5622 C CA  . ALA B 1 323 ? -6.222  -9.871  36.542  1.00 23.14 ?  323 ALA B CA  1 
ATOM   5623 C C   . ALA B 1 323 ? -7.312  -9.102  35.814  1.00 23.12 ?  323 ALA B C   1 
ATOM   5624 O O   . ALA B 1 323 ? -7.229  -7.881  35.669  1.00 21.97 ?  323 ALA B O   1 
ATOM   5625 C CB  . ALA B 1 323 ? -6.378  -9.709  38.057  1.00 23.18 ?  323 ALA B CB  1 
ATOM   5626 N N   . TRP B 1 324 ? -8.328  -9.825  35.362  1.00 22.59 ?  324 TRP B N   1 
ATOM   5627 C CA  . TRP B 1 324 ? -9.440  -9.268  34.603  1.00 24.35 ?  324 TRP B CA  1 
ATOM   5628 C C   . TRP B 1 324 ? -10.661 -9.349  35.502  1.00 22.78 ?  324 TRP B C   1 
ATOM   5629 O O   . TRP B 1 324 ? -11.079 -10.452 35.886  1.00 23.45 ?  324 TRP B O   1 
ATOM   5630 C CB  . TRP B 1 324 ? -9.620  -10.056 33.304  1.00 24.79 ?  324 TRP B CB  1 
ATOM   5631 C CG  . TRP B 1 324 ? -10.599 -9.548  32.262  1.00 25.49 ?  324 TRP B CG  1 
ATOM   5632 C CD1 . TRP B 1 324 ? -11.650 -10.243 31.735  1.00 20.52 ?  324 TRP B CD1 1 
ATOM   5633 C CD2 . TRP B 1 324 ? -10.573 -8.279  31.576  1.00 21.83 ?  324 TRP B CD2 1 
ATOM   5634 N NE1 . TRP B 1 324 ? -12.292 -9.482  30.788  1.00 20.98 ?  324 TRP B NE1 1 
ATOM   5635 C CE2 . TRP B 1 324 ? -11.655 -8.275  30.670  1.00 20.97 ?  324 TRP B CE2 1 
ATOM   5636 C CE3 . TRP B 1 324 ? -9.758  -7.142  31.664  1.00 23.36 ?  324 TRP B CE3 1 
ATOM   5637 C CZ2 . TRP B 1 324 ? -11.931 -7.192  29.840  1.00 22.71 ?  324 TRP B CZ2 1 
ATOM   5638 C CZ3 . TRP B 1 324 ? -10.041 -6.052  30.847  1.00 25.00 ?  324 TRP B CZ3 1 
ATOM   5639 C CH2 . TRP B 1 324 ? -11.116 -6.088  29.937  1.00 21.99 ?  324 TRP B CH2 1 
ATOM   5640 N N   . VAL B 1 325 ? -11.216 -8.187  35.853  1.00 26.81 ?  325 VAL B N   1 
ATOM   5641 C CA  . VAL B 1 325 ? -12.191 -8.063  36.930  1.00 25.17 ?  325 VAL B CA  1 
ATOM   5642 C C   . VAL B 1 325 ? -13.485 -7.471  36.391  1.00 24.16 ?  325 VAL B C   1 
ATOM   5643 O O   . VAL B 1 325 ? -13.492 -6.355  35.868  1.00 24.98 ?  325 VAL B O   1 
ATOM   5644 C CB  . VAL B 1 325 ? -11.650 -7.198  38.076  1.00 24.69 ?  325 VAL B CB  1 
ATOM   5645 C CG1 . VAL B 1 325 ? -12.617 -7.223  39.243  1.00 26.25 ?  325 VAL B CG1 1 
ATOM   5646 C CG2 . VAL B 1 325 ? -10.262 -7.671  38.478  1.00 24.29 ?  325 VAL B CG2 1 
ATOM   5647 N N   . ASP B 1 326 ? -14.578 -8.206  36.552  1.00 25.82 ?  326 ASP B N   1 
ATOM   5648 C CA  . ASP B 1 326 ? -15.909 -7.751  36.169  1.00 24.65 ?  326 ASP B CA  1 
ATOM   5649 C C   . ASP B 1 326 ? -16.420 -6.776  37.228  1.00 26.62 ?  326 ASP B C   1 
ATOM   5650 O O   . ASP B 1 326 ? -16.659 -7.173  38.372  1.00 26.78 ?  326 ASP B O   1 
ATOM   5651 C CB  . ASP B 1 326 ? -16.824 -8.967  36.030  1.00 26.98 ?  326 ASP B CB  1 
ATOM   5652 C CG  . ASP B 1 326 ? -18.227 -8.623  35.533  1.00 28.38 ?  326 ASP B CG  1 
ATOM   5653 O OD1 . ASP B 1 326 ? -18.691 -7.473  35.699  1.00 26.97 ?  326 ASP B OD1 1 
ATOM   5654 O OD2 . ASP B 1 326 ? -18.871 -9.533  34.968  1.00 30.40 -1 326 ASP B OD2 1 
ATOM   5655 N N   . ILE B 1 327 ? -16.609 -5.510  36.850  1.00 26.70 ?  327 ILE B N   1 
ATOM   5656 C CA  . ILE B 1 327 ? -17.131 -4.482  37.755  1.00 27.28 ?  327 ILE B CA  1 
ATOM   5657 C C   . ILE B 1 327 ? -18.562 -4.084  37.389  1.00 28.93 ?  327 ILE B C   1 
ATOM   5658 O O   . ILE B 1 327 ? -19.041 -3.032  37.829  1.00 30.89 ?  327 ILE B O   1 
ATOM   5659 C CB  . ILE B 1 327 ? -16.225 -3.234  37.795  1.00 22.58 ?  327 ILE B CB  1 
ATOM   5660 C CG1 . ILE B 1 327 ? -16.136 -2.599  36.400  1.00 27.44 ?  327 ILE B CG1 1 
ATOM   5661 C CG2 . ILE B 1 327 ? -14.829 -3.548  38.413  1.00 22.44 ?  327 ILE B CG2 1 
ATOM   5662 C CD1 . ILE B 1 327 ? -15.796 -1.115  36.420  1.00 27.03 ?  327 ILE B CD1 1 
ATOM   5663 N N   . SER B 1 328 ? -19.259 -4.901  36.599  1.00 31.90 ?  328 SER B N   1 
ATOM   5664 C CA  . SER B 1 328 ? -20.574 -4.501  36.098  1.00 32.15 ?  328 SER B CA  1 
ATOM   5665 C C   . SER B 1 328 ? -21.566 -4.216  37.223  1.00 35.05 ?  328 SER B C   1 
ATOM   5666 O O   . SER B 1 328 ? -22.445 -3.359  37.071  1.00 33.20 ?  328 SER B O   1 
ATOM   5667 C CB  . SER B 1 328 ? -21.137 -5.589  35.192  1.00 28.52 ?  328 SER B CB  1 
ATOM   5668 O OG  . SER B 1 328 ? -21.297 -6.791  35.910  1.00 31.88 ?  328 SER B OG  1 
ATOM   5669 N N   . ALA B 1 329 ? -21.449 -4.920  38.351  1.00 29.75 ?  329 ALA B N   1 
ATOM   5670 C CA  . ALA B 1 329 ? -22.408 -4.742  39.435  1.00 30.70 ?  329 ALA B CA  1 
ATOM   5671 C C   . ALA B 1 329 ? -22.359 -3.343  40.022  1.00 32.45 ?  329 ALA B C   1 
ATOM   5672 O O   . ALA B 1 329 ? -23.349 -2.894  40.609  1.00 36.34 ?  329 ALA B O   1 
ATOM   5673 C CB  . ALA B 1 329 ? -22.171 -5.784  40.532  1.00 36.39 ?  329 ALA B CB  1 
ATOM   5674 N N   . LEU B 1 330 ? -21.242 -2.633  39.861  1.00 32.40 ?  330 LEU B N   1 
ATOM   5675 C CA  . LEU B 1 330 ? -21.177 -1.243  40.288  1.00 30.71 ?  330 LEU B CA  1 
ATOM   5676 C C   . LEU B 1 330 ? -22.005 -0.317  39.407  1.00 37.67 ?  330 LEU B C   1 
ATOM   5677 O O   . LEU B 1 330 ? -22.167 0.859   39.756  1.00 40.37 ?  330 LEU B O   1 
ATOM   5678 C CB  . LEU B 1 330 ? -19.724 -0.779  40.305  1.00 33.33 ?  330 LEU B CB  1 
ATOM   5679 C CG  . LEU B 1 330 ? -18.820 -1.488  41.314  1.00 32.82 ?  330 LEU B CG  1 
ATOM   5680 C CD1 . LEU B 1 330 ? -17.382 -1.064  41.071  1.00 32.91 ?  330 LEU B CD1 1 
ATOM   5681 C CD2 . LEU B 1 330 ? -19.245 -1.168  42.735  1.00 34.72 ?  330 LEU B CD2 1 
ATOM   5682 N N   . GLY B 1 331 ? -22.517 -0.808  38.283  1.00 35.55 ?  331 GLY B N   1 
ATOM   5683 C CA  . GLY B 1 331 ? -23.343 0.012   37.409  1.00 37.60 ?  331 GLY B CA  1 
ATOM   5684 C C   . GLY B 1 331 ? -22.660 1.263   36.904  1.00 38.43 ?  331 GLY B C   1 
ATOM   5685 O O   . GLY B 1 331 ? -23.298 2.317   36.799  1.00 43.11 ?  331 GLY B O   1 
ATOM   5686 N N   . MET B 1 332 ? -21.377 1.174   36.573  1.00 34.29 ?  332 MET B N   1 
ATOM   5687 C CA  . MET B 1 332 ? -20.590 2.350   36.233  1.00 32.53 ?  332 MET B CA  1 
ATOM   5688 C C   . MET B 1 332 ? -19.606 1.986   35.131  1.00 33.34 ?  332 MET B C   1 
ATOM   5689 O O   . MET B 1 332 ? -18.887 0.992   35.247  1.00 32.27 ?  332 MET B O   1 
ATOM   5690 C CB  . MET B 1 332 ? -19.852 2.876   37.471  1.00 38.34 ?  332 MET B CB  1 
ATOM   5691 C CG  . MET B 1 332 ? -19.039 4.142   37.256  1.00 35.01 ?  332 MET B CG  1 
ATOM   5692 S SD  . MET B 1 332 ? -18.381 4.821   38.809  1.00 39.88 ?  332 MET B SD  1 
ATOM   5693 C CE  . MET B 1 332 ? -17.693 6.342   38.210  1.00 37.94 ?  332 MET B CE  1 
ATOM   5694 N N   . ASN B 1 333 ? -19.588 2.778   34.059  1.00 34.17 ?  333 ASN B N   1 
ATOM   5695 C CA  . ASN B 1 333 ? -18.657 2.539   32.961  1.00 31.20 ?  333 ASN B CA  1 
ATOM   5696 C C   . ASN B 1 333 ? -17.220 2.508   33.478  1.00 32.14 ?  333 ASN B C   1 
ATOM   5697 O O   . ASN B 1 333 ? -16.835 3.316   34.332  1.00 30.84 ?  333 ASN B O   1 
ATOM   5698 C CB  . ASN B 1 333 ? -18.824 3.625   31.897  1.00 33.39 ?  333 ASN B CB  1 
ATOM   5699 C CG  . ASN B 1 333 ? -17.951 3.395   30.689  1.00 36.33 ?  333 ASN B CG  1 
ATOM   5700 O OD1 . ASN B 1 333 ? -16.870 3.971   30.574  1.00 44.39 ?  333 ASN B OD1 1 
ATOM   5701 N ND2 . ASN B 1 333 ? -18.417 2.561   29.773  1.00 40.63 ?  333 ASN B ND2 1 
ATOM   5702 N N   . ALA B 1 334 ? -16.429 1.551   32.972  1.00 28.60 ?  334 ALA B N   1 
ATOM   5703 C CA  . ALA B 1 334 ? -15.118 1.288   33.568  1.00 28.05 ?  334 ALA B CA  1 
ATOM   5704 C C   . ALA B 1 334 ? -14.202 2.498   33.461  1.00 28.92 ?  334 ALA B C   1 
ATOM   5705 O O   . ALA B 1 334 ? -13.408 2.766   34.373  1.00 26.54 ?  334 ALA B O   1 
ATOM   5706 C CB  . ALA B 1 334 ? -14.463 0.066   32.915  1.00 24.75 ?  334 ALA B CB  1 
ATOM   5707 N N   . GLU B 1 335 ? -14.282 3.232   32.349  1.00 27.88 ?  335 GLU B N   1 
ATOM   5708 C CA  . GLU B 1 335 ? -13.465 4.432   32.198  1.00 31.84 ?  335 GLU B CA  1 
ATOM   5709 C C   . GLU B 1 335 ? -13.741 5.427   33.319  1.00 33.73 ?  335 GLU B C   1 
ATOM   5710 O O   . GLU B 1 335 ? -12.812 6.000   33.908  1.00 29.48 ?  335 GLU B O   1 
ATOM   5711 C CB  . GLU B 1 335 ? -13.738 5.078   30.841  1.00 36.73 ?  335 GLU B CB  1 
ATOM   5712 C CG  . GLU B 1 335 ? -12.580 5.021   29.881  1.00 38.63 ?  335 GLU B CG  1 
ATOM   5713 C CD  . GLU B 1 335 ? -12.877 5.774   28.600  1.00 46.39 ?  335 GLU B CD  1 
ATOM   5714 O OE1 . GLU B 1 335 ? -12.984 7.018   28.660  1.00 49.35 ?  335 GLU B OE1 1 
ATOM   5715 O OE2 . GLU B 1 335 ? -13.016 5.123   27.539  1.00 49.82 -1 335 GLU B OE2 1 
ATOM   5716 N N   . ASP B 1 336 ? -15.021 5.645   33.623  1.00 29.74 ?  336 ASP B N   1 
ATOM   5717 C CA  . ASP B 1 336 ? -15.395 6.560   34.691  1.00 31.95 ?  336 ASP B CA  1 
ATOM   5718 C C   . ASP B 1 336 ? -15.016 5.998   36.054  1.00 32.33 ?  336 ASP B C   1 
ATOM   5719 O O   . ASP B 1 336 ? -14.496 6.730   36.903  1.00 27.32 ?  336 ASP B O   1 
ATOM   5720 C CB  . ASP B 1 336 ? -16.892 6.847   34.641  1.00 32.47 ?  336 ASP B CB  1 
ATOM   5721 C CG  . ASP B 1 336 ? -17.299 7.610   33.398  1.00 35.73 ?  336 ASP B CG  1 
ATOM   5722 O OD1 . ASP B 1 336 ? -16.648 8.625   33.064  1.00 38.70 ?  336 ASP B OD1 1 
ATOM   5723 O OD2 . ASP B 1 336 ? -18.277 7.182   32.763  1.00 37.47 -1 336 ASP B OD2 1 
ATOM   5724 N N   . PHE B 1 337 ? -15.278 4.705   36.286  1.00 29.48 ?  337 PHE B N   1 
ATOM   5725 C CA  . PHE B 1 337 ? -14.864 4.091   37.546  1.00 30.21 ?  337 PHE B CA  1 
ATOM   5726 C C   . PHE B 1 337 ? -13.374 4.296   37.786  1.00 29.23 ?  337 PHE B C   1 
ATOM   5727 O O   . PHE B 1 337 ? -12.955 4.722   38.869  1.00 28.12 ?  337 PHE B O   1 
ATOM   5728 C CB  . PHE B 1 337 ? -15.201 2.596   37.560  1.00 28.31 ?  337 PHE B CB  1 
ATOM   5729 C CG  . PHE B 1 337 ? -14.780 1.908   38.825  1.00 30.11 ?  337 PHE B CG  1 
ATOM   5730 C CD1 . PHE B 1 337 ? -15.375 2.238   40.034  1.00 30.55 ?  337 PHE B CD1 1 
ATOM   5731 C CD2 . PHE B 1 337 ? -13.761 0.967   38.820  1.00 30.68 ?  337 PHE B CD2 1 
ATOM   5732 C CE1 . PHE B 1 337 ? -14.978 1.628   41.210  1.00 32.55 ?  337 PHE B CE1 1 
ATOM   5733 C CE2 . PHE B 1 337 ? -13.361 0.357   39.991  1.00 30.64 ?  337 PHE B CE2 1 
ATOM   5734 C CZ  . PHE B 1 337 ? -13.970 0.688   41.190  1.00 30.14 ?  337 PHE B CZ  1 
ATOM   5735 N N   . CYS B 1 338 ? -12.553 4.009   36.773  1.00 28.17 ?  338 CYS B N   1 
ATOM   5736 C CA  . CYS B 1 338 ? -11.106 4.080   36.957  1.00 28.32 ?  338 CYS B CA  1 
ATOM   5737 C C   . CYS B 1 338 ? -10.670 5.510   37.235  1.00 30.12 ?  338 CYS B C   1 
ATOM   5738 O O   . CYS B 1 338 ? -9.753  5.748   38.029  1.00 30.03 ?  338 CYS B O   1 
ATOM   5739 C CB  . CYS B 1 338 ? -10.407 3.530   35.715  1.00 29.71 ?  338 CYS B CB  1 
ATOM   5740 S SG  . CYS B 1 338 ? -10.345 1.734   35.716  1.00 25.83 ?  338 CYS B SG  1 
ATOM   5741 N N   . LYS B 1 339 ? -11.384 6.480   36.674  1.00 30.86 ?  339 LYS B N   1 
ATOM   5742 C CA  . LYS B 1 339 ? -11.067 7.909   36.939  1.00 31.16 ?  339 LYS B CA  1 
ATOM   5743 C C   . LYS B 1 339 ? -11.407 8.235   38.390  1.00 25.98 ?  339 LYS B C   1 
ATOM   5744 O O   . LYS B 1 339 ? -10.557 8.756   39.073  1.00 30.06 ?  339 LYS B O   1 
ATOM   5745 C CB  . LYS B 1 339 ? -11.901 8.807   36.029  1.00 29.88 ?  339 LYS B CB  1 
ATOM   5746 C CG  . LYS B 1 339 ? -11.354 10.212  35.841  1.00 36.85 ?  339 LYS B CG  1 
ATOM   5747 C CD  . LYS B 1 339 ? -11.867 10.885  34.590  1.00 40.45 ?  339 LYS B CD  1 
ATOM   5748 C CE  . LYS B 1 339 ? -11.892 12.395  34.702  1.00 40.44 ?  339 LYS B CE  1 
ATOM   5749 N NZ  . LYS B 1 339 ? -12.644 12.843  35.897  1.00 44.22 1  339 LYS B NZ  1 
ATOM   5750 N N   . TYR B 1 340 ? -12.603 7.885   38.812  1.00 26.69 ?  340 TYR B N   1 
ATOM   5751 C CA  . TYR B 1 340 ? -13.058 8.117   40.200  1.00 27.08 ?  340 TYR B CA  1 
ATOM   5752 C C   . TYR B 1 340 ? -12.129 7.433   41.197  1.00 32.25 ?  340 TYR B C   1 
ATOM   5753 O O   . TYR B 1 340 ? -11.759 8.027   42.177  1.00 26.14 ?  340 TYR B O   1 
ATOM   5754 C CB  . TYR B 1 340 ? -14.462 7.544   40.332  1.00 31.36 ?  340 TYR B CB  1 
ATOM   5755 C CG  . TYR B 1 340 ? -15.080 7.602   41.703  1.00 39.00 ?  340 TYR B CG  1 
ATOM   5756 C CD1 . TYR B 1 340 ? -15.666 8.767   42.163  1.00 45.97 ?  340 TYR B CD1 1 
ATOM   5757 C CD2 . TYR B 1 340 ? -15.107 6.492   42.529  1.00 38.03 ?  340 TYR B CD2 1 
ATOM   5758 C CE1 . TYR B 1 340 ? -16.247 8.837   43.416  1.00 44.58 ?  340 TYR B CE1 1 
ATOM   5759 C CE2 . TYR B 1 340 ? -15.671 6.550   43.791  1.00 43.21 ?  340 TYR B CE2 1 
ATOM   5760 C CZ  . TYR B 1 340 ? -16.250 7.725   44.233  1.00 43.60 ?  340 TYR B CZ  1 
ATOM   5761 O OH  . TYR B 1 340 ? -16.822 7.804   45.467  1.00 43.37 ?  340 TYR B OH  1 
ATOM   5762 N N   . LEU B 1 341 ? -11.807 6.177   40.919  1.00 27.95 ?  341 LEU B N   1 
ATOM   5763 C CA  . LEU B 1 341 ? -10.931 5.394   41.817  1.00 28.68 ?  341 LEU B CA  1 
ATOM   5764 C C   . LEU B 1 341 ? -9.570  6.087   41.956  1.00 28.88 ?  341 LEU B C   1 
ATOM   5765 O O   . LEU B 1 341 ? -9.057  6.158   43.067  1.00 28.40 ?  341 LEU B O   1 
ATOM   5766 C CB  . LEU B 1 341 ? -10.792 3.993   41.219  1.00 24.69 ?  341 LEU B CB  1 
ATOM   5767 C CG  . LEU B 1 341 ? -9.870  3.019   41.941  1.00 25.37 ?  341 LEU B CG  1 
ATOM   5768 C CD1 . LEU B 1 341 ? -10.473 2.566   43.255  1.00 23.37 ?  341 LEU B CD1 1 
ATOM   5769 C CD2 . LEU B 1 341 ? -9.610  1.823   41.053  1.00 26.87 ?  341 LEU B CD2 1 
ATOM   5770 N N   . ARG B 1 342 ? -9.033  6.572   40.840  1.00 26.17 ?  342 ARG B N   1 
ATOM   5771 C CA  . ARG B 1 342 ? -7.767  7.288   40.955  1.00 30.86 ?  342 ARG B CA  1 
ATOM   5772 C C   . ARG B 1 342 ? -7.919  8.539   41.808  1.00 26.75 ?  342 ARG B C   1 
ATOM   5773 O O   . ARG B 1 342 ? -7.057  8.841   42.642  1.00 30.14 ?  342 ARG B O   1 
ATOM   5774 C CB  . ARG B 1 342 ? -7.244  7.656   39.568  1.00 27.91 ?  342 ARG B CB  1 
ATOM   5775 C CG  . ARG B 1 342 ? -5.931  8.402   39.627  1.00 28.74 ?  342 ARG B CG  1 
ATOM   5776 C CD  . ARG B 1 342 ? -5.310  8.589   38.257  1.00 25.33 ?  342 ARG B CD  1 
ATOM   5777 N NE  . ARG B 1 342 ? -4.037  9.288   38.403  1.00 29.46 ?  342 ARG B NE  1 
ATOM   5778 C CZ  . ARG B 1 342 ? -3.141  9.457   37.435  1.00 31.91 ?  342 ARG B CZ  1 
ATOM   5779 N NH1 . ARG B 1 342 ? -3.376  8.994   36.217  1.00 34.23 1  342 ARG B NH1 1 
ATOM   5780 N NH2 . ARG B 1 342 ? -2.013  10.115  37.690  1.00 30.03 ?  342 ARG B NH2 1 
ATOM   5781 N N   . GLU B 1 343 ? -9.008  9.281   41.609  1.00 28.55 ?  343 GLU B N   1 
ATOM   5782 C CA  . GLU B 1 343 ? -9.188  10.532  42.334  1.00 30.74 ?  343 GLU B CA  1 
ATOM   5783 C C   . GLU B 1 343 ? -9.313  10.293  43.834  1.00 30.66 ?  343 GLU B C   1 
ATOM   5784 O O   . GLU B 1 343 ? -8.686  10.995  44.629  1.00 34.48 ?  343 GLU B O   1 
ATOM   5785 C CB  . GLU B 1 343 ? -10.410 11.277  41.800  1.00 29.12 ?  343 GLU B CB  1 
ATOM   5786 C CG  . GLU B 1 343 ? -10.271 11.677  40.329  1.00 37.40 ?  343 GLU B CG  1 
ATOM   5787 C CD  . GLU B 1 343 ? -11.534 12.303  39.739  1.00 43.46 ?  343 GLU B CD  1 
ATOM   5788 O OE1 . GLU B 1 343 ? -11.428 12.912  38.649  1.00 44.62 ?  343 GLU B OE1 1 
ATOM   5789 O OE2 . GLU B 1 343 ? -12.622 12.181  40.350  1.00 42.72 -1 343 GLU B OE2 1 
ATOM   5790 N N   . LYS B 1 344 ? -10.093 9.288   44.239  1.00 32.24 ?  344 LYS B N   1 
ATOM   5791 C CA  . LYS B 1 344 ? -10.373 9.079   45.657  1.00 31.17 ?  344 LYS B CA  1 
ATOM   5792 C C   . LYS B 1 344 ? -9.302  8.271   46.381  1.00 32.06 ?  344 LYS B C   1 
ATOM   5793 O O   . LYS B 1 344 ? -9.096  8.470   47.586  1.00 27.86 ?  344 LYS B O   1 
ATOM   5794 C CB  . LYS B 1 344 ? -11.735 8.402   45.826  1.00 36.23 ?  344 LYS B CB  1 
ATOM   5795 C CG  . LYS B 1 344 ? -12.880 9.187   45.209  1.00 34.71 ?  344 LYS B CG  1 
ATOM   5796 C CD  . LYS B 1 344 ? -13.218 10.432  46.032  1.00 41.97 ?  344 LYS B CD  1 
ATOM   5797 C CE  . LYS B 1 344 ? -14.375 11.231  45.417  1.00 50.15 ?  344 LYS B CE  1 
ATOM   5798 N NZ  . LYS B 1 344 ? -14.023 12.646  45.052  1.00 49.39 1  344 LYS B NZ  1 
ATOM   5799 N N   . THR B 1 345 ? -8.591  7.384   45.678  1.00 27.51 ?  345 THR B N   1 
ATOM   5800 C CA  . THR B 1 345 ? -7.674  6.458   46.321  1.00 28.56 ?  345 THR B CA  1 
ATOM   5801 C C   . THR B 1 345 ? -6.247  6.509   45.805  1.00 27.37 ?  345 THR B C   1 
ATOM   5802 O O   . THR B 1 345 ? -5.364  5.952   46.464  1.00 26.60 ?  345 THR B O   1 
ATOM   5803 C CB  . THR B 1 345 ? -8.171  5.013   46.165  1.00 27.88 ?  345 THR B CB  1 
ATOM   5804 O OG1 . THR B 1 345 ? -7.876  4.555   44.839  1.00 29.00 ?  345 THR B OG1 1 
ATOM   5805 C CG2 . THR B 1 345 ? -9.664  4.943   46.399  1.00 28.43 ?  345 THR B CG2 1 
ATOM   5806 N N   . GLY B 1 346 ? -5.991  7.114   44.645  1.00 29.38 ?  346 GLY B N   1 
ATOM   5807 C CA  . GLY B 1 346 ? -4.652  7.063   44.092  1.00 26.90 ?  346 GLY B CA  1 
ATOM   5808 C C   . GLY B 1 346 ? -4.305  5.774   43.375  1.00 28.83 ?  346 GLY B C   1 
ATOM   5809 O O   . GLY B 1 346 ? -3.199  5.665   42.827  1.00 25.44 ?  346 GLY B O   1 
ATOM   5810 N N   . LEU B 1 347 ? -5.199  4.790   43.374  1.00 27.18 ?  347 LEU B N   1 
ATOM   5811 C CA  . LEU B 1 347 ? -4.967  3.552   42.641  1.00 23.32 ?  347 LEU B CA  1 
ATOM   5812 C C   . LEU B 1 347 ? -5.218  3.765   41.155  1.00 24.73 ?  347 LEU B C   1 
ATOM   5813 O O   . LEU B 1 347 ? -6.273  4.274   40.766  1.00 25.13 ?  347 LEU B O   1 
ATOM   5814 C CB  . LEU B 1 347 ? -5.886  2.454   43.166  1.00 24.60 ?  347 LEU B CB  1 
ATOM   5815 C CG  . LEU B 1 347 ? -5.849  1.137   42.403  1.00 22.70 ?  347 LEU B CG  1 
ATOM   5816 C CD1 . LEU B 1 347 ? -4.449  0.543   42.387  1.00 25.19 ?  347 LEU B CD1 1 
ATOM   5817 C CD2 . LEU B 1 347 ? -6.850  0.169   43.029  1.00 24.38 ?  347 LEU B CD2 1 
ATOM   5818 N N   . ILE B 1 348 ? -4.261  3.362   40.323  1.00 20.41 ?  348 ILE B N   1 
ATOM   5819 C CA  . ILE B 1 348 ? -4.376  3.509   38.864  1.00 20.21 ?  348 ILE B CA  1 
ATOM   5820 C C   . ILE B 1 348 ? -4.380  2.114   38.246  1.00 24.49 ?  348 ILE B C   1 
ATOM   5821 O O   . ILE B 1 348 ? -3.356  1.415   38.261  1.00 24.14 ?  348 ILE B O   1 
ATOM   5822 C CB  . ILE B 1 348 ? -3.245  4.374   38.292  1.00 22.36 ?  348 ILE B CB  1 
ATOM   5823 C CG1 . ILE B 1 348 ? -3.164  5.687   39.070  1.00 20.60 ?  348 ILE B CG1 1 
ATOM   5824 C CG2 . ILE B 1 348 ? -3.472  4.656   36.803  1.00 22.75 ?  348 ILE B CG2 1 
ATOM   5825 C CD1 . ILE B 1 348 ? -1.862  6.447   38.848  1.00 27.02 ?  348 ILE B CD1 1 
ATOM   5826 N N   . ILE B 1 349 ? -5.537  1.694   37.726  1.00 22.42 ?  349 ILE B N   1 
ATOM   5827 C CA  . ILE B 1 349 ? -5.679  0.416   37.045  1.00 23.19 ?  349 ILE B CA  1 
ATOM   5828 C C   . ILE B 1 349 ? -6.206  0.681   35.634  1.00 23.91 ?  349 ILE B C   1 
ATOM   5829 O O   . ILE B 1 349 ? -6.576  1.806   35.287  1.00 22.84 ?  349 ILE B O   1 
ATOM   5830 C CB  . ILE B 1 349 ? -6.591  -0.569  37.809  1.00 20.22 ?  349 ILE B CB  1 
ATOM   5831 C CG1 . ILE B 1 349 ? -8.004  -0.001  37.967  1.00 23.59 ?  349 ILE B CG1 1 
ATOM   5832 C CG2 . ILE B 1 349 ? -5.999  -0.912  39.196  1.00 19.94 ?  349 ILE B CG2 1 
ATOM   5833 C CD1 . ILE B 1 349 ? -8.917  -0.898  38.797  1.00 22.30 ?  349 ILE B CD1 1 
ATOM   5834 N N   . SER B 1 350 ? -6.227  -0.372  34.812  1.00 20.70 ?  350 SER B N   1 
ATOM   5835 C CA  . SER B 1 350 ? -6.564  -0.234  33.392  1.00 23.40 ?  350 SER B CA  1 
ATOM   5836 C C   . SER B 1 350 ? -8.066  -0.371  33.162  1.00 24.77 ?  350 SER B C   1 
ATOM   5837 O O   . SER B 1 350 ? -8.654  -1.402  33.489  1.00 25.46 ?  350 SER B O   1 
ATOM   5838 C CB  . SER B 1 350 ? -5.824  -1.268  32.547  1.00 23.50 ?  350 SER B CB  1 
ATOM   5839 O OG  . SER B 1 350 ? -4.431  -1.139  32.718  1.00 29.74 ?  350 SER B OG  1 
ATOM   5840 N N   . ALA B 1 351 ? -8.685  0.661   32.585  1.00 26.03 ?  351 ALA B N   1 
ATOM   5841 C CA  . ALA B 1 351 ? -10.090 0.546   32.212  1.00 24.70 ?  351 ALA B CA  1 
ATOM   5842 C C   . ALA B 1 351 ? -10.240 -0.470  31.084  1.00 22.88 ?  351 ALA B C   1 
ATOM   5843 O O   . ALA B 1 351 ? -9.393  -0.565  30.194  1.00 24.37 ?  351 ALA B O   1 
ATOM   5844 C CB  . ALA B 1 351 ? -10.649 1.911   31.792  1.00 23.62 ?  351 ALA B CB  1 
ATOM   5845 N N   . GLY B 1 352 ? -11.299 -1.270  31.150  1.00 21.90 ?  352 GLY B N   1 
ATOM   5846 C CA  . GLY B 1 352 ? -11.492 -2.285  30.137  1.00 23.73 ?  352 GLY B CA  1 
ATOM   5847 C C   . GLY B 1 352 ? -11.941 -1.758  28.786  1.00 26.68 ?  352 GLY B C   1 
ATOM   5848 O O   . GLY B 1 352 ? -11.865 -2.505  27.809  1.00 22.70 ?  352 GLY B O   1 
ATOM   5849 N N   . ASN B 1 353 ? -12.370 -0.495  28.699  1.00 25.52 ?  353 ASN B N   1 
ATOM   5850 C CA  . ASN B 1 353 ? -12.998 -0.008  27.471  1.00 27.86 ?  353 ASN B CA  1 
ATOM   5851 C C   . ASN B 1 353 ? -12.097 -0.179  26.256  1.00 28.32 ?  353 ASN B C   1 
ATOM   5852 O O   . ASN B 1 353 ? -12.570 -0.540  25.170  1.00 26.51 ?  353 ASN B O   1 
ATOM   5853 C CB  . ASN B 1 353 ? -13.370 1.464   27.595  1.00 29.22 ?  353 ASN B CB  1 
ATOM   5854 C CG  . ASN B 1 353 ? -14.258 1.750   28.771  1.00 31.73 ?  353 ASN B CG  1 
ATOM   5855 O OD1 . ASN B 1 353 ? -13.908 1.471   29.913  1.00 29.78 ?  353 ASN B OD1 1 
ATOM   5856 N ND2 . ASN B 1 353 ? -15.422 2.331   28.495  1.00 35.67 ?  353 ASN B ND2 1 
ATOM   5857 N N   . GLY B 1 354 ? -10.811 0.135   26.400  1.00 26.39 ?  354 GLY B N   1 
ATOM   5858 C CA  . GLY B 1 354 ? -9.906  0.105   25.263  1.00 24.40 ?  354 GLY B CA  1 
ATOM   5859 C C   . GLY B 1 354 ? -9.641  -1.279  24.709  1.00 25.41 ?  354 GLY B C   1 
ATOM   5860 O O   . GLY B 1 354 ? -9.174  -1.394  23.574  1.00 24.60 ?  354 GLY B O   1 
ATOM   5861 N N   . TYR B 1 355 ? -9.922  -2.330  25.480  1.00 24.07 ?  355 TYR B N   1 
ATOM   5862 C CA  . TYR B 1 355 ? -9.844  -3.699  24.972  1.00 24.70 ?  355 TYR B CA  1 
ATOM   5863 C C   . TYR B 1 355 ? -11.045 -4.073  24.106  1.00 24.60 ?  355 TYR B C   1 
ATOM   5864 O O   . TYR B 1 355 ? -11.046 -5.158  23.513  1.00 22.14 ?  355 TYR B O   1 
ATOM   5865 C CB  . TYR B 1 355 ? -9.691  -4.687  26.142  1.00 18.86 ?  355 TYR B CB  1 
ATOM   5866 C CG  . TYR B 1 355 ? -8.497  -4.335  27.005  1.00 20.44 ?  355 TYR B CG  1 
ATOM   5867 C CD1 . TYR B 1 355 ? -7.209  -4.544  26.549  1.00 22.78 ?  355 TYR B CD1 1 
ATOM   5868 C CD2 . TYR B 1 355 ? -8.663  -3.725  28.247  1.00 21.75 ?  355 TYR B CD2 1 
ATOM   5869 C CE1 . TYR B 1 355 ? -6.109  -4.187  27.317  1.00 20.99 ?  355 TYR B CE1 1 
ATOM   5870 C CE2 . TYR B 1 355 ? -7.565  -3.364  29.024  1.00 24.93 ?  355 TYR B CE2 1 
ATOM   5871 C CZ  . TYR B 1 355 ? -6.298  -3.599  28.549  1.00 25.28 ?  355 TYR B CZ  1 
ATOM   5872 O OH  . TYR B 1 355 ? -5.206  -3.247  29.296  1.00 25.08 ?  355 TYR B OH  1 
ATOM   5873 N N   . ARG B 1 356 ? -12.040 -3.196  24.003  1.00 24.77 ?  356 ARG B N   1 
ATOM   5874 C CA  . ARG B 1 356 ? -13.282 -3.432  23.256  1.00 24.63 ?  356 ARG B CA  1 
ATOM   5875 C C   . ARG B 1 356 ? -13.968 -4.682  23.814  1.00 24.23 ?  356 ARG B C   1 
ATOM   5876 O O   . ARG B 1 356 ? -13.901 -4.942  25.024  1.00 23.14 ?  356 ARG B O   1 
ATOM   5877 C CB  . ARG B 1 356 ? -12.982 -3.455  21.764  1.00 26.66 ?  356 ARG B CB  1 
ATOM   5878 C CG  . ARG B 1 356 ? -12.333 -2.144  21.278  1.00 24.06 ?  356 ARG B CG  1 
ATOM   5879 C CD  . ARG B 1 356 ? -12.277 -2.018  19.765  1.00 24.53 ?  356 ARG B CD  1 
ATOM   5880 N NE  . ARG B 1 356 ? -11.536 -0.819  19.390  1.00 22.78 ?  356 ARG B NE  1 
ATOM   5881 C CZ  . ARG B 1 356 ? -11.165 -0.503  18.157  1.00 26.44 ?  356 ARG B CZ  1 
ATOM   5882 N NH1 . ARG B 1 356 ? -11.470 -1.299  17.135  1.00 24.31 1  356 ARG B NH1 1 
ATOM   5883 N NH2 . ARG B 1 356 ? -10.487 0.618   17.950  1.00 23.04 ?  356 ARG B NH2 1 
ATOM   5884 N N   . GLY B 1 357 ? -14.650 -5.451  22.965  1.00 23.62 ?  357 GLY B N   1 
ATOM   5885 C CA  . GLY B 1 357 ? -15.466 -6.538  23.492  1.00 21.01 ?  357 GLY B CA  1 
ATOM   5886 C C   . GLY B 1 357 ? -16.426 -6.009  24.531  1.00 28.67 ?  357 GLY B C   1 
ATOM   5887 O O   . GLY B 1 357 ? -16.990 -4.921  24.387  1.00 25.52 ?  357 GLY B O   1 
ATOM   5888 N N   . ASN B 1 358 ? -16.594 -6.752  25.622  1.00 27.68 ?  358 ASN B N   1 
ATOM   5889 C CA  . ASN B 1 358 ? -17.405 -6.251  26.724  1.00 24.54 ?  358 ASN B CA  1 
ATOM   5890 C C   . ASN B 1 358 ? -16.575 -5.513  27.765  1.00 27.54 ?  358 ASN B C   1 
ATOM   5891 O O   . ASN B 1 358 ? -16.972 -5.443  28.935  1.00 23.88 ?  358 ASN B O   1 
ATOM   5892 C CB  . ASN B 1 358 ? -18.199 -7.393  27.361  1.00 27.81 ?  358 ASN B CB  1 
ATOM   5893 C CG  . ASN B 1 358 ? -17.319 -8.461  27.977  1.00 28.51 ?  358 ASN B CG  1 
ATOM   5894 O OD1 . ASN B 1 358 ? -16.122 -8.594  27.663  1.00 29.11 ?  358 ASN B OD1 1 
ATOM   5895 N ND2 . ASN B 1 358 ? -17.910 -9.240  28.861  1.00 28.28 ?  358 ASN B ND2 1 
ATOM   5896 N N   . GLY B 1 359 ? -15.456 -4.913  27.348  1.00 23.68 ?  359 GLY B N   1 
ATOM   5897 C CA  . GLY B 1 359 ? -14.524 -4.300  28.277  1.00 27.87 ?  359 GLY B CA  1 
ATOM   5898 C C   . GLY B 1 359 ? -15.081 -3.132  29.063  1.00 29.31 ?  359 GLY B C   1 
ATOM   5899 O O   . GLY B 1 359 ? -14.498 -2.762  30.091  1.00 25.80 ?  359 GLY B O   1 
ATOM   5900 N N   . HIS B 1 360 ? -16.198 -2.541  28.622  1.00 27.91 ?  360 HIS B N   1 
ATOM   5901 C CA  . HIS B 1 360 ? -16.761 -1.431  29.391  1.00 27.86 ?  360 HIS B CA  1 
ATOM   5902 C C   . HIS B 1 360 ? -17.193 -1.873  30.780  1.00 29.17 ?  360 HIS B C   1 
ATOM   5903 O O   . HIS B 1 360 ? -17.389 -1.025  31.659  1.00 31.87 ?  360 HIS B O   1 
ATOM   5904 C CB  . HIS B 1 360 ? -17.943 -0.786  28.653  1.00 28.22 ?  360 HIS B CB  1 
ATOM   5905 C CG  . HIS B 1 360 ? -19.135 -1.682  28.517  1.00 26.67 ?  360 HIS B CG  1 
ATOM   5906 N ND1 . HIS B 1 360 ? -19.229 -2.653  27.542  1.00 34.06 ?  360 HIS B ND1 1 
ATOM   5907 C CD2 . HIS B 1 360 ? -20.274 -1.768  29.242  1.00 29.38 ?  360 HIS B CD2 1 
ATOM   5908 C CE1 . HIS B 1 360 ? -20.376 -3.298  27.670  1.00 30.28 ?  360 HIS B CE1 1 
ATOM   5909 N NE2 . HIS B 1 360 ? -21.029 -2.781  28.695  1.00 36.22 ?  360 HIS B NE2 1 
ATOM   5910 N N   . GLU B 1 361 ? -17.307 -3.181  31.003  1.00 32.74 ?  361 GLU B N   1 
ATOM   5911 C CA  . GLU B 1 361 ? -17.715 -3.749  32.277  1.00 28.88 ?  361 GLU B CA  1 
ATOM   5912 C C   . GLU B 1 361 ? -16.551 -4.266  33.102  1.00 25.74 ?  361 GLU B C   1 
ATOM   5913 O O   . GLU B 1 361 ? -16.788 -4.894  34.132  1.00 26.61 ?  361 GLU B O   1 
ATOM   5914 C CB  . GLU B 1 361 ? -18.697 -4.901  32.056  1.00 29.43 ?  361 GLU B CB  1 
ATOM   5915 C CG  . GLU B 1 361 ? -19.913 -4.569  31.231  1.00 34.54 ?  361 GLU B CG  1 
ATOM   5916 C CD  . GLU B 1 361 ? -20.962 -5.645  31.359  1.00 35.35 ?  361 GLU B CD  1 
ATOM   5917 O OE1 . GLU B 1 361 ? -22.031 -5.379  31.951  1.00 41.85 ?  361 GLU B OE1 1 
ATOM   5918 O OE2 . GLU B 1 361 ? -20.691 -6.775  30.905  1.00 42.36 -1 361 GLU B OE2 1 
ATOM   5919 N N   . PHE B 1 362 ? -15.306 -4.017  32.688  1.00 24.23 ?  362 PHE B N   1 
ATOM   5920 C CA  . PHE B 1 362 ? -14.157 -4.687  33.280  1.00 22.94 ?  362 PHE B CA  1 
ATOM   5921 C C   . PHE B 1 362 ? -13.017 -3.716  33.552  1.00 25.40 ?  362 PHE B C   1 
ATOM   5922 O O   . PHE B 1 362 ? -12.860 -2.698  32.876  1.00 23.09 ?  362 PHE B O   1 
ATOM   5923 C CB  . PHE B 1 362 ? -13.609 -5.794  32.371  1.00 25.93 ?  362 PHE B CB  1 
ATOM   5924 C CG  . PHE B 1 362 ? -14.445 -7.029  32.342  1.00 24.16 ?  362 PHE B CG  1 
ATOM   5925 C CD1 . PHE B 1 362 ? -15.623 -7.064  31.610  1.00 26.81 ?  362 PHE B CD1 1 
ATOM   5926 C CD2 . PHE B 1 362 ? -14.050 -8.166  33.037  1.00 25.66 ?  362 PHE B CD2 1 
ATOM   5927 C CE1 . PHE B 1 362 ? -16.405 -8.205  31.589  1.00 27.63 ?  362 PHE B CE1 1 
ATOM   5928 C CE2 . PHE B 1 362 ? -14.829 -9.308  33.007  1.00 26.46 ?  362 PHE B CE2 1 
ATOM   5929 C CZ  . PHE B 1 362 ? -16.006 -9.319  32.280  1.00 26.82 ?  362 PHE B CZ  1 
ATOM   5930 N N   . VAL B 1 363 ? -12.169 -4.098  34.509  1.00 23.19 ?  363 VAL B N   1 
ATOM   5931 C CA  . VAL B 1 363 ? -10.891 -3.438  34.727  1.00 21.89 ?  363 VAL B CA  1 
ATOM   5932 C C   . VAL B 1 363 ? -9.800  -4.503  34.682  1.00 20.04 ?  363 VAL B C   1 
ATOM   5933 O O   . VAL B 1 363 ? -10.050 -5.688  34.891  1.00 25.94 ?  363 VAL B O   1 
ATOM   5934 C CB  . VAL B 1 363 ? -10.848 -2.657  36.063  1.00 22.76 ?  363 VAL B CB  1 
ATOM   5935 C CG1 . VAL B 1 363 ? -11.982 -1.609  36.106  1.00 27.65 ?  363 VAL B CG1 1 
ATOM   5936 C CG2 . VAL B 1 363 ? -10.939 -3.607  37.254  1.00 24.41 ?  363 VAL B CG2 1 
ATOM   5937 N N   . ARG B 1 364 ? -8.576  -4.065  34.407  1.00 21.43 ?  364 ARG B N   1 
ATOM   5938 C CA  . ARG B 1 364 ? -7.415  -4.951  34.396  1.00 20.02 ?  364 ARG B CA  1 
ATOM   5939 C C   . ARG B 1 364 ? -6.403  -4.453  35.419  1.00 22.20 ?  364 ARG B C   1 
ATOM   5940 O O   . ARG B 1 364 ? -6.072  -3.264  35.438  1.00 21.85 ?  364 ARG B O   1 
ATOM   5941 C CB  . ARG B 1 364 ? -6.785  -5.014  33.006  1.00 18.24 ?  364 ARG B CB  1 
ATOM   5942 C CG  . ARG B 1 364 ? -5.855  -6.230  32.807  1.00 22.88 ?  364 ARG B CG  1 
ATOM   5943 C CD  . ARG B 1 364 ? -5.016  -6.105  31.547  1.00 22.07 ?  364 ARG B CD  1 
ATOM   5944 N NE  . ARG B 1 364 ? -3.944  -5.131  31.745  1.00 21.10 ?  364 ARG B NE  1 
ATOM   5945 C CZ  . ARG B 1 364 ? -3.028  -4.824  30.835  1.00 24.65 ?  364 ARG B CZ  1 
ATOM   5946 N NH1 . ARG B 1 364 ? -3.046  -5.407  29.633  1.00 22.39 1  364 ARG B NH1 1 
ATOM   5947 N NH2 . ARG B 1 364 ? -2.099  -3.921  31.123  1.00 22.93 ?  364 ARG B NH2 1 
ATOM   5948 N N   . ILE B 1 365 ? -5.905  -5.363  36.259  1.00 21.54 ?  365 ILE B N   1 
ATOM   5949 C CA  . ILE B 1 365 ? -5.037  -5.020  37.381  1.00 21.92 ?  365 ILE B CA  1 
ATOM   5950 C C   . ILE B 1 365 ? -3.748  -5.820  37.285  1.00 22.87 ?  365 ILE B C   1 
ATOM   5951 O O   . ILE B 1 365 ? -3.783  -7.047  37.181  1.00 24.54 ?  365 ILE B O   1 
ATOM   5952 C CB  . ILE B 1 365 ? -5.726  -5.289  38.729  1.00 25.12 ?  365 ILE B CB  1 
ATOM   5953 C CG1 . ILE B 1 365 ? -7.097  -4.596  38.775  1.00 23.58 ?  365 ILE B CG1 1 
ATOM   5954 C CG2 . ILE B 1 365 ? -4.844  -4.832  39.872  1.00 23.17 ?  365 ILE B CG2 1 
ATOM   5955 C CD1 . ILE B 1 365 ? -7.861  -4.843  40.074  1.00 22.56 ?  365 ILE B CD1 1 
ATOM   5956 N N   . ASN B 1 366 ? -2.619  -5.127  37.361  1.00 22.08 ?  366 ASN B N   1 
ATOM   5957 C CA  . ASN B 1 366 ? -1.299  -5.734  37.239  1.00 22.59 ?  366 ASN B CA  1 
ATOM   5958 C C   . ASN B 1 366 ? -0.796  -6.112  38.631  1.00 25.37 ?  366 ASN B C   1 
ATOM   5959 O O   . ASN B 1 366 ? -0.570  -5.226  39.461  1.00 23.79 ?  366 ASN B O   1 
ATOM   5960 C CB  . ASN B 1 366 ? -0.361  -4.733  36.557  1.00 20.12 ?  366 ASN B CB  1 
ATOM   5961 C CG  . ASN B 1 366 ? 1.049   -5.241  36.390  1.00 25.05 ?  366 ASN B CG  1 
ATOM   5962 O OD1 . ASN B 1 366 ? 1.448   -6.254  36.977  1.00 23.19 ?  366 ASN B OD1 1 
ATOM   5963 N ND2 . ASN B 1 366 ? 1.833   -4.519  35.584  1.00 22.17 ?  366 ASN B ND2 1 
ATOM   5964 N N   . LEU B 1 367 ? -0.607  -7.419  38.880  1.00 22.61 ?  367 LEU B N   1 
ATOM   5965 C CA  . LEU B 1 367 ? -0.180  -7.920  40.182  1.00 24.34 ?  367 LEU B CA  1 
ATOM   5966 C C   . LEU B 1 367 ? 1.289   -8.319  40.230  1.00 25.06 ?  367 LEU B C   1 
ATOM   5967 O O   . LEU B 1 367 ? 1.719   -8.950  41.206  1.00 22.87 ?  367 LEU B O   1 
ATOM   5968 C CB  . LEU B 1 367 ? -1.046  -9.110  40.607  1.00 24.46 ?  367 LEU B CB  1 
ATOM   5969 C CG  . LEU B 1 367 ? -2.538  -8.799  40.699  1.00 25.37 ?  367 LEU B CG  1 
ATOM   5970 C CD1 . LEU B 1 367 ? -3.351  -10.035 41.057  1.00 25.49 ?  367 LEU B CD1 1 
ATOM   5971 C CD2 . LEU B 1 367 ? -2.787  -7.679  41.679  1.00 25.85 ?  367 LEU B CD2 1 
ATOM   5972 N N   . ALA B 1 368 ? 2.079   -7.957  39.223  1.00 23.72 ?  368 ALA B N   1 
ATOM   5973 C CA  . ALA B 1 368 ? 3.514   -8.252  39.259  1.00 24.71 ?  368 ALA B CA  1 
ATOM   5974 C C   . ALA B 1 368 ? 4.235   -7.137  40.011  1.00 26.12 ?  368 ALA B C   1 
ATOM   5975 O O   . ALA B 1 368 ? 4.923   -6.287  39.441  1.00 24.98 ?  368 ALA B O   1 
ATOM   5976 C CB  . ALA B 1 368 ? 4.063   -8.415  37.847  1.00 22.79 ?  368 ALA B CB  1 
ATOM   5977 N N   . CYS B 1 369 ? 4.046   -7.140  41.322  1.00 21.76 ?  369 CYS B N   1 
ATOM   5978 C CA  . CYS B 1 369 ? 4.718   -6.178  42.176  1.00 23.36 ?  369 CYS B CA  1 
ATOM   5979 C C   . CYS B 1 369 ? 4.851   -6.814  43.545  1.00 26.43 ?  369 CYS B C   1 
ATOM   5980 O O   . CYS B 1 369 ? 4.152   -7.791  43.853  1.00 22.00 ?  369 CYS B O   1 
ATOM   5981 C CB  . CYS B 1 369 ? 3.950   -4.859  42.256  1.00 25.11 ?  369 CYS B CB  1 
ATOM   5982 S SG  . CYS B 1 369 ? 2.219   -5.182  42.704  1.00 25.02 ?  369 CYS B SG  1 
ATOM   5983 N N   . PRO B 1 370 ? 5.741   -6.298  44.388  1.00 24.92 ?  370 PRO B N   1 
ATOM   5984 C CA  . PRO B 1 370 ? 5.873   -6.827  45.757  1.00 26.50 ?  370 PRO B CA  1 
ATOM   5985 C C   . PRO B 1 370 ? 4.517   -6.934  46.440  1.00 27.18 ?  370 PRO B C   1 
ATOM   5986 O O   . PRO B 1 370 ? 3.609   -6.141  46.185  1.00 26.95 ?  370 PRO B O   1 
ATOM   5987 C CB  . PRO B 1 370 ? 6.770   -5.792  46.444  1.00 26.12 ?  370 PRO B CB  1 
ATOM   5988 C CG  . PRO B 1 370 ? 7.590   -5.194  45.297  1.00 23.94 ?  370 PRO B CG  1 
ATOM   5989 C CD  . PRO B 1 370 ? 6.743   -5.266  44.069  1.00 24.82 ?  370 PRO B CD  1 
ATOM   5990 N N   . LYS B 1 371 ? 4.387   -7.929  47.319  1.00 28.74 ?  371 LYS B N   1 
ATOM   5991 C CA  . LYS B 1 371 ? 3.099   -8.174  47.955  1.00 28.44 ?  371 LYS B CA  1 
ATOM   5992 C C   . LYS B 1 371 ? 2.610   -6.973  48.754  1.00 26.05 ?  371 LYS B C   1 
ATOM   5993 O O   . LYS B 1 371 ? 1.402   -6.827  48.961  1.00 28.64 ?  371 LYS B O   1 
ATOM   5994 C CB  . LYS B 1 371 ? 3.178   -9.397  48.866  1.00 32.61 ?  371 LYS B CB  1 
ATOM   5995 C CG  . LYS B 1 371 ? 1.804   -9.908  49.302  1.00 36.70 ?  371 LYS B CG  1 
ATOM   5996 C CD  . LYS B 1 371 ? 1.957   -11.111 50.188  1.00 41.51 ?  371 LYS B CD  1 
ATOM   5997 C CE  . LYS B 1 371 ? 0.612   -11.633 50.630  1.00 39.17 ?  371 LYS B CE  1 
ATOM   5998 N NZ  . LYS B 1 371 ? 0.603   -13.108 50.609  1.00 40.04 1  371 LYS B NZ  1 
ATOM   5999 N N   . GLU B 1 372 ? 3.517   -6.110  49.220  1.00 27.00 ?  372 GLU B N   1 
ATOM   6000 C CA  . GLU B 1 372 ? 3.076   -4.911  49.930  1.00 26.11 ?  372 GLU B CA  1 
ATOM   6001 C C   . GLU B 1 372 ? 2.238   -4.018  49.024  1.00 29.09 ?  372 GLU B C   1 
ATOM   6002 O O   . GLU B 1 372 ? 1.237   -3.432  49.458  1.00 27.25 ?  372 GLU B O   1 
ATOM   6003 C CB  . GLU B 1 372 ? 4.279   -4.132  50.469  1.00 34.54 ?  372 GLU B CB  1 
ATOM   6004 C CG  . GLU B 1 372 ? 4.980   -4.769  51.666  1.00 37.54 ?  372 GLU B CG  1 
ATOM   6005 C CD  . GLU B 1 372 ? 6.058   -5.754  51.258  1.00 41.29 ?  372 GLU B CD  1 
ATOM   6006 O OE1 . GLU B 1 372 ? 6.878   -6.131  52.118  1.00 40.89 ?  372 GLU B OE1 1 
ATOM   6007 O OE2 . GLU B 1 372 ? 6.086   -6.163  50.079  1.00 38.03 -1 372 GLU B OE2 1 
ATOM   6008 N N   . LEU B 1 373 ? 2.645   -3.892  47.761  1.00 26.12 ?  373 LEU B N   1 
ATOM   6009 C CA  . LEU B 1 373 ? 1.881   -3.103  46.800  1.00 25.92 ?  373 LEU B CA  1 
ATOM   6010 C C   . LEU B 1 373 ? 0.583   -3.803  46.404  1.00 26.13 ?  373 LEU B C   1 
ATOM   6011 O O   . LEU B 1 373 ? -0.438  -3.143  46.200  1.00 25.84 ?  373 LEU B O   1 
ATOM   6012 C CB  . LEU B 1 373 ? 2.736   -2.818  45.564  1.00 24.91 ?  373 LEU B CB  1 
ATOM   6013 C CG  . LEU B 1 373 ? 3.665   -1.609  45.690  1.00 27.80 ?  373 LEU B CG  1 
ATOM   6014 C CD1 . LEU B 1 373 ? 4.812   -1.882  46.653  1.00 28.96 ?  373 LEU B CD1 1 
ATOM   6015 C CD2 . LEU B 1 373 ? 4.180   -1.184  44.315  1.00 25.32 ?  373 LEU B CD2 1 
ATOM   6016 N N   . VAL B 1 374 ? 0.598   -5.136  46.288  1.00 25.40 ?  374 VAL B N   1 
ATOM   6017 C CA  . VAL B 1 374 ? -0.646  -5.865  46.029  1.00 26.67 ?  374 VAL B CA  1 
ATOM   6018 C C   . VAL B 1 374 ? -1.653  -5.596  47.136  1.00 25.27 ?  374 VAL B C   1 
ATOM   6019 O O   . VAL B 1 374 ? -2.838  -5.347  46.882  1.00 25.77 ?  374 VAL B O   1 
ATOM   6020 C CB  . VAL B 1 374 ? -0.377  -7.376  45.897  1.00 25.79 ?  374 VAL B CB  1 
ATOM   6021 C CG1 . VAL B 1 374 ? -1.700  -8.148  45.737  1.00 26.00 ?  374 VAL B CG1 1 
ATOM   6022 C CG2 . VAL B 1 374 ? 0.579   -7.656  44.740  1.00 25.47 ?  374 VAL B CG2 1 
ATOM   6023 N N   . ILE B 1 375 ? -1.199  -5.685  48.388  1.00 26.14 ?  375 ILE B N   1 
ATOM   6024 C CA  . ILE B 1 375 ? -2.072  -5.406  49.521  1.00 24.91 ?  375 ILE B CA  1 
ATOM   6025 C C   . ILE B 1 375 ? -2.614  -3.987  49.434  1.00 25.29 ?  375 ILE B C   1 
ATOM   6026 O O   . ILE B 1 375 ? -3.823  -3.752  49.562  1.00 24.62 ?  375 ILE B O   1 
ATOM   6027 C CB  . ILE B 1 375 ? -1.311  -5.639  50.839  1.00 25.55 ?  375 ILE B CB  1 
ATOM   6028 C CG1 . ILE B 1 375 ? -1.036  -7.129  51.054  1.00 25.64 ?  375 ILE B CG1 1 
ATOM   6029 C CG2 . ILE B 1 375 ? -2.071  -5.023  51.991  1.00 28.11 ?  375 ILE B CG2 1 
ATOM   6030 C CD1 . ILE B 1 375 ? -0.088  -7.426  52.223  1.00 31.95 ?  375 ILE B CD1 1 
ATOM   6031 N N   . ASP B 1 376 ? -1.717  -3.018  49.229  1.00 25.01 ?  376 ASP B N   1 
ATOM   6032 C CA  . ASP B 1 376 ? -2.113  -1.619  49.100  1.00 28.29 ?  376 ASP B CA  1 
ATOM   6033 C C   . ASP B 1 376 ? -3.183  -1.440  48.022  1.00 24.70 ?  376 ASP B C   1 
ATOM   6034 O O   . ASP B 1 376 ? -4.251  -0.865  48.270  1.00 23.60 ?  376 ASP B O   1 
ATOM   6035 C CB  . ASP B 1 376 ? -0.860  -0.788  48.780  1.00 23.85 ?  376 ASP B CB  1 
ATOM   6036 C CG  . ASP B 1 376 ? -1.056  0.686   48.993  1.00 27.98 ?  376 ASP B CG  1 
ATOM   6037 O OD1 . ASP B 1 376 ? -2.164  1.105   49.393  1.00 26.70 ?  376 ASP B OD1 1 
ATOM   6038 O OD2 . ASP B 1 376 ? -0.080  1.432   48.753  1.00 27.55 -1 376 ASP B OD2 1 
ATOM   6039 N N   . GLY B 1 377 ? -2.914  -1.949  46.817  1.00 25.49 ?  377 GLY B N   1 
ATOM   6040 C CA  . GLY B 1 377 ? -3.851  -1.755  45.717  1.00 22.80 ?  377 GLY B CA  1 
ATOM   6041 C C   . GLY B 1 377 ? -5.196  -2.403  45.974  1.00 24.64 ?  377 GLY B C   1 
ATOM   6042 O O   . GLY B 1 377 ? -6.243  -1.804  45.727  1.00 27.18 ?  377 GLY B O   1 
ATOM   6043 N N   . MET B 1 378 ? -5.202  -3.598  46.516  1.00 24.35 ?  378 MET B N   1 
ATOM   6044 C CA  . MET B 1 378 ? -6.479  -4.291  46.781  1.00 26.91 ?  378 MET B CA  1 
ATOM   6045 C C   . MET B 1 378 ? -7.271  -3.498  47.825  1.00 26.87 ?  378 MET B C   1 
ATOM   6046 O O   . MET B 1 378 ? -8.473  -3.349  47.676  1.00 24.98 ?  378 MET B O   1 
ATOM   6047 C CB  . MET B 1 378 ? -6.239  -5.727  47.242  1.00 26.73 ?  378 MET B CB  1 
ATOM   6048 C CG  . MET B 1 378 ? -5.738  -6.636  46.155  1.00 25.32 ?  378 MET B CG  1 
ATOM   6049 S SD  . MET B 1 378 ? -6.831  -6.658  44.734  1.00 29.43 ?  378 MET B SD  1 
ATOM   6050 C CE  . MET B 1 378 ? -5.875  -5.720  43.545  1.00 23.34 ?  378 MET B CE  1 
ATOM   6051 N N   . GLN B 1 379 ? -6.578  -2.997  48.840  1.00 28.07 ?  379 GLN B N   1 
ATOM   6052 C CA  . GLN B 1 379 ? -7.267  -2.241  49.909  1.00 27.04 ?  379 GLN B CA  1 
ATOM   6053 C C   . GLN B 1 379 ? -7.825  -0.952  49.317  1.00 29.95 ?  379 GLN B C   1 
ATOM   6054 O O   . GLN B 1 379 ? -8.923  -0.585  49.667  1.00 28.05 ?  379 GLN B O   1 
ATOM   6055 C CB  . GLN B 1 379 ? -6.334  -1.982  51.092  1.00 28.64 ?  379 GLN B CB  1 
ATOM   6056 C CG  . GLN B 1 379 ? -5.872  -3.235  51.821  1.00 32.81 ?  379 GLN B CG  1 
ATOM   6057 C CD  . GLN B 1 379 ? -6.905  -3.852  52.730  1.00 35.35 ?  379 GLN B CD  1 
ATOM   6058 O OE1 . GLN B 1 379 ? -7.889  -3.227  53.104  1.00 36.00 ?  379 GLN B OE1 1 
ATOM   6059 N NE2 . GLN B 1 379 ? -6.671  -5.097  53.103  1.00 38.37 ?  379 GLN B NE2 1 
ATOM   6060 N N   . ARG B 1 380 ? -7.078  -0.332  48.410  1.00 28.00 ?  380 ARG B N   1 
ATOM   6061 C CA  . ARG B 1 380 ? -7.542  0.925   47.770  1.00 29.93 ?  380 ARG B CA  1 
ATOM   6062 C C   . ARG B 1 380 ? -8.750  0.628   46.886  1.00 26.63 ?  380 ARG B C   1 
ATOM   6063 O O   . ARG B 1 380 ? -9.660  1.431   46.841  1.00 28.44 ?  380 ARG B O   1 
ATOM   6064 C CB  . ARG B 1 380 ? -6.435  1.563   46.932  1.00 25.71 ?  380 ARG B CB  1 
ATOM   6065 C CG  . ARG B 1 380 ? -5.336  2.235   47.737  1.00 25.93 ?  380 ARG B CG  1 
ATOM   6066 C CD  . ARG B 1 380 ? -4.335  2.854   46.794  1.00 26.26 ?  380 ARG B CD  1 
ATOM   6067 N NE  . ARG B 1 380 ? -3.012  2.989   47.368  1.00 28.85 ?  380 ARG B NE  1 
ATOM   6068 C CZ  . ARG B 1 380 ? -2.225  4.032   47.174  1.00 28.18 ?  380 ARG B CZ  1 
ATOM   6069 N NH1 . ARG B 1 380 ? -2.635  5.036   46.426  1.00 27.27 1  380 ARG B NH1 1 
ATOM   6070 N NH2 . ARG B 1 380 ? -1.029  4.064   47.725  1.00 31.26 ?  380 ARG B NH2 1 
ATOM   6071 N N   . LEU B 1 381 ? -8.729  -0.514  46.219  1.00 26.09 ?  381 LEU B N   1 
ATOM   6072 C CA  . LEU B 1 381 ? -9.898  -0.874  45.425  1.00 25.52 ?  381 LEU B CA  1 
ATOM   6073 C C   . LEU B 1 381 ? -11.138 -0.980  46.305  1.00 26.09 ?  381 LEU B C   1 
ATOM   6074 O O   . LEU B 1 381 ? -12.208 -0.474  45.955  1.00 24.90 ?  381 LEU B O   1 
ATOM   6075 C CB  . LEU B 1 381 ? -9.638  -2.194  44.691  1.00 25.40 ?  381 LEU B CB  1 
ATOM   6076 C CG  . LEU B 1 381 ? -10.779 -2.666  43.793  1.00 25.01 ?  381 LEU B CG  1 
ATOM   6077 C CD1 . LEU B 1 381 ? -11.156 -1.581  42.826  1.00 24.19 ?  381 LEU B CD1 1 
ATOM   6078 C CD2 . LEU B 1 381 ? -10.321 -3.915  43.041  1.00 22.51 ?  381 LEU B CD2 1 
ATOM   6079 N N   . LYS B 1 382 ? -11.017 -1.644  47.445  1.00 28.90 ?  382 LYS B N   1 
ATOM   6080 C CA  . LYS B 1 382 ? -12.179 -1.729  48.365  1.00 26.31 ?  382 LYS B CA  1 
ATOM   6081 C C   . LYS B 1 382 ? -12.582 -0.321  48.789  1.00 27.44 ?  382 LYS B C   1 
ATOM   6082 O O   . LYS B 1 382 ? -13.768 -0.038  48.851  1.00 26.92 ?  382 LYS B O   1 
ATOM   6083 C CB  . LYS B 1 382 ? -11.879 -2.531  49.626  1.00 31.17 ?  382 LYS B CB  1 
ATOM   6084 C CG  . LYS B 1 382 ? -13.111 -2.935  50.418  1.00 30.35 ?  382 LYS B CG  1 
ATOM   6085 C CD  . LYS B 1 382 ? -12.795 -3.706  51.666  1.00 32.41 ?  382 LYS B CD  1 
ATOM   6086 C CE  . LYS B 1 382 ? -14.011 -3.892  52.545  1.00 35.98 ?  382 LYS B CE  1 
ATOM   6087 N NZ  . LYS B 1 382 ? -13.673 -4.649  53.768  1.00 40.32 1  382 LYS B NZ  1 
ATOM   6088 N N   . GLN B 1 383 ? -11.586 0.492   49.117  1.00 30.00 ?  383 GLN B N   1 
ATOM   6089 C CA  . GLN B 1 383 ? -11.856 1.884   49.554  1.00 31.85 ?  383 GLN B CA  1 
ATOM   6090 C C   . GLN B 1 383 ? -12.707 2.562   48.469  1.00 31.78 ?  383 GLN B C   1 
ATOM   6091 O O   . GLN B 1 383 ? -13.686 3.195   48.807  1.00 37.78 ?  383 GLN B O   1 
ATOM   6092 C CB  . GLN B 1 383 ? -10.569 2.703   49.707  1.00 30.54 ?  383 GLN B CB  1 
ATOM   6093 C CG  . GLN B 1 383 ? -9.691  2.481   50.926  1.00 35.30 ?  383 GLN B CG  1 
ATOM   6094 C CD  . GLN B 1 383 ? -8.628  3.558   51.007  1.00 41.20 ?  383 GLN B CD  1 
ATOM   6095 O OE1 . GLN B 1 383 ? -8.112  4.023   49.995  1.00 41.58 ?  383 GLN B OE1 1 
ATOM   6096 N NE2 . GLN B 1 383 ? -8.286  3.958   52.219  1.00 45.60 ?  383 GLN B NE2 1 
ATOM   6097 N N   . GLY B 1 384 ? -12.346 2.392   47.197  1.00 30.74 ?  384 GLY B N   1 
ATOM   6098 C CA  . GLY B 1 384 ? -13.079 3.109   46.141  1.00 30.05 ?  384 GLY B CA  1 
ATOM   6099 C C   . GLY B 1 384 ? -14.490 2.588   45.961  1.00 33.35 ?  384 GLY B C   1 
ATOM   6100 O O   . GLY B 1 384 ? -15.372 3.387   45.689  1.00 32.53 ?  384 GLY B O   1 
ATOM   6101 N N   . VAL B 1 385 ? -14.657 1.276   46.065  1.00 26.90 ?  385 VAL B N   1 
ATOM   6102 C CA  . VAL B 1 385 ? -15.991 0.698   45.960  1.00 30.62 ?  385 VAL B CA  1 
ATOM   6103 C C   . VAL B 1 385 ? -16.857 1.128   47.140  1.00 35.97 ?  385 VAL B C   1 
ATOM   6104 O O   . VAL B 1 385 ? -18.026 1.500   46.967  1.00 39.30 ?  385 VAL B O   1 
ATOM   6105 C CB  . VAL B 1 385 ? -15.894 -0.835  45.855  1.00 33.33 ?  385 VAL B CB  1 
ATOM   6106 C CG1 . VAL B 1 385 ? -17.260 -1.473  46.089  1.00 32.43 ?  385 VAL B CG1 1 
ATOM   6107 C CG2 . VAL B 1 385 ? -15.312 -1.241  44.499  1.00 27.32 ?  385 VAL B CG2 1 
ATOM   6108 N N   . LEU B 1 386 ? -16.305 1.073   48.356  1.00 36.58 ?  386 LEU B N   1 
ATOM   6109 C CA  . LEU B 1 386 ? -17.044 1.544   49.526  1.00 39.91 ?  386 LEU B CA  1 
ATOM   6110 C C   . LEU B 1 386 ? -17.465 3.000   49.361  1.00 42.25 ?  386 LEU B C   1 
ATOM   6111 O O   . LEU B 1 386 ? -18.605 3.364   49.679  1.00 47.19 ?  386 LEU B O   1 
ATOM   6112 C CB  . LEU B 1 386 ? -16.196 1.372   50.791  1.00 38.32 ?  386 LEU B CB  1 
ATOM   6113 C CG  . LEU B 1 386 ? -16.259 -0.006  51.454  1.00 41.03 ?  386 LEU B CG  1 
ATOM   6114 C CD1 . LEU B 1 386 ? -15.329 -0.087  52.652  1.00 40.43 ?  386 LEU B CD1 1 
ATOM   6115 C CD2 . LEU B 1 386 ? -17.689 -0.372  51.855  1.00 44.84 ?  386 LEU B CD2 1 
ATOM   6116 N N   . ASN B 1 387 ? -16.578 3.831   48.818  1.00 38.43 ?  387 ASN B N   1 
ATOM   6117 C CA  . ASN B 1 387 ? -16.849 5.276   48.592  1.00 42.62 ?  387 ASN B CA  1 
ATOM   6118 C C   . ASN B 1 387 ? -18.004 5.448   47.598  1.00 45.81 ?  387 ASN B C   1 
ATOM   6119 O O   . ASN B 1 387 ? -18.601 6.530   47.584  1.00 43.90 ?  387 ASN B O   1 
ATOM   6120 C CB  . ASN B 1 387 ? -15.643 5.975   47.949  1.00 43.44 ?  387 ASN B CB  1 
ATOM   6121 C CG  . ASN B 1 387 ? -14.674 6.673   48.879  1.00 50.19 ?  387 ASN B CG  1 
ATOM   6122 O OD1 . ASN B 1 387 ? -15.024 7.647   49.536  1.00 50.35 ?  387 ASN B OD1 1 
ATOM   6123 N ND2 . ASN B 1 387 ? -13.429 6.227   48.892  1.00 45.85 ?  387 ASN B ND2 1 
ATOM   6124 N N   . LEU B 1 388 ? -18.309 4.420   46.803  1.00 43.76 ?  388 LEU B N   1 
ATOM   6125 C CA  . LEU B 1 388 ? -19.385 4.535   45.827  1.00 43.13 ?  388 LEU B CA  1 
ATOM   6126 C C   . LEU B 1 388 ? -20.749 4.248   46.445  1.00 50.35 ?  388 LEU B C   1 
ATOM   6127 O O   . LEU B 1 388 ? -21.720 4.953   46.152  1.00 56.30 ?  388 LEU B O   1 
ATOM   6128 C CB  . LEU B 1 388 ? -19.137 3.586   44.658  1.00 43.83 ?  388 LEU B CB  1 
ATOM   6129 C CG  . LEU B 1 388 ? -18.517 4.128   43.373  1.00 46.31 ?  388 LEU B CG  1 
ATOM   6130 C CD1 . LEU B 1 388 ? -18.230 2.963   42.435  1.00 43.88 ?  388 LEU B CD1 1 
ATOM   6131 C CD2 . LEU B 1 388 ? -19.423 5.147   42.689  1.00 44.43 ?  388 LEU B CD2 1 
ATOM   6132 N N   . ASN B 1 389 ? -20.842 3.222   47.293  1.00 49.76 ?  389 ASN B N   1 
ATOM   6133 C CA  . ASN B 1 389 ? -22.111 2.779   47.867  1.00 52.48 ?  389 ASN B CA  1 
ATOM   6134 C C   . ASN B 1 389 ? -22.581 3.627   49.045  1.00 57.27 ?  389 ASN B C   1 
ATOM   6135 O O   . ASN B 1 389 ? -23.538 3.224   49.718  1.00 62.70 ?  389 ASN B O   1 
ATOM   6136 C CB  . ASN B 1 389 ? -22.008 1.322   48.336  1.00 52.91 ?  389 ASN B CB  1 
ATOM   6137 C CG  . ASN B 1 389 ? -21.365 0.411   47.308  1.00 51.53 ?  389 ASN B CG  1 
ATOM   6138 O OD1 . ASN B 1 389 ? -21.436 0.657   46.107  1.00 54.21 ?  389 ASN B OD1 1 
ATOM   6139 N ND2 . ASN B 1 389 ? -20.740 -0.661  47.783  1.00 49.44 ?  389 ASN B ND2 1 
ATOM   6140 N N   . ASN B 1 390 ? -21.954 4.766   49.325  1.00 54.78 ?  390 ASN B N   1 
ATOM   6141 C CA  . ASN B 1 390 ? -22.192 5.441   50.603  1.00 59.27 ?  390 ASN B CA  1 
ATOM   6142 C C   . ASN B 1 390 ? -22.972 6.751   50.493  1.00 64.31 ?  390 ASN B C   1 
ATOM   6143 O O   . ASN B 1 390 ? -22.867 7.477   49.501  1.00 60.46 ?  390 ASN B O   1 
ATOM   6144 C CB  . ASN B 1 390 ? -20.858 5.701   51.305  1.00 57.04 ?  390 ASN B CB  1 
ATOM   6145 C CG  . ASN B 1 390 ? -20.609 4.744   52.454  1.00 60.51 ?  390 ASN B CG  1 
ATOM   6146 O OD1 . ASN B 1 390 ? -21.544 4.316   53.134  1.00 65.30 ?  390 ASN B OD1 1 
ATOM   6147 N ND2 . ASN B 1 390 ? -19.343 4.403   52.677  1.00 56.49 ?  390 ASN B ND2 1 
ATOM   6148 O OXT . ASN B 1 390 ? -23.719 7.112   51.415  1.00 63.80 -1 390 ASN B OXT 1 
HETATM 6149 O O   . HOH C 2 .   ? 53.965  -8.679  -9.703  1.00 51.92 ?  401 HOH A O   1 
HETATM 6150 O O   . HOH C 2 .   ? -0.073  17.288  6.882   1.00 32.39 ?  402 HOH A O   1 
HETATM 6151 O O   . HOH C 2 .   ? 17.336  -0.452  -3.944  1.00 41.14 ?  403 HOH A O   1 
HETATM 6152 O O   . HOH C 2 .   ? 6.587   17.875  -7.925  1.00 25.91 ?  404 HOH A O   1 
HETATM 6153 O O   . HOH C 2 .   ? 2.248   5.110   8.296   1.00 37.62 ?  405 HOH A O   1 
HETATM 6154 O O   . HOH C 2 .   ? 30.191  -3.336  14.919  1.00 28.96 ?  406 HOH A O   1 
HETATM 6155 O O   . HOH C 2 .   ? 24.265  21.091  24.920  1.00 32.50 ?  407 HOH A O   1 
HETATM 6156 O O   . HOH C 2 .   ? 0.759   10.221  -1.617  1.00 39.09 ?  408 HOH A O   1 
HETATM 6157 O O   . HOH C 2 .   ? 21.373  32.133  22.607  1.00 36.11 ?  409 HOH A O   1 
HETATM 6158 O O   . HOH C 2 .   ? 19.096  6.056   -8.868  1.00 32.06 ?  410 HOH A O   1 
HETATM 6159 O O   . HOH C 2 .   ? 42.137  17.588  8.138   1.00 38.74 ?  411 HOH A O   1 
HETATM 6160 O O   . HOH C 2 .   ? 24.950  11.528  14.266  1.00 24.53 ?  412 HOH A O   1 
HETATM 6161 O O   . HOH C 2 .   ? 34.299  -5.767  8.155   1.00 38.05 ?  413 HOH A O   1 
HETATM 6162 O O   . HOH C 2 .   ? 1.965   11.032  -7.857  1.00 31.49 ?  414 HOH A O   1 
HETATM 6163 O O   . HOH C 2 .   ? 10.812  2.054   19.082  1.00 28.45 ?  415 HOH A O   1 
HETATM 6164 O O   . HOH C 2 .   ? 37.141  8.273   23.151  1.00 28.69 ?  416 HOH A O   1 
HETATM 6165 O O   . HOH C 2 .   ? -0.006  4.406   -5.992  1.00 38.25 ?  417 HOH A O   1 
HETATM 6166 O O   . HOH C 2 .   ? 29.397  20.620  15.913  1.00 42.13 ?  418 HOH A O   1 
HETATM 6167 O O   . HOH C 2 .   ? 22.923  17.828  15.253  1.00 29.69 ?  419 HOH A O   1 
HETATM 6168 O O   . HOH C 2 .   ? 38.704  -2.876  0.026   1.00 35.42 ?  420 HOH A O   1 
HETATM 6169 O O   . HOH C 2 .   ? 0.928   6.538   1.104   1.00 32.66 ?  421 HOH A O   1 
HETATM 6170 O O   . HOH C 2 .   ? 22.563  9.023   6.568   1.00 27.97 ?  422 HOH A O   1 
HETATM 6171 O O   . HOH C 2 .   ? -1.928  6.979   7.646   1.00 28.32 ?  423 HOH A O   1 
HETATM 6172 O O   . HOH C 2 .   ? 39.363  1.182   11.275  1.00 29.73 ?  424 HOH A O   1 
HETATM 6173 O O   . HOH C 2 .   ? 26.718  11.817  32.064  1.00 32.06 ?  425 HOH A O   1 
HETATM 6174 O O   . HOH C 2 .   ? 20.959  19.829  12.565  1.00 28.65 ?  426 HOH A O   1 
HETATM 6175 O O   . HOH C 2 .   ? 22.887  15.286  16.421  1.00 26.28 ?  427 HOH A O   1 
HETATM 6176 O O   . HOH C 2 .   ? 29.786  7.041   14.336  1.00 25.33 ?  428 HOH A O   1 
HETATM 6177 O O   . HOH C 2 .   ? 25.652  26.321  6.169   1.00 31.95 ?  429 HOH A O   1 
HETATM 6178 O O   . HOH C 2 .   ? 19.702  5.168   37.529  1.00 34.17 ?  430 HOH A O   1 
HETATM 6179 O O   . HOH C 2 .   ? 6.984   -2.250  11.849  1.00 21.98 ?  431 HOH A O   1 
HETATM 6180 O O   . HOH C 2 .   ? 27.314  3.369   2.955   1.00 34.82 ?  432 HOH A O   1 
HETATM 6181 O O   . HOH C 2 .   ? 15.909  26.711  -10.732 1.00 39.21 ?  433 HOH A O   1 
HETATM 6182 O O   . HOH C 2 .   ? 13.875  25.827  21.954  1.00 34.30 ?  434 HOH A O   1 
HETATM 6183 O O   . HOH C 2 .   ? 21.021  18.175  -7.382  1.00 31.58 ?  435 HOH A O   1 
HETATM 6184 O O   . HOH C 2 .   ? 32.309  15.511  26.363  1.00 31.69 ?  436 HOH A O   1 
HETATM 6185 O O   . HOH C 2 .   ? 12.392  7.535   -11.697 1.00 32.89 ?  437 HOH A O   1 
HETATM 6186 O O   . HOH C 2 .   ? 21.455  9.721   -12.209 1.00 41.52 ?  438 HOH A O   1 
HETATM 6187 O O   . HOH C 2 .   ? 38.499  -7.109  -11.120 1.00 39.88 ?  439 HOH A O   1 
HETATM 6188 O O   . HOH C 2 .   ? 21.877  18.948  -9.854  1.00 33.78 ?  440 HOH A O   1 
HETATM 6189 O O   . HOH C 2 .   ? -0.676  10.681  5.200   1.00 30.14 ?  441 HOH A O   1 
HETATM 6190 O O   . HOH C 2 .   ? 5.321   3.313   22.979  1.00 43.15 ?  442 HOH A O   1 
HETATM 6191 O O   . HOH C 2 .   ? 8.110   9.095   18.977  1.00 26.07 ?  443 HOH A O   1 
HETATM 6192 O O   . HOH C 2 .   ? 10.977  14.824  -14.501 1.00 35.74 ?  444 HOH A O   1 
HETATM 6193 O O   . HOH C 2 .   ? 50.617  -1.660  6.649   1.00 44.12 ?  445 HOH A O   1 
HETATM 6194 O O   . HOH C 2 .   ? 13.690  1.560   33.673  1.00 22.34 ?  446 HOH A O   1 
HETATM 6195 O O   . HOH C 2 .   ? 13.113  1.041   31.025  1.00 22.99 ?  447 HOH A O   1 
HETATM 6196 O O   . HOH C 2 .   ? 6.287   -0.249  2.237   1.00 35.65 ?  448 HOH A O   1 
HETATM 6197 O O   . HOH C 2 .   ? 21.004  -1.757  40.908  1.00 38.59 ?  449 HOH A O   1 
HETATM 6198 O O   . HOH C 2 .   ? 21.475  2.468   13.706  1.00 33.60 ?  450 HOH A O   1 
HETATM 6199 O O   . HOH C 2 .   ? 16.305  -0.661  19.669  1.00 25.47 ?  451 HOH A O   1 
HETATM 6200 O O   . HOH C 2 .   ? 15.865  5.248   27.351  1.00 24.41 ?  452 HOH A O   1 
HETATM 6201 O O   . HOH C 2 .   ? 26.324  -0.029  41.544  1.00 41.07 ?  453 HOH A O   1 
HETATM 6202 O O   . HOH C 2 .   ? 47.677  17.286  5.013   1.00 44.92 ?  454 HOH A O   1 
HETATM 6203 O O   . HOH C 2 .   ? 23.960  14.481  6.956   1.00 23.06 ?  455 HOH A O   1 
HETATM 6204 O O   . HOH C 2 .   ? 42.514  -10.378 3.196   1.00 43.97 ?  456 HOH A O   1 
HETATM 6205 O O   . HOH C 2 .   ? 39.229  4.837   21.836  1.00 29.37 ?  457 HOH A O   1 
HETATM 6206 O O   . HOH C 2 .   ? 10.280  1.359   26.169  1.00 26.35 ?  458 HOH A O   1 
HETATM 6207 O O   . HOH C 2 .   ? 45.090  8.338   17.165  1.00 39.25 ?  459 HOH A O   1 
HETATM 6208 O O   . HOH C 2 .   ? 21.567  11.453  30.889  1.00 30.83 ?  460 HOH A O   1 
HETATM 6209 O O   . HOH C 2 .   ? 26.758  -8.378  21.630  1.00 24.79 ?  461 HOH A O   1 
HETATM 6210 O O   . HOH C 2 .   ? 21.309  7.491   33.470  1.00 23.82 ?  462 HOH A O   1 
HETATM 6211 O O   . HOH C 2 .   ? 6.778   5.671   24.557  1.00 33.57 ?  463 HOH A O   1 
HETATM 6212 O O   . HOH C 2 .   ? 27.132  14.327  13.012  1.00 23.50 ?  464 HOH A O   1 
HETATM 6213 O O   . HOH C 2 .   ? 37.197  -3.863  17.540  1.00 46.86 ?  465 HOH A O   1 
HETATM 6214 O O   . HOH C 2 .   ? 31.172  18.761  27.396  1.00 34.15 ?  466 HOH A O   1 
HETATM 6215 O O   . HOH C 2 .   ? 30.434  -5.638  20.585  1.00 26.67 ?  467 HOH A O   1 
HETATM 6216 O O   . HOH C 2 .   ? 43.960  -0.431  19.878  1.00 36.31 ?  468 HOH A O   1 
HETATM 6217 O O   . HOH C 2 .   ? 24.523  22.828  5.860   1.00 29.88 ?  469 HOH A O   1 
HETATM 6218 O O   . HOH C 2 .   ? -5.057  19.724  8.220   1.00 40.32 ?  470 HOH A O   1 
HETATM 6219 O O   . HOH C 2 .   ? 7.702   21.272  8.642   1.00 23.44 ?  471 HOH A O   1 
HETATM 6220 O O   . HOH C 2 .   ? 29.501  20.278  12.782  1.00 34.52 ?  472 HOH A O   1 
HETATM 6221 O O   . HOH C 2 .   ? 34.513  25.180  -13.331 1.00 41.15 ?  473 HOH A O   1 
HETATM 6222 O O   . HOH C 2 .   ? 33.972  4.405   4.246   1.00 30.94 ?  474 HOH A O   1 
HETATM 6223 O O   . HOH C 2 .   ? 3.739   24.222  18.849  1.00 37.45 ?  475 HOH A O   1 
HETATM 6224 O O   . HOH C 2 .   ? 15.083  3.270   20.851  1.00 21.04 ?  476 HOH A O   1 
HETATM 6225 O O   . HOH C 2 .   ? 39.770  20.352  22.108  1.00 43.73 ?  477 HOH A O   1 
HETATM 6226 O O   . HOH C 2 .   ? 31.125  9.340   21.953  1.00 23.96 ?  478 HOH A O   1 
HETATM 6227 O O   . HOH C 2 .   ? 42.018  9.459   -9.820  1.00 45.06 ?  479 HOH A O   1 
HETATM 6228 O O   . HOH C 2 .   ? 22.892  17.863  12.510  1.00 28.14 ?  480 HOH A O   1 
HETATM 6229 O O   . HOH C 2 .   ? 21.572  6.524   -11.239 1.00 40.08 ?  481 HOH A O   1 
HETATM 6230 O O   . HOH C 2 .   ? 38.082  19.552  -14.145 1.00 50.55 ?  482 HOH A O   1 
HETATM 6231 O O   . HOH C 2 .   ? 1.881   3.856   1.347   1.00 32.32 ?  483 HOH A O   1 
HETATM 6232 O O   . HOH C 2 .   ? 21.692  15.585  -0.849  1.00 25.76 ?  484 HOH A O   1 
HETATM 6233 O O   . HOH C 2 .   ? 37.314  13.587  1.287   1.00 35.85 ?  485 HOH A O   1 
HETATM 6234 O O   . HOH C 2 .   ? 6.789   2.931   18.233  1.00 29.46 ?  486 HOH A O   1 
HETATM 6235 O O   . HOH C 2 .   ? 30.678  -2.030  17.787  1.00 31.27 ?  487 HOH A O   1 
HETATM 6236 O O   . HOH C 2 .   ? 10.251  1.009   -6.665  1.00 32.07 ?  488 HOH A O   1 
HETATM 6237 O O   . HOH C 2 .   ? 3.969   1.638   1.165   1.00 27.00 ?  489 HOH A O   1 
HETATM 6238 O O   . HOH C 2 .   ? 3.471   2.716   7.000   1.00 26.31 ?  490 HOH A O   1 
HETATM 6239 O O   . HOH C 2 .   ? 20.196  13.520  -1.951  1.00 24.80 ?  491 HOH A O   1 
HETATM 6240 O O   . HOH C 2 .   ? 31.563  -12.368 21.802  1.00 40.10 ?  492 HOH A O   1 
HETATM 6241 O O   . HOH C 2 .   ? 4.118   -4.194  24.179  1.00 33.73 ?  493 HOH A O   1 
HETATM 6242 O O   . HOH C 2 .   ? 5.646   7.892   17.907  1.00 27.36 ?  494 HOH A O   1 
HETATM 6243 O O   . HOH C 2 .   ? 6.487   10.618  20.632  1.00 29.68 ?  495 HOH A O   1 
HETATM 6244 O O   . HOH C 2 .   ? 28.500  3.472   15.682  1.00 23.67 ?  496 HOH A O   1 
HETATM 6245 O O   . HOH C 2 .   ? 22.271  -0.292  0.063   1.00 36.16 ?  497 HOH A O   1 
HETATM 6246 O O   . HOH C 2 .   ? 33.128  17.520  -0.965  1.00 44.88 ?  498 HOH A O   1 
HETATM 6247 O O   . HOH C 2 .   ? 13.984  3.647   -8.536  1.00 26.66 ?  499 HOH A O   1 
HETATM 6248 O O   . HOH C 2 .   ? 7.837   17.581  21.366  1.00 31.22 ?  500 HOH A O   1 
HETATM 6249 O O   . HOH C 2 .   ? 14.431  30.152  11.705  1.00 45.19 ?  501 HOH A O   1 
HETATM 6250 O O   . HOH C 2 .   ? 9.273   29.095  -1.931  1.00 44.15 ?  502 HOH A O   1 
HETATM 6251 O O   . HOH C 2 .   ? 20.756  14.494  -13.356 1.00 36.77 ?  503 HOH A O   1 
HETATM 6252 O O   . HOH C 2 .   ? 11.809  30.444  -7.384  1.00 47.92 ?  504 HOH A O   1 
HETATM 6253 O O   . HOH C 2 .   ? 44.476  -12.606 1.559   1.00 36.89 ?  505 HOH A O   1 
HETATM 6254 O O   . HOH C 2 .   ? 32.976  -12.995 14.880  1.00 46.92 ?  506 HOH A O   1 
HETATM 6255 O O   . HOH C 2 .   ? 28.882  -6.494  18.894  1.00 32.26 ?  507 HOH A O   1 
HETATM 6256 O O   . HOH C 2 .   ? 27.304  5.396   5.644   1.00 38.54 ?  508 HOH A O   1 
HETATM 6257 O O   . HOH C 2 .   ? 27.976  5.099   13.669  1.00 25.11 ?  509 HOH A O   1 
HETATM 6258 O O   . HOH C 2 .   ? 42.661  -15.700 9.032   1.00 42.21 ?  510 HOH A O   1 
HETATM 6259 O O   . HOH C 2 .   ? 6.365   9.283   32.013  1.00 34.91 ?  511 HOH A O   1 
HETATM 6260 O O   . HOH C 2 .   ? 25.364  31.120  1.690   1.00 38.40 ?  512 HOH A O   1 
HETATM 6261 O O   . HOH C 2 .   ? 37.740  2.897   10.115  1.00 31.65 ?  513 HOH A O   1 
HETATM 6262 O O   . HOH C 2 .   ? 18.164  14.059  -16.372 1.00 41.44 ?  514 HOH A O   1 
HETATM 6263 O O   . HOH C 2 .   ? 26.824  29.009  5.113   1.00 36.01 ?  515 HOH A O   1 
HETATM 6264 O O   . HOH C 2 .   ? 5.177   3.563   9.315   1.00 27.65 ?  516 HOH A O   1 
HETATM 6265 O O   . HOH C 2 .   ? 4.337   -0.633  16.535  1.00 31.97 ?  517 HOH A O   1 
HETATM 6266 O O   . HOH C 2 .   ? 22.956  14.234  13.630  1.00 26.59 ?  518 HOH A O   1 
HETATM 6267 O O   . HOH C 2 .   ? 21.428  5.236   16.892  1.00 30.15 ?  519 HOH A O   1 
HETATM 6268 O O   . HOH C 2 .   ? 19.526  5.229   10.927  1.00 30.37 ?  520 HOH A O   1 
HETATM 6269 O O   . HOH C 2 .   ? 50.653  1.522   11.989  1.00 39.16 ?  521 HOH A O   1 
HETATM 6270 O O   . HOH C 2 .   ? 22.814  27.553  11.526  1.00 37.89 ?  522 HOH A O   1 
HETATM 6271 O O   . HOH C 2 .   ? 17.323  10.316  -12.578 1.00 41.05 ?  523 HOH A O   1 
HETATM 6272 O O   . HOH C 2 .   ? 0.692   9.461   17.720  1.00 36.83 ?  524 HOH A O   1 
HETATM 6273 O O   . HOH C 2 .   ? 26.062  -0.385  35.721  1.00 37.40 ?  525 HOH A O   1 
HETATM 6274 O O   . HOH C 2 .   ? 17.065  1.188   -9.766  1.00 41.35 ?  526 HOH A O   1 
HETATM 6275 O O   . HOH C 2 .   ? 4.466   13.126  -13.491 1.00 33.14 ?  527 HOH A O   1 
HETATM 6276 O O   . HOH C 2 .   ? 6.364   10.015  25.262  1.00 31.91 ?  528 HOH A O   1 
HETATM 6277 O O   . HOH C 2 .   ? 6.057   3.956   -15.420 1.00 41.99 ?  529 HOH A O   1 
HETATM 6278 O O   . HOH C 2 .   ? 10.979  1.074   33.932  1.00 30.74 ?  530 HOH A O   1 
HETATM 6279 O O   . HOH C 2 .   ? 7.471   7.197   23.091  1.00 35.01 ?  531 HOH A O   1 
HETATM 6280 O O   . HOH C 2 .   ? -1.922  12.039  2.777   1.00 33.83 ?  532 HOH A O   1 
HETATM 6281 O O   . HOH C 2 .   ? 0.599   12.059  16.607  1.00 35.15 ?  533 HOH A O   1 
HETATM 6282 O O   . HOH C 2 .   ? 22.382  16.806  -13.357 1.00 49.22 ?  534 HOH A O   1 
HETATM 6283 O O   . HOH C 2 .   ? 28.113  3.118   6.261   1.00 37.06 ?  535 HOH A O   1 
HETATM 6284 O O   . HOH C 2 .   ? 16.086  -1.814  -6.966  1.00 38.52 ?  536 HOH A O   1 
HETATM 6285 O O   . HOH C 2 .   ? 15.531  -2.318  0.045   1.00 31.24 ?  537 HOH A O   1 
HETATM 6286 O O   . HOH C 2 .   ? 30.438  11.999  3.733   1.00 29.40 ?  538 HOH A O   1 
HETATM 6287 O O   . HOH C 2 .   ? 32.145  -1.967  -0.969  1.00 39.40 ?  539 HOH A O   1 
HETATM 6288 O O   . HOH C 2 .   ? 5.390   17.293  19.702  1.00 36.31 ?  540 HOH A O   1 
HETATM 6289 O O   . HOH C 2 .   ? 17.432  31.576  9.018   1.00 32.68 ?  541 HOH A O   1 
HETATM 6290 O O   . HOH C 2 .   ? 2.455   26.353  10.655  1.00 49.43 ?  542 HOH A O   1 
HETATM 6291 O O   . HOH C 2 .   ? 20.265  6.887   13.441  1.00 24.67 ?  543 HOH A O   1 
HETATM 6292 O O   . HOH C 2 .   ? 0.511   23.654  8.138   1.00 44.52 ?  544 HOH A O   1 
HETATM 6293 O O   . HOH C 2 .   ? 37.580  10.225  -14.472 1.00 50.00 ?  545 HOH A O   1 
HETATM 6294 O O   . HOH C 2 .   ? 43.714  -4.828  12.049  1.00 41.91 ?  546 HOH A O   1 
HETATM 6295 O O   . HOH C 2 .   ? 7.213   -5.122  25.279  1.00 29.26 ?  547 HOH A O   1 
HETATM 6296 O O   . HOH C 2 .   ? 50.449  -8.294  -12.668 1.00 52.44 ?  548 HOH A O   1 
HETATM 6297 O O   . HOH C 2 .   ? 45.606  13.772  -2.055  1.00 45.47 ?  549 HOH A O   1 
HETATM 6298 O O   . HOH C 2 .   ? 9.276   -4.890  0.372   1.00 38.11 ?  550 HOH A O   1 
HETATM 6299 O O   . HOH C 2 .   ? 22.613  4.699   12.793  1.00 33.78 ?  551 HOH A O   1 
HETATM 6300 O O   . HOH C 2 .   ? -2.047  11.841  13.116  1.00 35.18 ?  552 HOH A O   1 
HETATM 6301 O O   . HOH C 2 .   ? 26.363  29.100  8.894   1.00 46.05 ?  553 HOH A O   1 
HETATM 6302 O O   . HOH C 2 .   ? 12.267  1.602   -8.353  1.00 33.28 ?  554 HOH A O   1 
HETATM 6303 O O   . HOH C 2 .   ? 39.109  -5.138  17.831  1.00 56.59 ?  555 HOH A O   1 
HETATM 6304 O O   . HOH C 2 .   ? 21.818  15.870  -15.387 1.00 47.34 ?  556 HOH A O   1 
HETATM 6305 O O   . HOH C 2 .   ? 0.000   11.329  0.000   0.50 34.66 ?  557 HOH A O   1 
HETATM 6306 O O   . HOH C 2 .   ? 24.492  29.751  10.921  1.00 41.07 ?  558 HOH A O   1 
HETATM 6307 O O   . HOH C 2 .   ? -1.593  10.220  10.747  1.00 30.49 ?  559 HOH A O   1 
HETATM 6308 O O   . HOH C 2 .   ? 11.515  5.518   -12.975 1.00 47.12 ?  560 HOH A O   1 
HETATM 6309 O O   . HOH C 2 .   ? 28.270  0.684   4.315   1.00 40.63 ?  561 HOH A O   1 
HETATM 6310 O O   . HOH C 2 .   ? 8.023   -2.981  21.392  1.00 32.14 ?  562 HOH A O   1 
HETATM 6311 O O   . HOH C 2 .   ? 2.545   16.336  1.314   1.00 40.98 ?  563 HOH A O   1 
HETATM 6312 O O   . HOH C 2 .   ? 0.000   2.232   0.000   0.50 30.02 ?  564 HOH A O   1 
HETATM 6313 O O   . HOH C 2 .   ? 43.461  -3.240  16.031  1.00 42.37 ?  565 HOH A O   1 
HETATM 6314 O O   . HOH D 2 .   ? -10.316 -15.242 4.442   1.00 23.16 ?  401 HOH B O   1 
HETATM 6315 O O   . HOH D 2 .   ? -14.617 -15.668 43.140  1.00 41.73 ?  402 HOH B O   1 
HETATM 6316 O O   . HOH D 2 .   ? -14.405 -16.767 35.898  1.00 37.74 ?  403 HOH B O   1 
HETATM 6317 O O   . HOH D 2 .   ? 8.459   2.075   33.037  1.00 28.59 ?  404 HOH B O   1 
HETATM 6318 O O   . HOH D 2 .   ? 2.075   0.562   48.158  1.00 38.76 ?  405 HOH B O   1 
HETATM 6319 O O   . HOH D 2 .   ? 10.149  -17.278 -3.075  1.00 32.65 ?  406 HOH B O   1 
HETATM 6320 O O   . HOH D 2 .   ? 19.092  -13.662 11.625  1.00 37.99 ?  407 HOH B O   1 
HETATM 6321 O O   . HOH D 2 .   ? 14.302  -10.002 41.299  1.00 25.92 ?  408 HOH B O   1 
HETATM 6322 O O   . HOH D 2 .   ? -3.380  -3.954  34.184  1.00 22.66 ?  409 HOH B O   1 
HETATM 6323 O O   . HOH D 2 .   ? -20.354 -8.988  29.189  1.00 38.44 ?  410 HOH B O   1 
HETATM 6324 O O   . HOH D 2 .   ? 7.489   -8.178  49.612  1.00 41.53 ?  411 HOH B O   1 
HETATM 6325 O O   . HOH D 2 .   ? 5.366   -16.186 1.076   1.00 32.74 ?  412 HOH B O   1 
HETATM 6326 O O   . HOH D 2 .   ? 3.223   -18.329 50.123  1.00 44.27 ?  413 HOH B O   1 
HETATM 6327 O O   . HOH D 2 .   ? 1.118   5.484   36.160  1.00 34.13 ?  414 HOH B O   1 
HETATM 6328 O O   . HOH D 2 .   ? -13.133 -3.633  16.773  1.00 31.45 ?  415 HOH B O   1 
HETATM 6329 O O   . HOH D 2 .   ? -15.370 -15.829 19.044  1.00 53.23 ?  416 HOH B O   1 
HETATM 6330 O O   . HOH D 2 .   ? -9.495  -1.498  52.121  1.00 33.61 ?  417 HOH B O   1 
HETATM 6331 O O   . HOH D 2 .   ? -15.437 -10.648 44.674  1.00 28.26 ?  418 HOH B O   1 
HETATM 6332 O O   . HOH D 2 .   ? -11.331 -22.300 27.063  1.00 44.75 ?  419 HOH B O   1 
HETATM 6333 O O   . HOH D 2 .   ? 7.026   -6.419  27.459  1.00 24.94 ?  420 HOH B O   1 
HETATM 6334 O O   . HOH D 2 .   ? 8.024   11.506  36.446  1.00 37.03 ?  421 HOH B O   1 
HETATM 6335 O O   . HOH D 2 .   ? 21.800  -13.713 11.751  1.00 32.28 ?  422 HOH B O   1 
HETATM 6336 O O   . HOH D 2 .   ? -3.158  -2.636  27.834  1.00 27.22 ?  423 HOH B O   1 
HETATM 6337 O O   . HOH D 2 .   ? -7.183  2.374   16.528  1.00 32.54 ?  424 HOH B O   1 
HETATM 6338 O O   . HOH D 2 .   ? -5.424  -17.773 51.929  1.00 33.84 ?  425 HOH B O   1 
HETATM 6339 O O   . HOH D 2 .   ? 21.732  -0.631  14.387  1.00 29.32 ?  426 HOH B O   1 
HETATM 6340 O O   . HOH D 2 .   ? 12.445  -23.308 7.317   1.00 34.62 ?  427 HOH B O   1 
HETATM 6341 O O   . HOH D 2 .   ? 17.407  -22.456 28.164  1.00 32.91 ?  428 HOH B O   1 
HETATM 6342 O O   . HOH D 2 .   ? -5.079  10.579  42.636  1.00 33.37 ?  429 HOH B O   1 
HETATM 6343 O O   . HOH D 2 .   ? 23.437  -19.741 22.860  1.00 35.21 ?  430 HOH B O   1 
HETATM 6344 O O   . HOH D 2 .   ? -12.615 1.241   14.815  1.00 36.49 ?  431 HOH B O   1 
HETATM 6345 O O   . HOH D 2 .   ? 8.327   -18.252 25.159  1.00 26.58 ?  432 HOH B O   1 
HETATM 6346 O O   . HOH D 2 .   ? 25.193  -13.879 32.547  1.00 36.67 ?  433 HOH B O   1 
HETATM 6347 O O   . HOH D 2 .   ? -0.101  -15.590 51.045  1.00 37.92 ?  434 HOH B O   1 
HETATM 6348 O O   . HOH D 2 .   ? 6.366   10.017  39.313  1.00 41.00 ?  435 HOH B O   1 
HETATM 6349 O O   . HOH D 2 .   ? -3.880  -14.222 35.141  1.00 33.90 ?  436 HOH B O   1 
HETATM 6350 O O   . HOH D 2 .   ? 23.007  -6.436  21.294  1.00 22.50 ?  437 HOH B O   1 
HETATM 6351 O O   . HOH D 2 .   ? 6.227   -19.698 22.592  1.00 20.51 ?  438 HOH B O   1 
HETATM 6352 O O   . HOH D 2 .   ? 29.607  -2.996  20.422  1.00 24.47 ?  439 HOH B O   1 
HETATM 6353 O O   . HOH D 2 .   ? 17.951  -11.081 10.701  1.00 32.49 ?  440 HOH B O   1 
HETATM 6354 O O   . HOH D 2 .   ? 15.145  -11.754 4.219   1.00 34.90 ?  441 HOH B O   1 
HETATM 6355 O O   . HOH D 2 .   ? 27.173  -2.265  19.469  1.00 24.64 ?  442 HOH B O   1 
HETATM 6356 O O   . HOH D 2 .   ? -1.300  -22.023 24.649  1.00 30.08 ?  443 HOH B O   1 
HETATM 6357 O O   . HOH D 2 .   ? 15.599  6.923   31.615  1.00 25.52 ?  444 HOH B O   1 
HETATM 6358 O O   . HOH D 2 .   ? 20.629  -27.374 22.696  1.00 40.99 ?  445 HOH B O   1 
HETATM 6359 O O   . HOH D 2 .   ? 15.831  -2.394  15.134  1.00 27.60 ?  446 HOH B O   1 
HETATM 6360 O O   . HOH D 2 .   ? 17.691  -17.836 36.949  1.00 27.80 ?  447 HOH B O   1 
HETATM 6361 O O   . HOH D 2 .   ? 21.472  -20.882 15.808  1.00 46.65 ?  448 HOH B O   1 
HETATM 6362 O O   . HOH D 2 .   ? -5.872  -2.604  -1.356  1.00 26.27 ?  449 HOH B O   1 
HETATM 6363 O O   . HOH D 2 .   ? 7.034   -7.719  32.414  1.00 18.39 ?  450 HOH B O   1 
HETATM 6364 O O   . HOH D 2 .   ? 7.285   -21.861 40.074  1.00 29.89 ?  451 HOH B O   1 
HETATM 6365 O O   . HOH D 2 .   ? 5.865   -14.595 29.032  1.00 21.62 ?  452 HOH B O   1 
HETATM 6366 O O   . HOH D 2 .   ? -11.138 -1.190  11.975  1.00 24.55 ?  453 HOH B O   1 
HETATM 6367 O O   . HOH D 2 .   ? -8.347  1.170   8.785   1.00 28.41 ?  454 HOH B O   1 
HETATM 6368 O O   . HOH D 2 .   ? -7.070  -11.809 19.061  1.00 22.37 ?  455 HOH B O   1 
HETATM 6369 O O   . HOH D 2 .   ? 16.281  -9.452  11.963  1.00 25.29 ?  456 HOH B O   1 
HETATM 6370 O O   . HOH D 2 .   ? 7.772   -12.072 27.473  1.00 21.76 ?  457 HOH B O   1 
HETATM 6371 O O   . HOH D 2 .   ? -1.966  8.492   46.165  1.00 38.53 ?  458 HOH B O   1 
HETATM 6372 O O   . HOH D 2 .   ? -19.450 -7.048  39.226  1.00 29.97 ?  459 HOH B O   1 
HETATM 6373 O O   . HOH D 2 .   ? -8.429  -12.604 36.123  1.00 21.80 ?  460 HOH B O   1 
HETATM 6374 O O   . HOH D 2 .   ? 27.781  -9.392  27.590  1.00 26.02 ?  461 HOH B O   1 
HETATM 6375 O O   . HOH D 2 .   ? -5.771  5.861   49.166  1.00 29.71 ?  462 HOH B O   1 
HETATM 6376 O O   . HOH D 2 .   ? 1.468   -3.427  39.163  1.00 24.99 ?  463 HOH B O   1 
HETATM 6377 O O   . HOH D 2 .   ? 2.425   -1.761  41.197  1.00 24.31 ?  464 HOH B O   1 
HETATM 6378 O O   . HOH D 2 .   ? -14.232 -4.907  9.731   1.00 28.67 ?  465 HOH B O   1 
HETATM 6379 O O   . HOH D 2 .   ? -13.863 -12.181 42.590  1.00 27.75 ?  466 HOH B O   1 
HETATM 6380 O O   . HOH D 2 .   ? 9.753   -15.992 25.500  1.00 25.81 ?  467 HOH B O   1 
HETATM 6381 O O   . HOH D 2 .   ? 1.049   -6.809  27.380  1.00 28.82 ?  468 HOH B O   1 
HETATM 6382 O O   . HOH D 2 .   ? 12.442  -6.867  43.077  1.00 28.55 ?  469 HOH B O   1 
HETATM 6383 O O   . HOH D 2 .   ? 3.899   -12.463 47.437  1.00 26.19 ?  470 HOH B O   1 
HETATM 6384 O O   . HOH D 2 .   ? 1.169   -0.842  25.834  1.00 36.22 ?  471 HOH B O   1 
HETATM 6385 O O   . HOH D 2 .   ? -2.220  6.114   10.376  1.00 27.56 ?  472 HOH B O   1 
HETATM 6386 O O   . HOH D 2 .   ? 16.608  -26.952 16.891  1.00 36.47 ?  473 HOH B O   1 
HETATM 6387 O O   . HOH D 2 .   ? 13.863  4.163   34.627  1.00 27.64 ?  474 HOH B O   1 
HETATM 6388 O O   . HOH D 2 .   ? 14.335  -10.821 35.156  1.00 23.03 ?  475 HOH B O   1 
HETATM 6389 O O   . HOH D 2 .   ? 13.682  -4.223  1.001   1.00 34.19 ?  476 HOH B O   1 
HETATM 6390 O O   . HOH D 2 .   ? -6.547  -14.133 20.736  1.00 23.22 ?  477 HOH B O   1 
HETATM 6391 O O   . HOH D 2 .   ? -0.229  -3.085  29.265  1.00 23.78 ?  478 HOH B O   1 
HETATM 6392 O O   . HOH D 2 .   ? 0.728   -13.776 24.650  1.00 21.06 ?  479 HOH B O   1 
HETATM 6393 O O   . HOH D 2 .   ? 9.019   -4.447  31.393  1.00 21.16 ?  480 HOH B O   1 
HETATM 6394 O O   . HOH D 2 .   ? 14.775  -6.568  -2.250  1.00 37.92 ?  481 HOH B O   1 
HETATM 6395 O O   . HOH D 2 .   ? -23.348 -3.177  33.013  0.50 44.66 ?  482 HOH B O   1 
HETATM 6396 O O   . HOH D 2 .   ? -1.393  0.364   25.865  1.00 39.12 ?  483 HOH B O   1 
HETATM 6397 O O   . HOH D 2 .   ? -5.770  -26.987 7.470   1.00 41.51 ?  484 HOH B O   1 
HETATM 6398 O O   . HOH D 2 .   ? 17.636  -18.255 11.878  1.00 43.83 ?  485 HOH B O   1 
HETATM 6399 O O   . HOH D 2 .   ? 12.372  5.118   32.383  1.00 28.94 ?  486 HOH B O   1 
HETATM 6400 O O   . HOH D 2 .   ? -9.505  0.442   21.490  1.00 31.24 ?  487 HOH B O   1 
HETATM 6401 O O   . HOH D 2 .   ? 11.398  -22.147 35.110  1.00 29.94 ?  488 HOH B O   1 
HETATM 6402 O O   . HOH D 2 .   ? 14.016  0.597   19.248  1.00 28.95 ?  489 HOH B O   1 
HETATM 6403 O O   . HOH D 2 .   ? 26.554  -16.753 14.246  1.00 42.82 ?  490 HOH B O   1 
HETATM 6404 O O   . HOH D 2 .   ? 25.369  -13.247 37.479  1.00 34.77 ?  491 HOH B O   1 
HETATM 6405 O O   . HOH D 2 .   ? 16.813  -4.092  19.179  1.00 23.51 ?  492 HOH B O   1 
HETATM 6406 O O   . HOH D 2 .   ? 22.669  -10.699 11.362  1.00 42.37 ?  493 HOH B O   1 
HETATM 6407 O O   . HOH D 2 .   ? -17.452 -11.437 7.239   1.00 39.36 ?  494 HOH B O   1 
HETATM 6408 O O   . HOH D 2 .   ? 10.106  2.703   8.996   1.00 23.32 ?  495 HOH B O   1 
HETATM 6409 O O   . HOH D 2 .   ? 0.536   0.028   4.386   1.00 27.54 ?  496 HOH B O   1 
HETATM 6410 O O   . HOH D 2 .   ? -7.856  3.709   38.479  1.00 27.87 ?  497 HOH B O   1 
HETATM 6411 O O   . HOH D 2 .   ? 22.951  -2.700  15.436  1.00 28.01 ?  498 HOH B O   1 
HETATM 6412 O O   . HOH D 2 .   ? 14.642  -10.116 -1.425  1.00 28.78 ?  499 HOH B O   1 
HETATM 6413 O O   . HOH D 2 .   ? 5.263   -20.455 8.717   1.00 28.35 ?  500 HOH B O   1 
HETATM 6414 O O   . HOH D 2 .   ? 5.867   -18.027 24.738  1.00 23.98 ?  501 HOH B O   1 
HETATM 6415 O O   . HOH D 2 .   ? 4.336   -20.658 31.191  1.00 25.51 ?  502 HOH B O   1 
HETATM 6416 O O   . HOH D 2 .   ? 9.481   2.619   41.231  1.00 42.84 ?  503 HOH B O   1 
HETATM 6417 O O   . HOH D 2 .   ? -20.910 -8.869  33.114  1.00 39.39 ?  504 HOH B O   1 
HETATM 6418 O O   . HOH D 2 .   ? 6.813   -9.394  47.434  1.00 29.23 ?  505 HOH B O   1 
HETATM 6419 O O   . HOH D 2 .   ? 10.776  -1.191  47.750  1.00 34.33 ?  506 HOH B O   1 
HETATM 6420 O O   . HOH D 2 .   ? 24.892  -13.201 27.137  1.00 29.68 ?  507 HOH B O   1 
HETATM 6421 O O   . HOH D 2 .   ? -16.843 -2.439  25.777  1.00 31.53 ?  508 HOH B O   1 
HETATM 6422 O O   . HOH D 2 .   ? 8.310   -2.780  24.379  1.00 31.74 ?  509 HOH B O   1 
HETATM 6423 O O   . HOH D 2 .   ? -4.062  -24.102 2.561   1.00 36.89 ?  510 HOH B O   1 
HETATM 6424 O O   . HOH D 2 .   ? 6.886   -5.805  30.334  1.00 21.22 ?  511 HOH B O   1 
HETATM 6425 O O   . HOH D 2 .   ? 21.893  -6.692  11.688  1.00 34.36 ?  512 HOH B O   1 
HETATM 6426 O O   . HOH D 2 .   ? 36.862  -1.725  24.672  1.00 34.42 ?  513 HOH B O   1 
HETATM 6427 O O   . HOH D 2 .   ? 1.593   -28.524 30.004  1.00 43.49 ?  514 HOH B O   1 
HETATM 6428 O O   . HOH D 2 .   ? 7.732   -2.813  6.897   1.00 25.30 ?  515 HOH B O   1 
HETATM 6429 O O   . HOH D 2 .   ? -15.423 -0.596  24.808  1.00 32.05 ?  516 HOH B O   1 
HETATM 6430 O O   . HOH D 2 .   ? 0.345   -3.794  1.376   1.00 44.51 ?  517 HOH B O   1 
HETATM 6431 O O   . HOH D 2 .   ? 1.713   8.137   34.933  1.00 41.84 ?  518 HOH B O   1 
HETATM 6432 O O   . HOH D 2 .   ? 7.600   -9.689  0.003   1.00 30.05 ?  519 HOH B O   1 
HETATM 6433 O O   . HOH D 2 .   ? 24.450  -15.774 28.860  1.00 43.12 ?  520 HOH B O   1 
HETATM 6434 O O   . HOH D 2 .   ? -22.949 -1.842  34.659  1.00 53.64 ?  521 HOH B O   1 
HETATM 6435 O O   . HOH D 2 .   ? 5.241   -30.804 13.979  1.00 42.72 ?  522 HOH B O   1 
HETATM 6436 O O   . HOH D 2 .   ? 1.695   -10.845 32.064  1.00 21.39 ?  523 HOH B O   1 
HETATM 6437 O O   . HOH D 2 .   ? 10.159  -2.448  20.241  1.00 29.65 ?  524 HOH B O   1 
HETATM 6438 O O   . HOH D 2 .   ? 7.354   -14.625 24.924  1.00 23.93 ?  525 HOH B O   1 
HETATM 6439 O O   . HOH D 2 .   ? 32.592  -7.203  26.605  1.00 39.46 ?  526 HOH B O   1 
HETATM 6440 O O   . HOH D 2 .   ? 6.008   -5.145  21.636  1.00 29.32 ?  527 HOH B O   1 
HETATM 6441 O O   . HOH D 2 .   ? -18.393 -11.181 17.082  1.00 30.64 ?  528 HOH B O   1 
HETATM 6442 O O   . HOH D 2 .   ? 11.442  -5.927  24.472  1.00 28.35 ?  529 HOH B O   1 
HETATM 6443 O O   . HOH D 2 .   ? -11.933 -19.688 2.188   1.00 35.84 ?  530 HOH B O   1 
HETATM 6444 O O   . HOH D 2 .   ? 4.148   6.758   44.461  1.00 42.71 ?  531 HOH B O   1 
HETATM 6445 O O   . HOH D 2 .   ? 29.093  -10.200 12.330  1.00 38.20 ?  532 HOH B O   1 
HETATM 6446 O O   . HOH D 2 .   ? 1.154   -1.927  2.333   1.00 37.91 ?  533 HOH B O   1 
HETATM 6447 O O   . HOH D 2 .   ? -4.330  -11.101 30.670  1.00 24.89 ?  534 HOH B O   1 
HETATM 6448 O O   . HOH D 2 .   ? 6.056   -1.628  5.037   1.00 20.45 ?  535 HOH B O   1 
HETATM 6449 O O   . HOH D 2 .   ? -5.928  7.965   35.092  1.00 37.99 ?  536 HOH B O   1 
HETATM 6450 O O   . HOH D 2 .   ? -0.529  -4.967  28.094  1.00 24.14 ?  537 HOH B O   1 
HETATM 6451 O O   . HOH D 2 .   ? 12.817  -24.856 34.340  1.00 44.35 ?  538 HOH B O   1 
HETATM 6452 O O   . HOH D 2 .   ? 16.112  -2.533  10.775  1.00 28.84 ?  539 HOH B O   1 
HETATM 6453 O O   . HOH D 2 .   ? -17.093 -3.751  49.383  1.00 43.06 ?  540 HOH B O   1 
HETATM 6454 O O   . HOH D 2 .   ? 19.286  -7.340  39.742  1.00 37.17 ?  541 HOH B O   1 
HETATM 6455 O O   . HOH D 2 .   ? 14.510  -18.255 3.712   1.00 38.03 ?  542 HOH B O   1 
HETATM 6456 O O   . HOH D 2 .   ? -16.175 -6.965  14.182  1.00 29.07 ?  543 HOH B O   1 
HETATM 6457 O O   . HOH D 2 .   ? -8.996  -21.174 0.906   1.00 45.51 ?  544 HOH B O   1 
HETATM 6458 O O   . HOH D 2 .   ? -22.675 7.839   46.044  1.00 50.71 ?  545 HOH B O   1 
HETATM 6459 O O   . HOH D 2 .   ? 24.483  -8.928  38.620  1.00 39.43 ?  546 HOH B O   1 
HETATM 6460 O O   . HOH D 2 .   ? 11.584  -27.008 8.511   1.00 33.94 ?  547 HOH B O   1 
HETATM 6461 O O   . HOH D 2 .   ? 20.926  1.516   11.755  1.00 41.13 ?  548 HOH B O   1 
HETATM 6462 O O   . HOH D 2 .   ? 9.056   -21.806 35.066  1.00 41.79 ?  549 HOH B O   1 
HETATM 6463 O O   . HOH D 2 .   ? 18.567  -20.750 35.463  1.00 39.88 ?  550 HOH B O   1 
HETATM 6464 O O   . HOH D 2 .   ? -16.885 -3.717  21.512  1.00 34.37 ?  551 HOH B O   1 
HETATM 6465 O O   . HOH D 2 .   ? 7.459   -28.546 15.483  1.00 30.31 ?  552 HOH B O   1 
HETATM 6466 O O   . HOH D 2 .   ? 4.488   -23.384 37.405  1.00 43.80 ?  553 HOH B O   1 
HETATM 6467 O O   . HOH D 2 .   ? -15.006 11.518  38.379  1.00 47.31 ?  554 HOH B O   1 
HETATM 6468 O O   . HOH D 2 .   ? -3.859  -0.039  29.793  1.00 41.12 ?  555 HOH B O   1 
HETATM 6469 O O   . HOH D 2 .   ? 10.359  -9.525  0.767   1.00 33.11 ?  556 HOH B O   1 
HETATM 6470 O O   . HOH D 2 .   ? 0.822   -26.229 3.630   1.00 46.99 ?  557 HOH B O   1 
HETATM 6471 O O   . HOH D 2 .   ? 7.771   -20.097 47.877  1.00 51.06 ?  558 HOH B O   1 
HETATM 6472 O O   . HOH D 2 .   ? -14.308 -3.496  14.698  1.00 39.92 ?  559 HOH B O   1 
HETATM 6473 O O   . HOH D 2 .   ? 2.912   -6.633  24.505  1.00 31.09 ?  560 HOH B O   1 
HETATM 6474 O O   . HOH D 2 .   ? -3.836  9.624   45.693  1.00 38.97 ?  561 HOH B O   1 
HETATM 6475 O O   . HOH D 2 .   ? -4.958  -13.028 53.380  1.00 40.59 ?  562 HOH B O   1 
HETATM 6476 O O   . HOH D 2 .   ? -1.238  7.570   33.618  1.00 52.93 ?  563 HOH B O   1 
HETATM 6477 O O   . HOH D 2 .   ? 16.538  -16.272 9.025   1.00 49.83 ?  564 HOH B O   1 
HETATM 6478 O O   . HOH D 2 .   ? -10.597 0.998   10.577  1.00 31.44 ?  565 HOH B O   1 
HETATM 6479 O O   . HOH D 2 .   ? -8.032  6.598   34.634  1.00 39.52 ?  566 HOH B O   1 
HETATM 6480 O O   . HOH D 2 .   ? -1.485  -0.523  28.879  1.00 32.78 ?  567 HOH B O   1 
HETATM 6481 O O   . HOH D 2 .   ? -22.629 5.607   39.447  1.00 57.37 ?  568 HOH B O   1 
HETATM 6482 O O   . HOH D 2 .   ? -3.303  6.455   32.759  1.00 50.63 ?  569 HOH B O   1 
HETATM 6483 O O   . HOH D 2 .   ? 3.927   9.240   31.293  1.00 54.77 ?  570 HOH B O   1 
HETATM 6484 O O   . HOH D 2 .   ? -24.471 3.122   43.227  1.00 59.30 ?  571 HOH B O   1 
HETATM 6485 O O   . HOH D 2 .   ? 20.510  -9.952  10.605  1.00 47.22 ?  572 HOH B O   1 
HETATM 6486 O O   . HOH D 2 .   ? 27.167  -12.289 28.533  1.00 38.16 ?  573 HOH B O   1 
HETATM 6487 O O   . HOH D 2 .   ? -15.197 -17.015 -1.026  1.00 42.01 ?  574 HOH B O   1 
HETATM 6488 O O   . HOH D 2 .   ? -15.876 -1.328  21.759  1.00 41.28 ?  575 HOH B O   1 
HETATM 6489 O O   . HOH D 2 .   ? 8.843   4.758   42.483  1.00 52.47 ?  576 HOH B O   1 
HETATM 6490 O O   . HOH D 2 .   ? -0.000  -0.509  0.000   0.50 42.40 ?  577 HOH B O   1 
# 
