data_9JVA
# 
_entry.id   9JVA 
# 
_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   9JVA         pdb_00009jva 10.2210/pdb9jva/pdb 
WWPDB D_1300052324 ?            ?                   
# 
_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                        9JVA 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-08 
_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)/PLP complex of Lactobacillus lactobacillus delbrueckii at 1.53 ANG' 
_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 non-polymer syn "PYRIDOXAL-5'-PHOSPHATE"          247.142   2   ?        ?              ? ? 
3 water       nat water                             18.015    667 ?        ?              ? ? 
# 
_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         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "PYRIDOXAL-5'-PHOSPHATE" PLP 
3 water                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
PLP non-polymer         . "PYRIDOXAL-5'-PHOSPHATE" 'VITAMIN B6 Phosphate' 'C8 H10 N O6 P'  247.142 
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   ?   ?   ?   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  25  LYS LYS 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 220 220 220 ASP ASP 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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PLP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PLP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 PLP 1   401 401 PLP PLP A . 
D 2 PLP 1   401 401 PLP PLP B . 
E 3 HOH 1   501 619 HOH HOH A . 
E 3 HOH 2   502 658 HOH HOH A . 
E 3 HOH 3   503 178 HOH HOH A . 
E 3 HOH 4   504 7   HOH HOH A . 
E 3 HOH 5   505 602 HOH HOH A . 
E 3 HOH 6   506 423 HOH HOH A . 
E 3 HOH 7   507 25  HOH HOH A . 
E 3 HOH 8   508 74  HOH HOH A . 
E 3 HOH 9   509 283 HOH HOH A . 
E 3 HOH 10  510 203 HOH HOH A . 
E 3 HOH 11  511 293 HOH HOH A . 
E 3 HOH 12  512 93  HOH HOH A . 
E 3 HOH 13  513 134 HOH HOH A . 
E 3 HOH 14  514 428 HOH HOH A . 
E 3 HOH 15  515 114 HOH HOH A . 
E 3 HOH 16  516 273 HOH HOH A . 
E 3 HOH 17  517 530 HOH HOH A . 
E 3 HOH 18  518 460 HOH HOH A . 
E 3 HOH 19  519 268 HOH HOH A . 
E 3 HOH 20  520 219 HOH HOH A . 
E 3 HOH 21  521 335 HOH HOH A . 
E 3 HOH 22  522 274 HOH HOH A . 
E 3 HOH 23  523 433 HOH HOH A . 
E 3 HOH 24  524 332 HOH HOH A . 
E 3 HOH 25  525 655 HOH HOH A . 
E 3 HOH 26  526 107 HOH HOH A . 
E 3 HOH 27  527 52  HOH HOH A . 
E 3 HOH 28  528 592 HOH HOH A . 
E 3 HOH 29  529 133 HOH HOH A . 
E 3 HOH 30  530 68  HOH HOH A . 
E 3 HOH 31  531 197 HOH HOH A . 
E 3 HOH 32  532 533 HOH HOH A . 
E 3 HOH 33  533 616 HOH HOH A . 
E 3 HOH 34  534 312 HOH HOH A . 
E 3 HOH 35  535 377 HOH HOH A . 
E 3 HOH 36  536 98  HOH HOH A . 
E 3 HOH 37  537 694 HOH HOH A . 
E 3 HOH 38  538 238 HOH HOH A . 
E 3 HOH 39  539 671 HOH HOH A . 
E 3 HOH 40  540 152 HOH HOH A . 
E 3 HOH 41  541 613 HOH HOH A . 
E 3 HOH 42  542 270 HOH HOH A . 
E 3 HOH 43  543 559 HOH HOH A . 
E 3 HOH 44  544 195 HOH HOH A . 
E 3 HOH 45  545 89  HOH HOH A . 
E 3 HOH 46  546 427 HOH HOH A . 
E 3 HOH 47  547 344 HOH HOH A . 
E 3 HOH 48  548 340 HOH HOH A . 
E 3 HOH 49  549 596 HOH HOH A . 
E 3 HOH 50  550 610 HOH HOH A . 
E 3 HOH 51  551 414 HOH HOH A . 
E 3 HOH 52  552 209 HOH HOH A . 
E 3 HOH 53  553 556 HOH HOH A . 
E 3 HOH 54  554 469 HOH HOH A . 
E 3 HOH 55  555 39  HOH HOH A . 
E 3 HOH 56  556 437 HOH HOH A . 
E 3 HOH 57  557 248 HOH HOH A . 
E 3 HOH 58  558 127 HOH HOH A . 
E 3 HOH 59  559 249 HOH HOH A . 
E 3 HOH 60  560 9   HOH HOH A . 
E 3 HOH 61  561 139 HOH HOH A . 
E 3 HOH 62  562 260 HOH HOH A . 
E 3 HOH 63  563 69  HOH HOH A . 
E 3 HOH 64  564 159 HOH HOH A . 
E 3 HOH 65  565 47  HOH HOH A . 
E 3 HOH 66  566 42  HOH HOH A . 
E 3 HOH 67  567 85  HOH HOH A . 
E 3 HOH 68  568 677 HOH HOH A . 
E 3 HOH 69  569 254 HOH HOH A . 
E 3 HOH 70  570 149 HOH HOH A . 
E 3 HOH 71  571 41  HOH HOH A . 
E 3 HOH 72  572 434 HOH HOH A . 
E 3 HOH 73  573 367 HOH HOH A . 
E 3 HOH 74  574 30  HOH HOH A . 
E 3 HOH 75  575 156 HOH HOH A . 
E 3 HOH 76  576 259 HOH HOH A . 
E 3 HOH 77  577 458 HOH HOH A . 
E 3 HOH 78  578 75  HOH HOH A . 
E 3 HOH 79  579 406 HOH HOH A . 
E 3 HOH 80  580 157 HOH HOH A . 
E 3 HOH 81  581 189 HOH HOH A . 
E 3 HOH 82  582 281 HOH HOH A . 
E 3 HOH 83  583 306 HOH HOH A . 
E 3 HOH 84  584 410 HOH HOH A . 
E 3 HOH 85  585 700 HOH HOH A . 
E 3 HOH 86  586 463 HOH HOH A . 
E 3 HOH 87  587 214 HOH HOH A . 
E 3 HOH 88  588 76  HOH HOH A . 
E 3 HOH 89  589 279 HOH HOH A . 
E 3 HOH 90  590 308 HOH HOH A . 
E 3 HOH 91  591 475 HOH HOH A . 
E 3 HOH 92  592 418 HOH HOH A . 
E 3 HOH 93  593 450 HOH HOH A . 
E 3 HOH 94  594 143 HOH HOH A . 
E 3 HOH 95  595 517 HOH HOH A . 
E 3 HOH 96  596 408 HOH HOH A . 
E 3 HOH 97  597 132 HOH HOH A . 
E 3 HOH 98  598 97  HOH HOH A . 
E 3 HOH 99  599 659 HOH HOH A . 
E 3 HOH 100 600 131 HOH HOH A . 
E 3 HOH 101 601 252 HOH HOH A . 
E 3 HOH 102 602 243 HOH HOH A . 
E 3 HOH 103 603 678 HOH HOH A . 
E 3 HOH 104 604 84  HOH HOH A . 
E 3 HOH 105 605 303 HOH HOH A . 
E 3 HOH 106 606 560 HOH HOH A . 
E 3 HOH 107 607 18  HOH HOH A . 
E 3 HOH 108 608 405 HOH HOH A . 
E 3 HOH 109 609 123 HOH HOH A . 
E 3 HOH 110 610 110 HOH HOH A . 
E 3 HOH 111 611 90  HOH HOH A . 
E 3 HOH 112 612 51  HOH HOH A . 
E 3 HOH 113 613 27  HOH HOH A . 
E 3 HOH 114 614 412 HOH HOH A . 
E 3 HOH 115 615 173 HOH HOH A . 
E 3 HOH 116 616 251 HOH HOH A . 
E 3 HOH 117 617 119 HOH HOH A . 
E 3 HOH 118 618 17  HOH HOH A . 
E 3 HOH 119 619 205 HOH HOH A . 
E 3 HOH 120 620 54  HOH HOH A . 
E 3 HOH 121 621 689 HOH HOH A . 
E 3 HOH 122 622 55  HOH HOH A . 
E 3 HOH 123 623 526 HOH HOH A . 
E 3 HOH 124 624 136 HOH HOH A . 
E 3 HOH 125 625 449 HOH HOH A . 
E 3 HOH 126 626 313 HOH HOH A . 
E 3 HOH 127 627 151 HOH HOH A . 
E 3 HOH 128 628 305 HOH HOH A . 
E 3 HOH 129 629 304 HOH HOH A . 
E 3 HOH 130 630 482 HOH HOH A . 
E 3 HOH 131 631 489 HOH HOH A . 
E 3 HOH 132 632 333 HOH HOH A . 
E 3 HOH 133 633 19  HOH HOH A . 
E 3 HOH 134 634 319 HOH HOH A . 
E 3 HOH 135 635 285 HOH HOH A . 
E 3 HOH 136 636 66  HOH HOH A . 
E 3 HOH 137 637 216 HOH HOH A . 
E 3 HOH 138 638 387 HOH HOH A . 
E 3 HOH 139 639 629 HOH HOH A . 
E 3 HOH 140 640 64  HOH HOH A . 
E 3 HOH 141 641 544 HOH HOH A . 
E 3 HOH 142 642 102 HOH HOH A . 
E 3 HOH 143 643 637 HOH HOH A . 
E 3 HOH 144 644 380 HOH HOH A . 
E 3 HOH 145 645 11  HOH HOH A . 
E 3 HOH 146 646 296 HOH HOH A . 
E 3 HOH 147 647 572 HOH HOH A . 
E 3 HOH 148 648 201 HOH HOH A . 
E 3 HOH 149 649 445 HOH HOH A . 
E 3 HOH 150 650 221 HOH HOH A . 
E 3 HOH 151 651 323 HOH HOH A . 
E 3 HOH 152 652 211 HOH HOH A . 
E 3 HOH 153 653 511 HOH HOH A . 
E 3 HOH 154 654 37  HOH HOH A . 
E 3 HOH 155 655 21  HOH HOH A . 
E 3 HOH 156 656 236 HOH HOH A . 
E 3 HOH 157 657 73  HOH HOH A . 
E 3 HOH 158 658 356 HOH HOH A . 
E 3 HOH 159 659 125 HOH HOH A . 
E 3 HOH 160 660 165 HOH HOH A . 
E 3 HOH 161 661 468 HOH HOH A . 
E 3 HOH 162 662 13  HOH HOH A . 
E 3 HOH 163 663 280 HOH HOH A . 
E 3 HOH 164 664 540 HOH HOH A . 
E 3 HOH 165 665 297 HOH HOH A . 
E 3 HOH 166 666 276 HOH HOH A . 
E 3 HOH 167 667 684 HOH HOH A . 
E 3 HOH 168 668 354 HOH HOH A . 
E 3 HOH 169 669 441 HOH HOH A . 
E 3 HOH 170 670 325 HOH HOH A . 
E 3 HOH 171 671 124 HOH HOH A . 
E 3 HOH 172 672 322 HOH HOH A . 
E 3 HOH 173 673 28  HOH HOH A . 
E 3 HOH 174 674 391 HOH HOH A . 
E 3 HOH 175 675 176 HOH HOH A . 
E 3 HOH 176 676 587 HOH HOH A . 
E 3 HOH 177 677 208 HOH HOH A . 
E 3 HOH 178 678 636 HOH HOH A . 
E 3 HOH 179 679 269 HOH HOH A . 
E 3 HOH 180 680 605 HOH HOH A . 
E 3 HOH 181 681 31  HOH HOH A . 
E 3 HOH 182 682 457 HOH HOH A . 
E 3 HOH 183 683 611 HOH HOH A . 
E 3 HOH 184 684 360 HOH HOH A . 
E 3 HOH 185 685 289 HOH HOH A . 
E 3 HOH 186 686 384 HOH HOH A . 
E 3 HOH 187 687 38  HOH HOH A . 
E 3 HOH 188 688 334 HOH HOH A . 
E 3 HOH 189 689 161 HOH HOH A . 
E 3 HOH 190 690 167 HOH HOH A . 
E 3 HOH 191 691 4   HOH HOH A . 
E 3 HOH 192 692 519 HOH HOH A . 
E 3 HOH 193 693 65  HOH HOH A . 
E 3 HOH 194 694 432 HOH HOH A . 
E 3 HOH 195 695 109 HOH HOH A . 
E 3 HOH 196 696 411 HOH HOH A . 
E 3 HOH 197 697 336 HOH HOH A . 
E 3 HOH 198 698 514 HOH HOH A . 
E 3 HOH 199 699 96  HOH HOH A . 
E 3 HOH 200 700 232 HOH HOH A . 
E 3 HOH 201 701 366 HOH HOH A . 
E 3 HOH 202 702 599 HOH HOH A . 
E 3 HOH 203 703 225 HOH HOH A . 
E 3 HOH 204 704 112 HOH HOH A . 
E 3 HOH 205 705 371 HOH HOH A . 
E 3 HOH 206 706 429 HOH HOH A . 
E 3 HOH 207 707 331 HOH HOH A . 
E 3 HOH 208 708 200 HOH HOH A . 
E 3 HOH 209 709 294 HOH HOH A . 
E 3 HOH 210 710 607 HOH HOH A . 
E 3 HOH 211 711 288 HOH HOH A . 
E 3 HOH 212 712 520 HOH HOH A . 
E 3 HOH 213 713 364 HOH HOH A . 
E 3 HOH 214 714 541 HOH HOH A . 
E 3 HOH 215 715 311 HOH HOH A . 
E 3 HOH 216 716 341 HOH HOH A . 
E 3 HOH 217 717 163 HOH HOH A . 
E 3 HOH 218 718 683 HOH HOH A . 
E 3 HOH 219 719 137 HOH HOH A . 
E 3 HOH 220 720 400 HOH HOH A . 
E 3 HOH 221 721 680 HOH HOH A . 
E 3 HOH 222 722 436 HOH HOH A . 
E 3 HOH 223 723 509 HOH HOH A . 
E 3 HOH 224 724 402 HOH HOH A . 
E 3 HOH 225 725 58  HOH HOH A . 
E 3 HOH 226 726 385 HOH HOH A . 
E 3 HOH 227 727 653 HOH HOH A . 
E 3 HOH 228 728 242 HOH HOH A . 
E 3 HOH 229 729 116 HOH HOH A . 
E 3 HOH 230 730 368 HOH HOH A . 
E 3 HOH 231 731 452 HOH HOH A . 
E 3 HOH 232 732 145 HOH HOH A . 
E 3 HOH 233 733 56  HOH HOH A . 
E 3 HOH 234 734 443 HOH HOH A . 
E 3 HOH 235 735 645 HOH HOH A . 
E 3 HOH 236 736 639 HOH HOH A . 
E 3 HOH 237 737 113 HOH HOH A . 
E 3 HOH 238 738 202 HOH HOH A . 
E 3 HOH 239 739 389 HOH HOH A . 
E 3 HOH 240 740 617 HOH HOH A . 
E 3 HOH 241 741 667 HOH HOH A . 
E 3 HOH 242 742 508 HOH HOH A . 
E 3 HOH 243 743 422 HOH HOH A . 
E 3 HOH 244 744 171 HOH HOH A . 
E 3 HOH 245 745 160 HOH HOH A . 
E 3 HOH 246 746 372 HOH HOH A . 
E 3 HOH 247 747 396 HOH HOH A . 
E 3 HOH 248 748 470 HOH HOH A . 
E 3 HOH 249 749 527 HOH HOH A . 
E 3 HOH 250 750 407 HOH HOH A . 
E 3 HOH 251 751 548 HOH HOH A . 
E 3 HOH 252 752 575 HOH HOH A . 
E 3 HOH 253 753 626 HOH HOH A . 
E 3 HOH 254 754 542 HOH HOH A . 
E 3 HOH 255 755 234 HOH HOH A . 
E 3 HOH 256 756 158 HOH HOH A . 
E 3 HOH 257 757 184 HOH HOH A . 
E 3 HOH 258 758 654 HOH HOH A . 
E 3 HOH 259 759 606 HOH HOH A . 
E 3 HOH 260 760 598 HOH HOH A . 
E 3 HOH 261 761 478 HOH HOH A . 
E 3 HOH 262 762 466 HOH HOH A . 
E 3 HOH 263 763 589 HOH HOH A . 
E 3 HOH 264 764 154 HOH HOH A . 
E 3 HOH 265 765 546 HOH HOH A . 
E 3 HOH 266 766 213 HOH HOH A . 
E 3 HOH 267 767 404 HOH HOH A . 
E 3 HOH 268 768 698 HOH HOH A . 
E 3 HOH 269 769 623 HOH HOH A . 
E 3 HOH 270 770 442 HOH HOH A . 
E 3 HOH 271 771 647 HOH HOH A . 
E 3 HOH 272 772 495 HOH HOH A . 
E 3 HOH 273 773 518 HOH HOH A . 
E 3 HOH 274 774 670 HOH HOH A . 
E 3 HOH 275 775 342 HOH HOH A . 
E 3 HOH 276 776 569 HOH HOH A . 
E 3 HOH 277 777 553 HOH HOH A . 
E 3 HOH 278 778 590 HOH HOH A . 
E 3 HOH 279 779 239 HOH HOH A . 
E 3 HOH 280 780 338 HOH HOH A . 
E 3 HOH 281 781 693 HOH HOH A . 
E 3 HOH 282 782 701 HOH HOH A . 
E 3 HOH 283 783 245 HOH HOH A . 
E 3 HOH 284 784 625 HOH HOH A . 
E 3 HOH 285 785 570 HOH HOH A . 
E 3 HOH 286 786 662 HOH HOH A . 
E 3 HOH 287 787 388 HOH HOH A . 
E 3 HOH 288 788 506 HOH HOH A . 
E 3 HOH 289 789 471 HOH HOH A . 
E 3 HOH 290 790 204 HOH HOH A . 
E 3 HOH 291 791 603 HOH HOH A . 
E 3 HOH 292 792 594 HOH HOH A . 
E 3 HOH 293 793 327 HOH HOH A . 
E 3 HOH 294 794 515 HOH HOH A . 
E 3 HOH 295 795 420 HOH HOH A . 
E 3 HOH 296 796 390 HOH HOH A . 
E 3 HOH 297 797 503 HOH HOH A . 
E 3 HOH 298 798 696 HOH HOH A . 
E 3 HOH 299 799 674 HOH HOH A . 
E 3 HOH 300 800 233 HOH HOH A . 
E 3 HOH 301 801 431 HOH HOH A . 
E 3 HOH 302 802 379 HOH HOH A . 
E 3 HOH 303 803 507 HOH HOH A . 
E 3 HOH 304 804 538 HOH HOH A . 
E 3 HOH 305 805 307 HOH HOH A . 
E 3 HOH 306 806 675 HOH HOH A . 
E 3 HOH 307 807 502 HOH HOH A . 
E 3 HOH 308 808 206 HOH HOH A . 
E 3 HOH 309 809 564 HOH HOH A . 
E 3 HOH 310 810 695 HOH HOH A . 
E 3 HOH 311 811 699 HOH HOH A . 
E 3 HOH 312 812 426 HOH HOH A . 
E 3 HOH 313 813 642 HOH HOH A . 
E 3 HOH 314 814 687 HOH HOH A . 
E 3 HOH 315 815 309 HOH HOH A . 
E 3 HOH 316 816 295 HOH HOH A . 
E 3 HOH 317 817 573 HOH HOH A . 
E 3 HOH 318 818 278 HOH HOH A . 
E 3 HOH 319 819 660 HOH HOH A . 
E 3 HOH 320 820 365 HOH HOH A . 
E 3 HOH 321 821 563 HOH HOH A . 
E 3 HOH 322 822 326 HOH HOH A . 
E 3 HOH 323 823 485 HOH HOH A . 
E 3 HOH 324 824 444 HOH HOH A . 
E 3 HOH 325 825 494 HOH HOH A . 
E 3 HOH 326 826 229 HOH HOH A . 
E 3 HOH 327 827 666 HOH HOH A . 
E 3 HOH 328 828 479 HOH HOH A . 
E 3 HOH 329 829 595 HOH HOH A . 
E 3 HOH 330 830 597 HOH HOH A . 
E 3 HOH 331 831 634 HOH HOH A . 
E 3 HOH 332 832 477 HOH HOH A . 
E 3 HOH 333 833 182 HOH HOH A . 
E 3 HOH 334 834 467 HOH HOH A . 
E 3 HOH 335 835 394 HOH HOH A . 
E 3 HOH 336 836 376 HOH HOH A . 
E 3 HOH 337 837 212 HOH HOH A . 
E 3 HOH 338 838 669 HOH HOH A . 
E 3 HOH 339 839 691 HOH HOH A . 
E 3 HOH 340 840 290 HOH HOH A . 
E 3 HOH 341 841 535 HOH HOH A . 
E 3 HOH 342 842 646 HOH HOH A . 
E 3 HOH 343 843 661 HOH HOH A . 
E 3 HOH 344 844 635 HOH HOH A . 
E 3 HOH 345 845 697 HOH HOH A . 
E 3 HOH 346 846 681 HOH HOH A . 
E 3 HOH 347 847 454 HOH HOH A . 
E 3 HOH 348 848 672 HOH HOH A . 
E 3 HOH 349 849 567 HOH HOH A . 
E 3 HOH 350 850 551 HOH HOH A . 
F 3 HOH 1   501 679 HOH HOH B . 
F 3 HOH 2   502 531 HOH HOH B . 
F 3 HOH 3   503 1   HOH HOH B . 
F 3 HOH 4   504 568 HOH HOH B . 
F 3 HOH 5   505 447 HOH HOH B . 
F 3 HOH 6   506 287 HOH HOH B . 
F 3 HOH 7   507 413 HOH HOH B . 
F 3 HOH 8   508 462 HOH HOH B . 
F 3 HOH 9   509 256 HOH HOH B . 
F 3 HOH 10  510 537 HOH HOH B . 
F 3 HOH 11  511 80  HOH HOH B . 
F 3 HOH 12  512 416 HOH HOH B . 
F 3 HOH 13  513 246 HOH HOH B . 
F 3 HOH 14  514 673 HOH HOH B . 
F 3 HOH 15  515 196 HOH HOH B . 
F 3 HOH 16  516 78  HOH HOH B . 
F 3 HOH 17  517 5   HOH HOH B . 
F 3 HOH 18  518 177 HOH HOH B . 
F 3 HOH 19  519 77  HOH HOH B . 
F 3 HOH 20  520 82  HOH HOH B . 
F 3 HOH 21  521 586 HOH HOH B . 
F 3 HOH 22  522 141 HOH HOH B . 
F 3 HOH 23  523 362 HOH HOH B . 
F 3 HOH 24  524 193 HOH HOH B . 
F 3 HOH 25  525 183 HOH HOH B . 
F 3 HOH 26  526 580 HOH HOH B . 
F 3 HOH 27  527 504 HOH HOH B . 
F 3 HOH 28  528 23  HOH HOH B . 
F 3 HOH 29  529 347 HOH HOH B . 
F 3 HOH 30  530 34  HOH HOH B . 
F 3 HOH 31  531 129 HOH HOH B . 
F 3 HOH 32  532 120 HOH HOH B . 
F 3 HOH 33  533 357 HOH HOH B . 
F 3 HOH 34  534 425 HOH HOH B . 
F 3 HOH 35  535 147 HOH HOH B . 
F 3 HOH 36  536 99  HOH HOH B . 
F 3 HOH 37  537 386 HOH HOH B . 
F 3 HOH 38  538 241 HOH HOH B . 
F 3 HOH 39  539 15  HOH HOH B . 
F 3 HOH 40  540 359 HOH HOH B . 
F 3 HOH 41  541 207 HOH HOH B . 
F 3 HOH 42  542 88  HOH HOH B . 
F 3 HOH 43  543 265 HOH HOH B . 
F 3 HOH 44  544 415 HOH HOH B . 
F 3 HOH 45  545 81  HOH HOH B . 
F 3 HOH 46  546 53  HOH HOH B . 
F 3 HOH 47  547 186 HOH HOH B . 
F 3 HOH 48  548 36  HOH HOH B . 
F 3 HOH 49  549 104 HOH HOH B . 
F 3 HOH 50  550 138 HOH HOH B . 
F 3 HOH 51  551 439 HOH HOH B . 
F 3 HOH 52  552 10  HOH HOH B . 
F 3 HOH 53  553 190 HOH HOH B . 
F 3 HOH 54  554 536 HOH HOH B . 
F 3 HOH 55  555 486 HOH HOH B . 
F 3 HOH 56  556 316 HOH HOH B . 
F 3 HOH 57  557 168 HOH HOH B . 
F 3 HOH 58  558 620 HOH HOH B . 
F 3 HOH 59  559 487 HOH HOH B . 
F 3 HOH 60  560 103 HOH HOH B . 
F 3 HOH 61  561 609 HOH HOH B . 
F 3 HOH 62  562 330 HOH HOH B . 
F 3 HOH 63  563 476 HOH HOH B . 
F 3 HOH 64  564 264 HOH HOH B . 
F 3 HOH 65  565 35  HOH HOH B . 
F 3 HOH 66  566 79  HOH HOH B . 
F 3 HOH 67  567 153 HOH HOH B . 
F 3 HOH 68  568 498 HOH HOH B . 
F 3 HOH 69  569 392 HOH HOH B . 
F 3 HOH 70  570 57  HOH HOH B . 
F 3 HOH 71  571 339 HOH HOH B . 
F 3 HOH 72  572 398 HOH HOH B . 
F 3 HOH 73  573 226 HOH HOH B . 
F 3 HOH 74  574 353 HOH HOH B . 
F 3 HOH 75  575 87  HOH HOH B . 
F 3 HOH 76  576 648 HOH HOH B . 
F 3 HOH 77  577 95  HOH HOH B . 
F 3 HOH 78  578 24  HOH HOH B . 
F 3 HOH 79  579 61  HOH HOH B . 
F 3 HOH 80  580 230 HOH HOH B . 
F 3 HOH 81  581 355 HOH HOH B . 
F 3 HOH 82  582 32  HOH HOH B . 
F 3 HOH 83  583 20  HOH HOH B . 
F 3 HOH 84  584 60  HOH HOH B . 
F 3 HOH 85  585 435 HOH HOH B . 
F 3 HOH 86  586 62  HOH HOH B . 
F 3 HOH 87  587 49  HOH HOH B . 
F 3 HOH 88  588 100 HOH HOH B . 
F 3 HOH 89  589 162 HOH HOH B . 
F 3 HOH 90  590 170 HOH HOH B . 
F 3 HOH 91  591 26  HOH HOH B . 
F 3 HOH 92  592 71  HOH HOH B . 
F 3 HOH 93  593 29  HOH HOH B . 
F 3 HOH 94  594 142 HOH HOH B . 
F 3 HOH 95  595 284 HOH HOH B . 
F 3 HOH 96  596 543 HOH HOH B . 
F 3 HOH 97  597 227 HOH HOH B . 
F 3 HOH 98  598 169 HOH HOH B . 
F 3 HOH 99  599 550 HOH HOH B . 
F 3 HOH 100 600 500 HOH HOH B . 
F 3 HOH 101 601 130 HOH HOH B . 
F 3 HOH 102 602 566 HOH HOH B . 
F 3 HOH 103 603 92  HOH HOH B . 
F 3 HOH 104 604 302 HOH HOH B . 
F 3 HOH 105 605 361 HOH HOH B . 
F 3 HOH 106 606 465 HOH HOH B . 
F 3 HOH 107 607 378 HOH HOH B . 
F 3 HOH 108 608 217 HOH HOH B . 
F 3 HOH 109 609 578 HOH HOH B . 
F 3 HOH 110 610 231 HOH HOH B . 
F 3 HOH 111 611 174 HOH HOH B . 
F 3 HOH 112 612 175 HOH HOH B . 
F 3 HOH 113 613 63  HOH HOH B . 
F 3 HOH 114 614 473 HOH HOH B . 
F 3 HOH 115 615 292 HOH HOH B . 
F 3 HOH 116 616 44  HOH HOH B . 
F 3 HOH 117 617 72  HOH HOH B . 
F 3 HOH 118 618 6   HOH HOH B . 
F 3 HOH 119 619 493 HOH HOH B . 
F 3 HOH 120 620 358 HOH HOH B . 
F 3 HOH 121 621 582 HOH HOH B . 
F 3 HOH 122 622 222 HOH HOH B . 
F 3 HOH 123 623 496 HOH HOH B . 
F 3 HOH 124 624 83  HOH HOH B . 
F 3 HOH 125 625 194 HOH HOH B . 
F 3 HOH 126 626 218 HOH HOH B . 
F 3 HOH 127 627 135 HOH HOH B . 
F 3 HOH 128 628 128 HOH HOH B . 
F 3 HOH 129 629 577 HOH HOH B . 
F 3 HOH 130 630 317 HOH HOH B . 
F 3 HOH 131 631 101 HOH HOH B . 
F 3 HOH 132 632 393 HOH HOH B . 
F 3 HOH 133 633 12  HOH HOH B . 
F 3 HOH 134 634 438 HOH HOH B . 
F 3 HOH 135 635 345 HOH HOH B . 
F 3 HOH 136 636 399 HOH HOH B . 
F 3 HOH 137 637 657 HOH HOH B . 
F 3 HOH 138 638 663 HOH HOH B . 
F 3 HOH 139 639 472 HOH HOH B . 
F 3 HOH 140 640 33  HOH HOH B . 
F 3 HOH 141 641 121 HOH HOH B . 
F 3 HOH 142 642 337 HOH HOH B . 
F 3 HOH 143 643 188 HOH HOH B . 
F 3 HOH 144 644 117 HOH HOH B . 
F 3 HOH 145 645 70  HOH HOH B . 
F 3 HOH 146 646 552 HOH HOH B . 
F 3 HOH 147 647 253 HOH HOH B . 
F 3 HOH 148 648 263 HOH HOH B . 
F 3 HOH 149 649 118 HOH HOH B . 
F 3 HOH 150 650 187 HOH HOH B . 
F 3 HOH 151 651 497 HOH HOH B . 
F 3 HOH 152 652 329 HOH HOH B . 
F 3 HOH 153 653 148 HOH HOH B . 
F 3 HOH 154 654 16  HOH HOH B . 
F 3 HOH 155 655 224 HOH HOH B . 
F 3 HOH 156 656 43  HOH HOH B . 
F 3 HOH 157 657 401 HOH HOH B . 
F 3 HOH 158 658 210 HOH HOH B . 
F 3 HOH 159 659 424 HOH HOH B . 
F 3 HOH 160 660 608 HOH HOH B . 
F 3 HOH 161 661 106 HOH HOH B . 
F 3 HOH 162 662 282 HOH HOH B . 
F 3 HOH 163 663 301 HOH HOH B . 
F 3 HOH 164 664 255 HOH HOH B . 
F 3 HOH 165 665 45  HOH HOH B . 
F 3 HOH 166 666 272 HOH HOH B . 
F 3 HOH 167 667 199 HOH HOH B . 
F 3 HOH 168 668 14  HOH HOH B . 
F 3 HOH 169 669 2   HOH HOH B . 
F 3 HOH 170 670 419 HOH HOH B . 
F 3 HOH 171 671 144 HOH HOH B . 
F 3 HOH 172 672 382 HOH HOH B . 
F 3 HOH 173 673 122 HOH HOH B . 
F 3 HOH 174 674 191 HOH HOH B . 
F 3 HOH 175 675 320 HOH HOH B . 
F 3 HOH 176 676 686 HOH HOH B . 
F 3 HOH 177 677 67  HOH HOH B . 
F 3 HOH 178 678 185 HOH HOH B . 
F 3 HOH 179 679 630 HOH HOH B . 
F 3 HOH 180 680 48  HOH HOH B . 
F 3 HOH 181 681 555 HOH HOH B . 
F 3 HOH 182 682 381 HOH HOH B . 
F 3 HOH 183 683 155 HOH HOH B . 
F 3 HOH 184 684 682 HOH HOH B . 
F 3 HOH 185 685 105 HOH HOH B . 
F 3 HOH 186 686 166 HOH HOH B . 
F 3 HOH 187 687 627 HOH HOH B . 
F 3 HOH 188 688 150 HOH HOH B . 
F 3 HOH 189 689 261 HOH HOH B . 
F 3 HOH 190 690 40  HOH HOH B . 
F 3 HOH 191 691 516 HOH HOH B . 
F 3 HOH 192 692 111 HOH HOH B . 
F 3 HOH 193 693 461 HOH HOH B . 
F 3 HOH 194 694 343 HOH HOH B . 
F 3 HOH 195 695 375 HOH HOH B . 
F 3 HOH 196 696 615 HOH HOH B . 
F 3 HOH 197 697 483 HOH HOH B . 
F 3 HOH 198 698 491 HOH HOH B . 
F 3 HOH 199 699 324 HOH HOH B . 
F 3 HOH 200 700 271 HOH HOH B . 
F 3 HOH 201 701 488 HOH HOH B . 
F 3 HOH 202 702 192 HOH HOH B . 
F 3 HOH 203 703 621 HOH HOH B . 
F 3 HOH 204 704 237 HOH HOH B . 
F 3 HOH 205 705 91  HOH HOH B . 
F 3 HOH 206 706 656 HOH HOH B . 
F 3 HOH 207 707 172 HOH HOH B . 
F 3 HOH 208 708 250 HOH HOH B . 
F 3 HOH 209 709 600 HOH HOH B . 
F 3 HOH 210 710 383 HOH HOH B . 
F 3 HOH 211 711 562 HOH HOH B . 
F 3 HOH 212 712 529 HOH HOH B . 
F 3 HOH 213 713 108 HOH HOH B . 
F 3 HOH 214 714 492 HOH HOH B . 
F 3 HOH 215 715 350 HOH HOH B . 
F 3 HOH 216 716 235 HOH HOH B . 
F 3 HOH 217 717 664 HOH HOH B . 
F 3 HOH 218 718 277 HOH HOH B . 
F 3 HOH 219 719 180 HOH HOH B . 
F 3 HOH 220 720 643 HOH HOH B . 
F 3 HOH 221 721 417 HOH HOH B . 
F 3 HOH 222 722 50  HOH HOH B . 
F 3 HOH 223 723 220 HOH HOH B . 
F 3 HOH 224 724 501 HOH HOH B . 
F 3 HOH 225 725 352 HOH HOH B . 
F 3 HOH 226 726 299 HOH HOH B . 
F 3 HOH 227 727 453 HOH HOH B . 
F 3 HOH 228 728 300 HOH HOH B . 
F 3 HOH 229 729 115 HOH HOH B . 
F 3 HOH 230 730 374 HOH HOH B . 
F 3 HOH 231 731 534 HOH HOH B . 
F 3 HOH 232 732 126 HOH HOH B . 
F 3 HOH 233 733 318 HOH HOH B . 
F 3 HOH 234 734 440 HOH HOH B . 
F 3 HOH 235 735 370 HOH HOH B . 
F 3 HOH 236 736 266 HOH HOH B . 
F 3 HOH 237 737 363 HOH HOH B . 
F 3 HOH 238 738 395 HOH HOH B . 
F 3 HOH 239 739 86  HOH HOH B . 
F 3 HOH 240 740 692 HOH HOH B . 
F 3 HOH 241 741 474 HOH HOH B . 
F 3 HOH 242 742 46  HOH HOH B . 
F 3 HOH 243 743 409 HOH HOH B . 
F 3 HOH 244 744 262 HOH HOH B . 
F 3 HOH 245 745 591 HOH HOH B . 
F 3 HOH 246 746 140 HOH HOH B . 
F 3 HOH 247 747 244 HOH HOH B . 
F 3 HOH 248 748 315 HOH HOH B . 
F 3 HOH 249 749 557 HOH HOH B . 
F 3 HOH 250 750 448 HOH HOH B . 
F 3 HOH 251 751 369 HOH HOH B . 
F 3 HOH 252 752 403 HOH HOH B . 
F 3 HOH 253 753 459 HOH HOH B . 
F 3 HOH 254 754 524 HOH HOH B . 
F 3 HOH 255 755 528 HOH HOH B . 
F 3 HOH 256 756 267 HOH HOH B . 
F 3 HOH 257 757 676 HOH HOH B . 
F 3 HOH 258 758 513 HOH HOH B . 
F 3 HOH 259 759 451 HOH HOH B . 
F 3 HOH 260 760 179 HOH HOH B . 
F 3 HOH 261 761 3   HOH HOH B . 
F 3 HOH 262 762 688 HOH HOH B . 
F 3 HOH 263 763 624 HOH HOH B . 
F 3 HOH 264 764 421 HOH HOH B . 
F 3 HOH 265 765 558 HOH HOH B . 
F 3 HOH 266 766 481 HOH HOH B . 
F 3 HOH 267 767 286 HOH HOH B . 
F 3 HOH 268 768 348 HOH HOH B . 
F 3 HOH 269 769 464 HOH HOH B . 
F 3 HOH 270 770 59  HOH HOH B . 
F 3 HOH 271 771 601 HOH HOH B . 
F 3 HOH 272 772 321 HOH HOH B . 
F 3 HOH 273 773 652 HOH HOH B . 
F 3 HOH 274 774 351 HOH HOH B . 
F 3 HOH 275 775 349 HOH HOH B . 
F 3 HOH 276 776 579 HOH HOH B . 
F 3 HOH 277 777 525 HOH HOH B . 
F 3 HOH 278 778 565 HOH HOH B . 
F 3 HOH 279 779 571 HOH HOH B . 
F 3 HOH 280 780 430 HOH HOH B . 
F 3 HOH 281 781 228 HOH HOH B . 
F 3 HOH 282 782 650 HOH HOH B . 
F 3 HOH 283 783 640 HOH HOH B . 
F 3 HOH 284 784 523 HOH HOH B . 
F 3 HOH 285 785 480 HOH HOH B . 
F 3 HOH 286 786 94  HOH HOH B . 
F 3 HOH 287 787 633 HOH HOH B . 
F 3 HOH 288 788 146 HOH HOH B . 
F 3 HOH 289 789 298 HOH HOH B . 
F 3 HOH 290 790 258 HOH HOH B . 
F 3 HOH 291 791 545 HOH HOH B . 
F 3 HOH 292 792 223 HOH HOH B . 
F 3 HOH 293 793 257 HOH HOH B . 
F 3 HOH 294 794 665 HOH HOH B . 
F 3 HOH 295 795 554 HOH HOH B . 
F 3 HOH 296 796 574 HOH HOH B . 
F 3 HOH 297 797 581 HOH HOH B . 
F 3 HOH 298 798 685 HOH HOH B . 
F 3 HOH 299 799 561 HOH HOH B . 
F 3 HOH 300 800 484 HOH HOH B . 
F 3 HOH 301 801 346 HOH HOH B . 
F 3 HOH 302 802 649 HOH HOH B . 
F 3 HOH 303 803 549 HOH HOH B . 
F 3 HOH 304 804 291 HOH HOH B . 
F 3 HOH 305 805 275 HOH HOH B . 
F 3 HOH 306 806 373 HOH HOH B . 
F 3 HOH 307 807 641 HOH HOH B . 
F 3 HOH 308 808 585 HOH HOH B . 
F 3 HOH 309 809 198 HOH HOH B . 
F 3 HOH 310 810 240 HOH HOH B . 
F 3 HOH 311 811 628 HOH HOH B . 
F 3 HOH 312 812 668 HOH HOH B . 
F 3 HOH 313 813 456 HOH HOH B . 
F 3 HOH 314 814 593 HOH HOH B . 
F 3 HOH 315 815 622 HOH HOH B . 
F 3 HOH 316 816 539 HOH HOH B . 
F 3 HOH 317 817 547 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   ? ? ? 1.16-3549-000 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .             2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .             3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .             4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   126.97 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JVA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     115.661 
_cell.length_a_esd                 ? 
_cell.length_b                     94.218 
_cell.length_b_esd                 ? 
_cell.length_c                     84.762 
_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                         9JVA 
_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                   9JVA 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.09 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.25 
_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    
;0.2 M Magnesium formate dihydrate 
(15-25 % w/v) Polyethylene glycol 3350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     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         2024-03-25 
_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   0.97 
_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        0.97 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JVA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.56 
_reflns.d_resolution_low                               66 
_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                                     65530 
_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                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10 
_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                              0.099 
_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                                    1.56 
_reflns_shell.d_res_low                                     1.64 
_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                             1348 
_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                                  0.534 
_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                                 9JVA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.08 
_refine.ls_d_res_low                             33.86 
_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                     65530 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.7 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1945 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1661 
_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                       2.08 
_refine_hist.d_res_low                        33.86 
_refine_hist.number_atoms_solvent             667 
_refine_hist.number_atoms_total               6855 
_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        6156 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_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                  0.1945 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1661 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.d_res_high                       2.08 
_refine_ls_shell.d_res_low                        2.28 
_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                10189 
_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               96.6 
_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                     9JVA 
_struct.title                        
'Three-dimensional structure of homo-dimer of cystathione beta lyase/PLP complex 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        9JVA 
_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 ? 
E N N 3 ? 
F N N 3 ? 
# 
_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 9JVA A 1 ? 390 ? A0AAC9VP02 1 ? 390 ? 1 390 
2 1 9JVA 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 9JVA GLU A 311 ? UNP A0AAC9VP02 VAL 311 'engineered mutation' 311 1 
1 9JVA ASP A 326 ? UNP A0AAC9VP02 ASN 326 'engineered mutation' 326 2 
2 9JVA GLU B 311 ? UNP A0AAC9VP02 VAL 311 'engineered mutation' 311 3 
2 9JVA 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)' 5560  ? 
1 MORE         -36   ? 
1 'SSA (A^2)'  28800 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 PRO A 213 ? VAL A 217 ? PRO A 213 VAL A 217 5 ? 5  
HELX_P HELX_P9  AA9 ASP A 218 ? ASN A 223 ? ASP A 218 ASN A 223 1 ? 6  
HELX_P HELX_P10 AB1 SER A 230 ? ASN A 236 ? SER A 230 ASN A 236 1 ? 7  
HELX_P HELX_P11 AB2 LEU A 237 ? HIS A 241 ? LEU A 237 HIS A 241 5 ? 5  
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 387 ? PRO A 370 ASN A 387 1 ? 18 
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 ALA B 221 ? ASN B 223 ? ALA B 221 ASN B 223 5 ? 3  
HELX_P HELX_P30 AD3 PRO B 231 ? ASN B 236 ? PRO B 231 ASN B 236 1 ? 6  
HELX_P HELX_P31 AD4 LEU B 237 ? HIS B 241 ? LEU B 237 HIS B 241 5 ? 5  
HELX_P HELX_P32 AD5 ASN B 249 ? GLY B 264 ? ASN B 249 GLY B 264 1 ? 16 
HELX_P HELX_P33 AD6 LEU B 271 ? GLY B 283 ? LEU B 271 GLY B 283 1 ? 13 
HELX_P HELX_P34 AD7 GLY B 283 ? VAL B 309 ? GLY B 283 VAL B 309 1 ? 27 
HELX_P HELX_P35 AD8 SER B 328 ? GLY B 331 ? SER B 328 GLY B 331 5 ? 4  
HELX_P HELX_P36 AD9 ASN B 333 ? GLY B 346 ? ASN B 333 GLY B 346 1 ? 14 
HELX_P HELX_P37 AE1 ASN B 353 ? ARG B 356 ? ASN B 353 ARG B 356 5 ? 4  
HELX_P HELX_P38 AE2 ASN B 358 ? HIS B 360 ? ASN B 358 HIS B 360 5 ? 3  
HELX_P HELX_P39 AE3 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 0.76  
2 ASN 167 A . ? ASN 167 A PRO 168 A ? PRO 168 A 1 0.23  
3 ASN 170 A . ? ASN 170 A PRO 171 A ? PRO 171 A 1 21.08 
4 GLU 115 B . ? GLU 115 B PRO 116 B ? PRO 116 B 1 -0.98 
5 ASN 167 B . ? ASN 167 B PRO 168 B ? PRO 168 B 1 -1.38 
6 ASN 170 B . ? ASN 170 B PRO 171 B ? PRO 171 B 1 17.99 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 7 ? 
AA7 ? 2 ? 
AA8 ? 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 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 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 ILE A 138 ? GLU A 140 ? ILE A 138 GLU A 140 
AA3 2 LYS A 143 ? SER A 145 ? LYS A 143 SER A 145 
AA4 1 LYS A 313 ? VAL A 314 ? LYS A 313 VAL A 314 
AA4 2 LEU A 322 ? ASP A 326 ? LEU A 322 ASP A 326 
AA4 3 PHE A 362 ? ASN A 366 ? PHE A 362 ASN A 366 
AA4 4 SER A 350 ? ALA A 351 ? SER A 350 ALA A 351 
AA5 1 LEU B 29  ? PRO B 30  ? LEU B 29  PRO B 30  
AA5 2 LEU B 347 ? ILE B 348 ? LEU B 347 ILE B 348 
AA6 1 CYS B 87  ? ALA B 90  ? CYS B 87  ALA B 90  
AA6 2 ALA B 243 ? ILE B 246 ? ALA B 243 ILE B 246 
AA6 3 VAL B 225 ? ILE B 229 ? VAL B 225 ILE B 229 
AA6 4 LEU B 194 ? ASP B 198 ? LEU B 194 ASP B 198 
AA6 5 VAL B 160 ? CYS B 166 ? VAL B 160 CYS B 166 
AA6 6 GLN B 110 ? VAL B 113 ? GLN B 110 VAL B 113 
AA6 7 ARG B 131 ? SER B 134 ? ARG B 131 SER B 134 
AA7 1 ILE B 138 ? GLU B 140 ? ILE B 138 GLU B 140 
AA7 2 LYS B 143 ? SER B 145 ? LYS B 143 SER B 145 
AA8 1 LYS B 313 ? VAL B 314 ? LYS B 313 VAL B 314 
AA8 2 LEU B 322 ? ASP B 326 ? LEU B 322 ASP B 326 
AA8 3 PHE B 362 ? ASN B 366 ? PHE B 362 ASN B 366 
AA8 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 ILE A 138 ? N ILE A 138 O SER A 145 ? O SER A 145 
AA4 1 2 N LYS A 313 ? N LYS A 313 O ASP A 326 ? O ASP A 326 
AA4 2 3 N ALA A 323 ? N ALA A 323 O ILE A 365 ? O ILE A 365 
AA4 3 4 O ARG A 364 ? O ARG A 364 N SER A 350 ? N SER A 350 
AA5 1 2 N LEU B 29  ? N LEU B 29  O ILE B 348 ? O ILE B 348 
AA6 1 2 N VAL B 88  ? N VAL B 88  O ALA B 245 ? O ALA B 245 
AA6 2 3 O ILE B 246 ? O ILE B 246 N SER B 227 ? N SER B 227 
AA6 3 4 O VAL B 226 ? O VAL B 226 N SER B 197 ? N SER B 197 
AA6 4 5 O ILE B 196 ? O ILE B 196 N MET B 163 ? N MET B 163 
AA6 5 6 O MET B 162 ? O MET B 162 N LEU B 112 ? N LEU B 112 
AA6 6 7 N ILE B 111 ? N ILE B 111 O ARG B 131 ? O ARG B 131 
AA7 1 2 N ILE B 138 ? N ILE B 138 O SER B 145 ? O SER B 145 
AA8 1 2 N LYS B 313 ? N LYS B 313 O ASP B 326 ? O ASP B 326 
AA8 2 3 N ALA B 323 ? N ALA B 323 O ILE B 365 ? O ILE B 365 
AA8 3 4 O ARG B 364 ? O ARG B 364 N SER B 350 ? N SER B 350 
# 
_pdbx_entry_details.entry_id                   9JVA 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NZ B LYS 233 ? ? O4A B PLP 401 ? ? 1.29 
2 1 NZ A LYS 233 ? ? O4A A PLP 401 ? ? 1.30 
3 1 CE B LYS 233 ? ? O4A B PLP 401 ? ? 1.45 
4 1 CE A LYS 233 ? ? O4A A PLP 401 ? ? 1.57 
5 1 NZ A LYS 233 ? ? C4A A PLP 401 ? ? 1.84 
# 
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  ? ? -91.12  37.84   
2  1 TRP A 32  ? ? -108.35 -63.34  
3  1 ASP A 37  ? ? -106.89 44.41   
4  1 TYR A 118 ? ? -39.42  127.58  
5  1 SER A 320 ? ? 79.04   167.07  
6  1 ARG A 356 ? ? 55.90   -145.14 
7  1 LYS B 27  ? ? 68.52   -1.06   
8  1 TRP B 32  ? ? -111.45 -73.43  
9  1 ASP B 37  ? ? -103.07 43.10   
10 1 ALA B 80  ? ? -150.92 89.39   
11 1 TYR B 118 ? ? -36.56  127.69  
12 1 SER B 320 ? ? 79.31   162.80  
13 1 ARG B 356 ? ? 57.65   -147.88 
# 
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 541 ? E HOH . 
2 1 A HOH 789 ? E HOH . 
3 1 A HOH 790 ? E HOH . 
4 1 B HOH 747 ? F HOH . 
5 1 B HOH 777 ? F HOH . 
6 1 B HOH 784 ? F HOH . 
7 1 B HOH 788 ? F HOH . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 850 ? 6.35 . 
2 1 O ? B HOH 817 ? 6.12 . 
# 
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 GLU 3 ? B GLU 3 
# 
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 
PLP N1   N Y N 273 
PLP C2   C Y N 274 
PLP C2A  C N N 275 
PLP C3   C Y N 276 
PLP O3   O N N 277 
PLP C4   C Y N 278 
PLP C4A  C N N 279 
PLP O4A  O N N 280 
PLP C5   C Y N 281 
PLP C6   C Y N 282 
PLP C5A  C N N 283 
PLP O4P  O N N 284 
PLP P    P N N 285 
PLP O1P  O N N 286 
PLP O2P  O N N 287 
PLP O3P  O N N 288 
PLP H2A1 H N N 289 
PLP H2A2 H N N 290 
PLP H2A3 H N N 291 
PLP HO3  H N N 292 
PLP H4A  H N N 293 
PLP H6   H N N 294 
PLP H5A1 H N N 295 
PLP H5A2 H N N 296 
PLP HOP2 H N N 297 
PLP HOP3 H N N 298 
PRO N    N N N 299 
PRO CA   C N S 300 
PRO C    C N N 301 
PRO O    O N N 302 
PRO CB   C N N 303 
PRO CG   C N N 304 
PRO CD   C N N 305 
PRO OXT  O N N 306 
PRO H    H N N 307 
PRO HA   H N N 308 
PRO HB2  H N N 309 
PRO HB3  H N N 310 
PRO HG2  H N N 311 
PRO HG3  H N N 312 
PRO HD2  H N N 313 
PRO HD3  H N N 314 
PRO HXT  H N N 315 
SER N    N N N 316 
SER CA   C N S 317 
SER C    C N N 318 
SER O    O N N 319 
SER CB   C N N 320 
SER OG   O N N 321 
SER OXT  O N N 322 
SER H    H N N 323 
SER H2   H N N 324 
SER HA   H N N 325 
SER HB2  H N N 326 
SER HB3  H N N 327 
SER HG   H N N 328 
SER HXT  H N N 329 
THR N    N N N 330 
THR CA   C N S 331 
THR C    C N N 332 
THR O    O N N 333 
THR CB   C N R 334 
THR OG1  O N N 335 
THR CG2  C N N 336 
THR OXT  O N N 337 
THR H    H N N 338 
THR H2   H N N 339 
THR HA   H N N 340 
THR HB   H N N 341 
THR HG1  H N N 342 
THR HG21 H N N 343 
THR HG22 H N N 344 
THR HG23 H N N 345 
THR HXT  H N N 346 
TRP N    N N N 347 
TRP CA   C N S 348 
TRP C    C N N 349 
TRP O    O N N 350 
TRP CB   C N N 351 
TRP CG   C Y N 352 
TRP CD1  C Y N 353 
TRP CD2  C Y N 354 
TRP NE1  N Y N 355 
TRP CE2  C Y N 356 
TRP CE3  C Y N 357 
TRP CZ2  C Y N 358 
TRP CZ3  C Y N 359 
TRP CH2  C Y N 360 
TRP OXT  O N N 361 
TRP H    H N N 362 
TRP H2   H N N 363 
TRP HA   H N N 364 
TRP HB2  H N N 365 
TRP HB3  H N N 366 
TRP HD1  H N N 367 
TRP HE1  H N N 368 
TRP HE3  H N N 369 
TRP HZ2  H N N 370 
TRP HZ3  H N N 371 
TRP HH2  H N N 372 
TRP HXT  H N N 373 
TYR N    N N N 374 
TYR CA   C N S 375 
TYR C    C N N 376 
TYR O    O N N 377 
TYR CB   C N N 378 
TYR CG   C Y N 379 
TYR CD1  C Y N 380 
TYR CD2  C Y N 381 
TYR CE1  C Y N 382 
TYR CE2  C Y N 383 
TYR CZ   C Y N 384 
TYR OH   O N N 385 
TYR OXT  O N N 386 
TYR H    H N N 387 
TYR H2   H N N 388 
TYR HA   H N N 389 
TYR HB2  H N N 390 
TYR HB3  H N N 391 
TYR HD1  H N N 392 
TYR HD2  H N N 393 
TYR HE1  H N N 394 
TYR HE2  H N N 395 
TYR HH   H N N 396 
TYR HXT  H N N 397 
VAL N    N N N 398 
VAL CA   C N S 399 
VAL C    C N N 400 
VAL O    O N N 401 
VAL CB   C N N 402 
VAL CG1  C N N 403 
VAL CG2  C N N 404 
VAL OXT  O N N 405 
VAL H    H N N 406 
VAL H2   H N N 407 
VAL HA   H N N 408 
VAL HB   H N N 409 
VAL HG11 H N N 410 
VAL HG12 H N N 411 
VAL HG13 H N N 412 
VAL HG21 H N N 413 
VAL HG22 H N N 414 
VAL HG23 H N N 415 
VAL HXT  H N N 416 
# 
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 
PLP N1  C2   doub Y N 260 
PLP N1  C6   sing Y N 261 
PLP C2  C2A  sing N N 262 
PLP C2  C3   sing Y N 263 
PLP C2A H2A1 sing N N 264 
PLP C2A H2A2 sing N N 265 
PLP C2A H2A3 sing N N 266 
PLP C3  O3   sing N N 267 
PLP C3  C4   doub Y N 268 
PLP O3  HO3  sing N N 269 
PLP C4  C4A  sing N N 270 
PLP C4  C5   sing Y N 271 
PLP C4A O4A  doub N N 272 
PLP C4A H4A  sing N N 273 
PLP C5  C6   doub Y N 274 
PLP C5  C5A  sing N N 275 
PLP C6  H6   sing N N 276 
PLP C5A O4P  sing N N 277 
PLP C5A H5A1 sing N N 278 
PLP C5A H5A2 sing N N 279 
PLP O4P P    sing N N 280 
PLP P   O1P  doub N N 281 
PLP P   O2P  sing N N 282 
PLP P   O3P  sing N N 283 
PLP O2P HOP2 sing N N 284 
PLP O3P HOP3 sing N N 285 
PRO N   CA   sing N N 286 
PRO N   CD   sing N N 287 
PRO N   H    sing N N 288 
PRO CA  C    sing N N 289 
PRO CA  CB   sing N N 290 
PRO CA  HA   sing N N 291 
PRO C   O    doub N N 292 
PRO C   OXT  sing N N 293 
PRO CB  CG   sing N N 294 
PRO CB  HB2  sing N N 295 
PRO CB  HB3  sing N N 296 
PRO CG  CD   sing N N 297 
PRO CG  HG2  sing N N 298 
PRO CG  HG3  sing N N 299 
PRO CD  HD2  sing N N 300 
PRO CD  HD3  sing N N 301 
PRO OXT HXT  sing N N 302 
SER N   CA   sing N N 303 
SER N   H    sing N N 304 
SER N   H2   sing N N 305 
SER CA  C    sing N N 306 
SER CA  CB   sing N N 307 
SER CA  HA   sing N N 308 
SER C   O    doub N N 309 
SER C   OXT  sing N N 310 
SER CB  OG   sing N N 311 
SER CB  HB2  sing N N 312 
SER CB  HB3  sing N N 313 
SER OG  HG   sing N N 314 
SER OXT HXT  sing N N 315 
THR N   CA   sing N N 316 
THR N   H    sing N N 317 
THR N   H2   sing N N 318 
THR CA  C    sing N N 319 
THR CA  CB   sing N N 320 
THR CA  HA   sing N N 321 
THR C   O    doub N N 322 
THR C   OXT  sing N N 323 
THR CB  OG1  sing N N 324 
THR CB  CG2  sing N N 325 
THR CB  HB   sing N N 326 
THR OG1 HG1  sing N N 327 
THR CG2 HG21 sing N N 328 
THR CG2 HG22 sing N N 329 
THR CG2 HG23 sing N N 330 
THR OXT HXT  sing N N 331 
TRP N   CA   sing N N 332 
TRP N   H    sing N N 333 
TRP N   H2   sing N N 334 
TRP CA  C    sing N N 335 
TRP CA  CB   sing N N 336 
TRP CA  HA   sing N N 337 
TRP C   O    doub N N 338 
TRP C   OXT  sing N N 339 
TRP CB  CG   sing N N 340 
TRP CB  HB2  sing N N 341 
TRP CB  HB3  sing N N 342 
TRP CG  CD1  doub Y N 343 
TRP CG  CD2  sing Y N 344 
TRP CD1 NE1  sing Y N 345 
TRP CD1 HD1  sing N N 346 
TRP CD2 CE2  doub Y N 347 
TRP CD2 CE3  sing Y N 348 
TRP NE1 CE2  sing Y N 349 
TRP NE1 HE1  sing N N 350 
TRP CE2 CZ2  sing Y N 351 
TRP CE3 CZ3  doub Y N 352 
TRP CE3 HE3  sing N N 353 
TRP CZ2 CH2  doub Y N 354 
TRP CZ2 HZ2  sing N N 355 
TRP CZ3 CH2  sing Y N 356 
TRP CZ3 HZ3  sing N N 357 
TRP CH2 HH2  sing N N 358 
TRP OXT HXT  sing N N 359 
TYR N   CA   sing N N 360 
TYR N   H    sing N N 361 
TYR N   H2   sing N N 362 
TYR CA  C    sing N N 363 
TYR CA  CB   sing N N 364 
TYR CA  HA   sing N N 365 
TYR C   O    doub N N 366 
TYR C   OXT  sing N N 367 
TYR CB  CG   sing N N 368 
TYR CB  HB2  sing N N 369 
TYR CB  HB3  sing N N 370 
TYR CG  CD1  doub Y N 371 
TYR CG  CD2  sing Y N 372 
TYR CD1 CE1  sing Y N 373 
TYR CD1 HD1  sing N N 374 
TYR CD2 CE2  doub Y N 375 
TYR CD2 HD2  sing N N 376 
TYR CE1 CZ   doub Y N 377 
TYR CE1 HE1  sing N N 378 
TYR CE2 CZ   sing Y N 379 
TYR CE2 HE2  sing N N 380 
TYR CZ  OH   sing N N 381 
TYR OH  HH   sing N N 382 
TYR OXT HXT  sing N N 383 
VAL N   CA   sing N N 384 
VAL N   H    sing N N 385 
VAL N   H2   sing N N 386 
VAL CA  C    sing N N 387 
VAL CA  CB   sing N N 388 
VAL CA  HA   sing N N 389 
VAL C   O    doub N N 390 
VAL C   OXT  sing N N 391 
VAL CB  CG1  sing N N 392 
VAL CB  CG2  sing N N 393 
VAL CB  HB   sing N N 394 
VAL CG1 HG11 sing N N 395 
VAL CG1 HG12 sing N N 396 
VAL CG1 HG13 sing N N 397 
VAL CG2 HG21 sing N N 398 
VAL CG2 HG22 sing N N 399 
VAL CG2 HG23 sing N N 400 
VAL OXT HXT  sing N N 401 
# 
_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                    9JVA 
_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]   0.008646 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006508 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010614 
_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]   0.014767 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 4   ? 45.164  15.768  26.728  1.00 48.99 ?  4   LYS A N   1 
ATOM   2    C CA  . LYS A 1 4   ? 43.771  15.398  26.362  1.00 45.73 ?  4   LYS A CA  1 
ATOM   3    C C   . LYS A 1 4   ? 42.982  14.879  27.568  1.00 40.86 ?  4   LYS A C   1 
ATOM   4    O O   . LYS A 1 4   ? 43.500  14.008  28.265  1.00 39.65 ?  4   LYS A O   1 
ATOM   5    C CB  . LYS A 1 4   ? 43.742  14.341  25.259  1.00 44.00 ?  4   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 4   ? 44.000  14.851  23.846  1.00 44.26 ?  4   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 4   ? 42.757  15.000  23.001  1.00 38.56 ?  4   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 4   ? 42.851  16.178  22.054  1.00 38.73 ?  4   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 4   ? 41.815  16.132  21.000  1.00 28.22 1  4   LYS A NZ  1 
ATOM   10   N N   . GLN A 1 5   ? 41.748  15.310  27.757  1.00 36.70 ?  5   GLN A N   1 
ATOM   11   C CA  . GLN A 1 5   ? 40.961  14.865  28.913  1.00 32.77 ?  5   GLN A CA  1 
ATOM   12   C C   . GLN A 1 5   ? 40.448  13.463  28.633  1.00 29.80 ?  5   GLN A C   1 
ATOM   13   O O   . GLN A 1 5   ? 40.402  12.675  29.562  1.00 30.88 ?  5   GLN A O   1 
ATOM   14   C CB  . GLN A 1 5   ? 39.798  15.833  29.094  1.00 29.67 ?  5   GLN A CB  1 
ATOM   15   C CG  . GLN A 1 5   ? 38.786  15.401  30.144  1.00 33.06 ?  5   GLN A CG  1 
ATOM   16   C CD  . GLN A 1 5   ? 37.790  16.471  30.516  1.00 37.45 ?  5   GLN A CD  1 
ATOM   17   O OE1 . GLN A 1 5   ? 37.467  17.357  29.729  1.00 40.14 ?  5   GLN A OE1 1 
ATOM   18   N NE2 . GLN A 1 5   ? 37.284  16.384  31.734  1.00 40.30 ?  5   GLN A NE2 1 
ATOM   19   N N   . TYR A 1 6   ? 40.209  13.141  27.367  1.00 24.35 ?  6   TYR A N   1 
ATOM   20   C CA  . TYR A 1 6   ? 39.523  11.904  27.034  1.00 22.82 ?  6   TYR A CA  1 
ATOM   21   C C   . TYR A 1 6   ? 40.420  11.003  26.202  1.00 24.36 ?  6   TYR A C   1 
ATOM   22   O O   . TYR A 1 6   ? 41.436  11.433  25.644  1.00 22.15 ?  6   TYR A O   1 
ATOM   23   C CB  . TYR A 1 6   ? 38.220  12.183  26.270  1.00 20.98 ?  6   TYR A CB  1 
ATOM   24   C CG  . TYR A 1 6   ? 37.267  13.137  26.971  1.00 22.46 ?  6   TYR A CG  1 
ATOM   25   C CD1 . TYR A 1 6   ? 36.512  12.723  28.057  1.00 22.47 ?  6   TYR A CD1 1 
ATOM   26   C CD2 . TYR A 1 6   ? 37.123  14.443  26.547  1.00 23.43 ?  6   TYR A CD2 1 
ATOM   27   C CE1 . TYR A 1 6   ? 35.630  13.587  28.690  1.00 22.52 ?  6   TYR A CE1 1 
ATOM   28   C CE2 . TYR A 1 6   ? 36.249  15.316  27.180  1.00 22.98 ?  6   TYR A CE2 1 
ATOM   29   C CZ  . TYR A 1 6   ? 35.508  14.881  28.251  1.00 21.48 ?  6   TYR A CZ  1 
ATOM   30   O OH  . TYR A 1 6   ? 34.636  15.742  28.880  1.00 22.07 ?  6   TYR A OH  1 
ATOM   31   N N   . ASP A 1 7   ? 40.011  9.743   26.102  1.00 20.99 ?  7   ASP A N   1 
ATOM   32   C CA  . ASP A 1 7   ? 40.823  8.703   25.485  1.00 21.66 ?  7   ASP A CA  1 
ATOM   33   C C   . ASP A 1 7   ? 40.454  8.559   24.011  1.00 21.34 ?  7   ASP A C   1 
ATOM   34   O O   . ASP A 1 7   ? 39.338  8.146   23.678  1.00 20.51 ?  7   ASP A O   1 
ATOM   35   C CB  . ASP A 1 7   ? 40.632  7.387   26.239  1.00 24.39 ?  7   ASP A CB  1 
ATOM   36   C CG  . ASP A 1 7   ? 41.433  6.230   25.652  1.00 24.45 ?  7   ASP A CG  1 
ATOM   37   O OD1 . ASP A 1 7   ? 42.076  6.358   24.588  1.00 25.32 ?  7   ASP A OD1 1 
ATOM   38   O OD2 . ASP A 1 7   ? 41.449  5.169   26.310  1.00 30.77 -1 7   ASP A OD2 1 
ATOM   39   N N   . PHE A 1 8   ? 41.401  8.882   23.132  1.00 18.45 ?  8   PHE A N   1 
ATOM   40   C CA  . PHE A 1 8   ? 41.255  8.632   21.706  1.00 18.64 ?  8   PHE A CA  1 
ATOM   41   C C   . PHE A 1 8   ? 42.370  7.746   21.170  1.00 19.34 ?  8   PHE A C   1 
ATOM   42   O O   . PHE A 1 8   ? 42.648  7.769   19.962  1.00 18.62 ?  8   PHE A O   1 
ATOM   43   C CB  . PHE A 1 8   ? 41.202  9.953   20.945  1.00 16.34 ?  8   PHE A CB  1 
ATOM   44   C CG  . PHE A 1 8   ? 40.044  10.815  21.338  1.00 16.70 ?  8   PHE A CG  1 
ATOM   45   C CD1 . PHE A 1 8   ? 38.796  10.612  20.766  1.00 16.19 ?  8   PHE A CD1 1 
ATOM   46   C CD2 . PHE A 1 8   ? 40.193  11.819  22.280  1.00 17.73 ?  8   PHE A CD2 1 
ATOM   47   C CE1 . PHE A 1 8   ? 37.724  11.408  21.112  1.00 17.07 ?  8   PHE A CE1 1 
ATOM   48   C CE2 . PHE A 1 8   ? 39.120  12.610  22.631  1.00 17.16 ?  8   PHE A CE2 1 
ATOM   49   C CZ  . PHE A 1 8   ? 37.882  12.401  22.041  1.00 17.49 ?  8   PHE A CZ  1 
ATOM   50   N N   . THR A 1 9   ? 43.016  6.956   22.038  1.00 20.02 ?  9   THR A N   1 
ATOM   51   C CA  . THR A 1 9   ? 44.081  6.069   21.589  1.00 20.64 ?  9   THR A CA  1 
ATOM   52   C C   . THR A 1 9   ? 43.770  4.583   21.717  1.00 21.50 ?  9   THR A C   1 
ATOM   53   O O   . THR A 1 9   ? 44.403  3.787   21.026  1.00 18.23 ?  9   THR A O   1 
ATOM   54   C CB  . THR A 1 9   ? 45.389  6.362   22.344  1.00 21.04 ?  9   THR A CB  1 
ATOM   55   O OG1 . THR A 1 9   ? 45.209  6.101   23.733  1.00 27.36 ?  9   THR A OG1 1 
ATOM   56   C CG2 . THR A 1 9   ? 45.788  7.818   22.179  1.00 24.03 ?  9   THR A CG2 1 
ATOM   57   N N   . HIS A 1 10  ? 42.828  4.172   22.557  1.00 19.64 ?  10  HIS A N   1 
ATOM   58   C CA  . HIS A 1 10  ? 42.578  2.749   22.767  1.00 20.28 ?  10  HIS A CA  1 
ATOM   59   C C   . HIS A 1 10  ? 41.289  2.327   22.072  1.00 20.43 ?  10  HIS A C   1 
ATOM   60   O O   . HIS A 1 10  ? 40.222  2.886   22.339  1.00 20.94 ?  10  HIS A O   1 
ATOM   61   C CB  . HIS A 1 10  ? 42.501  2.419   24.257  1.00 23.42 ?  10  HIS A CB  1 
ATOM   62   C CG  . HIS A 1 10  ? 43.757  2.725   25.000  1.00 23.57 ?  10  HIS A CG  1 
ATOM   63   N ND1 . HIS A 1 10  ? 43.878  3.812   25.839  1.00 27.12 ?  10  HIS A ND1 1 
ATOM   64   C CD2 . HIS A 1 10  ? 44.953  2.094   25.022  1.00 25.18 ?  10  HIS A CD2 1 
ATOM   65   C CE1 . HIS A 1 10  ? 45.094  3.831   26.355  1.00 24.83 ?  10  HIS A CE1 1 
ATOM   66   N NE2 . HIS A 1 10  ? 45.767  2.800   25.872  1.00 24.76 ?  10  HIS A NE2 1 
ATOM   67   N N   . VAL A 1 11  ? 41.386  1.326   21.210  1.00 20.70 ?  11  VAL A N   1 
ATOM   68   C CA  . VAL A 1 11  ? 40.197  0.853   20.488  1.00 18.61 ?  11  VAL A CA  1 
ATOM   69   C C   . VAL A 1 11  ? 39.295  0.077   21.445  1.00 20.03 ?  11  VAL A C   1 
ATOM   70   O O   . VAL A 1 11  ? 39.765  -0.853  22.118  1.00 18.44 ?  11  VAL A O   1 
ATOM   71   C CB  . VAL A 1 11  ? 40.608  -0.021  19.302  1.00 21.24 ?  11  VAL A CB  1 
ATOM   72   C CG1 . VAL A 1 11  ? 39.367  -0.636  18.641  1.00 17.84 ?  11  VAL A CG1 1 
ATOM   73   C CG2 . VAL A 1 11  ? 41.411  0.797   18.300  1.00 18.54 ?  11  VAL A CG2 1 
ATOM   74   N N   . PRO A 1 12  ? 38.004  0.398   21.528  1.00 18.08 ?  12  PRO A N   1 
ATOM   75   C CA  . PRO A 1 12  ? 37.100  -0.390  22.383  1.00 22.23 ?  12  PRO A CA  1 
ATOM   76   C C   . PRO A 1 12  ? 37.053  -1.857  21.978  1.00 17.94 ?  12  PRO A C   1 
ATOM   77   O O   . PRO A 1 12  ? 36.955  -2.186  20.793  1.00 17.42 ?  12  PRO A O   1 
ATOM   78   C CB  . PRO A 1 12  ? 35.740  0.287   22.172  1.00 19.78 ?  12  PRO A CB  1 
ATOM   79   C CG  . PRO A 1 12  ? 36.079  1.690   21.771  1.00 21.81 ?  12  PRO A CG  1 
ATOM   80   C CD  . PRO A 1 12  ? 37.349  1.596   20.970  1.00 20.56 ?  12  PRO A CD  1 
ATOM   81   N N   . LYS A 1 13  ? 37.098  -2.732  22.984  1.00 19.68 ?  13  LYS A N   1 
ATOM   82   C CA  . LYS A 1 13  ? 37.060  -4.188  22.812  1.00 19.07 ?  13  LYS A CA  1 
ATOM   83   C C   . LYS A 1 13  ? 35.608  -4.630  22.677  1.00 19.56 ?  13  LYS A C   1 
ATOM   84   O O   . LYS A 1 13  ? 34.874  -4.704  23.667  1.00 18.79 ?  13  LYS A O   1 
ATOM   85   C CB  . LYS A 1 13  ? 37.717  -4.881  24.000  1.00 20.89 ?  13  LYS A CB  1 
ATOM   86   C CG  . LYS A 1 13  ? 37.800  -6.394  23.874  1.00 24.80 ?  13  LYS A CG  1 
ATOM   87   C CD  . LYS A 1 13  ? 38.528  -6.970  25.076  1.00 34.29 ?  13  LYS A CD  1 
ATOM   88   C CE  . LYS A 1 13  ? 39.678  -7.873  24.655  1.00 34.69 ?  13  LYS A CE  1 
ATOM   89   N NZ  . LYS A 1 13  ? 39.195  -8.995  23.798  1.00 41.43 1  13  LYS A NZ  1 
ATOM   90   N N   . ARG A 1 14  ? 35.188  -4.935  21.453  1.00 16.39 ?  14  ARG A N   1 
ATOM   91   C CA  . ARG A 1 14  ? 33.793  -5.259  21.208  1.00 20.77 ?  14  ARG A CA  1 
ATOM   92   C C   . ARG A 1 14  ? 33.501  -6.720  21.551  1.00 21.24 ?  14  ARG A C   1 
ATOM   93   O O   . ARG A 1 14  ? 34.393  -7.574  21.604  1.00 18.76 ?  14  ARG A O   1 
ATOM   94   C CB  . ARG A 1 14  ? 33.418  -4.998  19.747  1.00 18.28 ?  14  ARG A CB  1 
ATOM   95   C CG  . ARG A 1 14  ? 34.110  -3.798  19.106  1.00 23.79 ?  14  ARG A CG  1 
ATOM   96   C CD  . ARG A 1 14  ? 33.688  -2.467  19.689  1.00 22.12 ?  14  ARG A CD  1 
ATOM   97   N NE  . ARG A 1 14  ? 33.371  -1.501  18.636  1.00 23.17 ?  14  ARG A NE  1 
ATOM   98   C CZ  . ARG A 1 14  ? 34.238  -0.650  18.089  1.00 22.50 ?  14  ARG A CZ  1 
ATOM   99   N NH1 . ARG A 1 14  ? 35.505  -0.615  18.500  1.00 20.56 1  14  ARG A NH1 1 
ATOM   100  N NH2 . ARG A 1 14  ? 33.829  0.184   17.136  1.00 20.39 ?  14  ARG A NH2 1 
ATOM   101  N N   . GLN A 1 15  ? 32.221  -6.995  21.781  1.00 19.36 ?  15  GLN A N   1 
ATOM   102  C CA  . GLN A 1 15  ? 31.745  -8.363  21.788  1.00 21.16 ?  15  GLN A CA  1 
ATOM   103  C C   . GLN A 1 15  ? 31.684  -8.887  20.353  1.00 19.98 ?  15  GLN A C   1 
ATOM   104  O O   . GLN A 1 15  ? 31.870  -8.145  19.376  1.00 19.03 ?  15  GLN A O   1 
ATOM   105  C CB  . GLN A 1 15  ? 30.382  -8.448  22.478  1.00 18.68 ?  15  GLN A CB  1 
ATOM   106  C CG  . GLN A 1 15  ? 30.388  -7.858  23.876  1.00 18.57 ?  15  GLN A CG  1 
ATOM   107  C CD  . GLN A 1 15  ? 29.233  -8.344  24.744  1.00 20.66 ?  15  GLN A CD  1 
ATOM   108  O OE1 . GLN A 1 15  ? 28.188  -8.757  24.241  1.00 20.10 ?  15  GLN A OE1 1 
ATOM   109  N NE2 . GLN A 1 15  ? 29.409  -8.266  26.056  1.00 18.47 ?  15  GLN A NE2 1 
ATOM   110  N N   . GLY A 1 16  ? 31.411  -10.190 20.236  1.00 17.69 ?  16  GLY A N   1 
ATOM   111  C CA  . GLY A 1 16  ? 31.555  -10.889 18.970  1.00 20.14 ?  16  GLY A CA  1 
ATOM   112  C C   . GLY A 1 16  ? 30.589  -10.474 17.878  1.00 18.91 ?  16  GLY A C   1 
ATOM   113  O O   . GLY A 1 16  ? 30.909  -10.635 16.696  1.00 22.39 ?  16  GLY A O   1 
ATOM   114  N N   . ASN A 1 17  ? 29.418  -9.947  18.229  1.00 17.68 ?  17  ASN A N   1 
ATOM   115  C CA  . ASN A 1 17  ? 28.419  -9.643  17.199  1.00 17.86 ?  17  ASN A CA  1 
ATOM   116  C C   . ASN A 1 17  ? 28.538  -8.218  16.661  1.00 21.37 ?  17  ASN A C   1 
ATOM   117  O O   . ASN A 1 17  ? 27.532  -7.557  16.395  1.00 21.09 ?  17  ASN A O   1 
ATOM   118  C CB  . ASN A 1 17  ? 27.014  -9.905  17.743  1.00 16.73 ?  17  ASN A CB  1 
ATOM   119  C CG  . ASN A 1 17  ? 26.623  -8.936  18.833  1.00 17.52 ?  17  ASN A CG  1 
ATOM   120  O OD1 . ASN A 1 17  ? 27.445  -8.573  19.677  1.00 20.74 ?  17  ASN A OD1 1 
ATOM   121  N ND2 . ASN A 1 17  ? 25.368  -8.510  18.826  1.00 17.09 ?  17  ASN A ND2 1 
ATOM   122  N N   . SER A 1 18  ? 29.752  -7.705  16.499  1.00 18.16 ?  18  SER A N   1 
ATOM   123  C CA  . SER A 1 18  ? 29.944  -6.357  15.980  1.00 20.61 ?  18  SER A CA  1 
ATOM   124  C C   . SER A 1 18  ? 29.988  -6.405  14.455  1.00 20.28 ?  18  SER A C   1 
ATOM   125  O O   . SER A 1 18  ? 30.660  -7.265  13.882  1.00 21.66 ?  18  SER A O   1 
ATOM   126  C CB  . SER A 1 18  ? 31.244  -5.768  16.543  1.00 21.50 ?  18  SER A CB  1 
ATOM   127  O OG  . SER A 1 18  ? 31.806  -4.797  15.681  1.00 21.01 ?  18  SER A OG  1 
ATOM   128  N N   . ILE A 1 19  ? 29.260  -5.501  13.795  1.00 16.79 ?  19  ILE A N   1 
ATOM   129  C CA  . ILE A 1 19  ? 29.324  -5.439  12.338  1.00 18.47 ?  19  ILE A CA  1 
ATOM   130  C C   . ILE A 1 19  ? 30.718  -5.029  11.883  1.00 21.92 ?  19  ILE A C   1 
ATOM   131  O O   . ILE A 1 19  ? 31.242  -5.550  10.888  1.00 19.63 ?  19  ILE A O   1 
ATOM   132  C CB  . ILE A 1 19  ? 28.254  -4.479  11.789  1.00 18.98 ?  19  ILE A CB  1 
ATOM   133  C CG1 . ILE A 1 19  ? 26.860  -4.977  12.174  1.00 20.68 ?  19  ILE A CG1 1 
ATOM   134  C CG2 . ILE A 1 19  ? 28.407  -4.320  10.268  1.00 19.78 ?  19  ILE A CG2 1 
ATOM   135  C CD1 . ILE A 1 19  ? 26.375  -6.107  11.345  1.00 22.71 ?  19  ILE A CD1 1 
ATOM   136  N N   . LYS A 1 20  ? 31.339  -4.085  12.596  1.00 18.84 ?  20  LYS A N   1 
ATOM   137  C CA  . LYS A 1 20  ? 32.629  -3.557  12.157  1.00 20.54 ?  20  LYS A CA  1 
ATOM   138  C C   . LYS A 1 20  ? 33.753  -4.544  12.431  1.00 19.93 ?  20  LYS A C   1 
ATOM   139  O O   . LYS A 1 20  ? 34.637  -4.736  11.588  1.00 18.66 ?  20  LYS A O   1 
ATOM   140  C CB  . LYS A 1 20  ? 32.911  -2.210  12.839  1.00 20.00 ?  20  LYS A CB  1 
ATOM   141  C CG  . LYS A 1 20  ? 34.267  -1.596  12.460  1.00 19.03 ?  20  LYS A CG  1 
ATOM   142  C CD  . LYS A 1 20  ? 34.476  -0.177  12.988  1.00 20.19 ?  20  LYS A CD  1 
ATOM   143  C CE  . LYS A 1 20  ? 35.439  0.582   12.060  1.00 20.92 ?  20  LYS A CE  1 
ATOM   144  N NZ  . LYS A 1 20  ? 35.808  1.948   12.531  1.00 18.85 1  20  LYS A NZ  1 
ATOM   145  N N   . TRP A 1 21  ? 33.746  -5.184  13.603  1.00 18.19 ?  21  TRP A N   1 
ATOM   146  C CA  . TRP A 1 21  ? 34.898  -5.967  14.021  1.00 20.26 ?  21  TRP A CA  1 
ATOM   147  C C   . TRP A 1 21  ? 34.636  -7.465  14.091  1.00 24.37 ?  21  TRP A C   1 
ATOM   148  O O   . TRP A 1 21  ? 35.579  -8.227  14.336  1.00 24.95 ?  21  TRP A O   1 
ATOM   149  C CB  . TRP A 1 21  ? 35.403  -5.463  15.375  1.00 18.46 ?  21  TRP A CB  1 
ATOM   150  C CG  . TRP A 1 21  ? 36.120  -4.152  15.267  1.00 20.99 ?  21  TRP A CG  1 
ATOM   151  C CD1 . TRP A 1 21  ? 35.613  -2.903  15.518  1.00 20.83 ?  21  TRP A CD1 1 
ATOM   152  C CD2 . TRP A 1 21  ? 37.481  -3.961  14.871  1.00 18.96 ?  21  TRP A CD2 1 
ATOM   153  N NE1 . TRP A 1 21  ? 36.589  -1.946  15.305  1.00 18.28 ?  21  TRP A NE1 1 
ATOM   154  C CE2 . TRP A 1 21  ? 37.741  -2.574  14.907  1.00 20.10 ?  21  TRP A CE2 1 
ATOM   155  C CE3 . TRP A 1 21  ? 38.507  -4.830  14.498  1.00 21.59 ?  21  TRP A CE3 1 
ATOM   156  C CZ2 . TRP A 1 21  ? 38.988  -2.040  14.587  1.00 18.04 ?  21  TRP A CZ2 1 
ATOM   157  C CZ3 . TRP A 1 21  ? 39.744  -4.298  14.187  1.00 21.68 ?  21  TRP A CZ3 1 
ATOM   158  C CH2 . TRP A 1 21  ? 39.972  -2.918  14.229  1.00 20.15 ?  21  TRP A CH2 1 
ATOM   159  N N   . GLY A 1 22  ? 33.393  -7.910  13.881  1.00 21.91 ?  22  GLY A N   1 
ATOM   160  C CA  . GLY A 1 22  ? 33.101  -9.324  13.956  1.00 24.85 ?  22  GLY A CA  1 
ATOM   161  C C   . GLY A 1 22  ? 33.384  -10.038 12.655  1.00 27.11 ?  22  GLY A C   1 
ATOM   162  O O   . GLY A 1 22  ? 33.391  -9.447  11.575  1.00 30.00 ?  22  GLY A O   1 
ATOM   163  N N   . GLY A 1 23  ? 33.633  -11.340 12.771  1.00 30.41 ?  23  GLY A N   1 
ATOM   164  C CA  . GLY A 1 23  ? 33.820  -12.170 11.594  1.00 31.44 ?  23  GLY A CA  1 
ATOM   165  C C   . GLY A 1 23  ? 35.017  -11.810 10.744  1.00 29.85 ?  23  GLY A C   1 
ATOM   166  O O   . GLY A 1 23  ? 35.022  -12.095 9.543   1.00 33.55 ?  23  GLY A O   1 
ATOM   167  N N   . LEU A 1 24  ? 36.029  -11.175 11.324  1.00 29.03 ?  24  LEU A N   1 
ATOM   168  C CA  . LEU A 1 24  ? 37.212  -10.788 10.574  1.00 28.31 ?  24  LEU A CA  1 
ATOM   169  C C   . LEU A 1 24  ? 38.251  -11.898 10.605  1.00 29.28 ?  24  LEU A C   1 
ATOM   170  O O   . LEU A 1 24  ? 38.302  -12.709 11.531  1.00 30.24 ?  24  LEU A O   1 
ATOM   171  C CB  . LEU A 1 24  ? 37.829  -9.509  11.135  1.00 26.75 ?  24  LEU A CB  1 
ATOM   172  C CG  . LEU A 1 24  ? 36.985  -8.245  11.046  1.00 26.15 ?  24  LEU A CG  1 
ATOM   173  C CD1 . LEU A 1 24  ? 37.718  -7.087  11.715  1.00 24.55 ?  24  LEU A CD1 1 
ATOM   174  C CD2 . LEU A 1 24  ? 36.654  -7.940  9.598   1.00 24.06 ?  24  LEU A CD2 1 
ATOM   175  N N   . LYS A 1 25  ? 39.087  -11.918 9.579   1.00 28.97 ?  25  LYS A N   1 
ATOM   176  C CA  . LYS A 1 25  ? 40.261  -12.765 9.576   1.00 29.29 ?  25  LYS A CA  1 
ATOM   177  C C   . LYS A 1 25  ? 41.415  -12.042 10.256  1.00 31.40 ?  25  LYS A C   1 
ATOM   178  O O   . LYS A 1 25  ? 41.354  -10.840 10.536  1.00 29.90 ?  25  LYS A O   1 
ATOM   179  C CB  . LYS A 1 25  ? 40.624  -13.157 8.152   1.00 30.30 ?  25  LYS A CB  1 
ATOM   180  C CG  . LYS A 1 25  ? 39.589  -14.042 7.517   1.00 32.26 ?  25  LYS A CG  1 
ATOM   181  C CD  . LYS A 1 25  ? 39.749  -14.065 6.018   1.00 34.50 ?  25  LYS A CD  1 
ATOM   182  C CE  . LYS A 1 25  ? 39.076  -15.289 5.454   1.00 32.66 ?  25  LYS A CE  1 
ATOM   183  N NZ  . LYS A 1 25  ? 37.811  -14.916 4.764   1.00 37.37 1  25  LYS A NZ  1 
ATOM   184  N N   . GLU A 1 26  ? 42.470  -12.802 10.542  1.00 33.32 ?  26  GLU A N   1 
ATOM   185  C CA  . GLU A 1 26  ? 43.610  -12.283 11.287  1.00 35.75 ?  26  GLU A CA  1 
ATOM   186  C C   . GLU A 1 26  ? 44.145  -10.997 10.674  1.00 29.44 ?  26  GLU A C   1 
ATOM   187  O O   . GLU A 1 26  ? 44.356  -10.911 9.460   1.00 31.85 ?  26  GLU A O   1 
ATOM   188  C CB  . GLU A 1 26  ? 44.721  -13.332 11.325  1.00 40.46 ?  26  GLU A CB  1 
ATOM   189  C CG  . GLU A 1 26  ? 45.479  -13.399 12.627  1.00 43.65 ?  26  GLU A CG  1 
ATOM   190  C CD  . GLU A 1 26  ? 46.728  -14.250 12.508  1.00 48.65 ?  26  GLU A CD  1 
ATOM   191  O OE1 . GLU A 1 26  ? 47.707  -13.984 13.237  1.00 53.17 ?  26  GLU A OE1 1 
ATOM   192  O OE2 . GLU A 1 26  ? 46.736  -15.181 11.671  1.00 49.69 -1 26  GLU A OE2 1 
ATOM   193  N N   . LYS A 1 27  ? 44.348  -9.997  11.528  1.00 29.63 ?  27  LYS A N   1 
ATOM   194  C CA  . LYS A 1 27  ? 45.003  -8.729  11.211  1.00 30.18 ?  27  LYS A CA  1 
ATOM   195  C C   . LYS A 1 27  ? 44.233  -7.870  10.207  1.00 25.35 ?  27  LYS A C   1 
ATOM   196  O O   . LYS A 1 27  ? 44.785  -6.883  9.705   1.00 24.11 ?  27  LYS A O   1 
ATOM   197  C CB  . LYS A 1 27  ? 46.444  -8.945  10.710  1.00 30.73 ?  27  LYS A CB  1 
ATOM   198  C CG  . LYS A 1 27  ? 47.245  -9.981  11.506  1.00 36.80 ?  27  LYS A CG  1 
ATOM   199  C CD  . LYS A 1 27  ? 48.754  -9.797  11.352  1.00 40.06 ?  27  LYS A CD  1 
ATOM   200  C CE  . LYS A 1 27  ? 49.490  -10.164 12.633  1.00 44.17 ?  27  LYS A CE  1 
ATOM   201  N NZ  . LYS A 1 27  ? 49.267  -11.594 12.991  1.00 48.45 1  27  LYS A NZ  1 
ATOM   202  N N   . GLU A 1 28  ? 42.975  -8.194  9.905   1.00 22.54 ?  28  GLU A N   1 
ATOM   203  C CA  . GLU A 1 28  ? 42.202  -7.327  9.025   1.00 23.52 ?  28  GLU A CA  1 
ATOM   204  C C   . GLU A 1 28  ? 41.875  -6.019  9.739   1.00 21.36 ?  28  GLU A C   1 
ATOM   205  O O   . GLU A 1 28  ? 41.730  -5.971  10.965  1.00 21.65 ?  28  GLU A O   1 
ATOM   206  C CB  . GLU A 1 28  ? 40.926  -8.026  8.545   1.00 23.17 ?  28  GLU A CB  1 
ATOM   207  C CG  . GLU A 1 28  ? 41.183  -9.034  7.419   1.00 24.47 ?  28  GLU A CG  1 
ATOM   208  C CD  . GLU A 1 28  ? 39.910  -9.584  6.788   1.00 26.98 ?  28  GLU A CD  1 
ATOM   209  O OE1 . GLU A 1 28  ? 39.903  -9.796  5.551   1.00 27.70 ?  28  GLU A OE1 1 
ATOM   210  O OE2 . GLU A 1 28  ? 38.929  -9.819  7.522   1.00 26.06 -1 28  GLU A OE2 1 
ATOM   211  N N   . LEU A 1 29  ? 41.806  -4.942  8.962   1.00 20.11 ?  29  LEU A N   1 
ATOM   212  C CA  . LEU A 1 29  ? 41.634  -3.591  9.498   1.00 19.27 ?  29  LEU A CA  1 
ATOM   213  C C   . LEU A 1 29  ? 40.395  -2.962  8.876   1.00 19.03 ?  29  LEU A C   1 
ATOM   214  O O   . LEU A 1 29  ? 40.427  -2.530  7.709   1.00 17.77 ?  29  LEU A O   1 
ATOM   215  C CB  . LEU A 1 29  ? 42.872  -2.736  9.232   1.00 20.39 ?  29  LEU A CB  1 
ATOM   216  C CG  . LEU A 1 29  ? 42.848  -1.271  9.670   1.00 20.40 ?  29  LEU A CG  1 
ATOM   217  C CD1 . LEU A 1 29  ? 42.430  -1.131  11.137  1.00 20.20 ?  29  LEU A CD1 1 
ATOM   218  C CD2 . LEU A 1 29  ? 44.217  -0.668  9.444   1.00 20.70 ?  29  LEU A CD2 1 
ATOM   219  N N   . PRO A 1 30  ? 39.275  -2.914  9.595   1.00 18.09 ?  30  PRO A N   1 
ATOM   220  C CA  . PRO A 1 30  ? 38.031  -2.391  9.019   1.00 15.79 ?  30  PRO A CA  1 
ATOM   221  C C   . PRO A 1 30  ? 38.015  -0.873  9.110   1.00 18.86 ?  30  PRO A C   1 
ATOM   222  O O   . PRO A 1 30  ? 38.188  -0.300  10.192  1.00 18.71 ?  30  PRO A O   1 
ATOM   223  C CB  . PRO A 1 30  ? 36.943  -3.020  9.899   1.00 17.95 ?  30  PRO A CB  1 
ATOM   224  C CG  . PRO A 1 30  ? 37.627  -3.157  11.259  1.00 17.86 ?  30  PRO A CG  1 
ATOM   225  C CD  . PRO A 1 30  ? 39.086  -3.461  10.949  1.00 18.86 ?  30  PRO A CD  1 
ATOM   226  N N   . MET A 1 31  ? 37.825  -0.220  7.968   1.00 16.53 ?  31  MET A N   1 
ATOM   227  C CA  . MET A 1 31  ? 37.677  1.233   7.925   1.00 18.21 ?  31  MET A CA  1 
ATOM   228  C C   . MET A 1 31  ? 36.563  1.618   6.963   1.00 15.79 ?  31  MET A C   1 
ATOM   229  O O   . MET A 1 31  ? 36.663  2.608   6.232   1.00 16.40 ?  31  MET A O   1 
ATOM   230  C CB  . MET A 1 31  ? 38.989  1.912   7.528   1.00 16.65 ?  31  MET A CB  1 
ATOM   231  C CG  . MET A 1 31  ? 40.154  1.583   8.450   1.00 18.10 ?  31  MET A CG  1 
ATOM   232  S SD  . MET A 1 31  ? 41.704  2.359   7.927   1.00 20.87 ?  31  MET A SD  1 
ATOM   233  C CE  . MET A 1 31  ? 41.570  3.952   8.749   1.00 19.89 ?  31  MET A CE  1 
ATOM   234  N N   . TRP A 1 32  ? 35.487  0.832   6.939   1.00 15.29 ?  32  TRP A N   1 
ATOM   235  C CA  . TRP A 1 32  ? 34.410  1.026   5.982   1.00 15.49 ?  32  TRP A CA  1 
ATOM   236  C C   . TRP A 1 32  ? 33.153  1.576   6.648   1.00 19.09 ?  32  TRP A C   1 
ATOM   237  O O   . TRP A 1 32  ? 32.771  2.719   6.386   1.00 22.17 ?  32  TRP A O   1 
ATOM   238  C CB  . TRP A 1 32  ? 34.134  -0.293  5.240   1.00 17.92 ?  32  TRP A CB  1 
ATOM   239  C CG  . TRP A 1 32  ? 33.717  -1.439  6.114   1.00 18.43 ?  32  TRP A CG  1 
ATOM   240  C CD1 . TRP A 1 32  ? 34.516  -2.180  6.943   1.00 19.04 ?  32  TRP A CD1 1 
ATOM   241  C CD2 . TRP A 1 32  ? 32.401  -1.978  6.232   1.00 18.89 ?  32  TRP A CD2 1 
ATOM   242  N NE1 . TRP A 1 32  ? 33.769  -3.147  7.580   1.00 19.55 ?  32  TRP A NE1 1 
ATOM   243  C CE2 . TRP A 1 32  ? 32.465  -3.041  7.165   1.00 20.42 ?  32  TRP A CE2 1 
ATOM   244  C CE3 . TRP A 1 32  ? 31.163  -1.658  5.650   1.00 19.84 ?  32  TRP A CE3 1 
ATOM   245  C CZ2 . TRP A 1 32  ? 31.335  -3.791  7.525   1.00 21.01 ?  32  TRP A CZ2 1 
ATOM   246  C CZ3 . TRP A 1 32  ? 30.042  -2.400  6.011   1.00 21.83 ?  32  TRP A CZ3 1 
ATOM   247  C CH2 . TRP A 1 32  ? 30.138  -3.456  6.940   1.00 20.24 ?  32  TRP A CH2 1 
ATOM   248  N N   . ILE A 1 33  ? 32.543  0.828   7.567   1.00 18.40 ?  33  ILE A N   1 
ATOM   249  C CA  . ILE A 1 33  ? 31.269  1.235   8.148   1.00 18.50 ?  33  ILE A CA  1 
ATOM   250  C C   . ILE A 1 33  ? 31.462  2.426   9.086   1.00 17.41 ?  33  ILE A C   1 
ATOM   251  O O   . ILE A 1 33  ? 32.489  2.554   9.770   1.00 17.51 ?  33  ILE A O   1 
ATOM   252  C CB  . ILE A 1 33  ? 30.628  0.033   8.867   1.00 18.75 ?  33  ILE A CB  1 
ATOM   253  C CG1 . ILE A 1 33  ? 29.225  0.383   9.349   1.00 20.90 ?  33  ILE A CG1 1 
ATOM   254  C CG2 . ILE A 1 33  ? 31.500  -0.448  10.017  1.00 19.43 ?  33  ILE A CG2 1 
ATOM   255  C CD1 . ILE A 1 33  ? 28.470  -0.824  9.829   1.00 23.80 ?  33  ILE A CD1 1 
ATOM   256  N N   . ALA A 1 34  ? 30.461  3.314   9.124   1.00 16.61 ?  34  ALA A N   1 
ATOM   257  C CA  . ALA A 1 34  ? 30.558  4.577   9.858   1.00 17.38 ?  34  ALA A CA  1 
ATOM   258  C C   . ALA A 1 34  ? 30.210  4.365   11.331  1.00 18.45 ?  34  ALA A C   1 
ATOM   259  O O   . ALA A 1 34  ? 29.118  4.693   11.811  1.00 16.45 ?  34  ALA A O   1 
ATOM   260  C CB  . ALA A 1 34  ? 29.661  5.634   9.239   1.00 17.16 ?  34  ALA A CB  1 
ATOM   261  N N   . GLU A 1 35  ? 31.173  3.813   12.059  1.00 14.69 ?  35  GLU A N   1 
ATOM   262  C CA  . GLU A 1 35  ? 31.200  3.896   13.513  1.00 14.94 ?  35  GLU A CA  1 
ATOM   263  C C   . GLU A 1 35  ? 32.646  4.110   13.924  1.00 16.23 ?  35  GLU A C   1 
ATOM   264  O O   . GLU A 1 35  ? 33.577  3.784   13.178  1.00 18.61 ?  35  GLU A O   1 
ATOM   265  C CB  . GLU A 1 35  ? 30.613  2.651   14.194  1.00 19.09 ?  35  GLU A CB  1 
ATOM   266  C CG  . GLU A 1 35  ? 31.442  1.390   14.029  1.00 19.93 ?  35  GLU A CG  1 
ATOM   267  C CD  . GLU A 1 35  ? 30.790  0.151   14.658  1.00 19.58 ?  35  GLU A CD  1 
ATOM   268  O OE1 . GLU A 1 35  ? 31.238  -0.310  15.735  1.00 22.14 ?  35  GLU A OE1 1 
ATOM   269  O OE2 . GLU A 1 35  ? 29.822  -0.367  14.066  1.00 23.54 -1 35  GLU A OE2 1 
ATOM   270  N N   . MET A 1 36  ? 32.829  4.654   15.119  1.00 14.13 ?  36  MET A N   1 
ATOM   271  C CA  . MET A 1 36  ? 34.164  5.032   15.561  1.00 14.11 ?  36  MET A CA  1 
ATOM   272  C C   . MET A 1 36  ? 34.860  3.909   16.308  1.00 16.38 ?  36  MET A C   1 
ATOM   273  O O   . MET A 1 36  ? 34.239  3.011   16.880  1.00 13.86 ?  36  MET A O   1 
ATOM   274  C CB  . MET A 1 36  ? 34.127  6.250   16.479  1.00 15.14 ?  36  MET A CB  1 
ATOM   275  C CG  . MET A 1 36  ? 33.248  7.369   16.022  1.00 18.69 ?  36  MET A CG  1 
ATOM   276  S SD  . MET A 1 36  ? 33.496  8.796   17.092  1.00 17.05 ?  36  MET A SD  1 
ATOM   277  C CE  . MET A 1 36  ? 32.145  9.811   16.540  1.00 16.95 ?  36  MET A CE  1 
ATOM   278  N N   . ASP A 1 37  ? 36.179  4.016   16.351  1.00 14.44 ?  37  ASP A N   1 
ATOM   279  C CA  . ASP A 1 37  ? 36.970  3.148   17.202  1.00 16.13 ?  37  ASP A CA  1 
ATOM   280  C C   . ASP A 1 37  ? 37.489  3.936   18.394  1.00 17.58 ?  37  ASP A C   1 
ATOM   281  O O   . ASP A 1 37  ? 38.660  3.825   18.773  1.00 16.90 ?  37  ASP A O   1 
ATOM   282  C CB  . ASP A 1 37  ? 38.075  2.498   16.378  1.00 18.13 ?  37  ASP A CB  1 
ATOM   283  C CG  . ASP A 1 37  ? 37.527  1.398   15.501  1.00 20.99 ?  37  ASP A CG  1 
ATOM   284  O OD1 . ASP A 1 37  ? 36.687  0.618   16.017  1.00 19.07 ?  37  ASP A OD1 1 
ATOM   285  O OD2 . ASP A 1 37  ? 37.873  1.341   14.304  1.00 19.18 -1 37  ASP A OD2 1 
ATOM   286  N N   . PHE A 1 38  ? 36.605  4.736   18.987  1.00 15.96 ?  38  PHE A N   1 
ATOM   287  C CA  . PHE A 1 38  ? 36.870  5.476   20.209  1.00 15.67 ?  38  PHE A CA  1 
ATOM   288  C C   . PHE A 1 38  ? 35.845  5.086   21.266  1.00 17.49 ?  38  PHE A C   1 
ATOM   289  O O   . PHE A 1 38  ? 34.689  4.790   20.945  1.00 15.80 ?  38  PHE A O   1 
ATOM   290  C CB  . PHE A 1 38  ? 36.780  6.990   19.980  1.00 16.13 ?  38  PHE A CB  1 
ATOM   291  C CG  . PHE A 1 38  ? 37.720  7.524   18.927  1.00 16.50 ?  38  PHE A CG  1 
ATOM   292  C CD1 . PHE A 1 38  ? 39.078  7.238   18.971  1.00 16.22 ?  38  PHE A CD1 1 
ATOM   293  C CD2 . PHE A 1 38  ? 37.244  8.353   17.921  1.00 15.19 ?  38  PHE A CD2 1 
ATOM   294  C CE1 . PHE A 1 38  ? 39.943  7.756   18.028  1.00 15.37 ?  38  PHE A CE1 1 
ATOM   295  C CE2 . PHE A 1 38  ? 38.096  8.875   16.958  1.00 16.18 ?  38  PHE A CE2 1 
ATOM   296  C CZ  . PHE A 1 38  ? 39.460  8.576   17.018  1.00 15.89 ?  38  PHE A CZ  1 
ATOM   297  N N   . ARG A 1 39  ? 36.265  5.106   22.533  1.00 18.82 ?  39  ARG A N   1 
ATOM   298  C CA  . ARG A 1 39  ? 35.301  5.021   23.627  1.00 20.65 ?  39  ARG A CA  1 
ATOM   299  C C   . ARG A 1 39  ? 34.360  6.215   23.594  1.00 17.34 ?  39  ARG A C   1 
ATOM   300  O O   . ARG A 1 39  ? 34.731  7.308   23.163  1.00 15.27 ?  39  ARG A O   1 
ATOM   301  C CB  . ARG A 1 39  ? 36.004  5.026   24.986  1.00 21.55 ?  39  ARG A CB  1 
ATOM   302  C CG  . ARG A 1 39  ? 37.349  4.391   25.022  1.00 31.13 ?  39  ARG A CG  1 
ATOM   303  C CD  . ARG A 1 39  ? 37.638  3.890   26.412  1.00 31.91 ?  39  ARG A CD  1 
ATOM   304  N NE  . ARG A 1 39  ? 37.102  2.545   26.552  1.00 36.98 ?  39  ARG A NE  1 
ATOM   305  C CZ  . ARG A 1 39  ? 37.683  1.465   26.039  1.00 34.61 ?  39  ARG A CZ  1 
ATOM   306  N NH1 . ARG A 1 39  ? 38.830  1.565   25.363  1.00 32.32 1  39  ARG A NH1 1 
ATOM   307  N NH2 . ARG A 1 39  ? 37.126  0.282   26.217  1.00 33.33 ?  39  ARG A NH2 1 
ATOM   308  N N   . ILE A 1 40  ? 33.134  6.016   24.101  1.00 15.16 ?  40  ILE A N   1 
ATOM   309  C CA  . ILE A 1 40  ? 32.190  7.125   24.181  1.00 14.96 ?  40  ILE A CA  1 
ATOM   310  C C   . ILE A 1 40  ? 32.558  8.035   25.349  1.00 15.09 ?  40  ILE A C   1 
ATOM   311  O O   . ILE A 1 40  ? 33.308  7.667   26.265  1.00 14.90 ?  40  ILE A O   1 
ATOM   312  C CB  . ILE A 1 40  ? 30.722  6.648   24.291  1.00 15.74 ?  40  ILE A CB  1 
ATOM   313  C CG1 . ILE A 1 40  ? 30.463  5.937   25.622  1.00 16.17 ?  40  ILE A CG1 1 
ATOM   314  C CG2 . ILE A 1 40  ? 30.353  5.737   23.113  1.00 14.07 ?  40  ILE A CG2 1 
ATOM   315  C CD1 . ILE A 1 40  ? 28.988  5.583   25.825  1.00 16.20 ?  40  ILE A CD1 1 
ATOM   316  N N   . ALA A 1 41  ? 32.040  9.253   25.286  1.00 15.48 ?  41  ALA A N   1 
ATOM   317  C CA  . ALA A 1 41  ? 32.242  10.229  26.341  1.00 16.05 ?  41  ALA A CA  1 
ATOM   318  C C   . ALA A 1 41  ? 31.883  9.624   27.702  1.00 18.63 ?  41  ALA A C   1 
ATOM   319  O O   . ALA A 1 41  ? 30.813  9.009   27.843  1.00 14.64 ?  41  ALA A O   1 
ATOM   320  C CB  . ALA A 1 41  ? 31.393  11.467  26.057  1.00 16.08 ?  41  ALA A CB  1 
ATOM   321  N N   . PRO A 1 42  ? 32.735  9.767   28.715  1.00 17.95 ?  42  PRO A N   1 
ATOM   322  C CA  . PRO A 1 42  ? 32.395  9.196   30.029  1.00 19.39 ?  42  PRO A CA  1 
ATOM   323  C C   . PRO A 1 42  ? 31.110  9.751   30.631  1.00 18.59 ?  42  PRO A C   1 
ATOM   324  O O   . PRO A 1 42  ? 30.489  9.068   31.452  1.00 18.56 ?  42  PRO A O   1 
ATOM   325  C CB  . PRO A 1 42  ? 33.621  9.527   30.891  1.00 24.59 ?  42  PRO A CB  1 
ATOM   326  C CG  . PRO A 1 42  ? 34.406  10.540  30.123  1.00 22.97 ?  42  PRO A CG  1 
ATOM   327  C CD  . PRO A 1 42  ? 34.091  10.343  28.681  1.00 18.28 ?  42  PRO A CD  1 
ATOM   328  N N   . GLU A 1 43  ? 30.702  10.969  30.268  1.00 17.18 ?  43  GLU A N   1 
ATOM   329  C CA  . GLU A 1 43  ? 29.448  11.514  30.778  1.00 17.96 ?  43  GLU A CA  1 
ATOM   330  C C   . GLU A 1 43  ? 28.246  10.749  30.231  1.00 19.98 ?  43  GLU A C   1 
ATOM   331  O O   . GLU A 1 43  ? 27.236  10.591  30.928  1.00 16.71 ?  43  GLU A O   1 
ATOM   332  C CB  . GLU A 1 43  ? 29.348  13.001  30.429  1.00 18.17 ?  43  GLU A CB  1 
ATOM   333  C CG  . GLU A 1 43  ? 30.475  13.860  31.020  1.00 22.15 ?  43  GLU A CG  1 
ATOM   334  C CD  . GLU A 1 43  ? 31.718  13.960  30.118  1.00 24.40 ?  43  GLU A CD  1 
ATOM   335  O OE1 . GLU A 1 43  ? 32.516  14.909  30.303  1.00 23.37 ?  43  GLU A OE1 1 
ATOM   336  O OE2 . GLU A 1 43  ? 31.905  13.100  29.231  1.00 19.89 -1 43  GLU A OE2 1 
ATOM   337  N N   . ILE A 1 44  ? 28.329  10.274  28.987  1.00 18.33 ?  44  ILE A N   1 
ATOM   338  C CA  . ILE A 1 44  ? 27.280  9.408   28.462  1.00 16.16 ?  44  ILE A CA  1 
ATOM   339  C C   . ILE A 1 44  ? 27.360  8.049   29.122  1.00 15.88 ?  44  ILE A C   1 
ATOM   340  O O   . ILE A 1 44  ? 26.342  7.480   29.545  1.00 16.08 ?  44  ILE A O   1 
ATOM   341  C CB  . ILE A 1 44  ? 27.397  9.293   26.930  1.00 12.10 ?  44  ILE A CB  1 
ATOM   342  C CG1 . ILE A 1 44  ? 27.429  10.681  26.303  1.00 15.81 ?  44  ILE A CG1 1 
ATOM   343  C CG2 . ILE A 1 44  ? 26.270  8.444   26.363  1.00 15.72 ?  44  ILE A CG2 1 
ATOM   344  C CD1 . ILE A 1 44  ? 27.828  10.653  24.825  1.00 14.20 ?  44  ILE A CD1 1 
ATOM   345  N N   . MET A 1 45  ? 28.581  7.523   29.251  1.00 17.25 ?  45  MET A N   1 
ATOM   346  C CA  . MET A 1 45  ? 28.778  6.216   29.856  1.00 19.13 ?  45  MET A CA  1 
ATOM   347  C C   . MET A 1 45  ? 28.186  6.165   31.258  1.00 16.90 ?  45  MET A C   1 
ATOM   348  O O   . MET A 1 45  ? 27.489  5.207   31.599  1.00 16.57 ?  45  MET A O   1 
ATOM   349  C CB  . MET A 1 45  ? 30.268  5.872   29.876  1.00 19.86 ?  45  MET A CB  1 
ATOM   350  C CG  . MET A 1 45  ? 30.583  4.436   30.203  1.00 23.40 ?  45  MET A CG  1 
ATOM   351  S SD  . MET A 1 45  ? 30.134  3.307   28.863  1.00 28.15 ?  45  MET A SD  1 
ATOM   352  C CE  . MET A 1 45  ? 28.616  2.653   29.533  1.00 21.16 ?  45  MET A CE  1 
ATOM   353  N N   . THR A 1 46  ? 28.411  7.203   32.074  1.00 17.42 ?  46  THR A N   1 
ATOM   354  C CA  . THR A 1 46  ? 27.895  7.149   33.442  1.00 19.63 ?  46  THR A CA  1 
ATOM   355  C C   . THR A 1 46  ? 26.376  7.136   33.464  1.00 18.27 ?  46  THR A C   1 
ATOM   356  O O   . THR A 1 46  ? 25.775  6.466   34.312  1.00 16.99 ?  46  THR A O   1 
ATOM   357  C CB  . THR A 1 46  ? 28.383  8.319   34.293  1.00 22.00 ?  46  THR A CB  1 
ATOM   358  O OG1 . THR A 1 46  ? 29.755  8.598   33.999  1.00 30.24 ?  46  THR A OG1 1 
ATOM   359  C CG2 . THR A 1 46  ? 28.263  7.937   35.748  1.00 23.64 ?  46  THR A CG2 1 
ATOM   360  N N   . SER A 1 47  ? 25.745  7.890   32.561  1.00 17.51 ?  47  SER A N   1 
ATOM   361  C CA  . SER A 1 47  ? 24.286  7.938   32.525  1.00 17.69 ?  47  SER A CA  1 
ATOM   362  C C   . SER A 1 47  ? 23.692  6.571   32.207  1.00 18.33 ?  47  SER A C   1 
ATOM   363  O O   . SER A 1 47  ? 22.613  6.232   32.705  1.00 15.90 ?  47  SER A O   1 
ATOM   364  C CB  . SER A 1 47  ? 23.817  8.967   31.499  1.00 19.02 ?  47  SER A CB  1 
ATOM   365  O OG  . SER A 1 47  ? 23.978  8.461   30.180  1.00 18.96 ?  47  SER A OG  1 
ATOM   366  N N   . MET A 1 48  ? 24.372  5.778   31.376  1.00 15.07 ?  48  MET A N   1 
ATOM   367  C CA  . MET A 1 48  ? 23.910  4.429   31.083  1.00 14.34 ?  48  MET A CA  1 
ATOM   368  C C   . MET A 1 48  ? 24.063  3.533   32.298  1.00 17.83 ?  48  MET A C   1 
ATOM   369  O O   . MET A 1 48  ? 23.166  2.747   32.631  1.00 16.70 ?  48  MET A O   1 
ATOM   370  C CB  . MET A 1 48  ? 24.707  3.852   29.918  1.00 17.84 ?  48  MET A CB  1 
ATOM   371  C CG  . MET A 1 48  ? 24.488  4.549   28.600  1.00 15.48 ?  48  MET A CG  1 
ATOM   372  S SD  . MET A 1 48  ? 25.503  3.707   27.370  1.00 19.88 ?  48  MET A SD  1 
ATOM   373  C CE  . MET A 1 48  ? 24.955  4.499   25.868  1.00 16.00 ?  48  MET A CE  1 
ATOM   374  N N   . GLU A 1 49  ? 25.234  3.612   32.943  1.00 17.23 ?  49  GLU A N   1 
ATOM   375  C CA  . GLU A 1 49  ? 25.510  2.809   34.127  1.00 19.61 ?  49  GLU A CA  1 
ATOM   376  C C   . GLU A 1 49  ? 24.541  3.122   35.249  1.00 19.49 ?  49  GLU A C   1 
ATOM   377  O O   . GLU A 1 49  ? 24.055  2.213   35.931  1.00 19.57 ?  49  GLU A O   1 
ATOM   378  C CB  . GLU A 1 49  ? 26.950  3.020   34.592  1.00 19.64 ?  49  GLU A CB  1 
ATOM   379  C CG  . GLU A 1 49  ? 27.878  2.331   33.647  1.00 25.69 ?  49  GLU A CG  1 
ATOM   380  C CD  . GLU A 1 49  ? 28.140  0.899   34.063  1.00 34.94 ?  49  GLU A CD  1 
ATOM   381  O OE1 . GLU A 1 49  ? 28.914  0.234   33.278  1.00 37.44 ?  49  GLU A OE1 1 
ATOM   382  O OE2 . GLU A 1 49  ? 27.621  0.398   35.074  1.00 34.69 -1 49  GLU A OE2 1 
ATOM   383  N N   . GLU A 1 50  ? 24.224  4.398   35.436  1.00 17.88 ?  50  GLU A N   1 
ATOM   384  C CA  . GLU A 1 50  ? 23.287  4.767   36.484  1.00 20.11 ?  50  GLU A CA  1 
ATOM   385  C C   . GLU A 1 50  ? 21.868  4.325   36.153  1.00 19.41 ?  50  GLU A C   1 
ATOM   386  O O   . GLU A 1 50  ? 21.113  3.944   37.059  1.00 20.09 ?  50  GLU A O   1 
ATOM   387  C CB  . GLU A 1 50  ? 23.347  6.270   36.718  1.00 21.39 ?  50  GLU A CB  1 
ATOM   388  C CG  . GLU A 1 50  ? 24.680  6.712   37.338  1.00 22.76 ?  50  GLU A CG  1 
ATOM   389  C CD  . GLU A 1 50  ? 24.935  8.199   37.191  1.00 30.67 ?  50  GLU A CD  1 
ATOM   390  O OE1 . GLU A 1 50  ? 24.137  8.882   36.506  1.00 31.43 ?  50  GLU A OE1 1 
ATOM   391  O OE2 . GLU A 1 50  ? 25.953  8.684   37.744  1.00 34.14 -1 50  GLU A OE2 1 
ATOM   392  N N   . LYS A 1 51  ? 21.484  4.363   34.875  1.00 15.55 ?  51  LYS A N   1 
ATOM   393  C CA  . LYS A 1 51  ? 20.134  3.928   34.510  1.00 17.07 ?  51  LYS A CA  1 
ATOM   394  C C   . LYS A 1 51  ? 19.960  2.427   34.723  1.00 17.53 ?  51  LYS A C   1 
ATOM   395  O O   . LYS A 1 51  ? 18.878  1.974   35.109  1.00 15.57 ?  51  LYS A O   1 
ATOM   396  C CB  . LYS A 1 51  ? 19.832  4.311   33.059  1.00 17.04 ?  51  LYS A CB  1 
ATOM   397  C CG  . LYS A 1 51  ? 18.516  3.738   32.498  1.00 16.29 ?  51  LYS A CG  1 
ATOM   398  C CD  . LYS A 1 51  ? 17.289  4.259   33.244  1.00 18.01 ?  51  LYS A CD  1 
ATOM   399  C CE  . LYS A 1 51  ? 15.970  3.751   32.644  1.00 16.84 ?  51  LYS A CE  1 
ATOM   400  N NZ  . LYS A 1 51  ? 15.651  4.388   31.322  1.00 18.31 1  51  LYS A NZ  1 
ATOM   401  N N   . LEU A 1 52  ? 21.015  1.635   34.492  1.00 17.40 ?  52  LEU A N   1 
ATOM   402  C CA  . LEU A 1 52  ? 20.909  0.197   34.724  1.00 16.04 ?  52  LEU A CA  1 
ATOM   403  C C   . LEU A 1 52  ? 20.634  -0.124  36.187  1.00 16.99 ?  52  LEU A C   1 
ATOM   404  O O   . LEU A 1 52  ? 20.057  -1.173  36.500  1.00 16.85 ?  52  LEU A O   1 
ATOM   405  C CB  . LEU A 1 52  ? 22.182  -0.510  34.266  1.00 18.96 ?  52  LEU A CB  1 
ATOM   406  C CG  . LEU A 1 52  ? 22.364  -0.693  32.756  1.00 17.48 ?  52  LEU A CG  1 
ATOM   407  C CD1 . LEU A 1 52  ? 23.368  -1.819  32.501  1.00 23.31 ?  52  LEU A CD1 1 
ATOM   408  C CD2 . LEU A 1 52  ? 21.034  -0.972  32.044  1.00 20.20 ?  52  LEU A CD2 1 
ATOM   409  N N   . LYS A 1 53  ? 21.000  0.772   37.079  1.00 16.72 ?  53  LYS A N   1 
ATOM   410  C CA  . LYS A 1 53  ? 20.795  0.532   38.529  1.00 19.86 ?  53  LYS A CA  1 
ATOM   411  C C   . LYS A 1 53  ? 19.307  0.475   38.890  1.00 17.89 ?  53  LYS A C   1 
ATOM   412  O O   . LYS A 1 53  ? 19.000  -0.046  39.946  1.00 20.14 ?  53  LYS A O   1 
ATOM   413  C CB  . LYS A 1 53  ? 21.539  1.615   39.312  1.00 20.39 ?  53  LYS A CB  1 
ATOM   414  C CG  . LYS A 1 53  ? 23.054  1.563   39.210  1.00 22.02 ?  53  LYS A CG  1 
ATOM   415  C CD  . LYS A 1 53  ? 23.631  0.197   39.485  1.00 24.20 ?  53  LYS A CD  1 
ATOM   416  C CE  . LYS A 1 53  ? 25.144  0.198   39.444  1.00 31.30 ?  53  LYS A CE  1 
ATOM   417  N NZ  . LYS A 1 53  ? 25.694  -1.167  39.297  1.00 31.98 1  53  LYS A NZ  1 
ATOM   418  N N   . VAL A 1 54  ? 18.427  1.012   38.054  1.00 16.62 ?  54  VAL A N   1 
ATOM   419  C CA  . VAL A 1 54  ? 16.995  0.871   38.331  1.00 16.34 ?  54  VAL A CA  1 
ATOM   420  C C   . VAL A 1 54  ? 16.611  -0.603  38.425  1.00 18.08 ?  54  VAL A C   1 
ATOM   421  O O   . VAL A 1 54  ? 15.718  -0.973  39.198  1.00 17.46 ?  54  VAL A O   1 
ATOM   422  C CB  . VAL A 1 54  ? 16.152  1.600   37.258  1.00 16.45 ?  54  VAL A CB  1 
ATOM   423  C CG1 . VAL A 1 54  ? 14.658  1.418   37.540  1.00 18.82 ?  54  VAL A CG1 1 
ATOM   424  C CG2 . VAL A 1 54  ? 16.492  3.085   37.191  1.00 17.66 ?  54  VAL A CG2 1 
ATOM   425  N N   . ALA A 1 55  ? 17.282  -1.463  37.656  1.00 15.23 ?  55  ALA A N   1 
ATOM   426  C CA  . ALA A 1 55  ? 17.105  -2.917  37.701  1.00 18.34 ?  55  ALA A CA  1 
ATOM   427  C C   . ALA A 1 55  ? 15.667  -3.335  37.406  1.00 17.07 ?  55  ALA A C   1 
ATOM   428  O O   . ALA A 1 55  ? 15.223  -4.399  37.839  1.00 17.36 ?  55  ALA A O   1 
ATOM   429  C CB  . ALA A 1 55  ? 17.558  -3.510  39.037  1.00 20.00 ?  55  ALA A CB  1 
ATOM   430  N N   . ALA A 1 56  ? 14.947  -2.513  36.651  1.00 16.46 ?  56  ALA A N   1 
ATOM   431  C CA  . ALA A 1 56  ? 13.617  -2.849  36.155  1.00 18.73 ?  56  ALA A CA  1 
ATOM   432  C C   . ALA A 1 56  ? 13.328  -1.923  34.985  1.00 16.96 ?  56  ALA A C   1 
ATOM   433  O O   . ALA A 1 56  ? 13.507  -0.709  35.104  1.00 18.49 ?  56  ALA A O   1 
ATOM   434  C CB  . ALA A 1 56  ? 12.561  -2.697  37.247  1.00 16.02 ?  56  ALA A CB  1 
ATOM   435  N N   . PHE A 1 57  ? 12.899  -2.477  33.853  1.00 15.12 ?  57  PHE A N   1 
ATOM   436  C CA  . PHE A 1 57  ? 12.863  -1.690  32.616  1.00 16.54 ?  57  PHE A CA  1 
ATOM   437  C C   . PHE A 1 57  ? 11.502  -1.817  31.929  1.00 16.27 ?  57  PHE A C   1 
ATOM   438  O O   . PHE A 1 57  ? 11.375  -2.341  30.825  1.00 15.69 ?  57  PHE A O   1 
ATOM   439  C CB  . PHE A 1 57  ? 14.032  -2.085  31.719  1.00 17.26 ?  57  PHE A CB  1 
ATOM   440  C CG  . PHE A 1 57  ? 15.341  -2.023  32.445  1.00 17.09 ?  57  PHE A CG  1 
ATOM   441  C CD1 . PHE A 1 57  ? 15.887  -0.794  32.807  1.00 14.95 ?  57  PHE A CD1 1 
ATOM   442  C CD2 . PHE A 1 57  ? 15.970  -3.182  32.858  1.00 16.53 ?  57  PHE A CD2 1 
ATOM   443  C CE1 . PHE A 1 57  ? 17.093  -0.735  33.539  1.00 16.91 ?  57  PHE A CE1 1 
ATOM   444  C CE2 . PHE A 1 57  ? 17.163  -3.133  33.568  1.00 19.12 ?  57  PHE A CE2 1 
ATOM   445  C CZ  . PHE A 1 57  ? 17.723  -1.904  33.905  1.00 18.82 ?  57  PHE A CZ  1 
ATOM   446  N N   . GLY A 1 58  ? 10.483  -1.273  32.583  1.00 17.75 ?  58  GLY A N   1 
ATOM   447  C CA  . GLY A 1 58  ? 9.171   -1.163  31.994  1.00 15.72 ?  58  GLY A CA  1 
ATOM   448  C C   . GLY A 1 58  ? 9.083   0.033   31.066  1.00 19.20 ?  58  GLY A C   1 
ATOM   449  O O   . GLY A 1 58  ? 10.089  0.593   30.623  1.00 18.74 ?  58  GLY A O   1 
ATOM   450  N N   . TYR A 1 59  ? 7.846   0.451   30.804  1.00 14.30 ?  59  TYR A N   1 
ATOM   451  C CA  . TYR A 1 59  ? 7.574   1.421   29.752  1.00 18.68 ?  59  TYR A CA  1 
ATOM   452  C C   . TYR A 1 59  ? 8.032   2.825   30.138  1.00 19.39 ?  59  TYR A C   1 
ATOM   453  O O   . TYR A 1 59  ? 7.972   3.234   31.302  1.00 17.84 ?  59  TYR A O   1 
ATOM   454  C CB  . TYR A 1 59  ? 6.083   1.427   29.423  1.00 16.78 ?  59  TYR A CB  1 
ATOM   455  C CG  . TYR A 1 59  ? 5.610   0.097   28.903  1.00 21.64 ?  59  TYR A CG  1 
ATOM   456  C CD1 . TYR A 1 59  ? 5.717   -0.218  27.555  1.00 24.58 ?  59  TYR A CD1 1 
ATOM   457  C CD2 . TYR A 1 59  ? 5.067   -0.855  29.757  1.00 21.02 ?  59  TYR A CD2 1 
ATOM   458  C CE1 . TYR A 1 59  ? 5.291   -1.440  27.069  1.00 24.61 ?  59  TYR A CE1 1 
ATOM   459  C CE2 . TYR A 1 59  ? 4.638   -2.085  29.273  1.00 22.07 ?  59  TYR A CE2 1 
ATOM   460  C CZ  . TYR A 1 59  ? 4.748   -2.361  27.926  1.00 24.04 ?  59  TYR A CZ  1 
ATOM   461  O OH  . TYR A 1 59  ? 4.334   -3.573  27.416  1.00 30.74 ?  59  TYR A OH  1 
ATOM   462  N N   . GLU A 1 60  ? 8.487   3.571   29.135  1.00 20.10 ?  60  GLU A N   1 
ATOM   463  C CA  . GLU A 1 60  ? 9.048   4.900   29.340  1.00 21.56 ?  60  GLU A CA  1 
ATOM   464  C C   . GLU A 1 60  ? 8.398   5.912   28.414  1.00 20.78 ?  60  GLU A C   1 
ATOM   465  O O   . GLU A 1 60  ? 8.168   5.629   27.236  1.00 22.59 ?  60  GLU A O   1 
ATOM   466  C CB  . GLU A 1 60  ? 10.555  4.893   29.086  1.00 22.11 ?  60  GLU A CB  1 
ATOM   467  C CG  . GLU A 1 60  ? 11.305  4.092   30.102  1.00 23.37 ?  60  GLU A CG  1 
ATOM   468  C CD  . GLU A 1 60  ? 12.786  4.239   29.948  1.00 21.97 ?  60  GLU A CD  1 
ATOM   469  O OE1 . GLU A 1 60  ? 13.509  3.267   30.265  1.00 22.62 ?  60  GLU A OE1 1 
ATOM   470  O OE2 . GLU A 1 60  ? 13.209  5.332   29.508  1.00 20.57 -1 60  GLU A OE2 1 
ATOM   471  N N   . SER A 1 61  ? 8.118   7.097   28.941  1.00 17.92 ?  61  SER A N   1 
ATOM   472  C CA  . SER A 1 61  ? 7.714   8.202   28.089  1.00 20.23 ?  61  SER A CA  1 
ATOM   473  C C   . SER A 1 61  ? 8.943   8.947   27.592  1.00 20.03 ?  61  SER A C   1 
ATOM   474  O O   . SER A 1 61  ? 10.050  8.801   28.117  1.00 17.90 ?  61  SER A O   1 
ATOM   475  C CB  . SER A 1 61  ? 6.807   9.159   28.847  1.00 20.48 ?  61  SER A CB  1 
ATOM   476  O OG  . SER A 1 61  ? 7.520   9.739   29.928  1.00 22.74 ?  61  SER A OG  1 
ATOM   477  N N   . VAL A 1 62  ? 8.740   9.787   26.576  1.00 18.09 ?  62  VAL A N   1 
ATOM   478  C CA  . VAL A 1 62  ? 9.739   10.764  26.168  1.00 16.51 ?  62  VAL A CA  1 
ATOM   479  C C   . VAL A 1 62  ? 9.533   12.012  27.022  1.00 16.46 ?  62  VAL A C   1 
ATOM   480  O O   . VAL A 1 62  ? 8.500   12.680  26.875  1.00 16.46 ?  62  VAL A O   1 
ATOM   481  C CB  . VAL A 1 62  ? 9.636   11.100  24.675  1.00 16.52 ?  62  VAL A CB  1 
ATOM   482  C CG1 . VAL A 1 62  ? 10.719  12.121  24.311  1.00 17.33 ?  62  VAL A CG1 1 
ATOM   483  C CG2 . VAL A 1 62  ? 9.789   9.827   23.833  1.00 17.46 ?  62  VAL A CG2 1 
ATOM   484  N N   . PRO A 1 63  ? 10.449  12.341  27.919  1.00 17.72 ?  63  PRO A N   1 
ATOM   485  C CA  . PRO A 1 63  ? 10.239  13.485  28.809  1.00 17.45 ?  63  PRO A CA  1 
ATOM   486  C C   . PRO A 1 63  ? 10.513  14.792  28.083  1.00 19.08 ?  63  PRO A C   1 
ATOM   487  O O   . PRO A 1 63  ? 11.259  14.841  27.104  1.00 16.80 ?  63  PRO A O   1 
ATOM   488  C CB  . PRO A 1 63  ? 11.264  13.245  29.921  1.00 18.94 ?  63  PRO A CB  1 
ATOM   489  C CG  . PRO A 1 63  ? 12.409  12.567  29.204  1.00 19.84 ?  63  PRO A CG  1 
ATOM   490  C CD  . PRO A 1 63  ? 11.771  11.720  28.103  1.00 17.36 ?  63  PRO A CD  1 
ATOM   491  N N   . ALA A 1 64  ? 9.874   15.865  28.565  1.00 17.81 ?  64  ALA A N   1 
ATOM   492  C CA  . ALA A 1 64  ? 10.151  17.190  28.018  1.00 18.70 ?  64  ALA A CA  1 
ATOM   493  C C   . ALA A 1 64  ? 11.642  17.489  28.020  1.00 17.21 ?  64  ALA A C   1 
ATOM   494  O O   . ALA A 1 64  ? 12.138  18.195  27.132  1.00 19.22 ?  64  ALA A O   1 
ATOM   495  C CB  . ALA A 1 64  ? 9.399   18.257  28.815  1.00 23.07 ?  64  ALA A CB  1 
ATOM   496  N N   . GLU A 1 65  ? 12.367  16.951  29.004  1.00 17.02 ?  65  GLU A N   1 
ATOM   497  C CA  . GLU A 1 65  ? 13.796  17.209  29.130  1.00 18.94 ?  65  GLU A CA  1 
ATOM   498  C C   . GLU A 1 65  ? 14.578  16.719  27.918  1.00 18.01 ?  65  GLU A C   1 
ATOM   499  O O   . GLU A 1 65  ? 15.654  17.257  27.618  1.00 16.55 ?  65  GLU A O   1 
ATOM   500  C CB  . GLU A 1 65  ? 14.323  16.549  30.396  1.00 21.34 ?  65  GLU A CB  1 
ATOM   501  C CG  . GLU A 1 65  ? 13.933  17.278  31.664  1.00 27.50 ?  65  GLU A CG  1 
ATOM   502  C CD  . GLU A 1 65  ? 12.710  16.692  32.332  1.00 31.87 ?  65  GLU A CD  1 
ATOM   503  O OE1 . GLU A 1 65  ? 12.708  16.647  33.582  1.00 34.85 ?  65  GLU A OE1 1 
ATOM   504  O OE2 . GLU A 1 65  ? 11.744  16.312  31.623  1.00 25.73 -1 65  GLU A OE2 1 
ATOM   505  N N   . TYR A 1 66  ? 14.079  15.684  27.237  1.00 14.06 ?  66  TYR A N   1 
ATOM   506  C CA  . TYR A 1 66  ? 14.748  15.193  26.032  1.00 15.45 ?  66  TYR A CA  1 
ATOM   507  C C   . TYR A 1 66  ? 14.746  16.262  24.947  1.00 15.32 ?  66  TYR A C   1 
ATOM   508  O O   . TYR A 1 66  ? 15.782  16.553  24.336  1.00 14.33 ?  66  TYR A O   1 
ATOM   509  C CB  . TYR A 1 66  ? 14.064  13.907  25.549  1.00 16.19 ?  66  TYR A CB  1 
ATOM   510  C CG  . TYR A 1 66  ? 14.659  13.255  24.307  1.00 14.23 ?  66  TYR A CG  1 
ATOM   511  C CD1 . TYR A 1 66  ? 15.758  12.399  24.401  1.00 17.68 ?  66  TYR A CD1 1 
ATOM   512  C CD2 . TYR A 1 66  ? 14.099  13.462  23.043  1.00 16.21 ?  66  TYR A CD2 1 
ATOM   513  C CE1 . TYR A 1 66  ? 16.295  11.791  23.270  1.00 19.52 ?  66  TYR A CE1 1 
ATOM   514  C CE2 . TYR A 1 66  ? 14.633  12.850  21.907  1.00 16.63 ?  66  TYR A CE2 1 
ATOM   515  C CZ  . TYR A 1 66  ? 15.740  12.023  22.029  1.00 18.08 ?  66  TYR A CZ  1 
ATOM   516  O OH  . TYR A 1 66  ? 16.295  11.400  20.921  1.00 16.52 ?  66  TYR A OH  1 
ATOM   517  N N   . TYR A 1 67  ? 13.586  16.871  24.701  1.00 13.96 ?  67  TYR A N   1 
ATOM   518  C CA  . TYR A 1 67  ? 13.514  17.897  23.671  1.00 14.94 ?  67  TYR A CA  1 
ATOM   519  C C   . TYR A 1 67  ? 14.252  19.161  24.089  1.00 15.48 ?  67  TYR A C   1 
ATOM   520  O O   . TYR A 1 67  ? 14.838  19.841  23.239  1.00 15.11 ?  67  TYR A O   1 
ATOM   521  C CB  . TYR A 1 67  ? 12.055  18.187  23.345  1.00 15.10 ?  67  TYR A CB  1 
ATOM   522  C CG  . TYR A 1 67  ? 11.329  16.951  22.862  1.00 16.87 ?  67  TYR A CG  1 
ATOM   523  C CD1 . TYR A 1 67  ? 11.904  16.126  21.900  1.00 16.21 ?  67  TYR A CD1 1 
ATOM   524  C CD2 . TYR A 1 67  ? 10.086  16.595  23.372  1.00 19.15 ?  67  TYR A CD2 1 
ATOM   525  C CE1 . TYR A 1 67  ? 11.254  14.988  21.437  1.00 19.38 ?  67  TYR A CE1 1 
ATOM   526  C CE2 . TYR A 1 67  ? 9.428   15.453  22.922  1.00 18.45 ?  67  TYR A CE2 1 
ATOM   527  C CZ  . TYR A 1 67  ? 10.017  14.656  21.948  1.00 16.33 ?  67  TYR A CZ  1 
ATOM   528  O OH  . TYR A 1 67  ? 9.381   13.518  21.488  1.00 17.57 ?  67  TYR A OH  1 
ATOM   529  N N   . LYS A 1 68  ? 14.264  19.479  25.388  1.00 15.72 ?  68  LYS A N   1 
ATOM   530  C CA  . LYS A 1 68  ? 15.031  20.632  25.845  1.00 16.41 ?  68  LYS A CA  1 
ATOM   531  C C   . LYS A 1 68  ? 16.529  20.410  25.675  1.00 14.37 ?  68  LYS A C   1 
ATOM   532  O O   . LYS A 1 68  ? 17.262  21.359  25.368  1.00 15.88 ?  68  LYS A O   1 
ATOM   533  C CB  . LYS A 1 68  ? 14.710  20.947  27.307  1.00 19.11 ?  68  LYS A CB  1 
ATOM   534  C CG  . LYS A 1 68  ? 15.646  22.001  27.871  1.00 17.54 ?  68  LYS A CG  1 
ATOM   535  C CD  . LYS A 1 68  ? 14.980  22.895  28.889  1.00 24.50 ?  68  LYS A CD  1 
ATOM   536  C CE  . LYS A 1 68  ? 16.026  23.608  29.719  1.00 26.38 ?  68  LYS A CE  1 
ATOM   537  N NZ  . LYS A 1 68  ? 17.260  23.942  28.951  1.00 29.03 1  68  LYS A NZ  1 
ATOM   538  N N   . ALA A 1 69  ? 16.994  19.169  25.863  1.00 15.40 ?  69  ALA A N   1 
ATOM   539  C CA  . ALA A 1 69  ? 18.399  18.848  25.625  1.00 15.90 ?  69  ALA A CA  1 
ATOM   540  C C   . ALA A 1 69  ? 18.746  18.980  24.149  1.00 14.56 ?  69  ALA A C   1 
ATOM   541  O O   . ALA A 1 69  ? 19.828  19.472  23.807  1.00 15.41 ?  69  ALA A O   1 
ATOM   542  C CB  . ALA A 1 69  ? 18.720  17.438  26.118  1.00 15.34 ?  69  ALA A CB  1 
ATOM   543  N N   . VAL A 1 70  ? 17.844  18.536  23.264  1.00 16.53 ?  70  VAL A N   1 
ATOM   544  C CA  . VAL A 1 70  ? 18.042  18.718  21.826  1.00 13.57 ?  70  VAL A CA  1 
ATOM   545  C C   . VAL A 1 70  ? 18.150  20.199  21.503  1.00 14.59 ?  70  VAL A C   1 
ATOM   546  O O   . VAL A 1 70  ? 19.055  20.631  20.785  1.00 14.98 ?  70  VAL A O   1 
ATOM   547  C CB  . VAL A 1 70  ? 16.895  18.056  21.039  1.00 14.16 ?  70  VAL A CB  1 
ATOM   548  C CG1 . VAL A 1 70  ? 16.801  18.619  19.629  1.00 13.95 ?  70  VAL A CG1 1 
ATOM   549  C CG2 . VAL A 1 70  ? 17.074  16.551  21.015  1.00 15.61 ?  70  VAL A CG2 1 
ATOM   550  N N   . ALA A 1 71  ? 17.228  21.001  22.040  1.00 11.77 ?  71  ALA A N   1 
ATOM   551  C CA  . ALA A 1 71  ? 17.235  22.433  21.750  1.00 13.26 ?  71  ALA A CA  1 
ATOM   552  C C   . ALA A 1 71  ? 18.502  23.109  22.264  1.00 14.96 ?  71  ALA A C   1 
ATOM   553  O O   . ALA A 1 71  ? 19.089  23.944  21.567  1.00 16.50 ?  71  ALA A O   1 
ATOM   554  C CB  . ALA A 1 71  ? 15.992  23.095  22.345  1.00 16.21 ?  71  ALA A CB  1 
ATOM   555  N N   . ASP A 1 72  ? 18.897  22.808  23.506  1.00 14.50 ?  72  ASP A N   1 
ATOM   556  C CA  . ASP A 1 72  ? 20.127  23.358  24.073  1.00 16.82 ?  72  ASP A CA  1 
ATOM   557  C C   . ASP A 1 72  ? 21.325  23.026  23.202  1.00 16.27 ?  72  ASP A C   1 
ATOM   558  O O   . ASP A 1 72  ? 22.186  23.880  22.946  1.00 16.79 ?  72  ASP A O   1 
ATOM   559  C CB  . ASP A 1 72  ? 20.372  22.794  25.470  1.00 17.82 ?  72  ASP A CB  1 
ATOM   560  C CG  . ASP A 1 72  ? 19.400  23.313  26.509  1.00 21.98 ?  72  ASP A CG  1 
ATOM   561  O OD1 . ASP A 1 72  ? 18.605  24.229  26.218  1.00 19.08 ?  72  ASP A OD1 1 
ATOM   562  O OD2 . ASP A 1 72  ? 19.461  22.789  27.642  1.00 23.92 -1 72  ASP A OD2 1 
ATOM   563  N N   . TRP A 1 73  ? 21.417  21.762  22.781  1.00 15.36 ?  73  TRP A N   1 
ATOM   564  C CA  . TRP A 1 73  ? 22.556  21.312  21.991  1.00 15.54 ?  73  TRP A CA  1 
ATOM   565  C C   . TRP A 1 73  ? 22.613  22.046  20.660  1.00 15.03 ?  73  TRP A C   1 
ATOM   566  O O   . TRP A 1 73  ? 23.672  22.535  20.249  1.00 15.87 ?  73  TRP A O   1 
ATOM   567  C CB  . TRP A 1 73  ? 22.465  19.801  21.761  1.00 14.24 ?  73  TRP A CB  1 
ATOM   568  C CG  . TRP A 1 73  ? 23.502  19.286  20.808  1.00 13.89 ?  73  TRP A CG  1 
ATOM   569  C CD1 . TRP A 1 73  ? 23.365  19.091  19.458  1.00 15.48 ?  73  TRP A CD1 1 
ATOM   570  C CD2 . TRP A 1 73  ? 24.832  18.889  21.136  1.00 14.87 ?  73  TRP A CD2 1 
ATOM   571  N NE1 . TRP A 1 73  ? 24.539  18.599  18.930  1.00 14.34 ?  73  TRP A NE1 1 
ATOM   572  C CE2 . TRP A 1 73  ? 25.452  18.471  19.941  1.00 14.55 ?  73  TRP A CE2 1 
ATOM   573  C CE3 . TRP A 1 73  ? 25.561  18.845  22.329  1.00 14.09 ?  73  TRP A CE3 1 
ATOM   574  C CZ2 . TRP A 1 73  ? 26.763  18.010  19.906  1.00 15.86 ?  73  TRP A CZ2 1 
ATOM   575  C CZ3 . TRP A 1 73  ? 26.869  18.394  22.289  1.00 15.63 ?  73  TRP A CZ3 1 
ATOM   576  C CH2 . TRP A 1 73  ? 27.454  17.988  21.081  1.00 15.98 ?  73  TRP A CH2 1 
ATOM   577  N N   . GLU A 1 74  ? 21.482  22.119  19.965  1.00 12.98 ?  74  GLU A N   1 
ATOM   578  C CA  . GLU A 1 74  ? 21.450  22.844  18.704  1.00 16.37 ?  74  GLU A CA  1 
ATOM   579  C C   . GLU A 1 74  ? 21.780  24.314  18.926  1.00 16.81 ?  74  GLU A C   1 
ATOM   580  O O   . GLU A 1 74  ? 22.445  24.940  18.094  1.00 16.37 ?  74  GLU A O   1 
ATOM   581  C CB  . GLU A 1 74  ? 20.078  22.698  18.035  1.00 15.99 ?  74  GLU A CB  1 
ATOM   582  C CG  . GLU A 1 74  ? 19.670  21.262  17.669  1.00 16.84 ?  74  GLU A CG  1 
ATOM   583  C CD  . GLU A 1 74  ? 20.401  20.738  16.437  1.00 20.89 ?  74  GLU A CD  1 
ATOM   584  O OE1 . GLU A 1 74  ? 21.512  20.191  16.584  1.00 20.36 ?  74  GLU A OE1 1 
ATOM   585  O OE2 . GLU A 1 74  ? 19.864  20.865  15.319  1.00 19.88 -1 74  GLU A OE2 1 
ATOM   586  N N   . GLU A 1 75  ? 21.354  24.884  20.049  1.00 15.57 ?  75  GLU A N   1 
ATOM   587  C CA  . GLU A 1 75  ? 21.629  26.331  20.278  1.00 15.23 ?  75  GLU A CA  1 
ATOM   588  C C   . GLU A 1 75  ? 23.123  26.522  20.564  1.00 17.08 ?  75  GLU A C   1 
ATOM   589  O O   . GLU A 1 75  ? 23.701  27.420  20.011  1.00 17.07 ?  75  GLU A O   1 
ATOM   590  C CB  . GLU A 1 75  ? 20.840  26.875  21.465  1.00 18.31 ?  75  GLU A CB  1 
ATOM   591  C CG  . GLU A 1 75  ? 21.056  28.357  21.684  1.00 22.94 ?  75  GLU A CG  1 
ATOM   592  C CD  . GLU A 1 75  ? 20.659  28.822  23.065  1.00 25.22 ?  75  GLU A CD  1 
ATOM   593  O OE1 . GLU A 1 75  ? 21.364  29.664  23.637  1.00 33.31 ?  75  GLU A OE1 1 
ATOM   594  O OE2 . GLU A 1 75  ? 19.663  28.327  23.566  1.00 25.99 -1 75  GLU A OE2 1 
ATOM   595  N N   . ILE A 1 76  ? 23.687  25.685  21.424  1.00 14.83 ?  76  ILE A N   1 
ATOM   596  C CA  . ILE A 1 76  ? 25.074  25.894  21.833  1.00 15.95 ?  76  ILE A CA  1 
ATOM   597  C C   . ILE A 1 76  ? 26.025  25.551  20.699  1.00 17.11 ?  76  ILE A C   1 
ATOM   598  O O   . ILE A 1 76  ? 26.982  26.288  20.425  1.00 17.83 ?  76  ILE A O   1 
ATOM   599  C CB  . ILE A 1 76  ? 25.387  25.068  23.089  1.00 16.74 ?  76  ILE A CB  1 
ATOM   600  C CG1 . ILE A 1 76  ? 24.630  25.631  24.287  1.00 18.86 ?  76  ILE A CG1 1 
ATOM   601  C CG2 . ILE A 1 76  ? 26.884  25.056  23.355  1.00 17.15 ?  76  ILE A CG2 1 
ATOM   602  C CD1 . ILE A 1 76  ? 24.730  24.754  25.513  1.00 22.70 ?  76  ILE A CD1 1 
ATOM   603  N N   . GLU A 1 77  ? 25.800  24.412  20.041  1.00 15.92 ?  77  GLU A N   1 
ATOM   604  C CA  . GLU A 1 77  ? 26.738  23.957  19.020  1.00 16.66 ?  77  GLU A CA  1 
ATOM   605  C C   . GLU A 1 77  ? 26.521  24.644  17.677  1.00 18.41 ?  77  GLU A C   1 
ATOM   606  O O   . GLU A 1 77  ? 27.489  24.875  16.939  1.00 17.91 ?  77  GLU A O   1 
ATOM   607  C CB  . GLU A 1 77  ? 26.647  22.438  18.859  1.00 15.78 ?  77  GLU A CB  1 
ATOM   608  C CG  . GLU A 1 77  ? 27.153  21.658  20.073  1.00 18.58 ?  77  GLU A CG  1 
ATOM   609  C CD  . GLU A 1 77  ? 28.667  21.727  20.250  1.00 19.51 ?  77  GLU A CD  1 
ATOM   610  O OE1 . GLU A 1 77  ? 29.128  21.718  21.408  1.00 25.03 ?  77  GLU A OE1 1 
ATOM   611  O OE2 . GLU A 1 77  ? 29.397  21.790  19.231  1.00 20.72 -1 77  GLU A OE2 1 
ATOM   612  N N   . HIS A 1 78  ? 25.267  24.986  17.342  1.00 16.08 ?  78  HIS A N   1 
ATOM   613  C CA  . HIS A 1 78  ? 24.945  25.498  15.980  1.00 17.21 ?  78  HIS A CA  1 
ATOM   614  C C   . HIS A 1 78  ? 24.244  26.856  15.975  1.00 20.14 ?  78  HIS A C   1 
ATOM   615  O O   . HIS A 1 78  ? 23.867  27.287  14.891  1.00 20.76 ?  78  HIS A O   1 
ATOM   616  C CB  . HIS A 1 78  ? 24.129  24.455  15.233  1.00 19.86 ?  78  HIS A CB  1 
ATOM   617  C CG  . HIS A 1 78  ? 24.765  23.113  15.231  1.00 19.59 ?  78  HIS A CG  1 
ATOM   618  N ND1 . HIS A 1 78  ? 26.065  22.927  14.840  1.00 19.79 ?  78  HIS A ND1 1 
ATOM   619  C CD2 . HIS A 1 78  ? 24.308  21.906  15.609  1.00 17.86 ?  78  HIS A CD2 1 
ATOM   620  C CE1 . HIS A 1 78  ? 26.383  21.664  14.951  1.00 20.59 ?  78  HIS A CE1 1 
ATOM   621  N NE2 . HIS A 1 78  ? 25.323  21.020  15.415  1.00 20.32 ?  78  HIS A NE2 1 
ATOM   622  N N   . ARG A 1 79  ? 24.062  27.467  17.141  1.00 18.50 ?  79  ARG A N   1 
ATOM   623  C CA  . ARG A 1 79  ? 23.414  28.799  17.243  1.00 16.72 ?  79  ARG A CA  1 
ATOM   624  C C   . ARG A 1 79  ? 22.026  28.767  16.593  1.00 19.44 ?  79  ARG A C   1 
ATOM   625  O O   . ARG A 1 79  ? 21.603  29.778  16.064  1.00 19.68 ?  79  ARG A O   1 
ATOM   626  C CB  . ARG A 1 79  ? 24.304  29.868  16.615  1.00 25.06 ?  79  ARG A CB  1 
ATOM   627  C CG  . ARG A 1 79  ? 25.573  30.147  17.400  1.00 34.11 ?  79  ARG A CG  1 
ATOM   628  C CD  . ARG A 1 79  ? 25.276  31.237  18.404  1.00 33.09 ?  79  ARG A CD  1 
ATOM   629  N NE  . ARG A 1 79  ? 26.487  31.662  19.079  1.00 41.08 ?  79  ARG A NE  1 
ATOM   630  C CZ  . ARG A 1 79  ? 26.512  32.232  20.274  1.00 36.27 ?  79  ARG A CZ  1 
ATOM   631  N NH1 . ARG A 1 79  ? 25.378  32.436  20.925  1.00 32.79 1  79  ARG A NH1 1 
ATOM   632  N NH2 . ARG A 1 79  ? 27.666  32.577  20.816  1.00 35.17 ?  79  ARG A NH2 1 
ATOM   633  N N   . ALA A 1 80  ? 21.341  27.633  16.697  1.00 17.33 ?  80  ALA A N   1 
ATOM   634  C CA  . ALA A 1 80  ? 20.081  27.463  15.981  1.00 17.30 ?  80  ALA A CA  1 
ATOM   635  C C   . ALA A 1 80  ? 19.170  26.684  16.919  1.00 19.64 ?  80  ALA A C   1 
ATOM   636  O O   . ALA A 1 80  ? 19.120  25.452  16.875  1.00 18.65 ?  80  ALA A O   1 
ATOM   637  C CB  . ALA A 1 80  ? 20.284  26.761  14.644  1.00 17.96 ?  80  ALA A CB  1 
ATOM   638  N N   . ARG A 1 81  ? 18.486  27.444  17.755  1.00 15.21 ?  81  ARG A N   1 
ATOM   639  C CA  . ARG A 1 81  ? 17.632  26.823  18.774  1.00 16.22 ?  81  ARG A CA  1 
ATOM   640  C C   . ARG A 1 81  ? 16.260  26.484  18.188  1.00 17.02 ?  81  ARG A C   1 
ATOM   641  O O   . ARG A 1 81  ? 15.522  27.400  17.906  1.00 18.22 ?  81  ARG A O   1 
ATOM   642  C CB  . ARG A 1 81  ? 17.491  27.679  20.028  1.00 16.31 ?  81  ARG A CB  1 
ATOM   643  C CG  . ARG A 1 81  ? 16.849  26.926  21.182  1.00 16.27 ?  81  ARG A CG  1 
ATOM   644  C CD  . ARG A 1 81  ? 16.520  27.741  22.415  1.00 17.74 ?  81  ARG A CD  1 
ATOM   645  N NE  . ARG A 1 81  ? 15.993  26.809  23.393  1.00 17.61 ?  81  ARG A NE  1 
ATOM   646  C CZ  . ARG A 1 81  ? 16.727  26.158  24.278  1.00 17.02 ?  81  ARG A CZ  1 
ATOM   647  N NH1 . ARG A 1 81  ? 18.027  26.367  24.345  1.00 20.19 1  81  ARG A NH1 1 
ATOM   648  N NH2 . ARG A 1 81  ? 16.160  25.306  25.105  1.00 18.92 ?  81  ARG A NH2 1 
ATOM   649  N N   . PRO A 1 82  ? 15.910  25.200  17.981  1.00 17.02 ?  82  PRO A N   1 
ATOM   650  C CA  . PRO A 1 82  ? 14.538  24.892  17.563  1.00 15.42 ?  82  PRO A CA  1 
ATOM   651  C C   . PRO A 1 82  ? 13.591  25.053  18.740  1.00 17.09 ?  82  PRO A C   1 
ATOM   652  O O   . PRO A 1 82  ? 13.985  24.978  19.907  1.00 15.94 ?  82  PRO A O   1 
ATOM   653  C CB  . PRO A 1 82  ? 14.626  23.427  17.123  1.00 14.95 ?  82  PRO A CB  1 
ATOM   654  C CG  . PRO A 1 82  ? 15.693  22.862  18.063  1.00 17.18 ?  82  PRO A CG  1 
ATOM   655  C CD  . PRO A 1 82  ? 16.702  23.978  18.225  1.00 16.72 ?  82  PRO A CD  1 
ATOM   656  N N   . LYS A 1 83  ? 12.319  25.274  18.414  1.00 14.95 ?  83  LYS A N   1 
ATOM   657  C CA  . LYS A 1 83  ? 11.276  25.235  19.426  1.00 16.57 ?  83  LYS A CA  1 
ATOM   658  C C   . LYS A 1 83  ? 11.080  23.794  19.878  1.00 14.30 ?  83  LYS A C   1 
ATOM   659  O O   . LYS A 1 83  ? 11.031  22.883  19.048  1.00 15.71 ?  83  LYS A O   1 
ATOM   660  C CB  . LYS A 1 83  ? 9.976   25.803  18.859  1.00 17.64 ?  83  LYS A CB  1 
ATOM   661  C CG  . LYS A 1 83  ? 8.929   26.111  19.909  1.00 20.67 ?  83  LYS A CG  1 
ATOM   662  C CD  . LYS A 1 83  ? 7.774   26.896  19.294  1.00 21.98 ?  83  LYS A CD  1 
ATOM   663  C CE  . LYS A 1 83  ? 6.544   26.867  20.192  1.00 21.33 ?  83  LYS A CE  1 
ATOM   664  N NZ  . LYS A 1 83  ? 5.355   27.323  19.425  1.00 27.02 1  83  LYS A NZ  1 
ATOM   665  N N   . GLU A 1 84  ? 11.013  23.582  21.194  1.00 14.91 ?  84  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84  ? 10.941  22.218  21.716  1.00 16.55 ?  84  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84  ? 9.708   21.487  21.196  1.00 17.68 ?  84  GLU A C   1 
ATOM   668  O O   . GLU A 1 84  ? 9.748   20.273  20.952  1.00 17.21 ?  84  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84  ? 10.940  22.234  23.249  1.00 17.04 ?  84  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84  ? 12.310  22.445  23.890  1.00 16.04 ?  84  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84  ? 12.628  23.916  24.104  1.00 16.96 ?  84  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84  ? 13.615  24.218  24.817  1.00 21.11 ?  84  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84  ? 11.902  24.774  23.549  1.00 20.02 -1 84  GLU A OE2 1 
ATOM   674  N N   . ASP A 1 85  ? 8.607   22.212  21.018  1.00 18.30 ?  85  ASP A N   1 
ATOM   675  C CA  . ASP A 1 85  ? 7.371   21.625  20.519  1.00 19.88 ?  85  ASP A CA  1 
ATOM   676  C C   . ASP A 1 85  ? 7.497   21.091  19.093  1.00 16.66 ?  85  ASP A C   1 
ATOM   677  O O   . ASP A 1 85  ? 6.638   20.319  18.659  1.00 17.74 ?  85  ASP A O   1 
ATOM   678  C CB  . ASP A 1 85  ? 6.256   22.670  20.588  1.00 19.85 ?  85  ASP A CB  1 
ATOM   679  C CG  . ASP A 1 85  ? 4.885   22.059  20.517  1.00 32.48 ?  85  ASP A CG  1 
ATOM   680  O OD1 . ASP A 1 85  ? 4.731   20.866  20.876  1.00 39.42 ?  85  ASP A OD1 1 
ATOM   681  O OD2 . ASP A 1 85  ? 3.965   22.786  20.088  1.00 32.99 -1 85  ASP A OD2 1 
ATOM   682  N N   . TRP A 1 86  ? 8.537   21.485  18.355  1.00 16.25 ?  86  TRP A N   1 
ATOM   683  C CA  . TRP A 1 86  ? 8.758   20.952  17.017  1.00 13.50 ?  86  TRP A CA  1 
ATOM   684  C C   . TRP A 1 86  ? 9.314   19.533  17.026  1.00 14.58 ?  86  TRP A C   1 
ATOM   685  O O   . TRP A 1 86  ? 9.361   18.895  15.965  1.00 15.28 ?  86  TRP A O   1 
ATOM   686  C CB  . TRP A 1 86  ? 9.738   21.836  16.249  1.00 17.64 ?  86  TRP A CB  1 
ATOM   687  C CG  . TRP A 1 86  ? 9.282   23.227  15.983  1.00 16.08 ?  86  TRP A CG  1 
ATOM   688  C CD1 . TRP A 1 86  ? 8.031   23.745  16.166  1.00 16.78 ?  86  TRP A CD1 1 
ATOM   689  C CD2 . TRP A 1 86  ? 10.081  24.277  15.452  1.00 15.38 ?  86  TRP A CD2 1 
ATOM   690  N NE1 . TRP A 1 86  ? 8.010   25.071  15.785  1.00 19.01 ?  86  TRP A NE1 1 
ATOM   691  C CE2 . TRP A 1 86  ? 9.259   25.415  15.338  1.00 18.72 ?  86  TRP A CE2 1 
ATOM   692  C CE3 . TRP A 1 86  ? 11.427  24.365  15.058  1.00 16.14 ?  86  TRP A CE3 1 
ATOM   693  C CZ2 . TRP A 1 86  ? 9.733   26.633  14.853  1.00 19.51 ?  86  TRP A CZ2 1 
ATOM   694  C CZ3 . TRP A 1 86  ? 11.900  25.580  14.583  1.00 16.88 ?  86  TRP A CZ3 1 
ATOM   695  C CH2 . TRP A 1 86  ? 11.047  26.696  14.480  1.00 18.21 ?  86  TRP A CH2 1 
ATOM   696  N N   . CYS A 1 87  ? 9.755   19.038  18.175  1.00 16.74 ?  87  CYS A N   1 
ATOM   697  C CA  . CYS A 1 87  ? 10.623  17.873  18.238  1.00 16.27 ?  87  CYS A CA  1 
ATOM   698  C C   . CYS A 1 87  ? 9.821   16.609  18.522  1.00 16.27 ?  87  CYS A C   1 
ATOM   699  O O   . CYS A 1 87  ? 8.921   16.604  19.371  1.00 16.92 ?  87  CYS A O   1 
ATOM   700  C CB  . CYS A 1 87  ? 11.697  18.084  19.306  1.00 17.02 ?  87  CYS A CB  1 
ATOM   701  S SG  . CYS A 1 87  ? 12.757  19.521  18.986  1.00 18.34 ?  87  CYS A SG  1 
ATOM   702  N N   . VAL A 1 88  ? 10.142  15.538  17.801  1.00 14.29 ?  88  VAL A N   1 
ATOM   703  C CA  . VAL A 1 88  ? 9.467   14.249  17.961  1.00 15.21 ?  88  VAL A CA  1 
ATOM   704  C C   . VAL A 1 88  ? 10.533  13.163  18.051  1.00 14.97 ?  88  VAL A C   1 
ATOM   705  O O   . VAL A 1 88  ? 11.360  13.026  17.144  1.00 14.89 ?  88  VAL A O   1 
ATOM   706  C CB  . VAL A 1 88  ? 8.488   13.951  16.808  1.00 16.05 ?  88  VAL A CB  1 
ATOM   707  C CG1 . VAL A 1 88  ? 7.763   12.621  17.053  1.00 17.90 ?  88  VAL A CG1 1 
ATOM   708  C CG2 . VAL A 1 88  ? 7.473   15.073  16.675  1.00 17.41 ?  88  VAL A CG2 1 
ATOM   709  N N   . PHE A 1 89  ? 10.522  12.398  19.138  1.00 14.34 ?  89  PHE A N   1 
ATOM   710  C CA  . PHE A 1 89  ? 11.461  11.286  19.258  1.00 14.45 ?  89  PHE A CA  1 
ATOM   711  C C   . PHE A 1 89  ? 11.244  10.252  18.157  1.00 15.69 ?  89  PHE A C   1 
ATOM   712  O O   . PHE A 1 89  ? 10.111  9.910   17.816  1.00 13.26 ?  89  PHE A O   1 
ATOM   713  C CB  . PHE A 1 89  ? 11.312  10.611  20.622  1.00 13.87 ?  89  PHE A CB  1 
ATOM   714  C CG  . PHE A 1 89  ? 12.169  9.382   20.775  1.00 13.99 ?  89  PHE A CG  1 
ATOM   715  C CD1 . PHE A 1 89  ? 11.715  8.133   20.368  1.00 16.76 ?  89  PHE A CD1 1 
ATOM   716  C CD2 . PHE A 1 89  ? 13.452  9.480   21.303  1.00 16.18 ?  89  PHE A CD2 1 
ATOM   717  C CE1 . PHE A 1 89  ? 12.524  7.010   20.480  1.00 13.84 ?  89  PHE A CE1 1 
ATOM   718  C CE2 . PHE A 1 89  ? 14.253  8.356   21.429  1.00 17.58 ?  89  PHE A CE2 1 
ATOM   719  C CZ  . PHE A 1 89  ? 13.790  7.124   21.027  1.00 15.51 ?  89  PHE A CZ  1 
ATOM   720  N N   . ALA A 1 90  ? 12.341  9.723   17.617  1.00 13.20 ?  90  ALA A N   1 
ATOM   721  C CA  . ALA A 1 90  ? 12.278  8.517   16.809  1.00 12.63 ?  90  ALA A CA  1 
ATOM   722  C C   . ALA A 1 90  ? 13.485  7.656   17.135  1.00 15.45 ?  90  ALA A C   1 
ATOM   723  O O   . ALA A 1 90  ? 14.521  8.160   17.572  1.00 15.74 ?  90  ALA A O   1 
ATOM   724  C CB  . ALA A 1 90  ? 12.233  8.818   15.295  1.00 13.46 ?  90  ALA A CB  1 
ATOM   725  N N   . SER A 1 91  ? 13.350  6.346   16.935  1.00 12.27 ?  91  SER A N   1 
ATOM   726  C CA  . SER A 1 91  ? 14.456  5.490   17.329  1.00 15.87 ?  91  SER A CA  1 
ATOM   727  C C   . SER A 1 91  ? 15.612  5.496   16.336  1.00 16.34 ?  91  SER A C   1 
ATOM   728  O O   . SER A 1 91  ? 16.663  4.929   16.648  1.00 16.58 ?  91  SER A O   1 
ATOM   729  C CB  . SER A 1 91  ? 13.964  4.059   17.559  1.00 18.12 ?  91  SER A CB  1 
ATOM   730  O OG  . SER A 1 91  ? 13.530  3.470   16.362  1.00 19.10 ?  91  SER A OG  1 
ATOM   731  N N   . GLY A 1 92  ? 15.470  6.133   15.175  1.00 15.20 ?  92  GLY A N   1 
ATOM   732  C CA  . GLY A 1 92  ? 16.547  6.142   14.204  1.00 18.11 ?  92  GLY A CA  1 
ATOM   733  C C   . GLY A 1 92  ? 16.209  7.059   13.055  1.00 15.88 ?  92  GLY A C   1 
ATOM   734  O O   . GLY A 1 92  ? 15.036  7.295   12.755  1.00 14.74 ?  92  GLY A O   1 
ATOM   735  N N   . VAL A 1 93  ? 17.260  7.585   12.419  1.00 15.76 ?  93  VAL A N   1 
ATOM   736  C CA  . VAL A 1 93  ? 17.074  8.532   11.321  1.00 15.08 ?  93  VAL A CA  1 
ATOM   737  C C   . VAL A 1 93  ? 16.556  7.813   10.081  1.00 15.21 ?  93  VAL A C   1 
ATOM   738  O O   . VAL A 1 93  ? 15.580  8.240   9.454   1.00 14.89 ?  93  VAL A O   1 
ATOM   739  C CB  . VAL A 1 93  ? 18.387  9.287   11.031  1.00 15.09 ?  93  VAL A CB  1 
ATOM   740  C CG1 . VAL A 1 93  ? 18.277  10.053  9.725   1.00 13.50 ?  93  VAL A CG1 1 
ATOM   741  C CG2 . VAL A 1 93  ? 18.731  10.231  12.180  1.00 15.26 ?  93  VAL A CG2 1 
ATOM   742  N N   . VAL A 1 94  ? 17.204  6.710   9.705   1.00 14.35 ?  94  VAL A N   1 
ATOM   743  C CA  . VAL A 1 94  ? 16.764  5.964   8.529   1.00 13.93 ?  94  VAL A CA  1 
ATOM   744  C C   . VAL A 1 94  ? 15.376  5.382   8.751   1.00 16.21 ?  94  VAL A C   1 
ATOM   745  O O   . VAL A 1 94  ? 14.524  5.508   7.849   1.00 14.64 ?  94  VAL A O   1 
ATOM   746  C CB  . VAL A 1 94  ? 17.822  4.927   8.133   1.00 18.36 ?  94  VAL A CB  1 
ATOM   747  C CG1 . VAL A 1 94  ? 17.263  3.931   7.126   1.00 20.23 ?  94  VAL A CG1 1 
ATOM   748  C CG2 . VAL A 1 94  ? 19.058  5.641   7.563   1.00 20.30 ?  94  VAL A CG2 1 
ATOM   749  N N   . PRO A 1 95  ? 15.055  4.775   9.903   1.00 14.87 ?  95  PRO A N   1 
ATOM   750  C CA  . PRO A 1 95  ? 13.650  4.388   10.145  1.00 15.97 ?  95  PRO A CA  1 
ATOM   751  C C   . PRO A 1 95  ? 12.669  5.550   10.064  1.00 14.95 ?  95  PRO A C   1 
ATOM   752  O O   . PRO A 1 95  ? 11.561  5.367   9.544   1.00 12.36 ?  95  PRO A O   1 
ATOM   753  C CB  . PRO A 1 95  ? 13.698  3.775   11.548  1.00 14.51 ?  95  PRO A CB  1 
ATOM   754  C CG  . PRO A 1 95  ? 15.119  3.253   11.680  1.00 17.75 ?  95  PRO A CG  1 
ATOM   755  C CD  . PRO A 1 95  ? 15.957  4.258   10.953  1.00 17.60 ?  95  PRO A CD  1 
ATOM   756  N N   . ALA A 1 96  ? 13.046  6.745   10.533  1.00 15.45 ?  96  ALA A N   1 
ATOM   757  C CA  . ALA A 1 96  ? 12.152  7.894   10.420  1.00 15.02 ?  96  ALA A CA  1 
ATOM   758  C C   . ALA A 1 96  ? 11.914  8.260   8.962   1.00 13.38 ?  96  ALA A C   1 
ATOM   759  O O   . ALA A 1 96  ? 10.783  8.581   8.576   1.00 14.21 ?  96  ALA A O   1 
ATOM   760  C CB  . ALA A 1 96  ? 12.710  9.091   11.186  1.00 15.64 ?  96  ALA A CB  1 
ATOM   761  N N   . ILE A 1 97  ? 12.964  8.212   8.135   1.00 13.29 ?  97  ILE A N   1 
ATOM   762  C CA  . ILE A 1 97  ? 12.792  8.489   6.713   1.00 14.77 ?  97  ILE A CA  1 
ATOM   763  C C   . ILE A 1 97  ? 11.871  7.454   6.091   1.00 13.03 ?  97  ILE A C   1 
ATOM   764  O O   . ILE A 1 97  ? 10.976  7.786   5.299   1.00 13.76 ?  97  ILE A O   1 
ATOM   765  C CB  . ILE A 1 97  ? 14.150  8.531   5.989   1.00 13.40 ?  97  ILE A CB  1 
ATOM   766  C CG1 . ILE A 1 97  ? 15.020  9.676   6.528   1.00 13.76 ?  97  ILE A CG1 1 
ATOM   767  C CG2 . ILE A 1 97  ? 13.932  8.699   4.492   1.00 15.67 ?  97  ILE A CG2 1 
ATOM   768  C CD1 . ILE A 1 97  ? 16.472  9.699   6.004   1.00 17.94 ?  97  ILE A CD1 1 
ATOM   769  N N   . SER A 1 98  ? 12.064  6.182   6.454   1.00 13.25 ?  98  SER A N   1 
ATOM   770  C CA  . SER A 1 98  ? 11.227  5.116   5.920   1.00 13.78 ?  98  SER A CA  1 
ATOM   771  C C   . SER A 1 98  ? 9.759   5.331   6.291   1.00 15.07 ?  98  SER A C   1 
ATOM   772  O O   . SER A 1 98  ? 8.865   5.209   5.442   1.00 14.80 ?  98  SER A O   1 
ATOM   773  C CB  . SER A 1 98  ? 11.732  3.761   6.422   1.00 13.10 ?  98  SER A CB  1 
ATOM   774  O OG  . SER A 1 98  ? 11.069  2.709   5.747   1.00 16.05 ?  98  SER A OG  1 
ATOM   775  N N   . ALA A 1 99  ? 9.492   5.689   7.549   1.00 13.27 ?  99  ALA A N   1 
ATOM   776  C CA  . ALA A 1 99  ? 8.117   5.960   7.952   1.00 12.46 ?  99  ALA A CA  1 
ATOM   777  C C   . ALA A 1 99  ? 7.529   7.136   7.166   1.00 15.41 ?  99  ALA A C   1 
ATOM   778  O O   . ALA A 1 99  ? 6.370   7.085   6.726   1.00 13.46 ?  99  ALA A O   1 
ATOM   779  C CB  . ALA A 1 99  ? 8.052   6.200   9.465   1.00 13.38 ?  99  ALA A CB  1 
ATOM   780  N N   . MET A 1 100 ? 8.323   8.184   6.932   1.00 12.73 ?  100 MET A N   1 
ATOM   781  C CA  . MET A 1 100 ? 7.800   9.371   6.262   1.00 17.90 ?  100 MET A CA  1 
ATOM   782  C C   . MET A 1 100 ? 7.642   9.172   4.760   1.00 15.64 ?  100 MET A C   1 
ATOM   783  O O   . MET A 1 100 ? 6.749   9.774   4.154   1.00 15.46 ?  100 MET A O   1 
ATOM   784  C CB  . MET A 1 100 ? 8.701   10.572  6.555   1.00 17.43 ?  100 MET A CB  1 
ATOM   785  C CG  . MET A 1 100 ? 8.638   10.975  8.018   1.00 16.84 ?  100 MET A CG  1 
ATOM   786  S SD  . MET A 1 100 ? 9.469   12.522  8.372   1.00 17.85 ?  100 MET A SD  1 
ATOM   787  C CE  . MET A 1 100 ? 11.176  12.065  8.089   1.00 16.58 ?  100 MET A CE  1 
ATOM   788  N N   . VAL A 1 101 ? 8.491   8.341   4.147   1.00 12.08 ?  101 VAL A N   1 
ATOM   789  C CA  . VAL A 1 101 ? 8.246   7.910   2.771   1.00 14.70 ?  101 VAL A CA  1 
ATOM   790  C C   . VAL A 1 101 ? 6.863   7.274   2.651   1.00 14.62 ?  101 VAL A C   1 
ATOM   791  O O   . VAL A 1 101 ? 6.080   7.594   1.745   1.00 14.96 ?  101 VAL A O   1 
ATOM   792  C CB  . VAL A 1 101 ? 9.351   6.945   2.311   1.00 14.96 ?  101 VAL A CB  1 
ATOM   793  C CG1 . VAL A 1 101 ? 8.887   6.163   1.067   1.00 17.62 ?  101 VAL A CG1 1 
ATOM   794  C CG2 . VAL A 1 101 ? 10.638  7.707   2.031   1.00 14.99 ?  101 VAL A CG2 1 
ATOM   795  N N   . ARG A 1 102 ? 6.536   6.359   3.566   1.00 13.54 ?  102 ARG A N   1 
ATOM   796  C CA  . ARG A 1 102 ? 5.240   5.695   3.473   1.00 15.56 ?  102 ARG A CA  1 
ATOM   797  C C   . ARG A 1 102 ? 4.090   6.652   3.770   1.00 15.73 ?  102 ARG A C   1 
ATOM   798  O O   . ARG A 1 102 ? 2.992   6.484   3.225   1.00 17.61 ?  102 ARG A O   1 
ATOM   799  C CB  . ARG A 1 102 ? 5.180   4.502   4.426   1.00 16.10 ?  102 ARG A CB  1 
ATOM   800  C CG  . ARG A 1 102 ? 6.034   3.306   4.033   1.00 17.32 ?  102 ARG A CG  1 
ATOM   801  C CD  . ARG A 1 102 ? 5.680   2.082   4.896   1.00 17.09 ?  102 ARG A CD  1 
ATOM   802  N NE  . ARG A 1 102 ? 5.929   2.321   6.320   1.00 17.03 ?  102 ARG A NE  1 
ATOM   803  C CZ  . ARG A 1 102 ? 7.135   2.278   6.881   1.00 19.90 ?  102 ARG A CZ  1 
ATOM   804  N NH1 . ARG A 1 102 ? 8.210   1.974   6.145   1.00 19.88 1  102 ARG A NH1 1 
ATOM   805  N NH2 . ARG A 1 102 ? 7.267   2.516   8.176   1.00 18.74 ?  102 ARG A NH2 1 
ATOM   806  N N   . GLN A 1 103 ? 4.315   7.653   4.621   1.00 15.13 ?  103 GLN A N   1 
ATOM   807  C CA  . GLN A 1 103 ? 3.234   8.517   5.080   1.00 13.85 ?  103 GLN A CA  1 
ATOM   808  C C   . GLN A 1 103 ? 2.941   9.678   4.138   1.00 18.06 ?  103 GLN A C   1 
ATOM   809  O O   . GLN A 1 103 ? 1.781   10.104  4.032   1.00 17.37 ?  103 GLN A O   1 
ATOM   810  C CB  . GLN A 1 103 ? 3.566   9.080   6.468   1.00 15.79 ?  103 GLN A CB  1 
ATOM   811  C CG  . GLN A 1 103 ? 2.345   9.601   7.182   1.00 18.73 ?  103 GLN A CG  1 
ATOM   812  C CD  . GLN A 1 103 ? 1.338   8.497   7.456   1.00 21.15 ?  103 GLN A CD  1 
ATOM   813  O OE1 . GLN A 1 103 ? 1.689   7.426   7.956   1.00 25.11 ?  103 GLN A OE1 1 
ATOM   814  N NE2 . GLN A 1 103 ? 0.086   8.739   7.095   1.00 23.34 ?  103 GLN A NE2 1 
ATOM   815  N N   . PHE A 1 104 ? 3.959   10.189  3.449   1.00 15.24 ?  104 PHE A N   1 
ATOM   816  C CA  . PHE A 1 104 ? 3.881   11.458  2.736   1.00 15.92 ?  104 PHE A CA  1 
ATOM   817  C C   . PHE A 1 104 ? 4.049   11.324  1.226   1.00 17.55 ?  104 PHE A C   1 
ATOM   818  O O   . PHE A 1 104 ? 4.059   12.343  0.524   1.00 18.00 ?  104 PHE A O   1 
ATOM   819  C CB  . PHE A 1 104 ? 4.937   12.422  3.293   1.00 16.58 ?  104 PHE A CB  1 
ATOM   820  C CG  . PHE A 1 104 ? 4.750   12.733  4.747   1.00 16.79 ?  104 PHE A CG  1 
ATOM   821  C CD1 . PHE A 1 104 ? 3.486   12.972  5.259   1.00 20.49 ?  104 PHE A CD1 1 
ATOM   822  C CD2 . PHE A 1 104 ? 5.831   12.786  5.604   1.00 19.59 ?  104 PHE A CD2 1 
ATOM   823  C CE1 . PHE A 1 104 ? 3.300   13.267  6.613   1.00 19.05 ?  104 PHE A CE1 1 
ATOM   824  C CE2 . PHE A 1 104 ? 5.656   13.080  6.942   1.00 18.68 ?  104 PHE A CE2 1 
ATOM   825  C CZ  . PHE A 1 104 ? 4.384   13.323  7.451   1.00 17.88 ?  104 PHE A CZ  1 
ATOM   826  N N   . THR A 1 105 ? 4.230   10.108  0.716   1.00 14.04 ?  105 THR A N   1 
ATOM   827  C CA  . THR A 1 105 ? 4.233   9.831   -0.716  1.00 16.84 ?  105 THR A CA  1 
ATOM   828  C C   . THR A 1 105 ? 3.386   8.596   -0.987  1.00 17.35 ?  105 THR A C   1 
ATOM   829  O O   . THR A 1 105 ? 2.965   7.884   -0.068  1.00 15.80 ?  105 THR A O   1 
ATOM   830  C CB  . THR A 1 105 ? 5.644   9.588   -1.274  1.00 17.52 ?  105 THR A CB  1 
ATOM   831  O OG1 . THR A 1 105 ? 6.095   8.295   -0.849  1.00 15.60 ?  105 THR A OG1 1 
ATOM   832  C CG2 . THR A 1 105 ? 6.626   10.669  -0.817  1.00 14.72 ?  105 THR A CG2 1 
ATOM   833  N N   . SER A 1 106 ? 3.127   8.358   -2.267  1.00 15.50 ?  106 SER A N   1 
ATOM   834  C CA  . SER A 1 106 ? 2.348   7.205   -2.710  1.00 15.44 ?  106 SER A CA  1 
ATOM   835  C C   . SER A 1 106 ? 3.248   6.209   -3.427  1.00 15.24 ?  106 SER A C   1 
ATOM   836  O O   . SER A 1 106 ? 4.262   6.606   -4.008  1.00 14.15 ?  106 SER A O   1 
ATOM   837  C CB  . SER A 1 106 ? 1.210   7.595   -3.662  1.00 17.83 ?  106 SER A CB  1 
ATOM   838  O OG  . SER A 1 106 ? 0.338   8.537   -3.068  1.00 22.50 ?  106 SER A OG  1 
ATOM   839  N N   . PRO A 1 107 ? 2.915   4.918   -3.408  1.00 15.06 ?  107 PRO A N   1 
ATOM   840  C CA  . PRO A 1 107 ? 3.685   3.954   -4.205  1.00 14.86 ?  107 PRO A CA  1 
ATOM   841  C C   . PRO A 1 107 ? 3.786   4.410   -5.653  1.00 14.21 ?  107 PRO A C   1 
ATOM   842  O O   . PRO A 1 107 ? 2.797   4.823   -6.267  1.00 15.25 ?  107 PRO A O   1 
ATOM   843  C CB  . PRO A 1 107 ? 2.877   2.658   -4.074  1.00 15.21 ?  107 PRO A CB  1 
ATOM   844  C CG  . PRO A 1 107 ? 2.133   2.811   -2.778  1.00 16.42 ?  107 PRO A CG  1 
ATOM   845  C CD  . PRO A 1 107 ? 1.808   4.274   -2.673  1.00 15.56 ?  107 PRO A CD  1 
ATOM   846  N N   . GLY A 1 108 ? 4.993   4.350   -6.194  1.00 13.16 ?  108 GLY A N   1 
ATOM   847  C CA  . GLY A 1 108 ? 5.247   4.778   -7.548  1.00 15.42 ?  108 GLY A CA  1 
ATOM   848  C C   . GLY A 1 108 ? 5.681   6.220   -7.675  1.00 15.12 ?  108 GLY A C   1 
ATOM   849  O O   . GLY A 1 108 ? 6.218   6.595   -8.720  1.00 16.16 ?  108 GLY A O   1 
ATOM   850  N N   . ASP A 1 109 ? 5.465   7.035   -6.644  1.00 14.84 ?  109 ASP A N   1 
ATOM   851  C CA  . ASP A 1 109 ? 5.913   8.419   -6.679  1.00 13.71 ?  109 ASP A CA  1 
ATOM   852  C C   . ASP A 1 109 ? 7.433   8.476   -6.699  1.00 15.75 ?  109 ASP A C   1 
ATOM   853  O O   . ASP A 1 109 ? 8.133   7.537   -6.298  1.00 15.30 ?  109 ASP A O   1 
ATOM   854  C CB  . ASP A 1 109 ? 5.425   9.214   -5.464  1.00 14.71 ?  109 ASP A CB  1 
ATOM   855  C CG  . ASP A 1 109 ? 3.948   9.543   -5.519  1.00 19.46 ?  109 ASP A CG  1 
ATOM   856  O OD1 . ASP A 1 109 ? 3.335   9.378   -6.592  1.00 19.89 ?  109 ASP A OD1 1 
ATOM   857  O OD2 . ASP A 1 109 ? 3.402   9.971   -4.470  1.00 19.84 -1 109 ASP A OD2 1 
ATOM   858  N N   . GLN A 1 110 ? 7.939   9.606   -7.165  1.00 13.32 ?  110 GLN A N   1 
ATOM   859  C CA  . GLN A 1 110 ? 9.370   9.822   -7.241  1.00 14.82 ?  110 GLN A CA  1 
ATOM   860  C C   . GLN A 1 110 ? 9.839   10.625  -6.038  1.00 13.37 ?  110 GLN A C   1 
ATOM   861  O O   . GLN A 1 110 ? 9.141   11.514  -5.542  1.00 14.72 ?  110 GLN A O   1 
ATOM   862  C CB  . GLN A 1 110 ? 9.731   10.537  -8.536  1.00 16.87 ?  110 GLN A CB  1 
ATOM   863  C CG  . GLN A 1 110 ? 9.485   9.704   -9.779  1.00 17.37 ?  110 GLN A CG  1 
ATOM   864  C CD  . GLN A 1 110 ? 9.959   10.418  -11.022 1.00 19.34 ?  110 GLN A CD  1 
ATOM   865  O OE1 . GLN A 1 110 ? 9.314   11.352  -11.501 1.00 23.26 ?  110 GLN A OE1 1 
ATOM   866  N NE2 . GLN A 1 110 ? 11.105  10.013  -11.526 1.00 17.48 ?  110 GLN A NE2 1 
ATOM   867  N N   . ILE A 1 111 ? 11.038  10.308  -5.573  1.00 12.97 ?  111 ILE A N   1 
ATOM   868  C CA  . ILE A 1 111 ? 11.640  10.973  -4.429  1.00 13.03 ?  111 ILE A CA  1 
ATOM   869  C C   . ILE A 1 111 ? 13.050  11.347  -4.839  1.00 13.97 ?  111 ILE A C   1 
ATOM   870  O O   . ILE A 1 111 ? 13.797  10.496  -5.334  1.00 13.01 ?  111 ILE A O   1 
ATOM   871  C CB  . ILE A 1 111 ? 11.628  10.075  -3.181  1.00 13.39 ?  111 ILE A CB  1 
ATOM   872  C CG1 . ILE A 1 111 ? 10.175  9.779   -2.781  1.00 13.16 ?  111 ILE A CG1 1 
ATOM   873  C CG2 . ILE A 1 111 ? 12.410  10.719  -2.031  1.00 14.24 ?  111 ILE A CG2 1 
ATOM   874  C CD1 . ILE A 1 111 ? 10.032  8.872   -1.596  1.00 15.29 ?  111 ILE A CD1 1 
ATOM   875  N N   . LEU A 1 112 ? 13.383  12.626  -4.705  1.00 11.83 ?  112 LEU A N   1 
ATOM   876  C CA  . LEU A 1 112 ? 14.602  13.164  -5.292  1.00 12.58 ?  112 LEU A CA  1 
ATOM   877  C C   . LEU A 1 112 ? 15.748  13.103  -4.298  1.00 14.19 ?  112 LEU A C   1 
ATOM   878  O O   . LEU A 1 112 ? 15.597  13.510  -3.142  1.00 12.73 ?  112 LEU A O   1 
ATOM   879  C CB  . LEU A 1 112 ? 14.397  14.609  -5.739  1.00 13.18 ?  112 LEU A CB  1 
ATOM   880  C CG  . LEU A 1 112 ? 15.574  15.242  -6.485  1.00 14.24 ?  112 LEU A CG  1 
ATOM   881  C CD1 . LEU A 1 112 ? 15.044  16.200  -7.538  1.00 16.36 ?  112 LEU A CD1 1 
ATOM   882  C CD2 . LEU A 1 112 ? 16.516  15.974  -5.546  1.00 16.30 ?  112 LEU A CD2 1 
ATOM   883  N N   . VAL A 1 113 ? 16.909  12.652  -4.773  1.00 12.41 ?  113 VAL A N   1 
ATOM   884  C CA  . VAL A 1 113 ? 18.155  12.702  -4.025  1.00 13.81 ?  113 VAL A CA  1 
ATOM   885  C C   . VAL A 1 113 ? 19.215  13.356  -4.911  1.00 14.11 ?  113 VAL A C   1 
ATOM   886  O O   . VAL A 1 113 ? 18.974  13.646  -6.083  1.00 15.95 ?  113 VAL A O   1 
ATOM   887  C CB  . VAL A 1 113 ? 18.603  11.305  -3.553  1.00 13.51 ?  113 VAL A CB  1 
ATOM   888  C CG1 . VAL A 1 113 ? 17.547  10.697  -2.622  1.00 14.08 ?  113 VAL A CG1 1 
ATOM   889  C CG2 . VAL A 1 113 ? 18.830  10.395  -4.763  1.00 15.09 ?  113 VAL A CG2 1 
ATOM   890  N N   . GLN A 1 114 ? 20.397  13.578  -4.343  1.00 11.51 ?  114 GLN A N   1 
ATOM   891  C CA  . GLN A 1 114 ? 21.513  14.211  -5.053  1.00 16.33 ?  114 GLN A CA  1 
ATOM   892  C C   . GLN A 1 114 ? 22.686  13.239  -5.085  1.00 12.93 ?  114 GLN A C   1 
ATOM   893  O O   . GLN A 1 114 ? 23.536  13.230  -4.193  1.00 12.05 ?  114 GLN A O   1 
ATOM   894  C CB  . GLN A 1 114 ? 21.902  15.535  -4.402  1.00 15.97 ?  114 GLN A CB  1 
ATOM   895  C CG  . GLN A 1 114 ? 20.778  16.548  -4.351  1.00 15.93 ?  114 GLN A CG  1 
ATOM   896  C CD  . GLN A 1 114 ? 21.150  17.791  -3.562  1.00 16.79 ?  114 GLN A CD  1 
ATOM   897  O OE1 . GLN A 1 114 ? 21.140  17.791  -2.324  1.00 16.51 ?  114 GLN A OE1 1 
ATOM   898  N NE2 . GLN A 1 114 ? 21.505  18.855  -4.279  1.00 16.90 ?  114 GLN A NE2 1 
ATOM   899  N N   . GLU A 1 115 ? 22.756  12.443  -6.146  1.00 14.17 ?  115 GLU A N   1 
ATOM   900  C CA  . GLU A 1 115 ? 23.789  11.422  -6.249  1.00 13.41 ?  115 GLU A CA  1 
ATOM   901  C C   . GLU A 1 115 ? 25.157  12.062  -6.494  1.00 16.07 ?  115 GLU A C   1 
ATOM   902  O O   . GLU A 1 115 ? 25.263  13.035  -7.251  1.00 14.99 ?  115 GLU A O   1 
ATOM   903  C CB  . GLU A 1 115 ? 23.463  10.454  -7.393  1.00 16.32 ?  115 GLU A CB  1 
ATOM   904  C CG  . GLU A 1 115 ? 22.228  9.566   -7.172  1.00 17.12 ?  115 GLU A CG  1 
ATOM   905  C CD  . GLU A 1 115 ? 22.010  8.561   -8.303  1.00 22.38 ?  115 GLU A CD  1 
ATOM   906  O OE1 . GLU A 1 115 ? 20.900  7.999   -8.413  1.00 21.83 ?  115 GLU A OE1 1 
ATOM   907  O OE2 . GLU A 1 115 ? 22.948  8.340   -9.092  1.00 21.46 -1 115 GLU A OE2 1 
ATOM   908  N N   . PRO A 1 116 ? 26.239  11.505  -5.923  1.00 15.48 ?  116 PRO A N   1 
ATOM   909  C CA  . PRO A 1 116 ? 26.296  10.312  -5.075  1.00 14.61 ?  116 PRO A CA  1 
ATOM   910  C C   . PRO A 1 116 ? 25.866  10.629  -3.652  1.00 13.90 ?  116 PRO A C   1 
ATOM   911  O O   . PRO A 1 116 ? 26.199  11.697  -3.142  1.00 12.89 ?  116 PRO A O   1 
ATOM   912  C CB  . PRO A 1 116 ? 27.774  9.926   -5.113  1.00 16.28 ?  116 PRO A CB  1 
ATOM   913  C CG  . PRO A 1 116 ? 28.489  11.235  -5.306  1.00 15.46 ?  116 PRO A CG  1 
ATOM   914  C CD  . PRO A 1 116 ? 27.584  12.062  -6.177  1.00 17.07 ?  116 PRO A CD  1 
ATOM   915  N N   . VAL A 1 117 ? 25.132  9.722   -3.005  1.00 13.97 ?  117 VAL A N   1 
ATOM   916  C CA  . VAL A 1 117 ? 24.644  9.972   -1.659  1.00 12.70 ?  117 VAL A CA  1 
ATOM   917  C C   . VAL A 1 117 ? 24.507  8.652   -0.916  1.00 12.31 ?  117 VAL A C   1 
ATOM   918  O O   . VAL A 1 117 ? 24.535  7.566   -1.505  1.00 14.28 ?  117 VAL A O   1 
ATOM   919  C CB  . VAL A 1 117 ? 23.307  10.750  -1.691  1.00 12.23 ?  117 VAL A CB  1 
ATOM   920  C CG1 . VAL A 1 117 ? 22.161  9.858   -2.156  1.00 14.92 ?  117 VAL A CG1 1 
ATOM   921  C CG2 . VAL A 1 117 ? 23.006  11.391  -0.324  1.00 13.17 ?  117 VAL A CG2 1 
ATOM   922  N N   . TYR A 1 118 ? 24.398  8.767   0.403   1.00 11.00 ?  118 TYR A N   1 
ATOM   923  C CA  . TYR A 1 118 ? 24.282  7.643   1.322   1.00 14.16 ?  118 TYR A CA  1 
ATOM   924  C C   . TYR A 1 118 ? 23.394  6.530   0.777   1.00 14.21 ?  118 TYR A C   1 
ATOM   925  O O   . TYR A 1 118 ? 22.243  6.762   0.393   1.00 13.41 ?  118 TYR A O   1 
ATOM   926  C CB  . TYR A 1 118 ? 23.727  8.173   2.642   1.00 14.92 ?  118 TYR A CB  1 
ATOM   927  C CG  . TYR A 1 118 ? 23.594  7.143   3.729   1.00 17.12 ?  118 TYR A CG  1 
ATOM   928  C CD1 . TYR A 1 118 ? 24.554  6.152   3.901   1.00 17.86 ?  118 TYR A CD1 1 
ATOM   929  C CD2 . TYR A 1 118 ? 22.515  7.179   4.604   1.00 18.30 ?  118 TYR A CD2 1 
ATOM   930  C CE1 . TYR A 1 118 ? 24.437  5.219   4.928   1.00 20.70 ?  118 TYR A CE1 1 
ATOM   931  C CE2 . TYR A 1 118 ? 22.393  6.257   5.621   1.00 20.25 ?  118 TYR A CE2 1 
ATOM   932  C CZ  . TYR A 1 118 ? 23.353  5.283   5.776   1.00 21.43 ?  118 TYR A CZ  1 
ATOM   933  O OH  . TYR A 1 118 ? 23.216  4.362   6.788   1.00 25.37 ?  118 TYR A OH  1 
ATOM   934  N N   . ASN A 1 119 ? 23.936  5.308   0.778   1.00 13.95 ?  119 ASN A N   1 
ATOM   935  C CA  . ASN A 1 119 ? 23.286  4.196   0.084   1.00 14.61 ?  119 ASN A CA  1 
ATOM   936  C C   . ASN A 1 119 ? 21.930  3.848   0.681   1.00 16.97 ?  119 ASN A C   1 
ATOM   937  O O   . ASN A 1 119 ? 21.053  3.365   -0.040  1.00 15.51 ?  119 ASN A O   1 
ATOM   938  C CB  . ASN A 1 119 ? 24.199  2.966   0.086   1.00 15.09 ?  119 ASN A CB  1 
ATOM   939  C CG  . ASN A 1 119 ? 24.699  2.631   1.459   1.00 16.76 ?  119 ASN A CG  1 
ATOM   940  O OD1 . ASN A 1 119 ? 25.560  3.318   2.000   1.00 20.92 ?  119 ASN A OD1 1 
ATOM   941  N ND2 . ASN A 1 119 ? 24.155  1.580   2.047   1.00 20.43 ?  119 ASN A ND2 1 
ATOM   942  N N   . MET A 1 120 ? 21.709  4.120   1.969   1.00 16.85 ?  120 MET A N   1 
ATOM   943  C CA  . MET A 1 120 ? 20.427  3.742   2.558   1.00 16.47 ?  120 MET A CA  1 
ATOM   944  C C   . MET A 1 120 ? 19.272  4.602   2.055   1.00 16.65 ?  120 MET A C   1 
ATOM   945  O O   . MET A 1 120 ? 18.114  4.191   2.190   1.00 15.62 ?  120 MET A O   1 
ATOM   946  C CB  . MET A 1 120 ? 20.511  3.793   4.085   1.00 19.62 ?  120 MET A CB  1 
ATOM   947  C CG  . MET A 1 120 ? 21.303  2.634   4.664   1.00 22.00 ?  120 MET A CG  1 
ATOM   948  S SD  . MET A 1 120 ? 20.520  1.043   4.324   1.00 32.28 ?  120 MET A SD  1 
ATOM   949  C CE  . MET A 1 120 ? 21.797  0.202   3.428   1.00 29.15 ?  120 MET A CE  1 
ATOM   950  N N   . PHE A 1 121 ? 19.548  5.779   1.486   1.00 14.38 ?  121 PHE A N   1 
ATOM   951  C CA  . PHE A 1 121 ? 18.491  6.552   0.840   1.00 16.02 ?  121 PHE A CA  1 
ATOM   952  C C   . PHE A 1 121 ? 17.812  5.729   -0.252  1.00 15.05 ?  121 PHE A C   1 
ATOM   953  O O   . PHE A 1 121 ? 16.578  5.664   -0.329  1.00 13.94 ?  121 PHE A O   1 
ATOM   954  C CB  . PHE A 1 121 ? 19.067  7.842   0.246   1.00 13.83 ?  121 PHE A CB  1 
ATOM   955  C CG  . PHE A 1 121 ? 19.381  8.915   1.260   1.00 15.00 ?  121 PHE A CG  1 
ATOM   956  C CD1 . PHE A 1 121 ? 19.390  8.644   2.616   1.00 16.35 ?  121 PHE A CD1 1 
ATOM   957  C CD2 . PHE A 1 121 ? 19.667  10.208  0.839   1.00 15.14 ?  121 PHE A CD2 1 
ATOM   958  C CE1 . PHE A 1 121 ? 19.693  9.648   3.541   1.00 18.28 ?  121 PHE A CE1 1 
ATOM   959  C CE2 . PHE A 1 121 ? 19.963  11.210  1.753   1.00 14.52 ?  121 PHE A CE2 1 
ATOM   960  C CZ  . PHE A 1 121 ? 19.990  10.924  3.102   1.00 15.19 ?  121 PHE A CZ  1 
ATOM   961  N N   . TYR A 1 122 ? 18.613  5.065   -1.091  1.00 14.39 ?  122 TYR A N   1 
ATOM   962  C CA  . TYR A 1 122 ? 18.066  4.227   -2.155  1.00 15.08 ?  122 TYR A CA  1 
ATOM   963  C C   . TYR A 1 122 ? 17.285  3.048   -1.584  1.00 16.16 ?  122 TYR A C   1 
ATOM   964  O O   . TYR A 1 122 ? 16.185  2.736   -2.062  1.00 15.40 ?  122 TYR A O   1 
ATOM   965  C CB  . TYR A 1 122 ? 19.194  3.722   -3.060  1.00 14.51 ?  122 TYR A CB  1 
ATOM   966  C CG  . TYR A 1 122 ? 20.173  4.780   -3.483  1.00 12.82 ?  122 TYR A CG  1 
ATOM   967  C CD1 . TYR A 1 122 ? 19.743  5.928   -4.128  1.00 14.78 ?  122 TYR A CD1 1 
ATOM   968  C CD2 . TYR A 1 122 ? 21.529  4.633   -3.239  1.00 13.93 ?  122 TYR A CD2 1 
ATOM   969  C CE1 . TYR A 1 122 ? 20.627  6.900   -4.528  1.00 15.61 ?  122 TYR A CE1 1 
ATOM   970  C CE2 . TYR A 1 122 ? 22.435  5.620   -3.622  1.00 14.17 ?  122 TYR A CE2 1 
ATOM   971  C CZ  . TYR A 1 122 ? 21.977  6.744   -4.267  1.00 13.82 ?  122 TYR A CZ  1 
ATOM   972  O OH  . TYR A 1 122 ? 22.847  7.723   -4.672  1.00 15.19 ?  122 TYR A OH  1 
ATOM   973  N N   . SER A 1 123 ? 17.829  2.404   -0.545  1.00 14.78 ?  123 SER A N   1 
ATOM   974  C CA  . SER A 1 123 ? 17.173  1.264   0.092   1.00 17.64 ?  123 SER A CA  1 
ATOM   975  C C   . SER A 1 123 ? 15.788  1.628   0.588   1.00 17.22 ?  123 SER A C   1 
ATOM   976  O O   . SER A 1 123 ? 14.822  0.887   0.375   1.00 15.57 ?  123 SER A O   1 
ATOM   977  C CB  . SER A 1 123 ? 18.009  0.750   1.279   1.00 18.46 ?  123 SER A CB  1 
ATOM   978  O OG  . SER A 1 123 ? 19.330  0.454   0.890   1.00 28.61 ?  123 SER A OG  1 
ATOM   979  N N   . VAL A 1 124 ? 15.673  2.747   1.297   1.00 15.91 ?  124 VAL A N   1 
ATOM   980  C CA  . VAL A 1 124 ? 14.375  3.052   1.882   1.00 16.96 ?  124 VAL A CA  1 
ATOM   981  C C   . VAL A 1 124 ? 13.404  3.582   0.833   1.00 17.26 ?  124 VAL A C   1 
ATOM   982  O O   . VAL A 1 124 ? 12.189  3.382   0.952   1.00 19.16 ?  124 VAL A O   1 
ATOM   983  C CB  . VAL A 1 124 ? 14.520  4.020   3.070   1.00 18.27 ?  124 VAL A CB  1 
ATOM   984  C CG1 . VAL A 1 124 ? 15.434  3.414   4.109   1.00 19.59 ?  124 VAL A CG1 1 
ATOM   985  C CG2 . VAL A 1 124 ? 15.039  5.360   2.621   1.00 18.94 ?  124 VAL A CG2 1 
ATOM   986  N N   . ILE A 1 125 ? 13.894  4.250   -0.210  1.00 14.06 ?  125 ILE A N   1 
ATOM   987  C CA  . ILE A 1 125 ? 12.989  4.722   -1.249  1.00 15.42 ?  125 ILE A CA  1 
ATOM   988  C C   . ILE A 1 125 ? 12.480  3.546   -2.076  1.00 13.82 ?  125 ILE A C   1 
ATOM   989  O O   . ILE A 1 125 ? 11.265  3.349   -2.228  1.00 13.10 ?  125 ILE A O   1 
ATOM   990  C CB  . ILE A 1 125 ? 13.684  5.787   -2.123  1.00 13.36 ?  125 ILE A CB  1 
ATOM   991  C CG1 . ILE A 1 125 ? 13.931  7.051   -1.300  1.00 13.96 ?  125 ILE A CG1 1 
ATOM   992  C CG2 . ILE A 1 125 ? 12.838  6.126   -3.371  1.00 13.27 ?  125 ILE A CG2 1 
ATOM   993  C CD1 . ILE A 1 125 ? 14.812  8.048   -1.986  1.00 17.18 ?  125 ILE A CD1 1 
ATOM   994  N N   . GLU A 1 126 ? 13.403  2.734   -2.601  1.00 13.80 ?  126 GLU A N   1 
ATOM   995  C CA  . GLU A 1 126 ? 13.026  1.650   -3.501  1.00 15.31 ?  126 GLU A CA  1 
ATOM   996  C C   . GLU A 1 126 ? 12.391  0.481   -2.746  1.00 13.56 ?  126 GLU A C   1 
ATOM   997  O O   . GLU A 1 126 ? 11.450  -0.138  -3.246  1.00 16.00 ?  126 GLU A O   1 
ATOM   998  C CB  . GLU A 1 126 ? 14.251  1.209   -4.313  1.00 17.57 ?  126 GLU A CB  1 
ATOM   999  C CG  . GLU A 1 126 ? 14.873  2.374   -5.108  1.00 16.33 ?  126 GLU A CG  1 
ATOM   1000 C CD  . GLU A 1 126 ? 16.185  2.029   -5.845  1.00 19.84 ?  126 GLU A CD  1 
ATOM   1001 O OE1 . GLU A 1 126 ? 16.457  2.672   -6.890  1.00 21.40 ?  126 GLU A OE1 1 
ATOM   1002 O OE2 . GLU A 1 126 ? 16.956  1.152   -5.382  1.00 17.81 -1 126 GLU A OE2 1 
ATOM   1003 N N   . GLY A 1 127 ? 12.863  0.185   -1.532  1.00 14.82 ?  127 GLY A N   1 
ATOM   1004 C CA  . GLY A 1 127 ? 12.268  -0.896  -0.762  1.00 15.71 ?  127 GLY A CA  1 
ATOM   1005 C C   . GLY A 1 127 ? 10.823  -0.627  -0.391  1.00 17.53 ?  127 GLY A C   1 
ATOM   1006 O O   . GLY A 1 127 ? 10.032  -1.565  -0.222  1.00 14.69 ?  127 GLY A O   1 
ATOM   1007 N N   . ASN A 1 128 ? 10.455  0.650   -0.262  1.00 13.58 ?  128 ASN A N   1 
ATOM   1008 C CA  . ASN A 1 128 ? 9.073   1.042   -0.027  1.00 13.49 ?  128 ASN A CA  1 
ATOM   1009 C C   . ASN A 1 128 ? 8.283   1.237   -1.320  1.00 14.64 ?  128 ASN A C   1 
ATOM   1010 O O   . ASN A 1 128 ? 7.125   1.654   -1.266  1.00 14.22 ?  128 ASN A O   1 
ATOM   1011 C CB  . ASN A 1 128 ? 9.025   2.329   0.806   1.00 14.54 ?  128 ASN A CB  1 
ATOM   1012 C CG  . ASN A 1 128 ? 9.254   2.071   2.285   1.00 16.43 ?  128 ASN A CG  1 
ATOM   1013 O OD1 . ASN A 1 128 ? 8.449   1.411   2.947   1.00 15.70 ?  128 ASN A OD1 1 
ATOM   1014 N ND2 . ASN A 1 128 ? 10.366  2.570   2.808   1.00 16.06 ?  128 ASN A ND2 1 
ATOM   1015 N N   . GLY A 1 129 ? 8.861   0.947   -2.478  1.00 14.28 ?  129 GLY A N   1 
ATOM   1016 C CA  . GLY A 1 129 ? 8.068   1.053   -3.691  1.00 13.19 ?  129 GLY A CA  1 
ATOM   1017 C C   . GLY A 1 129 ? 7.916   2.455   -4.227  1.00 14.38 ?  129 GLY A C   1 
ATOM   1018 O O   . GLY A 1 129 ? 6.946   2.741   -4.938  1.00 15.29 ?  129 GLY A O   1 
ATOM   1019 N N   . ARG A 1 130 ? 8.833   3.342   -3.888  1.00 12.94 ?  130 ARG A N   1 
ATOM   1020 C CA  . ARG A 1 130 ? 8.924   4.647   -4.510  1.00 13.22 ?  130 ARG A CA  1 
ATOM   1021 C C   . ARG A 1 130 ? 10.126  4.615   -5.446  1.00 14.56 ?  130 ARG A C   1 
ATOM   1022 O O   . ARG A 1 130 ? 10.943  3.688   -5.410  1.00 12.91 ?  130 ARG A O   1 
ATOM   1023 C CB  . ARG A 1 130 ? 9.022   5.747   -3.439  1.00 13.20 ?  130 ARG A CB  1 
ATOM   1024 C CG  . ARG A 1 130 ? 7.657   6.140   -2.811  1.00 12.45 ?  130 ARG A CG  1 
ATOM   1025 C CD  . ARG A 1 130 ? 6.972   5.007   -2.028  1.00 14.35 ?  130 ARG A CD  1 
ATOM   1026 N NE  . ARG A 1 130 ? 5.864   5.476   -1.184  1.00 12.84 ?  130 ARG A NE  1 
ATOM   1027 C CZ  . ARG A 1 130 ? 5.015   4.680   -0.533  1.00 13.41 ?  130 ARG A CZ  1 
ATOM   1028 N NH1 . ARG A 1 130 ? 5.109   3.361   -0.628  1.00 15.10 1  130 ARG A NH1 1 
ATOM   1029 N NH2 . ARG A 1 130 ? 4.051   5.200   0.209   1.00 14.50 ?  130 ARG A NH2 1 
ATOM   1030 N N   . ARG A 1 131 ? 10.217  5.618   -6.310  1.00 14.21 ?  131 ARG A N   1 
ATOM   1031 C CA  . ARG A 1 131 ? 11.210  5.624   -7.369  1.00 14.48 ?  131 ARG A CA  1 
ATOM   1032 C C   . ARG A 1 131 ? 12.222  6.734   -7.120  1.00 13.94 ?  131 ARG A C   1 
ATOM   1033 O O   . ARG A 1 131 ? 11.847  7.886   -6.884  1.00 15.53 ?  131 ARG A O   1 
ATOM   1034 C CB  . ARG A 1 131 ? 10.522  5.771   -8.728  1.00 15.99 ?  131 ARG A CB  1 
ATOM   1035 C CG  . ARG A 1 131 ? 9.756   4.492   -9.102  1.00 18.80 ?  131 ARG A CG  1 
ATOM   1036 C CD  . ARG A 1 131 ? 9.194   4.535   -10.510 1.00 22.89 ?  131 ARG A CD  1 
ATOM   1037 N NE  . ARG A 1 131 ? 7.947   5.288   -10.556 1.00 23.72 ?  131 ARG A NE  1 
ATOM   1038 C CZ  . ARG A 1 131 ? 7.112   5.283   -11.586 1.00 24.51 ?  131 ARG A CZ  1 
ATOM   1039 N NH1 . ARG A 1 131 ? 7.403   4.575   -12.674 1.00 26.40 1  131 ARG A NH1 1 
ATOM   1040 N NH2 . ARG A 1 131 ? 5.995   5.995   -11.532 1.00 26.42 ?  131 ARG A NH2 1 
ATOM   1041 N N   . VAL A 1 132 ? 13.503  6.368   -7.120  1.00 13.94 ?  132 VAL A N   1 
ATOM   1042 C CA  . VAL A 1 132 ? 14.568  7.352   -6.980  1.00 15.77 ?  132 VAL A CA  1 
ATOM   1043 C C   . VAL A 1 132 ? 14.655  8.183   -8.251  1.00 14.86 ?  132 VAL A C   1 
ATOM   1044 O O   . VAL A 1 132 ? 14.723  7.643   -9.361  1.00 15.57 ?  132 VAL A O   1 
ATOM   1045 C CB  . VAL A 1 132 ? 15.914  6.666   -6.704  1.00 15.78 ?  132 VAL A CB  1 
ATOM   1046 C CG1 . VAL A 1 132 ? 17.057  7.714   -6.656  1.00 16.51 ?  132 VAL A CG1 1 
ATOM   1047 C CG2 . VAL A 1 132 ? 15.863  5.862   -5.421  1.00 14.94 ?  132 VAL A CG2 1 
ATOM   1048 N N   . ILE A 1 133 ? 14.651  9.502   -8.097  1.00 14.08 ?  133 ILE A N   1 
ATOM   1049 C CA  . ILE A 1 133 ? 15.113  10.402  -9.145  1.00 15.03 ?  133 ILE A CA  1 
ATOM   1050 C C   . ILE A 1 133 ? 16.273  11.205  -8.572  1.00 16.08 ?  133 ILE A C   1 
ATOM   1051 O O   . ILE A 1 133 ? 16.267  11.580  -7.392  1.00 13.76 ?  133 ILE A O   1 
ATOM   1052 C CB  . ILE A 1 133 ? 13.994  11.318  -9.679  1.00 15.78 ?  133 ILE A CB  1 
ATOM   1053 C CG1 . ILE A 1 133 ? 14.506  12.130  -10.874 1.00 16.71 ?  133 ILE A CG1 1 
ATOM   1054 C CG2 . ILE A 1 133 ? 13.457  12.234  -8.582  1.00 15.36 ?  133 ILE A CG2 1 
ATOM   1055 C CD1 . ILE A 1 133 ? 13.404  12.835  -11.614 1.00 17.33 ?  133 ILE A CD1 1 
ATOM   1056 N N   . SER A 1 134 ? 17.294  11.434  -9.382  1.00 14.36 ?  134 SER A N   1 
ATOM   1057 C CA  . SER A 1 134 ? 18.453  12.170  -8.913  1.00 15.06 ?  134 SER A CA  1 
ATOM   1058 C C   . SER A 1 134 ? 18.662  13.408  -9.765  1.00 17.46 ?  134 SER A C   1 
ATOM   1059 O O   . SER A 1 134 ? 18.528  13.350  -10.992 1.00 18.69 ?  134 SER A O   1 
ATOM   1060 C CB  . SER A 1 134 ? 19.700  11.286  -8.950  1.00 15.66 ?  134 SER A CB  1 
ATOM   1061 O OG  . SER A 1 134 ? 20.877  12.022  -8.657  1.00 18.73 ?  134 SER A OG  1 
ATOM   1062 N N   . SER A 1 135 ? 18.957  14.531  -9.101  1.00 17.46 ?  135 SER A N   1 
ATOM   1063 C CA  . SER A 1 135 ? 19.672  15.639  -9.725  1.00 17.93 ?  135 SER A CA  1 
ATOM   1064 C C   . SER A 1 135 ? 21.126  15.420  -9.344  1.00 18.21 ?  135 SER A C   1 
ATOM   1065 O O   . SER A 1 135 ? 21.550  15.762  -8.240  1.00 17.78 ?  135 SER A O   1 
ATOM   1066 C CB  . SER A 1 135 ? 19.157  16.995  -9.255  1.00 16.69 ?  135 SER A CB  1 
ATOM   1067 O OG  . SER A 1 135 ? 19.808  18.045  -9.964  1.00 20.07 ?  135 SER A OG  1 
ATOM   1068 N N   . ASP A 1 136 ? 21.879  14.780  -10.243 1.00 16.68 ?  136 ASP A N   1 
ATOM   1069 C CA  . ASP A 1 136 ? 23.252  14.401  -9.941  1.00 16.74 ?  136 ASP A CA  1 
ATOM   1070 C C   . ASP A 1 136 ? 24.068  15.632  -9.590  1.00 19.74 ?  136 ASP A C   1 
ATOM   1071 O O   . ASP A 1 136 ? 23.935  16.685  -10.220 1.00 15.83 ?  136 ASP A O   1 
ATOM   1072 C CB  . ASP A 1 136 ? 23.898  13.705  -11.143 1.00 20.86 ?  136 ASP A CB  1 
ATOM   1073 C CG  . ASP A 1 136 ? 23.452  12.256  -11.319 1.00 23.58 ?  136 ASP A CG  1 
ATOM   1074 O OD1 . ASP A 1 136 ? 22.470  11.820  -10.684 1.00 20.41 ?  136 ASP A OD1 1 
ATOM   1075 O OD2 . ASP A 1 136 ? 24.076  11.557  -12.140 1.00 24.99 -1 136 ASP A OD2 1 
ATOM   1076 N N   . LEU A 1 137 ? 24.916  15.498  -8.573  1.00 16.03 ?  137 LEU A N   1 
ATOM   1077 C CA  . LEU A 1 137 ? 25.928  16.511  -8.337  1.00 17.28 ?  137 LEU A CA  1 
ATOM   1078 C C   . LEU A 1 137 ? 26.915  16.487  -9.498  1.00 17.49 ?  137 LEU A C   1 
ATOM   1079 O O   . LEU A 1 137 ? 27.303  15.414  -9.968  1.00 19.40 ?  137 LEU A O   1 
ATOM   1080 C CB  . LEU A 1 137 ? 26.634  16.252  -7.019  1.00 15.53 ?  137 LEU A CB  1 
ATOM   1081 C CG  . LEU A 1 137 ? 25.680  16.310  -5.831  1.00 16.97 ?  137 LEU A CG  1 
ATOM   1082 C CD1 . LEU A 1 137 ? 26.398  15.920  -4.554  1.00 17.35 ?  137 LEU A CD1 1 
ATOM   1083 C CD2 . LEU A 1 137 ? 25.085  17.712  -5.740  1.00 17.27 ?  137 LEU A CD2 1 
ATOM   1084 N N   . ILE A 1 138 ? 27.301  17.666  -9.972  1.00 19.67 ?  138 ILE A N   1 
ATOM   1085 C CA  . ILE A 1 138 ? 28.275  17.772  -11.054 1.00 20.78 ?  138 ILE A CA  1 
ATOM   1086 C C   . ILE A 1 138 ? 29.672  17.677  -10.456 1.00 20.16 ?  138 ILE A C   1 
ATOM   1087 O O   . ILE A 1 138 ? 29.981  18.341  -9.461  1.00 23.21 ?  138 ILE A O   1 
ATOM   1088 C CB  . ILE A 1 138 ? 28.086  19.084  -11.838 1.00 24.11 ?  138 ILE A CB  1 
ATOM   1089 C CG1 . ILE A 1 138 ? 26.653  19.211  -12.367 1.00 23.12 ?  138 ILE A CG1 1 
ATOM   1090 C CG2 . ILE A 1 138 ? 29.064  19.154  -13.000 1.00 25.46 ?  138 ILE A CG2 1 
ATOM   1091 C CD1 . ILE A 1 138 ? 26.112  17.922  -13.003 1.00 27.13 ?  138 ILE A CD1 1 
ATOM   1092 N N   . TYR A 1 139 ? 30.511  16.830  -11.035 1.00 16.89 ?  139 TYR A N   1 
ATOM   1093 C CA  . TYR A 1 139 ? 31.855  16.611  -10.513 1.00 19.91 ?  139 TYR A CA  1 
ATOM   1094 C C   . TYR A 1 139 ? 32.865  17.140  -11.528 1.00 23.04 ?  139 TYR A C   1 
ATOM   1095 O O   . TYR A 1 139 ? 32.990  16.593  -12.629 1.00 21.07 ?  139 TYR A O   1 
ATOM   1096 C CB  . TYR A 1 139 ? 32.099  15.131  -10.220 1.00 18.70 ?  139 TYR A CB  1 
ATOM   1097 C CG  . TYR A 1 139 ? 33.455  14.869  -9.604  1.00 18.76 ?  139 TYR A CG  1 
ATOM   1098 C CD1 . TYR A 1 139 ? 33.777  15.394  -8.365  1.00 18.76 ?  139 TYR A CD1 1 
ATOM   1099 C CD2 . TYR A 1 139 ? 34.404  14.093  -10.257 1.00 19.83 ?  139 TYR A CD2 1 
ATOM   1100 C CE1 . TYR A 1 139 ? 34.999  15.169  -7.797  1.00 20.26 ?  139 TYR A CE1 1 
ATOM   1101 C CE2 . TYR A 1 139 ? 35.642  13.857  -9.690  1.00 18.57 ?  139 TYR A CE2 1 
ATOM   1102 C CZ  . TYR A 1 139 ? 35.928  14.398  -8.456  1.00 20.15 ?  139 TYR A CZ  1 
ATOM   1103 O OH  . TYR A 1 139 ? 37.142  14.190  -7.855  1.00 20.48 ?  139 TYR A OH  1 
ATOM   1104 N N   . GLU A 1 140 ? 33.583  18.199  -11.154 1.00 23.77 ?  140 GLU A N   1 
ATOM   1105 C CA  . GLU A 1 140 ? 34.620  18.795  -11.988 1.00 26.50 ?  140 GLU A CA  1 
ATOM   1106 C C   . GLU A 1 140 ? 35.693  19.357  -11.064 1.00 27.51 ?  140 GLU A C   1 
ATOM   1107 O O   . GLU A 1 140 ? 35.371  19.918  -10.014 1.00 27.31 ?  140 GLU A O   1 
ATOM   1108 C CB  . GLU A 1 140 ? 34.039  19.904  -12.901 1.00 30.14 ?  140 GLU A CB  1 
ATOM   1109 C CG  . GLU A 1 140 ? 34.430  19.806  -14.394 1.00 39.61 ?  140 GLU A CG  1 
ATOM   1110 C CD  . GLU A 1 140 ? 33.804  20.906  -15.269 1.00 45.71 ?  140 GLU A CD  1 
ATOM   1111 O OE1 . GLU A 1 140 ? 32.609  21.238  -15.064 1.00 47.51 ?  140 GLU A OE1 1 
ATOM   1112 O OE2 . GLU A 1 140 ? 34.513  21.431  -16.163 1.00 46.51 -1 140 GLU A OE2 1 
ATOM   1113 N N   . ASN A 1 141 ? 36.967  19.180  -11.428 1.00 27.04 ?  141 ASN A N   1 
ATOM   1114 C CA  . ASN A 1 141 ? 38.077  19.777  -10.671 1.00 30.25 ?  141 ASN A CA  1 
ATOM   1115 C C   . ASN A 1 141 ? 38.095  19.314  -9.210  1.00 26.72 ?  141 ASN A C   1 
ATOM   1116 O O   . ASN A 1 141 ? 38.318  20.118  -8.305  1.00 27.04 ?  141 ASN A O   1 
ATOM   1117 C CB  . ASN A 1 141 ? 38.020  21.313  -10.707 1.00 30.27 ?  141 ASN A CB  1 
ATOM   1118 C CG  . ASN A 1 141 ? 38.282  21.903  -12.081 1.00 32.20 ?  141 ASN A CG  1 
ATOM   1119 O OD1 . ASN A 1 141 ? 38.900  21.277  -12.947 1.00 32.66 ?  141 ASN A OD1 1 
ATOM   1120 N ND2 . ASN A 1 141 ? 37.799  23.134  -12.285 1.00 31.76 ?  141 ASN A ND2 1 
ATOM   1121 N N   . SER A 1 142 ? 37.835  18.025  -8.965  1.00 26.70 ?  142 SER A N   1 
ATOM   1122 C CA  . SER A 1 142 ? 37.874  17.450  -7.613  1.00 23.46 ?  142 SER A CA  1 
ATOM   1123 C C   . SER A 1 142 ? 36.859  18.100  -6.670  1.00 22.70 ?  142 SER A C   1 
ATOM   1124 O O   . SER A 1 142 ? 37.037  18.105  -5.443  1.00 22.33 ?  142 SER A O   1 
ATOM   1125 C CB  . SER A 1 142 ? 39.278  17.537  -7.006  1.00 23.91 ?  142 SER A CB  1 
ATOM   1126 O OG  . SER A 1 142 ? 40.221  16.889  -7.837  1.00 27.45 ?  142 SER A OG  1 
ATOM   1127 N N   . LYS A 1 143 ? 35.778  18.646  -7.214  1.00 22.80 ?  143 LYS A N   1 
ATOM   1128 C CA  . LYS A 1 143 ? 34.760  19.213  -6.352  1.00 22.91 ?  143 LYS A CA  1 
ATOM   1129 C C   . LYS A 1 143 ? 33.389  18.991  -6.977  1.00 22.89 ?  143 LYS A C   1 
ATOM   1130 O O   . LYS A 1 143 ? 33.248  18.878  -8.199  1.00 23.26 ?  143 LYS A O   1 
ATOM   1131 C CB  . LYS A 1 143 ? 35.014  20.704  -6.080  1.00 28.85 ?  143 LYS A CB  1 
ATOM   1132 C CG  . LYS A 1 143 ? 34.931  21.598  -7.302  1.00 32.17 ?  143 LYS A CG  1 
ATOM   1133 C CD  . LYS A 1 143 ? 34.969  23.091  -6.919  1.00 37.80 ?  143 LYS A CD  1 
ATOM   1134 C CE  . LYS A 1 143 ? 33.810  23.488  -5.993  1.00 40.56 ?  143 LYS A CE  1 
ATOM   1135 N NZ  . LYS A 1 143 ? 32.492  23.666  -6.693  1.00 43.12 1  143 LYS A NZ  1 
ATOM   1136 N N   . TYR A 1 144 ? 32.383  18.917  -6.119  1.00 21.77 ?  144 TYR A N   1 
ATOM   1137 C CA  . TYR A 1 144 ? 31.013  18.698  -6.544  1.00 19.07 ?  144 TYR A CA  1 
ATOM   1138 C C   . TYR A 1 144 ? 30.239  20.007  -6.477  1.00 21.43 ?  144 TYR A C   1 
ATOM   1139 O O   . TYR A 1 144 ? 30.499  20.850  -5.615  1.00 23.41 ?  144 TYR A O   1 
ATOM   1140 C CB  . TYR A 1 144 ? 30.329  17.667  -5.646  1.00 18.83 ?  144 TYR A CB  1 
ATOM   1141 C CG  . TYR A 1 144 ? 30.767  16.228  -5.820  1.00 16.55 ?  144 TYR A CG  1 
ATOM   1142 C CD1 . TYR A 1 144 ? 30.191  15.405  -6.786  1.00 18.20 ?  144 TYR A CD1 1 
ATOM   1143 C CD2 . TYR A 1 144 ? 31.749  15.688  -5.003  1.00 16.19 ?  144 TYR A CD2 1 
ATOM   1144 C CE1 . TYR A 1 144 ? 30.580  14.077  -6.914  1.00 16.98 ?  144 TYR A CE1 1 
ATOM   1145 C CE2 . TYR A 1 144 ? 32.143  14.363  -5.131  1.00 15.11 ?  144 TYR A CE2 1 
ATOM   1146 C CZ  . TYR A 1 144 ? 31.563  13.573  -6.084  1.00 14.65 ?  144 TYR A CZ  1 
ATOM   1147 O OH  . TYR A 1 144 ? 31.962  12.263  -6.193  1.00 14.40 ?  144 TYR A OH  1 
ATOM   1148 N N   . SER A 1 145 ? 29.259  20.162  -7.368  1.00 22.26 ?  145 SER A N   1 
ATOM   1149 C CA  . SER A 1 145 ? 28.398  21.339  -7.345  1.00 20.77 ?  145 SER A CA  1 
ATOM   1150 C C   . SER A 1 145 ? 26.998  20.955  -7.811  1.00 19.94 ?  145 SER A C   1 
ATOM   1151 O O   . SER A 1 145 ? 26.770  19.863  -8.335  1.00 20.48 ?  145 SER A O   1 
ATOM   1152 C CB  . SER A 1 145 ? 28.970  22.463  -8.218  1.00 24.04 ?  145 SER A CB  1 
ATOM   1153 O OG  . SER A 1 145 ? 28.945  22.102  -9.581  1.00 23.31 ?  145 SER A OG  1 
ATOM   1154 N N   . VAL A 1 146 ? 26.058  21.880  -7.634  1.00 20.36 ?  146 VAL A N   1 
ATOM   1155 C CA  . VAL A 1 146 ? 24.641  21.644  -7.912  1.00 19.66 ?  146 VAL A CA  1 
ATOM   1156 C C   . VAL A 1 146 ? 24.270  22.283  -9.244  1.00 20.12 ?  146 VAL A C   1 
ATOM   1157 O O   . VAL A 1 146 ? 24.585  23.453  -9.493  1.00 18.40 ?  146 VAL A O   1 
ATOM   1158 C CB  . VAL A 1 146 ? 23.759  22.201  -6.781  1.00 20.11 ?  146 VAL A CB  1 
ATOM   1159 C CG1 . VAL A 1 146 ? 22.272  22.091  -7.146  1.00 18.60 ?  146 VAL A CG1 1 
ATOM   1160 C CG2 . VAL A 1 146 ? 24.061  21.478  -5.469  1.00 21.54 ?  146 VAL A CG2 1 
ATOM   1161 N N   . ASN A 1 147 ? 23.575  21.528  -10.089 1.00 21.40 ?  147 ASN A N   1 
ATOM   1162 C CA  . ASN A 1 147 ? 22.921  22.077  -11.273 1.00 20.96 ?  147 ASN A CA  1 
ATOM   1163 C C   . ASN A 1 147 ? 21.532  22.549  -10.836 1.00 19.70 ?  147 ASN A C   1 
ATOM   1164 O O   . ASN A 1 147 ? 20.594  21.754  -10.731 1.00 18.06 ?  147 ASN A O   1 
ATOM   1165 C CB  . ASN A 1 147 ? 22.873  21.032  -12.385 1.00 20.94 ?  147 ASN A CB  1 
ATOM   1166 C CG  . ASN A 1 147 ? 22.235  21.553  -13.664 1.00 20.89 ?  147 ASN A CG  1 
ATOM   1167 O OD1 . ASN A 1 147 ? 21.477  22.525  -13.658 1.00 20.72 ?  147 ASN A OD1 1 
ATOM   1168 N ND2 . ASN A 1 147 ? 22.530  20.888  -14.774 1.00 22.16 ?  147 ASN A ND2 1 
ATOM   1169 N N   . TRP A 1 148 ? 21.405  23.856  -10.573 1.00 18.81 ?  148 TRP A N   1 
ATOM   1170 C CA  . TRP A 1 148 ? 20.173  24.392  -9.997  1.00 20.97 ?  148 TRP A CA  1 
ATOM   1171 C C   . TRP A 1 148 ? 19.009  24.341  -10.976 1.00 19.81 ?  148 TRP A C   1 
ATOM   1172 O O   . TRP A 1 148 ? 17.859  24.151  -10.562 1.00 17.65 ?  148 TRP A O   1 
ATOM   1173 C CB  . TRP A 1 148 ? 20.410  25.825  -9.511  1.00 19.45 ?  148 TRP A CB  1 
ATOM   1174 C CG  . TRP A 1 148 ? 21.410  25.854  -8.419  1.00 20.79 ?  148 TRP A CG  1 
ATOM   1175 C CD1 . TRP A 1 148 ? 22.747  26.140  -8.528  1.00 21.21 ?  148 TRP A CD1 1 
ATOM   1176 C CD2 . TRP A 1 148 ? 21.179  25.522  -7.048  1.00 20.06 ?  148 TRP A CD2 1 
ATOM   1177 N NE1 . TRP A 1 148 ? 23.351  26.029  -7.299  1.00 21.64 ?  148 TRP A NE1 1 
ATOM   1178 C CE2 . TRP A 1 148 ? 22.412  25.646  -6.374  1.00 20.13 ?  148 TRP A CE2 1 
ATOM   1179 C CE3 . TRP A 1 148 ? 20.045  25.136  -6.322  1.00 21.09 ?  148 TRP A CE3 1 
ATOM   1180 C CZ2 . TRP A 1 148 ? 22.541  25.403  -5.007  1.00 20.75 ?  148 TRP A CZ2 1 
ATOM   1181 C CZ3 . TRP A 1 148 ? 20.174  24.893  -4.972  1.00 19.33 ?  148 TRP A CZ3 1 
ATOM   1182 C CH2 . TRP A 1 148 ? 21.410  25.029  -4.326  1.00 20.62 ?  148 TRP A CH2 1 
ATOM   1183 N N   . ALA A 1 149 ? 19.277  24.522  -12.269 1.00 19.81 ?  149 ALA A N   1 
ATOM   1184 C CA  . ALA A 1 149 ? 18.208  24.403  -13.253 1.00 21.67 ?  149 ALA A CA  1 
ATOM   1185 C C   . ALA A 1 149 ? 17.662  22.983  -13.279 1.00 18.71 ?  149 ALA A C   1 
ATOM   1186 O O   . ALA A 1 149 ? 16.443  22.775  -13.251 1.00 18.86 ?  149 ALA A O   1 
ATOM   1187 C CB  . ALA A 1 149 ? 18.710  24.820  -14.638 1.00 22.87 ?  149 ALA A CB  1 
ATOM   1188 N N   . ASP A 1 150 ? 18.555  21.996  -13.335 1.00 16.71 ?  150 ASP A N   1 
ATOM   1189 C CA  . ASP A 1 150 ? 18.139  20.599  -13.342 1.00 19.26 ?  150 ASP A CA  1 
ATOM   1190 C C   . ASP A 1 150 ? 17.390  20.252  -12.064 1.00 17.11 ?  150 ASP A C   1 
ATOM   1191 O O   . ASP A 1 150 ? 16.349  19.584  -12.102 1.00 16.76 ?  150 ASP A O   1 
ATOM   1192 C CB  . ASP A 1 150 ? 19.361  19.691  -13.514 1.00 19.17 ?  150 ASP A CB  1 
ATOM   1193 C CG  . ASP A 1 150 ? 18.992  18.200  -13.605 1.00 22.04 ?  150 ASP A CG  1 
ATOM   1194 O OD1 . ASP A 1 150 ? 18.381  17.791  -14.620 1.00 22.71 ?  150 ASP A OD1 1 
ATOM   1195 O OD2 . ASP A 1 150 ? 19.314  17.437  -12.658 1.00 19.21 -1 150 ASP A OD2 1 
ATOM   1196 N N   . LEU A 1 151 ? 17.916  20.691  -10.915 1.00 17.66 ?  151 LEU A N   1 
ATOM   1197 C CA  . LEU A 1 151 ? 17.267  20.406  -9.643  1.00 15.76 ?  151 LEU A CA  1 
ATOM   1198 C C   . LEU A 1 151 ? 15.846  20.951  -9.623  1.00 18.12 ?  151 LEU A C   1 
ATOM   1199 O O   . LEU A 1 151 ? 14.903  20.243  -9.244  1.00 14.97 ?  151 LEU A O   1 
ATOM   1200 C CB  . LEU A 1 151 ? 18.097  20.983  -8.498  1.00 15.95 ?  151 LEU A CB  1 
ATOM   1201 C CG  . LEU A 1 151 ? 17.517  20.859  -7.084  1.00 16.68 ?  151 LEU A CG  1 
ATOM   1202 C CD1 . LEU A 1 151 ? 17.200  19.400  -6.742  1.00 18.00 ?  151 LEU A CD1 1 
ATOM   1203 C CD2 . LEU A 1 151 ? 18.492  21.447  -6.084  1.00 19.35 ?  151 LEU A CD2 1 
ATOM   1204 N N   . GLU A 1 152 ? 15.663  22.204  -10.057 1.00 15.72 ?  152 GLU A N   1 
ATOM   1205 C CA  . GLU A 1 152 ? 14.330  22.800  -10.004 1.00 18.74 ?  152 GLU A CA  1 
ATOM   1206 C C   . GLU A 1 152 ? 13.376  22.116  -10.977 1.00 18.41 ?  152 GLU A C   1 
ATOM   1207 O O   . GLU A 1 152 ? 12.215  21.848  -10.637 1.00 17.73 ?  152 GLU A O   1 
ATOM   1208 C CB  . GLU A 1 152 ? 14.402  24.304  -10.288 1.00 19.14 ?  152 GLU A CB  1 
ATOM   1209 C CG  . GLU A 1 152 ? 13.013  24.921  -10.500 1.00 22.73 ?  152 GLU A CG  1 
ATOM   1210 C CD  . GLU A 1 152 ? 12.951  26.395  -10.173 1.00 25.97 ?  152 GLU A CD  1 
ATOM   1211 O OE1 . GLU A 1 152 ? 11.876  26.852  -9.724  1.00 26.52 ?  152 GLU A OE1 1 
ATOM   1212 O OE2 . GLU A 1 152 ? 13.971  27.096  -10.368 1.00 27.07 -1 152 GLU A OE2 1 
ATOM   1213 N N   . GLU A 1 153 ? 13.852  21.817  -12.189 1.00 19.43 ?  153 GLU A N   1 
ATOM   1214 C CA  . GLU A 1 153 ? 13.021  21.152  -13.185 1.00 19.63 ?  153 GLU A CA  1 
ATOM   1215 C C   . GLU A 1 153 ? 12.507  19.814  -12.663 1.00 17.78 ?  153 GLU A C   1 
ATOM   1216 O O   . GLU A 1 153 ? 11.342  19.451  -12.873 1.00 18.29 ?  153 GLU A O   1 
ATOM   1217 C CB  . GLU A 1 153 ? 13.831  20.976  -14.470 1.00 21.03 ?  153 GLU A CB  1 
ATOM   1218 C CG  . GLU A 1 153 ? 13.071  20.355  -15.615 1.00 25.30 ?  153 GLU A CG  1 
ATOM   1219 C CD  . GLU A 1 153 ? 13.971  20.051  -16.794 1.00 35.43 ?  153 GLU A CD  1 
ATOM   1220 O OE1 . GLU A 1 153 ? 13.761  19.009  -17.449 1.00 43.81 ?  153 GLU A OE1 1 
ATOM   1221 O OE2 . GLU A 1 153 ? 14.898  20.851  -17.055 1.00 36.58 -1 153 GLU A OE2 1 
ATOM   1222 N N   . LYS A 1 154 ? 13.349  19.087  -11.943 1.00 16.55 ?  154 LYS A N   1 
ATOM   1223 C CA  . LYS A 1 154 ? 12.922  17.810  -11.384 1.00 18.29 ?  154 LYS A CA  1 
ATOM   1224 C C   . LYS A 1 154 ? 11.980  18.003  -10.202 1.00 18.30 ?  154 LYS A C   1 
ATOM   1225 O O   . LYS A 1 154 ? 10.964  17.303  -10.102 1.00 17.74 ?  154 LYS A O   1 
ATOM   1226 C CB  . LYS A 1 154 ? 14.148  16.985  -11.007 1.00 16.89 ?  154 LYS A CB  1 
ATOM   1227 C CG  . LYS A 1 154 ? 14.781  16.349  -12.238 1.00 17.89 ?  154 LYS A CG  1 
ATOM   1228 C CD  . LYS A 1 154 ? 16.191  15.840  -12.001 1.00 17.14 ?  154 LYS A CD  1 
ATOM   1229 C CE  . LYS A 1 154 ? 16.764  15.256  -13.303 1.00 19.03 ?  154 LYS A CE  1 
ATOM   1230 N NZ  . LYS A 1 154 ? 18.206  14.942  -13.253 1.00 17.37 1  154 LYS A NZ  1 
ATOM   1231 N N   . LEU A 1 155 ? 12.272  18.961  -9.311  1.00 16.22 ?  155 LEU A N   1 
ATOM   1232 C CA  . LEU A 1 155 ? 11.366  19.224  -8.192  1.00 15.41 ?  155 LEU A CA  1 
ATOM   1233 C C   . LEU A 1 155 ? 9.990   19.651  -8.676  1.00 15.99 ?  155 LEU A C   1 
ATOM   1234 O O   . LEU A 1 155 ? 8.979   19.331  -8.038  1.00 16.87 ?  155 LEU A O   1 
ATOM   1235 C CB  . LEU A 1 155 ? 11.944  20.299  -7.275  1.00 16.94 ?  155 LEU A CB  1 
ATOM   1236 C CG  . LEU A 1 155 ? 13.146  19.892  -6.426  1.00 17.98 ?  155 LEU A CG  1 
ATOM   1237 C CD1 . LEU A 1 155 ? 13.714  21.111  -5.751  1.00 17.43 ?  155 LEU A CD1 1 
ATOM   1238 C CD2 . LEU A 1 155 ? 12.761  18.833  -5.403  1.00 19.20 ?  155 LEU A CD2 1 
ATOM   1239 N N   . ALA A 1 156 ? 9.929   20.350  -9.814  1.00 16.88 ?  156 ALA A N   1 
ATOM   1240 C CA  . ALA A 1 156 ? 8.671   20.832  -10.378 1.00 19.13 ?  156 ALA A CA  1 
ATOM   1241 C C   . ALA A 1 156 ? 7.855   19.734  -11.037 1.00 16.86 ?  156 ALA A C   1 
ATOM   1242 O O   . ALA A 1 156 ? 6.688   19.968  -11.379 1.00 18.48 ?  156 ALA A O   1 
ATOM   1243 C CB  . ALA A 1 156 ? 8.935   21.944  -11.402 1.00 17.56 ?  156 ALA A CB  1 
ATOM   1244 N N   . THR A 1 157 ? 8.428   18.559  -11.234 1.00 16.98 ?  157 THR A N   1 
ATOM   1245 C CA  . THR A 1 157 ? 7.673   17.454  -11.817 1.00 18.82 ?  157 THR A CA  1 
ATOM   1246 C C   . THR A 1 157 ? 6.569   16.997  -10.870 1.00 17.10 ?  157 THR A C   1 
ATOM   1247 O O   . THR A 1 157 ? 6.839   16.728  -9.697  1.00 15.87 ?  157 THR A O   1 
ATOM   1248 C CB  . THR A 1 157 ? 8.608   16.298  -12.137 1.00 21.05 ?  157 THR A CB  1 
ATOM   1249 O OG1 . THR A 1 157 ? 9.646   16.785  -13.000 1.00 22.21 ?  157 THR A OG1 1 
ATOM   1250 C CG2 . THR A 1 157 ? 7.843   15.173  -12.821 1.00 21.03 ?  157 THR A CG2 1 
ATOM   1251 N N   . PRO A 1 158 ? 5.320   16.896  -11.330 1.00 19.56 ?  158 PRO A N   1 
ATOM   1252 C CA  . PRO A 1 158 ? 4.237   16.580  -10.381 1.00 19.51 ?  158 PRO A CA  1 
ATOM   1253 C C   . PRO A 1 158 ? 4.471   15.301  -9.587  1.00 17.77 ?  158 PRO A C   1 
ATOM   1254 O O   . PRO A 1 158 ? 4.174   15.268  -8.390  1.00 18.32 ?  158 PRO A O   1 
ATOM   1255 C CB  . PRO A 1 158 ? 3.001   16.495  -11.290 1.00 18.72 ?  158 PRO A CB  1 
ATOM   1256 C CG  . PRO A 1 158 ? 3.327   17.419  -12.420 1.00 19.42 ?  158 PRO A CG  1 
ATOM   1257 C CD  . PRO A 1 158 ? 4.802   17.224  -12.669 1.00 19.53 ?  158 PRO A CD  1 
ATOM   1258 N N   . SER A 1 159 ? 5.030   14.258  -10.204 1.00 17.19 ?  159 SER A N   1 
ATOM   1259 C CA  . SER A 1 159 ? 5.248   12.996  -9.502  1.00 19.18 ?  159 SER A CA  1 
ATOM   1260 C C   . SER A 1 159 ? 6.410   13.052  -8.516  1.00 18.57 ?  159 SER A C   1 
ATOM   1261 O O   . SER A 1 159 ? 6.593   12.106  -7.744  1.00 17.91 ?  159 SER A O   1 
ATOM   1262 C CB  . SER A 1 159 ? 5.498   11.864  -10.501 1.00 21.41 ?  159 SER A CB  1 
ATOM   1263 O OG  . SER A 1 159 ? 6.586   12.180  -11.353 1.00 20.69 ?  159 SER A OG  1 
ATOM   1264 N N   . VAL A 1 160 ? 7.211   14.113  -8.528  1.00 16.20 ?  160 VAL A N   1 
ATOM   1265 C CA  . VAL A 1 160 ? 8.304   14.252  -7.573  1.00 16.33 ?  160 VAL A CA  1 
ATOM   1266 C C   . VAL A 1 160 ? 7.717   14.913  -6.332  1.00 17.63 ?  160 VAL A C   1 
ATOM   1267 O O   . VAL A 1 160 ? 7.363   16.096  -6.355  1.00 15.32 ?  160 VAL A O   1 
ATOM   1268 C CB  . VAL A 1 160 ? 9.475   15.052  -8.156  1.00 16.17 ?  160 VAL A CB  1 
ATOM   1269 C CG1 . VAL A 1 160 ? 10.546  15.231  -7.095  1.00 16.13 ?  160 VAL A CG1 1 
ATOM   1270 C CG2 . VAL A 1 160 ? 10.049  14.327  -9.360  1.00 15.39 ?  160 VAL A CG2 1 
ATOM   1271 N N   . ARG A 1 161 ? 7.584   14.136  -5.252  1.00 17.39 ?  161 ARG A N   1 
ATOM   1272 C CA  . ARG A 1 161 ? 6.796   14.550  -4.098  1.00 18.75 ?  161 ARG A CA  1 
ATOM   1273 C C   . ARG A 1 161 ? 7.616   14.824  -2.850  1.00 18.20 ?  161 ARG A C   1 
ATOM   1274 O O   . ARG A 1 161 ? 7.106   15.453  -1.917  1.00 17.88 ?  161 ARG A O   1 
ATOM   1275 C CB  . ARG A 1 161 ? 5.748   13.475  -3.763  1.00 21.01 ?  161 ARG A CB  1 
ATOM   1276 C CG  . ARG A 1 161 ? 4.840   13.076  -4.915  1.00 22.60 ?  161 ARG A CG  1 
ATOM   1277 C CD  . ARG A 1 161 ? 3.705   14.071  -5.166  1.00 22.98 ?  161 ARG A CD  1 
ATOM   1278 N NE  . ARG A 1 161 ? 3.158   14.711  -3.963  1.00 26.57 ?  161 ARG A NE  1 
ATOM   1279 C CZ  . ARG A 1 161 ? 2.532   14.098  -2.952  1.00 32.19 ?  161 ARG A CZ  1 
ATOM   1280 N NH1 . ARG A 1 161 ? 2.335   12.777  -2.942  1.00 29.49 1  161 ARG A NH1 1 
ATOM   1281 N NH2 . ARG A 1 161 ? 2.096   14.822  -1.928  1.00 31.11 ?  161 ARG A NH2 1 
ATOM   1282 N N   . MET A 1 162 ? 8.861   14.368  -2.807  1.00 16.04 ?  162 MET A N   1 
ATOM   1283 C CA  . MET A 1 162 ? 9.693   14.480  -1.623  1.00 15.40 ?  162 MET A CA  1 
ATOM   1284 C C   . MET A 1 162 ? 11.135  14.601  -2.080  1.00 15.34 ?  162 MET A C   1 
ATOM   1285 O O   . MET A 1 162 ? 11.519  14.032  -3.105  1.00 13.14 ?  162 MET A O   1 
ATOM   1286 C CB  . MET A 1 162 ? 9.514   13.257  -0.713  1.00 14.15 ?  162 MET A CB  1 
ATOM   1287 C CG  . MET A 1 162 ? 10.417  13.205  0.500   1.00 16.87 ?  162 MET A CG  1 
ATOM   1288 S SD  . MET A 1 162 ? 10.152  11.683  1.449   1.00 16.71 ?  162 MET A SD  1 
ATOM   1289 C CE  . MET A 1 162 ? 8.599   12.094  2.221   1.00 17.66 ?  162 MET A CE  1 
ATOM   1290 N N   . MET A 1 163 ? 11.928  15.340  -1.316  1.00 14.02 ?  163 MET A N   1 
ATOM   1291 C CA  . MET A 1 163 ? 13.370  15.389  -1.511  1.00 12.97 ?  163 MET A CA  1 
ATOM   1292 C C   . MET A 1 163 ? 14.061  14.945  -0.230  1.00 15.26 ?  163 MET A C   1 
ATOM   1293 O O   . MET A 1 163 ? 13.776  15.478  0.851   1.00 14.35 ?  163 MET A O   1 
ATOM   1294 C CB  . MET A 1 163 ? 13.837  16.792  -1.919  1.00 12.77 ?  163 MET A CB  1 
ATOM   1295 C CG  . MET A 1 163 ? 15.359  16.896  -2.114  1.00 13.33 ?  163 MET A CG  1 
ATOM   1296 S SD  . MET A 1 163 ? 15.884  18.541  -2.619  1.00 16.20 ?  163 MET A SD  1 
ATOM   1297 C CE  . MET A 1 163 ? 17.664  18.333  -2.568  1.00 12.31 ?  163 MET A CE  1 
ATOM   1298 N N   . VAL A 1 164 ? 14.952  13.964  -0.342  1.00 12.33 ?  164 VAL A N   1 
ATOM   1299 C CA  . VAL A 1 164 ? 15.754  13.526  0.793   1.00 13.00 ?  164 VAL A CA  1 
ATOM   1300 C C   . VAL A 1 164 ? 17.125  14.162  0.626   1.00 16.85 ?  164 VAL A C   1 
ATOM   1301 O O   . VAL A 1 164 ? 17.876  13.831  -0.297  1.00 15.75 ?  164 VAL A O   1 
ATOM   1302 C CB  . VAL A 1 164 ? 15.836  11.998  0.917   1.00 13.22 ?  164 VAL A CB  1 
ATOM   1303 C CG1 . VAL A 1 164 ? 16.554  11.619  2.222   1.00 14.90 ?  164 VAL A CG1 1 
ATOM   1304 C CG2 . VAL A 1 164 ? 14.427  11.390  0.888   1.00 17.84 ?  164 VAL A CG2 1 
ATOM   1305 N N   . PHE A 1 165 ? 17.418  15.083  1.531   1.00 13.72 ?  165 PHE A N   1 
ATOM   1306 C CA  . PHE A 1 165 ? 18.540  16.004  1.470   1.00 14.65 ?  165 PHE A CA  1 
ATOM   1307 C C   . PHE A 1 165 ? 19.504  15.608  2.574   1.00 15.83 ?  165 PHE A C   1 
ATOM   1308 O O   . PHE A 1 165 ? 19.107  15.499  3.738   1.00 15.91 ?  165 PHE A O   1 
ATOM   1309 C CB  . PHE A 1 165 ? 18.016  17.435  1.655   1.00 14.55 ?  165 PHE A CB  1 
ATOM   1310 C CG  . PHE A 1 165 ? 19.063  18.518  1.655   1.00 14.80 ?  165 PHE A CG  1 
ATOM   1311 C CD1 . PHE A 1 165 ? 20.046  18.593  0.672   1.00 18.16 ?  165 PHE A CD1 1 
ATOM   1312 C CD2 . PHE A 1 165 ? 19.003  19.527  2.607   1.00 16.26 ?  165 PHE A CD2 1 
ATOM   1313 C CE1 . PHE A 1 165 ? 20.984  19.640  0.681   1.00 14.51 ?  165 PHE A CE1 1 
ATOM   1314 C CE2 . PHE A 1 165 ? 19.933  20.568  2.621   1.00 15.98 ?  165 PHE A CE2 1 
ATOM   1315 C CZ  . PHE A 1 165 ? 20.923  20.622  1.663   1.00 13.55 ?  165 PHE A CZ  1 
ATOM   1316 N N   . CYS A 1 166 ? 20.758  15.357  2.202   1.00 14.25 ?  166 CYS A N   1 
ATOM   1317 C CA  . CYS A 1 166 ? 21.795  14.962  3.148   1.00 13.82 ?  166 CYS A CA  1 
ATOM   1318 C C   . CYS A 1 166 ? 22.585  16.208  3.538   1.00 15.23 ?  166 CYS A C   1 
ATOM   1319 O O   . CYS A 1 166 ? 23.285  16.787  2.693   1.00 16.04 ?  166 CYS A O   1 
ATOM   1320 C CB  . CYS A 1 166 ? 22.709  13.907  2.526   1.00 16.71 ?  166 CYS A CB  1 
ATOM   1321 S SG  . CYS A 1 166 ? 23.456  12.889  3.784   1.00 17.35 ?  166 CYS A SG  1 
ATOM   1322 N N   . ASN A 1 167 ? 22.506  16.606  4.802   1.00 15.49 ?  167 ASN A N   1 
ATOM   1323 C CA  . ASN A 1 167 ? 23.002  17.922  5.216   1.00 14.59 ?  167 ASN A CA  1 
ATOM   1324 C C   . ASN A 1 167 ? 23.658  17.847  6.595   1.00 14.28 ?  167 ASN A C   1 
ATOM   1325 O O   . ASN A 1 167 ? 22.959  17.957  7.612   1.00 14.21 ?  167 ASN A O   1 
ATOM   1326 C CB  . ASN A 1 167 ? 21.851  18.926  5.205   1.00 13.92 ?  167 ASN A CB  1 
ATOM   1327 C CG  . ASN A 1 167 ? 22.261  20.299  5.697   1.00 16.57 ?  167 ASN A CG  1 
ATOM   1328 O OD1 . ASN A 1 167 ? 23.374  20.738  5.462   1.00 16.02 ?  167 ASN A OD1 1 
ATOM   1329 N ND2 . ASN A 1 167 ? 21.353  20.985  6.380   1.00 16.49 ?  167 ASN A ND2 1 
ATOM   1330 N N   . PRO A 1 168 ? 24.998  17.701  6.679   1.00 12.32 ?  168 PRO A N   1 
ATOM   1331 C CA  . PRO A 1 168 ? 26.003  17.599  5.611   1.00 14.86 ?  168 PRO A CA  1 
ATOM   1332 C C   . PRO A 1 168 ? 25.864  16.336  4.766   1.00 14.77 ?  168 PRO A C   1 
ATOM   1333 O O   . PRO A 1 168 ? 25.343  15.307  5.218   1.00 13.85 ?  168 PRO A O   1 
ATOM   1334 C CB  . PRO A 1 168 ? 27.341  17.588  6.369   1.00 13.85 ?  168 PRO A CB  1 
ATOM   1335 C CG  . PRO A 1 168 ? 27.033  18.193  7.724   1.00 14.44 ?  168 PRO A CG  1 
ATOM   1336 C CD  . PRO A 1 168 ? 25.628  17.744  8.013   1.00 14.09 ?  168 PRO A CD  1 
ATOM   1337 N N   . HIS A 1 169 ? 26.365  16.437  3.539   1.00 13.84 ?  169 HIS A N   1 
ATOM   1338 C CA  . HIS A 1 169 ? 26.226  15.387  2.542   1.00 14.30 ?  169 HIS A CA  1 
ATOM   1339 C C   . HIS A 1 169 ? 27.272  14.290  2.732   1.00 15.01 ?  169 HIS A C   1 
ATOM   1340 O O   . HIS A 1 169 ? 28.480  14.553  2.702   1.00 17.74 ?  169 HIS A O   1 
ATOM   1341 C CB  . HIS A 1 169 ? 26.343  16.010  1.157   1.00 14.00 ?  169 HIS A CB  1 
ATOM   1342 C CG  . HIS A 1 169 ? 25.874  15.124  0.052   1.00 14.44 ?  169 HIS A CG  1 
ATOM   1343 N ND1 . HIS A 1 169 ? 24.616  15.233  -0.504  1.00 14.30 ?  169 HIS A ND1 1 
ATOM   1344 C CD2 . HIS A 1 169 ? 26.498  14.128  -0.622  1.00 12.85 ?  169 HIS A CD2 1 
ATOM   1345 C CE1 . HIS A 1 169 ? 24.486  14.342  -1.468  1.00 14.33 ?  169 HIS A CE1 1 
ATOM   1346 N NE2 . HIS A 1 169 ? 25.617  13.661  -1.562  1.00 13.28 ?  169 HIS A NE2 1 
ATOM   1347 N N   . ASN A 1 170 ? 26.763  13.062  2.803   1.00 14.07 ?  170 ASN A N   1 
ATOM   1348 C CA  . ASN A 1 170 ? 27.544  11.811  2.884   1.00 17.01 ?  170 ASN A CA  1 
ATOM   1349 C C   . ASN A 1 170 ? 27.274  11.106  1.543   1.00 15.73 ?  170 ASN A C   1 
ATOM   1350 O O   . ASN A 1 170 ? 26.137  10.971  1.181   1.00 14.14 ?  170 ASN A O   1 
ATOM   1351 C CB  . ASN A 1 170 ? 26.986  10.969  4.042   1.00 15.62 ?  170 ASN A CB  1 
ATOM   1352 C CG  . ASN A 1 170 ? 27.459  9.531   4.155   1.00 22.39 ?  170 ASN A CG  1 
ATOM   1353 O OD1 . ASN A 1 170 ? 28.562  9.185   3.766   1.00 25.80 ?  170 ASN A OD1 1 
ATOM   1354 N ND2 . ASN A 1 170 ? 26.643  8.679   4.744   1.00 21.85 ?  170 ASN A ND2 1 
ATOM   1355 N N   . PRO A 1 171 ? 28.308  10.711  0.772   1.00 15.56 ?  171 PRO A N   1 
ATOM   1356 C CA  . PRO A 1 171 ? 29.659  10.500  1.302   1.00 17.01 ?  171 PRO A CA  1 
ATOM   1357 C C   . PRO A 1 171 ? 30.736  11.558  1.035   1.00 16.29 ?  171 PRO A C   1 
ATOM   1358 O O   . PRO A 1 171 ? 31.843  11.349  1.425   1.00 17.63 ?  171 PRO A O   1 
ATOM   1359 C CB  . PRO A 1 171 ? 30.062  9.260   0.488   1.00 14.68 ?  171 PRO A CB  1 
ATOM   1360 C CG  . PRO A 1 171 ? 29.460  9.504   -0.871  1.00 14.99 ?  171 PRO A CG  1 
ATOM   1361 C CD  . PRO A 1 171 ? 28.184  10.271  -0.609  1.00 15.60 ?  171 PRO A CD  1 
ATOM   1362 N N   . ILE A 1 172 ? 30.349  12.653  0.406   1.00 14.74 ?  172 ILE A N   1 
ATOM   1363 C CA  . ILE A 1 172 ? 31.367  13.613  -0.021  1.00 15.59 ?  172 ILE A CA  1 
ATOM   1364 C C   . ILE A 1 172 ? 31.861  14.477  1.138   1.00 19.45 ?  172 ILE A C   1 
ATOM   1365 O O   . ILE A 1 172 ? 32.941  15.078  1.033   1.00 18.51 ?  172 ILE A O   1 
ATOM   1366 C CB  . ILE A 1 172 ? 30.862  14.482  -1.188  1.00 15.17 ?  172 ILE A CB  1 
ATOM   1367 C CG1 . ILE A 1 172 ? 29.852  15.532  -0.712  1.00 15.55 ?  172 ILE A CG1 1 
ATOM   1368 C CG2 . ILE A 1 172 ? 30.243  13.611  -2.286  1.00 15.80 ?  172 ILE A CG2 1 
ATOM   1369 C CD1 . ILE A 1 172 ? 29.199  16.317  -1.871  1.00 17.28 ?  172 ILE A CD1 1 
ATOM   1370 N N   . GLY A 1 173 ? 31.117  14.533  2.245   1.00 15.28 ?  173 GLY A N   1 
ATOM   1371 C CA  . GLY A 1 173 ? 31.540  15.248  3.438   1.00 16.58 ?  173 GLY A CA  1 
ATOM   1372 C C   . GLY A 1 173 ? 31.434  16.755  3.323   1.00 15.38 ?  173 GLY A C   1 
ATOM   1373 O O   . GLY A 1 173 ? 32.374  17.479  3.670   1.00 14.69 ?  173 GLY A O   1 
ATOM   1374 N N   . TYR A 1 174 ? 30.283  17.248  2.867   1.00 14.36 ?  174 TYR A N   1 
ATOM   1375 C CA  . TYR A 1 174 ? 30.103  18.664  2.558   1.00 15.66 ?  174 TYR A CA  1 
ATOM   1376 C C   . TYR A 1 174 ? 28.937  19.247  3.342   1.00 16.13 ?  174 TYR A C   1 
ATOM   1377 O O   . TYR A 1 174 ? 27.778  18.876  3.111   1.00 14.25 ?  174 TYR A O   1 
ATOM   1378 C CB  . TYR A 1 174 ? 29.866  18.876  1.063   1.00 16.91 ?  174 TYR A CB  1 
ATOM   1379 C CG  . TYR A 1 174 ? 29.615  20.331  0.745   1.00 16.31 ?  174 TYR A CG  1 
ATOM   1380 C CD1 . TYR A 1 174 ? 30.590  21.292  1.012   1.00 19.04 ?  174 TYR A CD1 1 
ATOM   1381 C CD2 . TYR A 1 174 ? 28.406  20.756  0.210   1.00 18.07 ?  174 TYR A CD2 1 
ATOM   1382 C CE1 . TYR A 1 174 ? 30.376  22.640  0.732   1.00 16.66 ?  174 TYR A CE1 1 
ATOM   1383 C CE2 . TYR A 1 174 ? 28.190  22.097  -0.084  1.00 17.51 ?  174 TYR A CE2 1 
ATOM   1384 C CZ  . TYR A 1 174 ? 29.172  23.035  0.188   1.00 16.99 ?  174 TYR A CZ  1 
ATOM   1385 O OH  . TYR A 1 174 ? 28.955  24.374  -0.082  1.00 18.74 ?  174 TYR A OH  1 
ATOM   1386 N N   . ALA A 1 175 ? 29.236  20.186  4.237   1.00 15.32 ?  175 ALA A N   1 
ATOM   1387 C CA  . ALA A 1 175 ? 28.194  20.938  4.924   1.00 14.86 ?  175 ALA A CA  1 
ATOM   1388 C C   . ALA A 1 175 ? 27.804  22.120  4.049   1.00 15.09 ?  175 ALA A C   1 
ATOM   1389 O O   . ALA A 1 175 ? 28.607  23.038  3.840   1.00 14.53 ?  175 ALA A O   1 
ATOM   1390 C CB  . ALA A 1 175 ? 28.665  21.396  6.302   1.00 16.30 ?  175 ALA A CB  1 
ATOM   1391 N N   . TRP A 1 176 ? 26.574  22.073  3.535   1.00 13.65 ?  176 TRP A N   1 
ATOM   1392 C CA  . TRP A 1 176 ? 26.015  23.100  2.664   1.00 14.25 ?  176 TRP A CA  1 
ATOM   1393 C C   . TRP A 1 176 ? 26.048  24.464  3.331   1.00 16.52 ?  176 TRP A C   1 
ATOM   1394 O O   . TRP A 1 176 ? 25.882  24.591  4.548   1.00 14.41 ?  176 TRP A O   1 
ATOM   1395 C CB  . TRP A 1 176 ? 24.561  22.756  2.299   1.00 13.66 ?  176 TRP A CB  1 
ATOM   1396 C CG  . TRP A 1 176 ? 24.419  21.396  1.716   1.00 14.67 ?  176 TRP A CG  1 
ATOM   1397 C CD1 . TRP A 1 176 ? 24.163  20.236  2.380   1.00 15.77 ?  176 TRP A CD1 1 
ATOM   1398 C CD2 . TRP A 1 176 ? 24.555  21.051  0.334   1.00 15.04 ?  176 TRP A CD2 1 
ATOM   1399 N NE1 . TRP A 1 176 ? 24.131  19.180  1.491   1.00 14.36 ?  176 TRP A NE1 1 
ATOM   1400 C CE2 . TRP A 1 176 ? 24.375  19.658  0.230   1.00 15.81 ?  176 TRP A CE2 1 
ATOM   1401 C CE3 . TRP A 1 176 ? 24.820  21.791  -0.828  1.00 18.62 ?  176 TRP A CE3 1 
ATOM   1402 C CZ2 . TRP A 1 176 ? 24.433  18.984  -0.988  1.00 17.87 ?  176 TRP A CZ2 1 
ATOM   1403 C CZ3 . TRP A 1 176 ? 24.887  21.115  -2.044  1.00 20.59 ?  176 TRP A CZ3 1 
ATOM   1404 C CH2 . TRP A 1 176 ? 24.695  19.721  -2.110  1.00 18.83 ?  176 TRP A CH2 1 
ATOM   1405 N N   . SER A 1 177 ? 26.250  25.492  2.515   1.00 16.21 ?  177 SER A N   1 
ATOM   1406 C CA  . SER A 1 177 ? 26.208  26.859  3.008   1.00 16.26 ?  177 SER A CA  1 
ATOM   1407 C C   . SER A 1 177 ? 24.780  27.264  3.355   1.00 16.99 ?  177 SER A C   1 
ATOM   1408 O O   . SER A 1 177 ? 23.810  26.621  2.947   1.00 16.51 ?  177 SER A O   1 
ATOM   1409 C CB  . SER A 1 177 ? 26.788  27.817  1.967   1.00 17.47 ?  177 SER A CB  1 
ATOM   1410 O OG  . SER A 1 177 ? 25.881  27.982  0.883   1.00 17.94 ?  177 SER A OG  1 
ATOM   1411 N N   . GLU A 1 178 ? 24.661  28.343  4.137   1.00 16.77 ?  178 GLU A N   1 
ATOM   1412 C CA  . GLU A 1 178 ? 23.341  28.859  4.485   1.00 18.85 ?  178 GLU A CA  1 
ATOM   1413 C C   . GLU A 1 178 ? 22.545  29.194  3.231   1.00 18.38 ?  178 GLU A C   1 
ATOM   1414 O O   . GLU A 1 178 ? 21.360  28.861  3.133   1.00 17.13 ?  178 GLU A O   1 
ATOM   1415 C CB  . GLU A 1 178 ? 23.475  30.090  5.390   1.00 19.65 ?  178 GLU A CB  1 
ATOM   1416 C CG  . GLU A 1 178 ? 22.154  30.857  5.575   1.00 23.01 ?  178 GLU A CG  1 
ATOM   1417 C CD  . GLU A 1 178 ? 22.287  32.088  6.466   1.00 30.69 ?  178 GLU A CD  1 
ATOM   1418 O OE1 . GLU A 1 178 ? 21.541  33.072  6.250   1.00 32.37 ?  178 GLU A OE1 1 
ATOM   1419 O OE2 . GLU A 1 178 ? 23.136  32.065  7.385   1.00 37.14 -1 178 GLU A OE2 1 
ATOM   1420 N N   . GLU A 1 179 ? 23.190  29.835  2.251   1.00 18.44 ?  179 GLU A N   1 
ATOM   1421 C CA  . GLU A 1 179 ? 22.511  30.178  1.000   1.00 20.56 ?  179 GLU A CA  1 
ATOM   1422 C C   . GLU A 1 179 ? 22.052  28.929  0.258   1.00 19.75 ?  179 GLU A C   1 
ATOM   1423 O O   . GLU A 1 179 ? 20.984  28.927  -0.367  1.00 18.64 ?  179 GLU A O   1 
ATOM   1424 C CB  . GLU A 1 179 ? 23.429  31.017  0.104   1.00 21.57 ?  179 GLU A CB  1 
ATOM   1425 C CG  . GLU A 1 179 ? 23.701  32.422  0.647   1.00 30.11 ?  179 GLU A CG  1 
ATOM   1426 C CD  . GLU A 1 179 ? 24.696  33.227  -0.194  1.00 40.90 ?  179 GLU A CD  1 
ATOM   1427 O OE1 . GLU A 1 179 ? 24.850  34.443  0.075   1.00 41.25 ?  179 GLU A OE1 1 
ATOM   1428 O OE2 . GLU A 1 179 ? 25.319  32.654  -1.122  1.00 44.53 -1 179 GLU A OE2 1 
ATOM   1429 N N   . GLU A 1 180 ? 22.846  27.856  0.315   1.00 17.23 ?  180 GLU A N   1 
ATOM   1430 C CA  . GLU A 1 180 ? 22.478  26.623  -0.375  1.00 16.78 ?  180 GLU A CA  1 
ATOM   1431 C C   . GLU A 1 180 ? 21.284  25.951  0.294   1.00 15.63 ?  180 GLU A C   1 
ATOM   1432 O O   . GLU A 1 180 ? 20.339  25.543  -0.386  1.00 16.34 ?  180 GLU A O   1 
ATOM   1433 C CB  . GLU A 1 180 ? 23.686  25.681  -0.451  1.00 17.59 ?  180 GLU A CB  1 
ATOM   1434 C CG  . GLU A 1 180 ? 24.627  26.073  -1.579  1.00 19.80 ?  180 GLU A CG  1 
ATOM   1435 C CD  . GLU A 1 180 ? 26.010  25.436  -1.474  1.00 20.91 ?  180 GLU A CD  1 
ATOM   1436 O OE1 . GLU A 1 180 ? 26.707  25.402  -2.504  1.00 23.87 ?  180 GLU A OE1 1 
ATOM   1437 O OE2 . GLU A 1 180 ? 26.400  24.967  -0.380  1.00 18.39 -1 180 GLU A OE2 1 
ATOM   1438 N N   . VAL A 1 181 ? 21.301  25.841  1.627   1.00 15.90 ?  181 VAL A N   1 
ATOM   1439 C CA  . VAL A 1 181 ? 20.189  25.200  2.326   1.00 14.78 ?  181 VAL A CA  1 
ATOM   1440 C C   . VAL A 1 181 ? 18.904  25.991  2.108   1.00 16.80 ?  181 VAL A C   1 
ATOM   1441 O O   . VAL A 1 181 ? 17.837  25.420  1.832   1.00 16.24 ?  181 VAL A O   1 
ATOM   1442 C CB  . VAL A 1 181 ? 20.513  25.047  3.825   1.00 16.08 ?  181 VAL A CB  1 
ATOM   1443 C CG1 . VAL A 1 181 ? 19.315  24.459  4.569   1.00 14.29 ?  181 VAL A CG1 1 
ATOM   1444 C CG2 . VAL A 1 181 ? 21.740  24.185  4.032   1.00 15.50 ?  181 VAL A CG2 1 
ATOM   1445 N N   . LYS A 1 182 ? 18.987  27.321  2.206   1.00 15.13 ?  182 LYS A N   1 
ATOM   1446 C CA  . LYS A 1 182 ? 17.807  28.159  2.014   1.00 16.93 ?  182 LYS A CA  1 
ATOM   1447 C C   . LYS A 1 182 ? 17.292  28.071  0.584   1.00 18.82 ?  182 LYS A C   1 
ATOM   1448 O O   . LYS A 1 182 ? 16.074  28.055  0.352   1.00 17.26 ?  182 LYS A O   1 
ATOM   1449 C CB  . LYS A 1 182 ? 18.141  29.601  2.379   1.00 15.47 ?  182 LYS A CB  1 
ATOM   1450 C CG  . LYS A 1 182 ? 18.304  29.810  3.888   1.00 18.35 ?  182 LYS A CG  1 
ATOM   1451 C CD  . LYS A 1 182 ? 18.518  31.281  4.214   1.00 24.66 ?  182 LYS A CD  1 
ATOM   1452 C CE  . LYS A 1 182 ? 18.212  31.562  5.682   1.00 29.35 ?  182 LYS A CE  1 
ATOM   1453 N NZ  . LYS A 1 182 ? 18.955  32.766  6.150   1.00 35.93 1  182 LYS A NZ  1 
ATOM   1454 N N   . ARG A 1 183 ? 18.207  27.987  -0.384  1.00 15.61 ?  183 ARG A N   1 
ATOM   1455 C CA  . ARG A 1 183 ? 17.796  27.895  -1.776  1.00 19.27 ?  183 ARG A CA  1 
ATOM   1456 C C   . ARG A 1 183 ? 17.069  26.583  -2.045  1.00 18.08 ?  183 ARG A C   1 
ATOM   1457 O O   . ARG A 1 183 ? 16.039  26.565  -2.734  1.00 16.72 ?  183 ARG A O   1 
ATOM   1458 C CB  . ARG A 1 183 ? 19.014  28.040  -2.683  1.00 19.82 ?  183 ARG A CB  1 
ATOM   1459 C CG  . ARG A 1 183 ? 18.672  28.099  -4.145  1.00 19.44 ?  183 ARG A CG  1 
ATOM   1460 C CD  . ARG A 1 183 ? 19.884  28.473  -4.998  1.00 23.35 ?  183 ARG A CD  1 
ATOM   1461 N NE  . ARG A 1 183 ? 19.481  28.717  -6.378  1.00 23.07 ?  183 ARG A NE  1 
ATOM   1462 C CZ  . ARG A 1 183 ? 20.317  29.079  -7.346  1.00 26.35 ?  183 ARG A CZ  1 
ATOM   1463 N NH1 . ARG A 1 183 ? 21.607  29.246  -7.080  1.00 22.85 1  183 ARG A NH1 1 
ATOM   1464 N NH2 . ARG A 1 183 ? 19.865  29.271  -8.580  1.00 27.12 ?  183 ARG A NH2 1 
ATOM   1465 N N   . ILE A 1 184 ? 17.590  25.476  -1.512  1.00 15.90 ?  184 ILE A N   1 
ATOM   1466 C CA  . ILE A 1 184 ? 16.955  24.178  -1.719  1.00 16.25 ?  184 ILE A CA  1 
ATOM   1467 C C   . ILE A 1 184 ? 15.596  24.137  -1.037  1.00 16.58 ?  184 ILE A C   1 
ATOM   1468 O O   . ILE A 1 184 ? 14.607  23.685  -1.630  1.00 17.40 ?  184 ILE A O   1 
ATOM   1469 C CB  . ILE A 1 184 ? 17.883  23.052  -1.233  1.00 16.13 ?  184 ILE A CB  1 
ATOM   1470 C CG1 . ILE A 1 184 ? 19.058  22.900  -2.206  1.00 16.70 ?  184 ILE A CG1 1 
ATOM   1471 C CG2 . ILE A 1 184 ? 17.123  21.745  -1.105  1.00 16.85 ?  184 ILE A CG2 1 
ATOM   1472 C CD1 . ILE A 1 184 ? 20.204  22.093  -1.659  1.00 17.69 ?  184 ILE A CD1 1 
ATOM   1473 N N   . ALA A 1 185 ? 15.513  24.650  0.196   1.00 15.73 ?  185 ALA A N   1 
ATOM   1474 C CA  . ALA A 1 185 ? 14.231  24.698  0.898   1.00 17.50 ?  185 ALA A CA  1 
ATOM   1475 C C   . ALA A 1 185 ? 13.204  25.539  0.143   1.00 19.03 ?  185 ALA A C   1 
ATOM   1476 O O   . ALA A 1 185 ? 12.032  25.158  0.051   1.00 19.23 ?  185 ALA A O   1 
ATOM   1477 C CB  . ALA A 1 185 ? 14.414  25.241  2.317   1.00 17.74 ?  185 ALA A CB  1 
ATOM   1478 N N   . GLU A 1 186 ? 13.611  26.692  -0.393  1.00 18.79 ?  186 GLU A N   1 
ATOM   1479 C CA  . GLU A 1 186 ? 12.638  27.521  -1.099  1.00 20.49 ?  186 GLU A CA  1 
ATOM   1480 C C   . GLU A 1 186 ? 12.190  26.857  -2.394  1.00 19.29 ?  186 GLU A C   1 
ATOM   1481 O O   . GLU A 1 186 ? 11.014  26.947  -2.763  1.00 17.96 ?  186 GLU A O   1 
ATOM   1482 C CB  . GLU A 1 186 ? 13.197  28.916  -1.385  1.00 21.36 ?  186 GLU A CB  1 
ATOM   1483 C CG  . GLU A 1 186 ? 12.180  29.833  -2.122  1.00 28.40 ?  186 GLU A CG  1 
ATOM   1484 C CD  . GLU A 1 186 ? 10.768  29.846  -1.470  1.00 35.13 ?  186 GLU A CD  1 
ATOM   1485 O OE1 . GLU A 1 186 ? 9.792   29.309  -2.066  1.00 28.70 ?  186 GLU A OE1 1 
ATOM   1486 O OE2 . GLU A 1 186 ? 10.633  30.403  -0.351  1.00 37.66 -1 186 GLU A OE2 1 
ATOM   1487 N N   . LEU A 1 187 ? 13.106  26.180  -3.095  1.00 18.18 ?  187 LEU A N   1 
ATOM   1488 C CA  . LEU A 1 187 ? 12.716  25.417  -4.276  1.00 18.77 ?  187 LEU A CA  1 
ATOM   1489 C C   . LEU A 1 187 ? 11.683  24.361  -3.912  1.00 17.46 ?  187 LEU A C   1 
ATOM   1490 O O   . LEU A 1 187 ? 10.652  24.219  -4.583  1.00 18.35 ?  187 LEU A O   1 
ATOM   1491 C CB  . LEU A 1 187 ? 13.946  24.769  -4.910  1.00 18.78 ?  187 LEU A CB  1 
ATOM   1492 C CG  . LEU A 1 187 ? 14.760  25.717  -5.789  1.00 20.21 ?  187 LEU A CG  1 
ATOM   1493 C CD1 . LEU A 1 187 ? 15.908  24.968  -6.447  1.00 18.52 ?  187 LEU A CD1 1 
ATOM   1494 C CD2 . LEU A 1 187 ? 13.885  26.397  -6.839  1.00 20.91 ?  187 LEU A CD2 1 
ATOM   1495 N N   . CYS A 1 188 ? 11.924  23.645  -2.812  1.00 16.63 ?  188 CYS A N   1 
ATOM   1496 C CA  . CYS A 1 188 ? 10.999  22.609  -2.374  1.00 17.69 ?  188 CYS A CA  1 
ATOM   1497 C C   . CYS A 1 188 ? 9.639   23.205  -2.044  1.00 15.46 ?  188 CYS A C   1 
ATOM   1498 O O   . CYS A 1 188 ? 8.605   22.716  -2.513  1.00 16.58 ?  188 CYS A O   1 
ATOM   1499 C CB  . CYS A 1 188 ? 11.595  21.881  -1.168  1.00 18.15 ?  188 CYS A CB  1 
ATOM   1500 S SG  . CYS A 1 188 ? 12.794  20.661  -1.705  1.00 14.96 ?  188 CYS A SG  1 
ATOM   1501 N N   . ALA A 1 189 ? 9.618   24.277  -1.246  1.00 17.64 ?  189 ALA A N   1 
ATOM   1502 C CA  . ALA A 1 189 ? 8.350   24.896  -0.863  1.00 18.65 ?  189 ALA A CA  1 
ATOM   1503 C C   . ALA A 1 189 ? 7.603   25.428  -2.081  1.00 18.35 ?  189 ALA A C   1 
ATOM   1504 O O   . ALA A 1 189 ? 6.386   25.255  -2.202  1.00 16.34 ?  189 ALA A O   1 
ATOM   1505 C CB  . ALA A 1 189 ? 8.601   26.019  0.139   1.00 19.98 ?  189 ALA A CB  1 
ATOM   1506 N N   . LYS A 1 190 ? 8.325   26.101  -2.983  1.00 20.14 ?  190 LYS A N   1 
ATOM   1507 C CA  . LYS A 1 190 ? 7.738   26.637  -4.207  1.00 21.56 ?  190 LYS A CA  1 
ATOM   1508 C C   . LYS A 1 190 ? 6.995   25.571  -4.999  1.00 19.54 ?  190 LYS A C   1 
ATOM   1509 O O   . LYS A 1 190 ? 5.982   25.861  -5.640  1.00 20.10 ?  190 LYS A O   1 
ATOM   1510 C CB  . LYS A 1 190 ? 8.844   27.263  -5.065  1.00 19.93 ?  190 LYS A CB  1 
ATOM   1511 C CG  . LYS A 1 190 ? 8.436   27.660  -6.474  1.00 22.18 ?  190 LYS A CG  1 
ATOM   1512 C CD  . LYS A 1 190 ? 9.637   28.203  -7.254  1.00 24.52 ?  190 LYS A CD  1 
ATOM   1513 C CE  . LYS A 1 190 ? 9.235   28.681  -8.646  1.00 28.25 ?  190 LYS A CE  1 
ATOM   1514 N NZ  . LYS A 1 190 ? 10.384  29.256  -9.405  1.00 32.24 1  190 LYS A NZ  1 
ATOM   1515 N N   . HIS A 1 191 ? 7.469   24.330  -4.960  1.00 19.14 ?  191 HIS A N   1 
ATOM   1516 C CA  . HIS A 1 191 ? 6.899   23.273  -5.781  1.00 20.37 ?  191 HIS A CA  1 
ATOM   1517 C C   . HIS A 1 191 ? 6.164   22.239  -4.943  1.00 19.16 ?  191 HIS A C   1 
ATOM   1518 O O   . HIS A 1 191 ? 5.851   21.148  -5.431  1.00 19.93 ?  191 HIS A O   1 
ATOM   1519 C CB  . HIS A 1 191 ? 8.004   22.651  -6.636  1.00 17.71 ?  191 HIS A CB  1 
ATOM   1520 C CG  . HIS A 1 191 ? 8.570   23.610  -7.636  1.00 19.77 ?  191 HIS A CG  1 
ATOM   1521 N ND1 . HIS A 1 191 ? 7.847   24.068  -8.720  1.00 21.26 ?  191 HIS A ND1 1 
ATOM   1522 C CD2 . HIS A 1 191 ? 9.770   24.237  -7.693  1.00 21.39 ?  191 HIS A CD2 1 
ATOM   1523 C CE1 . HIS A 1 191 ? 8.588   24.916  -9.412  1.00 23.47 ?  191 HIS A CE1 1 
ATOM   1524 N NE2 . HIS A 1 191 ? 9.758   25.037  -8.810  1.00 21.60 ?  191 HIS A NE2 1 
ATOM   1525 N N   . GLN A 1 192 ? 5.869   22.579  -3.691  1.00 18.87 ?  192 GLN A N   1 
ATOM   1526 C CA  . GLN A 1 192 ? 5.109   21.723  -2.788  1.00 19.05 ?  192 GLN A CA  1 
ATOM   1527 C C   . GLN A 1 192 ? 5.741   20.338  -2.697  1.00 19.67 ?  192 GLN A C   1 
ATOM   1528 O O   . GLN A 1 192 ? 5.079   19.308  -2.801  1.00 19.57 ?  192 GLN A O   1 
ATOM   1529 C CB  . GLN A 1 192 ? 3.641   21.656  -3.210  1.00 18.91 ?  192 GLN A CB  1 
ATOM   1530 C CG  . GLN A 1 192 ? 3.067   23.018  -3.539  1.00 22.36 ?  192 GLN A CG  1 
ATOM   1531 C CD  . GLN A 1 192 ? 1.700   22.927  -4.185  1.00 32.99 ?  192 GLN A CD  1 
ATOM   1532 O OE1 . GLN A 1 192 ? 1.512   22.221  -5.180  1.00 39.79 ?  192 GLN A OE1 1 
ATOM   1533 N NE2 . GLN A 1 192 ? 0.734   23.645  -3.624  1.00 34.54 ?  192 GLN A NE2 1 
ATOM   1534 N N   . VAL A 1 193 ? 7.055   20.333  -2.502  1.00 16.63 ?  193 VAL A N   1 
ATOM   1535 C CA  . VAL A 1 193 ? 7.825   19.123  -2.267  1.00 16.81 ?  193 VAL A CA  1 
ATOM   1536 C C   . VAL A 1 193 ? 8.277   19.144  -0.816  1.00 17.43 ?  193 VAL A C   1 
ATOM   1537 O O   . VAL A 1 193 ? 8.842   20.140  -0.354  1.00 15.21 ?  193 VAL A O   1 
ATOM   1538 C CB  . VAL A 1 193 ? 9.038   19.040  -3.214  1.00 15.76 ?  193 VAL A CB  1 
ATOM   1539 C CG1 . VAL A 1 193 ? 9.951   17.868  -2.831  1.00 16.42 ?  193 VAL A CG1 1 
ATOM   1540 C CG2 . VAL A 1 193 ? 8.586   18.957  -4.660  1.00 17.00 ?  193 VAL A CG2 1 
ATOM   1541 N N   . LEU A 1 194 ? 8.049   18.058  -0.095  1.00 17.71 ?  194 LEU A N   1 
ATOM   1542 C CA  . LEU A 1 194 ? 8.542   17.961  1.293   1.00 15.75 ?  194 LEU A CA  1 
ATOM   1543 C C   . LEU A 1 194 ? 10.056  17.732  1.320   1.00 15.23 ?  194 LEU A C   1 
ATOM   1544 O O   . LEU A 1 194 ? 10.532  16.800  0.705   1.00 15.26 ?  194 LEU A O   1 
ATOM   1545 C CB  . LEU A 1 194 ? 7.793   16.835  1.989   1.00 15.97 ?  194 LEU A CB  1 
ATOM   1546 C CG  . LEU A 1 194 ? 8.208   16.541  3.422   1.00 20.94 ?  194 LEU A CG  1 
ATOM   1547 C CD1 . LEU A 1 194 ? 8.106   17.783  4.273   1.00 22.42 ?  194 LEU A CD1 1 
ATOM   1548 C CD2 . LEU A 1 194 ? 7.325   15.456  3.990   1.00 19.67 ?  194 LEU A CD2 1 
ATOM   1549 N N   . LEU A 1 195 ? 10.742  18.583  2.039   1.00 14.32 ?  195 LEU A N   1 
ATOM   1550 C CA  . LEU A 1 195 ? 12.193  18.474  2.193   1.00 13.88 ?  195 LEU A CA  1 
ATOM   1551 C C   . LEU A 1 195 ? 12.521  17.707  3.470   1.00 14.48 ?  195 LEU A C   1 
ATOM   1552 O O   . LEU A 1 195 ? 12.225  18.178  4.573   1.00 14.40 ?  195 LEU A O   1 
ATOM   1553 C CB  . LEU A 1 195 ? 12.839  19.860  2.217   1.00 14.24 ?  195 LEU A CB  1 
ATOM   1554 C CG  . LEU A 1 195 ? 14.349  19.876  2.458   1.00 15.20 ?  195 LEU A CG  1 
ATOM   1555 C CD1 . LEU A 1 195 ? 15.012  19.161  1.291   1.00 15.20 ?  195 LEU A CD1 1 
ATOM   1556 C CD2 . LEU A 1 195 ? 14.886  21.302  2.613   1.00 16.01 ?  195 LEU A CD2 1 
ATOM   1557 N N   . ILE A 1 196 ? 13.110  16.525  3.325   1.00 13.34 ?  196 ILE A N   1 
ATOM   1558 C CA  . ILE A 1 196 ? 13.581  15.745  4.467   1.00 12.84 ?  196 ILE A CA  1 
ATOM   1559 C C   . ILE A 1 196 ? 15.080  15.985  4.578   1.00 16.03 ?  196 ILE A C   1 
ATOM   1560 O O   . ILE A 1 196 ? 15.849  15.528  3.725   1.00 14.86 ?  196 ILE A O   1 
ATOM   1561 C CB  . ILE A 1 196 ? 13.267  14.249  4.326   1.00 14.08 ?  196 ILE A CB  1 
ATOM   1562 C CG1 . ILE A 1 196 ? 11.788  14.027  4.011   1.00 17.32 ?  196 ILE A CG1 1 
ATOM   1563 C CG2 . ILE A 1 196 ? 13.636  13.506  5.603   1.00 16.42 ?  196 ILE A CG2 1 
ATOM   1564 C CD1 . ILE A 1 196 ? 10.838  14.620  5.057   1.00 16.38 ?  196 ILE A CD1 1 
ATOM   1565 N N   . SER A 1 197 ? 15.509  16.685  5.627   1.00 12.93 ?  197 SER A N   1 
ATOM   1566 C CA  . SER A 1 197 ? 16.908  17.079  5.760   1.00 13.31 ?  197 SER A CA  1 
ATOM   1567 C C   . SER A 1 197 ? 17.552  16.174  6.808   1.00 14.13 ?  197 SER A C   1 
ATOM   1568 O O   . SER A 1 197 ? 17.264  16.279  8.005   1.00 15.36 ?  197 SER A O   1 
ATOM   1569 C CB  . SER A 1 197 ? 17.021  18.559  6.123   1.00 13.81 ?  197 SER A CB  1 
ATOM   1570 O OG  . SER A 1 197 ? 18.363  18.935  6.415   1.00 16.16 ?  197 SER A OG  1 
ATOM   1571 N N   . ASP A 1 198 ? 18.389  15.259  6.342   1.00 13.08 ?  198 ASP A N   1 
ATOM   1572 C CA  . ASP A 1 198 ? 19.089  14.311  7.197   1.00 14.89 ?  198 ASP A CA  1 
ATOM   1573 C C   . ASP A 1 198 ? 20.364  14.993  7.679   1.00 14.56 ?  198 ASP A C   1 
ATOM   1574 O O   . ASP A 1 198 ? 21.316  15.165  6.914   1.00 14.21 ?  198 ASP A O   1 
ATOM   1575 C CB  . ASP A 1 198 ? 19.368  13.029  6.415   1.00 14.91 ?  198 ASP A CB  1 
ATOM   1576 C CG  . ASP A 1 198 ? 20.196  12.009  7.184   1.00 17.75 ?  198 ASP A CG  1 
ATOM   1577 O OD1 . ASP A 1 198 ? 20.759  12.287  8.279   1.00 15.68 ?  198 ASP A OD1 1 
ATOM   1578 O OD2 . ASP A 1 198 ? 20.302  10.882  6.653   1.00 20.72 -1 198 ASP A OD2 1 
ATOM   1579 N N   . GLU A 1 199 ? 20.377  15.383  8.951   1.00 14.78 ?  199 GLU A N   1 
ATOM   1580 C CA  . GLU A 1 199 ? 21.463  16.206  9.517   1.00 15.39 ?  199 GLU A CA  1 
ATOM   1581 C C   . GLU A 1 199 ? 22.258  15.402  10.526  1.00 14.59 ?  199 GLU A C   1 
ATOM   1582 O O   . GLU A 1 199 ? 22.772  15.970  11.466  1.00 14.65 ?  199 GLU A O   1 
ATOM   1583 C CB  . GLU A 1 199 ? 20.779  17.410  10.158  1.00 13.19 ?  199 GLU A CB  1 
ATOM   1584 C CG  . GLU A 1 199 ? 19.988  18.201  9.143   1.00 15.13 ?  199 GLU A CG  1 
ATOM   1585 C CD  . GLU A 1 199 ? 19.216  19.399  9.651   1.00 19.38 ?  199 GLU A CD  1 
ATOM   1586 O OE1 . GLU A 1 199 ? 18.547  20.031  8.833   1.00 19.18 ?  199 GLU A OE1 1 
ATOM   1587 O OE2 . GLU A 1 199 ? 19.277  19.681  10.847  1.00 20.40 -1 199 GLU A OE2 1 
ATOM   1588 N N   . ILE A 1 200 ? 22.387  14.113  10.264  1.00 12.64 ?  200 ILE A N   1 
ATOM   1589 C CA  . ILE A 1 200 ? 23.022  13.260  11.251  1.00 14.49 ?  200 ILE A CA  1 
ATOM   1590 C C   . ILE A 1 200 ? 24.520  13.520  11.344  1.00 14.49 ?  200 ILE A C   1 
ATOM   1591 O O   . ILE A 1 200 ? 25.130  13.185  12.364  1.00 13.68 ?  200 ILE A O   1 
ATOM   1592 C CB  . ILE A 1 200 ? 22.712  11.781  10.941  1.00 16.36 ?  200 ILE A CB  1 
ATOM   1593 C CG1 . ILE A 1 200 ? 22.877  10.936  12.214  1.00 19.17 ?  200 ILE A CG1 1 
ATOM   1594 C CG2 . ILE A 1 200 ? 23.596  11.288  9.808   1.00 18.55 ?  200 ILE A CG2 1 
ATOM   1595 C CD1 . ILE A 1 200 ? 22.558  9.489   12.051  1.00 21.48 ?  200 ILE A CD1 1 
ATOM   1596 N N   . HIS A 1 201 ? 25.137  14.100  10.307  1.00 12.06 ?  201 HIS A N   1 
ATOM   1597 C CA  . HIS A 1 201 ? 26.543  14.486  10.350  1.00 14.71 ?  201 HIS A CA  1 
ATOM   1598 C C   . HIS A 1 201 ? 26.752  15.935  10.785  1.00 16.07 ?  201 HIS A C   1 
ATOM   1599 O O   . HIS A 1 201 ? 27.885  16.433  10.728  1.00 14.27 ?  201 HIS A O   1 
ATOM   1600 C CB  . HIS A 1 201 ? 27.186  14.248  8.979   1.00 14.02 ?  201 HIS A CB  1 
ATOM   1601 C CG  . HIS A 1 201 ? 27.244  12.802  8.605   1.00 14.96 ?  201 HIS A CG  1 
ATOM   1602 N ND1 . HIS A 1 201 ? 28.248  11.963  9.039   1.00 16.93 ?  201 HIS A ND1 1 
ATOM   1603 C CD2 . HIS A 1 201 ? 26.410  12.042  7.858   1.00 15.73 ?  201 HIS A CD2 1 
ATOM   1604 C CE1 . HIS A 1 201 ? 28.027  10.744  8.578   1.00 17.97 ?  201 HIS A CE1 1 
ATOM   1605 N NE2 . HIS A 1 201 ? 26.916  10.764  7.861   1.00 16.62 ?  201 HIS A NE2 1 
ATOM   1606 N N   . GLY A 1 202 ? 25.698  16.600  11.268  1.00 13.61 ?  202 GLY A N   1 
ATOM   1607 C CA  . GLY A 1 202 ? 25.729  18.046  11.458  1.00 14.50 ?  202 GLY A CA  1 
ATOM   1608 C C   . GLY A 1 202 ? 26.626  18.518  12.581  1.00 16.38 ?  202 GLY A C   1 
ATOM   1609 O O   . GLY A 1 202 ? 27.036  19.690  12.579  1.00 15.09 ?  202 GLY A O   1 
ATOM   1610 N N   . ASP A 1 203 ? 26.943  17.642  13.533  1.00 13.52 ?  203 ASP A N   1 
ATOM   1611 C CA  . ASP A 1 203 ? 27.864  17.968  14.617  1.00 13.44 ?  203 ASP A CA  1 
ATOM   1612 C C   . ASP A 1 203 ? 29.313  17.713  14.256  1.00 15.31 ?  203 ASP A C   1 
ATOM   1613 O O   . ASP A 1 203 ? 30.188  17.869  15.117  1.00 15.04 ?  203 ASP A O   1 
ATOM   1614 C CB  . ASP A 1 203 ? 27.548  17.154  15.874  1.00 15.02 ?  203 ASP A CB  1 
ATOM   1615 C CG  . ASP A 1 203 ? 26.107  17.296  16.338  1.00 14.95 ?  203 ASP A CG  1 
ATOM   1616 O OD1 . ASP A 1 203 ? 25.541  18.404  16.257  1.00 15.96 ?  203 ASP A OD1 1 
ATOM   1617 O OD2 . ASP A 1 203 ? 25.549  16.290  16.827  1.00 17.63 -1 203 ASP A OD2 1 
ATOM   1618 N N   . LEU A 1 204 ? 29.592  17.277  13.040  1.00 13.90 ?  204 LEU A N   1 
ATOM   1619 C CA  . LEU A 1 204 ? 30.937  16.860  12.685  1.00 14.34 ?  204 LEU A CA  1 
ATOM   1620 C C   . LEU A 1 204 ? 31.517  17.731  11.572  1.00 15.87 ?  204 LEU A C   1 
ATOM   1621 O O   . LEU A 1 204 ? 32.281  17.254  10.734  1.00 14.94 ?  204 LEU A O   1 
ATOM   1622 C CB  . LEU A 1 204 ? 30.946  15.379  12.311  1.00 13.27 ?  204 LEU A CB  1 
ATOM   1623 C CG  . LEU A 1 204 ? 30.668  14.430  13.491  1.00 12.43 ?  204 LEU A CG  1 
ATOM   1624 C CD1 . LEU A 1 204 ? 30.258  13.037  13.024  1.00 16.83 ?  204 LEU A CD1 1 
ATOM   1625 C CD2 . LEU A 1 204 ? 31.857  14.350  14.472  1.00 12.38 ?  204 LEU A CD2 1 
ATOM   1626 N N   . VAL A 1 205 ? 31.159  19.012  11.546  1.00 16.18 ?  205 VAL A N   1 
ATOM   1627 C CA  . VAL A 1 205 ? 31.836  19.958  10.662  1.00 16.97 ?  205 VAL A CA  1 
ATOM   1628 C C   . VAL A 1 205 ? 33.204  20.249  11.265  1.00 19.73 ?  205 VAL A C   1 
ATOM   1629 O O   . VAL A 1 205 ? 33.301  20.644  12.431  1.00 19.61 ?  205 VAL A O   1 
ATOM   1630 C CB  . VAL A 1 205 ? 31.030  21.249  10.488  1.00 19.70 ?  205 VAL A CB  1 
ATOM   1631 C CG1 . VAL A 1 205 ? 31.798  22.202  9.580   1.00 20.83 ?  205 VAL A CG1 1 
ATOM   1632 C CG2 . VAL A 1 205 ? 29.645  20.944  9.939   1.00 16.78 ?  205 VAL A CG2 1 
ATOM   1633 N N   . LEU A 1 206 ? 34.260  20.044  10.480  1.00 14.70 ?  206 LEU A N   1 
ATOM   1634 C CA  . LEU A 1 206 ? 35.618  20.109  11.009  1.00 15.47 ?  206 LEU A CA  1 
ATOM   1635 C C   . LEU A 1 206 ? 36.313  21.440  10.765  1.00 18.23 ?  206 LEU A C   1 
ATOM   1636 O O   . LEU A 1 206 ? 37.309  21.722  11.438  1.00 19.35 ?  206 LEU A O   1 
ATOM   1637 C CB  . LEU A 1 206 ? 36.461  18.985  10.413  1.00 17.15 ?  206 LEU A CB  1 
ATOM   1638 C CG  . LEU A 1 206 ? 35.979  17.568  10.729  1.00 17.01 ?  206 LEU A CG  1 
ATOM   1639 C CD1 . LEU A 1 206 ? 36.943  16.543  10.163  1.00 18.13 ?  206 LEU A CD1 1 
ATOM   1640 C CD2 . LEU A 1 206 ? 35.776  17.367  12.226  1.00 16.93 ?  206 LEU A CD2 1 
ATOM   1641 N N   . THR A 1 207 ? 35.822  22.252  9.835   1.00 17.90 ?  207 THR A N   1 
ATOM   1642 C CA  . THR A 1 207 ? 36.319  23.604  9.614   1.00 18.57 ?  207 THR A CA  1 
ATOM   1643 C C   . THR A 1 207 ? 35.615  24.556  10.575  1.00 19.79 ?  207 THR A C   1 
ATOM   1644 O O   . THR A 1 207 ? 34.856  24.134  11.453  1.00 22.28 ?  207 THR A O   1 
ATOM   1645 C CB  . THR A 1 207 ? 36.082  24.045  8.171   1.00 18.13 ?  207 THR A CB  1 
ATOM   1646 O OG1 . THR A 1 207 ? 34.670  24.069  7.920   1.00 19.21 ?  207 THR A OG1 1 
ATOM   1647 C CG2 . THR A 1 207 ? 36.757  23.097  7.194   1.00 20.47 ?  207 THR A CG2 1 
ATOM   1648 N N   . ASP A 1 208 ? 35.804  25.861  10.378  1.00 19.11 ?  208 ASP A N   1 
ATOM   1649 C CA  . ASP A 1 208 ? 35.131  26.861  11.205  1.00 22.31 ?  208 ASP A CA  1 
ATOM   1650 C C   . ASP A 1 208 ? 33.724  27.166  10.715  1.00 22.81 ?  208 ASP A C   1 
ATOM   1651 O O   . ASP A 1 208 ? 33.048  28.028  11.284  1.00 25.77 ?  208 ASP A O   1 
ATOM   1652 C CB  . ASP A 1 208 ? 35.946  28.156  11.265  1.00 23.89 ?  208 ASP A CB  1 
ATOM   1653 C CG  . ASP A 1 208 ? 35.651  28.974  12.528  1.00 31.08 ?  208 ASP A CG  1 
ATOM   1654 O OD1 . ASP A 1 208 ? 35.305  28.371  13.576  1.00 29.01 ?  208 ASP A OD1 1 
ATOM   1655 O OD2 . ASP A 1 208 ? 35.757  30.223  12.464  1.00 37.73 -1 208 ASP A OD2 1 
ATOM   1656 N N   . GLU A 1 209 ? 33.268  26.466  9.692   1.00 21.42 ?  209 GLU A N   1 
ATOM   1657 C CA  . GLU A 1 209 ? 31.923  26.628  9.189   1.00 22.17 ?  209 GLU A CA  1 
ATOM   1658 C C   . GLU A 1 209 ? 30.959  25.822  10.053  1.00 22.65 ?  209 GLU A C   1 
ATOM   1659 O O   . GLU A 1 209 ? 31.358  25.050  10.927  1.00 24.78 ?  209 GLU A O   1 
ATOM   1660 C CB  . GLU A 1 209 ? 31.884  26.207  7.724   1.00 19.41 ?  209 GLU A CB  1 
ATOM   1661 C CG  . GLU A 1 209 ? 33.050  26.824  6.958   1.00 25.01 ?  209 GLU A CG  1 
ATOM   1662 C CD  . GLU A 1 209 ? 33.213  26.289  5.559   1.00 27.94 ?  209 GLU A CD  1 
ATOM   1663 O OE1 . GLU A 1 209 ? 32.895  27.025  4.597   1.00 31.24 ?  209 GLU A OE1 1 
ATOM   1664 O OE2 . GLU A 1 209 ? 33.676  25.131  5.423   1.00 29.61 -1 209 GLU A OE2 1 
ATOM   1665 N N   . ASP A 1 210 ? 29.695  26.049  9.828   1.00 24.39 ?  210 ASP A N   1 
ATOM   1666 C CA  . ASP A 1 210 ? 28.721  25.257  10.595  1.00 24.78 ?  210 ASP A CA  1 
ATOM   1667 C C   . ASP A 1 210 ? 27.549  24.844  9.716   1.00 23.85 ?  210 ASP A C   1 
ATOM   1668 O O   . ASP A 1 210 ? 27.421  25.375  8.620   1.00 22.06 ?  210 ASP A O   1 
ATOM   1669 C CB  . ASP A 1 210 ? 28.222  26.062  11.788  1.00 24.83 ?  210 ASP A CB  1 
ATOM   1670 C CG  . ASP A 1 210 ? 27.674  25.183  12.890  1.00 25.15 ?  210 ASP A CG  1 
ATOM   1671 O OD1 . ASP A 1 210 ? 27.824  23.963  12.788  1.00 29.95 ?  210 ASP A OD1 1 
ATOM   1672 O OD2 . ASP A 1 210 ? 27.112  25.732  13.819  1.00 30.85 -1 210 ASP A OD2 1 
ATOM   1673 N N   . ILE A 1 211 ? 26.770  23.891  10.203  1.00 22.07 ?  211 ILE A N   1 
ATOM   1674 C CA  . ILE A 1 211 ? 25.565  23.476  9.509   1.00 20.70 ?  211 ILE A CA  1 
ATOM   1675 C C   . ILE A 1 211 ? 24.520  24.585  9.597   1.00 21.83 ?  211 ILE A C   1 
ATOM   1676 O O   . ILE A 1 211 ? 24.468  25.359  10.567  1.00 21.60 ?  211 ILE A O   1 
ATOM   1677 C CB  . ILE A 1 211 ? 25.043  22.147  10.095  1.00 20.63 ?  211 ILE A CB  1 
ATOM   1678 C CG1 . ILE A 1 211 ? 23.894  21.592  9.248   1.00 22.32 ?  211 ILE A CG1 1 
ATOM   1679 C CG2 . ILE A 1 211 ? 24.598  22.309  11.572  1.00 20.95 ?  211 ILE A CG2 1 
ATOM   1680 C CD1 . ILE A 1 211 ? 23.146  20.431  9.888   1.00 22.08 ?  211 ILE A CD1 1 
ATOM   1681 N N   . THR A 1 212 ? 23.721  24.707  8.541   1.00 15.84 ?  212 THR A N   1 
ATOM   1682 C CA  . THR A 1 212 ? 22.458  25.427  8.575   1.00 17.50 ?  212 THR A CA  1 
ATOM   1683 C C   . THR A 1 212 ? 21.361  24.368  8.611   1.00 17.14 ?  212 THR A C   1 
ATOM   1684 O O   . THR A 1 212 ? 21.078  23.743  7.576   1.00 14.25 ?  212 THR A O   1 
ATOM   1685 C CB  . THR A 1 212 ? 22.303  26.331  7.345   1.00 18.59 ?  212 THR A CB  1 
ATOM   1686 O OG1 . THR A 1 212 ? 23.350  27.318  7.331   1.00 19.72 ?  212 THR A OG1 1 
ATOM   1687 C CG2 . THR A 1 212 ? 20.918  27.020  7.316   1.00 16.32 ?  212 THR A CG2 1 
ATOM   1688 N N   . PRO A 1 213 ? 20.756  24.084  9.766   1.00 16.51 ?  213 PRO A N   1 
ATOM   1689 C CA  . PRO A 1 213 ? 19.652  23.115  9.792   1.00 15.51 ?  213 PRO A CA  1 
ATOM   1690 C C   . PRO A 1 213 ? 18.470  23.610  8.978   1.00 16.95 ?  213 PRO A C   1 
ATOM   1691 O O   . PRO A 1 213 ? 18.183  24.809  8.926   1.00 14.78 ?  213 PRO A O   1 
ATOM   1692 C CB  . PRO A 1 213 ? 19.304  23.007  11.285  1.00 14.78 ?  213 PRO A CB  1 
ATOM   1693 C CG  . PRO A 1 213 ? 20.528  23.531  12.011  1.00 16.67 ?  213 PRO A CG  1 
ATOM   1694 C CD  . PRO A 1 213 ? 21.079  24.595  11.110  1.00 14.67 ?  213 PRO A CD  1 
ATOM   1695 N N   . ALA A 1 214 ? 17.778  22.665  8.339   1.00 13.96 ?  214 ALA A N   1 
ATOM   1696 C CA  . ALA A 1 214 ? 16.610  23.022  7.539   1.00 16.29 ?  214 ALA A CA  1 
ATOM   1697 C C   . ALA A 1 214 ? 15.556  23.748  8.367   1.00 15.81 ?  214 ALA A C   1 
ATOM   1698 O O   . ALA A 1 214 ? 14.873  24.644  7.850   1.00 15.71 ?  214 ALA A O   1 
ATOM   1699 C CB  . ALA A 1 214 ? 16.003  21.775  6.898   1.00 15.19 ?  214 ALA A CB  1 
ATOM   1700 N N   . PHE A 1 215 ? 15.410  23.394  9.651   1.00 14.06 ?  215 PHE A N   1 
ATOM   1701 C CA  . PHE A 1 215 ? 14.361  24.036  10.435  1.00 16.81 ?  215 PHE A CA  1 
ATOM   1702 C C   . PHE A 1 215 ? 14.588  25.530  10.635  1.00 16.64 ?  215 PHE A C   1 
ATOM   1703 O O   . PHE A 1 215 ? 13.674  26.207  11.109  1.00 15.99 ?  215 PHE A O   1 
ATOM   1704 C CB  . PHE A 1 215 ? 14.174  23.344  11.800  1.00 15.47 ?  215 PHE A CB  1 
ATOM   1705 C CG  . PHE A 1 215 ? 15.352  23.445  12.731  1.00 16.40 ?  215 PHE A CG  1 
ATOM   1706 C CD1 . PHE A 1 215 ? 15.644  24.636  13.404  1.00 16.17 ?  215 PHE A CD1 1 
ATOM   1707 C CD2 . PHE A 1 215 ? 16.125  22.325  12.993  1.00 13.79 ?  215 PHE A CD2 1 
ATOM   1708 C CE1 . PHE A 1 215 ? 16.713  24.701  14.298  1.00 16.10 ?  215 PHE A CE1 1 
ATOM   1709 C CE2 . PHE A 1 215 ? 17.206  22.384  13.869  1.00 15.74 ?  215 PHE A CE2 1 
ATOM   1710 C CZ  . PHE A 1 215 ? 17.499  23.574  14.521  1.00 16.55 ?  215 PHE A CZ  1 
ATOM   1711 N N   . THR A 1 216 ? 15.758  26.066  10.285  1.00 16.47 ?  216 THR A N   1 
ATOM   1712 C CA  . THR A 1 216 ? 16.005  27.497  10.451  1.00 17.37 ?  216 THR A CA  1 
ATOM   1713 C C   . THR A 1 216 ? 15.563  28.341  9.261   1.00 19.80 ?  216 THR A C   1 
ATOM   1714 O O   . THR A 1 216 ? 15.620  29.573  9.353   1.00 18.46 ?  216 THR A O   1 
ATOM   1715 C CB  . THR A 1 216 ? 17.496  27.773  10.699  1.00 16.28 ?  216 THR A CB  1 
ATOM   1716 O OG1 . THR A 1 216 ? 18.236  27.398  9.536   1.00 14.99 ?  216 THR A OG1 1 
ATOM   1717 C CG2 . THR A 1 216 ? 18.000  27.000  11.896  1.00 17.25 ?  216 THR A CG2 1 
ATOM   1718 N N   . VAL A 1 217 ? 15.137  27.729  8.149   1.00 16.73 ?  217 VAL A N   1 
ATOM   1719 C CA  . VAL A 1 217 ? 14.734  28.537  7.002   1.00 19.16 ?  217 VAL A CA  1 
ATOM   1720 C C   . VAL A 1 217 ? 13.486  29.349  7.352   1.00 22.24 ?  217 VAL A C   1 
ATOM   1721 O O   . VAL A 1 217 ? 12.704  29.005  8.246   1.00 19.98 ?  217 VAL A O   1 
ATOM   1722 C CB  . VAL A 1 217 ? 14.504  27.667  5.754   1.00 19.16 ?  217 VAL A CB  1 
ATOM   1723 C CG1 . VAL A 1 217 ? 15.735  26.797  5.467   1.00 17.89 ?  217 VAL A CG1 1 
ATOM   1724 C CG2 . VAL A 1 217 ? 13.262  26.797  5.930   1.00 17.59 ?  217 VAL A CG2 1 
ATOM   1725 N N   . ASP A 1 218 ? 13.298  30.450  6.630   1.00 23.68 ?  218 ASP A N   1 
ATOM   1726 C CA  . ASP A 1 218 ? 12.202  31.352  6.956   1.00 26.50 ?  218 ASP A CA  1 
ATOM   1727 C C   . ASP A 1 218 ? 10.855  30.715  6.621   1.00 25.24 ?  218 ASP A C   1 
ATOM   1728 O O   . ASP A 1 218 ? 10.758  29.749  5.859   1.00 22.64 ?  218 ASP A O   1 
ATOM   1729 C CB  . ASP A 1 218 ? 12.379  32.683  6.228   1.00 30.37 ?  218 ASP A CB  1 
ATOM   1730 C CG  . ASP A 1 218 ? 13.780  33.255  6.407   1.00 38.75 ?  218 ASP A CG  1 
ATOM   1731 O OD1 . ASP A 1 218 ? 14.109  33.666  7.544   1.00 41.45 ?  218 ASP A OD1 1 
ATOM   1732 O OD2 . ASP A 1 218 ? 14.565  33.272  5.425   1.00 44.19 -1 218 ASP A OD2 1 
ATOM   1733 N N   . TRP A 1 219 ? 9.800   31.281  7.205   1.00 26.30 ?  219 TRP A N   1 
ATOM   1734 C CA  . TRP A 1 219 ? 8.497   30.624  7.195   1.00 25.36 ?  219 TRP A CA  1 
ATOM   1735 C C   . TRP A 1 219 ? 7.862   30.508  5.815   1.00 29.99 ?  219 TRP A C   1 
ATOM   1736 O O   . TRP A 1 219 ? 6.900   29.747  5.668   1.00 34.88 ?  219 TRP A O   1 
ATOM   1737 C CB  . TRP A 1 219 ? 7.541   31.348  8.133   1.00 26.72 ?  219 TRP A CB  1 
ATOM   1738 C CG  . TRP A 1 219 ? 7.675   30.916  9.550   1.00 24.38 ?  219 TRP A CG  1 
ATOM   1739 C CD1 . TRP A 1 219 ? 8.219   31.635  10.570  1.00 26.72 ?  219 TRP A CD1 1 
ATOM   1740 C CD2 . TRP A 1 219 ? 7.276   29.657  10.113  1.00 24.03 ?  219 TRP A CD2 1 
ATOM   1741 N NE1 . TRP A 1 219 ? 8.169   30.917  11.738  1.00 26.70 ?  219 TRP A NE1 1 
ATOM   1742 C CE2 . TRP A 1 219 ? 7.597   29.698  11.486  1.00 25.76 ?  219 TRP A CE2 1 
ATOM   1743 C CE3 . TRP A 1 219 ? 6.669   28.509  9.594   1.00 22.45 ?  219 TRP A CE3 1 
ATOM   1744 C CZ2 . TRP A 1 219 ? 7.336   28.636  12.345  1.00 24.94 ?  219 TRP A CZ2 1 
ATOM   1745 C CZ3 . TRP A 1 219 ? 6.411   27.450  10.450  1.00 20.94 ?  219 TRP A CZ3 1 
ATOM   1746 C CH2 . TRP A 1 219 ? 6.748   27.521  11.809  1.00 23.34 ?  219 TRP A CH2 1 
ATOM   1747 N N   . ASP A 1 220 ? 8.348   31.227  4.806   1.00 31.13 ?  220 ASP A N   1 
ATOM   1748 C CA  . ASP A 1 220 ? 7.915   30.921  3.444   1.00 34.90 ?  220 ASP A CA  1 
ATOM   1749 C C   . ASP A 1 220 ? 8.095   29.444  3.116   1.00 36.43 ?  220 ASP A C   1 
ATOM   1750 O O   . ASP A 1 220 ? 7.315   28.873  2.343   1.00 39.54 ?  220 ASP A O   1 
ATOM   1751 C CB  . ASP A 1 220 ? 8.700   31.748  2.427   1.00 40.59 ?  220 ASP A CB  1 
ATOM   1752 C CG  . ASP A 1 220 ? 8.588   33.230  2.673   1.00 47.58 ?  220 ASP A CG  1 
ATOM   1753 O OD1 . ASP A 1 220 ? 7.467   33.695  2.980   1.00 49.43 ?  220 ASP A OD1 1 
ATOM   1754 O OD2 . ASP A 1 220 ? 9.621   33.927  2.561   1.00 47.89 -1 220 ASP A OD2 1 
ATOM   1755 N N   . ALA A 1 221 ? 9.108   28.812  3.701   1.00 28.75 ?  221 ALA A N   1 
ATOM   1756 C CA  . ALA A 1 221 ? 9.495   27.451  3.361   1.00 22.10 ?  221 ALA A CA  1 
ATOM   1757 C C   . ALA A 1 221 ? 9.563   26.531  4.563   1.00 17.89 ?  221 ALA A C   1 
ATOM   1758 O O   . ALA A 1 221 ? 9.559   25.304  4.377   1.00 17.08 ?  221 ALA A O   1 
ATOM   1759 C CB  . ALA A 1 221 ? 10.862  27.448  2.656   1.00 21.29 ?  221 ALA A CB  1 
ATOM   1760 N N   . LYS A 1 222 ? 9.614   27.076  5.781   1.00 18.21 ?  222 LYS A N   1 
ATOM   1761 C CA  . LYS A 1 222 ? 9.798   26.258  6.975   1.00 16.18 ?  222 LYS A CA  1 
ATOM   1762 C C   . LYS A 1 222 ? 8.681   25.242  7.142   1.00 15.40 ?  222 LYS A C   1 
ATOM   1763 O O   . LYS A 1 222 ? 8.874   24.220  7.801   1.00 17.05 ?  222 LYS A O   1 
ATOM   1764 C CB  . LYS A 1 222 ? 9.884   27.144  8.217   1.00 19.06 ?  222 LYS A CB  1 
ATOM   1765 C CG  . LYS A 1 222 ? 10.713  26.534  9.346   1.00 18.42 ?  222 LYS A CG  1 
ATOM   1766 C CD  . LYS A 1 222 ? 10.388  27.145  10.714  1.00 20.09 ?  222 LYS A CD  1 
ATOM   1767 C CE  . LYS A 1 222 ? 10.807  28.603  10.814  1.00 20.11 ?  222 LYS A CE  1 
ATOM   1768 N NZ  . LYS A 1 222 ? 12.289  28.713  10.967  1.00 19.38 1  222 LYS A NZ  1 
ATOM   1769 N N   . ASN A 1 223 ? 7.504   25.511  6.580   1.00 17.91 ?  223 ASN A N   1 
ATOM   1770 C CA  . ASN A 1 223 ? 6.403   24.561  6.689   1.00 17.45 ?  223 ASN A CA  1 
ATOM   1771 C C   . ASN A 1 223 ? 6.609   23.321  5.833   1.00 18.33 ?  223 ASN A C   1 
ATOM   1772 O O   . ASN A 1 223 ? 5.801   22.388  5.914   1.00 17.93 ?  223 ASN A O   1 
ATOM   1773 C CB  . ASN A 1 223 ? 5.088   25.218  6.278   1.00 19.96 ?  223 ASN A CB  1 
ATOM   1774 C CG  . ASN A 1 223 ? 4.549   26.129  7.335   1.00 23.29 ?  223 ASN A CG  1 
ATOM   1775 O OD1 . ASN A 1 223 ? 4.380   25.726  8.491   1.00 22.44 ?  223 ASN A OD1 1 
ATOM   1776 N ND2 . ASN A 1 223 ? 4.278   27.376  6.957   1.00 24.75 ?  223 ASN A ND2 1 
ATOM   1777 N N   . TRP A 1 224 ? 7.643   23.298  5.000   1.00 15.39 ?  224 TRP A N   1 
ATOM   1778 C CA  . TRP A 1 224 ? 7.879   22.189  4.093   1.00 16.39 ?  224 TRP A CA  1 
ATOM   1779 C C   . TRP A 1 224 ? 9.109   21.380  4.470   1.00 16.74 ?  224 TRP A C   1 
ATOM   1780 O O   . TRP A 1 224 ? 9.583   20.587  3.646   1.00 17.92 ?  224 TRP A O   1 
ATOM   1781 C CB  . TRP A 1 224 ? 8.020   22.705  2.656   1.00 15.24 ?  224 TRP A CB  1 
ATOM   1782 C CG  . TRP A 1 224 ? 6.750   23.234  2.132   1.00 17.00 ?  224 TRP A CG  1 
ATOM   1783 C CD1 . TRP A 1 224 ? 6.305   24.523  2.194   1.00 18.76 ?  224 TRP A CD1 1 
ATOM   1784 C CD2 . TRP A 1 224 ? 5.723   22.479  1.501   1.00 18.63 ?  224 TRP A CD2 1 
ATOM   1785 N NE1 . TRP A 1 224 ? 5.061   24.614  1.614   1.00 20.04 ?  224 TRP A NE1 1 
ATOM   1786 C CE2 . TRP A 1 224 ? 4.683   23.367  1.187   1.00 19.20 ?  224 TRP A CE2 1 
ATOM   1787 C CE3 . TRP A 1 224 ? 5.582   21.127  1.164   1.00 19.45 ?  224 TRP A CE3 1 
ATOM   1788 C CZ2 . TRP A 1 224 ? 3.520   22.951  0.549   1.00 22.48 ?  224 TRP A CZ2 1 
ATOM   1789 C CZ3 . TRP A 1 224 ? 4.426   20.717  0.537   1.00 20.75 ?  224 TRP A CZ3 1 
ATOM   1790 C CH2 . TRP A 1 224 ? 3.412   21.624  0.238   1.00 21.18 ?  224 TRP A CH2 1 
ATOM   1791 N N   . VAL A 1 225 ? 9.652   21.564  5.673   1.00 13.23 ?  225 VAL A N   1 
ATOM   1792 C CA  . VAL A 1 225 ? 10.924  20.932  6.017   1.00 13.51 ?  225 VAL A CA  1 
ATOM   1793 C C   . VAL A 1 225 ? 10.767  20.024  7.229   1.00 14.40 ?  225 VAL A C   1 
ATOM   1794 O O   . VAL A 1 225 ? 9.945   20.258  8.124   1.00 15.51 ?  225 VAL A O   1 
ATOM   1795 C CB  . VAL A 1 225 ? 12.071  21.951  6.261   1.00 15.77 ?  225 VAL A CB  1 
ATOM   1796 C CG1 . VAL A 1 225 ? 12.259  22.873  5.061   1.00 15.28 ?  225 VAL A CG1 1 
ATOM   1797 C CG2 . VAL A 1 225 ? 11.854  22.736  7.535   1.00 17.94 ?  225 VAL A CG2 1 
ATOM   1798 N N   . VAL A 1 226 ? 11.585  18.970  7.240   1.00 12.51 ?  226 VAL A N   1 
ATOM   1799 C CA  . VAL A 1 226 ? 11.789  18.086  8.383   1.00 15.17 ?  226 VAL A CA  1 
ATOM   1800 C C   . VAL A 1 226 ? 13.299  17.961  8.581   1.00 13.41 ?  226 VAL A C   1 
ATOM   1801 O O   . VAL A 1 226 ? 14.010  17.567  7.649   1.00 14.79 ?  226 VAL A O   1 
ATOM   1802 C CB  . VAL A 1 226 ? 11.170  16.691  8.164   1.00 17.34 ?  226 VAL A CB  1 
ATOM   1803 C CG1 . VAL A 1 226 ? 11.564  15.764  9.308   1.00 16.63 ?  226 VAL A CG1 1 
ATOM   1804 C CG2 . VAL A 1 226 ? 9.645   16.765  8.010   1.00 15.11 ?  226 VAL A CG2 1 
ATOM   1805 N N   . SER A 1 227 ? 13.789  18.306  9.771   1.00 11.35 ?  227 SER A N   1 
ATOM   1806 C CA  . SER A 1 227 ? 15.190  18.076  10.138  1.00 14.00 ?  227 SER A CA  1 
ATOM   1807 C C   . SER A 1 227 ? 15.297  16.823  11.000  1.00 16.61 ?  227 SER A C   1 
ATOM   1808 O O   . SER A 1 227 ? 14.540  16.666  11.964  1.00 16.59 ?  227 SER A O   1 
ATOM   1809 C CB  . SER A 1 227 ? 15.799  19.265  10.898  1.00 17.02 ?  227 SER A CB  1 
ATOM   1810 O OG  . SER A 1 227 ? 15.939  20.423  10.092  1.00 15.93 ?  227 SER A OG  1 
ATOM   1811 N N   . LEU A 1 228 ? 16.242  15.940  10.667  1.00 13.85 ?  228 LEU A N   1 
ATOM   1812 C CA  . LEU A 1 228 ? 16.474  14.727  11.443  1.00 13.92 ?  228 LEU A CA  1 
ATOM   1813 C C   . LEU A 1 228 ? 17.871  14.753  12.034  1.00 14.39 ?  228 LEU A C   1 
ATOM   1814 O O   . LEU A 1 228 ? 18.852  14.956  11.308  1.00 14.36 ?  228 LEU A O   1 
ATOM   1815 C CB  . LEU A 1 228 ? 16.317  13.461  10.593  1.00 15.00 ?  228 LEU A CB  1 
ATOM   1816 C CG  . LEU A 1 228 ? 14.966  13.312  9.918   1.00 15.28 ?  228 LEU A CG  1 
ATOM   1817 C CD1 . LEU A 1 228 ? 15.031  12.167  8.939   1.00 15.34 ?  228 LEU A CD1 1 
ATOM   1818 C CD2 . LEU A 1 228 ? 13.889  13.086  10.956  1.00 17.22 ?  228 LEU A CD2 1 
ATOM   1819 N N   . ILE A 1 229 ? 17.963  14.527  13.348  1.00 12.76 ?  229 ILE A N   1 
ATOM   1820 C CA  . ILE A 1 229 ? 19.232  14.531  14.066  1.00 14.05 ?  229 ILE A CA  1 
ATOM   1821 C C   . ILE A 1 229 ? 19.286  13.326  14.997  1.00 14.28 ?  229 ILE A C   1 
ATOM   1822 O O   . ILE A 1 229 ? 18.279  12.677  15.271  1.00 13.01 ?  229 ILE A O   1 
ATOM   1823 C CB  . ILE A 1 229 ? 19.453  15.830  14.869  1.00 15.20 ?  229 ILE A CB  1 
ATOM   1824 C CG1 . ILE A 1 229 ? 18.398  15.993  15.965  1.00 17.54 ?  229 ILE A CG1 1 
ATOM   1825 C CG2 . ILE A 1 229 ? 19.500  17.043  13.936  1.00 15.56 ?  229 ILE A CG2 1 
ATOM   1826 C CD1 . ILE A 1 229 ? 18.800  17.014  17.016  1.00 20.50 ?  229 ILE A CD1 1 
ATOM   1827 N N   . SER A 1 230 ? 20.487  13.033  15.482  1.00 15.00 ?  230 SER A N   1 
ATOM   1828 C CA  . SER A 1 230 ? 20.688  11.885  16.357  1.00 16.32 ?  230 SER A CA  1 
ATOM   1829 C C   . SER A 1 230 ? 22.058  12.013  17.004  1.00 16.29 ?  230 SER A C   1 
ATOM   1830 O O   . SER A 1 230 ? 22.979  12.563  16.381  1.00 14.82 ?  230 SER A O   1 
ATOM   1831 C CB  . SER A 1 230 ? 20.595  10.571  15.568  1.00 17.44 ?  230 SER A CB  1 
ATOM   1832 O OG  . SER A 1 230 ? 20.932  9.449   16.384  1.00 15.86 ?  230 SER A OG  1 
ATOM   1833 N N   . PRO A 1 231 ? 22.239  11.535  18.240  1.00 15.24 ?  231 PRO A N   1 
ATOM   1834 C CA  . PRO A 1 231 ? 23.596  11.448  18.796  1.00 15.33 ?  231 PRO A CA  1 
ATOM   1835 C C   . PRO A 1 231 ? 24.422  10.327  18.192  1.00 16.58 ?  231 PRO A C   1 
ATOM   1836 O O   . PRO A 1 231 ? 25.613  10.220  18.518  1.00 16.10 ?  231 PRO A O   1 
ATOM   1837 C CB  . PRO A 1 231 ? 23.353  11.214  20.302  1.00 16.85 ?  231 PRO A CB  1 
ATOM   1838 C CG  . PRO A 1 231 ? 21.986  10.600  20.388  1.00 15.98 ?  231 PRO A CG  1 
ATOM   1839 C CD  . PRO A 1 231 ? 21.199  11.142  19.208  1.00 15.92 ?  231 PRO A CD  1 
ATOM   1840 N N   . SER A 1 232 ? 23.851  9.500   17.312  1.00 15.22 ?  232 SER A N   1 
ATOM   1841 C CA  . SER A 1 232 ? 24.494  8.226   16.983  1.00 16.12 ?  232 SER A CA  1 
ATOM   1842 C C   . SER A 1 232 ? 25.829  8.425   16.269  1.00 15.26 ?  232 SER A C   1 
ATOM   1843 O O   . SER A 1 232 ? 26.843  7.857   16.687  1.00 15.98 ?  232 SER A O   1 
ATOM   1844 C CB  . SER A 1 232 ? 23.555  7.343   16.159  1.00 18.37 ?  232 SER A CB  1 
ATOM   1845 O OG  . SER A 1 232 ? 23.440  7.811   14.843  1.00 22.20 ?  232 SER A OG  1 
ATOM   1846 N N   . LYS A 1 233 ? 25.862  9.229   15.196  1.00 14.34 ?  233 LYS A N   1 
ATOM   1847 C CA  . LYS A 1 233 ? 27.133  9.452   14.500  1.00 16.19 ?  233 LYS A CA  1 
ATOM   1848 C C   . LYS A 1 233 ? 28.098  10.257  15.354  1.00 14.78 ?  233 LYS A C   1 
ATOM   1849 O O   . LYS A 1 233 ? 29.277  9.917   15.460  1.00 15.31 ?  233 LYS A O   1 
ATOM   1850 C CB  . LYS A 1 233 ? 26.922  10.175  13.172  1.00 17.06 ?  233 LYS A CB  1 
ATOM   1851 C CG  . LYS A 1 233 ? 26.355  9.322   12.111  1.00 22.47 ?  233 LYS A CG  1 
ATOM   1852 C CD  . LYS A 1 233 ? 27.409  8.486   11.440  1.00 25.25 ?  233 LYS A CD  1 
ATOM   1853 C CE  . LYS A 1 233 ? 26.729  7.240   10.937  1.00 23.67 ?  233 LYS A CE  1 
ATOM   1854 N NZ  . LYS A 1 233 ? 25.376  7.646   10.432  1.00 29.97 1  233 LYS A NZ  1 
ATOM   1855 N N   . THR A 1 234 ? 27.611  11.338  15.957  1.00 15.02 ?  234 THR A N   1 
ATOM   1856 C CA  . THR A 1 234 ? 28.472  12.246  16.704  1.00 13.64 ?  234 THR A CA  1 
ATOM   1857 C C   . THR A 1 234 ? 29.197  11.540  17.835  1.00 15.69 ?  234 THR A C   1 
ATOM   1858 O O   . THR A 1 234 ? 30.383  11.795  18.082  1.00 16.14 ?  234 THR A O   1 
ATOM   1859 C CB  . THR A 1 234 ? 27.622  13.377  17.272  1.00 16.83 ?  234 THR A CB  1 
ATOM   1860 O OG1 . THR A 1 234 ? 26.893  13.988  16.197  1.00 14.53 ?  234 THR A OG1 1 
ATOM   1861 C CG2 . THR A 1 234 ? 28.508  14.404  18.006  1.00 15.67 ?  234 THR A CG2 1 
ATOM   1862 N N   . PHE A 1 235 ? 28.503  10.653  18.546  1.00 13.67 ?  235 PHE A N   1 
ATOM   1863 C CA  . PHE A 1 235 ? 29.011  10.155  19.819  1.00 11.72 ?  235 PHE A CA  1 
ATOM   1864 C C   . PHE A 1 235 ? 29.328  8.666   19.797  1.00 13.54 ?  235 PHE A C   1 
ATOM   1865 O O   . PHE A 1 235 ? 29.625  8.098   20.855  1.00 13.70 ?  235 PHE A O   1 
ATOM   1866 C CB  . PHE A 1 235 ? 27.999  10.470  20.926  1.00 14.26 ?  235 PHE A CB  1 
ATOM   1867 C CG  . PHE A 1 235 ? 27.884  11.942  21.234  1.00 13.80 ?  235 PHE A CG  1 
ATOM   1868 C CD1 . PHE A 1 235 ? 28.874  12.586  21.959  1.00 12.71 ?  235 PHE A CD1 1 
ATOM   1869 C CD2 . PHE A 1 235 ? 26.788  12.679  20.785  1.00 15.33 ?  235 PHE A CD2 1 
ATOM   1870 C CE1 . PHE A 1 235 ? 28.773  13.961  22.236  1.00 13.82 ?  235 PHE A CE1 1 
ATOM   1871 C CE2 . PHE A 1 235 ? 26.679  14.046  21.057  1.00 15.45 ?  235 PHE A CE2 1 
ATOM   1872 C CZ  . PHE A 1 235 ? 27.673  14.680  21.781  1.00 14.42 ?  235 PHE A CZ  1 
ATOM   1873 N N   . ASN A 1 236 ? 29.276  8.026   18.622  1.00 12.26 ?  236 ASN A N   1 
ATOM   1874 C CA  . ASN A 1 236 ? 29.528  6.583   18.471  1.00 13.97 ?  236 ASN A CA  1 
ATOM   1875 C C   . ASN A 1 236 ? 28.484  5.736   19.206  1.00 14.84 ?  236 ASN A C   1 
ATOM   1876 O O   . ASN A 1 236 ? 28.811  4.851   20.003  1.00 14.55 ?  236 ASN A O   1 
ATOM   1877 C CB  . ASN A 1 236 ? 30.940  6.234   18.938  1.00 11.99 ?  236 ASN A CB  1 
ATOM   1878 C CG  . ASN A 1 236 ? 31.443  4.933   18.357  1.00 15.47 ?  236 ASN A CG  1 
ATOM   1879 O OD1 . ASN A 1 236 ? 30.959  4.465   17.327  1.00 15.63 ?  236 ASN A OD1 1 
ATOM   1880 N ND2 . ASN A 1 236 ? 32.437  4.350   19.012  1.00 14.63 ?  236 ASN A ND2 1 
ATOM   1881 N N   . LEU A 1 237 ? 27.213  5.989   18.892  1.00 14.82 ?  237 LEU A N   1 
ATOM   1882 C CA  . LEU A 1 237 ? 26.052  5.410   19.563  1.00 14.56 ?  237 LEU A CA  1 
ATOM   1883 C C   . LEU A 1 237 ? 25.056  4.877   18.545  1.00 14.70 ?  237 LEU A C   1 
ATOM   1884 O O   . LEU A 1 237 ? 23.843  5.047   18.690  1.00 15.23 ?  237 LEU A O   1 
ATOM   1885 C CB  . LEU A 1 237 ? 25.381  6.440   20.470  1.00 14.20 ?  237 LEU A CB  1 
ATOM   1886 C CG  . LEU A 1 237 ? 26.198  6.939   21.654  1.00 13.56 ?  237 LEU A CG  1 
ATOM   1887 C CD1 . LEU A 1 237 ? 25.448  8.074   22.313  1.00 15.88 ?  237 LEU A CD1 1 
ATOM   1888 C CD2 . LEU A 1 237 ? 26.412  5.791   22.648  1.00 16.98 ?  237 LEU A CD2 1 
ATOM   1889 N N   . ALA A 1 238 ? 25.562  4.234   17.491  1.00 14.67 ?  238 ALA A N   1 
ATOM   1890 C CA  . ALA A 1 238 ? 24.688  3.650   16.474  1.00 16.61 ?  238 ALA A CA  1 
ATOM   1891 C C   . ALA A 1 238 ? 23.659  2.715   17.097  1.00 16.31 ?  238 ALA A C   1 
ATOM   1892 O O   . ALA A 1 238 ? 22.485  2.730   16.711  1.00 16.06 ?  238 ALA A O   1 
ATOM   1893 C CB  . ALA A 1 238 ? 25.519  2.895   15.430  1.00 18.41 ?  238 ALA A CB  1 
ATOM   1894 N N   . ALA A 1 239 ? 24.073  1.906   18.074  1.00 13.05 ?  239 ALA A N   1 
ATOM   1895 C CA  . ALA A 1 239 ? 23.180  0.905   18.644  1.00 16.83 ?  239 ALA A CA  1 
ATOM   1896 C C   . ALA A 1 239 ? 22.305  1.457   19.769  1.00 14.67 ?  239 ALA A C   1 
ATOM   1897 O O   . ALA A 1 239 ? 21.540  0.694   20.357  1.00 15.40 ?  239 ALA A O   1 
ATOM   1898 C CB  . ALA A 1 239 ? 23.987  -0.306  19.141  1.00 15.90 ?  239 ALA A CB  1 
ATOM   1899 N N   . LEU A 1 240 ? 22.390  2.762   20.073  1.00 13.02 ?  240 LEU A N   1 
ATOM   1900 C CA  . LEU A 1 240 ? 21.552  3.338   21.124  1.00 14.44 ?  240 LEU A CA  1 
ATOM   1901 C C   . LEU A 1 240 ? 20.108  3.504   20.667  1.00 14.52 ?  240 LEU A C   1 
ATOM   1902 O O   . LEU A 1 240 ? 19.193  3.421   21.495  1.00 13.91 ?  240 LEU A O   1 
ATOM   1903 C CB  . LEU A 1 240 ? 22.105  4.691   21.588  1.00 13.88 ?  240 LEU A CB  1 
ATOM   1904 C CG  . LEU A 1 240 ? 21.289  5.413   22.677  1.00 15.16 ?  240 LEU A CG  1 
ATOM   1905 C CD1 . LEU A 1 240 ? 21.265  4.598   23.974  1.00 16.34 ?  240 LEU A CD1 1 
ATOM   1906 C CD2 . LEU A 1 240 ? 21.776  6.842   22.942  1.00 15.25 ?  240 LEU A CD2 1 
ATOM   1907 N N   . HIS A 1 241 ? 19.890  3.759   19.374  1.00 13.15 ?  241 HIS A N   1 
ATOM   1908 C CA  . HIS A 1 241 ? 18.541  3.903   18.801  1.00 15.49 ?  241 HIS A CA  1 
ATOM   1909 C C   . HIS A 1 241 ? 17.804  5.092   19.425  1.00 16.11 ?  241 HIS A C   1 
ATOM   1910 O O   . HIS A 1 241 ? 16.676  4.970   19.903  1.00 15.07 ?  241 HIS A O   1 
ATOM   1911 C CB  . HIS A 1 241 ? 17.709  2.620   18.952  1.00 18.15 ?  241 HIS A CB  1 
ATOM   1912 C CG  . HIS A 1 241 ? 18.200  1.453   18.152  1.00 17.93 ?  241 HIS A CG  1 
ATOM   1913 N ND1 . HIS A 1 241 ? 19.350  1.485   17.394  1.00 22.19 ?  241 HIS A ND1 1 
ATOM   1914 C CD2 . HIS A 1 241 ? 17.704  0.200   18.020  1.00 15.88 ?  241 HIS A CD2 1 
ATOM   1915 C CE1 . HIS A 1 241 ? 19.537  0.311   16.820  1.00 18.05 ?  241 HIS A CE1 1 
ATOM   1916 N NE2 . HIS A 1 241 ? 18.552  -0.488  17.184  1.00 22.25 ?  241 HIS A NE2 1 
ATOM   1917 N N   . ALA A 1 242 ? 18.451  6.260   19.402  1.00 14.91 ?  242 ALA A N   1 
ATOM   1918 C CA  . ALA A 1 242 ? 17.850  7.527   19.811  1.00 13.40 ?  242 ALA A CA  1 
ATOM   1919 C C   . ALA A 1 242 ? 18.073  8.543   18.702  1.00 17.69 ?  242 ALA A C   1 
ATOM   1920 O O   . ALA A 1 242 ? 19.201  8.700   18.226  1.00 17.60 ?  242 ALA A O   1 
ATOM   1921 C CB  . ALA A 1 242 ? 18.450  8.031   21.129  1.00 15.13 ?  242 ALA A CB  1 
ATOM   1922 N N   . ALA A 1 243 ? 17.004  9.217   18.284  1.00 13.65 ?  243 ALA A N   1 
ATOM   1923 C CA  . ALA A 1 243 ? 17.065  10.248  17.253  1.00 13.97 ?  243 ALA A CA  1 
ATOM   1924 C C   . ALA A 1 243 ? 15.927  11.226  17.509  1.00 16.84 ?  243 ALA A C   1 
ATOM   1925 O O   . ALA A 1 243 ? 15.120  11.045  18.427  1.00 14.97 ?  243 ALA A O   1 
ATOM   1926 C CB  . ALA A 1 243 ? 16.978  9.662   15.842  1.00 13.41 ?  243 ALA A CB  1 
ATOM   1927 N N   . CYS A 1 244 ? 15.864  12.274  16.700  1.00 14.64 ?  244 CYS A N   1 
ATOM   1928 C CA  . CYS A 1 244 ? 14.811  13.252  16.912  1.00 14.40 ?  244 CYS A CA  1 
ATOM   1929 C C   . CYS A 1 244 ? 14.492  13.885  15.570  1.00 14.34 ?  244 CYS A C   1 
ATOM   1930 O O   . CYS A 1 244 ? 15.410  14.268  14.842  1.00 14.82 ?  244 CYS A O   1 
ATOM   1931 C CB  . CYS A 1 244 ? 15.266  14.305  17.917  1.00 15.92 ?  244 CYS A CB  1 
ATOM   1932 S SG  . CYS A 1 244 ? 13.988  15.448  18.437  1.00 18.39 ?  244 CYS A SG  1 
ATOM   1933 N N   . ALA A 1 245 ? 13.205  13.962  15.239  1.00 13.66 ?  245 ALA A N   1 
ATOM   1934 C CA  . ALA A 1 245 ? 12.748  14.736  14.099  1.00 15.02 ?  245 ALA A CA  1 
ATOM   1935 C C   . ALA A 1 245 ? 12.340  16.117  14.600  1.00 14.67 ?  245 ALA A C   1 
ATOM   1936 O O   . ALA A 1 245 ? 11.775  16.252  15.687  1.00 16.67 ?  245 ALA A O   1 
ATOM   1937 C CB  . ALA A 1 245 ? 11.583  14.038  13.401  1.00 14.60 ?  245 ALA A CB  1 
ATOM   1938 N N   . ILE A 1 246 ? 12.682  17.140  13.835  1.00 12.01 ?  246 ILE A N   1 
ATOM   1939 C CA  . ILE A 1 246 ? 12.326  18.517  14.157  1.00 14.03 ?  246 ILE A CA  1 
ATOM   1940 C C   . ILE A 1 246 ? 11.431  18.978  13.020  1.00 14.98 ?  246 ILE A C   1 
ATOM   1941 O O   . ILE A 1 246 ? 11.895  19.126  11.883  1.00 13.45 ?  246 ILE A O   1 
ATOM   1942 C CB  . ILE A 1 246 ? 13.565  19.413  14.318  1.00 15.21 ?  246 ILE A CB  1 
ATOM   1943 C CG1 . ILE A 1 246 ? 14.464  18.847  15.429  1.00 16.03 ?  246 ILE A CG1 1 
ATOM   1944 C CG2 . ILE A 1 246 ? 13.127  20.858  14.622  1.00 15.48 ?  246 ILE A CG2 1 
ATOM   1945 C CD1 . ILE A 1 246 ? 15.816  19.539  15.584  1.00 18.87 ?  246 ILE A CD1 1 
ATOM   1946 N N   . ILE A 1 247 ? 10.140  19.141  13.302  1.00 13.93 ?  247 ILE A N   1 
ATOM   1947 C CA  . ILE A 1 247 ? 9.151   19.396  12.254  1.00 14.92 ?  247 ILE A CA  1 
ATOM   1948 C C   . ILE A 1 247 ? 8.355   20.645  12.617  1.00 15.36 ?  247 ILE A C   1 
ATOM   1949 O O   . ILE A 1 247 ? 7.418   20.571  13.429  1.00 15.02 ?  247 ILE A O   1 
ATOM   1950 C CB  . ILE A 1 247 ? 8.218   18.189  12.053  1.00 15.70 ?  247 ILE A CB  1 
ATOM   1951 C CG1 . ILE A 1 247 ? 9.018   16.921  11.753  1.00 17.27 ?  247 ILE A CG1 1 
ATOM   1952 C CG2 . ILE A 1 247 ? 7.258   18.449  10.887  1.00 14.50 ?  247 ILE A CG2 1 
ATOM   1953 C CD1 . ILE A 1 247 ? 8.176   15.643  11.888  1.00 16.27 ?  247 ILE A CD1 1 
ATOM   1954 N N   . PRO A 1 248 ? 8.691   21.807  12.060  1.00 15.16 ?  248 PRO A N   1 
ATOM   1955 C CA  . PRO A 1 248 ? 7.971   23.031  12.454  1.00 14.49 ?  248 PRO A CA  1 
ATOM   1956 C C   . PRO A 1 248 ? 6.486   23.012  12.139  1.00 15.14 ?  248 PRO A C   1 
ATOM   1957 O O   . PRO A 1 248 ? 5.685   23.548  12.919  1.00 16.61 ?  248 PRO A O   1 
ATOM   1958 C CB  . PRO A 1 248 ? 8.704   24.118  11.666  1.00 15.42 ?  248 PRO A CB  1 
ATOM   1959 C CG  . PRO A 1 248 ? 10.113  23.577  11.568  1.00 14.90 ?  248 PRO A CG  1 
ATOM   1960 C CD  . PRO A 1 248 ? 9.932   22.107  11.328  1.00 14.23 ?  248 PRO A CD  1 
ATOM   1961 N N   . ASN A 1 249 ? 6.092   22.424  11.027  1.00 14.06 ?  249 ASN A N   1 
ATOM   1962 C CA  . ASN A 1 249 ? 4.681   22.432  10.647  1.00 15.59 ?  249 ASN A CA  1 
ATOM   1963 C C   . ASN A 1 249 ? 3.915   21.489  11.562  1.00 17.51 ?  249 ASN A C   1 
ATOM   1964 O O   . ASN A 1 249 ? 4.212   20.291  11.579  1.00 16.52 ?  249 ASN A O   1 
ATOM   1965 C CB  . ASN A 1 249 ? 4.515   22.008  9.196   1.00 14.81 ?  249 ASN A CB  1 
ATOM   1966 C CG  . ASN A 1 249 ? 3.080   22.120  8.722   1.00 22.21 ?  249 ASN A CG  1 
ATOM   1967 O OD1 . ASN A 1 249 ? 2.199   21.430  9.219   1.00 20.34 ?  249 ASN A OD1 1 
ATOM   1968 N ND2 . ASN A 1 249 ? 2.839   22.999  7.760   1.00 27.15 ?  249 ASN A ND2 1 
ATOM   1969 N N   . PRO A 1 250 ? 2.916   21.970  12.311  1.00 16.42 ?  250 PRO A N   1 
ATOM   1970 C CA  . PRO A 1 250 ? 2.246   21.094  13.284  1.00 17.92 ?  250 PRO A CA  1 
ATOM   1971 C C   . PRO A 1 250 ? 1.422   19.986  12.649  1.00 17.54 ?  250 PRO A C   1 
ATOM   1972 O O   . PRO A 1 250 ? 1.294   18.910  13.250  1.00 16.74 ?  250 PRO A O   1 
ATOM   1973 C CB  . PRO A 1 250 ? 1.357   22.069  14.067  1.00 17.91 ?  250 PRO A CB  1 
ATOM   1974 C CG  . PRO A 1 250 ? 1.085   23.151  13.104  1.00 21.69 ?  250 PRO A CG  1 
ATOM   1975 C CD  . PRO A 1 250 ? 2.372   23.336  12.338  1.00 19.26 ?  250 PRO A CD  1 
ATOM   1976 N N   . ASP A 1 251 ? 0.853   20.210  11.464  1.00 18.55 ?  251 ASP A N   1 
ATOM   1977 C CA  . ASP A 1 251 ? 0.071   19.156  10.825  1.00 20.89 ?  251 ASP A CA  1 
ATOM   1978 C C   . ASP A 1 251 ? 0.980   18.035  10.334  1.00 18.90 ?  251 ASP A C   1 
ATOM   1979 O O   . ASP A 1 251 ? 0.711   16.847  10.563  1.00 16.34 ?  251 ASP A O   1 
ATOM   1980 C CB  . ASP A 1 251 ? -0.749  19.736  9.678   1.00 20.66 ?  251 ASP A CB  1 
ATOM   1981 C CG  . ASP A 1 251 ? -2.039  20.420  10.154  1.00 28.88 ?  251 ASP A CG  1 
ATOM   1982 O OD1 . ASP A 1 251 ? -2.276  20.506  11.383  1.00 27.75 ?  251 ASP A OD1 1 
ATOM   1983 O OD2 . ASP A 1 251 ? -2.821  20.877  9.289   1.00 38.87 -1 251 ASP A OD2 1 
ATOM   1984 N N   . LEU A 1 252 ? 2.082   18.393  9.697   1.00 17.81 ?  252 LEU A N   1 
ATOM   1985 C CA  . LEU A 1 252 ? 3.073   17.370  9.285   1.00 17.76 ?  252 LEU A CA  1 
ATOM   1986 C C   . LEU A 1 252 ? 3.633   16.677  10.519  1.00 16.25 ?  252 LEU A C   1 
ATOM   1987 O O   . LEU A 1 252 ? 3.842   15.494  10.463  1.00 16.22 ?  252 LEU A O   1 
ATOM   1988 C CB  . LEU A 1 252 ? 4.204   18.107  8.578   1.00 18.72 ?  252 LEU A CB  1 
ATOM   1989 C CG  . LEU A 1 252 ? 4.775   17.496  7.310   1.00 24.77 ?  252 LEU A CG  1 
ATOM   1990 C CD1 . LEU A 1 252 ? 3.673   17.201  6.311   1.00 23.20 ?  252 LEU A CD1 1 
ATOM   1991 C CD2 . LEU A 1 252 ? 5.766   18.480  6.722   1.00 21.38 ?  252 LEU A CD2 1 
ATOM   1992 N N   . ARG A 1 253 ? 3.886   17.448  11.566  1.00 16.25 ?  253 ARG A N   1 
ATOM   1993 C CA  . ARG A 1 253 ? 4.455   16.873  12.781  1.00 16.21 ?  253 ARG A CA  1 
ATOM   1994 C C   . ARG A 1 253 ? 3.539   15.811  13.375  1.00 16.85 ?  253 ARG A C   1 
ATOM   1995 O O   . ARG A 1 253 ? 3.994   14.738  13.786  1.00 14.60 ?  253 ARG A O   1 
ATOM   1996 C CB  . ARG A 1 253 ? 4.714   17.986  13.804  1.00 16.21 ?  253 ARG A CB  1 
ATOM   1997 C CG  . ARG A 1 253 ? 5.497   17.509  15.029  1.00 18.72 ?  253 ARG A CG  1 
ATOM   1998 C CD  . ARG A 1 253 ? 5.997   18.666  15.867  1.00 17.61 ?  253 ARG A CD  1 
ATOM   1999 N NE  . ARG A 1 253 ? 4.905   19.430  16.453  1.00 20.53 ?  253 ARG A NE  1 
ATOM   2000 C CZ  . ARG A 1 253 ? 4.623   20.697  16.167  1.00 16.80 ?  253 ARG A CZ  1 
ATOM   2001 N NH1 . ARG A 1 253 ? 5.347   21.378  15.289  1.00 15.92 1  253 ARG A NH1 1 
ATOM   2002 N NH2 . ARG A 1 253 ? 3.602   21.283  16.767  1.00 18.92 ?  253 ARG A NH2 1 
ATOM   2003 N N   . ALA A 1 254 ? 2.240   16.110  13.455  1.00 16.05 ?  254 ALA A N   1 
ATOM   2004 C CA  . ALA A 1 254 ? 1.285   15.143  13.979  1.00 17.45 ?  254 ALA A CA  1 
ATOM   2005 C C   . ALA A 1 254 ? 1.286   13.870  13.146  1.00 16.14 ?  254 ALA A C   1 
ATOM   2006 O O   . ALA A 1 254 ? 1.286   12.759  13.686  1.00 17.39 ?  254 ALA A O   1 
ATOM   2007 C CB  . ALA A 1 254 ? -0.116  15.755  14.016  1.00 19.22 ?  254 ALA A CB  1 
ATOM   2008 N N   . ARG A 1 255 ? 1.278   14.016  11.821  1.00 13.95 ?  255 ARG A N   1 
ATOM   2009 C CA  . ARG A 1 255 ? 1.223   12.848  10.946  1.00 15.48 ?  255 ARG A CA  1 
ATOM   2010 C C   . ARG A 1 255 ? 2.513   12.043  11.016  1.00 16.41 ?  255 ARG A C   1 
ATOM   2011 O O   . ARG A 1 255 ? 2.477   10.805  11.041  1.00 15.79 ?  255 ARG A O   1 
ATOM   2012 C CB  . ARG A 1 255 ? 0.923   13.292  9.515   1.00 15.44 ?  255 ARG A CB  1 
ATOM   2013 C CG  . ARG A 1 255 ? -0.460  13.958  9.377   1.00 16.60 ?  255 ARG A CG  1 
ATOM   2014 C CD  . ARG A 1 255 ? -0.579  14.692  8.075   1.00 18.28 ?  255 ARG A CD  1 
ATOM   2015 N NE  . ARG A 1 255 ? -0.440  13.774  6.952   1.00 20.24 ?  255 ARG A NE  1 
ATOM   2016 C CZ  . ARG A 1 255 ? -0.033  14.126  5.738   1.00 22.81 ?  255 ARG A CZ  1 
ATOM   2017 N NH1 . ARG A 1 255 ? 0.283   15.386  5.474   1.00 23.16 1  255 ARG A NH1 1 
ATOM   2018 N NH2 . ARG A 1 255 ? 0.054   13.214  4.785   1.00 23.80 ?  255 ARG A NH2 1 
ATOM   2019 N N   . ALA A 1 256 ? 3.660   12.719  11.070  1.00 16.95 ?  256 ALA A N   1 
ATOM   2020 C CA  . ALA A 1 256 ? 4.918   11.994  11.205  1.00 15.97 ?  256 ALA A CA  1 
ATOM   2021 C C   . ALA A 1 256 ? 4.988   11.245  12.532  1.00 15.42 ?  256 ALA A C   1 
ATOM   2022 O O   . ALA A 1 256 ? 5.408   10.081  12.574  1.00 15.90 ?  256 ALA A O   1 
ATOM   2023 C CB  . ALA A 1 256 ? 6.098   12.957  11.048  1.00 15.90 ?  256 ALA A CB  1 
ATOM   2024 N N   . GLU A 1 257 ? 4.555   11.882  13.624  1.00 15.78 ?  257 GLU A N   1 
ATOM   2025 C CA  . GLU A 1 257 ? 4.601   11.237  14.932  1.00 15.22 ?  257 GLU A CA  1 
ATOM   2026 C C   . GLU A 1 257 ? 3.741   9.981   14.951  1.00 20.33 ?  257 GLU A C   1 
ATOM   2027 O O   . GLU A 1 257 ? 4.151   8.942   15.484  1.00 19.09 ?  257 GLU A O   1 
ATOM   2028 C CB  . GLU A 1 257 ? 4.144   12.221  16.012  1.00 20.56 ?  257 GLU A CB  1 
ATOM   2029 C CG  . GLU A 1 257 ? 4.031   11.620  17.402  1.00 23.88 ?  257 GLU A CG  1 
ATOM   2030 C CD  . GLU A 1 257 ? 3.955   12.682  18.498  1.00 30.02 ?  257 GLU A CD  1 
ATOM   2031 O OE1 . GLU A 1 257 ? 4.100   12.325  19.689  1.00 32.47 ?  257 GLU A OE1 1 
ATOM   2032 O OE2 . GLU A 1 257 ? 3.755   13.875  18.167  1.00 37.27 -1 257 GLU A OE2 1 
ATOM   2033 N N   . GLU A 1 258 ? 2.544   10.054  14.362  1.00 16.57 ?  258 GLU A N   1 
ATOM   2034 C CA  . GLU A 1 258 ? 1.704   8.868   14.262  1.00 20.83 ?  258 GLU A CA  1 
ATOM   2035 C C   . GLU A 1 258 ? 2.370   7.788   13.413  1.00 20.20 ?  258 GLU A C   1 
ATOM   2036 O O   . GLU A 1 258 ? 2.280   6.598   13.733  1.00 20.84 ?  258 GLU A O   1 
ATOM   2037 C CB  . GLU A 1 258 ? 0.334   9.252   13.694  1.00 20.05 ?  258 GLU A CB  1 
ATOM   2038 C CG  . GLU A 1 258 ? -0.637  8.087   13.494  1.00 24.33 ?  258 GLU A CG  1 
ATOM   2039 C CD  . GLU A 1 258 ? -1.163  7.496   14.797  1.00 29.89 ?  258 GLU A CD  1 
ATOM   2040 O OE1 . GLU A 1 258 ? -1.944  6.512   14.732  1.00 31.89 ?  258 GLU A OE1 1 
ATOM   2041 O OE2 . GLU A 1 258 ? -0.806  8.002   15.887  1.00 28.32 -1 258 GLU A OE2 1 
ATOM   2042 N N   . SER A 1 259 ? 3.054   8.177   12.332  1.00 18.61 ?  259 SER A N   1 
ATOM   2043 C CA  . SER A 1 259 ? 3.721   7.172   11.511  1.00 19.50 ?  259 SER A CA  1 
ATOM   2044 C C   . SER A 1 259 ? 4.846   6.489   12.285  1.00 19.91 ?  259 SER A C   1 
ATOM   2045 O O   . SER A 1 259 ? 5.061   5.279   12.126  1.00 16.48 ?  259 SER A O   1 
ATOM   2046 C CB  . SER A 1 259 ? 4.248   7.785   10.211  1.00 15.68 ?  259 SER A CB  1 
ATOM   2047 O OG  . SER A 1 259 ? 5.475   8.476   10.406  1.00 21.89 ?  259 SER A OG  1 
ATOM   2048 N N   . PHE A 1 260 ? 5.562   7.237   13.135  1.00 14.51 ?  260 PHE A N   1 
ATOM   2049 C CA  . PHE A 1 260 ? 6.620   6.632   13.943  1.00 15.67 ?  260 PHE A CA  1 
ATOM   2050 C C   . PHE A 1 260 ? 6.036   5.611   14.902  1.00 16.26 ?  260 PHE A C   1 
ATOM   2051 O O   . PHE A 1 260 ? 6.555   4.499   15.047  1.00 16.23 ?  260 PHE A O   1 
ATOM   2052 C CB  . PHE A 1 260 ? 7.386   7.693   14.739  1.00 14.21 ?  260 PHE A CB  1 
ATOM   2053 C CG  . PHE A 1 260 ? 8.101   8.701   13.891  1.00 14.82 ?  260 PHE A CG  1 
ATOM   2054 C CD1 . PHE A 1 260 ? 8.256   8.497   12.527  1.00 13.75 ?  260 PHE A CD1 1 
ATOM   2055 C CD2 . PHE A 1 260 ? 8.619   9.859   14.461  1.00 13.56 ?  260 PHE A CD2 1 
ATOM   2056 C CE1 . PHE A 1 260 ? 8.898   9.431   11.738  1.00 15.32 ?  260 PHE A CE1 1 
ATOM   2057 C CE2 . PHE A 1 260 ? 9.252   10.802  13.671  1.00 14.30 ?  260 PHE A CE2 1 
ATOM   2058 C CZ  . PHE A 1 260 ? 9.397   10.580  12.309  1.00 16.28 ?  260 PHE A CZ  1 
ATOM   2059 N N   . PHE A 1 261 ? 4.959   5.989   15.587  1.00 18.30 ?  261 PHE A N   1 
ATOM   2060 C CA  . PHE A 1 261 ? 4.325   5.067   16.519  1.00 19.99 ?  261 PHE A CA  1 
ATOM   2061 C C   . PHE A 1 261 ? 3.853   3.814   15.801  1.00 20.21 ?  261 PHE A C   1 
ATOM   2062 O O   . PHE A 1 261 ? 4.038   2.698   16.299  1.00 22.56 ?  261 PHE A O   1 
ATOM   2063 C CB  . PHE A 1 261 ? 3.169   5.761   17.238  1.00 21.88 ?  261 PHE A CB  1 
ATOM   2064 C CG  . PHE A 1 261 ? 3.614   6.663   18.363  1.00 29.84 ?  261 PHE A CG  1 
ATOM   2065 C CD1 . PHE A 1 261 ? 4.528   6.213   19.313  1.00 28.81 ?  261 PHE A CD1 1 
ATOM   2066 C CD2 . PHE A 1 261 ? 3.130   7.965   18.468  1.00 31.86 ?  261 PHE A CD2 1 
ATOM   2067 C CE1 . PHE A 1 261 ? 4.941   7.039   20.347  1.00 31.16 ?  261 PHE A CE1 1 
ATOM   2068 C CE2 . PHE A 1 261 ? 3.539   8.794   19.499  1.00 29.56 ?  261 PHE A CE2 1 
ATOM   2069 C CZ  . PHE A 1 261 ? 4.448   8.333   20.436  1.00 29.84 ?  261 PHE A CZ  1 
ATOM   2070 N N   . LEU A 1 262 ? 3.278   3.976   14.610  1.00 18.51 ?  262 LEU A N   1 
ATOM   2071 C CA  . LEU A 1 262 ? 2.760   2.817   13.894  1.00 21.82 ?  262 LEU A CA  1 
ATOM   2072 C C   . LEU A 1 262 ? 3.880   1.887   13.458  1.00 21.25 ?  262 LEU A C   1 
ATOM   2073 O O   . LEU A 1 262 ? 3.735   0.663   13.533  1.00 22.83 ?  262 LEU A O   1 
ATOM   2074 C CB  . LEU A 1 262 ? 1.921   3.271   12.703  1.00 24.93 ?  262 LEU A CB  1 
ATOM   2075 C CG  . LEU A 1 262 ? 0.493   3.597   13.157  1.00 27.55 ?  262 LEU A CG  1 
ATOM   2076 C CD1 . LEU A 1 262 ? -0.345  4.113   12.010  1.00 26.88 ?  262 LEU A CD1 1 
ATOM   2077 C CD2 . LEU A 1 262 ? -0.157  2.369   13.782  1.00 26.10 ?  262 LEU A CD2 1 
ATOM   2078 N N   . ALA A 1 263 ? 5.018   2.444   13.035  1.00 18.18 ?  263 ALA A N   1 
ATOM   2079 C CA  . ALA A 1 263 ? 6.163   1.635   12.643  1.00 18.50 ?  263 ALA A CA  1 
ATOM   2080 C C   . ALA A 1 263 ? 6.884   0.989   13.824  1.00 18.89 ?  263 ALA A C   1 
ATOM   2081 O O   . ALA A 1 263 ? 7.731   0.116   13.601  1.00 17.76 ?  263 ALA A O   1 
ATOM   2082 C CB  . ALA A 1 263 ? 7.157   2.484   11.852  1.00 19.78 ?  263 ALA A CB  1 
ATOM   2083 N N   . GLY A 1 264 ? 6.584   1.390   15.057  1.00 18.76 ?  264 GLY A N   1 
ATOM   2084 C CA  . GLY A 1 264 ? 7.301   0.877   16.207  1.00 21.05 ?  264 GLY A CA  1 
ATOM   2085 C C   . GLY A 1 264 ? 8.606   1.582   16.499  1.00 19.21 ?  264 GLY A C   1 
ATOM   2086 O O   . GLY A 1 264 ? 9.492   0.999   17.127  1.00 19.96 ?  264 GLY A O   1 
ATOM   2087 N N   . ILE A 1 265 ? 8.760   2.827   16.062  1.00 13.75 ?  265 ILE A N   1 
ATOM   2088 C CA  . ILE A 1 265 ? 10.005  3.553   16.250  1.00 14.39 ?  265 ILE A CA  1 
ATOM   2089 C C   . ILE A 1 265 ? 9.798   4.834   17.037  1.00 16.06 ?  265 ILE A C   1 
ATOM   2090 O O   . ILE A 1 265 ? 10.676  5.695   17.052  1.00 15.90 ?  265 ILE A O   1 
ATOM   2091 C CB  . ILE A 1 265 ? 10.688  3.845   14.899  1.00 19.52 ?  265 ILE A CB  1 
ATOM   2092 C CG1 . ILE A 1 265 ? 9.843   4.813   14.057  1.00 16.44 ?  265 ILE A CG1 1 
ATOM   2093 C CG2 . ILE A 1 265 ? 10.967  2.543   14.145  1.00 17.38 ?  265 ILE A CG2 1 
ATOM   2094 C CD1 . ILE A 1 265 ? 10.509  5.188   12.702  1.00 17.09 ?  265 ILE A CD1 1 
ATOM   2095 N N   . GLY A 1 266 ? 8.650   4.985   17.687  1.00 14.35 ?  266 GLY A N   1 
ATOM   2096 C CA  . GLY A 1 266 ? 8.359   6.189   18.430  1.00 14.81 ?  266 GLY A CA  1 
ATOM   2097 C C   . GLY A 1 266 ? 8.551   6.093   19.928  1.00 18.73 ?  266 GLY A C   1 
ATOM   2098 O O   . GLY A 1 266 ? 8.333   7.086   20.628  1.00 17.25 ?  266 GLY A O   1 
ATOM   2099 N N   . GLU A 1 267 ? 8.952   4.936   20.446  1.00 16.56 ?  267 GLU A N   1 
ATOM   2100 C CA  . GLU A 1 267 ? 9.081   4.761   21.885  1.00 20.52 ?  267 GLU A CA  1 
ATOM   2101 C C   . GLU A 1 267 ? 10.507  4.375   22.254  1.00 19.25 ?  267 GLU A C   1 
ATOM   2102 O O   . GLU A 1 267 ? 11.107  3.508   21.595  1.00 16.51 ?  267 GLU A O   1 
ATOM   2103 C CB  . GLU A 1 267 ? 8.090   3.703   22.395  1.00 20.76 ?  267 GLU A CB  1 
ATOM   2104 C CG  . GLU A 1 267 ? 6.648   4.074   22.058  1.00 28.37 ?  267 GLU A CG  1 
ATOM   2105 C CD  . GLU A 1 267 ? 5.611   3.357   22.901  1.00 38.39 ?  267 GLU A CD  1 
ATOM   2106 O OE1 . GLU A 1 267 ? 5.986   2.648   23.864  1.00 42.69 ?  267 GLU A OE1 1 
ATOM   2107 O OE2 . GLU A 1 267 ? 4.409   3.522   22.599  1.00 44.58 -1 267 GLU A OE2 1 
ATOM   2108 N N   . PRO A 1 268 ? 11.084  4.993   23.283  1.00 15.69 ?  268 PRO A N   1 
ATOM   2109 C CA  . PRO A 1 268 ? 12.499  4.766   23.593  1.00 16.50 ?  268 PRO A CA  1 
ATOM   2110 C C   . PRO A 1 268 ? 12.734  3.423   24.265  1.00 16.42 ?  268 PRO A C   1 
ATOM   2111 O O   . PRO A 1 268 ? 11.907  2.920   25.033  1.00 15.74 ?  268 PRO A O   1 
ATOM   2112 C CB  . PRO A 1 268 ? 12.836  5.919   24.546  1.00 16.57 ?  268 PRO A CB  1 
ATOM   2113 C CG  . PRO A 1 268 ? 11.509  6.276   25.187  1.00 17.78 ?  268 PRO A CG  1 
ATOM   2114 C CD  . PRO A 1 268 ? 10.479  6.046   24.121  1.00 16.91 ?  268 PRO A CD  1 
ATOM   2115 N N   . ASN A 1 269 ? 13.889  2.843   23.959  1.00 14.24 ?  269 ASN A N   1 
ATOM   2116 C CA  . ASN A 1 269 ? 14.356  1.706   24.723  1.00 14.50 ?  269 ASN A CA  1 
ATOM   2117 C C   . ASN A 1 269 ? 14.893  2.199   26.068  1.00 15.50 ?  269 ASN A C   1 
ATOM   2118 O O   . ASN A 1 269 ? 14.872  3.394   26.379  1.00 15.66 ?  269 ASN A O   1 
ATOM   2119 C CB  . ASN A 1 269 ? 15.399  0.911   23.932  1.00 16.13 ?  269 ASN A CB  1 
ATOM   2120 C CG  . ASN A 1 269 ? 16.686  1.689   23.686  1.00 16.54 ?  269 ASN A CG  1 
ATOM   2121 O OD1 . ASN A 1 269 ? 17.243  2.288   24.599  1.00 16.62 ?  269 ASN A OD1 1 
ATOM   2122 N ND2 . ASN A 1 269 ? 17.188  1.641   22.448  1.00 14.93 ?  269 ASN A ND2 1 
ATOM   2123 N N   . LEU A 1 270 ? 15.434  1.269   26.855  1.00 14.20 ?  270 LEU A N   1 
ATOM   2124 C CA  . LEU A 1 270 ? 15.764  1.538   28.249  1.00 15.10 ?  270 LEU A CA  1 
ATOM   2125 C C   . LEU A 1 270 ? 16.927  2.518   28.433  1.00 16.32 ?  270 LEU A C   1 
ATOM   2126 O O   . LEU A 1 270 ? 17.091  3.052   29.532  1.00 16.47 ?  270 LEU A O   1 
ATOM   2127 C CB  . LEU A 1 270 ? 16.057  0.212   28.955  1.00 14.69 ?  270 LEU A CB  1 
ATOM   2128 C CG  . LEU A 1 270 ? 17.377  -0.552  28.756  1.00 15.38 ?  270 LEU A CG  1 
ATOM   2129 C CD1 . LEU A 1 270 ? 17.260  -1.881  29.466  1.00 16.90 ?  270 LEU A CD1 1 
ATOM   2130 C CD2 . LEU A 1 270 ? 17.782  -0.811  27.289  1.00 19.80 ?  270 LEU A CD2 1 
ATOM   2131 N N   . LEU A 1 271 ? 17.742  2.763   27.405  1.00 13.47 ?  271 LEU A N   1 
ATOM   2132 C CA  . LEU A 1 271 ? 18.874  3.670   27.541  1.00 14.29 ?  271 LEU A CA  1 
ATOM   2133 C C   . LEU A 1 271 ? 18.745  4.939   26.713  1.00 15.44 ?  271 LEU A C   1 
ATOM   2134 O O   . LEU A 1 271 ? 19.465  5.907   26.987  1.00 14.58 ?  271 LEU A O   1 
ATOM   2135 C CB  . LEU A 1 271 ? 20.184  2.952   27.169  1.00 15.75 ?  271 LEU A CB  1 
ATOM   2136 C CG  . LEU A 1 271 ? 20.645  1.896   28.186  1.00 16.49 ?  271 LEU A CG  1 
ATOM   2137 C CD1 . LEU A 1 271 ? 22.001  1.299   27.784  1.00 18.10 ?  271 LEU A CD1 1 
ATOM   2138 C CD2 . LEU A 1 271 ? 20.679  2.462   29.612  1.00 15.38 ?  271 LEU A CD2 1 
ATOM   2139 N N   . ALA A 1 272 ? 17.837  4.966   25.730  1.00 13.74 ?  272 ALA A N   1 
ATOM   2140 C CA  . ALA A 1 272 ? 17.810  6.053   24.751  1.00 13.95 ?  272 ALA A CA  1 
ATOM   2141 C C   . ALA A 1 272 ? 17.684  7.421   25.422  1.00 15.64 ?  272 ALA A C   1 
ATOM   2142 O O   . ALA A 1 272 ? 18.402  8.364   25.064  1.00 15.27 ?  272 ALA A O   1 
ATOM   2143 C CB  . ALA A 1 272 ? 16.668  5.840   23.758  1.00 15.16 ?  272 ALA A CB  1 
ATOM   2144 N N   . ILE A 1 273 ? 16.781  7.553   26.391  1.00 15.09 ?  273 ILE A N   1 
ATOM   2145 C CA  . ILE A 1 273 ? 16.494  8.865   26.979  1.00 15.05 ?  273 ILE A CA  1 
ATOM   2146 C C   . ILE A 1 273 ? 17.670  9.353   27.826  1.00 15.55 ?  273 ILE A C   1 
ATOM   2147 O O   . ILE A 1 273 ? 18.234  10.402  27.490  1.00 14.82 ?  273 ILE A O   1 
ATOM   2148 C CB  . ILE A 1 273 ? 15.182  8.866   27.790  1.00 15.83 ?  273 ILE A CB  1 
ATOM   2149 C CG1 . ILE A 1 273 ? 13.977  8.549   26.887  1.00 15.98 ?  273 ILE A CG1 1 
ATOM   2150 C CG2 . ILE A 1 273 ? 14.990  10.229  28.449  1.00 15.79 ?  273 ILE A CG2 1 
ATOM   2151 C CD1 . ILE A 1 273 ? 13.934  9.385   25.609  1.00 18.90 ?  273 ILE A CD1 1 
ATOM   2152 N N   . PRO A 1 274 ? 18.080  8.681   28.915  1.00 16.73 ?  274 PRO A N   1 
ATOM   2153 C CA  . PRO A 1 274 ? 19.194  9.243   29.704  1.00 15.98 ?  274 PRO A CA  1 
ATOM   2154 C C   . PRO A 1 274 ? 20.494  9.374   28.916  1.00 16.89 ?  274 PRO A C   1 
ATOM   2155 O O   . PRO A 1 274 ? 21.231  10.346  29.132  1.00 15.70 ?  274 PRO A O   1 
ATOM   2156 C CB  . PRO A 1 274 ? 19.343  8.258   30.870  1.00 18.76 ?  274 PRO A CB  1 
ATOM   2157 C CG  . PRO A 1 274 ? 18.755  6.968   30.364  1.00 18.52 ?  274 PRO A CG  1 
ATOM   2158 C CD  . PRO A 1 274 ? 17.614  7.393   29.482  1.00 14.91 ?  274 PRO A CD  1 
ATOM   2159 N N   . ALA A 1 275 ? 20.804  8.432   28.011  1.00 14.34 ?  275 ALA A N   1 
ATOM   2160 C CA  . ALA A 1 275 ? 22.056  8.530   27.258  1.00 15.19 ?  275 ALA A CA  1 
ATOM   2161 C C   . ALA A 1 275 ? 22.028  9.694   26.268  1.00 14.73 ?  275 ALA A C   1 
ATOM   2162 O O   . ALA A 1 275 ? 23.012  10.440  26.144  1.00 13.64 ?  275 ALA A O   1 
ATOM   2163 C CB  . ALA A 1 275 ? 22.354  7.209   26.544  1.00 16.54 ?  275 ALA A CB  1 
ATOM   2164 N N   . ALA A 1 276 ? 20.917  9.875   25.548  1.00 12.69 ?  276 ALA A N   1 
ATOM   2165 C CA  . ALA A 1 276 ? 20.861  10.991  24.605  1.00 14.31 ?  276 ALA A CA  1 
ATOM   2166 C C   . ALA A 1 276 ? 20.896  12.330  25.336  1.00 15.25 ?  276 ALA A C   1 
ATOM   2167 O O   . ALA A 1 276 ? 21.498  13.294  24.850  1.00 14.32 ?  276 ALA A O   1 
ATOM   2168 C CB  . ALA A 1 276 ? 19.610  10.889  23.739  1.00 14.28 ?  276 ALA A CB  1 
ATOM   2169 N N   . ILE A 1 277 ? 20.237  12.412  26.494  1.00 14.73 ?  277 ILE A N   1 
ATOM   2170 C CA  . ILE A 1 277 ? 20.236  13.647  27.274  1.00 15.16 ?  277 ILE A CA  1 
ATOM   2171 C C   . ILE A 1 277 ? 21.639  13.967  27.786  1.00 14.89 ?  277 ILE A C   1 
ATOM   2172 O O   . ILE A 1 277 ? 22.069  15.127  27.757  1.00 14.15 ?  277 ILE A O   1 
ATOM   2173 C CB  . ILE A 1 277 ? 19.216  13.543  28.428  1.00 16.63 ?  277 ILE A CB  1 
ATOM   2174 C CG1 . ILE A 1 277 ? 17.800  13.721  27.881  1.00 15.36 ?  277 ILE A CG1 1 
ATOM   2175 C CG2 . ILE A 1 277 ? 19.510  14.563  29.530  1.00 13.64 ?  277 ILE A CG2 1 
ATOM   2176 C CD1 . ILE A 1 277 ? 16.707  13.570  28.914  1.00 17.48 ?  277 ILE A CD1 1 
ATOM   2177 N N   . ALA A 1 278 ? 22.359  12.959  28.282  1.00 13.68 ?  278 ALA A N   1 
ATOM   2178 C CA  . ALA A 1 278 ? 23.725  13.197  28.738  1.00 16.82 ?  278 ALA A CA  1 
ATOM   2179 C C   . ALA A 1 278 ? 24.603  13.653  27.580  1.00 16.91 ?  278 ALA A C   1 
ATOM   2180 O O   . ALA A 1 278 ? 25.405  14.586  27.722  1.00 17.50 ?  278 ALA A O   1 
ATOM   2181 C CB  . ALA A 1 278 ? 24.303  11.938  29.387  1.00 15.71 ?  278 ALA A CB  1 
ATOM   2182 N N   . ALA A 1 279 ? 24.452  13.018  26.419  1.00 13.98 ?  279 ALA A N   1 
ATOM   2183 C CA  . ALA A 1 279 ? 25.226  13.417  25.250  1.00 16.13 ?  279 ALA A CA  1 
ATOM   2184 C C   . ALA A 1 279 ? 24.956  14.871  24.883  1.00 16.31 ?  279 ALA A C   1 
ATOM   2185 O O   . ALA A 1 279 ? 25.887  15.652  24.662  1.00 17.18 ?  279 ALA A O   1 
ATOM   2186 C CB  . ALA A 1 279 ? 24.899  12.501  24.077  1.00 14.59 ?  279 ALA A CB  1 
ATOM   2187 N N   . TYR A 1 280 ? 23.678  15.250  24.797  1.00 15.29 ?  280 TYR A N   1 
ATOM   2188 C CA  . TYR A 1 280 ? 23.329  16.586  24.341  1.00 15.78 ?  280 TYR A CA  1 
ATOM   2189 C C   . TYR A 1 280 ? 23.504  17.641  25.422  1.00 16.44 ?  280 TYR A C   1 
ATOM   2190 O O   . TYR A 1 280 ? 23.587  18.828  25.089  1.00 20.01 ?  280 TYR A O   1 
ATOM   2191 C CB  . TYR A 1 280 ? 21.892  16.599  23.824  1.00 13.89 ?  280 TYR A CB  1 
ATOM   2192 C CG  . TYR A 1 280 ? 21.733  16.015  22.436  1.00 16.29 ?  280 TYR A CG  1 
ATOM   2193 C CD1 . TYR A 1 280 ? 22.771  16.072  21.508  1.00 18.10 ?  280 TYR A CD1 1 
ATOM   2194 C CD2 . TYR A 1 280 ? 20.546  15.410  22.050  1.00 18.05 ?  280 TYR A CD2 1 
ATOM   2195 C CE1 . TYR A 1 280 ? 22.620  15.544  20.218  1.00 18.30 ?  280 TYR A CE1 1 
ATOM   2196 C CE2 . TYR A 1 280 ? 20.384  14.883  20.772  1.00 18.54 ?  280 TYR A CE2 1 
ATOM   2197 C CZ  . TYR A 1 280 ? 21.411  14.951  19.864  1.00 19.43 ?  280 TYR A CZ  1 
ATOM   2198 O OH  . TYR A 1 280 ? 21.232  14.421  18.602  1.00 18.81 ?  280 TYR A OH  1 
ATOM   2199 N N   . GLU A 1 281 ? 23.566  17.250  26.701  1.00 16.30 ?  281 GLU A N   1 
ATOM   2200 C CA  . GLU A 1 281 ? 23.831  18.222  27.754  1.00 18.88 ?  281 GLU A CA  1 
ATOM   2201 C C   . GLU A 1 281 ? 25.297  18.271  28.170  1.00 20.41 ?  281 GLU A C   1 
ATOM   2202 O O   . GLU A 1 281 ? 25.785  19.341  28.549  1.00 21.00 ?  281 GLU A O   1 
ATOM   2203 C CB  . GLU A 1 281 ? 22.963  17.930  28.985  1.00 21.77 ?  281 GLU A CB  1 
ATOM   2204 C CG  . GLU A 1 281 ? 21.467  18.202  28.769  1.00 20.65 ?  281 GLU A CG  1 
ATOM   2205 C CD  . GLU A 1 281 ? 21.122  19.697  28.664  1.00 31.37 ?  281 GLU A CD  1 
ATOM   2206 O OE1 . GLU A 1 281 ? 19.931  20.010  28.419  1.00 33.23 ?  281 GLU A OE1 1 
ATOM   2207 O OE2 . GLU A 1 281 ? 22.024  20.564  28.830  1.00 36.24 -1 281 GLU A OE2 1 
ATOM   2208 N N   . GLU A 1 282 ? 26.020  17.155  28.096  1.00 16.66 ?  282 GLU A N   1 
ATOM   2209 C CA  . GLU A 1 282 ? 27.374  17.094  28.629  1.00 18.59 ?  282 GLU A CA  1 
ATOM   2210 C C   . GLU A 1 282 ? 28.413  16.654  27.608  1.00 19.49 ?  282 GLU A C   1 
ATOM   2211 O O   . GLU A 1 282 ? 29.577  16.473  27.974  1.00 20.94 ?  282 GLU A O   1 
ATOM   2212 C CB  . GLU A 1 282 ? 27.424  16.153  29.837  1.00 20.83 ?  282 GLU A CB  1 
ATOM   2213 C CG  . GLU A 1 282 ? 26.505  16.566  30.965  1.00 25.69 ?  282 GLU A CG  1 
ATOM   2214 C CD  . GLU A 1 282 ? 26.490  15.543  32.080  1.00 34.41 ?  282 GLU A CD  1 
ATOM   2215 O OE1 . GLU A 1 282 ? 27.529  15.413  32.774  1.00 37.96 ?  282 GLU A OE1 1 
ATOM   2216 O OE2 . GLU A 1 282 ? 25.448  14.861  32.256  1.00 37.53 -1 282 GLU A OE2 1 
ATOM   2217 N N   . GLY A 1 283 ? 28.043  16.495  26.346  1.00 17.19 ?  283 GLY A N   1 
ATOM   2218 C CA  . GLY A 1 283 ? 29.020  15.995  25.402  1.00 16.74 ?  283 GLY A CA  1 
ATOM   2219 C C   . GLY A 1 283 ? 29.835  17.041  24.679  1.00 17.43 ?  283 GLY A C   1 
ATOM   2220 O O   . GLY A 1 283 ? 30.622  16.692  23.794  1.00 16.27 ?  283 GLY A O   1 
ATOM   2221 N N   . HIS A 1 284 ? 29.682  18.316  25.038  1.00 15.85 ?  284 HIS A N   1 
ATOM   2222 C CA  . HIS A 1 284 ? 30.338  19.396  24.305  1.00 15.44 ?  284 HIS A CA  1 
ATOM   2223 C C   . HIS A 1 284 ? 31.849  19.268  24.348  1.00 15.81 ?  284 HIS A C   1 
ATOM   2224 O O   . HIS A 1 284 ? 32.526  19.421  23.324  1.00 17.23 ?  284 HIS A O   1 
ATOM   2225 C CB  . HIS A 1 284 ? 29.925  20.736  24.894  1.00 19.12 ?  284 HIS A CB  1 
ATOM   2226 C CG  . HIS A 1 284 ? 28.470  21.021  24.748  1.00 19.10 ?  284 HIS A CG  1 
ATOM   2227 N ND1 . HIS A 1 284 ? 27.916  21.439  23.559  1.00 20.95 ?  284 HIS A ND1 1 
ATOM   2228 C CD2 . HIS A 1 284 ? 27.447  20.906  25.627  1.00 22.00 ?  284 HIS A CD2 1 
ATOM   2229 C CE1 . HIS A 1 284 ? 26.615  21.604  23.721  1.00 21.18 ?  284 HIS A CE1 1 
ATOM   2230 N NE2 . HIS A 1 284 ? 26.305  21.283  24.964  1.00 20.15 ?  284 HIS A NE2 1 
ATOM   2231 N N   . ASN A 1 285 ? 32.394  19.028  25.537  1.00 16.30 ?  285 ASN A N   1 
ATOM   2232 C CA  . ASN A 1 285 ? 33.841  18.984  25.697  1.00 16.58 ?  285 ASN A CA  1 
ATOM   2233 C C   . ASN A 1 285 ? 34.432  17.783  24.977  1.00 14.94 ?  285 ASN A C   1 
ATOM   2234 O O   . ASN A 1 285 ? 35.476  17.896  24.332  1.00 15.83 ?  285 ASN A O   1 
ATOM   2235 C CB  . ASN A 1 285 ? 34.196  18.950  27.180  1.00 19.09 ?  285 ASN A CB  1 
ATOM   2236 C CG  . ASN A 1 285 ? 33.903  20.263  27.878  1.00 19.63 ?  285 ASN A CG  1 
ATOM   2237 O OD1 . ASN A 1 285 ? 33.989  21.330  27.279  1.00 25.37 ?  285 ASN A OD1 1 
ATOM   2238 N ND2 . ASN A 1 285 ? 33.561  20.188  29.154  1.00 27.21 ?  285 ASN A ND2 1 
ATOM   2239 N N   . TRP A 1 286 ? 33.778  16.623  25.081  1.00 16.04 ?  286 TRP A N   1 
ATOM   2240 C CA  . TRP A 1 286 ? 34.260  15.433  24.386  1.00 15.14 ?  286 TRP A CA  1 
ATOM   2241 C C   . TRP A 1 286 ? 34.278  15.653  22.881  1.00 13.90 ?  286 TRP A C   1 
ATOM   2242 O O   . TRP A 1 286 ? 35.266  15.327  22.207  1.00 14.40 ?  286 TRP A O   1 
ATOM   2243 C CB  . TRP A 1 286 ? 33.393  14.220  24.736  1.00 14.84 ?  286 TRP A CB  1 
ATOM   2244 C CG  . TRP A 1 286 ? 33.871  12.957  24.093  1.00 14.87 ?  286 TRP A CG  1 
ATOM   2245 C CD1 . TRP A 1 286 ? 34.817  12.099  24.581  1.00 17.23 ?  286 TRP A CD1 1 
ATOM   2246 C CD2 . TRP A 1 286 ? 33.454  12.416  22.831  1.00 14.17 ?  286 TRP A CD2 1 
ATOM   2247 N NE1 . TRP A 1 286 ? 35.007  11.052  23.708  1.00 14.81 ?  286 TRP A NE1 1 
ATOM   2248 C CE2 . TRP A 1 286 ? 34.184  11.224  22.624  1.00 14.92 ?  286 TRP A CE2 1 
ATOM   2249 C CE3 . TRP A 1 286 ? 32.535  12.820  21.860  1.00 14.55 ?  286 TRP A CE3 1 
ATOM   2250 C CZ2 . TRP A 1 286 ? 34.017  10.432  21.487  1.00 14.18 ?  286 TRP A CZ2 1 
ATOM   2251 C CZ3 . TRP A 1 286 ? 32.379  12.039  20.723  1.00 14.53 ?  286 TRP A CZ3 1 
ATOM   2252 C CH2 . TRP A 1 286 ? 33.105  10.857  20.551  1.00 14.38 ?  286 TRP A CH2 1 
ATOM   2253 N N   . LEU A 1 287 ? 33.187  16.203  22.337  1.00 13.32 ?  287 LEU A N   1 
ATOM   2254 C CA  . LEU A 1 287 ? 33.117  16.474  20.901  1.00 12.07 ?  287 LEU A CA  1 
ATOM   2255 C C   . LEU A 1 287 ? 34.206  17.446  20.468  1.00 15.30 ?  287 LEU A C   1 
ATOM   2256 O O   . LEU A 1 287 ? 34.808  17.279  19.403  1.00 14.23 ?  287 LEU A O   1 
ATOM   2257 C CB  . LEU A 1 287 ? 31.746  17.027  20.528  1.00 13.32 ?  287 LEU A CB  1 
ATOM   2258 C CG  . LEU A 1 287 ? 31.559  17.450  19.064  1.00 15.11 ?  287 LEU A CG  1 
ATOM   2259 C CD1 . LEU A 1 287 ? 31.895  16.299  18.101  1.00 13.51 ?  287 LEU A CD1 1 
ATOM   2260 C CD2 . LEU A 1 287 ? 30.143  17.964  18.819  1.00 15.13 ?  287 LEU A CD2 1 
ATOM   2261 N N   . ARG A 1 288 ? 34.463  18.486  21.265  1.00 13.74 ?  288 ARG A N   1 
ATOM   2262 C CA  . ARG A 1 288 ? 35.553  19.396  20.912  1.00 17.84 ?  288 ARG A CA  1 
ATOM   2263 C C   . ARG A 1 288 ? 36.877  18.644  20.760  1.00 17.37 ?  288 ARG A C   1 
ATOM   2264 O O   . ARG A 1 288 ? 37.626  18.870  19.804  1.00 15.44 ?  288 ARG A O   1 
ATOM   2265 C CB  . ARG A 1 288 ? 35.678  20.505  21.950  1.00 18.94 ?  288 ARG A CB  1 
ATOM   2266 C CG  . ARG A 1 288 ? 36.845  21.439  21.674  1.00 20.82 ?  288 ARG A CG  1 
ATOM   2267 C CD  . ARG A 1 288 ? 36.916  22.517  22.724  1.00 24.07 ?  288 ARG A CD  1 
ATOM   2268 N NE  . ARG A 1 288 ? 37.786  23.615  22.295  1.00 31.66 ?  288 ARG A NE  1 
ATOM   2269 C CZ  . ARG A 1 288 ? 38.076  24.669  23.053  1.00 33.70 ?  288 ARG A CZ  1 
ATOM   2270 N NH1 . ARG A 1 288 ? 37.576  24.762  24.287  1.00 36.27 1  288 ARG A NH1 1 
ATOM   2271 N NH2 . ARG A 1 288 ? 38.872  25.622  22.586  1.00 28.34 ?  288 ARG A NH2 1 
ATOM   2272 N N   . GLU A 1 289 ? 37.159  17.727  21.667  1.00 14.93 ?  289 GLU A N   1 
ATOM   2273 C CA  . GLU A 1 289 ? 38.417  16.952  21.589  1.00 16.15 ?  289 GLU A CA  1 
ATOM   2274 C C   . GLU A 1 289 ? 38.356  15.979  20.404  1.00 17.21 ?  289 GLU A C   1 
ATOM   2275 O O   . GLU A 1 289 ? 39.360  15.822  19.728  1.00 16.72 ?  289 GLU A O   1 
ATOM   2276 C CB  . GLU A 1 289 ? 38.672  16.264  22.927  1.00 18.92 ?  289 GLU A CB  1 
ATOM   2277 C CG  . GLU A 1 289 ? 39.008  17.207  24.053  1.00 20.32 ?  289 GLU A CG  1 
ATOM   2278 C CD  . GLU A 1 289 ? 39.880  16.553  25.106  1.00 31.94 ?  289 GLU A CD  1 
ATOM   2279 O OE1 . GLU A 1 289 ? 40.491  17.283  25.895  1.00 39.01 ?  289 GLU A OE1 1 
ATOM   2280 O OE2 . GLU A 1 289 ? 39.959  15.318  25.121  1.00 30.01 -1 289 GLU A OE2 1 
ATOM   2281 N N   . LEU A 1 290 ? 37.200  15.336  20.203  1.00 14.48 ?  290 LEU A N   1 
ATOM   2282 C CA  . LEU A 1 290 ? 37.049  14.453  19.044  1.00 15.79 ?  290 LEU A CA  1 
ATOM   2283 C C   . LEU A 1 290 ? 37.378  15.182  17.744  1.00 14.68 ?  290 LEU A C   1 
ATOM   2284 O O   . LEU A 1 290 ? 38.100  14.658  16.890  1.00 17.25 ?  290 LEU A O   1 
ATOM   2285 C CB  . LEU A 1 290 ? 35.626  13.885  18.979  1.00 13.20 ?  290 LEU A CB  1 
ATOM   2286 C CG  . LEU A 1 290 ? 35.360  13.128  17.678  1.00 12.53 ?  290 LEU A CG  1 
ATOM   2287 C CD1 . LEU A 1 290 ? 36.144  11.814  17.670  1.00 15.75 ?  290 LEU A CD1 1 
ATOM   2288 C CD2 . LEU A 1 290 ? 33.859  12.899  17.418  1.00 14.70 ?  290 LEU A CD2 1 
ATOM   2289 N N   . LYS A 1 291 ? 36.864  16.404  17.584  1.00 15.10 ?  291 LYS A N   1 
ATOM   2290 C CA  . LYS A 1 291 ? 37.084  17.135  16.341  1.00 14.53 ?  291 LYS A CA  1 
ATOM   2291 C C   . LYS A 1 291 ? 38.569  17.388  16.102  1.00 17.73 ?  291 LYS A C   1 
ATOM   2292 O O   . LYS A 1 291 ? 39.039  17.332  14.960  1.00 16.44 ?  291 LYS A O   1 
ATOM   2293 C CB  . LYS A 1 291 ? 36.297  18.445  16.364  1.00 17.43 ?  291 LYS A CB  1 
ATOM   2294 C CG  . LYS A 1 291 ? 34.798  18.267  16.115  1.00 17.85 ?  291 LYS A CG  1 
ATOM   2295 C CD  . LYS A 1 291 ? 34.092  19.616  16.024  1.00 21.11 ?  291 LYS A CD  1 
ATOM   2296 C CE  . LYS A 1 291 ? 32.653  19.448  15.538  1.00 21.17 ?  291 LYS A CE  1 
ATOM   2297 N NZ  . LYS A 1 291 ? 32.015  20.697  15.063  1.00 20.65 1  291 LYS A NZ  1 
ATOM   2298 N N   . GLN A 1 292 ? 39.339  17.630  17.166  1.00 16.43 ?  292 GLN A N   1 
ATOM   2299 C CA  . GLN A 1 292 ? 40.766  17.842  16.952  1.00 18.07 ?  292 GLN A CA  1 
ATOM   2300 C C   . GLN A 1 292 ? 41.456  16.538  16.579  1.00 19.18 ?  292 GLN A C   1 
ATOM   2301 O O   . GLN A 1 292 ? 42.357  16.528  15.732  1.00 19.28 ?  292 GLN A O   1 
ATOM   2302 C CB  . GLN A 1 292 ? 41.413  18.472  18.183  1.00 21.98 ?  292 GLN A CB  1 
ATOM   2303 C CG  . GLN A 1 292 ? 42.711  19.222  17.829  1.00 27.48 ?  292 GLN A CG  1 
ATOM   2304 C CD  . GLN A 1 292 ? 42.707  19.824  16.404  1.00 25.86 ?  292 GLN A CD  1 
ATOM   2305 O OE1 . GLN A 1 292 ? 41.959  20.746  16.115  1.00 26.99 ?  292 GLN A OE1 1 
ATOM   2306 N NE2 . GLN A 1 292 ? 43.554  19.295  15.523  1.00 27.19 ?  292 GLN A NE2 1 
ATOM   2307 N N   . VAL A 1 293 ? 41.035  15.421  17.179  1.00 17.35 ?  293 VAL A N   1 
ATOM   2308 C CA  . VAL A 1 293 ? 41.573  14.124  16.769  1.00 16.43 ?  293 VAL A CA  1 
ATOM   2309 C C   . VAL A 1 293 ? 41.236  13.845  15.307  1.00 17.21 ?  293 VAL A C   1 
ATOM   2310 O O   . VAL A 1 293 ? 42.070  13.346  14.545  1.00 16.03 ?  293 VAL A O   1 
ATOM   2311 C CB  . VAL A 1 293 ? 41.047  13.012  17.697  1.00 19.21 ?  293 VAL A CB  1 
ATOM   2312 C CG1 . VAL A 1 293 ? 41.289  11.641  17.084  1.00 18.75 ?  293 VAL A CG1 1 
ATOM   2313 C CG2 . VAL A 1 293 ? 41.695  13.114  19.066  1.00 16.74 ?  293 VAL A CG2 1 
ATOM   2314 N N   . LEU A 1 294 ? 39.998  14.136  14.898  1.00 14.49 ?  294 LEU A N   1 
ATOM   2315 C CA  . LEU A 1 294 ? 39.612  13.908  13.509  1.00 14.56 ?  294 LEU A CA  1 
ATOM   2316 C C   . LEU A 1 294 ? 40.404  14.798  12.554  1.00 13.75 ?  294 LEU A C   1 
ATOM   2317 O O   . LEU A 1 294 ? 40.865  14.339  11.507  1.00 14.79 ?  294 LEU A O   1 
ATOM   2318 C CB  . LEU A 1 294 ? 38.107  14.132  13.343  1.00 13.83 ?  294 LEU A CB  1 
ATOM   2319 C CG  . LEU A 1 294 ? 37.178  13.192  14.132  1.00 14.08 ?  294 LEU A CG  1 
ATOM   2320 C CD1 . LEU A 1 294 ? 35.711  13.531  13.868  1.00 13.95 ?  294 LEU A CD1 1 
ATOM   2321 C CD2 . LEU A 1 294 ? 37.482  11.737  13.760  1.00 13.70 ?  294 LEU A CD2 1 
ATOM   2322 N N   . ARG A 1 295 ? 40.578  16.071  12.894  1.00 15.50 ?  295 ARG A N   1 
ATOM   2323 C CA  . ARG A 1 295 ? 41.370  16.941  12.030  1.00 16.57 ?  295 ARG A CA  1 
ATOM   2324 C C   . ARG A 1 295 ? 42.801  16.436  11.898  1.00 16.66 ?  295 ARG A C   1 
ATOM   2325 O O   . ARG A 1 295 ? 43.356  16.430  10.797  1.00 15.75 ?  295 ARG A O   1 
ATOM   2326 C CB  . ARG A 1 295 ? 41.337  18.374  12.561  1.00 19.69 ?  295 ARG A CB  1 
ATOM   2327 C CG  . ARG A 1 295 ? 40.073  19.115  12.194  1.00 19.24 ?  295 ARG A CG  1 
ATOM   2328 C CD  . ARG A 1 295 ? 40.161  20.589  12.554  1.00 22.43 ?  295 ARG A CD  1 
ATOM   2329 N NE  . ARG A 1 295 ? 40.223  20.768  13.997  1.00 20.60 ?  295 ARG A NE  1 
ATOM   2330 C CZ  . ARG A 1 295 ? 39.179  21.053  14.776  1.00 21.10 ?  295 ARG A CZ  1 
ATOM   2331 N NH1 . ARG A 1 295 ? 37.962  21.203  14.261  1.00 21.69 1  295 ARG A NH1 1 
ATOM   2332 N NH2 . ARG A 1 295 ? 39.361  21.194  16.080  1.00 21.14 ?  295 ARG A NH2 1 
ATOM   2333 N N   . ASP A 1 296 ? 43.411  16.002  13.010  1.00 16.47 ?  296 ASP A N   1 
ATOM   2334 C CA  . ASP A 1 296 ? 44.758  15.433  12.954  1.00 18.56 ?  296 ASP A CA  1 
ATOM   2335 C C   . ASP A 1 296 ? 44.820  14.220  12.035  1.00 17.54 ?  296 ASP A C   1 
ATOM   2336 O O   . ASP A 1 296 ? 45.779  14.062  11.267  1.00 17.39 ?  296 ASP A O   1 
ATOM   2337 C CB  . ASP A 1 296 ? 45.234  15.029  14.350  1.00 21.38 ?  296 ASP A CB  1 
ATOM   2338 C CG  . ASP A 1 296 ? 45.544  16.209  15.235  1.00 26.98 ?  296 ASP A CG  1 
ATOM   2339 O OD1 . ASP A 1 296 ? 45.567  17.355  14.740  1.00 26.66 ?  296 ASP A OD1 1 
ATOM   2340 O OD2 . ASP A 1 296 ? 45.775  15.988  16.447  1.00 28.45 -1 296 ASP A OD2 1 
ATOM   2341 N N   . ASN A 1 297 ? 43.819  13.332  12.110  1.00 14.91 ?  297 ASN A N   1 
ATOM   2342 C CA  . ASN A 1 297 ? 43.839  12.150  11.254  1.00 18.18 ?  297 ASN A CA  1 
ATOM   2343 C C   . ASN A 1 297 ? 43.666  12.533  9.789   1.00 15.95 ?  297 ASN A C   1 
ATOM   2344 O O   . ASN A 1 297 ? 44.335  11.970  8.919   1.00 16.76 ?  297 ASN A O   1 
ATOM   2345 C CB  . ASN A 1 297 ? 42.752  11.147  11.666  1.00 15.45 ?  297 ASN A CB  1 
ATOM   2346 C CG  . ASN A 1 297 ? 43.026  10.491  13.004  1.00 16.10 ?  297 ASN A CG  1 
ATOM   2347 O OD1 . ASN A 1 297 ? 44.112  10.627  13.583  1.00 18.28 ?  297 ASN A OD1 1 
ATOM   2348 N ND2 . ASN A 1 297 ? 42.029  9.762   13.513  1.00 15.80 ?  297 ASN A ND2 1 
ATOM   2349 N N   . PHE A 1 298 ? 42.757  13.468  9.497   1.00 16.22 ?  298 PHE A N   1 
ATOM   2350 C CA  . PHE A 1 298 ? 42.583  13.921  8.119   1.00 15.77 ?  298 PHE A CA  1 
ATOM   2351 C C   . PHE A 1 298 ? 43.842  14.603  7.601   1.00 16.88 ?  298 PHE A C   1 
ATOM   2352 O O   . PHE A 1 298 ? 44.228  14.404  6.445   1.00 15.42 ?  298 PHE A O   1 
ATOM   2353 C CB  . PHE A 1 298 ? 41.406  14.875  8.017   1.00 15.10 ?  298 PHE A CB  1 
ATOM   2354 C CG  . PHE A 1 298 ? 40.133  14.217  7.589   1.00 17.42 ?  298 PHE A CG  1 
ATOM   2355 C CD1 . PHE A 1 298 ? 39.913  13.906  6.258   1.00 20.19 ?  298 PHE A CD1 1 
ATOM   2356 C CD2 . PHE A 1 298 ? 39.155  13.907  8.516   1.00 19.57 ?  298 PHE A CD2 1 
ATOM   2357 C CE1 . PHE A 1 298 ? 38.725  13.312  5.855   1.00 20.70 ?  298 PHE A CE1 1 
ATOM   2358 C CE2 . PHE A 1 298 ? 37.967  13.304  8.114   1.00 21.63 ?  298 PHE A CE2 1 
ATOM   2359 C CZ  . PHE A 1 298 ? 37.758  13.015  6.781   1.00 20.02 ?  298 PHE A CZ  1 
ATOM   2360 N N   . ALA A 1 299 ? 44.475  15.433  8.434   1.00 17.39 ?  299 ALA A N   1 
ATOM   2361 C CA  . ALA A 1 299 ? 45.731  16.072  8.050   1.00 18.29 ?  299 ALA A CA  1 
ATOM   2362 C C   . ALA A 1 299 ? 46.798  15.028  7.757   1.00 19.43 ?  299 ALA A C   1 
ATOM   2363 O O   . ALA A 1 299 ? 47.499  15.105  6.739   1.00 19.24 ?  299 ALA A O   1 
ATOM   2364 C CB  . ALA A 1 299 ? 46.193  17.017  9.158   1.00 18.43 ?  299 ALA A CB  1 
ATOM   2365 N N   . TYR A 1 300 ? 46.922  14.026  8.632   1.00 16.53 ?  300 TYR A N   1 
ATOM   2366 C CA  . TYR A 1 300 ? 47.876  12.951  8.388   1.00 19.98 ?  300 TYR A CA  1 
ATOM   2367 C C   . TYR A 1 300 ? 47.573  12.238  7.079   1.00 21.19 ?  300 TYR A C   1 
ATOM   2368 O O   . TYR A 1 300 ? 48.465  12.034  6.245   1.00 22.16 ?  300 TYR A O   1 
ATOM   2369 C CB  . TYR A 1 300 ? 47.875  11.947  9.543   1.00 20.18 ?  300 TYR A CB  1 
ATOM   2370 C CG  . TYR A 1 300 ? 48.835  10.806  9.278   1.00 24.16 ?  300 TYR A CG  1 
ATOM   2371 C CD1 . TYR A 1 300 ? 50.171  10.908  9.637   1.00 25.37 ?  300 TYR A CD1 1 
ATOM   2372 C CD2 . TYR A 1 300 ? 48.415  9.644   8.624   1.00 22.65 ?  300 TYR A CD2 1 
ATOM   2373 C CE1 . TYR A 1 300 ? 51.060  9.878   9.376   1.00 26.60 ?  300 TYR A CE1 1 
ATOM   2374 C CE2 . TYR A 1 300 ? 49.299  8.612   8.353   1.00 24.08 ?  300 TYR A CE2 1 
ATOM   2375 C CZ  . TYR A 1 300 ? 50.620  8.737   8.738   1.00 25.79 ?  300 TYR A CZ  1 
ATOM   2376 O OH  . TYR A 1 300 ? 51.506  7.716   8.479   1.00 30.40 ?  300 TYR A OH  1 
ATOM   2377 N N   . ALA A 1 301 ? 46.313  11.839  6.885   1.00 18.68 ?  301 ALA A N   1 
ATOM   2378 C CA  . ALA A 1 301 ? 45.962  11.074  5.696   1.00 18.99 ?  301 ALA A CA  1 
ATOM   2379 C C   . ALA A 1 301 ? 46.191  11.875  4.426   1.00 19.25 ?  301 ALA A C   1 
ATOM   2380 O O   . ALA A 1 301 ? 46.700  11.340  3.438   1.00 20.19 ?  301 ALA A O   1 
ATOM   2381 C CB  . ALA A 1 301 ? 44.508  10.616  5.772   1.00 19.06 ?  301 ALA A CB  1 
ATOM   2382 N N   . ARG A 1 302 ? 45.800  13.151  4.420   1.00 17.50 ?  302 ARG A N   1 
ATOM   2383 C CA  . ARG A 1 302 ? 45.962  13.950  3.212   1.00 16.86 ?  302 ARG A CA  1 
ATOM   2384 C C   . ARG A 1 302 ? 47.435  14.146  2.876   1.00 19.45 ?  302 ARG A C   1 
ATOM   2385 O O   . ARG A 1 302 ? 47.835  14.020  1.711   1.00 19.68 ?  302 ARG A O   1 
ATOM   2386 C CB  . ARG A 1 302 ? 45.257  15.297  3.374   1.00 17.10 ?  302 ARG A CB  1 
ATOM   2387 C CG  . ARG A 1 302 ? 43.746  15.198  3.244   1.00 18.06 ?  302 ARG A CG  1 
ATOM   2388 C CD  . ARG A 1 302 ? 43.032  16.515  3.523   1.00 17.37 ?  302 ARG A CD  1 
ATOM   2389 N NE  . ARG A 1 302 ? 41.631  16.407  3.109   1.00 20.01 ?  302 ARG A NE  1 
ATOM   2390 C CZ  . ARG A 1 302 ? 40.580  16.635  3.893   1.00 19.47 ?  302 ARG A CZ  1 
ATOM   2391 N NH1 . ARG A 1 302 ? 40.750  17.017  5.153   1.00 19.45 1  302 ARG A NH1 1 
ATOM   2392 N NH2 . ARG A 1 302 ? 39.351  16.493  3.409   1.00 17.37 ?  302 ARG A NH2 1 
ATOM   2393 N N   . GLU A 1 303 ? 48.253  14.442  3.883   1.00 19.90 ?  303 GLU A N   1 
ATOM   2394 C CA  . GLU A 1 303 ? 49.669  14.669  3.630   1.00 22.91 ?  303 GLU A CA  1 
ATOM   2395 C C   . GLU A 1 303 ? 50.364  13.384  3.206   1.00 23.93 ?  303 GLU A C   1 
ATOM   2396 O O   . GLU A 1 303 ? 51.166  13.385  2.266   1.00 23.87 ?  303 GLU A O   1 
ATOM   2397 C CB  . GLU A 1 303 ? 50.335  15.262  4.872   1.00 26.18 ?  303 GLU A CB  1 
ATOM   2398 C CG  . GLU A 1 303 ? 51.668  15.930  4.571   1.00 31.97 ?  303 GLU A CG  1 
ATOM   2399 C CD  . GLU A 1 303 ? 52.860  15.067  4.977   1.00 42.72 ?  303 GLU A CD  1 
ATOM   2400 O OE1 . GLU A 1 303 ? 52.657  13.972  5.560   1.00 44.42 ?  303 GLU A OE1 1 
ATOM   2401 O OE2 . GLU A 1 303 ? 54.019  15.476  4.705   1.00 44.47 -1 303 GLU A OE2 1 
ATOM   2402 N N   . PHE A 1 304 ? 50.056  12.273  3.878   1.00 21.71 ?  304 PHE A N   1 
ATOM   2403 C CA  . PHE A 1 304 ? 50.669  10.998  3.531   1.00 20.71 ?  304 PHE A CA  1 
ATOM   2404 C C   . PHE A 1 304 ? 50.296  10.572  2.119   1.00 21.90 ?  304 PHE A C   1 
ATOM   2405 O O   . PHE A 1 304 ? 51.150  10.108  1.353   1.00 22.11 ?  304 PHE A O   1 
ATOM   2406 C CB  . PHE A 1 304 ? 50.248  9.928   4.543   1.00 21.52 ?  304 PHE A CB  1 
ATOM   2407 C CG  . PHE A 1 304 ? 50.736  8.541   4.206   1.00 22.19 ?  304 PHE A CG  1 
ATOM   2408 C CD1 . PHE A 1 304 ? 49.979  7.688   3.419   1.00 20.85 ?  304 PHE A CD1 1 
ATOM   2409 C CD2 . PHE A 1 304 ? 51.953  8.092   4.690   1.00 24.96 ?  304 PHE A CD2 1 
ATOM   2410 C CE1 . PHE A 1 304 ? 50.429  6.420   3.113   1.00 21.05 ?  304 PHE A CE1 1 
ATOM   2411 C CE2 . PHE A 1 304 ? 52.403  6.817   4.390   1.00 26.89 ?  304 PHE A CE2 1 
ATOM   2412 C CZ  . PHE A 1 304 ? 51.638  5.983   3.605   1.00 24.62 ?  304 PHE A CZ  1 
ATOM   2413 N N   . LEU A 1 305 ? 49.018  10.697  1.762   1.00 19.07 ?  305 LEU A N   1 
ATOM   2414 C CA  . LEU A 1 305 ? 48.580  10.221  0.458   1.00 20.87 ?  305 LEU A CA  1 
ATOM   2415 C C   . LEU A 1 305 ? 49.091  11.129  -0.652  1.00 21.28 ?  305 LEU A C   1 
ATOM   2416 O O   . LEU A 1 305 ? 49.445  10.654  -1.737  1.00 21.27 ?  305 LEU A O   1 
ATOM   2417 C CB  . LEU A 1 305 ? 47.056  10.108  0.429   1.00 20.54 ?  305 LEU A CB  1 
ATOM   2418 C CG  . LEU A 1 305 ? 46.536  8.945   1.277   1.00 18.98 ?  305 LEU A CG  1 
ATOM   2419 C CD1 . LEU A 1 305 ? 45.037  9.033   1.468   1.00 19.82 ?  305 LEU A CD1 1 
ATOM   2420 C CD2 . LEU A 1 305 ? 46.921  7.607   0.659   1.00 20.75 ?  305 LEU A CD2 1 
ATOM   2421 N N   . ALA A 1 306 ? 49.148  12.436  -0.400  1.00 20.89 ?  306 ALA A N   1 
ATOM   2422 C CA  . ALA A 1 306 ? 49.710  13.345  -1.395  1.00 21.04 ?  306 ALA A CA  1 
ATOM   2423 C C   . ALA A 1 306 ? 51.173  13.018  -1.669  1.00 22.79 ?  306 ALA A C   1 
ATOM   2424 O O   . ALA A 1 306 ? 51.635  13.090  -2.814  1.00 25.30 ?  306 ALA A O   1 
ATOM   2425 C CB  . ALA A 1 306 ? 49.568  14.791  -0.922  1.00 21.49 ?  306 ALA A CB  1 
ATOM   2426 N N   . LYS A 1 307 ? 51.911  12.651  -0.627  1.00 22.65 ?  307 LYS A N   1 
ATOM   2427 C CA  . LYS A 1 307 ? 53.336  12.377  -0.750  1.00 27.91 ?  307 LYS A CA  1 
ATOM   2428 C C   . LYS A 1 307 ? 53.621  10.959  -1.234  1.00 27.94 ?  307 LYS A C   1 
ATOM   2429 O O   . LYS A 1 307 ? 54.578  10.751  -1.986  1.00 30.81 ?  307 LYS A O   1 
ATOM   2430 C CB  . LYS A 1 307 ? 54.011  12.629  0.600   1.00 28.12 ?  307 LYS A CB  1 
ATOM   2431 C CG  . LYS A 1 307 ? 55.515  12.435  0.617   1.00 35.21 ?  307 LYS A CG  1 
ATOM   2432 C CD  . LYS A 1 307 ? 56.060  12.430  2.043   1.00 36.81 ?  307 LYS A CD  1 
ATOM   2433 C CE  . LYS A 1 307 ? 57.589  12.333  2.045   1.00 41.75 ?  307 LYS A CE  1 
ATOM   2434 N NZ  . LYS A 1 307 ? 58.125  11.392  3.079   1.00 39.79 1  307 LYS A NZ  1 
ATOM   2435 N N   . GLU A 1 308 ? 52.811  9.984   -0.831  1.00 23.31 ?  308 GLU A N   1 
ATOM   2436 C CA  . GLU A 1 308 ? 53.140  8.550   -1.073  1.00 25.47 ?  308 GLU A CA  1 
ATOM   2437 C C   . GLU A 1 308 ? 52.248  7.857   -2.104  1.00 23.53 ?  308 GLU A C   1 
ATOM   2438 O O   . GLU A 1 308 ? 52.683  6.860   -2.656  1.00 25.14 ?  308 GLU A O   1 
ATOM   2439 C CB  . GLU A 1 308 ? 53.094  7.781   0.252   1.00 25.97 ?  308 GLU A CB  1 
ATOM   2440 C CG  . GLU A 1 308 ? 53.928  8.406   1.345   1.00 27.98 ?  308 GLU A CG  1 
ATOM   2441 C CD  . GLU A 1 308 ? 55.401  8.098   1.205   1.00 34.17 ?  308 GLU A CD  1 
ATOM   2442 O OE1 . GLU A 1 308 ? 56.216  8.929   1.622   1.00 40.98 ?  308 GLU A OE1 1 
ATOM   2443 O OE2 . GLU A 1 308 ? 55.721  7.030   0.672   1.00 36.48 -1 308 GLU A OE2 1 
ATOM   2444 N N   . VAL A 1 309 ? 51.019  8.319   -2.268  1.00 22.75 ?  309 VAL A N   1 
ATOM   2445 C CA  . VAL A 1 309 ? 50.096  7.708   -3.223  1.00 24.17 ?  309 VAL A CA  1 
ATOM   2446 C C   . VAL A 1 309 ? 49.481  8.816   -4.069  1.00 22.39 ?  309 VAL A C   1 
ATOM   2447 O O   . VAL A 1 309 ? 48.279  9.093   -3.943  1.00 22.80 ?  309 VAL A O   1 
ATOM   2448 C CB  . VAL A 1 309 ? 49.004  6.880   -2.520  1.00 22.82 ?  309 VAL A CB  1 
ATOM   2449 C CG1 . VAL A 1 309 ? 48.313  5.981   -3.524  1.00 21.99 ?  309 VAL A CG1 1 
ATOM   2450 C CG2 . VAL A 1 309 ? 49.584  6.061   -1.375  1.00 24.67 ?  309 VAL A CG2 1 
ATOM   2451 N N   . PRO A 1 310 ? 50.258  9.491   -4.920  1.00 24.03 ?  310 PRO A N   1 
ATOM   2452 C CA  . PRO A 1 310 ? 49.684  10.554  -5.763  1.00 22.77 ?  310 PRO A CA  1 
ATOM   2453 C C   . PRO A 1 310 ? 48.627  10.062  -6.731  1.00 24.64 ?  310 PRO A C   1 
ATOM   2454 O O   . PRO A 1 310 ? 47.903  10.890  -7.293  1.00 24.78 ?  310 PRO A O   1 
ATOM   2455 C CB  . PRO A 1 310 ? 50.901  11.105  -6.516  1.00 24.09 ?  310 PRO A CB  1 
ATOM   2456 C CG  . PRO A 1 310 ? 51.887  9.973   -6.501  1.00 24.09 ?  310 PRO A CG  1 
ATOM   2457 C CD  . PRO A 1 310 ? 51.699  9.317   -5.163  1.00 22.65 ?  310 PRO A CD  1 
ATOM   2458 N N   . GLU A 1 311 ? 48.489  8.759   -6.892  1.00 23.83 ?  311 GLU A N   1 
ATOM   2459 C CA  . GLU A 1 311 ? 47.491  8.193   -7.832  1.00 23.68 ?  311 GLU A CA  1 
ATOM   2460 C C   . GLU A 1 311 ? 46.065  8.300   -7.263  1.00 22.05 ?  311 GLU A C   1 
ATOM   2461 O O   . GLU A 1 311 ? 45.137  7.983   -7.976  1.00 23.23 ?  311 GLU A O   1 
ATOM   2462 C CB  . GLU A 1 311 ? 47.881  6.759   -8.166  1.00 25.91 ?  311 GLU A CB  1 
ATOM   2463 C CG  . GLU A 1 311 ? 49.323  6.596   -8.603  1.00 32.09 ?  311 GLU A CG  1 
ATOM   2464 C CD  . GLU A 1 311 ? 50.252  6.080   -7.518  1.00 31.14 ?  311 GLU A CD  1 
ATOM   2465 O OE1 . GLU A 1 311 ? 50.079  6.483   -6.371  1.00 27.24 ?  311 GLU A OE1 1 
ATOM   2466 O OE2 . GLU A 1 311 ? 51.147  5.283   -7.833  1.00 39.20 -1 311 GLU A OE2 1 
ATOM   2467 N N   . VAL A 1 312 ? 45.922  8.682   -6.004  1.00 20.76 ?  312 VAL A N   1 
ATOM   2468 C CA  . VAL A 1 312 ? 44.604  8.888   -5.420  1.00 20.45 ?  312 VAL A CA  1 
ATOM   2469 C C   . VAL A 1 312 ? 44.523  10.329  -4.936  1.00 20.70 ?  312 VAL A C   1 
ATOM   2470 O O   . VAL A 1 312 ? 45.536  10.982  -4.681  1.00 23.10 ?  312 VAL A O   1 
ATOM   2471 C CB  . VAL A 1 312 ? 44.303  7.906   -4.268  1.00 20.24 ?  312 VAL A CB  1 
ATOM   2472 C CG1 . VAL A 1 312 ? 44.592  6.477   -4.708  1.00 20.19 ?  312 VAL A CG1 1 
ATOM   2473 C CG2 . VAL A 1 312 ? 45.102  8.270   -3.009  1.00 19.20 ?  312 VAL A CG2 1 
ATOM   2474 N N   . LYS A 1 313 ? 43.296  10.834  -4.812  1.00 19.33 ?  313 LYS A N   1 
ATOM   2475 C CA  . LYS A 1 313 ? 43.089  12.208  -4.364  1.00 20.10 ?  313 LYS A CA  1 
ATOM   2476 C C   . LYS A 1 313 ? 42.003  12.229  -3.294  1.00 20.45 ?  313 LYS A C   1 
ATOM   2477 O O   . LYS A 1 313 ? 40.830  11.970  -3.589  1.00 17.86 ?  313 LYS A O   1 
ATOM   2478 C CB  . LYS A 1 313 ? 42.733  13.125  -5.539  1.00 21.88 ?  313 LYS A CB  1 
ATOM   2479 C CG  . LYS A 1 313 ? 42.386  14.554  -5.126  1.00 23.25 ?  313 LYS A CG  1 
ATOM   2480 C CD  . LYS A 1 313 ? 43.529  15.180  -4.346  1.00 26.70 ?  313 LYS A CD  1 
ATOM   2481 C CE  . LYS A 1 313 ? 43.239  16.632  -4.006  1.00 30.82 ?  313 LYS A CE  1 
ATOM   2482 N NZ  . LYS A 1 313 ? 44.498  17.354  -3.635  1.00 34.03 1  313 LYS A NZ  1 
ATOM   2483 N N   . VAL A 1 314 ? 42.394  12.542  -2.057  1.00 19.25 ?  314 VAL A N   1 
ATOM   2484 C CA  . VAL A 1 314 ? 41.415  12.800  -1.008  1.00 18.86 ?  314 VAL A CA  1 
ATOM   2485 C C   . VAL A 1 314 ? 40.734  14.120  -1.322  1.00 20.04 ?  314 VAL A C   1 
ATOM   2486 O O   . VAL A 1 314 ? 41.398  15.154  -1.469  1.00 21.22 ?  314 VAL A O   1 
ATOM   2487 C CB  . VAL A 1 314 ? 42.069  12.842  0.380   1.00 19.11 ?  314 VAL A CB  1 
ATOM   2488 C CG1 . VAL A 1 314 ? 41.006  13.118  1.457   1.00 18.05 ?  314 VAL A CG1 1 
ATOM   2489 C CG2 . VAL A 1 314 ? 42.804  11.550  0.676   1.00 20.34 ?  314 VAL A CG2 1 
ATOM   2490 N N   . LEU A 1 315 ? 39.411  14.095  -1.434  1.00 17.31 ?  315 LEU A N   1 
ATOM   2491 C CA  . LEU A 1 315 ? 38.712  15.325  -1.768  1.00 17.50 ?  315 LEU A CA  1 
ATOM   2492 C C   . LEU A 1 315 ? 38.745  16.271  -0.582  1.00 16.78 ?  315 LEU A C   1 
ATOM   2493 O O   . LEU A 1 315 ? 38.744  15.848  0.579   1.00 14.99 ?  315 LEU A O   1 
ATOM   2494 C CB  . LEU A 1 315 ? 37.269  15.037  -2.183  1.00 18.06 ?  315 LEU A CB  1 
ATOM   2495 C CG  . LEU A 1 315 ? 37.047  14.953  -3.696  1.00 21.86 ?  315 LEU A CG  1 
ATOM   2496 C CD1 . LEU A 1 315 ? 38.011  13.955  -4.352  1.00 23.91 ?  315 LEU A CD1 1 
ATOM   2497 C CD2 . LEU A 1 315 ? 35.604  14.669  -4.045  1.00 17.39 ?  315 LEU A CD2 1 
ATOM   2498 N N   . ASP A 1 316 ? 38.825  17.567  -0.880  1.00 19.75 ?  316 ASP A N   1 
ATOM   2499 C CA  . ASP A 1 316 ? 38.607  18.556  0.164   1.00 22.92 ?  316 ASP A CA  1 
ATOM   2500 C C   . ASP A 1 316 ? 37.198  18.372  0.688   1.00 20.72 ?  316 ASP A C   1 
ATOM   2501 O O   . ASP A 1 316 ? 36.252  18.187  -0.084  1.00 23.63 ?  316 ASP A O   1 
ATOM   2502 C CB  . ASP A 1 316 ? 38.792  19.977  -0.364  1.00 21.36 ?  316 ASP A CB  1 
ATOM   2503 C CG  . ASP A 1 316 ? 40.237  20.296  -0.704  1.00 27.60 ?  316 ASP A CG  1 
ATOM   2504 O OD1 . ASP A 1 316 ? 41.136  19.509  -0.340  1.00 29.49 ?  316 ASP A OD1 1 
ATOM   2505 O OD2 . ASP A 1 316 ? 40.473  21.341  -1.343  1.00 31.48 -1 316 ASP A OD2 1 
ATOM   2506 N N   . SER A 1 317 ? 37.067  18.385  2.004   1.00 21.75 ?  317 SER A N   1 
ATOM   2507 C CA  . SER A 1 317 ? 35.779  18.180  2.636   1.00 22.59 ?  317 SER A CA  1 
ATOM   2508 C C   . SER A 1 317 ? 35.794  18.975  3.919   1.00 22.19 ?  317 SER A C   1 
ATOM   2509 O O   . SER A 1 317 ? 36.860  19.185  4.512   1.00 24.78 ?  317 SER A O   1 
ATOM   2510 C CB  . SER A 1 317 ? 35.525  16.702  2.930   1.00 20.78 ?  317 SER A CB  1 
ATOM   2511 O OG  . SER A 1 317 ? 36.563  16.184  3.742   1.00 24.33 ?  317 SER A OG  1 
ATOM   2512 N N   . ASN A 1 318 ? 34.620  19.427  4.347   1.00 18.36 ?  318 ASN A N   1 
ATOM   2513 C CA  . ASN A 1 318 ? 34.563  20.181  5.585   1.00 18.69 ?  318 ASN A CA  1 
ATOM   2514 C C   . ASN A 1 318 ? 33.776  19.489  6.692   1.00 16.91 ?  318 ASN A C   1 
ATOM   2515 O O   . ASN A 1 318 ? 33.689  20.047  7.787   1.00 16.85 ?  318 ASN A O   1 
ATOM   2516 C CB  . ASN A 1 318 ? 34.011  21.594  5.335   1.00 17.03 ?  318 ASN A CB  1 
ATOM   2517 C CG  . ASN A 1 318 ? 32.556  21.601  4.867   1.00 19.99 ?  318 ASN A CG  1 
ATOM   2518 O OD1 . ASN A 1 318 ? 31.939  20.556  4.692   1.00 17.09 ?  318 ASN A OD1 1 
ATOM   2519 N ND2 . ASN A 1 318 ? 32.003  22.798  4.672   1.00 19.77 ?  318 ASN A ND2 1 
ATOM   2520 N N   . ALA A 1 319 ? 33.242  18.282  6.467   1.00 16.46 ?  319 ALA A N   1 
ATOM   2521 C CA  . ALA A 1 319 ? 32.394  17.667  7.483   1.00 16.99 ?  319 ALA A CA  1 
ATOM   2522 C C   . ALA A 1 319 ? 32.490  16.148  7.431   1.00 17.35 ?  319 ALA A C   1 
ATOM   2523 O O   . ALA A 1 319 ? 32.839  15.560  6.402   1.00 16.13 ?  319 ALA A O   1 
ATOM   2524 C CB  . ALA A 1 319 ? 30.928  18.104  7.332   1.00 15.02 ?  319 ALA A CB  1 
ATOM   2525 N N   . SER A 1 320 ? 32.150  15.524  8.570   1.00 15.36 ?  320 SER A N   1 
ATOM   2526 C CA  . SER A 1 320 ? 32.098  14.075  8.764   1.00 15.42 ?  320 SER A CA  1 
ATOM   2527 C C   . SER A 1 320 ? 33.492  13.511  8.981   1.00 15.67 ?  320 SER A C   1 
ATOM   2528 O O   . SER A 1 320 ? 34.490  14.196  8.731   1.00 14.17 ?  320 SER A O   1 
ATOM   2529 C CB  . SER A 1 320 ? 31.428  13.354  7.581   1.00 15.71 ?  320 SER A CB  1 
ATOM   2530 O OG  . SER A 1 320 ? 32.399  12.880  6.633   1.00 17.13 ?  320 SER A OG  1 
ATOM   2531 N N   . TYR A 1 321 ? 33.579  12.259  9.431   1.00 12.24 ?  321 TYR A N   1 
ATOM   2532 C CA  . TYR A 1 321 ? 34.872  11.619  9.628   1.00 14.70 ?  321 TYR A CA  1 
ATOM   2533 C C   . TYR A 1 321 ? 35.179  10.625  8.521   1.00 16.18 ?  321 TYR A C   1 
ATOM   2534 O O   . TYR A 1 321 ? 36.042  9.756   8.676   1.00 15.84 ?  321 TYR A O   1 
ATOM   2535 C CB  . TYR A 1 321 ? 34.935  10.971  11.009  1.00 11.95 ?  321 TYR A CB  1 
ATOM   2536 C CG  . TYR A 1 321 ? 33.844  9.971   11.353  1.00 14.92 ?  321 TYR A CG  1 
ATOM   2537 C CD1 . TYR A 1 321 ? 33.805  8.704   10.751  1.00 15.55 ?  321 TYR A CD1 1 
ATOM   2538 C CD2 . TYR A 1 321 ? 32.896  10.263  12.335  1.00 14.57 ?  321 TYR A CD2 1 
ATOM   2539 C CE1 . TYR A 1 321 ? 32.840  7.765   11.096  1.00 18.33 ?  321 TYR A CE1 1 
ATOM   2540 C CE2 . TYR A 1 321 ? 31.907  9.330   12.689  1.00 17.57 ?  321 TYR A CE2 1 
ATOM   2541 C CZ  . TYR A 1 321 ? 31.893  8.084   12.068  1.00 17.73 ?  321 TYR A CZ  1 
ATOM   2542 O OH  . TYR A 1 321 ? 30.945  7.149   12.404  1.00 17.86 ?  321 TYR A OH  1 
ATOM   2543 N N   . LEU A 1 322 ? 34.504  10.768  7.392   1.00 14.22 ?  322 LEU A N   1 
ATOM   2544 C CA  . LEU A 1 322 ? 34.622  9.859   6.266   1.00 15.26 ?  322 LEU A CA  1 
ATOM   2545 C C   . LEU A 1 322 ? 35.349  10.580  5.146   1.00 18.69 ?  322 LEU A C   1 
ATOM   2546 O O   . LEU A 1 322 ? 34.920  11.658  4.717   1.00 19.59 ?  322 LEU A O   1 
ATOM   2547 C CB  . LEU A 1 322 ? 33.235  9.398   5.827   1.00 16.33 ?  322 LEU A CB  1 
ATOM   2548 C CG  . LEU A 1 322 ? 32.469  8.753   6.981   1.00 19.43 ?  322 LEU A CG  1 
ATOM   2549 C CD1 . LEU A 1 322 ? 30.992  8.765   6.653   1.00 22.26 ?  322 LEU A CD1 1 
ATOM   2550 C CD2 . LEU A 1 322 ? 32.995  7.339   7.230   1.00 20.27 ?  322 LEU A CD2 1 
ATOM   2551 N N   . ALA A 1 323 ? 36.461  10.005  4.701   1.00 14.86 ?  323 ALA A N   1 
ATOM   2552 C CA  . ALA A 1 323 ? 37.220  10.546  3.586   1.00 16.45 ?  323 ALA A CA  1 
ATOM   2553 C C   . ALA A 1 323 ? 36.655  9.968   2.295   1.00 14.94 ?  323 ALA A C   1 
ATOM   2554 O O   . ALA A 1 323 ? 36.392  8.766   2.210   1.00 14.32 ?  323 ALA A O   1 
ATOM   2555 C CB  . ALA A 1 323 ? 38.710  10.210  3.730   1.00 14.66 ?  323 ALA A CB  1 
ATOM   2556 N N   . TRP A 1 324 ? 36.440  10.829  1.313   1.00 12.91 ?  324 TRP A N   1 
ATOM   2557 C CA  . TRP A 1 324 ? 35.939  10.466  -0.010  1.00 14.65 ?  324 TRP A CA  1 
ATOM   2558 C C   . TRP A 1 324 ? 37.122  10.633  -0.943  1.00 16.48 ?  324 TRP A C   1 
ATOM   2559 O O   . TRP A 1 324 ? 37.624  11.750  -1.118  1.00 14.08 ?  324 TRP A O   1 
ATOM   2560 C CB  . TRP A 1 324 ? 34.770  11.363  -0.408  1.00 13.00 ?  324 TRP A CB  1 
ATOM   2561 C CG  . TRP A 1 324 ? 33.989  11.012  -1.651  1.00 13.24 ?  324 TRP A CG  1 
ATOM   2562 C CD1 . TRP A 1 324 ? 33.731  11.838  -2.695  1.00 15.13 ?  324 TRP A CD1 1 
ATOM   2563 C CD2 . TRP A 1 324 ? 33.287  9.780   -1.932  1.00 13.83 ?  324 TRP A CD2 1 
ATOM   2564 N NE1 . TRP A 1 324 ? 32.929  11.211  -3.617  1.00 12.69 ?  324 TRP A NE1 1 
ATOM   2565 C CE2 . TRP A 1 324 ? 32.638  9.946   -3.171  1.00 14.45 ?  324 TRP A CE2 1 
ATOM   2566 C CE3 . TRP A 1 324 ? 33.149  8.559   -1.258  1.00 12.85 ?  324 TRP A CE3 1 
ATOM   2567 C CZ2 . TRP A 1 324 ? 31.866  8.933   -3.760  1.00 14.26 ?  324 TRP A CZ2 1 
ATOM   2568 C CZ3 . TRP A 1 324 ? 32.377  7.546   -1.852  1.00 14.10 ?  324 TRP A CZ3 1 
ATOM   2569 C CH2 . TRP A 1 324 ? 31.743  7.746   -3.080  1.00 12.74 ?  324 TRP A CH2 1 
ATOM   2570 N N   . VAL A 1 325 ? 37.585  9.526   -1.510  1.00 15.76 ?  325 VAL A N   1 
ATOM   2571 C CA  . VAL A 1 325 ? 38.894  9.457   -2.145  1.00 16.89 ?  325 VAL A CA  1 
ATOM   2572 C C   . VAL A 1 325 ? 38.715  9.069   -3.603  1.00 16.73 ?  325 VAL A C   1 
ATOM   2573 O O   . VAL A 1 325 ? 38.256  7.958   -3.904  1.00 14.03 ?  325 VAL A O   1 
ATOM   2574 C CB  . VAL A 1 325 ? 39.812  8.460   -1.429  1.00 16.13 ?  325 VAL A CB  1 
ATOM   2575 C CG1 . VAL A 1 325 ? 41.184  8.497   -2.062  1.00 16.36 ?  325 VAL A CG1 1 
ATOM   2576 C CG2 . VAL A 1 325 ? 39.887  8.772   0.060   1.00 15.88 ?  325 VAL A CG2 1 
ATOM   2577 N N   . ASP A 1 326 ? 39.106  9.975   -4.497  1.00 15.55 ?  326 ASP A N   1 
ATOM   2578 C CA  . ASP A 1 326 ? 39.010  9.795   -5.945  1.00 16.59 ?  326 ASP A CA  1 
ATOM   2579 C C   . ASP A 1 326 ? 40.113  8.836   -6.384  1.00 17.69 ?  326 ASP A C   1 
ATOM   2580 O O   . ASP A 1 326 ? 41.304  9.155   -6.285  1.00 16.95 ?  326 ASP A O   1 
ATOM   2581 C CB  . ASP A 1 326 ? 39.124  11.157  -6.633  1.00 15.70 ?  326 ASP A CB  1 
ATOM   2582 C CG  . ASP A 1 326 ? 39.005  11.087  -8.163  1.00 18.80 ?  326 ASP A CG  1 
ATOM   2583 O OD1 . ASP A 1 326 ? 39.286  10.035  -8.772  1.00 20.38 ?  326 ASP A OD1 1 
ATOM   2584 O OD2 . ASP A 1 326 ? 38.659  12.125  -8.770  1.00 21.77 -1 326 ASP A OD2 1 
ATOM   2585 N N   . ILE A 1 327 ? 39.731  7.644   -6.831  1.00 16.88 ?  327 ILE A N   1 
ATOM   2586 C CA  . ILE A 1 327 ? 40.699  6.650   -7.268  1.00 16.76 ?  327 ILE A CA  1 
ATOM   2587 C C   . ILE A 1 327 ? 40.708  6.516   -8.792  1.00 19.27 ?  327 ILE A C   1 
ATOM   2588 O O   . ILE A 1 327 ? 41.234  5.531   -9.322  1.00 18.91 ?  327 ILE A O   1 
ATOM   2589 C CB  . ILE A 1 327 ? 40.452  5.284   -6.605  1.00 17.30 ?  327 ILE A CB  1 
ATOM   2590 C CG1 . ILE A 1 327 ? 39.113  4.707   -7.072  1.00 16.96 ?  327 ILE A CG1 1 
ATOM   2591 C CG2 . ILE A 1 327 ? 40.575  5.387   -5.073  1.00 15.52 ?  327 ILE A CG2 1 
ATOM   2592 C CD1 . ILE A 1 327 ? 39.018  3.214   -6.950  1.00 17.85 ?  327 ILE A CD1 1 
ATOM   2593 N N   . SER A 1 328 ? 40.131  7.492   -9.505  1.00 17.19 ?  328 SER A N   1 
ATOM   2594 C CA  . SER A 1 328 ? 39.992  7.377   -10.955 1.00 21.06 ?  328 SER A CA  1 
ATOM   2595 C C   . SER A 1 328 ? 41.337  7.175   -11.645 1.00 20.66 ?  328 SER A C   1 
ATOM   2596 O O   . SER A 1 328 ? 41.401  6.510   -12.686 1.00 21.57 ?  328 SER A O   1 
ATOM   2597 C CB  . SER A 1 328 ? 39.292  8.614   -11.524 1.00 20.82 ?  328 SER A CB  1 
ATOM   2598 O OG  . SER A 1 328 ? 40.097  9.767   -11.370 1.00 20.45 ?  328 SER A OG  1 
ATOM   2599 N N   . ALA A 1 329 ? 42.428  7.679   -11.076 1.00 21.39 ?  329 ALA A N   1 
ATOM   2600 C CA  . ALA A 1 329 ? 43.756  7.545   -11.711 1.00 21.91 ?  329 ALA A CA  1 
ATOM   2601 C C   . ALA A 1 329 ? 44.257  6.103   -11.621 1.00 24.05 ?  329 ALA A C   1 
ATOM   2602 O O   . ALA A 1 329 ? 45.147  5.766   -12.388 1.00 25.59 ?  329 ALA A O   1 
ATOM   2603 C CB  . ALA A 1 329 ? 44.745  8.517   -11.136 1.00 22.42 ?  329 ALA A CB  1 
ATOM   2604 N N   . LEU A 1 330 ? 43.695  5.314   -10.706 1.00 21.31 ?  330 LEU A N   1 
ATOM   2605 C CA  . LEU A 1 330 ? 44.066  3.904   -10.638 1.00 24.57 ?  330 LEU A CA  1 
ATOM   2606 C C   . LEU A 1 330 ? 43.556  3.107   -11.830 1.00 24.27 ?  330 LEU A C   1 
ATOM   2607 O O   . LEU A 1 330 ? 44.017  1.983   -12.043 1.00 23.76 ?  330 LEU A O   1 
ATOM   2608 C CB  . LEU A 1 330 ? 43.530  3.269   -9.351  1.00 19.96 ?  330 LEU A CB  1 
ATOM   2609 C CG  . LEU A 1 330 ? 44.173  3.703   -8.038  1.00 22.09 ?  330 LEU A CG  1 
ATOM   2610 C CD1 . LEU A 1 330 ? 43.755  2.766   -6.931  1.00 23.12 ?  330 LEU A CD1 1 
ATOM   2611 C CD2 . LEU A 1 330 ? 45.683  3.745   -8.159  1.00 25.69 ?  330 LEU A CD2 1 
ATOM   2612 N N   . GLY A 1 331 ? 42.602  3.641   -12.586 1.00 22.15 ?  331 GLY A N   1 
ATOM   2613 C CA  . GLY A 1 331 ? 42.045  2.904   -13.708 1.00 21.35 ?  331 GLY A CA  1 
ATOM   2614 C C   . GLY A 1 331 ? 41.371  1.601   -13.331 1.00 22.43 ?  331 GLY A C   1 
ATOM   2615 O O   . GLY A 1 331 ? 41.504  0.610   -14.056 1.00 20.69 ?  331 GLY A O   1 
ATOM   2616 N N   . MET A 1 332 ? 40.666  1.588   -12.201 1.00 21.20 ?  332 MET A N   1 
ATOM   2617 C CA  . MET A 1 332 ? 40.017  0.350   -11.704 1.00 19.93 ?  332 MET A CA  1 
ATOM   2618 C C   . MET A 1 332 ? 38.689  0.682   -11.022 1.00 20.46 ?  332 MET A C   1 
ATOM   2619 O O   . MET A 1 332 ? 38.640  1.643   -10.270 1.00 22.18 ?  332 MET A O   1 
ATOM   2620 C CB  . MET A 1 332 ? 40.903  -0.398  -10.711 1.00 18.31 ?  332 MET A CB  1 
ATOM   2621 C CG  . MET A 1 332 ? 40.456  -1.810  -10.431 1.00 20.84 ?  332 MET A CG  1 
ATOM   2622 S SD  . MET A 1 332 ? 41.641  -2.688  -9.384  1.00 26.15 ?  332 MET A SD  1 
ATOM   2623 C CE  . MET A 1 332 ? 41.315  -4.389  -9.836  1.00 30.08 ?  332 MET A CE  1 
ATOM   2624 N N   . ASN A 1 333 ? 37.655  -0.093  -11.330 1.00 18.97 ?  333 ASN A N   1 
ATOM   2625 C CA  . ASN A 1 333 ? 36.380  0.083   -10.643 1.00 20.29 ?  333 ASN A CA  1 
ATOM   2626 C C   . ASN A 1 333 ? 36.580  -0.048  -9.137  1.00 17.83 ?  333 ASN A C   1 
ATOM   2627 O O   . ASN A 1 333 ? 37.306  -0.923  -8.664  1.00 16.80 ?  333 ASN A O   1 
ATOM   2628 C CB  . ASN A 1 333 ? 35.368  -0.948  -11.130 1.00 19.48 ?  333 ASN A CB  1 
ATOM   2629 C CG  . ASN A 1 333 ? 33.973  -0.671  -10.623 1.00 22.96 ?  333 ASN A CG  1 
ATOM   2630 O OD1 . ASN A 1 333 ? 33.683  -0.830  -9.439  1.00 23.71 ?  333 ASN A OD1 1 
ATOM   2631 N ND2 . ASN A 1 333 ? 33.099  -0.251  -11.518 1.00 25.91 ?  333 ASN A ND2 1 
ATOM   2632 N N   . ALA A 1 334 ? 35.940  0.838   -8.377  1.00 17.30 ?  334 ALA A N   1 
ATOM   2633 C CA  . ALA A 1 334 ? 36.172  0.858   -6.937  1.00 16.91 ?  334 ALA A CA  1 
ATOM   2634 C C   . ALA A 1 334 ? 35.830  -0.479  -6.287  1.00 17.98 ?  334 ALA A C   1 
ATOM   2635 O O   . ALA A 1 334 ? 36.501  -0.901  -5.340  1.00 18.35 ?  334 ALA A O   1 
ATOM   2636 C CB  . ALA A 1 334 ? 35.368  1.983   -6.289  1.00 16.42 ?  334 ALA A CB  1 
ATOM   2637 N N   . GLU A 1 335 ? 34.775  -1.156  -6.755  1.00 18.26 ?  335 GLU A N   1 
ATOM   2638 C CA  . GLU A 1 335 ? 34.443  -2.435  -6.135  1.00 20.05 ?  335 GLU A CA  1 
ATOM   2639 C C   . GLU A 1 335 ? 35.527  -3.470  -6.412  1.00 19.89 ?  335 GLU A C   1 
ATOM   2640 O O   . GLU A 1 335 ? 35.883  -4.251  -5.525  1.00 20.76 ?  335 GLU A O   1 
ATOM   2641 C CB  . GLU A 1 335 ? 33.067  -2.923  -6.595  1.00 21.70 ?  335 GLU A CB  1 
ATOM   2642 C CG  . GLU A 1 335 ? 32.410  -3.894  -5.594  1.00 26.98 ?  335 GLU A CG  1 
ATOM   2643 C CD  . GLU A 1 335 ? 31.721  -3.199  -4.406  1.00 34.17 ?  335 GLU A CD  1 
ATOM   2644 O OE1 . GLU A 1 335 ? 32.159  -3.418  -3.239  1.00 33.32 ?  335 GLU A OE1 1 
ATOM   2645 O OE2 . GLU A 1 335 ? 30.729  -2.451  -4.631  1.00 34.87 -1 335 GLU A OE2 1 
ATOM   2646 N N   . ASP A 1 336 ? 36.146  -3.414  -7.582  1.00 20.31 ?  336 ASP A N   1 
ATOM   2647 C CA  . ASP A 1 336 ? 37.256  -4.344  -7.885  1.00 20.08 ?  336 ASP A CA  1 
ATOM   2648 C C   . ASP A 1 336 ? 38.453  -3.972  -7.022  1.00 18.82 ?  336 ASP A C   1 
ATOM   2649 O O   . ASP A 1 336 ? 39.102  -4.847  -6.500  1.00 21.18 ?  336 ASP A O   1 
ATOM   2650 C CB  . ASP A 1 336 ? 37.606  -4.246  -9.367  1.00 21.84 ?  336 ASP A CB  1 
ATOM   2651 C CG  . ASP A 1 336 ? 36.529  -4.829  -10.259 1.00 24.13 ?  336 ASP A CG  1 
ATOM   2652 O OD1 . ASP A 1 336 ? 35.786  -5.694  -9.778  1.00 26.44 ?  336 ASP A OD1 1 
ATOM   2653 O OD2 . ASP A 1 336 ? 36.449  -4.412  -11.417 1.00 24.36 -1 336 ASP A OD2 1 
ATOM   2654 N N   . PHE A 1 337 ? 38.693  -2.673  -6.895  1.00 17.18 ?  337 PHE A N   1 
ATOM   2655 C CA  . PHE A 1 337 ? 39.852  -2.243  -6.121  1.00 17.61 ?  337 PHE A CA  1 
ATOM   2656 C C   . PHE A 1 337 ? 39.718  -2.622  -4.652  1.00 17.81 ?  337 PHE A C   1 
ATOM   2657 O O   . PHE A 1 337 ? 40.691  -3.053  -4.024  1.00 17.85 ?  337 PHE A O   1 
ATOM   2658 C CB  . PHE A 1 337 ? 40.045  -0.735  -6.255  1.00 18.00 ?  337 PHE A CB  1 
ATOM   2659 C CG  . PHE A 1 337 ? 41.198  -0.215  -5.474  1.00 17.54 ?  337 PHE A CG  1 
ATOM   2660 C CD1 . PHE A 1 337 ? 42.490  -0.598  -5.805  1.00 19.63 ?  337 PHE A CD1 1 
ATOM   2661 C CD2 . PHE A 1 337 ? 41.005  0.631   -4.395  1.00 19.82 ?  337 PHE A CD2 1 
ATOM   2662 C CE1 . PHE A 1 337 ? 43.580  -0.134  -5.086  1.00 22.11 ?  337 PHE A CE1 1 
ATOM   2663 C CE2 . PHE A 1 337 ? 42.090  1.112   -3.665  1.00 20.96 ?  337 PHE A CE2 1 
ATOM   2664 C CZ  . PHE A 1 337 ? 43.383  0.726   -4.011  1.00 23.87 ?  337 PHE A CZ  1 
ATOM   2665 N N   . CYS A 1 338 ? 38.530  -2.453  -4.075  1.00 17.85 ?  338 CYS A N   1 
ATOM   2666 C CA  . CYS A 1 338 ? 38.389  -2.712  -2.648  1.00 18.86 ?  338 CYS A CA  1 
ATOM   2667 C C   . CYS A 1 338 ? 38.480  -4.204  -2.346  1.00 18.21 ?  338 CYS A C   1 
ATOM   2668 O O   . CYS A 1 338 ? 39.019  -4.597  -1.306  1.00 18.81 ?  338 CYS A O   1 
ATOM   2669 C CB  . CYS A 1 338 ? 37.074  -2.121  -2.134  1.00 17.08 ?  338 CYS A CB  1 
ATOM   2670 S SG  . CYS A 1 338 ? 37.074  -0.299  -2.114  1.00 18.52 ?  338 CYS A SG  1 
ATOM   2671 N N   . LYS A 1 339 ? 37.951  -5.047  -3.235  1.00 17.86 ?  339 LYS A N   1 
ATOM   2672 C CA  . LYS A 1 339 ? 38.111  -6.491  -3.078  1.00 19.89 ?  339 LYS A CA  1 
ATOM   2673 C C   . LYS A 1 339 ? 39.582  -6.881  -3.107  1.00 21.17 ?  339 LYS A C   1 
ATOM   2674 O O   . LYS A 1 339 ? 40.071  -7.592  -2.220  1.00 22.22 ?  339 LYS A O   1 
ATOM   2675 C CB  . LYS A 1 339 ? 37.358  -7.226  -4.183  1.00 22.32 ?  339 LYS A CB  1 
ATOM   2676 C CG  . LYS A 1 339 ? 37.388  -8.745  -4.044  1.00 28.44 ?  339 LYS A CG  1 
ATOM   2677 C CD  . LYS A 1 339 ? 36.281  -9.386  -4.876  1.00 34.07 ?  339 LYS A CD  1 
ATOM   2678 C CE  . LYS A 1 339 ? 36.548  -10.861 -5.142  1.00 39.37 ?  339 LYS A CE  1 
ATOM   2679 N NZ  . LYS A 1 339 ? 35.481  -11.454 -6.005  1.00 39.91 1  339 LYS A NZ  1 
ATOM   2680 N N   . TYR A 1 340 ? 40.298  -6.434  -4.140  1.00 20.86 ?  340 TYR A N   1 
ATOM   2681 C CA  . TYR A 1 340 ? 41.730  -6.697  -4.234  1.00 21.71 ?  340 TYR A CA  1 
ATOM   2682 C C   . TYR A 1 340 ? 42.461  -6.181  -3.000  1.00 22.57 ?  340 TYR A C   1 
ATOM   2683 O O   . TYR A 1 340 ? 43.330  -6.867  -2.443  1.00 20.99 ?  340 TYR A O   1 
ATOM   2684 C CB  . TYR A 1 340 ? 42.277  -6.050  -5.512  1.00 24.88 ?  340 TYR A CB  1 
ATOM   2685 C CG  . TYR A 1 340 ? 43.746  -5.712  -5.442  1.00 23.85 ?  340 TYR A CG  1 
ATOM   2686 C CD1 . TYR A 1 340 ? 44.713  -6.639  -5.821  1.00 27.44 ?  340 TYR A CD1 1 
ATOM   2687 C CD2 . TYR A 1 340 ? 44.168  -4.469  -4.979  1.00 26.45 ?  340 TYR A CD2 1 
ATOM   2688 C CE1 . TYR A 1 340 ? 46.060  -6.330  -5.744  1.00 28.95 ?  340 TYR A CE1 1 
ATOM   2689 C CE2 . TYR A 1 340 ? 45.498  -4.157  -4.891  1.00 29.50 ?  340 TYR A CE2 1 
ATOM   2690 C CZ  . TYR A 1 340 ? 46.444  -5.081  -5.270  1.00 31.33 ?  340 TYR A CZ  1 
ATOM   2691 O OH  . TYR A 1 340 ? 47.770  -4.728  -5.178  1.00 32.93 ?  340 TYR A OH  1 
ATOM   2692 N N   . LEU A 1 341 ? 42.108  -4.971  -2.551  1.00 20.20 ?  341 LEU A N   1 
ATOM   2693 C CA  . LEU A 1 341 ? 42.775  -4.368  -1.405  1.00 19.56 ?  341 LEU A CA  1 
ATOM   2694 C C   . LEU A 1 341 ? 42.600  -5.217  -0.148  1.00 21.46 ?  341 LEU A C   1 
ATOM   2695 O O   . LEU A 1 341 ? 43.563  -5.455  0.592   1.00 22.39 ?  341 LEU A O   1 
ATOM   2696 C CB  . LEU A 1 341 ? 42.231  -2.954  -1.199  1.00 21.73 ?  341 LEU A CB  1 
ATOM   2697 C CG  . LEU A 1 341 ? 42.837  -2.123  -0.076  1.00 23.63 ?  341 LEU A CG  1 
ATOM   2698 C CD1 . LEU A 1 341 ? 44.344  -1.943  -0.306  1.00 23.49 ?  341 LEU A CD1 1 
ATOM   2699 C CD2 . LEU A 1 341 ? 42.131  -0.773  -0.012  1.00 21.67 ?  341 LEU A CD2 1 
ATOM   2700 N N   . ARG A 1 342 ? 41.373  -5.682  0.117   1.00 20.33 ?  342 ARG A N   1 
ATOM   2701 C CA  . ARG A 1 342 ? 41.159  -6.542  1.276   1.00 20.75 ?  342 ARG A CA  1 
ATOM   2702 C C   . ARG A 1 342 ? 41.926  -7.854  1.144   1.00 22.39 ?  342 ARG A C   1 
ATOM   2703 O O   . ARG A 1 342 ? 42.540  -8.317  2.110   1.00 21.75 ?  342 ARG A O   1 
ATOM   2704 C CB  . ARG A 1 342 ? 39.669  -6.811  1.478   1.00 18.89 ?  342 ARG A CB  1 
ATOM   2705 C CG  . ARG A 1 342 ? 39.393  -7.717  2.679   1.00 20.42 ?  342 ARG A CG  1 
ATOM   2706 C CD  . ARG A 1 342 ? 37.914  -8.006  2.900   1.00 23.75 ?  342 ARG A CD  1 
ATOM   2707 N NE  . ARG A 1 342 ? 37.706  -8.640  4.204   1.00 24.53 ?  342 ARG A NE  1 
ATOM   2708 C CZ  . ARG A 1 342 ? 36.517  -8.871  4.752   1.00 27.22 ?  342 ARG A CZ  1 
ATOM   2709 N NH1 . ARG A 1 342 ? 35.411  -8.530  4.111   1.00 27.53 1  342 ARG A NH1 1 
ATOM   2710 N NH2 . ARG A 1 342 ? 36.435  -9.452  5.944   1.00 28.39 ?  342 ARG A NH2 1 
ATOM   2711 N N   . GLU A 1 343 ? 41.912  -8.462  -0.047  1.00 23.77 ?  343 GLU A N   1 
ATOM   2712 C CA  . GLU A 1 343 ? 42.630  -9.723  -0.256  1.00 24.15 ?  343 GLU A CA  1 
ATOM   2713 C C   . GLU A 1 343 ? 44.129  -9.571  -0.007  1.00 23.69 ?  343 GLU A C   1 
ATOM   2714 O O   . GLU A 1 343 ? 44.738  -10.394 0.690   1.00 25.48 ?  343 GLU A O   1 
ATOM   2715 C CB  . GLU A 1 343 ? 42.392  -10.233 -1.676  1.00 26.76 ?  343 GLU A CB  1 
ATOM   2716 C CG  . GLU A 1 343 ? 40.968  -10.648 -1.988  1.00 29.23 ?  343 GLU A CG  1 
ATOM   2717 C CD  . GLU A 1 343 ? 40.838  -11.179 -3.409  1.00 35.29 ?  343 GLU A CD  1 
ATOM   2718 O OE1 . GLU A 1 343 ? 39.971  -12.044 -3.655  1.00 44.04 ?  343 GLU A OE1 1 
ATOM   2719 O OE2 . GLU A 1 343 ? 41.611  -10.723 -4.283  1.00 41.72 -1 343 GLU A OE2 1 
ATOM   2720 N N   . LYS A 1 344 ? 44.743  -8.534  -0.565  1.00 22.96 ?  344 LYS A N   1 
ATOM   2721 C CA  . LYS A 1 344 ? 46.197  -8.419  -0.527  1.00 22.43 ?  344 LYS A CA  1 
ATOM   2722 C C   . LYS A 1 344 ? 46.731  -7.769  0.735   1.00 27.26 ?  344 LYS A C   1 
ATOM   2723 O O   . LYS A 1 344 ? 47.886  -8.024  1.100   1.00 25.34 ?  344 LYS A O   1 
ATOM   2724 C CB  . LYS A 1 344 ? 46.706  -7.620  -1.725  1.00 25.93 ?  344 LYS A CB  1 
ATOM   2725 C CG  . LYS A 1 344 ? 46.456  -8.302  -3.050  1.00 27.52 ?  344 LYS A CG  1 
ATOM   2726 C CD  . LYS A 1 344 ? 46.712  -9.811  -2.990  1.00 31.89 ?  344 LYS A CD  1 
ATOM   2727 C CE  . LYS A 1 344 ? 46.956  -10.344 -4.396  1.00 35.64 ?  344 LYS A CE  1 
ATOM   2728 N NZ  . LYS A 1 344 ? 47.834  -11.547 -4.393  1.00 38.92 1  344 LYS A NZ  1 
ATOM   2729 N N   . THR A 1 345 ? 45.945  -6.914  1.395   1.00 22.43 ?  345 THR A N   1 
ATOM   2730 C CA  . THR A 1 345 ? 46.436  -6.175  2.551   1.00 23.03 ?  345 THR A CA  1 
ATOM   2731 C C   . THR A 1 345 ? 45.591  -6.333  3.804   1.00 20.75 ?  345 THR A C   1 
ATOM   2732 O O   . THR A 1 345 ? 46.077  -5.994  4.887   1.00 21.49 ?  345 THR A O   1 
ATOM   2733 C CB  . THR A 1 345 ? 46.552  -4.669  2.243   1.00 23.96 ?  345 THR A CB  1 
ATOM   2734 O OG1 . THR A 1 345 ? 45.261  -4.047  2.349   1.00 21.98 ?  345 THR A OG1 1 
ATOM   2735 C CG2 . THR A 1 345 ? 47.121  -4.428  0.843   1.00 23.74 ?  345 THR A CG2 1 
ATOM   2736 N N   . GLY A 1 346 ? 44.362  -6.829  3.709   1.00 20.14 ?  346 GLY A N   1 
ATOM   2737 C CA  . GLY A 1 346 ? 43.494  -6.865  4.862   1.00 20.98 ?  346 GLY A CA  1 
ATOM   2738 C C   . GLY A 1 346 ? 42.800  -5.561  5.195   1.00 19.51 ?  346 GLY A C   1 
ATOM   2739 O O   . GLY A 1 346 ? 41.975  -5.540  6.117   1.00 22.82 ?  346 GLY A O   1 
ATOM   2740 N N   . LEU A 1 347 ? 43.099  -4.471  4.493   1.00 19.27 ?  347 LEU A N   1 
ATOM   2741 C CA  . LEU A 1 347 ? 42.387  -3.219  4.725   1.00 18.31 ?  347 LEU A CA  1 
ATOM   2742 C C   . LEU A 1 347 ? 41.006  -3.278  4.086   1.00 16.82 ?  347 LEU A C   1 
ATOM   2743 O O   . LEU A 1 347 ? 40.878  -3.588  2.897   1.00 18.44 ?  347 LEU A O   1 
ATOM   2744 C CB  . LEU A 1 347 ? 43.174  -2.048  4.150   1.00 18.93 ?  347 LEU A CB  1 
ATOM   2745 C CG  . LEU A 1 347 ? 42.416  -0.715  4.110   1.00 16.88 ?  347 LEU A CG  1 
ATOM   2746 C CD1 . LEU A 1 347 ? 42.126  -0.215  5.524   1.00 18.53 ?  347 LEU A CD1 1 
ATOM   2747 C CD2 . LEU A 1 347 ? 43.199  0.326   3.316   1.00 17.37 ?  347 LEU A CD2 1 
ATOM   2748 N N   . ILE A 1 348 ? 39.968  -2.980  4.863   1.00 14.71 ?  348 ILE A N   1 
ATOM   2749 C CA  . ILE A 1 348 ? 38.598  -3.035  4.369   1.00 15.47 ?  348 ILE A CA  1 
ATOM   2750 C C   . ILE A 1 348 ? 38.042  -1.617  4.345   1.00 16.08 ?  348 ILE A C   1 
ATOM   2751 O O   . ILE A 1 348 ? 37.768  -1.034  5.400   1.00 15.81 ?  348 ILE A O   1 
ATOM   2752 C CB  . ILE A 1 348 ? 37.714  -3.951  5.227   1.00 17.27 ?  348 ILE A CB  1 
ATOM   2753 C CG1 . ILE A 1 348 ? 38.385  -5.307  5.449   1.00 18.33 ?  348 ILE A CG1 1 
ATOM   2754 C CG2 . ILE A 1 348 ? 36.340  -4.115  4.581   1.00 15.08 ?  348 ILE A CG2 1 
ATOM   2755 C CD1 . ILE A 1 348 ? 37.705  -6.142  6.549   1.00 20.80 ?  348 ILE A CD1 1 
ATOM   2756 N N   . ILE A 1 349 ? 37.866  -1.058  3.148   1.00 14.59 ?  349 ILE A N   1 
ATOM   2757 C CA  . ILE A 1 349 ? 37.238  0.247   2.992   1.00 13.63 ?  349 ILE A CA  1 
ATOM   2758 C C   . ILE A 1 349 ? 36.011  0.085   2.110   1.00 15.64 ?  349 ILE A C   1 
ATOM   2759 O O   . ILE A 1 349 ? 35.778  -0.971  1.528   1.00 17.11 ?  349 ILE A O   1 
ATOM   2760 C CB  . ILE A 1 349 ? 38.198  1.311   2.424   1.00 14.40 ?  349 ILE A CB  1 
ATOM   2761 C CG1 . ILE A 1 349 ? 38.778  0.870   1.062   1.00 15.73 ?  349 ILE A CG1 1 
ATOM   2762 C CG2 . ILE A 1 349 ? 39.288  1.627   3.451   1.00 15.41 ?  349 ILE A CG2 1 
ATOM   2763 C CD1 . ILE A 1 349 ? 39.726  1.890   0.457   1.00 16.13 ?  349 ILE A CD1 1 
ATOM   2764 N N   . SER A 1 350 ? 35.211  1.148   2.026   1.00 14.56 ?  350 SER A N   1 
ATOM   2765 C CA  . SER A 1 350 ? 33.969  1.120   1.263   1.00 15.46 ?  350 SER A CA  1 
ATOM   2766 C C   . SER A 1 350 ? 34.192  1.479   -0.189  1.00 14.16 ?  350 SER A C   1 
ATOM   2767 O O   . SER A 1 350 ? 34.736  2.547   -0.498  1.00 13.99 ?  350 SER A O   1 
ATOM   2768 C CB  . SER A 1 350 ? 32.920  2.069   1.846   1.00 17.15 ?  350 SER A CB  1 
ATOM   2769 O OG  . SER A 1 350 ? 32.773  1.870   3.239   1.00 20.27 ?  350 SER A OG  1 
ATOM   2770 N N   . ALA A 1 351 ? 33.723  0.613   -1.079  1.00 14.46 ?  351 ALA A N   1 
ATOM   2771 C CA  . ALA A 1 351 ? 33.689  0.982   -2.482  1.00 15.48 ?  351 ALA A CA  1 
ATOM   2772 C C   . ALA A 1 351 ? 32.621  2.046   -2.676  1.00 14.06 ?  351 ALA A C   1 
ATOM   2773 O O   . ALA A 1 351 ? 31.582  2.027   -2.012  1.00 15.75 ?  351 ALA A O   1 
ATOM   2774 C CB  . ALA A 1 351 ? 33.410  -0.240  -3.360  1.00 17.06 ?  351 ALA A CB  1 
ATOM   2775 N N   . GLY A 1 352 ? 32.887  2.996   -3.568  1.00 12.62 ?  352 GLY A N   1 
ATOM   2776 C CA  . GLY A 1 352 ? 31.939  4.064   -3.781  1.00 14.78 ?  352 GLY A CA  1 
ATOM   2777 C C   . GLY A 1 352 ? 30.726  3.687   -4.594  1.00 15.78 ?  352 GLY A C   1 
ATOM   2778 O O   . GLY A 1 352 ? 29.777  4.476   -4.664  1.00 16.30 ?  352 GLY A O   1 
ATOM   2779 N N   . ASN A 1 353 ? 30.727  2.488   -5.187  1.00 15.65 ?  353 ASN A N   1 
ATOM   2780 C CA  . ASN A 1 353 ? 29.680  2.124   -6.138  1.00 15.74 ?  353 ASN A CA  1 
ATOM   2781 C C   . ASN A 1 353 ? 28.301  2.207   -5.507  1.00 15.34 ?  353 ASN A C   1 
ATOM   2782 O O   . ASN A 1 353 ? 27.341  2.618   -6.166  1.00 15.92 ?  353 ASN A O   1 
ATOM   2783 C CB  . ASN A 1 353 ? 29.906  0.713   -6.667  1.00 16.73 ?  353 ASN A CB  1 
ATOM   2784 C CG  . ASN A 1 353 ? 31.228  0.559   -7.362  1.00 19.21 ?  353 ASN A CG  1 
ATOM   2785 O OD1 . ASN A 1 353 ? 32.283  0.786   -6.773  1.00 19.11 ?  353 ASN A OD1 1 
ATOM   2786 N ND2 . ASN A 1 353 ? 31.182  0.162   -8.627  1.00 23.51 ?  353 ASN A ND2 1 
ATOM   2787 N N   . GLY A 1 354 ? 28.185  1.813   -4.234  1.00 13.51 ?  354 GLY A N   1 
ATOM   2788 C CA  . GLY A 1 354 ? 26.893  1.790   -3.562  1.00 16.43 ?  354 GLY A CA  1 
ATOM   2789 C C   . GLY A 1 354 ? 26.251  3.151   -3.414  1.00 15.70 ?  354 GLY A C   1 
ATOM   2790 O O   . GLY A 1 354 ? 25.027  3.237   -3.220  1.00 13.93 ?  354 GLY A O   1 
ATOM   2791 N N   . TYR A 1 355 ? 27.042  4.223   -3.514  1.00 15.45 ?  355 TYR A N   1 
ATOM   2792 C CA  . TYR A 1 355 ? 26.513  5.572   -3.405  1.00 14.80 ?  355 TYR A CA  1 
ATOM   2793 C C   . TYR A 1 355 ? 25.972  6.085   -4.733  1.00 15.41 ?  355 TYR A C   1 
ATOM   2794 O O   . TYR A 1 355 ? 25.463  7.210   -4.787  1.00 14.43 ?  355 TYR A O   1 
ATOM   2795 C CB  . TYR A 1 355 ? 27.599  6.501   -2.840  1.00 12.92 ?  355 TYR A CB  1 
ATOM   2796 C CG  . TYR A 1 355 ? 28.110  5.984   -1.515  1.00 16.72 ?  355 TYR A CG  1 
ATOM   2797 C CD1 . TYR A 1 355 ? 27.354  6.126   -0.355  1.00 15.27 ?  355 TYR A CD1 1 
ATOM   2798 C CD2 . TYR A 1 355 ? 29.321  5.302   -1.427  1.00 15.00 ?  355 TYR A CD2 1 
ATOM   2799 C CE1 . TYR A 1 355 ? 27.804  5.624   0.860   1.00 17.24 ?  355 TYR A CE1 1 
ATOM   2800 C CE2 . TYR A 1 355 ? 29.775  4.797   -0.209  1.00 17.28 ?  355 TYR A CE2 1 
ATOM   2801 C CZ  . TYR A 1 355 ? 29.007  4.952   0.924   1.00 17.77 ?  355 TYR A CZ  1 
ATOM   2802 O OH  . TYR A 1 355 ? 29.448  4.447   2.131   1.00 18.50 ?  355 TYR A OH  1 
ATOM   2803 N N   . ARG A 1 356 ? 26.041  5.270   -5.782  1.00 13.28 ?  356 ARG A N   1 
ATOM   2804 C CA  . ARG A 1 356 ? 25.605  5.603   -7.141  1.00 13.33 ?  356 ARG A CA  1 
ATOM   2805 C C   . ARG A 1 356 ? 26.343  6.872   -7.581  1.00 16.49 ?  356 ARG A C   1 
ATOM   2806 O O   . ARG A 1 356 ? 27.507  7.074   -7.216  1.00 16.60 ?  356 ARG A O   1 
ATOM   2807 C CB  . ARG A 1 356 ? 24.080  5.668   -7.189  1.00 15.30 ?  356 ARG A CB  1 
ATOM   2808 C CG  . ARG A 1 356 ? 23.479  4.318   -6.846  1.00 16.50 ?  356 ARG A CG  1 
ATOM   2809 C CD  . ARG A 1 356 ? 21.982  4.276   -7.032  1.00 14.44 ?  356 ARG A CD  1 
ATOM   2810 N NE  . ARG A 1 356 ? 21.442  3.041   -6.473  1.00 15.68 ?  356 ARG A NE  1 
ATOM   2811 C CZ  . ARG A 1 356 ? 20.148  2.745   -6.475  1.00 17.31 ?  356 ARG A CZ  1 
ATOM   2812 N NH1 . ARG A 1 356 ? 19.293  3.598   -7.021  1.00 17.26 1  356 ARG A NH1 1 
ATOM   2813 N NH2 . ARG A 1 356 ? 19.722  1.605   -5.944  1.00 17.00 ?  356 ARG A NH2 1 
ATOM   2814 N N   . GLY A 1 357 ? 25.698  7.734   -8.357  1.00 15.88 ?  357 GLY A N   1 
ATOM   2815 C CA  . GLY A 1 357 ? 26.428  8.870   -8.898  1.00 17.50 ?  357 GLY A CA  1 
ATOM   2816 C C   . GLY A 1 357 ? 27.677  8.412   -9.618  1.00 19.45 ?  357 GLY A C   1 
ATOM   2817 O O   . GLY A 1 357 ? 27.663  7.418   -10.354 1.00 18.23 ?  357 GLY A O   1 
ATOM   2818 N N   . ASN A 1 358 ? 28.786  9.113   -9.367  1.00 15.66 ?  358 ASN A N   1 
ATOM   2819 C CA  . ASN A 1 358 ? 30.092  8.744   -9.903  1.00 20.78 ?  358 ASN A CA  1 
ATOM   2820 C C   . ASN A 1 358 ? 30.911  7.931   -8.901  1.00 19.21 ?  358 ASN A C   1 
ATOM   2821 O O   . ASN A 1 358 ? 32.147  7.892   -8.986  1.00 15.90 ?  358 ASN A O   1 
ATOM   2822 C CB  . ASN A 1 358 ? 30.857  9.989   -10.365 1.00 19.89 ?  358 ASN A CB  1 
ATOM   2823 C CG  . ASN A 1 358 ? 31.288  10.900  -9.216  1.00 20.43 ?  358 ASN A CG  1 
ATOM   2824 O OD1 . ASN A 1 358 ? 30.713  10.874  -8.138  1.00 16.46 ?  358 ASN A OD1 1 
ATOM   2825 N ND2 . ASN A 1 358 ? 32.302  11.729  -9.465  1.00 19.32 ?  358 ASN A ND2 1 
ATOM   2826 N N   . GLY A 1 359 ? 30.223  7.224   -7.994  1.00 17.86 ?  359 GLY A N   1 
ATOM   2827 C CA  . GLY A 1 359 ? 30.848  6.517   -6.893  1.00 15.75 ?  359 GLY A CA  1 
ATOM   2828 C C   . GLY A 1 359 ? 31.781  5.392   -7.298  1.00 17.34 ?  359 GLY A C   1 
ATOM   2829 O O   . GLY A 1 359 ? 32.641  5.011   -6.504  1.00 16.23 ?  359 GLY A O   1 
ATOM   2830 N N   . HIS A 1 360 ? 31.662  4.870   -8.520  1.00 17.09 ?  360 HIS A N   1 
ATOM   2831 C CA  . HIS A 1 360 ? 32.573  3.797   -8.916  1.00 18.43 ?  360 HIS A CA  1 
ATOM   2832 C C   . HIS A 1 360 ? 34.008  4.280   -9.073  1.00 18.42 ?  360 HIS A C   1 
ATOM   2833 O O   . HIS A 1 360 ? 34.914  3.447   -9.193  1.00 18.39 ?  360 HIS A O   1 
ATOM   2834 C CB  . HIS A 1 360 ? 32.106  3.145   -10.217 1.00 20.35 ?  360 HIS A CB  1 
ATOM   2835 C CG  . HIS A 1 360 ? 32.195  4.047   -11.401 1.00 22.38 ?  360 HIS A CG  1 
ATOM   2836 N ND1 . HIS A 1 360 ? 31.234  4.993   -11.684 1.00 22.13 ?  360 HIS A ND1 1 
ATOM   2837 C CD2 . HIS A 1 360 ? 33.135  4.158   -12.369 1.00 26.69 ?  360 HIS A CD2 1 
ATOM   2838 C CE1 . HIS A 1 360 ? 31.575  5.647   -12.780 1.00 28.51 ?  360 HIS A CE1 1 
ATOM   2839 N NE2 . HIS A 1 360 ? 32.724  5.158   -13.216 1.00 28.96 ?  360 HIS A NE2 1 
ATOM   2840 N N   . GLU A 1 361 ? 34.237  5.591   -9.070  1.00 14.69 ?  361 GLU A N   1 
ATOM   2841 C CA  . GLU A 1 361 ? 35.580  6.147   -9.137  1.00 17.49 ?  361 GLU A CA  1 
ATOM   2842 C C   . GLU A 1 361 ? 36.112  6.567   -7.776  1.00 17.81 ?  361 GLU A C   1 
ATOM   2843 O O   . GLU A 1 361 ? 37.124  7.272   -7.712  1.00 17.56 ?  361 GLU A O   1 
ATOM   2844 C CB  . GLU A 1 361 ? 35.614  7.348   -10.074 1.00 20.49 ?  361 GLU A CB  1 
ATOM   2845 C CG  . GLU A 1 361 ? 34.886  7.150   -11.369 1.00 26.38 ?  361 GLU A CG  1 
ATOM   2846 C CD  . GLU A 1 361 ? 35.084  8.331   -12.287 1.00 30.24 ?  361 GLU A CD  1 
ATOM   2847 O OE1 . GLU A 1 361 ? 34.443  9.385   -12.050 1.00 34.17 ?  361 GLU A OE1 1 
ATOM   2848 O OE2 . GLU A 1 361 ? 35.897  8.206   -13.226 1.00 36.16 -1 361 GLU A OE2 1 
ATOM   2849 N N   . PHE A 1 362 ? 35.458  6.150   -6.692  1.00 13.50 ?  362 PHE A N   1 
ATOM   2850 C CA  . PHE A 1 362 ? 35.796  6.627   -5.361  1.00 13.65 ?  362 PHE A CA  1 
ATOM   2851 C C   . PHE A 1 362 ? 35.829  5.477   -4.370  1.00 13.11 ?  362 PHE A C   1 
ATOM   2852 O O   . PHE A 1 362 ? 35.214  4.428   -4.572  1.00 14.95 ?  362 PHE A O   1 
ATOM   2853 C CB  . PHE A 1 362 ? 34.780  7.679   -4.872  1.00 13.76 ?  362 PHE A CB  1 
ATOM   2854 C CG  . PHE A 1 362 ? 34.883  8.978   -5.585  1.00 14.57 ?  362 PHE A CG  1 
ATOM   2855 C CD1 . PHE A 1 362 ? 34.269  9.149   -6.808  1.00 14.68 ?  362 PHE A CD1 1 
ATOM   2856 C CD2 . PHE A 1 362 ? 35.618  10.026  -5.044  1.00 16.15 ?  362 PHE A CD2 1 
ATOM   2857 C CE1 . PHE A 1 362 ? 34.373  10.346  -7.493  1.00 17.59 ?  362 PHE A CE1 1 
ATOM   2858 C CE2 . PHE A 1 362 ? 35.735  11.233  -5.727  1.00 15.27 ?  362 PHE A CE2 1 
ATOM   2859 C CZ  . PHE A 1 362 ? 35.100  11.387  -6.951  1.00 17.11 ?  362 PHE A CZ  1 
ATOM   2860 N N   . VAL A 1 363 ? 36.560  5.688   -3.284  1.00 12.41 ?  363 VAL A N   1 
ATOM   2861 C CA  . VAL A 1 363 ? 36.426  4.849   -2.106  1.00 13.96 ?  363 VAL A CA  1 
ATOM   2862 C C   . VAL A 1 363 ? 36.176  5.770   -0.924  1.00 15.10 ?  363 VAL A C   1 
ATOM   2863 O O   . VAL A 1 363 ? 36.517  6.957   -0.943  1.00 13.74 ?  363 VAL A O   1 
ATOM   2864 C CB  . VAL A 1 363 ? 37.658  3.950   -1.852  1.00 14.41 ?  363 VAL A CB  1 
ATOM   2865 C CG1 . VAL A 1 363 ? 37.837  2.955   -3.009  1.00 14.31 ?  363 VAL A CG1 1 
ATOM   2866 C CG2 . VAL A 1 363 ? 38.910  4.782   -1.652  1.00 16.29 ?  363 VAL A CG2 1 
ATOM   2867 N N   . ARG A 1 364 ? 35.565  5.207   0.107   1.00 12.94 ?  364 ARG A N   1 
ATOM   2868 C CA  . ARG A 1 364 ? 35.242  5.946   1.319   1.00 14.50 ?  364 ARG A CA  1 
ATOM   2869 C C   . ARG A 1 364 ? 35.960  5.290   2.485   1.00 14.18 ?  364 ARG A C   1 
ATOM   2870 O O   . ARG A 1 364 ? 35.839  4.073   2.696   1.00 13.62 ?  364 ARG A O   1 
ATOM   2871 C CB  . ARG A 1 364 ? 33.728  5.998   1.570   1.00 13.93 ?  364 ARG A CB  1 
ATOM   2872 C CG  . ARG A 1 364 ? 33.321  7.135   2.540   1.00 14.76 ?  364 ARG A CG  1 
ATOM   2873 C CD  . ARG A 1 364 ? 31.880  7.025   3.055   1.00 17.24 ?  364 ARG A CD  1 
ATOM   2874 N NE  . ARG A 1 364 ? 31.727  5.915   3.991   1.00 16.22 ?  364 ARG A NE  1 
ATOM   2875 C CZ  . ARG A 1 364 ? 30.607  5.607   4.637   1.00 21.72 ?  364 ARG A CZ  1 
ATOM   2876 N NH1 . ARG A 1 364 ? 29.509  6.335   4.466   1.00 20.33 1  364 ARG A NH1 1 
ATOM   2877 N NH2 . ARG A 1 364 ? 30.590  4.566   5.464   1.00 20.77 ?  364 ARG A NH2 1 
ATOM   2878 N N   . ILE A 1 365 ? 36.706  6.093   3.233   1.00 14.61 ?  365 ILE A N   1 
ATOM   2879 C CA  . ILE A 1 365 ? 37.572  5.608   4.296   1.00 14.23 ?  365 ILE A CA  1 
ATOM   2880 C C   . ILE A 1 365 ? 37.188  6.287   5.600   1.00 15.64 ?  365 ILE A C   1 
ATOM   2881 O O   . ILE A 1 365 ? 37.092  7.518   5.670   1.00 16.55 ?  365 ILE A O   1 
ATOM   2882 C CB  . ILE A 1 365 ? 39.057  5.850   3.977   1.00 12.88 ?  365 ILE A CB  1 
ATOM   2883 C CG1 . ILE A 1 365 ? 39.386  5.308   2.587   1.00 13.20 ?  365 ILE A CG1 1 
ATOM   2884 C CG2 . ILE A 1 365 ? 39.939  5.201   5.035   1.00 15.62 ?  365 ILE A CG2 1 
ATOM   2885 C CD1 . ILE A 1 365 ? 40.851  5.425   2.222   1.00 14.58 ?  365 ILE A CD1 1 
ATOM   2886 N N   . ASN A 1 366 ? 36.973  5.476   6.624   1.00 14.91 ?  366 ASN A N   1 
ATOM   2887 C CA  . ASN A 1 366 ? 36.586  5.949   7.945   1.00 16.14 ?  366 ASN A CA  1 
ATOM   2888 C C   . ASN A 1 366 ? 37.833  6.296   8.750   1.00 16.24 ?  366 ASN A C   1 
ATOM   2889 O O   . ASN A 1 366 ? 38.619  5.409   9.099   1.00 17.14 ?  366 ASN A O   1 
ATOM   2890 C CB  . ASN A 1 366 ? 35.772  4.867   8.650   1.00 15.44 ?  366 ASN A CB  1 
ATOM   2891 C CG  . ASN A 1 366 ? 35.304  5.290   10.045  1.00 18.74 ?  366 ASN A CG  1 
ATOM   2892 O OD1 . ASN A 1 366 ? 35.823  6.232   10.653  1.00 16.91 ?  366 ASN A OD1 1 
ATOM   2893 N ND2 . ASN A 1 366 ? 34.310  4.581   10.553  1.00 16.84 ?  366 ASN A ND2 1 
ATOM   2894 N N   . LEU A 1 367 ? 37.993  7.576   9.085   1.00 14.83 ?  367 LEU A N   1 
ATOM   2895 C CA  . LEU A 1 367 ? 39.152  8.024   9.848   1.00 13.56 ?  367 LEU A CA  1 
ATOM   2896 C C   . LEU A 1 367 ? 38.859  8.219   11.331  1.00 16.70 ?  367 LEU A C   1 
ATOM   2897 O O   . LEU A 1 367 ? 39.713  8.741   12.054  1.00 16.16 ?  367 LEU A O   1 
ATOM   2898 C CB  . LEU A 1 367 ? 39.699  9.319   9.253   1.00 15.65 ?  367 LEU A CB  1 
ATOM   2899 C CG  . LEU A 1 367 ? 40.203  9.167   7.820   1.00 15.91 ?  367 LEU A CG  1 
ATOM   2900 C CD1 . LEU A 1 367 ? 40.750  10.505  7.314   1.00 17.11 ?  367 LEU A CD1 1 
ATOM   2901 C CD2 . LEU A 1 367 ? 41.243  8.066   7.716   1.00 15.48 ?  367 LEU A CD2 1 
ATOM   2902 N N   . ALA A 1 368 ? 37.689  7.804   11.814  1.00 13.18 ?  368 ALA A N   1 
ATOM   2903 C CA  . ALA A 1 368 ? 37.370  7.959   13.236  1.00 13.30 ?  368 ALA A CA  1 
ATOM   2904 C C   . ALA A 1 368 ? 37.926  6.778   14.035  1.00 13.59 ?  368 ALA A C   1 
ATOM   2905 O O   . ALA A 1 368 ? 37.209  5.918   14.556  1.00 14.94 ?  368 ALA A O   1 
ATOM   2906 C CB  . ALA A 1 368 ? 35.868  8.107   13.431  1.00 14.45 ?  368 ALA A CB  1 
ATOM   2907 N N   . CYS A 1 369 ? 39.247  6.760   14.139  1.00 15.33 ?  369 CYS A N   1 
ATOM   2908 C CA  . CYS A 1 369 ? 39.948  5.707   14.864  1.00 15.82 ?  369 CYS A CA  1 
ATOM   2909 C C   . CYS A 1 369 ? 41.298  6.279   15.320  1.00 14.86 ?  369 CYS A C   1 
ATOM   2910 O O   . CYS A 1 369 ? 41.737  7.297   14.811  1.00 16.95 ?  369 CYS A O   1 
ATOM   2911 C CB  . CYS A 1 369 ? 40.128  4.469   13.981  1.00 16.40 ?  369 CYS A CB  1 
ATOM   2912 S SG  . CYS A 1 369 ? 41.036  4.812   12.448  1.00 18.65 ?  369 CYS A SG  1 
ATOM   2913 N N   . PRO A 1 370 ? 41.921  5.626   16.301  1.00 17.38 ?  370 PRO A N   1 
ATOM   2914 C CA  . PRO A 1 370 ? 43.231  6.129   16.767  1.00 18.15 ?  370 PRO A CA  1 
ATOM   2915 C C   . PRO A 1 370 ? 44.221  6.279   15.630  1.00 19.37 ?  370 PRO A C   1 
ATOM   2916 O O   . PRO A 1 370 ? 44.171  5.562   14.621  1.00 16.63 ?  370 PRO A O   1 
ATOM   2917 C CB  . PRO A 1 370 ? 43.671  5.052   17.767  1.00 17.78 ?  370 PRO A CB  1 
ATOM   2918 C CG  . PRO A 1 370 ? 42.356  4.499   18.284  1.00 18.50 ?  370 PRO A CG  1 
ATOM   2919 C CD  . PRO A 1 370 ? 41.468  4.472   17.077  1.00 15.14 ?  370 PRO A CD  1 
ATOM   2920 N N   . LYS A 1 371 ? 45.124  7.247   15.808  1.00 19.64 ?  371 LYS A N   1 
ATOM   2921 C CA  . LYS A 1 371 ? 46.121  7.551   14.788  1.00 20.72 ?  371 LYS A CA  1 
ATOM   2922 C C   . LYS A 1 371 ? 46.924  6.319   14.404  1.00 18.37 ?  371 LYS A C   1 
ATOM   2923 O O   . LYS A 1 371 ? 47.281  6.153   13.235  1.00 20.90 ?  371 LYS A O   1 
ATOM   2924 C CB  . LYS A 1 371 ? 47.044  8.657   15.286  1.00 21.54 ?  371 LYS A CB  1 
ATOM   2925 C CG  . LYS A 1 371 ? 48.057  9.124   14.267  1.00 24.99 ?  371 LYS A CG  1 
ATOM   2926 C CD  . LYS A 1 371 ? 47.416  10.091  13.281  1.00 27.09 ?  371 LYS A CD  1 
ATOM   2927 C CE  . LYS A 1 371 ? 48.143  11.428  13.294  1.00 30.42 ?  371 LYS A CE  1 
ATOM   2928 N NZ  . LYS A 1 371 ? 49.617  11.242  13.332  1.00 35.92 1  371 LYS A NZ  1 
ATOM   2929 N N   . GLU A 1 372 ? 47.193  5.433   15.361  1.00 19.67 ?  372 GLU A N   1 
ATOM   2930 C CA  . GLU A 1 372 ? 47.920  4.208   15.047  1.00 22.14 ?  372 GLU A CA  1 
ATOM   2931 C C   . GLU A 1 372 ? 47.185  3.385   13.992  1.00 21.36 ?  372 GLU A C   1 
ATOM   2932 O O   . GLU A 1 372 ? 47.814  2.823   13.088  1.00 20.18 ?  372 GLU A O   1 
ATOM   2933 C CB  . GLU A 1 372 ? 48.144  3.409   16.334  1.00 25.72 ?  372 GLU A CB  1 
ATOM   2934 C CG  . GLU A 1 372 ? 48.615  4.283   17.514  1.00 33.90 ?  372 GLU A CG  1 
ATOM   2935 C CD  . GLU A 1 372 ? 47.442  4.802   18.387  1.00 31.94 ?  372 GLU A CD  1 
ATOM   2936 O OE1 . GLU A 1 372 ? 47.044  5.986   18.240  1.00 29.39 ?  372 GLU A OE1 1 
ATOM   2937 O OE2 . GLU A 1 372 ? 46.915  4.021   19.216  1.00 44.22 -1 372 GLU A OE2 1 
ATOM   2938 N N   . LEU A 1 373 ? 45.849  3.327   14.067  1.00 17.92 ?  373 LEU A N   1 
ATOM   2939 C CA  . LEU A 1 373 ? 45.084  2.632   13.037  1.00 18.12 ?  373 LEU A CA  1 
ATOM   2940 C C   . LEU A 1 373 ? 45.051  3.414   11.726  1.00 17.62 ?  373 LEU A C   1 
ATOM   2941 O O   . LEU A 1 373 ? 45.009  2.801   10.656  1.00 17.78 ?  373 LEU A O   1 
ATOM   2942 C CB  . LEU A 1 373 ? 43.657  2.341   13.520  1.00 17.69 ?  373 LEU A CB  1 
ATOM   2943 C CG  . LEU A 1 373 ? 43.440  1.035   14.302  1.00 18.92 ?  373 LEU A CG  1 
ATOM   2944 C CD1 . LEU A 1 373 ? 44.102  1.113   15.660  1.00 19.63 ?  373 LEU A CD1 1 
ATOM   2945 C CD2 . LEU A 1 373 ? 41.961  0.738   14.489  1.00 18.21 ?  373 LEU A CD2 1 
ATOM   2946 N N   . VAL A 1 374 ? 45.066  4.753   11.776  1.00 16.99 ?  374 VAL A N   1 
ATOM   2947 C CA  . VAL A 1 374 ? 45.145  5.530   10.536  1.00 17.37 ?  374 VAL A CA  1 
ATOM   2948 C C   . VAL A 1 374 ? 46.479  5.282   9.839   1.00 18.57 ?  374 VAL A C   1 
ATOM   2949 O O   . VAL A 1 374 ? 46.531  5.090   8.617   1.00 19.21 ?  374 VAL A O   1 
ATOM   2950 C CB  . VAL A 1 374 ? 44.921  7.031   10.808  1.00 16.83 ?  374 VAL A CB  1 
ATOM   2951 C CG1 . VAL A 1 374 ? 45.069  7.834   9.522   1.00 17.30 ?  374 VAL A CG1 1 
ATOM   2952 C CG2 . VAL A 1 374 ? 43.548  7.275   11.402  1.00 16.84 ?  374 VAL A CG2 1 
ATOM   2953 N N   . ILE A 1 375 ? 47.575  5.260   10.604  1.00 18.10 ?  375 ILE A N   1 
ATOM   2954 C CA  . ILE A 1 375 ? 48.891  5.019   10.005  1.00 18.58 ?  375 ILE A CA  1 
ATOM   2955 C C   . ILE A 1 375 ? 48.944  3.633   9.375   1.00 20.90 ?  375 ILE A C   1 
ATOM   2956 O O   . ILE A 1 375 ? 49.428  3.459   8.247   1.00 18.58 ?  375 ILE A O   1 
ATOM   2957 C CB  . ILE A 1 375 ? 50.001  5.193   11.057  1.00 20.13 ?  375 ILE A CB  1 
ATOM   2958 C CG1 . ILE A 1 375 ? 50.063  6.626   11.567  1.00 20.79 ?  375 ILE A CG1 1 
ATOM   2959 C CG2 . ILE A 1 375 ? 51.353  4.800   10.477  1.00 25.15 ?  375 ILE A CG2 1 
ATOM   2960 C CD1 . ILE A 1 375 ? 50.873  6.741   12.832  1.00 22.04 ?  375 ILE A CD1 1 
ATOM   2961 N N   . ASP A 1 376 ? 48.454  2.622   10.098  1.00 19.61 ?  376 ASP A N   1 
ATOM   2962 C CA  . ASP A 1 376 ? 48.392  1.268   9.561   1.00 17.70 ?  376 ASP A CA  1 
ATOM   2963 C C   . ASP A 1 376 ? 47.566  1.227   8.279   1.00 20.64 ?  376 ASP A C   1 
ATOM   2964 O O   . ASP A 1 376 ? 47.976  0.631   7.272   1.00 20.11 ?  376 ASP A O   1 
ATOM   2965 C CB  . ASP A 1 376 ? 47.807  0.337   10.629  1.00 19.94 ?  376 ASP A CB  1 
ATOM   2966 C CG  . ASP A 1 376 ? 47.828  -1.125  10.230  1.00 22.12 ?  376 ASP A CG  1 
ATOM   2967 O OD1 . ASP A 1 376 ? 48.462  -1.488  9.216   1.00 24.03 ?  376 ASP A OD1 1 
ATOM   2968 O OD2 . ASP A 1 376 ? 47.195  -1.924  10.950  1.00 24.27 -1 376 ASP A OD2 1 
ATOM   2969 N N   . GLY A 1 377 ? 46.393  1.865   8.297   1.00 18.78 ?  377 GLY A N   1 
ATOM   2970 C CA  . GLY A 1 377 ? 45.522  1.819   7.138   1.00 18.95 ?  377 GLY A CA  1 
ATOM   2971 C C   . GLY A 1 377 ? 46.106  2.518   5.928   1.00 17.89 ?  377 GLY A C   1 
ATOM   2972 O O   . GLY A 1 377 ? 45.953  2.048   4.800   1.00 18.30 ?  377 GLY A O   1 
ATOM   2973 N N   . MET A 1 378 ? 46.761  3.660   6.139   1.00 18.87 ?  378 MET A N   1 
ATOM   2974 C CA  . MET A 1 378 ? 47.363  4.384   5.025   1.00 18.78 ?  378 MET A CA  1 
ATOM   2975 C C   . MET A 1 378 ? 48.499  3.577   4.396   1.00 20.03 ?  378 MET A C   1 
ATOM   2976 O O   . MET A 1 378 ? 48.649  3.546   3.167   1.00 19.64 ?  378 MET A O   1 
ATOM   2977 C CB  . MET A 1 378 ? 47.865  5.745   5.504   1.00 20.76 ?  378 MET A CB  1 
ATOM   2978 C CG  . MET A 1 378 ? 46.748  6.736   5.858   1.00 22.12 ?  378 MET A CG  1 
ATOM   2979 S SD  . MET A 1 378 ? 45.600  7.063   4.501   1.00 23.76 ?  378 MET A SD  1 
ATOM   2980 C CE  . MET A 1 378 ? 44.116  6.240   5.042   1.00 22.79 ?  378 MET A CE  1 
ATOM   2981 N N   . GLN A 1 379 ? 49.298  2.900   5.222   1.00 21.65 ?  379 GLN A N   1 
ATOM   2982 C CA  . GLN A 1 379 ? 50.391  2.104   4.676   1.00 22.93 ?  379 GLN A CA  1 
ATOM   2983 C C   . GLN A 1 379 ? 49.854  0.913   3.896   1.00 22.65 ?  379 GLN A C   1 
ATOM   2984 O O   . GLN A 1 379 ? 50.380  0.573   2.832   1.00 21.83 ?  379 GLN A O   1 
ATOM   2985 C CB  . GLN A 1 379 ? 51.333  1.656   5.792   1.00 24.85 ?  379 GLN A CB  1 
ATOM   2986 C CG  . GLN A 1 379 ? 52.557  0.894   5.283   1.00 30.57 ?  379 GLN A CG  1 
ATOM   2987 C CD  . GLN A 1 379 ? 53.410  1.711   4.320   1.00 33.92 ?  379 GLN A CD  1 
ATOM   2988 O OE1 . GLN A 1 379 ? 53.785  1.233   3.242   1.00 35.09 ?  379 GLN A OE1 1 
ATOM   2989 N NE2 . GLN A 1 379 ? 53.718  2.948   4.704   1.00 33.03 ?  379 GLN A NE2 1 
ATOM   2990 N N   . ARG A 1 380 ? 48.789  0.285   4.394   1.00 21.78 ?  380 ARG A N   1 
ATOM   2991 C CA  . ARG A 1 380 ? 48.163  -0.795  3.644   1.00 20.40 ?  380 ARG A CA  1 
ATOM   2992 C C   . ARG A 1 380 ? 47.606  -0.287  2.320   1.00 20.42 ?  380 ARG A C   1 
ATOM   2993 O O   . ARG A 1 380 ? 47.725  -0.957  1.287   1.00 21.22 ?  380 ARG A O   1 
ATOM   2994 C CB  . ARG A 1 380 ? 47.057  -1.447  4.479   1.00 19.75 ?  380 ARG A CB  1 
ATOM   2995 C CG  . ARG A 1 380 ? 47.535  -2.299  5.646   1.00 21.38 ?  380 ARG A CG  1 
ATOM   2996 C CD  . ARG A 1 380 ? 46.333  -2.887  6.390   1.00 21.58 ?  380 ARG A CD  1 
ATOM   2997 N NE  . ARG A 1 380 ? 46.619  -3.249  7.777   1.00 17.78 ?  380 ARG A NE  1 
ATOM   2998 C CZ  . ARG A 1 380 ? 46.182  -4.356  8.373   1.00 19.81 ?  380 ARG A CZ  1 
ATOM   2999 N NH1 . ARG A 1 380 ? 45.453  -5.235  7.701   1.00 20.26 1  380 ARG A NH1 1 
ATOM   3000 N NH2 . ARG A 1 380 ? 46.474  -4.588  9.648   1.00 22.06 ?  380 ARG A NH2 1 
ATOM   3001 N N   . LEU A 1 381 ? 46.985  0.895   2.327   1.00 19.68 ?  381 LEU A N   1 
ATOM   3002 C CA  . LEU A 1 381 ? 46.460  1.445   1.083   1.00 19.20 ?  381 LEU A CA  1 
ATOM   3003 C C   . LEU A 1 381 ? 47.593  1.740   0.105   1.00 21.23 ?  381 LEU A C   1 
ATOM   3004 O O   . LEU A 1 381 ? 47.505  1.403   -1.081  1.00 18.97 ?  381 LEU A O   1 
ATOM   3005 C CB  . LEU A 1 381 ? 45.641  2.705   1.377   1.00 19.39 ?  381 LEU A CB  1 
ATOM   3006 C CG  . LEU A 1 381 ? 45.199  3.537   0.178   1.00 21.23 ?  381 LEU A CG  1 
ATOM   3007 C CD1 . LEU A 1 381 ? 44.317  2.708   -0.756  1.00 22.48 ?  381 LEU A CD1 1 
ATOM   3008 C CD2 . LEU A 1 381 ? 44.464  4.789   0.642   1.00 19.69 ?  381 LEU A CD2 1 
ATOM   3009 N N   . LYS A 1 382 ? 48.690  2.303   0.602   1.00 21.34 ?  382 LYS A N   1 
ATOM   3010 C CA  . LYS A 1 382 ? 49.876  2.545   -0.255  1.00 23.27 ?  382 LYS A CA  1 
ATOM   3011 C C   . LYS A 1 382 ? 50.372  1.223   -0.834  1.00 22.54 ?  382 LYS A C   1 
ATOM   3012 O O   . LYS A 1 382 ? 50.606  1.162   -2.030  1.00 25.51 ?  382 LYS A O   1 
ATOM   3013 C CB  . LYS A 1 382 ? 51.004  3.173   0.564   1.00 22.44 ?  382 LYS A CB  1 
ATOM   3014 C CG  . LYS A 1 382 ? 52.333  3.336   -0.156  1.00 24.59 ?  382 LYS A CG  1 
ATOM   3015 C CD  . LYS A 1 382 ? 53.369  4.052   0.671   1.00 28.24 ?  382 LYS A CD  1 
ATOM   3016 C CE  . LYS A 1 382 ? 54.698  3.333   0.689   1.00 36.06 ?  382 LYS A CE  1 
ATOM   3017 N NZ  . LYS A 1 382 ? 55.837  4.272   0.589   1.00 37.46 1  382 LYS A NZ  1 
ATOM   3018 N N   . GLN A 1 383 ? 50.525  0.221   0.018   1.00 30.00 ?  383 GLN A N   1 
ATOM   3019 C CA  . GLN A 1 383 ? 51.037  -1.092  -0.438  1.00 30.00 ?  383 GLN A CA  1 
ATOM   3020 C C   . GLN A 1 383 ? 50.117  -1.675  -1.518  1.00 30.00 ?  383 GLN A C   1 
ATOM   3021 O O   . GLN A 1 383 ? 50.617  -2.249  -2.464  1.00 30.00 ?  383 GLN A O   1 
ATOM   3022 C CB  . GLN A 1 383 ? 51.242  -2.028  0.750   1.00 30.00 ?  383 GLN A CB  1 
ATOM   3023 C CG  . GLN A 1 383 ? 52.449  -1.694  1.611   1.00 30.00 ?  383 GLN A CG  1 
ATOM   3024 C CD  . GLN A 1 383 ? 53.746  -1.752  0.846   1.00 30.00 ?  383 GLN A CD  1 
ATOM   3025 O OE1 . GLN A 1 383 ? 54.062  -2.749  0.202   1.00 30.00 ?  383 GLN A OE1 1 
ATOM   3026 N NE2 . GLN A 1 383 ? 54.510  -0.674  0.917   1.00 30.00 ?  383 GLN A NE2 1 
ATOM   3027 N N   . GLY A 1 384 ? 48.811  -1.540  -1.340  1.00 21.89 ?  384 GLY A N   1 
ATOM   3028 C CA  . GLY A 1 384 ? 47.872  -2.042  -2.344  1.00 21.64 ?  384 GLY A CA  1 
ATOM   3029 C C   . GLY A 1 384 ? 48.010  -1.286  -3.648  1.00 26.67 ?  384 GLY A C   1 
ATOM   3030 O O   . GLY A 1 384 ? 47.986  -1.920  -4.688  1.00 27.83 ?  384 GLY A O   1 
ATOM   3031 N N   . VAL A 1 385 ? 48.163  0.029   -3.569  1.00 24.78 ?  385 VAL A N   1 
ATOM   3032 C CA  . VAL A 1 385 ? 48.369  0.757   -4.817  1.00 26.15 ?  385 VAL A CA  1 
ATOM   3033 C C   . VAL A 1 385 ? 49.702  0.356   -5.438  1.00 28.95 ?  385 VAL A C   1 
ATOM   3034 O O   . VAL A 1 385 ? 49.781  0.065   -6.637  1.00 31.11 ?  385 VAL A O   1 
ATOM   3035 C CB  . VAL A 1 385 ? 48.280  2.279   -4.579  1.00 23.71 ?  385 VAL A CB  1 
ATOM   3036 C CG1 . VAL A 1 385 ? 48.751  3.040   -5.795  1.00 28.87 ?  385 VAL A CG1 1 
ATOM   3037 C CG2 . VAL A 1 385 ? 46.857  2.684   -4.232  1.00 24.98 ?  385 VAL A CG2 1 
ATOM   3038 N N   . LEU A 1 386 ? 50.758  0.293   -4.621  1.00 27.18 ?  386 LEU A N   1 
ATOM   3039 C CA  . LEU A 1 386 ? 52.082  -0.102  -5.102  1.00 33.31 ?  386 LEU A CA  1 
ATOM   3040 C C   . LEU A 1 386 ? 52.056  -1.443  -5.824  1.00 34.31 ?  386 LEU A C   1 
ATOM   3041 O O   . LEU A 1 386 ? 52.775  -1.635  -6.811  1.00 40.11 ?  386 LEU A O   1 
ATOM   3042 C CB  . LEU A 1 386 ? 53.063  -0.176  -3.932  1.00 32.51 ?  386 LEU A CB  1 
ATOM   3043 C CG  . LEU A 1 386 ? 53.986  1.010   -3.687  1.00 36.83 ?  386 LEU A CG  1 
ATOM   3044 C CD1 . LEU A 1 386 ? 55.067  0.604   -2.683  1.00 39.60 ?  386 LEU A CD1 1 
ATOM   3045 C CD2 . LEU A 1 386 ? 54.592  1.497   -5.000  1.00 37.33 ?  386 LEU A CD2 1 
ATOM   3046 N N   . ASN A 1 387 ? 51.260  -2.392  -5.334  1.00 34.41 ?  387 ASN A N   1 
ATOM   3047 C CA  . ASN A 1 387 ? 51.313  -3.758  -5.845  1.00 39.21 ?  387 ASN A CA  1 
ATOM   3048 C C   . ASN A 1 387 ? 50.477  -3.972  -7.101  1.00 42.82 ?  387 ASN A C   1 
ATOM   3049 O O   . ASN A 1 387 ? 50.481  -5.085  -7.640  1.00 43.97 ?  387 ASN A O   1 
ATOM   3050 C CB  . ASN A 1 387 ? 50.868  -4.744  -4.762  1.00 39.22 ?  387 ASN A CB  1 
ATOM   3051 C CG  . ASN A 1 387 ? 52.006  -5.164  -3.855  1.00 45.09 ?  387 ASN A CG  1 
ATOM   3052 O OD1 . ASN A 1 387 ? 52.986  -4.432  -3.694  1.00 45.33 ?  387 ASN A OD1 1 
ATOM   3053 N ND2 . ASN A 1 387 ? 51.881  -6.345  -3.249  1.00 44.81 ?  387 ASN A ND2 1 
ATOM   3054 N N   . LEU A 1 388 ? 49.765  -2.949  -7.581  1.00 39.74 ?  388 LEU A N   1 
ATOM   3055 C CA  . LEU A 1 388 ? 48.988  -3.106  -8.806  1.00 40.50 ?  388 LEU A CA  1 
ATOM   3056 C C   . LEU A 1 388 ? 49.893  -3.186  -10.031 1.00 46.71 ?  388 LEU A C   1 
ATOM   3057 O O   . LEU A 1 388 ? 49.744  -4.090  -10.864 1.00 51.20 ?  388 LEU A O   1 
ATOM   3058 C CB  . LEU A 1 388 ? 47.994  -1.958  -8.951  1.00 38.03 ?  388 LEU A CB  1 
ATOM   3059 C CG  . LEU A 1 388 ? 46.763  -1.995  -8.054  1.00 32.65 ?  388 LEU A CG  1 
ATOM   3060 C CD1 . LEU A 1 388 ? 45.888  -0.797  -8.357  1.00 30.85 ?  388 LEU A CD1 1 
ATOM   3061 C CD2 . LEU A 1 388 ? 45.992  -3.282  -8.269  1.00 33.23 ?  388 LEU A CD2 1 
ATOM   3062 N N   . ASN A 1 389 ? 50.833  -2.243  -10.168 1.00 49.63 ?  389 ASN A N   1 
ATOM   3063 C CA  . ASN A 1 389 ? 51.756  -2.244  -11.303 1.00 54.73 ?  389 ASN A CA  1 
ATOM   3064 C C   . ASN A 1 389 ? 52.989  -3.115  -11.065 1.00 55.09 ?  389 ASN A C   1 
ATOM   3065 O O   . ASN A 1 389 ? 53.968  -3.005  -11.816 1.00 58.73 ?  389 ASN A O   1 
ATOM   3066 C CB  . ASN A 1 389 ? 52.175  -0.812  -11.655 1.00 54.81 ?  389 ASN A CB  1 
ATOM   3067 C CG  . ASN A 1 389 ? 51.211  -0.148  -12.631 1.00 62.01 ?  389 ASN A CG  1 
ATOM   3068 O OD1 . ASN A 1 389 ? 51.557  0.115   -13.788 1.00 62.71 ?  389 ASN A OD1 1 
ATOM   3069 N ND2 . ASN A 1 389 ? 49.988  0.116   -12.169 1.00 60.22 ?  389 ASN A ND2 1 
ATOM   3070 N N   . ASN A 1 390 ? 52.952  -3.969  -10.043 1.00 53.79 ?  390 ASN A N   1 
ATOM   3071 C CA  . ASN A 1 390 ? 53.948  -5.017  -9.837  1.00 54.39 ?  390 ASN A CA  1 
ATOM   3072 C C   . ASN A 1 390 ? 53.348  -6.389  -10.171 1.00 55.87 ?  390 ASN A C   1 
ATOM   3073 O O   . ASN A 1 390 ? 52.127  -6.534  -10.292 1.00 54.14 ?  390 ASN A O   1 
ATOM   3074 C CB  . ASN A 1 390 ? 54.459  -5.013  -8.394  1.00 51.29 ?  390 ASN A CB  1 
ATOM   3075 C CG  . ASN A 1 390 ? 55.286  -3.786  -8.068  1.00 54.32 ?  390 ASN A CG  1 
ATOM   3076 O OD1 . ASN A 1 390 ? 56.034  -3.282  -8.909  1.00 56.55 ?  390 ASN A OD1 1 
ATOM   3077 N ND2 . ASN A 1 390 ? 55.159  -3.300  -6.835  1.00 50.39 ?  390 ASN A ND2 1 
ATOM   3078 O OXT . ASN A 1 390 ? 54.059  -7.390  -10.322 1.00 54.48 -1 390 ASN A OXT 1 
ATOM   3079 N N   . LYS B 1 4   ? 13.635  -18.145 49.072  1.00 55.44 ?  4   LYS B N   1 
ATOM   3080 C CA  . LYS B 1 4   ? 13.681  -17.303 47.841  1.00 47.80 ?  4   LYS B CA  1 
ATOM   3081 C C   . LYS B 1 4   ? 15.116  -16.792 47.660  1.00 42.31 ?  4   LYS B C   1 
ATOM   3082 O O   . LYS B 1 4   ? 15.569  -16.040 48.528  1.00 41.19 ?  4   LYS B O   1 
ATOM   3083 C CB  . LYS B 1 4   ? 12.678  -16.138 47.877  1.00 39.59 ?  4   LYS B CB  1 
ATOM   3084 C CG  . LYS B 1 4   ? 11.768  -16.019 46.664  1.00 38.27 ?  4   LYS B CG  1 
ATOM   3085 C CD  . LYS B 1 4   ? 10.291  -16.128 46.971  1.00 39.58 ?  4   LYS B CD  1 
ATOM   3086 C CE  . LYS B 1 4   ? 9.588   -17.165 46.122  1.00 34.49 ?  4   LYS B CE  1 
ATOM   3087 N NZ  . LYS B 1 4   ? 8.257   -17.511 46.673  1.00 34.53 1  4   LYS B NZ  1 
ATOM   3088 N N   . GLN B 1 5   ? 15.766  -17.150 46.546  1.00 37.46 ?  5   GLN B N   1 
ATOM   3089 C CA  . GLN B 1 5   ? 17.140  -16.643 46.275  1.00 37.63 ?  5   GLN B CA  1 
ATOM   3090 C C   . GLN B 1 5   ? 17.040  -15.203 45.727  1.00 35.49 ?  5   GLN B C   1 
ATOM   3091 O O   . GLN B 1 5   ? 17.982  -14.423 45.888  1.00 31.90 ?  5   GLN B O   1 
ATOM   3092 C CB  . GLN B 1 5   ? 17.965  -17.661 45.468  1.00 38.70 ?  5   GLN B CB  1 
ATOM   3093 C CG  . GLN B 1 5   ? 18.637  -17.115 44.219  1.00 41.18 ?  5   GLN B CG  1 
ATOM   3094 C CD  . GLN B 1 5   ? 20.127  -16.911 44.340  1.00 54.35 ?  5   GLN B CD  1 
ATOM   3095 O OE1 . GLN B 1 5   ? 20.661  -15.867 43.969  1.00 57.66 ?  5   GLN B OE1 1 
ATOM   3096 N NE2 . GLN B 1 5   ? 20.817  -17.918 44.850  1.00 53.74 ?  5   GLN B NE2 1 
ATOM   3097 N N   . TYR B 1 6   ? 15.888  -14.856 45.171  1.00 30.37 ?  6   TYR B N   1 
ATOM   3098 C CA  . TYR B 1 6   ? 15.763  -13.536 44.535  1.00 25.75 ?  6   TYR B CA  1 
ATOM   3099 C C   . TYR B 1 6   ? 14.872  -12.597 45.341  1.00 25.30 ?  6   TYR B C   1 
ATOM   3100 O O   . TYR B 1 6   ? 14.185  -13.042 46.242  1.00 29.79 ?  6   TYR B O   1 
ATOM   3101 C CB  . TYR B 1 6   ? 15.295  -13.746 43.103  1.00 21.65 ?  6   TYR B CB  1 
ATOM   3102 C CG  . TYR B 1 6   ? 16.149  -14.687 42.299  1.00 22.59 ?  6   TYR B CG  1 
ATOM   3103 C CD1 . TYR B 1 6   ? 17.386  -14.293 41.832  1.00 22.58 ?  6   TYR B CD1 1 
ATOM   3104 C CD2 . TYR B 1 6   ? 15.721  -15.964 41.997  1.00 23.28 ?  6   TYR B CD2 1 
ATOM   3105 C CE1 . TYR B 1 6   ? 18.169  -15.138 41.067  1.00 23.10 ?  6   TYR B CE1 1 
ATOM   3106 C CE2 . TYR B 1 6   ? 16.499  -16.830 41.253  1.00 23.96 ?  6   TYR B CE2 1 
ATOM   3107 C CZ  . TYR B 1 6   ? 17.723  -16.410 40.775  1.00 23.74 ?  6   TYR B CZ  1 
ATOM   3108 O OH  . TYR B 1 6   ? 18.495  -17.250 40.040  1.00 24.61 ?  6   TYR B OH  1 
ATOM   3109 N N   . ASP B 1 7   ? 14.858  -11.332 44.963  1.00 20.95 ?  7   ASP B N   1 
ATOM   3110 C CA  . ASP B 1 7   ? 14.137  -10.294 45.696  1.00 20.90 ?  7   ASP B CA  1 
ATOM   3111 C C   . ASP B 1 7   ? 12.787  -10.058 45.022  1.00 20.34 ?  7   ASP B C   1 
ATOM   3112 O O   . ASP B 1 7   ? 12.726  -9.521  43.912  1.00 19.70 ?  7   ASP B O   1 
ATOM   3113 C CB  . ASP B 1 7   ? 14.989  -9.023  45.730  1.00 22.23 ?  7   ASP B CB  1 
ATOM   3114 C CG  . ASP B 1 7   ? 14.295  -7.832  46.392  1.00 25.53 ?  7   ASP B CG  1 
ATOM   3115 O OD1 . ASP B 1 7   ? 13.052  -7.694  46.332  1.00 22.60 ?  7   ASP B OD1 1 
ATOM   3116 O OD2 . ASP B 1 7   ? 15.027  -6.985  46.950  1.00 29.19 -1 7   ASP B OD2 1 
ATOM   3117 N N   . PHE B 1 8   ? 11.700  -10.437 45.697  1.00 18.59 ?  8   PHE B N   1 
ATOM   3118 C CA  . PHE B 1 8   ? 10.355  -10.115 45.226  1.00 17.92 ?  8   PHE B CA  1 
ATOM   3119 C C   . PHE B 1 8   ? 9.599   -9.245  46.228  1.00 19.98 ?  8   PHE B C   1 
ATOM   3120 O O   . PHE B 1 8   ? 8.360   -9.243  46.246  1.00 18.94 ?  8   PHE B O   1 
ATOM   3121 C CB  . PHE B 1 8   ? 9.576   -11.397 44.901  1.00 16.50 ?  8   PHE B CB  1 
ATOM   3122 C CG  . PHE B 1 8   ? 10.194  -12.213 43.770  1.00 19.89 ?  8   PHE B CG  1 
ATOM   3123 C CD1 . PHE B 1 8   ? 9.929   -11.906 42.437  1.00 16.56 ?  8   PHE B CD1 1 
ATOM   3124 C CD2 . PHE B 1 8   ? 11.049  -13.277 44.047  1.00 18.89 ?  8   PHE B CD2 1 
ATOM   3125 C CE1 . PHE B 1 8   ? 10.500  -12.654 41.394  1.00 16.00 ?  8   PHE B CE1 1 
ATOM   3126 C CE2 . PHE B 1 8   ? 11.617  -14.027 43.017  1.00 18.91 ?  8   PHE B CE2 1 
ATOM   3127 C CZ  . PHE B 1 8   ? 11.343  -13.713 41.687  1.00 16.61 ?  8   PHE B CZ  1 
ATOM   3128 N N   . THR B 1 9   ? 10.320  -8.481  47.050  1.00 20.73 ?  9   THR B N   1 
ATOM   3129 C CA  . THR B 1 9   ? 9.690   -7.613  48.034  1.00 21.83 ?  9   THR B CA  1 
ATOM   3130 C C   . THR B 1 9   ? 9.942   -6.132  47.807  1.00 23.75 ?  9   THR B C   1 
ATOM   3131 O O   . THR B 1 9   ? 9.079   -5.326  48.133  1.00 25.56 ?  9   THR B O   1 
ATOM   3132 C CB  . THR B 1 9   ? 10.137  -7.989  49.460  1.00 25.37 ?  9   THR B CB  1 
ATOM   3133 O OG1 . THR B 1 9   ? 11.560  -7.892  49.567  1.00 29.31 ?  9   THR B OG1 1 
ATOM   3134 C CG2 . THR B 1 9   ? 9.711   -9.418  49.796  1.00 23.38 ?  9   THR B CG2 1 
ATOM   3135 N N   . HIS B 1 10  ? 11.074  -5.738  47.244  1.00 21.80 ?  10  HIS B N   1 
ATOM   3136 C CA  . HIS B 1 10  ? 11.370  -4.322  47.080  1.00 21.49 ?  10  HIS B CA  1 
ATOM   3137 C C   . HIS B 1 10  ? 10.959  -3.863  45.690  1.00 21.63 ?  10  HIS B C   1 
ATOM   3138 O O   . HIS B 1 10  ? 11.354  -4.474  44.695  1.00 21.44 ?  10  HIS B O   1 
ATOM   3139 C CB  . HIS B 1 10  ? 12.853  -4.052  47.310  1.00 22.59 ?  10  HIS B CB  1 
ATOM   3140 C CG  . HIS B 1 10  ? 13.312  -4.410  48.686  1.00 26.34 ?  10  HIS B CG  1 
ATOM   3141 N ND1 . HIS B 1 10  ? 13.938  -5.604  48.971  1.00 27.97 ?  10  HIS B ND1 1 
ATOM   3142 C CD2 . HIS B 1 10  ? 13.219  -3.743  49.862  1.00 30.61 ?  10  HIS B CD2 1 
ATOM   3143 C CE1 . HIS B 1 10  ? 14.220  -5.654  50.262  1.00 30.55 ?  10  HIS B CE1 1 
ATOM   3144 N NE2 . HIS B 1 10  ? 13.800  -4.534  50.823  1.00 35.26 ?  10  HIS B NE2 1 
ATOM   3145 N N   . VAL B 1 11  ? 10.164  -2.798  45.634  1.00 19.47 ?  11  VAL B N   1 
ATOM   3146 C CA  . VAL B 1 11  ? 9.758   -2.153  44.386  1.00 17.10 ?  11  VAL B CA  1 
ATOM   3147 C C   . VAL B 1 11  ? 10.918  -1.338  43.820  1.00 19.69 ?  11  VAL B C   1 
ATOM   3148 O O   . VAL B 1 11  ? 11.441  -0.444  44.502  1.00 17.99 ?  11  VAL B O   1 
ATOM   3149 C CB  . VAL B 1 11  ? 8.533   -1.251  44.598  1.00 19.82 ?  11  VAL B CB  1 
ATOM   3150 C CG1 . VAL B 1 11  ? 8.150   -0.560  43.293  1.00 18.22 ?  11  VAL B CG1 1 
ATOM   3151 C CG2 . VAL B 1 11  ? 7.382   -2.055  45.144  1.00 20.26 ?  11  VAL B CG2 1 
ATOM   3152 N N   . PRO B 1 12  ? 11.348  -1.604  42.586  1.00 20.86 ?  12  PRO B N   1 
ATOM   3153 C CA  . PRO B 1 12  ? 12.423  -0.798  41.996  1.00 18.21 ?  12  PRO B CA  1 
ATOM   3154 C C   . PRO B 1 12  ? 12.025  0.674   41.872  1.00 20.03 ?  12  PRO B C   1 
ATOM   3155 O O   . PRO B 1 12  ? 10.904  1.011   41.483  1.00 17.37 ?  12  PRO B O   1 
ATOM   3156 C CB  . PRO B 1 12  ? 12.646  -1.457  40.628  1.00 18.32 ?  12  PRO B CB  1 
ATOM   3157 C CG  . PRO B 1 12  ? 12.160  -2.863  40.797  1.00 17.87 ?  12  PRO B CG  1 
ATOM   3158 C CD  . PRO B 1 12  ? 10.996  -2.770  41.756  1.00 16.95 ?  12  PRO B CD  1 
ATOM   3159 N N   . LYS B 1 13  ? 12.953  1.553   42.248  1.00 20.22 ?  13  LYS B N   1 
ATOM   3160 C CA  . LYS B 1 13  ? 12.736  2.992   42.154  1.00 22.52 ?  13  LYS B CA  1 
ATOM   3161 C C   . LYS B 1 13  ? 13.087  3.448   40.743  1.00 20.28 ?  13  LYS B C   1 
ATOM   3162 O O   . LYS B 1 13  ? 14.236  3.307   40.305  1.00 21.01 ?  13  LYS B O   1 
ATOM   3163 C CB  . LYS B 1 13  ? 13.567  3.742   43.198  1.00 23.82 ?  13  LYS B CB  1 
ATOM   3164 C CG  . LYS B 1 13  ? 12.869  3.857   44.549  1.00 30.95 ?  13  LYS B CG  1 
ATOM   3165 C CD  . LYS B 1 13  ? 13.822  3.723   45.743  1.00 33.46 ?  13  LYS B CD  1 
ATOM   3166 C CE  . LYS B 1 13  ? 13.187  2.890   46.868  1.00 28.96 ?  13  LYS B CE  1 
ATOM   3167 N NZ  . LYS B 1 13  ? 11.857  3.436   47.303  1.00 35.44 1  13  LYS B NZ  1 
ATOM   3168 N N   . ARG B 1 14  ? 12.099  3.971   40.034  1.00 20.79 ?  14  ARG B N   1 
ATOM   3169 C CA  . ARG B 1 14  ? 12.254  4.313   38.632  1.00 19.21 ?  14  ARG B CA  1 
ATOM   3170 C C   . ARG B 1 14  ? 12.750  5.747   38.470  1.00 20.14 ?  14  ARG B C   1 
ATOM   3171 O O   . ARG B 1 14  ? 12.646  6.579   39.374  1.00 20.56 ?  14  ARG B O   1 
ATOM   3172 C CB  . ARG B 1 14  ? 10.928  4.150   37.885  1.00 19.99 ?  14  ARG B CB  1 
ATOM   3173 C CG  . ARG B 1 14  ? 10.083  2.976   38.335  1.00 23.19 ?  14  ARG B CG  1 
ATOM   3174 C CD  . ARG B 1 14  ? 10.745  1.644   38.049  1.00 19.24 ?  14  ARG B CD  1 
ATOM   3175 N NE  . ARG B 1 14  ? 9.786   0.728   37.440  1.00 20.72 ?  14  ARG B NE  1 
ATOM   3176 C CZ  . ARG B 1 14  ? 9.038   -0.149  38.106  1.00 20.16 ?  14  ARG B CZ  1 
ATOM   3177 N NH1 . ARG B 1 14  ? 9.142   -0.272  39.427  1.00 18.50 1  14  ARG B NH1 1 
ATOM   3178 N NH2 . ARG B 1 14  ? 8.189   -0.922  37.439  1.00 20.49 ?  14  ARG B NH2 1 
ATOM   3179 N N   . GLN B 1 15  ? 13.266  6.035   37.284  1.00 17.81 ?  15  GLN B N   1 
ATOM   3180 C CA  . GLN B 1 15  ? 13.515  7.417   36.908  1.00 19.78 ?  15  GLN B CA  1 
ATOM   3181 C C   . GLN B 1 15  ? 12.185  8.095   36.560  1.00 20.97 ?  15  GLN B C   1 
ATOM   3182 O O   . GLN B 1 15  ? 11.118  7.470   36.534  1.00 19.63 ?  15  GLN B O   1 
ATOM   3183 C CB  . GLN B 1 15  ? 14.520  7.476   35.760  1.00 19.27 ?  15  GLN B CB  1 
ATOM   3184 C CG  . GLN B 1 15  ? 15.922  7.072   36.204  1.00 20.25 ?  15  GLN B CG  1 
ATOM   3185 C CD  . GLN B 1 15  ? 17.002  7.409   35.206  1.00 21.79 ?  15  GLN B CD  1 
ATOM   3186 O OE1 . GLN B 1 15  ? 16.747  7.983   34.136  1.00 20.33 ?  15  GLN B OE1 1 
ATOM   3187 N NE2 . GLN B 1 15  ? 18.231  7.045   35.549  1.00 22.10 ?  15  GLN B NE2 1 
ATOM   3188 N N   . GLY B 1 16  ? 12.249  9.398   36.281  1.00 20.35 ?  16  GLY B N   1 
ATOM   3189 C CA  . GLY B 1 16  ? 11.040  10.204  36.221  1.00 22.54 ?  16  GLY B CA  1 
ATOM   3190 C C   . GLY B 1 16  ? 10.125  9.921   35.046  1.00 22.12 ?  16  GLY B C   1 
ATOM   3191 O O   . GLY B 1 16  ? 8.937   10.240  35.117  1.00 24.57 ?  16  GLY B O   1 
ATOM   3192 N N   . ASN B 1 17  ? 10.638  9.347   33.963  1.00 21.20 ?  17  ASN B N   1 
ATOM   3193 C CA  . ASN B 1 17  ? 9.819   9.146   32.774  1.00 20.56 ?  17  ASN B CA  1 
ATOM   3194 C C   . ASN B 1 17  ? 9.169   7.765   32.734  1.00 20.37 ?  17  ASN B C   1 
ATOM   3195 O O   . ASN B 1 17  ? 8.749   7.316   31.664  1.00 21.72 ?  17  ASN B O   1 
ATOM   3196 C CB  . ASN B 1 17  ? 10.650  9.392   31.508  1.00 17.88 ?  17  ASN B CB  1 
ATOM   3197 C CG  . ASN B 1 17  ? 11.769  8.378   31.336  1.00 18.68 ?  17  ASN B CG  1 
ATOM   3198 O OD1 . ASN B 1 17  ? 12.415  7.991   32.302  1.00 19.49 ?  17  ASN B OD1 1 
ATOM   3199 N ND2 . ASN B 1 17  ? 12.011  7.959   30.103  1.00 18.14 ?  17  ASN B ND2 1 
ATOM   3200 N N   . SER B 1 18  ? 9.057   7.095   33.874  1.00 20.97 ?  18  SER B N   1 
ATOM   3201 C CA  . SER B 1 18  ? 8.362   5.815   33.916  1.00 19.54 ?  18  SER B CA  1 
ATOM   3202 C C   . SER B 1 18  ? 6.868   6.032   33.700  1.00 20.48 ?  18  SER B C   1 
ATOM   3203 O O   . SER B 1 18  ? 6.259   6.905   34.325  1.00 21.31 ?  18  SER B O   1 
ATOM   3204 C CB  . SER B 1 18  ? 8.618   5.122   35.256  1.00 21.77 ?  18  SER B CB  1 
ATOM   3205 O OG  . SER B 1 18  ? 7.600   4.191   35.557  1.00 20.44 ?  18  SER B OG  1 
ATOM   3206 N N   . ILE B 1 19  ? 6.274   5.249   32.799  1.00 17.27 ?  19  ILE B N   1 
ATOM   3207 C CA  . ILE B 1 19  ? 4.830   5.341   32.599  1.00 18.70 ?  19  ILE B CA  1 
ATOM   3208 C C   . ILE B 1 19  ? 4.089   4.892   33.851  1.00 18.01 ?  19  ILE B C   1 
ATOM   3209 O O   . ILE B 1 19  ? 3.108   5.518   34.264  1.00 18.40 ?  19  ILE B O   1 
ATOM   3210 C CB  . ILE B 1 19  ? 4.396   4.519   31.375  1.00 18.90 ?  19  ILE B CB  1 
ATOM   3211 C CG1 . ILE B 1 19  ? 5.091   5.044   30.122  1.00 21.33 ?  19  ILE B CG1 1 
ATOM   3212 C CG2 . ILE B 1 19  ? 2.882   4.590   31.204  1.00 17.25 ?  19  ILE B CG2 1 
ATOM   3213 C CD1 . ILE B 1 19  ? 4.568   6.368   29.712  1.00 20.11 ?  19  ILE B CD1 1 
ATOM   3214 N N   . LYS B 1 20  ? 4.547   3.832   34.484  1.00 19.06 ?  20  LYS B N   1 
ATOM   3215 C CA  . LYS B 1 20  ? 3.747   3.288   35.608  1.00 18.41 ?  20  LYS B CA  1 
ATOM   3216 C C   . LYS B 1 20  ? 3.876   4.149   36.857  1.00 20.99 ?  20  LYS B C   1 
ATOM   3217 O O   . LYS B 1 20  ? 2.906   4.319   37.553  1.00 18.18 ?  20  LYS B O   1 
ATOM   3218 C CB  . LYS B 1 20  ? 4.218   1.875   35.946  1.00 19.04 ?  20  LYS B CB  1 
ATOM   3219 C CG  . LYS B 1 20  ? 3.400   1.129   36.990  1.00 16.73 ?  20  LYS B CG  1 
ATOM   3220 C CD  . LYS B 1 20  ? 3.794   -0.315  37.166  1.00 17.86 ?  20  LYS B CD  1 
ATOM   3221 C CE  . LYS B 1 20  ? 2.711   -1.120  37.846  1.00 18.13 ?  20  LYS B CE  1 
ATOM   3222 N NZ  . LYS B 1 20  ? 3.096   -2.537  38.010  1.00 17.55 1  20  LYS B NZ  1 
ATOM   3223 N N   . TRP B 1 21  ? 5.062   4.679   37.096  1.00 19.75 ?  21  TRP B N   1 
ATOM   3224 C CA  . TRP B 1 21  ? 5.292   5.355   38.363  1.00 22.33 ?  21  TRP B CA  1 
ATOM   3225 C C   . TRP B 1 21  ? 5.546   6.845   38.238  1.00 26.17 ?  21  TRP B C   1 
ATOM   3226 O O   . TRP B 1 21  ? 5.521   7.542   39.261  1.00 28.02 ?  21  TRP B O   1 
ATOM   3227 C CB  . TRP B 1 21  ? 6.471   4.706   39.094  1.00 22.47 ?  21  TRP B CB  1 
ATOM   3228 C CG  . TRP B 1 21  ? 6.114   3.376   39.608  1.00 18.77 ?  21  TRP B CG  1 
ATOM   3229 C CD1 . TRP B 1 21  ? 6.366   2.181   39.017  1.00 20.11 ?  21  TRP B CD1 1 
ATOM   3230 C CD2 . TRP B 1 21  ? 5.403   3.090   40.815  1.00 18.87 ?  21  TRP B CD2 1 
ATOM   3231 N NE1 . TRP B 1 21  ? 5.862   1.158   39.785  1.00 18.32 ?  21  TRP B NE1 1 
ATOM   3232 C CE2 . TRP B 1 21  ? 5.273   1.692   40.900  1.00 17.99 ?  21  TRP B CE2 1 
ATOM   3233 C CE3 . TRP B 1 21  ? 4.873   3.882   41.837  1.00 22.23 ?  21  TRP B CE3 1 
ATOM   3234 C CZ2 . TRP B 1 21  ? 4.630   1.061   41.972  1.00 20.19 ?  21  TRP B CZ2 1 
ATOM   3235 C CZ3 . TRP B 1 21  ? 4.243   3.256   42.909  1.00 21.66 ?  21  TRP B CZ3 1 
ATOM   3236 C CH2 . TRP B 1 21  ? 4.127   1.859   42.963  1.00 19.95 ?  21  TRP B CH2 1 
ATOM   3237 N N   . GLY B 1 22  ? 5.799   7.353   37.035  1.00 26.30 ?  22  GLY B N   1 
ATOM   3238 C CA  . GLY B 1 22  ? 6.077   8.771   36.889  1.00 28.51 ?  22  GLY B CA  1 
ATOM   3239 C C   . GLY B 1 22  ? 4.834   9.618   37.112  1.00 30.65 ?  22  GLY B C   1 
ATOM   3240 O O   . GLY B 1 22  ? 3.728   9.266   36.696  1.00 31.68 ?  22  GLY B O   1 
ATOM   3241 N N   . GLY B 1 23  ? 5.029   10.748  37.788  1.00 33.99 ?  23  GLY B N   1 
ATOM   3242 C CA  . GLY B 1 23  ? 3.975   11.738  37.909  1.00 36.69 ?  23  GLY B CA  1 
ATOM   3243 C C   . GLY B 1 23  ? 2.774   11.289  38.703  1.00 40.87 ?  23  GLY B C   1 
ATOM   3244 O O   . GLY B 1 23  ? 1.652   11.729  38.426  1.00 41.53 ?  23  GLY B O   1 
ATOM   3245 N N   . LEU B 1 24  ? 3.023   10.459  39.697  1.00 36.37 ?  24  LEU B N   1 
ATOM   3246 C CA  . LEU B 1 24  ? 1.905   9.949   40.499  1.00 37.01 ?  24  LEU B CA  1 
ATOM   3247 C C   . LEU B 1 24  ? 1.743   10.782  41.762  1.00 39.75 ?  24  LEU B C   1 
ATOM   3248 O O   . LEU B 1 24  ? 2.759   11.130  42.360  1.00 39.64 ?  24  LEU B O   1 
ATOM   3249 C CB  . LEU B 1 24  ? 2.189   8.494   40.869  1.00 31.93 ?  24  LEU B CB  1 
ATOM   3250 C CG  . LEU B 1 24  ? 1.776   7.482   39.813  1.00 27.92 ?  24  LEU B CG  1 
ATOM   3251 C CD1 . LEU B 1 24  ? 1.688   6.106   40.426  1.00 26.69 ?  24  LEU B CD1 1 
ATOM   3252 C CD2 . LEU B 1 24  ? 0.444   7.876   39.207  1.00 29.87 ?  24  LEU B CD2 1 
ATOM   3253 N N   . LYS B 1 25  ? 0.491   11.068  42.128  1.00 41.64 ?  25  LYS B N   1 
ATOM   3254 C CA  . LYS B 1 25  ? 0.251   11.700  43.415  1.00 44.18 ?  25  LYS B CA  1 
ATOM   3255 C C   . LYS B 1 25  ? 0.825   10.821  44.530  1.00 43.39 ?  25  LYS B C   1 
ATOM   3256 O O   . LYS B 1 25  ? 1.190   9.654   44.334  1.00 38.81 ?  25  LYS B O   1 
ATOM   3257 C CB  . LYS B 1 25  ? -1.247  11.954  43.639  1.00 41.02 ?  25  LYS B CB  1 
ATOM   3258 C CG  . LYS B 1 25  ? -1.804  13.224  42.990  1.00 39.54 ?  25  LYS B CG  1 
ATOM   3259 C CD  . LYS B 1 25  ? -3.068  13.714  43.685  1.00 39.08 ?  25  LYS B CD  1 
ATOM   3260 C CE  . LYS B 1 25  ? -4.310  13.313  42.902  1.00 42.62 ?  25  LYS B CE  1 
ATOM   3261 N NZ  . LYS B 1 25  ? -5.115  14.483  42.425  1.00 40.82 1  25  LYS B NZ  1 
ATOM   3262 N N   . GLU B 1 26  ? 0.928   11.338  45.750  1.00 46.71 ?  26  GLU B N   1 
ATOM   3263 C CA  . GLU B 1 26  ? 1.471   10.554  46.893  1.00 47.29 ?  26  GLU B CA  1 
ATOM   3264 C C   . GLU B 1 26  ? 0.500   9.427   47.246  1.00 42.26 ?  26  GLU B C   1 
ATOM   3265 O O   . GLU B 1 26  ? -0.713  9.660   47.106  1.00 43.40 ?  26  GLU B O   1 
ATOM   3266 C CB  . GLU B 1 26  ? 1.574   11.445  48.140  1.00 48.98 ?  26  GLU B CB  1 
ATOM   3267 C CG  . GLU B 1 26  ? 2.343   10.822  49.290  1.00 51.73 ?  26  GLU B CG  1 
ATOM   3268 C CD  . GLU B 1 26  ? 3.666   10.178  48.920  1.00 55.00 ?  26  GLU B CD  1 
ATOM   3269 O OE1 . GLU B 1 26  ? 4.552   10.899  48.419  1.00 53.62 ?  26  GLU B OE1 1 
ATOM   3270 O OE2 . GLU B 1 26  ? 3.811   8.960   49.142  1.00 56.41 -1 26  GLU B OE2 1 
ATOM   3271 N N   . LYS B 1 27  ? 0.993   8.262   47.639  1.00 30.00 ?  27  LYS B N   1 
ATOM   3272 C CA  . LYS B 1 27  ? 0.125   7.140   48.079  1.00 30.00 ?  27  LYS B CA  1 
ATOM   3273 C C   . LYS B 1 27  ? -0.687  6.560   46.912  1.00 30.00 ?  27  LYS B C   1 
ATOM   3274 O O   . LYS B 1 27  ? -1.357  5.563   47.137  1.00 30.00 ?  27  LYS B O   1 
ATOM   3275 C CB  . LYS B 1 27  ? -0.708  7.480   49.324  1.00 30.00 ?  27  LYS B CB  1 
ATOM   3276 C CG  . LYS B 1 27  ? -2.181  7.835   49.116  1.00 30.00 ?  27  LYS B CG  1 
ATOM   3277 C CD  . LYS B 1 27  ? -2.998  8.048   50.380  1.00 30.00 ?  27  LYS B CD  1 
ATOM   3278 C CE  . LYS B 1 27  ? -3.745  9.369   50.411  1.00 30.00 ?  27  LYS B CE  1 
ATOM   3279 N NZ  . LYS B 1 27  ? -2.913  10.508  49.962  1.00 30.00 1  27  LYS B NZ  1 
ATOM   3280 N N   . GLU B 1 28  ? -0.555  7.102   45.708  1.00 26.43 ?  28  GLU B N   1 
ATOM   3281 C CA  . GLU B 1 28  ? -1.255  6.461   44.581  1.00 24.92 ?  28  GLU B CA  1 
ATOM   3282 C C   . GLU B 1 28  ? -0.613  5.092   44.341  1.00 22.30 ?  28  GLU B C   1 
ATOM   3283 O O   . GLU B 1 28  ? 0.586   4.945   44.564  1.00 21.05 ?  28  GLU B O   1 
ATOM   3284 C CB  . GLU B 1 28  ? -1.336  7.353   43.350  1.00 26.99 ?  28  GLU B CB  1 
ATOM   3285 C CG  . GLU B 1 28  ? -2.446  8.381   43.420  1.00 31.25 ?  28  GLU B CG  1 
ATOM   3286 C CD  . GLU B 1 28  ? -2.722  9.131   42.128  1.00 34.18 ?  28  GLU B CD  1 
ATOM   3287 O OE1 . GLU B 1 28  ? -3.886  9.462   41.879  1.00 36.53 ?  28  GLU B OE1 1 
ATOM   3288 O OE2 . GLU B 1 28  ? -1.771  9.391   41.386  1.00 36.12 -1 28  GLU B OE2 1 
ATOM   3289 N N   . LEU B 1 29  ? -1.419  4.141   43.898  1.00 20.93 ?  29  LEU B N   1 
ATOM   3290 C CA  . LEU B 1 29  ? -0.981  2.758   43.731  1.00 18.85 ?  29  LEU B CA  1 
ATOM   3291 C C   . LEU B 1 29  ? -1.279  2.320   42.302  1.00 17.29 ?  29  LEU B C   1 
ATOM   3292 O O   . LEU B 1 29  ? -2.437  2.002   41.973  1.00 15.67 ?  29  LEU B O   1 
ATOM   3293 C CB  . LEU B 1 29  ? -1.675  1.849   44.740  1.00 16.82 ?  29  LEU B CB  1 
ATOM   3294 C CG  . LEU B 1 29  ? -1.362  0.357   44.662  1.00 15.77 ?  29  LEU B CG  1 
ATOM   3295 C CD1 . LEU B 1 29  ? 0.126   0.090   44.387  1.00 18.16 ?  29  LEU B CD1 1 
ATOM   3296 C CD2 . LEU B 1 29  ? -1.808  -0.359  45.950  1.00 16.37 ?  29  LEU B CD2 1 
ATOM   3297 N N   . PRO B 1 30  ? -0.282  2.295   41.419  1.00 18.09 ?  30  PRO B N   1 
ATOM   3298 C CA  . PRO B 1 30  ? -0.543  1.906   40.028  1.00 16.94 ?  30  PRO B CA  1 
ATOM   3299 C C   . PRO B 1 30  ? -0.550  0.389   39.899  1.00 17.23 ?  30  PRO B C   1 
ATOM   3300 O O   . PRO B 1 30  ? 0.414   -0.283  40.268  1.00 15.76 ?  30  PRO B O   1 
ATOM   3301 C CB  . PRO B 1 30  ? 0.624   2.535   39.259  1.00 16.48 ?  30  PRO B CB  1 
ATOM   3302 C CG  . PRO B 1 30  ? 1.743   2.536   40.243  1.00 18.19 ?  30  PRO B CG  1 
ATOM   3303 C CD  . PRO B 1 30  ? 1.123   2.697   41.626  1.00 17.49 ?  30  PRO B CD  1 
ATOM   3304 N N   . MET B 1 31  ? -1.652  -0.149  39.388  1.00 15.18 ?  31  MET B N   1 
ATOM   3305 C CA  . MET B 1 31  ? -1.771  -1.577  39.129  1.00 15.41 ?  31  MET B CA  1 
ATOM   3306 C C   . MET B 1 31  ? -2.424  -1.803  37.771  1.00 17.04 ?  31  MET B C   1 
ATOM   3307 O O   . MET B 1 31  ? -3.245  -2.708  37.598  1.00 15.74 ?  31  MET B O   1 
ATOM   3308 C CB  . MET B 1 31  ? -2.559  -2.277  40.244  1.00 15.56 ?  31  MET B CB  1 
ATOM   3309 C CG  . MET B 1 31  ? -1.868  -2.220  41.608  1.00 18.79 ?  31  MET B CG  1 
ATOM   3310 S SD  . MET B 1 31  ? -2.795  -3.069  42.894  1.00 20.92 ?  31  MET B SD  1 
ATOM   3311 C CE  . MET B 1 31  ? -2.172  -4.749  42.768  1.00 17.81 ?  31  MET B CE  1 
ATOM   3312 N N   . TRP B 1 32  ? -2.071  -0.982  36.782  1.00 18.01 ?  32  TRP B N   1 
ATOM   3313 C CA  . TRP B 1 32  ? -2.748  -1.011  35.488  1.00 16.60 ?  32  TRP B CA  1 
ATOM   3314 C C   . TRP B 1 32  ? -1.818  -1.538  34.405  1.00 19.91 ?  32  TRP B C   1 
ATOM   3315 O O   . TRP B 1 32  ? -1.952  -2.692  33.979  1.00 19.06 ?  32  TRP B O   1 
ATOM   3316 C CB  . TRP B 1 32  ? -3.327  0.380   35.145  1.00 18.27 ?  32  TRP B CB  1 
ATOM   3317 C CG  . TRP B 1 32  ? -2.334  1.524   35.049  1.00 18.32 ?  32  TRP B CG  1 
ATOM   3318 C CD1 . TRP B 1 32  ? -1.658  2.128   36.079  1.00 18.26 ?  32  TRP B CD1 1 
ATOM   3319 C CD2 . TRP B 1 32  ? -1.898  2.179   33.848  1.00 18.36 ?  32  TRP B CD2 1 
ATOM   3320 N NE1 . TRP B 1 32  ? -0.826  3.120   35.586  1.00 19.28 ?  32  TRP B NE1 1 
ATOM   3321 C CE2 . TRP B 1 32  ? -0.957  3.166   34.221  1.00 18.77 ?  32  TRP B CE2 1 
ATOM   3322 C CE3 . TRP B 1 32  ? -2.205  2.017   32.495  1.00 19.93 ?  32  TRP B CE3 1 
ATOM   3323 C CZ2 . TRP B 1 32  ? -0.333  3.995   33.284  1.00 18.99 ?  32  TRP B CZ2 1 
ATOM   3324 C CZ3 . TRP B 1 32  ? -1.587  2.844   31.570  1.00 21.61 ?  32  TRP B CZ3 1 
ATOM   3325 C CH2 . TRP B 1 32  ? -0.656  3.811   31.966  1.00 17.54 ?  32  TRP B CH2 1 
ATOM   3326 N N   . ILE B 1 33  ? -0.839  -0.745  33.977  1.00 18.17 ?  33  ILE B N   1 
ATOM   3327 C CA  . ILE B 1 33  ? 0.011   -1.115  32.857  1.00 17.62 ?  33  ILE B CA  1 
ATOM   3328 C C   . ILE B 1 33  ? 0.836   -2.368  33.184  1.00 17.01 ?  33  ILE B C   1 
ATOM   3329 O O   . ILE B 1 33  ? 1.257   -2.594  34.329  1.00 16.24 ?  33  ILE B O   1 
ATOM   3330 C CB  . ILE B 1 33  ? 0.905   0.087   32.500  1.00 18.75 ?  33  ILE B CB  1 
ATOM   3331 C CG1 . ILE B 1 33  ? 1.633   -0.126  31.168  1.00 20.76 ?  33  ILE B CG1 1 
ATOM   3332 C CG2 . ILE B 1 33  ? 1.874   0.410   33.655  1.00 18.87 ?  33  ILE B CG2 1 
ATOM   3333 C CD1 . ILE B 1 33  ? 2.383   1.127   30.700  1.00 19.34 ?  33  ILE B CD1 1 
ATOM   3334 N N   . ALA B 1 34  ? 1.056   -3.194  32.162  1.00 15.20 ?  34  ALA B N   1 
ATOM   3335 C CA  . ALA B 1 34  ? 1.611   -4.538  32.330  1.00 17.18 ?  34  ALA B CA  1 
ATOM   3336 C C   . ALA B 1 34  ? 3.134   -4.478  32.364  1.00 17.42 ?  34  ALA B C   1 
ATOM   3337 O O   . ALA B 1 34  ? 3.826   -4.788  31.396  1.00 18.04 ?  34  ALA B O   1 
ATOM   3338 C CB  . ALA B 1 34  ? 1.119   -5.456  31.219  1.00 19.44 ?  34  ALA B CB  1 
ATOM   3339 N N   . GLU B 1 35  ? 3.657   -4.055  33.512  1.00 15.74 ?  35  GLU B N   1 
ATOM   3340 C CA  . GLU B 1 35  ? 5.063   -4.223  33.846  1.00 15.74 ?  35  GLU B CA  1 
ATOM   3341 C C   . GLU B 1 35  ? 5.139   -4.548  35.325  1.00 16.30 ?  35  GLU B C   1 
ATOM   3342 O O   . GLU B 1 35  ? 4.226   -4.217  36.097  1.00 19.73 ?  35  GLU B O   1 
ATOM   3343 C CB  . GLU B 1 35  ? 5.905   -2.978  33.538  1.00 19.06 ?  35  GLU B CB  1 
ATOM   3344 C CG  . GLU B 1 35  ? 5.759   -1.885  34.577  1.00 18.42 ?  35  GLU B CG  1 
ATOM   3345 C CD  . GLU B 1 35  ? 6.426   -0.578  34.173  1.00 20.55 ?  35  GLU B CD  1 
ATOM   3346 O OE1 . GLU B 1 35  ? 7.325   -0.113  34.916  1.00 23.26 ?  35  GLU B OE1 1 
ATOM   3347 O OE2 . GLU B 1 35  ? 6.047   -0.019  33.113  1.00 20.91 -1 35  GLU B OE2 1 
ATOM   3348 N N   . MET B 1 36  ? 6.227   -5.199  35.716  1.00 14.07 ?  36  MET B N   1 
ATOM   3349 C CA  . MET B 1 36  ? 6.340   -5.719  37.071  1.00 17.22 ?  36  MET B CA  1 
ATOM   3350 C C   . MET B 1 36  ? 6.952   -4.701  38.016  1.00 17.53 ?  36  MET B C   1 
ATOM   3351 O O   . MET B 1 36  ? 7.744   -3.836  37.621  1.00 16.73 ?  36  MET B O   1 
ATOM   3352 C CB  . MET B 1 36  ? 7.184   -6.982  37.106  1.00 15.24 ?  36  MET B CB  1 
ATOM   3353 C CG  . MET B 1 36  ? 6.743   -8.078  36.176  1.00 16.72 ?  36  MET B CG  1 
ATOM   3354 S SD  . MET B 1 36  ? 7.738   -9.546  36.496  1.00 17.48 ?  36  MET B SD  1 
ATOM   3355 C CE  . MET B 1 36  ? 7.348   -10.523 35.057  1.00 16.66 ?  36  MET B CE  1 
ATOM   3356 N N   . ASP B 1 37  ? 6.616   -4.846  39.289  1.00 14.54 ?  37  ASP B N   1 
ATOM   3357 C CA  . ASP B 1 37  ? 7.322   -4.128  40.338  1.00 17.53 ?  37  ASP B CA  1 
ATOM   3358 C C   . ASP B 1 37  ? 8.299   -5.030  41.082  1.00 17.99 ?  37  ASP B C   1 
ATOM   3359 O O   . ASP B 1 37  ? 8.380   -5.005  42.310  1.00 16.90 ?  37  ASP B O   1 
ATOM   3360 C CB  . ASP B 1 37  ? 6.312   -3.471  41.262  1.00 17.05 ?  37  ASP B CB  1 
ATOM   3361 C CG  . ASP B 1 37  ? 5.643   -2.295  40.591  1.00 20.69 ?  37  ASP B CG  1 
ATOM   3362 O OD1 . ASP B 1 37  ? 6.358   -1.519  39.930  1.00 18.14 ?  37  ASP B OD1 1 
ATOM   3363 O OD2 . ASP B 1 37  ? 4.418   -2.149  40.681  1.00 21.11 -1 37  ASP B OD2 1 
ATOM   3364 N N   . PHE B 1 38  ? 9.035   -5.854  40.333  1.00 15.36 ?  38  PHE B N   1 
ATOM   3365 C CA  . PHE B 1 38  ? 10.154  -6.641  40.835  1.00 16.86 ?  38  PHE B CA  1 
ATOM   3366 C C   . PHE B 1 38  ? 11.420  -6.234  40.094  1.00 16.30 ?  38  PHE B C   1 
ATOM   3367 O O   . PHE B 1 38  ? 11.366  -5.874  38.917  1.00 16.39 ?  38  PHE B O   1 
ATOM   3368 C CB  . PHE B 1 38  ? 9.940   -8.148  40.632  1.00 16.38 ?  38  PHE B CB  1 
ATOM   3369 C CG  . PHE B 1 38  ? 8.642   -8.658  41.171  1.00 17.12 ?  38  PHE B CG  1 
ATOM   3370 C CD1 . PHE B 1 38  ? 8.334   -8.508  42.517  1.00 16.53 ?  38  PHE B CD1 1 
ATOM   3371 C CD2 . PHE B 1 38  ? 7.731   -9.292  40.338  1.00 17.18 ?  38  PHE B CD2 1 
ATOM   3372 C CE1 . PHE B 1 38  ? 7.126   -8.993  43.032  1.00 17.51 ?  38  PHE B CE1 1 
ATOM   3373 C CE2 . PHE B 1 38  ? 6.536   -9.778  40.843  1.00 15.38 ?  38  PHE B CE2 1 
ATOM   3374 C CZ  . PHE B 1 38  ? 6.231   -9.617  42.196  1.00 17.42 ?  38  PHE B CZ  1 
ATOM   3375 N N   . ARG B 1 39  ? 12.554  -6.280  40.796  1.00 17.80 ?  39  ARG B N   1 
ATOM   3376 C CA  . ARG B 1 39  ? 13.853  -6.199  40.138  1.00 17.83 ?  39  ARG B CA  1 
ATOM   3377 C C   . ARG B 1 39  ? 14.011  -7.363  39.164  1.00 16.88 ?  39  ARG B C   1 
ATOM   3378 O O   . ARG B 1 39  ? 13.495  -8.457  39.389  1.00 15.98 ?  39  ARG B O   1 
ATOM   3379 C CB  . ARG B 1 39  ? 14.982  -6.263  41.170  1.00 19.64 ?  39  ARG B CB  1 
ATOM   3380 C CG  . ARG B 1 39  ? 14.887  -5.262  42.307  1.00 24.29 ?  39  ARG B CG  1 
ATOM   3381 C CD  . ARG B 1 39  ? 15.875  -5.642  43.405  1.00 29.32 ?  39  ARG B CD  1 
ATOM   3382 N NE  . ARG B 1 39  ? 17.060  -6.311  42.855  1.00 32.07 ?  39  ARG B NE  1 
ATOM   3383 C CZ  . ARG B 1 39  ? 18.096  -5.673  42.304  1.00 36.97 ?  39  ARG B CZ  1 
ATOM   3384 N NH1 . ARG B 1 39  ? 18.090  -4.346  42.222  1.00 35.90 1  39  ARG B NH1 1 
ATOM   3385 N NH2 . ARG B 1 39  ? 19.140  -6.356  41.831  1.00 36.99 ?  39  ARG B NH2 1 
ATOM   3386 N N   . ILE B 1 40  ? 14.766  -7.139  38.087  1.00 16.67 ?  40  ILE B N   1 
ATOM   3387 C CA  . ILE B 1 40  ? 15.003  -8.215  37.131  1.00 16.66 ?  40  ILE B CA  1 
ATOM   3388 C C   . ILE B 1 40  ? 16.000  -9.217  37.694  1.00 15.96 ?  40  ILE B C   1 
ATOM   3389 O O   . ILE B 1 40  ? 16.702  -8.949  38.683  1.00 16.58 ?  40  ILE B O   1 
ATOM   3390 C CB  . ILE B 1 40  ? 15.481  -7.680  35.765  1.00 16.65 ?  40  ILE B CB  1 
ATOM   3391 C CG1 . ILE B 1 40  ? 16.875  -7.069  35.871  1.00 17.13 ?  40  ILE B CG1 1 
ATOM   3392 C CG2 . ILE B 1 40  ? 14.473  -6.678  35.190  1.00 18.02 ?  40  ILE B CG2 1 
ATOM   3393 C CD1 . ILE B 1 40  ? 17.454  -6.646  34.506  1.00 19.52 ?  40  ILE B CD1 1 
ATOM   3394 N N   . ALA B 1 41  ? 16.049  -10.380 37.079  1.00 16.48 ?  41  ALA B N   1 
ATOM   3395 C CA  . ALA B 1 41  ? 16.969  -11.423 37.502  1.00 17.69 ?  41  ALA B CA  1 
ATOM   3396 C C   . ALA B 1 41  ? 18.409  -10.916 37.477  1.00 19.45 ?  41  ALA B C   1 
ATOM   3397 O O   . ALA B 1 41  ? 18.817  -10.255 36.506  1.00 15.21 ?  41  ALA B O   1 
ATOM   3398 C CB  . ALA B 1 41  ? 16.817  -12.632 36.587  1.00 18.66 ?  41  ALA B CB  1 
ATOM   3399 N N   . PRO B 1 42  ? 19.201  -11.179 38.517  1.00 18.85 ?  42  PRO B N   1 
ATOM   3400 C CA  . PRO B 1 42  ? 20.570  -10.639 38.536  1.00 18.04 ?  42  PRO B CA  1 
ATOM   3401 C C   . PRO B 1 42  ? 21.450  -11.195 37.435  1.00 19.06 ?  42  PRO B C   1 
ATOM   3402 O O   . PRO B 1 42  ? 22.406  -10.518 37.045  1.00 18.43 ?  42  PRO B O   1 
ATOM   3403 C CB  . PRO B 1 42  ? 21.088  -11.022 39.932  1.00 22.58 ?  42  PRO B CB  1 
ATOM   3404 C CG  . PRO B 1 42  ? 20.198  -12.139 40.392  1.00 23.02 ?  42  PRO B CG  1 
ATOM   3405 C CD  . PRO B 1 42  ? 18.853  -11.877 39.768  1.00 20.08 ?  42  PRO B CD  1 
ATOM   3406 N N   . GLU B 1 43  ? 21.146  -12.385 36.908  1.00 17.69 ?  43  GLU B N   1 
ATOM   3407 C CA  . GLU B 1 43  ? 21.891  -12.912 35.765  1.00 20.58 ?  43  GLU B CA  1 
ATOM   3408 C C   . GLU B 1 43  ? 21.695  -12.047 34.524  1.00 20.40 ?  43  GLU B C   1 
ATOM   3409 O O   . GLU B 1 43  ? 22.607  -11.922 33.697  1.00 18.59 ?  43  GLU B O   1 
ATOM   3410 C CB  . GLU B 1 43  ? 21.471  -14.361 35.481  1.00 20.75 ?  43  GLU B CB  1 
ATOM   3411 C CG  . GLU B 1 43  ? 21.683  -15.334 36.653  1.00 21.15 ?  43  GLU B CG  1 
ATOM   3412 C CD  . GLU B 1 43  ? 20.526  -15.370 37.660  1.00 23.33 ?  43  GLU B CD  1 
ATOM   3413 O OE1 . GLU B 1 43  ? 20.512  -16.281 38.520  1.00 24.42 ?  43  GLU B OE1 1 
ATOM   3414 O OE2 . GLU B 1 43  ? 19.636  -14.495 37.619  1.00 23.04 -1 43  GLU B OE2 1 
ATOM   3415 N N   . ILE B 1 44  ? 20.514  -11.453 34.360  1.00 16.02 ?  44  ILE B N   1 
ATOM   3416 C CA  . ILE B 1 44  ? 20.318  -10.535 33.239  1.00 15.80 ?  44  ILE B CA  1 
ATOM   3417 C C   . ILE B 1 44  ? 21.058  -9.231  33.494  1.00 18.13 ?  44  ILE B C   1 
ATOM   3418 O O   . ILE B 1 44  ? 21.724  -8.693  32.598  1.00 15.20 ?  44  ILE B O   1 
ATOM   3419 C CB  . ILE B 1 44  ? 18.816  -10.291 32.986  1.00 15.96 ?  44  ILE B CB  1 
ATOM   3420 C CG1 . ILE B 1 44  ? 18.083  -11.625 32.863  1.00 17.80 ?  44  ILE B CG1 1 
ATOM   3421 C CG2 . ILE B 1 44  ? 18.599  -9.419  31.734  1.00 16.09 ?  44  ILE B CG2 1 
ATOM   3422 C CD1 . ILE B 1 44  ? 16.561  -11.504 32.805  1.00 15.83 ?  44  ILE B CD1 1 
ATOM   3423 N N   . MET B 1 45  ? 20.960  -8.706  34.721  1.00 17.12 ?  45  MET B N   1 
ATOM   3424 C CA  . MET B 1 45  ? 21.684  -7.488  35.077  1.00 18.23 ?  45  MET B CA  1 
ATOM   3425 C C   . MET B 1 45  ? 23.175  -7.642  34.847  1.00 17.59 ?  45  MET B C   1 
ATOM   3426 O O   . MET B 1 45  ? 23.829  -6.716  34.356  1.00 19.32 ?  45  MET B O   1 
ATOM   3427 C CB  . MET B 1 45  ? 21.440  -7.126  36.542  1.00 19.68 ?  45  MET B CB  1 
ATOM   3428 C CG  . MET B 1 45  ? 20.134  -6.410  36.815  1.00 24.16 ?  45  MET B CG  1 
ATOM   3429 S SD  . MET B 1 45  ? 20.106  -4.722  36.164  1.00 34.94 ?  45  MET B SD  1 
ATOM   3430 C CE  . MET B 1 45  ? 21.835  -4.288  36.317  1.00 25.23 ?  45  MET B CE  1 
ATOM   3431 N N   . THR B 1 46  ? 23.732  -8.799  35.214  1.00 14.77 ?  46  THR B N   1 
ATOM   3432 C CA  . THR B 1 46  ? 25.158  -9.035  34.999  1.00 20.61 ?  46  THR B CA  1 
ATOM   3433 C C   . THR B 1 46  ? 25.520  -8.917  33.523  1.00 19.76 ?  46  THR B C   1 
ATOM   3434 O O   . THR B 1 46  ? 26.568  -8.351  33.177  1.00 19.40 ?  46  THR B O   1 
ATOM   3435 C CB  . THR B 1 46  ? 25.559  -10.413 35.521  1.00 20.27 ?  46  THR B CB  1 
ATOM   3436 O OG1 . THR B 1 46  ? 25.315  -10.479 36.927  1.00 21.45 ?  46  THR B OG1 1 
ATOM   3437 C CG2 . THR B 1 46  ? 27.043  -10.674 35.260  1.00 23.10 ?  46  THR B CG2 1 
ATOM   3438 N N   . SER B 1 47  ? 24.659  -9.434  32.638  1.00 19.37 ?  47  SER B N   1 
ATOM   3439 C CA  . SER B 1 47  ? 24.956  -9.390  31.206  1.00 16.80 ?  47  SER B CA  1 
ATOM   3440 C C   . SER B 1 47  ? 24.932  -7.959  30.682  1.00 17.99 ?  47  SER B C   1 
ATOM   3441 O O   . SER B 1 47  ? 25.786  -7.568  29.876  1.00 18.61 ?  47  SER B O   1 
ATOM   3442 C CB  . SER B 1 47  ? 23.960  -10.253 30.432  1.00 20.49 ?  47  SER B CB  1 
ATOM   3443 O OG  . SER B 1 47  ? 22.683  -9.617  30.348  1.00 21.71 ?  47  SER B OG  1 
ATOM   3444 N N   . MET B 1 48  ? 23.965  -7.163  31.139  1.00 14.65 ?  48  MET B N   1 
ATOM   3445 C CA  . MET B 1 48  ? 23.889  -5.771  30.718  1.00 17.08 ?  48  MET B CA  1 
ATOM   3446 C C   . MET B 1 48  ? 25.112  -4.981  31.175  1.00 17.86 ?  48  MET B C   1 
ATOM   3447 O O   . MET B 1 48  ? 25.699  -4.228  30.389  1.00 16.77 ?  48  MET B O   1 
ATOM   3448 C CB  . MET B 1 48  ? 22.604  -5.146  31.250  1.00 17.23 ?  48  MET B CB  1 
ATOM   3449 C CG  . MET B 1 48  ? 21.349  -5.805  30.691  1.00 17.53 ?  48  MET B CG  1 
ATOM   3450 S SD  . MET B 1 48  ? 19.960  -4.941  31.409  1.00 22.68 ?  48  MET B SD  1 
ATOM   3451 C CE  . MET B 1 48  ? 18.559  -5.743  30.648  1.00 20.95 ?  48  MET B CE  1 
ATOM   3452 N N   . GLU B 1 49  ? 25.517  -5.144  32.416  1.00 17.58 ?  49  GLU B N   1 
ATOM   3453 C CA  . GLU B 1 49  ? 26.681  -4.406  32.957  1.00 18.86 ?  49  GLU B CA  1 
ATOM   3454 C C   . GLU B 1 49  ? 27.963  -4.820  32.221  1.00 20.57 ?  49  GLU B C   1 
ATOM   3455 O O   . GLU B 1 49  ? 28.798  -3.954  31.995  1.00 19.80 ?  49  GLU B O   1 
ATOM   3456 C CB  . GLU B 1 49  ? 26.695  -4.552  34.479  1.00 22.34 ?  49  GLU B CB  1 
ATOM   3457 C CG  . GLU B 1 49  ? 25.590  -3.740  35.117  1.00 26.08 ?  49  GLU B CG  1 
ATOM   3458 C CD  . GLU B 1 49  ? 25.373  -3.865  36.612  1.00 38.17 ?  49  GLU B CD  1 
ATOM   3459 O OE1 . GLU B 1 49  ? 25.584  -4.959  37.159  1.00 37.56 ?  49  GLU B OE1 1 
ATOM   3460 O OE2 . GLU B 1 49  ? 24.952  -2.867  37.216  1.00 41.01 -1 49  GLU B OE2 1 
ATOM   3461 N N   . GLU B 1 50  ? 28.095  -6.080  31.845  1.00 17.11 ?  50  GLU B N   1 
ATOM   3462 C CA  . GLU B 1 50  ? 29.271  -6.560  31.076  1.00 21.17 ?  50  GLU B CA  1 
ATOM   3463 C C   . GLU B 1 50  ? 29.287  -5.902  29.687  1.00 19.48 ?  50  GLU B C   1 
ATOM   3464 O O   . GLU B 1 50  ? 30.331  -5.507  29.221  1.00 19.99 ?  50  GLU B O   1 
ATOM   3465 C CB  . GLU B 1 50  ? 29.228  -8.079  30.975  1.00 20.13 ?  50  GLU B CB  1 
ATOM   3466 C CG  . GLU B 1 50  ? 30.256  -8.687  30.052  1.00 24.49 ?  50  GLU B CG  1 
ATOM   3467 C CD  . GLU B 1 50  ? 31.662  -8.497  30.573  1.00 32.35 ?  50  GLU B CD  1 
ATOM   3468 O OE1 . GLU B 1 50  ? 32.572  -8.330  29.750  1.00 36.23 ?  50  GLU B OE1 1 
ATOM   3469 O OE2 . GLU B 1 50  ? 31.829  -8.505  31.802  1.00 33.87 -1 50  GLU B OE2 1 
ATOM   3470 N N   . LYS B 1 51  ? 28.126  -5.818  29.072  1.00 15.89 ?  51  LYS B N   1 
ATOM   3471 C CA  . LYS B 1 51  ? 28.083  -5.217  27.744  1.00 15.30 ?  51  LYS B CA  1 
ATOM   3472 C C   . LYS B 1 51  ? 28.501  -3.755  27.787  1.00 18.29 ?  51  LYS B C   1 
ATOM   3473 O O   . LYS B 1 51  ? 29.171  -3.266  26.870  1.00 19.27 ?  51  LYS B O   1 
ATOM   3474 C CB  . LYS B 1 51  ? 26.677  -5.354  27.155  1.00 17.03 ?  51  LYS B CB  1 
ATOM   3475 C CG  . LYS B 1 51  ? 26.481  -4.695  25.775  1.00 14.89 ?  51  LYS B CG  1 
ATOM   3476 C CD  . LYS B 1 51  ? 27.481  -5.219  24.728  1.00 16.52 ?  51  LYS B CD  1 
ATOM   3477 C CE  . LYS B 1 51  ? 27.274  -4.543  23.380  1.00 17.22 ?  51  LYS B CE  1 
ATOM   3478 N NZ  . LYS B 1 51  ? 26.029  -5.052  22.733  1.00 18.07 1  51  LYS B NZ  1 
ATOM   3479 N N   . LEU B 1 52  ? 28.112  -3.032  28.840  1.00 17.72 ?  52  LEU B N   1 
ATOM   3480 C CA  . LEU B 1 52  ? 28.470  -1.619  28.919  1.00 17.40 ?  52  LEU B CA  1 
ATOM   3481 C C   . LEU B 1 52  ? 29.971  -1.414  29.028  1.00 19.04 ?  52  LEU B C   1 
ATOM   3482 O O   . LEU B 1 52  ? 30.455  -0.323  28.715  1.00 19.77 ?  52  LEU B O   1 
ATOM   3483 C CB  . LEU B 1 52  ? 27.780  -0.945  30.110  1.00 19.24 ?  52  LEU B CB  1 
ATOM   3484 C CG  . LEU B 1 52  ? 26.268  -0.731  30.062  1.00 19.41 ?  52  LEU B CG  1 
ATOM   3485 C CD1 . LEU B 1 52  ? 25.876  0.308   31.085  1.00 21.57 ?  52  LEU B CD1 1 
ATOM   3486 C CD2 . LEU B 1 52  ? 25.793  -0.321  28.682  1.00 17.81 ?  52  LEU B CD2 1 
ATOM   3487 N N   . LYS B 1 53  ? 30.706  -2.434  29.441  1.00 20.67 ?  53  LYS B N   1 
ATOM   3488 C CA  . LYS B 1 53  ? 32.187  -2.338  29.516  1.00 20.49 ?  53  LYS B CA  1 
ATOM   3489 C C   . LYS B 1 53  ? 32.797  -2.110  28.124  1.00 20.15 ?  53  LYS B C   1 
ATOM   3490 O O   . LYS B 1 53  ? 33.927  -1.671  28.071  1.00 19.45 ?  53  LYS B O   1 
ATOM   3491 C CB  . LYS B 1 53  ? 32.780  -3.610  30.117  1.00 20.38 ?  53  LYS B CB  1 
ATOM   3492 C CG  . LYS B 1 53  ? 32.581  -3.759  31.615  1.00 24.05 ?  53  LYS B CG  1 
ATOM   3493 C CD  . LYS B 1 53  ? 32.531  -5.198  32.053  1.00 32.48 ?  53  LYS B CD  1 
ATOM   3494 C CE  . LYS B 1 53  ? 33.876  -5.759  32.451  1.00 31.52 ?  53  LYS B CE  1 
ATOM   3495 N NZ  . LYS B 1 53  ? 33.729  -6.969  33.292  1.00 35.78 1  53  LYS B NZ  1 
ATOM   3496 N N   . VAL B 1 54  ? 32.059  -2.413  27.058  1.00 18.65 ?  54  VAL B N   1 
ATOM   3497 C CA  . VAL B 1 54  ? 32.607  -2.149  25.730  1.00 17.14 ?  54  VAL B CA  1 
ATOM   3498 C C   . VAL B 1 54  ? 32.896  -0.660  25.578  1.00 18.71 ?  54  VAL B C   1 
ATOM   3499 O O   . VAL B 1 54  ? 33.917  -0.267  25.001  1.00 20.63 ?  54  VAL B O   1 
ATOM   3500 C CB  . VAL B 1 54  ? 31.661  -2.671  24.628  1.00 17.89 ?  54  VAL B CB  1 
ATOM   3501 C CG1 . VAL B 1 54  ? 32.258  -2.383  23.249  1.00 19.28 ?  54  VAL B CG1 1 
ATOM   3502 C CG2 . VAL B 1 54  ? 31.422  -4.172  24.788  1.00 18.35 ?  54  VAL B CG2 1 
ATOM   3503 N N   . ALA B 1 55  ? 32.026  0.187   26.136  1.00 17.28 ?  55  ALA B N   1 
ATOM   3504 C CA  . ALA B 1 55  ? 32.181  1.646   26.165  1.00 17.26 ?  55  ALA B CA  1 
ATOM   3505 C C   . ALA B 1 55  ? 32.188  2.254   24.760  1.00 16.42 ?  55  ALA B C   1 
ATOM   3506 O O   . ALA B 1 55  ? 32.645  3.387   24.561  1.00 18.25 ?  55  ALA B O   1 
ATOM   3507 C CB  . ALA B 1 55  ? 33.425  2.067   26.953  1.00 20.71 ?  55  ALA B CB  1 
ATOM   3508 N N   . ALA B 1 56  ? 31.643  1.527   23.792  1.00 15.99 ?  56  ALA B N   1 
ATOM   3509 C CA  . ALA B 1 56  ? 31.348  2.050   22.466  1.00 15.18 ?  56  ALA B CA  1 
ATOM   3510 C C   . ALA B 1 56  ? 30.266  1.160   21.890  1.00 17.79 ?  56  ALA B C   1 
ATOM   3511 O O   . ALA B 1 56  ? 30.269  -0.050  22.135  1.00 18.56 ?  56  ALA B O   1 
ATOM   3512 C CB  . ALA B 1 56  ? 32.574  2.055   21.548  1.00 20.84 ?  56  ALA B CB  1 
ATOM   3513 N N   . PHE B 1 57  ? 29.343  1.750   21.127  1.00 15.88 ?  57  PHE B N   1 
ATOM   3514 C CA  . PHE B 1 57  ? 28.128  1.035   20.784  1.00 14.27 ?  57  PHE B CA  1 
ATOM   3515 C C   . PHE B 1 57  ? 27.770  1.261   19.320  1.00 16.20 ?  57  PHE B C   1 
ATOM   3516 O O   . PHE B 1 57  ? 26.789  1.917   18.973  1.00 15.07 ?  57  PHE B O   1 
ATOM   3517 C CB  . PHE B 1 57  ? 27.005  1.427   21.742  1.00 15.39 ?  57  PHE B CB  1 
ATOM   3518 C CG  . PHE B 1 57  ? 27.387  1.208   23.173  1.00 16.27 ?  57  PHE B CG  1 
ATOM   3519 C CD1 . PHE B 1 57  ? 27.515  -0.087  23.666  1.00 15.61 ?  57  PHE B CD1 1 
ATOM   3520 C CD2 . PHE B 1 57  ? 27.714  2.283   23.993  1.00 15.22 ?  57  PHE B CD2 1 
ATOM   3521 C CE1 . PHE B 1 57  ? 27.931  -0.311  24.982  1.00 18.81 ?  57  PHE B CE1 1 
ATOM   3522 C CE2 . PHE B 1 57  ? 28.121  2.067   25.312  1.00 18.95 ?  57  PHE B CE2 1 
ATOM   3523 C CZ  . PHE B 1 57  ? 28.226  0.765   25.800  1.00 20.64 ?  57  PHE B CZ  1 
ATOM   3524 N N   . GLY B 1 58  ? 28.584  0.674   18.448  1.00 16.47 ?  58  GLY B N   1 
ATOM   3525 C CA  . GLY B 1 58  ? 28.324  0.692   17.025  1.00 15.14 ?  58  GLY B CA  1 
ATOM   3526 C C   . GLY B 1 58  ? 27.352  -0.404  16.622  1.00 17.37 ?  58  GLY B C   1 
ATOM   3527 O O   . GLY B 1 58  ? 26.687  -1.034  17.446  1.00 16.28 ?  58  GLY B O   1 
ATOM   3528 N N   . TYR B 1 59  ? 27.305  -0.654  15.314  1.00 17.23 ?  59  TYR B N   1 
ATOM   3529 C CA  . TYR B 1 59  ? 26.277  -1.520  14.754  1.00 19.57 ?  59  TYR B CA  1 
ATOM   3530 C C   . TYR B 1 59  ? 26.469  -2.965  15.191  1.00 16.50 ?  59  TYR B C   1 
ATOM   3531 O O   . TYR B 1 59  ? 27.592  -3.466  15.274  1.00 18.34 ?  59  TYR B O   1 
ATOM   3532 C CB  . TYR B 1 59  ? 26.288  -1.439  13.232  1.00 18.25 ?  59  TYR B CB  1 
ATOM   3533 C CG  . TYR B 1 59  ? 25.942  -0.071  12.729  1.00 21.11 ?  59  TYR B CG  1 
ATOM   3534 C CD1 . TYR B 1 59  ? 24.620  0.315   12.584  1.00 22.31 ?  59  TYR B CD1 1 
ATOM   3535 C CD2 . TYR B 1 59  ? 26.945  0.847   12.417  1.00 21.59 ?  59  TYR B CD2 1 
ATOM   3536 C CE1 . TYR B 1 59  ? 24.298  1.571   12.125  1.00 26.84 ?  59  TYR B CE1 1 
ATOM   3537 C CE2 . TYR B 1 59  ? 26.635  2.106   11.961  1.00 21.43 ?  59  TYR B CE2 1 
ATOM   3538 C CZ  . TYR B 1 59  ? 25.319  2.457   11.809  1.00 26.31 ?  59  TYR B CZ  1 
ATOM   3539 O OH  . TYR B 1 59  ? 25.019  3.709   11.348  1.00 29.05 ?  59  TYR B OH  1 
ATOM   3540 N N   . GLU B 1 60  ? 25.353  -3.647  15.436  1.00 19.50 ?  60  GLU B N   1 
ATOM   3541 C CA  . GLU B 1 60  ? 25.388  -5.026  15.885  1.00 19.29 ?  60  GLU B CA  1 
ATOM   3542 C C   . GLU B 1 60  ? 24.654  -5.956  14.927  1.00 18.59 ?  60  GLU B C   1 
ATOM   3543 O O   . GLU B 1 60  ? 23.654  -5.582  14.299  1.00 18.13 ?  60  GLU B O   1 
ATOM   3544 C CB  . GLU B 1 60  ? 24.785  -5.146  17.280  1.00 20.40 ?  60  GLU B CB  1 
ATOM   3545 C CG  . GLU B 1 60  ? 25.747  -4.694  18.340  1.00 22.93 ?  60  GLU B CG  1 
ATOM   3546 C CD  . GLU B 1 60  ? 25.209  -4.918  19.720  1.00 21.49 ?  60  GLU B CD  1 
ATOM   3547 O OE1 . GLU B 1 60  ? 25.422  -4.041  20.580  1.00 20.90 ?  60  GLU B OE1 1 
ATOM   3548 O OE2 . GLU B 1 60  ? 24.552  -5.967  19.935  1.00 21.21 -1 60  GLU B OE2 1 
ATOM   3549 N N   . SER B 1 61  ? 25.159  -7.183  14.846  1.00 18.33 ?  61  SER B N   1 
ATOM   3550 C CA  . SER B 1 61  ? 24.511  -8.289  14.161  1.00 20.13 ?  61  SER B CA  1 
ATOM   3551 C C   . SER B 1 61  ? 23.799  -9.178  15.183  1.00 19.04 ?  61  SER B C   1 
ATOM   3552 O O   . SER B 1 61  ? 23.993  -9.058  16.399  1.00 16.96 ?  61  SER B O   1 
ATOM   3553 C CB  . SER B 1 61  ? 25.544  -9.094  13.367  1.00 20.42 ?  61  SER B CB  1 
ATOM   3554 O OG  . SER B 1 61  ? 26.467  -9.707  14.246  1.00 21.42 ?  61  SER B OG  1 
ATOM   3555 N N   . VAL B 1 62  ? 22.957  -10.076 14.682  1.00 18.34 ?  62  VAL B N   1 
ATOM   3556 C CA  . VAL B 1 62  ? 22.268  -11.045 15.520  1.00 17.46 ?  62  VAL B CA  1 
ATOM   3557 C C   . VAL B 1 62  ? 23.092  -12.353 15.479  1.00 16.54 ?  62  VAL B C   1 
ATOM   3558 O O   . VAL B 1 62  ? 23.187  -12.958 14.406  1.00 18.73 ?  62  VAL B O   1 
ATOM   3559 C CB  . VAL B 1 62  ? 20.832  -11.285 15.056  1.00 17.28 ?  62  VAL B CB  1 
ATOM   3560 C CG1 . VAL B 1 62  ? 20.139  -12.240 16.005  1.00 19.34 ?  62  VAL B CG1 1 
ATOM   3561 C CG2 . VAL B 1 62  ? 20.095  -9.959  14.968  1.00 18.40 ?  62  VAL B CG2 1 
ATOM   3562 N N   . PRO B 1 63  ? 23.672  -12.764 16.593  1.00 17.77 ?  63  PRO B N   1 
ATOM   3563 C CA  . PRO B 1 63  ? 24.545  -13.946 16.568  1.00 17.98 ?  63  PRO B CA  1 
ATOM   3564 C C   . PRO B 1 63  ? 23.745  -15.233 16.637  1.00 18.62 ?  63  PRO B C   1 
ATOM   3565 O O   . PRO B 1 63  ? 22.593  -15.263 17.071  1.00 17.10 ?  63  PRO B O   1 
ATOM   3566 C CB  . PRO B 1 63  ? 25.391  -13.768 17.834  1.00 18.54 ?  63  PRO B CB  1 
ATOM   3567 C CG  . PRO B 1 63  ? 24.456  -13.086 18.774  1.00 15.21 ?  63  PRO B CG  1 
ATOM   3568 C CD  . PRO B 1 63  ? 23.594  -12.170 17.928  1.00 17.17 ?  63  PRO B CD  1 
ATOM   3569 N N   . ALA B 1 64  ? 24.387  -16.315 16.186  1.00 20.11 ?  64  ALA B N   1 
ATOM   3570 C CA  . ALA B 1 64  ? 23.766  -17.633 16.295  1.00 19.81 ?  64  ALA B CA  1 
ATOM   3571 C C   . ALA B 1 64  ? 23.400  -17.958 17.736  1.00 18.01 ?  64  ALA B C   1 
ATOM   3572 O O   . ALA B 1 64  ? 22.393  -18.642 17.985  1.00 18.87 ?  64  ALA B O   1 
ATOM   3573 C CB  . ALA B 1 64  ? 24.703  -18.701 15.728  1.00 21.84 ?  64  ALA B CB  1 
ATOM   3574 N N   . GLU B 1 65  ? 24.202  -17.481 18.693  1.00 16.82 ?  65  GLU B N   1 
ATOM   3575 C CA  . GLU B 1 65  ? 23.924  -17.708 20.108  1.00 20.11 ?  65  GLU B CA  1 
ATOM   3576 C C   . GLU B 1 65  ? 22.547  -17.202 20.503  1.00 18.24 ?  65  GLU B C   1 
ATOM   3577 O O   . GLU B 1 65  ? 21.934  -17.739 21.431  1.00 17.37 ?  65  GLU B O   1 
ATOM   3578 C CB  . GLU B 1 65  ? 24.982  -17.025 20.970  1.00 19.15 ?  65  GLU B CB  1 
ATOM   3579 C CG  . GLU B 1 65  ? 26.332  -17.731 20.990  1.00 24.66 ?  65  GLU B CG  1 
ATOM   3580 C CD  . GLU B 1 65  ? 27.267  -17.306 19.860  1.00 29.12 ?  65  GLU B CD  1 
ATOM   3581 O OE1 . GLU B 1 65  ? 28.452  -17.722 19.897  1.00 30.03 ?  65  GLU B OE1 1 
ATOM   3582 O OE2 . GLU B 1 65  ? 26.834  -16.586 18.929  1.00 24.83 -1 65  GLU B OE2 1 
ATOM   3583 N N   . TYR B 1 66  ? 22.054  -16.164 19.833  1.00 14.30 ?  66  TYR B N   1 
ATOM   3584 C CA  . TYR B 1 66  ? 20.730  -15.647 20.167  1.00 17.16 ?  66  TYR B CA  1 
ATOM   3585 C C   . TYR B 1 66  ? 19.656  -16.663 19.824  1.00 17.44 ?  66  TYR B C   1 
ATOM   3586 O O   . TYR B 1 66  ? 18.787  -16.967 20.648  1.00 15.71 ?  66  TYR B O   1 
ATOM   3587 C CB  . TYR B 1 66  ? 20.476  -14.332 19.436  1.00 15.56 ?  66  TYR B CB  1 
ATOM   3588 C CG  . TYR B 1 66  ? 19.130  -13.706 19.718  1.00 15.90 ?  66  TYR B CG  1 
ATOM   3589 C CD1 . TYR B 1 66  ? 18.907  -13.001 20.893  1.00 16.45 ?  66  TYR B CD1 1 
ATOM   3590 C CD2 . TYR B 1 66  ? 18.085  -13.809 18.797  1.00 17.76 ?  66  TYR B CD2 1 
ATOM   3591 C CE1 . TYR B 1 66  ? 17.681  -12.414 21.153  1.00 20.79 ?  66  TYR B CE1 1 
ATOM   3592 C CE2 . TYR B 1 66  ? 16.855  -13.222 19.052  1.00 20.04 ?  66  TYR B CE2 1 
ATOM   3593 C CZ  . TYR B 1 66  ? 16.663  -12.533 20.233  1.00 18.58 ?  66  TYR B CZ  1 
ATOM   3594 O OH  . TYR B 1 66  ? 15.451  -11.937 20.492  1.00 20.67 ?  66  TYR B OH  1 
ATOM   3595 N N   . TYR B 1 67  ? 19.702  -17.202 18.602  1.00 17.05 ?  67  TYR B N   1 
ATOM   3596 C CA  . TYR B 1 67  ? 18.711  -18.186 18.188  1.00 17.50 ?  67  TYR B CA  1 
ATOM   3597 C C   . TYR B 1 67  ? 18.847  -19.472 18.985  1.00 15.52 ?  67  TYR B C   1 
ATOM   3598 O O   . TYR B 1 67  ? 17.839  -20.094 19.332  1.00 14.43 ?  67  TYR B O   1 
ATOM   3599 C CB  . TYR B 1 67  ? 18.833  -18.443 16.684  1.00 17.46 ?  67  TYR B CB  1 
ATOM   3600 C CG  . TYR B 1 67  ? 18.723  -17.163 15.885  1.00 20.72 ?  67  TYR B CG  1 
ATOM   3601 C CD1 . TYR B 1 67  ? 17.660  -16.300 16.106  1.00 22.70 ?  67  TYR B CD1 1 
ATOM   3602 C CD2 . TYR B 1 67  ? 19.689  -16.790 14.951  1.00 25.77 ?  67  TYR B CD2 1 
ATOM   3603 C CE1 . TYR B 1 67  ? 17.522  -15.132 15.405  1.00 24.72 ?  67  TYR B CE1 1 
ATOM   3604 C CE2 . TYR B 1 67  ? 19.556  -15.581 14.237  1.00 25.57 ?  67  TYR B CE2 1 
ATOM   3605 C CZ  . TYR B 1 67  ? 18.457  -14.770 14.482  1.00 24.89 ?  67  TYR B CZ  1 
ATOM   3606 O OH  . TYR B 1 67  ? 18.241  -13.566 13.825  1.00 29.43 ?  67  TYR B OH  1 
ATOM   3607 N N   . LYS B 1 68  ? 20.085  -19.884 19.299  1.00 15.72 ?  68  LYS B N   1 
ATOM   3608 C CA  . LYS B 1 68  ? 20.270  -21.060 20.145  1.00 16.00 ?  68  LYS B CA  1 
ATOM   3609 C C   . LYS B 1 68  ? 19.643  -20.858 21.518  1.00 15.34 ?  68  LYS B C   1 
ATOM   3610 O O   . LYS B 1 68  ? 18.992  -21.770 22.050  1.00 16.39 ?  68  LYS B O   1 
ATOM   3611 C CB  . LYS B 1 68  ? 21.755  -21.383 20.309  1.00 17.81 ?  68  LYS B CB  1 
ATOM   3612 C CG  . LYS B 1 68  ? 21.987  -22.419 21.392  1.00 21.40 ?  68  LYS B CG  1 
ATOM   3613 C CD  . LYS B 1 68  ? 23.458  -22.715 21.641  1.00 26.55 ?  68  LYS B CD  1 
ATOM   3614 C CE  . LYS B 1 68  ? 23.617  -23.887 22.605  1.00 29.59 ?  68  LYS B CE  1 
ATOM   3615 N NZ  . LYS B 1 68  ? 22.733  -25.043 22.247  1.00 33.10 1  68  LYS B NZ  1 
ATOM   3616 N N   . ALA B 1 69  ? 19.831  -19.670 22.107  1.00 17.17 ?  69  ALA B N   1 
ATOM   3617 C CA  . ALA B 1 69  ? 19.243  -19.369 23.409  1.00 16.73 ?  69  ALA B CA  1 
ATOM   3618 C C   . ALA B 1 69  ? 17.723  -19.455 23.353  1.00 16.60 ?  69  ALA B C   1 
ATOM   3619 O O   . ALA B 1 69  ? 17.093  -20.031 24.252  1.00 16.22 ?  69  ALA B O   1 
ATOM   3620 C CB  . ALA B 1 69  ? 19.684  -17.981 23.883  1.00 16.31 ?  69  ALA B CB  1 
ATOM   3621 N N   . VAL B 1 70  ? 17.129  -18.912 22.302  1.00 12.92 ?  70  VAL B N   1 
ATOM   3622 C CA  . VAL B 1 70  ? 15.650  -18.961 22.121  1.00 14.47 ?  70  VAL B CA  1 
ATOM   3623 C C   . VAL B 1 70  ? 15.214  -20.431 22.009  1.00 14.62 ?  70  VAL B C   1 
ATOM   3624 O O   . VAL B 1 70  ? 14.272  -20.816 22.675  1.00 14.56 ?  70  VAL B O   1 
ATOM   3625 C CB  . VAL B 1 70  ? 15.241  -18.126 20.894  1.00 14.15 ?  70  VAL B CB  1 
ATOM   3626 C CG1 . VAL B 1 70  ? 13.856  -18.480 20.383  1.00 15.60 ?  70  VAL B CG1 1 
ATOM   3627 C CG2 . VAL B 1 70  ? 15.370  -16.634 21.130  1.00 16.19 ?  70  VAL B CG2 1 
ATOM   3628 N N   . ALA B 1 71  ? 15.933  -21.204 21.208  1.00 14.19 ?  71  ALA B N   1 
ATOM   3629 C CA  . ALA B 1 71  ? 15.537  -22.591 20.989  1.00 15.18 ?  71  ALA B CA  1 
ATOM   3630 C C   . ALA B 1 71  ? 15.689  -23.423 22.257  1.00 15.68 ?  71  ALA B C   1 
ATOM   3631 O O   . ALA B 1 71  ? 14.823  -24.248 22.568  1.00 15.59 ?  71  ALA B O   1 
ATOM   3632 C CB  . ALA B 1 71  ? 16.353  -23.192 19.844  1.00 18.00 ?  71  ALA B CB  1 
ATOM   3633 N N   . ASP B 1 72  ? 16.799  -23.247 22.982  1.00 16.46 ?  72  ASP B N   1 
ATOM   3634 C CA  . ASP B 1 72  ? 16.975  -23.954 24.247  1.00 17.57 ?  72  ASP B CA  1 
ATOM   3635 C C   . ASP B 1 72  ? 15.892  -23.566 25.238  1.00 16.79 ?  72  ASP B C   1 
ATOM   3636 O O   . ASP B 1 72  ? 15.353  -24.427 25.942  1.00 17.70 ?  72  ASP B O   1 
ATOM   3637 C CB  . ASP B 1 72  ? 18.347  -23.659 24.852  1.00 17.36 ?  72  ASP B CB  1 
ATOM   3638 C CG  . ASP B 1 72  ? 19.492  -24.232 24.033  1.00 20.89 ?  72  ASP B CG  1 
ATOM   3639 O OD1 . ASP B 1 72  ? 19.245  -25.103 23.177  1.00 22.97 ?  72  ASP B OD1 1 
ATOM   3640 O OD2 . ASP B 1 72  ? 20.648  -23.812 24.269  1.00 21.99 -1 72  ASP B OD2 1 
ATOM   3641 N N   . TRP B 1 73  ? 15.572  -22.268 25.318  1.00 14.62 ?  73  TRP B N   1 
ATOM   3642 C CA  . TRP B 1 73  ? 14.562  -21.810 26.270  1.00 14.23 ?  73  TRP B CA  1 
ATOM   3643 C C   . TRP B 1 73  ? 13.215  -22.462 25.981  1.00 15.21 ?  73  TRP B C   1 
ATOM   3644 O O   . TRP B 1 73  ? 12.580  -23.028 26.877  1.00 15.17 ?  73  TRP B O   1 
ATOM   3645 C CB  . TRP B 1 73  ? 14.443  -20.284 26.224  1.00 16.21 ?  73  TRP B CB  1 
ATOM   3646 C CG  . TRP B 1 73  ? 13.304  -19.742 27.050  1.00 15.63 ?  73  TRP B CG  1 
ATOM   3647 C CD1 . TRP B 1 73  ? 12.045  -19.431 26.611  1.00 15.27 ?  73  TRP B CD1 1 
ATOM   3648 C CD2 . TRP B 1 73  ? 13.317  -19.465 28.458  1.00 16.26 ?  73  TRP B CD2 1 
ATOM   3649 N NE1 . TRP B 1 73  ? 11.278  -18.973 27.658  1.00 17.79 ?  73  TRP B NE1 1 
ATOM   3650 C CE2 . TRP B 1 73  ? 12.035  -18.986 28.802  1.00 15.27 ?  73  TRP B CE2 1 
ATOM   3651 C CE3 . TRP B 1 73  ? 14.287  -19.577 29.461  1.00 16.62 ?  73  TRP B CE3 1 
ATOM   3652 C CZ2 . TRP B 1 73  ? 11.700  -18.612 30.105  1.00 15.57 ?  73  TRP B CZ2 1 
ATOM   3653 C CZ3 . TRP B 1 73  ? 13.957  -19.200 30.748  1.00 15.36 ?  73  TRP B CZ3 1 
ATOM   3654 C CH2 . TRP B 1 73  ? 12.668  -18.722 31.059  1.00 15.09 ?  73  TRP B CH2 1 
ATOM   3655 N N   . GLU B 1 74  ? 12.785  -22.427 24.717  1.00 13.76 ?  74  GLU B N   1 
ATOM   3656 C CA  . GLU B 1 74  ? 11.513  -23.031 24.350  1.00 17.01 ?  74  GLU B CA  1 
ATOM   3657 C C   . GLU B 1 74  ? 11.524  -24.536 24.594  1.00 16.23 ?  74  GLU B C   1 
ATOM   3658 O O   . GLU B 1 74  ? 10.496  -25.113 24.957  1.00 17.13 ?  74  GLU B O   1 
ATOM   3659 C CB  . GLU B 1 74  ? 11.197  -22.738 22.883  1.00 15.53 ?  74  GLU B CB  1 
ATOM   3660 C CG  . GLU B 1 74  ? 11.012  -21.261 22.549  1.00 15.88 ?  74  GLU B CG  1 
ATOM   3661 C CD  . GLU B 1 74  ? 9.684   -20.723 23.026  1.00 19.24 ?  74  GLU B CD  1 
ATOM   3662 O OE1 . GLU B 1 74  ? 9.601   -20.304 24.192  1.00 22.06 ?  74  GLU B OE1 1 
ATOM   3663 O OE2 . GLU B 1 74  ? 8.717   -20.720 22.226  1.00 22.00 -1 74  GLU B OE2 1 
ATOM   3664 N N   . GLU B 1 75  ? 12.674  -25.193 24.405  1.00 18.79 ?  75  GLU B N   1 
ATOM   3665 C CA  . GLU B 1 75  ? 12.731  -26.626 24.670  1.00 17.41 ?  75  GLU B CA  1 
ATOM   3666 C C   . GLU B 1 75  ? 12.594  -26.916 26.161  1.00 20.00 ?  75  GLU B C   1 
ATOM   3667 O O   . GLU B 1 75  ? 11.793  -27.770 26.569  1.00 20.13 ?  75  GLU B O   1 
ATOM   3668 C CB  . GLU B 1 75  ? 14.033  -27.225 24.143  1.00 19.57 ?  75  GLU B CB  1 
ATOM   3669 C CG  . GLU B 1 75  ? 14.115  -28.715 24.431  1.00 21.13 ?  75  GLU B CG  1 
ATOM   3670 C CD  . GLU B 1 75  ? 15.163  -29.425 23.600  1.00 27.33 ?  75  GLU B CD  1 
ATOM   3671 O OE1 . GLU B 1 75  ? 14.899  -30.569 23.159  1.00 30.26 ?  75  GLU B OE1 1 
ATOM   3672 O OE2 . GLU B 1 75  ? 16.243  -28.844 23.386  1.00 26.03 -1 75  GLU B OE2 1 
ATOM   3673 N N   . ILE B 1 76  ? 13.382  -26.227 26.987  1.00 19.44 ?  76  ILE B N   1 
ATOM   3674 C CA  . ILE B 1 76  ? 13.405  -26.517 28.418  1.00 19.48 ?  76  ILE B CA  1 
ATOM   3675 C C   . ILE B 1 76  ? 12.086  -26.122 29.067  1.00 19.10 ?  76  ILE B C   1 
ATOM   3676 O O   . ILE B 1 76  ? 11.485  -26.897 29.818  1.00 19.97 ?  76  ILE B O   1 
ATOM   3677 C CB  . ILE B 1 76  ? 14.596  -25.806 29.089  1.00 17.70 ?  76  ILE B CB  1 
ATOM   3678 C CG1 . ILE B 1 76  ? 15.911  -26.455 28.651  1.00 21.76 ?  76  ILE B CG1 1 
ATOM   3679 C CG2 . ILE B 1 76  ? 14.455  -25.831 30.613  1.00 19.72 ?  76  ILE B CG2 1 
ATOM   3680 C CD1 . ILE B 1 76  ? 17.119  -25.546 28.810  1.00 23.98 ?  76  ILE B CD1 1 
ATOM   3681 N N   . GLU B 1 77  ? 11.617  -24.908 28.794  1.00 17.59 ?  77  GLU B N   1 
ATOM   3682 C CA  . GLU B 1 77  ? 10.430  -24.421 29.482  1.00 18.11 ?  77  GLU B CA  1 
ATOM   3683 C C   . GLU B 1 77  ? 9.139   -24.961 28.882  1.00 18.98 ?  77  GLU B C   1 
ATOM   3684 O O   . GLU B 1 77  ? 8.157   -25.117 29.609  1.00 19.77 ?  77  GLU B O   1 
ATOM   3685 C CB  . GLU B 1 77  ? 10.400  -22.888 29.478  1.00 18.50 ?  77  GLU B CB  1 
ATOM   3686 C CG  . GLU B 1 77  ? 11.512  -22.239 30.306  1.00 17.91 ?  77  GLU B CG  1 
ATOM   3687 C CD  . GLU B 1 77  ? 11.301  -22.372 31.818  1.00 19.67 ?  77  GLU B CD  1 
ATOM   3688 O OE1 . GLU B 1 77  ? 12.298  -22.573 32.549  1.00 22.63 ?  77  GLU B OE1 1 
ATOM   3689 O OE2 . GLU B 1 77  ? 10.149  -22.265 32.285  1.00 23.28 -1 77  GLU B OE2 1 
ATOM   3690 N N   . HIS B 1 78  ? 9.096   -25.246 27.579  1.00 17.49 ?  78  HIS B N   1 
ATOM   3691 C CA  . HIS B 1 78  ? 7.815   -25.543 26.943  1.00 20.11 ?  78  HIS B CA  1 
ATOM   3692 C C   . HIS B 1 78  ? 7.787   -26.868 26.194  1.00 19.69 ?  78  HIS B C   1 
ATOM   3693 O O   . HIS B 1 78  ? 6.783   -27.160 25.528  1.00 21.28 ?  78  HIS B O   1 
ATOM   3694 C CB  . HIS B 1 78  ? 7.416   -24.391 26.013  1.00 20.35 ?  78  HIS B CB  1 
ATOM   3695 C CG  . HIS B 1 78  ? 7.322   -23.078 26.724  1.00 19.46 ?  78  HIS B CG  1 
ATOM   3696 N ND1 . HIS B 1 78  ? 6.634   -22.931 27.909  1.00 24.14 ?  78  HIS B ND1 1 
ATOM   3697 C CD2 . HIS B 1 78  ? 7.867   -21.869 26.454  1.00 19.36 ?  78  HIS B CD2 1 
ATOM   3698 C CE1 . HIS B 1 78  ? 6.735   -21.680 28.325  1.00 24.06 ?  78  HIS B CE1 1 
ATOM   3699 N NE2 . HIS B 1 78  ? 7.483   -21.015 27.462  1.00 19.95 ?  78  HIS B NE2 1 
ATOM   3700 N N   . ARG B 1 79  ? 8.855   -27.674 26.293  1.00 18.74 ?  79  ARG B N   1 
ATOM   3701 C CA  . ARG B 1 79  ? 8.950   -28.980 25.628  1.00 22.96 ?  79  ARG B CA  1 
ATOM   3702 C C   . ARG B 1 79  ? 8.698   -28.864 24.130  1.00 22.21 ?  79  ARG B C   1 
ATOM   3703 O O   . ARG B 1 79  ? 8.071   -29.730 23.520  1.00 24.72 ?  79  ARG B O   1 
ATOM   3704 C CB  . ARG B 1 79  ? 7.987   -29.993 26.248  1.00 27.44 ?  79  ARG B CB  1 
ATOM   3705 C CG  . ARG B 1 79  ? 7.956   -29.979 27.759  1.00 29.24 ?  79  ARG B CG  1 
ATOM   3706 C CD  . ARG B 1 79  ? 7.157   -31.161 28.288  1.00 32.86 ?  79  ARG B CD  1 
ATOM   3707 N NE  . ARG B 1 79  ? 7.850   -32.427 28.064  1.00 43.78 ?  79  ARG B NE  1 
ATOM   3708 C CZ  . ARG B 1 79  ? 7.240   -33.596 27.882  1.00 46.61 ?  79  ARG B CZ  1 
ATOM   3709 N NH1 . ARG B 1 79  ? 5.912   -33.661 27.885  1.00 42.50 1  79  ARG B NH1 1 
ATOM   3710 N NH2 . ARG B 1 79  ? 7.960   -34.699 27.694  1.00 43.89 ?  79  ARG B NH2 1 
ATOM   3711 N N   . ALA B 1 80  ? 9.174   -27.776 23.532  1.00 19.22 ?  80  ALA B N   1 
ATOM   3712 C CA  . ALA B 1 80  ? 8.873   -27.496 22.125  1.00 21.38 ?  80  ALA B CA  1 
ATOM   3713 C C   . ALA B 1 80  ? 10.039  -26.698 21.541  1.00 19.19 ?  80  ALA B C   1 
ATOM   3714 O O   . ALA B 1 80  ? 10.023  -25.466 21.553  1.00 19.19 ?  80  ALA B O   1 
ATOM   3715 C CB  . ALA B 1 80  ? 7.563   -26.736 21.989  1.00 20.31 ?  80  ALA B CB  1 
ATOM   3716 N N   . ARG B 1 81  ? 11.033  -27.410 21.009  1.00 19.06 ?  81  ARG B N   1 
ATOM   3717 C CA  . ARG B 1 81  ? 12.209  -26.744 20.457  1.00 16.88 ?  81  ARG B CA  1 
ATOM   3718 C C   . ARG B 1 81  ? 11.925  -26.277 19.037  1.00 16.65 ?  81  ARG B C   1 
ATOM   3719 O O   . ARG B 1 81  ? 11.577  -27.100 18.184  1.00 20.60 ?  81  ARG B O   1 
ATOM   3720 C CB  . ARG B 1 81  ? 13.419  -27.671 20.453  1.00 19.64 ?  81  ARG B CB  1 
ATOM   3721 C CG  . ARG B 1 81  ? 14.704  -26.927 20.241  1.00 17.30 ?  81  ARG B CG  1 
ATOM   3722 C CD  . ARG B 1 81  ? 15.890  -27.865 20.058  1.00 21.58 ?  81  ARG B CD  1 
ATOM   3723 N NE  . ARG B 1 81  ? 17.076  -27.057 19.823  1.00 22.98 ?  81  ARG B NE  1 
ATOM   3724 C CZ  . ARG B 1 81  ? 17.791  -26.495 20.785  1.00 19.90 ?  81  ARG B CZ  1 
ATOM   3725 N NH1 . ARG B 1 81  ? 17.453  -26.681 22.057  1.00 21.21 1  81  ARG B NH1 1 
ATOM   3726 N NH2 . ARG B 1 81  ? 18.844  -25.748 20.476  1.00 22.38 ?  81  ARG B NH2 1 
ATOM   3727 N N   . PRO B 1 82  ? 12.047  -24.986 18.737  1.00 17.97 ?  82  PRO B N   1 
ATOM   3728 C CA  . PRO B 1 82  ? 12.034  -24.557 17.337  1.00 14.82 ?  82  PRO B CA  1 
ATOM   3729 C C   . PRO B 1 82  ? 13.368  -24.875 16.688  1.00 17.53 ?  82  PRO B C   1 
ATOM   3730 O O   . PRO B 1 82  ? 14.389  -25.029 17.356  1.00 17.51 ?  82  PRO B O   1 
ATOM   3731 C CB  . PRO B 1 82  ? 11.809  -23.042 17.433  1.00 19.51 ?  82  PRO B CB  1 
ATOM   3732 C CG  . PRO B 1 82  ? 12.491  -22.667 18.708  1.00 15.69 ?  82  PRO B CG  1 
ATOM   3733 C CD  . PRO B 1 82  ? 12.226  -23.847 19.659  1.00 17.06 ?  82  PRO B CD  1 
ATOM   3734 N N   . LYS B 1 83  ? 13.351  -24.997 15.365  1.00 18.74 ?  83  LYS B N   1 
ATOM   3735 C CA  . LYS B 1 83  ? 14.608  -24.997 14.638  1.00 20.42 ?  83  LYS B CA  1 
ATOM   3736 C C   . LYS B 1 83  ? 15.218  -23.609 14.723  1.00 17.08 ?  83  LYS B C   1 
ATOM   3737 O O   . LYS B 1 83  ? 14.513  -22.601 14.606  1.00 17.58 ?  83  LYS B O   1 
ATOM   3738 C CB  . LYS B 1 83  ? 14.396  -25.400 13.179  1.00 19.93 ?  83  LYS B CB  1 
ATOM   3739 C CG  . LYS B 1 83  ? 13.633  -26.702 13.008  1.00 21.56 ?  83  LYS B CG  1 
ATOM   3740 C CD  . LYS B 1 83  ? 14.527  -27.903 13.161  1.00 27.68 ?  83  LYS B CD  1 
ATOM   3741 C CE  . LYS B 1 83  ? 13.938  -29.083 12.405  1.00 34.50 ?  83  LYS B CE  1 
ATOM   3742 N NZ  . LYS B 1 83  ? 13.619  -28.704 10.986  1.00 31.93 1  83  LYS B NZ  1 
ATOM   3743 N N   . GLU B 1 84  ? 16.537  -23.553 14.941  1.00 16.71 ?  84  GLU B N   1 
ATOM   3744 C CA  . GLU B 1 84  ? 17.185  -22.257 15.107  1.00 18.08 ?  84  GLU B CA  1 
ATOM   3745 C C   . GLU B 1 84  ? 17.008  -21.388 13.871  1.00 18.64 ?  84  GLU B C   1 
ATOM   3746 O O   . GLU B 1 84  ? 16.873  -20.163 13.987  1.00 18.78 ?  84  GLU B O   1 
ATOM   3747 C CB  . GLU B 1 84  ? 18.673  -22.430 15.416  1.00 18.91 ?  84  GLU B CB  1 
ATOM   3748 C CG  . GLU B 1 84  ? 18.965  -22.815 16.852  1.00 19.49 ?  84  GLU B CG  1 
ATOM   3749 C CD  . GLU B 1 84  ? 19.010  -24.326 17.049  1.00 26.79 ?  84  GLU B CD  1 
ATOM   3750 O OE1 . GLU B 1 84  ? 19.539  -24.768 18.097  1.00 29.62 ?  84  GLU B OE1 1 
ATOM   3751 O OE2 . GLU B 1 84  ? 18.529  -25.074 16.151  1.00 28.31 -1 84  GLU B OE2 1 
ATOM   3752 N N   . ASP B 1 85  ? 17.009  -21.996 12.676  1.00 17.71 ?  85  ASP B N   1 
ATOM   3753 C CA  . ASP B 1 85  ? 16.878  -21.191 11.463  1.00 19.69 ?  85  ASP B CA  1 
ATOM   3754 C C   . ASP B 1 85  ? 15.461  -20.663 11.248  1.00 18.28 ?  85  ASP B C   1 
ATOM   3755 O O   . ASP B 1 85  ? 15.250  -19.860 10.334  1.00 16.22 ?  85  ASP B O   1 
ATOM   3756 C CB  . ASP B 1 85  ? 17.357  -21.960 10.213  1.00 24.40 ?  85  ASP B CB  1 
ATOM   3757 C CG  . ASP B 1 85  ? 16.686  -23.321 10.029  1.00 26.25 ?  85  ASP B CG  1 
ATOM   3758 O OD1 . ASP B 1 85  ? 15.955  -23.786 10.919  1.00 27.09 ?  85  ASP B OD1 1 
ATOM   3759 O OD2 . ASP B 1 85  ? 16.892  -23.937 8.956   1.00 36.17 -1 85  ASP B OD2 1 
ATOM   3760 N N   . TRP B 1 86  ? 14.493  -21.058 12.078  1.00 17.99 ?  86  TRP B N   1 
ATOM   3761 C CA  . TRP B 1 86  ? 13.162  -20.463 12.011  1.00 14.85 ?  86  TRP B CA  1 
ATOM   3762 C C   . TRP B 1 86  ? 13.112  -19.065 12.616  1.00 16.74 ?  86  TRP B C   1 
ATOM   3763 O O   . TRP B 1 86  ? 12.116  -18.356 12.433  1.00 15.60 ?  86  TRP B O   1 
ATOM   3764 C CB  . TRP B 1 86  ? 12.139  -21.341 12.750  1.00 17.01 ?  86  TRP B CB  1 
ATOM   3765 C CG  . TRP B 1 86  ? 11.859  -22.681 12.145  1.00 15.44 ?  86  TRP B CG  1 
ATOM   3766 C CD1 . TRP B 1 86  ? 12.310  -23.163 10.942  1.00 17.18 ?  86  TRP B CD1 1 
ATOM   3767 C CD2 . TRP B 1 86  ? 11.037  -23.714 12.710  1.00 16.97 ?  86  TRP B CD2 1 
ATOM   3768 N NE1 . TRP B 1 86  ? 11.818  -24.433 10.735  1.00 16.75 ?  86  TRP B NE1 1 
ATOM   3769 C CE2 . TRP B 1 86  ? 11.040  -24.794 11.805  1.00 18.65 ?  86  TRP B CE2 1 
ATOM   3770 C CE3 . TRP B 1 86  ? 10.305  -23.830 13.904  1.00 16.19 ?  86  TRP B CE3 1 
ATOM   3771 C CZ2 . TRP B 1 86  ? 10.343  -25.983 12.053  1.00 18.38 ?  86  TRP B CZ2 1 
ATOM   3772 C CZ3 . TRP B 1 86  ? 9.617   -25.012 14.152  1.00 15.77 ?  86  TRP B CZ3 1 
ATOM   3773 C CH2 . TRP B 1 86  ? 9.639   -26.070 13.227  1.00 18.72 ?  86  TRP B CH2 1 
ATOM   3774 N N   . CYS B 1 87  ? 14.153  -18.656 13.330  1.00 16.52 ?  87  CYS B N   1 
ATOM   3775 C CA  . CYS B 1 87  ? 14.082  -17.529 14.248  1.00 15.56 ?  87  CYS B CA  1 
ATOM   3776 C C   . CYS B 1 87  ? 14.602  -16.261 13.588  1.00 18.75 ?  87  CYS B C   1 
ATOM   3777 O O   . CYS B 1 87  ? 15.604  -16.294 12.870  1.00 18.18 ?  87  CYS B O   1 
ATOM   3778 C CB  . CYS B 1 87  ? 14.894  -17.830 15.508  1.00 18.24 ?  87  CYS B CB  1 
ATOM   3779 S SG  . CYS B 1 87  ? 14.302  -19.221 16.456  1.00 19.05 ?  87  CYS B SG  1 
ATOM   3780 N N   . VAL B 1 88  ? 13.913  -15.146 13.837  1.00 14.65 ?  88  VAL B N   1 
ATOM   3781 C CA  . VAL B 1 88  ? 14.262  -13.837 13.290  1.00 16.25 ?  88  VAL B CA  1 
ATOM   3782 C C   . VAL B 1 88  ? 14.140  -12.812 14.413  1.00 14.88 ?  88  VAL B C   1 
ATOM   3783 O O   . VAL B 1 88  ? 13.072  -12.674 15.011  1.00 15.20 ?  88  VAL B O   1 
ATOM   3784 C CB  . VAL B 1 88  ? 13.355  -13.427 12.115  1.00 16.50 ?  88  VAL B CB  1 
ATOM   3785 C CG1 . VAL B 1 88  ? 13.785  -12.086 11.535  1.00 16.39 ?  88  VAL B CG1 1 
ATOM   3786 C CG2 . VAL B 1 88  ? 13.344  -14.508 11.048  1.00 18.29 ?  88  VAL B CG2 1 
ATOM   3787 N N   . PHE B 1 89  ? 15.214  -12.085 14.687  1.00 13.91 ?  89  PHE B N   1 
ATOM   3788 C CA  . PHE B 1 89  ? 15.141  -11.008 15.672  1.00 15.42 ?  89  PHE B CA  1 
ATOM   3789 C C   . PHE B 1 89  ? 14.221  -9.869  15.210  1.00 15.14 ?  89  PHE B C   1 
ATOM   3790 O O   . PHE B 1 89  ? 14.224  -9.471  14.043  1.00 11.70 ?  89  PHE B O   1 
ATOM   3791 C CB  . PHE B 1 89  ? 16.545  -10.462 15.943  1.00 16.66 ?  89  PHE B CB  1 
ATOM   3792 C CG  . PHE B 1 89  ? 16.552  -9.281  16.861  1.00 13.53 ?  89  PHE B CG  1 
ATOM   3793 C CD1 . PHE B 1 89  ? 16.419  -7.999  16.362  1.00 14.13 ?  89  PHE B CD1 1 
ATOM   3794 C CD2 . PHE B 1 89  ? 16.665  -9.465  18.231  1.00 15.22 ?  89  PHE B CD2 1 
ATOM   3795 C CE1 . PHE B 1 89  ? 16.398  -6.904  17.212  1.00 15.50 ?  89  PHE B CE1 1 
ATOM   3796 C CE2 . PHE B 1 89  ? 16.635  -8.379  19.093  1.00 16.83 ?  89  PHE B CE2 1 
ATOM   3797 C CZ  . PHE B 1 89  ? 16.511  -7.099  18.584  1.00 15.48 ?  89  PHE B CZ  1 
ATOM   3798 N N   . ALA B 1 90  ? 13.445  -9.321  16.143  1.00 14.11 ?  90  ALA B N   1 
ATOM   3799 C CA  . ALA B 1 90  ? 12.764  -8.047  15.921  1.00 12.54 ?  90  ALA B CA  1 
ATOM   3800 C C   . ALA B 1 90  ? 12.829  -7.244  17.205  1.00 12.12 ?  90  ALA B C   1 
ATOM   3801 O O   . ALA B 1 90  ? 12.905  -7.807  18.298  1.00 11.61 ?  90  ALA B O   1 
ATOM   3802 C CB  . ALA B 1 90  ? 11.293  -8.208  15.479  1.00 12.98 ?  90  ALA B CB  1 
ATOM   3803 N N   . SER B 1 91  ? 12.799  -5.918  17.064  1.00 12.98 ?  91  SER B N   1 
ATOM   3804 C CA  . SER B 1 91  ? 12.884  -5.011  18.208  1.00 14.70 ?  91  SER B CA  1 
ATOM   3805 C C   . SER B 1 91  ? 11.659  -5.047  19.118  1.00 17.26 ?  91  SER B C   1 
ATOM   3806 O O   . SER B 1 91  ? 11.708  -4.499  20.224  1.00 18.03 ?  91  SER B O   1 
ATOM   3807 C CB  . SER B 1 91  ? 13.112  -3.593  17.704  1.00 15.82 ?  91  SER B CB  1 
ATOM   3808 O OG  . SER B 1 91  ? 14.442  -3.511  17.211  1.00 24.71 ?  91  SER B OG  1 
ATOM   3809 N N   . GLY B 1 92  ? 10.567  -5.658  18.714  1.00 17.73 ?  92  GLY B N   1 
ATOM   3810 C CA  . GLY B 1 92  ? 9.455   -5.789  19.630  1.00 15.30 ?  92  GLY B CA  1 
ATOM   3811 C C   . GLY B 1 92  ? 8.325   -6.536  18.968  1.00 17.84 ?  92  GLY B C   1 
ATOM   3812 O O   . GLY B 1 92  ? 8.263   -6.658  17.738  1.00 15.07 ?  92  GLY B O   1 
ATOM   3813 N N   . VAL B 1 93  ? 7.422   -7.030  19.808  1.00 16.12 ?  93  VAL B N   1 
ATOM   3814 C CA  . VAL B 1 93  ? 6.321   -7.845  19.302  1.00 16.43 ?  93  VAL B CA  1 
ATOM   3815 C C   . VAL B 1 93  ? 5.345   -6.995  18.493  1.00 14.56 ?  93  VAL B C   1 
ATOM   3816 O O   . VAL B 1 93  ? 5.017   -7.326  17.348  1.00 13.15 ?  93  VAL B O   1 
ATOM   3817 C CB  . VAL B 1 93  ? 5.633   -8.585  20.463  1.00 15.29 ?  93  VAL B CB  1 
ATOM   3818 C CG1 . VAL B 1 93  ? 4.313   -9.182  20.009  1.00 15.68 ?  93  VAL B CG1 1 
ATOM   3819 C CG2 . VAL B 1 93  ? 6.571   -9.680  21.010  1.00 14.45 ?  93  VAL B CG2 1 
ATOM   3820 N N   . VAL B 1 94  ? 4.857   -5.894  19.068  1.00 13.59 ?  94  VAL B N   1 
ATOM   3821 C CA  . VAL B 1 94  ? 3.884   -5.072  18.346  1.00 16.28 ?  94  VAL B CA  1 
ATOM   3822 C C   . VAL B 1 94  ? 4.487   -4.432  17.111  1.00 15.51 ?  94  VAL B C   1 
ATOM   3823 O O   . VAL B 1 94  ? 3.838   -4.475  16.038  1.00 16.18 ?  94  VAL B O   1 
ATOM   3824 C CB  . VAL B 1 94  ? 3.249   -4.047  19.312  1.00 19.11 ?  94  VAL B CB  1 
ATOM   3825 C CG1 . VAL B 1 94  ? 2.419   -3.035  18.540  1.00 18.38 ?  94  VAL B CG1 1 
ATOM   3826 C CG2 . VAL B 1 94  ? 2.384   -4.773  20.336  1.00 19.61 ?  94  VAL B CG2 1 
ATOM   3827 N N   . PRO B 1 95  ? 5.695   -3.836  17.137  1.00 16.73 ?  95  PRO B N   1 
ATOM   3828 C CA  . PRO B 1 95  ? 6.344   -3.423  15.880  1.00 16.10 ?  95  PRO B CA  1 
ATOM   3829 C C   . PRO B 1 95  ? 6.443   -4.543  14.857  1.00 14.75 ?  95  PRO B C   1 
ATOM   3830 O O   . PRO B 1 95  ? 6.257   -4.299  13.656  1.00 13.81 ?  95  PRO B O   1 
ATOM   3831 C CB  . PRO B 1 95  ? 7.739   -2.956  16.335  1.00 15.25 ?  95  PRO B CB  1 
ATOM   3832 C CG  . PRO B 1 95  ? 7.533   -2.500  17.733  1.00 16.15 ?  95  PRO B CG  1 
ATOM   3833 C CD  . PRO B 1 95  ? 6.497   -3.432  18.316  1.00 17.45 ?  95  PRO B CD  1 
ATOM   3834 N N   . ALA B 1 96  ? 6.707   -5.777  15.297  1.00 13.85 ?  96  ALA B N   1 
ATOM   3835 C CA  . ALA B 1 96  ? 6.767   -6.890  14.356  1.00 13.84 ?  96  ALA B CA  1 
ATOM   3836 C C   . ALA B 1 96  ? 5.396   -7.160  13.742  1.00 12.74 ?  96  ALA B C   1 
ATOM   3837 O O   . ALA B 1 96  ? 5.278   -7.340  12.525  1.00 12.23 ?  96  ALA B O   1 
ATOM   3838 C CB  . ALA B 1 96  ? 7.311   -8.145  15.034  1.00 13.92 ?  96  ALA B CB  1 
ATOM   3839 N N   . ILE B 1 97  ? 4.345   -7.179  14.564  1.00 13.19 ?  97  ILE B N   1 
ATOM   3840 C CA  . ILE B 1 97  ? 3.000   -7.332  14.014  1.00 12.38 ?  97  ILE B CA  1 
ATOM   3841 C C   . ILE B 1 97  ? 2.706   -6.216  13.016  1.00 12.78 ?  97  ILE B C   1 
ATOM   3842 O O   . ILE B 1 97  ? 2.160   -6.456  11.924  1.00 12.26 ?  97  ILE B O   1 
ATOM   3843 C CB  . ILE B 1 97  ? 1.954   -7.374  15.148  1.00 13.14 ?  97  ILE B CB  1 
ATOM   3844 C CG1 . ILE B 1 97  ? 2.131   -8.633  15.997  1.00 14.16 ?  97  ILE B CG1 1 
ATOM   3845 C CG2 . ILE B 1 97  ? 0.545   -7.349  14.579  1.00 12.61 ?  97  ILE B CG2 1 
ATOM   3846 C CD1 . ILE B 1 97  ? 1.226   -8.681  17.204  1.00 13.44 ?  97  ILE B CD1 1 
ATOM   3847 N N   . SER B 1 98  ? 3.077   -4.978  13.362  1.00 14.53 ?  98  SER B N   1 
ATOM   3848 C CA  . SER B 1 98  ? 2.793   -3.851  12.477  1.00 14.04 ?  98  SER B CA  1 
ATOM   3849 C C   . SER B 1 98  ? 3.460   -4.035  11.120  1.00 13.25 ?  98  SER B C   1 
ATOM   3850 O O   . SER B 1 98  ? 2.834   -3.804  10.077  1.00 13.63 ?  98  SER B O   1 
ATOM   3851 C CB  . SER B 1 98  ? 3.229   -2.537  13.132  1.00 15.32 ?  98  SER B CB  1 
ATOM   3852 O OG  . SER B 1 98  ? 2.810   -1.416  12.365  1.00 17.06 ?  98  SER B OG  1 
ATOM   3853 N N   . ALA B 1 99  ? 4.711   -4.502  11.114  1.00 13.04 ?  99  ALA B N   1 
ATOM   3854 C CA  . ALA B 1 99  ? 5.434   -4.731  9.868   1.00 14.03 ?  99  ALA B CA  1 
ATOM   3855 C C   . ALA B 1 99  ? 4.794   -5.848  9.045   1.00 16.08 ?  99  ALA B C   1 
ATOM   3856 O O   . ALA B 1 99  ? 4.675   -5.730  7.819   1.00 13.25 ?  99  ALA B O   1 
ATOM   3857 C CB  . ALA B 1 99  ? 6.900   -5.049  10.170  1.00 13.80 ?  99  ALA B CB  1 
ATOM   3858 N N   . MET B 1 100 ? 4.370   -6.937  9.699   1.00 12.57 ?  100 MET B N   1 
ATOM   3859 C CA  . MET B 1 100 ? 3.732   -8.036  8.977   1.00 16.06 ?  100 MET B CA  1 
ATOM   3860 C C   . MET B 1 100 ? 2.335   -7.662  8.485   1.00 16.03 ?  100 MET B C   1 
ATOM   3861 O O   . MET B 1 100 ? 1.902   -8.160  7.436   1.00 14.11 ?  100 MET B O   1 
ATOM   3862 C CB  . MET B 1 100 ? 3.697   -9.286  9.866   1.00 13.61 ?  100 MET B CB  1 
ATOM   3863 C CG  . MET B 1 100 ? 5.112   -9.805  10.115  1.00 15.90 ?  100 MET B CG  1 
ATOM   3864 S SD  . MET B 1 100 ? 5.259   -11.326 11.060  1.00 18.64 ?  100 MET B SD  1 
ATOM   3865 C CE  . MET B 1 100 ? 4.480   -10.795 12.605  1.00 16.59 ?  100 MET B CE  1 
ATOM   3866 N N   . VAL B 1 101 ? 1.628   -6.778  9.202   1.00 12.21 ?  101 VAL B N   1 
ATOM   3867 C CA  . VAL B 1 101 ? 0.381   -6.234  8.660   1.00 13.22 ?  101 VAL B CA  1 
ATOM   3868 C C   . VAL B 1 101 ? 0.655   -5.553  7.323   1.00 15.09 ?  101 VAL B C   1 
ATOM   3869 O O   . VAL B 1 101 ? -0.046  -5.778  6.329   1.00 14.79 ?  101 VAL B O   1 
ATOM   3870 C CB  . VAL B 1 101 ? -0.267  -5.263  9.663   1.00 15.20 ?  101 VAL B CB  1 
ATOM   3871 C CG1 . VAL B 1 101 ? -1.401  -4.475  8.998   1.00 15.04 ?  101 VAL B CG1 1 
ATOM   3872 C CG2 . VAL B 1 101 ? -0.814  -6.006  10.851  1.00 15.53 ?  101 VAL B CG2 1 
ATOM   3873 N N   . ARG B 1 102 ? 1.702   -4.724  7.269   1.00 12.64 ?  102 ARG B N   1 
ATOM   3874 C CA  . ARG B 1 102 ? 2.003   -4.038  6.019   1.00 16.27 ?  102 ARG B CA  1 
ATOM   3875 C C   . ARG B 1 102 ? 2.509   -5.010  4.948   1.00 16.45 ?  102 ARG B C   1 
ATOM   3876 O O   . ARG B 1 102 ? 2.167   -4.865  3.770   1.00 16.75 ?  102 ARG B O   1 
ATOM   3877 C CB  . ARG B 1 102 ? 3.012   -2.910  6.260   1.00 15.95 ?  102 ARG B CB  1 
ATOM   3878 C CG  . ARG B 1 102 ? 2.411   -1.682  6.969   1.00 16.72 ?  102 ARG B CG  1 
ATOM   3879 C CD  . ARG B 1 102 ? 3.357   -0.475  6.952   1.00 18.23 ?  102 ARG B CD  1 
ATOM   3880 N NE  . ARG B 1 102 ? 4.646   -0.821  7.544   1.00 18.12 ?  102 ARG B NE  1 
ATOM   3881 C CZ  . ARG B 1 102 ? 4.863   -0.900  8.853   1.00 18.42 ?  102 ARG B CZ  1 
ATOM   3882 N NH1 . ARG B 1 102 ? 3.880   -0.621  9.704   1.00 17.41 1  102 ARG B NH1 1 
ATOM   3883 N NH2 . ARG B 1 102 ? 6.055   -1.246  9.308   1.00 17.52 ?  102 ARG B NH2 1 
ATOM   3884 N N   . GLN B 1 103 ? 3.301   -6.016  5.327   1.00 14.14 ?  103 GLN B N   1 
ATOM   3885 C CA  . GLN B 1 103 ? 3.913   -6.873  4.311   1.00 17.09 ?  103 GLN B CA  1 
ATOM   3886 C C   . GLN B 1 103 ? 2.947   -7.916  3.765   1.00 17.15 ?  103 GLN B C   1 
ATOM   3887 O O   . GLN B 1 103 ? 3.022   -8.287  2.585   1.00 17.00 ?  103 GLN B O   1 
ATOM   3888 C CB  . GLN B 1 103 ? 5.137   -7.589  4.880   1.00 17.99 ?  103 GLN B CB  1 
ATOM   3889 C CG  . GLN B 1 103 ? 6.092   -8.016  3.791   1.00 17.99 ?  103 GLN B CG  1 
ATOM   3890 C CD  . GLN B 1 103 ? 6.555   -6.807  3.020   1.00 22.12 ?  103 GLN B CD  1 
ATOM   3891 O OE1 . GLN B 1 103 ? 6.934   -5.789  3.620   1.00 26.34 ?  103 GLN B OE1 1 
ATOM   3892 N NE2 . GLN B 1 103 ? 6.481   -6.877  1.697   1.00 20.88 ?  103 GLN B NE2 1 
ATOM   3893 N N   . PHE B 1 104 ? 2.067   -8.433  4.613   1.00 14.27 ?  104 PHE B N   1 
ATOM   3894 C CA  . PHE B 1 104 ? 1.333   -9.641  4.294   1.00 13.88 ?  104 PHE B CA  1 
ATOM   3895 C C   . PHE B 1 104 ? -0.145  -9.394  4.061   1.00 15.25 ?  104 PHE B C   1 
ATOM   3896 O O   . PHE B 1 104 ? -0.882  -10.346 3.803   1.00 14.76 ?  104 PHE B O   1 
ATOM   3897 C CB  . PHE B 1 104 ? 1.533   -10.678 5.408   1.00 14.18 ?  104 PHE B CB  1 
ATOM   3898 C CG  . PHE B 1 104 ? 2.972   -11.084 5.591   1.00 13.78 ?  104 PHE B CG  1 
ATOM   3899 C CD1 . PHE B 1 104 ? 3.799   -11.243 4.490   1.00 16.90 ?  104 PHE B CD1 1 
ATOM   3900 C CD2 . PHE B 1 104 ? 3.482   -11.315 6.845   1.00 14.89 ?  104 PHE B CD2 1 
ATOM   3901 C CE1 . PHE B 1 104 ? 5.130   -11.623 4.650   1.00 15.54 ?  104 PHE B CE1 1 
ATOM   3902 C CE2 . PHE B 1 104 ? 4.813   -11.696 7.015   1.00 15.17 ?  104 PHE B CE2 1 
ATOM   3903 C CZ  . PHE B 1 104 ? 5.633   -11.842 5.920   1.00 14.93 ?  104 PHE B CZ  1 
ATOM   3904 N N   . THR B 1 105 ? -0.604  -8.157  4.170   1.00 14.01 ?  105 THR B N   1 
ATOM   3905 C CA  . THR B 1 105 ? -1.969  -7.807  3.782   1.00 15.66 ?  105 THR B CA  1 
ATOM   3906 C C   . THR B 1 105 ? -1.929  -6.540  2.944   1.00 16.45 ?  105 THR B C   1 
ATOM   3907 O O   . THR B 1 105 ? -0.907  -5.861  2.864   1.00 15.06 ?  105 THR B O   1 
ATOM   3908 C CB  . THR B 1 105 ? -2.887  -7.576  4.995   1.00 14.23 ?  105 THR B CB  1 
ATOM   3909 O OG1 . THR B 1 105 ? -2.503  -6.361  5.656   1.00 14.46 ?  105 THR B OG1 1 
ATOM   3910 C CG2 . THR B 1 105 ? -2.832  -8.753  5.987   1.00 15.49 ?  105 THR B CG2 1 
ATOM   3911 N N   . SER B 1 106 ? -3.050  -6.217  2.317   1.00 14.13 ?  106 SER B N   1 
ATOM   3912 C CA  . SER B 1 106 ? -3.162  -4.974  1.567   1.00 16.27 ?  106 SER B CA  1 
ATOM   3913 C C   . SER B 1 106 ? -4.046  -3.980  2.309   1.00 16.10 ?  106 SER B C   1 
ATOM   3914 O O   . SER B 1 106 ? -4.856  -4.370  3.158   1.00 14.37 ?  106 SER B O   1 
ATOM   3915 C CB  . SER B 1 106 ? -3.734  -5.216  0.160   1.00 19.70 ?  106 SER B CB  1 
ATOM   3916 O OG  . SER B 1 106 ? -3.063  -6.283  -0.491  1.00 20.56 ?  106 SER B OG  1 
ATOM   3917 N N   . PRO B 1 107 ? -3.905  -2.681  2.027   1.00 18.36 ?  107 PRO B N   1 
ATOM   3918 C CA  . PRO B 1 107 ? -4.838  -1.703  2.601   1.00 14.91 ?  107 PRO B CA  1 
ATOM   3919 C C   . PRO B 1 107 ? -6.273  -2.111  2.311   1.00 15.20 ?  107 PRO B C   1 
ATOM   3920 O O   . PRO B 1 107 ? -6.603  -2.568  1.213   1.00 13.50 ?  107 PRO B O   1 
ATOM   3921 C CB  . PRO B 1 107 ? -4.465  -0.396  1.892   1.00 17.36 ?  107 PRO B CB  1 
ATOM   3922 C CG  . PRO B 1 107 ? -3.013  -0.583  1.532   1.00 17.16 ?  107 PRO B CG  1 
ATOM   3923 C CD  . PRO B 1 107 ? -2.879  -2.033  1.183   1.00 18.06 ?  107 PRO B CD  1 
ATOM   3924 N N   . GLY B 1 108 ? -7.118  -1.993  3.322   1.00 13.50 ?  108 GLY B N   1 
ATOM   3925 C CA  . GLY B 1 108 ? -8.500  -2.373  3.202   1.00 12.46 ?  108 GLY B CA  1 
ATOM   3926 C C   . GLY B 1 108 ? -8.800  -3.798  3.596   1.00 15.66 ?  108 GLY B C   1 
ATOM   3927 O O   . GLY B 1 108 ? -9.967  -4.117  3.849   1.00 15.43 ?  108 GLY B O   1 
ATOM   3928 N N   . ASP B 1 109 ? -7.792  -4.675  3.641   1.00 11.95 ?  109 ASP B N   1 
ATOM   3929 C CA  . ASP B 1 109 ? -8.037  -6.044  4.071   1.00 13.01 ?  109 ASP B CA  1 
ATOM   3930 C C   . ASP B 1 109 ? -8.464  -6.043  5.531   1.00 15.90 ?  109 ASP B C   1 
ATOM   3931 O O   . ASP B 1 109 ? -8.139  -5.126  6.303   1.00 13.04 ?  109 ASP B O   1 
ATOM   3932 C CB  . ASP B 1 109 ? -6.789  -6.922  3.919   1.00 13.10 ?  109 ASP B CB  1 
ATOM   3933 C CG  . ASP B 1 109 ? -6.492  -7.313  2.466   1.00 18.21 ?  109 ASP B CG  1 
ATOM   3934 O OD1 . ASP B 1 109 ? -7.404  -7.282  1.594   1.00 17.02 ?  109 ASP B OD1 1 
ATOM   3935 O OD2 . ASP B 1 109 ? -5.323  -7.695  2.208   1.00 17.79 -1 109 ASP B OD2 1 
ATOM   3936 N N   . GLN B 1 110 ? -9.214  -7.075  5.901   1.00 12.76 ?  110 GLN B N   1 
ATOM   3937 C CA  . GLN B 1 110 ? -9.639  -7.259  7.272   1.00 13.35 ?  110 GLN B CA  1 
ATOM   3938 C C   . GLN B 1 110 ? -8.676  -8.193  7.988   1.00 14.91 ?  110 GLN B C   1 
ATOM   3939 O O   . GLN B 1 110 ? -8.115  -9.122  7.393   1.00 12.97 ?  110 GLN B O   1 
ATOM   3940 C CB  . GLN B 1 110 ? -11.047 -7.831  7.312   1.00 14.82 ?  110 GLN B CB  1 
ATOM   3941 C CG  . GLN B 1 110 ? -12.055 -6.948  6.639   1.00 14.31 ?  110 GLN B CG  1 
ATOM   3942 C CD  . GLN B 1 110 ? -13.438 -7.484  6.824   1.00 19.10 ?  110 GLN B CD  1 
ATOM   3943 O OE1 . GLN B 1 110 ? -14.127 -7.121  7.780   1.00 17.16 ?  110 GLN B OE1 1 
ATOM   3944 N NE2 . GLN B 1 110 ? -13.855 -8.366  5.930   1.00 18.98 ?  110 GLN B NE2 1 
ATOM   3945 N N   . ILE B 1 111 ? -8.471  -7.927  9.270   1.00 12.96 ?  111 ILE B N   1 
ATOM   3946 C CA  . ILE B 1 111 ? -7.602  -8.738  10.105  1.00 14.17 ?  111 ILE B CA  1 
ATOM   3947 C C   . ILE B 1 111 ? -8.398  -9.155  11.331  1.00 12.38 ?  111 ILE B C   1 
ATOM   3948 O O   . ILE B 1 111 ? -9.013  -8.314  11.999  1.00 13.87 ?  111 ILE B O   1 
ATOM   3949 C CB  . ILE B 1 111 ? -6.309  -7.991  10.476  1.00 12.97 ?  111 ILE B CB  1 
ATOM   3950 C CG1 . ILE B 1 111 ? -5.561  -7.633  9.181   1.00 13.75 ?  111 ILE B CG1 1 
ATOM   3951 C CG2 . ILE B 1 111 ? -5.452  -8.838  11.385  1.00 14.70 ?  111 ILE B CG2 1 
ATOM   3952 C CD1 . ILE B 1 111 ? -4.327  -6.774  9.351   1.00 13.82 ?  111 ILE B CD1 1 
ATOM   3953 N N   . LEU B 1 112 ? -8.429  -10.456 11.591  1.00 11.69 ?  112 LEU B N   1 
ATOM   3954 C CA  . LEU B 1 112 ? -9.319  -11.008 12.599  1.00 13.02 ?  112 LEU B CA  1 
ATOM   3955 C C   . LEU B 1 112 ? -8.637  -11.060 13.958  1.00 11.93 ?  112 LEU B C   1 
ATOM   3956 O O   . LEU B 1 112 ? -7.483  -11.468 14.076  1.00 12.22 ?  112 LEU B O   1 
ATOM   3957 C CB  . LEU B 1 112 ? -9.777  -12.409 12.199  1.00 13.92 ?  112 LEU B CB  1 
ATOM   3958 C CG  . LEU B 1 112 ? -10.837 -13.044 13.103  1.00 14.78 ?  112 LEU B CG  1 
ATOM   3959 C CD1 . LEU B 1 112 ? -11.803 -13.850 12.257  1.00 16.96 ?  112 LEU B CD1 1 
ATOM   3960 C CD2 . LEU B 1 112 ? -10.230 -13.919 14.209  1.00 15.87 ?  112 LEU B CD2 1 
ATOM   3961 N N   . VAL B 1 113 ? -9.367  -10.629 14.983  1.00 14.54 ?  113 VAL B N   1 
ATOM   3962 C CA  . VAL B 1 113 ? -8.976  -10.807 16.373  1.00 12.81 ?  113 VAL B CA  1 
ATOM   3963 C C   . VAL B 1 113 ? -10.168 -11.423 17.095  1.00 13.59 ?  113 VAL B C   1 
ATOM   3964 O O   . VAL B 1 113 ? -11.251 -11.572 16.528  1.00 14.26 ?  113 VAL B O   1 
ATOM   3965 C CB  . VAL B 1 113 ? -8.550  -9.486  17.042  1.00 15.42 ?  113 VAL B CB  1 
ATOM   3966 C CG1 . VAL B 1 113 ? -7.375  -8.856  16.298  1.00 15.59 ?  113 VAL B CG1 1 
ATOM   3967 C CG2 . VAL B 1 113 ? -9.713  -8.539  17.094  1.00 14.69 ?  113 VAL B CG2 1 
ATOM   3968 N N   . GLN B 1 114 ? -9.960  -11.787 18.356  1.00 12.39 ?  114 GLN B N   1 
ATOM   3969 C CA  . GLN B 1 114 ? -11.006 -12.377 19.192  1.00 14.39 ?  114 GLN B CA  1 
ATOM   3970 C C   . GLN B 1 114 ? -11.221 -11.453 20.389  1.00 14.60 ?  114 GLN B C   1 
ATOM   3971 O O   . GLN B 1 114 ? -10.525 -11.570 21.401  1.00 13.41 ?  114 GLN B O   1 
ATOM   3972 C CB  . GLN B 1 114 ? -10.631 -13.797 19.634  1.00 15.73 ?  114 GLN B CB  1 
ATOM   3973 C CG  . GLN B 1 114 ? -10.306 -14.748 18.493  1.00 15.25 ?  114 GLN B CG  1 
ATOM   3974 C CD  . GLN B 1 114 ? -9.691  -16.032 18.992  1.00 18.46 ?  114 GLN B CD  1 
ATOM   3975 O OE1 . GLN B 1 114 ? -8.491  -16.097 19.283  1.00 19.08 ?  114 GLN B OE1 1 
ATOM   3976 N NE2 . GLN B 1 114 ? -10.506 -17.065 19.111  1.00 17.62 ?  114 GLN B NE2 1 
ATOM   3977 N N   . GLU B 1 115 ? -12.172 -10.525 20.266  1.00 13.96 ?  115 GLU B N   1 
ATOM   3978 C CA  . GLU B 1 115 ? -12.429 -9.557  21.327  1.00 15.78 ?  115 GLU B CA  1 
ATOM   3979 C C   . GLU B 1 115 ? -13.061 -10.230 22.546  1.00 14.47 ?  115 GLU B C   1 
ATOM   3980 O O   . GLU B 1 115 ? -13.852 -11.162 22.405  1.00 15.31 ?  115 GLU B O   1 
ATOM   3981 C CB  . GLU B 1 115 ? -13.363 -8.453  20.834  1.00 18.18 ?  115 GLU B CB  1 
ATOM   3982 C CG  . GLU B 1 115 ? -12.799 -7.616  19.713  1.00 18.15 ?  115 GLU B CG  1 
ATOM   3983 C CD  . GLU B 1 115 ? -13.764 -6.535  19.239  1.00 23.22 ?  115 GLU B CD  1 
ATOM   3984 O OE1 . GLU B 1 115 ? -13.534 -5.995  18.135  1.00 21.08 ?  115 GLU B OE1 1 
ATOM   3985 O OE2 . GLU B 1 115 ? -14.738 -6.233  19.962  1.00 19.35 -1 115 GLU B OE2 1 
ATOM   3986 N N   . PRO B 1 116 ? -12.756 -9.748  23.770  1.00 16.63 ?  116 PRO B N   1 
ATOM   3987 C CA  . PRO B 1 116 ? -11.849 -8.637  24.063  1.00 13.70 ?  116 PRO B CA  1 
ATOM   3988 C C   . PRO B 1 116 ? -10.402 -9.088  23.982  1.00 15.49 ?  116 PRO B C   1 
ATOM   3989 O O   . PRO B 1 116 ? -10.094 -10.218 24.329  1.00 13.73 ?  116 PRO B O   1 
ATOM   3990 C CB  . PRO B 1 116 ? -12.214 -8.258  25.493  1.00 14.85 ?  116 PRO B CB  1 
ATOM   3991 C CG  . PRO B 1 116 ? -12.622 -9.588  26.113  1.00 15.56 ?  116 PRO B CG  1 
ATOM   3992 C CD  . PRO B 1 116 ? -13.292 -10.360 24.999  1.00 16.01 ?  116 PRO B CD  1 
ATOM   3993 N N   . VAL B 1 117 ? -9.598  -8.220  23.427  1.00 15.01 ?  117 VAL B N   1 
ATOM   3994 C CA  . VAL B 1 117 ? -8.197  -8.598  23.196  1.00 15.11 ?  117 VAL B CA  1 
ATOM   3995 C C   . VAL B 1 117 ? -7.358  -7.374  23.422  1.00 12.81 ?  117 VAL B C   1 
ATOM   3996 O O   . VAL B 1 117 ? -7.836  -6.269  23.376  1.00 14.53 ?  117 VAL B O   1 
ATOM   3997 C CB  . VAL B 1 117 ? -7.926  -9.267  21.838  1.00 13.47 ?  117 VAL B CB  1 
ATOM   3998 C CG1 . VAL B 1 117 ? -7.910  -8.285  20.682  1.00 16.02 ?  117 VAL B CG1 1 
ATOM   3999 C CG2 . VAL B 1 117 ? -6.668  -10.116 21.854  1.00 13.73 ?  117 VAL B CG2 1 
ATOM   4000 N N   . TYR B 1 118 ? -6.065  -7.577  23.666  1.00 13.83 ?  118 TYR B N   1 
ATOM   4001 C CA  . TYR B 1 118 ? -5.051  -6.505  23.819  1.00 16.66 ?  118 TYR B CA  1 
ATOM   4002 C C   . TYR B 1 118 ? -5.302  -5.336  22.887  1.00 13.03 ?  118 TYR B C   1 
ATOM   4003 O O   . TYR B 1 118 ? -5.421  -5.483  21.679  1.00 13.21 ?  118 TYR B O   1 
ATOM   4004 C CB  . TYR B 1 118 ? -3.679  -7.101  23.523  1.00 15.87 ?  118 TYR B CB  1 
ATOM   4005 C CG  . TYR B 1 118 ? -2.499  -6.181  23.648  1.00 17.44 ?  118 TYR B CG  1 
ATOM   4006 C CD1 . TYR B 1 118 ? -2.365  -5.296  24.700  1.00 19.88 ?  118 TYR B CD1 1 
ATOM   4007 C CD2 . TYR B 1 118 ? -1.488  -6.243  22.714  1.00 19.64 ?  118 TYR B CD2 1 
ATOM   4008 C CE1 . TYR B 1 118 ? -1.259  -4.472  24.804  1.00 22.54 ?  118 TYR B CE1 1 
ATOM   4009 C CE2 . TYR B 1 118 ? -0.378  -5.434  22.803  1.00 21.88 ?  118 TYR B CE2 1 
ATOM   4010 C CZ  . TYR B 1 118 ? -0.258  -4.554  23.855  1.00 22.90 ?  118 TYR B CZ  1 
ATOM   4011 O OH  . TYR B 1 118 ? 0.854   -3.777  23.906  1.00 28.18 ?  118 TYR B OH  1 
ATOM   4012 N N   . ASN B 1 119 ? -5.334  -4.176  23.500  1.00 15.01 ?  119 ASN B N   1 
ATOM   4013 C CA  . ASN B 1 119 ? -5.698  -2.967  22.689  1.00 15.76 ?  119 ASN B CA  1 
ATOM   4014 C C   . ASN B 1 119 ? -4.769  -2.584  21.531  1.00 16.06 ?  119 ASN B C   1 
ATOM   4015 O O   . ASN B 1 119 ? -5.210  -1.984  20.585  1.00 15.53 ?  119 ASN B O   1 
ATOM   4016 C CB  . ASN B 1 119 ? -5.881  -1.755  23.606  1.00 19.25 ?  119 ASN B CB  1 
ATOM   4017 C CG  . ASN B 1 119 ? -4.729  -1.565  24.567  1.00 21.71 ?  119 ASN B CG  1 
ATOM   4018 O OD1 . ASN B 1 119 ? -4.491  -2.387  25.436  1.00 21.98 ?  119 ASN B OD1 1 
ATOM   4019 N ND2 . ASN B 1 119 ? -4.007  -0.474  24.416  1.00 23.64 ?  119 ASN B ND2 1 
ATOM   4020 N N   . MET B 1 120 ? -3.499  -2.904  21.651  1.00 16.57 ?  120 MET B N   1 
ATOM   4021 C CA  . MET B 1 120 ? -2.564  -2.453  20.601  1.00 17.66 ?  120 MET B CA  1 
ATOM   4022 C C   . MET B 1 120 ? -2.832  -3.198  19.299  1.00 17.28 ?  120 MET B C   1 
ATOM   4023 O O   . MET B 1 120 ? -2.406  -2.718  18.278  1.00 15.57 ?  120 MET B O   1 
ATOM   4024 C CB  . MET B 1 120 ? -1.102  -2.572  21.032  1.00 18.20 ?  120 MET B CB  1 
ATOM   4025 C CG  . MET B 1 120 ? -0.735  -1.545  22.068  1.00 21.07 ?  120 MET B CG  1 
ATOM   4026 S SD  . MET B 1 120 ? -0.752  0.083   21.313  1.00 30.47 ?  120 MET B SD  1 
ATOM   4027 C CE  . MET B 1 120 ? -2.070  0.881   22.220  1.00 29.12 ?  120 MET B CE  1 
ATOM   4028 N N   . PHE B 1 121 ? -3.496  -4.358  19.397  1.00 15.57 ?  121 PHE B N   1 
ATOM   4029 C CA  . PHE B 1 121 ? -3.871  -5.035  18.158  1.00 14.35 ?  121 PHE B CA  1 
ATOM   4030 C C   . PHE B 1 121 ? -4.724  -4.126  17.281  1.00 16.97 ?  121 PHE B C   1 
ATOM   4031 O O   . PHE B 1 121 ? -4.516  -4.049  16.063  1.00 16.69 ?  121 PHE B O   1 
ATOM   4032 C CB  . PHE B 1 121 ? -4.628  -6.323  18.463  1.00 15.85 ?  121 PHE B CB  1 
ATOM   4033 C CG  . PHE B 1 121 ? -3.769  -7.432  19.003  1.00 14.87 ?  121 PHE B CG  1 
ATOM   4034 C CD1 . PHE B 1 121 ? -2.419  -7.254  19.223  1.00 17.14 ?  121 PHE B CD1 1 
ATOM   4035 C CD2 . PHE B 1 121 ? -4.336  -8.672  19.276  1.00 19.41 ?  121 PHE B CD2 1 
ATOM   4036 C CE1 . PHE B 1 121 ? -1.648  -8.280  19.733  1.00 20.07 ?  121 PHE B CE1 1 
ATOM   4037 C CE2 . PHE B 1 121 ? -3.572  -9.704  19.778  1.00 18.66 ?  121 PHE B CE2 1 
ATOM   4038 C CZ  . PHE B 1 121 ? -2.227  -9.505  20.009  1.00 17.86 ?  121 PHE B CZ  1 
ATOM   4039 N N   . TYR B 1 122 ? -5.688  -3.421  17.891  1.00 16.14 ?  122 TYR B N   1 
ATOM   4040 C CA  . TYR B 1 122 ? -6.560  -2.531  17.131  1.00 15.61 ?  122 TYR B CA  1 
ATOM   4041 C C   . TYR B 1 122 ? -5.784  -1.354  16.561  1.00 16.24 ?  122 TYR B C   1 
ATOM   4042 O O   . TYR B 1 122 ? -6.012  -0.957  15.415  1.00 16.03 ?  122 TYR B O   1 
ATOM   4043 C CB  . TYR B 1 122 ? -7.696  -2.008  18.009  1.00 16.47 ?  122 TYR B CB  1 
ATOM   4044 C CG  . TYR B 1 122 ? -8.430  -3.059  18.793  1.00 14.95 ?  122 TYR B CG  1 
ATOM   4045 C CD1 . TYR B 1 122 ? -9.063  -4.117  18.153  1.00 16.67 ?  122 TYR B CD1 1 
ATOM   4046 C CD2 . TYR B 1 122 ? -8.513  -2.975  20.176  1.00 15.82 ?  122 TYR B CD2 1 
ATOM   4047 C CE1 . TYR B 1 122 ? -9.754  -5.084  18.870  1.00 16.21 ?  122 TYR B CE1 1 
ATOM   4048 C CE2 . TYR B 1 122 ? -9.188  -3.932  20.907  1.00 15.98 ?  122 TYR B CE2 1 
ATOM   4049 C CZ  . TYR B 1 122 ? -9.804  -4.982  20.252  1.00 17.95 ?  122 TYR B CZ  1 
ATOM   4050 O OH  . TYR B 1 122 ? -10.480 -5.923  20.988  1.00 16.30 ?  122 TYR B OH  1 
ATOM   4051 N N   . SER B 1 123 ? -4.870  -0.781  17.354  1.00 16.75 ?  123 SER B N   1 
ATOM   4052 C CA  . SER B 1 123 ? -4.054  0.338   16.888  1.00 18.36 ?  123 SER B CA  1 
ATOM   4053 C C   . SER B 1 123 ? -3.285  -0.025  15.621  1.00 17.30 ?  123 SER B C   1 
ATOM   4054 O O   . SER B 1 123 ? -3.291  0.730   14.642  1.00 18.38 ?  123 SER B O   1 
ATOM   4055 C CB  . SER B 1 123 ? -3.072  0.772   17.983  1.00 18.84 ?  123 SER B CB  1 
ATOM   4056 O OG  . SER B 1 123 ? -3.753  1.033   19.195  1.00 24.85 ?  123 SER B OG  1 
ATOM   4057 N N   . VAL B 1 124 ? -2.614  -1.180  15.620  1.00 17.01 ?  124 VAL B N   1 
ATOM   4058 C CA  . VAL B 1 124 ? -1.741  -1.477  14.489  1.00 17.18 ?  124 VAL B CA  1 
ATOM   4059 C C   . VAL B 1 124 ? -2.543  -1.922  13.282  1.00 18.87 ?  124 VAL B C   1 
ATOM   4060 O O   . VAL B 1 124 ? -2.115  -1.697  12.149  1.00 21.11 ?  124 VAL B O   1 
ATOM   4061 C CB  . VAL B 1 124 ? -0.661  -2.513  14.842  1.00 19.87 ?  124 VAL B CB  1 
ATOM   4062 C CG1 . VAL B 1 124 ? 0.183   -2.009  15.978  1.00 18.93 ?  124 VAL B CG1 1 
ATOM   4063 C CG2 . VAL B 1 124 ? -1.284  -3.855  15.195  1.00 20.91 ?  124 VAL B CG2 1 
ATOM   4064 N N   . ILE B 1 125 ? -3.706  -2.545  13.481  1.00 13.84 ?  125 ILE B N   1 
ATOM   4065 C CA  . ILE B 1 125 ? -4.541  -2.897  12.341  1.00 16.38 ?  125 ILE B CA  1 
ATOM   4066 C C   . ILE B 1 125 ? -5.129  -1.636  11.717  1.00 14.27 ?  125 ILE B C   1 
ATOM   4067 O O   . ILE B 1 125 ? -4.902  -1.340  10.539  1.00 13.48 ?  125 ILE B O   1 
ATOM   4068 C CB  . ILE B 1 125 ? -5.637  -3.892  12.759  1.00 14.26 ?  125 ILE B CB  1 
ATOM   4069 C CG1 . ILE B 1 125 ? -5.014  -5.230  13.164  1.00 15.41 ?  125 ILE B CG1 1 
ATOM   4070 C CG2 . ILE B 1 125 ? -6.627  -4.109  11.612  1.00 14.48 ?  125 ILE B CG2 1 
ATOM   4071 C CD1 . ILE B 1 125 ? -5.972  -6.133  13.942  1.00 14.29 ?  125 ILE B CD1 1 
ATOM   4072 N N   . GLU B 1 126 ? -5.862  -0.856  12.517  1.00 13.80 ?  126 GLU B N   1 
ATOM   4073 C CA  . GLU B 1 126 ? -6.579  0.305   12.000  1.00 15.71 ?  126 GLU B CA  1 
ATOM   4074 C C   . GLU B 1 126 ? -5.630  1.429   11.603  1.00 13.85 ?  126 GLU B C   1 
ATOM   4075 O O   . GLU B 1 126 ? -5.844  2.089   10.580  1.00 13.93 ?  126 GLU B O   1 
ATOM   4076 C CB  . GLU B 1 126 ? -7.603  0.791   13.033  1.00 17.44 ?  126 GLU B CB  1 
ATOM   4077 C CG  . GLU B 1 126 ? -8.580  -0.294  13.434  1.00 17.74 ?  126 GLU B CG  1 
ATOM   4078 C CD  . GLU B 1 126 ? -9.579  0.133   14.499  1.00 21.84 ?  126 GLU B CD  1 
ATOM   4079 O OE1 . GLU B 1 126 ? -10.732 -0.372  14.449  1.00 21.01 ?  126 GLU B OE1 1 
ATOM   4080 O OE2 . GLU B 1 126 ? -9.217  0.961   15.379  1.00 21.54 -1 126 GLU B OE2 1 
ATOM   4081 N N   . GLY B 1 127 ? -4.564  1.646   12.375  1.00 14.61 ?  127 GLY B N   1 
ATOM   4082 C CA  . GLY B 1 127 ? -3.608  2.681   12.015  1.00 18.73 ?  127 GLY B CA  1 
ATOM   4083 C C   . GLY B 1 127 ? -2.909  2.415   10.696  1.00 17.96 ?  127 GLY B C   1 
ATOM   4084 O O   . GLY B 1 127 ? -2.539  3.354   9.980   1.00 17.51 ?  127 GLY B O   1 
ATOM   4085 N N   . ASN B 1 128 ? -2.732  1.141   10.345  1.00 14.49 ?  128 ASN B N   1 
ATOM   4086 C CA  . ASN B 1 128 ? -2.121  0.772   9.077   1.00 15.93 ?  128 ASN B CA  1 
ATOM   4087 C C   . ASN B 1 128 ? -3.106  0.752   7.925   1.00 13.73 ?  128 ASN B C   1 
ATOM   4088 O O   . ASN B 1 128 ? -2.737  0.346   6.817   1.00 12.75 ?  128 ASN B O   1 
ATOM   4089 C CB  . ASN B 1 128 ? -1.452  -0.600  9.203   1.00 15.48 ?  128 ASN B CB  1 
ATOM   4090 C CG  . ASN B 1 128 ? -0.048  -0.504  9.767   1.00 19.33 ?  128 ASN B CG  1 
ATOM   4091 O OD1 . ASN B 1 128 ? 0.783   0.236   9.242   1.00 16.68 ?  128 ASN B OD1 1 
ATOM   4092 N ND2 . ASN B 1 128 ? 0.213   -1.219  10.863  1.00 16.45 ?  128 ASN B ND2 1 
ATOM   4093 N N   . GLY B 1 129 ? -4.348  1.165   8.143   1.00 12.10 ?  129 GLY B N   1 
ATOM   4094 C CA  . GLY B 1 129 ? -5.325  1.122   7.073   1.00 14.20 ?  129 GLY B CA  1 
ATOM   4095 C C   . GLY B 1 129 ? -5.845  -0.264  6.757   1.00 13.55 ?  129 GLY B C   1 
ATOM   4096 O O   . GLY B 1 129 ? -6.257  -0.522  5.621   1.00 12.95 ?  129 GLY B O   1 
ATOM   4097 N N   . ARG B 1 130 ? -5.824  -1.167  7.725   1.00 11.89 ?  130 ARG B N   1 
ATOM   4098 C CA  . ARG B 1 130 ? -6.551  -2.419  7.622   1.00 14.36 ?  130 ARG B CA  1 
ATOM   4099 C C   . ARG B 1 130 ? -7.755  -2.329  8.555   1.00 14.70 ?  130 ARG B C   1 
ATOM   4100 O O   . ARG B 1 130 ? -7.891  -1.378  9.330   1.00 15.01 ?  130 ARG B O   1 
ATOM   4101 C CB  . ARG B 1 130 ? -5.641  -3.611  7.935   1.00 12.55 ?  130 ARG B CB  1 
ATOM   4102 C CG  . ARG B 1 130 ? -4.697  -4.038  6.765   1.00 14.53 ?  130 ARG B CG  1 
ATOM   4103 C CD  . ARG B 1 130 ? -3.670  -2.962  6.343   1.00 12.96 ?  130 ARG B CD  1 
ATOM   4104 N NE  . ARG B 1 130 ? -2.667  -3.476  5.394   1.00 14.39 ?  130 ARG B NE  1 
ATOM   4105 C CZ  . ARG B 1 130 ? -1.733  -2.739  4.777   1.00 14.75 ?  130 ARG B CZ  1 
ATOM   4106 N NH1 . ARG B 1 130 ? -1.632  -1.429  4.989   1.00 14.61 1  130 ARG B NH1 1 
ATOM   4107 N NH2 . ARG B 1 130 ? -0.888  -3.312  3.936   1.00 16.44 ?  130 ARG B NH2 1 
ATOM   4108 N N   . ARG B 1 131 ? -8.662  -3.296  8.449   1.00 13.51 ?  131 ARG B N   1 
ATOM   4109 C CA  . ARG B 1 131 ? -9.930  -3.231  9.154   1.00 13.10 ?  131 ARG B CA  1 
ATOM   4110 C C   . ARG B 1 131 ? -9.994  -4.369  10.158  1.00 15.25 ?  131 ARG B C   1 
ATOM   4111 O O   . ARG B 1 131 ? -9.718  -5.525  9.814   1.00 14.00 ?  131 ARG B O   1 
ATOM   4112 C CB  . ARG B 1 131 ? -11.106 -3.285  8.171   1.00 14.34 ?  131 ARG B CB  1 
ATOM   4113 C CG  . ARG B 1 131 ? -11.225 -2.004  7.337   1.00 17.05 ?  131 ARG B CG  1 
ATOM   4114 C CD  . ARG B 1 131 ? -12.351 -2.079  6.313   1.00 17.18 ?  131 ARG B CD  1 
ATOM   4115 N NE  . ARG B 1 131 ? -12.095 -3.112  5.314   1.00 20.56 ?  131 ARG B NE  1 
ATOM   4116 C CZ  . ARG B 1 131 ? -13.018 -3.590  4.487   1.00 21.89 ?  131 ARG B CZ  1 
ATOM   4117 N NH1 . ARG B 1 131 ? -14.259 -3.118  4.543   1.00 23.01 1  131 ARG B NH1 1 
ATOM   4118 N NH2 . ARG B 1 131 ? -12.707 -4.533  3.603   1.00 22.91 ?  131 ARG B NH2 1 
ATOM   4119 N N   . VAL B 1 132 ? -10.324 -4.034  11.403  1.00 13.57 ?  132 VAL B N   1 
ATOM   4120 C CA  . VAL B 1 132 ? -10.503 -5.057  12.424  1.00 13.02 ?  132 VAL B CA  1 
ATOM   4121 C C   . VAL B 1 132 ? -11.810 -5.796  12.172  1.00 14.49 ?  132 VAL B C   1 
ATOM   4122 O O   . VAL B 1 132 ? -12.859 -5.181  11.955  1.00 13.25 ?  132 VAL B O   1 
ATOM   4123 C CB  . VAL B 1 132 ? -10.504 -4.434  13.825  1.00 16.47 ?  132 VAL B CB  1 
ATOM   4124 C CG1 . VAL B 1 132 ? -10.783 -5.526  14.865  1.00 16.77 ?  132 VAL B CG1 1 
ATOM   4125 C CG2 . VAL B 1 132 ? -9.190  -3.726  14.104  1.00 15.58 ?  132 VAL B CG2 1 
ATOM   4126 N N   . ILE B 1 133 ? -11.751 -7.123  12.187  1.00 13.63 ?  133 ILE B N   1 
ATOM   4127 C CA  . ILE B 1 133 ? -12.946 -7.946  12.307  1.00 13.75 ?  133 ILE B CA  1 
ATOM   4128 C C   . ILE B 1 133 ? -12.748 -8.845  13.518  1.00 15.37 ?  133 ILE B C   1 
ATOM   4129 O O   . ILE B 1 133 ? -11.625 -9.263  13.814  1.00 14.62 ?  133 ILE B O   1 
ATOM   4130 C CB  . ILE B 1 133 ? -13.237 -8.758  11.027  1.00 13.15 ?  133 ILE B CB  1 
ATOM   4131 C CG1 . ILE B 1 133 ? -14.568 -9.497  11.156  1.00 15.24 ?  133 ILE B CG1 1 
ATOM   4132 C CG2 . ILE B 1 133 ? -12.138 -9.739  10.737  1.00 14.34 ?  133 ILE B CG2 1 
ATOM   4133 C CD1 . ILE B 1 133 ? -15.018 -10.084 9.834   1.00 16.73 ?  133 ILE B CD1 1 
ATOM   4134 N N   . SER B 1 134 ? -13.821 -9.084  14.258  1.00 13.93 ?  134 SER B N   1 
ATOM   4135 C CA  . SER B 1 134 ? -13.741 -9.893  15.461  1.00 14.14 ?  134 SER B CA  1 
ATOM   4136 C C   . SER B 1 134 ? -14.700 -11.061 15.376  1.00 14.95 ?  134 SER B C   1 
ATOM   4137 O O   . SER B 1 134 ? -15.846 -10.910 14.937  1.00 15.77 ?  134 SER B O   1 
ATOM   4138 C CB  . SER B 1 134 ? -14.067 -9.078  16.713  1.00 19.60 ?  134 SER B CB  1 
ATOM   4139 O OG  . SER B 1 134 ? -14.154 -9.929  17.851  1.00 16.71 ?  134 SER B OG  1 
ATOM   4140 N N   . SER B 1 135 ? -14.226 -12.224 15.792  1.00 16.22 ?  135 SER B N   1 
ATOM   4141 C CA  . SER B 1 135 ? -15.116 -13.292 16.229  1.00 15.89 ?  135 SER B CA  1 
ATOM   4142 C C   . SER B 1 135 ? -15.101 -13.165 17.747  1.00 16.42 ?  135 SER B C   1 
ATOM   4143 O O   . SER B 1 135 ? -14.168 -13.632 18.405  1.00 14.70 ?  135 SER B O   1 
ATOM   4144 C CB  . SER B 1 135 ? -14.648 -14.661 15.745  1.00 16.79 ?  135 SER B CB  1 
ATOM   4145 O OG  . SER B 1 135 ? -15.565 -15.663 16.161  1.00 16.86 ?  135 SER B OG  1 
ATOM   4146 N N   . ASP B 1 136 ? -16.098 -12.464 18.294  1.00 16.62 ?  136 ASP B N   1 
ATOM   4147 C CA  . ASP B 1 136 ? -16.099 -12.168 19.718  1.00 16.59 ?  136 ASP B CA  1 
ATOM   4148 C C   . ASP B 1 136 ? -16.065 -13.466 20.508  1.00 15.18 ?  136 ASP B C   1 
ATOM   4149 O O   . ASP B 1 136 ? -16.688 -14.459 20.122  1.00 15.77 ?  136 ASP B O   1 
ATOM   4150 C CB  . ASP B 1 136 ? -17.345 -11.373 20.113  1.00 17.38 ?  136 ASP B CB  1 
ATOM   4151 C CG  . ASP B 1 136 ? -17.320 -9.927  19.638  1.00 23.83 ?  136 ASP B CG  1 
ATOM   4152 O OD1 . ASP B 1 136 ? -16.388 -9.505  18.911  1.00 20.38 ?  136 ASP B OD1 1 
ATOM   4153 O OD2 . ASP B 1 136 ? -18.266 -9.199  19.998  1.00 25.34 -1 136 ASP B OD2 1 
ATOM   4154 N N   . LEU B 1 137 ? -15.316 -13.464 21.602  1.00 13.36 ?  137 LEU B N   1 
ATOM   4155 C CA  . LEU B 1 137 ? -15.423 -14.560 22.549  1.00 15.69 ?  137 LEU B CA  1 
ATOM   4156 C C   . LEU B 1 137 ? -16.789 -14.508 23.221  1.00 17.28 ?  137 LEU B C   1 
ATOM   4157 O O   . LEU B 1 137 ? -17.272 -13.438 23.598  1.00 19.10 ?  137 LEU B O   1 
ATOM   4158 C CB  . LEU B 1 137 ? -14.315 -14.485 23.590  1.00 16.02 ?  137 LEU B CB  1 
ATOM   4159 C CG  . LEU B 1 137 ? -12.888 -14.565 23.026  1.00 15.02 ?  137 LEU B CG  1 
ATOM   4160 C CD1 . LEU B 1 137 ? -11.883 -14.349 24.146  1.00 16.64 ?  137 LEU B CD1 1 
ATOM   4161 C CD2 . LEU B 1 137 ? -12.628 -15.884 22.302  1.00 15.17 ?  137 LEU B CD2 1 
ATOM   4162 N N   . ILE B 1 138 ? -17.417 -15.665 23.349  1.00 18.69 ?  138 ILE B N   1 
ATOM   4163 C CA  . ILE B 1 138 ? -18.721 -15.758 23.992  1.00 22.07 ?  138 ILE B CA  1 
ATOM   4164 C C   . ILE B 1 138 ? -18.512 -15.784 25.499  1.00 17.57 ?  138 ILE B C   1 
ATOM   4165 O O   . ILE B 1 138 ? -17.724 -16.587 26.007  1.00 19.41 ?  138 ILE B O   1 
ATOM   4166 C CB  . ILE B 1 138 ? -19.470 -17.014 23.516  1.00 21.39 ?  138 ILE B CB  1 
ATOM   4167 C CG1 . ILE B 1 138 ? -19.854 -16.888 22.037  1.00 21.11 ?  138 ILE B CG1 1 
ATOM   4168 C CG2 . ILE B 1 138 ? -20.705 -17.251 24.356  1.00 26.84 ?  138 ILE B CG2 1 
ATOM   4169 C CD1 . ILE B 1 138 ? -20.525 -18.120 21.476  1.00 26.95 ?  138 ILE B CD1 1 
ATOM   4170 N N   . TYR B 1 139 ? -19.215 -14.912 26.217  1.00 19.28 ?  139 TYR B N   1 
ATOM   4171 C CA  . TYR B 1 139 ? -19.128 -14.845 27.677  1.00 21.61 ?  139 TYR B CA  1 
ATOM   4172 C C   . TYR B 1 139 ? -20.443 -15.331 28.280  1.00 22.85 ?  139 TYR B C   1 
ATOM   4173 O O   . TYR B 1 139 ? -21.481 -14.687 28.111  1.00 22.10 ?  139 TYR B O   1 
ATOM   4174 C CB  . TYR B 1 139 ? -18.822 -13.425 28.141  1.00 20.32 ?  139 TYR B CB  1 
ATOM   4175 C CG  . TYR B 1 139 ? -18.525 -13.303 29.621  1.00 19.67 ?  139 TYR B CG  1 
ATOM   4176 C CD1 . TYR B 1 139 ? -17.417 -13.921 30.180  1.00 19.15 ?  139 TYR B CD1 1 
ATOM   4177 C CD2 . TYR B 1 139 ? -19.348 -12.555 30.458  1.00 19.92 ?  139 TYR B CD2 1 
ATOM   4178 C CE1 . TYR B 1 139 ? -17.138 -13.797 31.540  1.00 18.55 ?  139 TYR B CE1 1 
ATOM   4179 C CE2 . TYR B 1 139 ? -19.075 -12.429 31.808  1.00 19.42 ?  139 TYR B CE2 1 
ATOM   4180 C CZ  . TYR B 1 139 ? -17.969 -13.056 32.341  1.00 20.29 ?  139 TYR B CZ  1 
ATOM   4181 O OH  . TYR B 1 139 ? -17.667 -12.940 33.685  1.00 18.42 ?  139 TYR B OH  1 
ATOM   4182 N N   . GLU B 1 140 ? -20.393 -16.471 28.970  1.00 22.67 ?  140 GLU B N   1 
ATOM   4183 C CA  . GLU B 1 140 ? -21.521 -17.016 29.713  1.00 27.80 ?  140 GLU B CA  1 
ATOM   4184 C C   . GLU B 1 140 ? -20.986 -17.663 30.978  1.00 25.93 ?  140 GLU B C   1 
ATOM   4185 O O   . GLU B 1 140 ? -19.942 -18.320 30.949  1.00 25.08 ?  140 GLU B O   1 
ATOM   4186 C CB  . GLU B 1 140 ? -22.318 -18.063 28.911  1.00 32.19 ?  140 GLU B CB  1 
ATOM   4187 C CG  . GLU B 1 140 ? -22.526 -17.745 27.438  1.00 37.49 ?  140 GLU B CG  1 
ATOM   4188 C CD  . GLU B 1 140 ? -22.768 -18.989 26.587  1.00 44.38 ?  140 GLU B CD  1 
ATOM   4189 O OE1 . GLU B 1 140 ? -23.946 -19.267 26.267  1.00 51.85 ?  140 GLU B OE1 1 
ATOM   4190 O OE2 . GLU B 1 140 ? -21.782 -19.679 26.229  1.00 41.89 -1 140 GLU B OE2 1 
ATOM   4191 N N   . ASN B 1 141 ? -21.703 -17.471 32.083  1.00 29.63 ?  141 ASN B N   1 
ATOM   4192 C CA  . ASN B 1 141 ? -21.372 -18.116 33.351  1.00 28.73 ?  141 ASN B CA  1 
ATOM   4193 C C   . ASN B 1 141 ? -19.912 -17.896 33.736  1.00 25.78 ?  141 ASN B C   1 
ATOM   4194 O O   . ASN B 1 141 ? -19.197 -18.830 34.099  1.00 26.60 ?  141 ASN B O   1 
ATOM   4195 C CB  . ASN B 1 141 ? -21.694 -19.605 33.293  1.00 31.19 ?  141 ASN B CB  1 
ATOM   4196 C CG  . ASN B 1 141 ? -23.038 -19.912 33.869  1.00 38.08 ?  141 ASN B CG  1 
ATOM   4197 O OD1 . ASN B 1 141 ? -23.271 -19.714 35.065  1.00 44.33 ?  141 ASN B OD1 1 
ATOM   4198 N ND2 . ASN B 1 141 ? -23.949 -20.383 33.025  1.00 39.18 ?  141 ASN B ND2 1 
ATOM   4199 N N   . SER B 1 142 ? -19.462 -16.647 33.617  1.00 24.90 ?  142 SER B N   1 
ATOM   4200 C CA  . SER B 1 142 ? -18.137 -16.220 34.066  1.00 24.49 ?  142 SER B CA  1 
ATOM   4201 C C   . SER B 1 142 ? -17.004 -16.860 33.275  1.00 22.68 ?  142 SER B C   1 
ATOM   4202 O O   . SER B 1 142 ? -15.849 -16.841 33.719  1.00 24.49 ?  142 SER B O   1 
ATOM   4203 C CB  . SER B 1 142 ? -17.943 -16.494 35.561  1.00 26.56 ?  142 SER B CB  1 
ATOM   4204 O OG  . SER B 1 142 ? -18.946 -15.834 36.305  1.00 31.19 ?  142 SER B OG  1 
ATOM   4205 N N   . LYS B 1 143 ? -17.293 -17.415 32.100  1.00 23.25 ?  143 LYS B N   1 
ATOM   4206 C CA  . LYS B 1 143 ? -16.276 -18.061 31.283  1.00 22.08 ?  143 LYS B CA  1 
ATOM   4207 C C   . LYS B 1 143 ? -16.412 -17.600 29.839  1.00 20.71 ?  143 LYS B C   1 
ATOM   4208 O O   . LYS B 1 143 ? -17.526 -17.411 29.337  1.00 20.33 ?  143 LYS B O   1 
ATOM   4209 C CB  . LYS B 1 143 ? -16.380 -19.602 31.331  1.00 27.16 ?  143 LYS B CB  1 
ATOM   4210 C CG  . LYS B 1 143 ? -16.549 -20.182 32.724  1.00 28.17 ?  143 LYS B CG  1 
ATOM   4211 C CD  . LYS B 1 143 ? -15.530 -21.270 33.025  1.00 34.51 ?  143 LYS B CD  1 
ATOM   4212 C CE  . LYS B 1 143 ? -16.005 -22.190 34.159  1.00 38.15 ?  143 LYS B CE  1 
ATOM   4213 N NZ  . LYS B 1 143 ? -16.688 -23.426 33.647  1.00 37.40 1  143 LYS B NZ  1 
ATOM   4214 N N   . TYR B 1 144 ? -15.276 -17.446 29.174  1.00 22.81 ?  144 TYR B N   1 
ATOM   4215 C CA  . TYR B 1 144 ? -15.254 -17.140 27.751  1.00 18.48 ?  144 TYR B CA  1 
ATOM   4216 C C   . TYR B 1 144 ? -15.102 -18.424 26.944  1.00 22.03 ?  144 TYR B C   1 
ATOM   4217 O O   . TYR B 1 144 ? -14.469 -19.383 27.388  1.00 22.99 ?  144 TYR B O   1 
ATOM   4218 C CB  . TYR B 1 144 ? -14.100 -16.196 27.423  1.00 19.35 ?  144 TYR B CB  1 
ATOM   4219 C CG  . TYR B 1 144 ? -14.282 -14.762 27.862  1.00 17.10 ?  144 TYR B CG  1 
ATOM   4220 C CD1 . TYR B 1 144 ? -14.968 -13.845 27.061  1.00 15.89 ?  144 TYR B CD1 1 
ATOM   4221 C CD2 . TYR B 1 144 ? -13.732 -14.314 29.057  1.00 16.67 ?  144 TYR B CD2 1 
ATOM   4222 C CE1 . TYR B 1 144 ? -15.119 -12.521 27.454  1.00 14.76 ?  144 TYR B CE1 1 
ATOM   4223 C CE2 . TYR B 1 144 ? -13.873 -12.992 29.461  1.00 15.18 ?  144 TYR B CE2 1 
ATOM   4224 C CZ  . TYR B 1 144 ? -14.568 -12.106 28.658  1.00 15.67 ?  144 TYR B CZ  1 
ATOM   4225 O OH  . TYR B 1 144 ? -14.676 -10.807 29.068  1.00 13.05 ?  144 TYR B OH  1 
ATOM   4226 N N   . SER B 1 145 ? -15.670 -18.428 25.739  1.00 21.89 ?  145 SER B N   1 
ATOM   4227 C CA  . SER B 1 145 ? -15.499 -19.553 24.834  1.00 18.55 ?  145 SER B CA  1 
ATOM   4228 C C   . SER B 1 145 ? -15.551 -19.047 23.401  1.00 19.50 ?  145 SER B C   1 
ATOM   4229 O O   . SER B 1 145 ? -16.012 -17.940 23.130  1.00 19.12 ?  145 SER B O   1 
ATOM   4230 C CB  . SER B 1 145 ? -16.569 -20.626 25.047  1.00 21.94 ?  145 SER B CB  1 
ATOM   4231 O OG  . SER B 1 145 ? -17.865 -20.094 24.847  1.00 21.98 ?  145 SER B OG  1 
ATOM   4232 N N   . VAL B 1 146 ? -15.087 -19.882 22.495  1.00 19.07 ?  146 VAL B N   1 
ATOM   4233 C CA  . VAL B 1 146 ? -15.007 -19.556 21.077  1.00 18.95 ?  146 VAL B CA  1 
ATOM   4234 C C   . VAL B 1 146 ? -16.265 -20.036 20.367  1.00 21.39 ?  146 VAL B C   1 
ATOM   4235 O O   . VAL B 1 146 ? -16.732 -21.163 20.584  1.00 19.72 ?  146 VAL B O   1 
ATOM   4236 C CB  . VAL B 1 146 ? -13.748 -20.183 20.455  1.00 19.42 ?  146 VAL B CB  1 
ATOM   4237 C CG1 . VAL B 1 146 ? -13.749 -20.003 18.946  1.00 19.10 ?  146 VAL B CG1 1 
ATOM   4238 C CG2 . VAL B 1 146 ? -12.496 -19.581 21.076  1.00 21.12 ?  146 VAL B CG2 1 
ATOM   4239 N N   . ASN B 1 147 ? -16.813 -19.181 19.499  1.00 18.12 ?  147 ASN B N   1 
ATOM   4240 C CA  . ASN B 1 147 ? -17.872 -19.572 18.573  1.00 19.03 ?  147 ASN B CA  1 
ATOM   4241 C C   . ASN B 1 147 ? -17.160 -20.054 17.314  1.00 17.51 ?  147 ASN B C   1 
ATOM   4242 O O   . ASN B 1 147 ? -16.834 -19.272 16.419  1.00 16.54 ?  147 ASN B O   1 
ATOM   4243 C CB  . ASN B 1 147 ? -18.815 -18.406 18.302  1.00 18.12 ?  147 ASN B CB  1 
ATOM   4244 C CG  . ASN B 1 147 ? -19.964 -18.780 17.370  1.00 20.21 ?  147 ASN B CG  1 
ATOM   4245 O OD1 . ASN B 1 147 ? -19.904 -19.780 16.655  1.00 20.62 ?  147 ASN B OD1 1 
ATOM   4246 N ND2 . ASN B 1 147 ? -21.014 -17.969 17.373  1.00 23.41 ?  147 ASN B ND2 1 
ATOM   4247 N N   . TRP B 1 148 ? -16.893 -21.361 17.253  1.00 17.63 ?  148 TRP B N   1 
ATOM   4248 C CA  . TRP B 1 148 ? -16.009 -21.874 16.210  1.00 17.72 ?  148 TRP B CA  1 
ATOM   4249 C C   . TRP B 1 148 ? -16.601 -21.707 14.819  1.00 17.04 ?  148 TRP B C   1 
ATOM   4250 O O   . TRP B 1 148 ? -15.854 -21.472 13.860  1.00 15.69 ?  148 TRP B O   1 
ATOM   4251 C CB  . TRP B 1 148 ? -15.672 -23.341 16.470  1.00 18.69 ?  148 TRP B CB  1 
ATOM   4252 C CG  . TRP B 1 148 ? -14.792 -23.509 17.639  1.00 19.70 ?  148 TRP B CG  1 
ATOM   4253 C CD1 . TRP B 1 148 ? -15.168 -23.850 18.907  1.00 20.81 ?  148 TRP B CD1 1 
ATOM   4254 C CD2 . TRP B 1 148 ? -13.374 -23.310 17.678  1.00 19.17 ?  148 TRP B CD2 1 
ATOM   4255 N NE1 . TRP B 1 148 ? -14.064 -23.894 19.729  1.00 24.58 ?  148 TRP B NE1 1 
ATOM   4256 C CE2 . TRP B 1 148 ? -12.954 -23.560 18.997  1.00 22.07 ?  148 TRP B CE2 1 
ATOM   4257 C CE3 . TRP B 1 148 ? -12.421 -22.950 16.723  1.00 18.53 ?  148 TRP B CE3 1 
ATOM   4258 C CZ2 . TRP B 1 148 ? -11.622 -23.462 19.385  1.00 21.68 ?  148 TRP B CZ2 1 
ATOM   4259 C CZ3 . TRP B 1 148 ? -11.104 -22.856 17.107  1.00 20.07 ?  148 TRP B CZ3 1 
ATOM   4260 C CH2 . TRP B 1 148 ? -10.715 -23.107 18.430  1.00 21.55 ?  148 TRP B CH2 1 
ATOM   4261 N N   . ALA B 1 149 ? -17.924 -21.834 14.683  1.00 14.87 ?  149 ALA B N   1 
ATOM   4262 C CA  . ALA B 1 149 ? -18.545 -21.663 13.372  1.00 17.08 ?  149 ALA B CA  1 
ATOM   4263 C C   . ALA B 1 149 ? -18.409 -20.226 12.889  1.00 17.41 ?  149 ALA B C   1 
ATOM   4264 O O   . ALA B 1 149 ? -18.118 -19.984 11.712  1.00 15.04 ?  149 ALA B O   1 
ATOM   4265 C CB  . ALA B 1 149 ? -20.014 -22.067 13.427  1.00 19.45 ?  149 ALA B CB  1 
ATOM   4266 N N   . ASP B 1 150 ? -18.619 -19.265 13.792  1.00 17.44 ?  150 ASP B N   1 
ATOM   4267 C CA  . ASP B 1 150 ? -18.462 -17.859 13.448  1.00 17.50 ?  150 ASP B CA  1 
ATOM   4268 C C   . ASP B 1 150 ? -17.015 -17.549 13.103  1.00 15.60 ?  150 ASP B C   1 
ATOM   4269 O O   . ASP B 1 150 ? -16.731 -16.874 12.104  1.00 15.69 ?  150 ASP B O   1 
ATOM   4270 C CB  . ASP B 1 150 ? -18.939 -16.987 14.611  1.00 20.49 ?  150 ASP B CB  1 
ATOM   4271 C CG  . ASP B 1 150 ? -18.797 -15.492 14.327  1.00 21.43 ?  150 ASP B CG  1 
ATOM   4272 O OD1 . ASP B 1 150 ? -19.610 -14.959 13.550  1.00 20.30 ?  150 ASP B OD1 1 
ATOM   4273 O OD2 . ASP B 1 150 ? -17.881 -14.847 14.885  1.00 20.12 -1 150 ASP B OD2 1 
ATOM   4274 N N   . LEU B 1 151 ? -16.087 -18.023 13.933  1.00 15.08 ?  151 LEU B N   1 
ATOM   4275 C CA  . LEU B 1 151 ? -14.667 -17.852 13.635  1.00 15.73 ?  151 LEU B CA  1 
ATOM   4276 C C   . LEU B 1 151 ? -14.344 -18.317 12.223  1.00 16.30 ?  151 LEU B C   1 
ATOM   4277 O O   . LEU B 1 151 ? -13.710 -17.591 11.443  1.00 15.29 ?  151 LEU B O   1 
ATOM   4278 C CB  . LEU B 1 151 ? -13.823 -18.617 14.650  1.00 13.85 ?  151 LEU B CB  1 
ATOM   4279 C CG  . LEU B 1 151 ? -12.312 -18.607 14.417  1.00 16.62 ?  151 LEU B CG  1 
ATOM   4280 C CD1 . LEU B 1 151 ? -11.864 -17.152 14.397  1.00 18.16 ?  151 LEU B CD1 1 
ATOM   4281 C CD2 . LEU B 1 151 ? -11.633 -19.363 15.530  1.00 16.65 ?  151 LEU B CD2 1 
ATOM   4282 N N   . GLU B 1 152 ? -14.783 -19.527 11.865  1.00 14.74 ?  152 GLU B N   1 
ATOM   4283 C CA  . GLU B 1 152 ? -14.402 -20.058 10.559  1.00 15.72 ?  152 GLU B CA  1 
ATOM   4284 C C   . GLU B 1 152 ? -15.055 -19.285 9.422   1.00 15.84 ?  152 GLU B C   1 
ATOM   4285 O O   . GLU B 1 152 ? -14.415 -19.026 8.397   1.00 15.71 ?  152 GLU B O   1 
ATOM   4286 C CB  . GLU B 1 152 ? -14.744 -21.543 10.449  1.00 17.46 ?  152 GLU B CB  1 
ATOM   4287 C CG  . GLU B 1 152 ? -14.538 -22.058 9.027   1.00 18.96 ?  152 GLU B CG  1 
ATOM   4288 C CD  . GLU B 1 152 ? -14.477 -23.566 8.941   1.00 23.49 ?  152 GLU B CD  1 
ATOM   4289 O OE1 . GLU B 1 152 ? -13.810 -24.079 8.004   1.00 21.66 ?  152 GLU B OE1 1 
ATOM   4290 O OE2 . GLU B 1 152 ? -15.102 -24.233 9.798   1.00 23.15 -1 152 GLU B OE2 1 
ATOM   4291 N N   . GLU B 1 153 ? -16.329 -18.917 9.576   1.00 15.20 ?  153 GLU B N   1 
ATOM   4292 C CA  . GLU B 1 153 ? -16.998 -18.134 8.546   1.00 18.33 ?  153 GLU B CA  1 
ATOM   4293 C C   . GLU B 1 153 ? -16.248 -16.833 8.285   1.00 16.27 ?  153 GLU B C   1 
ATOM   4294 O O   . GLU B 1 153 ? -16.107 -16.406 7.137   1.00 15.79 ?  153 GLU B O   1 
ATOM   4295 C CB  . GLU B 1 153 ? -18.446 -17.862 8.954   1.00 18.93 ?  153 GLU B CB  1 
ATOM   4296 C CG  . GLU B 1 153 ? -19.200 -17.015 7.963   1.00 24.07 ?  153 GLU B CG  1 
ATOM   4297 C CD  . GLU B 1 153 ? -20.247 -16.120 8.610   1.00 35.75 ?  153 GLU B CD  1 
ATOM   4298 O OE1 . GLU B 1 153 ? -20.472 -15.002 8.087   1.00 44.14 ?  153 GLU B OE1 1 
ATOM   4299 O OE2 . GLU B 1 153 ? -20.841 -16.516 9.644   1.00 36.63 -1 153 GLU B OE2 1 
ATOM   4300 N N   . LYS B 1 154 ? -15.711 -16.219 9.337   1.00 14.11 ?  154 LYS B N   1 
ATOM   4301 C CA  . LYS B 1 154 ? -14.991 -14.972 9.155   1.00 15.93 ?  154 LYS B CA  1 
ATOM   4302 C C   . LYS B 1 154 ? -13.633 -15.218 8.514   1.00 15.35 ?  154 LYS B C   1 
ATOM   4303 O O   . LYS B 1 154 ? -13.262 -14.516 7.570   1.00 14.24 ?  154 LYS B O   1 
ATOM   4304 C CB  . LYS B 1 154 ? -14.886 -14.250 10.499  1.00 14.67 ?  154 LYS B CB  1 
ATOM   4305 C CG  . LYS B 1 154 ? -16.222 -13.591 10.858  1.00 15.89 ?  154 LYS B CG  1 
ATOM   4306 C CD  . LYS B 1 154 ? -16.302 -13.041 12.266  1.00 16.13 ?  154 LYS B CD  1 
ATOM   4307 C CE  . LYS B 1 154 ? -17.667 -12.382 12.471  1.00 19.72 ?  154 LYS B CE  1 
ATOM   4308 N NZ  . LYS B 1 154 ? -18.041 -12.258 13.900  1.00 18.86 1  154 LYS B NZ  1 
ATOM   4309 N N   . LEU B 1 155 ? -12.908 -16.246 8.964   1.00 14.83 ?  155 LEU B N   1 
ATOM   4310 C CA  . LEU B 1 155 ? -11.622 -16.571 8.344   1.00 14.59 ?  155 LEU B CA  1 
ATOM   4311 C C   . LEU B 1 155 ? -11.783 -16.905 6.864   1.00 16.75 ?  155 LEU B C   1 
ATOM   4312 O O   . LEU B 1 155 ? -10.917 -16.569 6.052   1.00 14.53 ?  155 LEU B O   1 
ATOM   4313 C CB  . LEU B 1 155 ? -10.962 -17.741 9.078   1.00 15.65 ?  155 LEU B CB  1 
ATOM   4314 C CG  . LEU B 1 155 ? -10.456 -17.481 10.495  1.00 15.24 ?  155 LEU B CG  1 
ATOM   4315 C CD1 . LEU B 1 155 ? -9.996  -18.789 11.130  1.00 17.23 ?  155 LEU B CD1 1 
ATOM   4316 C CD2 . LEU B 1 155 ? -9.317  -16.456 10.476  1.00 17.27 ?  155 LEU B CD2 1 
ATOM   4317 N N   . ALA B 1 156 ? -12.880 -17.577 6.501   1.00 14.02 ?  156 ALA B N   1 
ATOM   4318 C CA  . ALA B 1 156 ? -13.161 -17.950 5.118   1.00 17.18 ?  156 ALA B CA  1 
ATOM   4319 C C   . ALA B 1 156 ? -13.588 -16.772 4.244   1.00 18.13 ?  156 ALA B C   1 
ATOM   4320 O O   . ALA B 1 156 ? -13.722 -16.942 3.025   1.00 17.36 ?  156 ALA B O   1 
ATOM   4321 C CB  . ALA B 1 156 ? -14.251 -19.022 5.087   1.00 18.39 ?  156 ALA B CB  1 
ATOM   4322 N N   . THR B 1 157 ? -13.800 -15.597 4.822   1.00 16.17 ?  157 THR B N   1 
ATOM   4323 C CA  . THR B 1 157 ? -14.176 -14.432 4.035   1.00 16.56 ?  157 THR B CA  1 
ATOM   4324 C C   . THR B 1 157 ? -12.983 -13.983 3.198   1.00 16.07 ?  157 THR B C   1 
ATOM   4325 O O   . THR B 1 157 ? -11.863 -13.929 3.710   1.00 16.33 ?  157 THR B O   1 
ATOM   4326 C CB  . THR B 1 157 ? -14.650 -13.314 4.962   1.00 17.65 ?  157 THR B CB  1 
ATOM   4327 O OG1 . THR B 1 157 ? -15.785 -13.781 5.708   1.00 20.36 ?  157 THR B OG1 1 
ATOM   4328 C CG2 . THR B 1 157 ? -15.044 -12.072 4.184   1.00 18.54 ?  157 THR B CG2 1 
ATOM   4329 N N   . PRO B 1 158 ? -13.178 -13.671 1.915   1.00 18.45 ?  158 PRO B N   1 
ATOM   4330 C CA  . PRO B 1 158 ? -12.022 -13.369 1.050   1.00 17.70 ?  158 PRO B CA  1 
ATOM   4331 C C   . PRO B 1 158 ? -11.166 -12.217 1.541   1.00 15.21 ?  158 PRO B C   1 
ATOM   4332 O O   . PRO B 1 158 ? -9.937  -12.290 1.445   1.00 15.84 ?  158 PRO B O   1 
ATOM   4333 C CB  . PRO B 1 158 ? -12.681 -13.049 -0.296  1.00 18.55 ?  158 PRO B CB  1 
ATOM   4334 C CG  . PRO B 1 158 ? -13.943 -13.844 -0.267  1.00 20.04 ?  158 PRO B CG  1 
ATOM   4335 C CD  . PRO B 1 158 ? -14.426 -13.805 1.152   1.00 20.35 ?  158 PRO B CD  1 
ATOM   4336 N N   . SER B 1 159 ? -11.773 -11.164 2.081   1.00 16.97 ?  159 SER B N   1 
ATOM   4337 C CA  . SER B 1 159 ? -10.999 -10.005 2.489   1.00 18.47 ?  159 SER B CA  1 
ATOM   4338 C C   . SER B 1 159 ? -10.343 -10.185 3.852   1.00 15.60 ?  159 SER B C   1 
ATOM   4339 O O   . SER B 1 159 ? -9.528  -9.341  4.244   1.00 14.43 ?  159 SER B O   1 
ATOM   4340 C CB  . SER B 1 159 ? -11.883 -8.749  2.489   1.00 20.11 ?  159 SER B CB  1 
ATOM   4341 O OG  . SER B 1 159 ? -12.947 -8.868  3.409   1.00 17.85 ?  159 SER B OG  1 
ATOM   4342 N N   . VAL B 1 160 ? -10.659 -11.259 4.575   1.00 13.38 ?  160 VAL B N   1 
ATOM   4343 C CA  . VAL B 1 160 ? -10.020 -11.531 5.857   1.00 13.43 ?  160 VAL B CA  1 
ATOM   4344 C C   . VAL B 1 160 ? -8.741  -12.306 5.570   1.00 14.70 ?  160 VAL B C   1 
ATOM   4345 O O   . VAL B 1 160 ? -8.780  -13.465 5.145   1.00 14.29 ?  160 VAL B O   1 
ATOM   4346 C CB  . VAL B 1 160 ? -10.950 -12.297 6.804   1.00 15.44 ?  160 VAL B CB  1 
ATOM   4347 C CG1 . VAL B 1 160 ? -10.186 -12.739 8.053   1.00 13.02 ?  160 VAL B CG1 1 
ATOM   4348 C CG2 . VAL B 1 160 ? -12.150 -11.421 7.171   1.00 13.89 ?  160 VAL B CG2 1 
ATOM   4349 N N   . ARG B 1 161 ? -7.595  -11.663 5.804   1.00 15.18 ?  161 ARG B N   1 
ATOM   4350 C CA  . ARG B 1 161 ? -6.327  -12.160 5.286   1.00 15.56 ?  161 ARG B CA  1 
ATOM   4351 C C   . ARG B 1 161 ? -5.335  -12.578 6.355   1.00 14.67 ?  161 ARG B C   1 
ATOM   4352 O O   . ARG B 1 161 ? -4.320  -13.209 6.023   1.00 15.35 ?  161 ARG B O   1 
ATOM   4353 C CB  . ARG B 1 161 ? -5.688  -11.087 4.395   1.00 17.85 ?  161 ARG B CB  1 
ATOM   4354 C CG  . ARG B 1 161 ? -6.597  -10.700 3.237   1.00 18.08 ?  161 ARG B CG  1 
ATOM   4355 C CD  . ARG B 1 161 ? -6.605  -11.801 2.197   1.00 18.68 ?  161 ARG B CD  1 
ATOM   4356 N NE  . ARG B 1 161 ? -5.259  -12.327 2.029   1.00 17.91 ?  161 ARG B NE  1 
ATOM   4357 C CZ  . ARG B 1 161 ? -4.946  -13.605 2.178   1.00 20.41 ?  161 ARG B CZ  1 
ATOM   4358 N NH1 . ARG B 1 161 ? -5.894  -14.497 2.475   1.00 17.88 1  161 ARG B NH1 1 
ATOM   4359 N NH2 . ARG B 1 161 ? -3.689  -13.987 2.030   1.00 19.43 ?  161 ARG B NH2 1 
ATOM   4360 N N   . MET B 1 162 ? -5.590  -12.242 7.610   1.00 13.57 ?  162 MET B N   1 
ATOM   4361 C CA  . MET B 1 162 ? -4.675  -12.509 8.705   1.00 14.54 ?  162 MET B CA  1 
ATOM   4362 C C   . MET B 1 162 ? -5.491  -12.625 9.980   1.00 15.63 ?  162 MET B C   1 
ATOM   4363 O O   . MET B 1 162 ? -6.537  -11.983 10.135  1.00 14.15 ?  162 MET B O   1 
ATOM   4364 C CB  . MET B 1 162 ? -3.616  -11.398 8.823   1.00 14.10 ?  162 MET B CB  1 
ATOM   4365 C CG  . MET B 1 162 ? -2.722  -11.442 10.058  1.00 15.12 ?  162 MET B CG  1 
ATOM   4366 S SD  . MET B 1 162 ? -1.538  -10.039 10.070  1.00 17.67 ?  162 MET B SD  1 
ATOM   4367 C CE  . MET B 1 162 ? -0.523  -10.393 8.655   1.00 15.00 ?  162 MET B CE  1 
ATOM   4368 N N   . MET B 1 163 ? -5.011  -13.463 10.888  1.00 13.75 ?  163 MET B N   1 
ATOM   4369 C CA  . MET B 1 163 ? -5.576  -13.567 12.221  1.00 13.64 ?  163 MET B CA  1 
ATOM   4370 C C   . MET B 1 163 ? -4.467  -13.272 13.209  1.00 13.95 ?  163 MET B C   1 
ATOM   4371 O O   . MET B 1 163 ? -3.397  -13.889 13.143  1.00 14.06 ?  163 MET B O   1 
ATOM   4372 C CB  . MET B 1 163 ? -6.166  -14.946 12.477  1.00 14.54 ?  163 MET B CB  1 
ATOM   4373 C CG  . MET B 1 163 ? -6.617  -15.103 13.912  1.00 16.51 ?  163 MET B CG  1 
ATOM   4374 S SD  . MET B 1 163 ? -7.382  -16.696 14.215  1.00 16.60 ?  163 MET B SD  1 
ATOM   4375 C CE  . MET B 1 163 ? -8.027  -16.457 15.876  1.00 17.80 ?  163 MET B CE  1 
ATOM   4376 N N   . VAL B 1 164 ? -4.701  -12.313 14.093  1.00 13.29 ?  164 VAL B N   1 
ATOM   4377 C CA  . VAL B 1 164 ? -3.760  -12.004 15.160  1.00 11.74 ?  164 VAL B CA  1 
ATOM   4378 C C   . VAL B 1 164 ? -4.283  -12.714 16.401  1.00 15.42 ?  164 VAL B C   1 
ATOM   4379 O O   . VAL B 1 164 ? -5.288  -12.307 17.000  1.00 17.77 ?  164 VAL B O   1 
ATOM   4380 C CB  . VAL B 1 164 ? -3.584  -10.495 15.378  1.00 15.14 ?  164 VAL B CB  1 
ATOM   4381 C CG1 . VAL B 1 164 ? -2.536  -10.245 16.460  1.00 16.03 ?  164 VAL B CG1 1 
ATOM   4382 C CG2 . VAL B 1 164 ? -3.158  -9.812  14.069  1.00 16.84 ?  164 VAL B CG2 1 
ATOM   4383 N N   . PHE B 1 165 ? -3.605  -13.794 16.748  1.00 14.19 ?  165 PHE B N   1 
ATOM   4384 C CA  . PHE B 1 165 ? -4.037  -14.758 17.748  1.00 13.61 ?  165 PHE B CA  1 
ATOM   4385 C C   . PHE B 1 165 ? -3.218  -14.534 19.009  1.00 16.67 ?  165 PHE B C   1 
ATOM   4386 O O   . PHE B 1 165 ? -1.986  -14.548 18.965  1.00 15.66 ?  165 PHE B O   1 
ATOM   4387 C CB  . PHE B 1 165 ? -3.840  -16.162 17.184  1.00 14.28 ?  165 PHE B CB  1 
ATOM   4388 C CG  . PHE B 1 165 ? -4.143  -17.267 18.133  1.00 14.16 ?  165 PHE B CG  1 
ATOM   4389 C CD1 . PHE B 1 165 ? -5.350  -17.309 18.826  1.00 15.05 ?  165 PHE B CD1 1 
ATOM   4390 C CD2 . PHE B 1 165 ? -3.231  -18.305 18.303  1.00 15.52 ?  165 PHE B CD2 1 
ATOM   4391 C CE1 . PHE B 1 165 ? -5.625  -18.363 19.697  1.00 17.60 ?  165 PHE B CE1 1 
ATOM   4392 C CE2 . PHE B 1 165 ? -3.518  -19.368 19.156  1.00 15.53 ?  165 PHE B CE2 1 
ATOM   4393 C CZ  . PHE B 1 165 ? -4.707  -19.388 19.857  1.00 14.60 ?  165 PHE B CZ  1 
ATOM   4394 N N   . CYS B 1 166 ? -3.892  -14.288 20.118  1.00 14.46 ?  166 CYS B N   1 
ATOM   4395 C CA  . CYS B 1 166 ? -3.220  -13.917 21.353  1.00 13.81 ?  166 CYS B CA  1 
ATOM   4396 C C   . CYS B 1 166 ? -3.133  -15.181 22.205  1.00 15.88 ?  166 CYS B C   1 
ATOM   4397 O O   . CYS B 1 166 ? -4.153  -15.683 22.700  1.00 17.55 ?  166 CYS B O   1 
ATOM   4398 C CB  . CYS B 1 166 ? -3.974  -12.787 22.060  1.00 17.01 ?  166 CYS B CB  1 
ATOM   4399 S SG  . CYS B 1 166 ? -2.967  -11.988 23.312  1.00 16.01 ?  166 CYS B SG  1 
ATOM   4400 N N   . ASN B 1 167 ? -1.934  -15.743 22.300  1.00 14.26 ?  167 ASN B N   1 
ATOM   4401 C CA  . ASN B 1 167 ? -1.748  -17.097 22.873  1.00 13.69 ?  167 ASN B CA  1 
ATOM   4402 C C   . ASN B 1 167 ? -0.557  -17.121 23.840  1.00 13.41 ?  167 ASN B C   1 
ATOM   4403 O O   . ASN B 1 167 ? 0.524   -17.256 23.332  1.00 15.00 ?  167 ASN B O   1 
ATOM   4404 C CB  . ASN B 1 167 ? -1.498  -18.067 21.718  1.00 14.80 ?  167 ASN B CB  1 
ATOM   4405 C CG  . ASN B 1 167 ? -1.228  -19.495 22.128  1.00 17.81 ?  167 ASN B CG  1 
ATOM   4406 O OD1 . ASN B 1 167 ? -1.743  -19.960 23.130  1.00 14.53 ?  167 ASN B OD1 1 
ATOM   4407 N ND2 . ASN B 1 167 ? -0.418  -20.186 21.345  1.00 17.20 ?  167 ASN B ND2 1 
ATOM   4408 N N   . PRO B 1 168 ? -0.711  -17.007 25.188  1.00 12.80 ?  168 PRO B N   1 
ATOM   4409 C CA  . PRO B 1 168 ? -1.951  -16.820 25.962  1.00 13.75 ?  168 PRO B CA  1 
ATOM   4410 C C   . PRO B 1 168 ? -2.722  -15.537 25.673  1.00 14.72 ?  168 PRO B C   1 
ATOM   4411 O O   . PRO B 1 168 ? -2.114  -14.596 25.294  1.00 14.62 ?  168 PRO B O   1 
ATOM   4412 C CB  . PRO B 1 168 ? -1.599  -16.923 27.430  1.00 13.84 ?  168 PRO B CB  1 
ATOM   4413 C CG  . PRO B 1 168 ? -0.336  -17.717 27.417  1.00 14.93 ?  168 PRO B CG  1 
ATOM   4414 C CD  . PRO B 1 168 ? 0.348   -17.141 26.207  1.00 16.15 ?  168 PRO B CD  1 
ATOM   4415 N N   . HIS B 1 169 ? -4.043  -15.558 25.846  1.00 12.18 ?  169 HIS B N   1 
ATOM   4416 C CA  . HIS B 1 169 ? -4.902  -14.436 25.479  1.00 14.85 ?  169 HIS B CA  1 
ATOM   4417 C C   . HIS B 1 169 ? -4.902  -13.398 26.592  1.00 17.38 ?  169 HIS B C   1 
ATOM   4418 O O   . HIS B 1 169 ? -5.211  -13.720 27.744  1.00 17.28 ?  169 HIS B O   1 
ATOM   4419 C CB  . HIS B 1 169 ? -6.321  -14.942 25.219  1.00 13.96 ?  169 HIS B CB  1 
ATOM   4420 C CG  . HIS B 1 169 ? -7.206  -13.948 24.538  1.00 15.91 ?  169 HIS B CG  1 
ATOM   4421 N ND1 . HIS B 1 169 ? -7.415  -13.957 23.177  1.00 14.97 ?  169 HIS B ND1 1 
ATOM   4422 C CD2 . HIS B 1 169 ? -7.935  -12.913 25.024  1.00 13.71 ?  169 HIS B CD2 1 
ATOM   4423 C CE1 . HIS B 1 169 ? -8.242  -12.980 22.852  1.00 14.06 ?  169 HIS B CE1 1 
ATOM   4424 N NE2 . HIS B 1 169 ? -8.572  -12.329 23.953  1.00 15.98 ?  169 HIS B NE2 1 
ATOM   4425 N N   . ASN B 1 170 ? -4.534  -12.159 26.251  1.00 14.88 ?  170 ASN B N   1 
ATOM   4426 C CA  . ASN B 1 170 ? -4.594  -10.936 27.051  1.00 15.10 ?  170 ASN B CA  1 
ATOM   4427 C C   . ASN B 1 170 ? -5.816  -10.149 26.615  1.00 16.52 ?  170 ASN B C   1 
ATOM   4428 O O   . ASN B 1 170 ? -5.939  -9.836  25.425  1.00 15.63 ?  170 ASN B O   1 
ATOM   4429 C CB  . ASN B 1 170 ? -3.308  -10.116 26.851  1.00 17.54 ?  170 ASN B CB  1 
ATOM   4430 C CG  . ASN B 1 170 ? -3.345  -8.724  27.501  1.00 20.35 ?  170 ASN B CG  1 
ATOM   4431 O OD1 . ASN B 1 170 ? -4.012  -8.500  28.503  1.00 24.09 ?  170 ASN B OD1 1 
ATOM   4432 N ND2 . ASN B 1 170 ? -2.553  -7.801  26.956  1.00 20.34 ?  170 ASN B ND2 1 
ATOM   4433 N N   . PRO B 1 171 ? -6.737  -9.769  27.518  1.00 14.52 ?  171 PRO B N   1 
ATOM   4434 C CA  . PRO B 1 171 ? -6.601  -9.685  28.973  1.00 16.20 ?  171 PRO B CA  1 
ATOM   4435 C C   . PRO B 1 171 ? -7.207  -10.792 29.829  1.00 16.26 ?  171 PRO B C   1 
ATOM   4436 O O   . PRO B 1 171 ? -7.100  -10.703 31.067  1.00 18.33 ?  171 PRO B O   1 
ATOM   4437 C CB  . PRO B 1 171 ? -7.327  -8.379  29.270  1.00 17.25 ?  171 PRO B CB  1 
ATOM   4438 C CG  . PRO B 1 171 ? -8.497  -8.426  28.318  1.00 17.25 ?  171 PRO B CG  1 
ATOM   4439 C CD  . PRO B 1 171 ? -7.994  -9.142  27.066  1.00 15.66 ?  171 PRO B CD  1 
ATOM   4440 N N   . ILE B 1 172 ? -7.836  -11.792 29.213  1.00 15.67 ?  172 ILE B N   1 
ATOM   4441 C CA  . ILE B 1 172 ? -8.551  -12.800 29.998  1.00 17.14 ?  172 ILE B CA  1 
ATOM   4442 C C   . ILE B 1 172 ? -7.611  -13.807 30.649  1.00 18.63 ?  172 ILE B C   1 
ATOM   4443 O O   . ILE B 1 172 ? -8.024  -14.524 31.563  1.00 20.29 ?  172 ILE B O   1 
ATOM   4444 C CB  . ILE B 1 172 ? -9.593  -13.521 29.128  1.00 18.59 ?  172 ILE B CB  1 
ATOM   4445 C CG1 . ILE B 1 172 ? -8.924  -14.510 28.172  1.00 16.74 ?  172 ILE B CG1 1 
ATOM   4446 C CG2 . ILE B 1 172 ? -10.423 -12.506 28.344  1.00 18.42 ?  172 ILE B CG2 1 
ATOM   4447 C CD1 . ILE B 1 172 ? -9.933  -15.237 27.276  1.00 19.63 ?  172 ILE B CD1 1 
ATOM   4448 N N   . GLY B 1 173 ? -6.364  -13.883 30.203  1.00 15.57 ?  173 GLY B N   1 
ATOM   4449 C CA  . GLY B 1 173 ? -5.385  -14.726 30.855  1.00 15.31 ?  173 GLY B CA  1 
ATOM   4450 C C   . GLY B 1 173 ? -5.539  -16.199 30.569  1.00 17.00 ?  173 GLY B C   1 
ATOM   4451 O O   . GLY B 1 173 ? -5.415  -17.018 31.486  1.00 15.43 ?  173 GLY B O   1 
ATOM   4452 N N   . TYR B 1 174 ? -5.782  -16.570 29.311  1.00 14.29 ?  174 TYR B N   1 
ATOM   4453 C CA  . TYR B 1 174 ? -6.115  -17.948 28.964  1.00 17.44 ?  174 TYR B CA  1 
ATOM   4454 C C   . TYR B 1 174 ? -5.066  -18.520 28.024  1.00 16.54 ?  174 TYR B C   1 
ATOM   4455 O O   . TYR B 1 174 ? -4.892  -18.025 26.905  1.00 16.27 ?  174 TYR B O   1 
ATOM   4456 C CB  . TYR B 1 174 ? -7.497  -18.038 28.322  1.00 17.21 ?  174 TYR B CB  1 
ATOM   4457 C CG  . TYR B 1 174 ? -7.831  -19.445 27.907  1.00 19.68 ?  174 TYR B CG  1 
ATOM   4458 C CD1 . TYR B 1 174 ? -7.867  -20.478 28.842  1.00 21.15 ?  174 TYR B CD1 1 
ATOM   4459 C CD2 . TYR B 1 174 ? -8.093  -19.752 26.579  1.00 18.26 ?  174 TYR B CD2 1 
ATOM   4460 C CE1 . TYR B 1 174 ? -8.162  -21.780 28.457  1.00 22.49 ?  174 TYR B CE1 1 
ATOM   4461 C CE2 . TYR B 1 174 ? -8.401  -21.046 26.193  1.00 20.19 ?  174 TYR B CE2 1 
ATOM   4462 C CZ  . TYR B 1 174 ? -8.434  -22.049 27.124  1.00 21.99 ?  174 TYR B CZ  1 
ATOM   4463 O OH  . TYR B 1 174 ? -8.728  -23.322 26.704  1.00 23.01 ?  174 TYR B OH  1 
ATOM   4464 N N   . ALA B 1 175 ? -4.374  -19.560 28.479  1.00 16.32 ?  175 ALA B N   1 
ATOM   4465 C CA  . ALA B 1 175 ? -3.464  -20.324 27.639  1.00 16.25 ?  175 ALA B CA  1 
ATOM   4466 C C   . ALA B 1 175 ? -4.275  -21.386 26.906  1.00 18.20 ?  175 ALA B C   1 
ATOM   4467 O O   . ALA B 1 175 ? -4.752  -22.351 27.520  1.00 15.38 ?  175 ALA B O   1 
ATOM   4468 C CB  . ALA B 1 175 ? -2.352  -20.948 28.479  1.00 18.67 ?  175 ALA B CB  1 
ATOM   4469 N N   . TRP B 1 176 ? -4.442  -21.199 25.596  1.00 15.40 ?  176 TRP B N   1 
ATOM   4470 C CA  . TRP B 1 176 ? -5.228  -22.112 24.775  1.00 17.13 ?  176 TRP B CA  1 
ATOM   4471 C C   . TRP B 1 176 ? -4.683  -23.533 24.855  1.00 18.17 ?  176 TRP B C   1 
ATOM   4472 O O   . TRP B 1 176 ? -3.476  -23.756 24.933  1.00 15.58 ?  176 TRP B O   1 
ATOM   4473 C CB  . TRP B 1 176 ? -5.219  -21.654 23.314  1.00 16.44 ?  176 TRP B CB  1 
ATOM   4474 C CG  . TRP B 1 176 ? -5.650  -20.248 23.151  1.00 15.66 ?  176 TRP B CG  1 
ATOM   4475 C CD1 . TRP B 1 176 ? -4.861  -19.140 23.163  1.00 16.22 ?  176 TRP B CD1 1 
ATOM   4476 C CD2 . TRP B 1 176 ? -6.989  -19.790 22.982  1.00 16.22 ?  176 TRP B CD2 1 
ATOM   4477 N NE1 . TRP B 1 176 ? -5.629  -18.011 23.002  1.00 15.81 ?  176 TRP B NE1 1 
ATOM   4478 C CE2 . TRP B 1 176 ? -6.942  -18.386 22.885  1.00 17.35 ?  176 TRP B CE2 1 
ATOM   4479 C CE3 . TRP B 1 176 ? -8.228  -20.433 22.889  1.00 19.57 ?  176 TRP B CE3 1 
ATOM   4480 C CZ2 . TRP B 1 176 ? -8.085  -17.612 22.709  1.00 18.05 ?  176 TRP B CZ2 1 
ATOM   4481 C CZ3 . TRP B 1 176 ? -9.355  -19.667 22.715  1.00 22.92 ?  176 TRP B CZ3 1 
ATOM   4482 C CH2 . TRP B 1 176 ? -9.278  -18.268 22.621  1.00 19.69 ?  176 TRP B CH2 1 
ATOM   4483 N N   . SER B 1 177 ? -5.585  -24.506 24.786  1.00 18.30 ?  177 SER B N   1 
ATOM   4484 C CA  . SER B 1 177 ? -5.157  -25.897 24.789  1.00 19.05 ?  177 SER B CA  1 
ATOM   4485 C C   . SER B 1 177 ? -4.518  -26.275 23.452  1.00 18.64 ?  177 SER B C   1 
ATOM   4486 O O   . SER B 1 177 ? -4.634  -25.564 22.451  1.00 16.09 ?  177 SER B O   1 
ATOM   4487 C CB  . SER B 1 177 ? -6.339  -26.814 25.058  1.00 23.47 ?  177 SER B CB  1 
ATOM   4488 O OG  . SER B 1 177 ? -7.086  -26.939 23.874  1.00 20.76 ?  177 SER B OG  1 
ATOM   4489 N N   . GLU B 1 178 ? -3.854  -27.438 23.447  1.00 18.48 ?  178 GLU B N   1 
ATOM   4490 C CA  . GLU B 1 178 ? -3.204  -27.933 22.236  1.00 18.80 ?  178 GLU B CA  1 
ATOM   4491 C C   . GLU B 1 178 ? -4.194  -28.100 21.094  1.00 20.43 ?  178 GLU B C   1 
ATOM   4492 O O   . GLU B 1 178 ? -3.939  -27.641 19.976  1.00 17.26 ?  178 GLU B O   1 
ATOM   4493 C CB  . GLU B 1 178 ? -2.488  -29.257 22.502  1.00 22.85 ?  178 GLU B CB  1 
ATOM   4494 C CG  . GLU B 1 178 ? -1.506  -29.610 21.391  1.00 24.05 ?  178 GLU B CG  1 
ATOM   4495 C CD  . GLU B 1 178 ? -0.948  -31.021 21.497  1.00 30.95 ?  178 GLU B CD  1 
ATOM   4496 O OE1 . GLU B 1 178 ? -1.089  -31.808 20.534  1.00 34.76 ?  178 GLU B OE1 1 
ATOM   4497 O OE2 . GLU B 1 178 ? -0.361  -31.343 22.546  1.00 32.97 -1 178 GLU B OE2 1 
ATOM   4498 N N   . GLU B 1 179 ? -5.330  -28.759 21.331  1.00 18.46 ?  179 GLU B N   1 
ATOM   4499 C CA  . GLU B 1 179 ? -6.211  -28.906 20.176  1.00 23.16 ?  179 GLU B CA  1 
ATOM   4500 C C   . GLU B 1 179 ? -6.870  -27.591 19.789  1.00 20.78 ?  179 GLU B C   1 
ATOM   4501 O O   . GLU B 1 179 ? -7.212  -27.429 18.618  1.00 19.47 ?  179 GLU B O   1 
ATOM   4502 C CB  . GLU B 1 179 ? -7.257  -30.025 20.352  1.00 29.97 ?  179 GLU B CB  1 
ATOM   4503 C CG  . GLU B 1 179 ? -7.875  -30.253 21.710  1.00 36.67 ?  179 GLU B CG  1 
ATOM   4504 C CD  . GLU B 1 179 ? -9.170  -31.094 21.642  1.00 46.29 ?  179 GLU B CD  1 
ATOM   4505 O OE1 . GLU B 1 179 ? -10.188 -30.678 22.267  1.00 49.03 ?  179 GLU B OE1 1 
ATOM   4506 O OE2 . GLU B 1 179 ? -9.159  -32.151 20.947  1.00 45.59 -1 179 GLU B OE2 1 
ATOM   4507 N N   . GLU B 1 180 ? -6.990  -26.632 20.716  1.00 18.87 ?  180 GLU B N   1 
ATOM   4508 C CA  . GLU B 1 180 ? -7.426  -25.282 20.358  1.00 20.66 ?  180 GLU B CA  1 
ATOM   4509 C C   . GLU B 1 180 ? -6.460  -24.637 19.371  1.00 18.14 ?  180 GLU B C   1 
ATOM   4510 O O   . GLU B 1 180 ? -6.863  -24.145 18.310  1.00 14.88 ?  180 GLU B O   1 
ATOM   4511 C CB  . GLU B 1 180 ? -7.527  -24.417 21.615  1.00 21.02 ?  180 GLU B CB  1 
ATOM   4512 C CG  . GLU B 1 180 ? -8.895  -24.249 22.183  1.00 27.40 ?  180 GLU B CG  1 
ATOM   4513 C CD  . GLU B 1 180 ? -8.886  -23.968 23.703  1.00 25.35 ?  180 GLU B CD  1 
ATOM   4514 O OE1 . GLU B 1 180 ? -9.980  -23.863 24.280  1.00 32.60 ?  180 GLU B OE1 1 
ATOM   4515 O OE2 . GLU B 1 180 ? -7.814  -23.863 24.314  1.00 23.61 -1 180 GLU B OE2 1 
ATOM   4516 N N   . VAL B 1 181 ? -5.177  -24.605 19.729  1.00 15.49 ?  181 VAL B N   1 
ATOM   4517 C CA  . VAL B 1 181 ? -4.173  -23.990 18.861  1.00 15.91 ?  181 VAL B CA  1 
ATOM   4518 C C   . VAL B 1 181 ? -4.094  -24.724 17.529  1.00 15.44 ?  181 VAL B C   1 
ATOM   4519 O O   . VAL B 1 181 ? -4.050  -24.101 16.458  1.00 17.66 ?  181 VAL B O   1 
ATOM   4520 C CB  . VAL B 1 181 ? -2.807  -23.955 19.568  1.00 16.38 ?  181 VAL B CB  1 
ATOM   4521 C CG1 . VAL B 1 181 ? -1.725  -23.387 18.611  1.00 14.04 ?  181 VAL B CG1 1 
ATOM   4522 C CG2 . VAL B 1 181 ? -2.911  -23.115 20.839  1.00 15.78 ?  181 VAL B CG2 1 
ATOM   4523 N N   . LYS B 1 182 ? -4.082  -26.057 17.574  1.00 15.99 ?  182 LYS B N   1 
ATOM   4524 C CA  . LYS B 1 182 ? -4.025  -26.836 16.343  1.00 18.46 ?  182 LYS B CA  1 
ATOM   4525 C C   . LYS B 1 182 ? -5.237  -26.564 15.468  1.00 17.02 ?  182 LYS B C   1 
ATOM   4526 O O   . LYS B 1 182 ? -5.108  -26.422 14.244  1.00 17.29 ?  182 LYS B O   1 
ATOM   4527 C CB  . LYS B 1 182 ? -3.905  -28.322 16.672  1.00 16.20 ?  182 LYS B CB  1 
ATOM   4528 C CG  . LYS B 1 182 ? -2.560  -28.658 17.285  1.00 19.84 ?  182 LYS B CG  1 
ATOM   4529 C CD  . LYS B 1 182 ? -2.276  -30.150 17.321  1.00 24.69 ?  182 LYS B CD  1 
ATOM   4530 C CE  . LYS B 1 182 ? -0.798  -30.373 17.641  1.00 28.87 ?  182 LYS B CE  1 
ATOM   4531 N NZ  . LYS B 1 182 ? -0.405  -31.805 17.630  1.00 34.91 1  182 LYS B NZ  1 
ATOM   4532 N N   . ARG B 1 183 ? -6.418  -26.438 16.047  1.00 16.32 ?  183 ARG B N   1 
ATOM   4533 C CA  . ARG B 1 183 ? -7.645  -26.173 15.256  1.00 19.25 ?  183 ARG B CA  1 
ATOM   4534 C C   . ARG B 1 183 ? -7.606  -24.787 14.614  1.00 18.31 ?  183 ARG B C   1 
ATOM   4535 O O   . ARG B 1 183 ? -8.007  -24.676 13.474  1.00 17.38 ?  183 ARG B O   1 
ATOM   4536 C CB  . ARG B 1 183 ? -8.914  -26.298 16.099  1.00 19.51 ?  183 ARG B CB  1 
ATOM   4537 C CG  . ARG B 1 183 ? -10.212 -26.243 15.311  1.00 21.43 ?  183 ARG B CG  1 
ATOM   4538 C CD  . ARG B 1 183 ? -11.408 -26.366 16.233  1.00 28.93 ?  183 ARG B CD  1 
ATOM   4539 N NE  . ARG B 1 183 ? -11.566 -27.664 16.865  1.00 35.38 ?  183 ARG B NE  1 
ATOM   4540 C CZ  . ARG B 1 183 ? -11.519 -27.885 18.172  1.00 32.64 ?  183 ARG B CZ  1 
ATOM   4541 N NH1 . ARG B 1 183 ? -11.298 -26.891 19.012  1.00 37.36 1  183 ARG B NH1 1 
ATOM   4542 N NH2 . ARG B 1 183 ? -11.677 -29.108 18.636  1.00 39.93 ?  183 ARG B NH2 1 
ATOM   4543 N N   . ILE B 1 184 ? -7.141  -23.799 15.376  1.00 15.61 ?  184 ILE B N   1 
ATOM   4544 C CA  . ILE B 1 184 ? -7.067  -22.452 14.823  1.00 18.02 ?  184 ILE B CA  1 
ATOM   4545 C C   . ILE B 1 184 ? -6.073  -22.408 13.669  1.00 15.85 ?  184 ILE B C   1 
ATOM   4546 O O   . ILE B 1 184 ? -6.369  -21.860 12.594  1.00 13.32 ?  184 ILE B O   1 
ATOM   4547 C CB  . ILE B 1 184 ? -6.730  -21.448 15.936  1.00 16.18 ?  184 ILE B CB  1 
ATOM   4548 C CG1 . ILE B 1 184 ? -7.932  -21.339 16.874  1.00 17.24 ?  184 ILE B CG1 1 
ATOM   4549 C CG2 . ILE B 1 184 ? -6.371  -20.091 15.359  1.00 15.94 ?  184 ILE B CG2 1 
ATOM   4550 C CD1 . ILE B 1 184 ? -7.722  -20.446 18.051  1.00 18.86 ?  184 ILE B CD1 1 
ATOM   4551 N N   . ALA B 1 185 ? -4.897  -23.024 13.853  1.00 14.01 ?  185 ALA B N   1 
ATOM   4552 C CA  . ALA B 1 185 ? -3.904  -23.067 12.778  1.00 17.35 ?  185 ALA B CA  1 
ATOM   4553 C C   . ALA B 1 185 ? -4.433  -23.797 11.544  1.00 17.24 ?  185 ALA B C   1 
ATOM   4554 O O   . ALA B 1 185 ? -4.207  -23.350 10.415  1.00 15.10 ?  185 ALA B O   1 
ATOM   4555 C CB  . ALA B 1 185 ? -2.606  -23.722 13.264  1.00 15.19 ?  185 ALA B CB  1 
ATOM   4556 N N   . GLU B 1 186 ? -5.133  -24.925 11.735  1.00 17.77 ?  186 GLU B N   1 
ATOM   4557 C CA  . GLU B 1 186 ? -5.680  -25.650 10.583  1.00 18.98 ?  186 GLU B CA  1 
ATOM   4558 C C   . GLU B 1 186 ? -6.746  -24.830 9.861   1.00 18.72 ?  186 GLU B C   1 
ATOM   4559 O O   . GLU B 1 186 ? -6.812  -24.849 8.627   1.00 17.51 ?  186 GLU B O   1 
ATOM   4560 C CB  . GLU B 1 186 ? -6.252  -27.009 11.005  1.00 23.06 ?  186 GLU B CB  1 
ATOM   4561 C CG  . GLU B 1 186 ? -5.217  -27.992 11.552  1.00 27.99 ?  186 GLU B CG  1 
ATOM   4562 C CD  . GLU B 1 186 ? -4.498  -28.804 10.479  1.00 31.65 ?  186 GLU B CD  1 
ATOM   4563 O OE1 . GLU B 1 186 ? -4.616  -28.470 9.279   1.00 37.05 ?  186 GLU B OE1 1 
ATOM   4564 O OE2 . GLU B 1 186 ? -3.807  -29.786 10.840  1.00 41.31 -1 186 GLU B OE2 1 
ATOM   4565 N N   . LEU B 1 187 ? -7.593  -24.114 10.609  1.00 16.55 ?  187 LEU B N   1 
ATOM   4566 C CA  . LEU B 1 187 ? -8.589  -23.242 9.991   1.00 17.86 ?  187 LEU B CA  1 
ATOM   4567 C C   . LEU B 1 187 ? -7.916  -22.148 9.164   1.00 16.04 ?  187 LEU B C   1 
ATOM   4568 O O   . LEU B 1 187 ? -8.308  -21.875 8.025   1.00 15.34 ?  187 LEU B O   1 
ATOM   4569 C CB  . LEU B 1 187 ? -9.477  -22.622 11.072  1.00 15.36 ?  187 LEU B CB  1 
ATOM   4570 C CG  . LEU B 1 187 ? -10.551 -23.476 11.754  1.00 19.27 ?  187 LEU B CG  1 
ATOM   4571 C CD1 . LEU B 1 187 ? -11.275 -22.667 12.845  1.00 21.14 ?  187 LEU B CD1 1 
ATOM   4572 C CD2 . LEU B 1 187 ? -11.551 -23.983 10.739  1.00 19.64 ?  187 LEU B CD2 1 
ATOM   4573 N N   . CYS B 1 188 ? -6.897  -21.512 9.741   1.00 15.80 ?  188 CYS B N   1 
ATOM   4574 C CA  . CYS B 1 188 ? -6.154  -20.475 9.045   1.00 15.98 ?  188 CYS B CA  1 
ATOM   4575 C C   . CYS B 1 188 ? -5.549  -21.011 7.759   1.00 16.16 ?  188 CYS B C   1 
ATOM   4576 O O   . CYS B 1 188 ? -5.733  -20.438 6.676   1.00 15.11 ?  188 CYS B O   1 
ATOM   4577 C CB  . CYS B 1 188 ? -5.076  -19.950 9.986   1.00 15.52 ?  188 CYS B CB  1 
ATOM   4578 S SG  . CYS B 1 188 ? -5.864  -18.682 11.039  1.00 16.50 ?  188 CYS B SG  1 
ATOM   4579 N N   . ALA B 1 189 ? -4.847  -22.135 7.862   1.00 14.12 ?  189 ALA B N   1 
ATOM   4580 C CA  . ALA B 1 189 ? -4.178  -22.724 6.709   1.00 17.81 ?  189 ALA B CA  1 
ATOM   4581 C C   . ALA B 1 189 ? -5.183  -23.100 5.632   1.00 18.35 ?  189 ALA B C   1 
ATOM   4582 O O   . ALA B 1 189 ? -4.993  -22.780 4.452   1.00 17.46 ?  189 ALA B O   1 
ATOM   4583 C CB  . ALA B 1 189 ? -3.390  -23.946 7.166   1.00 17.71 ?  189 ALA B CB  1 
ATOM   4584 N N   . LYS B 1 190 ? -6.256  -23.795 6.024   1.00 16.49 ?  190 LYS B N   1 
ATOM   4585 C CA  . LYS B 1 190 ? -7.293  -24.188 5.073   1.00 16.67 ?  190 LYS B CA  1 
ATOM   4586 C C   . LYS B 1 190 ? -7.820  -22.991 4.297   1.00 16.88 ?  190 LYS B C   1 
ATOM   4587 O O   . LYS B 1 190 ? -8.058  -23.076 3.087   1.00 15.85 ?  190 LYS B O   1 
ATOM   4588 C CB  . LYS B 1 190 ? -8.437  -24.887 5.812   1.00 19.73 ?  190 LYS B CB  1 
ATOM   4589 C CG  . LYS B 1 190 ? -9.561  -25.400 4.915   1.00 21.72 ?  190 LYS B CG  1 
ATOM   4590 C CD  . LYS B 1 190 ? -10.869 -25.551 5.696   1.00 29.45 ?  190 LYS B CD  1 
ATOM   4591 C CE  . LYS B 1 190 ? -10.658 -26.068 7.137   1.00 29.09 ?  190 LYS B CE  1 
ATOM   4592 N NZ  . LYS B 1 190 ? -11.947 -26.292 7.924   1.00 21.56 1  190 LYS B NZ  1 
ATOM   4593 N N   . HIS B 1 191 ? -7.998  -21.859 4.969   1.00 14.38 ?  191 HIS B N   1 
ATOM   4594 C CA  . HIS B 1 191 ? -8.568  -20.676 4.342   1.00 16.05 ?  191 HIS B CA  1 
ATOM   4595 C C   . HIS B 1 191 ? -7.512  -19.679 3.872   1.00 15.20 ?  191 HIS B C   1 
ATOM   4596 O O   . HIS B 1 191 ? -7.856  -18.545 3.528   1.00 15.47 ?  191 HIS B O   1 
ATOM   4597 C CB  . HIS B 1 191 ? -9.570  -20.045 5.306   1.00 15.77 ?  191 HIS B CB  1 
ATOM   4598 C CG  . HIS B 1 191 ? -10.757 -20.925 5.555   1.00 17.65 ?  191 HIS B CG  1 
ATOM   4599 N ND1 . HIS B 1 191 ? -11.641 -21.267 4.554   1.00 16.61 ?  191 HIS B ND1 1 
ATOM   4600 C CD2 . HIS B 1 191 ? -11.179 -21.574 6.668   1.00 17.60 ?  191 HIS B CD2 1 
ATOM   4601 C CE1 . HIS B 1 191 ? -12.567 -22.075 5.044   1.00 17.30 ?  191 HIS B CE1 1 
ATOM   4602 N NE2 . HIS B 1 191 ? -12.316 -22.269 6.327   1.00 17.11 ?  191 HIS B NE2 1 
ATOM   4603 N N   . GLN B 1 192 ? -6.241  -20.095 3.832   1.00 14.26 ?  192 GLN B N   1 
ATOM   4604 C CA  . GLN B 1 192 ? -5.126  -19.301 3.295   1.00 14.71 ?  192 GLN B CA  1 
ATOM   4605 C C   . GLN B 1 192 ? -4.979  -17.968 4.026   1.00 16.73 ?  192 GLN B C   1 
ATOM   4606 O O   . GLN B 1 192 ? -4.701  -16.925 3.429   1.00 15.18 ?  192 GLN B O   1 
ATOM   4607 C CB  . GLN B 1 192 ? -5.275  -19.104 1.786   1.00 17.83 ?  192 GLN B CB  1 
ATOM   4608 C CG  . GLN B 1 192 ? -5.438  -20.429 1.039   1.00 18.99 ?  192 GLN B CG  1 
ATOM   4609 C CD  . GLN B 1 192 ? -5.655  -20.242 -0.448  1.00 21.47 ?  192 GLN B CD  1 
ATOM   4610 O OE1 . GLN B 1 192 ? -4.754  -19.793 -1.154  1.00 20.47 ?  192 GLN B OE1 1 
ATOM   4611 N NE2 . GLN B 1 192 ? -6.848  -20.590 -0.936  1.00 20.01 ?  192 GLN B NE2 1 
ATOM   4612 N N   . VAL B 1 193 ? -5.138  -18.022 5.342   1.00 12.66 ?  193 VAL B N   1 
ATOM   4613 C CA  . VAL B 1 193 ? -5.022  -16.882 6.232   1.00 14.43 ?  193 VAL B CA  1 
ATOM   4614 C C   . VAL B 1 193 ? -3.765  -17.080 7.061   1.00 14.33 ?  193 VAL B C   1 
ATOM   4615 O O   . VAL B 1 193 ? -3.509  -18.180 7.567   1.00 14.45 ?  193 VAL B O   1 
ATOM   4616 C CB  . VAL B 1 193 ? -6.261  -16.772 7.134   1.00 14.66 ?  193 VAL B CB  1 
ATOM   4617 C CG1 . VAL B 1 193 ? -6.033  -15.758 8.250   1.00 15.17 ?  193 VAL B CG1 1 
ATOM   4618 C CG2 . VAL B 1 193 ? -7.473  -16.420 6.302   1.00 13.33 ?  193 VAL B CG2 1 
ATOM   4619 N N   . LEU B 1 194 ? -2.976  -16.025 7.193   1.00 14.81 ?  194 LEU B N   1 
ATOM   4620 C CA  . LEU B 1 194 ? -1.771  -16.113 7.999   1.00 14.16 ?  194 LEU B CA  1 
ATOM   4621 C C   . LEU B 1 194 ? -2.119  -15.995 9.476   1.00 14.93 ?  194 LEU B C   1 
ATOM   4622 O O   . LEU B 1 194 ? -2.821  -15.061 9.886   1.00 14.16 ?  194 LEU B O   1 
ATOM   4623 C CB  . LEU B 1 194 ? -0.787  -15.023 7.582   1.00 16.54 ?  194 LEU B CB  1 
ATOM   4624 C CG  . LEU B 1 194 ? 0.622   -15.406 7.949   1.00 23.47 ?  194 LEU B CG  1 
ATOM   4625 C CD1 . LEU B 1 194 ? 1.081   -16.472 6.940   1.00 19.70 ?  194 LEU B CD1 1 
ATOM   4626 C CD2 . LEU B 1 194 ? 1.491   -14.163 7.863   1.00 24.72 ?  194 LEU B CD2 1 
ATOM   4627 N N   . LEU B 1 195 ? -1.629  -16.939 10.271  1.00 12.41 ?  195 LEU B N   1 
ATOM   4628 C CA  . LEU B 1 195 ? -1.859  -16.934 11.717  1.00 13.84 ?  195 LEU B CA  1 
ATOM   4629 C C   . LEU B 1 195 ? -0.665  -16.284 12.410  1.00 13.44 ?  195 LEU B C   1 
ATOM   4630 O O   . LEU B 1 195 ? 0.440   -16.832 12.409  1.00 15.31 ?  195 LEU B O   1 
ATOM   4631 C CB  . LEU B 1 195 ? -2.080  -18.353 12.234  1.00 14.91 ?  195 LEU B CB  1 
ATOM   4632 C CG  . LEU B 1 195 ? -2.245  -18.468 13.743  1.00 13.32 ?  195 LEU B CG  1 
ATOM   4633 C CD1 . LEU B 1 195 ? -3.521  -17.758 14.172  1.00 13.64 ?  195 LEU B CD1 1 
ATOM   4634 C CD2 . LEU B 1 195 ? -2.286  -19.938 14.178  1.00 13.06 ?  195 LEU B CD2 1 
ATOM   4635 N N   . ILE B 1 196 ? -0.880  -15.112 12.988  1.00 12.34 ?  196 ILE B N   1 
ATOM   4636 C CA  . ILE B 1 196 ? 0.145   -14.433 13.765  1.00 13.32 ?  196 ILE B CA  1 
ATOM   4637 C C   . ILE B 1 196 ? -0.129  -14.754 15.227  1.00 15.81 ?  196 ILE B C   1 
ATOM   4638 O O   . ILE B 1 196 ? -1.084  -14.235 15.822  1.00 14.49 ?  196 ILE B O   1 
ATOM   4639 C CB  . ILE B 1 196 ? 0.164   -12.920 13.515  1.00 16.34 ?  196 ILE B CB  1 
ATOM   4640 C CG1 . ILE B 1 196 ? 0.327   -12.599 12.019  1.00 16.13 ?  196 ILE B CG1 1 
ATOM   4641 C CG2 . ILE B 1 196 ? 1.277   -12.284 14.340  1.00 16.27 ?  196 ILE B CG2 1 
ATOM   4642 C CD1 . ILE B 1 196 ? 1.515   -13.277 11.357  1.00 16.27 ?  196 ILE B CD1 1 
ATOM   4643 N N   . SER B 1 197 ? 0.713   -15.607 15.814  1.00 13.30 ?  197 SER B N   1 
ATOM   4644 C CA  . SER B 1 197 ? 0.503   -16.076 17.180  1.00 14.83 ?  197 SER B CA  1 
ATOM   4645 C C   . SER B 1 197 ? 1.389   -15.253 18.110  1.00 16.59 ?  197 SER B C   1 
ATOM   4646 O O   . SER B 1 197 ? 2.614   -15.426 18.138  1.00 15.90 ?  197 SER B O   1 
ATOM   4647 C CB  . SER B 1 197 ? 0.795   -17.572 17.296  1.00 12.31 ?  197 SER B CB  1 
ATOM   4648 O OG  . SER B 1 197 ? 0.583   -18.051 18.626  1.00 18.67 ?  197 SER B OG  1 
ATOM   4649 N N   . ASP B 1 198 ? 0.768   -14.348 18.863  1.00 14.45 ?  198 ASP B N   1 
ATOM   4650 C CA  . ASP B 1 198 ? 1.474   -13.492 19.813  1.00 15.30 ?  198 ASP B CA  1 
ATOM   4651 C C   . ASP B 1 198 ? 1.619   -14.275 21.113  1.00 15.57 ?  198 ASP B C   1 
ATOM   4652 O O   . ASP B 1 198 ? 0.663   -14.408 21.873  1.00 15.59 ?  198 ASP B O   1 
ATOM   4653 C CB  . ASP B 1 198 ? 0.699   -12.192 19.989  1.00 15.65 ?  198 ASP B CB  1 
ATOM   4654 C CG  . ASP B 1 198 ? 1.278   -11.270 21.050  1.00 18.20 ?  198 ASP B CG  1 
ATOM   4655 O OD1 . ASP B 1 198 ? 2.150   -11.665 21.858  1.00 16.23 ?  198 ASP B OD1 1 
ATOM   4656 O OD2 . ASP B 1 198 ? 0.836   -10.106 21.061  1.00 22.63 -1 198 ASP B OD2 1 
ATOM   4657 N N   . GLU B 1 199 ? 2.825   -14.767 21.400  1.00 12.92 ?  199 GLU B N   1 
ATOM   4658 C CA  . GLU B 1 199 ? 3.050   -15.658 22.573  1.00 15.41 ?  199 GLU B CA  1 
ATOM   4659 C C   . GLU B 1 199 ? 3.858   -14.951 23.658  1.00 14.82 ?  199 GLU B C   1 
ATOM   4660 O O   . GLU B 1 199 ? 4.597   -15.601 24.361  1.00 14.33 ?  199 GLU B O   1 
ATOM   4661 C CB  . GLU B 1 199 ? 3.723   -16.942 22.094  1.00 15.57 ?  199 GLU B CB  1 
ATOM   4662 C CG  . GLU B 1 199 ? 2.832   -17.759 21.183  1.00 16.60 ?  199 GLU B CG  1 
ATOM   4663 C CD  . GLU B 1 199 ? 3.495   -18.783 20.287  1.00 18.51 ?  199 GLU B CD  1 
ATOM   4664 O OE1 . GLU B 1 199 ? 2.841   -19.235 19.339  1.00 17.96 ?  199 GLU B OE1 1 
ATOM   4665 O OE2 . GLU B 1 199 ? 4.648   -19.113 20.534  1.00 18.90 -1 199 GLU B OE2 1 
ATOM   4666 N N   . ILE B 1 200 ? 3.671   -13.642 23.753  1.00 12.69 ?  200 ILE B N   1 
ATOM   4667 C CA  . ILE B 1 200 ? 4.482   -12.886 24.694  1.00 12.69 ?  200 ILE B CA  1 
ATOM   4668 C C   . ILE B 1 200 ? 4.171   -13.265 26.136  1.00 13.36 ?  200 ILE B C   1 
ATOM   4669 O O   . ILE B 1 200 ? 5.023   -13.079 27.004  1.00 14.35 ?  200 ILE B O   1 
ATOM   4670 C CB  . ILE B 1 200 ? 4.307   -11.377 24.425  1.00 17.07 ?  200 ILE B CB  1 
ATOM   4671 C CG1 . ILE B 1 200 ? 5.453   -10.576 25.064  1.00 16.71 ?  200 ILE B CG1 1 
ATOM   4672 C CG2 . ILE B 1 200 ? 2.941   -10.916 24.881  1.00 18.65 ?  200 ILE B CG2 1 
ATOM   4673 C CD1 . ILE B 1 200 ? 5.529   -9.156  24.618  1.00 17.85 ?  200 ILE B CD1 1 
ATOM   4674 N N   . HIS B 1 201 ? 2.988   -13.826 26.421  1.00 11.68 ?  201 HIS B N   1 
ATOM   4675 C CA  . HIS B 1 201 ? 2.668   -14.278 27.775  1.00 14.23 ?  201 HIS B CA  1 
ATOM   4676 C C   . HIS B 1 201 ? 2.963   -15.760 27.993  1.00 12.70 ?  201 HIS B C   1 
ATOM   4677 O O   . HIS B 1 201 ? 2.603   -16.305 29.042  1.00 14.11 ?  201 HIS B O   1 
ATOM   4678 C CB  . HIS B 1 201 ? 1.207   -13.976 28.107  1.00 11.95 ?  201 HIS B CB  1 
ATOM   4679 C CG  . HIS B 1 201 ? 0.904   -12.516 28.144  1.00 17.00 ?  201 HIS B CG  1 
ATOM   4680 N ND1 . HIS B 1 201 ? 1.070   -11.748 29.278  1.00 18.92 ?  201 HIS B ND1 1 
ATOM   4681 C CD2 . HIS B 1 201 ? 0.468   -11.678 27.177  1.00 17.19 ?  201 HIS B CD2 1 
ATOM   4682 C CE1 . HIS B 1 201 ? 0.745   -10.496 29.002  1.00 19.63 ?  201 HIS B CE1 1 
ATOM   4683 N NE2 . HIS B 1 201 ? 0.370   -10.430 27.736  1.00 17.42 ?  201 HIS B NE2 1 
ATOM   4684 N N   . GLY B 1 202 ? 3.654   -16.403 27.045  1.00 12.72 ?  202 GLY B N   1 
ATOM   4685 C CA  . GLY B 1 202 ? 3.735   -17.854 27.039  1.00 14.89 ?  202 GLY B CA  1 
ATOM   4686 C C   . GLY B 1 202 ? 4.555   -18.430 28.175  1.00 17.37 ?  202 GLY B C   1 
ATOM   4687 O O   . GLY B 1 202 ? 4.378   -19.598 28.543  1.00 14.93 ?  202 GLY B O   1 
ATOM   4688 N N   . ASP B 1 203 ? 5.493   -17.654 28.707  1.00 15.07 ?  203 ASP B N   1 
ATOM   4689 C CA  . ASP B 1 203 ? 6.289   -18.128 29.827  1.00 14.80 ?  203 ASP B CA  1 
ATOM   4690 C C   . ASP B 1 203 ? 5.566   -17.991 31.153  1.00 15.07 ?  203 ASP B C   1 
ATOM   4691 O O   . ASP B 1 203 ? 6.127   -18.374 32.186  1.00 14.49 ?  203 ASP B O   1 
ATOM   4692 C CB  . ASP B 1 203 ? 7.607   -17.366 29.902  1.00 15.70 ?  203 ASP B CB  1 
ATOM   4693 C CG  . ASP B 1 203 ? 8.425   -17.476 28.629  1.00 18.34 ?  203 ASP B CG  1 
ATOM   4694 O OD1 . ASP B 1 203 ? 8.447   -18.564 28.006  1.00 16.92 ?  203 ASP B OD1 1 
ATOM   4695 O OD2 . ASP B 1 203 ? 9.053   -16.466 28.265  1.00 18.18 -1 203 ASP B OD2 1 
ATOM   4696 N N   . LEU B 1 204 ? 4.351   -17.442 31.153  1.00 11.63 ?  204 LEU B N   1 
ATOM   4697 C CA  . LEU B 1 204 ? 3.675   -17.049 32.380  1.00 14.55 ?  204 LEU B CA  1 
ATOM   4698 C C   . LEU B 1 204 ? 2.414   -17.869 32.621  1.00 15.31 ?  204 LEU B C   1 
ATOM   4699 O O   . LEU B 1 204 ? 1.460   -17.391 33.236  1.00 14.58 ?  204 LEU B O   1 
ATOM   4700 C CB  . LEU B 1 204 ? 3.358   -15.553 32.366  1.00 14.61 ?  204 LEU B CB  1 
ATOM   4701 C CG  . LEU B 1 204 ? 4.601   -14.658 32.447  1.00 14.98 ?  204 LEU B CG  1 
ATOM   4702 C CD1 . LEU B 1 204 ? 4.278   -13.208 32.153  1.00 14.73 ?  204 LEU B CD1 1 
ATOM   4703 C CD2 . LEU B 1 204 ? 5.236   -14.789 33.820  1.00 15.13 ?  204 LEU B CD2 1 
ATOM   4704 N N   . VAL B 1 205 ? 2.401   -19.113 32.150  1.00 14.13 ?  205 VAL B N   1 
ATOM   4705 C CA  . VAL B 1 205 ? 1.320   -20.013 32.513  1.00 15.06 ?  205 VAL B CA  1 
ATOM   4706 C C   . VAL B 1 205 ? 1.541   -20.456 33.949  1.00 16.26 ?  205 VAL B C   1 
ATOM   4707 O O   . VAL B 1 205 ? 2.638   -20.894 34.321  1.00 18.73 ?  205 VAL B O   1 
ATOM   4708 C CB  . VAL B 1 205 ? 1.249   -21.200 31.539  1.00 17.77 ?  205 VAL B CB  1 
ATOM   4709 C CG1 . VAL B 1 205 ? 0.070   -22.084 31.889  1.00 20.41 ?  205 VAL B CG1 1 
ATOM   4710 C CG2 . VAL B 1 205 ? 1.123   -20.694 30.095  1.00 16.04 ?  205 VAL B CG2 1 
ATOM   4711 N N   . LEU B 1 206 ? 0.515   -20.291 34.783  1.00 16.19 ?  206 LEU B N   1 
ATOM   4712 C CA  . LEU B 1 206 ? 0.674   -20.474 36.221  1.00 19.17 ?  206 LEU B CA  1 
ATOM   4713 C C   . LEU B 1 206 ? 0.192   -21.828 36.718  1.00 22.66 ?  206 LEU B C   1 
ATOM   4714 O O   . LEU B 1 206 ? 0.566   -22.237 37.825  1.00 24.05 ?  206 LEU B O   1 
ATOM   4715 C CB  . LEU B 1 206 ? -0.056  -19.359 36.972  1.00 16.83 ?  206 LEU B CB  1 
ATOM   4716 C CG  . LEU B 1 206 ? 0.464   -17.957 36.661  1.00 16.93 ?  206 LEU B CG  1 
ATOM   4717 C CD1 . LEU B 1 206 ? -0.154  -16.931 37.588  1.00 16.20 ?  206 LEU B CD1 1 
ATOM   4718 C CD2 . LEU B 1 206 ? 2.001   -17.915 36.734  1.00 17.21 ?  206 LEU B CD2 1 
ATOM   4719 N N   . THR B 1 207 ? -0.617  -22.527 35.940  1.00 22.98 ?  207 THR B N   1 
ATOM   4720 C CA  . THR B 1 207 ? -1.067  -23.862 36.294  1.00 23.10 ?  207 THR B CA  1 
ATOM   4721 C C   . THR B 1 207 ? -0.051  -24.866 35.771  1.00 27.39 ?  207 THR B C   1 
ATOM   4722 O O   . THR B 1 207 ? 1.022   -24.492 35.291  1.00 28.08 ?  207 THR B O   1 
ATOM   4723 C CB  . THR B 1 207 ? -2.458  -24.116 35.727  1.00 21.41 ?  207 THR B CB  1 
ATOM   4724 O OG1 . THR B 1 207 ? -2.372  -24.209 34.297  1.00 23.82 ?  207 THR B OG1 1 
ATOM   4725 C CG2 . THR B 1 207 ? -3.396  -22.981 36.105  1.00 24.74 ?  207 THR B CG2 1 
ATOM   4726 N N   . ASP B 1 208 ? -0.377  -26.156 35.843  1.00 26.12 ?  208 ASP B N   1 
ATOM   4727 C CA  . ASP B 1 208 ? 0.504   -27.166 35.268  1.00 28.98 ?  208 ASP B CA  1 
ATOM   4728 C C   . ASP B 1 208 ? 0.291   -27.331 33.776  1.00 27.98 ?  208 ASP B C   1 
ATOM   4729 O O   . ASP B 1 208 ? 0.995   -28.128 33.143  1.00 31.23 ?  208 ASP B O   1 
ATOM   4730 C CB  . ASP B 1 208 ? 0.315   -28.507 35.975  1.00 32.40 ?  208 ASP B CB  1 
ATOM   4731 C CG  . ASP B 1 208 ? 1.015   -28.547 37.314  1.00 35.43 ?  208 ASP B CG  1 
ATOM   4732 O OD1 . ASP B 1 208 ? 1.680   -27.544 37.664  1.00 41.12 ?  208 ASP B OD1 1 
ATOM   4733 O OD2 . ASP B 1 208 ? 0.901   -29.573 38.014  1.00 36.32 -1 208 ASP B OD2 1 
ATOM   4734 N N   . GLU B 1 209 ? -0.665  -26.604 33.206  1.00 24.11 ?  209 GLU B N   1 
ATOM   4735 C CA  . GLU B 1 209 ? -0.781  -26.537 31.764  1.00 24.54 ?  209 GLU B CA  1 
ATOM   4736 C C   . GLU B 1 209 ? 0.371   -25.707 31.198  1.00 25.97 ?  209 GLU B C   1 
ATOM   4737 O O   . GLU B 1 209 ? 1.170   -25.104 31.925  1.00 25.75 ?  209 GLU B O   1 
ATOM   4738 C CB  . GLU B 1 209 ? -2.137  -25.956 31.370  1.00 23.78 ?  209 GLU B CB  1 
ATOM   4739 C CG  . GLU B 1 209 ? -3.303  -26.652 32.067  1.00 33.33 ?  209 GLU B CG  1 
ATOM   4740 C CD  . GLU B 1 209 ? -4.553  -25.802 32.155  1.00 34.95 ?  209 GLU B CD  1 
ATOM   4741 O OE1 . GLU B 1 209 ? -4.514  -24.726 32.803  1.00 32.15 ?  209 GLU B OE1 1 
ATOM   4742 O OE2 . GLU B 1 209 ? -5.580  -26.217 31.575  1.00 39.63 -1 209 GLU B OE2 1 
ATOM   4743 N N   . ASP B 1 210 ? 0.474   -25.695 29.880  1.00 24.46 ?  210 ASP B N   1 
ATOM   4744 C CA  . ASP B 1 210 ? 1.553   -24.951 29.266  1.00 23.68 ?  210 ASP B CA  1 
ATOM   4745 C C   . ASP B 1 210 ? 1.086   -24.431 27.921  1.00 20.46 ?  210 ASP B C   1 
ATOM   4746 O O   . ASP B 1 210 ? 0.042   -24.834 27.400  1.00 21.20 ?  210 ASP B O   1 
ATOM   4747 C CB  . ASP B 1 210 ? 2.810   -25.809 29.128  1.00 25.37 ?  210 ASP B CB  1 
ATOM   4748 C CG  . ASP B 1 210 ? 4.069   -24.976 28.949  1.00 27.09 ?  210 ASP B CG  1 
ATOM   4749 O OD1 . ASP B 1 210 ? 4.056   -23.765 29.267  1.00 30.31 ?  210 ASP B OD1 1 
ATOM   4750 O OD2 . ASP B 1 210 ? 5.079   -25.544 28.499  1.00 31.70 -1 210 ASP B OD2 1 
ATOM   4751 N N   . ILE B 1 211 ? 1.892   -23.533 27.397  1.00 21.79 ?  211 ILE B N   1 
ATOM   4752 C CA  . ILE B 1 211 ? 1.604   -22.965 26.072  1.00 19.28 ?  211 ILE B CA  1 
ATOM   4753 C C   . ILE B 1 211 ? 1.796   -24.003 24.991  1.00 21.59 ?  211 ILE B C   1 
ATOM   4754 O O   . ILE B 1 211 ? 2.660   -24.861 25.145  1.00 22.07 ?  211 ILE B O   1 
ATOM   4755 C CB  . ILE B 1 211 ? 2.583   -21.802 25.797  1.00 22.12 ?  211 ILE B CB  1 
ATOM   4756 C CG1 . ILE B 1 211 ? 2.429   -21.207 24.403  1.00 22.73 ?  211 ILE B CG1 1 
ATOM   4757 C CG2 . ILE B 1 211 ? 4.019   -22.206 26.029  1.00 19.98 ?  211 ILE B CG2 1 
ATOM   4758 C CD1 . ILE B 1 211 ? 1.447   -20.124 24.381  1.00 24.07 ?  211 ILE B CD1 1 
ATOM   4759 N N   . THR B 1 212 ? 0.916   -24.001 24.010  1.00 17.84 ?  212 THR B N   1 
ATOM   4760 C CA  . THR B 1 212 ? 1.207   -24.681 22.756  1.00 17.53 ?  212 THR B CA  1 
ATOM   4761 C C   . THR B 1 212 ? 1.618   -23.614 21.753  1.00 16.92 ?  212 THR B C   1 
ATOM   4762 O O   . THR B 1 212 ? 0.763   -22.828 21.316  1.00 16.65 ?  212 THR B O   1 
ATOM   4763 C CB  . THR B 1 212 ? -0.005  -25.464 22.249  1.00 17.83 ?  212 THR B CB  1 
ATOM   4764 O OG1 . THR B 1 212 ? -0.331  -26.516 23.181  1.00 17.62 ?  212 THR B OG1 1 
ATOM   4765 C CG2 . THR B 1 212 ? 0.287   -26.074 20.862  1.00 17.64 ?  212 THR B CG2 1 
ATOM   4766 N N   . PRO B 1 213 ? 2.897   -23.490 21.412  1.00 15.29 ?  213 PRO B N   1 
ATOM   4767 C CA  . PRO B 1 213 ? 3.285   -22.490 20.414  1.00 14.71 ?  213 PRO B CA  1 
ATOM   4768 C C   . PRO B 1 213 ? 2.738   -22.862 19.050  1.00 15.21 ?  213 PRO B C   1 
ATOM   4769 O O   . PRO B 1 213 ? 2.616   -24.038 18.707  1.00 13.83 ?  213 PRO B O   1 
ATOM   4770 C CB  . PRO B 1 213 ? 4.819   -22.544 20.429  1.00 15.07 ?  213 PRO B CB  1 
ATOM   4771 C CG  . PRO B 1 213 ? 5.174   -23.166 21.761  1.00 18.77 ?  213 PRO B CG  1 
ATOM   4772 C CD  . PRO B 1 213 ? 4.068   -24.160 22.007  1.00 16.88 ?  213 PRO B CD  1 
ATOM   4773 N N   . ALA B 1 214 ? 2.402   -21.840 18.262  1.00 16.81 ?  214 ALA B N   1 
ATOM   4774 C CA  . ALA B 1 214 ? 1.858   -22.122 16.939  1.00 16.09 ?  214 ALA B CA  1 
ATOM   4775 C C   . ALA B 1 214 ? 2.868   -22.864 16.062  1.00 15.67 ?  214 ALA B C   1 
ATOM   4776 O O   . ALA B 1 214 ? 2.473   -23.670 15.205  1.00 17.09 ?  214 ALA B O   1 
ATOM   4777 C CB  . ALA B 1 214 ? 1.409   -20.826 16.273  1.00 15.99 ?  214 ALA B CB  1 
ATOM   4778 N N   . PHE B 1 215 ? 4.168   -22.624 16.260  1.00 15.70 ?  215 PHE B N   1 
ATOM   4779 C CA  . PHE B 1 215 ? 5.151   -23.293 15.415  1.00 17.36 ?  215 PHE B CA  1 
ATOM   4780 C C   . PHE B 1 215 ? 5.200   -24.809 15.611  1.00 15.78 ?  215 PHE B C   1 
ATOM   4781 O O   . PHE B 1 215 ? 5.845   -25.486 14.803  1.00 18.02 ?  215 PHE B O   1 
ATOM   4782 C CB  . PHE B 1 215 ? 6.557   -22.683 15.604  1.00 16.18 ?  215 PHE B CB  1 
ATOM   4783 C CG  . PHE B 1 215 ? 7.154   -22.860 16.983  1.00 18.00 ?  215 PHE B CG  1 
ATOM   4784 C CD1 . PHE B 1 215 ? 7.663   -24.090 17.394  1.00 16.68 ?  215 PHE B CD1 1 
ATOM   4785 C CD2 . PHE B 1 215 ? 7.269   -21.778 17.842  1.00 17.57 ?  215 PHE B CD2 1 
ATOM   4786 C CE1 . PHE B 1 215 ? 8.230   -24.245 18.649  1.00 17.69 ?  215 PHE B CE1 1 
ATOM   4787 C CE2 . PHE B 1 215 ? 7.855   -21.926 19.093  1.00 16.21 ?  215 PHE B CE2 1 
ATOM   4788 C CZ  . PHE B 1 215 ? 8.330   -23.164 19.496  1.00 15.80 ?  215 PHE B CZ  1 
ATOM   4789 N N   . THR B 1 216 ? 4.535   -25.367 16.631  1.00 15.96 ?  216 THR B N   1 
ATOM   4790 C CA  . THR B 1 216 ? 4.535   -26.817 16.825  1.00 16.12 ?  216 THR B CA  1 
ATOM   4791 C C   . THR B 1 216 ? 3.442   -27.542 16.050  1.00 19.03 ?  216 THR B C   1 
ATOM   4792 O O   . THR B 1 216 ? 3.434   -28.776 16.056  1.00 19.56 ?  216 THR B O   1 
ATOM   4793 C CB  . THR B 1 216 ? 4.381   -27.178 18.318  1.00 19.65 ?  216 THR B CB  1 
ATOM   4794 O OG1 . THR B 1 216 ? 3.074   -26.804 18.764  1.00 17.33 ?  216 THR B OG1 1 
ATOM   4795 C CG2 . THR B 1 216 ? 5.434   -26.481 19.164  1.00 18.78 ?  216 THR B CG2 1 
ATOM   4796 N N   . VAL B 1 217 ? 2.506   -26.826 15.408  1.00 17.00 ?  217 VAL B N   1 
ATOM   4797 C CA  . VAL B 1 217 ? 1.439   -27.506 14.656  1.00 20.21 ?  217 VAL B CA  1 
ATOM   4798 C C   . VAL B 1 217 ? 2.040   -28.256 13.466  1.00 20.51 ?  217 VAL B C   1 
ATOM   4799 O O   . VAL B 1 217 ? 3.125   -27.935 12.975  1.00 19.11 ?  217 VAL B O   1 
ATOM   4800 C CB  . VAL B 1 217 ? 0.357   -26.506 14.207  1.00 19.16 ?  217 VAL B CB  1 
ATOM   4801 C CG1 . VAL B 1 217 ? -0.078  -25.656 15.387  1.00 17.75 ?  217 VAL B CG1 1 
ATOM   4802 C CG2 . VAL B 1 217 ? 0.865   -25.596 13.072  1.00 18.59 ?  217 VAL B CG2 1 
ATOM   4803 N N   . ASP B 1 218 ? 1.333   -29.289 13.011  1.00 22.47 ?  218 ASP B N   1 
ATOM   4804 C CA  . ASP B 1 218 ? 1.900   -30.142 11.973  1.00 24.13 ?  218 ASP B CA  1 
ATOM   4805 C C   . ASP B 1 218 ? 1.953   -29.413 10.627  1.00 22.95 ?  218 ASP B C   1 
ATOM   4806 O O   . ASP B 1 218 ? 1.289   -28.400 10.405  1.00 24.31 ?  218 ASP B O   1 
ATOM   4807 C CB  . ASP B 1 218 ? 1.106   -31.442 11.837  1.00 28.42 ?  218 ASP B CB  1 
ATOM   4808 C CG  . ASP B 1 218 ? 0.911   -32.153 13.163  1.00 32.27 ?  218 ASP B CG  1 
ATOM   4809 O OD1 . ASP B 1 218 ? 1.842   -32.141 13.999  1.00 38.15 ?  218 ASP B OD1 1 
ATOM   4810 O OD2 . ASP B 1 218 ? -0.169  -32.745 13.361  1.00 41.99 -1 218 ASP B OD2 1 
ATOM   4811 N N   . TRP B 1 219 ? 2.735   -29.979 9.707   1.00 25.73 ?  219 TRP B N   1 
ATOM   4812 C CA  . TRP B 1 219 ? 3.091   -29.324 8.452   1.00 26.58 ?  219 TRP B CA  1 
ATOM   4813 C C   . TRP B 1 219 ? 1.933   -29.132 7.476   1.00 29.29 ?  219 TRP B C   1 
ATOM   4814 O O   . TRP B 1 219 ? 2.091   -28.372 6.516   1.00 31.37 ?  219 TRP B O   1 
ATOM   4815 C CB  . TRP B 1 219 ? 4.199   -30.104 7.769   1.00 26.24 ?  219 TRP B CB  1 
ATOM   4816 C CG  . TRP B 1 219 ? 5.525   -29.778 8.330   1.00 25.99 ?  219 TRP B CG  1 
ATOM   4817 C CD1 . TRP B 1 219 ? 6.304   -30.581 9.108   1.00 28.19 ?  219 TRP B CD1 1 
ATOM   4818 C CD2 . TRP B 1 219 ? 6.245   -28.551 8.167   1.00 26.68 ?  219 TRP B CD2 1 
ATOM   4819 N NE1 . TRP B 1 219 ? 7.473   -29.936 9.433   1.00 28.54 ?  219 TRP B NE1 1 
ATOM   4820 C CE2 . TRP B 1 219 ? 7.462   -28.688 8.871   1.00 28.08 ?  219 TRP B CE2 1 
ATOM   4821 C CE3 . TRP B 1 219 ? 5.983   -27.353 7.494   1.00 25.59 ?  219 TRP B CE3 1 
ATOM   4822 C CZ2 . TRP B 1 219 ? 8.413   -27.675 8.920   1.00 28.07 ?  219 TRP B CZ2 1 
ATOM   4823 C CZ3 . TRP B 1 219 ? 6.933   -26.344 7.543   1.00 23.88 ?  219 TRP B CZ3 1 
ATOM   4824 C CH2 . TRP B 1 219 ? 8.132   -26.513 8.254   1.00 24.21 ?  219 TRP B CH2 1 
ATOM   4825 N N   . ASP B 1 220 ? 0.782   -29.771 7.676   1.00 29.87 ?  220 ASP B N   1 
ATOM   4826 C CA  . ASP B 1 220 ? -0.393  -29.336 6.920   1.00 34.00 ?  220 ASP B CA  1 
ATOM   4827 C C   . ASP B 1 220 ? -0.658  -27.841 7.110   1.00 35.37 ?  220 ASP B C   1 
ATOM   4828 O O   . ASP B 1 220 ? -1.228  -27.188 6.225   1.00 40.04 ?  220 ASP B O   1 
ATOM   4829 C CB  . ASP B 1 220 ? -1.644  -30.120 7.343   1.00 39.21 ?  220 ASP B CB  1 
ATOM   4830 C CG  . ASP B 1 220 ? -1.396  -31.616 7.481   1.00 43.65 ?  220 ASP B CG  1 
ATOM   4831 O OD1 . ASP B 1 220 ? -0.421  -32.003 8.164   1.00 44.05 ?  220 ASP B OD1 1 
ATOM   4832 O OD2 . ASP B 1 220 ? -2.188  -32.405 6.916   1.00 47.26 -1 220 ASP B OD2 1 
ATOM   4833 N N   . ALA B 1 221 ? -0.242  -27.287 8.250   1.00 24.09 ?  221 ALA B N   1 
ATOM   4834 C CA  . ALA B 1 221 ? -0.618  -25.949 8.684   1.00 19.97 ?  221 ALA B CA  1 
ATOM   4835 C C   . ALA B 1 221 ? 0.560   -25.116 9.153   1.00 18.76 ?  221 ALA B C   1 
ATOM   4836 O O   . ALA B 1 221 ? 0.436   -23.885 9.216   1.00 15.88 ?  221 ALA B O   1 
ATOM   4837 C CB  . ALA B 1 221 ? -1.644  -26.026 9.826   1.00 23.49 ?  221 ALA B CB  1 
ATOM   4838 N N   . LYS B 1 222 ? 1.697   -25.738 9.477   1.00 19.39 ?  222 LYS B N   1 
ATOM   4839 C CA  . LYS B 1 222 ? 2.832   -25.005 10.018  1.00 17.75 ?  222 LYS B CA  1 
ATOM   4840 C C   . LYS B 1 222 ? 3.360   -23.970 9.041   1.00 16.68 ?  222 LYS B C   1 
ATOM   4841 O O   . LYS B 1 222 ? 4.050   -23.036 9.457   1.00 16.03 ?  222 LYS B O   1 
ATOM   4842 C CB  . LYS B 1 222 ? 3.951   -25.973 10.415  1.00 19.16 ?  222 LYS B CB  1 
ATOM   4843 C CG  . LYS B 1 222 ? 4.886   -25.438 11.504  1.00 18.62 ?  222 LYS B CG  1 
ATOM   4844 C CD  . LYS B 1 222 ? 6.224   -26.164 11.513  1.00 19.38 ?  222 LYS B CD  1 
ATOM   4845 C CE  . LYS B 1 222 ? 6.095   -27.623 11.940  1.00 20.27 ?  222 LYS B CE  1 
ATOM   4846 N NZ  . LYS B 1 222 ? 5.837   -27.787 13.401  1.00 18.56 1  222 LYS B NZ  1 
ATOM   4847 N N   . ASN B 1 223 ? 3.039   -24.095 7.756   1.00 18.83 ?  223 ASN B N   1 
ATOM   4848 C CA  . ASN B 1 223 ? 3.527   -23.115 6.798   1.00 16.63 ?  223 ASN B CA  1 
ATOM   4849 C C   . ASN B 1 223 ? 2.741   -21.818 6.812   1.00 17.58 ?  223 ASN B C   1 
ATOM   4850 O O   . ASN B 1 223 ? 3.059   -20.928 6.017   1.00 12.98 ?  223 ASN B O   1 
ATOM   4851 C CB  . ASN B 1 223 ? 3.512   -23.691 5.391   1.00 19.64 ?  223 ASN B CB  1 
ATOM   4852 C CG  . ASN B 1 223 ? 4.855   -24.224 5.003   1.00 25.66 ?  223 ASN B CG  1 
ATOM   4853 O OD1 . ASN B 1 223 ? 5.782   -23.457 4.742   1.00 25.16 ?  223 ASN B OD1 1 
ATOM   4854 N ND2 . ASN B 1 223 ? 4.985   -25.544 4.989   1.00 26.07 ?  223 ASN B ND2 1 
ATOM   4855 N N   . TRP B 1 224 ? 1.736   -21.694 7.683   1.00 15.59 ?  224 TRP B N   1 
ATOM   4856 C CA  . TRP B 1 224 ? 0.878   -20.515 7.741   1.00 15.75 ?  224 TRP B CA  1 
ATOM   4857 C C   . TRP B 1 224 ? 0.974   -19.789 9.075   1.00 15.83 ?  224 TRP B C   1 
ATOM   4858 O O   . TRP B 1 224 ? 0.134   -18.933 9.362   1.00 18.63 ?  224 TRP B O   1 
ATOM   4859 C CB  . TRP B 1 224 ? -0.578  -20.903 7.467   1.00 15.49 ?  224 TRP B CB  1 
ATOM   4860 C CG  . TRP B 1 224 ? -0.774  -21.410 6.079   1.00 16.25 ?  224 TRP B CG  1 
ATOM   4861 C CD1 . TRP B 1 224 ? -0.639  -22.695 5.639   1.00 18.06 ?  224 TRP B CD1 1 
ATOM   4862 C CD2 . TRP B 1 224 ? -1.110  -20.623 4.931   1.00 17.87 ?  224 TRP B CD2 1 
ATOM   4863 N NE1 . TRP B 1 224 ? -0.889  -22.756 4.289   1.00 18.80 ?  224 TRP B NE1 1 
ATOM   4864 C CE2 . TRP B 1 224 ? -1.168  -21.495 3.830   1.00 19.12 ?  224 TRP B CE2 1 
ATOM   4865 C CE3 . TRP B 1 224 ? -1.367  -19.263 4.734   1.00 17.03 ?  224 TRP B CE3 1 
ATOM   4866 C CZ2 . TRP B 1 224 ? -1.485  -21.058 2.552   1.00 18.67 ?  224 TRP B CZ2 1 
ATOM   4867 C CZ3 . TRP B 1 224 ? -1.668  -18.826 3.454   1.00 17.57 ?  224 TRP B CZ3 1 
ATOM   4868 C CH2 . TRP B 1 224 ? -1.721  -19.722 2.382   1.00 19.50 ?  224 TRP B CH2 1 
ATOM   4869 N N   . VAL B 1 225 ? 1.969   -20.102 9.903   1.00 14.41 ?  225 VAL B N   1 
ATOM   4870 C CA  . VAL B 1 225 ? 2.010   -19.568 11.261  1.00 13.46 ?  225 VAL B CA  1 
ATOM   4871 C C   . VAL B 1 225 ? 3.276   -18.746 11.486  1.00 13.11 ?  225 VAL B C   1 
ATOM   4872 O O   . VAL B 1 225 ? 4.336   -18.980 10.892  1.00 13.00 ?  225 VAL B O   1 
ATOM   4873 C CB  . VAL B 1 225 ? 1.884   -20.679 12.341  1.00 15.20 ?  225 VAL B CB  1 
ATOM   4874 C CG1 . VAL B 1 225 ? 0.683   -21.569 12.051  1.00 14.95 ?  225 VAL B CG1 1 
ATOM   4875 C CG2 . VAL B 1 225 ? 3.170   -21.501 12.456  1.00 14.98 ?  225 VAL B CG2 1 
ATOM   4876 N N   . VAL B 1 226 ? 3.133   -17.750 12.358  1.00 13.30 ?  226 VAL B N   1 
ATOM   4877 C CA  . VAL B 1 226 ? 4.226   -16.967 12.916  1.00 12.51 ?  226 VAL B CA  1 
ATOM   4878 C C   . VAL B 1 226 ? 4.016   -16.955 14.428  1.00 13.86 ?  226 VAL B C   1 
ATOM   4879 O O   . VAL B 1 226 ? 2.933   -16.587 14.902  1.00 16.28 ?  226 VAL B O   1 
ATOM   4880 C CB  . VAL B 1 226 ? 4.265   -15.526 12.364  1.00 16.41 ?  226 VAL B CB  1 
ATOM   4881 C CG1 . VAL B 1 226 ? 5.352   -14.702 13.069  1.00 13.89 ?  226 VAL B CG1 1 
ATOM   4882 C CG2 . VAL B 1 226 ? 4.490   -15.516 10.842  1.00 15.09 ?  226 VAL B CG2 1 
ATOM   4883 N N   . SER B 1 227 ? 5.018   -17.404 15.176  1.00 14.43 ?  227 SER B N   1 
ATOM   4884 C CA  . SER B 1 227 ? 5.058   -17.281 16.631  1.00 16.66 ?  227 SER B CA  1 
ATOM   4885 C C   . SER B 1 227 ? 5.921   -16.081 17.008  1.00 14.78 ?  227 SER B C   1 
ATOM   4886 O O   . SER B 1 227 ? 7.034   -15.928 16.497  1.00 16.93 ?  227 SER B O   1 
ATOM   4887 C CB  . SER B 1 227 ? 5.608   -18.560 17.280  1.00 15.26 ?  227 SER B CB  1 
ATOM   4888 O OG  . SER B 1 227 ? 4.653   -19.607 17.242  1.00 16.30 ?  227 SER B OG  1 
ATOM   4889 N N   . LEU B 1 228 ? 5.406   -15.217 17.877  1.00 13.26 ?  228 LEU B N   1 
ATOM   4890 C CA  . LEU B 1 228 ? 6.168   -14.070 18.356  1.00 14.96 ?  228 LEU B CA  1 
ATOM   4891 C C   . LEU B 1 228 ? 6.401   -14.242 19.846  1.00 12.59 ?  228 LEU B C   1 
ATOM   4892 O O   . LEU B 1 228 ? 5.440   -14.414 20.601  1.00 14.42 ?  228 LEU B O   1 
ATOM   4893 C CB  . LEU B 1 228 ? 5.431   -12.756 18.093  1.00 14.01 ?  228 LEU B CB  1 
ATOM   4894 C CG  . LEU B 1 228 ? 5.198   -12.475 16.610  1.00 16.04 ?  228 LEU B CG  1 
ATOM   4895 C CD1 . LEU B 1 228 ? 4.189   -11.354 16.437  1.00 14.80 ?  228 LEU B CD1 1 
ATOM   4896 C CD2 . LEU B 1 228 ? 6.513   -12.114 15.939  1.00 17.35 ?  228 LEU B CD2 1 
ATOM   4897 N N   . ILE B 1 229 ? 7.672   -14.204 20.230  1.00 13.13 ?  229 ILE B N   1 
ATOM   4898 C CA  . ILE B 1 229 ? 8.065   -14.291 21.656  1.00 14.62 ?  229 ILE B CA  1 
ATOM   4899 C C   . ILE B 1 229 ? 8.982   -13.125 22.014  1.00 14.63 ?  229 ILE B C   1 
ATOM   4900 O O   . ILE B 1 229 ? 9.496   -12.487 21.116  1.00 14.59 ?  229 ILE B O   1 
ATOM   4901 C CB  . ILE B 1 229 ? 8.735   -15.637 21.985  1.00 14.36 ?  229 ILE B CB  1 
ATOM   4902 C CG1 . ILE B 1 229 ? 10.106  -15.797 21.328  1.00 16.71 ?  229 ILE B CG1 1 
ATOM   4903 C CG2 . ILE B 1 229 ? 7.819   -16.812 21.684  1.00 17.12 ?  229 ILE B CG2 1 
ATOM   4904 C CD1 . ILE B 1 229 ? 10.913  -16.905 21.940  1.00 17.91 ?  229 ILE B CD1 1 
ATOM   4905 N N   . SER B 1 230 ? 9.194   -12.945 23.307  1.00 14.02 ?  230 SER B N   1 
ATOM   4906 C CA  . SER B 1 230 ? 10.031  -11.861 23.802  1.00 15.24 ?  230 SER B CA  1 
ATOM   4907 C C   . SER B 1 230 ? 10.311  -12.122 25.268  1.00 15.26 ?  230 SER B C   1 
ATOM   4908 O O   . SER B 1 230 ? 9.467   -12.695 25.955  1.00 14.95 ?  230 SER B O   1 
ATOM   4909 C CB  . SER B 1 230 ? 9.340   -10.497 23.636  1.00 17.96 ?  230 SER B CB  1 
ATOM   4910 O OG  . SER B 1 230 ? 10.110  -9.457  24.216  1.00 17.04 ?  230 SER B OG  1 
ATOM   4911 N N   . PRO B 1 231 ? 11.469  -11.716 25.780  1.00 15.84 ?  231 PRO B N   1 
ATOM   4912 C CA  . PRO B 1 231 ? 11.682  -11.773 27.229  1.00 15.30 ?  231 PRO B CA  1 
ATOM   4913 C C   . PRO B 1 231 ? 10.992  -10.653 27.990  1.00 16.70 ?  231 PRO B C   1 
ATOM   4914 O O   . PRO B 1 231 ? 11.098  -10.612 29.220  1.00 15.44 ?  231 PRO B O   1 
ATOM   4915 C CB  . PRO B 1 231 ? 13.205  -11.659 27.352  1.00 17.25 ?  231 PRO B CB  1 
ATOM   4916 C CG  . PRO B 1 231 ? 13.600  -10.842 26.168  1.00 17.71 ?  231 PRO B CG  1 
ATOM   4917 C CD  . PRO B 1 231 ? 12.660  -11.240 25.057  1.00 15.68 ?  231 PRO B CD  1 
ATOM   4918 N N   . SER B 1 232 ? 10.333  -9.731  27.288  1.00 15.65 ?  232 SER B N   1 
ATOM   4919 C CA  . SER B 1 232 ? 9.777   -8.481  27.871  1.00 18.26 ?  232 SER B CA  1 
ATOM   4920 C C   . SER B 1 232 ? 8.812   -8.731  29.020  1.00 15.19 ?  232 SER B C   1 
ATOM   4921 O O   . SER B 1 232 ? 9.011   -8.201  30.098  1.00 16.63 ?  232 SER B O   1 
ATOM   4922 C CB  . SER B 1 232 ? 9.143   -7.609  26.791  1.00 20.90 ?  232 SER B CB  1 
ATOM   4923 O OG  . SER B 1 232 ? 7.881   -8.074  26.400  1.00 24.75 ?  232 SER B OG  1 
ATOM   4924 N N   . LYS B 1 233 ? 7.752   -9.456  28.715  1.00 15.94 ?  233 LYS B N   1 
ATOM   4925 C CA  . LYS B 1 233 ? 6.758   -9.692  29.766  1.00 17.88 ?  233 LYS B CA  1 
ATOM   4926 C C   . LYS B 1 233 ? 7.308   -10.606 30.850  1.00 14.43 ?  233 LYS B C   1 
ATOM   4927 O O   . LYS B 1 233 ? 7.119   -10.347 32.041  1.00 15.17 ?  233 LYS B O   1 
ATOM   4928 C CB  . LYS B 1 233 ? 5.479   -10.299 29.197  1.00 15.10 ?  233 LYS B CB  1 
ATOM   4929 C CG  . LYS B 1 233 ? 4.606   -9.354  28.469  1.00 21.52 ?  233 LYS B CG  1 
ATOM   4930 C CD  . LYS B 1 233 ? 3.849   -8.453  29.417  1.00 21.66 ?  233 LYS B CD  1 
ATOM   4931 C CE  . LYS B 1 233 ? 3.369   -7.274  28.625  1.00 27.47 ?  233 LYS B CE  1 
ATOM   4932 N NZ  . LYS B 1 233 ? 3.037   -7.832  27.263  1.00 29.70 1  233 LYS B NZ  1 
ATOM   4933 N N   . THR B 1 234 ? 7.969   -11.696 30.451  1.00 13.51 ?  234 THR B N   1 
ATOM   4934 C CA  . THR B 1 234 ? 8.455   -12.683 31.413  1.00 14.28 ?  234 THR B CA  1 
ATOM   4935 C C   . THR B 1 234 ? 9.404   -12.074 32.436  1.00 15.17 ?  234 THR B C   1 
ATOM   4936 O O   . THR B 1 234 ? 9.359   -12.432 33.620  1.00 15.42 ?  234 THR B O   1 
ATOM   4937 C CB  . THR B 1 234 ? 9.168   -13.817 30.677  1.00 16.00 ?  234 THR B CB  1 
ATOM   4938 O OG1 . THR B 1 234 ? 8.350   -14.281 29.600  1.00 14.08 ?  234 THR B OG1 1 
ATOM   4939 C CG2 . THR B 1 234 ? 9.504   -14.967 31.640  1.00 16.26 ?  234 THR B CG2 1 
ATOM   4940 N N   . PHE B 1 235 ? 10.304  -11.184 31.995  1.00 15.51 ?  235 PHE B N   1 
ATOM   4941 C CA  . PHE B 1 235 ? 11.447  -10.780 32.811  1.00 13.30 ?  235 PHE B CA  1 
ATOM   4942 C C   . PHE B 1 235 ? 11.428  -9.303  33.181  1.00 13.72 ?  235 PHE B C   1 
ATOM   4943 O O   . PHE B 1 235 ? 12.403  -8.816  33.758  1.00 12.13 ?  235 PHE B O   1 
ATOM   4944 C CB  . PHE B 1 235 ? 12.758  -11.130 32.091  1.00 12.91 ?  235 PHE B CB  1 
ATOM   4945 C CG  . PHE B 1 235 ? 12.979  -12.604 31.954  1.00 14.69 ?  235 PHE B CG  1 
ATOM   4946 C CD1 . PHE B 1 235 ? 13.366  -13.359 33.044  1.00 16.33 ?  235 PHE B CD1 1 
ATOM   4947 C CD2 . PHE B 1 235 ? 12.733  -13.246 30.755  1.00 12.93 ?  235 PHE B CD2 1 
ATOM   4948 C CE1 . PHE B 1 235 ? 13.546  -14.734 32.915  1.00 16.27 ?  235 PHE B CE1 1 
ATOM   4949 C CE2 . PHE B 1 235 ? 12.908  -14.621 30.631  1.00 14.34 ?  235 PHE B CE2 1 
ATOM   4950 C CZ  . PHE B 1 235 ? 13.321  -15.354 31.701  1.00 16.51 ?  235 PHE B CZ  1 
ATOM   4951 N N   . ASN B 1 236 ? 10.328  -8.594  32.902  1.00 13.01 ?  236 ASN B N   1 
ATOM   4952 C CA  . ASN B 1 236 ? 10.168  -7.168  33.219  1.00 14.02 ?  236 ASN B CA  1 
ATOM   4953 C C   . ASN B 1 236 ? 11.122  -6.302  32.386  1.00 17.42 ?  236 ASN B C   1 
ATOM   4954 O O   . ASN B 1 236 ? 11.839  -5.444  32.915  1.00 14.70 ?  236 ASN B O   1 
ATOM   4955 C CB  . ASN B 1 236 ? 10.343  -6.901  34.719  1.00 13.19 ?  236 ASN B CB  1 
ATOM   4956 C CG  . ASN B 1 236 ? 9.684   -5.604  35.155  1.00 16.51 ?  236 ASN B CG  1 
ATOM   4957 O OD1 . ASN B 1 236 ? 8.817   -5.085  34.457  1.00 15.61 ?  236 ASN B OD1 1 
ATOM   4958 N ND2 . ASN B 1 236 ? 10.071  -5.090  36.321  1.00 16.24 ?  236 ASN B ND2 1 
ATOM   4959 N N   . LEU B 1 237 ? 11.087  -6.500  31.063  1.00 15.45 ?  237 LEU B N   1 
ATOM   4960 C CA  . LEU B 1 237 ? 12.055  -5.917  30.129  1.00 15.18 ?  237 LEU B CA  1 
ATOM   4961 C C   . LEU B 1 237 ? 11.346  -5.258  28.947  1.00 16.89 ?  237 LEU B C   1 
ATOM   4962 O O   . LEU B 1 237 ? 11.808  -5.326  27.802  1.00 13.11 ?  237 LEU B O   1 
ATOM   4963 C CB  . LEU B 1 237 ? 13.045  -6.977  29.634  1.00 13.45 ?  237 LEU B CB  1 
ATOM   4964 C CG  . LEU B 1 237 ? 13.982  -7.608  30.672  1.00 15.28 ?  237 LEU B CG  1 
ATOM   4965 C CD1 . LEU B 1 237 ? 14.816  -8.728  30.034  1.00 14.22 ?  237 LEU B CD1 1 
ATOM   4966 C CD2 . LEU B 1 237 ? 14.895  -6.540  31.271  1.00 15.64 ?  237 LEU B CD2 1 
ATOM   4967 N N   . ALA B 1 238 ? 10.212  -4.617  29.185  1.00 14.20 ?  238 ALA B N   1 
ATOM   4968 C CA  . ALA B 1 238 ? 9.471   -3.984  28.076  1.00 18.79 ?  238 ALA B CA  1 
ATOM   4969 C C   . ALA B 1 238 ? 10.355  -3.006  27.273  1.00 18.47 ?  238 ALA B C   1 
ATOM   4970 O O   . ALA B 1 238 ? 10.230  -2.981  26.058  1.00 19.71 ?  238 ALA B O   1 
ATOM   4971 C CB  . ALA B 1 238 ? 8.265   -3.284  28.613  1.00 18.30 ?  238 ALA B CB  1 
ATOM   4972 N N   . ALA B 1 239 ? 11.176  -2.215  27.958  1.00 15.17 ?  239 ALA B N   1 
ATOM   4973 C CA  . ALA B 1 239 ? 11.995  -1.247  27.233  1.00 16.76 ?  239 ALA B CA  1 
ATOM   4974 C C   . ALA B 1 239 ? 13.303  -1.829  26.708  1.00 17.53 ?  239 ALA B C   1 
ATOM   4975 O O   . ALA B 1 239 ? 14.124  -1.077  26.168  1.00 14.51 ?  239 ALA B O   1 
ATOM   4976 C CB  . ALA B 1 239 ? 12.304  -0.033  28.116  1.00 15.30 ?  239 ALA B CB  1 
ATOM   4977 N N   . LEU B 1 240 ? 13.531  -3.137  26.850  1.00 12.27 ?  240 LEU B N   1 
ATOM   4978 C CA  . LEU B 1 240 ? 14.729  -3.722  26.250  1.00 15.34 ?  240 LEU B CA  1 
ATOM   4979 C C   . LEU B 1 240 ? 14.630  -3.753  24.731  1.00 15.93 ?  240 LEU B C   1 
ATOM   4980 O O   . LEU B 1 240 ? 15.653  -3.648  24.040  1.00 16.52 ?  240 LEU B O   1 
ATOM   4981 C CB  . LEU B 1 240 ? 14.959  -5.133  26.780  1.00 12.84 ?  240 LEU B CB  1 
ATOM   4982 C CG  . LEU B 1 240 ? 16.190  -5.865  26.232  1.00 13.60 ?  240 LEU B CG  1 
ATOM   4983 C CD1 . LEU B 1 240 ? 17.478  -5.158  26.632  1.00 16.35 ?  240 LEU B CD1 1 
ATOM   4984 C CD2 . LEU B 1 240 ? 16.201  -7.335  26.672  1.00 12.86 ?  240 LEU B CD2 1 
ATOM   4985 N N   . HIS B 1 241 ? 13.412  -3.907  24.207  1.00 13.92 ?  241 HIS B N   1 
ATOM   4986 C CA  . HIS B 1 241 ? 13.151  -3.992  22.770  1.00 14.68 ?  241 HIS B CA  1 
ATOM   4987 C C   . HIS B 1 241 ? 13.897  -5.170  22.143  1.00 18.19 ?  241 HIS B C   1 
ATOM   4988 O O   . HIS B 1 241 ? 14.658  -5.029  21.182  1.00 15.32 ?  241 HIS B O   1 
ATOM   4989 C CB  . HIS B 1 241 ? 13.477  -2.673  22.066  1.00 18.20 ?  241 HIS B CB  1 
ATOM   4990 C CG  . HIS B 1 241 ? 12.570  -1.547  22.457  1.00 18.92 ?  241 HIS B CG  1 
ATOM   4991 N ND1 . HIS B 1 241 ? 12.625  -0.304  21.862  1.00 19.22 ?  241 HIS B ND1 1 
ATOM   4992 C CD2 . HIS B 1 241 ? 11.590  -1.472  23.390  1.00 19.16 ?  241 HIS B CD2 1 
ATOM   4993 C CE1 . HIS B 1 241 ? 11.718  0.487   22.413  1.00 20.38 ?  241 HIS B CE1 1 
ATOM   4994 N NE2 . HIS B 1 241 ? 11.077  -0.198  23.343  1.00 20.28 ?  241 HIS B NE2 1 
ATOM   4995 N N   . ALA B 1 242 ? 13.670  -6.356  22.703  1.00 15.17 ?  242 ALA B N   1 
ATOM   4996 C CA  . ALA B 1 242 ? 14.199  -7.594  22.145  1.00 16.18 ?  242 ALA B CA  1 
ATOM   4997 C C   . ALA B 1 242 ? 13.035  -8.557  21.964  1.00 17.08 ?  242 ALA B C   1 
ATOM   4998 O O   . ALA B 1 242 ? 12.269  -8.786  22.901  1.00 16.62 ?  242 ALA B O   1 
ATOM   4999 C CB  . ALA B 1 242 ? 15.281  -8.204  23.045  1.00 16.23 ?  242 ALA B CB  1 
ATOM   5000 N N   . ALA B 1 243 ? 12.875  -9.082  20.755  1.00 14.28 ?  243 ALA B N   1 
ATOM   5001 C CA  . ALA B 1 243 ? 11.827  -10.052 20.472  1.00 14.90 ?  243 ALA B CA  1 
ATOM   5002 C C   . ALA B 1 243 ? 12.354  -11.013 19.424  1.00 16.20 ?  243 ALA B C   1 
ATOM   5003 O O   . ALA B 1 243 ? 13.457  -10.847 18.894  1.00 13.98 ?  243 ALA B O   1 
ATOM   5004 C CB  . ALA B 1 243 ? 10.529  -9.393  19.981  1.00 15.16 ?  243 ALA B CB  1 
ATOM   5005 N N   . CYS B 1 244 ? 11.553  -12.028 19.128  1.00 14.20 ?  244 CYS B N   1 
ATOM   5006 C CA  . CYS B 1 244 ? 11.957  -13.013 18.140  1.00 15.59 ?  244 CYS B CA  1 
ATOM   5007 C C   . CYS B 1 244 ? 10.710  -13.522 17.433  1.00 17.05 ?  244 CYS B C   1 
ATOM   5008 O O   . CYS B 1 244 ? 9.759   -13.943 18.095  1.00 14.38 ?  244 CYS B O   1 
ATOM   5009 C CB  . CYS B 1 244 ? 12.712  -14.166 18.816  1.00 17.28 ?  244 CYS B CB  1 
ATOM   5010 S SG  . CYS B 1 244 ? 13.446  -15.317 17.655  1.00 20.84 ?  244 CYS B SG  1 
ATOM   5011 N N   . ALA B 1 245 ? 10.710  -13.474 16.103  1.00 14.61 ?  245 ALA B N   1 
ATOM   5012 C CA  . ALA B 1 245 ? 9.679   -14.131 15.316  1.00 15.89 ?  245 ALA B CA  1 
ATOM   5013 C C   . ALA B 1 245 ? 10.165  -15.527 14.953  1.00 16.37 ?  245 ALA B C   1 
ATOM   5014 O O   . ALA B 1 245 ? 11.303  -15.699 14.506  1.00 18.93 ?  245 ALA B O   1 
ATOM   5015 C CB  . ALA B 1 245 ? 9.338   -13.335 14.051  1.00 14.35 ?  245 ALA B CB  1 
ATOM   5016 N N   . ILE B 1 246 ? 9.304   -16.521 15.145  1.00 12.82 ?  246 ILE B N   1 
ATOM   5017 C CA  . ILE B 1 246 ? 9.622   -17.907 14.823  1.00 14.92 ?  246 ILE B CA  1 
ATOM   5018 C C   . ILE B 1 246 ? 8.700   -18.302 13.679  1.00 13.67 ?  246 ILE B C   1 
ATOM   5019 O O   . ILE B 1 246 ? 7.482   -18.409 13.857  1.00 14.20 ?  246 ILE B O   1 
ATOM   5020 C CB  . ILE B 1 246 ? 9.461   -18.824 16.044  1.00 15.09 ?  246 ILE B CB  1 
ATOM   5021 C CG1 . ILE B 1 246 ? 10.433  -18.403 17.154  1.00 15.72 ?  246 ILE B CG1 1 
ATOM   5022 C CG2 . ILE B 1 246 ? 9.673   -20.281 15.663  1.00 15.30 ?  246 ILE B CG2 1 
ATOM   5023 C CD1 . ILE B 1 246 ? 10.097  -19.025 18.501  1.00 16.30 ?  246 ILE B CD1 1 
ATOM   5024 N N   . ILE B 1 247 ? 9.277   -18.479 12.497  1.00 12.59 ?  247 ILE B N   1 
ATOM   5025 C CA  . ILE B 1 247 ? 8.528   -18.587 11.250  1.00 12.80 ?  247 ILE B CA  1 
ATOM   5026 C C   . ILE B 1 247 ? 9.028   -19.806 10.486  1.00 14.18 ?  247 ILE B C   1 
ATOM   5027 O O   . ILE B 1 247 ? 10.053  -19.722 9.797   1.00 14.46 ?  247 ILE B O   1 
ATOM   5028 C CB  . ILE B 1 247 ? 8.661   -17.304 10.409  1.00 14.14 ?  247 ILE B CB  1 
ATOM   5029 C CG1 . ILE B 1 247 ? 8.288   -16.077 11.243  1.00 13.02 ?  247 ILE B CG1 1 
ATOM   5030 C CG2 . ILE B 1 247 ? 7.768   -17.372 9.170   1.00 14.13 ?  247 ILE B CG2 1 
ATOM   5031 C CD1 . ILE B 1 247 ? 8.415   -14.745 10.489  1.00 14.92 ?  247 ILE B CD1 1 
ATOM   5032 N N   . PRO B 1 248 ? 8.357   -20.957 10.590  1.00 14.51 ?  248 PRO B N   1 
ATOM   5033 C CA  . PRO B 1 248 ? 8.865   -22.160 9.905   1.00 13.42 ?  248 PRO B CA  1 
ATOM   5034 C C   . PRO B 1 248 ? 8.945   -22.023 8.394   1.00 15.68 ?  248 PRO B C   1 
ATOM   5035 O O   . PRO B 1 248 ? 9.849   -22.592 7.765   1.00 17.04 ?  248 PRO B O   1 
ATOM   5036 C CB  . PRO B 1 248 ? 7.855   -23.235 10.323  1.00 15.11 ?  248 PRO B CB  1 
ATOM   5037 C CG  . PRO B 1 248 ? 7.390   -22.761 11.710  1.00 12.89 ?  248 PRO B CG  1 
ATOM   5038 C CD  . PRO B 1 248 ? 7.304   -21.270 11.575  1.00 14.86 ?  248 PRO B CD  1 
ATOM   5039 N N   . ASN B 1 249 ? 8.003   -21.325 7.795   1.00 11.18 ?  249 ASN B N   1 
ATOM   5040 C CA  . ASN B 1 249 ? 7.959   -21.142 6.340   1.00 15.68 ?  249 ASN B CA  1 
ATOM   5041 C C   . ASN B 1 249 ? 9.165   -20.316 5.913   1.00 13.85 ?  249 ASN B C   1 
ATOM   5042 O O   . ASN B 1 249 ? 9.208   -19.119 6.221   1.00 13.80 ?  249 ASN B O   1 
ATOM   5043 C CB  . ASN B 1 249 ? 6.644   -20.447 5.946   1.00 14.88 ?  249 ASN B CB  1 
ATOM   5044 C CG  . ASN B 1 249 ? 6.497   -20.211 4.427   1.00 16.51 ?  249 ASN B CG  1 
ATOM   5045 O OD1 . ASN B 1 249 ? 7.464   -19.960 3.711   1.00 15.83 ?  249 ASN B OD1 1 
ATOM   5046 N ND2 . ASN B 1 249 ? 5.255   -20.260 3.947   1.00 15.96 ?  249 ASN B ND2 1 
ATOM   5047 N N   . PRO B 1 250 ? 10.129  -20.876 5.169   1.00 17.65 ?  250 PRO B N   1 
ATOM   5048 C CA  . PRO B 1 250 ? 11.371  -20.118 4.907   1.00 15.72 ?  250 PRO B CA  1 
ATOM   5049 C C   . PRO B 1 250 ? 11.151  -18.863 4.080   1.00 16.86 ?  250 PRO B C   1 
ATOM   5050 O O   . PRO B 1 250 ? 11.836  -17.854 4.297   1.00 16.47 ?  250 PRO B O   1 
ATOM   5051 C CB  . PRO B 1 250 ? 12.266  -21.136 4.182   1.00 19.97 ?  250 PRO B CB  1 
ATOM   5052 C CG  . PRO B 1 250 ? 11.322  -22.136 3.612   1.00 23.23 ?  250 PRO B CG  1 
ATOM   5053 C CD  . PRO B 1 250 ? 10.162  -22.221 4.569   1.00 18.54 ?  250 PRO B CD  1 
ATOM   5054 N N   . ASP B 1 251 ? 10.194  -18.875 3.158   1.00 16.63 ?  251 ASP B N   1 
ATOM   5055 C CA  . ASP B 1 251 ? 10.009  -17.695 2.331   1.00 18.11 ?  251 ASP B CA  1 
ATOM   5056 C C   . ASP B 1 251 ? 9.261   -16.597 3.081   1.00 16.75 ?  251 ASP B C   1 
ATOM   5057 O O   . ASP B 1 251 ? 9.663   -15.429 3.053   1.00 16.77 ?  251 ASP B O   1 
ATOM   5058 C CB  . ASP B 1 251 ? 9.292   -18.072 1.046   1.00 18.32 ?  251 ASP B CB  1 
ATOM   5059 C CG  . ASP B 1 251 ? 9.369   -16.972 0.031   1.00 20.96 ?  251 ASP B CG  1 
ATOM   5060 O OD1 . ASP B 1 251 ? 10.484  -16.753 -0.504  1.00 23.84 ?  251 ASP B OD1 1 
ATOM   5061 O OD2 . ASP B 1 251 ? 8.319   -16.333 -0.209  1.00 21.21 -1 251 ASP B OD2 1 
ATOM   5062 N N   . LEU B 1 252 ? 8.175   -16.959 3.759   1.00 16.62 ?  252 LEU B N   1 
ATOM   5063 C CA  . LEU B 1 252 ? 7.519   -16.025 4.664   1.00 16.83 ?  252 LEU B CA  1 
ATOM   5064 C C   . LEU B 1 252 ? 8.510   -15.446 5.665   1.00 14.33 ?  252 LEU B C   1 
ATOM   5065 O O   . LEU B 1 252 ? 8.530   -14.234 5.902   1.00 13.45 ?  252 LEU B O   1 
ATOM   5066 C CB  . LEU B 1 252 ? 6.391   -16.741 5.388   1.00 15.42 ?  252 LEU B CB  1 
ATOM   5067 C CG  . LEU B 1 252 ? 5.371   -15.870 6.084   1.00 18.34 ?  252 LEU B CG  1 
ATOM   5068 C CD1 . LEU B 1 252 ? 4.465   -15.233 5.042   1.00 17.58 ?  252 LEU B CD1 1 
ATOM   5069 C CD2 . LEU B 1 252 ? 4.581   -16.766 7.023   1.00 19.34 ?  252 LEU B CD2 1 
ATOM   5070 N N   . ARG B 1 253 ? 9.362   -16.301 6.231   1.00 14.03 ?  253 ARG B N   1 
ATOM   5071 C CA  . ARG B 1 253 ? 10.369  -15.854 7.185   1.00 14.84 ?  253 ARG B CA  1 
ATOM   5072 C C   . ARG B 1 253 ? 11.276  -14.778 6.592   1.00 15.63 ?  253 ARG B C   1 
ATOM   5073 O O   . ARG B 1 253 ? 11.485  -13.724 7.203   1.00 14.09 ?  253 ARG B O   1 
ATOM   5074 C CB  . ARG B 1 253 ? 11.197  -17.046 7.639   1.00 15.74 ?  253 ARG B CB  1 
ATOM   5075 C CG  . ARG B 1 253 ? 12.257  -16.666 8.623   1.00 16.28 ?  253 ARG B CG  1 
ATOM   5076 C CD  . ARG B 1 253 ? 12.810  -17.909 9.254   1.00 18.17 ?  253 ARG B CD  1 
ATOM   5077 N NE  . ARG B 1 253 ? 13.670  -18.609 8.318   1.00 19.68 ?  253 ARG B NE  1 
ATOM   5078 C CZ  . ARG B 1 253 ? 13.460  -19.842 7.866   1.00 17.63 ?  253 ARG B CZ  1 
ATOM   5079 N NH1 . ARG B 1 253 ? 12.397  -20.532 8.243   1.00 15.78 1  253 ARG B NH1 1 
ATOM   5080 N NH2 . ARG B 1 253 ? 14.333  -20.386 7.032   1.00 19.74 ?  253 ARG B NH2 1 
ATOM   5081 N N   . ALA B 1 254 ? 11.843  -15.038 5.409   1.00 14.31 ?  254 ALA B N   1 
ATOM   5082 C CA  . ALA B 1 254 ? 12.737  -14.065 4.781   1.00 15.86 ?  254 ALA B CA  1 
ATOM   5083 C C   . ALA B 1 254 ? 12.012  -12.756 4.463   1.00 15.59 ?  254 ALA B C   1 
ATOM   5084 O O   . ALA B 1 254 ? 12.596  -11.667 4.583   1.00 14.16 ?  254 ALA B O   1 
ATOM   5085 C CB  . ALA B 1 254 ? 13.340  -14.670 3.518   1.00 15.88 ?  254 ALA B CB  1 
ATOM   5086 N N   . ARG B 1 255 ? 10.747  -12.845 4.027   1.00 13.99 ?  255 ARG B N   1 
ATOM   5087 C CA  . ARG B 1 255 ? 9.957   -11.643 3.773   1.00 14.41 ?  255 ARG B CA  1 
ATOM   5088 C C   . ARG B 1 255 ? 9.708   -10.862 5.056   1.00 15.23 ?  255 ARG B C   1 
ATOM   5089 O O   . ARG B 1 255 ? 9.774   -9.624  5.059   1.00 14.36 ?  255 ARG B O   1 
ATOM   5090 C CB  . ARG B 1 255 ? 8.631   -12.016 3.118   1.00 13.80 ?  255 ARG B CB  1 
ATOM   5091 C CG  . ARG B 1 255 ? 8.798   -12.555 1.707   1.00 14.84 ?  255 ARG B CG  1 
ATOM   5092 C CD  . ARG B 1 255 ? 7.498   -13.068 1.177   1.00 17.80 ?  255 ARG B CD  1 
ATOM   5093 N NE  . ARG B 1 255 ? 6.479   -12.025 1.138   1.00 17.59 ?  255 ARG B NE  1 
ATOM   5094 C CZ  . ARG B 1 255 ? 5.172   -12.273 1.190   1.00 18.78 ?  255 ARG B CZ  1 
ATOM   5095 N NH1 . ARG B 1 255 ? 4.743   -13.524 1.298   1.00 19.01 1  255 ARG B NH1 1 
ATOM   5096 N NH2 . ARG B 1 255 ? 4.295   -11.275 1.131   1.00 19.82 ?  255 ARG B NH2 1 
ATOM   5097 N N   . ALA B 1 256 ? 9.404   -11.564 6.151   1.00 14.81 ?  256 ALA B N   1 
ATOM   5098 C CA  . ALA B 1 256 ? 9.224   -10.886 7.430   1.00 14.02 ?  256 ALA B CA  1 
ATOM   5099 C C   . ALA B 1 256 ? 10.501  -10.167 7.849   1.00 13.79 ?  256 ALA B C   1 
ATOM   5100 O O   . ALA B 1 256 ? 10.462  -8.998  8.261   1.00 17.11 ?  256 ALA B O   1 
ATOM   5101 C CB  . ALA B 1 256 ? 8.791   -11.892 8.504   1.00 14.31 ?  256 ALA B CB  1 
ATOM   5102 N N   . GLU B 1 257 ? 11.647  -10.844 7.719   1.00 16.58 ?  257 GLU B N   1 
ATOM   5103 C CA  . GLU B 1 257 ? 12.929  -10.237 8.047   1.00 16.64 ?  257 GLU B CA  1 
ATOM   5104 C C   . GLU B 1 257 ? 13.154  -8.967  7.242   1.00 15.37 ?  257 GLU B C   1 
ATOM   5105 O O   . GLU B 1 257 ? 13.587  -7.944  7.786   1.00 15.62 ?  257 GLU B O   1 
ATOM   5106 C CB  . GLU B 1 257 ? 14.056  -11.233 7.789   1.00 17.75 ?  257 GLU B CB  1 
ATOM   5107 C CG  . GLU B 1 257 ? 15.415  -10.720 8.196   1.00 21.28 ?  257 GLU B CG  1 
ATOM   5108 C CD  . GLU B 1 257 ? 16.513  -11.739 7.982   1.00 21.82 ?  257 GLU B CD  1 
ATOM   5109 O OE1 . GLU B 1 257 ? 17.445  -11.792 8.809   1.00 23.66 ?  257 GLU B OE1 1 
ATOM   5110 O OE2 . GLU B 1 257 ? 16.440  -12.482 6.980   1.00 25.86 -1 257 GLU B OE2 1 
ATOM   5111 N N   . GLU B 1 258 ? 12.836  -9.008  5.947   1.00 15.12 ?  258 GLU B N   1 
ATOM   5112 C CA  . GLU B 1 258 ? 13.034  -7.842  5.095   1.00 16.89 ?  258 GLU B CA  1 
ATOM   5113 C C   . GLU B 1 258 ? 12.114  -6.702  5.514   1.00 16.75 ?  258 GLU B C   1 
ATOM   5114 O O   . GLU B 1 258 ? 12.532  -5.536  5.536   1.00 17.50 ?  258 GLU B O   1 
ATOM   5115 C CB  . GLU B 1 258 ? 12.815  -8.220  3.627   1.00 20.66 ?  258 GLU B CB  1 
ATOM   5116 C CG  . GLU B 1 258 ? 14.086  -8.764  2.959   1.00 23.29 ?  258 GLU B CG  1 
ATOM   5117 C CD  . GLU B 1 258 ? 13.868  -9.254  1.524   1.00 26.87 ?  258 GLU B CD  1 
ATOM   5118 O OE1 . GLU B 1 258 ? 14.697  -10.059 1.032   1.00 28.40 ?  258 GLU B OE1 1 
ATOM   5119 O OE2 . GLU B 1 258 ? 12.868  -8.846  0.892   1.00 28.59 -1 258 GLU B OE2 1 
ATOM   5120 N N   . SER B 1 259 ? 10.869  -7.024  5.884   1.00 16.98 ?  259 SER B N   1 
ATOM   5121 C CA  . SER B 1 259 ? 9.953   -5.999  6.374   1.00 17.24 ?  259 SER B CA  1 
ATOM   5122 C C   . SER B 1 259 ? 10.445  -5.402  7.686   1.00 16.06 ?  259 SER B C   1 
ATOM   5123 O O   . SER B 1 259 ? 10.248  -4.204  7.921   1.00 15.36 ?  259 SER B O   1 
ATOM   5124 C CB  . SER B 1 259 ? 8.534   -6.565  6.535   1.00 17.29 ?  259 SER B CB  1 
ATOM   5125 O OG  . SER B 1 259 ? 8.361   -7.260  7.773   1.00 19.26 ?  259 SER B OG  1 
ATOM   5126 N N   . PHE B 1 260 ? 11.087  -6.205  8.543   1.00 13.72 ?  260 PHE B N   1 
ATOM   5127 C CA  . PHE B 1 260 ? 11.649  -5.660  9.777   1.00 14.70 ?  260 PHE B CA  1 
ATOM   5128 C C   . PHE B 1 260 ? 12.764  -4.669  9.464   1.00 14.96 ?  260 PHE B C   1 
ATOM   5129 O O   . PHE B 1 260 ? 12.853  -3.596  10.075  1.00 13.83 ?  260 PHE B O   1 
ATOM   5130 C CB  . PHE B 1 260 ? 12.190  -6.780  10.675  1.00 15.35 ?  260 PHE B CB  1 
ATOM   5131 C CG  . PHE B 1 260 ? 11.154  -7.777  11.139  1.00 14.13 ?  260 PHE B CG  1 
ATOM   5132 C CD1 . PHE B 1 260 ? 9.798   -7.525  11.010  1.00 13.49 ?  260 PHE B CD1 1 
ATOM   5133 C CD2 . PHE B 1 260 ? 11.548  -8.983  11.686  1.00 13.18 ?  260 PHE B CD2 1 
ATOM   5134 C CE1 . PHE B 1 260 ? 8.857   -8.449  11.420  1.00 15.98 ?  260 PHE B CE1 1 
ATOM   5135 C CE2 . PHE B 1 260 ? 10.622  -9.905  12.092  1.00 14.40 ?  260 PHE B CE2 1 
ATOM   5136 C CZ  . PHE B 1 260 ? 9.261   -9.632  11.960  1.00 12.61 ?  260 PHE B CZ  1 
ATOM   5137 N N   . PHE B 1 261 ? 13.637  -5.016  8.521   1.00 15.60 ?  261 PHE B N   1 
ATOM   5138 C CA  . PHE B 1 261 ? 14.736  -4.115  8.206   1.00 18.79 ?  261 PHE B CA  1 
ATOM   5139 C C   . PHE B 1 261 ? 14.227  -2.821  7.594   1.00 18.10 ?  261 PHE B C   1 
ATOM   5140 O O   . PHE B 1 261 ? 14.709  -1.735  7.936   1.00 19.89 ?  261 PHE B O   1 
ATOM   5141 C CB  . PHE B 1 261 ? 15.729  -4.804  7.284   1.00 19.27 ?  261 PHE B CB  1 
ATOM   5142 C CG  . PHE B 1 261 ? 16.701  -5.670  8.016   1.00 24.48 ?  261 PHE B CG  1 
ATOM   5143 C CD1 . PHE B 1 261 ? 17.559  -5.119  8.952   1.00 25.19 ?  261 PHE B CD1 1 
ATOM   5144 C CD2 . PHE B 1 261 ? 16.753  -7.034  7.779   1.00 28.95 ?  261 PHE B CD2 1 
ATOM   5145 C CE1 . PHE B 1 261 ? 18.455  -5.906  9.637   1.00 26.57 ?  261 PHE B CE1 1 
ATOM   5146 C CE2 . PHE B 1 261 ? 17.658  -7.837  8.463   1.00 27.97 ?  261 PHE B CE2 1 
ATOM   5147 C CZ  . PHE B 1 261 ? 18.505  -7.269  9.396   1.00 31.13 ?  261 PHE B CZ  1 
ATOM   5148 N N   . LEU B 1 262 ? 13.228  -2.910  6.719   1.00 15.78 ?  262 LEU B N   1 
ATOM   5149 C CA  . LEU B 1 262 ? 12.712  -1.703  6.083   1.00 17.49 ?  262 LEU B CA  1 
ATOM   5150 C C   . LEU B 1 262 ? 12.006  -0.794  7.082   1.00 17.27 ?  262 LEU B C   1 
ATOM   5151 O O   . LEU B 1 262 ? 12.072  0.433   6.952   1.00 20.30 ?  262 LEU B O   1 
ATOM   5152 C CB  . LEU B 1 262 ? 11.765  -2.078  4.952   1.00 21.66 ?  262 LEU B CB  1 
ATOM   5153 C CG  . LEU B 1 262 ? 11.341  -0.933  4.041   1.00 20.95 ?  262 LEU B CG  1 
ATOM   5154 C CD1 . LEU B 1 262 ? 12.540  -0.410  3.250   1.00 19.85 ?  262 LEU B CD1 1 
ATOM   5155 C CD2 . LEU B 1 262 ? 10.212  -1.404  3.117   1.00 22.80 ?  262 LEU B CD2 1 
ATOM   5156 N N   . ALA B 1 263 ? 11.341  -1.366  8.089   1.00 14.64 ?  263 ALA B N   1 
ATOM   5157 C CA  . ALA B 1 263 ? 10.672  -0.546  9.092   1.00 15.09 ?  263 ALA B CA  1 
ATOM   5158 C C   . ALA B 1 263 ? 11.630  0.012   10.136  1.00 16.13 ?  263 ALA B C   1 
ATOM   5159 O O   . ALA B 1 263 ? 11.273  0.965   10.839  1.00 16.84 ?  263 ALA B O   1 
ATOM   5160 C CB  . ALA B 1 263 ? 9.571   -1.346  9.789   1.00 15.26 ?  263 ALA B CB  1 
ATOM   5161 N N   . GLY B 1 264 ? 12.831  -0.542  10.248  1.00 17.25 ?  264 GLY B N   1 
ATOM   5162 C CA  . GLY B 1 264 ? 13.775  -0.088  11.243  1.00 18.29 ?  264 GLY B CA  1 
ATOM   5163 C C   . GLY B 1 264 ? 13.683  -0.820  12.557  1.00 19.12 ?  264 GLY B C   1 
ATOM   5164 O O   . GLY B 1 264 ? 14.078  -0.273  13.592  1.00 19.86 ?  264 GLY B O   1 
ATOM   5165 N N   . ILE B 1 265 ? 13.189  -2.056  12.551  1.00 13.05 ?  265 ILE B N   1 
ATOM   5166 C CA  . ILE B 1 265 ? 13.050  -2.840  13.768  1.00 14.22 ?  265 ILE B CA  1 
ATOM   5167 C C   . ILE B 1 265 ? 13.790  -4.165  13.678  1.00 15.38 ?  265 ILE B C   1 
ATOM   5168 O O   . ILE B 1 265 ? 13.517  -5.071  14.467  1.00 14.08 ?  265 ILE B O   1 
ATOM   5169 C CB  . ILE B 1 265 ? 11.562  -3.077  14.108  1.00 16.57 ?  265 ILE B CB  1 
ATOM   5170 C CG1 . ILE B 1 265 ? 10.892  -3.882  12.971  1.00 15.07 ?  265 ILE B CG1 1 
ATOM   5171 C CG2 . ILE B 1 265 ? 10.863  -1.752  14.373  1.00 17.18 ?  265 ILE B CG2 1 
ATOM   5172 C CD1 . ILE B 1 265 ? 9.462   -4.278  13.253  1.00 17.88 ?  265 ILE B CD1 1 
ATOM   5173 N N   . GLY B 1 266 ? 14.705  -4.305  12.719  1.00 13.88 ?  266 GLY B N   1 
ATOM   5174 C CA  . GLY B 1 266 ? 15.392  -5.558  12.471  1.00 15.01 ?  266 GLY B CA  1 
ATOM   5175 C C   . GLY B 1 266 ? 16.762  -5.647  13.122  1.00 16.46 ?  266 GLY B C   1 
ATOM   5176 O O   . GLY B 1 266 ? 17.362  -6.725  13.164  1.00 17.46 ?  266 GLY B O   1 
ATOM   5177 N N   . GLU B 1 267 ? 17.262  -4.525  13.642  1.00 15.35 ?  267 GLU B N   1 
ATOM   5178 C CA  . GLU B 1 267 ? 18.612  -4.430  14.195  1.00 16.74 ?  267 GLU B CA  1 
ATOM   5179 C C   . GLU B 1 267 ? 18.571  -4.269  15.711  1.00 16.96 ?  267 GLU B C   1 
ATOM   5180 O O   . GLU B 1 267 ? 17.845  -3.399  16.213  1.00 16.24 ?  267 GLU B O   1 
ATOM   5181 C CB  . GLU B 1 267 ? 19.343  -3.242  13.567  1.00 19.81 ?  267 GLU B CB  1 
ATOM   5182 C CG  . GLU B 1 267 ? 20.672  -2.907  14.213  1.00 25.14 ?  267 GLU B CG  1 
ATOM   5183 C CD  . GLU B 1 267 ? 21.226  -1.554  13.746  1.00 31.52 ?  267 GLU B CD  1 
ATOM   5184 O OE1 . GLU B 1 267 ? 21.307  -0.607  14.582  1.00 27.64 ?  267 GLU B OE1 1 
ATOM   5185 O OE2 . GLU B 1 267 ? 21.586  -1.448  12.546  1.00 33.16 -1 267 GLU B OE2 1 
ATOM   5186 N N   . PRO B 1 268 ? 19.326  -5.058  16.476  1.00 15.43 ?  268 PRO B N   1 
ATOM   5187 C CA  . PRO B 1 268 ? 19.273  -4.920  17.941  1.00 14.88 ?  268 PRO B CA  1 
ATOM   5188 C C   . PRO B 1 268 ? 19.926  -3.636  18.423  1.00 15.32 ?  268 PRO B C   1 
ATOM   5189 O O   . PRO B 1 268 ? 20.907  -3.148  17.853  1.00 14.74 ?  268 PRO B O   1 
ATOM   5190 C CB  . PRO B 1 268 ? 20.035  -6.150  18.447  1.00 14.92 ?  268 PRO B CB  1 
ATOM   5191 C CG  . PRO B 1 268 ? 20.913  -6.537  17.309  1.00 18.05 ?  268 PRO B CG  1 
ATOM   5192 C CD  . PRO B 1 268 ? 20.153  -6.203  16.058  1.00 16.97 ?  268 PRO B CD  1 
ATOM   5193 N N   . ASN B 1 269 ? 19.375  -3.097  19.506  1.00 14.46 ?  269 ASN B N   1 
ATOM   5194 C CA  . ASN B 1 269 ? 20.067  -2.038  20.223  1.00 15.87 ?  269 ASN B CA  1 
ATOM   5195 C C   . ASN B 1 269 ? 21.205  -2.635  21.051  1.00 14.55 ?  269 ASN B C   1 
ATOM   5196 O O   . ASN B 1 269 ? 21.399  -3.853  21.105  1.00 13.68 ?  269 ASN B O   1 
ATOM   5197 C CB  . ASN B 1 269 ? 19.098  -1.240  21.096  1.00 12.65 ?  269 ASN B CB  1 
ATOM   5198 C CG  . ASN B 1 269 ? 18.492  -2.064  22.220  1.00 16.11 ?  269 ASN B CG  1 
ATOM   5199 O OD1 . ASN B 1 269 ? 19.199  -2.701  23.004  1.00 14.83 ?  269 ASN B OD1 1 
ATOM   5200 N ND2 . ASN B 1 269 ? 17.158  -2.033  22.319  1.00 15.33 ?  269 ASN B ND2 1 
ATOM   5201 N N   . LEU B 1 270 ? 21.936  -1.759  21.744  1.00 12.15 ?  270 LEU B N   1 
ATOM   5202 C CA  . LEU B 1 270 ? 23.189  -2.129  22.400  1.00 16.53 ?  270 LEU B CA  1 
ATOM   5203 C C   . LEU B 1 270 ? 23.022  -3.165  23.518  1.00 15.37 ?  270 LEU B C   1 
ATOM   5204 O O   . LEU B 1 270 ? 24.011  -3.777  23.919  1.00 16.27 ?  270 LEU B O   1 
ATOM   5205 C CB  . LEU B 1 270 ? 23.874  -0.857  22.932  1.00 16.19 ?  270 LEU B CB  1 
ATOM   5206 C CG  . LEU B 1 270 ? 23.328  -0.067  24.144  1.00 18.21 ?  270 LEU B CG  1 
ATOM   5207 C CD1 . LEU B 1 270 ? 24.093  1.221   24.350  1.00 20.57 ?  270 LEU B CD1 1 
ATOM   5208 C CD2 . LEU B 1 270 ? 21.838  0.278   24.042  1.00 19.68 ?  270 LEU B CD2 1 
ATOM   5209 N N   . LEU B 1 271 ? 21.817  -3.378  24.047  1.00 12.90 ?  271 LEU B N   1 
ATOM   5210 C CA  . LEU B 1 271 ? 21.646  -4.339  25.129  1.00 15.04 ?  271 LEU B CA  1 
ATOM   5211 C C   . LEU B 1 271 ? 20.815  -5.557  24.753  1.00 14.86 ?  271 LEU B C   1 
ATOM   5212 O O   . LEU B 1 271 ? 20.889  -6.574  25.451  1.00 15.82 ?  271 LEU B O   1 
ATOM   5213 C CB  . LEU B 1 271 ? 21.004  -3.656  26.350  1.00 15.49 ?  271 LEU B CB  1 
ATOM   5214 C CG  . LEU B 1 271 ? 21.932  -2.728  27.148  1.00 16.81 ?  271 LEU B CG  1 
ATOM   5215 C CD1 . LEU B 1 271 ? 21.230  -2.282  28.431  1.00 18.69 ?  271 LEU B CD1 1 
ATOM   5216 C CD2 . LEU B 1 271 ? 23.274  -3.404  27.467  1.00 17.31 ?  271 LEU B CD2 1 
ATOM   5217 N N   . ALA B 1 272 ? 20.031  -5.479  23.672  1.00 14.09 ?  272 ALA B N   1 
ATOM   5218 C CA  . ALA B 1 272 ? 19.010  -6.490  23.408  1.00 13.96 ?  272 ALA B CA  1 
ATOM   5219 C C   . ALA B 1 272 ? 19.603  -7.898  23.325  1.00 14.30 ?  272 ALA B C   1 
ATOM   5220 O O   . ALA B 1 272 ? 19.037  -8.850  23.872  1.00 14.50 ?  272 ALA B O   1 
ATOM   5221 C CB  . ALA B 1 272 ? 18.268  -6.140  22.116  1.00 16.06 ?  272 ALA B CB  1 
ATOM   5222 N N   . ILE B 1 273 ? 20.740  -8.054  22.661  1.00 12.85 ?  273 ILE B N   1 
ATOM   5223 C CA  . ILE B 1 273 ? 21.280  -9.396  22.443  1.00 15.20 ?  273 ILE B CA  1 
ATOM   5224 C C   . ILE B 1 273 ? 21.852  -10.000 23.722  1.00 15.08 ?  273 ILE B C   1 
ATOM   5225 O O   . ILE B 1 273 ? 21.431  -11.103 24.094  1.00 14.60 ?  273 ILE B O   1 
ATOM   5226 C CB  . ILE B 1 273 ? 22.331  -9.414  21.322  1.00 14.18 ?  273 ILE B CB  1 
ATOM   5227 C CG1 . ILE B 1 273 ? 21.705  -8.987  19.985  1.00 15.96 ?  273 ILE B CG1 1 
ATOM   5228 C CG2 . ILE B 1 273 ? 22.968  -10.806 21.249  1.00 16.39 ?  273 ILE B CG2 1 
ATOM   5229 C CD1 . ILE B 1 273 ? 20.423  -9.762  19.612  1.00 14.79 ?  273 ILE B CD1 1 
ATOM   5230 N N   . PRO B 1 274 ? 22.810  -9.367  24.421  1.00 15.10 ?  274 PRO B N   1 
ATOM   5231 C CA  . PRO B 1 274 ? 23.310  -10.013 25.649  1.00 17.87 ?  274 PRO B CA  1 
ATOM   5232 C C   . PRO B 1 274 ? 22.238  -10.190 26.723  1.00 17.18 ?  274 PRO B C   1 
ATOM   5233 O O   . PRO B 1 274 ? 22.229  -11.225 27.405  1.00 15.75 ?  274 PRO B O   1 
ATOM   5234 C CB  . PRO B 1 274 ? 24.455  -9.088  26.096  1.00 17.79 ?  274 PRO B CB  1 
ATOM   5235 C CG  . PRO B 1 274 ? 24.161  -7.776  25.460  1.00 16.14 ?  274 PRO B CG  1 
ATOM   5236 C CD  . PRO B 1 274 ? 23.504  -8.091  24.154  1.00 16.06 ?  274 PRO B CD  1 
ATOM   5237 N N   . ALA B 1 275 ? 21.313  -9.231  26.865  1.00 15.18 ?  275 ALA B N   1 
ATOM   5238 C CA  . ALA B 1 275 ? 20.275  -9.345  27.888  1.00 17.09 ?  275 ALA B CA  1 
ATOM   5239 C C   . ALA B 1 275 ? 19.299  -10.481 27.583  1.00 16.82 ?  275 ALA B C   1 
ATOM   5240 O O   . ALA B 1 275 ? 18.960  -11.272 28.474  1.00 15.16 ?  275 ALA B O   1 
ATOM   5241 C CB  . ALA B 1 275 ? 19.533  -8.017  28.031  1.00 15.82 ?  275 ALA B CB  1 
ATOM   5242 N N   . ALA B 1 276 ? 18.813  -10.568 26.335  1.00 15.09 ?  276 ALA B N   1 
ATOM   5243 C CA  . ALA B 1 276 ? 17.914  -11.666 25.976  1.00 15.98 ?  276 ALA B CA  1 
ATOM   5244 C C   . ALA B 1 276 ? 18.611  -13.019 26.090  1.00 16.36 ?  276 ALA B C   1 
ATOM   5245 O O   . ALA B 1 276 ? 18.001  -14.006 26.523  1.00 15.96 ?  276 ALA B O   1 
ATOM   5246 C CB  . ALA B 1 276 ? 17.373  -11.478 24.559  1.00 14.90 ?  276 ALA B CB  1 
ATOM   5247 N N   . ILE B 1 277 ? 19.884  -13.094 25.691  1.00 13.62 ?  277 ILE B N   1 
ATOM   5248 C CA  . ILE B 1 277 ? 20.596  -14.359 25.810  1.00 15.00 ?  277 ILE B CA  1 
ATOM   5249 C C   . ILE B 1 277 ? 20.697  -14.763 27.271  1.00 14.68 ?  277 ILE B C   1 
ATOM   5250 O O   . ILE B 1 277 ? 20.441  -15.920 27.626  1.00 15.99 ?  277 ILE B O   1 
ATOM   5251 C CB  . ILE B 1 277 ? 21.982  -14.273 25.141  1.00 14.65 ?  277 ILE B CB  1 
ATOM   5252 C CG1 . ILE B 1 277 ? 21.838  -14.225 23.614  1.00 12.49 ?  277 ILE B CG1 1 
ATOM   5253 C CG2 . ILE B 1 277 ? 22.840  -15.474 25.536  1.00 18.68 ?  277 ILE B CG2 1 
ATOM   5254 C CD1 . ILE B 1 277 ? 23.179  -14.131 22.869  1.00 17.43 ?  277 ILE B CD1 1 
ATOM   5255 N N   . ALA B 1 278 ? 21.022  -13.807 28.144  1.00 14.65 ?  278 ALA B N   1 
ATOM   5256 C CA  . ALA B 1 278 ? 21.112  -14.109 29.569  1.00 17.73 ?  278 ALA B CA  1 
ATOM   5257 C C   . ALA B 1 278 ? 19.768  -14.558 30.124  1.00 17.64 ?  278 ALA B C   1 
ATOM   5258 O O   . ALA B 1 278 ? 19.701  -15.539 30.877  1.00 18.45 ?  278 ALA B O   1 
ATOM   5259 C CB  . ALA B 1 278 ? 21.632  -12.898 30.339  1.00 16.33 ?  278 ALA B CB  1 
ATOM   5260 N N   . ALA B 1 279 ? 18.683  -13.861 29.764  1.00 15.74 ?  279 ALA B N   1 
ATOM   5261 C CA  . ALA B 1 279 ? 17.362  -14.269 30.242  1.00 16.23 ?  279 ALA B CA  1 
ATOM   5262 C C   . ALA B 1 279 ? 17.042  -15.698 29.816  1.00 17.08 ?  279 ALA B C   1 
ATOM   5263 O O   . ALA B 1 279 ? 16.657  -16.538 30.641  1.00 18.82 ?  279 ALA B O   1 
ATOM   5264 C CB  . ALA B 1 279 ? 16.294  -13.310 29.727  1.00 16.30 ?  279 ALA B CB  1 
ATOM   5265 N N   . TYR B 1 280 ? 17.221  -15.995 28.527  1.00 15.12 ?  280 TYR B N   1 
ATOM   5266 C CA  . TYR B 1 280 ? 16.856  -17.288 27.958  1.00 18.47 ?  280 TYR B CA  1 
ATOM   5267 C C   . TYR B 1 280 ? 17.821  -18.416 28.321  1.00 18.75 ?  280 TYR B C   1 
ATOM   5268 O O   . TYR B 1 280 ? 17.450  -19.598 28.221  1.00 18.81 ?  280 TYR B O   1 
ATOM   5269 C CB  . TYR B 1 280 ? 16.758  -17.143 26.440  1.00 17.11 ?  280 TYR B CB  1 
ATOM   5270 C CG  . TYR B 1 280 ? 15.477  -16.483 25.985  1.00 16.03 ?  280 TYR B CG  1 
ATOM   5271 C CD1 . TYR B 1 280 ? 14.312  -16.581 26.749  1.00 16.64 ?  280 TYR B CD1 1 
ATOM   5272 C CD2 . TYR B 1 280 ? 15.424  -15.763 24.793  1.00 16.76 ?  280 TYR B CD2 1 
ATOM   5273 C CE1 . TYR B 1 280 ? 13.121  -15.992 26.340  1.00 17.74 ?  280 TYR B CE1 1 
ATOM   5274 C CE2 . TYR B 1 280 ? 14.228  -15.162 24.376  1.00 19.10 ?  280 TYR B CE2 1 
ATOM   5275 C CZ  . TYR B 1 280 ? 13.090  -15.280 25.156  1.00 17.93 ?  280 TYR B CZ  1 
ATOM   5276 O OH  . TYR B 1 280 ? 11.911  -14.697 24.746  1.00 20.31 ?  280 TYR B OH  1 
ATOM   5277 N N   . GLU B 1 281 ? 19.043  -18.097 28.730  1.00 16.94 ?  281 GLU B N   1 
ATOM   5278 C CA  . GLU B 1 281 ? 19.970  -19.129 29.177  1.00 20.07 ?  281 GLU B CA  1 
ATOM   5279 C C   . GLU B 1 281 ? 19.995  -19.284 30.690  1.00 21.39 ?  281 GLU B C   1 
ATOM   5280 O O   . GLU B 1 281 ? 20.172  -20.403 31.191  1.00 22.34 ?  281 GLU B O   1 
ATOM   5281 C CB  . GLU B 1 281 ? 21.381  -18.817 28.678  1.00 19.20 ?  281 GLU B CB  1 
ATOM   5282 C CG  . GLU B 1 281 ? 21.516  -19.027 27.190  1.00 23.10 ?  281 GLU B CG  1 
ATOM   5283 C CD  . GLU B 1 281 ? 22.922  -18.808 26.688  1.00 32.15 ?  281 GLU B CD  1 
ATOM   5284 O OE1 . GLU B 1 281 ? 23.776  -18.328 27.473  1.00 33.51 ?  281 GLU B OE1 1 
ATOM   5285 O OE2 . GLU B 1 281 ? 23.167  -19.125 25.501  1.00 36.93 -1 281 GLU B OE2 1 
ATOM   5286 N N   . GLU B 1 282 ? 19.804  -18.194 31.426  1.00 18.69 ?  282 GLU B N   1 
ATOM   5287 C CA  . GLU B 1 282 ? 20.053  -18.197 32.860  1.00 21.06 ?  282 GLU B CA  1 
ATOM   5288 C C   . GLU B 1 282 ? 18.864  -17.710 33.676  1.00 18.20 ?  282 GLU B C   1 
ATOM   5289 O O   . GLU B 1 282 ? 18.998  -17.544 34.895  1.00 19.99 ?  282 GLU B O   1 
ATOM   5290 C CB  . GLU B 1 282 ? 21.292  -17.349 33.177  1.00 22.79 ?  282 GLU B CB  1 
ATOM   5291 C CG  . GLU B 1 282 ? 22.604  -18.114 33.024  1.00 25.63 ?  282 GLU B CG  1 
ATOM   5292 C CD  . GLU B 1 282 ? 23.736  -17.256 32.479  1.00 36.11 ?  282 GLU B CD  1 
ATOM   5293 O OE1 . GLU B 1 282 ? 23.609  -16.009 32.471  1.00 38.05 ?  282 GLU B OE1 1 
ATOM   5294 O OE2 . GLU B 1 282 ? 24.769  -17.828 32.061  1.00 45.93 -1 282 GLU B OE2 1 
ATOM   5295 N N   . GLY B 1 283 ? 17.713  -17.486 33.053  1.00 18.15 ?  283 GLY B N   1 
ATOM   5296 C CA  . GLY B 1 283 ? 16.567  -16.971 33.775  1.00 18.74 ?  283 GLY B CA  1 
ATOM   5297 C C   . GLY B 1 283 ? 15.608  -18.010 34.320  1.00 18.14 ?  283 GLY B C   1 
ATOM   5298 O O   . GLY B 1 283 ? 14.556  -17.647 34.857  1.00 17.15 ?  283 GLY B O   1 
ATOM   5299 N N   . HIS B 1 284 ? 15.923  -19.302 34.199  1.00 16.07 ?  284 HIS B N   1 
ATOM   5300 C CA  . HIS B 1 284 ? 14.954  -20.328 34.586  1.00 17.23 ?  284 HIS B CA  1 
ATOM   5301 C C   . HIS B 1 284 ? 14.652  -20.282 36.079  1.00 17.02 ?  284 HIS B C   1 
ATOM   5302 O O   . HIS B 1 284 ? 13.494  -20.422 36.493  1.00 18.67 ?  284 HIS B O   1 
ATOM   5303 C CB  . HIS B 1 284 ? 15.463  -21.721 34.212  1.00 19.20 ?  284 HIS B CB  1 
ATOM   5304 C CG  . HIS B 1 284 ? 15.714  -21.909 32.748  1.00 19.85 ?  284 HIS B CG  1 
ATOM   5305 N ND1 . HIS B 1 284 ? 14.718  -22.258 31.863  1.00 19.68 ?  284 HIS B ND1 1 
ATOM   5306 C CD2 . HIS B 1 284 ? 16.854  -21.824 32.021  1.00 20.95 ?  284 HIS B CD2 1 
ATOM   5307 C CE1 . HIS B 1 284 ? 15.232  -22.378 30.652  1.00 20.95 ?  284 HIS B CE1 1 
ATOM   5308 N NE2 . HIS B 1 284 ? 16.525  -22.117 30.719  1.00 22.64 ?  284 HIS B NE2 1 
ATOM   5309 N N   . ASN B 1 285 ? 15.684  -20.142 36.901  1.00 16.34 ?  285 ASN B N   1 
ATOM   5310 C CA  . ASN B 1 285 ? 15.475  -20.180 38.343  1.00 18.25 ?  285 ASN B CA  1 
ATOM   5311 C C   . ASN B 1 285 ? 14.675  -18.976 38.803  1.00 17.86 ?  285 ASN B C   1 
ATOM   5312 O O   . ASN B 1 285 ? 13.793  -19.099 39.664  1.00 18.90 ?  285 ASN B O   1 
ATOM   5313 C CB  . ASN B 1 285 ? 16.817  -20.238 39.065  1.00 21.66 ?  285 ASN B CB  1 
ATOM   5314 C CG  . ASN B 1 285 ? 17.531  -21.546 38.850  1.00 25.02 ?  285 ASN B CG  1 
ATOM   5315 O OD1 . ASN B 1 285 ? 16.914  -22.616 38.839  1.00 23.66 ?  285 ASN B OD1 1 
ATOM   5316 N ND2 . ASN B 1 285 ? 18.840  -21.472 38.672  1.00 27.80 ?  285 ASN B ND2 1 
ATOM   5317 N N   . TRP B 1 286 ? 14.951  -17.805 38.225  1.00 15.88 ?  286 TRP B N   1 
ATOM   5318 C CA  . TRP B 1 286 ? 14.204  -16.616 38.622  1.00 16.01 ?  286 TRP B CA  1 
ATOM   5319 C C   . TRP B 1 286 ? 12.739  -16.741 38.232  1.00 16.22 ?  286 TRP B C   1 
ATOM   5320 O O   . TRP B 1 286 ? 11.849  -16.386 39.013  1.00 14.71 ?  286 TRP B O   1 
ATOM   5321 C CB  . TRP B 1 286 ? 14.830  -15.381 37.987  1.00 16.07 ?  286 TRP B CB  1 
ATOM   5322 C CG  . TRP B 1 286 ? 14.193  -14.108 38.418  1.00 16.66 ?  286 TRP B CG  1 
ATOM   5323 C CD1 . TRP B 1 286 ? 14.520  -13.357 39.493  1.00 14.71 ?  286 TRP B CD1 1 
ATOM   5324 C CD2 . TRP B 1 286 ? 13.111  -13.432 37.764  1.00 14.55 ?  286 TRP B CD2 1 
ATOM   5325 N NE1 . TRP B 1 286 ? 13.719  -12.243 39.556  1.00 15.32 ?  286 TRP B NE1 1 
ATOM   5326 C CE2 . TRP B 1 286 ? 12.839  -12.269 38.508  1.00 15.13 ?  286 TRP B CE2 1 
ATOM   5327 C CE3 . TRP B 1 286 ? 12.354  -13.697 36.619  1.00 15.37 ?  286 TRP B CE3 1 
ATOM   5328 C CZ2 . TRP B 1 286 ? 11.833  -11.375 38.154  1.00 16.24 ?  286 TRP B CZ2 1 
ATOM   5329 C CZ3 . TRP B 1 286 ? 11.357  -12.805 36.264  1.00 15.83 ?  286 TRP B CZ3 1 
ATOM   5330 C CH2 . TRP B 1 286 ? 11.105  -11.661 37.025  1.00 14.44 ?  286 TRP B CH2 1 
ATOM   5331 N N   . LEU B 1 287 ? 12.472  -17.246 37.024  1.00 15.62 ?  287 LEU B N   1 
ATOM   5332 C CA  . LEU B 1 287 ? 11.092  -17.442 36.593  1.00 14.03 ?  287 LEU B CA  1 
ATOM   5333 C C   . LEU B 1 287 ? 10.358  -18.430 37.495  1.00 15.51 ?  287 LEU B C   1 
ATOM   5334 O O   . LEU B 1 287 ? 9.187   -18.212 37.830  1.00 15.51 ?  287 LEU B O   1 
ATOM   5335 C CB  . LEU B 1 287 ? 11.051  -17.913 35.139  1.00 13.88 ?  287 LEU B CB  1 
ATOM   5336 C CG  . LEU B 1 287 ? 9.660   -18.202 34.575  1.00 16.47 ?  287 LEU B CG  1 
ATOM   5337 C CD1 . LEU B 1 287 ? 8.756   -17.006 34.775  1.00 14.77 ?  287 LEU B CD1 1 
ATOM   5338 C CD2 . LEU B 1 287 ? 9.762   -18.578 33.099  1.00 14.65 ?  287 LEU B CD2 1 
ATOM   5339 N N   . ARG B 1 288 ? 11.022  -19.518 37.905  1.00 15.51 ?  288 ARG B N   1 
ATOM   5340 C CA  . ARG B 1 288 ? 10.371  -20.473 38.804  1.00 18.72 ?  288 ARG B CA  1 
ATOM   5341 C C   . ARG B 1 288 ? 9.917   -19.784 40.084  1.00 18.88 ?  288 ARG B C   1 
ATOM   5342 O O   . ARG B 1 288 ? 8.767   -19.940 40.518  1.00 16.90 ?  288 ARG B O   1 
ATOM   5343 C CB  . ARG B 1 288 ? 11.305  -21.644 39.134  1.00 21.58 ?  288 ARG B CB  1 
ATOM   5344 C CG  . ARG B 1 288 ? 10.640  -22.689 40.043  1.00 24.68 ?  288 ARG B CG  1 
ATOM   5345 C CD  . ARG B 1 288 ? 11.615  -23.780 40.434  1.00 26.23 ?  288 ARG B CD  1 
ATOM   5346 N NE  . ARG B 1 288 ? 12.928  -23.199 40.689  1.00 31.96 ?  288 ARG B NE  1 
ATOM   5347 C CZ  . ARG B 1 288 ? 13.303  -22.622 41.833  1.00 35.64 ?  288 ARG B CZ  1 
ATOM   5348 N NH1 . ARG B 1 288 ? 12.471  -22.571 42.881  1.00 35.52 1  288 ARG B NH1 1 
ATOM   5349 N NH2 . ARG B 1 288 ? 14.527  -22.103 41.929  1.00 36.72 ?  288 ARG B NH2 1 
ATOM   5350 N N   . GLU B 1 289 ? 10.778  -18.971 40.663  1.00 16.30 ?  289 GLU B N   1 
ATOM   5351 C CA  . GLU B 1 289 ? 10.401  -18.261 41.906  1.00 19.54 ?  289 GLU B CA  1 
ATOM   5352 C C   . GLU B 1 289 ? 9.343   -17.194 41.603  1.00 17.51 ?  289 GLU B C   1 
ATOM   5353 O O   . GLU B 1 289 ? 8.499   -16.972 42.443  1.00 16.62 ?  289 GLU B O   1 
ATOM   5354 C CB  . GLU B 1 289 ? 11.635  -17.690 42.605  1.00 20.30 ?  289 GLU B CB  1 
ATOM   5355 C CG  . GLU B 1 289 ? 12.662  -18.735 42.959  1.00 27.52 ?  289 GLU B CG  1 
ATOM   5356 C CD  . GLU B 1 289 ? 13.619  -18.259 44.035  1.00 37.62 ?  289 GLU B CD  1 
ATOM   5357 O OE1 . GLU B 1 289 ? 14.264  -19.115 44.662  1.00 39.41 ?  289 GLU B OE1 1 
ATOM   5358 O OE2 . GLU B 1 289 ? 13.689  -17.035 44.256  1.00 31.78 -1 289 GLU B OE2 1 
ATOM   5359 N N   . LEU B 1 290 ? 9.452   -16.533 40.449  1.00 15.26 ?  290 LEU B N   1 
ATOM   5360 C CA  . LEU B 1 290 ? 8.422   -15.559 40.093  1.00 14.69 ?  290 LEU B CA  1 
ATOM   5361 C C   . LEU B 1 290 ? 7.037   -16.198 40.088  1.00 16.84 ?  290 LEU B C   1 
ATOM   5362 O O   . LEU B 1 290 ? 6.080   -15.631 40.634  1.00 14.12 ?  290 LEU B O   1 
ATOM   5363 C CB  . LEU B 1 290 ? 8.715   -14.933 38.730  1.00 14.08 ?  290 LEU B CB  1 
ATOM   5364 C CG  . LEU B 1 290 ? 7.538   -14.117 38.196  1.00 14.35 ?  290 LEU B CG  1 
ATOM   5365 C CD1 . LEU B 1 290 ? 7.357   -12.858 39.026  1.00 15.61 ?  290 LEU B CD1 1 
ATOM   5366 C CD2 . LEU B 1 290 ? 7.786   -13.750 36.730  1.00 15.55 ?  290 LEU B CD2 1 
ATOM   5367 N N   . LYS B 1 291 ? 6.918   -17.395 39.503  1.00 14.30 ?  291 LYS B N   1 
ATOM   5368 C CA  . LYS B 1 291 ? 5.606   -18.017 39.388  1.00 15.30 ?  291 LYS B CA  1 
ATOM   5369 C C   . LYS B 1 291 ? 5.052   -18.399 40.756  1.00 15.59 ?  291 LYS B C   1 
ATOM   5370 O O   . LYS B 1 291 ? 3.834   -18.344 40.969  1.00 13.57 ?  291 LYS B O   1 
ATOM   5371 C CB  . LYS B 1 291 ? 5.697   -19.225 38.470  1.00 17.45 ?  291 LYS B CB  1 
ATOM   5372 C CG  . LYS B 1 291 ? 5.913   -18.866 37.003  1.00 15.52 ?  291 LYS B CG  1 
ATOM   5373 C CD  . LYS B 1 291 ? 5.866   -20.134 36.171  1.00 19.61 ?  291 LYS B CD  1 
ATOM   5374 C CE  . LYS B 1 291 ? 5.776   -19.811 34.700  1.00 17.13 ?  291 LYS B CE  1 
ATOM   5375 N NZ  . LYS B 1 291 ? 5.807   -21.023 33.844  1.00 21.35 1  291 LYS B NZ  1 
ATOM   5376 N N   . GLN B 1 292 ? 5.926   -18.768 41.696  1.00 15.29 ?  292 GLN B N   1 
ATOM   5377 C CA  . GLN B 1 292 ? 5.483   -18.980 43.072  1.00 17.46 ?  292 GLN B CA  1 
ATOM   5378 C C   . GLN B 1 292 ? 4.912   -17.700 43.669  1.00 15.93 ?  292 GLN B C   1 
ATOM   5379 O O   . GLN B 1 292 ? 3.859   -17.724 44.318  1.00 14.83 ?  292 GLN B O   1 
ATOM   5380 C CB  . GLN B 1 292 ? 6.640   -19.508 43.919  1.00 18.07 ?  292 GLN B CB  1 
ATOM   5381 C CG  . GLN B 1 292 ? 7.180   -20.855 43.446  1.00 20.99 ?  292 GLN B CG  1 
ATOM   5382 C CD  . GLN B 1 292 ? 8.546   -21.188 44.038  1.00 28.31 ?  292 GLN B CD  1 
ATOM   5383 O OE1 . GLN B 1 292 ? 9.073   -20.449 44.874  1.00 33.72 ?  292 GLN B OE1 1 
ATOM   5384 N NE2 . GLN B 1 292 ? 9.129   -22.305 43.597  1.00 33.78 ?  292 GLN B NE2 1 
ATOM   5385 N N   . VAL B 1 293 ? 5.573   -16.565 43.436  1.00 13.18 ?  293 VAL B N   1 
ATOM   5386 C CA  . VAL B 1 293 ? 5.067   -15.294 43.956  1.00 14.92 ?  293 VAL B CA  1 
ATOM   5387 C C   . VAL B 1 293 ? 3.740   -14.935 43.299  1.00 15.22 ?  293 VAL B C   1 
ATOM   5388 O O   . VAL B 1 293 ? 2.797   -14.481 43.970  1.00 14.00 ?  293 VAL B O   1 
ATOM   5389 C CB  . VAL B 1 293 ? 6.113   -14.179 43.760  1.00 16.62 ?  293 VAL B CB  1 
ATOM   5390 C CG1 . VAL B 1 293 ? 5.520   -12.809 44.110  1.00 16.86 ?  293 VAL B CG1 1 
ATOM   5391 C CG2 . VAL B 1 293 ? 7.351   -14.465 44.602  1.00 17.70 ?  293 VAL B CG2 1 
ATOM   5392 N N   . LEU B 1 294 ? 3.651   -15.106 41.978  1.00 14.19 ?  294 LEU B N   1 
ATOM   5393 C CA  . LEU B 1 294 ? 2.419   -14.772 41.272  1.00 13.84 ?  294 LEU B CA  1 
ATOM   5394 C C   . LEU B 1 294 ? 1.275   -15.685 41.693  1.00 15.41 ?  294 LEU B C   1 
ATOM   5395 O O   . LEU B 1 294 ? 0.146   -15.217 41.890  1.00 14.59 ?  294 LEU B O   1 
ATOM   5396 C CB  . LEU B 1 294 ? 2.632   -14.842 39.757  1.00 15.53 ?  294 LEU B CB  1 
ATOM   5397 C CG  . LEU B 1 294 ? 3.631   -13.850 39.164  1.00 14.96 ?  294 LEU B CG  1 
ATOM   5398 C CD1 . LEU B 1 294 ? 3.739   -14.087 37.667  1.00 13.58 ?  294 LEU B CD1 1 
ATOM   5399 C CD2 . LEU B 1 294 ? 3.219   -12.411 39.434  1.00 14.13 ?  294 LEU B CD2 1 
ATOM   5400 N N   . ARG B 1 295 ? 1.539   -16.992 41.819  1.00 14.46 ?  295 ARG B N   1 
ATOM   5401 C CA  . ARG B 1 295 ? 0.494   -17.894 42.299  1.00 17.58 ?  295 ARG B CA  1 
ATOM   5402 C C   . ARG B 1 295 ? 0.008   -17.487 43.686  1.00 14.89 ?  295 ARG B C   1 
ATOM   5403 O O   . ARG B 1 295 ? -1.196  -17.501 43.958  1.00 14.17 ?  295 ARG B O   1 
ATOM   5404 C CB  . ARG B 1 295 ? 0.996   -19.337 42.308  1.00 16.72 ?  295 ARG B CB  1 
ATOM   5405 C CG  . ARG B 1 295 ? 0.846   -20.022 40.958  1.00 17.25 ?  295 ARG B CG  1 
ATOM   5406 C CD  . ARG B 1 295 ? 1.140   -21.510 41.056  1.00 21.68 ?  295 ARG B CD  1 
ATOM   5407 N NE  . ARG B 1 295 ? 2.534   -21.720 41.391  1.00 23.81 ?  295 ARG B NE  1 
ATOM   5408 C CZ  . ARG B 1 295 ? 3.487   -21.957 40.492  1.00 24.50 ?  295 ARG B CZ  1 
ATOM   5409 N NH1 . ARG B 1 295 ? 3.182   -22.038 39.206  1.00 24.44 1  295 ARG B NH1 1 
ATOM   5410 N NH2 . ARG B 1 295 ? 4.735   -22.122 40.887  1.00 23.87 ?  295 ARG B NH2 1 
ATOM   5411 N N   . ASP B 1 296 ? 0.932   -17.106 44.570  1.00 15.40 ?  296 ASP B N   1 
ATOM   5412 C CA  . ASP B 1 296 ? 0.553   -16.615 45.892  1.00 16.06 ?  296 ASP B CA  1 
ATOM   5413 C C   . ASP B 1 296 ? -0.276  -15.339 45.805  1.00 18.55 ?  296 ASP B C   1 
ATOM   5414 O O   . ASP B 1 296 ? -1.270  -15.185 46.527  1.00 16.26 ?  296 ASP B O   1 
ATOM   5415 C CB  . ASP B 1 296 ? 1.798   -16.367 46.732  1.00 16.35 ?  296 ASP B CB  1 
ATOM   5416 C CG  . ASP B 1 296 ? 1.478   -16.306 48.212  1.00 23.89 ?  296 ASP B CG  1 
ATOM   5417 O OD1 . ASP B 1 296 ? 0.789   -17.224 48.720  1.00 24.31 ?  296 ASP B OD1 1 
ATOM   5418 O OD2 . ASP B 1 296 ? 1.868   -15.307 48.846  1.00 25.38 -1 296 ASP B OD2 1 
ATOM   5419 N N   . ASN B 1 297 ? 0.115   -14.409 44.928  1.00 14.63 ?  297 ASN B N   1 
ATOM   5420 C CA  . ASN B 1 297 ? -0.623  -13.158 44.815  1.00 15.49 ?  297 ASN B CA  1 
ATOM   5421 C C   . ASN B 1 297 ? -2.027  -13.396 44.268  1.00 15.53 ?  297 ASN B C   1 
ATOM   5422 O O   . ASN B 1 297 ? -2.994  -12.794 44.752  1.00 15.17 ?  297 ASN B O   1 
ATOM   5423 C CB  . ASN B 1 297 ? 0.138   -12.165 43.928  1.00 12.75 ?  297 ASN B CB  1 
ATOM   5424 C CG  . ASN B 1 297 ? 1.367   -11.566 44.619  1.00 15.52 ?  297 ASN B CG  1 
ATOM   5425 O OD1 . ASN B 1 297 ? 1.583   -11.759 45.820  1.00 18.35 ?  297 ASN B OD1 1 
ATOM   5426 N ND2 . ASN B 1 297 ? 2.176   -10.837 43.858  1.00 14.66 ?  297 ASN B ND2 1 
ATOM   5427 N N   . PHE B 1 298 ? -2.159  -14.262 43.253  1.00 14.94 ?  298 PHE B N   1 
ATOM   5428 C CA  . PHE B 1 298 ? -3.485  -14.583 42.726  1.00 16.38 ?  298 PHE B CA  1 
ATOM   5429 C C   . PHE B 1 298 ? -4.329  -15.300 43.767  1.00 15.59 ?  298 PHE B C   1 
ATOM   5430 O O   . PHE B 1 298 ? -5.540  -15.055 43.868  1.00 16.06 ?  298 PHE B O   1 
ATOM   5431 C CB  . PHE B 1 298 ? -3.377  -15.448 41.471  1.00 14.48 ?  298 PHE B CB  1 
ATOM   5432 C CG  . PHE B 1 298 ? -3.429  -14.669 40.188  1.00 18.30 ?  298 PHE B CG  1 
ATOM   5433 C CD1 . PHE B 1 298 ? -4.640  -14.349 39.605  1.00 19.36 ?  298 PHE B CD1 1 
ATOM   5434 C CD2 . PHE B 1 298 ? -2.262  -14.259 39.564  1.00 19.81 ?  298 PHE B CD2 1 
ATOM   5435 C CE1 . PHE B 1 298 ? -4.701  -13.650 38.416  1.00 20.03 ?  298 PHE B CE1 1 
ATOM   5436 C CE2 . PHE B 1 298 ? -2.317  -13.549 38.370  1.00 21.43 ?  298 PHE B CE2 1 
ATOM   5437 C CZ  . PHE B 1 298 ? -3.543  -13.256 37.797  1.00 18.89 ?  298 PHE B CZ  1 
ATOM   5438 N N   . ALA B 1 299 ? -3.713  -16.210 44.528  1.00 15.43 ?  299 ALA B N   1 
ATOM   5439 C CA  . ALA B 1 299 ? -4.441  -16.898 45.586  1.00 15.89 ?  299 ALA B CA  1 
ATOM   5440 C C   . ALA B 1 299 ? -4.960  -15.905 46.612  1.00 17.55 ?  299 ALA B C   1 
ATOM   5441 O O   . ALA B 1 299 ? -6.105  -16.015 47.062  1.00 16.67 ?  299 ALA B O   1 
ATOM   5442 C CB  . ALA B 1 299 ? -3.555  -17.951 46.255  1.00 17.51 ?  299 ALA B CB  1 
ATOM   5443 N N   . TYR B 1 300 ? -4.143  -14.910 46.976  1.00 16.85 ?  300 TYR B N   1 
ATOM   5444 C CA  . TYR B 1 300 ? -4.609  -13.895 47.917  1.00 17.57 ?  300 TYR B CA  1 
ATOM   5445 C C   . TYR B 1 300 ? -5.759  -13.090 47.321  1.00 16.62 ?  300 TYR B C   1 
ATOM   5446 O O   . TYR B 1 300 ? -6.804  -12.914 47.960  1.00 15.86 ?  300 TYR B O   1 
ATOM   5447 C CB  . TYR B 1 300 ? -3.463  -12.968 48.343  1.00 17.14 ?  300 TYR B CB  1 
ATOM   5448 C CG  . TYR B 1 300 ? -3.956  -11.968 49.357  1.00 19.66 ?  300 TYR B CG  1 
ATOM   5449 C CD1 . TYR B 1 300 ? -3.966  -12.277 50.703  1.00 20.81 ?  300 TYR B CD1 1 
ATOM   5450 C CD2 . TYR B 1 300 ? -4.489  -10.752 48.961  1.00 17.77 ?  300 TYR B CD2 1 
ATOM   5451 C CE1 . TYR B 1 300 ? -4.465  -11.391 51.635  1.00 20.58 ?  300 TYR B CE1 1 
ATOM   5452 C CE2 . TYR B 1 300 ? -4.990  -9.864  49.878  1.00 19.37 ?  300 TYR B CE2 1 
ATOM   5453 C CZ  . TYR B 1 300 ? -4.973  -10.193 51.216  1.00 19.59 ?  300 TYR B CZ  1 
ATOM   5454 O OH  . TYR B 1 300 ? -5.458  -9.310  52.141  1.00 22.34 ?  300 TYR B OH  1 
ATOM   5455 N N   . ALA B 1 301 ? -5.589  -12.599 46.086  1.00 14.45 ?  301 ALA B N   1 
ATOM   5456 C CA  . ALA B 1 301 ? -6.631  -11.795 45.455  1.00 16.76 ?  301 ALA B CA  1 
ATOM   5457 C C   . ALA B 1 301 ? -7.930  -12.578 45.348  1.00 14.98 ?  301 ALA B C   1 
ATOM   5458 O O   . ALA B 1 301 ? -9.011  -12.061 45.654  1.00 15.77 ?  301 ALA B O   1 
ATOM   5459 C CB  . ALA B 1 301 ? -6.177  -11.319 44.073  1.00 13.58 ?  301 ALA B CB  1 
ATOM   5460 N N   . ARG B 1 302 ? -7.842  -13.840 44.923  1.00 15.28 ?  302 ARG B N   1 
ATOM   5461 C CA  . ARG B 1 302 ? -9.055  -14.625 44.737  1.00 14.85 ?  302 ARG B CA  1 
ATOM   5462 C C   . ARG B 1 302 ? -9.723  -14.929 46.067  1.00 16.37 ?  302 ARG B C   1 
ATOM   5463 O O   . ARG B 1 302 ? -10.938 -14.770 46.193  1.00 14.99 ?  302 ARG B O   1 
ATOM   5464 C CB  . ARG B 1 302 ? -8.751  -15.907 43.973  1.00 14.10 ?  302 ARG B CB  1 
ATOM   5465 C CG  . ARG B 1 302 ? -8.583  -15.662 42.469  1.00 16.04 ?  302 ARG B CG  1 
ATOM   5466 C CD  . ARG B 1 302 ? -8.387  -16.965 41.702  1.00 18.97 ?  302 ARG B CD  1 
ATOM   5467 N NE  . ARG B 1 302 ? -8.451  -16.729 40.259  1.00 19.61 ?  302 ARG B NE  1 
ATOM   5468 C CZ  . ARG B 1 302 ? -7.417  -16.839 39.433  1.00 21.17 ?  302 ARG B CZ  1 
ATOM   5469 N NH1 . ARG B 1 302 ? -6.227  -17.214 39.888  1.00 17.78 1  302 ARG B NH1 1 
ATOM   5470 N NH2 . ARG B 1 302 ? -7.582  -16.597 38.138  1.00 19.16 ?  302 ARG B NH2 1 
ATOM   5471 N N   . GLU B 1 303 ? -8.947  -15.317 47.082  1.00 15.05 ?  303 GLU B N   1 
ATOM   5472 C CA  . GLU B 1 303 ? -9.545  -15.590 48.384  1.00 17.93 ?  303 GLU B CA  1 
ATOM   5473 C C   . GLU B 1 303 ? -10.145 -14.324 48.984  1.00 18.93 ?  303 GLU B C   1 
ATOM   5474 O O   . GLU B 1 303 ? -11.272 -14.341 49.503  1.00 18.37 ?  303 GLU B O   1 
ATOM   5475 C CB  . GLU B 1 303 ? -8.503  -16.183 49.326  1.00 15.77 ?  303 GLU B CB  1 
ATOM   5476 C CG  . GLU B 1 303 ? -9.041  -16.409 50.730  1.00 20.63 ?  303 GLU B CG  1 
ATOM   5477 C CD  . GLU B 1 303 ? -8.729  -15.255 51.654  1.00 29.14 ?  303 GLU B CD  1 
ATOM   5478 O OE1 . GLU B 1 303 ? -7.604  -14.712 51.555  1.00 32.49 ?  303 GLU B OE1 1 
ATOM   5479 O OE2 . GLU B 1 303 ? -9.606  -14.892 52.475  1.00 32.90 -1 303 GLU B OE2 1 
ATOM   5480 N N   . PHE B 1 304 ? -9.413  -13.211 48.900  1.00 15.32 ?  304 PHE B N   1 
ATOM   5481 C CA  . PHE B 1 304 ? -9.875  -11.959 49.493  1.00 17.65 ?  304 PHE B CA  1 
ATOM   5482 C C   . PHE B 1 304 ? -11.103 -11.406 48.775  1.00 17.86 ?  304 PHE B C   1 
ATOM   5483 O O   . PHE B 1 304 ? -12.111 -11.092 49.413  1.00 16.76 ?  304 PHE B O   1 
ATOM   5484 C CB  . PHE B 1 304 ? -8.748  -10.920 49.497  1.00 17.09 ?  304 PHE B CB  1 
ATOM   5485 C CG  . PHE B 1 304 ? -9.181  -9.566  50.004  1.00 18.49 ?  304 PHE B CG  1 
ATOM   5486 C CD1 . PHE B 1 304 ? -9.117  -9.270  51.355  1.00 18.86 ?  304 PHE B CD1 1 
ATOM   5487 C CD2 . PHE B 1 304 ? -9.677  -8.603  49.140  1.00 15.86 ?  304 PHE B CD2 1 
ATOM   5488 C CE1 . PHE B 1 304 ? -9.522  -8.029  51.828  1.00 20.63 ?  304 PHE B CE1 1 
ATOM   5489 C CE2 . PHE B 1 304 ? -10.075 -7.355  49.611  1.00 17.24 ?  304 PHE B CE2 1 
ATOM   5490 C CZ  . PHE B 1 304 ? -9.998  -7.076  50.953  1.00 18.48 ?  304 PHE B CZ  1 
ATOM   5491 N N   . LEU B 1 305 ? -11.090 -11.349 47.454  1.00 17.67 ?  305 LEU B N   1 
ATOM   5492 C CA  . LEU B 1 305 ? -12.259 -10.747 46.770  1.00 18.29 ?  305 LEU B CA  1 
ATOM   5493 C C   . LEU B 1 305 ? -13.468 -11.678 46.885  1.00 22.98 ?  305 LEU B C   1 
ATOM   5494 O O   . LEU B 1 305 ? -14.566 -11.187 46.928  1.00 21.46 ?  305 LEU B O   1 
ATOM   5495 C CB  . LEU B 1 305 ? -11.910 -10.410 45.322  1.00 20.87 ?  305 LEU B CB  1 
ATOM   5496 C CG  . LEU B 1 305 ? -10.872 -9.300  45.158  1.00 20.04 ?  305 LEU B CG  1 
ATOM   5497 C CD1 . LEU B 1 305 ? -10.529 -9.080  43.699  1.00 17.09 ?  305 LEU B CD1 1 
ATOM   5498 C CD2 . LEU B 1 305 ? -11.355 -8.002  45.766  1.00 15.78 ?  305 LEU B CD2 1 
ATOM   5499 N N   . ALA B 1 306 ? -13.244 -12.993 46.928  1.00 20.71 ?  306 ALA B N   1 
ATOM   5500 C CA  . ALA B 1 306 ? -14.373 -13.935 47.138  1.00 25.25 ?  306 ALA B CA  1 
ATOM   5501 C C   . ALA B 1 306 ? -15.026 -13.745 48.509  1.00 29.44 ?  306 ALA B C   1 
ATOM   5502 O O   . ALA B 1 306 ? -16.253 -13.846 48.583  1.00 34.00 ?  306 ALA B O   1 
ATOM   5503 C CB  . ALA B 1 306 ? -13.926 -15.346 47.010  1.00 23.81 ?  306 ALA B CB  1 
ATOM   5504 N N   . LYS B 1 307 ? -14.215 -13.463 49.507  1.00 29.60 ?  307 LYS B N   1 
ATOM   5505 C CA  . LYS B 1 307 ? -14.708 -13.279 50.894  1.00 24.39 ?  307 LYS B CA  1 
ATOM   5506 C C   . LYS B 1 307 ? -15.241 -11.857 51.121  1.00 25.39 ?  307 LYS B C   1 
ATOM   5507 O O   . LYS B 1 307 ? -16.321 -11.754 51.685  1.00 26.98 ?  307 LYS B O   1 
ATOM   5508 C CB  . LYS B 1 307 ? -13.582 -13.561 51.889  1.00 27.77 ?  307 LYS B CB  1 
ATOM   5509 C CG  . LYS B 1 307 ? -13.992 -13.643 53.350  1.00 27.30 ?  307 LYS B CG  1 
ATOM   5510 C CD  . LYS B 1 307 ? -12.815 -13.849 54.265  1.00 31.21 ?  307 LYS B CD  1 
ATOM   5511 C CE  . LYS B 1 307 ? -13.231 -14.320 55.639  1.00 39.38 ?  307 LYS B CE  1 
ATOM   5512 N NZ  . LYS B 1 307 ? -14.656 -14.722 55.657  1.00 40.26 1  307 LYS B NZ  1 
ATOM   5513 N N   . GLU B 1 308 ? -14.539 -10.824 50.641  1.00 23.67 ?  308 GLU B N   1 
ATOM   5514 C CA  . GLU B 1 308 ? -14.973 -9.480  51.020  1.00 22.36 ?  308 GLU B CA  1 
ATOM   5515 C C   . GLU B 1 308 ? -15.699 -8.673  49.948  1.00 22.40 ?  308 GLU B C   1 
ATOM   5516 O O   . GLU B 1 308 ? -16.328 -7.668  50.293  1.00 19.28 ?  308 GLU B O   1 
ATOM   5517 C CB  . GLU B 1 308 ? -13.750 -8.669  51.457  1.00 22.13 ?  308 GLU B CB  1 
ATOM   5518 C CG  . GLU B 1 308 ? -12.922 -9.364  52.499  1.00 23.08 ?  308 GLU B CG  1 
ATOM   5519 C CD  . GLU B 1 308 ? -13.637 -9.455  53.827  1.00 26.84 ?  308 GLU B CD  1 
ATOM   5520 O OE1 . GLU B 1 308 ? -13.315 -10.345 54.645  1.00 33.59 ?  308 GLU B OE1 1 
ATOM   5521 O OE2 . GLU B 1 308 ? -14.535 -8.621  54.054  1.00 28.66 -1 308 GLU B OE2 1 
ATOM   5522 N N   . VAL B 1 309 ? -15.592 -9.039  48.671  1.00 17.50 ?  309 VAL B N   1 
ATOM   5523 C CA  . VAL B 1 309 ? -16.175 -8.249  47.581  1.00 18.97 ?  309 VAL B CA  1 
ATOM   5524 C C   . VAL B 1 309 ? -16.950 -9.181  46.654  1.00 22.19 ?  309 VAL B C   1 
ATOM   5525 O O   . VAL B 1 309 ? -16.542 -9.403  45.502  1.00 19.89 ?  309 VAL B O   1 
ATOM   5526 C CB  . VAL B 1 309 ? -15.092 -7.465  46.818  1.00 19.91 ?  309 VAL B CB  1 
ATOM   5527 C CG1 . VAL B 1 309 ? -15.714 -6.319  46.058  1.00 18.18 ?  309 VAL B CG1 1 
ATOM   5528 C CG2 . VAL B 1 309 ? -14.031 -6.941  47.808  1.00 17.65 ?  309 VAL B CG2 1 
ATOM   5529 N N   . PRO B 1 310 ? -18.077 -9.743  47.103  1.00 22.78 ?  310 PRO B N   1 
ATOM   5530 C CA  . PRO B 1 310 ? -18.844 -10.651 46.234  1.00 23.06 ?  310 PRO B CA  1 
ATOM   5531 C C   . PRO B 1 310 ? -19.452 -9.973  45.016  1.00 23.10 ?  310 PRO B C   1 
ATOM   5532 O O   . PRO B 1 310 ? -19.888 -10.679 44.100  1.00 23.71 ?  310 PRO B O   1 
ATOM   5533 C CB  . PRO B 1 310 ? -19.930 -11.198 47.171  1.00 24.19 ?  310 PRO B CB  1 
ATOM   5534 C CG  . PRO B 1 310 ? -20.086 -10.136 48.219  1.00 22.71 ?  310 PRO B CG  1 
ATOM   5535 C CD  . PRO B 1 310 ? -18.716 -9.551  48.422  1.00 20.62 ?  310 PRO B CD  1 
ATOM   5536 N N   . GLU B 1 311 ? -19.482 -8.638  44.966  1.00 20.39 ?  311 GLU B N   1 
ATOM   5537 C CA  . GLU B 1 311 ? -20.034 -7.912  43.828  1.00 24.26 ?  311 GLU B CA  1 
ATOM   5538 C C   . GLU B 1 311 ? -19.127 -7.920  42.598  1.00 23.35 ?  311 GLU B C   1 
ATOM   5539 O O   . GLU B 1 311 ? -19.574 -7.511  41.521  1.00 26.13 ?  311 GLU B O   1 
ATOM   5540 C CB  . GLU B 1 311 ? -20.333 -6.464  44.229  1.00 23.53 ?  311 GLU B CB  1 
ATOM   5541 C CG  . GLU B 1 311 ? -21.145 -6.348  45.505  1.00 26.20 ?  311 GLU B CG  1 
ATOM   5542 C CD  . GLU B 1 311 ? -20.284 -6.047  46.715  1.00 31.62 ?  311 GLU B CD  1 
ATOM   5543 O OE1 . GLU B 1 311 ? -20.506 -4.990  47.353  1.00 39.46 ?  311 GLU B OE1 1 
ATOM   5544 O OE2 . GLU B 1 311 ? -19.377 -6.857  47.029  1.00 25.09 -1 311 GLU B OE2 1 
ATOM   5545 N N   . VAL B 1 312 ? -17.872 -8.346  42.726  1.00 19.65 ?  312 VAL B N   1 
ATOM   5546 C CA  . VAL B 1 312 ? -16.993 -8.517  41.576  1.00 19.00 ?  312 VAL B CA  1 
ATOM   5547 C C   . VAL B 1 312 ? -16.615 -9.991  41.483  1.00 20.37 ?  312 VAL B C   1 
ATOM   5548 O O   . VAL B 1 312 ? -16.725 -10.748 42.452  1.00 22.11 ?  312 VAL B O   1 
ATOM   5549 C CB  . VAL B 1 312 ? -15.740 -7.608  41.652  1.00 18.07 ?  312 VAL B CB  1 
ATOM   5550 C CG1 . VAL B 1 312 ? -16.154 -6.154  41.892  1.00 17.61 ?  312 VAL B CG1 1 
ATOM   5551 C CG2 . VAL B 1 312 ? -14.785 -8.084  42.728  1.00 19.21 ?  312 VAL B CG2 1 
ATOM   5552 N N   . LYS B 1 313 ? -16.204 -10.412 40.284  1.00 18.48 ?  313 LYS B N   1 
ATOM   5553 C CA  . LYS B 1 313 ? -15.859 -11.809 40.025  1.00 18.07 ?  313 LYS B CA  1 
ATOM   5554 C C   . LYS B 1 313 ? -14.527 -11.854 39.296  1.00 17.94 ?  313 LYS B C   1 
ATOM   5555 O O   . LYS B 1 313 ? -14.460 -11.513 38.111  1.00 16.97 ?  313 LYS B O   1 
ATOM   5556 C CB  . LYS B 1 313 ? -16.938 -12.512 39.196  1.00 22.33 ?  313 LYS B CB  1 
ATOM   5557 C CG  . LYS B 1 313 ? -18.361 -12.481 39.773  1.00 30.53 ?  313 LYS B CG  1 
ATOM   5558 C CD  . LYS B 1 313 ? -19.337 -13.221 38.837  1.00 34.98 ?  313 LYS B CD  1 
ATOM   5559 C CE  . LYS B 1 313 ? -20.805 -12.792 39.020  1.00 37.90 ?  313 LYS B CE  1 
ATOM   5560 N NZ  . LYS B 1 313 ? -21.032 -11.307 38.925  1.00 37.89 1  313 LYS B NZ  1 
ATOM   5561 N N   . VAL B 1 314 ? -13.471 -12.272 39.989  1.00 16.88 ?  314 VAL B N   1 
ATOM   5562 C CA  . VAL B 1 314 ? -12.199 -12.532 39.321  1.00 18.40 ?  314 VAL B CA  1 
ATOM   5563 C C   . VAL B 1 314 ? -12.364 -13.747 38.416  1.00 18.06 ?  314 VAL B C   1 
ATOM   5564 O O   . VAL B 1 314 ? -12.755 -14.830 38.872  1.00 17.44 ?  314 VAL B O   1 
ATOM   5565 C CB  . VAL B 1 314 ? -11.071 -12.746 40.339  1.00 17.82 ?  314 VAL B CB  1 
ATOM   5566 C CG1 . VAL B 1 314 ? -9.744  -12.968 39.622  1.00 17.74 ?  314 VAL B CG1 1 
ATOM   5567 C CG2 . VAL B 1 314 ? -10.955 -11.543 41.249  1.00 17.14 ?  314 VAL B CG2 1 
ATOM   5568 N N   . LEU B 1 315 ? -12.087 -13.573 37.125  1.00 16.45 ?  315 LEU B N   1 
ATOM   5569 C CA  . LEU B 1 315 ? -12.191 -14.702 36.213  1.00 17.48 ?  315 LEU B CA  1 
ATOM   5570 C C   . LEU B 1 315 ? -11.110 -15.737 36.493  1.00 17.84 ?  315 LEU B C   1 
ATOM   5571 O O   . LEU B 1 315 ? -9.963  -15.406 36.818  1.00 16.08 ?  315 LEU B O   1 
ATOM   5572 C CB  . LEU B 1 315 ? -12.108 -14.243 34.757  1.00 17.06 ?  315 LEU B CB  1 
ATOM   5573 C CG  . LEU B 1 315 ? -13.383 -13.564 34.242  1.00 21.17 ?  315 LEU B CG  1 
ATOM   5574 C CD1 . LEU B 1 315 ? -13.516 -13.808 32.752  1.00 18.41 ?  315 LEU B CD1 1 
ATOM   5575 C CD2 . LEU B 1 315 ? -14.663 -14.011 34.995  1.00 20.75 ?  315 LEU B CD2 1 
ATOM   5576 N N   . ASP B 1 316 ? -11.502 -17.004 36.395  1.00 18.32 ?  316 ASP B N   1 
ATOM   5577 C CA  . ASP B 1 316 ? -10.543 -18.096 36.344  1.00 19.92 ?  316 ASP B CA  1 
ATOM   5578 C C   . ASP B 1 316 ? -9.605  -17.896 35.158  1.00 21.76 ?  316 ASP B C   1 
ATOM   5579 O O   . ASP B 1 316 ? -10.047 -17.742 34.019  1.00 23.27 ?  316 ASP B O   1 
ATOM   5580 C CB  . ASP B 1 316 ? -11.305 -19.412 36.224  1.00 23.86 ?  316 ASP B CB  1 
ATOM   5581 C CG  . ASP B 1 316 ? -10.437 -20.632 36.460  1.00 28.75 ?  316 ASP B CG  1 
ATOM   5582 O OD1 . ASP B 1 316 ? -9.227  -20.486 36.771  1.00 28.87 ?  316 ASP B OD1 1 
ATOM   5583 O OD2 . ASP B 1 316 ? -10.995 -21.748 36.340  1.00 31.32 -1 316 ASP B OD2 1 
ATOM   5584 N N   . SER B 1 317 ? -8.308  -17.871 35.432  1.00 22.07 ?  317 SER B N   1 
ATOM   5585 C CA  . SER B 1 317 ? -7.296  -17.684 34.406  1.00 20.06 ?  317 SER B CA  1 
ATOM   5586 C C   . SER B 1 317 ? -6.135  -18.598 34.740  1.00 21.46 ?  317 SER B C   1 
ATOM   5587 O O   . SER B 1 317 ? -5.882  -18.888 35.913  1.00 22.27 ?  317 SER B O   1 
ATOM   5588 C CB  . SER B 1 317 ? -6.821  -16.218 34.322  1.00 19.55 ?  317 SER B CB  1 
ATOM   5589 O OG  . SER B 1 317 ? -6.344  -15.764 35.577  1.00 20.74 ?  317 SER B OG  1 
ATOM   5590 N N   . ASN B 1 318 ? -5.441  -19.077 33.708  1.00 16.12 ?  318 ASN B N   1 
ATOM   5591 C CA  . ASN B 1 318 ? -4.305  -19.956 33.928  1.00 16.21 ?  318 ASN B CA  1 
ATOM   5592 C C   . ASN B 1 318 ? -2.981  -19.346 33.473  1.00 16.78 ?  318 ASN B C   1 
ATOM   5593 O O   . ASN B 1 318 ? -1.938  -20.007 33.590  1.00 18.84 ?  318 ASN B O   1 
ATOM   5594 C CB  . ASN B 1 318 ? -4.544  -21.311 33.244  1.00 17.33 ?  318 ASN B CB  1 
ATOM   5595 C CG  . ASN B 1 318 ? -4.643  -21.204 31.733  1.00 19.51 ?  318 ASN B CG  1 
ATOM   5596 O OD1 . ASN B 1 318 ? -4.554  -20.114 31.166  1.00 17.47 ?  318 ASN B OD1 1 
ATOM   5597 N ND2 . ASN B 1 318 ? -4.809  -22.348 31.066  1.00 20.19 ?  318 ASN B ND2 1 
ATOM   5598 N N   . ALA B 1 319 ? -3.043  -18.123 32.963  1.00 14.41 ?  319 ALA B N   1 
ATOM   5599 C CA  . ALA B 1 319 ? -1.824  -17.496 32.436  1.00 14.97 ?  319 ALA B CA  1 
ATOM   5600 C C   . ALA B 1 319 ? -1.790  -15.997 32.672  1.00 15.21 ?  319 ALA B C   1 
ATOM   5601 O O   . ALA B 1 319 ? -2.843  -15.419 32.863  1.00 16.11 ?  319 ALA B O   1 
ATOM   5602 C CB  . ALA B 1 319 ? -1.665  -17.806 30.971  1.00 15.89 ?  319 ALA B CB  1 
ATOM   5603 N N   . SER B 1 320 ? -0.578  -15.448 32.669  1.00 14.18 ?  320 SER B N   1 
ATOM   5604 C CA  . SER B 1 320 ? -0.365  -13.997 32.846  1.00 14.53 ?  320 SER B CA  1 
ATOM   5605 C C   . SER B 1 320 ? -0.452  -13.556 34.303  1.00 14.85 ?  320 SER B C   1 
ATOM   5606 O O   . SER B 1 320 ? -0.960  -14.298 35.116  1.00 15.41 ?  320 SER B O   1 
ATOM   5607 C CB  . SER B 1 320 ? -1.205  -13.132 31.937  1.00 17.95 ?  320 SER B CB  1 
ATOM   5608 O OG  . SER B 1 320 ? -2.357  -12.646 32.614  1.00 19.18 ?  320 SER B OG  1 
ATOM   5609 N N   . TYR B 1 321 ? 0.069   -12.371 34.565  1.00 13.12 ?  321 TYR B N   1 
ATOM   5610 C CA  . TYR B 1 321 ? 0.014   -11.772 35.916  1.00 14.59 ?  321 TYR B CA  1 
ATOM   5611 C C   . TYR B 1 321 ? -1.085  -10.715 35.990  1.00 15.27 ?  321 TYR B C   1 
ATOM   5612 O O   . TYR B 1 321 ? -1.110  -9.973  36.950  1.00 17.33 ?  321 TYR B O   1 
ATOM   5613 C CB  . TYR B 1 321 ? 1.398   -11.248 36.285  1.00 15.70 ?  321 TYR B CB  1 
ATOM   5614 C CG  . TYR B 1 321 ? 2.053   -10.234 35.384  1.00 15.65 ?  321 TYR B CG  1 
ATOM   5615 C CD1 . TYR B 1 321 ? 1.561   -8.948  35.258  1.00 15.19 ?  321 TYR B CD1 1 
ATOM   5616 C CD2 . TYR B 1 321 ? 3.239   -10.535 34.743  1.00 16.64 ?  321 TYR B CD2 1 
ATOM   5617 C CE1 . TYR B 1 321 ? 2.196   -8.002  34.478  1.00 16.41 ?  321 TYR B CE1 1 
ATOM   5618 C CE2 . TYR B 1 321 ? 3.883   -9.604  33.951  1.00 16.14 ?  321 TYR B CE2 1 
ATOM   5619 C CZ  . TYR B 1 321 ? 3.365   -8.333  33.826  1.00 16.00 ?  321 TYR B CZ  1 
ATOM   5620 O OH  . TYR B 1 321 ? 3.998   -7.412  33.056  1.00 18.94 ?  321 TYR B OH  1 
ATOM   5621 N N   . LEU B 1 322 ? -1.974  -10.722 35.013  1.00 15.60 ?  322 LEU B N   1 
ATOM   5622 C CA  . LEU B 1 322 ? -3.076  -9.771  34.947  1.00 15.29 ?  322 LEU B CA  1 
ATOM   5623 C C   . LEU B 1 322 ? -4.381  -10.470 35.313  1.00 17.96 ?  322 LEU B C   1 
ATOM   5624 O O   . LEU B 1 322 ? -4.714  -11.525 34.753  1.00 18.16 ?  322 LEU B O   1 
ATOM   5625 C CB  . LEU B 1 322 ? -3.173  -9.160  33.547  1.00 16.74 ?  322 LEU B CB  1 
ATOM   5626 C CG  . LEU B 1 322 ? -1.870  -8.478  33.114  1.00 17.97 ?  322 LEU B CG  1 
ATOM   5627 C CD1 . LEU B 1 322 ? -1.798  -8.280  31.598  1.00 23.30 ?  322 LEU B CD1 1 
ATOM   5628 C CD2 . LEU B 1 322 ? -1.693  -7.149  33.861  1.00 18.42 ?  322 LEU B CD2 1 
ATOM   5629 N N   . ALA B 1 323 ? -5.121  -9.878  36.237  1.00 14.03 ?  323 ALA B N   1 
ATOM   5630 C CA  . ALA B 1 323 ? -6.413  -10.404 36.641  1.00 15.39 ?  323 ALA B CA  1 
ATOM   5631 C C   . ALA B 1 323 ? -7.497  -9.641  35.902  1.00 16.50 ?  323 ALA B C   1 
ATOM   5632 O O   . ALA B 1 323 ? -7.423  -8.415  35.767  1.00 15.91 ?  323 ALA B O   1 
ATOM   5633 C CB  . ALA B 1 323 ? -6.605  -10.292 38.154  1.00 13.72 ?  323 ALA B CB  1 
ATOM   5634 N N   . TRP B 1 324 ? -8.493  -10.378 35.414  1.00 15.70 ?  324 TRP B N   1 
ATOM   5635 C CA  . TRP B 1 324 ? -9.615  -9.850  34.646  1.00 16.66 ?  324 TRP B CA  1 
ATOM   5636 C C   . TRP B 1 324 ? -10.849 -10.032 35.516  1.00 15.66 ?  324 TRP B C   1 
ATOM   5637 O O   . TRP B 1 324 ? -11.224 -11.166 35.848  1.00 15.71 ?  324 TRP B O   1 
ATOM   5638 C CB  . TRP B 1 324 ? -9.729  -10.592 33.318  1.00 16.35 ?  324 TRP B CB  1 
ATOM   5639 C CG  . TRP B 1 324 ? -10.701 -10.082 32.269  1.00 15.04 ?  324 TRP B CG  1 
ATOM   5640 C CD1 . TRP B 1 324 ? -11.710 -10.793 31.704  1.00 14.67 ?  324 TRP B CD1 1 
ATOM   5641 C CD2 . TRP B 1 324 ? -10.688 -8.805  31.601  1.00 14.40 ?  324 TRP B CD2 1 
ATOM   5642 N NE1 . TRP B 1 324 ? -12.340 -10.050 30.742  1.00 14.70 ?  324 TRP B NE1 1 
ATOM   5643 C CE2 . TRP B 1 324 ? -11.740 -8.820  30.660  1.00 14.64 ?  324 TRP B CE2 1 
ATOM   5644 C CE3 . TRP B 1 324 ? -9.904  -7.655  31.716  1.00 14.60 ?  324 TRP B CE3 1 
ATOM   5645 C CZ2 . TRP B 1 324 ? -12.026 -7.731  29.826  1.00 14.26 ?  324 TRP B CZ2 1 
ATOM   5646 C CZ3 . TRP B 1 324 ? -10.187 -6.564  30.892  1.00 13.62 ?  324 TRP B CZ3 1 
ATOM   5647 C CH2 . TRP B 1 324 ? -11.242 -6.611  29.955  1.00 14.19 ?  324 TRP B CH2 1 
ATOM   5648 N N   . VAL B 1 325 ? -11.444 -8.920  35.920  1.00 14.61 ?  325 VAL B N   1 
ATOM   5649 C CA  . VAL B 1 325 ? -12.414 -8.888  37.009  1.00 15.42 ?  325 VAL B CA  1 
ATOM   5650 C C   . VAL B 1 325 ? -13.723 -8.347  36.468  1.00 15.11 ?  325 VAL B C   1 
ATOM   5651 O O   . VAL B 1 325 ? -13.795 -7.186  36.042  1.00 16.00 ?  325 VAL B O   1 
ATOM   5652 C CB  . VAL B 1 325 ? -11.922 -8.027  38.179  1.00 16.16 ?  325 VAL B CB  1 
ATOM   5653 C CG1 . VAL B 1 325 ? -12.889 -8.140  39.337  1.00 16.50 ?  325 VAL B CG1 1 
ATOM   5654 C CG2 . VAL B 1 325 ? -10.519 -8.455  38.595  1.00 15.05 ?  325 VAL B CG2 1 
ATOM   5655 N N   . ASP B 1 326 ? -14.753 -9.183  36.500  1.00 14.62 ?  326 ASP B N   1 
ATOM   5656 C CA  . ASP B 1 326 ? -16.105 -8.818  36.091  1.00 15.72 ?  326 ASP B CA  1 
ATOM   5657 C C   . ASP B 1 326 ? -16.709 -7.860  37.116  1.00 17.31 ?  326 ASP B C   1 
ATOM   5658 O O   . ASP B 1 326 ? -16.951 -8.245  38.268  1.00 16.61 ?  326 ASP B O   1 
ATOM   5659 C CB  . ASP B 1 326 ? -16.925 -10.100 35.965  1.00 16.55 ?  326 ASP B CB  1 
ATOM   5660 C CG  . ASP B 1 326 ? -18.363 -9.869  35.505  1.00 19.58 ?  326 ASP B CG  1 
ATOM   5661 O OD1 . ASP B 1 326 ? -18.924 -8.779  35.706  1.00 18.05 ?  326 ASP B OD1 1 
ATOM   5662 O OD2 . ASP B 1 326 ? -18.950 -10.819 34.949  1.00 21.90 -1 326 ASP B OD2 1 
ATOM   5663 N N   . ILE B 1 327 ? -16.978 -6.621  36.704  1.00 16.18 ?  327 ILE B N   1 
ATOM   5664 C CA  . ILE B 1 327 ? -17.622 -5.662  37.600  1.00 16.77 ?  327 ILE B CA  1 
ATOM   5665 C C   . ILE B 1 327 ? -19.040 -5.335  37.140  1.00 17.27 ?  327 ILE B C   1 
ATOM   5666 O O   . ILE B 1 327 ? -19.580 -4.284  37.493  1.00 18.11 ?  327 ILE B O   1 
ATOM   5667 C CB  . ILE B 1 327 ? -16.783 -4.377  37.743  1.00 17.13 ?  327 ILE B CB  1 
ATOM   5668 C CG1 . ILE B 1 327 ? -16.701 -3.625  36.407  1.00 17.56 ?  327 ILE B CG1 1 
ATOM   5669 C CG2 . ILE B 1 327 ? -15.394 -4.707  38.286  1.00 16.18 ?  327 ILE B CG2 1 
ATOM   5670 C CD1 . ILE B 1 327 ? -16.378 -2.144  36.552  1.00 18.02 ?  327 ILE B CD1 1 
ATOM   5671 N N   . SER B 1 328 ? -19.669 -6.251  36.397  1.00 17.56 ?  328 SER B N   1 
ATOM   5672 C CA  . SER B 1 328 ? -20.997 -5.987  35.837  1.00 18.51 ?  328 SER B CA  1 
ATOM   5673 C C   . SER B 1 328 ? -22.016 -5.676  36.928  1.00 21.75 ?  328 SER B C   1 
ATOM   5674 O O   . SER B 1 328 ? -22.920 -4.858  36.725  1.00 20.00 ?  328 SER B O   1 
ATOM   5675 C CB  . SER B 1 328 ? -21.469 -7.182  35.006  1.00 21.07 ?  328 SER B CB  1 
ATOM   5676 O OG  . SER B 1 328 ? -21.576 -8.337  35.821  1.00 21.45 ?  328 SER B OG  1 
ATOM   5677 N N   . ALA B 1 329 ? -21.889 -6.320  38.090  1.00 19.69 ?  329 ALA B N   1 
ATOM   5678 C CA  . ALA B 1 329 ? -22.860 -6.121  39.162  1.00 19.71 ?  329 ALA B CA  1 
ATOM   5679 C C   . ALA B 1 329 ? -22.815 -4.713  39.739  1.00 21.07 ?  329 ALA B C   1 
ATOM   5680 O O   . ALA B 1 329 ? -23.748 -4.318  40.445  1.00 23.55 ?  329 ALA B O   1 
ATOM   5681 C CB  . ALA B 1 329 ? -22.636 -7.140  40.280  1.00 21.68 ?  329 ALA B CB  1 
ATOM   5682 N N   . LEU B 1 330 ? -21.757 -3.951  39.478  1.00 18.16 ?  330 LEU B N   1 
ATOM   5683 C CA  . LEU B 1 330 ? -21.717 -2.573  39.945  1.00 19.75 ?  330 LEU B CA  1 
ATOM   5684 C C   . LEU B 1 330 ? -22.578 -1.634  39.106  1.00 21.16 ?  330 LEU B C   1 
ATOM   5685 O O   . LEU B 1 330 ? -22.846 -0.511  39.547  1.00 24.10 ?  330 LEU B O   1 
ATOM   5686 C CB  . LEU B 1 330 ? -20.274 -2.059  39.971  1.00 18.14 ?  330 LEU B CB  1 
ATOM   5687 C CG  . LEU B 1 330 ? -19.249 -2.824  40.804  1.00 21.54 ?  330 LEU B CG  1 
ATOM   5688 C CD1 . LEU B 1 330 ? -17.928 -2.094  40.747  1.00 21.52 ?  330 LEU B CD1 1 
ATOM   5689 C CD2 . LEU B 1 330 ? -19.709 -2.964  42.237  1.00 23.87 ?  330 LEU B CD2 1 
ATOM   5690 N N   . GLY B 1 331 ? -23.016 -2.056  37.923  1.00 22.41 ?  331 GLY B N   1 
ATOM   5691 C CA  . GLY B 1 331 ? -23.868 -1.215  37.093  1.00 24.95 ?  331 GLY B CA  1 
ATOM   5692 C C   . GLY B 1 331 ? -23.215 0.084   36.674  1.00 25.47 ?  331 GLY B C   1 
ATOM   5693 O O   . GLY B 1 331 ? -23.883 1.125   36.604  1.00 26.58 ?  331 GLY B O   1 
ATOM   5694 N N   . MET B 1 332 ? -21.917 0.046   36.391  1.00 22.85 ?  332 MET B N   1 
ATOM   5695 C CA  . MET B 1 332 ? -21.143 1.241   36.104  1.00 24.28 ?  332 MET B CA  1 
ATOM   5696 C C   . MET B 1 332 ? -20.141 0.906   35.010  1.00 24.15 ?  332 MET B C   1 
ATOM   5697 O O   . MET B 1 332 ? -19.476 -0.132  35.080  1.00 25.48 ?  332 MET B O   1 
ATOM   5698 C CB  . MET B 1 332 ? -20.430 1.722   37.371  1.00 23.33 ?  332 MET B CB  1 
ATOM   5699 C CG  . MET B 1 332 ? -19.921 3.131   37.318  1.00 25.43 ?  332 MET B CG  1 
ATOM   5700 S SD  . MET B 1 332 ? -19.153 3.539   38.890  1.00 30.86 ?  332 MET B SD  1 
ATOM   5701 C CE  . MET B 1 332 ? -18.562 5.188   38.556  1.00 23.93 ?  332 MET B CE  1 
ATOM   5702 N N   . ASN B 1 333 ? -20.064 1.756   33.987  1.00 22.06 ?  333 ASN B N   1 
ATOM   5703 C CA  . ASN B 1 333 ? -19.066 1.570   32.941  1.00 21.37 ?  333 ASN B CA  1 
ATOM   5704 C C   . ASN B 1 333 ? -17.673 1.538   33.556  1.00 20.68 ?  333 ASN B C   1 
ATOM   5705 O O   . ASN B 1 333 ? -17.360 2.316   34.460  1.00 21.39 ?  333 ASN B O   1 
ATOM   5706 C CB  . ASN B 1 333 ? -19.176 2.699   31.918  1.00 24.12 ?  333 ASN B CB  1 
ATOM   5707 C CG  . ASN B 1 333 ? -18.266 2.495   30.731  1.00 26.99 ?  333 ASN B CG  1 
ATOM   5708 O OD1 . ASN B 1 333 ? -17.051 2.649   30.827  1.00 27.43 ?  333 ASN B OD1 1 
ATOM   5709 N ND2 . ASN B 1 333 ? -18.854 2.147   29.599  1.00 32.54 ?  333 ASN B ND2 1 
ATOM   5710 N N   . ALA B 1 334 ? -16.837 0.612   33.080  1.00 20.12 ?  334 ALA B N   1 
ATOM   5711 C CA  . ALA B 1 334 ? -15.544 0.390   33.722  1.00 19.44 ?  334 ALA B CA  1 
ATOM   5712 C C   . ALA B 1 334 ? -14.681 1.658   33.749  1.00 21.36 ?  334 ALA B C   1 
ATOM   5713 O O   . ALA B 1 334 ? -13.967 1.907   34.730  1.00 19.08 ?  334 ALA B O   1 
ATOM   5714 C CB  . ALA B 1 334 ? -14.813 -0.749  33.019  1.00 20.07 ?  334 ALA B CB  1 
ATOM   5715 N N   . GLU B 1 335 ? -14.726 2.473   32.689  1.00 20.86 ?  335 GLU B N   1 
ATOM   5716 C CA  . GLU B 1 335 ? -13.904 3.680   32.672  1.00 21.50 ?  335 GLU B CA  1 
ATOM   5717 C C   . GLU B 1 335 ? -14.331 4.655   33.756  1.00 21.33 ?  335 GLU B C   1 
ATOM   5718 O O   . GLU B 1 335 ? -13.480 5.248   34.429  1.00 21.04 ?  335 GLU B O   1 
ATOM   5719 C CB  . GLU B 1 335 ? -13.956 4.347   31.297  1.00 25.31 ?  335 GLU B CB  1 
ATOM   5720 C CG  . GLU B 1 335 ? -13.409 3.459   30.233  1.00 30.53 ?  335 GLU B CG  1 
ATOM   5721 C CD  . GLU B 1 335 ? -12.437 4.138   29.306  1.00 38.25 ?  335 GLU B CD  1 
ATOM   5722 O OE1 . GLU B 1 335 ? -12.777 5.229   28.806  1.00 50.54 ?  335 GLU B OE1 1 
ATOM   5723 O OE2 . GLU B 1 335 ? -11.339 3.571   29.072  1.00 40.28 -1 335 GLU B OE2 1 
ATOM   5724 N N   . ASP B 1 336 ? -15.645 4.824   33.943  1.00 24.27 ?  336 ASP B N   1 
ATOM   5725 C CA  . ASP B 1 336 ? -16.146 5.664   35.027  1.00 23.96 ?  336 ASP B CA  1 
ATOM   5726 C C   . ASP B 1 336 ? -15.752 5.097   36.385  1.00 20.68 ?  336 ASP B C   1 
ATOM   5727 O O   . ASP B 1 336 ? -15.349 5.847   37.280  1.00 20.98 ?  336 ASP B O   1 
ATOM   5728 C CB  . ASP B 1 336 ? -17.668 5.812   34.924  1.00 26.75 ?  336 ASP B CB  1 
ATOM   5729 C CG  . ASP B 1 336 ? -18.113 6.357   33.574  1.00 29.41 ?  336 ASP B CG  1 
ATOM   5730 O OD1 . ASP B 1 336 ? -17.335 7.105   32.943  1.00 30.73 ?  336 ASP B OD1 1 
ATOM   5731 O OD2 . ASP B 1 336 ? -19.239 6.034   33.136  1.00 34.15 -1 336 ASP B OD2 1 
ATOM   5732 N N   . PHE B 1 337 ? -15.857 3.773   36.556  1.00 20.37 ?  337 PHE B N   1 
ATOM   5733 C CA  . PHE B 1 337 ? -15.515 3.160   37.838  1.00 17.78 ?  337 PHE B CA  1 
ATOM   5734 C C   . PHE B 1 337 ? -14.036 3.345   38.162  1.00 19.80 ?  337 PHE B C   1 
ATOM   5735 O O   . PHE B 1 337 ? -13.675 3.710   39.290  1.00 19.46 ?  337 PHE B O   1 
ATOM   5736 C CB  . PHE B 1 337 ? -15.877 1.675   37.836  1.00 19.92 ?  337 PHE B CB  1 
ATOM   5737 C CG  . PHE B 1 337 ? -15.382 0.948   39.050  1.00 18.05 ?  337 PHE B CG  1 
ATOM   5738 C CD1 . PHE B 1 337 ? -15.986 1.144   40.282  1.00 21.04 ?  337 PHE B CD1 1 
ATOM   5739 C CD2 . PHE B 1 337 ? -14.291 0.107   38.973  1.00 16.04 ?  337 PHE B CD2 1 
ATOM   5740 C CE1 . PHE B 1 337 ? -15.510 0.487   41.422  1.00 21.29 ?  337 PHE B CE1 1 
ATOM   5741 C CE2 . PHE B 1 337 ? -13.810 -0.548  40.093  1.00 19.88 ?  337 PHE B CE2 1 
ATOM   5742 C CZ  . PHE B 1 337 ? -14.420 -0.366  41.321  1.00 20.36 ?  337 PHE B CZ  1 
ATOM   5743 N N   . CYS B 1 338 ? -13.162 3.115   37.175  1.00 17.72 ?  338 CYS B N   1 
ATOM   5744 C CA  . CYS B 1 338 ? -11.726 3.277   37.401  1.00 19.26 ?  338 CYS B CA  1 
ATOM   5745 C C   . CYS B 1 338 ? -11.370 4.721   37.739  1.00 20.74 ?  338 CYS B C   1 
ATOM   5746 O O   . CYS B 1 338 ? -10.478 4.978   38.562  1.00 18.89 ?  338 CYS B O   1 
ATOM   5747 C CB  . CYS B 1 338 ? -10.955 2.806   36.165  1.00 17.99 ?  338 CYS B CB  1 
ATOM   5748 S SG  . CYS B 1 338 ? -11.010 0.980   36.003  1.00 18.80 ?  338 CYS B SG  1 
ATOM   5749 N N   . LYS B 1 339 ? -12.049 5.678   37.107  1.00 20.23 ?  339 LYS B N   1 
ATOM   5750 C CA  . LYS B 1 339 ? -11.834 7.077   37.444  1.00 19.63 ?  339 LYS B CA  1 
ATOM   5751 C C   . LYS B 1 339 ? -12.265 7.358   38.880  1.00 22.29 ?  339 LYS B C   1 
ATOM   5752 O O   . LYS B 1 339 ? -11.509 7.940   39.670  1.00 20.64 ?  339 LYS B O   1 
ATOM   5753 C CB  . LYS B 1 339 ? -12.591 7.960   36.453  1.00 24.42 ?  339 LYS B CB  1 
ATOM   5754 C CG  . LYS B 1 339 ? -12.526 9.443   36.785  1.00 27.11 ?  339 LYS B CG  1 
ATOM   5755 C CD  . LYS B 1 339 ? -13.040 10.309  35.635  1.00 34.51 ?  339 LYS B CD  1 
ATOM   5756 C CE  . LYS B 1 339 ? -13.203 11.769  36.063  1.00 34.20 ?  339 LYS B CE  1 
ATOM   5757 N NZ  . LYS B 1 339 ? -13.314 12.684  34.889  1.00 40.99 1  339 LYS B NZ  1 
ATOM   5758 N N   . TYR B 1 340 ? -13.477 6.925   39.240  1.00 20.28 ?  340 TYR B N   1 
ATOM   5759 C CA  . TYR B 1 340 ? -13.960 7.087   40.606  1.00 21.01 ?  340 TYR B CA  1 
ATOM   5760 C C   . TYR B 1 340 ? -13.039 6.393   41.598  1.00 21.06 ?  340 TYR B C   1 
ATOM   5761 O O   . TYR B 1 340 ? -12.695 6.954   42.646  1.00 21.79 ?  340 TYR B O   1 
ATOM   5762 C CB  . TYR B 1 340 ? -15.385 6.542   40.708  1.00 23.02 ?  340 TYR B CB  1 
ATOM   5763 C CG  . TYR B 1 340 ? -15.754 5.964   42.059  1.00 23.77 ?  340 TYR B CG  1 
ATOM   5764 C CD1 . TYR B 1 340 ? -15.543 4.618   42.341  1.00 26.48 ?  340 TYR B CD1 1 
ATOM   5765 C CD2 . TYR B 1 340 ? -16.346 6.753   43.043  1.00 28.14 ?  340 TYR B CD2 1 
ATOM   5766 C CE1 . TYR B 1 340 ? -15.888 4.076   43.566  1.00 26.25 ?  340 TYR B CE1 1 
ATOM   5767 C CE2 . TYR B 1 340 ? -16.696 6.216   44.277  1.00 26.66 ?  340 TYR B CE2 1 
ATOM   5768 C CZ  . TYR B 1 340 ? -16.458 4.875   44.528  1.00 28.28 ?  340 TYR B CZ  1 
ATOM   5769 O OH  . TYR B 1 340 ? -16.790 4.310   45.741  1.00 29.51 ?  340 TYR B OH  1 
ATOM   5770 N N   . LEU B 1 341 ? -12.597 5.176   41.291  1.00 20.60 ?  341 LEU B N   1 
ATOM   5771 C CA  . LEU B 1 341 ? -11.751 4.398   42.233  1.00 19.03 ?  341 LEU B CA  1 
ATOM   5772 C C   . LEU B 1 341 ? -10.415 5.101   42.462  1.00 19.02 ?  341 LEU B C   1 
ATOM   5773 O O   . LEU B 1 341 ? -9.954  5.127   43.585  1.00 19.40 ?  341 LEU B O   1 
ATOM   5774 C CB  . LEU B 1 341 ? -11.534 3.010   41.627  1.00 21.54 ?  341 LEU B CB  1 
ATOM   5775 C CG  . LEU B 1 341 ? -10.636 2.065   42.416  1.00 20.89 ?  341 LEU B CG  1 
ATOM   5776 C CD1 . LEU B 1 341 ? -11.318 1.620   43.693  1.00 19.01 ?  341 LEU B CD1 1 
ATOM   5777 C CD2 . LEU B 1 341 ? -10.286 0.863   41.573  1.00 20.03 ?  341 LEU B CD2 1 
ATOM   5778 N N   . ARG B 1 342 ? -9.847  5.648   41.394  1.00 18.41 ?  342 ARG B N   1 
ATOM   5779 C CA  . ARG B 1 342 ? -8.595  6.373   41.581  1.00 19.55 ?  342 ARG B CA  1 
ATOM   5780 C C   . ARG B 1 342 ? -8.801  7.623   42.423  1.00 22.45 ?  342 ARG B C   1 
ATOM   5781 O O   . ARG B 1 342 ? -7.990  7.926   43.308  1.00 21.41 ?  342 ARG B O   1 
ATOM   5782 C CB  . ARG B 1 342 ? -7.991  6.747   40.229  1.00 19.96 ?  342 ARG B CB  1 
ATOM   5783 C CG  . ARG B 1 342 ? -6.789  7.677   40.344  1.00 22.80 ?  342 ARG B CG  1 
ATOM   5784 C CD  . ARG B 1 342 ? -6.190  8.003   38.986  1.00 24.15 ?  342 ARG B CD  1 
ATOM   5785 N NE  . ARG B 1 342 ? -4.870  8.607   39.141  1.00 27.16 ?  342 ARG B NE  1 
ATOM   5786 C CZ  . ARG B 1 342 ? -4.020  8.824   38.143  1.00 28.93 ?  342 ARG B CZ  1 
ATOM   5787 N NH1 . ARG B 1 342 ? -4.350  8.488   36.906  1.00 30.07 1  342 ARG B NH1 1 
ATOM   5788 N NH2 . ARG B 1 342 ? -2.838  9.378   38.388  1.00 29.27 ?  342 ARG B NH2 1 
ATOM   5789 N N   . GLU B 1 343 ? -9.879  8.364   42.165  1.00 22.56 ?  343 GLU B N   1 
ATOM   5790 C CA  . GLU B 1 343 ? -10.111 9.579   42.933  1.00 21.61 ?  343 GLU B CA  1 
ATOM   5791 C C   . GLU B 1 343 ? -10.383 9.264   44.396  1.00 23.07 ?  343 GLU B C   1 
ATOM   5792 O O   . GLU B 1 343 ? -9.938  10.004  45.281  1.00 23.93 ?  343 GLU B O   1 
ATOM   5793 C CB  . GLU B 1 343 ? -11.249 10.383  42.303  1.00 25.50 ?  343 GLU B CB  1 
ATOM   5794 C CG  . GLU B 1 343 ? -10.802 11.066  40.998  1.00 31.60 ?  343 GLU B CG  1 
ATOM   5795 C CD  . GLU B 1 343 ? -11.934 11.340  39.998  1.00 36.90 ?  343 GLU B CD  1 
ATOM   5796 O OE1 . GLU B 1 343 ? -11.660 11.977  38.948  1.00 39.56 ?  343 GLU B OE1 1 
ATOM   5797 O OE2 . GLU B 1 343 ? -13.094 10.938  40.256  1.00 40.07 -1 343 GLU B OE2 1 
ATOM   5798 N N   . LYS B 1 344 ? -11.047 8.149   44.678  1.00 21.45 ?  344 LYS B N   1 
ATOM   5799 C CA  . LYS B 1 344 ? -11.437 7.863   46.050  1.00 22.50 ?  344 LYS B CA  1 
ATOM   5800 C C   . LYS B 1 344 ? -10.392 7.088   46.838  1.00 22.96 ?  344 LYS B C   1 
ATOM   5801 O O   . LYS B 1 344 ? -10.266 7.307   48.048  1.00 25.14 ?  344 LYS B O   1 
ATOM   5802 C CB  . LYS B 1 344 ? -12.775 7.124   46.063  1.00 22.15 ?  344 LYS B CB  1 
ATOM   5803 C CG  . LYS B 1 344 ? -13.950 8.000   45.587  1.00 25.94 ?  344 LYS B CG  1 
ATOM   5804 C CD  . LYS B 1 344 ? -14.105 9.323   46.400  1.00 31.16 ?  344 LYS B CD  1 
ATOM   5805 C CE  . LYS B 1 344 ? -13.466 10.570  45.711  1.00 35.01 ?  344 LYS B CE  1 
ATOM   5806 N NZ  . LYS B 1 344 ? -13.152 11.721  46.646  1.00 35.46 1  344 LYS B NZ  1 
ATOM   5807 N N   . THR B 1 345 ? -9.620  6.213   46.194  1.00 20.19 ?  345 THR B N   1 
ATOM   5808 C CA  . THR B 1 345 ? -8.689  5.355   46.907  1.00 19.23 ?  345 THR B CA  1 
ATOM   5809 C C   . THR B 1 345 ? -7.238  5.503   46.475  1.00 19.02 ?  345 THR B C   1 
ATOM   5810 O O   . THR B 1 345 ? -6.359  4.963   47.153  1.00 20.93 ?  345 THR B O   1 
ATOM   5811 C CB  . THR B 1 345 ? -9.074  3.879   46.730  1.00 22.13 ?  345 THR B CB  1 
ATOM   5812 O OG1 . THR B 1 345 ? -8.806  3.500   45.370  1.00 19.15 ?  345 THR B OG1 1 
ATOM   5813 C CG2 . THR B 1 345 ? -10.551 3.651   47.050  1.00 20.89 ?  345 THR B CG2 1 
ATOM   5814 N N   . GLY B 1 346 ? -6.960  6.175   45.361  1.00 17.83 ?  346 GLY B N   1 
ATOM   5815 C CA  . GLY B 1 346 ? -5.616  6.219   44.811  1.00 21.63 ?  346 GLY B CA  1 
ATOM   5816 C C   . GLY B 1 346 ? -5.198  4.987   44.033  1.00 19.97 ?  346 GLY B C   1 
ATOM   5817 O O   . GLY B 1 346 ? -4.094  4.973   43.469  1.00 19.19 ?  346 GLY B O   1 
ATOM   5818 N N   . LEU B 1 347 ? -6.067  3.986   43.980  1.00 17.76 ?  347 LEU B N   1 
ATOM   5819 C CA  . LEU B 1 347 ? -5.790  2.754   43.196  1.00 16.78 ?  347 LEU B CA  1 
ATOM   5820 C C   . LEU B 1 347 ? -6.025  3.003   41.709  1.00 16.85 ?  347 LEU B C   1 
ATOM   5821 O O   . LEU B 1 347 ? -7.090  3.461   41.361  1.00 16.05 ?  347 LEU B O   1 
ATOM   5822 C CB  . LEU B 1 347 ? -6.666  1.592   43.671  1.00 17.20 ?  347 LEU B CB  1 
ATOM   5823 C CG  . LEU B 1 347 ? -6.520  0.283   42.905  1.00 16.00 ?  347 LEU B CG  1 
ATOM   5824 C CD1 . LEU B 1 347 ? -5.102  -0.247  42.996  1.00 15.22 ?  347 LEU B CD1 1 
ATOM   5825 C CD2 . LEU B 1 347 ? -7.502  -0.750  43.424  1.00 18.58 ?  347 LEU B CD2 1 
ATOM   5826 N N   . ILE B 1 348 ? -5.025  2.677   40.893  1.00 17.05 ?  348 ILE B N   1 
ATOM   5827 C CA  . ILE B 1 348 ? -5.123  2.891   39.453  1.00 16.17 ?  348 ILE B CA  1 
ATOM   5828 C C   . ILE B 1 348 ? -5.087  1.526   38.776  1.00 18.91 ?  348 ILE B C   1 
ATOM   5829 O O   . ILE B 1 348 ? -4.033  0.873   38.724  1.00 17.45 ?  348 ILE B O   1 
ATOM   5830 C CB  . ILE B 1 348 ? -4.004  3.797   38.920  1.00 18.37 ?  348 ILE B CB  1 
ATOM   5831 C CG1 . ILE B 1 348 ? -3.960  5.111   39.701  1.00 18.76 ?  348 ILE B CG1 1 
ATOM   5832 C CG2 . ILE B 1 348 ? -4.215  4.068   37.442  1.00 18.82 ?  348 ILE B CG2 1 
ATOM   5833 C CD1 . ILE B 1 348 ? -2.692  5.909   39.482  1.00 24.43 ?  348 ILE B CD1 1 
ATOM   5834 N N   . ILE B 1 349 ? -6.230  1.094   38.250  1.00 15.22 ?  349 ILE B N   1 
ATOM   5835 C CA  . ILE B 1 349 ? -6.315  -0.153  37.511  1.00 16.61 ?  349 ILE B CA  1 
ATOM   5836 C C   . ILE B 1 349 ? -6.807  0.167   36.105  1.00 16.71 ?  349 ILE B C   1 
ATOM   5837 O O   . ILE B 1 349 ? -7.234  1.285   35.816  1.00 19.37 ?  349 ILE B O   1 
ATOM   5838 C CB  . ILE B 1 349 ? -7.212  -1.192  38.210  1.00 15.23 ?  349 ILE B CB  1 
ATOM   5839 C CG1 . ILE B 1 349 ? -8.608  -0.613  38.474  1.00 18.33 ?  349 ILE B CG1 1 
ATOM   5840 C CG2 . ILE B 1 349 ? -6.552  -1.633  39.510  1.00 14.13 ?  349 ILE B CG2 1 
ATOM   5841 C CD1 . ILE B 1 349 ? -9.568  -1.619  39.123  1.00 17.12 ?  349 ILE B CD1 1 
ATOM   5842 N N   . SER B 1 350 ? -6.701  -0.819  35.212  1.00 16.36 ?  350 SER B N   1 
ATOM   5843 C CA  . SER B 1 350 ? -7.071  -0.630  33.815  1.00 17.03 ?  350 SER B CA  1 
ATOM   5844 C C   . SER B 1 350 ? -8.561  -0.851  33.624  1.00 17.63 ?  350 SER B C   1 
ATOM   5845 O O   . SER B 1 350 ? -9.090  -1.902  33.997  1.00 17.42 ?  350 SER B O   1 
ATOM   5846 C CB  . SER B 1 350 ? -6.303  -1.583  32.905  1.00 20.14 ?  350 SER B CB  1 
ATOM   5847 O OG  . SER B 1 350 ? -4.915  -1.303  32.941  1.00 22.60 ?  350 SER B OG  1 
ATOM   5848 N N   . ALA B 1 351 ? -9.228  0.126   33.024  1.00 18.03 ?  351 ALA B N   1 
ATOM   5849 C CA  . ALA B 1 351 ? -10.602 -0.078  32.593  1.00 17.07 ?  351 ALA B CA  1 
ATOM   5850 C C   . ALA B 1 351 ? -10.620 -1.049  31.424  1.00 17.59 ?  351 ALA B C   1 
ATOM   5851 O O   . ALA B 1 351 ? -9.726  -1.040  30.576  1.00 17.87 ?  351 ALA B O   1 
ATOM   5852 C CB  . ALA B 1 351 ? -11.245 1.250   32.198  1.00 19.14 ?  351 ALA B CB  1 
ATOM   5853 N N   . GLY B 1 352 ? -11.631 -1.914  31.387  1.00 14.44 ?  352 GLY B N   1 
ATOM   5854 C CA  . GLY B 1 352 ? -11.657 -2.912  30.335  1.00 15.34 ?  352 GLY B CA  1 
ATOM   5855 C C   . GLY B 1 352 ? -12.073 -2.408  28.967  1.00 15.38 ?  352 GLY B C   1 
ATOM   5856 O O   . GLY B 1 352 ? -11.933 -3.153  27.992  1.00 14.86 ?  352 GLY B O   1 
ATOM   5857 N N   . ASN B 1 353 ? -12.569 -1.168  28.875  1.00 16.36 ?  353 ASN B N   1 
ATOM   5858 C CA  . ASN B 1 353 ? -13.180 -0.681  27.637  1.00 18.27 ?  353 ASN B CA  1 
ATOM   5859 C C   . ASN B 1 353 ? -12.230 -0.761  26.447  1.00 17.67 ?  353 ASN B C   1 
ATOM   5860 O O   . ASN B 1 353 ? -12.645 -1.137  25.346  1.00 17.09 ?  353 ASN B O   1 
ATOM   5861 C CB  . ASN B 1 353 ? -13.654 0.760   27.815  1.00 19.98 ?  353 ASN B CB  1 
ATOM   5862 C CG  . ASN B 1 353 ? -14.704 0.896   28.900  1.00 23.13 ?  353 ASN B CG  1 
ATOM   5863 O OD1 . ASN B 1 353 ? -14.466 0.539   30.056  1.00 21.89 ?  353 ASN B OD1 1 
ATOM   5864 N ND2 . ASN B 1 353 ? -15.863 1.434   28.539  1.00 22.84 ?  353 ASN B ND2 1 
ATOM   5865 N N   . GLY B 1 354 ? -10.960 -0.387  26.642  1.00 17.40 ?  354 GLY B N   1 
ATOM   5866 C CA  . GLY B 1 354 ? -10.012 -0.363  25.541  1.00 20.05 ?  354 GLY B CA  1 
ATOM   5867 C C   . GLY B 1 354 ? -9.773  -1.712  24.902  1.00 19.05 ?  354 GLY B C   1 
ATOM   5868 O O   . GLY B 1 354 ? -9.303  -1.778  23.760  1.00 16.55 ?  354 GLY B O   1 
ATOM   5869 N N   . TYR B 1 355 ? -10.100 -2.791  25.598  1.00 15.71 ?  355 TYR B N   1 
ATOM   5870 C CA  . TYR B 1 355 ? -9.963  -4.150  24.994  1.00 16.88 ?  355 TYR B CA  1 
ATOM   5871 C C   . TYR B 1 355 ? -11.158 -4.494  24.094  1.00 15.83 ?  355 TYR B C   1 
ATOM   5872 O O   . TYR B 1 355 ? -11.162 -5.539  23.501  1.00 14.53 ?  355 TYR B O   1 
ATOM   5873 C CB  . TYR B 1 355 ? -9.725  -5.177  26.100  1.00 16.76 ?  355 TYR B CB  1 
ATOM   5874 C CG  . TYR B 1 355 ? -8.568  -4.817  26.986  1.00 16.91 ?  355 TYR B CG  1 
ATOM   5875 C CD1 . TYR B 1 355 ? -7.272  -5.055  26.579  1.00 16.74 ?  355 TYR B CD1 1 
ATOM   5876 C CD2 . TYR B 1 355 ? -8.768  -4.198  28.205  1.00 17.73 ?  355 TYR B CD2 1 
ATOM   5877 C CE1 . TYR B 1 355 ? -6.197  -4.707  27.370  1.00 18.59 ?  355 TYR B CE1 1 
ATOM   5878 C CE2 . TYR B 1 355 ? -7.706  -3.840  29.009  1.00 19.97 ?  355 TYR B CE2 1 
ATOM   5879 C CZ  . TYR B 1 355 ? -6.419  -4.094  28.584  1.00 20.90 ?  355 TYR B CZ  1 
ATOM   5880 O OH  . TYR B 1 355 ? -5.367  -3.754  29.363  1.00 20.53 ?  355 TYR B OH  1 
ATOM   5881 N N   . ARG B 1 356 ? -12.112 -3.589  24.042  1.00 15.08 ?  356 ARG B N   1 
ATOM   5882 C CA  . ARG B 1 356 ? -13.339 -3.777  23.249  1.00 14.86 ?  356 ARG B CA  1 
ATOM   5883 C C   . ARG B 1 356 ? -14.050 -5.053  23.711  1.00 17.17 ?  356 ARG B C   1 
ATOM   5884 O O   . ARG B 1 356 ? -13.964 -5.385  24.869  1.00 15.36 ?  356 ARG B O   1 
ATOM   5885 C CB  . ARG B 1 356 ? -13.069 -3.721  21.739  1.00 14.49 ?  356 ARG B CB  1 
ATOM   5886 C CG  . ARG B 1 356 ? -12.463 -2.404  21.279  1.00 17.78 ?  356 ARG B CG  1 
ATOM   5887 C CD  . ARG B 1 356 ? -12.294 -2.285  19.775  1.00 15.87 ?  356 ARG B CD  1 
ATOM   5888 N NE  . ARG B 1 356 ? -11.586 -1.073  19.402  1.00 16.47 ?  356 ARG B NE  1 
ATOM   5889 C CZ  . ARG B 1 356 ? -11.200 -0.772  18.171  1.00 18.77 ?  356 ARG B CZ  1 
ATOM   5890 N NH1 . ARG B 1 356 ? -11.430 -1.614  17.184  1.00 19.20 1  356 ARG B NH1 1 
ATOM   5891 N NH2 . ARG B 1 356 ? -10.571 0.361   17.934  1.00 19.32 ?  356 ARG B NH2 1 
ATOM   5892 N N   . GLY B 1 357 ? -14.726 -5.732  22.795  1.00 16.68 ?  357 GLY B N   1 
ATOM   5893 C CA  . GLY B 1 357 ? -15.561 -6.858  23.234  1.00 17.18 ?  357 GLY B CA  1 
ATOM   5894 C C   . GLY B 1 357 ? -16.518 -6.432  24.336  1.00 17.23 ?  357 GLY B C   1 
ATOM   5895 O O   . GLY B 1 357 ? -17.115 -5.378  24.222  1.00 16.55 ?  357 GLY B O   1 
ATOM   5896 N N   . ASN B 1 358 ? -16.620 -7.234  25.391  1.00 16.16 ?  358 ASN B N   1 
ATOM   5897 C CA  . ASN B 1 358 ? -17.424 -6.852  26.549  1.00 17.73 ?  358 ASN B CA  1 
ATOM   5898 C C   . ASN B 1 358 ? -16.589 -6.206  27.654  1.00 19.17 ?  358 ASN B C   1 
ATOM   5899 O O   . ASN B 1 358 ? -16.987 -6.218  28.831  1.00 17.92 ?  358 ASN B O   1 
ATOM   5900 C CB  . ASN B 1 358 ? -18.210 -8.058  27.085  1.00 19.61 ?  358 ASN B CB  1 
ATOM   5901 C CG  . ASN B 1 358 ? -17.321 -9.152  27.677  1.00 20.59 ?  358 ASN B CG  1 
ATOM   5902 O OD1 . ASN B 1 358 ? -16.119 -9.221  27.418  1.00 14.76 ?  358 ASN B OD1 1 
ATOM   5903 N ND2 . ASN B 1 358 ? -17.928 -10.028 28.472  1.00 20.78 ?  358 ASN B ND2 1 
ATOM   5904 N N   . GLY B 1 359 ? -15.450 -5.608  27.288  1.00 17.25 ?  359 GLY B N   1 
ATOM   5905 C CA  . GLY B 1 359 ? -14.522 -5.041  28.254  1.00 17.84 ?  359 GLY B CA  1 
ATOM   5906 C C   . GLY B 1 359 ? -15.094 -3.928  29.120  1.00 17.95 ?  359 GLY B C   1 
ATOM   5907 O O   . GLY B 1 359 ? -14.592 -3.704  30.223  1.00 16.59 ?  359 GLY B O   1 
ATOM   5908 N N   . HIS B 1 360 ? -16.134 -3.229  28.654  1.00 18.64 ?  360 HIS B N   1 
ATOM   5909 C CA  . HIS B 1 360 ? -16.736 -2.169  29.463  1.00 20.61 ?  360 HIS B CA  1 
ATOM   5910 C C   . HIS B 1 360 ? -17.315 -2.677  30.785  1.00 21.10 ?  360 HIS B C   1 
ATOM   5911 O O   . HIS B 1 360 ? -17.653 -1.855  31.646  1.00 21.15 ?  360 HIS B O   1 
ATOM   5912 C CB  . HIS B 1 360 ? -17.841 -1.467  28.672  1.00 22.79 ?  360 HIS B CB  1 
ATOM   5913 C CG  . HIS B 1 360 ? -19.051 -2.319  28.476  1.00 25.25 ?  360 HIS B CG  1 
ATOM   5914 N ND1 . HIS B 1 360 ? -19.087 -3.356  27.568  1.00 27.53 ?  360 HIS B ND1 1 
ATOM   5915 C CD2 . HIS B 1 360 ? -20.251 -2.324  29.104  1.00 27.71 ?  360 HIS B CD2 1 
ATOM   5916 C CE1 . HIS B 1 360 ? -20.268 -3.947  27.626  1.00 27.78 ?  360 HIS B CE1 1 
ATOM   5917 N NE2 . HIS B 1 360 ? -20.992 -3.340  28.551  1.00 30.43 ?  360 HIS B NE2 1 
ATOM   5918 N N   . GLU B 1 361 ? -17.458 -3.993  30.959  1.00 18.35 ?  361 GLU B N   1 
ATOM   5919 C CA  . GLU B 1 361 ? -17.930 -4.591  32.203  1.00 20.21 ?  361 GLU B CA  1 
ATOM   5920 C C   . GLU B 1 361 ? -16.801 -5.152  33.056  1.00 16.87 ?  361 GLU B C   1 
ATOM   5921 O O   . GLU B 1 361 ? -17.074 -5.862  34.029  1.00 16.17 ?  361 GLU B O   1 
ATOM   5922 C CB  . GLU B 1 361 ? -18.936 -5.706  31.907  1.00 23.78 ?  361 GLU B CB  1 
ATOM   5923 C CG  . GLU B 1 361 ? -20.274 -5.222  31.382  1.00 28.89 ?  361 GLU B CG  1 
ATOM   5924 C CD  . GLU B 1 361 ? -21.172 -6.374  30.972  1.00 33.06 ?  361 GLU B CD  1 
ATOM   5925 O OE1 . GLU B 1 361 ? -20.673 -7.524  30.920  1.00 37.37 ?  361 GLU B OE1 1 
ATOM   5926 O OE2 . GLU B 1 361 ? -22.367 -6.132  30.697  1.00 42.43 -1 361 GLU B OE2 1 
ATOM   5927 N N   . PHE B 1 362 ? -15.544 -4.860  32.721  1.00 15.11 ?  362 PHE B N   1 
ATOM   5928 C CA  . PHE B 1 362 ? -14.417 -5.489  33.391  1.00 17.62 ?  362 PHE B CA  1 
ATOM   5929 C C   . PHE B 1 362 ? -13.358 -4.460  33.745  1.00 15.65 ?  362 PHE B C   1 
ATOM   5930 O O   . PHE B 1 362 ? -13.271 -3.383  33.152  1.00 15.85 ?  362 PHE B O   1 
ATOM   5931 C CB  . PHE B 1 362 ? -13.762 -6.573  32.533  1.00 13.28 ?  362 PHE B CB  1 
ATOM   5932 C CG  . PHE B 1 362 ? -14.591 -7.813  32.358  1.00 15.04 ?  362 PHE B CG  1 
ATOM   5933 C CD1 . PHE B 1 362 ? -15.621 -7.845  31.436  1.00 17.39 ?  362 PHE B CD1 1 
ATOM   5934 C CD2 . PHE B 1 362 ? -14.313 -8.959  33.103  1.00 18.58 ?  362 PHE B CD2 1 
ATOM   5935 C CE1 . PHE B 1 362 ? -16.381 -8.995  31.265  1.00 18.99 ?  362 PHE B CE1 1 
ATOM   5936 C CE2 . PHE B 1 362 ? -15.053 -10.113 32.942  1.00 15.50 ?  362 PHE B CE2 1 
ATOM   5937 C CZ  . PHE B 1 362 ? -16.096 -10.132 32.013  1.00 16.34 ?  362 PHE B CZ  1 
ATOM   5938 N N   . VAL B 1 363 ? -12.535 -4.816  34.720  1.00 14.81 ?  363 VAL B N   1 
ATOM   5939 C CA  . VAL B 1 363 ? -11.296 -4.097  34.984  1.00 14.99 ?  363 VAL B CA  1 
ATOM   5940 C C   . VAL B 1 363 ? -10.167 -5.115  34.940  1.00 15.72 ?  363 VAL B C   1 
ATOM   5941 O O   . VAL B 1 363 ? -10.380 -6.315  35.154  1.00 13.95 ?  363 VAL B O   1 
ATOM   5942 C CB  . VAL B 1 363 ? -11.320 -3.343  36.336  1.00 15.13 ?  363 VAL B CB  1 
ATOM   5943 C CG1 . VAL B 1 363 ? -12.434 -2.308  36.356  1.00 15.77 ?  363 VAL B CG1 1 
ATOM   5944 C CG2 . VAL B 1 363 ? -11.472 -4.323  37.498  1.00 14.55 ?  363 VAL B CG2 1 
ATOM   5945 N N   . ARG B 1 364 ? -8.957  -4.638  34.647  1.00 15.28 ?  364 ARG B N   1 
ATOM   5946 C CA  . ARG B 1 364 ? -7.777  -5.497  34.598  1.00 16.73 ?  364 ARG B CA  1 
ATOM   5947 C C   . ARG B 1 364 ? -6.795  -5.017  35.651  1.00 15.47 ?  364 ARG B C   1 
ATOM   5948 O O   . ARG B 1 364 ? -6.471  -3.827  35.695  1.00 16.15 ?  364 ARG B O   1 
ATOM   5949 C CB  . ARG B 1 364 ? -7.117  -5.482  33.217  1.00 15.17 ?  364 ARG B CB  1 
ATOM   5950 C CG  . ARG B 1 364 ? -6.166  -6.663  32.976  1.00 17.36 ?  364 ARG B CG  1 
ATOM   5951 C CD  . ARG B 1 364 ? -5.363  -6.457  31.697  1.00 19.55 ?  364 ARG B CD  1 
ATOM   5952 N NE  . ARG B 1 364 ? -4.341  -5.437  31.914  1.00 18.66 ?  364 ARG B NE  1 
ATOM   5953 C CZ  . ARG B 1 364 ? -3.370  -5.148  31.066  1.00 22.33 ?  364 ARG B CZ  1 
ATOM   5954 N NH1 . ARG B 1 364 ? -3.276  -5.798  29.906  1.00 22.00 1  364 ARG B NH1 1 
ATOM   5955 N NH2 . ARG B 1 364 ? -2.490  -4.210  31.387  1.00 21.53 ?  364 ARG B NH2 1 
ATOM   5956 N N   . ILE B 1 365 ? -6.331  -5.935  36.499  1.00 14.74 ?  365 ILE B N   1 
ATOM   5957 C CA  . ILE B 1 365 ? -5.478  -5.602  37.634  1.00 14.98 ?  365 ILE B CA  1 
ATOM   5958 C C   . ILE B 1 365 ? -4.166  -6.373  37.522  1.00 13.74 ?  365 ILE B C   1 
ATOM   5959 O O   . ILE B 1 365 ? -4.164  -7.602  37.373  1.00 14.72 ?  365 ILE B O   1 
ATOM   5960 C CB  . ILE B 1 365 ? -6.182  -5.905  38.976  1.00 11.84 ?  365 ILE B CB  1 
ATOM   5961 C CG1 . ILE B 1 365 ? -7.525  -5.171  39.054  1.00 13.33 ?  365 ILE B CG1 1 
ATOM   5962 C CG2 . ILE B 1 365 ? -5.298  -5.521  40.130  1.00 13.28 ?  365 ILE B CG2 1 
ATOM   5963 C CD1 . ILE B 1 365 ? -8.391  -5.609  40.244  1.00 13.49 ?  365 ILE B CD1 1 
ATOM   5964 N N   . ASN B 1 366 ? -3.061  -5.651  37.625  1.00 13.70 ?  366 ASN B N   1 
ATOM   5965 C CA  . ASN B 1 366 ? -1.716  -6.204  37.516  1.00 14.60 ?  366 ASN B CA  1 
ATOM   5966 C C   . ASN B 1 366 ? -1.240  -6.682  38.892  1.00 15.27 ?  366 ASN B C   1 
ATOM   5967 O O   . ASN B 1 366 ? -1.073  -5.878  39.818  1.00 17.87 ?  366 ASN B O   1 
ATOM   5968 C CB  . ASN B 1 366 ? -0.802  -5.119  36.943  1.00 15.27 ?  366 ASN B CB  1 
ATOM   5969 C CG  . ASN B 1 366 ? 0.662   -5.536  36.852  1.00 17.21 ?  366 ASN B CG  1 
ATOM   5970 O OD1 . ASN B 1 366 ? 1.082   -6.578  37.366  1.00 16.28 ?  366 ASN B OD1 1 
ATOM   5971 N ND2 . ASN B 1 366 ? 1.460   -4.694  36.180  1.00 17.25 ?  366 ASN B ND2 1 
ATOM   5972 N N   . LEU B 1 367 ? -1.002  -7.986  39.022  1.00 14.04 ?  367 LEU B N   1 
ATOM   5973 C CA  . LEU B 1 367 ? -0.636  -8.586  40.303  1.00 16.26 ?  367 LEU B CA  1 
ATOM   5974 C C   . LEU B 1 367 ? 0.842   -8.926  40.399  1.00 15.03 ?  367 LEU B C   1 
ATOM   5975 O O   . LEU B 1 367 ? 1.260   -9.575  41.369  1.00 14.38 ?  367 LEU B O   1 
ATOM   5976 C CB  . LEU B 1 367 ? -1.471  -9.842  40.560  1.00 15.30 ?  367 LEU B CB  1 
ATOM   5977 C CG  . LEU B 1 367 ? -2.975  -9.614  40.716  1.00 13.28 ?  367 LEU B CG  1 
ATOM   5978 C CD1 . LEU B 1 367 ? -3.700  -10.935 40.993  1.00 16.05 ?  367 LEU B CD1 1 
ATOM   5979 C CD2 . LEU B 1 367 ? -3.246  -8.578  41.803  1.00 15.42 ?  367 LEU B CD2 1 
ATOM   5980 N N   . ALA B 1 368 ? 1.644   -8.499  39.427  1.00 14.75 ?  368 ALA B N   1 
ATOM   5981 C CA  . ALA B 1 368 ? 3.092   -8.721  39.466  1.00 15.87 ?  368 ALA B CA  1 
ATOM   5982 C C   . ALA B 1 368 ? 3.769   -7.600  40.251  1.00 16.04 ?  368 ALA B C   1 
ATOM   5983 O O   . ALA B 1 368 ? 4.551   -6.804  39.724  1.00 15.24 ?  368 ALA B O   1 
ATOM   5984 C CB  . ALA B 1 368 ? 3.657   -8.817  38.056  1.00 15.92 ?  368 ALA B CB  1 
ATOM   5985 N N   . CYS B 1 369 ? 3.445   -7.544  41.537  1.00 14.39 ?  369 CYS B N   1 
ATOM   5986 C CA  . CYS B 1 369 ? 4.120   -6.627  42.439  1.00 14.83 ?  369 CYS B CA  1 
ATOM   5987 C C   . CYS B 1 369 ? 4.274   -7.321  43.789  1.00 16.55 ?  369 CYS B C   1 
ATOM   5988 O O   . CYS B 1 369 ? 3.700   -8.402  43.994  1.00 15.34 ?  369 CYS B O   1 
ATOM   5989 C CB  . CYS B 1 369 ? 3.321   -5.343  42.594  1.00 13.98 ?  369 CYS B CB  1 
ATOM   5990 S SG  . CYS B 1 369 ? 1.602   -5.746  42.983  1.00 19.60 ?  369 CYS B SG  1 
ATOM   5991 N N   . PRO B 1 370 ? 5.040   -6.755  44.724  1.00 15.26 ?  370 PRO B N   1 
ATOM   5992 C CA  . PRO B 1 370 ? 5.194   -7.396  46.036  1.00 16.99 ?  370 PRO B CA  1 
ATOM   5993 C C   . PRO B 1 370 ? 3.852   -7.604  46.719  1.00 19.82 ?  370 PRO B C   1 
ATOM   5994 O O   . PRO B 1 370 ? 2.885   -6.875  46.482  1.00 16.73 ?  370 PRO B O   1 
ATOM   5995 C CB  . PRO B 1 370 ? 6.068   -6.406  46.808  1.00 20.77 ?  370 PRO B CB  1 
ATOM   5996 C CG  . PRO B 1 370 ? 6.906   -5.780  45.739  1.00 20.08 ?  370 PRO B CG  1 
ATOM   5997 C CD  . PRO B 1 370 ? 5.961   -5.613  44.570  1.00 16.92 ?  370 PRO B CD  1 
ATOM   5998 N N   . LYS B 1 371 ? 3.801   -8.624  47.575  1.00 17.57 ?  371 LYS B N   1 
ATOM   5999 C CA  . LYS B 1 371 ? 2.532   -8.980  48.199  1.00 19.28 ?  371 LYS B CA  1 
ATOM   6000 C C   . LYS B 1 371 ? 1.944   -7.816  48.992  1.00 17.17 ?  371 LYS B C   1 
ATOM   6001 O O   . LYS B 1 371 ? 0.724   -7.652  49.016  1.00 16.90 ?  371 LYS B O   1 
ATOM   6002 C CB  . LYS B 1 371 ? 2.699   -10.210 49.082  1.00 17.59 ?  371 LYS B CB  1 
ATOM   6003 C CG  . LYS B 1 371 ? 1.363   -10.807 49.533  1.00 20.37 ?  371 LYS B CG  1 
ATOM   6004 C CD  . LYS B 1 371 ? 1.477   -12.295 49.728  1.00 26.32 ?  371 LYS B CD  1 
ATOM   6005 C CE  . LYS B 1 371 ? 0.156   -12.920 50.169  1.00 25.93 ?  371 LYS B CE  1 
ATOM   6006 N NZ  . LYS B 1 371 ? 0.355   -14.368 50.477  1.00 30.56 1  371 LYS B NZ  1 
ATOM   6007 N N   . GLU B 1 372 ? 2.784   -6.982  49.629  1.00 19.92 ?  372 GLU B N   1 
ATOM   6008 C CA  . GLU B 1 372 ? 2.252   -5.823  50.359  1.00 21.64 ?  372 GLU B CA  1 
ATOM   6009 C C   . GLU B 1 372 ? 1.420   -4.925  49.459  1.00 20.03 ?  372 GLU B C   1 
ATOM   6010 O O   . GLU B 1 372 ? 0.390   -4.379  49.885  1.00 17.58 ?  372 GLU B O   1 
ATOM   6011 C CB  . GLU B 1 372 ? 3.373   -4.984  50.971  1.00 26.68 ?  372 GLU B CB  1 
ATOM   6012 C CG  . GLU B 1 372 ? 4.365   -5.676  51.841  1.00 34.94 ?  372 GLU B CG  1 
ATOM   6013 C CD  . GLU B 1 372 ? 5.396   -6.416  51.063  1.00 47.35 ?  372 GLU B CD  1 
ATOM   6014 O OE1 . GLU B 1 372 ? 5.473   -7.627  51.145  1.00 52.65 ?  372 GLU B OE1 1 
ATOM   6015 O OE2 . GLU B 1 372 ? 6.133   -5.762  50.264  1.00 46.45 -1 372 GLU B OE2 1 
ATOM   6016 N N   . LEU B 1 373 ? 1.864   -4.736  48.215  1.00 17.97 ?  373 LEU B N   1 
ATOM   6017 C CA  . LEU B 1 373 ? 1.094   -3.912  47.289  1.00 16.85 ?  373 LEU B CA  1 
ATOM   6018 C C   . LEU B 1 373 ? -0.202  -4.602  46.895  1.00 16.93 ?  373 LEU B C   1 
ATOM   6019 O O   . LEU B 1 373 ? -1.238  -3.944  46.741  1.00 15.61 ?  373 LEU B O   1 
ATOM   6020 C CB  . LEU B 1 373 ? 1.924   -3.579  46.048  1.00 18.05 ?  373 LEU B CB  1 
ATOM   6021 C CG  . LEU B 1 373 ? 2.698   -2.256  46.094  1.00 20.27 ?  373 LEU B CG  1 
ATOM   6022 C CD1 . LEU B 1 373 ? 3.740   -2.320  47.165  1.00 22.05 ?  373 LEU B CD1 1 
ATOM   6023 C CD2 . LEU B 1 373 ? 3.358   -1.922  44.748  1.00 19.33 ?  373 LEU B CD2 1 
ATOM   6024 N N   . VAL B 1 374 ? -0.170  -5.928  46.730  1.00 15.72 ?  374 VAL B N   1 
ATOM   6025 C CA  . VAL B 1 374 ? -1.408  -6.647  46.428  1.00 15.54 ?  374 VAL B CA  1 
ATOM   6026 C C   . VAL B 1 374 ? -2.403  -6.496  47.576  1.00 15.86 ?  374 VAL B C   1 
ATOM   6027 O O   . VAL B 1 374 ? -3.584  -6.216  47.352  1.00 16.76 ?  374 VAL B O   1 
ATOM   6028 C CB  . VAL B 1 374 ? -1.129  -8.127  46.125  1.00 15.62 ?  374 VAL B CB  1 
ATOM   6029 C CG1 . VAL B 1 374 ? -2.449  -8.861  45.914  1.00 16.30 ?  374 VAL B CG1 1 
ATOM   6030 C CG2 . VAL B 1 374 ? -0.217  -8.263  44.895  1.00 16.92 ?  374 VAL B CG2 1 
ATOM   6031 N N   . ILE B 1 375 ? -1.936  -6.676  48.819  1.00 15.73 ?  375 ILE B N   1 
ATOM   6032 C CA  . ILE B 1 375 ? -2.808  -6.519  49.991  1.00 18.77 ?  375 ILE B CA  1 
ATOM   6033 C C   . ILE B 1 375 ? -3.398  -5.116  50.022  1.00 16.43 ?  375 ILE B C   1 
ATOM   6034 O O   . ILE B 1 375 ? -4.604  -4.930  50.217  1.00 17.03 ?  375 ILE B O   1 
ATOM   6035 C CB  . ILE B 1 375 ? -2.031  -6.819  51.291  1.00 20.00 ?  375 ILE B CB  1 
ATOM   6036 C CG1 . ILE B 1 375 ? -1.681  -8.306  51.404  1.00 19.36 ?  375 ILE B CG1 1 
ATOM   6037 C CG2 . ILE B 1 375 ? -2.822  -6.356  52.516  1.00 19.93 ?  375 ILE B CG2 1 
ATOM   6038 C CD1 . ILE B 1 375 ? -0.619  -8.594  52.451  1.00 19.14 ?  375 ILE B CD1 1 
ATOM   6039 N N   . ASP B 1 376 ? -2.550  -4.110  49.816  1.00 17.91 ?  376 ASP B N   1 
ATOM   6040 C CA  . ASP B 1 376 ? -3.001  -2.723  49.771  1.00 16.67 ?  376 ASP B CA  1 
ATOM   6041 C C   . ASP B 1 376 ? -4.049  -2.532  48.683  1.00 16.44 ?  376 ASP B C   1 
ATOM   6042 O O   . ASP B 1 376 ? -5.137  -2.004  48.940  1.00 15.31 ?  376 ASP B O   1 
ATOM   6043 C CB  . ASP B 1 376 ? -1.783  -1.813  49.540  1.00 18.17 ?  376 ASP B CB  1 
ATOM   6044 C CG  . ASP B 1 376 ? -2.106  -0.328  49.655  1.00 21.98 ?  376 ASP B CG  1 
ATOM   6045 O OD1 . ASP B 1 376 ? -3.265  0.038   49.990  1.00 19.80 ?  376 ASP B OD1 1 
ATOM   6046 O OD2 . ASP B 1 376 ? -1.180  0.479   49.405  1.00 20.37 -1 376 ASP B OD2 1 
ATOM   6047 N N   . GLY B 1 377 ? -3.745  -2.983  47.461  1.00 16.18 ?  377 GLY B N   1 
ATOM   6048 C CA  . GLY B 1 377 ? -4.643  -2.745  46.338  1.00 16.27 ?  377 GLY B CA  1 
ATOM   6049 C C   . GLY B 1 377 ? -5.994  -3.417  46.493  1.00 14.82 ?  377 GLY B C   1 
ATOM   6050 O O   . GLY B 1 377 ? -7.025  -2.847  46.138  1.00 15.70 ?  377 GLY B O   1 
ATOM   6051 N N   . MET B 1 378 ? -6.006  -4.654  46.990  1.00 16.74 ?  378 MET B N   1 
ATOM   6052 C CA  . MET B 1 378 ? -7.272  -5.354  47.188  1.00 15.99 ?  378 MET B CA  1 
ATOM   6053 C C   . MET B 1 378 ? -8.150  -4.627  48.197  1.00 15.85 ?  378 MET B C   1 
ATOM   6054 O O   . MET B 1 378 ? -9.365  -4.514  48.005  1.00 14.21 ?  378 MET B O   1 
ATOM   6055 C CB  . MET B 1 378 ? -7.022  -6.791  47.641  1.00 17.00 ?  378 MET B CB  1 
ATOM   6056 C CG  . MET B 1 378 ? -6.369  -7.694  46.585  1.00 13.76 ?  378 MET B CG  1 
ATOM   6057 S SD  . MET B 1 378 ? -7.335  -7.866  45.085  1.00 18.54 ?  378 MET B SD  1 
ATOM   6058 C CE  . MET B 1 378 ? -6.435  -6.795  43.972  1.00 17.90 ?  378 MET B CE  1 
ATOM   6059 N N   . GLN B 1 379 ? -7.552  -4.135  49.283  1.00 16.08 ?  379 GLN B N   1 
ATOM   6060 C CA  . GLN B 1 379 ? -8.322  -3.383  50.262  1.00 16.60 ?  379 GLN B CA  1 
ATOM   6061 C C   . GLN B 1 379 ? -8.861  -2.092  49.659  1.00 15.49 ?  379 GLN B C   1 
ATOM   6062 O O   . GLN B 1 379 ? -9.994  -1.692  49.943  1.00 14.75 ?  379 GLN B O   1 
ATOM   6063 C CB  . GLN B 1 379 ? -7.470  -3.100  51.500  1.00 17.38 ?  379 GLN B CB  1 
ATOM   6064 C CG  . GLN B 1 379 ? -8.193  -2.288  52.584  1.00 18.23 ?  379 GLN B CG  1 
ATOM   6065 C CD  . GLN B 1 379 ? -9.461  -2.954  53.105  1.00 17.34 ?  379 GLN B CD  1 
ATOM   6066 O OE1 . GLN B 1 379 ? -9.522  -4.173  53.251  1.00 18.40 ?  379 GLN B OE1 1 
ATOM   6067 N NE2 . GLN B 1 379 ? -10.473 -2.150  53.403  1.00 19.10 ?  379 GLN B NE2 1 
ATOM   6068 N N   . ARG B 1 380 ? -8.072  -1.436  48.807  1.00 15.52 ?  380 ARG B N   1 
ATOM   6069 C CA  . ARG B 1 380 ? -8.558  -0.224  48.154  1.00 17.00 ?  380 ARG B CA  1 
ATOM   6070 C C   . ARG B 1 380 ? -9.715  -0.530  47.216  1.00 16.07 ?  380 ARG B C   1 
ATOM   6071 O O   . ARG B 1 380 ? -10.683 0.236   47.145  1.00 16.15 ?  380 ARG B O   1 
ATOM   6072 C CB  . ARG B 1 380 ? -7.426  0.458   47.386  1.00 17.68 ?  380 ARG B CB  1 
ATOM   6073 C CG  . ARG B 1 380 ? -6.268  0.905   48.259  1.00 16.04 ?  380 ARG B CG  1 
ATOM   6074 C CD  . ARG B 1 380 ? -5.400  1.890   47.502  1.00 18.62 ?  380 ARG B CD  1 
ATOM   6075 N NE  . ARG B 1 380 ? -4.091  2.064   48.116  1.00 18.77 ?  380 ARG B NE  1 
ATOM   6076 C CZ  . ARG B 1 380 ? -3.287  3.093   47.864  1.00 19.46 ?  380 ARG B CZ  1 
ATOM   6077 N NH1 . ARG B 1 380 ? -3.677  4.044   47.027  1.00 17.78 1  380 ARG B NH1 1 
ATOM   6078 N NH2 . ARG B 1 380 ? -2.093  3.166   48.438  1.00 19.13 ?  380 ARG B NH2 1 
ATOM   6079 N N   . LEU B 1 381 ? -9.620  -1.633  46.465  1.00 14.72 ?  381 LEU B N   1 
ATOM   6080 C CA  . LEU B 1 381 ? -10.727 -2.044  45.609  1.00 16.71 ?  381 LEU B CA  1 
ATOM   6081 C C   . LEU B 1 381 ? -11.973 -2.335  46.431  1.00 17.36 ?  381 LEU B C   1 
ATOM   6082 O O   . LEU B 1 381 ? -13.087 -1.957  46.039  1.00 16.62 ?  381 LEU B O   1 
ATOM   6083 C CB  . LEU B 1 381 ? -10.331 -3.276  44.789  1.00 16.82 ?  381 LEU B CB  1 
ATOM   6084 C CG  . LEU B 1 381 ? -11.410 -3.857  43.870  1.00 17.60 ?  381 LEU B CG  1 
ATOM   6085 C CD1 . LEU B 1 381 ? -11.875 -2.833  42.845  1.00 21.38 ?  381 LEU B CD1 1 
ATOM   6086 C CD2 . LEU B 1 381 ? -10.883 -5.116  43.189  1.00 17.99 ?  381 LEU B CD2 1 
ATOM   6087 N N   . LYS B 1 382 ? -11.807 -3.008  47.575  1.00 15.73 ?  382 LYS B N   1 
ATOM   6088 C CA  . LYS B 1 382 ? -12.947 -3.240  48.460  1.00 17.66 ?  382 LYS B CA  1 
ATOM   6089 C C   . LYS B 1 382 ? -13.551 -1.917  48.912  1.00 18.60 ?  382 LYS B C   1 
ATOM   6090 O O   . LYS B 1 382 ? -14.770 -1.715  48.830  1.00 19.20 ?  382 LYS B O   1 
ATOM   6091 C CB  . LYS B 1 382 ? -12.528 -4.084  49.666  1.00 17.72 ?  382 LYS B CB  1 
ATOM   6092 C CG  . LYS B 1 382 ? -13.651 -4.273  50.680  1.00 19.75 ?  382 LYS B CG  1 
ATOM   6093 C CD  . LYS B 1 382 ? -13.158 -4.971  51.940  1.00 20.21 ?  382 LYS B CD  1 
ATOM   6094 C CE  . LYS B 1 382 ? -14.321 -5.317  52.868  1.00 22.25 ?  382 LYS B CE  1 
ATOM   6095 N NZ  . LYS B 1 382 ? -13.774 -5.807  54.158  1.00 21.54 1  382 LYS B NZ  1 
ATOM   6096 N N   . GLN B 1 383 ? -12.702 -0.991  49.368  1.00 17.38 ?  383 GLN B N   1 
ATOM   6097 C CA  . GLN B 1 383 ? -13.169 0.347   49.731  1.00 20.83 ?  383 GLN B CA  1 
ATOM   6098 C C   . GLN B 1 383 ? -13.956 0.998   48.605  1.00 21.48 ?  383 GLN B C   1 
ATOM   6099 O O   . GLN B 1 383 ? -15.035 1.558   48.832  1.00 23.60 ?  383 GLN B O   1 
ATOM   6100 C CB  . GLN B 1 383 ? -11.986 1.237   50.104  1.00 19.57 ?  383 GLN B CB  1 
ATOM   6101 C CG  . GLN B 1 383 ? -11.474 1.027   51.500  1.00 20.05 ?  383 GLN B CG  1 
ATOM   6102 C CD  . GLN B 1 383 ? -12.488 1.384   52.569  1.00 26.44 ?  383 GLN B CD  1 
ATOM   6103 O OE1 . GLN B 1 383 ? -13.020 0.509   53.255  1.00 26.57 ?  383 GLN B OE1 1 
ATOM   6104 N NE2 . GLN B 1 383 ? -12.753 2.676   52.726  1.00 27.99 ?  383 GLN B NE2 1 
ATOM   6105 N N   . GLY B 1 384 ? -13.426 0.954   47.382  1.00 19.56 ?  384 GLY B N   1 
ATOM   6106 C CA  . GLY B 1 384 ? -14.108 1.610   46.284  1.00 20.51 ?  384 GLY B CA  1 
ATOM   6107 C C   . GLY B 1 384 ? -15.460 0.997   45.982  1.00 23.80 ?  384 GLY B C   1 
ATOM   6108 O O   . GLY B 1 384 ? -16.429 1.717   45.725  1.00 27.40 ?  384 GLY B O   1 
ATOM   6109 N N   . VAL B 1 385 ? -15.553 -0.337  46.015  1.00 20.97 ?  385 VAL B N   1 
ATOM   6110 C CA  . VAL B 1 385 ? -16.816 -0.995  45.673  1.00 25.49 ?  385 VAL B CA  1 
ATOM   6111 C C   . VAL B 1 385 ? -17.885 -0.689  46.717  1.00 27.52 ?  385 VAL B C   1 
ATOM   6112 O O   . VAL B 1 385 ? -19.011 -0.313  46.380  1.00 29.48 ?  385 VAL B O   1 
ATOM   6113 C CB  . VAL B 1 385 ? -16.617 -2.512  45.510  1.00 27.61 ?  385 VAL B CB  1 
ATOM   6114 C CG1 . VAL B 1 385 ? -17.972 -3.229  45.503  1.00 27.75 ?  385 VAL B CG1 1 
ATOM   6115 C CG2 . VAL B 1 385 ? -15.846 -2.805  44.255  1.00 26.72 ?  385 VAL B CG2 1 
ATOM   6116 N N   . LEU B 1 386 ? -17.522 -0.871  47.978  1.00 28.85 ?  386 LEU B N   1 
ATOM   6117 C CA  . LEU B 1 386 ? -18.521 -0.717  49.063  1.00 33.72 ?  386 LEU B CA  1 
ATOM   6118 C C   . LEU B 1 386 ? -18.896 0.749   49.310  1.00 35.53 ?  386 LEU B C   1 
ATOM   6119 O O   . LEU B 1 386 ? -19.969 0.930   49.849  1.00 43.59 ?  386 LEU B O   1 
ATOM   6120 C CB  . LEU B 1 386 ? -17.997 -1.414  50.325  1.00 35.45 ?  386 LEU B CB  1 
ATOM   6121 C CG  . LEU B 1 386 ? -18.265 -2.916  50.472  1.00 33.78 ?  386 LEU B CG  1 
ATOM   6122 C CD1 . LEU B 1 386 ? -17.491 -3.750  49.469  1.00 25.89 ?  386 LEU B CD1 1 
ATOM   6123 C CD2 . LEU B 1 386 ? -17.934 -3.386  51.878  1.00 34.00 ?  386 LEU B CD2 1 
ATOM   6124 N N   . ASN B 1 387 ? -18.093 1.748   48.934  1.00 32.56 ?  387 ASN B N   1 
ATOM   6125 C CA  . ASN B 1 387 ? -18.470 3.153   49.084  1.00 37.68 ?  387 ASN B CA  1 
ATOM   6126 C C   . ASN B 1 387 ? -19.353 3.652   47.946  1.00 38.64 ?  387 ASN B C   1 
ATOM   6127 O O   . ASN B 1 387 ? -19.910 4.750   48.050  1.00 39.06 ?  387 ASN B O   1 
ATOM   6128 C CB  . ASN B 1 387 ? -17.231 4.047   49.202  1.00 34.31 ?  387 ASN B CB  1 
ATOM   6129 C CG  . ASN B 1 387 ? -16.507 3.883   50.535  1.00 42.55 ?  387 ASN B CG  1 
ATOM   6130 O OD1 . ASN B 1 387 ? -16.624 2.852   51.206  1.00 41.42 ?  387 ASN B OD1 1 
ATOM   6131 N ND2 . ASN B 1 387 ? -15.777 4.922   50.938  1.00 42.77 ?  387 ASN B ND2 1 
ATOM   6132 N N   . LEU B 1 388 ? -19.448 2.855   46.877  1.00 34.68 ?  388 LEU B N   1 
ATOM   6133 C CA  . LEU B 1 388 ? -20.404 3.183   45.792  1.00 37.44 ?  388 LEU B CA  1 
ATOM   6134 C C   . LEU B 1 388 ? -21.760 2.874   46.410  1.00 45.11 ?  388 LEU B C   1 
ATOM   6135 O O   . LEU B 1 388 ? -22.704 3.590   46.093  1.00 52.37 ?  388 LEU B O   1 
ATOM   6136 C CB  . LEU B 1 388 ? -20.190 2.203   44.640  1.00 34.23 ?  388 LEU B CB  1 
ATOM   6137 C CG  . LEU B 1 388 ? -19.363 2.663   43.449  1.00 31.10 ?  388 LEU B CG  1 
ATOM   6138 C CD1 . LEU B 1 388 ? -19.401 1.598   42.366  1.00 31.72 ?  388 LEU B CD1 1 
ATOM   6139 C CD2 . LEU B 1 388 ? -19.878 3.982   42.911  1.00 32.72 ?  388 LEU B CD2 1 
ATOM   6140 N N   . ASN B 1 389 ? -21.807 1.854   47.280  1.00 47.92 ?  389 ASN B N   1 
ATOM   6141 C CA  . ASN B 1 389 ? -23.051 1.399   47.954  1.00 52.08 ?  389 ASN B CA  1 
ATOM   6142 C C   . ASN B 1 389 ? -23.706 2.584   48.619  1.00 55.53 ?  389 ASN B C   1 
ATOM   6143 O O   . ASN B 1 389 ? -24.936 2.673   48.557  1.00 58.07 ?  389 ASN B O   1 
ATOM   6144 C CB  . ASN B 1 389 ? -22.816 0.269   48.954  1.00 54.77 ?  389 ASN B CB  1 
ATOM   6145 C CG  . ASN B 1 389 ? -24.031 -0.121  49.771  1.00 59.89 ?  389 ASN B CG  1 
ATOM   6146 O OD1 . ASN B 1 389 ? -24.032 0.016   50.995  1.00 57.82 ?  389 ASN B OD1 1 
ATOM   6147 N ND2 . ASN B 1 389 ? -25.055 -0.633  49.109  1.00 52.43 ?  389 ASN B ND2 1 
ATOM   6148 N N   . ASN B 1 390 ? -22.903 3.457   49.212  1.00 56.27 ?  390 ASN B N   1 
ATOM   6149 C CA  . ASN B 1 390 ? -23.458 4.717   49.770  1.00 57.81 ?  390 ASN B CA  1 
ATOM   6150 C C   . ASN B 1 390 ? -23.929 5.584   48.584  1.00 62.46 ?  390 ASN B C   1 
ATOM   6151 O O   . ASN B 1 390 ? -25.124 5.842   48.476  1.00 62.23 ?  390 ASN B O   1 
ATOM   6152 C CB  . ASN B 1 390 ? -22.456 5.348   50.735  1.00 54.36 ?  390 ASN B CB  1 
ATOM   6153 C CG  . ASN B 1 390 ? -21.592 4.329   51.457  1.00 49.19 ?  390 ASN B CG  1 
ATOM   6154 O OD1 . ASN B 1 390 ? -20.372 4.455   51.487  1.00 48.56 ?  390 ASN B OD1 1 
ATOM   6155 N ND2 . ASN B 1 390 ? -22.205 3.329   52.068  1.00 49.05 ?  390 ASN B ND2 1 
ATOM   6156 O OXT . ASN B 1 390 ? -23.082 5.983   47.781  1.00 62.28 -1 390 ASN B OXT 1 
HETATM 6157 N N1  . PLP C 2 .   ? 22.007  9.135   7.494   1.00 18.90 ?  401 PLP A N1  1 
HETATM 6158 C C2  . PLP C 2 .   ? 23.275  9.233   7.130   1.00 19.07 ?  401 PLP A C2  1 
HETATM 6159 C C2A . PLP C 2 .   ? 23.666  10.316  6.122   1.00 17.76 ?  401 PLP A C2A 1 
HETATM 6160 C C3  . PLP C 2 .   ? 24.233  8.373   7.654   1.00 19.28 ?  401 PLP A C3  1 
HETATM 6161 O O3  . PLP C 2 .   ? 25.567  8.482   7.277   1.00 19.61 ?  401 PLP A O3  1 
HETATM 6162 C C4  . PLP C 2 .   ? 23.844  7.401   8.582   1.00 21.27 ?  401 PLP A C4  1 
HETATM 6163 C C4A . PLP C 2 .   ? 24.836  6.401   9.191   1.00 26.69 ?  401 PLP A C4A 1 
HETATM 6164 O O4A . PLP C 2 .   ? 26.058  7.012   9.531   1.00 27.11 ?  401 PLP A O4A 1 
HETATM 6165 C C5  . PLP C 2 .   ? 22.497  7.336   8.939   1.00 20.79 ?  401 PLP A C5  1 
HETATM 6166 C C6  . PLP C 2 .   ? 21.601  8.225   8.370   1.00 19.44 ?  401 PLP A C6  1 
HETATM 6167 C C5A . PLP C 2 .   ? 22.016  6.253   9.920   1.00 25.25 ?  401 PLP A C5A 1 
HETATM 6168 O O4P . PLP C 2 .   ? 21.639  6.799   11.151  1.00 34.27 ?  401 PLP A O4P 1 
HETATM 6169 P P   . PLP C 2 .   ? 20.640  5.994   12.224  1.00 38.21 ?  401 PLP A P   1 
HETATM 6170 O O1P . PLP C 2 .   ? 21.373  4.764   12.708  1.00 36.86 ?  401 PLP A O1P 1 
HETATM 6171 O O2P . PLP C 2 .   ? 19.363  5.577   11.507  1.00 24.24 -1 401 PLP A O2P 1 
HETATM 6172 O O3P . PLP C 2 .   ? 20.282  6.891   13.421  1.00 32.67 -1 401 PLP A O3P 1 
HETATM 6173 N N1  . PLP D 2 .   ? 1.409   -8.441  23.009  1.00 19.30 ?  401 PLP B N1  1 
HETATM 6174 C C2  . PLP D 2 .   ? 0.637   -8.606  24.065  1.00 18.10 ?  401 PLP B C2  1 
HETATM 6175 C C2A . PLP D 2 .   ? -0.491  -9.646  24.022  1.00 18.93 ?  401 PLP B C2A 1 
HETATM 6176 C C3  . PLP D 2 .   ? 0.833   -7.844  25.208  1.00 20.25 ?  401 PLP B C3  1 
HETATM 6177 O O3  . PLP D 2 .   ? 0.030   -8.001  26.334  1.00 20.41 ?  401 PLP B O3  1 
HETATM 6178 C C4  . PLP D 2 .   ? 1.866   -6.911  25.238  1.00 23.40 ?  401 PLP B C4  1 
HETATM 6179 C C4A . PLP D 2 .   ? 2.100   -6.007  26.449  1.00 27.43 ?  401 PLP B C4A 1 
HETATM 6180 O O4A . PLP D 2 .   ? 2.875   -6.564  27.463  1.00 29.41 ?  401 PLP B O4A 1 
HETATM 6181 C C5  . PLP D 2 .   ? 2.655   -6.762  24.108  1.00 21.74 ?  401 PLP B C5  1 
HETATM 6182 C C6  . PLP D 2 .   ? 2.398   -7.554  23.001  1.00 20.06 ?  401 PLP B C6  1 
HETATM 6183 C C5A . PLP D 2 .   ? 3.782   -5.722  24.117  1.00 24.70 ?  401 PLP B C5A 1 
HETATM 6184 O O4P . PLP D 2 .   ? 4.912   -6.324  23.548  1.00 31.27 ?  401 PLP B O4P 1 
HETATM 6185 P P   . PLP D 2 .   ? 6.238   -5.414  23.115  1.00 42.62 ?  401 PLP B P   1 
HETATM 6186 O O1P . PLP D 2 .   ? 6.405   -4.398  24.244  1.00 36.86 ?  401 PLP B O1P 1 
HETATM 6187 O O2P . PLP D 2 .   ? 5.941   -4.753  21.763  1.00 22.99 -1 401 PLP B O2P 1 
HETATM 6188 O O3P . PLP D 2 .   ? 7.504   -6.296  22.987  1.00 33.16 -1 401 PLP B O3P 1 
HETATM 6189 O O   . HOH E 3 .   ? 44.928  14.346  17.714  1.00 37.93 ?  501 HOH A O   1 
HETATM 6190 O O   . HOH E 3 .   ? 49.670  -6.213  -11.644 1.00 43.15 ?  502 HOH A O   1 
HETATM 6191 O O   . HOH E 3 .   ? 3.698   16.909  -4.037  1.00 28.53 ?  503 HOH A O   1 
HETATM 6192 O O   . HOH E 3 .   ? 7.071   17.957  -7.638  1.00 16.40 ?  504 HOH A O   1 
HETATM 6193 O O   . HOH E 3 .   ? 14.200  29.231  -9.478  1.00 39.00 ?  505 HOH A O   1 
HETATM 6194 O O   . HOH E 3 .   ? 24.708  2.964   7.912   1.00 33.86 ?  506 HOH A O   1 
HETATM 6195 O O   . HOH E 3 .   ? 12.559  1.375   31.430  1.00 17.73 ?  507 HOH A O   1 
HETATM 6196 O O   . HOH E 3 .   ? 47.265  11.661  -3.134  1.00 21.93 ?  508 HOH A O   1 
HETATM 6197 O O   . HOH E 3 .   ? 25.454  -0.198  35.994  1.00 35.26 ?  509 HOH A O   1 
HETATM 6198 O O   . HOH E 3 .   ? 33.172  11.441  -12.472 1.00 28.24 ?  510 HOH A O   1 
HETATM 6199 O O   . HOH E 3 .   ? 30.707  -7.362  9.291   1.00 27.52 ?  511 HOH A O   1 
HETATM 6200 O O   . HOH E 3 .   ? 22.766  18.266  15.658  1.00 20.22 ?  512 HOH A O   1 
HETATM 6201 O O   . HOH E 3 .   ? 6.638   27.538  4.571   1.00 23.65 ?  513 HOH A O   1 
HETATM 6202 O O   . HOH E 3 .   ? 10.036  2.336   19.680  1.00 35.90 ?  514 HOH A O   1 
HETATM 6203 O O   . HOH E 3 .   ? 6.120   11.245  20.670  1.00 21.94 ?  515 HOH A O   1 
HETATM 6204 O O   . HOH E 3 .   ? 46.420  -1.202  13.215  1.00 26.36 ?  516 HOH A O   1 
HETATM 6205 O O   . HOH E 3 .   ? 26.408  11.026  36.988  1.00 29.85 ?  517 HOH A O   1 
HETATM 6206 O O   . HOH E 3 .   ? 26.986  29.410  -0.857  1.00 27.95 ?  518 HOH A O   1 
HETATM 6207 O O   . HOH E 3 .   ? 12.258  30.792  1.524   1.00 28.15 ?  519 HOH A O   1 
HETATM 6208 O O   . HOH E 3 .   ? 19.422  5.978   -8.631  1.00 22.73 ?  520 HOH A O   1 
HETATM 6209 O O   . HOH E 3 .   ? 34.309  -4.724  -3.286  1.00 26.23 ?  521 HOH A O   1 
HETATM 6210 O O   . HOH E 3 .   ? 26.898  9.296   39.997  1.00 26.73 ?  522 HOH A O   1 
HETATM 6211 O O   . HOH E 3 .   ? 51.428  12.507  7.204   1.00 31.53 ?  523 HOH A O   1 
HETATM 6212 O O   . HOH E 3 .   ? 36.468  -10.816 13.791  1.00 29.21 ?  524 HOH A O   1 
HETATM 6213 O O   . HOH E 3 .   ? 21.628  9.011   36.822  1.00 36.85 ?  525 HOH A O   1 
HETATM 6214 O O   . HOH E 3 .   ? 30.155  -2.595  15.562  1.00 24.12 ?  526 HOH A O   1 
HETATM 6215 O O   . HOH E 3 .   ? 20.930  20.225  13.104  1.00 18.65 ?  527 HOH A O   1 
HETATM 6216 O O   . HOH E 3 .   ? 53.587  11.613  5.711   1.00 37.49 ?  528 HOH A O   1 
HETATM 6217 O O   . HOH E 3 .   ? 14.936  2.148   14.710  1.00 23.22 ?  529 HOH A O   1 
HETATM 6218 O O   . HOH E 3 .   ? 36.888  8.790   24.026  1.00 19.60 ?  530 HOH A O   1 
HETATM 6219 O O   . HOH E 3 .   ? 10.750  -1.064  17.972  1.00 25.86 ?  531 HOH A O   1 
HETATM 6220 O O   . HOH E 3 .   ? 34.713  22.501  13.490  1.00 32.45 ?  532 HOH A O   1 
HETATM 6221 O O   . HOH E 3 .   ? 21.626  9.612   -11.673 1.00 38.95 ?  533 HOH A O   1 
HETATM 6222 O O   . HOH E 3 .   ? 14.940  30.973  4.349   1.00 28.57 ?  534 HOH A O   1 
HETATM 6223 O O   . HOH E 3 .   ? 1.370   4.708   4.127   1.00 26.68 ?  535 HOH A O   1 
HETATM 6224 O O   . HOH E 3 .   ? 23.797  21.437  25.499  1.00 20.50 ?  536 HOH A O   1 
HETATM 6225 O O   . HOH E 3 .   ? 47.344  -11.032 14.613  1.00 42.22 ?  537 HOH A O   1 
HETATM 6226 O O   . HOH E 3 .   ? 18.740  29.937  25.367  1.00 27.36 ?  538 HOH A O   1 
HETATM 6227 O O   . HOH E 3 .   ? 44.175  14.490  30.716  1.00 44.37 ?  539 HOH A O   1 
HETATM 6228 O O   . HOH E 3 .   ? 26.620  -8.123  22.271  1.00 20.49 ?  540 HOH A O   1 
HETATM 6229 O O   . HOH E 3 .   ? 32.340  8.378   33.858  0.50 31.56 ?  541 HOH A O   1 
HETATM 6230 O O   . HOH E 3 .   ? 6.423   4.244   -15.058 1.00 29.86 ?  542 HOH A O   1 
HETATM 6231 O O   . HOH E 3 .   ? 40.279  14.298  -8.046  1.00 36.40 ?  543 HOH A O   1 
HETATM 6232 O O   . HOH E 3 .   ? 13.296  26.155  26.525  1.00 21.72 ?  544 HOH A O   1 
HETATM 6233 O O   . HOH E 3 .   ? 32.009  16.104  27.125  1.00 20.52 ?  545 HOH A O   1 
HETATM 6234 O O   . HOH E 3 .   ? 3.612   17.112  -6.640  1.00 29.01 ?  546 HOH A O   1 
HETATM 6235 O O   . HOH E 3 .   ? 34.875  -3.358  0.998   1.00 26.95 ?  547 HOH A O   1 
HETATM 6236 O O   . HOH E 3 .   ? 19.192  5.475   37.939  1.00 27.80 ?  548 HOH A O   1 
HETATM 6237 O O   . HOH E 3 .   ? 6.234   12.176  -13.950 1.00 35.72 ?  549 HOH A O   1 
HETATM 6238 O O   . HOH E 3 .   ? 14.684  5.242   -10.422 1.00 31.95 ?  550 HOH A O   1 
HETATM 6239 O O   . HOH E 3 .   ? 35.729  19.090  -2.494  1.00 30.29 ?  551 HOH A O   1 
HETATM 6240 O O   . HOH E 3 .   ? 0.806   7.059   1.188   1.00 23.85 ?  552 HOH A O   1 
HETATM 6241 O O   . HOH E 3 .   ? 9.630   20.177  -14.735 1.00 32.36 ?  553 HOH A O   1 
HETATM 6242 O O   . HOH E 3 .   ? 38.619  21.111  4.873   1.00 29.17 ?  554 HOH A O   1 
HETATM 6243 O O   . HOH E 3 .   ? 27.007  14.731  13.672  1.00 15.07 ?  555 HOH A O   1 
HETATM 6244 O O   . HOH E 3 .   ? 23.408  27.134  12.201  1.00 25.90 ?  556 HOH A O   1 
HETATM 6245 O O   . HOH E 3 .   ? 50.631  -1.481  7.711   1.00 24.46 ?  557 HOH A O   1 
HETATM 6246 O O   . HOH E 3 .   ? 39.312  1.428   12.090  1.00 20.54 ?  558 HOH A O   1 
HETATM 6247 O O   . HOH E 3 .   ? 27.491  3.699   3.768   1.00 23.28 ?  559 HOH A O   1 
HETATM 6248 O O   . HOH E 3 .   ? 41.919  17.009  0.345   1.00 17.11 ?  560 HOH A O   1 
HETATM 6249 O O   . HOH E 3 .   ? 31.849  21.019  21.324  1.00 20.35 ?  561 HOH A O   1 
HETATM 6250 O O   . HOH E 3 .   ? 21.151  3.232   10.558  1.00 32.01 ?  562 HOH A O   1 
HETATM 6251 O O   . HOH E 3 .   ? 15.416  5.414   28.038  1.00 17.72 ?  563 HOH A O   1 
HETATM 6252 O O   . HOH E 3 .   ? 34.387  -5.416  9.032   1.00 21.40 ?  564 HOH A O   1 
HETATM 6253 O O   . HOH E 3 .   ? 34.062  4.423   4.803   1.00 18.12 ?  565 HOH A O   1 
HETATM 6254 O O   . HOH E 3 .   ? 25.793  26.239  6.636   1.00 17.39 ?  566 HOH A O   1 
HETATM 6255 O O   . HOH E 3 .   ? 38.917  18.303  -3.446  1.00 22.64 ?  567 HOH A O   1 
HETATM 6256 O O   . HOH E 3 .   ? 34.061  -4.269  -12.612 1.00 35.94 ?  568 HOH A O   1 
HETATM 6257 O O   . HOH E 3 .   ? 9.543   25.609  24.509  1.00 21.50 ?  569 HOH A O   1 
HETATM 6258 O O   . HOH E 3 .   ? 22.841  18.209  12.939  1.00 18.15 ?  570 HOH A O   1 
HETATM 6259 O O   . HOH E 3 .   ? 37.709  21.131  18.191  1.00 21.08 ?  571 HOH A O   1 
HETATM 6260 O O   . HOH E 3 .   ? 35.727  24.662  3.756   1.00 29.08 ?  572 HOH A O   1 
HETATM 6261 O O   . HOH E 3 .   ? 22.499  6.365   -10.857 1.00 33.15 ?  573 HOH A O   1 
HETATM 6262 O O   . HOH E 3 .   ? 24.548  22.966  6.399   1.00 16.67 ?  574 HOH A O   1 
HETATM 6263 O O   . HOH E 3 .   ? 39.529  4.040   -11.098 1.00 23.18 ?  575 HOH A O   1 
HETATM 6264 O O   . HOH E 3 .   ? 12.812  7.943   -11.348 1.00 24.64 ?  576 HOH A O   1 
HETATM 6265 O O   . HOH E 3 .   ? 43.775  21.403  13.863  1.00 37.78 ?  577 HOH A O   1 
HETATM 6266 O O   . HOH E 3 .   ? 13.267  27.037  22.983  1.00 19.53 ?  578 HOH A O   1 
HETATM 6267 O O   . HOH E 3 .   ? 39.328  -7.353  -7.487  1.00 28.23 ?  579 HOH A O   1 
HETATM 6268 O O   . HOH E 3 .   ? -0.736  10.647  5.092   1.00 25.54 ?  580 HOH A O   1 
HETATM 6269 O O   . HOH E 3 .   ? -0.134  17.683  6.838   1.00 27.55 ?  581 HOH A O   1 
HETATM 6270 O O   . HOH E 3 .   ? 38.735  18.744  27.348  1.00 33.78 ?  582 HOH A O   1 
HETATM 6271 O O   . HOH E 3 .   ? 40.239  -0.674  24.783  1.00 27.18 ?  583 HOH A O   1 
HETATM 6272 O O   . HOH E 3 .   ? 17.726  -0.278  -3.212  1.00 27.08 ?  584 HOH A O   1 
HETATM 6273 O O   . HOH E 3 .   ? 13.294  1.059   17.581  1.00 38.93 ?  585 HOH A O   1 
HETATM 6274 O O   . HOH E 3 .   ? 22.412  31.403  25.438  1.00 38.45 ?  586 HOH A O   1 
HETATM 6275 O O   . HOH E 3 .   ? 24.020  8.906   -11.522 1.00 27.93 ?  587 HOH A O   1 
HETATM 6276 O O   . HOH E 3 .   ? 26.085  12.107  32.865  1.00 21.34 ?  588 HOH A O   1 
HETATM 6277 O O   . HOH E 3 .   ? 3.465   3.012   7.230   1.00 21.99 ?  589 HOH A O   1 
HETATM 6278 O O   . HOH E 3 .   ? 31.524  -11.990 22.268  1.00 28.95 ?  590 HOH A O   1 
HETATM 6279 O O   . HOH E 3 .   ? 0.855   18.836  15.932  1.00 26.06 ?  591 HOH A O   1 
HETATM 6280 O O   . HOH E 3 .   ? 11.436  15.120  -14.195 1.00 33.24 ?  592 HOH A O   1 
HETATM 6281 O O   . HOH E 3 .   ? 5.163   18.332  19.976  1.00 28.52 ?  593 HOH A O   1 
HETATM 6282 O O   . HOH E 3 .   ? 10.663  20.299  26.227  1.00 21.42 ?  594 HOH A O   1 
HETATM 6283 O O   . HOH E 3 .   ? 50.997  5.416   7.109   1.00 34.03 ?  595 HOH A O   1 
HETATM 6284 O O   . HOH E 3 .   ? 32.636  25.467  2.376   1.00 31.79 ?  596 HOH A O   1 
HETATM 6285 O O   . HOH E 3 .   ? 29.881  7.307   14.949  1.00 15.77 ?  597 HOH A O   1 
HETATM 6286 O O   . HOH E 3 .   ? 2.344   7.118   -7.754  1.00 19.33 ?  598 HOH A O   1 
HETATM 6287 O O   . HOH E 3 .   ? 47.804  17.569  13.194  1.00 37.72 ?  599 HOH A O   1 
HETATM 6288 O O   . HOH E 3 .   ? 42.195  -10.224 4.038   1.00 27.45 ?  600 HOH A O   1 
HETATM 6289 O O   . HOH E 3 .   ? 0.200   9.511   10.253  1.00 22.62 ?  601 HOH A O   1 
HETATM 6290 O O   . HOH E 3 .   ? 16.671  26.649  -10.329 1.00 27.10 ?  602 HOH A O   1 
HETATM 6291 O O   . HOH E 3 .   ? 25.902  27.044  -4.542  1.00 34.81 ?  603 HOH A O   1 
HETATM 6292 O O   . HOH E 3 .   ? 37.901  -2.515  -12.757 1.00 19.59 ?  604 HOH A O   1 
HETATM 6293 O O   . HOH E 3 .   ? 2.091   11.413  -7.948  1.00 25.53 ?  605 HOH A O   1 
HETATM 6294 O O   . HOH E 3 .   ? 47.760  5.308   24.364  1.00 31.43 ?  606 HOH A O   1 
HETATM 6295 O O   . HOH E 3 .   ? 42.348  18.338  9.095   1.00 17.90 ?  607 HOH A O   1 
HETATM 6296 O O   . HOH E 3 .   ? 6.771   13.350  22.333  1.00 27.01 ?  608 HOH A O   1 
HETATM 6297 O O   . HOH E 3 .   ? 30.623  -1.433  18.596  1.00 22.10 ?  609 HOH A O   1 
HETATM 6298 O O   . HOH E 3 .   ? 21.021  14.490  -12.843 1.00 22.38 ?  610 HOH A O   1 
HETATM 6299 O O   . HOH E 3 .   ? 22.412  18.874  -9.535  1.00 19.60 ?  611 HOH A O   1 
HETATM 6300 O O   . HOH E 3 .   ? 22.827  15.870  16.755  1.00 18.38 ?  612 HOH A O   1 
HETATM 6301 O O   . HOH E 3 .   ? 29.492  20.697  13.324  1.00 16.52 ?  613 HOH A O   1 
HETATM 6302 O O   . HOH E 3 .   ? 22.652  29.399  9.000   1.00 29.74 ?  614 HOH A O   1 
HETATM 6303 O O   . HOH E 3 .   ? 13.136  1.792   34.003  1.00 20.84 ?  615 HOH A O   1 
HETATM 6304 O O   . HOH E 3 .   ? 17.347  1.438   -9.192  1.00 26.35 ?  616 HOH A O   1 
HETATM 6305 O O   . HOH E 3 .   ? 21.475  18.253  -7.055  1.00 20.17 ?  617 HOH A O   1 
HETATM 6306 O O   . HOH E 3 .   ? 20.385  13.728  -1.445  1.00 14.35 ?  618 HOH A O   1 
HETATM 6307 O O   . HOH E 3 .   ? 28.774  4.900   -10.107 1.00 23.60 ?  619 HOH A O   1 
HETATM 6308 O O   . HOH E 3 .   ? 14.889  3.478   21.395  1.00 16.86 ?  620 HOH A O   1 
HETATM 6309 O O   . HOH E 3 .   ? 21.799  28.041  25.833  1.00 39.48 ?  621 HOH A O   1 
HETATM 6310 O O   . HOH E 3 .   ? 38.990  -2.914  0.990   1.00 16.93 ?  622 HOH A O   1 
HETATM 6311 O O   . HOH E 3 .   ? 33.285  15.056  32.957  1.00 32.09 ?  623 HOH A O   1 
HETATM 6312 O O   . HOH E 3 .   ? 44.692  8.599   18.291  1.00 20.40 ?  624 HOH A O   1 
HETATM 6313 O O   . HOH E 3 .   ? -2.019  23.621  -3.917  1.00 32.69 ?  625 HOH A O   1 
HETATM 6314 O O   . HOH E 3 .   ? 26.930  24.093  -6.208  1.00 29.24 ?  626 HOH A O   1 
HETATM 6315 O O   . HOH E 3 .   ? 10.568  1.084   -6.288  1.00 19.34 ?  627 HOH A O   1 
HETATM 6316 O O   . HOH E 3 .   ? 26.999  29.458  5.129   1.00 23.80 ?  628 HOH A O   1 
HETATM 6317 O O   . HOH E 3 .   ? 45.117  12.998  -1.771  1.00 25.33 ?  629 HOH A O   1 
HETATM 6318 O O   . HOH E 3 .   ? 18.613  13.821  -15.760 1.00 32.82 ?  630 HOH A O   1 
HETATM 6319 O O   . HOH E 3 .   ? 30.445  23.392  13.504  1.00 33.15 ?  631 HOH A O   1 
HETATM 6320 O O   . HOH E 3 .   ? 6.579   13.497  25.038  1.00 26.98 ?  632 HOH A O   1 
HETATM 6321 O O   . HOH E 3 .   ? 7.727   21.830  8.715   1.00 15.63 ?  633 HOH A O   1 
HETATM 6322 O O   . HOH E 3 .   ? 43.589  10.468  23.798  1.00 25.06 ?  634 HOH A O   1 
HETATM 6323 O O   . HOH E 3 .   ? 3.694   1.888   1.266   1.00 23.14 ?  635 HOH A O   1 
HETATM 6324 O O   . HOH E 3 .   ? 14.221  3.719   -8.182  1.00 17.04 ?  636 HOH A O   1 
HETATM 6325 O O   . HOH E 3 .   ? 25.441  6.206   -11.521 1.00 28.16 ?  637 HOH A O   1 
HETATM 6326 O O   . HOH E 3 .   ? 28.064  23.210  -3.567  1.00 27.30 ?  638 HOH A O   1 
HETATM 6327 O O   . HOH E 3 .   ? 6.164   10.125  25.556  1.00 31.73 ?  639 HOH A O   1 
HETATM 6328 O O   . HOH E 3 .   ? 30.223  -5.090  21.360  1.00 19.18 ?  640 HOH A O   1 
HETATM 6329 O O   . HOH E 3 .   ? 26.840  11.421  -11.764 1.00 28.53 ?  641 HOH A O   1 
HETATM 6330 O O   . HOH E 3 .   ? 27.941  5.485   14.217  1.00 17.51 ?  642 HOH A O   1 
HETATM 6331 O O   . HOH E 3 .   ? 44.292  -13.322 8.051   1.00 39.58 ?  643 HOH A O   1 
HETATM 6332 O O   . HOH E 3 .   ? 48.272  14.996  12.116  1.00 26.84 ?  644 HOH A O   1 
HETATM 6333 O O   . HOH E 3 .   ? 6.602   -1.911  12.041  1.00 13.85 ?  645 HOH A O   1 
HETATM 6334 O O   . HOH E 3 .   ? 41.787  -7.560  13.273  1.00 32.69 ?  646 HOH A O   1 
HETATM 6335 O O   . HOH E 3 .   ? 43.246  19.411  -2.186  1.00 32.77 ?  647 HOH A O   1 
HETATM 6336 O O   . HOH E 3 .   ? 43.004  1.066   -16.383 1.00 19.49 ?  648 HOH A O   1 
HETATM 6337 O O   . HOH E 3 .   ? 20.443  -2.000  41.351  1.00 29.86 ?  649 HOH A O   1 
HETATM 6338 O O   . HOH E 3 .   ? 0.439   12.440  16.343  1.00 24.74 ?  650 HOH A O   1 
HETATM 6339 O O   . HOH E 3 .   ? -0.009  4.884   -6.226  1.00 24.63 ?  651 HOH A O   1 
HETATM 6340 O O   . HOH E 3 .   ? 27.427  2.992   -8.947  1.00 22.04 ?  652 HOH A O   1 
HETATM 6341 O O   . HOH E 3 .   ? 18.205  3.409   14.861  1.00 27.56 ?  653 HOH A O   1 
HETATM 6342 O O   . HOH E 3 .   ? 20.774  7.710   34.229  1.00 18.28 ?  654 HOH A O   1 
HETATM 6343 O O   . HOH E 3 .   ? 30.899  9.765   22.771  1.00 15.00 ?  655 HOH A O   1 
HETATM 6344 O O   . HOH E 3 .   ? 50.338  1.610   13.324  1.00 24.59 ?  656 HOH A O   1 
HETATM 6345 O O   . HOH E 3 .   ? 21.113  11.947  31.439  1.00 16.42 ?  657 HOH A O   1 
HETATM 6346 O O   . HOH E 3 .   ? 34.964  13.929  3.061   1.00 37.88 ?  658 HOH A O   1 
HETATM 6347 O O   . HOH E 3 .   ? 42.944  18.236  6.424   1.00 21.43 ?  659 HOH A O   1 
HETATM 6348 O O   . HOH E 3 .   ? 6.928   7.542   23.024  1.00 27.38 ?  660 HOH A O   1 
HETATM 6349 O O   . HOH E 3 .   ? 14.804  24.866  -14.195 1.00 24.87 ?  661 HOH A O   1 
HETATM 6350 O O   . HOH E 3 .   ? 21.764  15.794  -0.430  1.00 14.21 ?  662 HOH A O   1 
HETATM 6351 O O   . HOH E 3 .   ? 6.086   -0.001  2.319   1.00 28.20 ?  663 HOH A O   1 
HETATM 6352 O O   . HOH E 3 .   ? 31.752  20.876  -9.519  1.00 29.36 ?  664 HOH A O   1 
HETATM 6353 O O   . HOH E 3 .   ? 24.183  10.900  34.530  1.00 25.05 ?  665 HOH A O   1 
HETATM 6354 O O   . HOH E 3 .   ? 43.794  -0.150  21.064  1.00 25.68 ?  666 HOH A O   1 
HETATM 6355 O O   . HOH E 3 .   ? 5.060   14.956  0.110   1.00 37.05 ?  667 HOH A O   1 
HETATM 6356 O O   . HOH E 3 .   ? 45.730  14.873  0.025   1.00 24.39 ?  668 HOH A O   1 
HETATM 6357 O O   . HOH E 3 .   ? 33.914  -8.401  17.430  1.00 27.36 ?  669 HOH A O   1 
HETATM 6358 O O   . HOH E 3 .   ? 6.449   8.794   -10.498 1.00 23.78 ?  670 HOH A O   1 
HETATM 6359 O O   . HOH E 3 .   ? 39.074  5.466   22.743  1.00 20.70 ?  671 HOH A O   1 
HETATM 6360 O O   . HOH E 3 .   ? 15.924  0.361   41.697  1.00 25.83 ?  672 HOH A O   1 
HETATM 6361 O O   . HOH E 3 .   ? 7.715   9.586   19.308  1.00 18.38 ?  673 HOH A O   1 
HETATM 6362 O O   . HOH E 3 .   ? 36.089  22.735  15.753  1.00 29.21 ?  674 HOH A O   1 
HETATM 6363 O O   . HOH E 3 .   ? 17.566  10.208  -11.934 1.00 22.02 ?  675 HOH A O   1 
HETATM 6364 O O   . HOH E 3 .   ? 27.505  19.905  30.747  1.00 40.08 ?  676 HOH A O   1 
HETATM 6365 O O   . HOH E 3 .   ? 5.499   19.645  -7.824  1.00 25.30 ?  677 HOH A O   1 
HETATM 6366 O O   . HOH E 3 .   ? 43.359  -4.615  12.869  1.00 40.74 ?  678 HOH A O   1 
HETATM 6367 O O   . HOH E 3 .   ? 21.183  5.390   17.425  1.00 21.93 ?  679 HOH A O   1 
HETATM 6368 O O   . HOH E 3 .   ? 4.630   16.870  -1.388  1.00 37.59 ?  680 HOH A O   1 
HETATM 6369 O O   . HOH E 3 .   ? 24.071  14.606  7.706   1.00 12.32 ?  681 HOH A O   1 
HETATM 6370 O O   . HOH E 3 .   ? 23.555  22.818  27.966  1.00 39.91 ?  682 HOH A O   1 
HETATM 6371 O O   . HOH E 3 .   ? 50.283  13.666  11.963  1.00 40.92 ?  683 HOH A O   1 
HETATM 6372 O O   . HOH E 3 .   ? 4.940   26.142  13.873  1.00 29.25 ?  684 HOH A O   1 
HETATM 6373 O O   . HOH E 3 .   ? 28.482  -5.921  19.378  1.00 22.97 ?  685 HOH A O   1 
HETATM 6374 O O   . HOH E 3 .   ? 33.482  17.950  -0.770  1.00 37.32 ?  686 HOH A O   1 
HETATM 6375 O O   . HOH E 3 .   ? 30.836  11.339  10.095  1.00 17.72 ?  687 HOH A O   1 
HETATM 6376 O O   . HOH E 3 .   ? 1.591   4.110   1.191   1.00 27.85 ?  688 HOH A O   1 
HETATM 6377 O O   . HOH E 3 .   ? 42.678  9.399   -8.787  1.00 20.37 ?  689 HOH A O   1 
HETATM 6378 O O   . HOH E 3 .   ? 35.886  15.913  6.910   1.00 22.91 ?  690 HOH A O   1 
HETATM 6379 O O   . HOH E 3 .   ? 28.258  3.838   16.594  1.00 15.68 ?  691 HOH A O   1 
HETATM 6380 O O   . HOH E 3 .   ? 22.670  17.267  -12.728 1.00 30.83 ?  692 HOH A O   1 
HETATM 6381 O O   . HOH E 3 .   ? 38.201  17.424  6.406   1.00 21.20 ?  693 HOH A O   1 
HETATM 6382 O O   . HOH E 3 .   ? 14.408  29.126  2.435   1.00 23.38 ?  694 HOH A O   1 
HETATM 6383 O O   . HOH E 3 .   ? 25.732  31.098  2.730   1.00 20.76 ?  695 HOH A O   1 
HETATM 6384 O O   . HOH E 3 .   ? 10.923  -4.300  -0.088  1.00 31.93 ?  696 HOH A O   1 
HETATM 6385 O O   . HOH E 3 .   ? 35.982  8.706   26.515  1.00 23.20 ?  697 HOH A O   1 
HETATM 6386 O O   . HOH E 3 .   ? 15.999  30.774  11.953  1.00 35.12 ?  698 HOH A O   1 
HETATM 6387 O O   . HOH E 3 .   ? 37.776  3.293   10.887  1.00 19.90 ?  699 HOH A O   1 
HETATM 6388 O O   . HOH E 3 .   ? 18.439  3.019   12.504  1.00 26.28 ?  700 HOH A O   1 
HETATM 6389 O O   . HOH E 3 .   ? 48.957  -5.891  5.217   1.00 27.26 ?  701 HOH A O   1 
HETATM 6390 O O   . HOH E 3 .   ? 21.887  29.875  -10.572 1.00 34.45 ?  702 HOH A O   1 
HETATM 6391 O O   . HOH E 3 .   ? 4.043   5.629   7.668   1.00 22.63 ?  703 HOH A O   1 
HETATM 6392 O O   . HOH E 3 .   ? 6.013   27.180  15.712  1.00 22.22 ?  704 HOH A O   1 
HETATM 6393 O O   . HOH E 3 .   ? 5.038   23.401  -9.074  1.00 30.52 ?  705 HOH A O   1 
HETATM 6394 O O   . HOH E 3 .   ? 43.387  -12.959 0.947   1.00 35.81 ?  706 HOH A O   1 
HETATM 6395 O O   . HOH E 3 .   ? 21.635  7.233   18.896  1.00 24.79 ?  707 HOH A O   1 
HETATM 6396 O O   . HOH E 3 .   ? 4.975   3.706   9.663   1.00 24.36 ?  708 HOH A O   1 
HETATM 6397 O O   . HOH E 3 .   ? 32.459  -1.903  -0.287  1.00 24.29 ?  709 HOH A O   1 
HETATM 6398 O O   . HOH E 3 .   ? 17.381  0.795   14.830  1.00 35.21 ?  710 HOH A O   1 
HETATM 6399 O O   . HOH E 3 .   ? 10.666  33.512  8.895   1.00 29.94 ?  711 HOH A O   1 
HETATM 6400 O O   . HOH E 3 .   ? 15.231  28.789  -4.467  1.00 25.48 ?  712 HOH A O   1 
HETATM 6401 O O   . HOH E 3 .   ? 17.185  6.264   -10.168 1.00 29.45 ?  713 HOH A O   1 
HETATM 6402 O O   . HOH E 3 .   ? 22.633  14.160  31.804  1.00 31.56 ?  714 HOH A O   1 
HETATM 6403 O O   . HOH E 3 .   ? 16.606  28.852  -6.963  1.00 32.52 ?  715 HOH A O   1 
HETATM 6404 O O   . HOH E 3 .   ? 9.998   3.677   -13.731 1.00 28.68 ?  716 HOH A O   1 
HETATM 6405 O O   . HOH E 3 .   ? 30.732  19.254  27.957  1.00 21.40 ?  717 HOH A O   1 
HETATM 6406 O O   . HOH E 3 .   ? 24.275  31.837  10.091  1.00 41.65 ?  718 HOH A O   1 
HETATM 6407 O O   . HOH E 3 .   ? 7.511   17.954  21.577  1.00 22.36 ?  719 HOH A O   1 
HETATM 6408 O O   . HOH E 3 .   ? 21.192  0.931   -1.702  1.00 22.99 ?  720 HOH A O   1 
HETATM 6409 O O   . HOH E 3 .   ? 10.551  12.486  -13.929 1.00 33.21 ?  721 HOH A O   1 
HETATM 6410 O O   . HOH E 3 .   ? 27.495  6.252   6.623   1.00 27.89 ?  722 HOH A O   1 
HETATM 6411 O O   . HOH E 3 .   ? 19.565  31.474  -0.854  1.00 26.59 ?  723 HOH A O   1 
HETATM 6412 O O   . HOH E 3 .   ? 33.658  0.113   -14.398 1.00 36.29 ?  724 HOH A O   1 
HETATM 6413 O O   . HOH E 3 .   ? 37.440  13.561  1.929   1.00 15.42 ?  725 HOH A O   1 
HETATM 6414 O O   . HOH E 3 .   ? 25.431  6.082   13.501  1.00 23.96 ?  726 HOH A O   1 
HETATM 6415 O O   . HOH E 3 .   ? 51.736  10.431  15.235  1.00 42.53 ?  727 HOH A O   1 
HETATM 6416 O O   . HOH E 3 .   ? 6.517   3.083   18.470  1.00 22.93 ?  728 HOH A O   1 
HETATM 6417 O O   . HOH E 3 .   ? 30.889  11.965  4.163   1.00 19.75 ?  729 HOH A O   1 
HETATM 6418 O O   . HOH E 3 .   ? 49.821  -4.115  9.431   1.00 35.20 ?  730 HOH A O   1 
HETATM 6419 O O   . HOH E 3 .   ? 31.203  17.562  30.491  1.00 33.71 ?  731 HOH A O   1 
HETATM 6420 O O   . HOH E 3 .   ? 28.378  3.318   7.005   1.00 22.73 ?  732 HOH A O   1 
HETATM 6421 O O   . HOH E 3 .   ? 22.606  14.723  14.260  1.00 16.62 ?  733 HOH A O   1 
HETATM 6422 O O   . HOH E 3 .   ? 45.250  -8.747  7.431   1.00 29.18 ?  734 HOH A O   1 
HETATM 6423 O O   . HOH E 3 .   ? 9.214   14.871  32.244  1.00 36.52 ?  735 HOH A O   1 
HETATM 6424 O O   . HOH E 3 .   ? 30.046  0.701   2.981   1.00 35.53 ?  736 HOH A O   1 
HETATM 6425 O O   . HOH E 3 .   ? 15.387  -2.034  0.225   1.00 23.17 ?  737 HOH A O   1 
HETATM 6426 O O   . HOH E 3 .   ? 9.463   2.089   26.529  1.00 23.85 ?  738 HOH A O   1 
HETATM 6427 O O   . HOH E 3 .   ? 33.526  -9.890  6.462   1.00 33.74 ?  739 HOH A O   1 
HETATM 6428 O O   . HOH E 3 .   ? 4.146   28.231  -5.678  1.00 37.82 ?  740 HOH A O   1 
HETATM 6429 O O   . HOH E 3 .   ? 0.377   10.074  17.719  1.00 37.09 ?  741 HOH A O   1 
HETATM 6430 O O   . HOH E 3 .   ? 30.937  6.283   35.522  1.00 33.23 ?  742 HOH A O   1 
HETATM 6431 O O   . HOH E 3 .   ? 37.155  20.241  25.237  1.00 27.36 ?  743 HOH A O   1 
HETATM 6432 O O   . HOH E 3 .   ? 13.928  28.888  13.502  1.00 25.71 ?  744 HOH A O   1 
HETATM 6433 O O   . HOH E 3 .   ? 4.716   13.926  -13.195 1.00 24.00 ?  745 HOH A O   1 
HETATM 6434 O O   . HOH E 3 .   ? 10.396  2.852   33.076  1.00 31.56 ?  746 HOH A O   1 
HETATM 6435 O O   . HOH E 3 .   ? 21.722  25.903  -13.410 1.00 29.34 ?  747 HOH A O   1 
HETATM 6436 O O   . HOH E 3 .   ? 29.552  15.464  -13.567 1.00 28.10 ?  748 HOH A O   1 
HETATM 6437 O O   . HOH E 3 .   ? 6.356   6.516   24.968  1.00 36.78 ?  749 HOH A O   1 
HETATM 6438 O O   . HOH E 3 .   ? -0.086  10.976  -1.292  1.00 29.75 ?  750 HOH A O   1 
HETATM 6439 O O   . HOH E 3 .   ? 4.079   -0.534  16.315  1.00 29.40 ?  751 HOH A O   1 
HETATM 6440 O O   . HOH E 3 .   ? 40.467  -9.409  -6.787  1.00 39.14 ?  752 HOH A O   1 
HETATM 6441 O O   . HOH E 3 .   ? 33.798  20.477  1.603   1.00 32.48 ?  753 HOH A O   1 
HETATM 6442 O O   . HOH E 3 .   ? -0.115  23.360  8.702   1.00 32.87 ?  754 HOH A O   1 
HETATM 6443 O O   . HOH E 3 .   ? 32.906  19.066  -3.108  1.00 30.33 ?  755 HOH A O   1 
HETATM 6444 O O   . HOH E 3 .   ? 45.372  19.482  12.543  1.00 26.06 ?  756 HOH A O   1 
HETATM 6445 O O   . HOH E 3 .   ? 23.481  25.770  -11.776 1.00 26.00 ?  757 HOH A O   1 
HETATM 6446 O O   . HOH E 3 .   ? 34.334  -6.343  26.206  1.00 37.86 ?  758 HOH A O   1 
HETATM 6447 O O   . HOH E 3 .   ? 48.599  15.271  17.459  1.00 40.69 ?  759 HOH A O   1 
HETATM 6448 O O   . HOH E 3 .   ? 38.416  15.935  -11.176 1.00 27.06 ?  760 HOH A O   1 
HETATM 6449 O O   . HOH E 3 .   ? 27.302  12.167  -9.463  1.00 27.79 ?  761 HOH A O   1 
HETATM 6450 O O   . HOH E 3 .   ? 46.795  18.069  -5.641  1.00 40.75 ?  762 HOH A O   1 
HETATM 6451 O O   . HOH E 3 .   ? 53.989  7.679   10.425  1.00 29.96 ?  763 HOH A O   1 
HETATM 6452 O O   . HOH E 3 .   ? 37.282  -5.080  19.095  1.00 24.81 ?  764 HOH A O   1 
HETATM 6453 O O   . HOH E 3 .   ? 38.238  -8.261  16.069  1.00 35.26 ?  765 HOH A O   1 
HETATM 6454 O O   . HOH E 3 .   ? 7.671   24.525  22.983  1.00 21.64 ?  766 HOH A O   1 
HETATM 6455 O O   . HOH E 3 .   ? 3.514   21.224  4.024   1.00 35.92 ?  767 HOH A O   1 
HETATM 6456 O O   . HOH E 3 .   ? 34.972  -9.218  24.283  1.00 38.12 ?  768 HOH A O   1 
HETATM 6457 O O   . HOH E 3 .   ? 8.536   7.851   -12.428 1.00 38.87 ?  769 HOH A O   1 
HETATM 6458 O O   . HOH E 3 .   ? 39.719  19.904  3.079   1.00 27.58 ?  770 HOH A O   1 
HETATM 6459 O O   . HOH E 3 .   ? 34.148  5.933   28.873  1.00 38.46 ?  771 HOH A O   1 
HETATM 6460 O O   . HOH E 3 .   ? 19.713  11.914  -13.693 1.00 34.33 ?  772 HOH A O   1 
HETATM 6461 O O   . HOH E 3 .   ? 23.288  28.865  -4.286  1.00 28.60 ?  773 HOH A O   1 
HETATM 6462 O O   . HOH E 3 .   ? -2.724  23.823  10.749  1.00 42.22 ?  774 HOH A O   1 
HETATM 6463 O O   . HOH E 3 .   ? 15.673  27.975  14.651  1.00 28.35 ?  775 HOH A O   1 
HETATM 6464 O O   . HOH E 3 .   ? 46.269  -9.534  3.915   1.00 41.87 ?  776 HOH A O   1 
HETATM 6465 O O   . HOH E 3 .   ? 33.069  -8.226  8.505   1.00 36.57 ?  777 HOH A O   1 
HETATM 6466 O O   . HOH E 3 .   ? 13.912  14.325  35.632  1.00 40.51 ?  778 HOH A O   1 
HETATM 6467 O O   . HOH E 3 .   ? 1.508   14.514  2.059   1.00 28.84 ?  779 HOH A O   1 
HETATM 6468 O O   . HOH E 3 .   ? 1.417   16.898  2.677   1.00 33.59 ?  780 HOH A O   1 
HETATM 6469 O O   . HOH E 3 .   ? 43.927  18.253  24.787  1.00 47.92 ?  781 HOH A O   1 
HETATM 6470 O O   . HOH E 3 .   ? 32.018  8.769   -14.338 1.00 36.45 ?  782 HOH A O   1 
HETATM 6471 O O   . HOH E 3 .   ? 15.033  14.147  33.468  1.00 38.05 ?  783 HOH A O   1 
HETATM 6472 O O   . HOH E 3 .   ? -0.859  20.065  -6.371  1.00 31.69 ?  784 HOH A O   1 
HETATM 6473 O O   . HOH E 3 .   ? 16.792  31.152  -0.990  1.00 35.87 ?  785 HOH A O   1 
HETATM 6474 O O   . HOH E 3 .   ? 32.748  21.263  18.593  1.00 37.46 ?  786 HOH A O   1 
HETATM 6475 O O   . HOH E 3 .   ? 39.005  -11.042 14.482  1.00 38.70 ?  787 HOH A O   1 
HETATM 6476 O O   . HOH E 3 .   ? -2.038  12.609  12.731  1.00 22.18 ?  788 HOH A O   1 
HETATM 6477 O O   . HOH E 3 .   ? 32.340  10.906  33.858  0.50 31.30 ?  789 HOH A O   1 
HETATM 6478 O O   . HOH E 3 .   ? 0.000   12.757  0.000   0.50 26.74 ?  790 HOH A O   1 
HETATM 6479 O O   . HOH E 3 .   ? 4.186   9.030   -11.608 1.00 33.79 ?  791 HOH A O   1 
HETATM 6480 O O   . HOH E 3 .   ? 43.859  6.930   28.210  1.00 34.38 ?  792 HOH A O   1 
HETATM 6481 O O   . HOH E 3 .   ? 2.829   17.021  0.763   1.00 35.61 ?  793 HOH A O   1 
HETATM 6482 O O   . HOH E 3 .   ? 27.630  12.833  35.253  1.00 28.64 ?  794 HOH A O   1 
HETATM 6483 O O   . HOH E 3 .   ? 35.419  -5.244  -0.667  1.00 35.84 ?  795 HOH A O   1 
HETATM 6484 O O   . HOH E 3 .   ? 2.119   17.485  17.750  1.00 36.25 ?  796 HOH A O   1 
HETATM 6485 O O   . HOH E 3 .   ? 50.029  16.202  9.172   1.00 36.90 ?  797 HOH A O   1 
HETATM 6486 O O   . HOH E 3 .   ? 23.261  17.820  32.458  1.00 38.26 ?  798 HOH A O   1 
HETATM 6487 O O   . HOH E 3 .   ? 29.631  8.267   -13.375 1.00 35.10 ?  799 HOH A O   1 
HETATM 6488 O O   . HOH E 3 .   ? 44.670  17.173  0.090   1.00 26.61 ?  800 HOH A O   1 
HETATM 6489 O O   . HOH E 3 .   ? 17.971  28.020  -12.412 1.00 32.10 ?  801 HOH A O   1 
HETATM 6490 O O   . HOH E 3 .   ? 44.728  -10.219 5.326   1.00 35.32 ?  802 HOH A O   1 
HETATM 6491 O O   . HOH E 3 .   ? 12.147  20.571  30.145  1.00 25.57 ?  803 HOH A O   1 
HETATM 6492 O O   . HOH E 3 .   ? 20.253  28.110  -13.240 1.00 34.83 ?  804 HOH A O   1 
HETATM 6493 O O   . HOH E 3 .   ? 30.345  12.415  34.521  1.00 34.89 ?  805 HOH A O   1 
HETATM 6494 O O   . HOH E 3 .   ? 47.658  -2.478  14.789  1.00 39.87 ?  806 HOH A O   1 
HETATM 6495 O O   . HOH E 3 .   ? 12.539  1.322   -8.081  1.00 19.61 ?  807 HOH A O   1 
HETATM 6496 O O   . HOH E 3 .   ? 39.672  18.630  8.557   1.00 22.49 ?  808 HOH A O   1 
HETATM 6497 O O   . HOH E 3 .   ? 40.636  20.854  21.342  1.00 32.71 ?  809 HOH A O   1 
HETATM 6498 O O   . HOH E 3 .   ? 51.061  -5.642  1.304   1.00 38.50 ?  810 HOH A O   1 
HETATM 6499 O O   . HOH E 3 .   ? 35.153  24.841  19.579  1.00 40.11 ?  811 HOH A O   1 
HETATM 6500 O O   . HOH E 3 .   ? 36.765  -7.669  18.135  1.00 28.80 ?  812 HOH A O   1 
HETATM 6501 O O   . HOH E 3 .   ? 28.953  -9.460  10.939  1.00 34.62 ?  813 HOH A O   1 
HETATM 6502 O O   . HOH E 3 .   ? 7.260   22.012  24.835  1.00 32.43 ?  814 HOH A O   1 
HETATM 6503 O O   . HOH E 3 .   ? 22.975  7.576   -13.076 1.00 34.24 ?  815 HOH A O   1 
HETATM 6504 O O   . HOH E 3 .   ? 28.464  1.112   5.188   1.00 28.14 ?  816 HOH A O   1 
HETATM 6505 O O   . HOH E 3 .   ? 14.504  -0.414  -8.694  1.00 30.32 ?  817 HOH A O   1 
HETATM 6506 O O   . HOH E 3 .   ? 49.414  18.615  7.589   1.00 24.89 ?  818 HOH A O   1 
HETATM 6507 O O   . HOH E 3 .   ? 35.834  26.936  1.720   1.00 41.45 ?  819 HOH A O   1 
HETATM 6508 O O   . HOH E 3 .   ? 30.253  12.839  -12.869 1.00 31.20 ?  820 HOH A O   1 
HETATM 6509 O O   . HOH E 3 .   ? 43.390  -0.999  24.116  1.00 33.21 ?  821 HOH A O   1 
HETATM 6510 O O   . HOH E 3 .   ? 11.021  21.989  28.406  1.00 26.11 ?  822 HOH A O   1 
HETATM 6511 O O   . HOH E 3 .   ? 43.864  11.631  -9.714  1.00 31.49 ?  823 HOH A O   1 
HETATM 6512 O O   . HOH E 3 .   ? 43.084  13.898  -8.763  1.00 34.05 ?  824 HOH A O   1 
HETATM 6513 O O   . HOH E 3 .   ? 25.505  7.633   -14.005 1.00 43.27 ?  825 HOH A O   1 
HETATM 6514 O O   . HOH E 3 .   ? 46.605  -1.933  -13.777 1.00 31.71 ?  826 HOH A O   1 
HETATM 6515 O O   . HOH E 3 .   ? 3.943   25.673  -9.390  1.00 39.39 ?  827 HOH A O   1 
HETATM 6516 O O   . HOH E 3 .   ? 22.581  15.589  -14.803 1.00 38.40 ?  828 HOH A O   1 
HETATM 6517 O O   . HOH E 3 .   ? 21.270  10.480  33.654  1.00 34.67 ?  829 HOH A O   1 
HETATM 6518 O O   . HOH E 3 .   ? 31.231  -2.038  2.012   1.00 35.52 ?  830 HOH A O   1 
HETATM 6519 O O   . HOH E 3 .   ? 1.970   2.325   4.138   1.00 42.36 ?  831 HOH A O   1 
HETATM 6520 O O   . HOH E 3 .   ? 18.473  12.082  32.172  1.00 25.39 ?  832 HOH A O   1 
HETATM 6521 O O   . HOH E 3 .   ? 35.124  22.282  18.358  1.00 26.29 ?  833 HOH A O   1 
HETATM 6522 O O   . HOH E 3 .   ? 24.932  3.692   -10.225 1.00 29.98 ?  834 HOH A O   1 
HETATM 6523 O O   . HOH E 3 .   ? 12.386  5.627   -12.672 1.00 33.71 ?  835 HOH A O   1 
HETATM 6524 O O   . HOH E 3 .   ? 18.448  1.474   9.636   1.00 24.64 ?  836 HOH A O   1 
HETATM 6525 O O   . HOH E 3 .   ? -2.122  10.673  10.863  1.00 23.29 ?  837 HOH A O   1 
HETATM 6526 O O   . HOH E 3 .   ? 46.626  -8.657  15.382  1.00 39.24 ?  838 HOH A O   1 
HETATM 6527 O O   . HOH E 3 .   ? 4.326   8.116   26.502  1.00 35.06 ?  839 HOH A O   1 
HETATM 6528 O O   . HOH E 3 .   ? 43.945  -2.797  14.180  1.00 28.15 ?  840 HOH A O   1 
HETATM 6529 O O   . HOH E 3 .   ? 15.571  31.204  -3.391  1.00 34.08 ?  841 HOH A O   1 
HETATM 6530 O O   . HOH E 3 .   ? 52.371  3.235   14.296  1.00 40.51 ?  842 HOH A O   1 
HETATM 6531 O O   . HOH E 3 .   ? 43.791  16.726  32.152  1.00 43.90 ?  843 HOH A O   1 
HETATM 6532 O O   . HOH E 3 .   ? 3.639   15.568  -15.589 1.00 32.58 ?  844 HOH A O   1 
HETATM 6533 O O   . HOH E 3 .   ? -2.814  18.466  15.880  1.00 38.59 ?  845 HOH A O   1 
HETATM 6534 O O   . HOH E 3 .   ? 44.641  -1.471  18.465  1.00 36.01 ?  846 HOH A O   1 
HETATM 6535 O O   . HOH E 3 .   ? 40.877  -7.598  15.847  1.00 36.51 ?  847 HOH A O   1 
HETATM 6536 O O   . HOH E 3 .   ? 17.577  14.882  32.783  1.00 36.88 ?  848 HOH A O   1 
HETATM 6537 O O   . HOH E 3 .   ? 20.610  16.780  32.936  1.00 43.49 ?  849 HOH A O   1 
HETATM 6538 O O   . HOH E 3 .   ? 43.233  -2.604  16.581  1.00 31.54 ?  850 HOH A O   1 
HETATM 6539 O O   . HOH F 3 .   ? 21.634  -3.124  11.046  1.00 37.41 ?  501 HOH B O   1 
HETATM 6540 O O   . HOH F 3 .   ? 12.679  -17.362 -0.606  1.00 36.51 ?  502 HOH B O   1 
HETATM 6541 O O   . HOH F 3 .   ? -9.952  -15.279 4.308   1.00 10.32 ?  503 HOH B O   1 
HETATM 6542 O O   . HOH F 3 .   ? -19.231 -13.202 8.869   1.00 32.15 ?  504 HOH B O   1 
HETATM 6543 O O   . HOH F 3 .   ? 20.679  -0.529  10.608  1.00 33.34 ?  505 HOH B O   1 
HETATM 6544 O O   . HOH F 3 .   ? 18.094  -30.052 22.474  1.00 30.19 ?  506 HOH B O   1 
HETATM 6545 O O   . HOH F 3 .   ? -6.753  4.925   49.580  1.00 35.48 ?  507 HOH B O   1 
HETATM 6546 O O   . HOH F 3 .   ? -14.559 -1.363  52.775  1.00 24.56 ?  508 HOH B O   1 
HETATM 6547 O O   . HOH F 3 .   ? 1.375   -2.470  25.961  1.00 29.89 ?  509 HOH B O   1 
HETATM 6548 O O   . HOH F 3 .   ? -17.165 -6.651  20.358  1.00 37.04 ?  510 HOH B O   1 
HETATM 6549 O O   . HOH F 3 .   ? 7.117   -22.306 40.164  1.00 18.85 ?  511 HOH B O   1 
HETATM 6550 O O   . HOH F 3 .   ? 36.001  -7.820  32.687  1.00 26.57 ?  512 HOH B O   1 
HETATM 6551 O O   . HOH F 3 .   ? -18.908 -18.958 26.822  1.00 24.95 ?  513 HOH B O   1 
HETATM 6552 O O   . HOH F 3 .   ? -1.842  -15.120 51.420  1.00 38.18 ?  514 HOH B O   1 
HETATM 6553 O O   . HOH F 3 .   ? -18.434 -8.911  22.508  1.00 30.20 ?  515 HOH B O   1 
HETATM 6554 O O   . HOH F 3 .   ? 7.671   2.174   33.859  1.00 23.60 ?  516 HOH B O   1 
HETATM 6555 O O   . HOH F 3 .   ? 10.220  -17.262 -2.982  1.00 18.11 ?  517 HOH B O   1 
HETATM 6556 O O   . HOH F 3 .   ? -20.538 -2.315  35.851  1.00 23.81 ?  518 HOH B O   1 
HETATM 6557 O O   . HOH F 3 .   ? 18.010  -10.642 11.012  1.00 20.52 ?  519 HOH B O   1 
HETATM 6558 O O   . HOH F 3 .   ? 6.370   -19.797 22.605  1.00 19.52 ?  520 HOH B O   1 
HETATM 6559 O O   . HOH F 3 .   ? -21.413 -11.378 34.546  1.00 31.85 ?  521 HOH B O   1 
HETATM 6560 O O   . HOH F 3 .   ? 14.636  -10.366 -1.507  1.00 20.07 ?  522 HOH B O   1 
HETATM 6561 O O   . HOH F 3 .   ? 3.297   -23.364 35.614  1.00 28.14 ?  523 HOH B O   1 
HETATM 6562 O O   . HOH F 3 .   ? 16.659  -26.629 17.333  1.00 25.66 ?  524 HOH B O   1 
HETATM 6563 O O   . HOH F 3 .   ? 16.149  -1.936  14.961  1.00 22.00 ?  525 HOH B O   1 
HETATM 6564 O O   . HOH F 3 .   ? -4.563  -1.483  30.257  1.00 38.37 ?  526 HOH B O   1 
HETATM 6565 O O   . HOH F 3 .   ? 0.852   -4.939  1.232   1.00 26.92 ?  527 HOH B O   1 
HETATM 6566 O O   . HOH F 3 .   ? -15.719 -11.946 44.497  1.00 21.07 ?  528 HOH B O   1 
HETATM 6567 O O   . HOH F 3 .   ? -15.233 -25.707 6.605   1.00 34.37 ?  529 HOH B O   1 
HETATM 6568 O O   . HOH F 3 .   ? -2.665  -18.965 42.424  1.00 17.74 ?  530 HOH B O   1 
HETATM 6569 O O   . HOH F 3 .   ? -9.432  0.062   21.952  1.00 22.80 ?  531 HOH B O   1 
HETATM 6570 O O   . HOH F 3 .   ? -13.389 -3.726  16.891  1.00 21.76 ?  532 HOH B O   1 
HETATM 6571 O O   . HOH F 3 .   ? -6.592  -10.568 54.108  1.00 31.12 ?  533 HOH B O   1 
HETATM 6572 O O   . HOH F 3 .   ? 26.581  -12.285 14.607  1.00 28.74 ?  534 HOH B O   1 
HETATM 6573 O O   . HOH F 3 .   ? -17.694 -24.197 10.086  1.00 23.21 ?  535 HOH B O   1 
HETATM 6574 O O   . HOH F 3 .   ? 1.169   -25.936 6.375   1.00 24.06 ?  536 HOH B O   1 
HETATM 6575 O O   . HOH F 3 .   ? -5.828  -2.369  -1.270  1.00 27.56 ?  537 HOH B O   1 
HETATM 6576 O O   . HOH F 3 .   ? 9.679   -15.912 25.782  1.00 20.65 ?  538 HOH B O   1 
HETATM 6577 O O   . HOH F 3 .   ? 22.688  -6.047  21.780  1.00 15.99 ?  539 HOH B O   1 
HETATM 6578 O O   . HOH F 3 .   ? 34.856  -9.404  30.470  1.00 32.12 ?  540 HOH B O   1 
HETATM 6579 O O   . HOH F 3 .   ? 1.225   -0.309  48.704  1.00 25.20 ?  541 HOH B O   1 
HETATM 6580 O O   . HOH F 3 .   ? 15.236  7.197   32.135  1.00 20.16 ?  542 HOH B O   1 
HETATM 6581 O O   . HOH F 3 .   ? -4.881  -8.498  -0.259  1.00 22.80 ?  543 HOH B O   1 
HETATM 6582 O O   . HOH F 3 .   ? -11.932 -22.292 25.090  1.00 33.74 ?  544 HOH B O   1 
HETATM 6583 O O   . HOH F 3 .   ? -14.209 -17.640 35.620  1.00 22.67 ?  545 HOH B O   1 
HETATM 6584 O O   . HOH F 3 .   ? 13.607  -10.145 41.409  1.00 16.96 ?  546 HOH B O   1 
HETATM 6585 O O   . HOH F 3 .   ? 11.966  -6.716  43.453  1.00 20.79 ?  547 HOH B O   1 
HETATM 6586 O O   . HOH F 3 .   ? -4.047  -4.237  34.412  1.00 18.12 ?  548 HOH B O   1 
HETATM 6587 O O   . HOH F 3 .   ? 0.531   5.237   36.860  1.00 21.22 ?  549 HOH B O   1 
HETATM 6588 O O   . HOH F 3 .   ? 8.427   -18.221 25.310  1.00 19.95 ?  550 HOH B O   1 
HETATM 6589 O O   . HOH F 3 .   ? -3.652  -17.395 -1.071  1.00 36.92 ?  551 HOH B O   1 
HETATM 6590 O O   . HOH F 3 .   ? -1.267  -22.257 24.342  1.00 16.76 ?  552 HOH B O   1 
HETATM 6591 O O   . HOH F 3 .   ? 24.735  -13.374 33.115  1.00 25.33 ?  553 HOH B O   1 
HETATM 6592 O O   . HOH F 3 .   ? 24.948  -12.939 37.825  1.00 35.21 ?  554 HOH B O   1 
HETATM 6593 O O   . HOH F 3 .   ? 4.277   -26.837 24.455  1.00 34.05 ?  555 HOH B O   1 
HETATM 6594 O O   . HOH F 3 .   ? 21.131  -27.031 22.948  1.00 32.37 ?  556 HOH B O   1 
HETATM 6595 O O   . HOH F 3 .   ? 17.704  -22.242 28.282  1.00 23.40 ?  557 HOH B O   1 
HETATM 6596 O O   . HOH F 3 .   ? -2.902  2.026   51.715  1.00 38.43 ?  558 HOH B O   1 
HETATM 6597 O O   . HOH F 3 .   ? -12.791 1.230   14.959  1.00 34.89 ?  559 HOH B O   1 
HETATM 6598 O O   . HOH F 3 .   ? 22.870  -2.091  16.140  1.00 21.69 ?  560 HOH B O   1 
HETATM 6599 O O   . HOH F 3 .   ? 5.703   -27.992 29.350  1.00 38.41 ?  561 HOH B O   1 
HETATM 6600 O O   . HOH F 3 .   ? 5.816   -15.961 1.166   1.00 24.61 ?  562 HOH B O   1 
HETATM 6601 O O   . HOH F 3 .   ? -9.339  0.699   28.590  1.00 29.26 ?  563 HOH B O   1 
HETATM 6602 O O   . HOH F 3 .   ? -7.272  2.368   16.550  1.00 25.04 ?  564 HOH B O   1 
HETATM 6603 O O   . HOH F 3 .   ? -1.571  -25.668 25.391  1.00 17.84 ?  565 HOH B O   1 
HETATM 6604 O O   . HOH F 3 .   ? 26.875  -1.835  20.167  1.00 17.77 ?  566 HOH B O   1 
HETATM 6605 O O   . HOH F 3 .   ? 6.243   -10.020 47.685  1.00 20.69 ?  567 HOH B O   1 
HETATM 6606 O O   . HOH F 3 .   ? 8.014   -24.109 41.964  1.00 33.92 ?  568 HOH B O   1 
HETATM 6607 O O   . HOH F 3 .   ? 9.322   -8.327  2.756   1.00 25.22 ?  569 HOH B O   1 
HETATM 6608 O O   . HOH F 3 .   ? -19.807 -8.245  38.950  1.00 18.82 ?  570 HOH B O   1 
HETATM 6609 O O   . HOH F 3 .   ? -3.823  -24.050 2.389   1.00 28.59 ?  571 HOH B O   1 
HETATM 6610 O O   . HOH F 3 .   ? -6.094  9.716   43.974  1.00 27.84 ?  572 HOH B O   1 
HETATM 6611 O O   . HOH F 3 .   ? -14.313 -4.950  9.700   1.00 21.84 ?  573 HOH B O   1 
HETATM 6612 O O   . HOH F 3 .   ? -24.184 -16.485 31.713  1.00 34.88 ?  574 HOH B O   1 
HETATM 6613 O O   . HOH F 3 .   ? 8.727   -14.580 -2.218  1.00 17.83 ?  575 HOH B O   1 
HETATM 6614 O O   . HOH F 3 .   ? 19.336  -19.346 41.528  1.00 40.11 ?  576 HOH B O   1 
HETATM 6615 O O   . HOH F 3 .   ? 1.864   -2.333  41.554  1.00 18.72 ?  577 HOH B O   1 
HETATM 6616 O O   . HOH F 3 .   ? -15.836 -16.655 18.788  1.00 19.13 ?  578 HOH B O   1 
HETATM 6617 O O   . HOH F 3 .   ? 6.664   -7.663  32.658  1.00 15.23 ?  579 HOH B O   1 
HETATM 6618 O O   . HOH F 3 .   ? -11.174 -5.680  54.906  1.00 23.28 ?  580 HOH B O   1 
HETATM 6619 O O   . HOH F 3 .   ? 15.300  -11.594 4.446   1.00 22.52 ?  581 HOH B O   1 
HETATM 6620 O O   . HOH F 3 .   ? -7.119  -12.156 18.998  1.00 16.86 ?  582 HOH B O   1 
HETATM 6621 O O   . HOH F 3 .   ? -6.223  -6.826  51.354  1.00 17.46 ?  583 HOH B O   1 
HETATM 6622 O O   . HOH F 3 .   ? 17.553  -17.283 37.183  1.00 18.63 ?  584 HOH B O   1 
HETATM 6623 O O   . HOH F 3 .   ? -2.825  -16.447 1.258   1.00 30.10 ?  585 HOH B O   1 
HETATM 6624 O O   . HOH F 3 .   ? -8.387  3.091   38.995  1.00 19.04 ?  586 HOH B O   1 
HETATM 6625 O O   . HOH F 3 .   ? 16.154  -8.932  12.116  1.00 17.64 ?  587 HOH B O   1 
HETATM 6626 O O   . HOH F 3 .   ? -13.079 -16.313 18.617  1.00 19.46 ?  588 HOH B O   1 
HETATM 6627 O O   . HOH F 3 .   ? -3.244  -2.882  27.815  1.00 24.95 ?  589 HOH B O   1 
HETATM 6628 O O   . HOH F 3 .   ? 14.511  -18.047 3.780   1.00 25.56 ?  590 HOH B O   1 
HETATM 6629 O O   . HOH F 3 .   ? 4.487   -20.797 30.998  1.00 17.26 ?  591 HOH B O   1 
HETATM 6630 O O   . HOH F 3 .   ? -11.214 -16.919 39.734  1.00 21.74 ?  592 HOH B O   1 
HETATM 6631 O O   . HOH F 3 .   ? 5.668   -14.760 29.071  1.00 16.23 ?  593 HOH B O   1 
HETATM 6632 O O   . HOH F 3 .   ? -2.866  -10.991 1.955   1.00 20.94 ?  594 HOH B O   1 
HETATM 6633 O O   . HOH F 3 .   ? -3.130  -15.840 35.772  1.00 23.81 ?  595 HOH B O   1 
HETATM 6634 O O   . HOH F 3 .   ? -10.049 -6.775  1.078   1.00 33.97 ?  596 HOH B O   1 
HETATM 6635 O O   . HOH F 3 .   ? 11.598  -11.833 48.057  1.00 26.78 ?  597 HOH B O   1 
HETATM 6636 O O   . HOH F 3 .   ? -15.233 -24.009 12.531  1.00 21.80 ?  598 HOH B O   1 
HETATM 6637 O O   . HOH F 3 .   ? 18.288  10.245  33.921  1.00 31.46 ?  599 HOH B O   1 
HETATM 6638 O O   . HOH F 3 .   ? -8.905  -12.440 53.501  1.00 32.62 ?  600 HOH B O   1 
HETATM 6639 O O   . HOH F 3 .   ? -7.443  -5.904  53.751  1.00 21.37 ?  601 HOH B O   1 
HETATM 6640 O O   . HOH F 3 .   ? -7.867  -4.617  -0.119  1.00 36.17 ?  602 HOH B O   1 
HETATM 6641 O O   . HOH F 3 .   ? -5.409  -0.065  51.715  1.00 22.41 ?  603 HOH B O   1 
HETATM 6642 O O   . HOH F 3 .   ? 5.828   -30.049 16.541  1.00 30.26 ?  604 HOH B O   1 
HETATM 6643 O O   . HOH F 3 .   ? -7.084  3.817   34.734  1.00 29.36 ?  605 HOH B O   1 
HETATM 6644 O O   . HOH F 3 .   ? -17.367 -17.271 4.834   1.00 26.40 ?  606 HOH B O   1 
HETATM 6645 O O   . HOH F 3 .   ? 1.085   -2.198  2.352   1.00 30.98 ?  607 HOH B O   1 
HETATM 6646 O O   . HOH F 3 .   ? 3.078   -19.907 45.825  1.00 22.92 ?  608 HOH B O   1 
HETATM 6647 O O   . HOH F 3 .   ? -1.742  -12.822 4.685   1.00 29.84 ?  609 HOH B O   1 
HETATM 6648 O O   . HOH F 3 .   ? -3.177  -28.614 25.857  1.00 24.68 ?  610 HOH B O   1 
HETATM 6649 O O   . HOH F 3 .   ? -2.021  -20.209 -1.284  1.00 25.63 ?  611 HOH B O   1 
HETATM 6650 O O   . HOH F 3 .   ? 0.839   1.710   6.900   1.00 19.76 ?  612 HOH B O   1 
HETATM 6651 O O   . HOH F 3 .   ? 24.440  -12.871 27.662  1.00 19.23 ?  613 HOH B O   1 
HETATM 6652 O O   . HOH F 3 .   ? 25.573  -17.923 24.822  1.00 32.09 ?  614 HOH B O   1 
HETATM 6653 O O   . HOH F 3 .   ? 21.726  -20.590 16.122  1.00 24.21 ?  615 HOH B O   1 
HETATM 6654 O O   . HOH F 3 .   ? -6.662  -14.365 20.457  1.00 16.26 ?  616 HOH B O   1 
HETATM 6655 O O   . HOH F 3 .   ? -8.393  -13.210 36.157  1.00 17.31 ?  617 HOH B O   1 
HETATM 6656 O O   . HOH F 3 .   ? 9.937   3.024   9.535   1.00 13.54 ?  618 HOH B O   1 
HETATM 6657 O O   . HOH F 3 .   ? -2.558  6.100   10.414  1.00 30.02 ?  619 HOH B O   1 
HETATM 6658 O O   . HOH F 3 .   ? -16.253 -23.496 22.020  1.00 28.39 ?  620 HOH B O   1 
HETATM 6659 O O   . HOH F 3 .   ? 27.964  -6.398  37.135  1.00 32.98 ?  621 HOH B O   1 
HETATM 6660 O O   . HOH F 3 .   ? -16.810 -3.068  25.743  1.00 23.12 ?  622 HOH B O   1 
HETATM 6661 O O   . HOH F 3 .   ? 16.892  -19.324 6.766   1.00 34.72 ?  623 HOH B O   1 
HETATM 6662 O O   . HOH F 3 .   ? -12.472 -16.785 50.087  1.00 19.86 ?  624 HOH B O   1 
HETATM 6663 O O   . HOH F 3 .   ? 1.426   -28.674 23.310  1.00 28.35 ?  625 HOH B O   1 
HETATM 6664 O O   . HOH F 3 .   ? 5.828   -18.092 24.595  1.00 18.89 ?  626 HOH B O   1 
HETATM 6665 O O   . HOH F 3 .   ? 13.251  4.214   35.170  1.00 19.95 ?  627 HOH B O   1 
HETATM 6666 O O   . HOH F 3 .   ? -8.472  1.299   8.798   1.00 20.56 ?  628 HOH B O   1 
HETATM 6667 O O   . HOH F 3 .   ? 1.858   -29.132 19.723  1.00 33.61 ?  629 HOH B O   1 
HETATM 6668 O O   . HOH F 3 .   ? 11.419  -24.855 7.276   1.00 25.85 ?  630 HOH B O   1 
HETATM 6669 O O   . HOH F 3 .   ? -12.143 -15.013 43.679  1.00 20.15 ?  631 HOH B O   1 
HETATM 6670 O O   . HOH F 3 .   ? -11.165 -20.141 2.036   1.00 25.48 ?  632 HOH B O   1 
HETATM 6671 O O   . HOH F 3 .   ? 5.344   -20.611 8.848   1.00 14.26 ?  633 HOH B O   1 
HETATM 6672 O O   . HOH F 3 .   ? 10.177  0.738   34.664  1.00 27.89 ?  634 HOH B O   1 
HETATM 6673 O O   . HOH F 3 .   ? 14.612  10.717  37.018  1.00 25.38 ?  635 HOH B O   1 
HETATM 6674 O O   . HOH F 3 .   ? -10.961 -17.169 53.402  1.00 27.45 ?  636 HOH B O   1 
HETATM 6675 O O   . HOH F 3 .   ? 6.582   7.707   41.856  1.00 32.96 ?  637 HOH B O   1 
HETATM 6676 O O   . HOH F 3 .   ? -16.875 -7.366  8.321   1.00 30.72 ?  638 HOH B O   1 
HETATM 6677 O O   . HOH F 3 .   ? 7.978   -2.067  24.222  1.00 29.61 ?  639 HOH B O   1 
HETATM 6678 O O   . HOH F 3 .   ? 16.604  -3.546  19.698  1.00 17.66 ?  640 HOH B O   1 
HETATM 6679 O O   . HOH F 3 .   ? 22.534  -10.361 11.914  1.00 23.60 ?  641 HOH B O   1 
HETATM 6680 O O   . HOH F 3 .   ? 8.048   -24.941 3.974   1.00 32.10 ?  642 HOH B O   1 
HETATM 6681 O O   . HOH F 3 .   ? -8.974  -21.562 0.897   1.00 20.87 ?  643 HOH B O   1 
HETATM 6682 O O   . HOH F 3 .   ? -18.729 -21.604 9.488   1.00 19.95 ?  644 HOH B O   1 
HETATM 6683 O O   . HOH F 3 .   ? -13.846 -13.161 42.640  1.00 18.87 ?  645 HOH B O   1 
HETATM 6684 O O   . HOH F 3 .   ? 3.281   -2.619  2.476   1.00 33.42 ?  646 HOH B O   1 
HETATM 6685 O O   . HOH F 3 .   ? 9.723   -1.486  48.093  1.00 24.01 ?  647 HOH B O   1 
HETATM 6686 O O   . HOH F 3 .   ? -21.416 4.233   33.970  1.00 27.18 ?  648 HOH B O   1 
HETATM 6687 O O   . HOH F 3 .   ? -4.242  -17.611 37.822  1.00 20.12 ?  649 HOH B O   1 
HETATM 6688 O O   . HOH F 3 .   ? -15.372 -1.018  24.629  1.00 23.24 ?  650 HOH B O   1 
HETATM 6689 O O   . HOH F 3 .   ? -17.177 -12.047 7.448   1.00 28.02 ?  651 HOH B O   1 
HETATM 6690 O O   . HOH F 3 .   ? -4.479  3.211   15.279  1.00 25.62 ?  652 HOH B O   1 
HETATM 6691 O O   . HOH F 3 .   ? 29.319  -2.511  21.111  1.00 20.37 ?  653 HOH B O   1 
HETATM 6692 O O   . HOH F 3 .   ? 13.749  -10.746 35.330  1.00 14.44 ?  654 HOH B O   1 
HETATM 6693 O O   . HOH F 3 .   ? -7.337  -29.829 17.123  1.00 24.98 ?  655 HOH B O   1 
HETATM 6694 O O   . HOH F 3 .   ? -0.404  -2.927  29.750  1.00 20.66 ?  656 HOH B O   1 
HETATM 6695 O O   . HOH F 3 .   ? 6.235   -4.261  5.900   1.00 29.35 ?  657 HOH B O   1 
HETATM 6696 O O   . HOH F 3 .   ? -6.048  -27.186 7.197   1.00 25.98 ?  658 HOH B O   1 
HETATM 6697 O O   . HOH F 3 .   ? -17.364 -13.642 53.534  1.00 32.48 ?  659 HOH B O   1 
HETATM 6698 O O   . HOH F 3 .   ? 15.045  -5.694  53.098  1.00 42.44 ?  660 HOH B O   1 
HETATM 6699 O O   . HOH F 3 .   ? -6.774  -18.773 47.201  1.00 17.16 ?  661 HOH B O   1 
HETATM 6700 O O   . HOH F 3 .   ? 0.595   0.254   4.454   1.00 23.40 ?  662 HOH B O   1 
HETATM 6701 O O   . HOH F 3 .   ? 13.005  1.691   19.869  1.00 24.42 ?  663 HOH B O   1 
HETATM 6702 O O   . HOH F 3 .   ? 22.190  -5.837  11.871  1.00 28.28 ?  664 HOH B O   1 
HETATM 6703 O O   . HOH F 3 .   ? 27.339  -8.980  27.951  1.00 19.35 ?  665 HOH B O   1 
HETATM 6704 O O   . HOH F 3 .   ? -7.886  -9.428  -0.216  1.00 20.80 ?  666 HOH B O   1 
HETATM 6705 O O   . HOH F 3 .   ? 7.856   -28.466 15.293  1.00 23.83 ?  667 HOH B O   1 
HETATM 6706 O O   . HOH F 3 .   ? 0.584   -13.902 24.689  1.00 13.15 ?  668 HOH B O   1 
HETATM 6707 O O   . HOH F 3 .   ? 8.614   -4.262  31.733  1.00 15.00 ?  669 HOH B O   1 
HETATM 6708 O O   . HOH F 3 .   ? 0.229   -17.281 51.517  1.00 35.28 ?  670 HOH B O   1 
HETATM 6709 O O   . HOH F 3 .   ? -19.952 -22.633 16.641  1.00 22.59 ?  671 HOH B O   1 
HETATM 6710 O O   . HOH F 3 .   ? 4.189   -32.192 10.779  1.00 30.28 ?  672 HOH B O   1 
HETATM 6711 O O   . HOH F 3 .   ? 6.107   -1.437  5.165   1.00 21.73 ?  673 HOH B O   1 
HETATM 6712 O O   . HOH F 3 .   ? 3.404   -13.512 47.156  1.00 20.35 ?  674 HOH B O   1 
HETATM 6713 O O   . HOH F 3 .   ? -0.958  -5.743  28.232  1.00 27.09 ?  675 HOH B O   1 
HETATM 6714 O O   . HOH F 3 .   ? 2.969   6.533   44.617  1.00 36.03 ?  676 HOH B O   1 
HETATM 6715 O O   . HOH F 3 .   ? 6.462   -5.726  30.777  1.00 17.64 ?  677 HOH B O   1 
HETATM 6716 O O   . HOH F 3 .   ? -14.044 -22.281 23.665  1.00 28.73 ?  678 HOH B O   1 
HETATM 6717 O O   . HOH F 3 .   ? -14.333 -3.458  13.718  1.00 37.18 ?  679 HOH B O   1 
HETATM 6718 O O   . HOH F 3 .   ? -13.994 -26.845 10.246  1.00 18.57 ?  680 HOH B O   1 
HETATM 6719 O O   . HOH F 3 .   ? -17.030 -6.905  17.869  1.00 36.27 ?  681 HOH B O   1 
HETATM 6720 O O   . HOH F 3 .   ? -21.074 -13.097 24.974  1.00 28.19 ?  682 HOH B O   1 
HETATM 6721 O O   . HOH F 3 .   ? -18.465 -11.685 16.833  1.00 20.73 ?  683 HOH B O   1 
HETATM 6722 O O   . HOH F 3 .   ? 21.127  -22.985 30.309  1.00 38.85 ?  684 HOH B O   1 
HETATM 6723 O O   . HOH F 3 .   ? 11.386  -21.945 35.221  1.00 20.91 ?  685 HOH B O   1 
HETATM 6724 O O   . HOH F 3 .   ? -12.724 -17.874 30.468  1.00 23.23 ?  686 HOH B O   1 
HETATM 6725 O O   . HOH F 3 .   ? 12.386  -30.474 27.412  1.00 34.32 ?  687 HOH B O   1 
HETATM 6726 O O   . HOH F 3 .   ? 0.966   -3.844  39.520  1.00 17.79 ?  688 HOH B O   1 
HETATM 6727 O O   . HOH F 3 .   ? 29.140  -9.689  13.128  1.00 25.16 ?  689 HOH B O   1 
HETATM 6728 O O   . HOH F 3 .   ? -11.388 -1.367  11.807  1.00 19.23 ?  690 HOH B O   1 
HETATM 6729 O O   . HOH F 3 .   ? -0.210  -3.447  52.565  1.00 30.15 ?  691 HOH B O   1 
HETATM 6730 O O   . HOH F 3 .   ? -12.360 -28.162 5.745   1.00 23.16 ?  692 HOH B O   1 
HETATM 6731 O O   . HOH F 3 .   ? 1.340   -24.955 38.933  1.00 36.09 ?  693 HOH B O   1 
HETATM 6732 O O   . HOH F 3 .   ? 14.630  -4.603  3.756   1.00 25.38 ?  694 HOH B O   1 
HETATM 6733 O O   . HOH F 3 .   ? -17.122 -3.583  21.937  1.00 29.53 ?  695 HOH B O   1 
HETATM 6734 O O   . HOH F 3 .   ? 20.494  -19.144 37.993  1.00 30.37 ?  696 HOH B O   1 
HETATM 6735 O O   . HOH F 3 .   ? -16.495 8.523   37.376  1.00 35.73 ?  697 HOH B O   1 
HETATM 6736 O O   . HOH F 3 .   ? 4.947   -23.551 37.449  1.00 34.32 ?  698 HOH B O   1 
HETATM 6737 O O   . HOH F 3 .   ? -8.140  2.708   32.223  1.00 25.62 ?  699 HOH B O   1 
HETATM 6738 O O   . HOH F 3 .   ? 12.070  5.191   33.035  1.00 24.22 ?  700 HOH B O   1 
HETATM 6739 O O   . HOH F 3 .   ? 20.051  -7.452  12.293  1.00 26.59 ?  701 HOH B O   1 
HETATM 6740 O O   . HOH F 3 .   ? 31.993  -7.098  27.165  1.00 27.79 ?  702 HOH B O   1 
HETATM 6741 O O   . HOH F 3 .   ? 15.415  -15.067 7.882   1.00 36.53 ?  703 HOH B O   1 
HETATM 6742 O O   . HOH F 3 .   ? -9.672  9.911   38.359  1.00 28.88 ?  704 HOH B O   1 
HETATM 6743 O O   . HOH F 3 .   ? -16.265 -7.513  13.824  1.00 21.98 ?  705 HOH B O   1 
HETATM 6744 O O   . HOH F 3 .   ? 6.149   -30.705 13.250  1.00 39.83 ?  706 HOH B O   1 
HETATM 6745 O O   . HOH F 3 .   ? 12.234  -26.645 8.841   1.00 26.24 ?  707 HOH B O   1 
HETATM 6746 O O   . HOH F 3 .   ? -4.214  -11.481 30.649  1.00 19.81 ?  708 HOH B O   1 
HETATM 6747 O O   . HOH F 3 .   ? -3.778  -32.657 9.388   1.00 44.57 ?  709 HOH B O   1 
HETATM 6748 O O   . HOH F 3 .   ? 21.720  -13.821 11.995  1.00 25.58 ?  710 HOH B O   1 
HETATM 6749 O O   . HOH F 3 .   ? 30.296  -10.239 33.637  1.00 31.34 ?  711 HOH B O   1 
HETATM 6750 O O   . HOH F 3 .   ? -15.363 2.006   54.256  1.00 33.08 ?  712 HOH B O   1 
HETATM 6751 O O   . HOH F 3 .   ? 1.457   -11.195 32.159  1.00 18.32 ?  713 HOH B O   1 
HETATM 6752 O O   . HOH F 3 .   ? 8.782   -27.746 17.449  1.00 28.78 ?  714 HOH B O   1 
HETATM 6753 O O   . HOH F 3 .   ? -20.700 -11.020 13.489  1.00 31.88 ?  715 HOH B O   1 
HETATM 6754 O O   . HOH F 3 .   ? 8.501   0.204   24.749  1.00 29.69 ?  716 HOH B O   1 
HETATM 6755 O O   . HOH F 3 .   ? -6.062  -24.951 28.073  1.00 39.00 ?  717 HOH B O   1 
HETATM 6756 O O   . HOH F 3 .   ? -3.979  -32.339 20.147  1.00 29.43 ?  718 HOH B O   1 
HETATM 6757 O O   . HOH F 3 .   ? -1.378  -29.610 14.180  1.00 24.25 ?  719 HOH B O   1 
HETATM 6758 O O   . HOH F 3 .   ? -23.623 2.085   40.769  1.00 41.04 ?  720 HOH B O   1 
HETATM 6759 O O   . HOH F 3 .   ? 23.854  -8.880  39.060  1.00 23.57 ?  721 HOH B O   1 
HETATM 6760 O O   . HOH F 3 .   ? -5.496  -18.580 42.427  1.00 18.82 ?  722 HOH B O   1 
HETATM 6761 O O   . HOH F 3 .   ? 1.974   -21.987 44.304  1.00 25.17 ?  723 HOH B O   1 
HETATM 6762 O O   . HOH F 3 .   ? 1.812   -19.338 3.827   1.00 25.35 ?  724 HOH B O   1 
HETATM 6763 O O   . HOH F 3 .   ? 6.437   -6.046  28.039  1.00 24.66 ?  725 HOH B O   1 
HETATM 6764 O O   . HOH F 3 .   ? -9.237  -17.456 31.162  1.00 26.73 ?  726 HOH B O   1 
HETATM 6765 O O   . HOH F 3 .   ? -18.137 -9.058  15.416  1.00 40.02 ?  727 HOH B O   1 
HETATM 6766 O O   . HOH F 3 .   ? 18.400  -20.395 35.577  1.00 22.04 ?  728 HOH B O   1 
HETATM 6767 O O   . HOH F 3 .   ? 7.854   -2.569  7.165   1.00 20.87 ?  729 HOH B O   1 
HETATM 6768 O O   . HOH F 3 .   ? -2.399  7.659   34.786  1.00 35.05 ?  730 HOH B O   1 
HETATM 6769 O O   . HOH F 3 .   ? 7.805   -2.411  21.584  1.00 33.33 ?  731 HOH B O   1 
HETATM 6770 O O   . HOH F 3 .   ? 7.412   -14.747 24.994  1.00 17.87 ?  732 HOH B O   1 
HETATM 6771 O O   . HOH F 3 .   ? -15.700 -1.425  6.579   1.00 25.59 ?  733 HOH B O   1 
HETATM 6772 O O   . HOH F 3 .   ? 8.923   7.613   38.602  1.00 29.40 ?  734 HOH B O   1 
HETATM 6773 O O   . HOH F 3 .   ? -8.594  -20.051 39.693  1.00 27.83 ?  735 HOH B O   1 
HETATM 6774 O O   . HOH F 3 .   ? 9.838   -5.351  2.900   1.00 25.73 ?  736 HOH B O   1 
HETATM 6775 O O   . HOH F 3 .   ? -6.679  0.660   20.641  1.00 26.33 ?  737 HOH B O   1 
HETATM 6776 O O   . HOH F 3 .   ? 16.758  -16.410 10.042  1.00 31.28 ?  738 HOH B O   1 
HETATM 6777 O O   . HOH F 3 .   ? -5.605  -30.292 23.964  1.00 23.07 ?  739 HOH B O   1 
HETATM 6778 O O   . HOH F 3 .   ? -15.441 -21.986 28.676  1.00 38.98 ?  740 HOH B O   1 
HETATM 6779 O O   . HOH F 3 .   ? -2.004  -16.186 49.504  1.00 37.64 ?  741 HOH B O   1 
HETATM 6780 O O   . HOH F 3 .   ? 16.504  -2.282  11.238  1.00 18.15 ?  742 HOH B O   1 
HETATM 6781 O O   . HOH F 3 .   ? -16.387 1.694   25.507  1.00 32.01 ?  743 HOH B O   1 
HETATM 6782 O O   . HOH F 3 .   ? 13.528  -23.339 7.508   1.00 28.93 ?  744 HOH B O   1 
HETATM 6783 O O   . HOH F 3 .   ? -7.171  0.005   29.154  1.00 40.87 ?  745 HOH B O   1 
HETATM 6784 O O   . HOH F 3 .   ? 9.408   4.198   41.578  1.00 24.37 ?  746 HOH B O   1 
HETATM 6785 O O   . HOH F 3 .   ? -0.000  -6.683  0.000   0.50 26.39 ?  747 HOH B O   1 
HETATM 6786 O O   . HOH F 3 .   ? -16.795 -9.323  6.370   1.00 25.43 ?  748 HOH B O   1 
HETATM 6787 O O   . HOH F 3 .   ? 10.319  -30.381 20.267  1.00 31.38 ?  749 HOH B O   1 
HETATM 6788 O O   . HOH F 3 .   ? -15.694 -5.450  15.914  1.00 29.75 ?  750 HOH B O   1 
HETATM 6789 O O   . HOH F 3 .   ? -16.595 -10.247 23.687  1.00 26.23 ?  751 HOH B O   1 
HETATM 6790 O O   . HOH F 3 .   ? -21.101 -9.717  28.670  1.00 30.83 ?  752 HOH B O   1 
HETATM 6791 O O   . HOH F 3 .   ? -5.552  -23.488 -0.755  1.00 34.54 ?  753 HOH B O   1 
HETATM 6792 O O   . HOH F 3 .   ? 9.014   12.672  33.037  1.00 30.12 ?  754 HOH B O   1 
HETATM 6793 O O   . HOH F 3 .   ? -3.323  -27.506 35.686  1.00 27.16 ?  755 HOH B O   1 
HETATM 6794 O O   . HOH F 3 .   ? 21.579  -7.543  40.050  1.00 27.12 ?  756 HOH B O   1 
HETATM 6795 O O   . HOH F 3 .   ? 9.550   -0.550  20.406  1.00 37.93 ?  757 HOH B O   1 
HETATM 6796 O O   . HOH F 3 .   ? -9.810  -27.082 12.034  1.00 25.87 ?  758 HOH B O   1 
HETATM 6797 O O   . HOH F 3 .   ? -8.873  5.825   35.759  1.00 29.62 ?  759 HOH B O   1 
HETATM 6798 O O   . HOH F 3 .   ? 24.341  -15.443 29.082  1.00 26.65 ?  760 HOH B O   1 
HETATM 6799 O O   . HOH F 3 .   ? -18.734 -23.507 19.165  1.00 16.75 ?  761 HOH B O   1 
HETATM 6800 O O   . HOH F 3 .   ? -22.766 -11.601 28.713  1.00 37.97 ?  762 HOH B O   1 
HETATM 6801 O O   . HOH F 3 .   ? 36.662  -3.636  27.343  1.00 33.54 ?  763 HOH B O   1 
HETATM 6802 O O   . HOH F 3 .   ? -10.700 4.709   50.770  1.00 25.87 ?  764 HOH B O   1 
HETATM 6803 O O   . HOH F 3 .   ? -22.094 -2.876  33.809  1.00 36.59 ?  765 HOH B O   1 
HETATM 6804 O O   . HOH F 3 .   ? -19.614 -16.622 4.932   1.00 36.63 ?  766 HOH B O   1 
HETATM 6805 O O   . HOH F 3 .   ? 20.100  -23.350 27.862  1.00 26.70 ?  767 HOH B O   1 
HETATM 6806 O O   . HOH F 3 .   ? 8.847   -21.717 35.783  1.00 27.83 ?  768 HOH B O   1 
HETATM 6807 O O   . HOH F 3 .   ? 27.058  -12.131 31.602  1.00 32.38 ?  769 HOH B O   1 
HETATM 6808 O O   . HOH F 3 .   ? 13.500  11.616  33.053  1.00 21.09 ?  770 HOH B O   1 
HETATM 6809 O O   . HOH F 3 .   ? -7.254  -29.641 14.245  1.00 32.20 ?  771 HOH B O   1 
HETATM 6810 O O   . HOH F 3 .   ? 0.003   7.564   34.997  1.00 33.72 ?  772 HOH B O   1 
HETATM 6811 O O   . HOH F 3 .   ? 19.902  -18.987 11.978  1.00 37.55 ?  773 HOH B O   1 
HETATM 6812 O O   . HOH F 3 .   ? 25.614  -14.554 35.446  1.00 32.66 ?  774 HOH B O   1 
HETATM 6813 O O   . HOH F 3 .   ? -11.679 2.626   12.136  1.00 27.70 ?  775 HOH B O   1 
HETATM 6814 O O   . HOH F 3 .   ? -5.306  -27.268 4.514   1.00 37.63 ?  776 HOH B O   1 
HETATM 6815 O O   . HOH F 3 .   ? -0.000  -3.328  0.000   0.50 34.99 ?  777 HOH B O   1 
HETATM 6816 O O   . HOH F 3 .   ? 17.366  -10.688 -1.785  1.00 33.13 ?  778 HOH B O   1 
HETATM 6817 O O   . HOH F 3 .   ? 17.774  0.231   12.282  1.00 34.22 ?  779 HOH B O   1 
HETATM 6818 O O   . HOH F 3 .   ? -5.510  2.352   31.528  1.00 36.37 ?  780 HOH B O   1 
HETATM 6819 O O   . HOH F 3 .   ? -18.007 -21.236 6.832   1.00 27.02 ?  781 HOH B O   1 
HETATM 6820 O O   . HOH F 3 .   ? -17.859 -25.889 7.463   1.00 38.22 ?  782 HOH B O   1 
HETATM 6821 O O   . HOH F 3 .   ? -5.360  9.754   46.090  1.00 40.90 ?  783 HOH B O   1 
HETATM 6822 O O   . HOH F 3 .   ? -0.000  -11.168 0.000   0.50 34.03 ?  784 HOH B O   1 
HETATM 6823 O O   . HOH F 3 .   ? -14.948 -18.647 56.323  1.00 29.58 ?  785 HOH B O   1 
HETATM 6824 O O   . HOH F 3 .   ? -10.964 0.958   10.370  1.00 21.26 ?  786 HOH B O   1 
HETATM 6825 O O   . HOH F 3 .   ? 4.688   -0.576  19.300  1.00 32.83 ?  787 HOH B O   1 
HETATM 6826 O O   . HOH F 3 .   ? -0.000  -9.118  0.000   0.50 26.81 ?  788 HOH B O   1 
HETATM 6827 O O   . HOH F 3 .   ? -12.291 2.944   24.684  1.00 31.99 ?  789 HOH B O   1 
HETATM 6828 O O   . HOH F 3 .   ? -2.510  -18.968 39.667  1.00 21.61 ?  790 HOH B O   1 
HETATM 6829 O O   . HOH F 3 .   ? 3.978   -28.342 22.478  1.00 33.31 ?  791 HOH B O   1 
HETATM 6830 O O   . HOH F 3 .   ? -8.523  3.431   50.313  1.00 27.91 ?  792 HOH B O   1 
HETATM 6831 O O   . HOH F 3 .   ? -2.085  -0.594  29.402  1.00 25.70 ?  793 HOH B O   1 
HETATM 6832 O O   . HOH F 3 .   ? 15.887  -28.907 16.306  1.00 39.47 ?  794 HOH B O   1 
HETATM 6833 O O   . HOH F 3 .   ? -18.748 -5.298  18.610  1.00 35.05 ?  795 HOH B O   1 
HETATM 6834 O O   . HOH F 3 .   ? -8.661  -22.121 32.659  1.00 34.74 ?  796 HOH B O   1 
HETATM 6835 O O   . HOH F 3 .   ? 7.622   -29.574 19.353  1.00 35.03 ?  797 HOH B O   1 
HETATM 6836 O O   . HOH F 3 .   ? 22.051  -3.826  40.107  1.00 38.48 ?  798 HOH B O   1 
HETATM 6837 O O   . HOH F 3 .   ? -5.567  -3.807  54.660  1.00 37.35 ?  799 HOH B O   1 
HETATM 6838 O O   . HOH F 3 .   ? -1.527  -25.063 40.153  1.00 39.64 ?  800 HOH B O   1 
HETATM 6839 O O   . HOH F 3 .   ? 20.413  -9.574  11.185  1.00 29.87 ?  801 HOH B O   1 
HETATM 6840 O O   . HOH F 3 .   ? -7.865  -7.860  55.487  1.00 37.72 ?  802 HOH B O   1 
HETATM 6841 O O   . HOH F 3 .   ? 2.459   0.160   24.947  1.00 37.58 ?  803 HOH B O   1 
HETATM 6842 O O   . HOH F 3 .   ? 26.718  -11.780 28.915  1.00 26.75 ?  804 HOH B O   1 
HETATM 6843 O O   . HOH F 3 .   ? 13.452  -4.096  1.421   1.00 28.28 ?  805 HOH B O   1 
HETATM 6844 O O   . HOH F 3 .   ? 25.763  -13.094 25.360  1.00 26.19 ?  806 HOH B O   1 
HETATM 6845 O O   . HOH F 3 .   ? 22.191  -20.177 13.748  1.00 37.43 ?  807 HOH B O   1 
HETATM 6846 O O   . HOH F 3 .   ? 15.197  -17.078 1.386   1.00 30.92 ?  808 HOH B O   1 
HETATM 6847 O O   . HOH F 3 .   ? 7.776   -23.177 37.488  1.00 24.40 ?  809 HOH B O   1 
HETATM 6848 O O   . HOH F 3 .   ? 5.693   -12.724 48.363  1.00 25.32 ?  810 HOH B O   1 
HETATM 6849 O O   . HOH F 3 .   ? 29.390  -12.509 32.507  1.00 36.66 ?  811 HOH B O   1 
HETATM 6850 O O   . HOH F 3 .   ? 23.826  -8.183  10.227  1.00 36.71 ?  812 HOH B O   1 
HETATM 6851 O O   . HOH F 3 .   ? 26.431  -15.687 24.407  1.00 28.62 ?  813 HOH B O   1 
HETATM 6852 O O   . HOH F 3 .   ? 2.955   1.500   47.092  1.00 35.24 ?  814 HOH B O   1 
HETATM 6853 O O   . HOH F 3 .   ? 9.384   -25.284 37.892  1.00 37.39 ?  815 HOH B O   1 
HETATM 6854 O O   . HOH F 3 .   ? 5.237   6.745   44.303  1.00 34.86 ?  816 HOH B O   1 
HETATM 6855 O O   . HOH F 3 .   ? 5.700   1.323   46.404  1.00 31.04 ?  817 HOH B O   1 
# 
