data_8RM2
# 
_entry.id   8RM2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   8RM2         pdb_00008rm2 10.2210/pdb8rm2/pdb 
WWPDB D_1292135734 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_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                        8RM2 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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                 3 
_pdbx_contact_author.email              oded.livnah@mail.huji.ac.il 
_pdbx_contact_author.name_first         Oded 
_pdbx_contact_author.name_last          Livnah 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8682-2106 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Livnah, O.' 1 ? 
'Gutman, D.' 2 ? 
# 
_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                     'Erk2 MAP kinase T188E mutant' 
_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 'Livnah, O.' 1 ? 
primary 'Gutman, D.' 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 'Mitogen-activated protein kinase 1' 42258.520 1   2.7.11.24 ? ? ? 
2 non-polymer syn 'SULFATE ION'                        96.063    2   ?         ? ? ? 
3 water       nat water                                18.015    152 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;MAP kinase 1,MAPK 1,ERT1,Extracellular signal-regulated kinase 2,ERK-2,MAP kinase isoform p42,p42-MAPK,Mitogen-activated protein kinase 2,MAP kinase 2,MAPK 2
;
# 
_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       
;AHHHHHHMAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKIL
LRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNL
LLNTTCDLKICDFGLARVADPDHDHTGFLTEYVAERWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLD
QLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQ
YYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AHHHHHHMAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKIL
LRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNL
LLNTTCDLKICDFGLARVADPDHDHTGFLTEYVAERWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLD
QLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQ
YYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   MET n 
1 9   ALA n 
1 10  ALA n 
1 11  ALA n 
1 12  ALA n 
1 13  ALA n 
1 14  ALA n 
1 15  GLY n 
1 16  PRO n 
1 17  GLU n 
1 18  MET n 
1 19  VAL n 
1 20  ARG n 
1 21  GLY n 
1 22  GLN n 
1 23  VAL n 
1 24  PHE n 
1 25  ASP n 
1 26  VAL n 
1 27  GLY n 
1 28  PRO n 
1 29  ARG n 
1 30  TYR n 
1 31  THR n 
1 32  ASN n 
1 33  LEU n 
1 34  SER n 
1 35  TYR n 
1 36  ILE n 
1 37  GLY n 
1 38  GLU n 
1 39  GLY n 
1 40  ALA n 
1 41  TYR n 
1 42  GLY n 
1 43  MET n 
1 44  VAL n 
1 45  CYS n 
1 46  SER n 
1 47  ALA n 
1 48  TYR n 
1 49  ASP n 
1 50  ASN n 
1 51  LEU n 
1 52  ASN n 
1 53  LYS n 
1 54  VAL n 
1 55  ARG n 
1 56  VAL n 
1 57  ALA n 
1 58  ILE n 
1 59  LYS n 
1 60  LYS n 
1 61  ILE n 
1 62  SER n 
1 63  PRO n 
1 64  PHE n 
1 65  GLU n 
1 66  HIS n 
1 67  GLN n 
1 68  THR n 
1 69  TYR n 
1 70  CYS n 
1 71  GLN n 
1 72  ARG n 
1 73  THR n 
1 74  LEU n 
1 75  ARG n 
1 76  GLU n 
1 77  ILE n 
1 78  LYS n 
1 79  ILE n 
1 80  LEU n 
1 81  LEU n 
1 82  ARG n 
1 83  PHE n 
1 84  ARG n 
1 85  HIS n 
1 86  GLU n 
1 87  ASN n 
1 88  ILE n 
1 89  ILE n 
1 90  GLY n 
1 91  ILE n 
1 92  ASN n 
1 93  ASP n 
1 94  ILE n 
1 95  ILE n 
1 96  ARG n 
1 97  ALA n 
1 98  PRO n 
1 99  THR n 
1 100 ILE n 
1 101 GLU n 
1 102 GLN n 
1 103 MET n 
1 104 LYS n 
1 105 ASP n 
1 106 VAL n 
1 107 TYR n 
1 108 ILE n 
1 109 VAL n 
1 110 GLN n 
1 111 ASP n 
1 112 LEU n 
1 113 MET n 
1 114 GLU n 
1 115 THR n 
1 116 ASP n 
1 117 LEU n 
1 118 TYR n 
1 119 LYS n 
1 120 LEU n 
1 121 LEU n 
1 122 LYS n 
1 123 THR n 
1 124 GLN n 
1 125 HIS n 
1 126 LEU n 
1 127 SER n 
1 128 ASN n 
1 129 ASP n 
1 130 HIS n 
1 131 ILE n 
1 132 CYS n 
1 133 TYR n 
1 134 PHE n 
1 135 LEU n 
1 136 TYR n 
1 137 GLN n 
1 138 ILE n 
1 139 LEU n 
1 140 ARG n 
1 141 GLY n 
1 142 LEU n 
1 143 LYS n 
1 144 TYR n 
1 145 ILE n 
1 146 HIS n 
1 147 SER n 
1 148 ALA n 
1 149 ASN n 
1 150 VAL n 
1 151 LEU n 
1 152 HIS n 
1 153 ARG n 
1 154 ASP n 
1 155 LEU n 
1 156 LYS n 
1 157 PRO n 
1 158 SER n 
1 159 ASN n 
1 160 LEU n 
1 161 LEU n 
1 162 LEU n 
1 163 ASN n 
1 164 THR n 
1 165 THR n 
1 166 CYS n 
1 167 ASP n 
1 168 LEU n 
1 169 LYS n 
1 170 ILE n 
1 171 CYS n 
1 172 ASP n 
1 173 PHE n 
1 174 GLY n 
1 175 LEU n 
1 176 ALA n 
1 177 ARG n 
1 178 VAL n 
1 179 ALA n 
1 180 ASP n 
1 181 PRO n 
1 182 ASP n 
1 183 HIS n 
1 184 ASP n 
1 185 HIS n 
1 186 THR n 
1 187 GLY n 
1 188 PHE n 
1 189 LEU n 
1 190 THR n 
1 191 GLU n 
1 192 TYR n 
1 193 VAL n 
1 194 ALA n 
1 195 GLU n 
1 196 ARG n 
1 197 TRP n 
1 198 TYR n 
1 199 ARG n 
1 200 ALA n 
1 201 PRO n 
1 202 GLU n 
1 203 ILE n 
1 204 MET n 
1 205 LEU n 
1 206 ASN n 
1 207 SER n 
1 208 LYS n 
1 209 GLY n 
1 210 TYR n 
1 211 THR n 
1 212 LYS n 
1 213 SER n 
1 214 ILE n 
1 215 ASP n 
1 216 ILE n 
1 217 TRP n 
1 218 SER n 
1 219 VAL n 
1 220 GLY n 
1 221 CYS n 
1 222 ILE n 
1 223 LEU n 
1 224 ALA n 
1 225 GLU n 
1 226 MET n 
1 227 LEU n 
1 228 SER n 
1 229 ASN n 
1 230 ARG n 
1 231 PRO n 
1 232 ILE n 
1 233 PHE n 
1 234 PRO n 
1 235 GLY n 
1 236 LYS n 
1 237 HIS n 
1 238 TYR n 
1 239 LEU n 
1 240 ASP n 
1 241 GLN n 
1 242 LEU n 
1 243 ASN n 
1 244 HIS n 
1 245 ILE n 
1 246 LEU n 
1 247 GLY n 
1 248 ILE n 
1 249 LEU n 
1 250 GLY n 
1 251 SER n 
1 252 PRO n 
1 253 SER n 
1 254 GLN n 
1 255 GLU n 
1 256 ASP n 
1 257 LEU n 
1 258 ASN n 
1 259 CYS n 
1 260 ILE n 
1 261 ILE n 
1 262 ASN n 
1 263 LEU n 
1 264 LYS n 
1 265 ALA n 
1 266 ARG n 
1 267 ASN n 
1 268 TYR n 
1 269 LEU n 
1 270 LEU n 
1 271 SER n 
1 272 LEU n 
1 273 PRO n 
1 274 HIS n 
1 275 LYS n 
1 276 ASN n 
1 277 LYS n 
1 278 VAL n 
1 279 PRO n 
1 280 TRP n 
1 281 ASN n 
1 282 ARG n 
1 283 LEU n 
1 284 PHE n 
1 285 PRO n 
1 286 ASN n 
1 287 ALA n 
1 288 ASP n 
1 289 SER n 
1 290 LYS n 
1 291 ALA n 
1 292 LEU n 
1 293 ASP n 
1 294 LEU n 
1 295 LEU n 
1 296 ASP n 
1 297 LYS n 
1 298 MET n 
1 299 LEU n 
1 300 THR n 
1 301 PHE n 
1 302 ASN n 
1 303 PRO n 
1 304 HIS n 
1 305 LYS n 
1 306 ARG n 
1 307 ILE n 
1 308 GLU n 
1 309 VAL n 
1 310 GLU n 
1 311 GLN n 
1 312 ALA n 
1 313 LEU n 
1 314 ALA n 
1 315 HIS n 
1 316 PRO n 
1 317 TYR n 
1 318 LEU n 
1 319 GLU n 
1 320 GLN n 
1 321 TYR n 
1 322 TYR n 
1 323 ASP n 
1 324 PRO n 
1 325 SER n 
1 326 ASP n 
1 327 GLU n 
1 328 PRO n 
1 329 ILE n 
1 330 ALA n 
1 331 GLU n 
1 332 ALA n 
1 333 PRO n 
1 334 PHE n 
1 335 LYS n 
1 336 PHE n 
1 337 ASP n 
1 338 MET n 
1 339 GLU n 
1 340 LEU n 
1 341 ASP n 
1 342 ASP n 
1 343 LEU n 
1 344 PRO n 
1 345 LYS n 
1 346 GLU n 
1 347 LYS n 
1 348 LEU n 
1 349 LYS n 
1 350 GLU n 
1 351 LEU n 
1 352 ILE n 
1 353 PHE n 
1 354 GLU n 
1 355 GLU n 
1 356 THR n 
1 357 ALA n 
1 358 ARG n 
1 359 PHE n 
1 360 GLN n 
1 361 PRO n 
1 362 GLY n 
1 363 TYR n 
1 364 ARG n 
1 365 SER 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                   365 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Mapk1, Erk2, Mapk, Prkm1' 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
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   ALA 1   -6  ?   ?   ?   A . n 
A 1 2   HIS 2   -5  ?   ?   ?   A . n 
A 1 3   HIS 3   -4  ?   ?   ?   A . n 
A 1 4   HIS 4   -3  ?   ?   ?   A . n 
A 1 5   HIS 5   -2  ?   ?   ?   A . n 
A 1 6   HIS 6   -1  ?   ?   ?   A . n 
A 1 7   HIS 7   0   ?   ?   ?   A . n 
A 1 8   MET 8   1   ?   ?   ?   A . n 
A 1 9   ALA 9   2   ?   ?   ?   A . n 
A 1 10  ALA 10  3   ?   ?   ?   A . n 
A 1 11  ALA 11  4   4   ALA ALA A . n 
A 1 12  ALA 12  5   5   ALA ALA A . n 
A 1 13  ALA 13  6   6   ALA ALA A . n 
A 1 14  ALA 14  7   7   ALA ALA A . n 
A 1 15  GLY 15  8   8   GLY GLY A . n 
A 1 16  PRO 16  9   9   PRO PRO A . n 
A 1 17  GLU 17  10  ?   ?   ?   A . n 
A 1 18  MET 18  11  ?   ?   ?   A . n 
A 1 19  VAL 19  12  ?   ?   ?   A . n 
A 1 20  ARG 20  13  ?   ?   ?   A . n 
A 1 21  GLY 21  14  ?   ?   ?   A . n 
A 1 22  GLN 22  15  15  GLN GLN A . n 
A 1 23  VAL 23  16  16  VAL VAL A . n 
A 1 24  PHE 24  17  17  PHE PHE A . n 
A 1 25  ASP 25  18  18  ASP ASP A . n 
A 1 26  VAL 26  19  19  VAL VAL A . n 
A 1 27  GLY 27  20  20  GLY GLY A . n 
A 1 28  PRO 28  21  21  PRO PRO A . n 
A 1 29  ARG 29  22  22  ARG ARG A . n 
A 1 30  TYR 30  23  23  TYR TYR A . n 
A 1 31  THR 31  24  24  THR THR A . n 
A 1 32  ASN 32  25  25  ASN ASN A . n 
A 1 33  LEU 33  26  26  LEU LEU A . n 
A 1 34  SER 34  27  27  SER SER A . n 
A 1 35  TYR 35  28  28  TYR TYR A . n 
A 1 36  ILE 36  29  29  ILE ILE A . n 
A 1 37  GLY 37  30  30  GLY GLY A . n 
A 1 38  GLU 38  31  31  GLU GLU A . n 
A 1 39  GLY 39  32  32  GLY GLY A . n 
A 1 40  ALA 40  33  33  ALA ALA A . n 
A 1 41  TYR 41  34  34  TYR TYR A . n 
A 1 42  GLY 42  35  35  GLY GLY A . n 
A 1 43  MET 43  36  36  MET MET A . n 
A 1 44  VAL 44  37  37  VAL VAL A . n 
A 1 45  CYS 45  38  38  CYS CYS A . n 
A 1 46  SER 46  39  39  SER SER A . n 
A 1 47  ALA 47  40  40  ALA ALA A . n 
A 1 48  TYR 48  41  41  TYR TYR A . n 
A 1 49  ASP 49  42  42  ASP ASP A . n 
A 1 50  ASN 50  43  43  ASN ASN A . n 
A 1 51  LEU 51  44  44  LEU LEU A . n 
A 1 52  ASN 52  45  45  ASN ASN A . n 
A 1 53  LYS 53  46  46  LYS LYS A . n 
A 1 54  VAL 54  47  47  VAL VAL A . n 
A 1 55  ARG 55  48  48  ARG ARG A . n 
A 1 56  VAL 56  49  49  VAL VAL A . n 
A 1 57  ALA 57  50  50  ALA ALA A . n 
A 1 58  ILE 58  51  51  ILE ILE A . n 
A 1 59  LYS 59  52  52  LYS LYS A . n 
A 1 60  LYS 60  53  53  LYS LYS A . n 
A 1 61  ILE 61  54  54  ILE ILE A . n 
A 1 62  SER 62  55  55  SER SER A . n 
A 1 63  PRO 63  56  56  PRO PRO A . n 
A 1 64  PHE 64  57  57  PHE PHE A . n 
A 1 65  GLU 65  58  58  GLU GLU A . n 
A 1 66  HIS 66  59  59  HIS HIS A . n 
A 1 67  GLN 67  60  60  GLN GLN A . n 
A 1 68  THR 68  61  61  THR THR A . n 
A 1 69  TYR 69  62  62  TYR TYR A . n 
A 1 70  CYS 70  63  63  CYS CYS A . n 
A 1 71  GLN 71  64  64  GLN GLN A . n 
A 1 72  ARG 72  65  65  ARG ARG A . n 
A 1 73  THR 73  66  66  THR THR A . n 
A 1 74  LEU 74  67  67  LEU LEU A . n 
A 1 75  ARG 75  68  68  ARG ARG A . n 
A 1 76  GLU 76  69  69  GLU GLU A . n 
A 1 77  ILE 77  70  70  ILE ILE A . n 
A 1 78  LYS 78  71  71  LYS LYS A . n 
A 1 79  ILE 79  72  72  ILE ILE A . n 
A 1 80  LEU 80  73  73  LEU LEU A . n 
A 1 81  LEU 81  74  74  LEU LEU A . n 
A 1 82  ARG 82  75  75  ARG ARG A . n 
A 1 83  PHE 83  76  76  PHE PHE A . n 
A 1 84  ARG 84  77  77  ARG ARG A . n 
A 1 85  HIS 85  78  78  HIS HIS A . n 
A 1 86  GLU 86  79  79  GLU GLU A . n 
A 1 87  ASN 87  80  80  ASN ASN A . n 
A 1 88  ILE 88  81  81  ILE ILE A . n 
A 1 89  ILE 89  82  82  ILE ILE A . n 
A 1 90  GLY 90  83  83  GLY GLY A . n 
A 1 91  ILE 91  84  84  ILE ILE A . n 
A 1 92  ASN 92  85  85  ASN ASN A . n 
A 1 93  ASP 93  86  86  ASP ASP A . n 
A 1 94  ILE 94  87  87  ILE ILE A . n 
A 1 95  ILE 95  88  88  ILE ILE A . n 
A 1 96  ARG 96  89  89  ARG ARG A . n 
A 1 97  ALA 97  90  90  ALA ALA A . n 
A 1 98  PRO 98  91  91  PRO PRO A . n 
A 1 99  THR 99  92  92  THR THR A . n 
A 1 100 ILE 100 93  93  ILE ILE A . n 
A 1 101 GLU 101 94  94  GLU GLU A . n 
A 1 102 GLN 102 95  95  GLN GLN A . n 
A 1 103 MET 103 96  96  MET MET A . n 
A 1 104 LYS 104 97  97  LYS LYS A . n 
A 1 105 ASP 105 98  98  ASP ASP A . n 
A 1 106 VAL 106 99  99  VAL VAL A . n 
A 1 107 TYR 107 100 100 TYR TYR A . n 
A 1 108 ILE 108 101 101 ILE ILE A . n 
A 1 109 VAL 109 102 102 VAL VAL A . n 
A 1 110 GLN 110 103 103 GLN GLN A . n 
A 1 111 ASP 111 104 104 ASP ASP A . n 
A 1 112 LEU 112 105 105 LEU LEU A . n 
A 1 113 MET 113 106 106 MET MET A . n 
A 1 114 GLU 114 107 107 GLU GLU A . n 
A 1 115 THR 115 108 108 THR THR A . n 
A 1 116 ASP 116 109 109 ASP ASP A . n 
A 1 117 LEU 117 110 110 LEU LEU A . n 
A 1 118 TYR 118 111 111 TYR TYR A . n 
A 1 119 LYS 119 112 112 LYS LYS A . n 
A 1 120 LEU 120 113 113 LEU LEU A . n 
A 1 121 LEU 121 114 114 LEU LEU A . n 
A 1 122 LYS 122 115 115 LYS LYS A . n 
A 1 123 THR 123 116 116 THR THR A . n 
A 1 124 GLN 124 117 117 GLN GLN A . n 
A 1 125 HIS 125 118 118 HIS HIS A . n 
A 1 126 LEU 126 119 119 LEU LEU A . n 
A 1 127 SER 127 120 120 SER SER A . n 
A 1 128 ASN 128 121 121 ASN ASN A . n 
A 1 129 ASP 129 122 122 ASP ASP A . n 
A 1 130 HIS 130 123 123 HIS HIS A . n 
A 1 131 ILE 131 124 124 ILE ILE A . n 
A 1 132 CYS 132 125 125 CYS CYS A . n 
A 1 133 TYR 133 126 126 TYR TYR A . n 
A 1 134 PHE 134 127 127 PHE PHE A . n 
A 1 135 LEU 135 128 128 LEU LEU A . n 
A 1 136 TYR 136 129 129 TYR TYR A . n 
A 1 137 GLN 137 130 130 GLN GLN A . n 
A 1 138 ILE 138 131 131 ILE ILE A . n 
A 1 139 LEU 139 132 132 LEU LEU A . n 
A 1 140 ARG 140 133 133 ARG ARG A . n 
A 1 141 GLY 141 134 134 GLY GLY A . n 
A 1 142 LEU 142 135 135 LEU LEU A . n 
A 1 143 LYS 143 136 136 LYS LYS A . n 
A 1 144 TYR 144 137 137 TYR TYR A . n 
A 1 145 ILE 145 138 138 ILE ILE A . n 
A 1 146 HIS 146 139 139 HIS HIS A . n 
A 1 147 SER 147 140 140 SER SER A . n 
A 1 148 ALA 148 141 141 ALA ALA A . n 
A 1 149 ASN 149 142 142 ASN ASN A . n 
A 1 150 VAL 150 143 143 VAL VAL A . n 
A 1 151 LEU 151 144 144 LEU LEU A . n 
A 1 152 HIS 152 145 145 HIS HIS A . n 
A 1 153 ARG 153 146 146 ARG ARG A . n 
A 1 154 ASP 154 147 147 ASP ASP A . n 
A 1 155 LEU 155 148 148 LEU LEU A . n 
A 1 156 LYS 156 149 149 LYS LYS A . n 
A 1 157 PRO 157 150 150 PRO PRO A . n 
A 1 158 SER 158 151 151 SER SER A . n 
A 1 159 ASN 159 152 152 ASN ASN A . n 
A 1 160 LEU 160 153 153 LEU LEU A . n 
A 1 161 LEU 161 154 154 LEU LEU A . n 
A 1 162 LEU 162 155 155 LEU LEU A . n 
A 1 163 ASN 163 156 156 ASN ASN A . n 
A 1 164 THR 164 157 157 THR THR A . n 
A 1 165 THR 165 158 158 THR THR A . n 
A 1 166 CYS 166 159 159 CYS CYS A . n 
A 1 167 ASP 167 160 160 ASP ASP A . n 
A 1 168 LEU 168 161 161 LEU LEU A . n 
A 1 169 LYS 169 162 162 LYS LYS A . n 
A 1 170 ILE 170 163 163 ILE ILE A . n 
A 1 171 CYS 171 164 164 CYS CYS A . n 
A 1 172 ASP 172 165 165 ASP ASP A . n 
A 1 173 PHE 173 166 166 PHE PHE A . n 
A 1 174 GLY 174 167 167 GLY GLY A . n 
A 1 175 LEU 175 168 168 LEU LEU A . n 
A 1 176 ALA 176 169 169 ALA ALA A . n 
A 1 177 ARG 177 170 170 ARG ARG A . n 
A 1 178 VAL 178 171 171 VAL VAL A . n 
A 1 179 ALA 179 172 172 ALA ALA A . n 
A 1 180 ASP 180 173 173 ASP ASP A . n 
A 1 181 PRO 181 174 174 PRO PRO A . n 
A 1 182 ASP 182 175 175 ASP ASP A . n 
A 1 183 HIS 183 176 176 HIS HIS A . n 
A 1 184 ASP 184 177 177 ASP ASP A . n 
A 1 185 HIS 185 178 178 HIS HIS A . n 
A 1 186 THR 186 179 179 THR THR A . n 
A 1 187 GLY 187 180 180 GLY GLY A . n 
A 1 188 PHE 188 181 181 PHE PHE A . n 
A 1 189 LEU 189 182 182 LEU LEU A . n 
A 1 190 THR 190 183 183 THR THR A . n 
A 1 191 GLU 191 184 184 GLU GLU A . n 
A 1 192 TYR 192 185 185 TYR TYR A . n 
A 1 193 VAL 193 186 186 VAL VAL A . n 
A 1 194 ALA 194 187 187 ALA ALA A . n 
A 1 195 GLU 195 188 188 GLU GLU A . n 
A 1 196 ARG 196 189 189 ARG ARG A . n 
A 1 197 TRP 197 190 190 TRP TRP A . n 
A 1 198 TYR 198 191 191 TYR TYR A . n 
A 1 199 ARG 199 192 192 ARG ARG A . n 
A 1 200 ALA 200 193 193 ALA ALA A . n 
A 1 201 PRO 201 194 194 PRO PRO A . n 
A 1 202 GLU 202 195 195 GLU GLU A . n 
A 1 203 ILE 203 196 196 ILE ILE A . n 
A 1 204 MET 204 197 197 MET MET A . n 
A 1 205 LEU 205 198 198 LEU LEU A . n 
A 1 206 ASN 206 199 199 ASN ASN A . n 
A 1 207 SER 207 200 200 SER SER A . n 
A 1 208 LYS 208 201 201 LYS LYS A . n 
A 1 209 GLY 209 202 202 GLY GLY A . n 
A 1 210 TYR 210 203 203 TYR TYR A . n 
A 1 211 THR 211 204 204 THR THR A . n 
A 1 212 LYS 212 205 205 LYS LYS A . n 
A 1 213 SER 213 206 206 SER SER A . n 
A 1 214 ILE 214 207 207 ILE ILE A . n 
A 1 215 ASP 215 208 208 ASP ASP A . n 
A 1 216 ILE 216 209 209 ILE ILE A . n 
A 1 217 TRP 217 210 210 TRP TRP A . n 
A 1 218 SER 218 211 211 SER SER A . n 
A 1 219 VAL 219 212 212 VAL VAL A . n 
A 1 220 GLY 220 213 213 GLY GLY A . n 
A 1 221 CYS 221 214 214 CYS CYS A . n 
A 1 222 ILE 222 215 215 ILE ILE A . n 
A 1 223 LEU 223 216 216 LEU LEU A . n 
A 1 224 ALA 224 217 217 ALA ALA A . n 
A 1 225 GLU 225 218 218 GLU GLU A . n 
A 1 226 MET 226 219 219 MET MET A . n 
A 1 227 LEU 227 220 220 LEU LEU A . n 
A 1 228 SER 228 221 221 SER SER A . n 
A 1 229 ASN 229 222 222 ASN ASN A . n 
A 1 230 ARG 230 223 223 ARG ARG A . n 
A 1 231 PRO 231 224 224 PRO PRO A . n 
A 1 232 ILE 232 225 225 ILE ILE A . n 
A 1 233 PHE 233 226 226 PHE PHE A . n 
A 1 234 PRO 234 227 227 PRO PRO A . n 
A 1 235 GLY 235 228 228 GLY GLY A . n 
A 1 236 LYS 236 229 229 LYS LYS A . n 
A 1 237 HIS 237 230 230 HIS HIS A . n 
A 1 238 TYR 238 231 231 TYR TYR A . n 
A 1 239 LEU 239 232 232 LEU LEU A . n 
A 1 240 ASP 240 233 233 ASP ASP A . n 
A 1 241 GLN 241 234 234 GLN GLN A . n 
A 1 242 LEU 242 235 235 LEU LEU A . n 
A 1 243 ASN 243 236 236 ASN ASN A . n 
A 1 244 HIS 244 237 237 HIS HIS A . n 
A 1 245 ILE 245 238 238 ILE ILE A . n 
A 1 246 LEU 246 239 239 LEU LEU A . n 
A 1 247 GLY 247 240 240 GLY GLY A . n 
A 1 248 ILE 248 241 241 ILE ILE A . n 
A 1 249 LEU 249 242 242 LEU LEU A . n 
A 1 250 GLY 250 243 243 GLY GLY A . n 
A 1 251 SER 251 244 244 SER SER A . n 
A 1 252 PRO 252 245 245 PRO PRO A . n 
A 1 253 SER 253 246 246 SER SER A . n 
A 1 254 GLN 254 247 247 GLN GLN A . n 
A 1 255 GLU 255 248 248 GLU GLU A . n 
A 1 256 ASP 256 249 249 ASP ASP A . n 
A 1 257 LEU 257 250 250 LEU LEU A . n 
A 1 258 ASN 258 251 251 ASN ASN A . n 
A 1 259 CYS 259 252 252 CYS CYS A . n 
A 1 260 ILE 260 253 253 ILE ILE A . n 
A 1 261 ILE 261 254 254 ILE ILE A . n 
A 1 262 ASN 262 255 255 ASN ASN A . n 
A 1 263 LEU 263 256 256 LEU LEU A . n 
A 1 264 LYS 264 257 257 LYS LYS A . n 
A 1 265 ALA 265 258 258 ALA ALA A . n 
A 1 266 ARG 266 259 259 ARG ARG A . n 
A 1 267 ASN 267 260 260 ASN ASN A . n 
A 1 268 TYR 268 261 261 TYR TYR A . n 
A 1 269 LEU 269 262 262 LEU LEU A . n 
A 1 270 LEU 270 263 263 LEU LEU A . n 
A 1 271 SER 271 264 264 SER SER A . n 
A 1 272 LEU 272 265 265 LEU LEU A . n 
A 1 273 PRO 273 266 266 PRO PRO A . n 
A 1 274 HIS 274 267 267 HIS HIS A . n 
A 1 275 LYS 275 268 268 LYS LYS A . n 
A 1 276 ASN 276 269 269 ASN ASN A . n 
A 1 277 LYS 277 270 270 LYS LYS A . n 
A 1 278 VAL 278 271 271 VAL VAL A . n 
A 1 279 PRO 279 272 272 PRO PRO A . n 
A 1 280 TRP 280 273 273 TRP TRP A . n 
A 1 281 ASN 281 274 274 ASN ASN A . n 
A 1 282 ARG 282 275 275 ARG ARG A . n 
A 1 283 LEU 283 276 276 LEU LEU A . n 
A 1 284 PHE 284 277 277 PHE PHE A . n 
A 1 285 PRO 285 278 278 PRO PRO A . n 
A 1 286 ASN 286 279 279 ASN ASN A . n 
A 1 287 ALA 287 280 280 ALA ALA A . n 
A 1 288 ASP 288 281 281 ASP ASP A . n 
A 1 289 SER 289 282 282 SER SER A . n 
A 1 290 LYS 290 283 283 LYS LYS A . n 
A 1 291 ALA 291 284 284 ALA ALA A . n 
A 1 292 LEU 292 285 285 LEU LEU A . n 
A 1 293 ASP 293 286 286 ASP ASP A . n 
A 1 294 LEU 294 287 287 LEU LEU A . n 
A 1 295 LEU 295 288 288 LEU LEU A . n 
A 1 296 ASP 296 289 289 ASP ASP A . n 
A 1 297 LYS 297 290 290 LYS LYS A . n 
A 1 298 MET 298 291 291 MET MET A . n 
A 1 299 LEU 299 292 292 LEU LEU A . n 
A 1 300 THR 300 293 293 THR THR A . n 
A 1 301 PHE 301 294 294 PHE PHE A . n 
A 1 302 ASN 302 295 295 ASN ASN A . n 
A 1 303 PRO 303 296 296 PRO PRO A . n 
A 1 304 HIS 304 297 297 HIS HIS A . n 
A 1 305 LYS 305 298 298 LYS LYS A . n 
A 1 306 ARG 306 299 299 ARG ARG A . n 
A 1 307 ILE 307 300 300 ILE ILE A . n 
A 1 308 GLU 308 301 301 GLU GLU A . n 
A 1 309 VAL 309 302 302 VAL VAL A . n 
A 1 310 GLU 310 303 303 GLU GLU A . n 
A 1 311 GLN 311 304 304 GLN GLN A . n 
A 1 312 ALA 312 305 305 ALA ALA A . n 
A 1 313 LEU 313 306 306 LEU LEU A . n 
A 1 314 ALA 314 307 307 ALA ALA A . n 
A 1 315 HIS 315 308 308 HIS HIS A . n 
A 1 316 PRO 316 309 309 PRO PRO A . n 
A 1 317 TYR 317 310 310 TYR TYR A . n 
A 1 318 LEU 318 311 311 LEU LEU A . n 
A 1 319 GLU 319 312 312 GLU GLU A . n 
A 1 320 GLN 320 313 313 GLN GLN A . n 
A 1 321 TYR 321 314 314 TYR TYR A . n 
A 1 322 TYR 322 315 315 TYR TYR A . n 
A 1 323 ASP 323 316 316 ASP ASP A . n 
A 1 324 PRO 324 317 317 PRO PRO A . n 
A 1 325 SER 325 318 318 SER SER A . n 
A 1 326 ASP 326 319 319 ASP ASP A . n 
A 1 327 GLU 327 320 320 GLU GLU A . n 
A 1 328 PRO 328 321 321 PRO PRO A . n 
A 1 329 ILE 329 322 322 ILE ILE A . n 
A 1 330 ALA 330 323 323 ALA ALA A . n 
A 1 331 GLU 331 324 324 GLU GLU A . n 
A 1 332 ALA 332 325 325 ALA ALA A . n 
A 1 333 PRO 333 326 326 PRO PRO A . n 
A 1 334 PHE 334 327 327 PHE PHE A . n 
A 1 335 LYS 335 328 328 LYS LYS A . n 
A 1 336 PHE 336 329 329 PHE PHE A . n 
A 1 337 ASP 337 330 330 ASP ASP A . n 
A 1 338 MET 338 331 331 MET MET A . n 
A 1 339 GLU 339 332 332 GLU GLU A . n 
A 1 340 LEU 340 333 333 LEU LEU A . n 
A 1 341 ASP 341 334 334 ASP ASP A . n 
A 1 342 ASP 342 335 335 ASP ASP A . n 
A 1 343 LEU 343 336 336 LEU LEU A . n 
A 1 344 PRO 344 337 337 PRO PRO A . n 
A 1 345 LYS 345 338 338 LYS LYS A . n 
A 1 346 GLU 346 339 339 GLU GLU A . n 
A 1 347 LYS 347 340 340 LYS LYS A . n 
A 1 348 LEU 348 341 341 LEU LEU A . n 
A 1 349 LYS 349 342 342 LYS LYS A . n 
A 1 350 GLU 350 343 343 GLU GLU A . n 
A 1 351 LEU 351 344 344 LEU LEU A . n 
A 1 352 ILE 352 345 345 ILE ILE A . n 
A 1 353 PHE 353 346 346 PHE PHE A . n 
A 1 354 GLU 354 347 347 GLU GLU A . n 
A 1 355 GLU 355 348 348 GLU GLU A . n 
A 1 356 THR 356 349 349 THR THR A . n 
A 1 357 ALA 357 350 350 ALA ALA A . n 
A 1 358 ARG 358 351 351 ARG ARG A . n 
A 1 359 PHE 359 352 352 PHE PHE A . n 
A 1 360 GLN 360 353 353 GLN GLN A . n 
A 1 361 PRO 361 354 354 PRO PRO A . n 
A 1 362 GLY 362 355 355 GLY GLY A . n 
A 1 363 TYR 363 356 ?   ?   ?   A . n 
A 1 364 ARG 364 357 ?   ?   ?   A . n 
A 1 365 SER 365 358 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SO4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SO4 
_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 
B 2 SO4 1   401 401 SO4 SO4 A . 
C 2 SO4 1   402 403 SO4 SO4 A . 
D 3 HOH 1   501 127 HOH HOH A . 
D 3 HOH 2   502 37  HOH HOH A . 
D 3 HOH 3   503 88  HOH HOH A . 
D 3 HOH 4   504 96  HOH HOH A . 
D 3 HOH 5   505 78  HOH HOH A . 
D 3 HOH 6   506 148 HOH HOH A . 
D 3 HOH 7   507 70  HOH HOH A . 
D 3 HOH 8   508 132 HOH HOH A . 
D 3 HOH 9   509 111 HOH HOH A . 
D 3 HOH 10  510 145 HOH HOH A . 
D 3 HOH 11  511 24  HOH HOH A . 
D 3 HOH 12  512 46  HOH HOH A . 
D 3 HOH 13  513 52  HOH HOH A . 
D 3 HOH 14  514 20  HOH HOH A . 
D 3 HOH 15  515 91  HOH HOH A . 
D 3 HOH 16  516 137 HOH HOH A . 
D 3 HOH 17  517 51  HOH HOH A . 
D 3 HOH 18  518 92  HOH HOH A . 
D 3 HOH 19  519 124 HOH HOH A . 
D 3 HOH 20  520 40  HOH HOH A . 
D 3 HOH 21  521 12  HOH HOH A . 
D 3 HOH 22  522 71  HOH HOH A . 
D 3 HOH 23  523 130 HOH HOH A . 
D 3 HOH 24  524 101 HOH HOH A . 
D 3 HOH 25  525 134 HOH HOH A . 
D 3 HOH 26  526 158 HOH HOH A . 
D 3 HOH 27  527 116 HOH HOH A . 
D 3 HOH 28  528 75  HOH HOH A . 
D 3 HOH 29  529 32  HOH HOH A . 
D 3 HOH 30  530 3   HOH HOH A . 
D 3 HOH 31  531 21  HOH HOH A . 
D 3 HOH 32  532 112 HOH HOH A . 
D 3 HOH 33  533 28  HOH HOH A . 
D 3 HOH 34  534 67  HOH HOH A . 
D 3 HOH 35  535 87  HOH HOH A . 
D 3 HOH 36  536 44  HOH HOH A . 
D 3 HOH 37  537 57  HOH HOH A . 
D 3 HOH 38  538 105 HOH HOH A . 
D 3 HOH 39  539 13  HOH HOH A . 
D 3 HOH 40  540 35  HOH HOH A . 
D 3 HOH 41  541 82  HOH HOH A . 
D 3 HOH 42  542 43  HOH HOH A . 
D 3 HOH 43  543 72  HOH HOH A . 
D 3 HOH 44  544 33  HOH HOH A . 
D 3 HOH 45  545 22  HOH HOH A . 
D 3 HOH 46  546 74  HOH HOH A . 
D 3 HOH 47  547 95  HOH HOH A . 
D 3 HOH 48  548 89  HOH HOH A . 
D 3 HOH 49  549 110 HOH HOH A . 
D 3 HOH 50  550 27  HOH HOH A . 
D 3 HOH 51  551 8   HOH HOH A . 
D 3 HOH 52  552 41  HOH HOH A . 
D 3 HOH 53  553 31  HOH HOH A . 
D 3 HOH 54  554 99  HOH HOH A . 
D 3 HOH 55  555 18  HOH HOH A . 
D 3 HOH 56  556 6   HOH HOH A . 
D 3 HOH 57  557 80  HOH HOH A . 
D 3 HOH 58  558 5   HOH HOH A . 
D 3 HOH 59  559 58  HOH HOH A . 
D 3 HOH 60  560 2   HOH HOH A . 
D 3 HOH 61  561 150 HOH HOH A . 
D 3 HOH 62  562 19  HOH HOH A . 
D 3 HOH 63  563 11  HOH HOH A . 
D 3 HOH 64  564 129 HOH HOH A . 
D 3 HOH 65  565 139 HOH HOH A . 
D 3 HOH 66  566 62  HOH HOH A . 
D 3 HOH 67  567 159 HOH HOH A . 
D 3 HOH 68  568 126 HOH HOH A . 
D 3 HOH 69  569 38  HOH HOH A . 
D 3 HOH 70  570 36  HOH HOH A . 
D 3 HOH 71  571 61  HOH HOH A . 
D 3 HOH 72  572 86  HOH HOH A . 
D 3 HOH 73  573 30  HOH HOH A . 
D 3 HOH 74  574 151 HOH HOH A . 
D 3 HOH 75  575 108 HOH HOH A . 
D 3 HOH 76  576 136 HOH HOH A . 
D 3 HOH 77  577 77  HOH HOH A . 
D 3 HOH 78  578 9   HOH HOH A . 
D 3 HOH 79  579 118 HOH HOH A . 
D 3 HOH 80  580 133 HOH HOH A . 
D 3 HOH 81  581 59  HOH HOH A . 
D 3 HOH 82  582 17  HOH HOH A . 
D 3 HOH 83  583 7   HOH HOH A . 
D 3 HOH 84  584 143 HOH HOH A . 
D 3 HOH 85  585 55  HOH HOH A . 
D 3 HOH 86  586 120 HOH HOH A . 
D 3 HOH 87  587 25  HOH HOH A . 
D 3 HOH 88  588 42  HOH HOH A . 
D 3 HOH 89  589 73  HOH HOH A . 
D 3 HOH 90  590 109 HOH HOH A . 
D 3 HOH 91  591 23  HOH HOH A . 
D 3 HOH 92  592 123 HOH HOH A . 
D 3 HOH 93  593 1   HOH HOH A . 
D 3 HOH 94  594 100 HOH HOH A . 
D 3 HOH 95  595 4   HOH HOH A . 
D 3 HOH 96  596 161 HOH HOH A . 
D 3 HOH 97  597 29  HOH HOH A . 
D 3 HOH 98  598 117 HOH HOH A . 
D 3 HOH 99  599 15  HOH HOH A . 
D 3 HOH 100 600 45  HOH HOH A . 
D 3 HOH 101 601 14  HOH HOH A . 
D 3 HOH 102 602 66  HOH HOH A . 
D 3 HOH 103 603 49  HOH HOH A . 
D 3 HOH 104 604 79  HOH HOH A . 
D 3 HOH 105 605 39  HOH HOH A . 
D 3 HOH 106 606 138 HOH HOH A . 
D 3 HOH 107 607 10  HOH HOH A . 
D 3 HOH 108 608 107 HOH HOH A . 
D 3 HOH 109 609 104 HOH HOH A . 
D 3 HOH 110 610 98  HOH HOH A . 
D 3 HOH 111 611 121 HOH HOH A . 
D 3 HOH 112 612 16  HOH HOH A . 
D 3 HOH 113 613 122 HOH HOH A . 
D 3 HOH 114 614 141 HOH HOH A . 
D 3 HOH 115 615 76  HOH HOH A . 
D 3 HOH 116 616 47  HOH HOH A . 
D 3 HOH 117 617 65  HOH HOH A . 
D 3 HOH 118 618 26  HOH HOH A . 
D 3 HOH 119 619 90  HOH HOH A . 
D 3 HOH 120 620 50  HOH HOH A . 
D 3 HOH 121 621 144 HOH HOH A . 
D 3 HOH 122 622 115 HOH HOH A . 
D 3 HOH 123 623 113 HOH HOH A . 
D 3 HOH 124 624 102 HOH HOH A . 
D 3 HOH 125 625 94  HOH HOH A . 
D 3 HOH 126 626 157 HOH HOH A . 
D 3 HOH 127 627 103 HOH HOH A . 
D 3 HOH 128 628 163 HOH HOH A . 
D 3 HOH 129 629 34  HOH HOH A . 
D 3 HOH 130 630 97  HOH HOH A . 
D 3 HOH 131 631 69  HOH HOH A . 
D 3 HOH 132 632 93  HOH HOH A . 
D 3 HOH 133 633 53  HOH HOH A . 
D 3 HOH 134 634 84  HOH HOH A . 
D 3 HOH 135 635 81  HOH HOH A . 
D 3 HOH 136 636 64  HOH HOH A . 
D 3 HOH 137 637 155 HOH HOH A . 
D 3 HOH 138 638 83  HOH HOH A . 
D 3 HOH 139 639 162 HOH HOH A . 
D 3 HOH 140 640 128 HOH HOH A . 
D 3 HOH 141 641 60  HOH HOH A . 
D 3 HOH 142 642 85  HOH HOH A . 
D 3 HOH 143 643 146 HOH HOH A . 
D 3 HOH 144 644 149 HOH HOH A . 
D 3 HOH 145 645 135 HOH HOH A . 
D 3 HOH 146 646 147 HOH HOH A . 
D 3 HOH 147 647 119 HOH HOH A . 
D 3 HOH 148 648 160 HOH HOH A . 
D 3 HOH 149 649 142 HOH HOH A . 
D 3 HOH 150 650 114 HOH HOH A . 
D 3 HOH 151 651 106 HOH HOH A . 
D 3 HOH 152 652 131 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.02 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RM2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.306 
_cell.length_a_esd                 ? 
_cell.length_b                     68.880 
_cell.length_b_esd                 ? 
_cell.length_c                     59.705 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8RM2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8RM2 
_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             2.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.65 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    '0.2M ammonium sulfate, 0.1M MES monohydrate pH=6.5 and 30% w/v PEG monomethylether 5,000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-09-04 
_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   0.965 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.965 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RM2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               43.66 
_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                                     53453 
_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                           95.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.0 
_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                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.046 
_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                                    1.55 
_reflns_shell.d_res_low                                     1.58 
_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                             2597 
_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                                  0.612 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               0.511 
_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]                            -0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.650 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8RM2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.55 
_refine.ls_d_res_low                             43.66 
_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                     50792 
_refine.ls_number_reflns_R_free                  2618 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.48 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20209 
_refine.ls_R_factor_R_free                       0.23639 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20037 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.088 
_refine.pdbx_overall_ESU_R_Free                  0.091 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.401 
_refine.overall_SU_ML                            0.081 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        43.66 
_refine_hist.number_atoms_solvent             152 
_refine_hist.number_atoms_total               2984 
_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        2822 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.013  2902 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  2761 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.751  1.642  3936 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.424  1.580  6372 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.128  5.000  347  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 36.584 22.675 157  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.906 15.000 513  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 22.403 15.000 17   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.085  0.200  374  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  3236 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  654  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.642  2.578  1388 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.629  2.574  1386 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.721  3.853  1732 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.721  3.853  1732 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.478  2.983  1514 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.450  2.976  1507 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.246  4.313  2192 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.693  30.909 3318 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.693  30.770 3290 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.550 
_refine_ls_shell.d_res_low                        1.590 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             177 
_refine_ls_shell.number_reflns_R_work             3725 
_refine_ls_shell.percent_reflns_obs               99.54 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.333 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.365 
# 
_struct.entry_id                     8RM2 
_struct.title                        'Erk2 MAP kinase T188E mutant' 
_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        8RM2 
_struct_keywords.text            'Keywords: MAP kinases, SIGNAL TRANSDUCTION, PHOSPHORYLATION, erk, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 2 ? 
C N N 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MK01_RAT 
_struct_ref.pdbx_db_accession          P63086 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHEN
IIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCD
LKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILG
ILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDE
PIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_struct_ref.pdbx_align_begin           0 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8RM2 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 8 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 365 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P63086 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  358 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       358 
# 
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 8RM2 ALA A 1   ? UNP P63086 ?   ?   'expression tag'      -6  1 
1 8RM2 HIS A 2   ? UNP P63086 ?   ?   'expression tag'      -5  2 
1 8RM2 HIS A 3   ? UNP P63086 ?   ?   'expression tag'      -4  3 
1 8RM2 HIS A 4   ? UNP P63086 ?   ?   'expression tag'      -3  4 
1 8RM2 HIS A 5   ? UNP P63086 ?   ?   'expression tag'      -2  5 
1 8RM2 HIS A 6   ? UNP P63086 ?   ?   'expression tag'      -1  6 
1 8RM2 HIS A 7   ? UNP P63086 ?   ?   'expression tag'      0   7 
1 8RM2 GLU A 195 ? UNP P63086 THR 188 'engineered mutation' 188 8 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 380   ? 
1 MORE         -28   ? 
1 'SSA (A^2)'  16340 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 66  ? PHE A 83  ? HIS A 59  PHE A 76  1 ? 18 
HELX_P HELX_P2  AA2 LEU A 117 ? GLN A 124 ? LEU A 110 GLN A 117 1 ? 8  
HELX_P HELX_P3  AA3 SER A 127 ? ALA A 148 ? SER A 120 ALA A 141 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 156 ? SER A 158 ? LYS A 149 SER A 151 5 ? 3  
HELX_P HELX_P5  AA5 ASP A 180 ? ASP A 184 ? ASP A 173 ASP A 177 5 ? 5  
HELX_P HELX_P6  AA6 GLU A 195 ? ARG A 199 ? GLU A 188 ARG A 192 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 200 ? ASN A 206 ? ALA A 193 ASN A 199 1 ? 7  
HELX_P HELX_P8  AA8 LYS A 212 ? ASN A 229 ? LYS A 205 ASN A 222 1 ? 18 
HELX_P HELX_P9  AA9 HIS A 237 ? GLY A 250 ? HIS A 230 GLY A 243 1 ? 14 
HELX_P HELX_P10 AB1 SER A 253 ? CYS A 259 ? SER A 246 CYS A 252 1 ? 7  
HELX_P HELX_P11 AB2 ASN A 262 ? LEU A 272 ? ASN A 255 LEU A 265 1 ? 11 
HELX_P HELX_P12 AB3 PRO A 279 ? PHE A 284 ? PRO A 272 PHE A 277 1 ? 6  
HELX_P HELX_P13 AB4 ASP A 288 ? LEU A 299 ? ASP A 281 LEU A 292 1 ? 12 
HELX_P HELX_P14 AB5 GLU A 308 ? ALA A 314 ? GLU A 301 ALA A 307 1 ? 7  
HELX_P HELX_P15 AB6 HIS A 315 ? GLU A 319 ? HIS A 308 GLU A 312 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 323 ? GLU A 327 ? ASP A 316 GLU A 320 5 ? 5  
HELX_P HELX_P17 AB8 PRO A 344 ? THR A 356 ? PRO A 337 THR A 349 1 ? 13 
HELX_P HELX_P18 AB9 ALA A 357 ? GLN A 360 ? ALA A 350 GLN A 353 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 30  ? GLU A 38  ? TYR A 23  GLU A 31  
AA1 2 MET A 43  ? ASP A 49  ? MET A 36  ASP A 42  
AA1 3 VAL A 54  ? ILE A 61  ? VAL A 47  ILE A 54  
AA1 4 VAL A 106 ? ASP A 111 ? VAL A 99  ASP A 104 
AA1 5 ASP A 93  ? ILE A 95  ? ASP A 86  ILE A 88  
AA2 1 THR A 115 ? ASP A 116 ? THR A 108 ASP A 109 
AA2 2 LEU A 160 ? LEU A 162 ? LEU A 153 LEU A 155 
AA2 3 LEU A 168 ? ILE A 170 ? LEU A 161 ILE A 163 
AA3 1 VAL A 150 ? LEU A 151 ? VAL A 143 LEU A 144 
AA3 2 ARG A 177 ? VAL A 178 ? ARG A 170 VAL A 171 
# 
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 THR A 31  ? N THR A 24  O TYR A 48  ? O TYR A 41  
AA1 2 3 N MET A 43  ? N MET A 36  O LYS A 60  ? O LYS A 53  
AA1 3 4 N ILE A 61  ? N ILE A 54  O VAL A 106 ? O VAL A 99  
AA1 4 5 O VAL A 109 ? O VAL A 102 N ASP A 93  ? N ASP A 86  
AA2 1 2 N THR A 115 ? N THR A 108 O LEU A 162 ? O LEU A 155 
AA2 2 3 N LEU A 161 ? N LEU A 154 O LYS A 169 ? O LYS A 162 
AA3 1 2 N LEU A 151 ? N LEU A 144 O ARG A 177 ? O ARG A 170 
# 
_pdbx_entry_details.entry_id                   8RM2 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 610 ? ? O A HOH 639 ? ? 1.98 
2 1 O A HOH 637 ? ? O A HOH 645 ? ? 2.11 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 75 ? ? CZ A ARG 75 ? ? NH2 A ARG 75 ? ? 116.80 120.30 -3.50  0.50 N 
2 1 CB A ARG 89 ? ? CG A ARG 89 ? ? CD  A ARG 89 ? ? 128.40 111.60 16.80  2.60 N 
3 1 CD A ARG 89 ? ? NE A ARG 89 ? ? CZ  A ARG 89 ? ? 140.24 123.60 16.64  1.40 N 
4 1 NE A ARG 89 ? ? CZ A ARG 89 ? ? NH1 A ARG 89 ? ? 133.88 120.30 13.58  0.50 N 
5 1 NE A ARG 89 ? ? CZ A ARG 89 ? ? NH2 A ARG 89 ? ? 108.64 120.30 -11.66 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 146 ? ? 76.93   -0.81  
2 1 ASP A 147 ? ? -143.23 40.05  
3 1 ASP A 165 ? ? 65.67   78.13  
4 1 ASP A 173 ? ? -155.44 61.36  
5 1 LEU A 182 ? ? 71.39   33.47  
6 1 LEU A 198 ? ? -106.10 -62.31 
7 1 ASN A 199 ? ? -158.84 19.26  
8 1 LEU A 292 ? ? -95.89  49.68  
9 1 ASP A 316 ? ? -162.12 87.72  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    8 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    9 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -146.58 
# 
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 ALA -6  ? A ALA 1   
2  1 Y 1 A HIS -5  ? A HIS 2   
3  1 Y 1 A HIS -4  ? A HIS 3   
4  1 Y 1 A HIS -3  ? A HIS 4   
5  1 Y 1 A HIS -2  ? A HIS 5   
6  1 Y 1 A HIS -1  ? A HIS 6   
7  1 Y 1 A HIS 0   ? A HIS 7   
8  1 Y 1 A MET 1   ? A MET 8   
9  1 Y 1 A ALA 2   ? A ALA 9   
10 1 Y 1 A ALA 3   ? A ALA 10  
11 1 Y 1 A GLU 10  ? A GLU 17  
12 1 Y 1 A MET 11  ? A MET 18  
13 1 Y 1 A VAL 12  ? A VAL 19  
14 1 Y 1 A ARG 13  ? A ARG 20  
15 1 Y 1 A GLY 14  ? A GLY 21  
16 1 Y 1 A TYR 356 ? A TYR 363 
17 1 Y 1 A ARG 357 ? A ARG 364 
18 1 Y 1 A SER 358 ? A SER 365 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4S31 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RM2 
_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]   0.020701 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007136 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014518 
_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]   0.017716 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 11  ? -11.514 21.396  -8.866  1.00 44.89 ? 4   ALA A N   1 
ATOM   2    C CA  . ALA A 1 11  ? -10.843 20.918  -7.612  1.00 50.42 ? 4   ALA A CA  1 
ATOM   3    C C   . ALA A 1 11  ? -11.432 21.653  -6.400  1.00 49.83 ? 4   ALA A C   1 
ATOM   4    O O   . ALA A 1 11  ? -11.442 22.890  -6.414  1.00 42.35 ? 4   ALA A O   1 
ATOM   5    C CB  . ALA A 1 11  ? -9.353  21.128  -7.707  1.00 51.74 ? 4   ALA A CB  1 
ATOM   6    N N   . ALA A 1 12  ? -11.887 20.915  -5.381  1.00 50.34 ? 5   ALA A N   1 
ATOM   7    C CA  . ALA A 1 12  ? -12.495 21.468  -4.149  1.00 47.92 ? 5   ALA A CA  1 
ATOM   8    C C   . ALA A 1 12  ? -11.426 22.282  -3.416  1.00 47.03 ? 5   ALA A C   1 
ATOM   9    O O   . ALA A 1 12  ? -10.234 21.914  -3.492  1.00 42.67 ? 5   ALA A O   1 
ATOM   10   C CB  . ALA A 1 12  ? -13.058 20.356  -3.293  1.00 48.00 ? 5   ALA A CB  1 
ATOM   11   N N   . ALA A 1 13  ? -11.831 23.369  -2.766  1.00 46.70 ? 6   ALA A N   1 
ATOM   12   C CA  . ALA A 1 13  ? -10.935 24.323  -2.084  1.00 48.98 ? 6   ALA A CA  1 
ATOM   13   C C   . ALA A 1 13  ? -11.334 24.384  -0.608  1.00 48.63 ? 6   ALA A C   1 
ATOM   14   O O   . ALA A 1 13  ? -12.497 24.097  -0.305  1.00 50.75 ? 6   ALA A O   1 
ATOM   15   C CB  . ALA A 1 13  ? -11.010 25.676  -2.756  1.00 48.93 ? 6   ALA A CB  1 
ATOM   16   N N   . ALA A 1 14  ? -10.380 24.707  0.264   1.00 50.25 ? 7   ALA A N   1 
ATOM   17   C CA  . ALA A 1 14  ? -10.576 24.899  1.719   1.00 51.27 ? 7   ALA A CA  1 
ATOM   18   C C   . ALA A 1 14  ? -9.509  25.887  2.205   1.00 50.02 ? 7   ALA A C   1 
ATOM   19   O O   . ALA A 1 14  ? -8.327  25.653  1.904   1.00 54.44 ? 7   ALA A O   1 
ATOM   20   C CB  . ALA A 1 14  ? -10.519 23.562  2.445   1.00 50.37 ? 7   ALA A CB  1 
ATOM   21   N N   . GLY A 1 15  ? -9.918  26.979  2.875   1.00 54.94 ? 8   GLY A N   1 
ATOM   22   C CA  . GLY A 1 15  ? -9.048  28.125  3.221   1.00 52.70 ? 8   GLY A CA  1 
ATOM   23   C C   . GLY A 1 15  ? -8.279  28.620  1.997   1.00 55.25 ? 8   GLY A C   1 
ATOM   24   O O   . GLY A 1 15  ? -7.163  29.123  2.120   1.00 49.42 ? 8   GLY A O   1 
ATOM   25   N N   . PRO A 1 16  ? -8.885  28.542  0.784   1.00 65.75 ? 9   PRO A N   1 
ATOM   26   C CA  . PRO A 1 16  ? -8.131  28.284  -0.445  1.00 69.89 ? 9   PRO A CA  1 
ATOM   27   C C   . PRO A 1 16  ? -6.890  29.164  -0.650  1.00 62.56 ? 9   PRO A C   1 
ATOM   28   O O   . PRO A 1 16  ? -6.167  28.854  -1.588  1.00 63.11 ? 9   PRO A O   1 
ATOM   29   C CB  . PRO A 1 16  ? -9.116  28.523  -1.603  1.00 74.07 ? 9   PRO A CB  1 
ATOM   30   C CG  . PRO A 1 16  ? -10.444 28.926  -0.965  1.00 76.03 ? 9   PRO A CG  1 
ATOM   31   C CD  . PRO A 1 16  ? -10.324 28.724  0.532   1.00 71.74 ? 9   PRO A CD  1 
ATOM   32   N N   . GLN A 1 22  ? -5.926  25.831  0.766   1.00 68.19 ? 15  GLN A N   1 
ATOM   33   C CA  . GLN A 1 22  ? -5.687  25.956  -0.698  1.00 61.13 ? 15  GLN A CA  1 
ATOM   34   C C   . GLN A 1 22  ? -6.536  24.909  -1.437  1.00 46.22 ? 15  GLN A C   1 
ATOM   35   O O   . GLN A 1 22  ? -7.654  24.610  -0.991  1.00 44.34 ? 15  GLN A O   1 
ATOM   36   C CB  . GLN A 1 22  ? -4.187  25.834  -0.998  1.00 68.09 ? 15  GLN A CB  1 
ATOM   37   C CG  . GLN A 1 22  ? -3.742  26.720  -2.162  1.00 76.98 ? 15  GLN A CG  1 
ATOM   38   C CD  . GLN A 1 22  ? -2.574  26.176  -2.951  1.00 77.67 ? 15  GLN A CD  1 
ATOM   39   O OE1 . GLN A 1 22  ? -1.457  26.687  -2.876  1.00 80.05 ? 15  GLN A OE1 1 
ATOM   40   N NE2 . GLN A 1 22  ? -2.826  25.143  -3.739  1.00 74.16 ? 15  GLN A NE2 1 
ATOM   41   N N   . VAL A 1 23  ? -6.021  24.371  -2.538  1.00 40.61 ? 16  VAL A N   1 
ATOM   42   C CA  . VAL A 1 23  ? -6.519  23.101  -3.144  1.00 40.73 ? 16  VAL A CA  1 
ATOM   43   C C   . VAL A 1 23  ? -6.547  22.019  -2.048  1.00 35.77 ? 16  VAL A C   1 
ATOM   44   O O   . VAL A 1 23  ? -5.486  21.766  -1.443  1.00 39.14 ? 16  VAL A O   1 
ATOM   45   C CB  . VAL A 1 23  ? -5.635  22.629  -4.316  1.00 41.62 ? 16  VAL A CB  1 
ATOM   46   C CG1 . VAL A 1 23  ? -6.128  21.301  -4.877  1.00 39.91 ? 16  VAL A CG1 1 
ATOM   47   C CG2 . VAL A 1 23  ? -5.507  23.670  -5.421  1.00 42.90 ? 16  VAL A CG2 1 
ATOM   48   N N   . PHE A 1 24  ? -7.707  21.402  -1.846  1.00 32.97 ? 17  PHE A N   1 
ATOM   49   C CA  . PHE A 1 24  ? -7.907  20.161  -1.057  1.00 34.29 ? 17  PHE A CA  1 
ATOM   50   C C   . PHE A 1 24  ? -8.754  19.207  -1.903  1.00 29.21 ? 17  PHE A C   1 
ATOM   51   O O   . PHE A 1 24  ? -9.982  19.095  -1.756  1.00 34.08 ? 17  PHE A O   1 
ATOM   52   C CB  . PHE A 1 24  ? -8.499  20.474  0.321   1.00 32.60 ? 17  PHE A CB  1 
ATOM   53   C CG  . PHE A 1 24  ? -8.097  19.453  1.359   1.00 31.89 ? 17  PHE A CG  1 
ATOM   54   C CD1 . PHE A 1 24  ? -8.827  18.293  1.518   1.00 31.72 ? 17  PHE A CD1 1 
ATOM   55   C CD2 . PHE A 1 24  ? -6.965  19.638  2.130   1.00 35.27 ? 17  PHE A CD2 1 
ATOM   56   C CE1 . PHE A 1 24  ? -8.452  17.344  2.464   1.00 32.67 ? 17  PHE A CE1 1 
ATOM   57   C CE2 . PHE A 1 24  ? -6.604  18.702  3.091   1.00 31.77 ? 17  PHE A CE2 1 
ATOM   58   C CZ  . PHE A 1 24  ? -7.347  17.558  3.245   1.00 30.51 ? 17  PHE A CZ  1 
ATOM   59   N N   . ASP A 1 25  ? -8.076  18.544  -2.823  1.00 33.00 ? 18  ASP A N   1 
ATOM   60   C CA  . ASP A 1 25  ? -8.706  17.862  -3.975  1.00 34.00 ? 18  ASP A CA  1 
ATOM   61   C C   . ASP A 1 25  ? -8.793  16.355  -3.742  1.00 32.57 ? 18  ASP A C   1 
ATOM   62   O O   . ASP A 1 25  ? -7.868  15.672  -4.145  1.00 28.19 ? 18  ASP A O   1 
ATOM   63   C CB  . ASP A 1 25  ? -7.862  18.147  -5.213  1.00 39.55 ? 18  ASP A CB  1 
ATOM   64   C CG  . ASP A 1 25  ? -8.411  17.500  -6.465  1.00 39.73 ? 18  ASP A CG  1 
ATOM   65   O OD1 . ASP A 1 25  ? -9.639  17.396  -6.562  1.00 42.48 ? 18  ASP A OD1 1 
ATOM   66   O OD2 . ASP A 1 25  ? -7.595  17.098  -7.310  1.00 49.66 ? 18  ASP A OD2 1 
ATOM   67   N N   . VAL A 1 26  ? -9.880  15.836  -3.183  1.00 32.72 ? 19  VAL A N   1 
ATOM   68   C CA  . VAL A 1 26  ? -9.870  14.420  -2.718  1.00 35.61 ? 19  VAL A CA  1 
ATOM   69   C C   . VAL A 1 26  ? -10.923 13.600  -3.464  1.00 42.79 ? 19  VAL A C   1 
ATOM   70   O O   . VAL A 1 26  ? -11.633 12.813  -2.817  1.00 42.86 ? 19  VAL A O   1 
ATOM   71   C CB  . VAL A 1 26  ? -9.984  14.348  -1.178  1.00 33.82 ? 19  VAL A CB  1 
ATOM   72   C CG1 . VAL A 1 26  ? -8.703  14.850  -0.545  1.00 34.91 ? 19  VAL A CG1 1 
ATOM   73   C CG2 . VAL A 1 26  ? -11.184 15.115  -0.630  1.00 38.31 ? 19  VAL A CG2 1 
ATOM   74   N N   . GLY A 1 27  ? -10.969 13.746  -4.798  1.00 53.30 ? 20  GLY A N   1 
ATOM   75   C CA  . GLY A 1 27  ? -11.576 12.773  -5.733  1.00 46.36 ? 20  GLY A CA  1 
ATOM   76   C C   . GLY A 1 27  ? -13.071 12.625  -5.509  1.00 50.11 ? 20  GLY A C   1 
ATOM   77   O O   . GLY A 1 27  ? -13.668 13.439  -4.807  1.00 58.05 ? 20  GLY A O   1 
ATOM   78   N N   . PRO A 1 28  ? -13.714 11.590  -6.098  1.00 50.52 ? 21  PRO A N   1 
ATOM   79   C CA  . PRO A 1 28  ? -15.162 11.413  -5.956  1.00 52.52 ? 21  PRO A CA  1 
ATOM   80   C C   . PRO A 1 28  ? -15.545 10.955  -4.531  1.00 49.09 ? 21  PRO A C   1 
ATOM   81   O O   . PRO A 1 28  ? -16.482 11.512  -3.924  1.00 44.26 ? 21  PRO A O   1 
ATOM   82   C CB  . PRO A 1 28  ? -15.476 10.371  -7.052  1.00 50.98 ? 21  PRO A CB  1 
ATOM   83   C CG  . PRO A 1 28  ? -14.198 9.563   -7.211  1.00 53.06 ? 21  PRO A CG  1 
ATOM   84   C CD  . PRO A 1 28  ? -13.078 10.539  -6.916  1.00 50.84 ? 21  PRO A CD  1 
ATOM   85   N N   . ARG A 1 29  ? -14.768 10.011  -3.997  1.00 46.75 ? 22  ARG A N   1 
ATOM   86   C CA  . ARG A 1 29  ? -15.063 9.229   -2.763  1.00 44.53 ? 22  ARG A CA  1 
ATOM   87   C C   . ARG A 1 29  ? -15.344 10.139  -1.550  1.00 41.06 ? 22  ARG A C   1 
ATOM   88   O O   . ARG A 1 29  ? -16.180 9.739   -0.718  1.00 43.44 ? 22  ARG A O   1 
ATOM   89   C CB  . ARG A 1 29  ? -13.907 8.259   -2.508  1.00 44.60 ? 22  ARG A CB  1 
ATOM   90   C CG  . ARG A 1 29  ? -13.924 7.612   -1.130  1.00 46.40 ? 22  ARG A CG  1 
ATOM   91   C CD  . ARG A 1 29  ? -14.215 6.141   -1.130  1.00 47.45 ? 22  ARG A CD  1 
ATOM   92   N NE  . ARG A 1 29  ? -13.004 5.349   -1.222  1.00 50.63 ? 22  ARG A NE  1 
ATOM   93   C CZ  . ARG A 1 29  ? -12.479 4.589   -0.264  1.00 45.03 ? 22  ARG A CZ  1 
ATOM   94   N NH1 . ARG A 1 29  ? -13.032 4.494   0.929   1.00 48.77 ? 22  ARG A NH1 1 
ATOM   95   N NH2 . ARG A 1 29  ? -11.386 3.899   -0.522  1.00 42.76 ? 22  ARG A NH2 1 
ATOM   96   N N   . TYR A 1 30  ? -14.683 11.290  -1.403  1.00 40.51 ? 23  TYR A N   1 
ATOM   97   C CA  . TYR A 1 30  ? -14.653 12.049  -0.119  1.00 39.82 ? 23  TYR A CA  1 
ATOM   98   C C   . TYR A 1 30  ? -15.229 13.446  -0.327  1.00 42.33 ? 23  TYR A C   1 
ATOM   99   O O   . TYR A 1 30  ? -14.686 14.179  -1.166  1.00 42.37 ? 23  TYR A O   1 
ATOM   100  C CB  . TYR A 1 30  ? -13.225 12.144  0.437   1.00 35.09 ? 23  TYR A CB  1 
ATOM   101  C CG  . TYR A 1 30  ? -12.559 10.803  0.573   1.00 31.73 ? 23  TYR A CG  1 
ATOM   102  C CD1 . TYR A 1 30  ? -12.845 9.986   1.655   1.00 27.16 ? 23  TYR A CD1 1 
ATOM   103  C CD2 . TYR A 1 30  ? -11.661 10.334  -0.374  1.00 29.18 ? 23  TYR A CD2 1 
ATOM   104  C CE1 . TYR A 1 30  ? -12.312 8.718   1.762   1.00 27.59 ? 23  TYR A CE1 1 
ATOM   105  C CE2 . TYR A 1 30  ? -11.090 9.076   -0.264  1.00 28.86 ? 23  TYR A CE2 1 
ATOM   106  C CZ  . TYR A 1 30  ? -11.369 8.293   0.849   1.00 25.93 ? 23  TYR A CZ  1 
ATOM   107  O OH  . TYR A 1 30  ? -10.849 7.054   1.002   1.00 25.77 ? 23  TYR A OH  1 
ATOM   108  N N   . THR A 1 31  ? -16.261 13.801  0.447   1.00 47.60 ? 24  THR A N   1 
ATOM   109  C CA  . THR A 1 31  ? -17.040 15.059  0.300   1.00 48.33 ? 24  THR A CA  1 
ATOM   110  C C   . THR A 1 31  ? -17.237 15.737  1.661   1.00 50.88 ? 24  THR A C   1 
ATOM   111  O O   . THR A 1 31  ? -16.765 15.201  2.678   1.00 44.66 ? 24  THR A O   1 
ATOM   112  C CB  . THR A 1 31  ? -18.372 14.746  -0.388  1.00 47.18 ? 24  THR A CB  1 
ATOM   113  O OG1 . THR A 1 31  ? -19.046 13.720  0.336   1.00 41.80 ? 24  THR A OG1 1 
ATOM   114  C CG2 . THR A 1 31  ? -18.193 14.275  -1.813  1.00 48.73 ? 24  THR A CG2 1 
ATOM   115  N N   . ASN A 1 32  ? -17.891 16.896  1.680   1.00 49.41 ? 25  ASN A N   1 
ATOM   116  C CA  . ASN A 1 32  ? -18.339 17.547  2.939   1.00 51.63 ? 25  ASN A CA  1 
ATOM   117  C C   . ASN A 1 32  ? -17.119 17.763  3.843   1.00 49.85 ? 25  ASN A C   1 
ATOM   118  O O   . ASN A 1 32  ? -17.180 17.396  5.037   1.00 44.00 ? 25  ASN A O   1 
ATOM   119  C CB  . ASN A 1 32  ? -19.439 16.711  3.603   1.00 54.24 ? 25  ASN A CB  1 
ATOM   120  C CG  . ASN A 1 32  ? -20.572 16.404  2.646   1.00 55.18 ? 25  ASN A CG  1 
ATOM   121  O OD1 . ASN A 1 32  ? -21.404 17.263  2.371   1.00 59.80 ? 25  ASN A OD1 1 
ATOM   122  N ND2 . ASN A 1 32  ? -20.600 15.198  2.107   1.00 55.76 ? 25  ASN A ND2 1 
ATOM   123  N N   . LEU A 1 33  ? -16.072 18.346  3.264   1.00 50.86 ? 26  LEU A N   1 
ATOM   124  C CA  . LEU A 1 33  ? -14.778 18.702  3.897   1.00 50.11 ? 26  LEU A CA  1 
ATOM   125  C C   . LEU A 1 33  ? -15.031 19.687  5.034   1.00 55.42 ? 26  LEU A C   1 
ATOM   126  O O   . LEU A 1 33  ? -15.909 20.564  4.881   1.00 58.98 ? 26  LEU A O   1 
ATOM   127  C CB  . LEU A 1 33  ? -13.853 19.346  2.858   1.00 51.27 ? 26  LEU A CB  1 
ATOM   128  C CG  . LEU A 1 33  ? -13.044 18.412  1.948   1.00 51.89 ? 26  LEU A CG  1 
ATOM   129  C CD1 . LEU A 1 33  ? -13.824 17.167  1.545   1.00 52.15 ? 26  LEU A CD1 1 
ATOM   130  C CD2 . LEU A 1 33  ? -12.572 19.166  0.710   1.00 50.97 ? 26  LEU A CD2 1 
ATOM   131  N N   . SER A 1 34  ? -14.254 19.579  6.108   1.00 43.24 ? 27  SER A N   1 
ATOM   132  C CA  . SER A 1 34  ? -14.221 20.572  7.204   1.00 46.97 ? 27  SER A CA  1 
ATOM   133  C C   . SER A 1 34  ? -12.773 20.726  7.674   1.00 46.71 ? 27  SER A C   1 
ATOM   134  O O   . SER A 1 34  ? -12.135 19.701  8.001   1.00 48.65 ? 27  SER A O   1 
ATOM   135  C CB  . SER A 1 34  ? -15.163 20.170  8.306   1.00 46.65 ? 27  SER A CB  1 
ATOM   136  O OG  . SER A 1 34  ? -14.868 20.883  9.491   1.00 49.53 ? 27  SER A OG  1 
ATOM   137  N N   . TYR A 1 35  ? -12.244 21.942  7.609   1.00 42.19 ? 28  TYR A N   1 
ATOM   138  C CA  . TYR A 1 35  ? -10.879 22.277  8.075   1.00 46.02 ? 28  TYR A CA  1 
ATOM   139  C C   . TYR A 1 35  ? -10.754 21.803  9.529   1.00 47.58 ? 28  TYR A C   1 
ATOM   140  O O   . TYR A 1 35  ? -11.607 22.190  10.331  1.00 50.06 ? 28  TYR A O   1 
ATOM   141  C CB  . TYR A 1 35  ? -10.653 23.783  7.946   1.00 43.83 ? 28  TYR A CB  1 
ATOM   142  C CG  . TYR A 1 35  ? -9.306  24.233  8.432   1.00 45.89 ? 28  TYR A CG  1 
ATOM   143  C CD1 . TYR A 1 35  ? -8.200  24.164  7.608   1.00 47.24 ? 28  TYR A CD1 1 
ATOM   144  C CD2 . TYR A 1 35  ? -9.128  24.693  9.728   1.00 52.03 ? 28  TYR A CD2 1 
ATOM   145  C CE1 . TYR A 1 35  ? -6.948  24.555  8.048   1.00 49.56 ? 28  TYR A CE1 1 
ATOM   146  C CE2 . TYR A 1 35  ? -7.886  25.101  10.183  1.00 48.59 ? 28  TYR A CE2 1 
ATOM   147  C CZ  . TYR A 1 35  ? -6.793  25.036  9.339   1.00 52.24 ? 28  TYR A CZ  1 
ATOM   148  O OH  . TYR A 1 35  ? -5.563  25.419  9.787   1.00 57.74 ? 28  TYR A OH  1 
ATOM   149  N N   . ILE A 1 36  ? -9.784  20.949  9.857   1.00 49.33 ? 29  ILE A N   1 
ATOM   150  C CA  . ILE A 1 36  ? -9.515  20.560  11.274  1.00 52.89 ? 29  ILE A CA  1 
ATOM   151  C C   . ILE A 1 36  ? -8.034  20.803  11.568  1.00 53.63 ? 29  ILE A C   1 
ATOM   152  O O   . ILE A 1 36  ? -7.450  20.027  12.350  1.00 58.98 ? 29  ILE A O   1 
ATOM   153  C CB  . ILE A 1 36  ? -9.989  19.122  11.602  1.00 53.64 ? 29  ILE A CB  1 
ATOM   154  C CG1 . ILE A 1 36  ? -9.161  18.026  10.934  1.00 58.74 ? 29  ILE A CG1 1 
ATOM   155  C CG2 . ILE A 1 36  ? -11.463 18.946  11.272  1.00 57.72 ? 29  ILE A CG2 1 
ATOM   156  C CD1 . ILE A 1 36  ? -9.672  16.625  11.236  1.00 58.51 ? 29  ILE A CD1 1 
ATOM   157  N N   . GLY A 1 37  ? -7.456  21.842  10.958  1.00 50.99 ? 30  GLY A N   1 
ATOM   158  C CA  . GLY A 1 37  ? -6.159  22.414  11.363  1.00 51.59 ? 30  GLY A CA  1 
ATOM   159  C C   . GLY A 1 37  ? -5.047  22.151  10.361  1.00 56.18 ? 30  GLY A C   1 
ATOM   160  O O   . GLY A 1 37  ? -5.306  21.489  9.331   1.00 59.36 ? 30  GLY A O   1 
ATOM   161  N N   . GLU A 1 38  ? -3.856  22.675  10.667  1.00 56.22 ? 31  GLU A N   1 
ATOM   162  C CA  . GLU A 1 38  ? -2.590  22.505  9.910   1.00 60.32 ? 31  GLU A CA  1 
ATOM   163  C C   . GLU A 1 38  ? -1.818  21.300  10.467  1.00 63.66 ? 31  GLU A C   1 
ATOM   164  O O   . GLU A 1 38  ? -1.993  20.973  11.658  1.00 64.72 ? 31  GLU A O   1 
ATOM   165  C CB  . GLU A 1 38  ? -1.746  23.780  10.010  1.00 62.35 ? 31  GLU A CB  1 
ATOM   166  C CG  . GLU A 1 38  ? -0.793  23.984  8.843   1.00 64.50 ? 31  GLU A CG  1 
ATOM   167  C CD  . GLU A 1 38  ? -1.468  24.327  7.522   1.00 61.63 ? 31  GLU A CD  1 
ATOM   168  O OE1 . GLU A 1 38  ? -2.705  24.536  7.513   1.00 59.89 ? 31  GLU A OE1 1 
ATOM   169  O OE2 . GLU A 1 38  ? -0.758  24.378  6.497   1.00 64.97 ? 31  GLU A OE2 1 
ATOM   170  N N   . GLY A 1 39  ? -1.016  20.657  9.613   1.00 68.52 ? 32  GLY A N   1 
ATOM   171  C CA  . GLY A 1 39  ? -0.052  19.599  9.968   1.00 68.10 ? 32  GLY A CA  1 
ATOM   172  C C   . GLY A 1 39  ? 1.355   20.027  9.595   1.00 71.49 ? 32  GLY A C   1 
ATOM   173  O O   . GLY A 1 39  ? 1.616   21.249  9.567   1.00 82.47 ? 32  GLY A O   1 
ATOM   174  N N   . ALA A 1 40  ? 2.223   19.065  9.282   1.00 74.23 ? 33  ALA A N   1 
ATOM   175  C CA  . ALA A 1 40  ? 3.667   19.279  9.029   1.00 72.01 ? 33  ALA A CA  1 
ATOM   176  C C   . ALA A 1 40  ? 3.874   19.944  7.660   1.00 70.01 ? 33  ALA A C   1 
ATOM   177  O O   . ALA A 1 40  ? 4.348   21.095  7.636   1.00 67.03 ? 33  ALA A O   1 
ATOM   178  C CB  . ALA A 1 40  ? 4.405   17.966  9.134   1.00 72.37 ? 33  ALA A CB  1 
ATOM   179  N N   . TYR A 1 41  ? 3.541   19.242  6.569   1.00 67.71 ? 34  TYR A N   1 
ATOM   180  C CA  . TYR A 1 41  ? 3.781   19.674  5.159   1.00 65.63 ? 34  TYR A CA  1 
ATOM   181  C C   . TYR A 1 41  ? 2.447   19.857  4.435   1.00 54.94 ? 34  TYR A C   1 
ATOM   182  O O   . TYR A 1 41  ? 2.378   19.596  3.233   1.00 53.46 ? 34  TYR A O   1 
ATOM   183  C CB  . TYR A 1 41  ? 4.625   18.658  4.381   1.00 68.75 ? 34  TYR A CB  1 
ATOM   184  C CG  . TYR A 1 41  ? 5.722   18.012  5.181   1.00 73.57 ? 34  TYR A CG  1 
ATOM   185  C CD1 . TYR A 1 41  ? 6.616   18.783  5.903   1.00 74.28 ? 34  TYR A CD1 1 
ATOM   186  C CD2 . TYR A 1 41  ? 5.854   16.633  5.234   1.00 74.05 ? 34  TYR A CD2 1 
ATOM   187  C CE1 . TYR A 1 41  ? 7.619   18.201  6.659   1.00 79.78 ? 34  TYR A CE1 1 
ATOM   188  C CE2 . TYR A 1 41  ? 6.853   16.034  5.984   1.00 76.97 ? 34  TYR A CE2 1 
ATOM   189  C CZ  . TYR A 1 41  ? 7.738   16.823  6.698   1.00 79.75 ? 34  TYR A CZ  1 
ATOM   190  O OH  . TYR A 1 41  ? 8.730   16.257  7.437   1.00 78.25 ? 34  TYR A OH  1 
ATOM   191  N N   . GLY A 1 42  ? 1.418   20.281  5.160   1.00 46.20 ? 35  GLY A N   1 
ATOM   192  C CA  . GLY A 1 42  ? 0.100   20.603  4.591   1.00 47.79 ? 35  GLY A CA  1 
ATOM   193  C C   . GLY A 1 42  ? -0.970  20.540  5.656   1.00 47.73 ? 35  GLY A C   1 
ATOM   194  O O   . GLY A 1 42  ? -0.601  20.377  6.830   1.00 46.41 ? 35  GLY A O   1 
ATOM   195  N N   . MET A 1 43  ? -2.233  20.621  5.233   1.00 44.38 ? 36  MET A N   1 
ATOM   196  C CA  . MET A 1 43  ? -3.420  20.862  6.083   1.00 44.20 ? 36  MET A CA  1 
ATOM   197  C C   . MET A 1 43  ? -4.249  19.583  6.235   1.00 45.91 ? 36  MET A C   1 
ATOM   198  O O   . MET A 1 43  ? -4.100  18.631  5.428   1.00 35.72 ? 36  MET A O   1 
ATOM   199  C CB  . MET A 1 43  ? -4.286  21.989  5.506   1.00 49.45 ? 36  MET A CB  1 
ATOM   200  C CG  . MET A 1 43  ? -5.617  21.561  4.891   1.00 51.37 ? 36  MET A CG  1 
ATOM   201  S SD  . MET A 1 43  ? -6.522  22.912  4.048   1.00 60.00 ? 36  MET A SD  1 
ATOM   202  C CE  . MET A 1 43  ? -5.176  23.983  3.535   1.00 55.76 ? 36  MET A CE  1 
ATOM   203  N N   . VAL A 1 44  ? -5.100  19.581  7.263   1.00 38.72 ? 37  VAL A N   1 
ATOM   204  C CA  . VAL A 1 44  ? -5.916  18.410  7.656   1.00 36.51 ? 37  VAL A CA  1 
ATOM   205  C C   . VAL A 1 44  ? -7.386  18.818  7.633   1.00 35.31 ? 37  VAL A C   1 
ATOM   206  O O   . VAL A 1 44  ? -7.702  19.869  8.203   1.00 38.88 ? 37  VAL A O   1 
ATOM   207  C CB  . VAL A 1 44  ? -5.475  17.888  9.036   1.00 34.19 ? 37  VAL A CB  1 
ATOM   208  C CG1 . VAL A 1 44  ? -6.252  16.636  9.401   1.00 31.74 ? 37  VAL A CG1 1 
ATOM   209  C CG2 . VAL A 1 44  ? -3.977  17.642  9.092   1.00 33.23 ? 37  VAL A CG2 1 
ATOM   210  N N   . CYS A 1 45  ? -8.233  18.002  7.001   1.00 35.15 ? 38  CYS A N   1 
ATOM   211  C CA  . CYS A 1 45  ? -9.705  18.146  6.995   1.00 36.78 ? 38  CYS A CA  1 
ATOM   212  C C   . CYS A 1 45  ? -10.352 16.805  7.321   1.00 36.66 ? 38  CYS A C   1 
ATOM   213  O O   . CYS A 1 45  ? -9.780  15.758  6.999   1.00 39.55 ? 38  CYS A O   1 
ATOM   214  C CB  . CYS A 1 45  ? -10.213 18.635  5.638   1.00 41.17 ? 38  CYS A CB  1 
ATOM   215  S SG  . CYS A 1 45  ? -9.454  20.191  5.105   1.00 41.24 ? 38  CYS A SG  1 
ATOM   216  N N   . SER A 1 46  ? -11.528 16.838  7.927   1.00 31.55 ? 39  SER A N   1 
ATOM   217  C CA  . SER A 1 46  ? -12.425 15.675  7.978   1.00 33.25 ? 39  SER A CA  1 
ATOM   218  C C   . SER A 1 46  ? -13.216 15.695  6.683   1.00 31.54 ? 39  SER A C   1 
ATOM   219  O O   . SER A 1 46  ? -13.292 16.769  6.054   1.00 38.76 ? 39  SER A O   1 
ATOM   220  C CB  . SER A 1 46  ? -13.315 15.664  9.187   1.00 34.10 ? 39  SER A CB  1 
ATOM   221  O OG  . SER A 1 46  ? -14.409 16.555  9.025   1.00 32.82 ? 39  SER A OG  1 
ATOM   222  N N   . ALA A 1 47  ? -13.766 14.550  6.310   1.00 34.28 ? 40  ALA A N   1 
ATOM   223  C CA  . ALA A 1 47  ? -14.543 14.370  5.069   1.00 35.91 ? 40  ALA A CA  1 
ATOM   224  C C   . ALA A 1 47  ? -15.454 13.173  5.249   1.00 40.69 ? 40  ALA A C   1 
ATOM   225  O O   . ALA A 1 47  ? -15.156 12.303  6.079   1.00 37.12 ? 40  ALA A O   1 
ATOM   226  C CB  . ALA A 1 47  ? -13.632 14.146  3.879   1.00 34.19 ? 40  ALA A CB  1 
ATOM   227  N N   . TYR A 1 48  ? -16.519 13.134  4.466   1.00 35.86 ? 41  TYR A N   1 
ATOM   228  C CA  . TYR A 1 48  ? -17.449 11.998  4.419   1.00 39.85 ? 41  TYR A CA  1 
ATOM   229  C C   . TYR A 1 48  ? -16.893 11.015  3.399   1.00 41.18 ? 41  TYR A C   1 
ATOM   230  O O   . TYR A 1 48  ? -16.729 11.410  2.230   1.00 41.20 ? 41  TYR A O   1 
ATOM   231  C CB  . TYR A 1 48  ? -18.866 12.473  4.085   1.00 39.21 ? 41  TYR A CB  1 
ATOM   232  C CG  . TYR A 1 48  ? -19.859 11.351  4.171   1.00 44.27 ? 41  TYR A CG  1 
ATOM   233  C CD1 . TYR A 1 48  ? -20.219 10.827  5.403   1.00 47.37 ? 41  TYR A CD1 1 
ATOM   234  C CD2 . TYR A 1 48  ? -20.374 10.760  3.028   1.00 49.19 ? 41  TYR A CD2 1 
ATOM   235  C CE1 . TYR A 1 48  ? -21.089 9.758   5.499   1.00 45.83 ? 41  TYR A CE1 1 
ATOM   236  C CE2 . TYR A 1 48  ? -21.249 9.689   3.107   1.00 48.33 ? 41  TYR A CE2 1 
ATOM   237  C CZ  . TYR A 1 48  ? -21.607 9.192   4.349   1.00 47.46 ? 41  TYR A CZ  1 
ATOM   238  O OH  . TYR A 1 48  ? -22.484 8.155   4.436   1.00 47.14 ? 41  TYR A OH  1 
ATOM   239  N N   . ASP A 1 49  ? -16.540 9.821   3.855   1.00 38.31 ? 42  ASP A N   1 
ATOM   240  C CA  . ASP A 1 49  ? -16.205 8.670   2.988   1.00 39.13 ? 42  ASP A CA  1 
ATOM   241  C C   . ASP A 1 49  ? -17.537 8.097   2.503   1.00 42.80 ? 42  ASP A C   1 
ATOM   242  O O   . ASP A 1 49  ? -18.229 7.386   3.278   1.00 37.37 ? 42  ASP A O   1 
ATOM   243  C CB  . ASP A 1 49  ? -15.304 7.665   3.705   1.00 38.95 ? 42  ASP A CB  1 
ATOM   244  C CG  . ASP A 1 49  ? -15.011 6.428   2.878   1.00 43.15 ? 42  ASP A CG  1 
ATOM   245  O OD1 . ASP A 1 49  ? -15.694 6.237   1.850   1.00 40.66 ? 42  ASP A OD1 1 
ATOM   246  O OD2 . ASP A 1 49  ? -14.089 5.677   3.246   1.00 37.72 ? 42  ASP A OD2 1 
ATOM   247  N N   . ASN A 1 50  ? -17.833 8.368   1.231   1.00 44.25 ? 43  ASN A N   1 
ATOM   248  C CA  . ASN A 1 50  ? -19.080 7.972   0.530   1.00 41.76 ? 43  ASN A CA  1 
ATOM   249  C C   . ASN A 1 50  ? -19.098 6.462   0.303   1.00 44.49 ? 43  ASN A C   1 
ATOM   250  O O   . ASN A 1 50  ? -20.142 5.977   -0.113  1.00 49.85 ? 43  ASN A O   1 
ATOM   251  C CB  . ASN A 1 50  ? -19.219 8.743   -0.791  1.00 42.12 ? 43  ASN A CB  1 
ATOM   252  C CG  . ASN A 1 50  ? -19.696 10.166  -0.586  1.00 41.44 ? 43  ASN A CG  1 
ATOM   253  O OD1 . ASN A 1 50  ? -20.874 10.377  -0.316  1.00 41.76 ? 43  ASN A OD1 1 
ATOM   254  N ND2 . ASN A 1 50  ? -18.813 11.151  -0.687  1.00 41.91 ? 43  ASN A ND2 1 
ATOM   255  N N   . LEU A 1 51  ? -17.990 5.745   0.527   1.00 45.18 ? 44  LEU A N   1 
ATOM   256  C CA  . LEU A 1 51  ? -17.905 4.281   0.249   1.00 47.02 ? 44  LEU A CA  1 
ATOM   257  C C   . LEU A 1 51  ? -18.095 3.493   1.550   1.00 52.40 ? 44  LEU A C   1 
ATOM   258  O O   . LEU A 1 51  ? -18.756 2.445   1.502   1.00 54.16 ? 44  LEU A O   1 
ATOM   259  C CB  . LEU A 1 51  ? -16.557 3.958   -0.401  1.00 48.42 ? 44  LEU A CB  1 
ATOM   260  C CG  . LEU A 1 51  ? -16.415 2.603   -1.096  1.00 53.52 ? 44  LEU A CG  1 
ATOM   261  C CD1 . LEU A 1 51  ? -16.180 1.477   -0.112  1.00 57.19 ? 44  LEU A CD1 1 
ATOM   262  C CD2 . LEU A 1 51  ? -17.612 2.292   -1.983  1.00 57.63 ? 44  LEU A CD2 1 
ATOM   263  N N   . ASN A 1 52  ? -17.523 3.952   2.667   1.00 49.83 ? 45  ASN A N   1 
ATOM   264  C CA  . ASN A 1 52  ? -17.643 3.240   3.970   1.00 47.54 ? 45  ASN A CA  1 
ATOM   265  C C   . ASN A 1 52  ? -18.723 3.921   4.814   1.00 46.04 ? 45  ASN A C   1 
ATOM   266  O O   . ASN A 1 52  ? -19.051 3.368   5.887   1.00 46.93 ? 45  ASN A O   1 
ATOM   267  C CB  . ASN A 1 52  ? -16.309 3.175   4.715   1.00 44.55 ? 45  ASN A CB  1 
ATOM   268  C CG  . ASN A 1 52  ? -15.282 2.301   4.035   1.00 46.40 ? 45  ASN A CG  1 
ATOM   269  O OD1 . ASN A 1 52  ? -14.090 2.456   4.268   1.00 48.67 ? 45  ASN A OD1 1 
ATOM   270  N ND2 . ASN A 1 52  ? -15.715 1.355   3.223   1.00 48.43 ? 45  ASN A ND2 1 
ATOM   271  N N   . LYS A 1 53  ? -19.211 5.083   4.368   1.00 45.14 ? 46  LYS A N   1 
ATOM   272  C CA  . LYS A 1 53  ? -20.317 5.834   5.011   1.00 48.47 ? 46  LYS A CA  1 
ATOM   273  C C   . LYS A 1 53  ? -19.906 6.241   6.424   1.00 46.51 ? 46  LYS A C   1 
ATOM   274  O O   . LYS A 1 53  ? -20.687 6.006   7.358   1.00 43.98 ? 46  LYS A O   1 
ATOM   275  C CB  . LYS A 1 53  ? -21.576 4.963   5.063   1.00 49.05 ? 46  LYS A CB  1 
ATOM   276  C CG  . LYS A 1 53  ? -22.070 4.459   3.717   1.00 51.44 ? 46  LYS A CG  1 
ATOM   277  C CD  . LYS A 1 53  ? -22.766 5.545   2.944   1.00 52.62 ? 46  LYS A CD  1 
ATOM   278  C CE  . LYS A 1 53  ? -23.490 5.051   1.710   1.00 56.12 ? 46  LYS A CE  1 
ATOM   279  N NZ  . LYS A 1 53  ? -22.798 5.481   0.469   1.00 58.29 ? 46  LYS A NZ  1 
ATOM   280  N N   . VAL A 1 54  ? -18.729 6.833   6.573   1.00 40.30 ? 47  VAL A N   1 
ATOM   281  C CA  . VAL A 1 54  ? -18.212 7.361   7.868   1.00 37.98 ? 47  VAL A CA  1 
ATOM   282  C C   . VAL A 1 54  ? -17.435 8.647   7.588   1.00 37.13 ? 47  VAL A C   1 
ATOM   283  O O   . VAL A 1 54  ? -16.911 8.818   6.457   1.00 32.19 ? 47  VAL A O   1 
ATOM   284  C CB  . VAL A 1 54  ? -17.343 6.316   8.603   1.00 41.12 ? 47  VAL A CB  1 
ATOM   285  C CG1 . VAL A 1 54  ? -18.134 5.070   8.968   1.00 43.85 ? 47  VAL A CG1 1 
ATOM   286  C CG2 . VAL A 1 54  ? -16.112 5.920   7.802   1.00 37.21 ? 47  VAL A CG2 1 
ATOM   287  N N   . ARG A 1 55  ? -17.330 9.530   8.577   1.00 33.87 ? 48  ARG A N   1 
ATOM   288  C CA  . ARG A 1 55  ? -16.398 10.670  8.470   1.00 33.50 ? 48  ARG A CA  1 
ATOM   289  C C   . ARG A 1 55  ? -14.971 10.153  8.722   1.00 35.72 ? 48  ARG A C   1 
ATOM   290  O O   . ARG A 1 55  ? -14.792 9.305   9.592   1.00 34.82 ? 48  ARG A O   1 
ATOM   291  C CB  . ARG A 1 55  ? -16.844 11.818  9.366   1.00 38.86 ? 48  ARG A CB  1 
ATOM   292  C CG  . ARG A 1 55  ? -18.129 12.461  8.852   1.00 40.40 ? 48  ARG A CG  1 
ATOM   293  C CD  . ARG A 1 55  ? -18.317 13.830  9.466   1.00 41.81 ? 48  ARG A CD  1 
ATOM   294  N NE  . ARG A 1 55  ? -17.359 14.813  8.988   1.00 39.80 ? 48  ARG A NE  1 
ATOM   295  C CZ  . ARG A 1 55  ? -17.369 15.368  7.775   1.00 41.75 ? 48  ARG A CZ  1 
ATOM   296  N NH1 . ARG A 1 55  ? -18.273 15.009  6.877   1.00 43.29 ? 48  ARG A NH1 1 
ATOM   297  N NH2 . ARG A 1 55  ? -16.460 16.272  7.462   1.00 39.02 ? 48  ARG A NH2 1 
ATOM   298  N N   . VAL A 1 56  ? -14.021 10.592  7.892   1.00 29.59 ? 49  VAL A N   1 
ATOM   299  C CA  . VAL A 1 56  ? -12.596 10.165  7.936   1.00 27.31 ? 49  VAL A CA  1 
ATOM   300  C C   . VAL A 1 56  ? -11.777 11.433  8.089   1.00 27.19 ? 49  VAL A C   1 
ATOM   301  O O   . VAL A 1 56  ? -12.329 12.536  7.896   1.00 31.28 ? 49  VAL A O   1 
ATOM   302  C CB  . VAL A 1 56  ? -12.188 9.335   6.709   1.00 27.86 ? 49  VAL A CB  1 
ATOM   303  C CG1 . VAL A 1 56  ? -12.861 7.979   6.653   1.00 30.48 ? 49  VAL A CG1 1 
ATOM   304  C CG2 . VAL A 1 56  ? -12.437 10.074  5.406   1.00 31.15 ? 49  VAL A CG2 1 
ATOM   305  N N   . ALA A 1 57  ? -10.513 11.299  8.475   1.00 25.68 ? 50  ALA A N   1 
ATOM   306  C CA  . ALA A 1 57  ? -9.499  12.369  8.489   1.00 23.70 ? 50  ALA A CA  1 
ATOM   307  C C   . ALA A 1 57  ? -8.702  12.248  7.193   1.00 27.92 ? 50  ALA A C   1 
ATOM   308  O O   . ALA A 1 57  ? -8.430  11.104  6.765   1.00 25.40 ? 50  ALA A O   1 
ATOM   309  C CB  . ALA A 1 57  ? -8.582  12.225  9.677   1.00 25.87 ? 50  ALA A CB  1 
ATOM   310  N N   . ILE A 1 58  ? -8.375  13.389  6.594   1.00 26.07 ? 51  ILE A N   1 
ATOM   311  C CA  . ILE A 1 58  ? -7.514  13.422  5.383   1.00 25.95 ? 51  ILE A CA  1 
ATOM   312  C C   . ILE A 1 58  ? -6.438  14.461  5.604   1.00 27.47 ? 51  ILE A C   1 
ATOM   313  O O   . ILE A 1 58  ? -6.769  15.607  5.894   1.00 31.59 ? 51  ILE A O   1 
ATOM   314  C CB  . ILE A 1 58  ? -8.329  13.697  4.107   1.00 24.61 ? 51  ILE A CB  1 
ATOM   315  C CG1 . ILE A 1 58  ? -9.446  12.670  3.949   1.00 26.43 ? 51  ILE A CG1 1 
ATOM   316  C CG2 . ILE A 1 58  ? -7.364  13.697  2.926   1.00 23.43 ? 51  ILE A CG2 1 
ATOM   317  C CD1 . ILE A 1 58  ? -10.278 12.812  2.687   1.00 24.18 ? 51  ILE A CD1 1 
ATOM   318  N N   . LYS A 1 59  ? -5.183  14.048  5.493   1.00 25.34 ? 52  LYS A N   1 
ATOM   319  C CA  . LYS A 1 59  ? -4.023  14.952  5.609   1.00 27.83 ? 52  LYS A CA  1 
ATOM   320  C C   . LYS A 1 59  ? -3.467  15.190  4.204   1.00 25.39 ? 52  LYS A C   1 
ATOM   321  O O   . LYS A 1 59  ? -3.097  14.216  3.563   1.00 25.22 ? 52  LYS A O   1 
ATOM   322  C CB  . LYS A 1 59  ? -2.903  14.375  6.484   1.00 31.72 ? 52  LYS A CB  1 
ATOM   323  C CG  . LYS A 1 59  ? -3.324  13.939  7.885   1.00 40.68 ? 52  LYS A CG  1 
ATOM   324  C CD  . LYS A 1 59  ? -2.154  13.512  8.769   1.00 43.02 ? 52  LYS A CD  1 
ATOM   325  C CE  . LYS A 1 59  ? -1.342  12.367  8.193   1.00 51.03 ? 52  LYS A CE  1 
ATOM   326  N NZ  . LYS A 1 59  ? -0.411  11.788  9.197   1.00 53.28 ? 52  LYS A NZ  1 
ATOM   327  N N   . LYS A 1 60  ? -3.327  16.451  3.818   1.00 27.18 ? 53  LYS A N   1 
ATOM   328  C CA  . LYS A 1 60  ? -2.690  16.831  2.533   1.00 29.76 ? 53  LYS A CA  1 
ATOM   329  C C   . LYS A 1 60  ? -1.212  17.073  2.788   1.00 28.19 ? 53  LYS A C   1 
ATOM   330  O O   . LYS A 1 60  ? -0.886  17.825  3.722   1.00 35.92 ? 53  LYS A O   1 
ATOM   331  C CB  . LYS A 1 60  ? -3.338  18.088  1.945   1.00 31.66 ? 53  LYS A CB  1 
ATOM   332  C CG  . LYS A 1 60  ? -2.622  18.623  0.717   1.00 33.04 ? 53  LYS A CG  1 
ATOM   333  C CD  . LYS A 1 60  ? -3.155  19.948  0.242   1.00 36.33 ? 53  LYS A CD  1 
ATOM   334  C CE  . LYS A 1 60  ? -2.443  20.394  -1.018  1.00 41.51 ? 53  LYS A CE  1 
ATOM   335  N NZ  . LYS A 1 60  ? -2.938  21.714  -1.485  1.00 42.16 ? 53  LYS A NZ  1 
ATOM   336  N N   . ILE A 1 61  ? -0.345  16.384  2.064   1.00 27.27 ? 54  ILE A N   1 
ATOM   337  C CA  . ILE A 1 61  ? 1.128   16.470  2.249   1.00 26.69 ? 54  ILE A CA  1 
ATOM   338  C C   . ILE A 1 61  ? 1.768   16.976  0.966   1.00 28.24 ? 54  ILE A C   1 
ATOM   339  O O   . ILE A 1 61  ? 1.544   16.360  -0.087  1.00 27.46 ? 54  ILE A O   1 
ATOM   340  C CB  . ILE A 1 61  ? 1.717   15.105  2.643   1.00 30.01 ? 54  ILE A CB  1 
ATOM   341  C CG1 . ILE A 1 61  ? 1.052   14.536  3.896   1.00 31.64 ? 54  ILE A CG1 1 
ATOM   342  C CG2 . ILE A 1 61  ? 3.222   15.209  2.819   1.00 34.12 ? 54  ILE A CG2 1 
ATOM   343  C CD1 . ILE A 1 61  ? 1.603   13.193  4.292   1.00 32.94 ? 54  ILE A CD1 1 
ATOM   344  N N   . SER A 1 62  ? 2.638   17.980  1.086   1.00 28.36 ? 55  SER A N   1 
ATOM   345  C CA  . SER A 1 62  ? 3.390   18.565  -0.046  1.00 30.15 ? 55  SER A CA  1 
ATOM   346  C C   . SER A 1 62  ? 4.873   18.571  0.284   1.00 30.29 ? 55  SER A C   1 
ATOM   347  O O   . SER A 1 62  ? 5.441   19.606  0.615   1.00 35.03 ? 55  SER A O   1 
ATOM   348  C CB  . SER A 1 62  ? 2.819   19.929  -0.364  1.00 31.46 ? 55  SER A CB  1 
ATOM   349  O OG  . SER A 1 62  ? 1.394   19.869  -0.376  1.00 35.19 ? 55  SER A OG  1 
ATOM   350  N N   . PRO A 1 63  ? 5.575   17.418  0.210   1.00 28.84 ? 56  PRO A N   1 
ATOM   351  C CA  . PRO A 1 63  ? 6.982   17.355  0.606   1.00 27.76 ? 56  PRO A CA  1 
ATOM   352  C C   . PRO A 1 63  ? 8.074   17.393  -0.477  1.00 27.58 ? 56  PRO A C   1 
ATOM   353  O O   . PRO A 1 63  ? 9.208   17.439  -0.115  1.00 30.72 ? 56  PRO A O   1 
ATOM   354  C CB  . PRO A 1 63  ? 6.937   15.963  1.250   1.00 28.81 ? 56  PRO A CB  1 
ATOM   355  C CG  . PRO A 1 63  ? 6.127   15.164  0.228   1.00 28.87 ? 56  PRO A CG  1 
ATOM   356  C CD  . PRO A 1 63  ? 5.043   16.114  -0.200  1.00 27.32 ? 56  PRO A CD  1 
ATOM   357  N N   . PHE A 1 64  ? 7.753   17.449  -1.773  1.00 23.90 ? 57  PHE A N   1 
ATOM   358  C CA  . PHE A 1 64  ? 8.673   16.991  -2.841  1.00 26.85 ? 57  PHE A CA  1 
ATOM   359  C C   . PHE A 1 64  ? 9.799   18.016  -3.096  1.00 29.38 ? 57  PHE A C   1 
ATOM   360  O O   . PHE A 1 64  ? 10.812  17.609  -3.722  1.00 32.18 ? 57  PHE A O   1 
ATOM   361  C CB  . PHE A 1 64  ? 7.864   16.634  -4.090  1.00 27.28 ? 57  PHE A CB  1 
ATOM   362  C CG  . PHE A 1 64  ? 6.875   15.524  -3.845  1.00 23.85 ? 57  PHE A CG  1 
ATOM   363  C CD1 . PHE A 1 64  ? 7.326   14.277  -3.450  1.00 23.04 ? 57  PHE A CD1 1 
ATOM   364  C CD2 . PHE A 1 64  ? 5.510   15.721  -4.011  1.00 24.73 ? 57  PHE A CD2 1 
ATOM   365  C CE1 . PHE A 1 64  ? 6.440   13.237  -3.240  1.00 24.25 ? 57  PHE A CE1 1 
ATOM   366  C CE2 . PHE A 1 64  ? 4.624   14.677  -3.780  1.00 22.36 ? 57  PHE A CE2 1 
ATOM   367  C CZ  . PHE A 1 64  ? 5.093   13.442  -3.404  1.00 22.30 ? 57  PHE A CZ  1 
ATOM   368  N N   . GLU A 1 65  ? 9.692   19.222  -2.521  1.00 33.70 ? 58  GLU A N   1 
ATOM   369  C CA  . GLU A 1 65  ? 10.747  20.285  -2.603  1.00 42.08 ? 58  GLU A CA  1 
ATOM   370  C C   . GLU A 1 65  ? 11.959  19.960  -1.709  1.00 46.48 ? 58  GLU A C   1 
ATOM   371  O O   . GLU A 1 65  ? 13.085  20.428  -2.029  1.00 41.85 ? 58  GLU A O   1 
ATOM   372  C CB  . GLU A 1 65  ? 10.219  21.652  -2.159  1.00 42.53 ? 58  GLU A CB  1 
ATOM   373  C CG  . GLU A 1 65  ? 8.904   22.058  -2.776  1.00 46.63 ? 58  GLU A CG  1 
ATOM   374  C CD  . GLU A 1 65  ? 8.921   22.294  -4.274  1.00 51.75 ? 58  GLU A CD  1 
ATOM   375  O OE1 . GLU A 1 65  ? 9.664   21.586  -4.983  1.00 52.85 ? 58  GLU A OE1 1 
ATOM   376  O OE2 . GLU A 1 65  ? 8.172   23.181  -4.725  1.00 58.90 ? 58  GLU A OE2 1 
ATOM   377  N N   . HIS A 1 66  ? 11.757  19.249  -0.594  1.00 43.91 ? 59  HIS A N   1 
ATOM   378  C CA  . HIS A 1 66  ? 12.773  19.108  0.489   1.00 45.77 ? 59  HIS A CA  1 
ATOM   379  C C   . HIS A 1 66  ? 13.088  17.639  0.752   1.00 44.33 ? 59  HIS A C   1 
ATOM   380  O O   . HIS A 1 66  ? 12.136  16.861  1.052   1.00 38.52 ? 59  HIS A O   1 
ATOM   381  C CB  . HIS A 1 66  ? 12.289  19.823  1.751   1.00 46.68 ? 59  HIS A CB  1 
ATOM   382  C CG  . HIS A 1 66  ? 12.267  21.297  1.564   1.00 55.38 ? 59  HIS A CG  1 
ATOM   383  N ND1 . HIS A 1 66  ? 11.098  22.032  1.613   1.00 57.51 ? 59  HIS A ND1 1 
ATOM   384  C CD2 . HIS A 1 66  ? 13.259  22.162  1.258   1.00 54.02 ? 59  HIS A CD2 1 
ATOM   385  C CE1 . HIS A 1 66  ? 11.374  23.296  1.362   1.00 53.67 ? 59  HIS A CE1 1 
ATOM   386  N NE2 . HIS A 1 66  ? 12.691  23.399  1.147   1.00 56.48 ? 59  HIS A NE2 1 
ATOM   387  N N   . GLN A 1 67  ? 14.370  17.291  0.658   1.00 40.49 ? 60  GLN A N   1 
ATOM   388  C CA  . GLN A 1 67  ? 14.884  15.927  0.900   1.00 40.59 ? 60  GLN A CA  1 
ATOM   389  C C   . GLN A 1 67  ? 14.310  15.453  2.243   1.00 38.61 ? 60  GLN A C   1 
ATOM   390  O O   . GLN A 1 67  ? 13.880  14.277  2.310   1.00 32.93 ? 60  GLN A O   1 
ATOM   391  C CB  . GLN A 1 67  ? 16.416  15.937  0.802   1.00 41.09 ? 60  GLN A CB  1 
ATOM   392  C CG  . GLN A 1 67  ? 17.051  14.579  0.509   1.00 44.66 ? 60  GLN A CG  1 
ATOM   393  C CD  . GLN A 1 67  ? 17.257  13.721  1.735   1.00 44.76 ? 60  GLN A CD  1 
ATOM   394  O OE1 . GLN A 1 67  ? 17.569  12.536  1.652   1.00 50.04 ? 60  GLN A OE1 1 
ATOM   395  N NE2 . GLN A 1 67  ? 17.096  14.312  2.908   1.00 49.32 ? 60  GLN A NE2 1 
ATOM   396  N N   . THR A 1 68  ? 14.292  16.330  3.260   1.00 36.82 ? 61  THR A N   1 
ATOM   397  C CA  . THR A 1 68  ? 13.920  15.991  4.661   1.00 36.70 ? 61  THR A CA  1 
ATOM   398  C C   . THR A 1 68  ? 12.440  15.623  4.726   1.00 34.54 ? 61  THR A C   1 
ATOM   399  O O   . THR A 1 68  ? 12.115  14.598  5.397   1.00 31.69 ? 61  THR A O   1 
ATOM   400  C CB  . THR A 1 68  ? 14.204  17.128  5.657   1.00 41.62 ? 61  THR A CB  1 
ATOM   401  O OG1 . THR A 1 68  ? 15.620  17.266  5.725   1.00 43.77 ? 61  THR A OG1 1 
ATOM   402  C CG2 . THR A 1 68  ? 13.699  16.854  7.060   1.00 40.70 ? 61  THR A CG2 1 
ATOM   403  N N   . TYR A 1 69  ? 11.598  16.459  4.118   1.00 32.74 ? 62  TYR A N   1 
ATOM   404  C CA  . TYR A 1 69  ? 10.125  16.281  4.054   1.00 35.23 ? 62  TYR A CA  1 
ATOM   405  C C   . TYR A 1 69  ? 9.813   14.984  3.313   1.00 29.66 ? 62  TYR A C   1 
ATOM   406  O O   . TYR A 1 69  ? 8.919   14.242  3.770   1.00 29.19 ? 62  TYR A O   1 
ATOM   407  C CB  . TYR A 1 69  ? 9.438   17.437  3.329   1.00 40.47 ? 62  TYR A CB  1 
ATOM   408  C CG  . TYR A 1 69  ? 9.425   18.751  4.068   1.00 49.90 ? 62  TYR A CG  1 
ATOM   409  C CD1 . TYR A 1 69  ? 10.293  19.000  5.124   1.00 55.42 ? 62  TYR A CD1 1 
ATOM   410  C CD2 . TYR A 1 69  ? 8.554   19.762  3.688   1.00 54.54 ? 62  TYR A CD2 1 
ATOM   411  C CE1 . TYR A 1 69  ? 10.278  20.209  5.797   1.00 54.84 ? 62  TYR A CE1 1 
ATOM   412  C CE2 . TYR A 1 69  ? 8.533   20.982  4.347   1.00 58.07 ? 62  TYR A CE2 1 
ATOM   413  C CZ  . TYR A 1 69  ? 9.394   21.200  5.410   1.00 57.42 ? 62  TYR A CZ  1 
ATOM   414  O OH  . TYR A 1 69  ? 9.385   22.389  6.075   1.00 57.80 ? 62  TYR A OH  1 
ATOM   415  N N   . CYS A 1 70  ? 10.518  14.729  2.213   1.00 29.50 ? 63  CYS A N   1 
ATOM   416  C CA  . CYS A 1 70  ? 10.413  13.462  1.440   1.00 28.63 ? 63  CYS A CA  1 
ATOM   417  C C   . CYS A 1 70  ? 10.771  12.247  2.298   1.00 28.17 ? 63  CYS A C   1 
ATOM   418  O O   . CYS A 1 70  ? 10.073  11.232  2.215   1.00 24.25 ? 63  CYS A O   1 
ATOM   419  C CB  . CYS A 1 70  ? 11.332  13.448  0.235   1.00 31.77 ? 63  CYS A CB  1 
ATOM   420  S SG  . CYS A 1 70  ? 10.670  14.439  -1.116  1.00 31.37 ? 63  CYS A SG  1 
ATOM   421  N N   . GLN A 1 71  ? 11.899  12.295  3.011   1.00 26.75 ? 64  GLN A N   1 
ATOM   422  C CA  . GLN A 1 71  ? 12.345  11.181  3.874   1.00 27.61 ? 64  GLN A CA  1 
ATOM   423  C C   . GLN A 1 71  ? 11.284  10.863  4.935   1.00 23.33 ? 64  GLN A C   1 
ATOM   424  O O   . GLN A 1 71  ? 10.961  9.680   5.121   1.00 24.05 ? 64  GLN A O   1 
ATOM   425  C CB  . GLN A 1 71  ? 13.628  11.570  4.606   1.00 35.05 ? 64  GLN A CB  1 
ATOM   426  C CG  . GLN A 1 71  ? 14.884  11.054  3.952   1.00 41.96 ? 64  GLN A CG  1 
ATOM   427  C CD  . GLN A 1 71  ? 16.027  11.255  4.918   1.00 50.45 ? 64  GLN A CD  1 
ATOM   428  O OE1 . GLN A 1 71  ? 16.538  10.305  5.514   1.00 60.01 ? 64  GLN A OE1 1 
ATOM   429  N NE2 . GLN A 1 71  ? 16.377  12.514  5.136   1.00 47.82 ? 64  GLN A NE2 1 
ATOM   430  N N   . ARG A 1 72  ? 10.787  11.877  5.625   1.00 23.22 ? 65  ARG A N   1 
ATOM   431  C CA  . ARG A 1 72  ? 9.851   11.668  6.757   1.00 27.69 ? 65  ARG A CA  1 
ATOM   432  C C   . ARG A 1 72  ? 8.532   11.122  6.210   1.00 25.71 ? 65  ARG A C   1 
ATOM   433  O O   . ARG A 1 72  ? 7.943   10.197  6.805   1.00 23.15 ? 65  ARG A O   1 
ATOM   434  C CB  . ARG A 1 72  ? 9.623   12.969  7.530   1.00 29.42 ? 65  ARG A CB  1 
ATOM   435  C CG  . ARG A 1 72  ? 10.882  13.436  8.249   1.00 34.32 ? 65  ARG A CG  1 
ATOM   436  C CD  . ARG A 1 72  ? 10.629  14.621  9.152   1.00 35.36 ? 65  ARG A CD  1 
ATOM   437  N NE  . ARG A 1 72  ? 11.889  15.093  9.735   1.00 40.41 ? 65  ARG A NE  1 
ATOM   438  C CZ  . ARG A 1 72  ? 12.031  16.250  10.380  1.00 41.99 ? 65  ARG A CZ  1 
ATOM   439  N NH1 . ARG A 1 72  ? 10.994  17.054  10.535  1.00 41.16 ? 65  ARG A NH1 1 
ATOM   440  N NH2 . ARG A 1 72  ? 13.207  16.592  10.885  1.00 46.34 ? 65  ARG A NH2 1 
ATOM   441  N N   . THR A 1 73  ? 8.063   11.673  5.090   1.00 23.09 ? 66  THR A N   1 
ATOM   442  C CA  . THR A 1 73  ? 6.843   11.182  4.389   1.00 21.59 ? 66  THR A CA  1 
ATOM   443  C C   . THR A 1 73  ? 7.028   9.731   3.971   1.00 17.95 ? 66  THR A C   1 
ATOM   444  O O   . THR A 1 73  ? 6.120   8.899   4.253   1.00 17.55 ? 66  THR A O   1 
ATOM   445  C CB  . THR A 1 73  ? 6.522   12.081  3.190   1.00 22.01 ? 66  THR A CB  1 
ATOM   446  O OG1 . THR A 1 73  ? 6.283   13.375  3.719   1.00 21.33 ? 66  THR A OG1 1 
ATOM   447  C CG2 . THR A 1 73  ? 5.314   11.621  2.404   1.00 21.25 ? 66  THR A CG2 1 
ATOM   448  N N   . LEU A 1 74  ? 8.115   9.386   3.294   1.00 17.75 ? 67  LEU A N   1 
ATOM   449  C CA  . LEU A 1 74  ? 8.332   7.998   2.877   1.00 18.41 ? 67  LEU A CA  1 
ATOM   450  C C   . LEU A 1 74  ? 8.409   7.069   4.093   1.00 21.65 ? 67  LEU A C   1 
ATOM   451  O O   . LEU A 1 74  ? 7.747   6.011   4.112   1.00 17.99 ? 67  LEU A O   1 
ATOM   452  C CB  . LEU A 1 74  ? 9.588   7.918   2.021   1.00 20.36 ? 67  LEU A CB  1 
ATOM   453  C CG  . LEU A 1 74  ? 9.894   6.537   1.464   1.00 21.53 ? 67  LEU A CG  1 
ATOM   454  C CD1 . LEU A 1 74  ? 8.719   5.973   0.660   1.00 21.32 ? 67  LEU A CD1 1 
ATOM   455  C CD2 . LEU A 1 74  ? 11.153  6.609   0.606   1.00 23.92 ? 67  LEU A CD2 1 
ATOM   456  N N   . ARG A 1 75  ? 9.164   7.453   5.131   1.00 23.86 ? 68  ARG A N   1 
ATOM   457  C CA  . ARG A 1 75  ? 9.289   6.600   6.346   1.00 25.31 ? 68  ARG A CA  1 
ATOM   458  C C   . ARG A 1 75  ? 7.901   6.308   6.906   1.00 22.42 ? 68  ARG A C   1 
ATOM   459  O O   . ARG A 1 75  ? 7.581   5.115   7.145   1.00 23.84 ? 68  ARG A O   1 
ATOM   460  C CB  . ARG A 1 75  ? 10.102  7.369   7.397   1.00 29.78 ? 68  ARG A CB  1 
ATOM   461  C CG  . ARG A 1 75  ? 11.319  6.672   7.939   1.00 35.06 ? 68  ARG A CG  1 
ATOM   462  C CD  . ARG A 1 75  ? 12.024  7.681   8.841   1.00 32.07 ? 68  ARG A CD  1 
ATOM   463  N NE  . ARG A 1 75  ? 13.266  8.163   8.271   1.00 30.19 ? 68  ARG A NE  1 
ATOM   464  C CZ  . ARG A 1 75  ? 14.316  7.375   8.035   1.00 38.04 ? 68  ARG A CZ  1 
ATOM   465  N NH1 . ARG A 1 75  ? 14.271  6.083   8.328   1.00 43.89 ? 68  ARG A NH1 1 
ATOM   466  N NH2 . ARG A 1 75  ? 15.425  7.884   7.532   1.00 42.33 ? 68  ARG A NH2 1 
ATOM   467  N N   . GLU A 1 76  ? 7.103   7.351   7.098   1.00 20.44 ? 69  GLU A N   1 
ATOM   468  C CA  . GLU A 1 76  ? 5.765   7.257   7.682   1.00 24.00 ? 69  GLU A CA  1 
ATOM   469  C C   . GLU A 1 76  ? 4.922   6.348   6.804   1.00 21.79 ? 69  GLU A C   1 
ATOM   470  O O   . GLU A 1 76  ? 4.282   5.415   7.335   1.00 21.31 ? 69  GLU A O   1 
ATOM   471  C CB  . GLU A 1 76  ? 5.136   8.634   7.787   1.00 26.77 ? 69  GLU A CB  1 
ATOM   472  C CG  . GLU A 1 76  ? 3.726   8.601   8.283   1.00 32.02 ? 69  GLU A CG  1 
ATOM   473  C CD  . GLU A 1 76  ? 3.613   9.476   9.504   1.00 36.48 ? 69  GLU A CD  1 
ATOM   474  O OE1 . GLU A 1 76  ? 4.272   10.539  9.543   1.00 44.73 ? 69  GLU A OE1 1 
ATOM   475  O OE2 . GLU A 1 76  ? 2.959   9.062   10.412  1.00 36.11 ? 69  GLU A OE2 1 
ATOM   476  N N   . ILE A 1 77  ? 4.935   6.556   5.485   1.00 19.25 ? 70  ILE A N   1 
ATOM   477  C CA  . ILE A 1 77  ? 4.047   5.732   4.619   1.00 18.85 ? 70  ILE A CA  1 
ATOM   478  C C   . ILE A 1 77  ? 4.468   4.259   4.662   1.00 16.36 ? 70  ILE A C   1 
ATOM   479  O O   . ILE A 1 77  ? 3.590   3.412   4.820   1.00 17.03 ? 70  ILE A O   1 
ATOM   480  C CB  . ILE A 1 77  ? 4.000   6.295   3.167   1.00 18.64 ? 70  ILE A CB  1 
ATOM   481  C CG1 . ILE A 1 77  ? 3.301   7.658   3.124   1.00 21.45 ? 70  ILE A CG1 1 
ATOM   482  C CG2 . ILE A 1 77  ? 3.352   5.281   2.245   1.00 20.79 ? 70  ILE A CG2 1 
ATOM   483  C CD1 . ILE A 1 77  ? 3.400   8.428   1.802   1.00 21.42 ? 70  ILE A CD1 1 
ATOM   484  N N   . LYS A 1 78  ? 5.753   3.956   4.469   1.00 17.33 ? 71  LYS A N   1 
ATOM   485  C CA  . LYS A 1 78  ? 6.291   2.577   4.483   1.00 19.49 ? 71  LYS A CA  1 
ATOM   486  C C   . LYS A 1 78  ? 5.896   1.897   5.791   1.00 19.20 ? 71  LYS A C   1 
ATOM   487  O O   . LYS A 1 78  ? 5.411   0.745   5.754   1.00 18.36 ? 71  LYS A O   1 
ATOM   488  C CB  . LYS A 1 78  ? 7.810   2.529   4.309   1.00 23.82 ? 71  LYS A CB  1 
ATOM   489  C CG  . LYS A 1 78  ? 8.277   2.828   2.893   1.00 28.53 ? 71  LYS A CG  1 
ATOM   490  C CD  . LYS A 1 78  ? 9.778   2.949   2.762   1.00 33.79 ? 71  LYS A CD  1 
ATOM   491  C CE  . LYS A 1 78  ? 10.476  1.616   2.694   1.00 36.83 ? 71  LYS A CE  1 
ATOM   492  N NZ  . LYS A 1 78  ? 10.069  0.829   1.505   1.00 40.25 ? 71  LYS A NZ  1 
ATOM   493  N N   . ILE A 1 79  ? 6.096   2.574   6.918   1.00 18.98 ? 72  ILE A N   1 
ATOM   494  C CA  . ILE A 1 79  ? 5.810   1.933   8.235   1.00 18.11 ? 72  ILE A CA  1 
ATOM   495  C C   . ILE A 1 79  ? 4.305   1.703   8.405   1.00 16.69 ? 72  ILE A C   1 
ATOM   496  O O   . ILE A 1 79  ? 3.903   0.599   8.735   1.00 18.30 ? 72  ILE A O   1 
ATOM   497  C CB  . ILE A 1 79  ? 6.427   2.779   9.368   1.00 17.59 ? 72  ILE A CB  1 
ATOM   498  C CG1 . ILE A 1 79  ? 7.961   2.744   9.282   1.00 19.31 ? 72  ILE A CG1 1 
ATOM   499  C CG2 . ILE A 1 79  ? 5.919   2.279   10.701  1.00 19.42 ? 72  ILE A CG2 1 
ATOM   500  C CD1 . ILE A 1 79  ? 8.667   3.784   10.118  1.00 20.06 ? 72  ILE A CD1 1 
ATOM   501  N N   . LEU A 1 80  ? 3.479   2.735   8.219   1.00 17.23 ? 73  LEU A N   1 
ATOM   502  C CA  . LEU A 1 80  ? 2.025   2.653   8.458   1.00 17.75 ? 73  LEU A CA  1 
ATOM   503  C C   . LEU A 1 80  ? 1.371   1.659   7.522   1.00 19.19 ? 73  LEU A C   1 
ATOM   504  O O   . LEU A 1 80  ? 0.425   1.011   7.949   1.00 18.10 ? 73  LEU A O   1 
ATOM   505  C CB  . LEU A 1 80  ? 1.393   4.031   8.378   1.00 19.41 ? 73  LEU A CB  1 
ATOM   506  C CG  . LEU A 1 80  ? 1.762   4.941   9.543   1.00 21.08 ? 73  LEU A CG  1 
ATOM   507  C CD1 . LEU A 1 80  ? 1.020   6.243   9.422   1.00 23.33 ? 73  LEU A CD1 1 
ATOM   508  C CD2 . LEU A 1 80  ? 1.546   4.250   10.892  1.00 22.11 ? 73  LEU A CD2 1 
ATOM   509  N N   . LEU A 1 81  ? 1.868   1.518   6.291   1.00 19.19 ? 74  LEU A N   1 
ATOM   510  C CA  . LEU A 1 81  ? 1.291   0.523   5.369   1.00 19.25 ? 74  LEU A CA  1 
ATOM   511  C C   . LEU A 1 81  ? 1.705   -0.876  5.825   1.00 20.92 ? 74  LEU A C   1 
ATOM   512  O O   . LEU A 1 81  ? 0.934   -1.786  5.611   1.00 23.06 ? 74  LEU A O   1 
ATOM   513  C CB  . LEU A 1 81  ? 1.742   0.786   3.932   1.00 18.69 ? 74  LEU A CB  1 
ATOM   514  C CG  . LEU A 1 81  ? 1.148   2.022   3.320   1.00 19.37 ? 74  LEU A CG  1 
ATOM   515  C CD1 . LEU A 1 81  ? 1.661   2.227   1.883   1.00 22.47 ? 74  LEU A CD1 1 
ATOM   516  C CD2 . LEU A 1 81  ? -0.362  1.956   3.335   1.00 20.36 ? 74  LEU A CD2 1 
ATOM   517  N N   . ARG A 1 82  ? 2.871   -1.053  6.443   1.00 19.33 ? 75  ARG A N   1 
ATOM   518  C CA  . ARG A 1 82  ? 3.325   -2.412  6.815   1.00 21.71 ? 75  ARG A CA  1 
ATOM   519  C C   . ARG A 1 82  ? 2.643   -2.835  8.128   1.00 21.68 ? 75  ARG A C   1 
ATOM   520  O O   . ARG A 1 82  ? 2.272   -3.985  8.303   1.00 23.93 ? 75  ARG A O   1 
ATOM   521  C CB  . ARG A 1 82  ? 4.832   -2.449  7.055   1.00 28.04 ? 75  ARG A CB  1 
ATOM   522  C CG  . ARG A 1 82  ? 5.353   -3.865  7.205   1.00 32.16 ? 75  ARG A CG  1 
ATOM   523  C CD  . ARG A 1 82  ? 6.174   -4.211  5.982   1.00 35.77 ? 75  ARG A CD  1 
ATOM   524  N NE  . ARG A 1 82  ? 7.385   -4.662  6.577   1.00 39.08 ? 75  ARG A NE  1 
ATOM   525  C CZ  . ARG A 1 82  ? 8.593   -4.568  6.093   1.00 33.65 ? 75  ARG A CZ  1 
ATOM   526  N NH1 . ARG A 1 82  ? 8.845   -4.049  4.903   1.00 32.06 ? 75  ARG A NH1 1 
ATOM   527  N NH2 . ARG A 1 82  ? 9.560   -5.073  6.817   1.00 35.41 ? 75  ARG A NH2 1 
ATOM   528  N N   . PHE A 1 83  ? 2.385   -1.893  8.989   1.00 19.02 ? 76  PHE A N   1 
ATOM   529  C CA  . PHE A 1 83  ? 1.819   -2.163  10.331  1.00 18.11 ? 76  PHE A CA  1 
ATOM   530  C C   . PHE A 1 83  ? 0.320   -2.376  10.217  1.00 20.30 ? 76  PHE A C   1 
ATOM   531  O O   . PHE A 1 83  ? -0.393  -1.691  9.445   1.00 18.90 ? 76  PHE A O   1 
ATOM   532  C CB  . PHE A 1 83  ? 2.103   -0.979  11.245  1.00 17.63 ? 76  PHE A CB  1 
ATOM   533  C CG  . PHE A 1 83  ? 3.507   -0.874  11.772  1.00 16.39 ? 76  PHE A CG  1 
ATOM   534  C CD1 . PHE A 1 83  ? 4.498   -1.761  11.390  1.00 17.31 ? 76  PHE A CD1 1 
ATOM   535  C CD2 . PHE A 1 83  ? 3.822   0.126   12.689  1.00 18.21 ? 76  PHE A CD2 1 
ATOM   536  C CE1 . PHE A 1 83  ? 5.788   -1.638  11.886  1.00 18.99 ? 76  PHE A CE1 1 
ATOM   537  C CE2 . PHE A 1 83  ? 5.098   0.204   13.229  1.00 18.50 ? 76  PHE A CE2 1 
ATOM   538  C CZ  . PHE A 1 83  ? 6.077   -0.677  12.823  1.00 17.73 ? 76  PHE A CZ  1 
ATOM   539  N N   . ARG A 1 84  ? -0.185  -3.296  11.020  1.00 17.55 ? 77  ARG A N   1 
ATOM   540  C CA  . ARG A 1 84  ? -1.627  -3.471  11.176  1.00 19.18 ? 77  ARG A CA  1 
ATOM   541  C C   . ARG A 1 84  ? -1.905  -3.767  12.643  1.00 16.81 ? 77  ARG A C   1 
ATOM   542  O O   . ARG A 1 84  ? -1.620  -4.878  13.102  1.00 18.51 ? 77  ARG A O   1 
ATOM   543  C CB  . ARG A 1 84  ? -2.141  -4.592  10.273  1.00 24.49 ? 77  ARG A CB  1 
ATOM   544  C CG  . ARG A 1 84  ? -3.653  -4.712  10.291  1.00 33.15 ? 77  ARG A CG  1 
ATOM   545  C CD  . ARG A 1 84  ? -4.110  -5.761  9.278   1.00 41.03 ? 77  ARG A CD  1 
ATOM   546  N NE  . ARG A 1 84  ? -5.565  -5.739  9.169   1.00 53.82 ? 77  ARG A NE  1 
ATOM   547  C CZ  . ARG A 1 84  ? -6.274  -5.102  8.231   1.00 61.02 ? 77  ARG A CZ  1 
ATOM   548  N NH1 . ARG A 1 84  ? -5.676  -4.434  7.255   1.00 63.37 ? 77  ARG A NH1 1 
ATOM   549  N NH2 . ARG A 1 84  ? -7.597  -5.152  8.271   1.00 64.40 ? 77  ARG A NH2 1 
ATOM   550  N N   . HIS A 1 85  ? -2.415  -2.791  13.355  1.00 16.50 ? 78  HIS A N   1 
ATOM   551  C CA  . HIS A 1 85  ? -2.595  -2.916  14.815  1.00 15.68 ? 78  HIS A CA  1 
ATOM   552  C C   . HIS A 1 85  ? -3.689  -1.966  15.288  1.00 15.10 ? 78  HIS A C   1 
ATOM   553  O O   . HIS A 1 85  ? -3.659  -0.818  14.889  1.00 16.30 ? 78  HIS A O   1 
ATOM   554  C CB  . HIS A 1 85  ? -1.262  -2.748  15.537  1.00 14.53 ? 78  HIS A CB  1 
ATOM   555  C CG  . HIS A 1 85  ? -1.375  -3.005  16.996  1.00 14.04 ? 78  HIS A CG  1 
ATOM   556  N ND1 . HIS A 1 85  ? -0.928  -4.178  17.605  1.00 17.08 ? 78  HIS A ND1 1 
ATOM   557  C CD2 . HIS A 1 85  ? -1.838  -2.209  17.958  1.00 12.36 ? 78  HIS A CD2 1 
ATOM   558  C CE1 . HIS A 1 85  ? -1.088  -4.062  18.923  1.00 13.35 ? 78  HIS A CE1 1 
ATOM   559  N NE2 . HIS A 1 85  ? -1.716  -2.849  19.148  1.00 17.76 ? 78  HIS A NE2 1 
ATOM   560  N N   . GLU A 1 86  ? -4.528  -2.419  16.207  1.00 16.91 ? 79  GLU A N   1 
ATOM   561  C CA  . GLU A 1 86  ? -5.633  -1.572  16.744  1.00 17.22 ? 79  GLU A CA  1 
ATOM   562  C C   . GLU A 1 86  ? -5.152  -0.273  17.371  1.00 15.98 ? 79  GLU A C   1 
ATOM   563  O O   . GLU A 1 86  ? -5.939  0.707   17.376  1.00 16.74 ? 79  GLU A O   1 
ATOM   564  C CB  . GLU A 1 86  ? -6.467  -2.295  17.789  1.00 20.39 ? 79  GLU A CB  1 
ATOM   565  C CG  . GLU A 1 86  ? -7.199  -3.464  17.211  1.00 26.50 ? 79  GLU A CG  1 
ATOM   566  C CD  . GLU A 1 86  ? -7.865  -4.322  18.259  1.00 32.63 ? 79  GLU A CD  1 
ATOM   567  O OE1 . GLU A 1 86  ? -7.571  -4.113  19.455  1.00 27.50 ? 79  GLU A OE1 1 
ATOM   568  O OE2 . GLU A 1 86  ? -8.715  -5.180  17.860  1.00 41.15 ? 79  GLU A OE2 1 
ATOM   569  N N   . ASN A 1 87  ? -3.929  -0.214  17.926  1.00 14.72 ? 80  ASN A N   1 
ATOM   570  C CA  . ASN A 1 87  ? -3.442  0.975   18.628  1.00 13.05 ? 80  ASN A CA  1 
ATOM   571  C C   . ASN A 1 87  ? -2.429  1.762   17.807  1.00 12.69 ? 80  ASN A C   1 
ATOM   572  O O   . ASN A 1 87  ? -1.681  2.554   18.384  1.00 12.76 ? 80  ASN A O   1 
ATOM   573  C CB  . ASN A 1 87  ? -2.895  0.614   20.012  1.00 14.13 ? 80  ASN A CB  1 
ATOM   574  C CG  . ASN A 1 87  ? -3.915  -0.130  20.837  1.00 14.89 ? 80  ASN A CG  1 
ATOM   575  O OD1 . ASN A 1 87  ? -3.744  -1.311  21.161  1.00 14.35 ? 80  ASN A OD1 1 
ATOM   576  N ND2 . ASN A 1 87  ? -5.003  0.541   21.190  1.00 17.04 ? 80  ASN A ND2 1 
ATOM   577  N N   . ILE A 1 88  ? -2.438  1.545   16.490  1.00 13.89 ? 81  ILE A N   1 
ATOM   578  C CA  . ILE A 1 88  ? -1.551  2.292   15.574  1.00 15.16 ? 81  ILE A CA  1 
ATOM   579  C C   . ILE A 1 88  ? -2.435  2.798   14.453  1.00 14.91 ? 81  ILE A C   1 
ATOM   580  O O   . ILE A 1 88  ? -3.200  2.009   13.921  1.00 17.30 ? 81  ILE A O   1 
ATOM   581  C CB  . ILE A 1 88  ? -0.407  1.429   15.043  1.00 15.40 ? 81  ILE A CB  1 
ATOM   582  C CG1 . ILE A 1 88  ? 0.424   0.907   16.222  1.00 15.21 ? 81  ILE A CG1 1 
ATOM   583  C CG2 . ILE A 1 88  ? 0.436   2.239   14.077  1.00 15.06 ? 81  ILE A CG2 1 
ATOM   584  C CD1 . ILE A 1 88  ? 1.424   -0.123  15.805  1.00 17.91 ? 81  ILE A CD1 1 
ATOM   585  N N   . ILE A 1 89  ? -2.348  4.083   14.159  1.00 15.42 ? 82  ILE A N   1 
ATOM   586  C CA  . ILE A 1 89  ? -3.254  4.647   13.132  1.00 16.09 ? 82  ILE A CA  1 
ATOM   587  C C   . ILE A 1 89  ? -2.961  3.922   11.811  1.00 16.36 ? 82  ILE A C   1 
ATOM   588  O O   . ILE A 1 89  ? -1.783  3.723   11.454  1.00 16.45 ? 82  ILE A O   1 
ATOM   589  C CB  . ILE A 1 89  ? -3.081  6.166   13.078  1.00 17.18 ? 82  ILE A CB  1 
ATOM   590  C CG1 . ILE A 1 89  ? -4.238  6.810   12.302  1.00 19.49 ? 82  ILE A CG1 1 
ATOM   591  C CG2 . ILE A 1 89  ? -1.755  6.547   12.488  1.00 16.23 ? 82  ILE A CG2 1 
ATOM   592  C CD1 . ILE A 1 89  ? -5.607  6.457   12.790  1.00 20.16 ? 82  ILE A CD1 1 
ATOM   593  N N   . GLY A 1 90  ? -4.010  3.557   11.084  1.00 18.06 ? 83  GLY A N   1 
ATOM   594  C CA  . GLY A 1 90  ? -3.842  2.898   9.783   1.00 19.71 ? 83  GLY A CA  1 
ATOM   595  C C   . GLY A 1 90  ? -3.930  3.933   8.679   1.00 20.42 ? 83  GLY A C   1 
ATOM   596  O O   . GLY A 1 90  ? -4.478  5.043   8.940   1.00 25.96 ? 83  GLY A O   1 
ATOM   597  N N   . ILE A 1 91  ? -3.362  3.637   7.523   1.00 20.95 ? 84  ILE A N   1 
ATOM   598  C CA  . ILE A 1 91  ? -3.693  4.396   6.276   1.00 19.74 ? 84  ILE A CA  1 
ATOM   599  C C   . ILE A 1 91  ? -4.793  3.647   5.535   1.00 20.07 ? 84  ILE A C   1 
ATOM   600  O O   . ILE A 1 91  ? -4.582  2.504   5.166   1.00 22.86 ? 84  ILE A O   1 
ATOM   601  C CB  . ILE A 1 91  ? -2.459  4.622   5.416   1.00 22.46 ? 84  ILE A CB  1 
ATOM   602  C CG1 . ILE A 1 91  ? -1.396  5.450   6.137   1.00 21.83 ? 84  ILE A CG1 1 
ATOM   603  C CG2 . ILE A 1 91  ? -2.857  5.222   4.073   1.00 20.18 ? 84  ILE A CG2 1 
ATOM   604  C CD1 . ILE A 1 91  ? -0.058  5.394   5.415   1.00 22.43 ? 84  ILE A CD1 1 
ATOM   605  N N   . ASN A 1 92  ? -5.945  4.294   5.398   1.00 22.72 ? 85  ASN A N   1 
ATOM   606  C CA  . ASN A 1 92  ? -7.168  3.715   4.781   1.00 22.22 ? 85  ASN A CA  1 
ATOM   607  C C   . ASN A 1 92  ? -7.122  3.921   3.277   1.00 22.32 ? 85  ASN A C   1 
ATOM   608  O O   . ASN A 1 92  ? -7.617  3.052   2.542   1.00 22.79 ? 85  ASN A O   1 
ATOM   609  C CB  . ASN A 1 92  ? -8.430  4.412   5.260   1.00 23.90 ? 85  ASN A CB  1 
ATOM   610  C CG  . ASN A 1 92  ? -8.694  4.297   6.741   1.00 27.42 ? 85  ASN A CG  1 
ATOM   611  O OD1 . ASN A 1 92  ? -9.585  4.959   7.256   1.00 32.82 ? 85  ASN A OD1 1 
ATOM   612  N ND2 . ASN A 1 92  ? -7.951  3.449   7.411   1.00 26.61 ? 85  ASN A ND2 1 
ATOM   613  N N   . ASP A 1 93  ? -6.515  5.025   2.847   1.00 21.72 ? 86  ASP A N   1 
ATOM   614  C CA  . ASP A 1 93  ? -6.437  5.355   1.403   1.00 22.47 ? 86  ASP A CA  1 
ATOM   615  C C   . ASP A 1 93  ? -5.301  6.353   1.219   1.00 21.32 ? 86  ASP A C   1 
ATOM   616  O O   . ASP A 1 93  ? -4.938  7.037   2.181   1.00 19.87 ? 86  ASP A O   1 
ATOM   617  C CB  . ASP A 1 93  ? -7.773  5.947   0.935   1.00 22.29 ? 86  ASP A CB  1 
ATOM   618  C CG  . ASP A 1 93  ? -7.997  5.871   -0.564  1.00 25.20 ? 86  ASP A CG  1 
ATOM   619  O OD1 . ASP A 1 93  ? -7.158  5.269   -1.268  1.00 24.51 ? 86  ASP A OD1 1 
ATOM   620  O OD2 . ASP A 1 93  ? -9.054  6.404   -0.983  1.00 30.07 ? 86  ASP A OD2 1 
ATOM   621  N N   . ILE A 1 94  ? -4.806  6.464   0.004   1.00 20.81 ? 87  ILE A N   1 
ATOM   622  C CA  . ILE A 1 94  ? -3.853  7.536   -0.358  1.00 20.66 ? 87  ILE A CA  1 
ATOM   623  C C   . ILE A 1 94  ? -4.259  8.036   -1.731  1.00 19.89 ? 87  ILE A C   1 
ATOM   624  O O   . ILE A 1 94  ? -4.419  7.197   -2.604  1.00 21.55 ? 87  ILE A O   1 
ATOM   625  C CB  . ILE A 1 94  ? -2.386  7.071   -0.382  1.00 20.49 ? 87  ILE A CB  1 
ATOM   626  C CG1 . ILE A 1 94  ? -1.966  6.464   0.957   1.00 19.90 ? 87  ILE A CG1 1 
ATOM   627  C CG2 . ILE A 1 94  ? -1.496  8.251   -0.742  1.00 20.33 ? 87  ILE A CG2 1 
ATOM   628  C CD1 . ILE A 1 94  ? -0.553  5.987   0.973   1.00 22.30 ? 87  ILE A CD1 1 
ATOM   629  N N   . ILE A 1 95  ? -4.493  9.341   -1.804  1.00 22.01 ? 88  ILE A N   1 
ATOM   630  C CA  . ILE A 1 95  ? -4.945  10.034  -3.041  1.00 23.79 ? 88  ILE A CA  1 
ATOM   631  C C   . ILE A 1 95  ? -3.734  10.773  -3.607  1.00 21.40 ? 88  ILE A C   1 
ATOM   632  O O   . ILE A 1 95  ? -3.106  11.579  -2.898  1.00 20.60 ? 88  ILE A O   1 
ATOM   633  C CB  . ILE A 1 95  ? -6.116  10.984  -2.758  1.00 28.13 ? 88  ILE A CB  1 
ATOM   634  C CG1 . ILE A 1 95  ? -7.230  10.289  -1.977  1.00 34.48 ? 88  ILE A CG1 1 
ATOM   635  C CG2 . ILE A 1 95  ? -6.645  11.597  -4.065  1.00 30.69 ? 88  ILE A CG2 1 
ATOM   636  C CD1 . ILE A 1 95  ? -7.990  11.238  -1.067  1.00 37.49 ? 88  ILE A CD1 1 
ATOM   637  N N   . ARG A 1 96  ? -3.420  10.524  -4.871  1.00 20.41 ? 89  ARG A N   1 
ATOM   638  C CA  . ARG A 1 96  ? -2.363  11.270  -5.564  1.00 19.95 ? 89  ARG A CA  1 
ATOM   639  C C   . ARG A 1 96  ? -2.648  11.118  -7.050  1.00 19.09 ? 89  ARG A C   1 
ATOM   640  O O   . ARG A 1 96  ? -3.474  10.255  -7.451  1.00 17.93 ? 89  ARG A O   1 
ATOM   641  C CB  . ARG A 1 96  ? -0.923  10.832  -5.212  1.00 20.30 ? 89  ARG A CB  1 
ATOM   642  C CG  . ARG A 1 96  ? -0.695  9.337   -5.007  1.00 25.33 ? 89  ARG A CG  1 
ATOM   643  C CD  . ARG A 1 96  ? 0.560   8.502   -5.347  1.00 32.02 ? 89  ARG A CD  1 
ATOM   644  N NE  . ARG A 1 96  ? 0.189   8.010   -6.619  1.00 27.97 ? 89  ARG A NE  1 
ATOM   645  C CZ  . ARG A 1 96  ? 0.431   6.971   -7.435  1.00 23.33 ? 89  ARG A CZ  1 
ATOM   646  N NH1 . ARG A 1 96  ? 1.212   5.901   -7.355  1.00 20.98 ? 89  ARG A NH1 1 
ATOM   647  N NH2 . ARG A 1 96  ? -0.262  7.134   -8.539  1.00 19.84 ? 89  ARG A NH2 1 
ATOM   648  N N   . ALA A 1 97  ? -2.064  12.016  -7.803  1.00 21.33 ? 90  ALA A N   1 
ATOM   649  C CA  . ALA A 1 97  ? -2.133  12.001  -9.272  1.00 20.19 ? 90  ALA A CA  1 
ATOM   650  C C   . ALA A 1 97  ? -1.685  10.656  -9.805  1.00 19.79 ? 90  ALA A C   1 
ATOM   651  O O   . ALA A 1 97  ? -0.850  9.949   -9.251  1.00 19.56 ? 90  ALA A O   1 
ATOM   652  C CB  . ALA A 1 97  ? -1.231  13.079  -9.810  1.00 20.45 ? 90  ALA A CB  1 
ATOM   653  N N   . PRO A 1 98  ? -2.099  10.293  -11.036 1.00 18.90 ? 91  PRO A N   1 
ATOM   654  C CA  . PRO A 1 98  ? -1.693  9.006   -11.611 1.00 17.89 ? 91  PRO A CA  1 
ATOM   655  C C   . PRO A 1 98  ? -0.263  8.929   -12.156 1.00 16.77 ? 91  PRO A C   1 
ATOM   656  O O   . PRO A 1 98  ? 0.180   7.862   -12.490 1.00 19.98 ? 91  PRO A O   1 
ATOM   657  C CB  . PRO A 1 98  ? -2.697  8.823   -12.780 1.00 19.16 ? 91  PRO A CB  1 
ATOM   658  C CG  . PRO A 1 98  ? -3.057  10.253  -13.119 1.00 19.27 ? 91  PRO A CG  1 
ATOM   659  C CD  . PRO A 1 98  ? -3.112  11.003  -11.813 1.00 18.91 ? 91  PRO A CD  1 
ATOM   660  N N   . THR A 1 99  ? 0.435   10.045  -12.244 1.00 18.02 ? 92  THR A N   1 
ATOM   661  C CA  . THR A 1 99  ? 1.814   10.087  -12.773 1.00 20.22 ? 92  THR A CA  1 
ATOM   662  C C   . THR A 1 99  ? 2.698   10.852  -11.802 1.00 18.93 ? 92  THR A C   1 
ATOM   663  O O   . THR A 1 99  ? 2.182   11.730  -11.107 1.00 19.15 ? 92  THR A O   1 
ATOM   664  C CB  . THR A 1 99  ? 1.834   10.727  -14.159 1.00 23.26 ? 92  THR A CB  1 
ATOM   665  O OG1 . THR A 1 99  ? 1.447   12.098  -14.051 1.00 21.89 ? 92  THR A OG1 1 
ATOM   666  C CG2 . THR A 1 99  ? 0.866   10.018  -15.069 1.00 23.96 ? 92  THR A CG2 1 
ATOM   667  N N   . ILE A 1 100 ? 3.976   10.519  -11.784 1.00 19.42 ? 93  ILE A N   1 
ATOM   668  C CA  . ILE A 1 100 ? 4.984   11.247  -10.968 1.00 24.60 ? 93  ILE A CA  1 
ATOM   669  C C   . ILE A 1 100 ? 4.970   12.707  -11.382 1.00 26.48 ? 93  ILE A C   1 
ATOM   670  O O   . ILE A 1 100 ? 4.997   13.597  -10.494 1.00 24.92 ? 93  ILE A O   1 
ATOM   671  C CB  . ILE A 1 100 ? 6.394   10.659  -11.099 1.00 29.72 ? 93  ILE A CB  1 
ATOM   672  C CG1 . ILE A 1 100 ? 6.551   9.387   -10.265 1.00 33.86 ? 93  ILE A CG1 1 
ATOM   673  C CG2 . ILE A 1 100 ? 7.423   11.720  -10.717 1.00 34.24 ? 93  ILE A CG2 1 
ATOM   674  C CD1 . ILE A 1 100 ? 7.974   8.884   -10.140 1.00 34.86 ? 93  ILE A CD1 1 
ATOM   675  N N   . GLU A 1 101 ? 4.881   12.949  -12.695 1.00 27.58 ? 94  GLU A N   1 
ATOM   676  C CA  . GLU A 1 101 ? 4.955   14.329  -13.225 1.00 29.24 ? 94  GLU A CA  1 
ATOM   677  C C   . GLU A 1 101 ? 3.813   15.139  -12.625 1.00 27.75 ? 94  GLU A C   1 
ATOM   678  O O   . GLU A 1 101 ? 4.007   16.333  -12.323 1.00 29.05 ? 94  GLU A O   1 
ATOM   679  C CB  . GLU A 1 101 ? 4.853   14.334  -14.751 1.00 31.25 ? 94  GLU A CB  1 
ATOM   680  C CG  . GLU A 1 101 ? 6.046   13.763  -15.452 1.00 33.79 ? 94  GLU A CG  1 
ATOM   681  C CD  . GLU A 1 101 ? 6.035   12.269  -15.706 1.00 35.78 ? 94  GLU A CD  1 
ATOM   682  O OE1 . GLU A 1 101 ? 5.209   11.556  -15.103 1.00 34.40 ? 94  GLU A OE1 1 
ATOM   683  O OE2 . GLU A 1 101 ? 6.862   11.826  -16.511 1.00 35.58 ? 94  GLU A OE2 1 
ATOM   684  N N   . GLN A 1 102 ? 2.614   14.550  -12.502 1.00 21.08 ? 95  GLN A N   1 
ATOM   685  C CA  . GLN A 1 102 ? 1.435   15.336  -12.084 1.00 18.87 ? 95  GLN A CA  1 
ATOM   686  C C   . GLN A 1 102 ? 1.322   15.305  -10.551 1.00 17.17 ? 95  GLN A C   1 
ATOM   687  O O   . GLN A 1 102 ? 0.451   15.983  -10.057 1.00 20.78 ? 95  GLN A O   1 
ATOM   688  C CB  . GLN A 1 102 ? 0.139   14.817  -12.721 1.00 19.69 ? 95  GLN A CB  1 
ATOM   689  C CG  . GLN A 1 102 ? 0.099   15.013  -14.229 1.00 19.29 ? 95  GLN A CG  1 
ATOM   690  C CD  . GLN A 1 102 ? -1.007  14.182  -14.826 1.00 22.16 ? 95  GLN A CD  1 
ATOM   691  O OE1 . GLN A 1 102 ? -0.939  12.955  -14.896 1.00 21.28 ? 95  GLN A OE1 1 
ATOM   692  N NE2 . GLN A 1 102 ? -2.054  14.852  -15.263 1.00 22.81 ? 95  GLN A NE2 1 
ATOM   693  N N   . MET A 1 103 ? 2.139   14.503  -9.871  1.00 20.28 ? 96  MET A N   1 
ATOM   694  C CA  . MET A 1 103 ? 1.966   14.343  -8.389  1.00 19.83 ? 96  MET A CA  1 
ATOM   695  C C   . MET A 1 103 ? 2.693   15.509  -7.698  1.00 19.33 ? 96  MET A C   1 
ATOM   696  O O   . MET A 1 103 ? 3.907   15.497  -7.707  1.00 23.06 ? 96  MET A O   1 
ATOM   697  C CB  . MET A 1 103 ? 2.508   13.004  -7.882  1.00 22.19 ? 96  MET A CB  1 
ATOM   698  C CG  . MET A 1 103 ? 2.416   12.880  -6.341  1.00 19.40 ? 96  MET A CG  1 
ATOM   699  S SD  . MET A 1 103 ? 2.928   11.255  -5.838  1.00 21.19 ? 96  MET A SD  1 
ATOM   700  C CE  . MET A 1 103 ? 4.680   11.322  -6.220  1.00 21.28 ? 96  MET A CE  1 
ATOM   701  N N   . LYS A 1 104 ? 1.966   16.480  -7.168  1.00 22.06 ? 97  LYS A N   1 
ATOM   702  C CA  . LYS A 1 104 ? 2.569   17.633  -6.442  1.00 26.82 ? 97  LYS A CA  1 
ATOM   703  C C   . LYS A 1 104 ? 2.310   17.482  -4.945  1.00 27.74 ? 97  LYS A C   1 
ATOM   704  O O   . LYS A 1 104 ? 2.959   18.172  -4.173  1.00 31.88 ? 97  LYS A O   1 
ATOM   705  C CB  . LYS A 1 104 ? 1.957   18.964  -6.892  1.00 32.60 ? 97  LYS A CB  1 
ATOM   706  C CG  . LYS A 1 104 ? 1.996   19.241  -8.393  1.00 37.15 ? 97  LYS A CG  1 
ATOM   707  C CD  . LYS A 1 104 ? 3.238   18.753  -9.098  1.00 40.73 ? 97  LYS A CD  1 
ATOM   708  C CE  . LYS A 1 104 ? 3.220   19.071  -10.580 1.00 42.37 ? 97  LYS A CE  1 
ATOM   709  N NZ  . LYS A 1 104 ? 3.124   20.531  -10.798 1.00 47.70 ? 97  LYS A NZ  1 
ATOM   710  N N   . ASP A 1 105 ? 1.368   16.624  -4.585  1.00 24.92 ? 98  ASP A N   1 
ATOM   711  C CA  . ASP A 1 105 ? 0.765   16.500  -3.230  1.00 24.98 ? 98  ASP A CA  1 
ATOM   712  C C   . ASP A 1 105 ? 0.302   15.062  -3.068  1.00 24.00 ? 98  ASP A C   1 
ATOM   713  O O   . ASP A 1 105 ? 0.089   14.362  -4.083  1.00 22.30 ? 98  ASP A O   1 
ATOM   714  C CB  . ASP A 1 105 ? -0.477  17.359  -2.989  1.00 26.35 ? 98  ASP A CB  1 
ATOM   715  C CG  . ASP A 1 105 ? -0.363  18.802  -3.445  1.00 32.87 ? 98  ASP A CG  1 
ATOM   716  O OD1 . ASP A 1 105 ? 0.289   19.575  -2.750  1.00 32.36 ? 98  ASP A OD1 1 
ATOM   717  O OD2 . ASP A 1 105 ? -0.960  19.128  -4.496  1.00 35.91 ? 98  ASP A OD2 1 
ATOM   718  N N   . VAL A 1 106 ? 0.164   14.625  -1.822  1.00 22.67 ? 99  VAL A N   1 
ATOM   719  C CA  . VAL A 1 106 ? -0.390  13.278  -1.520  1.00 22.44 ? 99  VAL A CA  1 
ATOM   720  C C   . VAL A 1 106 ? -1.367  13.499  -0.384  1.00 24.07 ? 99  VAL A C   1 
ATOM   721  O O   . VAL A 1 106 ? -1.099  14.353  0.435   1.00 27.20 ? 99  VAL A O   1 
ATOM   722  C CB  . VAL A 1 106 ? 0.712   12.284  -1.148  1.00 28.94 ? 99  VAL A CB  1 
ATOM   723  C CG1 . VAL A 1 106 ? 0.140   10.997  -0.584  1.00 31.12 ? 99  VAL A CG1 1 
ATOM   724  C CG2 . VAL A 1 106 ? 1.622   12.014  -2.326  1.00 30.27 ? 99  VAL A CG2 1 
ATOM   725  N N   . TYR A 1 107 ? -2.515  12.863  -0.442  1.00 21.09 ? 100 TYR A N   1 
ATOM   726  C CA  . TYR A 1 107 ? -3.503  12.956  0.651   1.00 23.29 ? 100 TYR A CA  1 
ATOM   727  C C   . TYR A 1 107 ? -3.560  11.603  1.337   1.00 22.02 ? 100 TYR A C   1 
ATOM   728  O O   . TYR A 1 107 ? -3.806  10.587  0.676   1.00 18.48 ? 100 TYR A O   1 
ATOM   729  C CB  . TYR A 1 107 ? -4.874  13.355  0.127   1.00 24.08 ? 100 TYR A CB  1 
ATOM   730  C CG  . TYR A 1 107 ? -4.912  14.662  -0.624  1.00 26.26 ? 100 TYR A CG  1 
ATOM   731  C CD1 . TYR A 1 107 ? -4.525  14.745  -1.959  1.00 27.31 ? 100 TYR A CD1 1 
ATOM   732  C CD2 . TYR A 1 107 ? -5.393  15.801  -0.016  1.00 28.16 ? 100 TYR A CD2 1 
ATOM   733  C CE1 . TYR A 1 107 ? -4.583  15.944  -2.653  1.00 29.21 ? 100 TYR A CE1 1 
ATOM   734  C CE2 . TYR A 1 107 ? -5.446  17.007  -0.694  1.00 29.14 ? 100 TYR A CE2 1 
ATOM   735  C CZ  . TYR A 1 107 ? -5.060  17.078  -2.023  1.00 33.65 ? 100 TYR A CZ  1 
ATOM   736  O OH  . TYR A 1 107 ? -5.146  18.284  -2.687  1.00 34.98 ? 100 TYR A OH  1 
ATOM   737  N N   . ILE A 1 108 ? -3.367  11.610  2.654   1.00 21.09 ? 101 ILE A N   1 
ATOM   738  C CA  . ILE A 1 108 ? -3.433  10.350  3.436   1.00 19.99 ? 101 ILE A CA  1 
ATOM   739  C C   . ILE A 1 108 ? -4.780  10.308  4.160   1.00 18.51 ? 101 ILE A C   1 
ATOM   740  O O   . ILE A 1 108 ? -5.025  11.239  4.937   1.00 22.27 ? 101 ILE A O   1 
ATOM   741  C CB  . ILE A 1 108 ? -2.230  10.311  4.387   1.00 22.03 ? 101 ILE A CB  1 
ATOM   742  C CG1 . ILE A 1 108 ? -0.933  10.474  3.590   1.00 24.86 ? 101 ILE A CG1 1 
ATOM   743  C CG2 . ILE A 1 108 ? -2.300  9.010   5.184   1.00 20.50 ? 101 ILE A CG2 1 
ATOM   744  C CD1 . ILE A 1 108 ? 0.304   10.165  4.362   1.00 30.46 ? 101 ILE A CD1 1 
ATOM   745  N N   . VAL A 1 109 ? -5.548  9.246   3.958   1.00 19.91 ? 102 VAL A N   1 
ATOM   746  C CA  . VAL A 1 109 ? -6.900  9.055   4.546   1.00 21.18 ? 102 VAL A CA  1 
ATOM   747  C C   . VAL A 1 109 ? -6.688  8.130   5.737   1.00 20.53 ? 102 VAL A C   1 
ATOM   748  O O   . VAL A 1 109 ? -6.161  7.030   5.527   1.00 18.22 ? 102 VAL A O   1 
ATOM   749  C CB  . VAL A 1 109 ? -7.932  8.466   3.572   1.00 22.70 ? 102 VAL A CB  1 
ATOM   750  C CG1 . VAL A 1 109 ? -9.310  8.391   4.215   1.00 24.74 ? 102 VAL A CG1 1 
ATOM   751  C CG2 . VAL A 1 109 ? -8.005  9.287   2.288   1.00 24.96 ? 102 VAL A CG2 1 
ATOM   752  N N   . GLN A 1 110 ? -7.139  8.584   6.887   1.00 21.91 ? 103 GLN A N   1 
ATOM   753  C CA  . GLN A 1 110 ? -7.052  7.831   8.151   1.00 23.13 ? 103 GLN A CA  1 
ATOM   754  C C   . GLN A 1 110 ? -8.406  7.853   8.845   1.00 25.36 ? 103 GLN A C   1 
ATOM   755  O O   . GLN A 1 110 ? -9.213  8.763   8.606   1.00 22.61 ? 103 GLN A O   1 
ATOM   756  C CB  . GLN A 1 110 ? -5.931  8.449   8.971   1.00 22.55 ? 103 GLN A CB  1 
ATOM   757  C CG  . GLN A 1 110 ? -4.606  8.327   8.229   1.00 25.70 ? 103 GLN A CG  1 
ATOM   758  C CD  . GLN A 1 110 ? -3.434  8.812   9.039   1.00 27.61 ? 103 GLN A CD  1 
ATOM   759  O OE1 . GLN A 1 110 ? -3.487  9.873   9.633   1.00 34.13 ? 103 GLN A OE1 1 
ATOM   760  N NE2 . GLN A 1 110 ? -2.435  7.970   9.173   1.00 29.63 ? 103 GLN A NE2 1 
ATOM   761  N N   . ASP A 1 111 ? -8.629  6.876   9.718   1.00 24.67 ? 104 ASP A N   1 
ATOM   762  C CA  . ASP A 1 111 ? -9.764  6.956   10.664  1.00 24.53 ? 104 ASP A CA  1 
ATOM   763  C C   . ASP A 1 111 ? -9.830  8.347   11.306  1.00 24.31 ? 104 ASP A C   1 
ATOM   764  O O   . ASP A 1 111 ? -8.816  8.940   11.766  1.00 24.22 ? 104 ASP A O   1 
ATOM   765  C CB  . ASP A 1 111 ? -9.657  5.883   11.751  1.00 25.00 ? 104 ASP A CB  1 
ATOM   766  C CG  . ASP A 1 111 ? -9.820  4.474   11.251  1.00 31.27 ? 104 ASP A CG  1 
ATOM   767  O OD1 . ASP A 1 111 ? -10.240 4.290   10.086  1.00 30.38 ? 104 ASP A OD1 1 
ATOM   768  O OD2 . ASP A 1 111 ? -9.459  3.574   12.019  1.00 33.83 ? 104 ASP A OD2 1 
ATOM   769  N N   . LEU A 1 112 ? -11.043 8.864   11.417  1.00 24.99 ? 105 LEU A N   1 
ATOM   770  C CA  . LEU A 1 112 ? -11.258 10.146  12.106  1.00 25.22 ? 105 LEU A CA  1 
ATOM   771  C C   . LEU A 1 112 ? -11.202 9.873   13.607  1.00 27.37 ? 105 LEU A C   1 
ATOM   772  O O   . LEU A 1 112 ? -12.028 9.074   14.135  1.00 27.19 ? 105 LEU A O   1 
ATOM   773  C CB  . LEU A 1 112 ? -12.613 10.765  11.742  1.00 26.35 ? 105 LEU A CB  1 
ATOM   774  C CG  . LEU A 1 112 ? -12.890 12.109  12.403  1.00 28.63 ? 105 LEU A CG  1 
ATOM   775  C CD1 . LEU A 1 112 ? -11.825 13.130  12.063  1.00 30.01 ? 105 LEU A CD1 1 
ATOM   776  C CD2 . LEU A 1 112 ? -14.281 12.619  12.043  1.00 33.16 ? 105 LEU A CD2 1 
ATOM   777  N N   . MET A 1 113 ? -10.260 10.529  14.249  1.00 26.38 ? 106 MET A N   1 
ATOM   778  C CA  . MET A 1 113 ? -10.074 10.485  15.709  1.00 27.85 ? 106 MET A CA  1 
ATOM   779  C C   . MET A 1 113 ? -10.390 11.894  16.170  1.00 31.16 ? 106 MET A C   1 
ATOM   780  O O   . MET A 1 113 ? -9.707  12.824  15.712  1.00 34.10 ? 106 MET A O   1 
ATOM   781  C CB  . MET A 1 113 ? -8.633  10.089  16.048  1.00 26.07 ? 106 MET A CB  1 
ATOM   782  C CG  . MET A 1 113 ? -8.226  8.775   15.401  1.00 21.93 ? 106 MET A CG  1 
ATOM   783  S SD  . MET A 1 113 ? -9.128  7.340   16.047  1.00 23.28 ? 106 MET A SD  1 
ATOM   784  C CE  . MET A 1 113 ? -8.203  7.079   17.567  1.00 21.49 ? 106 MET A CE  1 
ATOM   785  N N   . GLU A 1 114 ? -11.399 12.008  17.023  1.00 31.50 ? 107 GLU A N   1 
ATOM   786  C CA  . GLU A 1 114 ? -11.984 13.302  17.436  1.00 38.43 ? 107 GLU A CA  1 
ATOM   787  C C   . GLU A 1 114 ? -10.971 14.121  18.228  1.00 35.27 ? 107 GLU A C   1 
ATOM   788  O O   . GLU A 1 114 ? -11.032 15.350  18.147  1.00 31.26 ? 107 GLU A O   1 
ATOM   789  C CB  . GLU A 1 114 ? -13.277 13.054  18.207  1.00 43.59 ? 107 GLU A CB  1 
ATOM   790  C CG  . GLU A 1 114 ? -14.445 12.746  17.281  1.00 45.73 ? 107 GLU A CG  1 
ATOM   791  C CD  . GLU A 1 114 ? -14.428 11.360  16.656  1.00 48.56 ? 107 GLU A CD  1 
ATOM   792  O OE1 . GLU A 1 114 ? -15.329 11.112  15.844  1.00 47.31 ? 107 GLU A OE1 1 
ATOM   793  O OE2 . GLU A 1 114 ? -13.532 10.508  17.010  1.00 36.05 ? 107 GLU A OE2 1 
ATOM   794  N N   . THR A 1 115 ? -10.027 13.507  18.940  1.00 28.31 ? 108 THR A N   1 
ATOM   795  C CA  . THR A 1 115 ? -9.085  14.330  19.713  1.00 23.38 ? 108 THR A CA  1 
ATOM   796  C C   . THR A 1 115 ? -7.738  13.619  19.851  1.00 24.48 ? 108 THR A C   1 
ATOM   797  O O   . THR A 1 115 ? -7.513  12.635  19.157  1.00 21.74 ? 108 THR A O   1 
ATOM   798  C CB  . THR A 1 115 ? -9.694  14.699  21.073  1.00 24.74 ? 108 THR A CB  1 
ATOM   799  O OG1 . THR A 1 115 ? -8.903  15.752  21.599  1.00 26.77 ? 108 THR A OG1 1 
ATOM   800  C CG2 . THR A 1 115 ? -9.781  13.592  22.094  1.00 24.08 ? 108 THR A CG2 1 
ATOM   801  N N   . ASP A 1 116 ? -6.873  14.221  20.642  1.00 22.68 ? 109 ASP A N   1 
ATOM   802  C CA  . ASP A 1 116 ? -5.558  13.628  20.977  1.00 21.73 ? 109 ASP A CA  1 
ATOM   803  C C   . ASP A 1 116 ? -5.290  13.894  22.445  1.00 20.65 ? 109 ASP A C   1 
ATOM   804  O O   . ASP A 1 116 ? -5.960  14.747  23.061  1.00 20.40 ? 109 ASP A O   1 
ATOM   805  C CB  . ASP A 1 116 ? -4.464  14.087  20.030  1.00 20.30 ? 109 ASP A CB  1 
ATOM   806  C CG  . ASP A 1 116 ? -4.150  15.553  20.132  1.00 24.06 ? 109 ASP A CG  1 
ATOM   807  O OD1 . ASP A 1 116 ? -3.841  16.011  21.215  1.00 26.35 ? 109 ASP A OD1 1 
ATOM   808  O OD2 . ASP A 1 116 ? -4.158  16.198  19.082  1.00 26.96 ? 109 ASP A OD2 1 
ATOM   809  N N   . LEU A 1 117 ? -4.306  13.205  23.011  1.00 18.39 ? 110 LEU A N   1 
ATOM   810  C CA  . LEU A 1 117 ? -4.121  13.278  24.468  1.00 17.92 ? 110 LEU A CA  1 
ATOM   811  C C   . LEU A 1 117 ? -3.617  14.688  24.838  1.00 18.08 ? 110 LEU A C   1 
ATOM   812  O O   . LEU A 1 117 ? -3.853  15.142  25.981  1.00 21.83 ? 110 LEU A O   1 
ATOM   813  C CB  . LEU A 1 117 ? -3.147  12.178  24.888  1.00 18.19 ? 110 LEU A CB  1 
ATOM   814  C CG  . LEU A 1 117 ? -2.905  12.089  26.392  1.00 18.08 ? 110 LEU A CG  1 
ATOM   815  C CD1 . LEU A 1 117 ? -4.189  11.722  27.134  1.00 22.18 ? 110 LEU A CD1 1 
ATOM   816  C CD2 . LEU A 1 117 ? -1.870  11.022  26.694  1.00 18.52 ? 110 LEU A CD2 1 
ATOM   817  N N   . TYR A 1 118 ? -2.862  15.326  23.955  1.00 18.28 ? 111 TYR A N   1 
ATOM   818  C CA  . TYR A 1 118 ? -2.417  16.734  24.157  1.00 20.46 ? 111 TYR A CA  1 
ATOM   819  C C   . TYR A 1 118 ? -3.653  17.637  24.411  1.00 19.76 ? 111 TYR A C   1 
ATOM   820  O O   . TYR A 1 118 ? -3.723  18.300  25.487  1.00 21.90 ? 111 TYR A O   1 
ATOM   821  C CB  . TYR A 1 118 ? -1.641  17.236  22.953  1.00 22.74 ? 111 TYR A CB  1 
ATOM   822  C CG  . TYR A 1 118 ? -1.208  18.676  22.992  1.00 28.54 ? 111 TYR A CG  1 
ATOM   823  C CD1 . TYR A 1 118 ? -0.114  19.080  23.738  1.00 29.23 ? 111 TYR A CD1 1 
ATOM   824  C CD2 . TYR A 1 118 ? -1.858  19.619  22.208  1.00 33.12 ? 111 TYR A CD2 1 
ATOM   825  C CE1 . TYR A 1 118 ? 0.316   20.394  23.743  1.00 33.63 ? 111 TYR A CE1 1 
ATOM   826  C CE2 . TYR A 1 118 ? -1.462  20.948  22.231  1.00 38.57 ? 111 TYR A CE2 1 
ATOM   827  C CZ  . TYR A 1 118 ? -0.374  21.327  22.993  1.00 36.76 ? 111 TYR A CZ  1 
ATOM   828  O OH  . TYR A 1 118 ? 0.023   22.627  23.013  1.00 53.49 ? 111 TYR A OH  1 
ATOM   829  N N   . LYS A 1 119 ? -4.553  17.649  23.455  1.00 22.88 ? 112 LYS A N   1 
ATOM   830  C CA  . LYS A 1 119 ? -5.798  18.468  23.518  1.00 26.22 ? 112 LYS A CA  1 
ATOM   831  C C   . LYS A 1 119 ? -6.582  18.074  24.748  1.00 26.12 ? 112 LYS A C   1 
ATOM   832  O O   . LYS A 1 119 ? -7.016  18.968  25.491  1.00 27.51 ? 112 LYS A O   1 
ATOM   833  C CB  . LYS A 1 119 ? -6.650  18.263  22.279  1.00 26.75 ? 112 LYS A CB  1 
ATOM   834  C CG  . LYS A 1 119 ? -6.053  18.909  21.051  1.00 28.79 ? 112 LYS A CG  1 
ATOM   835  C CD  . LYS A 1 119 ? -6.837  18.629  19.814  1.00 33.48 ? 112 LYS A CD  1 
ATOM   836  C CE  . LYS A 1 119 ? -6.185  19.232  18.589  1.00 37.64 ? 112 LYS A CE  1 
ATOM   837  N NZ  . LYS A 1 119 ? -7.007  18.951  17.393  1.00 45.23 ? 112 LYS A NZ  1 
ATOM   838  N N   . LEU A 1 120 ? -6.772  16.780  24.968  1.00 24.84 ? 113 LEU A N   1 
ATOM   839  C CA  . LEU A 1 120 ? -7.555  16.288  26.137  1.00 26.58 ? 113 LEU A CA  1 
ATOM   840  C C   . LEU A 1 120 ? -6.925  16.763  27.458  1.00 28.39 ? 113 LEU A C   1 
ATOM   841  O O   . LEU A 1 120 ? -7.672  17.290  28.298  1.00 26.42 ? 113 LEU A O   1 
ATOM   842  C CB  . LEU A 1 120 ? -7.656  14.765  26.075  1.00 29.26 ? 113 LEU A CB  1 
ATOM   843  C CG  . LEU A 1 120 ? -8.731  14.129  26.955  1.00 30.59 ? 113 LEU A CG  1 
ATOM   844  C CD1 . LEU A 1 120 ? -10.124 14.497  26.456  1.00 32.73 ? 113 LEU A CD1 1 
ATOM   845  C CD2 . LEU A 1 120 ? -8.555  12.618  26.976  1.00 33.67 ? 113 LEU A CD2 1 
ATOM   846  N N   . LEU A 1 121 ? -5.594  16.670  27.638  1.00 23.86 ? 114 LEU A N   1 
ATOM   847  C CA  . LEU A 1 121 ? -4.944  17.065  28.907  1.00 24.94 ? 114 LEU A CA  1 
ATOM   848  C C   . LEU A 1 121 ? -4.993  18.584  29.118  1.00 24.24 ? 114 LEU A C   1 
ATOM   849  O O   . LEU A 1 121 ? -4.772  18.967  30.275  1.00 28.09 ? 114 LEU A O   1 
ATOM   850  C CB  . LEU A 1 121 ? -3.498  16.560  28.927  1.00 27.02 ? 114 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 121 ? -3.362  15.056  29.113  1.00 29.90 ? 114 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 121 ? -1.914  14.648  28.939  1.00 32.65 ? 114 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 121 ? -3.894  14.611  30.482  1.00 32.11 ? 114 LEU A CD2 1 
ATOM   854  N N   . LYS A 1 122 ? -5.270  19.382  28.074  1.00 27.05 ? 115 LYS A N   1 
ATOM   855  C CA  . LYS A 1 122 ? -5.414  20.866  28.190  1.00 29.94 ? 115 LYS A CA  1 
ATOM   856  C C   . LYS A 1 122 ? -6.563  21.167  29.165  1.00 29.08 ? 115 LYS A C   1 
ATOM   857  O O   . LYS A 1 122 ? -6.456  22.142  29.946  1.00 30.92 ? 115 LYS A O   1 
ATOM   858  C CB  . LYS A 1 122 ? -5.699  21.551  26.849  1.00 34.85 ? 115 LYS A CB  1 
ATOM   859  C CG  . LYS A 1 122 ? -4.508  21.725  25.917  1.00 39.23 ? 115 LYS A CG  1 
ATOM   860  C CD  . LYS A 1 122 ? -4.886  22.043  24.475  1.00 46.43 ? 115 LYS A CD  1 
ATOM   861  C CE  . LYS A 1 122 ? -5.047  23.522  24.194  1.00 51.14 ? 115 LYS A CE  1 
ATOM   862  N NZ  . LYS A 1 122 ? -4.595  23.858  22.824  1.00 55.68 ? 115 LYS A NZ  1 
ATOM   863  N N   . THR A 1 123 ? -7.624  20.365  29.145  1.00 27.15 ? 116 THR A N   1 
ATOM   864  C CA  . THR A 1 123 ? -8.881  20.718  29.845  1.00 27.22 ? 116 THR A CA  1 
ATOM   865  C C   . THR A 1 123 ? -9.447  19.581  30.683  1.00 27.05 ? 116 THR A C   1 
ATOM   866  O O   . THR A 1 123 ? -10.333 19.876  31.501  1.00 27.71 ? 116 THR A O   1 
ATOM   867  C CB  . THR A 1 123 ? -9.984  21.135  28.866  1.00 30.15 ? 116 THR A CB  1 
ATOM   868  O OG1 . THR A 1 123 ? -10.182 20.035  27.980  1.00 33.05 ? 116 THR A OG1 1 
ATOM   869  C CG2 . THR A 1 123 ? -9.662  22.410  28.120  1.00 34.97 ? 116 THR A CG2 1 
ATOM   870  N N   . GLN A 1 124 ? -9.072  18.321  30.494  1.00 22.77 ? 117 GLN A N   1 
ATOM   871  C CA  . GLN A 1 124 ? -9.778  17.235  31.211  1.00 23.84 ? 117 GLN A CA  1 
ATOM   872  C C   . GLN A 1 124 ? -8.867  16.581  32.254  1.00 25.64 ? 117 GLN A C   1 
ATOM   873  O O   . GLN A 1 124 ? -7.743  16.202  31.896  1.00 28.80 ? 117 GLN A O   1 
ATOM   874  C CB  . GLN A 1 124 ? -10.327 16.184  30.243  1.00 23.66 ? 117 GLN A CB  1 
ATOM   875  C CG  . GLN A 1 124 ? -11.211 16.759  29.139  1.00 24.29 ? 117 GLN A CG  1 
ATOM   876  C CD  . GLN A 1 124 ? -12.448 17.448  29.661  1.00 25.99 ? 117 GLN A CD  1 
ATOM   877  O OE1 . GLN A 1 124 ? -13.187 16.877  30.436  1.00 27.22 ? 117 GLN A OE1 1 
ATOM   878  N NE2 . GLN A 1 124 ? -12.612 18.717  29.334  1.00 30.12 ? 117 GLN A NE2 1 
ATOM   879  N N   . HIS A 1 125 ? -9.393  16.343  33.449  1.00 25.71 ? 118 HIS A N   1 
ATOM   880  C CA  . HIS A 1 125 ? -8.771  15.483  34.490  1.00 29.19 ? 118 HIS A CA  1 
ATOM   881  C C   . HIS A 1 125 ? -9.008  14.025  34.125  1.00 25.75 ? 118 HIS A C   1 
ATOM   882  O O   . HIS A 1 125 ? -10.151 13.634  33.873  1.00 25.55 ? 118 HIS A O   1 
ATOM   883  C CB  . HIS A 1 125 ? -9.326  15.825  35.875  1.00 36.89 ? 118 HIS A CB  1 
ATOM   884  C CG  . HIS A 1 125 ? -8.829  14.952  36.975  1.00 39.90 ? 118 HIS A CG  1 
ATOM   885  N ND1 . HIS A 1 125 ? -9.570  13.867  37.451  1.00 42.97 ? 118 HIS A ND1 1 
ATOM   886  C CD2 . HIS A 1 125 ? -7.701  15.018  37.720  1.00 42.16 ? 118 HIS A CD2 1 
ATOM   887  C CE1 . HIS A 1 125 ? -8.900  13.290  38.431  1.00 47.38 ? 118 HIS A CE1 1 
ATOM   888  N NE2 . HIS A 1 125 ? -7.754  13.986  38.621  1.00 50.68 ? 118 HIS A NE2 1 
ATOM   889  N N   . LEU A 1 126 ? -7.973  13.205  34.075  1.00 23.53 ? 119 LEU A N   1 
ATOM   890  C CA  . LEU A 1 126 ? -8.184  11.769  33.769  1.00 24.28 ? 119 LEU A CA  1 
ATOM   891  C C   . LEU A 1 126 ? -8.484  11.013  35.062  1.00 24.86 ? 119 LEU A C   1 
ATOM   892  O O   . LEU A 1 126 ? -7.700  11.145  35.987  1.00 27.10 ? 119 LEU A O   1 
ATOM   893  C CB  . LEU A 1 126 ? -6.935  11.194  33.090  1.00 25.61 ? 119 LEU A CB  1 
ATOM   894  C CG  . LEU A 1 126 ? -6.864  11.357  31.571  1.00 25.07 ? 119 LEU A CG  1 
ATOM   895  C CD1 . LEU A 1 126 ? -7.023  12.788  31.158  1.00 27.80 ? 119 LEU A CD1 1 
ATOM   896  C CD2 . LEU A 1 126 ? -5.552  10.823  31.006  1.00 29.27 ? 119 LEU A CD2 1 
ATOM   897  N N   . SER A 1 127 ? -9.498  10.141  35.045  1.00 26.76 ? 120 SER A N   1 
ATOM   898  C CA  . SER A 1 127 ? -9.765  9.141   36.101  1.00 27.89 ? 120 SER A CA  1 
ATOM   899  C C   . SER A 1 127 ? -8.577  8.185   36.132  1.00 27.58 ? 120 SER A C   1 
ATOM   900  O O   . SER A 1 127 ? -7.894  8.080   35.079  1.00 21.18 ? 120 SER A O   1 
ATOM   901  C CB  . SER A 1 127 ? -11.101 8.416   35.881  1.00 30.21 ? 120 SER A CB  1 
ATOM   902  O OG  . SER A 1 127 ? -11.038 7.379   34.882  1.00 28.40 ? 120 SER A OG  1 
ATOM   903  N N   . ASN A 1 128 ? -8.315  7.542   37.264  1.00 25.54 ? 121 ASN A N   1 
ATOM   904  C CA  . ASN A 1 128 ? -7.326  6.440   37.344  1.00 26.63 ? 121 ASN A CA  1 
ATOM   905  C C   . ASN A 1 128 ? -7.678  5.374   36.302  1.00 23.07 ? 121 ASN A C   1 
ATOM   906  O O   . ASN A 1 128 ? -6.766  4.818   35.648  1.00 23.57 ? 121 ASN A O   1 
ATOM   907  C CB  . ASN A 1 128 ? -7.245  5.802   38.728  1.00 27.30 ? 121 ASN A CB  1 
ATOM   908  C CG  . ASN A 1 128 ? -6.136  4.778   38.823  1.00 31.16 ? 121 ASN A CG  1 
ATOM   909  O OD1 . ASN A 1 128 ? -6.348  3.659   39.310  1.00 43.33 ? 121 ASN A OD1 1 
ATOM   910  N ND2 . ASN A 1 128 ? -4.949  5.140   38.354  1.00 27.50 ? 121 ASN A ND2 1 
ATOM   911  N N   . ASP A 1 129 ? -8.965  5.080   36.097  1.00 21.94 ? 122 ASP A N   1 
ATOM   912  C CA  . ASP A 1 129 ? -9.349  4.039   35.107  1.00 24.18 ? 122 ASP A CA  1 
ATOM   913  C C   . ASP A 1 129 ? -8.955  4.503   33.694  1.00 20.22 ? 122 ASP A C   1 
ATOM   914  O O   . ASP A 1 129 ? -8.527  3.676   32.930  1.00 21.73 ? 122 ASP A O   1 
ATOM   915  C CB  . ASP A 1 129 ? -10.844 3.690   35.151  1.00 28.42 ? 122 ASP A CB  1 
ATOM   916  C CG  . ASP A 1 129 ? -11.267 2.875   36.372  1.00 35.10 ? 122 ASP A CG  1 
ATOM   917  O OD1 . ASP A 1 129 ? -10.410 2.164   36.978  1.00 38.25 ? 122 ASP A OD1 1 
ATOM   918  O OD2 . ASP A 1 129 ? -12.462 2.935   36.700  1.00 43.45 ? 122 ASP A OD2 1 
ATOM   919  N N   . HIS A 1 130 ? -9.125  5.771   33.343  1.00 18.63 ? 123 HIS A N   1 
ATOM   920  C CA  . HIS A 1 130 ? -8.717  6.315   32.027  1.00 18.35 ? 123 HIS A CA  1 
ATOM   921  C C   . HIS A 1 130 ? -7.192  6.245   31.900  1.00 18.07 ? 123 HIS A C   1 
ATOM   922  O O   . HIS A 1 130 ? -6.727  5.913   30.793  1.00 17.67 ? 123 HIS A O   1 
ATOM   923  C CB  . HIS A 1 130 ? -9.179  7.748   31.811  1.00 19.30 ? 123 HIS A CB  1 
ATOM   924  C CG  . HIS A 1 130 ? -10.607 7.775   31.405  1.00 22.07 ? 123 HIS A CG  1 
ATOM   925  N ND1 . HIS A 1 130 ? -11.614 7.835   32.332  1.00 25.57 ? 123 HIS A ND1 1 
ATOM   926  C CD2 . HIS A 1 130 ? -11.190 7.647   30.205  1.00 23.68 ? 123 HIS A CD2 1 
ATOM   927  C CE1 . HIS A 1 130 ? -12.765 7.797   31.703  1.00 26.52 ? 123 HIS A CE1 1 
ATOM   928  N NE2 . HIS A 1 130 ? -12.547 7.674   30.409  1.00 23.49 ? 123 HIS A NE2 1 
ATOM   929  N N   . ILE A 1 131 ? -6.486  6.689   32.928  1.00 17.94 ? 124 ILE A N   1 
ATOM   930  C CA  . ILE A 1 131 ? -4.987  6.690   32.887  1.00 17.56 ? 124 ILE A CA  1 
ATOM   931  C C   . ILE A 1 131 ? -4.533  5.269   32.585  1.00 17.72 ? 124 ILE A C   1 
ATOM   932  O O   . ILE A 1 131 ? -3.661  5.073   31.732  1.00 18.08 ? 124 ILE A O   1 
ATOM   933  C CB  . ILE A 1 131 ? -4.384  7.214   34.193  1.00 19.12 ? 124 ILE A CB  1 
ATOM   934  C CG1 . ILE A 1 131 ? -4.691  8.698   34.395  1.00 21.74 ? 124 ILE A CG1 1 
ATOM   935  C CG2 . ILE A 1 131 ? -2.871  6.967   34.219  1.00 19.74 ? 124 ILE A CG2 1 
ATOM   936  C CD1 . ILE A 1 131 ? -4.206  9.242   35.701  1.00 22.02 ? 124 ILE A CD1 1 
ATOM   937  N N   . CYS A 1 132 ? -5.098  4.285   33.263  1.00 18.12 ? 125 CYS A N   1 
ATOM   938  C CA  . CYS A 1 132 ? -4.706  2.866   33.179  1.00 18.96 ? 125 CYS A CA  1 
ATOM   939  C C   . CYS A 1 132 ? -4.995  2.349   31.766  1.00 18.20 ? 125 CYS A C   1 
ATOM   940  O O   . CYS A 1 132 ? -4.152  1.677   31.153  1.00 17.25 ? 125 CYS A O   1 
ATOM   941  C CB  . CYS A 1 132 ? -5.479  2.118   34.269  1.00 19.16 ? 125 CYS A CB  1 
ATOM   942  S SG  . CYS A 1 132 ? -5.024  0.393   34.431  1.00 23.40 ? 125 CYS A SG  1 
ATOM   943  N N   . TYR A 1 133 ? -6.197  2.604   31.262  1.00 16.74 ? 126 TYR A N   1 
ATOM   944  C CA  . TYR A 1 133 ? -6.604  2.132   29.921  1.00 17.72 ? 126 TYR A CA  1 
ATOM   945  C C   . TYR A 1 133 ? -5.758  2.792   28.834  1.00 14.69 ? 126 TYR A C   1 
ATOM   946  O O   . TYR A 1 133 ? -5.319  2.105   27.896  1.00 16.02 ? 126 TYR A O   1 
ATOM   947  C CB  . TYR A 1 133 ? -8.084  2.451   29.730  1.00 19.07 ? 126 TYR A CB  1 
ATOM   948  C CG  . TYR A 1 133 ? -8.655  1.923   28.446  1.00 19.10 ? 126 TYR A CG  1 
ATOM   949  C CD1 . TYR A 1 133 ? -8.410  0.637   28.013  1.00 23.64 ? 126 TYR A CD1 1 
ATOM   950  C CD2 . TYR A 1 133 ? -9.494  2.723   27.697  1.00 20.48 ? 126 TYR A CD2 1 
ATOM   951  C CE1 . TYR A 1 133 ? -8.976  0.160   26.841  1.00 25.65 ? 126 TYR A CE1 1 
ATOM   952  C CE2 . TYR A 1 133 ? -10.035 2.285   26.505  1.00 22.07 ? 126 TYR A CE2 1 
ATOM   953  C CZ  . TYR A 1 133 ? -9.789  0.993   26.091  1.00 24.91 ? 126 TYR A CZ  1 
ATOM   954  O OH  . TYR A 1 133 ? -10.333 0.506   24.934  1.00 29.00 ? 126 TYR A OH  1 
ATOM   955  N N   . PHE A 1 134 ? -5.509  4.090   28.940  1.00 14.89 ? 127 PHE A N   1 
ATOM   956  C CA  . PHE A 1 134 ? -4.682  4.812   27.951  1.00 15.49 ? 127 PHE A CA  1 
ATOM   957  C C   . PHE A 1 134 ? -3.268  4.244   27.975  1.00 14.95 ? 127 PHE A C   1 
ATOM   958  O O   . PHE A 1 134 ? -2.699  3.988   26.909  1.00 14.61 ? 127 PHE A O   1 
ATOM   959  C CB  . PHE A 1 134 ? -4.640  6.322   28.188  1.00 16.57 ? 127 PHE A CB  1 
ATOM   960  C CG  . PHE A 1 134 ? -5.936  7.029   27.909  1.00 17.67 ? 127 PHE A CG  1 
ATOM   961  C CD1 . PHE A 1 134 ? -6.918  6.438   27.137  1.00 22.21 ? 127 PHE A CD1 1 
ATOM   962  C CD2 . PHE A 1 134 ? -6.146  8.313   28.383  1.00 21.04 ? 127 PHE A CD2 1 
ATOM   963  C CE1 . PHE A 1 134 ? -8.112  7.105   26.879  1.00 25.15 ? 127 PHE A CE1 1 
ATOM   964  C CE2 . PHE A 1 134 ? -7.362  8.962   28.172  1.00 21.48 ? 127 PHE A CE2 1 
ATOM   965  C CZ  . PHE A 1 134 ? -8.313  8.376   27.381  1.00 23.90 ? 127 PHE A CZ  1 
ATOM   966  N N   . LEU A 1 135 ? -2.711  4.050   29.168  1.00 15.90 ? 128 LEU A N   1 
ATOM   967  C CA  . LEU A 1 135 ? -1.314  3.556   29.299  1.00 14.66 ? 128 LEU A CA  1 
ATOM   968  C C   . LEU A 1 135 ? -1.260  2.164   28.700  1.00 14.46 ? 128 LEU A C   1 
ATOM   969  O O   . LEU A 1 135 ? -0.320  1.847   27.917  1.00 14.59 ? 128 LEU A O   1 
ATOM   970  C CB  . LEU A 1 135 ? -0.899  3.529   30.765  1.00 16.31 ? 128 LEU A CB  1 
ATOM   971  C CG  . LEU A 1 135 ? 0.508   3.000   31.010  1.00 15.68 ? 128 LEU A CG  1 
ATOM   972  C CD1 . LEU A 1 135 ? 1.530   3.847   30.295  1.00 16.71 ? 128 LEU A CD1 1 
ATOM   973  C CD2 . LEU A 1 135 ? 0.789   2.887   32.512  1.00 15.24 ? 128 LEU A CD2 1 
ATOM   974  N N   . TYR A 1 136 ? -2.258  1.332   29.016  1.00 13.81 ? 129 TYR A N   1 
ATOM   975  C CA  . TYR A 1 136 ? -2.301  -0.039  28.453  1.00 12.63 ? 129 TYR A CA  1 
ATOM   976  C C   . TYR A 1 136 ? -2.254  0.032   26.918  1.00 13.10 ? 129 TYR A C   1 
ATOM   977  O O   . TYR A 1 136 ? -1.478  -0.689  26.275  1.00 13.92 ? 129 TYR A O   1 
ATOM   978  C CB  . TYR A 1 136 ? -3.531  -0.816  28.915  1.00 14.28 ? 129 TYR A CB  1 
ATOM   979  C CG  . TYR A 1 136 ? -3.660  -2.135  28.237  1.00 13.76 ? 129 TYR A CG  1 
ATOM   980  C CD1 . TYR A 1 136 ? -2.788  -3.153  28.536  1.00 14.36 ? 129 TYR A CD1 1 
ATOM   981  C CD2 . TYR A 1 136 ? -4.584  -2.363  27.213  1.00 14.04 ? 129 TYR A CD2 1 
ATOM   982  C CE1 . TYR A 1 136 ? -2.864  -4.378  27.909  1.00 15.28 ? 129 TYR A CE1 1 
ATOM   983  C CE2 . TYR A 1 136 ? -4.693  -3.599  26.600  1.00 14.55 ? 129 TYR A CE2 1 
ATOM   984  C CZ  . TYR A 1 136 ? -3.790  -4.597  26.912  1.00 14.53 ? 129 TYR A CZ  1 
ATOM   985  O OH  . TYR A 1 136 ? -3.847  -5.828  26.294  1.00 16.34 ? 129 TYR A OH  1 
ATOM   986  N N   . GLN A 1 137 ? -3.091  0.870   26.318  1.00 12.81 ? 130 GLN A N   1 
ATOM   987  C CA  . GLN A 1 137 ? -3.191  0.930   24.836  1.00 13.50 ? 130 GLN A CA  1 
ATOM   988  C C   . GLN A 1 137 ? -1.866  1.461   24.270  1.00 12.90 ? 130 GLN A C   1 
ATOM   989  O O   . GLN A 1 137 ? -1.486  1.005   23.185  1.00 13.17 ? 130 GLN A O   1 
ATOM   990  C CB  . GLN A 1 137 ? -4.366  1.803   24.383  1.00 14.40 ? 130 GLN A CB  1 
ATOM   991  C CG  . GLN A 1 137 ? -5.709  1.177   24.721  1.00 15.01 ? 130 GLN A CG  1 
ATOM   992  C CD  . GLN A 1 137 ? -6.835  2.060   24.255  1.00 15.47 ? 130 GLN A CD  1 
ATOM   993  O OE1 . GLN A 1 137 ? -7.189  2.030   23.096  1.00 16.54 ? 130 GLN A OE1 1 
ATOM   994  N NE2 . GLN A 1 137 ? -7.268  2.957   25.109  1.00 17.33 ? 130 GLN A NE2 1 
ATOM   995  N N   . ILE A 1 138 ? -1.259  2.483   24.900  1.00 12.96 ? 131 ILE A N   1 
ATOM   996  C CA  . ILE A 1 138 ? 0.045   3.036   24.438  1.00 13.15 ? 131 ILE A CA  1 
ATOM   997  C C   . ILE A 1 138 ? 1.050   1.872   24.382  1.00 13.09 ? 131 ILE A C   1 
ATOM   998  O O   . ILE A 1 138 ? 1.731   1.671   23.371  1.00 12.37 ? 131 ILE A O   1 
ATOM   999  C CB  . ILE A 1 138 ? 0.570   4.157   25.353  1.00 13.82 ? 131 ILE A CB  1 
ATOM   1000 C CG1 . ILE A 1 138 ? -0.386  5.351   25.375  1.00 13.10 ? 131 ILE A CG1 1 
ATOM   1001 C CG2 . ILE A 1 138 ? 1.954   4.579   24.855  1.00 13.28 ? 131 ILE A CG2 1 
ATOM   1002 C CD1 . ILE A 1 138 ? -0.131  6.391   26.421  1.00 15.64 ? 131 ILE A CD1 1 
ATOM   1003 N N   . LEU A 1 139 ? 1.121   1.107   25.465  1.00 13.30 ? 132 LEU A N   1 
ATOM   1004 C CA  . LEU A 1 139 ? 2.148   0.040   25.555  1.00 12.03 ? 132 LEU A CA  1 
ATOM   1005 C C   . LEU A 1 139 ? 1.804   -1.131  24.640  1.00 12.55 ? 132 LEU A C   1 
ATOM   1006 O O   . LEU A 1 139 ? 2.705   -1.771  24.087  1.00 12.95 ? 132 LEU A O   1 
ATOM   1007 C CB  . LEU A 1 139 ? 2.263   -0.387  27.003  1.00 12.33 ? 132 LEU A CB  1 
ATOM   1008 C CG  . LEU A 1 139 ? 2.894   0.597   27.982  1.00 13.50 ? 132 LEU A CG  1 
ATOM   1009 C CD1 . LEU A 1 139 ? 2.595   0.134   29.396  1.00 14.21 ? 132 LEU A CD1 1 
ATOM   1010 C CD2 . LEU A 1 139 ? 4.405   0.730   27.759  1.00 13.91 ? 132 LEU A CD2 1 
ATOM   1011 N N   . ARG A 1 140 ? 0.519   -1.411  24.447  1.00 12.57 ? 133 ARG A N   1 
ATOM   1012 C CA  . ARG A 1 140 ? 0.091   -2.460  23.518  1.00 11.82 ? 133 ARG A CA  1 
ATOM   1013 C C   . ARG A 1 140 ? 0.545   -2.091  22.088  1.00 13.17 ? 133 ARG A C   1 
ATOM   1014 O O   . ARG A 1 140 ? 1.102   -2.904  21.416  1.00 13.05 ? 133 ARG A O   1 
ATOM   1015 C CB  . ARG A 1 140 ? -1.404  -2.644  23.599  1.00 12.56 ? 133 ARG A CB  1 
ATOM   1016 C CG  . ARG A 1 140 ? -1.891  -3.840  22.819  1.00 13.21 ? 133 ARG A CG  1 
ATOM   1017 C CD  . ARG A 1 140 ? -3.345  -4.058  23.162  1.00 14.34 ? 133 ARG A CD  1 
ATOM   1018 N NE  . ARG A 1 140 ? -3.948  -5.147  22.377  1.00 15.93 ? 133 ARG A NE  1 
ATOM   1019 C CZ  . ARG A 1 140 ? -4.813  -4.987  21.381  1.00 18.75 ? 133 ARG A CZ  1 
ATOM   1020 N NH1 . ARG A 1 140 ? -5.158  -3.775  20.976  1.00 22.35 ? 133 ARG A NH1 1 
ATOM   1021 N NH2 . ARG A 1 140 ? -5.350  -6.035  20.792  1.00 18.36 ? 133 ARG A NH2 1 
ATOM   1022 N N   . GLY A 1 141 ? 0.308   -0.854  21.659  1.00 12.28 ? 134 GLY A N   1 
ATOM   1023 C CA  . GLY A 1 141 ? 0.785   -0.377  20.363  1.00 11.81 ? 134 GLY A CA  1 
ATOM   1024 C C   . GLY A 1 141 ? 2.299   -0.411  20.335  1.00 11.88 ? 134 GLY A C   1 
ATOM   1025 O O   . GLY A 1 141 ? 2.862   -0.834  19.326  1.00 11.44 ? 134 GLY A O   1 
ATOM   1026 N N   . LEU A 1 142 ? 2.945   0.056   21.389  1.00 12.57 ? 135 LEU A N   1 
ATOM   1027 C CA  . LEU A 1 142 ? 4.432   0.153   21.406  1.00 12.23 ? 135 LEU A CA  1 
ATOM   1028 C C   . LEU A 1 142 ? 5.061   -1.243  21.344  1.00 12.48 ? 135 LEU A C   1 
ATOM   1029 O O   . LEU A 1 142 ? 6.063   -1.424  20.627  1.00 12.81 ? 135 LEU A O   1 
ATOM   1030 C CB  . LEU A 1 142 ? 4.907   0.980   22.587  1.00 13.10 ? 135 LEU A CB  1 
ATOM   1031 C CG  . LEU A 1 142 ? 6.392   1.276   22.579  1.00 13.22 ? 135 LEU A CG  1 
ATOM   1032 C CD1 . LEU A 1 142 ? 6.800   2.078   21.351  1.00 15.32 ? 135 LEU A CD1 1 
ATOM   1033 C CD2 . LEU A 1 142 ? 6.782   2.041   23.826  1.00 14.48 ? 135 LEU A CD2 1 
ATOM   1034 N N   . LYS A 1 143 ? 4.431   -2.242  21.950  1.00 12.29 ? 136 LYS A N   1 
ATOM   1035 C CA  . LYS A 1 143 ? 4.895   -3.638  21.856  1.00 12.60 ? 136 LYS A CA  1 
ATOM   1036 C C   . LYS A 1 143 ? 4.961   -4.061  20.386  1.00 13.86 ? 136 LYS A C   1 
ATOM   1037 O O   . LYS A 1 143 ? 5.958   -4.625  19.945  1.00 14.53 ? 136 LYS A O   1 
ATOM   1038 C CB  . LYS A 1 143 ? 3.971   -4.565  22.612  1.00 12.61 ? 136 LYS A CB  1 
ATOM   1039 C CG  . LYS A 1 143 ? 4.326   -6.019  22.463  1.00 14.04 ? 136 LYS A CG  1 
ATOM   1040 C CD  . LYS A 1 143 ? 3.430   -6.943  23.162  1.00 14.28 ? 136 LYS A CD  1 
ATOM   1041 C CE  . LYS A 1 143 ? 3.865   -8.383  22.973  1.00 16.92 ? 136 LYS A CE  1 
ATOM   1042 N NZ  . LYS A 1 143 ? 2.848   -9.276  23.552  1.00 19.07 ? 136 LYS A NZ  1 
ATOM   1043 N N   . TYR A 1 144 ? 3.909   -3.797  19.650  1.00 14.18 ? 137 TYR A N   1 
ATOM   1044 C CA  . TYR A 1 144 ? 3.935   -4.093  18.210  1.00 12.36 ? 137 TYR A CA  1 
ATOM   1045 C C   . TYR A 1 144 ? 5.070   -3.371  17.486  1.00 12.80 ? 137 TYR A C   1 
ATOM   1046 O O   . TYR A 1 144 ? 5.836   -3.998  16.685  1.00 14.49 ? 137 TYR A O   1 
ATOM   1047 C CB  . TYR A 1 144 ? 2.538   -3.821  17.669  1.00 13.89 ? 137 TYR A CB  1 
ATOM   1048 C CG  . TYR A 1 144 ? 2.364   -4.204  16.233  1.00 14.09 ? 137 TYR A CG  1 
ATOM   1049 C CD1 . TYR A 1 144 ? 2.710   -3.300  15.243  1.00 15.23 ? 137 TYR A CD1 1 
ATOM   1050 C CD2 . TYR A 1 144 ? 1.852   -5.427  15.853  1.00 17.15 ? 137 TYR A CD2 1 
ATOM   1051 C CE1 . TYR A 1 144 ? 2.537   -3.632  13.919  1.00 15.15 ? 137 TYR A CE1 1 
ATOM   1052 C CE2 . TYR A 1 144 ? 1.655   -5.764  14.524  1.00 14.83 ? 137 TYR A CE2 1 
ATOM   1053 C CZ  . TYR A 1 144 ? 2.009   -4.848  13.560  1.00 15.39 ? 137 TYR A CZ  1 
ATOM   1054 O OH  . TYR A 1 144 ? 1.806   -5.135  12.241  1.00 18.25 ? 137 TYR A OH  1 
ATOM   1055 N N   . ILE A 1 145 ? 5.127   -2.054  17.614  1.00 12.48 ? 138 ILE A N   1 
ATOM   1056 C CA  . ILE A 1 145 ? 6.165   -1.215  16.980  1.00 12.73 ? 138 ILE A CA  1 
ATOM   1057 C C   . ILE A 1 145 ? 7.543   -1.830  17.248  1.00 11.61 ? 138 ILE A C   1 
ATOM   1058 O O   . ILE A 1 145 ? 8.299   -2.101  16.296  1.00 12.32 ? 138 ILE A O   1 
ATOM   1059 C CB  . ILE A 1 145 ? 6.099   0.236   17.457  1.00 13.32 ? 138 ILE A CB  1 
ATOM   1060 C CG1 . ILE A 1 145 ? 4.750   0.856   17.124  1.00 14.13 ? 138 ILE A CG1 1 
ATOM   1061 C CG2 . ILE A 1 145 ? 7.238   1.060   16.909  1.00 14.54 ? 138 ILE A CG2 1 
ATOM   1062 C CD1 . ILE A 1 145 ? 4.502   2.163   17.807  1.00 15.97 ? 138 ILE A CD1 1 
ATOM   1063 N N   . HIS A 1 146 ? 7.850   -2.069  18.520  1.00 11.78 ? 139 HIS A N   1 
ATOM   1064 C CA  . HIS A 1 146 ? 9.177   -2.586  18.913  1.00 12.52 ? 139 HIS A CA  1 
ATOM   1065 C C   . HIS A 1 146 ? 9.377   -3.988  18.353  1.00 13.14 ? 139 HIS A C   1 
ATOM   1066 O O   . HIS A 1 146 ? 10.494  -4.289  17.970  1.00 13.98 ? 139 HIS A O   1 
ATOM   1067 C CB  . HIS A 1 146 ? 9.329   -2.548  20.436  1.00 11.91 ? 139 HIS A CB  1 
ATOM   1068 C CG  . HIS A 1 146 ? 9.598   -1.171  20.919  1.00 10.98 ? 139 HIS A CG  1 
ATOM   1069 N ND1 . HIS A 1 146 ? 9.827   -0.901  22.267  1.00 12.08 ? 139 HIS A ND1 1 
ATOM   1070 C CD2 . HIS A 1 146 ? 9.757   -0.003  20.252  1.00 11.58 ? 139 HIS A CD2 1 
ATOM   1071 C CE1 . HIS A 1 146 ? 10.062  0.396   22.375  1.00 11.14 ? 139 HIS A CE1 1 
ATOM   1072 N NE2 . HIS A 1 146 ? 10.040  0.958   21.177  1.00 12.57 ? 139 HIS A NE2 1 
ATOM   1073 N N   . SER A 1 147 ? 8.299   -4.790  18.283  1.00 13.51 ? 140 SER A N   1 
ATOM   1074 C CA  . SER A 1 147 ? 8.406   -6.174  17.747  1.00 13.14 ? 140 SER A CA  1 
ATOM   1075 C C   . SER A 1 147 ? 8.733   -6.139  16.245  1.00 15.22 ? 140 SER A C   1 
ATOM   1076 O O   . SER A 1 147 ? 9.257   -7.140  15.762  1.00 17.85 ? 140 SER A O   1 
ATOM   1077 C CB  . SER A 1 147 ? 7.142   -6.961  17.980  1.00 14.43 ? 140 SER A CB  1 
ATOM   1078 O OG  . SER A 1 147 ? 6.120   -6.523  17.078  1.00 15.59 ? 140 SER A OG  1 
ATOM   1079 N N   . ALA A 1 148 ? 8.510   -5.008  15.569  1.00 14.78 ? 141 ALA A N   1 
ATOM   1080 C CA  . ALA A 1 148 ? 8.829   -4.800  14.139  1.00 15.67 ? 141 ALA A CA  1 
ATOM   1081 C C   . ALA A 1 148 ? 10.236  -4.246  14.005  1.00 16.19 ? 141 ALA A C   1 
ATOM   1082 O O   . ALA A 1 148 ? 10.629  -3.917  12.895  1.00 16.79 ? 141 ALA A O   1 
ATOM   1083 C CB  . ALA A 1 148 ? 7.805   -3.903  13.507  1.00 16.71 ? 141 ALA A CB  1 
ATOM   1084 N N   . ASN A 1 149 ? 10.951  -4.154  15.116  1.00 16.32 ? 142 ASN A N   1 
ATOM   1085 C CA  . ASN A 1 149 ? 12.335  -3.670  15.170  1.00 17.52 ? 142 ASN A CA  1 
ATOM   1086 C C   . ASN A 1 149 ? 12.312  -2.191  14.867  1.00 15.90 ? 142 ASN A C   1 
ATOM   1087 O O   . ASN A 1 149 ? 13.315  -1.698  14.363  1.00 17.02 ? 142 ASN A O   1 
ATOM   1088 C CB  . ASN A 1 149 ? 13.259  -4.445  14.223  1.00 19.17 ? 142 ASN A CB  1 
ATOM   1089 C CG  . ASN A 1 149 ? 14.709  -4.262  14.581  1.00 22.55 ? 142 ASN A CG  1 
ATOM   1090 O OD1 . ASN A 1 149 ? 15.062  -4.207  15.749  1.00 25.97 ? 142 ASN A OD1 1 
ATOM   1091 N ND2 . ASN A 1 149 ? 15.552  -4.205  13.565  1.00 25.34 ? 142 ASN A ND2 1 
ATOM   1092 N N   . VAL A 1 150 ? 11.186  -1.515  15.124  1.00 14.76 ? 143 VAL A N   1 
ATOM   1093 C CA  . VAL A 1 150 ? 11.035  -0.073  14.832  1.00 15.68 ? 143 VAL A CA  1 
ATOM   1094 C C   . VAL A 1 150 ? 11.010  0.692   16.146  1.00 14.45 ? 143 VAL A C   1 
ATOM   1095 O O   . VAL A 1 150 ? 10.485  0.158   17.133  1.00 15.17 ? 143 VAL A O   1 
ATOM   1096 C CB  . VAL A 1 150 ? 9.799   0.225   13.979  1.00 15.97 ? 143 VAL A CB  1 
ATOM   1097 C CG1 . VAL A 1 150 ? 9.592   1.740   13.861  1.00 17.14 ? 143 VAL A CG1 1 
ATOM   1098 C CG2 . VAL A 1 150 ? 9.940   -0.469  12.622  1.00 18.00 ? 143 VAL A CG2 1 
ATOM   1099 N N   . LEU A 1 151 ? 11.609  1.877   16.139  1.00 15.05 ? 144 LEU A N   1 
ATOM   1100 C CA  . LEU A 1 151 ? 11.514  2.851   17.242  1.00 16.50 ? 144 LEU A CA  1 
ATOM   1101 C C   . LEU A 1 151 ? 10.656  4.013   16.786  1.00 16.33 ? 144 LEU A C   1 
ATOM   1102 O O   . LEU A 1 151 ? 10.864  4.586   15.683  1.00 17.15 ? 144 LEU A O   1 
ATOM   1103 C CB  . LEU A 1 151 ? 12.892  3.362   17.602  1.00 16.99 ? 144 LEU A CB  1 
ATOM   1104 C CG  . LEU A 1 151 ? 13.935  2.286   17.776  1.00 19.74 ? 144 LEU A CG  1 
ATOM   1105 C CD1 . LEU A 1 151 ? 15.274  2.933   17.962  1.00 21.55 ? 144 LEU A CD1 1 
ATOM   1106 C CD2 . LEU A 1 151 ? 13.551  1.400   18.932  1.00 20.58 ? 144 LEU A CD2 1 
ATOM   1107 N N   . HIS A 1 152 ? 9.734   4.448   17.610  1.00 15.63 ? 145 HIS A N   1 
ATOM   1108 C CA  . HIS A 1 152 ? 8.885   5.590   17.207  1.00 15.49 ? 145 HIS A CA  1 
ATOM   1109 C C   . HIS A 1 152 ? 9.697   6.879   17.284  1.00 16.31 ? 145 HIS A C   1 
ATOM   1110 O O   . HIS A 1 152 ? 9.625   7.676   16.317  1.00 17.62 ? 145 HIS A O   1 
ATOM   1111 C CB  . HIS A 1 152 ? 7.635   5.630   18.090  1.00 15.47 ? 145 HIS A CB  1 
ATOM   1112 C CG  . HIS A 1 152 ? 6.700   6.704   17.688  1.00 14.39 ? 145 HIS A CG  1 
ATOM   1113 N ND1 . HIS A 1 152 ? 6.936   8.009   17.988  1.00 16.24 ? 145 HIS A ND1 1 
ATOM   1114 C CD2 . HIS A 1 152 ? 5.545   6.649   16.975  1.00 16.16 ? 145 HIS A CD2 1 
ATOM   1115 C CE1 . HIS A 1 152 ? 5.936   8.730   17.526  1.00 16.89 ? 145 HIS A CE1 1 
ATOM   1116 N NE2 . HIS A 1 152 ? 5.043   7.929   16.921  1.00 14.92 ? 145 HIS A NE2 1 
ATOM   1117 N N   . ARG A 1 153 ? 10.333  7.139   18.425  1.00 15.81 ? 146 ARG A N   1 
ATOM   1118 C CA  . ARG A 1 153 ? 11.307  8.232   18.667  1.00 16.83 ? 146 ARG A CA  1 
ATOM   1119 C C   . ARG A 1 153 ? 10.617  9.587   18.842  1.00 17.48 ? 146 ARG A C   1 
ATOM   1120 O O   . ARG A 1 153 ? 11.349  10.535  19.218  1.00 21.50 ? 146 ARG A O   1 
ATOM   1121 C CB  . ARG A 1 153 ? 12.406  8.280   17.593  1.00 17.98 ? 146 ARG A CB  1 
ATOM   1122 C CG  . ARG A 1 153 ? 13.050  6.914   17.418  1.00 17.12 ? 146 ARG A CG  1 
ATOM   1123 C CD  . ARG A 1 153 ? 14.155  6.878   16.406  1.00 20.17 ? 146 ARG A CD  1 
ATOM   1124 N NE  . ARG A 1 153 ? 15.270  7.726   16.740  1.00 21.91 ? 146 ARG A NE  1 
ATOM   1125 C CZ  . ARG A 1 153 ? 15.613  8.851   16.139  1.00 24.34 ? 146 ARG A CZ  1 
ATOM   1126 N NH1 . ARG A 1 153 ? 14.913  9.339   15.126  1.00 24.35 ? 146 ARG A NH1 1 
ATOM   1127 N NH2 . ARG A 1 153 ? 16.715  9.461   16.533  1.00 24.65 ? 146 ARG A NH2 1 
ATOM   1128 N N   . ASP A 1 154 ? 9.290   9.685   18.754  1.00 17.28 ? 147 ASP A N   1 
ATOM   1129 C CA  . ASP A 1 154 ? 8.660   11.011  19.005  1.00 17.16 ? 147 ASP A CA  1 
ATOM   1130 C C   . ASP A 1 154 ? 7.341   10.814  19.733  1.00 17.81 ? 147 ASP A C   1 
ATOM   1131 O O   . ASP A 1 154 ? 6.355   11.475  19.396  1.00 18.04 ? 147 ASP A O   1 
ATOM   1132 C CB  . ASP A 1 154 ? 8.464   11.810  17.727  1.00 19.06 ? 147 ASP A CB  1 
ATOM   1133 C CG  . ASP A 1 154 ? 8.380   13.310  17.969  1.00 21.88 ? 147 ASP A CG  1 
ATOM   1134 O OD1 . ASP A 1 154 ? 8.658   13.778  19.082  1.00 23.05 ? 147 ASP A OD1 1 
ATOM   1135 O OD2 . ASP A 1 154 ? 7.929   13.965  17.042  1.00 30.23 ? 147 ASP A OD2 1 
ATOM   1136 N N   . LEU A 1 155 ? 7.319   9.882   20.680  1.00 15.46 ? 148 LEU A N   1 
ATOM   1137 C CA  . LEU A 1 155 ? 6.095   9.678   21.488  1.00 15.29 ? 148 LEU A CA  1 
ATOM   1138 C C   . LEU A 1 155 ? 5.882   10.896  22.350  1.00 15.04 ? 148 LEU A C   1 
ATOM   1139 O O   . LEU A 1 155 ? 6.769   11.320  23.101  1.00 17.68 ? 148 LEU A O   1 
ATOM   1140 C CB  . LEU A 1 155 ? 6.138   8.413   22.322  1.00 15.23 ? 148 LEU A CB  1 
ATOM   1141 C CG  . LEU A 1 155 ? 6.188   7.137   21.509  1.00 15.50 ? 148 LEU A CG  1 
ATOM   1142 C CD1 . LEU A 1 155 ? 6.497   5.965   22.416  1.00 15.94 ? 148 LEU A CD1 1 
ATOM   1143 C CD2 . LEU A 1 155 ? 4.921   6.890   20.735  1.00 15.96 ? 148 LEU A CD2 1 
ATOM   1144 N N   . LYS A 1 156 ? 4.663   11.407  22.275  1.00 17.00 ? 149 LYS A N   1 
ATOM   1145 C CA  . LYS A 1 156 ? 4.229   12.553  23.075  1.00 16.79 ? 149 LYS A CA  1 
ATOM   1146 C C   . LYS A 1 156 ? 2.713   12.611  22.982  1.00 16.41 ? 149 LYS A C   1 
ATOM   1147 O O   . LYS A 1 156 ? 2.103   11.961  22.135  1.00 16.63 ? 149 LYS A O   1 
ATOM   1148 C CB  . LYS A 1 156 ? 4.881   13.838  22.577  1.00 18.32 ? 149 LYS A CB  1 
ATOM   1149 C CG  . LYS A 1 156 ? 4.535   14.253  21.170  1.00 20.57 ? 149 LYS A CG  1 
ATOM   1150 C CD  . LYS A 1 156 ? 5.348   15.465  20.741  1.00 23.69 ? 149 LYS A CD  1 
ATOM   1151 C CE  . LYS A 1 156 ? 5.419   15.571  19.238  1.00 28.62 ? 149 LYS A CE  1 
ATOM   1152 N NZ  . LYS A 1 156 ? 5.821   16.938  18.833  1.00 33.13 ? 149 LYS A NZ  1 
ATOM   1153 N N   . PRO A 1 157 ? 2.057   13.347  23.894  1.00 17.13 ? 150 PRO A N   1 
ATOM   1154 C CA  . PRO A 1 157 ? 0.590   13.373  23.914  1.00 17.17 ? 150 PRO A CA  1 
ATOM   1155 C C   . PRO A 1 157 ? -0.096  13.722  22.590  1.00 18.53 ? 150 PRO A C   1 
ATOM   1156 O O   . PRO A 1 157 ? -1.105  13.122  22.287  1.00 16.62 ? 150 PRO A O   1 
ATOM   1157 C CB  . PRO A 1 157 ? 0.281   14.423  24.981  1.00 18.58 ? 150 PRO A CB  1 
ATOM   1158 C CG  . PRO A 1 157 ? 1.469   14.311  25.945  1.00 19.05 ? 150 PRO A CG  1 
ATOM   1159 C CD  . PRO A 1 157 ? 2.645   14.107  25.002  1.00 18.75 ? 150 PRO A CD  1 
ATOM   1160 N N   . SER A 1 158 ? 0.475   14.636  21.793  1.00 18.03 ? 151 SER A N   1 
ATOM   1161 C CA  . SER A 1 158 ? -0.107  15.063  20.488  1.00 18.88 ? 151 SER A CA  1 
ATOM   1162 C C   . SER A 1 158 ? -0.037  13.939  19.441  1.00 20.14 ? 151 SER A C   1 
ATOM   1163 O O   . SER A 1 158 ? -0.768  13.996  18.452  1.00 18.13 ? 151 SER A O   1 
ATOM   1164 C CB  . SER A 1 158 ? 0.492   16.361  19.990  1.00 21.88 ? 151 SER A CB  1 
ATOM   1165 O OG  . SER A 1 158 ? 1.896   16.270  19.865  1.00 26.15 ? 151 SER A OG  1 
ATOM   1166 N N   . ASN A 1 159 ? 0.807   12.917  19.646  1.00 17.55 ? 152 ASN A N   1 
ATOM   1167 C CA  . ASN A 1 159 ? 0.909   11.767  18.711  1.00 17.21 ? 152 ASN A CA  1 
ATOM   1168 C C   . ASN A 1 159 ? 0.129   10.581  19.268  1.00 16.35 ? 152 ASN A C   1 
ATOM   1169 O O   . ASN A 1 159 ? 0.255   9.492   18.713  1.00 16.15 ? 152 ASN A O   1 
ATOM   1170 C CB  . ASN A 1 159 ? 2.372   11.379  18.443  1.00 20.54 ? 152 ASN A CB  1 
ATOM   1171 C CG  . ASN A 1 159 ? 3.130   12.400  17.632  1.00 24.14 ? 152 ASN A CG  1 
ATOM   1172 O OD1 . ASN A 1 159 ? 4.364   12.458  17.660  1.00 24.94 ? 152 ASN A OD1 1 
ATOM   1173 N ND2 . ASN A 1 159 ? 2.388   13.182  16.868  1.00 22.63 ? 152 ASN A ND2 1 
ATOM   1174 N N   . LEU A 1 160 ? -0.748  10.797  20.243  1.00 15.06 ? 153 LEU A N   1 
ATOM   1175 C CA  . LEU A 1 160 ? -1.692  9.768   20.705  1.00 15.20 ? 153 LEU A CA  1 
ATOM   1176 C C   . LEU A 1 160 ? -3.113  10.220  20.405  1.00 16.25 ? 153 LEU A C   1 
ATOM   1177 O O   . LEU A 1 160 ? -3.614  11.054  21.153  1.00 17.59 ? 153 LEU A O   1 
ATOM   1178 C CB  . LEU A 1 160 ? -1.455  9.556   22.188  1.00 15.56 ? 153 LEU A CB  1 
ATOM   1179 C CG  . LEU A 1 160 ? -0.009  9.221   22.560  1.00 14.97 ? 153 LEU A CG  1 
ATOM   1180 C CD1 . LEU A 1 160 ? 0.122   9.047   24.074  1.00 15.69 ? 153 LEU A CD1 1 
ATOM   1181 C CD2 . LEU A 1 160 ? 0.479   7.966   21.846  1.00 15.89 ? 153 LEU A CD2 1 
ATOM   1182 N N   . LEU A 1 161 ? -3.684  9.636   19.374  1.00 18.54 ? 154 LEU A N   1 
ATOM   1183 C CA  . LEU A 1 161 ? -5.051  9.993   18.911  1.00 18.22 ? 154 LEU A CA  1 
ATOM   1184 C C   . LEU A 1 161 ? -6.073  9.246   19.733  1.00 18.69 ? 154 LEU A C   1 
ATOM   1185 O O   . LEU A 1 161 ? -5.861  8.046   20.035  1.00 17.01 ? 154 LEU A O   1 
ATOM   1186 C CB  . LEU A 1 161 ? -5.191  9.674   17.431  1.00 18.35 ? 154 LEU A CB  1 
ATOM   1187 C CG  . LEU A 1 161 ? -4.135  10.305  16.530  1.00 20.25 ? 154 LEU A CG  1 
ATOM   1188 C CD1 . LEU A 1 161 ? -4.402  9.947   15.079  1.00 23.88 ? 154 LEU A CD1 1 
ATOM   1189 C CD2 . LEU A 1 161 ? -4.073  11.795  16.719  1.00 23.99 ? 154 LEU A CD2 1 
ATOM   1190 N N   . LEU A 1 162 ? -7.228  9.886   19.995  1.00 20.38 ? 155 LEU A N   1 
ATOM   1191 C CA  . LEU A 1 162 ? -8.339  9.251   20.737  1.00 20.14 ? 155 LEU A CA  1 
ATOM   1192 C C   . LEU A 1 162 ? -9.635  9.509   19.991  1.00 19.52 ? 155 LEU A C   1 
ATOM   1193 O O   . LEU A 1 162 ? -9.765  10.562  19.447  1.00 21.82 ? 155 LEU A O   1 
ATOM   1194 C CB  . LEU A 1 162 ? -8.452  9.844   22.131  1.00 22.70 ? 155 LEU A CB  1 
ATOM   1195 C CG  . LEU A 1 162 ? -7.191  9.669   22.965  1.00 26.49 ? 155 LEU A CG  1 
ATOM   1196 C CD1 . LEU A 1 162 ? -7.092  10.762  24.023  1.00 29.53 ? 155 LEU A CD1 1 
ATOM   1197 C CD2 . LEU A 1 162 ? -7.208  8.290   23.552  1.00 23.87 ? 155 LEU A CD2 1 
ATOM   1198 N N   . ASN A 1 163 ? -10.494 8.528   20.003  1.00 20.17 ? 156 ASN A N   1 
ATOM   1199 C CA  . ASN A 1 163 ? -11.850 8.707   19.430  1.00 24.18 ? 156 ASN A CA  1 
ATOM   1200 C C   . ASN A 1 163 ? -12.845 8.781   20.583  1.00 24.51 ? 156 ASN A C   1 
ATOM   1201 O O   . ASN A 1 163 ? -12.440 8.843   21.729  1.00 21.51 ? 156 ASN A O   1 
ATOM   1202 C CB  . ASN A 1 163 ? -12.144 7.604   18.434  1.00 23.10 ? 156 ASN A CB  1 
ATOM   1203 C CG  . ASN A 1 163 ? -12.291 6.260   19.089  1.00 24.47 ? 156 ASN A CG  1 
ATOM   1204 O OD1 . ASN A 1 163 ? -12.395 6.123   20.323  1.00 24.20 ? 156 ASN A OD1 1 
ATOM   1205 N ND2 . ASN A 1 163 ? -12.315 5.246   18.249  1.00 26.59 ? 156 ASN A ND2 1 
ATOM   1206 N N   . THR A 1 164 ? -14.150 8.805   20.286  1.00 30.33 ? 157 THR A N   1 
ATOM   1207 C CA  . THR A 1 164 ? -15.139 9.216   21.305  1.00 27.15 ? 157 THR A CA  1 
ATOM   1208 C C   . THR A 1 164 ? -15.376 8.074   22.288  1.00 27.06 ? 157 THR A C   1 
ATOM   1209 O O   . THR A 1 164 ? -16.014 8.324   23.314  1.00 25.26 ? 157 THR A O   1 
ATOM   1210 C CB  . THR A 1 164 ? -16.401 9.756   20.610  1.00 29.45 ? 157 THR A CB  1 
ATOM   1211 O OG1 . THR A 1 164 ? -16.976 8.678   19.885  1.00 31.44 ? 157 THR A OG1 1 
ATOM   1212 C CG2 . THR A 1 164 ? -16.090 10.898  19.673  1.00 30.80 ? 157 THR A CG2 1 
ATOM   1213 N N   . THR A 1 165 ? -14.840 6.871   22.024  1.00 22.64 ? 158 THR A N   1 
ATOM   1214 C CA  . THR A 1 165 ? -14.930 5.699   22.907  1.00 24.60 ? 158 THR A CA  1 
ATOM   1215 C C   . THR A 1 165 ? -13.544 5.411   23.503  1.00 25.30 ? 158 THR A C   1 
ATOM   1216 O O   . THR A 1 165 ? -13.357 4.303   23.940  1.00 27.60 ? 158 THR A O   1 
ATOM   1217 C CB  . THR A 1 165 ? -15.490 4.517   22.127  1.00 25.47 ? 158 THR A CB  1 
ATOM   1218 O OG1 . THR A 1 165 ? -14.793 4.479   20.886  1.00 25.60 ? 158 THR A OG1 1 
ATOM   1219 C CG2 . THR A 1 165 ? -16.955 4.689   21.808  1.00 28.63 ? 158 THR A CG2 1 
ATOM   1220 N N   . CYS A 1 166 ? -12.684 6.417   23.547  1.00 22.62 ? 159 CYS A N   1 
ATOM   1221 C CA  . CYS A 1 166 ? -11.348 6.362   24.185  1.00 24.29 ? 159 CYS A CA  1 
ATOM   1222 C C   . CYS A 1 166 ? -10.518 5.220   23.566  1.00 23.11 ? 159 CYS A C   1 
ATOM   1223 O O   . CYS A 1 166 ? -9.604  4.737   24.232  1.00 21.43 ? 159 CYS A O   1 
ATOM   1224 C CB  . CYS A 1 166 ? -11.507 6.274   25.697  1.00 30.35 ? 159 CYS A CB  1 
ATOM   1225 S SG  . CYS A 1 166 ? -12.184 7.832   26.355  1.00 32.14 ? 159 CYS A SG  1 
ATOM   1226 N N   . ASP A 1 167 ? -10.742 4.870   22.301  1.00 21.82 ? 160 ASP A N   1 
ATOM   1227 C CA  . ASP A 1 167 ? -9.745  4.024   21.582  1.00 22.49 ? 160 ASP A CA  1 
ATOM   1228 C C   . ASP A 1 167 ? -8.538  4.899   21.318  1.00 18.77 ? 160 ASP A C   1 
ATOM   1229 O O   . ASP A 1 167 ? -8.718  6.023   20.872  1.00 17.91 ? 160 ASP A O   1 
ATOM   1230 C CB  . ASP A 1 167 ? -10.214 3.511   20.230  1.00 24.39 ? 160 ASP A CB  1 
ATOM   1231 C CG  . ASP A 1 167 ? -11.399 2.607   20.405  1.00 28.82 ? 160 ASP A CG  1 
ATOM   1232 O OD1 . ASP A 1 167 ? -11.341 1.746   21.296  1.00 30.73 ? 160 ASP A OD1 1 
ATOM   1233 O OD2 . ASP A 1 167 ? -12.380 2.842   19.698  1.00 36.14 ? 160 ASP A OD2 1 
ATOM   1234 N N   . LEU A 1 168 ? -7.324  4.388   21.553  1.00 16.05 ? 161 LEU A N   1 
ATOM   1235 C CA  . LEU A 1 168 ? -6.108  5.212   21.430  1.00 15.89 ? 161 LEU A CA  1 
ATOM   1236 C C   . LEU A 1 168 ? -5.289  4.647   20.276  1.00 15.03 ? 161 LEU A C   1 
ATOM   1237 O O   . LEU A 1 168 ? -5.179  3.435   20.190  1.00 16.30 ? 161 LEU A O   1 
ATOM   1238 C CB  . LEU A 1 168 ? -5.351  5.211   22.756  1.00 17.33 ? 161 LEU A CB  1 
ATOM   1239 C CG  . LEU A 1 168 ? -4.064  6.028   22.799  1.00 15.79 ? 161 LEU A CG  1 
ATOM   1240 C CD1 . LEU A 1 168 ? -3.828  6.509   24.227  1.00 16.46 ? 161 LEU A CD1 1 
ATOM   1241 C CD2 . LEU A 1 168 ? -2.889  5.207   22.277  1.00 17.02 ? 161 LEU A CD2 1 
ATOM   1242 N N   . LYS A 1 169 ? -4.773  5.521   19.429  1.00 14.76 ? 162 LYS A N   1 
ATOM   1243 C CA  . LYS A 1 169 ? -3.938  5.124   18.271  1.00 15.97 ? 162 LYS A CA  1 
ATOM   1244 C C   . LYS A 1 169 ? -2.695  5.993   18.188  1.00 16.33 ? 162 LYS A C   1 
ATOM   1245 O O   . LYS A 1 169 ? -2.772  7.240   18.213  1.00 14.99 ? 162 LYS A O   1 
ATOM   1246 C CB  . LYS A 1 169 ? -4.726  5.178   16.968  1.00 16.57 ? 162 LYS A CB  1 
ATOM   1247 C CG  . LYS A 1 169 ? -5.829  4.159   16.900  1.00 18.74 ? 162 LYS A CG  1 
ATOM   1248 C CD  . LYS A 1 169 ? -6.563  4.154   15.582  1.00 19.85 ? 162 LYS A CD  1 
ATOM   1249 C CE  . LYS A 1 169 ? -7.899  3.464   15.628  1.00 23.57 ? 162 LYS A CE  1 
ATOM   1250 N NZ  . LYS A 1 169 ? -7.737  2.015   15.461  1.00 26.33 ? 162 LYS A NZ  1 
ATOM   1251 N N   . ILE A 1 170 ? -1.539  5.338   18.125  1.00 13.33 ? 163 ILE A N   1 
ATOM   1252 C CA  . ILE A 1 170 ? -0.277  6.074   18.009  1.00 13.92 ? 163 ILE A CA  1 
ATOM   1253 C C   . ILE A 1 170 ? -0.181  6.554   16.554  1.00 13.55 ? 163 ILE A C   1 
ATOM   1254 O O   . ILE A 1 170 ? -0.438  5.768   15.642  1.00 14.33 ? 163 ILE A O   1 
ATOM   1255 C CB  . ILE A 1 170 ? 0.904   5.153   18.399  1.00 13.90 ? 163 ILE A CB  1 
ATOM   1256 C CG1 . ILE A 1 170 ? 0.783   4.661   19.847  1.00 13.25 ? 163 ILE A CG1 1 
ATOM   1257 C CG2 . ILE A 1 170 ? 2.256   5.826   18.160  1.00 13.56 ? 163 ILE A CG2 1 
ATOM   1258 C CD1 . ILE A 1 170 ? 1.688   3.487   20.189  1.00 14.11 ? 163 ILE A CD1 1 
ATOM   1259 N N   . CYS A 1 171 ? 0.314   7.768   16.369  1.00 16.37 ? 164 CYS A N   1 
ATOM   1260 C CA  . CYS A 1 171 ? 0.514   8.293   15.012  1.00 17.74 ? 164 CYS A CA  1 
ATOM   1261 C C   . CYS A 1 171 ? 1.871   8.988   14.930  1.00 19.46 ? 164 CYS A C   1 
ATOM   1262 O O   . CYS A 1 171 ? 2.631   8.987   15.913  1.00 20.10 ? 164 CYS A O   1 
ATOM   1263 C CB  . CYS A 1 171 ? -0.638  9.217   14.631  1.00 19.60 ? 164 CYS A CB  1 
ATOM   1264 S SG  . CYS A 1 171 ? -0.629  10.781  15.514  1.00 21.90 ? 164 CYS A SG  1 
ATOM   1265 N N   . ASP A 1 172 ? 2.154   9.520   13.744  1.00 20.47 ? 165 ASP A N   1 
ATOM   1266 C CA  . ASP A 1 172 ? 3.336   10.362  13.424  1.00 21.63 ? 165 ASP A CA  1 
ATOM   1267 C C   . ASP A 1 172 ? 4.636   9.558   13.544  1.00 20.98 ? 165 ASP A C   1 
ATOM   1268 O O   . ASP A 1 172 ? 5.385   9.767   14.495  1.00 21.19 ? 165 ASP A O   1 
ATOM   1269 C CB  . ASP A 1 172 ? 3.391   11.636  14.246  1.00 26.54 ? 165 ASP A CB  1 
ATOM   1270 C CG  . ASP A 1 172 ? 4.456   12.588  13.729  1.00 34.93 ? 165 ASP A CG  1 
ATOM   1271 O OD1 . ASP A 1 172 ? 5.228   12.188  12.800  1.00 35.37 ? 165 ASP A OD1 1 
ATOM   1272 O OD2 . ASP A 1 172 ? 4.529   13.712  14.267  1.00 44.80 ? 165 ASP A OD2 1 
ATOM   1273 N N   . PHE A 1 173 ? 4.930   8.744   12.541  1.00 20.17 ? 166 PHE A N   1 
ATOM   1274 C CA  . PHE A 1 173 ? 6.181   7.940   12.452  1.00 17.89 ? 166 PHE A CA  1 
ATOM   1275 C C   . PHE A 1 173 ? 7.231   8.612   11.577  1.00 18.76 ? 166 PHE A C   1 
ATOM   1276 O O   . PHE A 1 173 ? 8.174   7.920   11.118  1.00 20.16 ? 166 PHE A O   1 
ATOM   1277 C CB  . PHE A 1 173 ? 5.855   6.553   11.936  1.00 22.03 ? 166 PHE A CB  1 
ATOM   1278 C CG  . PHE A 1 173 ? 5.124   5.677   12.926  1.00 19.59 ? 166 PHE A CG  1 
ATOM   1279 C CD1 . PHE A 1 173 ? 3.774   5.836   13.196  1.00 19.17 ? 166 PHE A CD1 1 
ATOM   1280 C CD2 . PHE A 1 173 ? 5.800   4.698   13.629  1.00 21.73 ? 166 PHE A CD2 1 
ATOM   1281 C CE1 . PHE A 1 173 ? 3.113   5.033   14.121  1.00 18.67 ? 166 PHE A CE1 1 
ATOM   1282 C CE2 . PHE A 1 173 ? 5.141   3.877   14.540  1.00 18.48 ? 166 PHE A CE2 1 
ATOM   1283 C CZ  . PHE A 1 173 ? 3.789   4.025   14.779  1.00 18.80 ? 166 PHE A CZ  1 
ATOM   1284 N N   . GLY A 1 174 ? 7.155   9.926   11.460  1.00 20.30 ? 167 GLY A N   1 
ATOM   1285 C CA  . GLY A 1 174 ? 8.097   10.679  10.605  1.00 22.47 ? 167 GLY A CA  1 
ATOM   1286 C C   . GLY A 1 174 ? 9.521   10.608  11.119  1.00 22.32 ? 167 GLY A C   1 
ATOM   1287 O O   . GLY A 1 174 ? 10.442  10.681  10.287  1.00 24.42 ? 167 GLY A O   1 
ATOM   1288 N N   . LEU A 1 175 ? 9.738   10.436  12.425  1.00 20.74 ? 168 LEU A N   1 
ATOM   1289 C CA  . LEU A 1 175 ? 11.101  10.379  13.034  1.00 20.32 ? 168 LEU A CA  1 
ATOM   1290 C C   . LEU A 1 175 ? 11.462  8.933   13.408  1.00 18.53 ? 168 LEU A C   1 
ATOM   1291 O O   . LEU A 1 175 ? 12.518  8.711   14.054  1.00 21.68 ? 168 LEU A O   1 
ATOM   1292 C CB  . LEU A 1 175 ? 11.142  11.272  14.277  1.00 22.67 ? 168 LEU A CB  1 
ATOM   1293 C CG  . LEU A 1 175 ? 11.022  12.780  14.077  1.00 27.67 ? 168 LEU A CG  1 
ATOM   1294 C CD1 . LEU A 1 175 ? 11.351  13.515  15.365  1.00 27.86 ? 168 LEU A CD1 1 
ATOM   1295 C CD2 . LEU A 1 175 ? 11.933  13.240  12.955  1.00 28.13 ? 168 LEU A CD2 1 
ATOM   1296 N N   . ALA A 1 176 ? 10.659  7.979   12.997  1.00 18.53 ? 169 ALA A N   1 
ATOM   1297 C CA  . ALA A 1 176 ? 10.851  6.569   13.372  1.00 19.95 ? 169 ALA A CA  1 
ATOM   1298 C C   . ALA A 1 176 ? 12.079  6.005   12.665  1.00 22.71 ? 169 ALA A C   1 
ATOM   1299 O O   . ALA A 1 176 ? 12.443  6.476   11.546  1.00 25.38 ? 169 ALA A O   1 
ATOM   1300 C CB  . ALA A 1 176 ? 9.604   5.800   13.077  1.00 20.16 ? 169 ALA A CB  1 
ATOM   1301 N N   . ARG A 1 177 ? 12.757  5.068   13.302  1.00 21.90 ? 170 ARG A N   1 
ATOM   1302 C CA  . ARG A 1 177 ? 13.946  4.408   12.721  1.00 22.87 ? 170 ARG A CA  1 
ATOM   1303 C C   . ARG A 1 177 ? 13.885  2.919   13.027  1.00 22.32 ? 170 ARG A C   1 
ATOM   1304 O O   . ARG A 1 177 ? 13.226  2.498   13.998  1.00 19.40 ? 170 ARG A O   1 
ATOM   1305 C CB  . ARG A 1 177 ? 15.274  4.973   13.216  1.00 24.16 ? 170 ARG A CB  1 
ATOM   1306 C CG  . ARG A 1 177 ? 15.490  6.451   12.915  1.00 28.73 ? 170 ARG A CG  1 
ATOM   1307 C CD  . ARG A 1 177 ? 16.166  6.727   11.569  1.00 37.43 ? 170 ARG A CD  1 
ATOM   1308 N NE  . ARG A 1 177 ? 16.641  8.100   11.592  1.00 42.30 ? 170 ARG A NE  1 
ATOM   1309 C CZ  . ARG A 1 177 ? 15.857  9.187   11.558  1.00 47.43 ? 170 ARG A CZ  1 
ATOM   1310 N NH1 . ARG A 1 177 ? 14.539  9.080   11.442  1.00 37.10 ? 170 ARG A NH1 1 
ATOM   1311 N NH2 . ARG A 1 177 ? 16.404  10.391  11.661  1.00 50.13 ? 170 ARG A NH2 1 
ATOM   1312 N N   . VAL A 1 178 ? 14.544  2.139   12.183  1.00 18.84 ? 171 VAL A N   1 
ATOM   1313 C CA  . VAL A 1 178 ? 14.876  0.746   12.549  1.00 21.16 ? 171 VAL A CA  1 
ATOM   1314 C C   . VAL A 1 178 ? 15.869  0.782   13.725  1.00 20.33 ? 171 VAL A C   1 
ATOM   1315 O O   . VAL A 1 178 ? 16.846  1.558   13.684  1.00 21.73 ? 171 VAL A O   1 
ATOM   1316 C CB  . VAL A 1 178 ? 15.394  -0.003  11.321  1.00 22.17 ? 171 VAL A CB  1 
ATOM   1317 C CG1 . VAL A 1 178 ? 15.803  -1.421  11.649  1.00 21.92 ? 171 VAL A CG1 1 
ATOM   1318 C CG2 . VAL A 1 178 ? 14.343  0.031   10.231  1.00 25.08 ? 171 VAL A CG2 1 
ATOM   1319 N N   . ALA A 1 179 ? 15.650  -0.047  14.740  1.00 19.90 ? 172 ALA A N   1 
ATOM   1320 C CA  . ALA A 1 179 ? 16.487  -0.094  15.960  1.00 21.80 ? 172 ALA A CA  1 
ATOM   1321 C C   . ALA A 1 179 ? 17.928  -0.441  15.562  1.00 24.98 ? 172 ALA A C   1 
ATOM   1322 O O   . ALA A 1 179 ? 18.102  -1.179  14.553  1.00 21.99 ? 172 ALA A O   1 
ATOM   1323 C CB  . ALA A 1 179 ? 15.894  -1.055  16.947  1.00 22.80 ? 172 ALA A CB  1 
ATOM   1324 N N   . ASP A 1 180 ? 18.923  0.148   16.236  1.00 21.82 ? 173 ASP A N   1 
ATOM   1325 C CA  . ASP A 1 180 ? 20.357  0.013   15.821  1.00 22.86 ? 173 ASP A CA  1 
ATOM   1326 C C   . ASP A 1 180 ? 21.191  0.246   17.069  1.00 22.91 ? 173 ASP A C   1 
ATOM   1327 O O   . ASP A 1 180 ? 21.944  1.222   17.147  1.00 25.19 ? 173 ASP A O   1 
ATOM   1328 C CB  . ASP A 1 180 ? 20.693  0.976   14.685  1.00 26.12 ? 173 ASP A CB  1 
ATOM   1329 C CG  . ASP A 1 180 ? 22.055  0.772   14.019  1.00 28.37 ? 173 ASP A CG  1 
ATOM   1330 O OD1 . ASP A 1 180 ? 22.720  -0.212  14.320  1.00 33.67 ? 173 ASP A OD1 1 
ATOM   1331 O OD2 . ASP A 1 180 ? 22.423  1.613   13.195  1.00 30.78 ? 173 ASP A OD2 1 
ATOM   1332 N N   . PRO A 1 181 ? 21.010  -0.613  18.094  1.00 25.30 ? 174 PRO A N   1 
ATOM   1333 C CA  . PRO A 1 181 ? 21.685  -0.451  19.381  1.00 27.88 ? 174 PRO A CA  1 
ATOM   1334 C C   . PRO A 1 181 ? 23.212  -0.411  19.223  1.00 33.20 ? 174 PRO A C   1 
ATOM   1335 O O   . PRO A 1 181 ? 23.874  0.304   20.007  1.00 32.67 ? 174 PRO A O   1 
ATOM   1336 C CB  . PRO A 1 181 ? 21.240  -1.670  20.214  1.00 29.72 ? 174 PRO A CB  1 
ATOM   1337 C CG  . PRO A 1 181 ? 20.599  -2.613  19.234  1.00 29.48 ? 174 PRO A CG  1 
ATOM   1338 C CD  . PRO A 1 181 ? 20.066  -1.750  18.121  1.00 28.61 ? 174 PRO A CD  1 
ATOM   1339 N N   . ASP A 1 182 ? 23.729  -1.127  18.215  1.00 29.99 ? 175 ASP A N   1 
ATOM   1340 C CA  . ASP A 1 182 ? 25.189  -1.212  17.928  1.00 35.53 ? 175 ASP A CA  1 
ATOM   1341 C C   . ASP A 1 182 ? 25.759  0.153   17.610  1.00 35.92 ? 175 ASP A C   1 
ATOM   1342 O O   . ASP A 1 182 ? 26.955  0.342   17.888  1.00 39.31 ? 175 ASP A O   1 
ATOM   1343 C CB  . ASP A 1 182 ? 25.503  -2.102  16.720  1.00 39.40 ? 175 ASP A CB  1 
ATOM   1344 C CG  . ASP A 1 182 ? 25.476  -3.557  17.096  1.00 37.74 ? 175 ASP A CG  1 
ATOM   1345 O OD1 . ASP A 1 182 ? 25.103  -3.828  18.234  1.00 41.28 ? 175 ASP A OD1 1 
ATOM   1346 O OD2 . ASP A 1 182 ? 25.840  -4.399  16.244  1.00 52.33 ? 175 ASP A OD2 1 
ATOM   1347 N N   . HIS A 1 183 ? 24.955  1.018   16.993  1.00 28.60 ? 176 HIS A N   1 
ATOM   1348 C CA  . HIS A 1 183 ? 25.384  2.322   16.428  1.00 32.57 ? 176 HIS A CA  1 
ATOM   1349 C C   . HIS A 1 183 ? 24.682  3.461   17.178  1.00 26.07 ? 176 HIS A C   1 
ATOM   1350 O O   . HIS A 1 183 ? 24.494  4.518   16.591  1.00 29.35 ? 176 HIS A O   1 
ATOM   1351 C CB  . HIS A 1 183 ? 25.140  2.285   14.916  1.00 34.35 ? 176 HIS A CB  1 
ATOM   1352 C CG  . HIS A 1 183 ? 25.952  1.212   14.260  1.00 40.99 ? 176 HIS A CG  1 
ATOM   1353 N ND1 . HIS A 1 183 ? 25.566  -0.126  14.264  1.00 47.31 ? 176 HIS A ND1 1 
ATOM   1354 C CD2 . HIS A 1 183 ? 27.154  1.256   13.638  1.00 42.18 ? 176 HIS A CD2 1 
ATOM   1355 C CE1 . HIS A 1 183 ? 26.479  -0.852  13.647  1.00 47.88 ? 176 HIS A CE1 1 
ATOM   1356 N NE2 . HIS A 1 183 ? 27.463  -0.023  13.255  1.00 47.20 ? 176 HIS A NE2 1 
ATOM   1357 N N   . ASP A 1 184 ? 24.395  3.245   18.467  1.00 28.09 ? 177 ASP A N   1 
ATOM   1358 C CA  . ASP A 1 184 ? 23.611  4.191   19.301  1.00 24.84 ? 177 ASP A CA  1 
ATOM   1359 C C   . ASP A 1 184 ? 24.524  5.264   19.915  1.00 25.43 ? 177 ASP A C   1 
ATOM   1360 O O   . ASP A 1 184 ? 24.029  6.340   20.296  1.00 23.88 ? 177 ASP A O   1 
ATOM   1361 C CB  . ASP A 1 184 ? 22.847  3.459   20.403  1.00 25.50 ? 177 ASP A CB  1 
ATOM   1362 C CG  . ASP A 1 184 ? 21.882  4.383   21.126  1.00 26.88 ? 177 ASP A CG  1 
ATOM   1363 O OD1 . ASP A 1 184 ? 21.082  5.020   20.428  1.00 27.58 ? 177 ASP A OD1 1 
ATOM   1364 O OD2 . ASP A 1 184 ? 22.020  4.514   22.336  1.00 30.86 ? 177 ASP A OD2 1 
ATOM   1365 N N   . HIS A 1 185 ? 25.826  5.045   19.964  1.00 26.87 ? 178 HIS A N   1 
ATOM   1366 C CA  . HIS A 1 185 ? 26.705  5.957   20.733  1.00 27.87 ? 178 HIS A CA  1 
ATOM   1367 C C   . HIS A 1 185 ? 27.013  7.226   19.935  1.00 26.15 ? 178 HIS A C   1 
ATOM   1368 O O   . HIS A 1 185 ? 27.226  7.215   18.679  1.00 25.65 ? 178 HIS A O   1 
ATOM   1369 C CB  . HIS A 1 185 ? 27.977  5.261   21.201  1.00 31.64 ? 178 HIS A CB  1 
ATOM   1370 C CG  . HIS A 1 185 ? 28.554  5.979   22.370  1.00 40.74 ? 178 HIS A CG  1 
ATOM   1371 N ND1 . HIS A 1 185 ? 29.240  7.191   22.231  1.00 47.72 ? 178 HIS A ND1 1 
ATOM   1372 C CD2 . HIS A 1 185 ? 28.497  5.731   23.700  1.00 47.49 ? 178 HIS A CD2 1 
ATOM   1373 C CE1 . HIS A 1 185 ? 29.584  7.651   23.418  1.00 31.11 ? 178 HIS A CE1 1 
ATOM   1374 N NE2 . HIS A 1 185 ? 29.159  6.764   24.341  1.00 49.19 ? 178 HIS A NE2 1 
ATOM   1375 N N   . THR A 1 186 ? 27.118  8.333   20.652  1.00 22.94 ? 179 THR A N   1 
ATOM   1376 C CA  . THR A 1 186 ? 27.468  9.610   20.018  1.00 22.11 ? 179 THR A CA  1 
ATOM   1377 C C   . THR A 1 186 ? 28.107  10.481  21.102  1.00 19.59 ? 179 THR A C   1 
ATOM   1378 O O   . THR A 1 186 ? 28.148  10.055  22.255  1.00 23.76 ? 179 THR A O   1 
ATOM   1379 C CB  . THR A 1 186 ? 26.244  10.257  19.350  1.00 24.32 ? 179 THR A CB  1 
ATOM   1380 O OG1 . THR A 1 186 ? 26.678  11.375  18.563  1.00 25.79 ? 179 THR A OG1 1 
ATOM   1381 C CG2 . THR A 1 186 ? 25.169  10.675  20.337  1.00 22.62 ? 179 THR A CG2 1 
ATOM   1382 N N   . GLY A 1 187 ? 28.612  11.639  20.690  1.00 21.11 ? 180 GLY A N   1 
ATOM   1383 C CA  . GLY A 1 187 ? 29.208  12.602  21.607  1.00 23.08 ? 180 GLY A CA  1 
ATOM   1384 C C   . GLY A 1 187 ? 28.168  13.311  22.461  1.00 24.13 ? 180 GLY A C   1 
ATOM   1385 O O   . GLY A 1 187 ? 26.959  13.115  22.290  1.00 23.31 ? 180 GLY A O   1 
ATOM   1386 N N   . PHE A 1 188 ? 28.673  14.019  23.454  1.00 22.46 ? 181 PHE A N   1 
ATOM   1387 C CA  . PHE A 1 188 ? 27.933  14.870  24.408  1.00 22.49 ? 181 PHE A CA  1 
ATOM   1388 C C   . PHE A 1 188 ? 27.326  16.031  23.618  1.00 22.14 ? 181 PHE A C   1 
ATOM   1389 O O   . PHE A 1 188 ? 27.995  16.631  22.762  1.00 23.97 ? 181 PHE A O   1 
ATOM   1390 C CB  . PHE A 1 188 ? 28.923  15.325  25.491  1.00 21.81 ? 181 PHE A CB  1 
ATOM   1391 C CG  . PHE A 1 188 ? 28.336  16.195  26.580  1.00 21.94 ? 181 PHE A CG  1 
ATOM   1392 C CD1 . PHE A 1 188 ? 27.137  15.864  27.200  1.00 21.18 ? 181 PHE A CD1 1 
ATOM   1393 C CD2 . PHE A 1 188 ? 28.970  17.374  26.974  1.00 22.34 ? 181 PHE A CD2 1 
ATOM   1394 C CE1 . PHE A 1 188 ? 26.592  16.673  28.175  1.00 21.33 ? 181 PHE A CE1 1 
ATOM   1395 C CE2 . PHE A 1 188 ? 28.426  18.163  27.969  1.00 20.15 ? 181 PHE A CE2 1 
ATOM   1396 C CZ  . PHE A 1 188 ? 27.226  17.829  28.548  1.00 20.82 ? 181 PHE A CZ  1 
ATOM   1397 N N   . LEU A 1 189 ? 26.065  16.331  23.888  1.00 22.02 ? 182 LEU A N   1 
ATOM   1398 C CA  . LEU A 1 189 ? 25.378  17.511  23.306  1.00 23.57 ? 182 LEU A CA  1 
ATOM   1399 C C   . LEU A 1 189 ? 25.112  17.281  21.818  1.00 24.31 ? 182 LEU A C   1 
ATOM   1400 O O   . LEU A 1 189 ? 25.203  18.258  21.070  1.00 24.45 ? 182 LEU A O   1 
ATOM   1401 C CB  . LEU A 1 189 ? 26.253  18.759  23.491  1.00 25.87 ? 182 LEU A CB  1 
ATOM   1402 C CG  . LEU A 1 189 ? 26.630  19.112  24.925  1.00 29.74 ? 182 LEU A CG  1 
ATOM   1403 C CD1 . LEU A 1 189 ? 27.576  20.310  24.956  1.00 30.74 ? 182 LEU A CD1 1 
ATOM   1404 C CD2 . LEU A 1 189 ? 25.388  19.389  25.722  1.00 28.75 ? 182 LEU A CD2 1 
ATOM   1405 N N   . THR A 1 190 ? 24.845  16.042  21.382  1.00 22.22 ? 183 THR A N   1 
ATOM   1406 C CA  . THR A 1 190 ? 24.499  15.789  19.961  1.00 23.96 ? 183 THR A CA  1 
ATOM   1407 C C   . THR A 1 190 ? 23.083  16.298  19.684  1.00 27.10 ? 183 THR A C   1 
ATOM   1408 O O   . THR A 1 190 ? 22.172  15.916  20.449  1.00 25.76 ? 183 THR A O   1 
ATOM   1409 C CB  . THR A 1 190 ? 24.593  14.315  19.583  1.00 26.26 ? 183 THR A CB  1 
ATOM   1410 O OG1 . THR A 1 190 ? 25.927  13.906  19.907  1.00 26.57 ? 183 THR A OG1 1 
ATOM   1411 C CG2 . THR A 1 190 ? 24.256  14.109  18.119  1.00 26.17 ? 183 THR A CG2 1 
ATOM   1412 N N   . GLU A 1 191 ? 22.912  17.101  18.624  1.00 25.91 ? 184 GLU A N   1 
ATOM   1413 C CA  . GLU A 1 191 ? 21.609  17.734  18.249  1.00 30.68 ? 184 GLU A CA  1 
ATOM   1414 C C   . GLU A 1 191 ? 20.556  16.635  18.055  1.00 29.60 ? 184 GLU A C   1 
ATOM   1415 O O   . GLU A 1 191 ? 20.870  15.562  17.507  1.00 26.54 ? 184 GLU A O   1 
ATOM   1416 C CB  . GLU A 1 191 ? 21.741  18.580  16.969  1.00 36.11 ? 184 GLU A CB  1 
ATOM   1417 C CG  . GLU A 1 191 ? 22.443  19.935  17.172  1.00 44.23 ? 184 GLU A CG  1 
ATOM   1418 C CD  . GLU A 1 191 ? 22.276  20.638  18.522  1.00 50.92 ? 184 GLU A CD  1 
ATOM   1419 O OE1 . GLU A 1 191 ? 21.113  20.881  18.953  1.00 48.93 ? 184 GLU A OE1 1 
ATOM   1420 O OE2 . GLU A 1 191 ? 23.318  20.953  19.159  1.00 55.54 ? 184 GLU A OE2 1 
ATOM   1421 N N   . TYR A 1 192 ? 19.326  16.899  18.473  1.00 27.81 ? 185 TYR A N   1 
ATOM   1422 C CA  . TYR A 1 192 ? 18.220  15.912  18.401  1.00 28.12 ? 185 TYR A CA  1 
ATOM   1423 C C   . TYR A 1 192 ? 16.975  16.624  17.884  1.00 29.22 ? 185 TYR A C   1 
ATOM   1424 O O   . TYR A 1 192 ? 16.849  17.850  18.147  1.00 31.48 ? 185 TYR A O   1 
ATOM   1425 C CB  . TYR A 1 192 ? 17.946  15.352  19.787  1.00 26.67 ? 185 TYR A CB  1 
ATOM   1426 C CG  . TYR A 1 192 ? 17.316  13.991  19.773  1.00 28.88 ? 185 TYR A CG  1 
ATOM   1427 C CD1 . TYR A 1 192 ? 18.012  12.914  19.256  1.00 26.53 ? 185 TYR A CD1 1 
ATOM   1428 C CD2 . TYR A 1 192 ? 16.033  13.778  20.270  1.00 27.07 ? 185 TYR A CD2 1 
ATOM   1429 C CE1 . TYR A 1 192 ? 17.452  11.651  19.196  1.00 30.34 ? 185 TYR A CE1 1 
ATOM   1430 C CE2 . TYR A 1 192 ? 15.474  12.514  20.225  1.00 27.16 ? 185 TYR A CE2 1 
ATOM   1431 C CZ  . TYR A 1 192 ? 16.187  11.450  19.705  1.00 29.48 ? 185 TYR A CZ  1 
ATOM   1432 O OH  . TYR A 1 192 ? 15.674  10.181  19.681  1.00 34.02 ? 185 TYR A OH  1 
ATOM   1433 N N   . VAL A 1 193 ? 16.101  15.891  17.193  1.00 30.94 ? 186 VAL A N   1 
ATOM   1434 C CA  . VAL A 1 193 ? 14.899  16.467  16.521  1.00 31.63 ? 186 VAL A CA  1 
ATOM   1435 C C   . VAL A 1 193 ? 13.661  16.282  17.428  1.00 31.69 ? 186 VAL A C   1 
ATOM   1436 O O   . VAL A 1 193 ? 12.859  17.226  17.510  1.00 32.67 ? 186 VAL A O   1 
ATOM   1437 C CB  . VAL A 1 193 ? 14.702  15.844  15.121  1.00 35.82 ? 186 VAL A CB  1 
ATOM   1438 C CG1 . VAL A 1 193 ? 13.571  16.533  14.368  1.00 34.58 ? 186 VAL A CG1 1 
ATOM   1439 C CG2 . VAL A 1 193 ? 15.983  15.885  14.299  1.00 38.98 ? 186 VAL A CG2 1 
ATOM   1440 N N   . ALA A 1 194 ? 13.487  15.138  18.102  1.00 27.47 ? 187 ALA A N   1 
ATOM   1441 C CA  . ALA A 1 194 ? 12.196  14.806  18.766  1.00 26.95 ? 187 ALA A CA  1 
ATOM   1442 C C   . ALA A 1 194 ? 11.921  15.776  19.920  1.00 30.05 ? 187 ALA A C   1 
ATOM   1443 O O   . ALA A 1 194 ? 12.871  16.338  20.478  1.00 25.81 ? 187 ALA A O   1 
ATOM   1444 C CB  . ALA A 1 194 ? 12.144  13.364  19.259  1.00 26.99 ? 187 ALA A CB  1 
ATOM   1445 N N   . GLU A 1 195 ? 10.641  15.939  20.286  1.00 27.79 ? 188 GLU A N   1 
ATOM   1446 C CA  . GLU A 1 195 ? 10.221  16.999  21.241  1.00 30.02 ? 188 GLU A CA  1 
ATOM   1447 C C   . GLU A 1 195 ? 11.038  16.853  22.526  1.00 27.34 ? 188 GLU A C   1 
ATOM   1448 O O   . GLU A 1 195 ? 11.066  15.711  23.112  1.00 23.24 ? 188 GLU A O   1 
ATOM   1449 C CB  . GLU A 1 195 ? 8.721   16.948  21.535  1.00 31.18 ? 188 GLU A CB  1 
ATOM   1450 C CG  . GLU A 1 195 ? 8.310   17.680  22.825  1.00 35.12 ? 188 GLU A CG  1 
ATOM   1451 C CD  . GLU A 1 195 ? 8.360   19.199  22.841  1.00 42.36 ? 188 GLU A CD  1 
ATOM   1452 O OE1 . GLU A 1 195 ? 7.772   19.770  21.907  1.00 43.16 ? 188 GLU A OE1 1 
ATOM   1453 O OE2 . GLU A 1 195 ? 8.940   19.810  23.830  1.00 34.61 ? 188 GLU A OE2 1 
ATOM   1454 N N   . ARG A 1 196 ? 11.579  17.992  22.987  1.00 23.90 ? 189 ARG A N   1 
ATOM   1455 C CA  . ARG A 1 196 ? 12.570  18.056  24.087  1.00 23.59 ? 189 ARG A CA  1 
ATOM   1456 C C   . ARG A 1 196 ? 12.011  17.377  25.347  1.00 19.33 ? 189 ARG A C   1 
ATOM   1457 O O   . ARG A 1 196 ? 12.715  16.641  25.980  1.00 20.67 ? 189 ARG A O   1 
ATOM   1458 C CB  . ARG A 1 196 ? 12.899  19.521  24.375  1.00 25.57 ? 189 ARG A CB  1 
ATOM   1459 C CG  . ARG A 1 196 ? 13.863  19.689  25.528  1.00 28.47 ? 189 ARG A CG  1 
ATOM   1460 C CD  . ARG A 1 196 ? 14.085  21.133  25.975  1.00 30.40 ? 189 ARG A CD  1 
ATOM   1461 N NE  . ARG A 1 196 ? 14.356  21.982  24.828  1.00 33.39 ? 189 ARG A NE  1 
ATOM   1462 C CZ  . ARG A 1 196 ? 13.798  23.172  24.565  1.00 37.58 ? 189 ARG A CZ  1 
ATOM   1463 N NH1 . ARG A 1 196 ? 12.987  23.778  25.422  1.00 31.58 ? 189 ARG A NH1 1 
ATOM   1464 N NH2 . ARG A 1 196 ? 14.147  23.801  23.459  1.00 37.24 ? 189 ARG A NH2 1 
ATOM   1465 N N   . TRP A 1 197 ? 10.784  17.703  25.745  1.00 18.74 ? 190 TRP A N   1 
ATOM   1466 C CA  . TRP A 1 197 ? 10.275  17.337  27.082  1.00 18.33 ? 190 TRP A CA  1 
ATOM   1467 C C   . TRP A 1 197 ? 10.136  15.808  27.210  1.00 16.49 ? 190 TRP A C   1 
ATOM   1468 O O   . TRP A 1 197 ? 10.032  15.367  28.325  1.00 18.22 ? 190 TRP A O   1 
ATOM   1469 C CB  . TRP A 1 197 ? 8.899   17.959  27.303  1.00 21.17 ? 190 TRP A CB  1 
ATOM   1470 C CG  . TRP A 1 197 ? 8.912   19.452  27.335  1.00 23.68 ? 190 TRP A CG  1 
ATOM   1471 C CD1 . TRP A 1 197 ? 9.967   20.296  27.492  1.00 27.28 ? 190 TRP A CD1 1 
ATOM   1472 C CD2 . TRP A 1 197 ? 7.730   20.264  27.316  1.00 25.43 ? 190 TRP A CD2 1 
ATOM   1473 N NE1 . TRP A 1 197 ? 9.532   21.604  27.482  1.00 26.46 ? 190 TRP A NE1 1 
ATOM   1474 C CE2 . TRP A 1 197 ? 8.156   21.605  27.415  1.00 29.73 ? 190 TRP A CE2 1 
ATOM   1475 C CE3 . TRP A 1 197 ? 6.371   19.976  27.170  1.00 28.56 ? 190 TRP A CE3 1 
ATOM   1476 C CZ2 . TRP A 1 197 ? 7.249   22.667  27.399  1.00 32.67 ? 190 TRP A CZ2 1 
ATOM   1477 C CZ3 . TRP A 1 197 ? 5.477   21.028  27.154  1.00 32.54 ? 190 TRP A CZ3 1 
ATOM   1478 C CH2 . TRP A 1 197 ? 5.914   22.347  27.277  1.00 32.22 ? 190 TRP A CH2 1 
ATOM   1479 N N   . TYR A 1 198 ? 10.147  15.065  26.112  1.00 16.50 ? 191 TYR A N   1 
ATOM   1480 C CA  . TYR A 1 198 ? 9.920   13.597  26.188  1.00 15.09 ? 191 TYR A CA  1 
ATOM   1481 C C   . TYR A 1 198 ? 11.186  12.827  25.863  1.00 13.72 ? 191 TYR A C   1 
ATOM   1482 O O   . TYR A 1 198 ? 11.162  11.608  25.806  1.00 14.69 ? 191 TYR A O   1 
ATOM   1483 C CB  . TYR A 1 198 ? 8.738   13.208  25.304  1.00 14.25 ? 191 TYR A CB  1 
ATOM   1484 C CG  . TYR A 1 198 ? 7.514   14.019  25.669  1.00 15.47 ? 191 TYR A CG  1 
ATOM   1485 C CD1 . TYR A 1 198 ? 6.677   13.623  26.672  1.00 16.74 ? 191 TYR A CD1 1 
ATOM   1486 C CD2 . TYR A 1 198 ? 7.263   15.219  25.047  1.00 17.55 ? 191 TYR A CD2 1 
ATOM   1487 C CE1 . TYR A 1 198 ? 5.593   14.407  27.053  1.00 17.93 ? 191 TYR A CE1 1 
ATOM   1488 C CE2 . TYR A 1 198 ? 6.188   16.024  25.410  1.00 17.53 ? 191 TYR A CE2 1 
ATOM   1489 C CZ  . TYR A 1 198 ? 5.379   15.621  26.446  1.00 18.36 ? 191 TYR A CZ  1 
ATOM   1490 O OH  . TYR A 1 198 ? 4.303   16.393  26.800  1.00 20.24 ? 191 TYR A OH  1 
ATOM   1491 N N   . ARG A 1 199 ? 12.308  13.514  25.772  1.00 16.41 ? 192 ARG A N   1 
ATOM   1492 C CA  . ARG A 1 199 ? 13.611  12.873  25.456  1.00 17.75 ? 192 ARG A CA  1 
ATOM   1493 C C   . ARG A 1 199 ? 14.232  12.222  26.681  1.00 15.24 ? 192 ARG A C   1 
ATOM   1494 O O   . ARG A 1 199 ? 14.392  12.868  27.739  1.00 16.67 ? 192 ARG A O   1 
ATOM   1495 C CB  . ARG A 1 199 ? 14.635  13.922  25.016  1.00 18.71 ? 192 ARG A CB  1 
ATOM   1496 C CG  . ARG A 1 199 ? 14.293  14.648  23.757  1.00 21.13 ? 192 ARG A CG  1 
ATOM   1497 C CD  . ARG A 1 199 ? 15.309  15.755  23.548  1.00 24.29 ? 192 ARG A CD  1 
ATOM   1498 N NE  . ARG A 1 199 ? 14.965  16.493  22.369  1.00 24.57 ? 192 ARG A NE  1 
ATOM   1499 C CZ  . ARG A 1 199 ? 15.457  17.689  22.059  1.00 29.90 ? 192 ARG A CZ  1 
ATOM   1500 N NH1 . ARG A 1 199 ? 16.386  18.253  22.822  1.00 32.78 ? 192 ARG A NH1 1 
ATOM   1501 N NH2 . ARG A 1 199 ? 14.992  18.306  20.996  1.00 28.86 ? 192 ARG A NH2 1 
ATOM   1502 N N   . ALA A 1 200 ? 14.726  10.992  26.517  1.00 15.70 ? 193 ALA A N   1 
ATOM   1503 C CA  . ALA A 1 200 ? 15.444  10.249  27.560  1.00 16.00 ? 193 ALA A CA  1 
ATOM   1504 C C   . ALA A 1 200 ? 16.747  10.970  27.913  1.00 14.85 ? 193 ALA A C   1 
ATOM   1505 O O   . ALA A 1 200 ? 17.312  11.620  27.052  1.00 16.28 ? 193 ALA A O   1 
ATOM   1506 C CB  . ALA A 1 200 ? 15.721  8.843   27.070  1.00 16.32 ? 193 ALA A CB  1 
ATOM   1507 N N   . PRO A 1 201 ? 17.218  10.822  29.163  1.00 17.11 ? 194 PRO A N   1 
ATOM   1508 C CA  . PRO A 1 201 ? 18.427  11.511  29.622  1.00 16.73 ? 194 PRO A CA  1 
ATOM   1509 C C   . PRO A 1 201 ? 19.604  11.193  28.694  1.00 15.83 ? 194 PRO A C   1 
ATOM   1510 O O   . PRO A 1 201 ? 20.410  12.162  28.347  1.00 17.63 ? 194 PRO A O   1 
ATOM   1511 C CB  . PRO A 1 201 ? 18.608  11.061  31.067  1.00 18.59 ? 194 PRO A CB  1 
ATOM   1512 C CG  . PRO A 1 201 ? 17.719  9.843   31.239  1.00 20.14 ? 194 PRO A CG  1 
ATOM   1513 C CD  . PRO A 1 201 ? 16.601  10.037  30.230  1.00 17.16 ? 194 PRO A CD  1 
ATOM   1514 N N   . GLU A 1 202 ? 19.733  9.934   28.241  1.00 15.49 ? 195 GLU A N   1 
ATOM   1515 C CA  . GLU A 1 202 ? 20.922  9.503   27.425  1.00 15.41 ? 195 GLU A CA  1 
ATOM   1516 C C   . GLU A 1 202 ? 20.987  10.265  26.081  1.00 16.04 ? 195 GLU A C   1 
ATOM   1517 O O   . GLU A 1 202 ? 22.068  10.402  25.522  1.00 17.65 ? 195 GLU A O   1 
ATOM   1518 C CB  . GLU A 1 202 ? 20.920  7.973   27.262  1.00 16.03 ? 195 GLU A CB  1 
ATOM   1519 C CG  . GLU A 1 202 ? 19.702  7.401   26.562  1.00 16.59 ? 195 GLU A CG  1 
ATOM   1520 C CD  . GLU A 1 202 ? 18.535  7.031   27.458  1.00 17.07 ? 195 GLU A CD  1 
ATOM   1521 O OE1 . GLU A 1 202 ? 18.430  7.545   28.618  1.00 17.22 ? 195 GLU A OE1 1 
ATOM   1522 O OE2 . GLU A 1 202 ? 17.710  6.187   27.010  1.00 16.57 ? 195 GLU A OE2 1 
ATOM   1523 N N   . ILE A 1 203 ? 19.877  10.826  25.563  1.00 15.80 ? 196 ILE A N   1 
ATOM   1524 C CA  . ILE A 1 203 ? 19.929  11.587  24.294  1.00 18.16 ? 196 ILE A CA  1 
ATOM   1525 C C   . ILE A 1 203 ? 20.853  12.793  24.476  1.00 20.61 ? 196 ILE A C   1 
ATOM   1526 O O   . ILE A 1 203 ? 21.559  13.122  23.527  1.00 20.82 ? 196 ILE A O   1 
ATOM   1527 C CB  . ILE A 1 203 ? 18.518  12.037  23.894  1.00 20.46 ? 196 ILE A CB  1 
ATOM   1528 C CG1 . ILE A 1 203 ? 17.637  10.832  23.599  1.00 20.99 ? 196 ILE A CG1 1 
ATOM   1529 C CG2 . ILE A 1 203 ? 18.564  13.039  22.750  1.00 22.37 ? 196 ILE A CG2 1 
ATOM   1530 C CD1 . ILE A 1 203 ? 18.190  9.901   22.625  1.00 23.22 ? 196 ILE A CD1 1 
ATOM   1531 N N   . MET A 1 204 ? 20.866  13.382  25.662  1.00 20.17 ? 197 MET A N   1 
ATOM   1532 C CA  . MET A 1 204 ? 21.638  14.622  25.921  1.00 23.21 ? 197 MET A CA  1 
ATOM   1533 C C   . MET A 1 204 ? 23.083  14.256  26.272  1.00 24.53 ? 197 MET A C   1 
ATOM   1534 O O   . MET A 1 204 ? 23.958  15.147  26.224  1.00 29.61 ? 197 MET A O   1 
ATOM   1535 C CB  . MET A 1 204 ? 20.984  15.435  27.035  1.00 22.92 ? 197 MET A CB  1 
ATOM   1536 C CG  . MET A 1 204 ? 19.760  16.183  26.561  1.00 24.35 ? 197 MET A CG  1 
ATOM   1537 S SD  . MET A 1 204 ? 18.252  15.188  26.428  1.00 24.96 ? 197 MET A SD  1 
ATOM   1538 C CE  . MET A 1 204 ? 17.797  14.983  28.140  1.00 24.39 ? 197 MET A CE  1 
ATOM   1539 N N   . LEU A 1 205 ? 23.335  12.984  26.526  1.00 19.47 ? 198 LEU A N   1 
ATOM   1540 C CA  . LEU A 1 205 ? 24.631  12.542  27.052  1.00 18.94 ? 198 LEU A CA  1 
ATOM   1541 C C   . LEU A 1 205 ? 25.429  11.844  25.954  1.00 22.34 ? 198 LEU A C   1 
ATOM   1542 O O   . LEU A 1 205 ? 26.519  12.331  25.606  1.00 22.06 ? 198 LEU A O   1 
ATOM   1543 C CB  . LEU A 1 205 ? 24.348  11.644  28.244  1.00 18.64 ? 198 LEU A CB  1 
ATOM   1544 C CG  . LEU A 1 205 ? 23.776  12.394  29.446  1.00 20.00 ? 198 LEU A CG  1 
ATOM   1545 C CD1 . LEU A 1 205 ? 23.298  11.425  30.509  1.00 20.58 ? 198 LEU A CD1 1 
ATOM   1546 C CD2 . LEU A 1 205 ? 24.843  13.344  30.006  1.00 21.16 ? 198 LEU A CD2 1 
ATOM   1547 N N   . ASN A 1 206 ? 24.906  10.735  25.442  1.00 20.52 ? 199 ASN A N   1 
ATOM   1548 C CA  . ASN A 1 206 ? 25.726  9.827   24.619  1.00 21.47 ? 199 ASN A CA  1 
ATOM   1549 C C   . ASN A 1 206 ? 24.899  8.918   23.712  1.00 21.09 ? 199 ASN A C   1 
ATOM   1550 O O   . ASN A 1 206 ? 25.424  7.845   23.278  1.00 21.61 ? 199 ASN A O   1 
ATOM   1551 C CB  . ASN A 1 206 ? 26.553  8.948   25.551  1.00 22.09 ? 199 ASN A CB  1 
ATOM   1552 C CG  . ASN A 1 206 ? 25.723  7.974   26.356  1.00 24.09 ? 199 ASN A CG  1 
ATOM   1553 O OD1 . ASN A 1 206 ? 24.474  7.991   26.350  1.00 23.71 ? 199 ASN A OD1 1 
ATOM   1554 N ND2 . ASN A 1 206 ? 26.410  7.055   27.013  1.00 29.69 ? 199 ASN A ND2 1 
ATOM   1555 N N   . SER A 1 207 ? 23.639  9.257   23.439  1.00 19.92 ? 200 SER A N   1 
ATOM   1556 C CA  . SER A 1 207 ? 22.714  8.353   22.713  1.00 20.20 ? 200 SER A CA  1 
ATOM   1557 C C   . SER A 1 207 ? 22.143  9.052   21.487  1.00 20.84 ? 200 SER A C   1 
ATOM   1558 O O   . SER A 1 207 ? 21.694  10.206  21.614  1.00 21.11 ? 200 SER A O   1 
ATOM   1559 C CB  . SER A 1 207 ? 21.590  7.845   23.572  1.00 21.57 ? 200 SER A CB  1 
ATOM   1560 O OG  . SER A 1 207 ? 20.747  6.975   22.826  1.00 23.59 ? 200 SER A OG  1 
ATOM   1561 N N   . LYS A 1 208 ? 22.146  8.350   20.339  1.00 20.43 ? 201 LYS A N   1 
ATOM   1562 C CA  . LYS A 1 208 ? 21.422  8.778   19.110  1.00 20.78 ? 201 LYS A CA  1 
ATOM   1563 C C   . LYS A 1 208 ? 19.917  8.443   19.157  1.00 18.41 ? 201 LYS A C   1 
ATOM   1564 O O   . LYS A 1 208 ? 19.214  8.799   18.179  1.00 20.52 ? 201 LYS A O   1 
ATOM   1565 C CB  . LYS A 1 208 ? 22.033  8.098   17.896  1.00 23.03 ? 201 LYS A CB  1 
ATOM   1566 C CG  . LYS A 1 208 ? 23.439  8.589   17.589  1.00 24.76 ? 201 LYS A CG  1 
ATOM   1567 C CD  . LYS A 1 208 ? 23.927  8.101   16.244  1.00 28.91 ? 201 LYS A CD  1 
ATOM   1568 C CE  . LYS A 1 208 ? 25.295  8.634   15.874  1.00 38.41 ? 201 LYS A CE  1 
ATOM   1569 N NZ  . LYS A 1 208 ? 26.073  7.629   15.107  1.00 45.92 ? 201 LYS A NZ  1 
ATOM   1570 N N   . GLY A 1 209 ? 19.443  7.748   20.182  1.00 18.38 ? 202 GLY A N   1 
ATOM   1571 C CA  . GLY A 1 209 ? 18.029  7.371   20.246  1.00 18.75 ? 202 GLY A CA  1 
ATOM   1572 C C   . GLY A 1 209 ? 17.740  6.252   19.279  1.00 18.86 ? 202 GLY A C   1 
ATOM   1573 O O   . GLY A 1 209 ? 16.638  6.232   18.700  1.00 18.78 ? 202 GLY A O   1 
ATOM   1574 N N   . TYR A 1 210 ? 18.661  5.282   19.175  1.00 17.82 ? 203 TYR A N   1 
ATOM   1575 C CA  . TYR A 1 210 ? 18.513  4.123   18.267  1.00 19.14 ? 203 TYR A CA  1 
ATOM   1576 C C   . TYR A 1 210 ? 18.220  2.841   19.041  1.00 19.09 ? 203 TYR A C   1 
ATOM   1577 O O   . TYR A 1 210 ? 18.387  1.742   18.488  1.00 19.07 ? 203 TYR A O   1 
ATOM   1578 C CB  . TYR A 1 210 ? 19.775  3.912   17.415  1.00 21.96 ? 203 TYR A CB  1 
ATOM   1579 C CG  . TYR A 1 210 ? 20.046  4.959   16.364  1.00 24.20 ? 203 TYR A CG  1 
ATOM   1580 C CD1 . TYR A 1 210 ? 19.181  6.013   16.135  1.00 24.86 ? 203 TYR A CD1 1 
ATOM   1581 C CD2 . TYR A 1 210 ? 21.222  4.921   15.622  1.00 30.12 ? 203 TYR A CD2 1 
ATOM   1582 C CE1 . TYR A 1 210 ? 19.433  6.985   15.190  1.00 30.21 ? 203 TYR A CE1 1 
ATOM   1583 C CE2 . TYR A 1 210 ? 21.500  5.894   14.675  1.00 31.22 ? 203 TYR A CE2 1 
ATOM   1584 C CZ  . TYR A 1 210 ? 20.609  6.934   14.470  1.00 32.55 ? 203 TYR A CZ  1 
ATOM   1585 O OH  . TYR A 1 210 ? 20.828  7.888   13.529  1.00 41.14 ? 203 TYR A OH  1 
ATOM   1586 N N   . THR A 1 211 ? 17.829  2.945   20.307  1.00 18.93 ? 204 THR A N   1 
ATOM   1587 C CA  . THR A 1 211 ? 17.473  1.767   21.127  1.00 20.47 ? 204 THR A CA  1 
ATOM   1588 C C   . THR A 1 211 ? 16.058  1.943   21.664  1.00 19.09 ? 204 THR A C   1 
ATOM   1589 O O   . THR A 1 211 ? 15.612  3.091   21.849  1.00 22.50 ? 204 THR A O   1 
ATOM   1590 C CB  . THR A 1 211 ? 18.505  1.484   22.236  1.00 25.12 ? 204 THR A CB  1 
ATOM   1591 O OG1 . THR A 1 211 ? 18.187  2.341   23.313  1.00 35.33 ? 204 THR A OG1 1 
ATOM   1592 C CG2 . THR A 1 211 ? 19.954  1.711   21.825  1.00 26.28 ? 204 THR A CG2 1 
ATOM   1593 N N   . LYS A 1 212 ? 15.388  0.822   21.901  1.00 16.80 ? 205 LYS A N   1 
ATOM   1594 C CA  . LYS A 1 212 ? 13.975  0.731   22.302  1.00 15.94 ? 205 LYS A CA  1 
ATOM   1595 C C   . LYS A 1 212 ? 13.732  1.481   23.605  1.00 15.21 ? 205 LYS A C   1 
ATOM   1596 O O   . LYS A 1 212 ? 12.630  1.984   23.772  1.00 15.84 ? 205 LYS A O   1 
ATOM   1597 C CB  . LYS A 1 212 ? 13.559  -0.736  22.404  1.00 16.36 ? 205 LYS A CB  1 
ATOM   1598 C CG  . LYS A 1 212 ? 13.379  -1.384  21.039  1.00 19.36 ? 205 LYS A CG  1 
ATOM   1599 C CD  . LYS A 1 212 ? 13.127  -2.833  21.118  1.00 19.31 ? 205 LYS A CD  1 
ATOM   1600 C CE  . LYS A 1 212 ? 13.091  -3.455  19.740  1.00 19.62 ? 205 LYS A CE  1 
ATOM   1601 N NZ  . LYS A 1 212 ? 12.874  -4.919  19.809  1.00 20.20 ? 205 LYS A NZ  1 
ATOM   1602 N N   . SER A 1 213 ? 14.728  1.578   24.481  1.00 14.10 ? 206 SER A N   1 
ATOM   1603 C CA  . SER A 1 213 ? 14.566  2.185   25.818  1.00 14.41 ? 206 SER A CA  1 
ATOM   1604 C C   . SER A 1 213 ? 14.226  3.680   25.677  1.00 13.69 ? 206 SER A C   1 
ATOM   1605 O O   . SER A 1 213 ? 13.735  4.271   26.616  1.00 14.48 ? 206 SER A O   1 
ATOM   1606 C CB  . SER A 1 213 ? 15.790  1.994   26.641  1.00 18.25 ? 206 SER A CB  1 
ATOM   1607 O OG  . SER A 1 213 ? 16.904  2.423   25.901  1.00 19.40 ? 206 SER A OG  1 
ATOM   1608 N N   . ILE A 1 214 ? 14.526  4.311   24.567  1.00 15.53 ? 207 ILE A N   1 
ATOM   1609 C CA  . ILE A 1 214 ? 14.176  5.765   24.454  1.00 17.50 ? 207 ILE A CA  1 
ATOM   1610 C C   . ILE A 1 214 ? 12.657  5.942   24.370  1.00 15.03 ? 207 ILE A C   1 
ATOM   1611 O O   . ILE A 1 214 ? 12.176  6.951   24.903  1.00 15.60 ? 207 ILE A O   1 
ATOM   1612 C CB  . ILE A 1 214 ? 14.839  6.505   23.295  1.00 23.35 ? 207 ILE A CB  1 
ATOM   1613 C CG1 . ILE A 1 214 ? 14.492  5.860   21.963  1.00 23.94 ? 207 ILE A CG1 1 
ATOM   1614 C CG2 . ILE A 1 214 ? 16.338  6.674   23.575  1.00 25.61 ? 207 ILE A CG2 1 
ATOM   1615 C CD1 . ILE A 1 214 ? 13.457  6.603   21.183  1.00 29.49 ? 207 ILE A CD1 1 
ATOM   1616 N N   . ASP A 1 215 ? 11.949  4.975   23.811  1.00 12.54 ? 208 ASP A N   1 
ATOM   1617 C CA  . ASP A 1 215 ? 10.490  5.094   23.695  1.00 12.55 ? 208 ASP A CA  1 
ATOM   1618 C C   . ASP A 1 215 ? 9.842   4.878   25.061  1.00 13.27 ? 208 ASP A C   1 
ATOM   1619 O O   . ASP A 1 215 ? 8.844   5.529   25.349  1.00 11.57 ? 208 ASP A O   1 
ATOM   1620 C CB  . ASP A 1 215 ? 9.920   4.130   22.677  1.00 13.32 ? 208 ASP A CB  1 
ATOM   1621 C CG  . ASP A 1 215 ? 10.105  4.525   21.232  1.00 13.47 ? 208 ASP A CG  1 
ATOM   1622 O OD1 . ASP A 1 215 ? 10.189  5.768   20.932  1.00 16.19 ? 208 ASP A OD1 1 
ATOM   1623 O OD2 . ASP A 1 215 ? 10.126  3.625   20.448  1.00 15.21 ? 208 ASP A OD2 1 
ATOM   1624 N N   . ILE A 1 216 ? 10.365  3.970   25.858  1.00 13.24 ? 209 ILE A N   1 
ATOM   1625 C CA  . ILE A 1 216 ? 9.813   3.705   27.220  1.00 13.70 ? 209 ILE A CA  1 
ATOM   1626 C C   . ILE A 1 216 ? 9.936   4.958   28.077  1.00 12.70 ? 209 ILE A C   1 
ATOM   1627 O O   . ILE A 1 216 ? 8.978   5.261   28.787  1.00 12.92 ? 209 ILE A O   1 
ATOM   1628 C CB  . ILE A 1 216 ? 10.459  2.475   27.854  1.00 17.15 ? 209 ILE A CB  1 
ATOM   1629 C CG1 . ILE A 1 216 ? 10.065  1.191   27.115  1.00 19.56 ? 209 ILE A CG1 1 
ATOM   1630 C CG2 . ILE A 1 216 ? 10.144  2.364   29.326  1.00 18.13 ? 209 ILE A CG2 1 
ATOM   1631 C CD1 . ILE A 1 216 ? 8.630   0.785   27.242  1.00 22.40 ? 209 ILE A CD1 1 
ATOM   1632 N N   . TRP A 1 217 ? 11.031  5.711   27.980  1.00 12.45 ? 210 TRP A N   1 
ATOM   1633 C CA  . TRP A 1 217 ? 11.171  6.982   28.725  1.00 12.26 ? 210 TRP A CA  1 
ATOM   1634 C C   . TRP A 1 217 ? 10.015  7.923   28.338  1.00 12.34 ? 210 TRP A C   1 
ATOM   1635 O O   . TRP A 1 217 ? 9.398   8.473   29.218  1.00 13.43 ? 210 TRP A O   1 
ATOM   1636 C CB  . TRP A 1 217 ? 12.515  7.611   28.384  1.00 12.23 ? 210 TRP A CB  1 
ATOM   1637 C CG  . TRP A 1 217 ? 12.675  8.900   29.107  1.00 12.61 ? 210 TRP A CG  1 
ATOM   1638 C CD1 . TRP A 1 217 ? 12.268  10.137  28.721  1.00 15.03 ? 210 TRP A CD1 1 
ATOM   1639 C CD2 . TRP A 1 217 ? 13.186  9.012   30.436  1.00 13.51 ? 210 TRP A CD2 1 
ATOM   1640 N NE1 . TRP A 1 217 ? 12.545  11.017  29.732  1.00 15.70 ? 210 TRP A NE1 1 
ATOM   1641 C CE2 . TRP A 1 217 ? 13.107  10.367  30.788  1.00 15.26 ? 210 TRP A CE2 1 
ATOM   1642 C CE3 . TRP A 1 217 ? 13.720  8.104   31.337  1.00 14.38 ? 210 TRP A CE3 1 
ATOM   1643 C CZ2 . TRP A 1 217 ? 13.546  10.808  32.040  1.00 16.04 ? 210 TRP A CZ2 1 
ATOM   1644 C CZ3 . TRP A 1 217 ? 14.175  8.541   32.554  1.00 16.23 ? 210 TRP A CZ3 1 
ATOM   1645 C CH2 . TRP A 1 217 ? 14.097  9.898   32.887  1.00 16.04 ? 210 TRP A CH2 1 
ATOM   1646 N N   . SER A 1 218 ? 9.754   8.102   27.050  1.00 12.28 ? 211 SER A N   1 
ATOM   1647 C CA  . SER A 1 218 ? 8.694   9.004   26.563  1.00 12.22 ? 211 SER A CA  1 
ATOM   1648 C C   . SER A 1 218 ? 7.352   8.534   27.149  1.00 13.05 ? 211 SER A C   1 
ATOM   1649 O O   . SER A 1 218 ? 6.590   9.382   27.662  1.00 14.48 ? 211 SER A O   1 
ATOM   1650 C CB  . SER A 1 218 ? 8.652   9.037   25.050  1.00 12.02 ? 211 SER A CB  1 
ATOM   1651 O OG  . SER A 1 218 ? 9.918   9.367   24.487  1.00 13.08 ? 211 SER A OG  1 
ATOM   1652 N N   . VAL A 1 219 ? 7.112   7.226   27.168  1.00 13.16 ? 212 VAL A N   1 
ATOM   1653 C CA  . VAL A 1 219 ? 5.833   6.699   27.745  1.00 13.62 ? 212 VAL A CA  1 
ATOM   1654 C C   . VAL A 1 219 ? 5.777   7.081   29.238  1.00 14.30 ? 212 VAL A C   1 
ATOM   1655 O O   . VAL A 1 219 ? 4.730   7.503   29.748  1.00 14.04 ? 212 VAL A O   1 
ATOM   1656 C CB  . VAL A 1 219 ? 5.662   5.186   27.532  1.00 12.92 ? 212 VAL A CB  1 
ATOM   1657 C CG1 . VAL A 1 219 ? 4.372   4.731   28.193  1.00 16.31 ? 212 VAL A CG1 1 
ATOM   1658 C CG2 . VAL A 1 219 ? 5.606   4.898   26.054  1.00 16.46 ? 212 VAL A CG2 1 
ATOM   1659 N N   . GLY A 1 220 ? 6.891   6.974   29.937  1.00 12.91 ? 213 GLY A N   1 
ATOM   1660 C CA  . GLY A 1 220 ? 6.983   7.352   31.336  1.00 12.53 ? 213 GLY A CA  1 
ATOM   1661 C C   . GLY A 1 220 ? 6.598   8.813   31.504  1.00 13.70 ? 213 GLY A C   1 
ATOM   1662 O O   . GLY A 1 220 ? 5.824   9.157   32.428  1.00 14.98 ? 213 GLY A O   1 
ATOM   1663 N N   . CYS A 1 221 ? 7.144   9.692   30.658  1.00 13.42 ? 214 CYS A N   1 
ATOM   1664 C CA  . CYS A 1 221 ? 6.836   11.145  30.680  1.00 15.26 ? 214 CYS A CA  1 
ATOM   1665 C C   . CYS A 1 221 ? 5.327   11.334  30.486  1.00 15.01 ? 214 CYS A C   1 
ATOM   1666 O O   . CYS A 1 221 ? 4.705   12.177  31.183  1.00 15.88 ? 214 CYS A O   1 
ATOM   1667 C CB  . CYS A 1 221 ? 7.627   11.838  29.587  1.00 15.60 ? 214 CYS A CB  1 
ATOM   1668 S SG  . CYS A 1 221 ? 9.392   11.916  29.979  1.00 16.34 ? 214 CYS A SG  1 
ATOM   1669 N N   . ILE A 1 222 ? 4.754   10.607  29.547  1.00 14.55 ? 215 ILE A N   1 
ATOM   1670 C CA  . ILE A 1 222 ? 3.302   10.695  29.212  1.00 16.13 ? 215 ILE A CA  1 
ATOM   1671 C C   . ILE A 1 222 ? 2.507   10.217  30.422  1.00 16.06 ? 215 ILE A C   1 
ATOM   1672 O O   . ILE A 1 222 ? 1.446   10.857  30.743  1.00 18.06 ? 215 ILE A O   1 
ATOM   1673 C CB  . ILE A 1 222 ? 3.001   9.919   27.921  1.00 15.87 ? 215 ILE A CB  1 
ATOM   1674 C CG1 . ILE A 1 222 ? 3.713   10.554  26.737  1.00 16.02 ? 215 ILE A CG1 1 
ATOM   1675 C CG2 . ILE A 1 222 ? 1.500   9.827   27.679  1.00 17.18 ? 215 ILE A CG2 1 
ATOM   1676 C CD1 . ILE A 1 222 ? 3.781   9.713   25.498  1.00 15.88 ? 215 ILE A CD1 1 
ATOM   1677 N N   . LEU A 1 223 ? 2.898   9.138   31.070  1.00 16.67 ? 216 LEU A N   1 
ATOM   1678 C CA  . LEU A 1 223 ? 2.205   8.653   32.302  1.00 17.01 ? 216 LEU A CA  1 
ATOM   1679 C C   . LEU A 1 223 ? 2.205   9.765   33.376  1.00 19.48 ? 216 LEU A C   1 
ATOM   1680 O O   . LEU A 1 223 ? 1.136   10.111  33.915  1.00 18.02 ? 216 LEU A O   1 
ATOM   1681 C CB  . LEU A 1 223 ? 2.864   7.368   32.791  1.00 15.56 ? 216 LEU A CB  1 
ATOM   1682 C CG  . LEU A 1 223 ? 2.305   6.842   34.124  1.00 16.22 ? 216 LEU A CG  1 
ATOM   1683 C CD1 . LEU A 1 223 ? 0.777   6.669   34.069  1.00 16.99 ? 216 LEU A CD1 1 
ATOM   1684 C CD2 . LEU A 1 223 ? 2.978   5.529   34.452  1.00 16.05 ? 216 LEU A CD2 1 
ATOM   1685 N N   . ALA A 1 224 ? 3.347   10.381  33.633  1.00 17.94 ? 217 ALA A N   1 
ATOM   1686 C CA  . ALA A 1 224 ? 3.450   11.468  34.630  1.00 19.37 ? 217 ALA A CA  1 
ATOM   1687 C C   . ALA A 1 224 ? 2.488   12.577  34.239  1.00 19.97 ? 217 ALA A C   1 
ATOM   1688 O O   . ALA A 1 224 ? 1.850   13.139  35.146  1.00 20.42 ? 217 ALA A O   1 
ATOM   1689 C CB  . ALA A 1 224 ? 4.864   11.965  34.718  1.00 19.06 ? 217 ALA A CB  1 
ATOM   1690 N N   . GLU A 1 225 ? 2.455   12.953  32.966  1.00 17.83 ? 218 GLU A N   1 
ATOM   1691 C CA  . GLU A 1 225 ? 1.611   14.038  32.446  1.00 19.29 ? 218 GLU A CA  1 
ATOM   1692 C C   . GLU A 1 225 ? 0.136   13.684  32.657  1.00 20.39 ? 218 GLU A C   1 
ATOM   1693 O O   . GLU A 1 225 ? -0.618  14.567  33.061  1.00 21.59 ? 218 GLU A O   1 
ATOM   1694 C CB  . GLU A 1 225 ? 1.969   14.311  31.004  1.00 20.28 ? 218 GLU A CB  1 
ATOM   1695 C CG  . GLU A 1 225 ? 1.405   15.611  30.504  1.00 22.12 ? 218 GLU A CG  1 
ATOM   1696 C CD  . GLU A 1 225 ? 2.169   16.201  29.331  1.00 23.81 ? 218 GLU A CD  1 
ATOM   1697 O OE1 . GLU A 1 225 ? 3.272   15.710  29.008  1.00 20.44 ? 218 GLU A OE1 1 
ATOM   1698 O OE2 . GLU A 1 225 ? 1.642   17.134  28.738  1.00 24.97 ? 218 GLU A OE2 1 
ATOM   1699 N N   . MET A 1 226 ? -0.232  12.411  32.488  1.00 18.32 ? 219 MET A N   1 
ATOM   1700 C CA  . MET A 1 226 ? -1.645  11.984  32.665  1.00 20.15 ? 219 MET A CA  1 
ATOM   1701 C C   . MET A 1 226 ? -2.014  12.100  34.139  1.00 21.99 ? 219 MET A C   1 
ATOM   1702 O O   . MET A 1 226 ? -3.215  12.333  34.409  1.00 24.17 ? 219 MET A O   1 
ATOM   1703 C CB  . MET A 1 226 ? -1.859  10.554  32.176  1.00 18.00 ? 219 MET A CB  1 
ATOM   1704 C CG  . MET A 1 226 ? -1.898  10.445  30.680  1.00 18.78 ? 219 MET A CG  1 
ATOM   1705 S SD  . MET A 1 226 ? -2.536  8.909   30.070  1.00 20.35 ? 219 MET A SD  1 
ATOM   1706 C CE  . MET A 1 226 ? -1.134  7.835   30.392  1.00 21.30 ? 219 MET A CE  1 
ATOM   1707 N N   . LEU A 1 227 ? -1.055  11.911  35.043  1.00 20.14 ? 220 LEU A N   1 
ATOM   1708 C CA  . LEU A 1 227 ? -1.326  11.873  36.503  1.00 22.00 ? 220 LEU A CA  1 
ATOM   1709 C C   . LEU A 1 227 ? -1.556  13.290  37.029  1.00 26.70 ? 220 LEU A C   1 
ATOM   1710 O O   . LEU A 1 227 ? -2.192  13.408  38.063  1.00 29.02 ? 220 LEU A O   1 
ATOM   1711 C CB  . LEU A 1 227 ? -0.182  11.196  37.248  1.00 22.20 ? 220 LEU A CB  1 
ATOM   1712 C CG  . LEU A 1 227 ? -0.036  9.701   37.013  1.00 21.23 ? 220 LEU A CG  1 
ATOM   1713 C CD1 . LEU A 1 227 ? 1.310   9.207   37.487  1.00 22.73 ? 220 LEU A CD1 1 
ATOM   1714 C CD2 . LEU A 1 227 ? -1.164  8.932   37.668  1.00 22.35 ? 220 LEU A CD2 1 
ATOM   1715 N N   . SER A 1 228 ? -1.035  14.320  36.373  1.00 27.64 ? 221 SER A N   1 
ATOM   1716 C CA  . SER A 1 228 ? -1.058  15.696  36.918  1.00 29.71 ? 221 SER A CA  1 
ATOM   1717 C C   . SER A 1 228 ? -1.546  16.721  35.902  1.00 29.35 ? 221 SER A C   1 
ATOM   1718 O O   . SER A 1 228 ? -1.620  17.907  36.275  1.00 29.22 ? 221 SER A O   1 
ATOM   1719 C CB  . SER A 1 228 ? 0.305   16.066  37.432  1.00 34.42 ? 221 SER A CB  1 
ATOM   1720 O OG  . SER A 1 228 ? 1.194   16.180  36.330  1.00 35.13 ? 221 SER A OG  1 
ATOM   1721 N N   . ASN A 1 229 ? -1.782  16.347  34.641  1.00 28.00 ? 222 ASN A N   1 
ATOM   1722 C CA  . ASN A 1 229 ? -2.090  17.331  33.577  1.00 28.59 ? 222 ASN A CA  1 
ATOM   1723 C C   . ASN A 1 229 ? -0.976  18.376  33.408  1.00 29.21 ? 222 ASN A C   1 
ATOM   1724 O O   . ASN A 1 229 ? -1.262  19.482  32.958  1.00 37.59 ? 222 ASN A O   1 
ATOM   1725 C CB  . ASN A 1 229 ? -3.408  18.057  33.884  1.00 27.73 ? 222 ASN A CB  1 
ATOM   1726 C CG  . ASN A 1 229 ? -4.603  17.136  33.779  1.00 25.90 ? 222 ASN A CG  1 
ATOM   1727 O OD1 . ASN A 1 229 ? -4.913  16.409  34.723  1.00 31.06 ? 222 ASN A OD1 1 
ATOM   1728 N ND2 . ASN A 1 229 ? -5.229  17.123  32.624  1.00 26.99 ? 222 ASN A ND2 1 
ATOM   1729 N N   . ARG A 1 230 ? 0.270   18.089  33.753  1.00 29.95 ? 223 ARG A N   1 
ATOM   1730 C CA  . ARG A 1 230 ? 1.364   19.017  33.362  1.00 30.31 ? 223 ARG A CA  1 
ATOM   1731 C C   . ARG A 1 230 ? 2.579   18.174  32.999  1.00 26.74 ? 223 ARG A C   1 
ATOM   1732 O O   . ARG A 1 230 ? 2.721   17.070  33.517  1.00 23.19 ? 223 ARG A O   1 
ATOM   1733 C CB  . ARG A 1 230 ? 1.606   20.083  34.436  1.00 38.73 ? 223 ARG A CB  1 
ATOM   1734 C CG  . ARG A 1 230 ? 2.412   19.632  35.646  1.00 45.95 ? 223 ARG A CG  1 
ATOM   1735 C CD  . ARG A 1 230 ? 2.952   20.838  36.415  1.00 50.18 ? 223 ARG A CD  1 
ATOM   1736 N NE  . ARG A 1 230 ? 4.404   20.780  36.632  1.00 55.68 ? 223 ARG A NE  1 
ATOM   1737 C CZ  . ARG A 1 230 ? 5.347   20.930  35.690  1.00 53.08 ? 223 ARG A CZ  1 
ATOM   1738 N NH1 . ARG A 1 230 ? 5.022   21.151  34.422  1.00 46.97 ? 223 ARG A NH1 1 
ATOM   1739 N NH2 . ARG A 1 230 ? 6.627   20.843  36.026  1.00 54.22 ? 223 ARG A NH2 1 
ATOM   1740 N N   . PRO A 1 231 ? 3.419   18.656  32.056  1.00 24.79 ? 224 PRO A N   1 
ATOM   1741 C CA  . PRO A 1 231 ? 4.599   17.907  31.631  1.00 24.53 ? 224 PRO A CA  1 
ATOM   1742 C C   . PRO A 1 231 ? 5.516   17.800  32.849  1.00 26.02 ? 224 PRO A C   1 
ATOM   1743 O O   . PRO A 1 231 ? 5.639   18.749  33.607  1.00 25.29 ? 224 PRO A O   1 
ATOM   1744 C CB  . PRO A 1 231 ? 5.253   18.725  30.512  1.00 26.80 ? 224 PRO A CB  1 
ATOM   1745 C CG  . PRO A 1 231 ? 4.598   20.093  30.575  1.00 30.81 ? 224 PRO A CG  1 
ATOM   1746 C CD  . PRO A 1 231 ? 3.329   19.964  31.402  1.00 28.90 ? 224 PRO A CD  1 
ATOM   1747 N N   . ILE A 1 232 ? 6.110   16.632  33.055  1.00 21.74 ? 225 ILE A N   1 
ATOM   1748 C CA  . ILE A 1 232 ? 6.918   16.374  34.271  1.00 21.66 ? 225 ILE A CA  1 
ATOM   1749 C C   . ILE A 1 232 ? 8.285   17.054  34.117  1.00 20.51 ? 225 ILE A C   1 
ATOM   1750 O O   . ILE A 1 232 ? 8.843   17.519  35.139  1.00 23.69 ? 225 ILE A O   1 
ATOM   1751 C CB  . ILE A 1 232 ? 7.057   14.871  34.564  1.00 21.71 ? 225 ILE A CB  1 
ATOM   1752 C CG1 . ILE A 1 232 ? 7.917   14.642  35.809  1.00 24.23 ? 225 ILE A CG1 1 
ATOM   1753 C CG2 . ILE A 1 232 ? 7.546   14.120  33.323  1.00 20.62 ? 225 ILE A CG2 1 
ATOM   1754 C CD1 . ILE A 1 232 ? 7.951   13.235  36.323  1.00 24.76 ? 225 ILE A CD1 1 
ATOM   1755 N N   . PHE A 1 233 ? 8.827   17.102  32.911  1.00 20.72 ? 226 PHE A N   1 
ATOM   1756 C CA  . PHE A 1 233 ? 10.188  17.624  32.648  1.00 21.79 ? 226 PHE A CA  1 
ATOM   1757 C C   . PHE A 1 233 ? 10.131  18.708  31.576  1.00 23.59 ? 226 PHE A C   1 
ATOM   1758 O O   . PHE A 1 233 ? 10.603  18.528  30.443  1.00 21.49 ? 226 PHE A O   1 
ATOM   1759 C CB  . PHE A 1 233 ? 11.103  16.470  32.234  1.00 21.63 ? 226 PHE A CB  1 
ATOM   1760 C CG  . PHE A 1 233 ? 11.201  15.319  33.195  1.00 19.70 ? 226 PHE A CG  1 
ATOM   1761 C CD1 . PHE A 1 233 ? 11.539  15.489  34.532  1.00 18.93 ? 226 PHE A CD1 1 
ATOM   1762 C CD2 . PHE A 1 233 ? 11.018  14.011  32.734  1.00 20.65 ? 226 PHE A CD2 1 
ATOM   1763 C CE1 . PHE A 1 233 ? 11.649  14.403  35.382  1.00 19.97 ? 226 PHE A CE1 1 
ATOM   1764 C CE2 . PHE A 1 233 ? 11.143  12.931  33.591  1.00 20.29 ? 226 PHE A CE2 1 
ATOM   1765 C CZ  . PHE A 1 233 ? 11.440  13.127  34.924  1.00 18.46 ? 226 PHE A CZ  1 
ATOM   1766 N N   . PRO A 1 234 ? 9.494   19.883  31.861  1.00 24.78 ? 227 PRO A N   1 
ATOM   1767 C CA  . PRO A 1 234 ? 9.378   20.939  30.868  1.00 25.25 ? 227 PRO A CA  1 
ATOM   1768 C C   . PRO A 1 234 ? 10.679  21.753  30.787  1.00 34.00 ? 227 PRO A C   1 
ATOM   1769 O O   . PRO A 1 234 ? 10.708  22.939  31.158  1.00 29.68 ? 227 PRO A O   1 
ATOM   1770 C CB  . PRO A 1 234 ? 8.218   21.773  31.444  1.00 22.99 ? 227 PRO A CB  1 
ATOM   1771 C CG  . PRO A 1 234 ? 8.452   21.700  32.895  1.00 22.57 ? 227 PRO A CG  1 
ATOM   1772 C CD  . PRO A 1 234 ? 8.879   20.264  33.151  1.00 24.67 ? 227 PRO A CD  1 
ATOM   1773 N N   . GLY A 1 235 ? 11.753  21.097  30.346  1.00 30.40 ? 228 GLY A N   1 
ATOM   1774 C CA  . GLY A 1 235 ? 13.050  21.749  30.068  1.00 29.12 ? 228 GLY A CA  1 
ATOM   1775 C C   . GLY A 1 235 ? 12.903  22.895  29.076  1.00 30.01 ? 228 GLY A C   1 
ATOM   1776 O O   . GLY A 1 235 ? 12.164  22.766  28.111  1.00 28.72 ? 228 GLY A O   1 
ATOM   1777 N N   . LYS A 1 236 ? 13.572  24.021  29.322  1.00 35.64 ? 229 LYS A N   1 
ATOM   1778 C CA  . LYS A 1 236 ? 13.455  25.231  28.457  1.00 40.13 ? 229 LYS A CA  1 
ATOM   1779 C C   . LYS A 1 236 ? 14.542  25.208  27.379  1.00 41.44 ? 229 LYS A C   1 
ATOM   1780 O O   . LYS A 1 236 ? 14.420  25.976  26.402  1.00 40.41 ? 229 LYS A O   1 
ATOM   1781 C CB  . LYS A 1 236 ? 13.514  26.494  29.320  1.00 43.81 ? 229 LYS A CB  1 
ATOM   1782 C CG  . LYS A 1 236 ? 12.278  26.671  30.195  1.00 46.00 ? 229 LYS A CG  1 
ATOM   1783 C CD  . LYS A 1 236 ? 12.096  28.058  30.759  1.00 51.21 ? 229 LYS A CD  1 
ATOM   1784 C CE  . LYS A 1 236 ? 10.897  28.135  31.681  1.00 52.32 ? 229 LYS A CE  1 
ATOM   1785 N NZ  . LYS A 1 236 ? 11.238  27.611  33.023  1.00 58.61 ? 229 LYS A NZ  1 
ATOM   1786 N N   . HIS A 1 237 ? 15.533  24.331  27.551  1.00 32.17 ? 230 HIS A N   1 
ATOM   1787 C CA  . HIS A 1 237 ? 16.719  24.205  26.675  1.00 32.56 ? 230 HIS A CA  1 
ATOM   1788 C C   . HIS A 1 237 ? 17.337  22.809  26.831  1.00 32.57 ? 230 HIS A C   1 
ATOM   1789 O O   . HIS A 1 237 ? 16.973  22.055  27.743  1.00 29.41 ? 230 HIS A O   1 
ATOM   1790 C CB  . HIS A 1 237 ? 17.719  25.360  26.914  1.00 30.08 ? 230 HIS A CB  1 
ATOM   1791 C CG  . HIS A 1 237 ? 18.281  25.437  28.301  1.00 31.41 ? 230 HIS A CG  1 
ATOM   1792 N ND1 . HIS A 1 237 ? 19.376  24.669  28.712  1.00 31.56 ? 230 HIS A ND1 1 
ATOM   1793 C CD2 . HIS A 1 237 ? 17.881  26.165  29.367  1.00 29.58 ? 230 HIS A CD2 1 
ATOM   1794 C CE1 . HIS A 1 237 ? 19.623  24.922  29.988  1.00 34.09 ? 230 HIS A CE1 1 
ATOM   1795 N NE2 . HIS A 1 237 ? 18.707  25.842  30.430  1.00 32.36 ? 230 HIS A NE2 1 
ATOM   1796 N N   . TYR A 1 238 ? 18.294  22.508  25.976  1.00 30.63 ? 231 TYR A N   1 
ATOM   1797 C CA  . TYR A 1 238 ? 18.764  21.131  25.721  1.00 30.67 ? 231 TYR A CA  1 
ATOM   1798 C C   . TYR A 1 238 ? 19.297  20.558  27.037  1.00 30.53 ? 231 TYR A C   1 
ATOM   1799 O O   . TYR A 1 238 ? 18.751  19.506  27.463  1.00 31.57 ? 231 TYR A O   1 
ATOM   1800 C CB  . TYR A 1 238 ? 19.664  21.175  24.476  1.00 33.19 ? 231 TYR A CB  1 
ATOM   1801 C CG  . TYR A 1 238 ? 20.335  19.871  24.123  1.00 28.59 ? 231 TYR A CG  1 
ATOM   1802 C CD1 . TYR A 1 238 ? 21.378  19.402  24.906  1.00 28.48 ? 231 TYR A CD1 1 
ATOM   1803 C CD2 . TYR A 1 238 ? 19.952  19.118  23.025  1.00 31.26 ? 231 TYR A CD2 1 
ATOM   1804 C CE1 . TYR A 1 238 ? 22.038  18.217  24.602  1.00 29.58 ? 231 TYR A CE1 1 
ATOM   1805 C CE2 . TYR A 1 238 ? 20.590  17.914  22.717  1.00 29.00 ? 231 TYR A CE2 1 
ATOM   1806 C CZ  . TYR A 1 238 ? 21.649  17.471  23.502  1.00 29.74 ? 231 TYR A CZ  1 
ATOM   1807 O OH  . TYR A 1 238 ? 22.321  16.293  23.239  1.00 30.01 ? 231 TYR A OH  1 
ATOM   1808 N N   . LEU A 1 239 ? 20.208  21.251  27.745  1.00 26.69 ? 232 LEU A N   1 
ATOM   1809 C CA  . LEU A 1 239 ? 20.776  20.769  29.037  1.00 30.79 ? 232 LEU A CA  1 
ATOM   1810 C C   . LEU A 1 239 ? 19.776  20.910  30.192  1.00 29.90 ? 232 LEU A C   1 
ATOM   1811 O O   . LEU A 1 239 ? 19.921  20.168  31.174  1.00 33.23 ? 232 LEU A O   1 
ATOM   1812 C CB  . LEU A 1 239 ? 22.078  21.517  29.351  1.00 34.91 ? 232 LEU A CB  1 
ATOM   1813 C CG  . LEU A 1 239 ? 23.315  20.656  29.566  1.00 33.50 ? 232 LEU A CG  1 
ATOM   1814 C CD1 . LEU A 1 239 ? 23.352  19.431  28.676  1.00 33.39 ? 232 LEU A CD1 1 
ATOM   1815 C CD2 . LEU A 1 239 ? 24.578  21.487  29.382  1.00 34.76 ? 232 LEU A CD2 1 
ATOM   1816 N N   . ASP A 1 240 ? 18.808  21.830  30.098  1.00 31.86 ? 233 ASP A N   1 
ATOM   1817 C CA  . ASP A 1 240 ? 17.782  22.083  31.154  1.00 30.47 ? 233 ASP A CA  1 
ATOM   1818 C C   . ASP A 1 240 ? 16.894  20.850  31.255  1.00 29.47 ? 233 ASP A C   1 
ATOM   1819 O O   . ASP A 1 240 ? 16.451  20.500  32.391  1.00 33.67 ? 233 ASP A O   1 
ATOM   1820 C CB  . ASP A 1 240 ? 16.922  23.305  30.815  1.00 30.67 ? 233 ASP A CB  1 
ATOM   1821 C CG  . ASP A 1 240 ? 16.087  23.877  31.955  1.00 31.68 ? 233 ASP A CG  1 
ATOM   1822 O OD1 . ASP A 1 240 ? 16.591  23.960  33.088  1.00 35.70 ? 233 ASP A OD1 1 
ATOM   1823 O OD2 . ASP A 1 240 ? 14.916  24.211  31.691  1.00 34.26 ? 233 ASP A OD2 1 
ATOM   1824 N N   . GLN A 1 241 ? 16.658  20.207  30.119  1.00 30.09 ? 234 GLN A N   1 
ATOM   1825 C CA  . GLN A 1 241 ? 15.930  18.914  30.091  1.00 26.61 ? 234 GLN A CA  1 
ATOM   1826 C C   . GLN A 1 241 ? 16.592  17.974  31.113  1.00 30.00 ? 234 GLN A C   1 
ATOM   1827 O O   . GLN A 1 241 ? 15.889  17.359  31.904  1.00 26.59 ? 234 GLN A O   1 
ATOM   1828 C CB  . GLN A 1 241 ? 15.902  18.349  28.669  1.00 26.51 ? 234 GLN A CB  1 
ATOM   1829 C CG  . GLN A 1 241 ? 14.842  17.279  28.500  1.00 22.76 ? 234 GLN A CG  1 
ATOM   1830 C CD  . GLN A 1 241 ? 13.466  17.736  28.920  1.00 24.15 ? 234 GLN A CD  1 
ATOM   1831 O OE1 . GLN A 1 241 ? 13.055  18.861  28.635  1.00 23.82 ? 234 GLN A OE1 1 
ATOM   1832 N NE2 . GLN A 1 241 ? 12.683  16.835  29.498  1.00 22.16 ? 234 GLN A NE2 1 
ATOM   1833 N N   . LEU A 1 242 ? 17.930  17.945  31.198  1.00 26.55 ? 235 LEU A N   1 
ATOM   1834 C CA  . LEU A 1 242 ? 18.649  17.030  32.112  1.00 26.85 ? 235 LEU A CA  1 
ATOM   1835 C C   . LEU A 1 242 ? 18.554  17.522  33.554  1.00 27.32 ? 235 LEU A C   1 
ATOM   1836 O O   . LEU A 1 242 ? 18.352  16.683  34.429  1.00 24.53 ? 235 LEU A O   1 
ATOM   1837 C CB  . LEU A 1 242 ? 20.092  16.913  31.602  1.00 29.73 ? 235 LEU A CB  1 
ATOM   1838 C CG  . LEU A 1 242 ? 20.915  15.722  32.043  1.00 33.08 ? 235 LEU A CG  1 
ATOM   1839 C CD1 . LEU A 1 242 ? 20.148  14.415  31.924  1.00 31.38 ? 235 LEU A CD1 1 
ATOM   1840 C CD2 . LEU A 1 242 ? 22.208  15.668  31.222  1.00 31.74 ? 235 LEU A CD2 1 
ATOM   1841 N N   . ASN A 1 243 ? 18.684  18.835  33.817  1.00 24.76 ? 236 ASN A N   1 
ATOM   1842 C CA  . ASN A 1 243 ? 18.567  19.378  35.185  1.00 31.77 ? 236 ASN A CA  1 
ATOM   1843 C C   . ASN A 1 243 ? 17.161  19.053  35.701  1.00 26.91 ? 236 ASN A C   1 
ATOM   1844 O O   . ASN A 1 243 ? 17.075  18.684  36.869  1.00 31.08 ? 236 ASN A O   1 
ATOM   1845 C CB  . ASN A 1 243 ? 18.919  20.864  35.265  1.00 37.46 ? 236 ASN A CB  1 
ATOM   1846 C CG  . ASN A 1 243 ? 20.403  21.146  35.440  1.00 44.40 ? 236 ASN A CG  1 
ATOM   1847 O OD1 . ASN A 1 243 ? 20.797  22.304  35.534  1.00 60.53 ? 236 ASN A OD1 1 
ATOM   1848 N ND2 . ASN A 1 243 ? 21.245  20.126  35.508  1.00 42.33 ? 236 ASN A ND2 1 
ATOM   1849 N N   . HIS A 1 244 ? 16.136  19.121  34.841  1.00 30.31 ? 237 HIS A N   1 
ATOM   1850 C CA  . HIS A 1 244 ? 14.735  18.782  35.222  1.00 27.72 ? 237 HIS A CA  1 
ATOM   1851 C C   . HIS A 1 244 ? 14.680  17.327  35.642  1.00 22.21 ? 237 HIS A C   1 
ATOM   1852 O O   . HIS A 1 244 ? 14.103  17.033  36.710  1.00 24.00 ? 237 HIS A O   1 
ATOM   1853 C CB  . HIS A 1 244 ? 13.748  19.081  34.103  1.00 27.68 ? 237 HIS A CB  1 
ATOM   1854 C CG  . HIS A 1 244 ? 13.188  20.453  34.215  1.00 30.97 ? 237 HIS A CG  1 
ATOM   1855 N ND1 . HIS A 1 244 ? 13.848  21.566  33.714  1.00 33.40 ? 237 HIS A ND1 1 
ATOM   1856 C CD2 . HIS A 1 244 ? 12.044  20.902  34.776  1.00 31.76 ? 237 HIS A CD2 1 
ATOM   1857 C CE1 . HIS A 1 244 ? 13.112  22.645  33.948  1.00 32.80 ? 237 HIS A CE1 1 
ATOM   1858 N NE2 . HIS A 1 244 ? 12.016  22.267  34.619  1.00 34.68 ? 237 HIS A NE2 1 
ATOM   1859 N N   . ILE A 1 245 ? 15.224  16.447  34.796  1.00 21.68 ? 238 ILE A N   1 
ATOM   1860 C CA  . ILE A 1 245 ? 15.201  14.996  35.076  1.00 19.92 ? 238 ILE A CA  1 
ATOM   1861 C C   . ILE A 1 245 ? 15.933  14.761  36.408  1.00 21.18 ? 238 ILE A C   1 
ATOM   1862 O O   . ILE A 1 245 ? 15.394  14.075  37.286  1.00 20.01 ? 238 ILE A O   1 
ATOM   1863 C CB  . ILE A 1 245 ? 15.770  14.210  33.885  1.00 20.83 ? 238 ILE A CB  1 
ATOM   1864 C CG1 . ILE A 1 245 ? 14.844  14.341  32.671  1.00 21.40 ? 238 ILE A CG1 1 
ATOM   1865 C CG2 . ILE A 1 245 ? 15.989  12.761  34.267  1.00 21.78 ? 238 ILE A CG2 1 
ATOM   1866 C CD1 . ILE A 1 245 ? 15.459  13.957  31.372  1.00 22.31 ? 238 ILE A CD1 1 
ATOM   1867 N N   . LEU A 1 246 ? 17.139  15.306  36.588  1.00 21.84 ? 239 LEU A N   1 
ATOM   1868 C CA  . LEU A 1 246 ? 17.930  14.978  37.797  1.00 23.78 ? 239 LEU A CA  1 
ATOM   1869 C C   . LEU A 1 246 ? 17.348  15.669  39.036  1.00 22.82 ? 239 LEU A C   1 
ATOM   1870 O O   . LEU A 1 246 ? 17.571  15.161  40.137  1.00 24.93 ? 239 LEU A O   1 
ATOM   1871 C CB  . LEU A 1 246 ? 19.376  15.393  37.553  1.00 26.03 ? 239 LEU A CB  1 
ATOM   1872 C CG  . LEU A 1 246 ? 20.078  14.740  36.370  1.00 28.48 ? 239 LEU A CG  1 
ATOM   1873 C CD1 . LEU A 1 246 ? 21.535  15.137  36.392  1.00 26.78 ? 239 LEU A CD1 1 
ATOM   1874 C CD2 . LEU A 1 246 ? 19.916  13.245  36.403  1.00 28.57 ? 239 LEU A CD2 1 
ATOM   1875 N N   . GLY A 1 247 ? 16.562  16.724  38.860  1.00 27.94 ? 240 GLY A N   1 
ATOM   1876 C CA  . GLY A 1 247 ? 15.899  17.416  39.981  1.00 28.56 ? 240 GLY A CA  1 
ATOM   1877 C C   . GLY A 1 247 ? 14.837  16.525  40.600  1.00 28.82 ? 240 GLY A C   1 
ATOM   1878 O O   . GLY A 1 247 ? 14.579  16.649  41.807  1.00 29.02 ? 240 GLY A O   1 
ATOM   1879 N N   . ILE A 1 248 ? 14.316  15.552  39.838  1.00 26.32 ? 241 ILE A N   1 
ATOM   1880 C CA  . ILE A 1 248 ? 13.330  14.588  40.393  1.00 26.26 ? 241 ILE A CA  1 
ATOM   1881 C C   . ILE A 1 248 ? 14.005  13.251  40.719  1.00 22.70 ? 241 ILE A C   1 
ATOM   1882 O O   . ILE A 1 248 ? 13.738  12.666  41.753  1.00 23.33 ? 241 ILE A O   1 
ATOM   1883 C CB  . ILE A 1 248 ? 12.128  14.490  39.445  1.00 24.97 ? 241 ILE A CB  1 
ATOM   1884 C CG1 . ILE A 1 248 ? 11.334  15.807  39.518  1.00 29.76 ? 241 ILE A CG1 1 
ATOM   1885 C CG2 . ILE A 1 248 ? 11.271  13.283  39.775  1.00 24.98 ? 241 ILE A CG2 1 
ATOM   1886 C CD1 . ILE A 1 248 ? 10.365  16.043  38.383  1.00 31.82 ? 241 ILE A CD1 1 
ATOM   1887 N N   . LEU A 1 249 ? 14.776  12.712  39.782  1.00 22.50 ? 242 LEU A N   1 
ATOM   1888 C CA  . LEU A 1 249 ? 15.362  11.365  39.937  1.00 21.65 ? 242 LEU A CA  1 
ATOM   1889 C C   . LEU A 1 249 ? 16.487  11.417  40.967  1.00 21.08 ? 242 LEU A C   1 
ATOM   1890 O O   . LEU A 1 249 ? 16.813  10.397  41.506  1.00 19.84 ? 242 LEU A O   1 
ATOM   1891 C CB  . LEU A 1 249 ? 15.954  10.871  38.613  1.00 22.31 ? 242 LEU A CB  1 
ATOM   1892 C CG  . LEU A 1 249 ? 14.981  10.493  37.499  1.00 23.20 ? 242 LEU A CG  1 
ATOM   1893 C CD1 . LEU A 1 249 ? 15.609  9.470   36.576  1.00 20.17 ? 242 LEU A CD1 1 
ATOM   1894 C CD2 . LEU A 1 249 ? 13.678  9.989   38.012  1.00 25.46 ? 242 LEU A CD2 1 
ATOM   1895 N N   . GLY A 1 250 ? 17.101  12.572  41.089  1.00 23.04 ? 243 GLY A N   1 
ATOM   1896 C CA  . GLY A 1 250 ? 18.312  12.732  41.884  1.00 21.05 ? 243 GLY A CA  1 
ATOM   1897 C C   . GLY A 1 250 ? 19.520  12.445  41.012  1.00 21.93 ? 243 GLY A C   1 
ATOM   1898 O O   . GLY A 1 250 ? 19.404  11.955  39.839  1.00 21.75 ? 243 GLY A O   1 
ATOM   1899 N N   . SER A 1 251 ? 20.672  12.741  41.554  1.00 18.29 ? 244 SER A N   1 
ATOM   1900 C CA  . SER A 1 251 ? 21.984  12.440  40.952  1.00 17.44 ? 244 SER A CA  1 
ATOM   1901 C C   . SER A 1 251 ? 22.081  10.977  40.574  1.00 18.58 ? 244 SER A C   1 
ATOM   1902 O O   . SER A 1 251 ? 21.689  10.111  41.359  1.00 19.33 ? 244 SER A O   1 
ATOM   1903 C CB  . SER A 1 251 ? 23.077  12.831  41.933  1.00 17.71 ? 244 SER A CB  1 
ATOM   1904 O OG  . SER A 1 251 ? 23.039  14.220  42.108  1.00 17.17 ? 244 SER A OG  1 
ATOM   1905 N N   . PRO A 1 252 ? 22.585  10.675  39.359  1.00 17.92 ? 245 PRO A N   1 
ATOM   1906 C CA  . PRO A 1 252 ? 22.898  9.313   38.983  1.00 20.74 ? 245 PRO A CA  1 
ATOM   1907 C C   . PRO A 1 252 ? 23.917  8.674   39.936  1.00 23.45 ? 245 PRO A C   1 
ATOM   1908 O O   . PRO A 1 252 ? 24.890  9.317   40.302  1.00 20.71 ? 245 PRO A O   1 
ATOM   1909 C CB  . PRO A 1 252 ? 23.521  9.378   37.584  1.00 21.88 ? 245 PRO A CB  1 
ATOM   1910 C CG  . PRO A 1 252 ? 23.337  10.773  37.116  1.00 23.01 ? 245 PRO A CG  1 
ATOM   1911 C CD  . PRO A 1 252 ? 22.776  11.612  38.247  1.00 21.17 ? 245 PRO A CD  1 
ATOM   1912 N N   . SER A 1 253 ? 23.680  7.394   40.202  1.00 22.42 ? 246 SER A N   1 
ATOM   1913 C CA  . SER A 1 253 ? 24.520  6.508   41.015  1.00 23.47 ? 246 SER A CA  1 
ATOM   1914 C C   . SER A 1 253 ? 25.872  6.348   40.333  1.00 22.50 ? 246 SER A C   1 
ATOM   1915 O O   . SER A 1 253 ? 26.003  6.548   39.115  1.00 20.88 ? 246 SER A O   1 
ATOM   1916 C CB  . SER A 1 253 ? 23.862  5.179   41.179  1.00 22.36 ? 246 SER A CB  1 
ATOM   1917 O OG  . SER A 1 253 ? 23.950  4.434   39.976  1.00 22.57 ? 246 SER A OG  1 
ATOM   1918 N N   . GLN A 1 254 ? 26.867  5.961   41.107  1.00 23.09 ? 247 GLN A N   1 
ATOM   1919 C CA  . GLN A 1 254 ? 28.199  5.660   40.552  1.00 24.29 ? 247 GLN A CA  1 
ATOM   1920 C C   . GLN A 1 254 ? 28.057  4.574   39.486  1.00 23.43 ? 247 GLN A C   1 
ATOM   1921 O O   . GLN A 1 254 ? 28.658  4.691   38.430  1.00 24.81 ? 247 GLN A O   1 
ATOM   1922 C CB  . GLN A 1 254 ? 29.118  5.253   41.708  1.00 26.54 ? 247 GLN A CB  1 
ATOM   1923 C CG  . GLN A 1 254 ? 30.528  4.945   41.251  1.00 31.74 ? 247 GLN A CG  1 
ATOM   1924 C CD  . GLN A 1 254 ? 31.381  4.672   42.463  1.00 39.04 ? 247 GLN A CD  1 
ATOM   1925 O OE1 . GLN A 1 254 ? 31.073  3.812   43.299  1.00 41.19 ? 247 GLN A OE1 1 
ATOM   1926 N NE2 . GLN A 1 254 ? 32.475  5.397   42.558  1.00 44.40 ? 247 GLN A NE2 1 
ATOM   1927 N N   . GLU A 1 255 ? 27.255  3.547   39.749  1.00 25.45 ? 248 GLU A N   1 
ATOM   1928 C CA  . GLU A 1 255 ? 26.982  2.435   38.802  1.00 27.78 ? 248 GLU A CA  1 
ATOM   1929 C C   . GLU A 1 255 ? 26.492  2.988   37.457  1.00 25.10 ? 248 GLU A C   1 
ATOM   1930 O O   . GLU A 1 255 ? 27.025  2.576   36.414  1.00 28.84 ? 248 GLU A O   1 
ATOM   1931 C CB  . GLU A 1 255 ? 25.908  1.512   39.386  1.00 32.04 ? 248 GLU A CB  1 
ATOM   1932 C CG  . GLU A 1 255 ? 25.764  0.196   38.660  1.00 37.03 ? 248 GLU A CG  1 
ATOM   1933 C CD  . GLU A 1 255 ? 24.838  -0.737  39.420  1.00 40.54 ? 248 GLU A CD  1 
ATOM   1934 O OE1 . GLU A 1 255 ? 23.949  -1.291  38.798  1.00 40.41 ? 248 GLU A OE1 1 
ATOM   1935 O OE2 . GLU A 1 255 ? 24.999  -0.866  40.653  1.00 52.29 ? 248 GLU A OE2 1 
ATOM   1936 N N   . ASP A 1 256 ? 25.511  3.891   37.486  1.00 22.24 ? 249 ASP A N   1 
ATOM   1937 C CA  . ASP A 1 256 ? 24.877  4.431   36.262  1.00 24.34 ? 249 ASP A CA  1 
ATOM   1938 C C   . ASP A 1 256 ? 25.856  5.353   35.542  1.00 22.79 ? 249 ASP A C   1 
ATOM   1939 O O   . ASP A 1 256 ? 25.905  5.333   34.300  1.00 24.31 ? 249 ASP A O   1 
ATOM   1940 C CB  . ASP A 1 256 ? 23.585  5.111   36.644  1.00 24.16 ? 249 ASP A CB  1 
ATOM   1941 C CG  . ASP A 1 256 ? 22.502  4.109   37.040  1.00 25.29 ? 249 ASP A CG  1 
ATOM   1942 O OD1 . ASP A 1 256 ? 22.704  2.865   36.914  1.00 28.36 ? 249 ASP A OD1 1 
ATOM   1943 O OD2 . ASP A 1 256 ? 21.511  4.590   37.515  1.00 24.17 ? 249 ASP A OD2 1 
ATOM   1944 N N   . LEU A 1 257 ? 26.703  6.050   36.287  1.00 22.55 ? 250 LEU A N   1 
ATOM   1945 C CA  . LEU A 1 257 ? 27.739  6.894   35.658  1.00 25.83 ? 250 LEU A CA  1 
ATOM   1946 C C   . LEU A 1 257 ? 28.756  5.983   34.999  1.00 26.53 ? 250 LEU A C   1 
ATOM   1947 O O   . LEU A 1 257 ? 29.168  6.314   33.905  1.00 26.36 ? 250 LEU A O   1 
ATOM   1948 C CB  . LEU A 1 257 ? 28.451  7.782   36.669  1.00 25.76 ? 250 LEU A CB  1 
ATOM   1949 C CG  . LEU A 1 257 ? 27.648  8.960   37.175  1.00 29.71 ? 250 LEU A CG  1 
ATOM   1950 C CD1 . LEU A 1 257 ? 28.437  9.652   38.273  1.00 33.02 ? 250 LEU A CD1 1 
ATOM   1951 C CD2 . LEU A 1 257 ? 27.343  9.923   36.053  1.00 30.56 ? 250 LEU A CD2 1 
ATOM   1952 N N   . ASN A 1 258 ? 29.139  4.894   35.670  1.00 31.20 ? 251 ASN A N   1 
ATOM   1953 C CA  . ASN A 1 258 ? 30.163  3.951   35.145  1.00 33.50 ? 251 ASN A CA  1 
ATOM   1954 C C   . ASN A 1 258 ? 29.712  3.438   33.779  1.00 35.25 ? 251 ASN A C   1 
ATOM   1955 O O   . ASN A 1 258 ? 30.586  3.125   32.951  1.00 42.20 ? 251 ASN A O   1 
ATOM   1956 C CB  . ASN A 1 258 ? 30.488  2.809   36.119  1.00 32.65 ? 251 ASN A CB  1 
ATOM   1957 C CG  . ASN A 1 258 ? 31.234  3.251   37.364  1.00 35.91 ? 251 ASN A CG  1 
ATOM   1958 O OD1 . ASN A 1 258 ? 31.320  2.502   38.339  1.00 43.25 ? 251 ASN A OD1 1 
ATOM   1959 N ND2 . ASN A 1 258 ? 31.761  4.468   37.369  1.00 36.09 ? 251 ASN A ND2 1 
ATOM   1960 N N   . CYS A 1 259 ? 28.405  3.406   33.509  1.00 30.85 ? 252 CYS A N   1 
ATOM   1961 C CA  . CYS A 1 259 ? 27.867  2.980   32.194  1.00 31.48 ? 252 CYS A CA  1 
ATOM   1962 C C   . CYS A 1 259 ? 28.026  4.051   31.099  1.00 32.48 ? 252 CYS A C   1 
ATOM   1963 O O   . CYS A 1 259 ? 27.815  3.701   29.935  1.00 41.88 ? 252 CYS A O   1 
ATOM   1964 C CB  . CYS A 1 259 ? 26.407  2.573   32.346  1.00 31.79 ? 252 CYS A CB  1 
ATOM   1965 S SG  . CYS A 1 259 ? 26.225  1.117   33.405  1.00 38.96 ? 252 CYS A SG  1 
ATOM   1966 N N   . ILE A 1 260 ? 28.318  5.315   31.445  1.00 26.59 ? 253 ILE A N   1 
ATOM   1967 C CA  . ILE A 1 260 ? 28.589  6.431   30.507  1.00 26.82 ? 253 ILE A CA  1 
ATOM   1968 C C   . ILE A 1 260 ? 30.114  6.570   30.320  1.00 28.63 ? 253 ILE A C   1 
ATOM   1969 O O   . ILE A 1 260 ? 30.767  7.284   31.094  1.00 29.47 ? 253 ILE A O   1 
ATOM   1970 C CB  . ILE A 1 260 ? 27.990  7.744   31.023  1.00 26.62 ? 253 ILE A CB  1 
ATOM   1971 C CG1 . ILE A 1 260 ? 26.482  7.628   31.275  1.00 24.05 ? 253 ILE A CG1 1 
ATOM   1972 C CG2 . ILE A 1 260 ? 28.310  8.875   30.058  1.00 25.48 ? 253 ILE A CG2 1 
ATOM   1973 C CD1 . ILE A 1 260 ? 25.988  8.636   32.219  1.00 26.28 ? 253 ILE A CD1 1 
ATOM   1974 N N   . ILE A 1 261 ? 30.642  6.010   29.250  1.00 32.56 ? 254 ILE A N   1 
ATOM   1975 C CA  . ILE A 1 261 ? 32.126  5.996   29.073  1.00 32.98 ? 254 ILE A CA  1 
ATOM   1976 C C   . ILE A 1 261 ? 32.580  7.277   28.373  1.00 31.54 ? 254 ILE A C   1 
ATOM   1977 O O   . ILE A 1 261 ? 33.734  7.669   28.573  1.00 34.90 ? 254 ILE A O   1 
ATOM   1978 C CB  . ILE A 1 261 ? 32.533  4.678   28.408  1.00 38.06 ? 254 ILE A CB  1 
ATOM   1979 C CG1 . ILE A 1 261 ? 31.889  4.489   27.038  1.00 45.09 ? 254 ILE A CG1 1 
ATOM   1980 C CG2 . ILE A 1 261 ? 32.173  3.542   29.374  1.00 41.33 ? 254 ILE A CG2 1 
ATOM   1981 C CD1 . ILE A 1 261 ? 32.636  5.125   25.925  1.00 48.78 ? 254 ILE A CD1 1 
ATOM   1982 N N   . ASN A 1 262 ? 31.693  7.956   27.634  1.00 29.45 ? 255 ASN A N   1 
ATOM   1983 C CA  . ASN A 1 262 ? 31.980  9.284   27.035  1.00 28.61 ? 255 ASN A CA  1 
ATOM   1984 C C   . ASN A 1 262 ? 32.449  10.227  28.154  1.00 27.72 ? 255 ASN A C   1 
ATOM   1985 O O   . ASN A 1 262 ? 31.651  10.535  29.082  1.00 24.36 ? 255 ASN A O   1 
ATOM   1986 C CB  . ASN A 1 262 ? 30.747  9.664   26.210  1.00 29.35 ? 255 ASN A CB  1 
ATOM   1987 C CG  . ASN A 1 262 ? 30.428  11.121  25.997  1.00 36.34 ? 255 ASN A CG  1 
ATOM   1988 O OD1 . ASN A 1 262 ? 29.286  11.417  25.634  1.00 46.45 ? 255 ASN A OD1 1 
ATOM   1989 N ND2 . ASN A 1 262 ? 31.374  12.032  26.153  1.00 27.42 ? 255 ASN A ND2 1 
ATOM   1990 N N   . LEU A 1 263 ? 33.700  10.700  28.113  1.00 25.55 ? 256 LEU A N   1 
ATOM   1991 C CA  . LEU A 1 263 ? 34.282  11.488  29.237  1.00 29.30 ? 256 LEU A CA  1 
ATOM   1992 C C   . LEU A 1 263 ? 33.534  12.808  29.394  1.00 23.57 ? 256 LEU A C   1 
ATOM   1993 O O   . LEU A 1 263 ? 33.290  13.201  30.538  1.00 23.55 ? 256 LEU A O   1 
ATOM   1994 C CB  . LEU A 1 263 ? 35.769  11.788  29.001  1.00 31.44 ? 256 LEU A CB  1 
ATOM   1995 C CG  . LEU A 1 263 ? 36.750  11.537  30.144  1.00 34.45 ? 256 LEU A CG  1 
ATOM   1996 C CD1 . LEU A 1 263 ? 37.930  12.491  30.062  1.00 37.01 ? 256 LEU A CD1 1 
ATOM   1997 C CD2 . LEU A 1 263 ? 36.148  11.608  31.531  1.00 31.34 ? 256 LEU A CD2 1 
ATOM   1998 N N   . LYS A 1 264 ? 33.221  13.508  28.299  1.00 22.51 ? 257 LYS A N   1 
ATOM   1999 C CA  . LYS A 1 264 ? 32.576  14.825  28.366  1.00 21.07 ? 257 LYS A CA  1 
ATOM   2000 C C   . LYS A 1 264 ? 31.193  14.658  29.005  1.00 19.82 ? 257 LYS A C   1 
ATOM   2001 O O   . LYS A 1 264 ? 30.890  15.435  29.910  1.00 20.15 ? 257 LYS A O   1 
ATOM   2002 C CB  . LYS A 1 264 ? 32.451  15.482  26.997  1.00 27.12 ? 257 LYS A CB  1 
ATOM   2003 C CG  . LYS A 1 264 ? 33.733  16.175  26.538  1.00 34.65 ? 257 LYS A CG  1 
ATOM   2004 C CD  . LYS A 1 264 ? 33.523  17.133  25.373  1.00 38.33 ? 257 LYS A CD  1 
ATOM   2005 C CE  . LYS A 1 264 ? 32.986  16.437  24.142  1.00 49.49 ? 257 LYS A CE  1 
ATOM   2006 N NZ  . LYS A 1 264 ? 33.065  17.280  22.920  1.00 54.17 ? 257 LYS A NZ  1 
ATOM   2007 N N   . ALA A 1 265 ? 30.445  13.633  28.621  1.00 19.06 ? 258 ALA A N   1 
ATOM   2008 C CA  . ALA A 1 265 ? 29.111  13.416  29.239  1.00 17.47 ? 258 ALA A CA  1 
ATOM   2009 C C   . ALA A 1 265 ? 29.300  13.052  30.717  1.00 17.24 ? 258 ALA A C   1 
ATOM   2010 O O   . ALA A 1 265 ? 28.631  13.657  31.583  1.00 16.60 ? 258 ALA A O   1 
ATOM   2011 C CB  . ALA A 1 265 ? 28.295  12.383  28.505  1.00 17.32 ? 258 ALA A CB  1 
ATOM   2012 N N   . ARG A 1 266 ? 30.186  12.116  31.037  1.00 17.20 ? 259 ARG A N   1 
ATOM   2013 C CA  . ARG A 1 266 ? 30.378  11.705  32.453  1.00 19.98 ? 259 ARG A CA  1 
ATOM   2014 C C   . ARG A 1 266 ? 30.851  12.899  33.291  1.00 20.05 ? 259 ARG A C   1 
ATOM   2015 O O   . ARG A 1 266 ? 30.283  13.124  34.373  1.00 19.38 ? 259 ARG A O   1 
ATOM   2016 C CB  . ARG A 1 266 ? 31.347  10.535  32.587  1.00 24.57 ? 259 ARG A CB  1 
ATOM   2017 C CG  . ARG A 1 266 ? 31.256  9.963   33.994  1.00 27.99 ? 259 ARG A CG  1 
ATOM   2018 C CD  . ARG A 1 266 ? 32.388  9.050   34.292  1.00 29.12 ? 259 ARG A CD  1 
ATOM   2019 N NE  . ARG A 1 266 ? 32.187  7.805   33.590  1.00 30.37 ? 259 ARG A NE  1 
ATOM   2020 C CZ  . ARG A 1 266 ? 32.837  6.699   33.896  1.00 32.34 ? 259 ARG A CZ  1 
ATOM   2021 N NH1 . ARG A 1 266 ? 33.716  6.717   34.887  1.00 33.63 ? 259 ARG A NH1 1 
ATOM   2022 N NH2 . ARG A 1 266 ? 32.617  5.597   33.212  1.00 30.30 ? 259 ARG A NH2 1 
ATOM   2023 N N   . ASN A 1 267 ? 31.775  13.712  32.796  1.00 18.29 ? 260 ASN A N   1 
ATOM   2024 C CA  . ASN A 1 267 ? 32.299  14.859  33.576  1.00 20.10 ? 260 ASN A CA  1 
ATOM   2025 C C   . ASN A 1 267 ? 31.254  15.934  33.743  1.00 19.77 ? 260 ASN A C   1 
ATOM   2026 O O   . ASN A 1 267 ? 31.235  16.572  34.797  1.00 19.45 ? 260 ASN A O   1 
ATOM   2027 C CB  . ASN A 1 267 ? 33.537  15.507  32.965  1.00 20.53 ? 260 ASN A CB  1 
ATOM   2028 C CG  . ASN A 1 267 ? 34.756  14.688  33.273  1.00 24.67 ? 260 ASN A CG  1 
ATOM   2029 O OD1 . ASN A 1 267 ? 35.795  14.864  32.645  1.00 25.89 ? 260 ASN A OD1 1 
ATOM   2030 N ND2 . ASN A 1 267 ? 34.649  13.871  34.304  1.00 24.48 ? 260 ASN A ND2 1 
ATOM   2031 N N   . TYR A 1 268 ? 30.381  16.105  32.767  1.00 17.71 ? 261 TYR A N   1 
ATOM   2032 C CA  . TYR A 1 268 ? 29.278  17.060  32.949  1.00 18.30 ? 261 TYR A CA  1 
ATOM   2033 C C   . TYR A 1 268 ? 28.462  16.631  34.182  1.00 17.87 ? 261 TYR A C   1 
ATOM   2034 O O   . TYR A 1 268 ? 28.141  17.440  35.053  1.00 17.54 ? 261 TYR A O   1 
ATOM   2035 C CB  . TYR A 1 268 ? 28.391  17.114  31.720  1.00 18.85 ? 261 TYR A CB  1 
ATOM   2036 C CG  . TYR A 1 268 ? 27.222  17.985  32.005  1.00 18.04 ? 261 TYR A CG  1 
ATOM   2037 C CD1 . TYR A 1 268 ? 27.410  19.345  32.147  1.00 18.49 ? 261 TYR A CD1 1 
ATOM   2038 C CD2 . TYR A 1 268 ? 25.968  17.452  32.230  1.00 17.50 ? 261 TYR A CD2 1 
ATOM   2039 C CE1 . TYR A 1 268 ? 26.334  20.175  32.373  1.00 19.53 ? 261 TYR A CE1 1 
ATOM   2040 C CE2 . TYR A 1 268 ? 24.907  18.264  32.532  1.00 18.81 ? 261 TYR A CE2 1 
ATOM   2041 C CZ  . TYR A 1 268 ? 25.095  19.636  32.614  1.00 18.65 ? 261 TYR A CZ  1 
ATOM   2042 O OH  . TYR A 1 268 ? 24.080  20.469  32.924  1.00 21.94 ? 261 TYR A OH  1 
ATOM   2043 N N   . LEU A 1 269 ? 28.062  15.359  34.239  1.00 15.64 ? 262 LEU A N   1 
ATOM   2044 C CA  . LEU A 1 269 ? 27.222  14.885  35.380  1.00 16.31 ? 262 LEU A CA  1 
ATOM   2045 C C   . LEU A 1 269 ? 27.974  15.021  36.700  1.00 14.63 ? 262 LEU A C   1 
ATOM   2046 O O   . LEU A 1 269 ? 27.364  15.401  37.708  1.00 17.51 ? 262 LEU A O   1 
ATOM   2047 C CB  . LEU A 1 269 ? 26.812  13.436  35.137  1.00 15.84 ? 262 LEU A CB  1 
ATOM   2048 C CG  . LEU A 1 269 ? 25.878  13.242  33.944  1.00 16.94 ? 262 LEU A CG  1 
ATOM   2049 C CD1 . LEU A 1 269 ? 25.742  11.741  33.683  1.00 17.78 ? 262 LEU A CD1 1 
ATOM   2050 C CD2 . LEU A 1 269 ? 24.534  13.921  34.193  1.00 19.14 ? 262 LEU A CD2 1 
ATOM   2051 N N   . LEU A 1 270 ? 29.264  14.732  36.683  1.00 15.49 ? 263 LEU A N   1 
ATOM   2052 C CA  . LEU A 1 270 ? 30.107  14.861  37.896  1.00 17.00 ? 263 LEU A CA  1 
ATOM   2053 C C   . LEU A 1 270 ? 30.235  16.304  38.357  1.00 16.73 ? 263 LEU A C   1 
ATOM   2054 O O   . LEU A 1 270 ? 30.364  16.506  39.578  1.00 18.04 ? 263 LEU A O   1 
ATOM   2055 C CB  . LEU A 1 270 ? 31.481  14.268  37.610  1.00 18.52 ? 263 LEU A CB  1 
ATOM   2056 C CG  . LEU A 1 270 ? 31.531  12.757  37.504  1.00 22.61 ? 263 LEU A CG  1 
ATOM   2057 C CD1 . LEU A 1 270 ? 32.924  12.294  37.112  1.00 24.70 ? 263 LEU A CD1 1 
ATOM   2058 C CD2 . LEU A 1 270 ? 31.090  12.101  38.800  1.00 22.89 ? 263 LEU A CD2 1 
ATOM   2059 N N   . SER A 1 271 ? 30.117  17.278  37.460  1.00 17.02 ? 264 SER A N   1 
ATOM   2060 C CA  . SER A 1 271 ? 30.225  18.728  37.752  1.00 19.95 ? 264 SER A CA  1 
ATOM   2061 C C   . SER A 1 271 ? 29.011  19.233  38.526  1.00 20.47 ? 264 SER A C   1 
ATOM   2062 O O   . SER A 1 271 ? 29.109  20.328  39.102  1.00 23.13 ? 264 SER A O   1 
ATOM   2063 C CB  . SER A 1 271 ? 30.429  19.543  36.459  1.00 18.56 ? 264 SER A CB  1 
ATOM   2064 O OG  . SER A 1 271 ? 29.228  19.739  35.734  1.00 19.48 ? 264 SER A OG  1 
ATOM   2065 N N   . LEU A 1 272 ? 27.883  18.527  38.475  1.00 17.45 ? 265 LEU A N   1 
ATOM   2066 C CA  . LEU A 1 272 ? 26.602  19.044  38.992  1.00 18.32 ? 265 LEU A CA  1 
ATOM   2067 C C   . LEU A 1 272 ? 26.596  18.853  40.496  1.00 18.38 ? 265 LEU A C   1 
ATOM   2068 O O   . LEU A 1 272 ? 27.100  17.836  40.976  1.00 19.65 ? 265 LEU A O   1 
ATOM   2069 C CB  . LEU A 1 272 ? 25.488  18.240  38.356  1.00 18.85 ? 265 LEU A CB  1 
ATOM   2070 C CG  . LEU A 1 272 ? 25.357  18.422  36.849  1.00 19.88 ? 265 LEU A CG  1 
ATOM   2071 C CD1 . LEU A 1 272 ? 24.216  17.567  36.349  1.00 20.08 ? 265 LEU A CD1 1 
ATOM   2072 C CD2 . LEU A 1 272 ? 25.131  19.872  36.508  1.00 20.01 ? 265 LEU A CD2 1 
ATOM   2073 N N   . PRO A 1 273 ? 25.964  19.770  41.248  1.00 20.16 ? 266 PRO A N   1 
ATOM   2074 C CA  . PRO A 1 273 ? 25.761  19.547  42.678  1.00 20.57 ? 266 PRO A CA  1 
ATOM   2075 C C   . PRO A 1 273 ? 24.909  18.288  42.876  1.00 21.28 ? 266 PRO A C   1 
ATOM   2076 O O   . PRO A 1 273 ? 24.057  17.944  42.073  1.00 21.59 ? 266 PRO A O   1 
ATOM   2077 C CB  . PRO A 1 273 ? 25.005  20.783  43.150  1.00 21.64 ? 266 PRO A CB  1 
ATOM   2078 C CG  . PRO A 1 273 ? 25.217  21.799  42.077  1.00 23.35 ? 266 PRO A CG  1 
ATOM   2079 C CD  . PRO A 1 273 ? 25.317  21.006  40.792  1.00 21.81 ? 266 PRO A CD  1 
ATOM   2080 N N   . HIS A 1 274 ? 25.114  17.615  43.981  1.00 22.18 ? 267 HIS A N   1 
ATOM   2081 C CA  . HIS A 1 274 ? 24.268  16.473  44.413  1.00 22.40 ? 267 HIS A CA  1 
ATOM   2082 C C   . HIS A 1 274 ? 22.806  16.879  44.540  1.00 22.66 ? 267 HIS A C   1 
ATOM   2083 O O   . HIS A 1 274 ? 22.496  17.936  45.119  1.00 22.10 ? 267 HIS A O   1 
ATOM   2084 C CB  . HIS A 1 274 ? 24.767  15.900  45.756  1.00 24.35 ? 267 HIS A CB  1 
ATOM   2085 C CG  . HIS A 1 274 ? 24.012  14.672  46.136  1.00 26.08 ? 267 HIS A CG  1 
ATOM   2086 N ND1 . HIS A 1 274 ? 23.303  14.570  47.326  1.00 36.49 ? 267 HIS A ND1 1 
ATOM   2087 C CD2 . HIS A 1 274 ? 23.752  13.544  45.452  1.00 27.69 ? 267 HIS A CD2 1 
ATOM   2088 C CE1 . HIS A 1 274 ? 22.698  13.396  47.369  1.00 32.50 ? 267 HIS A CE1 1 
ATOM   2089 N NE2 . HIS A 1 274 ? 22.947  12.762  46.234  1.00 29.64 ? 267 HIS A NE2 1 
ATOM   2090 N N   . LYS A 1 275 ? 21.922  16.031  44.028  1.00 20.36 ? 268 LYS A N   1 
ATOM   2091 C CA  . LYS A 1 275 ? 20.463  16.241  44.088  1.00 22.86 ? 268 LYS A CA  1 
ATOM   2092 C C   . LYS A 1 275 ? 19.903  14.932  44.603  1.00 22.24 ? 268 LYS A C   1 
ATOM   2093 O O   . LYS A 1 275 ? 20.301  13.825  44.102  1.00 22.95 ? 268 LYS A O   1 
ATOM   2094 C CB  . LYS A 1 275 ? 19.886  16.629  42.724  1.00 24.89 ? 268 LYS A CB  1 
ATOM   2095 C CG  . LYS A 1 275 ? 20.290  18.013  42.233  1.00 29.63 ? 268 LYS A CG  1 
ATOM   2096 C CD  . LYS A 1 275 ? 20.034  18.251  40.746  1.00 36.93 ? 268 LYS A CD  1 
ATOM   2097 C CE  . LYS A 1 275 ? 21.235  18.003  39.842  1.00 40.58 ? 268 LYS A CE  1 
ATOM   2098 N NZ  . LYS A 1 275 ? 21.243  18.921  38.676  1.00 37.87 ? 268 LYS A NZ  1 
ATOM   2099 N N   . ASN A 1 276 ? 19.021  15.043  45.595  1.00 23.85 ? 269 ASN A N   1 
ATOM   2100 C CA  . ASN A 1 276 ? 18.305  13.849  46.070  1.00 25.07 ? 269 ASN A CA  1 
ATOM   2101 C C   . ASN A 1 276 ? 17.049  13.629  45.223  1.00 21.70 ? 269 ASN A C   1 
ATOM   2102 O O   . ASN A 1 276 ? 16.463  14.602  44.705  1.00 23.03 ? 269 ASN A O   1 
ATOM   2103 C CB  . ASN A 1 276 ? 18.041  13.932  47.574  1.00 29.10 ? 269 ASN A CB  1 
ATOM   2104 C CG  . ASN A 1 276 ? 19.291  13.623  48.369  1.00 31.90 ? 269 ASN A CG  1 
ATOM   2105 O OD1 . ASN A 1 276 ? 19.855  12.525  48.266  1.00 35.43 ? 269 ASN A OD1 1 
ATOM   2106 N ND2 . ASN A 1 276 ? 19.712  14.570  49.188  1.00 36.74 ? 269 ASN A ND2 1 
ATOM   2107 N N   . LYS A 1 277 ? 16.631  12.369  45.197  1.00 26.24 ? 270 LYS A N   1 
ATOM   2108 C CA  . LYS A 1 277 ? 15.366  11.902  44.598  1.00 27.27 ? 270 LYS A CA  1 
ATOM   2109 C C   . LYS A 1 277 ? 14.182  12.611  45.284  1.00 28.74 ? 270 LYS A C   1 
ATOM   2110 O O   . LYS A 1 277 ? 14.188  12.742  46.521  1.00 29.88 ? 270 LYS A O   1 
ATOM   2111 C CB  . LYS A 1 277 ? 15.305  10.376  44.723  1.00 29.27 ? 270 LYS A CB  1 
ATOM   2112 C CG  . LYS A 1 277 ? 14.062  9.724   44.130  1.00 34.12 ? 270 LYS A CG  1 
ATOM   2113 C CD  . LYS A 1 277 ? 14.253  8.239   43.788  1.00 36.42 ? 270 LYS A CD  1 
ATOM   2114 C CE  . LYS A 1 277 ? 13.115  7.657   42.949  1.00 39.60 ? 270 LYS A CE  1 
ATOM   2115 N NZ  . LYS A 1 277 ? 13.058  8.190   41.554  1.00 35.25 ? 270 LYS A NZ  1 
ATOM   2116 N N   . VAL A 1 278 ? 13.225  13.092  44.497  1.00 29.98 ? 271 VAL A N   1 
ATOM   2117 C CA  . VAL A 1 278 ? 11.896  13.568  44.969  1.00 29.40 ? 271 VAL A CA  1 
ATOM   2118 C C   . VAL A 1 278 ? 10.971  12.371  44.847  1.00 32.86 ? 271 VAL A C   1 
ATOM   2119 O O   . VAL A 1 278 ? 10.800  11.871  43.750  1.00 28.52 ? 271 VAL A O   1 
ATOM   2120 C CB  . VAL A 1 278 ? 11.367  14.742  44.127  1.00 31.37 ? 271 VAL A CB  1 
ATOM   2121 C CG1 . VAL A 1 278 ? 9.997   15.217  44.593  1.00 34.13 ? 271 VAL A CG1 1 
ATOM   2122 C CG2 . VAL A 1 278 ? 12.363  15.890  44.103  1.00 36.59 ? 271 VAL A CG2 1 
ATOM   2123 N N   . PRO A 1 279 ? 10.357  11.901  45.946  1.00 28.70 ? 272 PRO A N   1 
ATOM   2124 C CA  . PRO A 1 279 ? 9.505   10.713  45.909  1.00 27.65 ? 272 PRO A CA  1 
ATOM   2125 C C   . PRO A 1 279 ? 8.301   10.983  45.009  1.00 26.68 ? 272 PRO A C   1 
ATOM   2126 O O   . PRO A 1 279 ? 7.716   12.069  45.032  1.00 23.71 ? 272 PRO A O   1 
ATOM   2127 C CB  . PRO A 1 279 ? 9.069   10.496  47.370  1.00 29.99 ? 272 PRO A CB  1 
ATOM   2128 C CG  . PRO A 1 279 ? 10.028  11.343  48.176  1.00 31.13 ? 272 PRO A CG  1 
ATOM   2129 C CD  . PRO A 1 279 ? 10.411  12.504  47.283  1.00 29.52 ? 272 PRO A CD  1 
ATOM   2130 N N   . TRP A 1 280 ? 7.956   9.999   44.186  1.00 24.09 ? 273 TRP A N   1 
ATOM   2131 C CA  . TRP A 1 280 ? 6.815   10.131  43.257  1.00 26.11 ? 273 TRP A CA  1 
ATOM   2132 C C   . TRP A 1 280 ? 5.520   10.468  44.018  1.00 25.08 ? 273 TRP A C   1 
ATOM   2133 O O   . TRP A 1 280 ? 4.695   11.224  43.457  1.00 24.78 ? 273 TRP A O   1 
ATOM   2134 C CB  . TRP A 1 280 ? 6.660   8.828   42.484  1.00 26.04 ? 273 TRP A CB  1 
ATOM   2135 C CG  . TRP A 1 280 ? 7.849   8.505   41.651  1.00 27.35 ? 273 TRP A CG  1 
ATOM   2136 C CD1 . TRP A 1 280 ? 8.713   7.461   41.785  1.00 29.21 ? 273 TRP A CD1 1 
ATOM   2137 C CD2 . TRP A 1 280 ? 8.266   9.241   40.505  1.00 25.61 ? 273 TRP A CD2 1 
ATOM   2138 N NE1 . TRP A 1 280 ? 9.663   7.521   40.806  1.00 30.37 ? 273 TRP A NE1 1 
ATOM   2139 C CE2 . TRP A 1 280 ? 9.417   8.601   40.012  1.00 26.70 ? 273 TRP A CE2 1 
ATOM   2140 C CE3 . TRP A 1 280 ? 7.793   10.395  39.887  1.00 25.24 ? 273 TRP A CE3 1 
ATOM   2141 C CZ2 . TRP A 1 280 ? 10.097  9.079   38.904  1.00 23.37 ? 273 TRP A CZ2 1 
ATOM   2142 C CZ3 . TRP A 1 280 ? 8.472   10.868  38.790  1.00 28.09 ? 273 TRP A CZ3 1 
ATOM   2143 C CH2 . TRP A 1 280 ? 9.590   10.205  38.304  1.00 24.51 ? 273 TRP A CH2 1 
ATOM   2144 N N   . ASN A 1 281 ? 5.332   9.878   45.197  1.00 27.42 ? 274 ASN A N   1 
ATOM   2145 C CA  . ASN A 1 281 ? 4.086   10.114  45.984  1.00 29.05 ? 274 ASN A CA  1 
ATOM   2146 C C   . ASN A 1 281 ? 4.051   11.566  46.459  1.00 31.55 ? 274 ASN A C   1 
ATOM   2147 O O   . ASN A 1 281 ? 2.930   12.083  46.673  1.00 32.37 ? 274 ASN A O   1 
ATOM   2148 C CB  . ASN A 1 281 ? 3.823   9.055   47.059  1.00 32.17 ? 274 ASN A CB  1 
ATOM   2149 C CG  . ASN A 1 281 ? 4.851   8.947   48.162  1.00 37.26 ? 274 ASN A CG  1 
ATOM   2150 O OD1 . ASN A 1 281 ? 4.755   8.045   48.991  1.00 46.76 ? 274 ASN A OD1 1 
ATOM   2151 N ND2 . ASN A 1 281 ? 5.816   9.841   48.209  1.00 33.85 ? 274 ASN A ND2 1 
ATOM   2152 N N   . ARG A 1 282 ? 5.202   12.233  46.571  1.00 30.85 ? 275 ARG A N   1 
ATOM   2153 C CA  . ARG A 1 282 ? 5.231   13.676  46.915  1.00 35.63 ? 275 ARG A CA  1 
ATOM   2154 C C   . ARG A 1 282 ? 4.776   14.469  45.699  1.00 33.05 ? 275 ARG A C   1 
ATOM   2155 O O   . ARG A 1 282 ? 3.985   15.398  45.894  1.00 38.25 ? 275 ARG A O   1 
ATOM   2156 C CB  . ARG A 1 282 ? 6.597   14.171  47.411  1.00 38.02 ? 275 ARG A CB  1 
ATOM   2157 C CG  . ARG A 1 282 ? 6.569   15.635  47.832  1.00 44.62 ? 275 ARG A CG  1 
ATOM   2158 C CD  . ARG A 1 282 ? 7.922   16.237  48.137  1.00 47.35 ? 275 ARG A CD  1 
ATOM   2159 N NE  . ARG A 1 282 ? 8.519   15.554  49.279  1.00 52.72 ? 275 ARG A NE  1 
ATOM   2160 C CZ  . ARG A 1 282 ? 9.820   15.543  49.563  1.00 50.78 ? 275 ARG A CZ  1 
ATOM   2161 N NH1 . ARG A 1 282 ? 10.683  16.188  48.791  1.00 50.51 ? 275 ARG A NH1 1 
ATOM   2162 N NH2 . ARG A 1 282 ? 10.249  14.875  50.621  1.00 51.56 ? 275 ARG A NH2 1 
ATOM   2163 N N   . LEU A 1 283 ? 5.205   14.089  44.488  1.00 29.13 ? 276 LEU A N   1 
ATOM   2164 C CA  . LEU A 1 283 ? 4.838   14.777  43.224  1.00 28.32 ? 276 LEU A CA  1 
ATOM   2165 C C   . LEU A 1 283 ? 3.376   14.493  42.869  1.00 27.12 ? 276 LEU A C   1 
ATOM   2166 O O   . LEU A 1 283 ? 2.769   15.387  42.356  1.00 28.63 ? 276 LEU A O   1 
ATOM   2167 C CB  . LEU A 1 283 ? 5.743   14.321  42.071  1.00 31.81 ? 276 LEU A CB  1 
ATOM   2168 C CG  . LEU A 1 283 ? 7.141   14.940  41.987  1.00 33.92 ? 276 LEU A CG  1 
ATOM   2169 C CD1 . LEU A 1 283 ? 7.928   14.244  40.890  1.00 37.26 ? 276 LEU A CD1 1 
ATOM   2170 C CD2 . LEU A 1 283 ? 7.100   16.439  41.715  1.00 37.09 ? 276 LEU A CD2 1 
ATOM   2171 N N   . PHE A 1 284 ? 2.863   13.285  43.159  1.00 25.79 ? 277 PHE A N   1 
ATOM   2172 C CA  . PHE A 1 284 ? 1.570   12.759  42.659  1.00 28.13 ? 277 PHE A CA  1 
ATOM   2173 C C   . PHE A 1 284 ? 0.811   12.149  43.825  1.00 28.11 ? 277 PHE A C   1 
ATOM   2174 O O   . PHE A 1 284 ? 0.685   10.932  43.939  1.00 27.95 ? 277 PHE A O   1 
ATOM   2175 C CB  . PHE A 1 284 ? 1.843   11.735  41.555  1.00 27.39 ? 277 PHE A CB  1 
ATOM   2176 C CG  . PHE A 1 284 ? 2.654   12.272  40.400  1.00 26.43 ? 277 PHE A CG  1 
ATOM   2177 C CD1 . PHE A 1 284 ? 2.185   13.328  39.633  1.00 28.63 ? 277 PHE A CD1 1 
ATOM   2178 C CD2 . PHE A 1 284 ? 3.887   11.729  40.087  1.00 27.34 ? 277 PHE A CD2 1 
ATOM   2179 C CE1 . PHE A 1 284 ? 2.923   13.802  38.558  1.00 30.29 ? 277 PHE A CE1 1 
ATOM   2180 C CE2 . PHE A 1 284 ? 4.637   12.229  39.038  1.00 26.14 ? 277 PHE A CE2 1 
ATOM   2181 C CZ  . PHE A 1 284 ? 4.157   13.268  38.284  1.00 27.21 ? 277 PHE A CZ  1 
ATOM   2182 N N   . PRO A 1 285 ? 0.375   12.978  44.797  1.00 30.28 ? 278 PRO A N   1 
ATOM   2183 C CA  . PRO A 1 285 ? -0.200  12.463  46.034  1.00 30.20 ? 278 PRO A CA  1 
ATOM   2184 C C   . PRO A 1 285 ? -1.551  11.762  45.817  1.00 30.97 ? 278 PRO A C   1 
ATOM   2185 O O   . PRO A 1 285 ? -1.915  10.972  46.659  1.00 31.59 ? 278 PRO A O   1 
ATOM   2186 C CB  . PRO A 1 285 ? -0.373  13.708  46.923  1.00 33.37 ? 278 PRO A CB  1 
ATOM   2187 C CG  . PRO A 1 285 ? -0.351  14.886  45.959  1.00 33.71 ? 278 PRO A CG  1 
ATOM   2188 C CD  . PRO A 1 285 ? 0.460   14.442  44.754  1.00 32.81 ? 278 PRO A CD  1 
ATOM   2189 N N   . ASN A 1 286 ? -2.216  12.049  44.694  1.00 33.53 ? 279 ASN A N   1 
ATOM   2190 C CA  . ASN A 1 286 ? -3.553  11.488  44.344  1.00 36.93 ? 279 ASN A CA  1 
ATOM   2191 C C   . ASN A 1 286 ? -3.364  10.192  43.533  1.00 34.87 ? 279 ASN A C   1 
ATOM   2192 O O   . ASN A 1 286 ? -4.360  9.547   43.243  1.00 30.59 ? 279 ASN A O   1 
ATOM   2193 C CB  . ASN A 1 286 ? -4.434  12.491  43.576  1.00 43.92 ? 279 ASN A CB  1 
ATOM   2194 C CG  . ASN A 1 286 ? -4.291  13.954  43.965  1.00 52.10 ? 279 ASN A CG  1 
ATOM   2195 O OD1 . ASN A 1 286 ? -4.741  14.846  43.246  1.00 54.48 ? 279 ASN A OD1 1 
ATOM   2196 N ND2 . ASN A 1 286 ? -3.668  14.237  45.093  1.00 60.80 ? 279 ASN A ND2 1 
ATOM   2197 N N   . ALA A 1 287 ? -2.128  9.791   43.200  1.00 30.35 ? 280 ALA A N   1 
ATOM   2198 C CA  . ALA A 1 287 ? -1.853  8.699   42.233  1.00 27.35 ? 280 ALA A CA  1 
ATOM   2199 C C   . ALA A 1 287 ? -2.000  7.322   42.865  1.00 26.17 ? 280 ALA A C   1 
ATOM   2200 O O   . ALA A 1 287 ? -1.685  7.119   44.022  1.00 28.41 ? 280 ALA A O   1 
ATOM   2201 C CB  . ALA A 1 287 ? -0.463  8.846   41.628  1.00 26.25 ? 280 ALA A CB  1 
ATOM   2202 N N   . ASP A 1 288 ? -2.451  6.355   42.080  1.00 25.15 ? 281 ASP A N   1 
ATOM   2203 C CA  . ASP A 1 288 ? -2.447  4.930   42.449  1.00 25.39 ? 281 ASP A CA  1 
ATOM   2204 C C   . ASP A 1 288 ? -1.004  4.488   42.704  1.00 26.77 ? 281 ASP A C   1 
ATOM   2205 O O   . ASP A 1 288 ? -0.109  4.785   41.864  1.00 20.98 ? 281 ASP A O   1 
ATOM   2206 C CB  . ASP A 1 288 ? -3.137  4.165   41.325  1.00 27.94 ? 281 ASP A CB  1 
ATOM   2207 C CG  . ASP A 1 288 ? -3.362  2.696   41.556  1.00 33.00 ? 281 ASP A CG  1 
ATOM   2208 O OD1 . ASP A 1 288 ? -2.490  2.040   42.099  1.00 35.28 ? 281 ASP A OD1 1 
ATOM   2209 O OD2 . ASP A 1 288 ? -4.417  2.224   41.119  1.00 40.27 ? 281 ASP A OD2 1 
ATOM   2210 N N   . SER A 1 289 ? -0.754  3.811   43.821  1.00 23.53 ? 282 SER A N   1 
ATOM   2211 C CA  . SER A 1 289 ? 0.616   3.398   44.199  1.00 25.53 ? 282 SER A CA  1 
ATOM   2212 C C   . SER A 1 289 ? 1.226   2.507   43.102  1.00 26.31 ? 282 SER A C   1 
ATOM   2213 O O   . SER A 1 289 ? 2.472   2.608   42.863  1.00 23.07 ? 282 SER A O   1 
ATOM   2214 C CB  . SER A 1 289 ? 0.650   2.756   45.581  1.00 29.22 ? 282 SER A CB  1 
ATOM   2215 O OG  . SER A 1 289 ? 0.072   1.457   45.581  1.00 31.71 ? 282 SER A OG  1 
ATOM   2216 N N   . LYS A 1 290 ? 0.409   1.703   42.418  1.00 22.56 ? 283 LYS A N   1 
ATOM   2217 C CA  . LYS A 1 290 ? 0.933   0.743   41.424  1.00 23.59 ? 283 LYS A CA  1 
ATOM   2218 C C   . LYS A 1 290 ? 1.364   1.551   40.199  1.00 20.16 ? 283 LYS A C   1 
ATOM   2219 O O   . LYS A 1 290 ? 2.349   1.145   39.570  1.00 20.90 ? 283 LYS A O   1 
ATOM   2220 C CB  . LYS A 1 290 ? -0.111  -0.320  41.092  1.00 25.76 ? 283 LYS A CB  1 
ATOM   2221 C CG  . LYS A 1 290 ? -0.379  -1.289  42.233  1.00 27.81 ? 283 LYS A CG  1 
ATOM   2222 C CD  . LYS A 1 290 ? -1.265  -2.431  41.841  1.00 30.63 ? 283 LYS A CD  1 
ATOM   2223 C CE  . LYS A 1 290 ? -1.591  -3.330  43.010  1.00 38.87 ? 283 LYS A CE  1 
ATOM   2224 N NZ  . LYS A 1 290 ? -2.568  -4.375  42.613  1.00 39.80 ? 283 LYS A NZ  1 
ATOM   2225 N N   . ALA A 1 291 ? 0.669   2.648   39.911  1.00 19.59 ? 284 ALA A N   1 
ATOM   2226 C CA  . ALA A 1 291 ? 0.972   3.531   38.755  1.00 19.32 ? 284 ALA A CA  1 
ATOM   2227 C C   . ALA A 1 291 ? 2.323   4.183   39.014  1.00 19.34 ? 284 ALA A C   1 
ATOM   2228 O O   . ALA A 1 291 ? 3.165   4.223   38.115  1.00 18.17 ? 284 ALA A O   1 
ATOM   2229 C CB  . ALA A 1 291 ? -0.074  4.574   38.512  1.00 18.51 ? 284 ALA A CB  1 
ATOM   2230 N N   . LEU A 1 292 ? 2.555   4.592   40.262  1.00 18.93 ? 285 LEU A N   1 
ATOM   2231 C CA  . LEU A 1 292 ? 3.840   5.209   40.636  1.00 19.12 ? 285 LEU A CA  1 
ATOM   2232 C C   . LEU A 1 292 ? 4.977   4.201   40.600  1.00 19.68 ? 285 LEU A C   1 
ATOM   2233 O O   . LEU A 1 292 ? 6.071   4.603   40.194  1.00 19.19 ? 285 LEU A O   1 
ATOM   2234 C CB  . LEU A 1 292 ? 3.697   5.895   41.991  1.00 19.50 ? 285 LEU A CB  1 
ATOM   2235 C CG  . LEU A 1 292 ? 2.737   7.070   42.004  1.00 21.34 ? 285 LEU A CG  1 
ATOM   2236 C CD1 . LEU A 1 292 ? 2.817   7.767   43.349  1.00 23.04 ? 285 LEU A CD1 1 
ATOM   2237 C CD2 . LEU A 1 292 ? 2.975   8.048   40.879  1.00 25.54 ? 285 LEU A CD2 1 
ATOM   2238 N N   . ASP A 1 293 ? 4.749   2.931   40.947  1.00 18.58 ? 286 ASP A N   1 
ATOM   2239 C CA  . ASP A 1 293 ? 5.779   1.897   40.869  1.00 20.50 ? 286 ASP A CA  1 
ATOM   2240 C C   . ASP A 1 293 ? 6.192   1.754   39.395  1.00 18.11 ? 286 ASP A C   1 
ATOM   2241 O O   . ASP A 1 293 ? 7.374   1.690   39.108  1.00 20.24 ? 286 ASP A O   1 
ATOM   2242 C CB  . ASP A 1 293 ? 5.268   0.560   41.394  1.00 21.73 ? 286 ASP A CB  1 
ATOM   2243 C CG  . ASP A 1 293 ? 6.389   -0.414  41.496  1.00 21.76 ? 286 ASP A CG  1 
ATOM   2244 O OD1 . ASP A 1 293 ? 7.266   -0.226  42.421  1.00 28.51 ? 286 ASP A OD1 1 
ATOM   2245 O OD2 . ASP A 1 293 ? 6.460   -1.301  40.669  1.00 23.60 ? 286 ASP A OD2 1 
ATOM   2246 N N   . LEU A 1 294 ? 5.199   1.668   38.509  1.00 17.26 ? 287 LEU A N   1 
ATOM   2247 C CA  . LEU A 1 294 ? 5.492   1.492   37.070  1.00 16.17 ? 287 LEU A CA  1 
ATOM   2248 C C   . LEU A 1 294 ? 6.161   2.764   36.548  1.00 16.54 ? 287 LEU A C   1 
ATOM   2249 O O   . LEU A 1 294 ? 7.128   2.653   35.774  1.00 17.00 ? 287 LEU A O   1 
ATOM   2250 C CB  . LEU A 1 294 ? 4.181   1.178   36.358  1.00 16.27 ? 287 LEU A CB  1 
ATOM   2251 C CG  . LEU A 1 294 ? 4.313   1.022   34.834  1.00 15.53 ? 287 LEU A CG  1 
ATOM   2252 C CD1 . LEU A 1 294 ? 5.386   0.033   34.454  1.00 17.05 ? 287 LEU A CD1 1 
ATOM   2253 C CD2 . LEU A 1 294 ? 2.996   0.595   34.267  1.00 17.56 ? 287 LEU A CD2 1 
ATOM   2254 N N   . LEU A 1 295 ? 5.686   3.952   36.905  1.00 16.34 ? 288 LEU A N   1 
ATOM   2255 C CA  . LEU A 1 295 ? 6.332   5.220   36.519  1.00 17.54 ? 288 LEU A CA  1 
ATOM   2256 C C   . LEU A 1 295 ? 7.820   5.183   36.881  1.00 18.29 ? 288 LEU A C   1 
ATOM   2257 O O   . LEU A 1 295 ? 8.674   5.566   36.040  1.00 16.45 ? 288 LEU A O   1 
ATOM   2258 C CB  . LEU A 1 295 ? 5.594   6.380   37.201  1.00 18.10 ? 288 LEU A CB  1 
ATOM   2259 C CG  . LEU A 1 295 ? 6.143   7.762   36.865  1.00 18.13 ? 288 LEU A CG  1 
ATOM   2260 C CD1 . LEU A 1 295 ? 6.076   8.028   35.363  1.00 18.11 ? 288 LEU A CD1 1 
ATOM   2261 C CD2 . LEU A 1 295 ? 5.401   8.828   37.629  1.00 18.71 ? 288 LEU A CD2 1 
ATOM   2262 N N   . ASP A 1 296 ? 8.126   4.735   38.101  1.00 17.25 ? 289 ASP A N   1 
ATOM   2263 C CA  . ASP A 1 296 ? 9.522   4.670   38.586  1.00 19.17 ? 289 ASP A CA  1 
ATOM   2264 C C   . ASP A 1 296 ? 10.355  3.853   37.604  1.00 19.50 ? 289 ASP A C   1 
ATOM   2265 O O   . ASP A 1 296 ? 11.546  4.198   37.332  1.00 19.56 ? 289 ASP A O   1 
ATOM   2266 C CB  . ASP A 1 296 ? 9.569   4.099   39.992  1.00 20.68 ? 289 ASP A CB  1 
ATOM   2267 C CG  . ASP A 1 296 ? 10.976  4.123   40.530  1.00 24.89 ? 289 ASP A CG  1 
ATOM   2268 O OD1 . ASP A 1 296 ? 11.480  5.208   40.668  1.00 23.35 ? 289 ASP A OD1 1 
ATOM   2269 O OD2 . ASP A 1 296 ? 11.568  3.064   40.622  1.00 30.65 ? 289 ASP A OD2 1 
ATOM   2270 N N   . LYS A 1 297 ? 9.823   2.710   37.188  1.00 16.53 ? 290 LYS A N   1 
ATOM   2271 C CA  . LYS A 1 297 ? 10.546  1.744   36.361  1.00 17.18 ? 290 LYS A CA  1 
ATOM   2272 C C   . LYS A 1 297 ? 10.685  2.250   34.925  1.00 16.45 ? 290 LYS A C   1 
ATOM   2273 O O   . LYS A 1 297 ? 11.669  1.886   34.281  1.00 16.23 ? 290 LYS A O   1 
ATOM   2274 C CB  . LYS A 1 297 ? 9.803   0.424   36.456  1.00 17.86 ? 290 LYS A CB  1 
ATOM   2275 C CG  . LYS A 1 297 ? 9.977   -0.232  37.806  1.00 20.24 ? 290 LYS A CG  1 
ATOM   2276 C CD  . LYS A 1 297 ? 9.227   -1.541  37.865  1.00 24.75 ? 290 LYS A CD  1 
ATOM   2277 C CE  . LYS A 1 297 ? 9.681   -2.458  38.985  1.00 28.25 ? 290 LYS A CE  1 
ATOM   2278 N NZ  . LYS A 1 297 ? 9.239   -1.943  40.289  1.00 29.67 ? 290 LYS A NZ  1 
ATOM   2279 N N   . MET A 1 298 ? 9.748   3.071   34.447  1.00 15.19 ? 291 MET A N   1 
ATOM   2280 C CA  . MET A 1 298 ? 9.854   3.656   33.082  1.00 15.83 ? 291 MET A CA  1 
ATOM   2281 C C   . MET A 1 298 ? 10.798  4.860   33.139  1.00 16.66 ? 291 MET A C   1 
ATOM   2282 O O   . MET A 1 298 ? 11.594  5.021   32.214  1.00 19.75 ? 291 MET A O   1 
ATOM   2283 C CB  . MET A 1 298 ? 8.482   4.089   32.571  1.00 15.99 ? 291 MET A CB  1 
ATOM   2284 C CG  . MET A 1 298 ? 7.566   2.917   32.441  1.00 18.29 ? 291 MET A CG  1 
ATOM   2285 S SD  . MET A 1 298 ? 5.997   3.515   31.746  1.00 23.75 ? 291 MET A SD  1 
ATOM   2286 C CE  . MET A 1 298 ? 5.150   2.012   31.330  1.00 28.63 ? 291 MET A CE  1 
ATOM   2287 N N   . LEU A 1 299 ? 10.769  5.661   34.197  1.00 16.93 ? 292 LEU A N   1 
ATOM   2288 C CA  . LEU A 1 299 ? 11.664  6.852   34.312  1.00 17.05 ? 292 LEU A CA  1 
ATOM   2289 C C   . LEU A 1 299 ? 12.907  6.493   35.120  1.00 17.77 ? 292 LEU A C   1 
ATOM   2290 O O   . LEU A 1 299 ? 13.179  7.116   36.157  1.00 19.26 ? 292 LEU A O   1 
ATOM   2291 C CB  . LEU A 1 299 ? 10.888  8.028   34.896  1.00 17.56 ? 292 LEU A CB  1 
ATOM   2292 C CG  . LEU A 1 299 ? 9.742   8.506   34.004  1.00 17.35 ? 292 LEU A CG  1 
ATOM   2293 C CD1 . LEU A 1 299 ? 9.098   9.752   34.589  1.00 18.26 ? 292 LEU A CD1 1 
ATOM   2294 C CD2 . LEU A 1 299 ? 10.190  8.731   32.567  1.00 16.22 ? 292 LEU A CD2 1 
ATOM   2295 N N   . THR A 1 300 ? 13.521  5.396   34.734  1.00 17.33 ? 293 THR A N   1 
ATOM   2296 C CA  . THR A 1 300 ? 14.801  4.927   35.280  1.00 19.01 ? 293 THR A CA  1 
ATOM   2297 C C   . THR A 1 300 ? 15.911  5.583   34.452  1.00 17.56 ? 293 THR A C   1 
ATOM   2298 O O   . THR A 1 300 ? 15.902  5.509   33.209  1.00 15.74 ? 293 THR A O   1 
ATOM   2299 C CB  . THR A 1 300 ? 14.776  3.401   35.313  1.00 21.39 ? 293 THR A CB  1 
ATOM   2300 O OG1 . THR A 1 300 ? 13.926  3.044   36.397  1.00 21.81 ? 293 THR A OG1 1 
ATOM   2301 C CG2 . THR A 1 300 ? 16.129  2.773   35.533  1.00 23.78 ? 293 THR A CG2 1 
ATOM   2302 N N   . PHE A 1 301 ? 16.889  6.184   35.122  1.00 17.88 ? 294 PHE A N   1 
ATOM   2303 C CA  . PHE A 1 301 ? 17.984  6.901   34.429  1.00 18.49 ? 294 PHE A CA  1 
ATOM   2304 C C   . PHE A 1 301 ? 18.759  5.986   33.478  1.00 17.77 ? 294 PHE A C   1 
ATOM   2305 O O   . PHE A 1 301 ? 19.021  6.375   32.293  1.00 18.43 ? 294 PHE A O   1 
ATOM   2306 C CB  . PHE A 1 301 ? 18.934  7.515   35.463  1.00 18.47 ? 294 PHE A CB  1 
ATOM   2307 C CG  . PHE A 1 301 ? 20.069  8.254   34.813  1.00 19.90 ? 294 PHE A CG  1 
ATOM   2308 C CD1 . PHE A 1 301 ? 19.935  9.575   34.424  1.00 20.11 ? 294 PHE A CD1 1 
ATOM   2309 C CD2 . PHE A 1 301 ? 21.271  7.597   34.569  1.00 19.24 ? 294 PHE A CD2 1 
ATOM   2310 C CE1 . PHE A 1 301 ? 21.001  10.229  33.814  1.00 20.86 ? 294 PHE A CE1 1 
ATOM   2311 C CE2 . PHE A 1 301 ? 22.328  8.254   33.958  1.00 20.65 ? 294 PHE A CE2 1 
ATOM   2312 C CZ  . PHE A 1 301 ? 22.186  9.576   33.592  1.00 20.58 ? 294 PHE A CZ  1 
ATOM   2313 N N   . ASN A 1 302 ? 19.197  4.844   33.981  1.00 18.57 ? 295 ASN A N   1 
ATOM   2314 C CA  . ASN A 1 302 ? 20.044  3.896   33.227  1.00 20.82 ? 295 ASN A CA  1 
ATOM   2315 C C   . ASN A 1 302 ? 19.165  3.186   32.205  1.00 18.80 ? 295 ASN A C   1 
ATOM   2316 O O   . ASN A 1 302 ? 18.248  2.482   32.624  1.00 19.70 ? 295 ASN A O   1 
ATOM   2317 C CB  . ASN A 1 302 ? 20.636  2.845   34.150  1.00 21.26 ? 295 ASN A CB  1 
ATOM   2318 C CG  . ASN A 1 302 ? 21.621  1.933   33.442  1.00 28.94 ? 295 ASN A CG  1 
ATOM   2319 O OD1 . ASN A 1 302 ? 21.408  1.508   32.329  1.00 31.07 ? 295 ASN A OD1 1 
ATOM   2320 N ND2 . ASN A 1 302 ? 22.680  1.549   34.136  1.00 32.56 ? 295 ASN A ND2 1 
ATOM   2321 N N   . PRO A 1 303 ? 19.387  3.353   30.887  1.00 18.80 ? 296 PRO A N   1 
ATOM   2322 C CA  . PRO A 1 303 ? 18.491  2.735   29.901  1.00 19.15 ? 296 PRO A CA  1 
ATOM   2323 C C   . PRO A 1 303 ? 18.541  1.210   29.884  1.00 20.77 ? 296 PRO A C   1 
ATOM   2324 O O   . PRO A 1 303 ? 17.579  0.588   29.526  1.00 20.85 ? 296 PRO A O   1 
ATOM   2325 C CB  . PRO A 1 303 ? 18.972  3.261   28.540  1.00 20.41 ? 296 PRO A CB  1 
ATOM   2326 C CG  . PRO A 1 303 ? 20.385  3.735   28.776  1.00 22.19 ? 296 PRO A CG  1 
ATOM   2327 C CD  . PRO A 1 303 ? 20.441  4.170   30.237  1.00 20.65 ? 296 PRO A CD  1 
ATOM   2328 N N   . HIS A 1 304 ? 19.654  0.634   30.349  1.00 20.31 ? 297 HIS A N   1 
ATOM   2329 C CA  . HIS A 1 304 ? 19.784  -0.847  30.476  1.00 24.93 ? 297 HIS A CA  1 
ATOM   2330 C C   . HIS A 1 304 ? 18.848  -1.378  31.574  1.00 26.78 ? 297 HIS A C   1 
ATOM   2331 O O   . HIS A 1 304 ? 18.293  -2.467  31.367  1.00 34.01 ? 297 HIS A O   1 
ATOM   2332 C CB  . HIS A 1 304 ? 21.273  -1.223  30.680  1.00 29.31 ? 297 HIS A CB  1 
ATOM   2333 C CG  . HIS A 1 304 ? 22.174  -0.730  29.586  1.00 36.20 ? 297 HIS A CG  1 
ATOM   2334 N ND1 . HIS A 1 304 ? 23.039  0.348   29.750  1.00 44.03 ? 297 HIS A ND1 1 
ATOM   2335 C CD2 . HIS A 1 304 ? 22.344  -1.141  28.311  1.00 40.21 ? 297 HIS A CD2 1 
ATOM   2336 C CE1 . HIS A 1 304 ? 23.680  0.581   28.625  1.00 40.21 ? 297 HIS A CE1 1 
ATOM   2337 N NE2 . HIS A 1 304 ? 23.271  -0.310  27.727  1.00 44.36 ? 297 HIS A NE2 1 
ATOM   2338 N N   . LYS A 1 305 ? 18.621  -0.630  32.656  1.00 21.75 ? 298 LYS A N   1 
ATOM   2339 C CA  . LYS A 1 305 ? 17.804  -1.038  33.822  1.00 22.98 ? 298 LYS A CA  1 
ATOM   2340 C C   . LYS A 1 305 ? 16.336  -0.653  33.608  1.00 19.81 ? 298 LYS A C   1 
ATOM   2341 O O   . LYS A 1 305 ? 15.492  -1.149  34.306  1.00 20.46 ? 298 LYS A O   1 
ATOM   2342 C CB  . LYS A 1 305 ? 18.280  -0.381  35.118  1.00 24.71 ? 298 LYS A CB  1 
ATOM   2343 C CG  . LYS A 1 305 ? 19.637  -0.864  35.639  1.00 31.11 ? 298 LYS A CG  1 
ATOM   2344 C CD  . LYS A 1 305 ? 20.030  -0.139  36.930  1.00 35.43 ? 298 LYS A CD  1 
ATOM   2345 C CE  . LYS A 1 305 ? 21.481  -0.348  37.345  1.00 41.50 ? 298 LYS A CE  1 
ATOM   2346 N NZ  . LYS A 1 305 ? 21.963  0.769   38.201  1.00 42.49 ? 298 LYS A NZ  1 
ATOM   2347 N N   . ARG A 1 306 ? 16.085  0.229   32.667  1.00 17.56 ? 299 ARG A N   1 
ATOM   2348 C CA  . ARG A 1 306 ? 14.715  0.686   32.334  1.00 16.77 ? 299 ARG A CA  1 
ATOM   2349 C C   . ARG A 1 306 ? 13.848  -0.519  31.959  1.00 18.12 ? 299 ARG A C   1 
ATOM   2350 O O   . ARG A 1 306 ? 14.272  -1.366  31.192  1.00 17.77 ? 299 ARG A O   1 
ATOM   2351 C CB  . ARG A 1 306 ? 14.773  1.743   31.230  1.00 16.59 ? 299 ARG A CB  1 
ATOM   2352 C CG  . ARG A 1 306 ? 13.552  2.643   31.125  1.00 18.05 ? 299 ARG A CG  1 
ATOM   2353 C CD  . ARG A 1 306 ? 13.747  3.779   30.138  1.00 17.01 ? 299 ARG A CD  1 
ATOM   2354 N NE  . ARG A 1 306 ? 14.857  4.610   30.573  1.00 15.78 ? 299 ARG A NE  1 
ATOM   2355 C CZ  . ARG A 1 306 ? 15.697  5.279   29.785  1.00 14.38 ? 299 ARG A CZ  1 
ATOM   2356 N NH1 . ARG A 1 306 ? 15.562  5.283   28.465  1.00 14.33 ? 299 ARG A NH1 1 
ATOM   2357 N NH2 . ARG A 1 306 ? 16.700  5.938   30.342  1.00 15.48 ? 299 ARG A NH2 1 
ATOM   2358 N N   . ILE A 1 307 ? 12.603  -0.481  32.389  1.00 16.96 ? 300 ILE A N   1 
ATOM   2359 C CA  . ILE A 1 307 ? 11.615  -1.548  32.076  1.00 16.90 ? 300 ILE A CA  1 
ATOM   2360 C C   . ILE A 1 307 ? 11.416  -1.634  30.559  1.00 16.44 ? 300 ILE A C   1 
ATOM   2361 O O   . ILE A 1 307 ? 11.413  -0.607  29.874  1.00 15.78 ? 300 ILE A O   1 
ATOM   2362 C CB  . ILE A 1 307 ? 10.305  -1.334  32.859  1.00 15.76 ? 300 ILE A CB  1 
ATOM   2363 C CG1 . ILE A 1 307 ? 9.467   -2.618  32.857  1.00 17.44 ? 300 ILE A CG1 1 
ATOM   2364 C CG2 . ILE A 1 307 ? 9.541   -0.121  32.374  1.00 18.08 ? 300 ILE A CG2 1 
ATOM   2365 C CD1 . ILE A 1 307 ? 8.415   -2.658  33.923  1.00 17.85 ? 300 ILE A CD1 1 
ATOM   2366 N N   . GLU A 1 308 ? 11.260  -2.857  30.057  1.00 16.89 ? 301 GLU A N   1 
ATOM   2367 C CA  . GLU A 1 308 ? 10.931  -3.141  28.653  1.00 18.79 ? 301 GLU A CA  1 
ATOM   2368 C C   . GLU A 1 308 ? 9.419   -3.065  28.475  1.00 16.02 ? 301 GLU A C   1 
ATOM   2369 O O   . GLU A 1 308 ? 8.695   -3.208  29.471  1.00 15.61 ? 301 GLU A O   1 
ATOM   2370 C CB  . GLU A 1 308 ? 11.362  -4.561  28.289  1.00 23.60 ? 301 GLU A CB  1 
ATOM   2371 C CG  . GLU A 1 308 ? 12.763  -4.869  28.781  1.00 31.54 ? 301 GLU A CG  1 
ATOM   2372 C CD  . GLU A 1 308 ? 13.766  -4.215  27.870  1.00 34.20 ? 301 GLU A CD  1 
ATOM   2373 O OE1 . GLU A 1 308 ? 13.447  -4.088  26.685  1.00 36.89 ? 301 GLU A OE1 1 
ATOM   2374 O OE2 . GLU A 1 308 ? 14.885  -3.883  28.339  1.00 44.75 ? 301 GLU A OE2 1 
ATOM   2375 N N   . VAL A 1 309 ? 8.992   -2.919  27.239  1.00 16.60 ? 302 VAL A N   1 
ATOM   2376 C CA  . VAL A 1 309 ? 7.531   -2.738  26.976  1.00 16.24 ? 302 VAL A CA  1 
ATOM   2377 C C   . VAL A 1 309 ? 6.730   -3.926  27.548  1.00 17.37 ? 302 VAL A C   1 
ATOM   2378 O O   . VAL A 1 309 ? 5.686   -3.662  28.210  1.00 18.45 ? 302 VAL A O   1 
ATOM   2379 C CB  . VAL A 1 309 ? 7.256   -2.470  25.491  1.00 17.91 ? 302 VAL A CB  1 
ATOM   2380 C CG1 . VAL A 1 309 ? 7.634   -3.623  24.560  1.00 20.86 ? 302 VAL A CG1 1 
ATOM   2381 C CG2 . VAL A 1 309 ? 5.770   -2.093  25.278  1.00 17.68 ? 302 VAL A CG2 1 
ATOM   2382 N N   . GLU A 1 310 ? 7.223   -5.145  27.365  1.00 17.49 ? 303 GLU A N   1 
ATOM   2383 C CA  . GLU A 1 310 ? 6.464   -6.363  27.733  1.00 20.84 ? 303 GLU A CA  1 
ATOM   2384 C C   . GLU A 1 310 ? 6.437   -6.488  29.251  1.00 20.07 ? 303 GLU A C   1 
ATOM   2385 O O   . GLU A 1 310 ? 5.421   -6.892  29.793  1.00 17.36 ? 303 GLU A O   1 
ATOM   2386 C CB  . GLU A 1 310 ? 6.999   -7.564  26.987  1.00 26.02 ? 303 GLU A CB  1 
ATOM   2387 C CG  . GLU A 1 310 ? 6.377   -7.613  25.595  1.00 33.46 ? 303 GLU A CG  1 
ATOM   2388 C CD  . GLU A 1 310 ? 7.152   -8.224  24.437  1.00 42.23 ? 303 GLU A CD  1 
ATOM   2389 O OE1 . GLU A 1 310 ? 7.056   -9.471  24.244  1.00 44.36 ? 303 GLU A OE1 1 
ATOM   2390 O OE2 . GLU A 1 310 ? 7.802   -7.443  23.680  1.00 41.74 ? 303 GLU A OE2 1 
ATOM   2391 N N   . GLN A 1 311 ? 7.502   -6.045  29.917  1.00 18.49 ? 304 GLN A N   1 
ATOM   2392 C CA  . GLN A 1 311 ? 7.511   -5.995  31.390  1.00 18.66 ? 304 GLN A CA  1 
ATOM   2393 C C   . GLN A 1 311 ? 6.500   -4.989  31.910  1.00 18.19 ? 304 GLN A C   1 
ATOM   2394 O O   . GLN A 1 311 ? 5.844   -5.217  32.969  1.00 19.17 ? 304 GLN A O   1 
ATOM   2395 C CB  . GLN A 1 311 ? 8.902   -5.674  31.904  1.00 19.82 ? 304 GLN A CB  1 
ATOM   2396 C CG  . GLN A 1 311 ? 9.838   -6.839  31.725  1.00 21.71 ? 304 GLN A CG  1 
ATOM   2397 C CD  . GLN A 1 311 ? 11.242  -6.445  32.112  1.00 23.26 ? 304 GLN A CD  1 
ATOM   2398 O OE1 . GLN A 1 311 ? 11.715  -5.353  31.796  1.00 22.35 ? 304 GLN A OE1 1 
ATOM   2399 N NE2 . GLN A 1 311 ? 11.950  -7.392  32.696  1.00 26.12 ? 304 GLN A NE2 1 
ATOM   2400 N N   . ALA A 1 312 ? 6.369   -3.861  31.218  1.00 15.95 ? 305 ALA A N   1 
ATOM   2401 C CA  . ALA A 1 312 ? 5.437   -2.821  31.631  1.00 16.34 ? 305 ALA A CA  1 
ATOM   2402 C C   . ALA A 1 312 ? 4.016   -3.372  31.506  1.00 15.03 ? 305 ALA A C   1 
ATOM   2403 O O   . ALA A 1 312 ? 3.204   -3.097  32.386  1.00 14.05 ? 305 ALA A O   1 
ATOM   2404 C CB  . ALA A 1 312 ? 5.661   -1.598  30.806  1.00 16.44 ? 305 ALA A CB  1 
ATOM   2405 N N   . LEU A 1 313 ? 3.709   -4.031  30.394  1.00 15.57 ? 306 LEU A N   1 
ATOM   2406 C CA  . LEU A 1 313 ? 2.356   -4.585  30.162  1.00 14.75 ? 306 LEU A CA  1 
ATOM   2407 C C   . LEU A 1 313 ? 2.014   -5.590  31.252  1.00 16.64 ? 306 LEU A C   1 
ATOM   2408 O O   . LEU A 1 313 ? 0.847   -5.635  31.664  1.00 16.53 ? 306 LEU A O   1 
ATOM   2409 C CB  . LEU A 1 313 ? 2.306   -5.241  28.800  1.00 15.65 ? 306 LEU A CB  1 
ATOM   2410 C CG  . LEU A 1 313 ? 2.131   -4.281  27.638  1.00 15.97 ? 306 LEU A CG  1 
ATOM   2411 C CD1 . LEU A 1 313 ? 2.499   -4.991  26.374  1.00 16.27 ? 306 LEU A CD1 1 
ATOM   2412 C CD2 . LEU A 1 313 ? 0.699   -3.760  27.583  1.00 16.81 ? 306 LEU A CD2 1 
ATOM   2413 N N   . ALA A 1 314 ? 3.024   -6.273  31.767  1.00 17.89 ? 307 ALA A N   1 
ATOM   2414 C CA  . ALA A 1 314 ? 2.886   -7.331  32.806  1.00 19.25 ? 307 ALA A CA  1 
ATOM   2415 C C   . ALA A 1 314 ? 2.864   -6.732  34.217  1.00 19.87 ? 307 ALA A C   1 
ATOM   2416 O O   . ALA A 1 314 ? 2.694   -7.489  35.226  1.00 20.48 ? 307 ALA A O   1 
ATOM   2417 C CB  . ALA A 1 314 ? 4.006   -8.340  32.632  1.00 17.87 ? 307 ALA A CB  1 
ATOM   2418 N N   . HIS A 1 315 ? 3.015   -5.420  34.363  1.00 18.36 ? 308 HIS A N   1 
ATOM   2419 C CA  . HIS A 1 315 ? 3.080   -4.788  35.703  1.00 19.29 ? 308 HIS A CA  1 
ATOM   2420 C C   . HIS A 1 315 ? 1.700   -4.849  36.358  1.00 19.20 ? 308 HIS A C   1 
ATOM   2421 O O   . HIS A 1 315 ? 0.660   -4.650  35.734  1.00 17.45 ? 308 HIS A O   1 
ATOM   2422 C CB  . HIS A 1 315 ? 3.549   -3.344  35.550  1.00 17.72 ? 308 HIS A CB  1 
ATOM   2423 C CG  . HIS A 1 315 ? 3.812   -2.704  36.847  1.00 17.57 ? 308 HIS A CG  1 
ATOM   2424 N ND1 . HIS A 1 315 ? 2.814   -2.144  37.601  1.00 18.68 ? 308 HIS A ND1 1 
ATOM   2425 C CD2 . HIS A 1 315 ? 4.955   -2.536  37.533  1.00 18.18 ? 308 HIS A CD2 1 
ATOM   2426 C CE1 . HIS A 1 315 ? 3.333   -1.643  38.692  1.00 18.45 ? 308 HIS A CE1 1 
ATOM   2427 N NE2 . HIS A 1 315 ? 4.649   -1.851  38.669  1.00 17.83 ? 308 HIS A NE2 1 
ATOM   2428 N N   . PRO A 1 316 ? 1.642   -5.033  37.690  1.00 20.31 ? 309 PRO A N   1 
ATOM   2429 C CA  . PRO A 1 316 ? 0.358   -5.035  38.398  1.00 20.93 ? 309 PRO A CA  1 
ATOM   2430 C C   . PRO A 1 316 ? -0.601  -3.881  38.111  1.00 20.17 ? 309 PRO A C   1 
ATOM   2431 O O   . PRO A 1 316 ? -1.800  -4.093  38.146  1.00 20.28 ? 309 PRO A O   1 
ATOM   2432 C CB  . PRO A 1 316 ? 0.849   -5.021  39.854  1.00 21.16 ? 309 PRO A CB  1 
ATOM   2433 C CG  . PRO A 1 316 ? 2.055   -5.880  39.789  1.00 21.87 ? 309 PRO A CG  1 
ATOM   2434 C CD  . PRO A 1 316 ? 2.780   -5.334  38.568  1.00 21.94 ? 309 PRO A CD  1 
ATOM   2435 N N   . TYR A 1 317 ? -0.104  -2.701  37.733  1.00 19.38 ? 310 TYR A N   1 
ATOM   2436 C CA  . TYR A 1 317 ? -0.951  -1.539  37.468  1.00 19.10 ? 310 TYR A CA  1 
ATOM   2437 C C   . TYR A 1 317 ? -1.908  -1.893  36.326  1.00 16.53 ? 310 TYR A C   1 
ATOM   2438 O O   . TYR A 1 317 ? -3.031  -1.403  36.357  1.00 17.54 ? 310 TYR A O   1 
ATOM   2439 C CB  . TYR A 1 317 ? -0.120  -0.290  37.146  1.00 17.51 ? 310 TYR A CB  1 
ATOM   2440 C CG  . TYR A 1 317 ? -0.973  0.912   36.910  1.00 19.32 ? 310 TYR A CG  1 
ATOM   2441 C CD1 . TYR A 1 317 ? -1.950  1.313   37.817  1.00 19.10 ? 310 TYR A CD1 1 
ATOM   2442 C CD2 . TYR A 1 317 ? -0.872  1.621   35.730  1.00 18.48 ? 310 TYR A CD2 1 
ATOM   2443 C CE1 . TYR A 1 317 ? -2.770  2.391   37.560  1.00 19.73 ? 310 TYR A CE1 1 
ATOM   2444 C CE2 . TYR A 1 317 ? -1.625  2.755   35.501  1.00 20.57 ? 310 TYR A CE2 1 
ATOM   2445 C CZ  . TYR A 1 317 ? -2.606  3.123   36.395  1.00 21.55 ? 310 TYR A CZ  1 
ATOM   2446 O OH  . TYR A 1 317 ? -3.370  4.220   36.161  1.00 22.23 ? 310 TYR A OH  1 
ATOM   2447 N N   . LEU A 1 318 ? -1.446  -2.747  35.400  1.00 18.28 ? 311 LEU A N   1 
ATOM   2448 C CA  . LEU A 1 318 ? -2.177  -3.019  34.145  1.00 17.13 ? 311 LEU A CA  1 
ATOM   2449 C C   . LEU A 1 318 ? -2.857  -4.390  34.189  1.00 19.23 ? 311 LEU A C   1 
ATOM   2450 O O   . LEU A 1 318 ? -3.291  -4.879  33.130  1.00 18.67 ? 311 LEU A O   1 
ATOM   2451 C CB  . LEU A 1 318 ? -1.216  -2.918  32.965  1.00 16.92 ? 311 LEU A CB  1 
ATOM   2452 C CG  . LEU A 1 318 ? -0.693  -1.502  32.763  1.00 16.73 ? 311 LEU A CG  1 
ATOM   2453 C CD1 . LEU A 1 318 ? 0.305   -1.427  31.647  1.00 17.46 ? 311 LEU A CD1 1 
ATOM   2454 C CD2 . LEU A 1 318 ? -1.817  -0.500  32.560  1.00 18.34 ? 311 LEU A CD2 1 
ATOM   2455 N N   . GLU A 1 319 ? -3.001  -4.983  35.374  1.00 19.39 ? 312 GLU A N   1 
ATOM   2456 C CA  . GLU A 1 319 ? -3.470  -6.385  35.496  1.00 22.16 ? 312 GLU A CA  1 
ATOM   2457 C C   . GLU A 1 319 ? -4.906  -6.536  34.993  1.00 20.44 ? 312 GLU A C   1 
ATOM   2458 O O   . GLU A 1 319 ? -5.216  -7.609  34.444  1.00 20.55 ? 312 GLU A O   1 
ATOM   2459 C CB  . GLU A 1 319 ? -3.313  -6.907  36.927  1.00 25.67 ? 312 GLU A CB  1 
ATOM   2460 C CG  . GLU A 1 319 ? -4.021  -6.105  37.983  1.00 33.51 ? 312 GLU A CG  1 
ATOM   2461 C CD  . GLU A 1 319 ? -3.533  -6.532  39.364  1.00 39.35 ? 312 GLU A CD  1 
ATOM   2462 O OE1 . GLU A 1 319 ? -3.333  -7.754  39.534  1.00 44.55 ? 312 GLU A OE1 1 
ATOM   2463 O OE2 . GLU A 1 319 ? -3.261  -5.643  40.218  1.00 44.67 ? 312 GLU A OE2 1 
ATOM   2464 N N   . GLN A 1 320 ? -5.708  -5.482  34.981  1.00 21.60 ? 313 GLN A N   1 
ATOM   2465 C CA  . GLN A 1 320 ? -7.110  -5.618  34.493  1.00 23.48 ? 313 GLN A CA  1 
ATOM   2466 C C   . GLN A 1 320 ? -7.123  -5.893  32.998  1.00 22.45 ? 313 GLN A C   1 
ATOM   2467 O O   . GLN A 1 320 ? -8.091  -6.447  32.524  1.00 23.80 ? 313 GLN A O   1 
ATOM   2468 C CB  . GLN A 1 320 ? -7.899  -4.356  34.750  1.00 26.03 ? 313 GLN A CB  1 
ATOM   2469 C CG  . GLN A 1 320 ? -8.066  -4.116  36.234  1.00 32.17 ? 313 GLN A CG  1 
ATOM   2470 C CD  . GLN A 1 320 ? -8.563  -2.711  36.431  1.00 38.50 ? 313 GLN A CD  1 
ATOM   2471 O OE1 . GLN A 1 320 ? -7.835  -1.720  36.244  1.00 33.21 ? 313 GLN A OE1 1 
ATOM   2472 N NE2 . GLN A 1 320 ? -9.842  -2.635  36.769  1.00 41.61 ? 313 GLN A NE2 1 
ATOM   2473 N N   . TYR A 1 321 ? -6.102  -5.436  32.277  1.00 18.22 ? 314 TYR A N   1 
ATOM   2474 C CA  . TYR A 1 321 ? -6.035  -5.432  30.796  1.00 17.66 ? 314 TYR A CA  1 
ATOM   2475 C C   . TYR A 1 321 ? -5.056  -6.453  30.215  1.00 17.58 ? 314 TYR A C   1 
ATOM   2476 O O   . TYR A 1 321 ? -5.281  -6.963  29.092  1.00 16.48 ? 314 TYR A O   1 
ATOM   2477 C CB  . TYR A 1 321 ? -5.634  -4.053  30.290  1.00 19.41 ? 314 TYR A CB  1 
ATOM   2478 C CG  . TYR A 1 321 ? -6.658  -3.011  30.595  1.00 18.01 ? 314 TYR A CG  1 
ATOM   2479 C CD1 . TYR A 1 321 ? -7.915  -3.079  29.997  1.00 24.50 ? 314 TYR A CD1 1 
ATOM   2480 C CD2 . TYR A 1 321 ? -6.429  -2.041  31.533  1.00 19.91 ? 314 TYR A CD2 1 
ATOM   2481 C CE1 . TYR A 1 321 ? -8.905  -2.161  30.307  1.00 23.84 ? 314 TYR A CE1 1 
ATOM   2482 C CE2 . TYR A 1 321 ? -7.422  -1.132  31.875  1.00 22.87 ? 314 TYR A CE2 1 
ATOM   2483 C CZ  . TYR A 1 321 ? -8.649  -1.183  31.237  1.00 26.56 ? 314 TYR A CZ  1 
ATOM   2484 O OH  . TYR A 1 321 ? -9.619  -0.272  31.546  1.00 30.53 ? 314 TYR A OH  1 
ATOM   2485 N N   . TYR A 1 322 ? -3.994  -6.774  30.946  1.00 18.57 ? 315 TYR A N   1 
ATOM   2486 C CA  . TYR A 1 322 ? -2.868  -7.589  30.444  1.00 16.94 ? 315 TYR A CA  1 
ATOM   2487 C C   . TYR A 1 322 ? -3.341  -8.954  29.950  1.00 18.26 ? 315 TYR A C   1 
ATOM   2488 O O   . TYR A 1 322 ? -4.049  -9.677  30.673  1.00 20.37 ? 315 TYR A O   1 
ATOM   2489 C CB  . TYR A 1 322 ? -1.849  -7.768  31.556  1.00 18.66 ? 315 TYR A CB  1 
ATOM   2490 C CG  . TYR A 1 322 ? -0.646  -8.556  31.162  1.00 20.24 ? 315 TYR A CG  1 
ATOM   2491 C CD1 . TYR A 1 322 ? 0.029   -8.285  29.987  1.00 19.06 ? 315 TYR A CD1 1 
ATOM   2492 C CD2 . TYR A 1 322 ? -0.170  -9.576  31.970  1.00 22.63 ? 315 TYR A CD2 1 
ATOM   2493 C CE1 . TYR A 1 322 ? 1.185   -8.968  29.662  1.00 22.26 ? 315 TYR A CE1 1 
ATOM   2494 C CE2 . TYR A 1 322 ? 0.956   -10.292 31.637  1.00 22.50 ? 315 TYR A CE2 1 
ATOM   2495 C CZ  . TYR A 1 322 ? 1.641   -9.985  30.483  1.00 22.55 ? 315 TYR A CZ  1 
ATOM   2496 O OH  . TYR A 1 322 ? 2.779   -10.679 30.181  1.00 22.82 ? 315 TYR A OH  1 
ATOM   2497 N N   . ASP A 1 323 ? -3.013  -9.280  28.711  1.00 17.94 ? 316 ASP A N   1 
ATOM   2498 C CA  . ASP A 1 323 ? -3.416  -10.527 28.038  1.00 19.65 ? 316 ASP A CA  1 
ATOM   2499 C C   . ASP A 1 323 ? -2.482  -10.698 26.848  1.00 18.04 ? 316 ASP A C   1 
ATOM   2500 O O   . ASP A 1 323 ? -2.751  -10.179 25.768  1.00 17.67 ? 316 ASP A O   1 
ATOM   2501 C CB  . ASP A 1 323 ? -4.854  -10.486 27.550  1.00 19.90 ? 316 ASP A CB  1 
ATOM   2502 C CG  . ASP A 1 323 ? -5.273  -11.789 26.888  1.00 21.85 ? 316 ASP A CG  1 
ATOM   2503 O OD1 . ASP A 1 323 ? -4.407  -12.667 26.753  1.00 26.00 ? 316 ASP A OD1 1 
ATOM   2504 O OD2 . ASP A 1 323 ? -6.397  -11.842 26.407  1.00 25.47 ? 316 ASP A OD2 1 
ATOM   2505 N N   . PRO A 1 324 ? -1.315  -11.339 27.037  1.00 18.47 ? 317 PRO A N   1 
ATOM   2506 C CA  . PRO A 1 324 ? -0.304  -11.345 25.984  1.00 20.96 ? 317 PRO A CA  1 
ATOM   2507 C C   . PRO A 1 324 ? -0.812  -11.990 24.695  1.00 20.40 ? 317 PRO A C   1 
ATOM   2508 O O   . PRO A 1 324 ? -0.328  -11.599 23.678  1.00 22.02 ? 317 PRO A O   1 
ATOM   2509 C CB  . PRO A 1 324 ? 0.903   -12.108 26.558  1.00 20.10 ? 317 PRO A CB  1 
ATOM   2510 C CG  . PRO A 1 324 ? 0.644   -12.193 28.029  1.00 20.72 ? 317 PRO A CG  1 
ATOM   2511 C CD  . PRO A 1 324 ? -0.819  -11.924 28.300  1.00 19.17 ? 317 PRO A CD  1 
ATOM   2512 N N   . SER A 1 325 ? -1.813  -12.856 24.750  1.00 19.74 ? 318 SER A N   1 
ATOM   2513 C CA  A SER A 1 325 ? -2.440  -13.503 23.564  0.50 20.95 ? 318 SER A CA  1 
ATOM   2514 C CA  B SER A 1 325 ? -2.418  -13.491 23.550  0.50 23.13 ? 318 SER A CA  1 
ATOM   2515 C C   . SER A 1 325 ? -3.240  -12.473 22.753  1.00 21.77 ? 318 SER A C   1 
ATOM   2516 O O   . SER A 1 325 ? -3.526  -12.745 21.562  1.00 23.88 ? 318 SER A O   1 
ATOM   2517 C CB  A SER A 1 325 ? -3.284  -14.702 23.957  0.50 19.98 ? 318 SER A CB  1 
ATOM   2518 C CB  B SER A 1 325 ? -3.235  -14.670 23.943  0.50 24.61 ? 318 SER A CB  1 
ATOM   2519 O OG  A SER A 1 325 ? -4.556  -14.341 24.489  0.50 16.93 ? 318 SER A OG  1 
ATOM   2520 O OG  B SER A 1 325 ? -2.399  -15.628 24.566  0.50 27.89 ? 318 SER A OG  1 
ATOM   2521 N N   . ASP A 1 326 ? -3.574  -11.337 23.379  1.00 18.63 ? 319 ASP A N   1 
ATOM   2522 C CA  . ASP A 1 326 ? -4.345  -10.247 22.746  1.00 19.13 ? 319 ASP A CA  1 
ATOM   2523 C C   . ASP A 1 326 ? -3.455  -9.013  22.579  1.00 16.40 ? 319 ASP A C   1 
ATOM   2524 O O   . ASP A 1 326 ? -3.992  -7.910  22.453  1.00 17.38 ? 319 ASP A O   1 
ATOM   2525 C CB  . ASP A 1 326 ? -5.568  -9.907  23.586  1.00 19.82 ? 319 ASP A CB  1 
ATOM   2526 C CG  . ASP A 1 326 ? -6.554  -9.008  22.873  1.00 22.82 ? 319 ASP A CG  1 
ATOM   2527 O OD1 . ASP A 1 326 ? -6.732  -9.180  21.651  1.00 24.01 ? 319 ASP A OD1 1 
ATOM   2528 O OD2 . ASP A 1 326 ? -7.047  -8.074  23.545  1.00 24.94 ? 319 ASP A OD2 1 
ATOM   2529 N N   . GLU A 1 327 ? -2.140  -9.206  22.548  1.00 18.40 ? 320 GLU A N   1 
ATOM   2530 C CA  . GLU A 1 327 ? -1.138  -8.109  22.479  1.00 17.51 ? 320 GLU A CA  1 
ATOM   2531 C C   . GLU A 1 327 ? -0.216  -8.515  21.342  1.00 19.54 ? 320 GLU A C   1 
ATOM   2532 O O   . GLU A 1 327 ? 0.865   -9.064  21.561  1.00 19.34 ? 320 GLU A O   1 
ATOM   2533 C CB  . GLU A 1 327 ? -0.449  -7.907  23.811  1.00 20.18 ? 320 GLU A CB  1 
ATOM   2534 C CG  . GLU A 1 327 ? -1.369  -7.276  24.846  1.00 18.53 ? 320 GLU A CG  1 
ATOM   2535 C CD  . GLU A 1 327 ? -0.969  -7.506  26.276  1.00 19.66 ? 320 GLU A CD  1 
ATOM   2536 O OE1 . GLU A 1 327 ? 0.210   -7.992  26.526  1.00 21.16 ? 320 GLU A OE1 1 
ATOM   2537 O OE2 . GLU A 1 327 ? -1.800  -7.203  27.107  1.00 17.01 ? 320 GLU A OE2 1 
ATOM   2538 N N   . PRO A 1 328 ? -0.699  -8.370  20.113  1.00 17.76 ? 321 PRO A N   1 
ATOM   2539 C CA  . PRO A 1 328 ? 0.014   -8.958  18.994  1.00 19.33 ? 321 PRO A CA  1 
ATOM   2540 C C   . PRO A 1 328 ? 1.371   -8.321  18.686  1.00 18.45 ? 321 PRO A C   1 
ATOM   2541 O O   . PRO A 1 328 ? 1.631   -7.151  18.968  1.00 16.22 ? 321 PRO A O   1 
ATOM   2542 C CB  . PRO A 1 328 ? -0.917  -8.784  17.785  1.00 21.23 ? 321 PRO A CB  1 
ATOM   2543 C CG  . PRO A 1 328 ? -2.043  -7.888  18.242  1.00 23.55 ? 321 PRO A CG  1 
ATOM   2544 C CD  . PRO A 1 328 ? -1.977  -7.750  19.744  1.00 19.90 ? 321 PRO A CD  1 
ATOM   2545 N N   . ILE A 1 329 ? 2.212   -9.114  18.020  1.00 17.79 ? 322 ILE A N   1 
ATOM   2546 C CA  . ILE A 1 329 ? 3.515   -8.643  17.494  1.00 15.47 ? 322 ILE A CA  1 
ATOM   2547 C C   . ILE A 1 329 ? 3.467   -8.707  15.974  1.00 15.82 ? 322 ILE A C   1 
ATOM   2548 O O   . ILE A 1 329 ? 2.541   -9.316  15.397  1.00 18.45 ? 322 ILE A O   1 
ATOM   2549 C CB  . ILE A 1 329 ? 4.662   -9.458  18.075  1.00 16.99 ? 322 ILE A CB  1 
ATOM   2550 C CG1 . ILE A 1 329 ? 4.649   -10.931 17.663  1.00 18.36 ? 322 ILE A CG1 1 
ATOM   2551 C CG2 . ILE A 1 329 ? 4.699   -9.280  19.597  1.00 19.41 ? 322 ILE A CG2 1 
ATOM   2552 C CD1 . ILE A 1 329 ? 5.920   -11.669 18.029  1.00 20.72 ? 322 ILE A CD1 1 
ATOM   2553 N N   . ALA A 1 330 ? 4.433   -8.051  15.371  1.00 16.02 ? 323 ALA A N   1 
ATOM   2554 C CA  . ALA A 1 330 ? 4.439   -7.737  13.936  1.00 17.44 ? 323 ALA A CA  1 
ATOM   2555 C C   . ALA A 1 330 ? 4.821   -9.002  13.169  1.00 20.54 ? 323 ALA A C   1 
ATOM   2556 O O   . ALA A 1 330 ? 5.715   -9.714  13.595  1.00 18.25 ? 323 ALA A O   1 
ATOM   2557 C CB  . ALA A 1 330 ? 5.417   -6.636  13.716  1.00 16.47 ? 323 ALA A CB  1 
ATOM   2558 N N   . GLU A 1 331 ? 4.105   -9.271  12.088  1.00 22.54 ? 324 GLU A N   1 
ATOM   2559 C CA  . GLU A 1 331 ? 4.397   -10.437 11.227  1.00 25.98 ? 324 GLU A CA  1 
ATOM   2560 C C   . GLU A 1 331 ? 5.696   -10.164 10.488  1.00 29.03 ? 324 GLU A C   1 
ATOM   2561 O O   . GLU A 1 331 ? 6.476   -11.118 10.308  1.00 33.17 ? 324 GLU A O   1 
ATOM   2562 C CB  . GLU A 1 331 ? 3.233   -10.668 10.256  1.00 28.71 ? 324 GLU A CB  1 
ATOM   2563 C CG  . GLU A 1 331 ? 2.020   -11.272 10.952  1.00 35.79 ? 324 GLU A CG  1 
ATOM   2564 C CD  . GLU A 1 331 ? 0.679   -11.215 10.236  1.00 42.69 ? 324 GLU A CD  1 
ATOM   2565 O OE1 . GLU A 1 331 ? 0.632   -10.687 9.104   1.00 48.43 ? 324 GLU A OE1 1 
ATOM   2566 O OE2 . GLU A 1 331 ? -0.314  -11.728 10.806  1.00 42.46 ? 324 GLU A OE2 1 
ATOM   2567 N N   . ALA A 1 332 ? 5.917   -8.903  10.107  1.00 26.81 ? 325 ALA A N   1 
ATOM   2568 C CA  . ALA A 1 332 ? 6.966   -8.515  9.122   1.00 25.19 ? 325 ALA A CA  1 
ATOM   2569 C C   . ALA A 1 332 ? 7.796   -7.375  9.685   1.00 23.99 ? 325 ALA A C   1 
ATOM   2570 O O   . ALA A 1 332 ? 7.643   -6.249  9.244   1.00 26.73 ? 325 ALA A O   1 
ATOM   2571 C CB  . ALA A 1 332 ? 6.332   -8.170  7.798   1.00 25.60 ? 325 ALA A CB  1 
ATOM   2572 N N   . PRO A 1 333 ? 8.715   -7.665  10.639  1.00 22.35 ? 326 PRO A N   1 
ATOM   2573 C CA  . PRO A 1 333 ? 9.689   -6.682  11.105  1.00 24.72 ? 326 PRO A CA  1 
ATOM   2574 C C   . PRO A 1 333 ? 10.622  -6.080  10.051  1.00 24.94 ? 326 PRO A C   1 
ATOM   2575 O O   . PRO A 1 333 ? 10.931  -6.713  9.040   1.00 25.26 ? 326 PRO A O   1 
ATOM   2576 C CB  . PRO A 1 333 ? 10.604  -7.440  12.072  1.00 26.11 ? 326 PRO A CB  1 
ATOM   2577 C CG  . PRO A 1 333 ? 9.805   -8.639  12.454  1.00 28.73 ? 326 PRO A CG  1 
ATOM   2578 C CD  . PRO A 1 333 ? 8.956   -8.981  11.235  1.00 25.47 ? 326 PRO A CD  1 
ATOM   2579 N N   . PHE A 1 334 ? 11.018  -4.844  10.277  1.00 21.85 ? 327 PHE A N   1 
ATOM   2580 C CA  . PHE A 1 334 ? 12.028  -4.160  9.437   1.00 26.37 ? 327 PHE A CA  1 
ATOM   2581 C C   . PHE A 1 334 ? 13.378  -4.644  9.942   1.00 30.31 ? 327 PHE A C   1 
ATOM   2582 O O   . PHE A 1 334 ? 13.850  -4.126  10.985  1.00 34.54 ? 327 PHE A O   1 
ATOM   2583 C CB  . PHE A 1 334 ? 11.908  -2.640  9.481   1.00 26.35 ? 327 PHE A CB  1 
ATOM   2584 C CG  . PHE A 1 334 ? 10.692  -2.069  8.806   1.00 28.47 ? 327 PHE A CG  1 
ATOM   2585 C CD1 . PHE A 1 334 ? 9.485   -1.981  9.477   1.00 26.55 ? 327 PHE A CD1 1 
ATOM   2586 C CD2 . PHE A 1 334 ? 10.753  -1.621  7.498   1.00 28.86 ? 327 PHE A CD2 1 
ATOM   2587 C CE1 . PHE A 1 334 ? 8.361   -1.459  8.866   1.00 29.23 ? 327 PHE A CE1 1 
ATOM   2588 C CE2 . PHE A 1 334 ? 9.618   -1.103  6.880   1.00 28.49 ? 327 PHE A CE2 1 
ATOM   2589 C CZ  . PHE A 1 334 ? 8.433   -1.022  7.564   1.00 29.94 ? 327 PHE A CZ  1 
ATOM   2590 N N   . LYS A 1 335 ? 13.964  -5.615  9.238   1.00 32.75 ? 328 LYS A N   1 
ATOM   2591 C CA  . LYS A 1 335 ? 15.217  -6.293  9.659   1.00 41.13 ? 328 LYS A CA  1 
ATOM   2592 C C   . LYS A 1 335 ? 16.400  -5.352  9.391   1.00 40.70 ? 328 LYS A C   1 
ATOM   2593 O O   . LYS A 1 335 ? 17.386  -5.421  10.133  1.00 43.05 ? 328 LYS A O   1 
ATOM   2594 C CB  . LYS A 1 335 ? 15.324  -7.651  8.944   1.00 49.20 ? 328 LYS A CB  1 
ATOM   2595 C CG  . LYS A 1 335 ? 16.017  -8.775  9.717   1.00 57.27 ? 328 LYS A CG  1 
ATOM   2596 C CD  . LYS A 1 335 ? 15.216  -9.423  10.856  1.00 57.86 ? 328 LYS A CD  1 
ATOM   2597 C CE  . LYS A 1 335 ? 16.007  -10.487 11.601  1.00 52.06 ? 328 LYS A CE  1 
ATOM   2598 N NZ  . LYS A 1 335 ? 15.445  -10.797 12.936  1.00 47.44 ? 328 LYS A NZ  1 
ATOM   2599 N N   . PHE A 1 336 ? 16.340  -4.500  8.364   1.00 38.91 ? 329 PHE A N   1 
ATOM   2600 C CA  . PHE A 1 336 ? 17.509  -3.664  7.975   1.00 39.75 ? 329 PHE A CA  1 
ATOM   2601 C C   . PHE A 1 336 ? 17.131  -2.184  7.992   1.00 38.59 ? 329 PHE A C   1 
ATOM   2602 O O   . PHE A 1 336 ? 15.960  -1.840  7.839   1.00 30.52 ? 329 PHE A O   1 
ATOM   2603 C CB  . PHE A 1 336 ? 18.069  -4.090  6.613   1.00 47.54 ? 329 PHE A CB  1 
ATOM   2604 C CG  . PHE A 1 336 ? 18.103  -5.585  6.409   1.00 47.83 ? 329 PHE A CG  1 
ATOM   2605 C CD1 . PHE A 1 336 ? 18.950  -6.382  7.167   1.00 54.97 ? 329 PHE A CD1 1 
ATOM   2606 C CD2 . PHE A 1 336 ? 17.253  -6.203  5.504   1.00 51.75 ? 329 PHE A CD2 1 
ATOM   2607 C CE1 . PHE A 1 336 ? 18.961  -7.762  7.011   1.00 56.47 ? 329 PHE A CE1 1 
ATOM   2608 C CE2 . PHE A 1 336 ? 17.266  -7.582  5.346   1.00 57.60 ? 329 PHE A CE2 1 
ATOM   2609 C CZ  . PHE A 1 336 ? 18.125  -8.359  6.094   1.00 58.17 ? 329 PHE A CZ  1 
ATOM   2610 N N   . ASP A 1 337 ? 18.141  -1.338  8.185   1.00 36.41 ? 330 ASP A N   1 
ATOM   2611 C CA  . ASP A 1 337 ? 18.064  0.131   7.994   1.00 41.06 ? 330 ASP A CA  1 
ATOM   2612 C C   . ASP A 1 337 ? 17.370  0.394   6.646   1.00 47.70 ? 330 ASP A C   1 
ATOM   2613 O O   . ASP A 1 337 ? 17.765  -0.227  5.634   1.00 39.39 ? 330 ASP A O   1 
ATOM   2614 C CB  . ASP A 1 337 ? 19.470  0.750   8.034   1.00 44.63 ? 330 ASP A CB  1 
ATOM   2615 C CG  . ASP A 1 337 ? 20.280  0.443   9.293   1.00 51.03 ? 330 ASP A CG  1 
ATOM   2616 O OD1 . ASP A 1 337 ? 19.662  0.332   10.380  1.00 46.77 ? 330 ASP A OD1 1 
ATOM   2617 O OD2 . ASP A 1 337 ? 21.537  0.304   9.179   1.00 50.16 ? 330 ASP A OD2 1 
ATOM   2618 N N   . MET A 1 338 ? 16.354  1.256   6.629   1.00 51.36 ? 331 MET A N   1 
ATOM   2619 C CA  . MET A 1 338 ? 15.771  1.774   5.371   1.00 56.04 ? 331 MET A CA  1 
ATOM   2620 C C   . MET A 1 338 ? 16.662  2.927   4.918   1.00 65.82 ? 331 MET A C   1 
ATOM   2621 O O   . MET A 1 338 ? 16.538  4.030   5.487   1.00 85.94 ? 331 MET A O   1 
ATOM   2622 C CB  . MET A 1 338 ? 14.326  2.243   5.546   1.00 59.60 ? 331 MET A CB  1 
ATOM   2623 C CG  . MET A 1 338 ? 14.004  2.887   6.887   1.00 61.86 ? 331 MET A CG  1 
ATOM   2624 S SD  . MET A 1 338 ? 12.236  2.730   7.305   1.00 58.92 ? 331 MET A SD  1 
ATOM   2625 C CE  . MET A 1 338 ? 11.512  2.710   5.671   1.00 56.71 ? 331 MET A CE  1 
ATOM   2626 N N   . GLU A 1 339 ? 17.571  2.655   3.984   1.00 61.97 ? 332 GLU A N   1 
ATOM   2627 C CA  . GLU A 1 339 ? 18.708  3.557   3.673   1.00 60.64 ? 332 GLU A CA  1 
ATOM   2628 C C   . GLU A 1 339 ? 18.165  4.737   2.878   1.00 55.70 ? 332 GLU A C   1 
ATOM   2629 O O   . GLU A 1 339 ? 18.228  4.684   1.649   1.00 56.39 ? 332 GLU A O   1 
ATOM   2630 C CB  . GLU A 1 339 ? 19.807  2.816   2.918   1.00 64.64 ? 332 GLU A CB  1 
ATOM   2631 C CG  . GLU A 1 339 ? 20.614  1.896   3.810   1.00 67.63 ? 332 GLU A CG  1 
ATOM   2632 C CD  . GLU A 1 339 ? 21.496  0.953   3.018   1.00 70.12 ? 332 GLU A CD  1 
ATOM   2633 O OE1 . GLU A 1 339 ? 20.953  -0.020  2.461   1.00 74.62 ? 332 GLU A OE1 1 
ATOM   2634 O OE2 . GLU A 1 339 ? 22.707  1.219   2.925   1.00 67.30 ? 332 GLU A OE2 1 
ATOM   2635 N N   . LEU A 1 340 ? 17.649  5.734   3.604   1.00 52.29 ? 333 LEU A N   1 
ATOM   2636 C CA  . LEU A 1 340 ? 16.854  6.883   3.097   1.00 51.65 ? 333 LEU A CA  1 
ATOM   2637 C C   . LEU A 1 340 ? 17.637  8.188   3.262   1.00 54.02 ? 333 LEU A C   1 
ATOM   2638 O O   . LEU A 1 340 ? 17.253  9.186   2.624   1.00 49.86 ? 333 LEU A O   1 
ATOM   2639 C CB  . LEU A 1 340 ? 15.555  6.953   3.909   1.00 49.87 ? 333 LEU A CB  1 
ATOM   2640 C CG  . LEU A 1 340 ? 14.316  6.307   3.294   1.00 48.79 ? 333 LEU A CG  1 
ATOM   2641 C CD1 . LEU A 1 340 ? 14.649  5.103   2.431   1.00 42.31 ? 333 LEU A CD1 1 
ATOM   2642 C CD2 . LEU A 1 340 ? 13.307  5.950   4.379   1.00 49.18 ? 333 LEU A CD2 1 
ATOM   2643 N N   . ASP A 1 341 ? 18.687  8.179   4.092   1.00 57.38 ? 334 ASP A N   1 
ATOM   2644 C CA  . ASP A 1 341 ? 19.276  9.409   4.686   1.00 60.07 ? 334 ASP A CA  1 
ATOM   2645 C C   . ASP A 1 341 ? 19.973  10.221  3.593   1.00 52.92 ? 334 ASP A C   1 
ATOM   2646 O O   . ASP A 1 341 ? 19.838  11.461  3.618   1.00 55.34 ? 334 ASP A O   1 
ATOM   2647 C CB  . ASP A 1 341 ? 20.157  9.072   5.893   1.00 67.90 ? 334 ASP A CB  1 
ATOM   2648 C CG  . ASP A 1 341 ? 19.355  8.925   7.180   1.00 75.52 ? 334 ASP A CG  1 
ATOM   2649 O OD1 . ASP A 1 341 ? 18.869  9.966   7.689   1.00 75.47 ? 334 ASP A OD1 1 
ATOM   2650 O OD2 . ASP A 1 341 ? 19.198  7.773   7.652   1.00 76.99 ? 334 ASP A OD2 1 
ATOM   2651 N N   . ASP A 1 342 ? 20.612  9.555   2.631   1.00 50.47 ? 335 ASP A N   1 
ATOM   2652 C CA  . ASP A 1 342 ? 21.365  10.218  1.533   1.00 55.92 ? 335 ASP A CA  1 
ATOM   2653 C C   . ASP A 1 342 ? 20.784  9.815   0.165   1.00 54.92 ? 335 ASP A C   1 
ATOM   2654 O O   . ASP A 1 342 ? 21.576  9.620   -0.773  1.00 56.58 ? 335 ASP A O   1 
ATOM   2655 C CB  . ASP A 1 342 ? 22.864  9.908   1.661   1.00 62.41 ? 335 ASP A CB  1 
ATOM   2656 C CG  . ASP A 1 342 ? 23.173  8.421   1.733   1.00 66.44 ? 335 ASP A CG  1 
ATOM   2657 O OD1 . ASP A 1 342 ? 22.210  7.625   1.794   1.00 74.70 ? 335 ASP A OD1 1 
ATOM   2658 O OD2 . ASP A 1 342 ? 24.364  8.065   1.732   1.00 62.51 ? 335 ASP A OD2 1 
ATOM   2659 N N   . LEU A 1 343 ? 19.453  9.701   0.041   1.00 46.96 ? 336 LEU A N   1 
ATOM   2660 C CA  . LEU A 1 343 ? 18.755  9.555   -1.268  1.00 43.58 ? 336 LEU A CA  1 
ATOM   2661 C C   . LEU A 1 343 ? 18.296  10.940  -1.724  1.00 43.64 ? 336 LEU A C   1 
ATOM   2662 O O   . LEU A 1 343 ? 17.744  11.706  -0.930  1.00 40.00 ? 336 LEU A O   1 
ATOM   2663 C CB  . LEU A 1 343 ? 17.564  8.597   -1.126  1.00 45.25 ? 336 LEU A CB  1 
ATOM   2664 C CG  . LEU A 1 343 ? 17.912  7.127   -0.901  1.00 45.08 ? 336 LEU A CG  1 
ATOM   2665 C CD1 . LEU A 1 343 ? 16.652  6.276   -0.831  1.00 45.24 ? 336 LEU A CD1 1 
ATOM   2666 C CD2 . LEU A 1 343 ? 18.835  6.611   -1.993  1.00 48.22 ? 336 LEU A CD2 1 
ATOM   2667 N N   . PRO A 1 344 ? 18.493  11.316  -3.011  1.00 41.80 ? 337 PRO A N   1 
ATOM   2668 C CA  . PRO A 1 344 ? 18.026  12.612  -3.490  1.00 40.83 ? 337 PRO A CA  1 
ATOM   2669 C C   . PRO A 1 344 ? 16.488  12.649  -3.450  1.00 40.03 ? 337 PRO A C   1 
ATOM   2670 O O   . PRO A 1 344 ? 15.876  11.595  -3.573  1.00 33.39 ? 337 PRO A O   1 
ATOM   2671 C CB  . PRO A 1 344 ? 18.549  12.692  -4.930  1.00 43.72 ? 337 PRO A CB  1 
ATOM   2672 C CG  . PRO A 1 344 ? 18.712  11.238  -5.357  1.00 46.85 ? 337 PRO A CG  1 
ATOM   2673 C CD  . PRO A 1 344 ? 19.082  10.495  -4.084  1.00 46.37 ? 337 PRO A CD  1 
ATOM   2674 N N   . LYS A 1 345 ? 15.912  13.836  -3.275  1.00 34.65 ? 338 LYS A N   1 
ATOM   2675 C CA  . LYS A 1 345 ? 14.453  14.103  -3.405  1.00 40.84 ? 338 LYS A CA  1 
ATOM   2676 C C   . LYS A 1 345 ? 13.829  13.284  -4.539  1.00 38.41 ? 338 LYS A C   1 
ATOM   2677 O O   . LYS A 1 345 ? 12.727  12.737  -4.337  1.00 32.73 ? 338 LYS A O   1 
ATOM   2678 C CB  . LYS A 1 345 ? 14.175  15.548  -3.815  1.00 49.67 ? 338 LYS A CB  1 
ATOM   2679 C CG  . LYS A 1 345 ? 14.420  16.612  -2.764  1.00 58.92 ? 338 LYS A CG  1 
ATOM   2680 C CD  . LYS A 1 345 ? 14.496  18.007  -3.361  1.00 65.28 ? 338 LYS A CD  1 
ATOM   2681 C CE  . LYS A 1 345 ? 15.764  18.270  -4.154  1.00 71.48 ? 338 LYS A CE  1 
ATOM   2682 N NZ  . LYS A 1 345 ? 15.555  18.129  -5.614  1.00 69.65 ? 338 LYS A NZ  1 
ATOM   2683 N N   . GLU A 1 346 ? 14.462  13.262  -5.718  1.00 32.70 ? 339 GLU A N   1 
ATOM   2684 C CA  . GLU A 1 346 ? 13.831  12.761  -6.964  1.00 31.66 ? 339 GLU A CA  1 
ATOM   2685 C C   . GLU A 1 346 ? 13.573  11.256  -6.825  1.00 29.22 ? 339 GLU A C   1 
ATOM   2686 O O   . GLU A 1 346 ? 12.485  10.766  -7.230  1.00 28.21 ? 339 GLU A O   1 
ATOM   2687 C CB  . GLU A 1 346 ? 14.742  13.098  -8.146  1.00 33.89 ? 339 GLU A CB  1 
ATOM   2688 C CG  . GLU A 1 346 ? 14.853  14.606  -8.392  1.00 34.20 ? 339 GLU A CG  1 
ATOM   2689 C CD  . GLU A 1 346 ? 15.944  15.320  -7.604  1.00 36.52 ? 339 GLU A CD  1 
ATOM   2690 O OE1 . GLU A 1 346 ? 16.831  14.648  -7.027  1.00 36.79 ? 339 GLU A OE1 1 
ATOM   2691 O OE2 . GLU A 1 346 ? 15.872  16.555  -7.510  1.00 49.67 ? 339 GLU A OE2 1 
ATOM   2692 N N   . LYS A 1 347 ? 14.520  10.560  -6.224  1.00 28.04 ? 340 LYS A N   1 
ATOM   2693 C CA  . LYS A 1 347 ? 14.430  9.103   -5.974  1.00 31.14 ? 340 LYS A CA  1 
ATOM   2694 C C   . LYS A 1 347 ? 13.362  8.897   -4.888  1.00 27.87 ? 340 LYS A C   1 
ATOM   2695 O O   . LYS A 1 347 ? 12.616  7.919   -4.961  1.00 27.31 ? 340 LYS A O   1 
ATOM   2696 C CB  . LYS A 1 347 ? 15.809  8.574   -5.569  1.00 37.92 ? 340 LYS A CB  1 
ATOM   2697 C CG  . LYS A 1 347 ? 15.997  7.090   -5.806  1.00 48.64 ? 340 LYS A CG  1 
ATOM   2698 C CD  . LYS A 1 347 ? 16.401  6.730   -7.243  1.00 54.39 ? 340 LYS A CD  1 
ATOM   2699 C CE  . LYS A 1 347 ? 16.953  5.318   -7.311  1.00 61.78 ? 340 LYS A CE  1 
ATOM   2700 N NZ  . LYS A 1 347 ? 17.391  4.924   -8.673  1.00 66.21 ? 340 LYS A NZ  1 
ATOM   2701 N N   . LEU A 1 348 ? 13.347  9.769   -3.882  1.00 28.64 ? 341 LEU A N   1 
ATOM   2702 C CA  . LEU A 1 348 ? 12.400  9.643   -2.741  1.00 26.31 ? 341 LEU A CA  1 
ATOM   2703 C C   . LEU A 1 348 ? 10.984  9.827   -3.300  1.00 27.83 ? 341 LEU A C   1 
ATOM   2704 O O   . LEU A 1 348 ? 10.111  9.066   -2.912  1.00 22.91 ? 341 LEU A O   1 
ATOM   2705 C CB  . LEU A 1 348 ? 12.710  10.685  -1.671  1.00 29.77 ? 341 LEU A CB  1 
ATOM   2706 C CG  . LEU A 1 348 ? 13.936  10.393  -0.792  1.00 29.98 ? 341 LEU A CG  1 
ATOM   2707 C CD1 . LEU A 1 348 ? 14.276  11.607  0.050   1.00 29.56 ? 341 LEU A CD1 1 
ATOM   2708 C CD2 . LEU A 1 348 ? 13.697  9.203   0.106   1.00 31.57 ? 341 LEU A CD2 1 
ATOM   2709 N N   . LYS A 1 349 ? 10.799  10.777  -4.212  1.00 26.66 ? 342 LYS A N   1 
ATOM   2710 C CA  . LYS A 1 349 ? 9.482   11.003  -4.853  1.00 25.70 ? 342 LYS A CA  1 
ATOM   2711 C C   . LYS A 1 349 ? 9.044   9.743   -5.599  1.00 26.19 ? 342 LYS A C   1 
ATOM   2712 O O   . LYS A 1 349 ? 7.863   9.334   -5.425  1.00 25.86 ? 342 LYS A O   1 
ATOM   2713 C CB  . LYS A 1 349 ? 9.502   12.221  -5.774  1.00 26.47 ? 342 LYS A CB  1 
ATOM   2714 C CG  . LYS A 1 349 ? 8.167   12.453  -6.451  1.00 26.90 ? 342 LYS A CG  1 
ATOM   2715 C CD  . LYS A 1 349 ? 8.122   13.657  -7.358  1.00 26.20 ? 342 LYS A CD  1 
ATOM   2716 C CE  . LYS A 1 349 ? 6.699   14.084  -7.630  1.00 24.99 ? 342 LYS A CE  1 
ATOM   2717 N NZ  . LYS A 1 349 ? 6.622   15.178  -8.624  1.00 28.38 ? 342 LYS A NZ  1 
ATOM   2718 N N   . GLU A 1 350 ? 9.922   9.159   -6.399  1.00 26.87 ? 343 GLU A N   1 
ATOM   2719 C CA  . GLU A 1 350 ? 9.704   7.851   -7.065  1.00 29.16 ? 343 GLU A CA  1 
ATOM   2720 C C   . GLU A 1 350 ? 9.319   6.782   -6.040  1.00 28.24 ? 343 GLU A C   1 
ATOM   2721 O O   . GLU A 1 350 ? 8.389   6.013   -6.332  1.00 25.45 ? 343 GLU A O   1 
ATOM   2722 C CB  . GLU A 1 350 ? 10.979  7.370   -7.775  1.00 33.73 ? 343 GLU A CB  1 
ATOM   2723 C CG  . GLU A 1 350 ? 11.436  8.224   -8.930  1.00 40.84 ? 343 GLU A CG  1 
ATOM   2724 C CD  . GLU A 1 350 ? 12.821  7.803   -9.428  1.00 44.23 ? 343 GLU A CD  1 
ATOM   2725 O OE1 . GLU A 1 350 ? 13.563  8.654   -9.996  1.00 51.14 ? 343 GLU A OE1 1 
ATOM   2726 O OE2 . GLU A 1 350 ? 13.153  6.611   -9.256  1.00 48.73 ? 343 GLU A OE2 1 
ATOM   2727 N N   . LEU A 1 351 ? 10.001  6.712   -4.880  1.00 23.55 ? 344 LEU A N   1 
ATOM   2728 C CA  . LEU A 1 351 ? 9.700   5.658   -3.885  1.00 22.98 ? 344 LEU A CA  1 
ATOM   2729 C C   . LEU A 1 351 ? 8.319   5.926   -3.310  1.00 20.89 ? 344 LEU A C   1 
ATOM   2730 O O   . LEU A 1 351 ? 7.609   4.964   -3.081  1.00 20.59 ? 344 LEU A O   1 
ATOM   2731 C CB  . LEU A 1 351 ? 10.732  5.616   -2.749  1.00 26.91 ? 344 LEU A CB  1 
ATOM   2732 C CG  . LEU A 1 351 ? 12.009  4.778   -2.928  1.00 33.83 ? 344 LEU A CG  1 
ATOM   2733 C CD1 . LEU A 1 351 ? 11.942  3.802   -4.089  1.00 33.32 ? 344 LEU A CD1 1 
ATOM   2734 C CD2 . LEU A 1 351 ? 13.233  5.666   -3.024  1.00 38.01 ? 344 LEU A CD2 1 
ATOM   2735 N N   . ILE A 1 352 ? 7.983   7.176   -3.055  1.00 18.07 ? 345 ILE A N   1 
ATOM   2736 C CA  . ILE A 1 352 ? 6.642   7.559   -2.514  1.00 19.21 ? 345 ILE A CA  1 
ATOM   2737 C C   . ILE A 1 352 ? 5.593   7.202   -3.562  1.00 18.24 ? 345 ILE A C   1 
ATOM   2738 O O   . ILE A 1 352 ? 4.541   6.654   -3.215  1.00 17.21 ? 345 ILE A O   1 
ATOM   2739 C CB  . ILE A 1 352 ? 6.587   9.049   -2.113  1.00 18.43 ? 345 ILE A CB  1 
ATOM   2740 C CG1 . ILE A 1 352 ? 7.420   9.278   -0.844  1.00 20.46 ? 345 ILE A CG1 1 
ATOM   2741 C CG2 . ILE A 1 352 ? 5.161   9.529   -1.960  1.00 19.31 ? 345 ILE A CG2 1 
ATOM   2742 C CD1 . ILE A 1 352 ? 7.709   10.725  -0.571  1.00 20.66 ? 345 ILE A CD1 1 
ATOM   2743 N N   . PHE A 1 353 ? 5.854   7.564   -4.805  1.00 21.14 ? 346 PHE A N   1 
ATOM   2744 C CA  . PHE A 1 353 ? 4.947   7.157   -5.911  1.00 20.30 ? 346 PHE A CA  1 
ATOM   2745 C C   . PHE A 1 353 ? 4.701   5.640   -5.881  1.00 19.71 ? 346 PHE A C   1 
ATOM   2746 O O   . PHE A 1 353 ? 3.544   5.181   -5.902  1.00 20.80 ? 346 PHE A O   1 
ATOM   2747 C CB  . PHE A 1 353 ? 5.533   7.624   -7.244  1.00 21.38 ? 346 PHE A CB  1 
ATOM   2748 C CG  . PHE A 1 353 ? 4.567   7.442   -8.384  1.00 20.25 ? 346 PHE A CG  1 
ATOM   2749 C CD1 . PHE A 1 353 ? 3.532   8.347   -8.591  1.00 20.68 ? 346 PHE A CD1 1 
ATOM   2750 C CD2 . PHE A 1 353 ? 4.674   6.341   -9.215  1.00 22.77 ? 346 PHE A CD2 1 
ATOM   2751 C CE1 . PHE A 1 353 ? 2.664   8.184   -9.664  1.00 19.11 ? 346 PHE A CE1 1 
ATOM   2752 C CE2 . PHE A 1 353 ? 3.765   6.150   -10.248 1.00 22.98 ? 346 PHE A CE2 1 
ATOM   2753 C CZ  . PHE A 1 353 ? 2.785   7.088   -10.488 1.00 21.50 ? 346 PHE A CZ  1 
ATOM   2754 N N   . GLU A 1 354 ? 5.763   4.832   -5.864  1.00 20.41 ? 347 GLU A N   1 
ATOM   2755 C CA  . GLU A 1 354 ? 5.688   3.350   -5.857  1.00 25.42 ? 347 GLU A CA  1 
ATOM   2756 C C   . GLU A 1 354 ? 4.965   2.863   -4.598  1.00 24.39 ? 347 GLU A C   1 
ATOM   2757 O O   . GLU A 1 354 ? 4.110   1.955   -4.698  1.00 24.79 ? 347 GLU A O   1 
ATOM   2758 C CB  . GLU A 1 354 ? 7.094   2.732   -5.854  1.00 28.35 ? 347 GLU A CB  1 
ATOM   2759 C CG  . GLU A 1 354 ? 7.884   2.918   -7.139  1.00 38.39 ? 347 GLU A CG  1 
ATOM   2760 C CD  . GLU A 1 354 ? 9.314   2.385   -7.095  1.00 43.61 ? 347 GLU A CD  1 
ATOM   2761 O OE1 . GLU A 1 354 ? 9.675   1.704   -6.110  1.00 47.09 ? 347 GLU A OE1 1 
ATOM   2762 O OE2 . GLU A 1 354 ? 10.075  2.644   -8.052  1.00 53.72 ? 347 GLU A OE2 1 
ATOM   2763 N N   . GLU A 1 355 ? 5.319   3.434   -3.442  1.00 23.23 ? 348 GLU A N   1 
ATOM   2764 C CA  . GLU A 1 355 ? 4.756   3.039   -2.121  1.00 24.15 ? 348 GLU A CA  1 
ATOM   2765 C C   . GLU A 1 355 ? 3.245   3.253   -2.119  1.00 24.12 ? 348 GLU A C   1 
ATOM   2766 O O   . GLU A 1 355 ? 2.550   2.503   -1.416  1.00 24.79 ? 348 GLU A O   1 
ATOM   2767 C CB  . GLU A 1 355 ? 5.279   3.893   -0.958  1.00 31.43 ? 348 GLU A CB  1 
ATOM   2768 C CG  . GLU A 1 355 ? 6.179   3.246   0.088   1.00 37.50 ? 348 GLU A CG  1 
ATOM   2769 C CD  . GLU A 1 355 ? 6.355   1.745   0.146   1.00 36.47 ? 348 GLU A CD  1 
ATOM   2770 O OE1 . GLU A 1 355 ? 5.523   1.053   0.805   1.00 43.06 ? 348 GLU A OE1 1 
ATOM   2771 O OE2 . GLU A 1 355 ? 7.343   1.289   -0.444  1.00 34.10 ? 348 GLU A OE2 1 
ATOM   2772 N N   . THR A 1 356 ? 2.724   4.227   -2.873  1.00 21.26 ? 349 THR A N   1 
ATOM   2773 C CA  . THR A 1 356 ? 1.309   4.651   -2.805  1.00 18.61 ? 349 THR A CA  1 
ATOM   2774 C C   . THR A 1 356 ? 0.488   4.013   -3.944  1.00 19.88 ? 349 THR A C   1 
ATOM   2775 O O   . THR A 1 356 ? -0.723  4.232   -3.963  1.00 19.62 ? 349 THR A O   1 
ATOM   2776 C CB  . THR A 1 356 ? 1.192   6.181   -2.750  1.00 18.73 ? 349 THR A CB  1 
ATOM   2777 O OG1 . THR A 1 356 ? 1.849   6.710   -3.898  1.00 18.52 ? 349 THR A OG1 1 
ATOM   2778 C CG2 . THR A 1 356 ? 1.807   6.775   -1.490  1.00 20.14 ? 349 THR A CG2 1 
ATOM   2779 N N   . ALA A 1 357 ? 1.109   3.225   -4.802  1.00 20.36 ? 350 ALA A N   1 
ATOM   2780 C CA  . ALA A 1 357 ? 0.518   2.696   -6.057  1.00 22.91 ? 350 ALA A CA  1 
ATOM   2781 C C   . ALA A 1 357 ? -0.695  1.785   -5.775  1.00 24.54 ? 350 ALA A C   1 
ATOM   2782 O O   . ALA A 1 357 ? -1.697  1.837   -6.578  1.00 26.60 ? 350 ALA A O   1 
ATOM   2783 C CB  . ALA A 1 357 ? 1.571   1.973   -6.841  1.00 22.80 ? 350 ALA A CB  1 
ATOM   2784 N N   . ARG A 1 358 ? -0.698  1.061   -4.654  1.00 27.51 ? 351 ARG A N   1 
ATOM   2785 C CA  . ARG A 1 358 ? -1.769  0.069   -4.309  1.00 28.73 ? 351 ARG A CA  1 
ATOM   2786 C C   . ARG A 1 358 ? -3.159  0.732   -4.172  1.00 28.49 ? 351 ARG A C   1 
ATOM   2787 O O   . ARG A 1 358 ? -4.189  0.035   -4.290  1.00 25.11 ? 351 ARG A O   1 
ATOM   2788 C CB  . ARG A 1 358 ? -1.329  -0.728  -3.072  1.00 33.11 ? 351 ARG A CB  1 
ATOM   2789 C CG  . ARG A 1 358 ? -1.525  -0.045  -1.723  1.00 35.41 ? 351 ARG A CG  1 
ATOM   2790 C CD  . ARG A 1 358 ? -0.725  -0.712  -0.600  1.00 38.35 ? 351 ARG A CD  1 
ATOM   2791 N NE  . ARG A 1 358 ? 0.703   -0.463  -0.784  1.00 45.54 ? 351 ARG A NE  1 
ATOM   2792 C CZ  . ARG A 1 358 ? 1.705   -1.002  -0.078  1.00 48.03 ? 351 ARG A CZ  1 
ATOM   2793 N NH1 . ARG A 1 358 ? 1.462   -1.850  0.909   1.00 46.38 ? 351 ARG A NH1 1 
ATOM   2794 N NH2 . ARG A 1 358 ? 2.957   -0.654  -0.351  1.00 46.24 ? 351 ARG A NH2 1 
ATOM   2795 N N   . PHE A 1 359 ? -3.255  2.039   -3.959  1.00 22.84 ? 352 PHE A N   1 
ATOM   2796 C CA  . PHE A 1 359 ? -4.536  2.721   -3.710  1.00 23.93 ? 352 PHE A CA  1 
ATOM   2797 C C   . PHE A 1 359 ? -5.113  3.292   -5.014  1.00 23.72 ? 352 PHE A C   1 
ATOM   2798 O O   . PHE A 1 359 ? -6.175  3.906   -4.954  1.00 26.30 ? 352 PHE A O   1 
ATOM   2799 C CB  . PHE A 1 359 ? -4.365  3.796   -2.652  1.00 24.45 ? 352 PHE A CB  1 
ATOM   2800 C CG  . PHE A 1 359 ? -3.996  3.226   -1.313  1.00 24.23 ? 352 PHE A CG  1 
ATOM   2801 C CD1 . PHE A 1 359 ? -4.950  2.603   -0.520  1.00 27.86 ? 352 PHE A CD1 1 
ATOM   2802 C CD2 . PHE A 1 359 ? -2.694  3.288   -0.850  1.00 26.31 ? 352 PHE A CD2 1 
ATOM   2803 C CE1 . PHE A 1 359 ? -4.607  2.068   0.708   1.00 26.54 ? 352 PHE A CE1 1 
ATOM   2804 C CE2 . PHE A 1 359 ? -2.349  2.724   0.374   1.00 27.41 ? 352 PHE A CE2 1 
ATOM   2805 C CZ  . PHE A 1 359 ? -3.306  2.132   1.155   1.00 25.79 ? 352 PHE A CZ  1 
ATOM   2806 N N   . GLN A 1 360 ? -4.395  3.140   -6.114  1.00 24.81 ? 353 GLN A N   1 
ATOM   2807 C CA  . GLN A 1 360 ? -4.848  3.692   -7.420  1.00 30.33 ? 353 GLN A CA  1 
ATOM   2808 C C   . GLN A 1 360 ? -5.966  2.809   -7.969  1.00 39.59 ? 353 GLN A C   1 
ATOM   2809 O O   . GLN A 1 360 ? -5.924  1.598   -7.788  1.00 36.04 ? 353 GLN A O   1 
ATOM   2810 C CB  . GLN A 1 360 ? -3.661  3.824   -8.368  1.00 30.16 ? 353 GLN A CB  1 
ATOM   2811 C CG  . GLN A 1 360 ? -2.749  4.988   -7.978  1.00 28.78 ? 353 GLN A CG  1 
ATOM   2812 C CD  . GLN A 1 360 ? -3.478  6.308   -7.979  1.00 31.54 ? 353 GLN A CD  1 
ATOM   2813 O OE1 . GLN A 1 360 ? -3.624  6.984   -6.948  1.00 28.91 ? 353 GLN A OE1 1 
ATOM   2814 N NE2 . GLN A 1 360 ? -3.985  6.684   -9.154  1.00 30.48 ? 353 GLN A NE2 1 
ATOM   2815 N N   . PRO A 1 361 ? -7.000  3.395   -8.622  1.00 47.41 ? 354 PRO A N   1 
ATOM   2816 C CA  . PRO A 1 361 ? -7.794  2.650   -9.603  1.00 50.53 ? 354 PRO A CA  1 
ATOM   2817 C C   . PRO A 1 361 ? -6.802  1.983   -10.580 1.00 50.18 ? 354 PRO A C   1 
ATOM   2818 O O   . PRO A 1 361 ? -6.755  0.757   -10.621 1.00 50.18 ? 354 PRO A O   1 
ATOM   2819 C CB  . PRO A 1 361 ? -8.706  3.720   -10.231 1.00 50.02 ? 354 PRO A CB  1 
ATOM   2820 C CG  . PRO A 1 361 ? -8.118  5.059   -9.810  1.00 51.12 ? 354 PRO A CG  1 
ATOM   2821 C CD  . PRO A 1 361 ? -7.442  4.793   -8.479  1.00 48.27 ? 354 PRO A CD  1 
ATOM   2822 N N   . GLY A 1 362 ? -5.994  2.803   -11.276 1.00 49.76 ? 355 GLY A N   1 
ATOM   2823 C CA  . GLY A 1 362 ? -4.736  2.414   -11.947 1.00 49.66 ? 355 GLY A CA  1 
ATOM   2824 C C   . GLY A 1 362 ? -4.886  1.190   -12.847 1.00 56.50 ? 355 GLY A C   1 
ATOM   2825 O O   . GLY A 1 362 ? -5.156  1.298   -14.055 1.00 48.56 ? 355 GLY A O   1 
HETATM 2826 S S   . SO4 B 2 .   ? 16.559  21.739  21.732  1.00 38.57 ? 401 SO4 A S   1 
HETATM 2827 O O1  . SO4 B 2 .   ? 15.419  22.591  21.519  1.00 42.80 ? 401 SO4 A O1  1 
HETATM 2828 O O2  . SO4 B 2 .   ? 16.548  20.700  20.718  1.00 36.09 ? 401 SO4 A O2  1 
HETATM 2829 O O3  . SO4 B 2 .   ? 17.779  22.524  21.621  1.00 43.60 ? 401 SO4 A O3  1 
HETATM 2830 O O4  . SO4 B 2 .   ? 16.520  21.166  23.084  1.00 34.73 ? 401 SO4 A O4  1 
HETATM 2831 S S   . SO4 C 2 .   ? 13.021  -5.687  5.727   1.00 55.09 ? 402 SO4 A S   1 
HETATM 2832 O O1  . SO4 C 2 .   ? 13.248  -6.358  4.455   1.00 59.18 ? 402 SO4 A O1  1 
HETATM 2833 O O2  . SO4 C 2 .   ? 11.751  -4.992  5.697   1.00 41.58 ? 402 SO4 A O2  1 
HETATM 2834 O O3  . SO4 C 2 .   ? 14.076  -4.718  5.985   1.00 52.91 ? 402 SO4 A O3  1 
HETATM 2835 O O4  . SO4 C 2 .   ? 12.995  -6.692  6.793   1.00 44.89 ? 402 SO4 A O4  1 
HETATM 2836 O O   . HOH D 3 .   ? 21.722  19.650  33.325  1.00 37.06 ? 501 HOH A O   1 
HETATM 2837 O O   . HOH D 3 .   ? -6.397  2.204   -15.768 1.00 35.71 ? 502 HOH A O   1 
HETATM 2838 O O   . HOH D 3 .   ? -5.426  14.139  34.275  1.00 33.17 ? 503 HOH A O   1 
HETATM 2839 O O   . HOH D 3 .   ? 13.394  9.881   20.344  1.00 33.75 ? 504 HOH A O   1 
HETATM 2840 O O   . HOH D 3 .   ? 21.235  6.222   39.245  1.00 31.78 ? 505 HOH A O   1 
HETATM 2841 O O   . HOH D 3 .   ? 29.144  6.775   26.747  1.00 43.14 ? 506 HOH A O   1 
HETATM 2842 O O   . HOH D 3 .   ? -4.629  9.004   -9.628  1.00 28.90 ? 507 HOH A O   1 
HETATM 2843 O O   . HOH D 3 .   ? -9.226  1.176   33.495  1.00 36.47 ? 508 HOH A O   1 
HETATM 2844 O O   . HOH D 3 .   ? -12.286 2.102   23.692  1.00 33.12 ? 509 HOH A O   1 
HETATM 2845 O O   . HOH D 3 .   ? -6.046  -6.435  25.102  1.00 31.93 ? 510 HOH A O   1 
HETATM 2846 O O   . HOH D 3 .   ? 11.488  10.103  41.873  1.00 33.83 ? 511 HOH A O   1 
HETATM 2847 O O   . HOH D 3 .   ? 32.270  17.517  29.944  1.00 29.33 ? 512 HOH A O   1 
HETATM 2848 O O   . HOH D 3 .   ? -3.606  6.999   39.356  1.00 28.26 ? 513 HOH A O   1 
HETATM 2849 O O   . HOH D 3 .   ? -6.797  4.829   9.863   1.00 22.18 ? 514 HOH A O   1 
HETATM 2850 O O   . HOH D 3 .   ? 10.863  15.366  -4.906  1.00 31.82 ? 515 HOH A O   1 
HETATM 2851 O O   . HOH D 3 .   ? 12.870  18.653  38.231  1.00 30.31 ? 516 HOH A O   1 
HETATM 2852 O O   . HOH D 3 .   ? -3.090  -11.309 19.459  1.00 31.70 ? 517 HOH A O   1 
HETATM 2853 O O   . HOH D 3 .   ? 18.982  19.577  19.629  1.00 32.60 ? 518 HOH A O   1 
HETATM 2854 O O   . HOH D 3 .   ? 17.185  5.873   7.191   1.00 47.60 ? 519 HOH A O   1 
HETATM 2855 O O   . HOH D 3 .   ? 2.640   -8.811  26.132  1.00 25.16 ? 520 HOH A O   1 
HETATM 2856 O O   . HOH D 3 .   ? 23.414  15.785  40.073  1.00 29.16 ? 521 HOH A O   1 
HETATM 2857 O O   . HOH D 3 .   ? 13.104  6.490   38.683  1.00 32.93 ? 522 HOH A O   1 
HETATM 2858 O O   . HOH D 3 .   ? 24.888  5.317   23.685  1.00 38.93 ? 523 HOH A O   1 
HETATM 2859 O O   . HOH D 3 .   ? 8.310   16.445  18.193  1.00 42.67 ? 524 HOH A O   1 
HETATM 2860 O O   . HOH D 3 .   ? -3.709  -9.720  34.086  1.00 43.22 ? 525 HOH A O   1 
HETATM 2861 O O   . HOH D 3 .   ? 35.996  11.731  34.997  1.00 38.67 ? 526 HOH A O   1 
HETATM 2862 O O   . HOH D 3 .   ? 7.355   12.636  14.277  1.00 35.16 ? 527 HOH A O   1 
HETATM 2863 O O   . HOH D 3 .   ? 18.553  4.811   22.493  1.00 29.26 ? 528 HOH A O   1 
HETATM 2864 O O   . HOH D 3 .   ? 6.377   -6.323  35.299  1.00 23.93 ? 529 HOH A O   1 
HETATM 2865 O O   . HOH D 3 .   ? 25.197  14.198  38.600  1.00 17.35 ? 530 HOH A O   1 
HETATM 2866 O O   . HOH D 3 .   ? 19.369  28.379  30.757  1.00 24.42 ? 531 HOH A O   1 
HETATM 2867 O O   . HOH D 3 .   ? -4.837  5.766   -11.504 1.00 31.77 ? 532 HOH A O   1 
HETATM 2868 O O   . HOH D 3 .   ? 15.836  -1.264  28.736  1.00 24.32 ? 533 HOH A O   1 
HETATM 2869 O O   . HOH D 3 .   ? 10.648  19.146  36.233  1.00 25.13 ? 534 HOH A O   1 
HETATM 2870 O O   . HOH D 3 .   ? -5.202  -9.368  19.476  1.00 29.93 ? 535 HOH A O   1 
HETATM 2871 O O   . HOH D 3 .   ? 5.323   -0.527  3.405   1.00 29.95 ? 536 HOH A O   1 
HETATM 2872 O O   . HOH D 3 .   ? 3.687   15.556  35.498  1.00 28.43 ? 537 HOH A O   1 
HETATM 2873 O O   . HOH D 3 .   ? 31.181  22.012  39.252  1.00 33.54 ? 538 HOH A O   1 
HETATM 2874 O O   . HOH D 3 .   ? -1.147  14.363  -6.456  1.00 20.44 ? 539 HOH A O   1 
HETATM 2875 O O   . HOH D 3 .   ? 18.513  4.455   25.131  1.00 24.53 ? 540 HOH A O   1 
HETATM 2876 O O   . HOH D 3 .   ? 11.218  13.070  22.689  1.00 24.88 ? 541 HOH A O   1 
HETATM 2877 O O   . HOH D 3 .   ? 20.613  7.888   30.750  1.00 25.89 ? 542 HOH A O   1 
HETATM 2878 O O   . HOH D 3 .   ? 21.558  12.533  20.277  1.00 30.85 ? 543 HOH A O   1 
HETATM 2879 O O   . HOH D 3 .   ? 24.792  22.763  34.141  1.00 26.29 ? 544 HOH A O   1 
HETATM 2880 O O   . HOH D 3 .   ? 18.991  4.037   36.736  1.00 20.49 ? 545 HOH A O   1 
HETATM 2881 O O   . HOH D 3 .   ? -8.169  3.496   -3.033  1.00 30.73 ? 546 HOH A O   1 
HETATM 2882 O O   . HOH D 3 .   ? 3.137   18.105  25.070  1.00 24.67 ? 547 HOH A O   1 
HETATM 2883 O O   . HOH D 3 .   ? 19.414  10.024  37.951  1.00 27.75 ? 548 HOH A O   1 
HETATM 2884 O O   . HOH D 3 .   ? 16.909  2.338   -9.287  1.00 49.09 ? 549 HOH A O   1 
HETATM 2885 O O   . HOH D 3 .   ? -5.383  -2.831  35.911  1.00 25.30 ? 550 HOH A O   1 
HETATM 2886 O O   . HOH D 3 .   ? -0.387  -6.495  34.039  1.00 17.34 ? 551 HOH A O   1 
HETATM 2887 O O   . HOH D 3 .   ? -2.191  1.007   7.221   1.00 20.71 ? 552 HOH A O   1 
HETATM 2888 O O   . HOH D 3 .   ? 4.325   -9.238  28.459  1.00 23.45 ? 553 HOH A O   1 
HETATM 2889 O O   . HOH D 3 .   ? -0.467  5.677   -10.993 1.00 28.22 ? 554 HOH A O   1 
HETATM 2890 O O   . HOH D 3 .   ? 7.961   -5.842  21.477  1.00 18.62 ? 555 HOH A O   1 
HETATM 2891 O O   . HOH D 3 .   ? 12.995  9.543   24.660  1.00 18.64 ? 556 HOH A O   1 
HETATM 2892 O O   . HOH D 3 .   ? -0.978  17.993  -11.231 1.00 25.81 ? 557 HOH A O   1 
HETATM 2893 O O   . HOH D 3 .   ? 9.587   8.284   21.817  1.00 15.21 ? 558 HOH A O   1 
HETATM 2894 O O   . HOH D 3 .   ? -1.920  -6.454  15.320  1.00 24.38 ? 559 HOH A O   1 
HETATM 2895 O O   . HOH D 3 .   ? 26.006  11.783  39.888  1.00 20.91 ? 560 HOH A O   1 
HETATM 2896 O O   . HOH D 3 .   ? 14.794  -3.974  31.846  1.00 35.81 ? 561 HOH A O   1 
HETATM 2897 O O   . HOH D 3 .   ? 8.574   12.876  21.743  1.00 27.62 ? 562 HOH A O   1 
HETATM 2898 O O   . HOH D 3 .   ? 8.203   9.452   14.778  1.00 19.19 ? 563 HOH A O   1 
HETATM 2899 O O   . HOH D 3 .   ? 18.474  24.274  23.622  1.00 32.41 ? 564 HOH A O   1 
HETATM 2900 O O   . HOH D 3 .   ? -3.592  18.238  -4.954  1.00 35.36 ? 565 HOH A O   1 
HETATM 2901 O O   . HOH D 3 .   ? 13.591  -6.014  17.223  1.00 21.49 ? 566 HOH A O   1 
HETATM 2902 O O   . HOH D 3 .   ? 7.354   17.564  -7.451  1.00 36.19 ? 567 HOH A O   1 
HETATM 2903 O O   . HOH D 3 .   ? 28.062  22.226  35.474  1.00 32.39 ? 568 HOH A O   1 
HETATM 2904 O O   . HOH D 3 .   ? -2.453  6.442   -4.503  1.00 22.66 ? 569 HOH A O   1 
HETATM 2905 O O   . HOH D 3 .   ? 1.488   -7.789  11.529  1.00 28.22 ? 570 HOH A O   1 
HETATM 2906 O O   . HOH D 3 .   ? -1.629  19.200  27.075  1.00 27.37 ? 571 HOH A O   1 
HETATM 2907 O O   . HOH D 3 .   ? -6.613  10.541  12.317  1.00 33.35 ? 572 HOH A O   1 
HETATM 2908 O O   . HOH D 3 .   ? 17.093  6.048   37.891  1.00 22.71 ? 573 HOH A O   1 
HETATM 2909 O O   . HOH D 3 .   ? -11.683 17.692  34.279  1.00 30.61 ? 574 HOH A O   1 
HETATM 2910 O O   . HOH D 3 .   ? 5.264   18.919  -2.798  1.00 29.56 ? 575 HOH A O   1 
HETATM 2911 O O   . HOH D 3 .   ? 19.213  8.844   41.527  1.00 39.10 ? 576 HOH A O   1 
HETATM 2912 O O   . HOH D 3 .   ? -6.726  3.028   12.173  1.00 24.11 ? 577 HOH A O   1 
HETATM 2913 O O   . HOH D 3 .   ? 12.228  13.884  29.211  1.00 17.12 ? 578 HOH A O   1 
HETATM 2914 O O   . HOH D 3 .   ? -5.958  0.764   13.706  1.00 26.94 ? 579 HOH A O   1 
HETATM 2915 O O   . HOH D 3 .   ? 18.022  10.669  46.927  1.00 39.52 ? 580 HOH A O   1 
HETATM 2916 O O   . HOH D 3 .   ? 24.312  13.732  22.948  1.00 22.71 ? 581 HOH A O   1 
HETATM 2917 O O   . HOH D 3 .   ? 13.525  0.059   28.165  1.00 18.78 ? 582 HOH A O   1 
HETATM 2918 O O   . HOH D 3 .   ? 5.462   14.806  30.570  1.00 19.08 ? 583 HOH A O   1 
HETATM 2919 O O   . HOH D 3 .   ? 33.590  17.298  36.140  1.00 34.59 ? 584 HOH A O   1 
HETATM 2920 O O   . HOH D 3 .   ? -13.184 7.223   10.578  1.00 26.32 ? 585 HOH A O   1 
HETATM 2921 O O   . HOH D 3 .   ? 11.516  20.163  21.195  1.00 35.16 ? 586 HOH A O   1 
HETATM 2922 O O   . HOH D 3 .   ? 10.715  -5.552  21.509  1.00 22.68 ? 587 HOH A O   1 
HETATM 2923 O O   . HOH D 3 .   ? -5.709  8.659   -6.040  1.00 25.27 ? 588 HOH A O   1 
HETATM 2924 O O   . HOH D 3 .   ? -8.730  0.572   21.224  1.00 33.23 ? 589 HOH A O   1 
HETATM 2925 O O   . HOH D 3 .   ? -11.780 5.704   4.884   1.00 46.72 ? 590 HOH A O   1 
HETATM 2926 O O   . HOH D 3 .   ? 17.062  17.876  25.546  1.00 28.12 ? 591 HOH A O   1 
HETATM 2927 O O   . HOH D 3 .   ? -2.661  11.651  40.238  1.00 33.15 ? 592 HOH A O   1 
HETATM 2928 O O   . HOH D 3 .   ? 0.248   -5.554  20.881  1.00 14.25 ? 593 HOH A O   1 
HETATM 2929 O O   . HOH D 3 .   ? 23.507  4.935   32.829  1.00 28.23 ? 594 HOH A O   1 
HETATM 2930 O O   . HOH D 3 .   ? 8.000   16.023  30.411  1.00 18.31 ? 595 HOH A O   1 
HETATM 2931 O O   . HOH D 3 .   ? 21.246  23.628  26.571  1.00 30.41 ? 596 HOH A O   1 
HETATM 2932 O O   . HOH D 3 .   ? 13.116  -0.477  35.743  1.00 25.00 ? 597 HOH A O   1 
HETATM 2933 O O   . HOH D 3 .   ? 18.236  17.479  46.868  1.00 33.63 ? 598 HOH A O   1 
HETATM 2934 O O   . HOH D 3 .   ? -2.496  -0.097  12.115  1.00 18.73 ? 599 HOH A O   1 
HETATM 2935 O O   . HOH D 3 .   ? 4.691   8.239   -13.363 1.00 29.11 ? 600 HOH A O   1 
HETATM 2936 O O   . HOH D 3 .   ? 2.416   16.598  22.663  1.00 19.67 ? 601 HOH A O   1 
HETATM 2937 O O   . HOH D 3 .   ? 1.322   -11.838 18.265  1.00 27.75 ? 602 HOH A O   1 
HETATM 2938 O O   . HOH D 3 .   ? -4.274  -5.236  16.758  1.00 25.70 ? 603 HOH A O   1 
HETATM 2939 O O   . HOH D 3 .   ? 7.769   -9.613  15.684  1.00 27.91 ? 604 HOH A O   1 
HETATM 2940 O O   . HOH D 3 .   ? 10.683  -2.230  24.702  1.00 22.83 ? 605 HOH A O   1 
HETATM 2941 O O   . HOH D 3 .   ? 0.304   8.581   45.609  1.00 37.79 ? 606 HOH A O   1 
HETATM 2942 O O   . HOH D 3 .   ? -0.602  1.169   10.691  1.00 17.24 ? 607 HOH A O   1 
HETATM 2943 O O   . HOH D 3 .   ? 19.465  10.468  13.639  1.00 36.99 ? 608 HOH A O   1 
HETATM 2944 O O   . HOH D 3 .   ? 25.177  17.768  16.895  1.00 30.66 ? 609 HOH A O   1 
HETATM 2945 O O   . HOH D 3 .   ? -4.559  -0.644  38.737  1.00 41.73 ? 610 HOH A O   1 
HETATM 2946 O O   . HOH D 3 .   ? 15.297  -5.872  21.184  1.00 40.93 ? 611 HOH A O   1 
HETATM 2947 O O   . HOH D 3 .   ? 16.954  -1.497  20.983  1.00 22.20 ? 612 HOH A O   1 
HETATM 2948 O O   . HOH D 3 .   ? 7.939   20.616  -0.574  1.00 35.46 ? 613 HOH A O   1 
HETATM 2949 O O   . HOH D 3 .   ? -19.234 9.223   10.811  1.00 49.71 ? 614 HOH A O   1 
HETATM 2950 O O   . HOH D 3 .   ? 22.391  -2.611  16.040  1.00 36.51 ? 615 HOH A O   1 
HETATM 2951 O O   . HOH D 3 .   ? 26.312  2.698   42.424  1.00 32.00 ? 616 HOH A O   1 
HETATM 2952 O O   . HOH D 3 .   ? 0.882   4.028   -9.638  1.00 29.92 ? 617 HOH A O   1 
HETATM 2953 O O   . HOH D 3 .   ? -0.925  17.108  -6.772  1.00 30.50 ? 618 HOH A O   1 
HETATM 2954 O O   . HOH D 3 .   ? 3.519   18.573  20.854  1.00 31.88 ? 619 HOH A O   1 
HETATM 2955 O O   . HOH D 3 .   ? 31.788  13.789  23.743  1.00 37.94 ? 620 HOH A O   1 
HETATM 2956 O O   . HOH D 3 .   ? 5.216   -3.924  41.472  1.00 37.06 ? 621 HOH A O   1 
HETATM 2957 O O   . HOH D 3 .   ? 21.322  12.593  17.790  1.00 37.84 ? 622 HOH A O   1 
HETATM 2958 O O   . HOH D 3 .   ? -1.011  2.129   -9.524  1.00 31.51 ? 623 HOH A O   1 
HETATM 2959 O O   . HOH D 3 .   ? 5.594   -11.508 30.991  1.00 42.01 ? 624 HOH A O   1 
HETATM 2960 O O   . HOH D 3 .   ? -10.994 5.751   38.280  1.00 34.12 ? 625 HOH A O   1 
HETATM 2961 O O   . HOH D 3 .   ? 28.428  4.616   27.076  1.00 42.94 ? 626 HOH A O   1 
HETATM 2962 O O   . HOH D 3 .   ? 29.355  18.758  42.860  1.00 34.04 ? 627 HOH A O   1 
HETATM 2963 O O   . HOH D 3 .   ? 26.316  5.275   44.060  1.00 27.82 ? 628 HOH A O   1 
HETATM 2964 O O   . HOH D 3 .   ? -7.158  -1.318  22.375  1.00 26.54 ? 629 HOH A O   1 
HETATM 2965 O O   . HOH D 3 .   ? 20.999  3.944   25.190  1.00 28.03 ? 630 HOH A O   1 
HETATM 2966 O O   . HOH D 3 .   ? 34.104  8.768   37.174  1.00 31.09 ? 631 HOH A O   1 
HETATM 2967 O O   . HOH D 3 .   ? 4.286   -6.021  10.391  1.00 33.07 ? 632 HOH A O   1 
HETATM 2968 O O   . HOH D 3 .   ? -1.456  12.966  41.675  1.00 35.48 ? 633 HOH A O   1 
HETATM 2969 O O   . HOH D 3 .   ? 12.870  -1.025  25.711  1.00 22.94 ? 634 HOH A O   1 
HETATM 2970 O O   . HOH D 3 .   ? 10.117  -4.904  41.444  1.00 46.56 ? 635 HOH A O   1 
HETATM 2971 O O   . HOH D 3 .   ? 16.042  3.441   9.280   1.00 31.46 ? 636 HOH A O   1 
HETATM 2972 O O   . HOH D 3 .   ? 16.510  19.856  0.110   1.00 49.25 ? 637 HOH A O   1 
HETATM 2973 O O   . HOH D 3 .   ? 12.667  10.946  22.314  1.00 38.55 ? 638 HOH A O   1 
HETATM 2974 O O   . HOH D 3 .   ? -6.231  0.360   38.400  1.00 43.67 ? 639 HOH A O   1 
HETATM 2975 O O   . HOH D 3 .   ? -7.350  -3.988  23.670  1.00 32.94 ? 640 HOH A O   1 
HETATM 2976 O O   . HOH D 3 .   ? 11.145  -4.742  24.106  1.00 32.98 ? 641 HOH A O   1 
HETATM 2977 O O   . HOH D 3 .   ? -0.566  -8.863  35.336  1.00 28.15 ? 642 HOH A O   1 
HETATM 2978 O O   . HOH D 3 .   ? -5.975  -2.748  12.990  1.00 38.11 ? 643 HOH A O   1 
HETATM 2979 O O   . HOH D 3 .   ? -5.777  -4.922  13.885  1.00 36.20 ? 644 HOH A O   1 
HETATM 2980 O O   . HOH D 3 .   ? 17.195  18.469  -1.328  1.00 54.85 ? 645 HOH A O   1 
HETATM 2981 O O   . HOH D 3 .   ? 3.095   -2.736  41.929  1.00 36.93 ? 646 HOH A O   1 
HETATM 2982 O O   . HOH D 3 .   ? 18.225  1.927   38.726  1.00 33.81 ? 647 HOH A O   1 
HETATM 2983 O O   . HOH D 3 .   ? 21.300  24.636  24.108  1.00 33.05 ? 648 HOH A O   1 
HETATM 2984 O O   . HOH D 3 .   ? 19.116  7.755   39.062  1.00 35.22 ? 649 HOH A O   1 
HETATM 2985 O O   . HOH D 3 .   ? 22.908  6.688   30.759  1.00 30.02 ? 650 HOH A O   1 
HETATM 2986 O O   . HOH D 3 .   ? 7.581   -4.535  37.200  1.00 27.17 ? 651 HOH A O   1 
HETATM 2987 O O   . HOH D 3 .   ? 16.689  -0.262  38.389  1.00 35.57 ? 652 HOH A O   1 
# 
