data_8VWM
# 
_entry.id   8VWM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8VWM         pdb_00008vwm 10.2210/pdb8vwm/pdb 
WWPDB D_1000281329 ?            ?                   
# 
_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       2025-02-05 
# 
_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                        8VWM 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yxf423@med.miami.edu 
_pdbx_contact_author.name_first         Yangbo 
_pdbx_contact_author.name_last          Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5894-9476 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Park, H.' 1 ? 
'Feng, Y.' 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                     
'A structural study of selectivity mechanisms for JNK3 and p38 alpha with indazole scaffold probing compounds' 
_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 'Park, H.' 1 ? 
primary 'Feng, Y.' 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 14' 42238.117 1   2.7.11.24 ? ? ? 
2 non-polymer syn 
'(4P)-4-{6-[(azetidin-1-yl)methyl]-5-(2-chloro-6-fluoroanilino)-1H-indazol-1-yl}-N-methylthiophene-2-carboxamide' 469.962   1   ? 
? ? ? 
3 non-polymer syn 'octyl beta-D-glucopyranoside' 292.369   2   ?         ? ? ? 
4 water       nat water 18.015    345 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'MAP kinase 14,MAPK 14,CRK1,Mitogen-activated protein kinase p38 alpha,MAP kinase p38 alpha' 
# 
_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       
;MAHHHHHHSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRELR
LLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKP
SNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLK
LILRLVGTPGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHD
PDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRELR
LLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKP
SNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLK
LILRLVGTPGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHD
PDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
;
_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 '(4P)-4-{6-[(azetidin-1-yl)methyl]-5-(2-chloro-6-fluoroanilino)-1H-indazol-1-yl}-N-methylthiophene-2-carboxamide' WHE 
3 'octyl beta-D-glucopyranoside'                                                                                    BOG 
4 water                                                                                                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   SER n 
1 10  GLN n 
1 11  GLU n 
1 12  ARG n 
1 13  PRO n 
1 14  THR n 
1 15  PHE n 
1 16  TYR n 
1 17  ARG n 
1 18  GLN n 
1 19  GLU n 
1 20  LEU n 
1 21  ASN n 
1 22  LYS n 
1 23  THR n 
1 24  ILE n 
1 25  TRP n 
1 26  GLU n 
1 27  VAL n 
1 28  PRO n 
1 29  GLU n 
1 30  ARG n 
1 31  TYR n 
1 32  GLN n 
1 33  ASN n 
1 34  LEU n 
1 35  SER n 
1 36  PRO n 
1 37  VAL n 
1 38  GLY n 
1 39  SER n 
1 40  GLY n 
1 41  ALA n 
1 42  TYR n 
1 43  GLY n 
1 44  SER n 
1 45  VAL n 
1 46  CYS n 
1 47  ALA n 
1 48  ALA n 
1 49  PHE n 
1 50  ASP n 
1 51  THR n 
1 52  LYS n 
1 53  THR n 
1 54  GLY n 
1 55  HIS n 
1 56  ARG n 
1 57  VAL n 
1 58  ALA n 
1 59  VAL n 
1 60  LYS n 
1 61  LYS n 
1 62  LEU n 
1 63  SER n 
1 64  ARG n 
1 65  PRO n 
1 66  PHE n 
1 67  GLN n 
1 68  SER n 
1 69  ILE n 
1 70  ILE n 
1 71  HIS n 
1 72  ALA n 
1 73  LYS n 
1 74  ARG n 
1 75  THR n 
1 76  TYR n 
1 77  ARG n 
1 78  GLU n 
1 79  LEU n 
1 80  ARG n 
1 81  LEU n 
1 82  LEU n 
1 83  LYS n 
1 84  HIS n 
1 85  MET n 
1 86  LYS n 
1 87  HIS n 
1 88  GLU n 
1 89  ASN n 
1 90  VAL n 
1 91  ILE n 
1 92  GLY n 
1 93  LEU n 
1 94  LEU n 
1 95  ASP n 
1 96  VAL n 
1 97  PHE n 
1 98  THR n 
1 99  PRO n 
1 100 ALA n 
1 101 ARG n 
1 102 SER n 
1 103 LEU n 
1 104 GLU n 
1 105 GLU n 
1 106 PHE n 
1 107 ASN n 
1 108 ASP n 
1 109 VAL n 
1 110 TYR n 
1 111 LEU n 
1 112 VAL n 
1 113 THR n 
1 114 HIS n 
1 115 LEU n 
1 116 MET n 
1 117 GLY n 
1 118 ALA n 
1 119 ASP n 
1 120 LEU n 
1 121 ASN n 
1 122 ASN n 
1 123 ILE n 
1 124 VAL n 
1 125 LYS n 
1 126 CYS n 
1 127 GLN n 
1 128 LYS n 
1 129 LEU n 
1 130 THR n 
1 131 ASP n 
1 132 ASP n 
1 133 HIS n 
1 134 VAL n 
1 135 GLN n 
1 136 PHE n 
1 137 LEU n 
1 138 ILE n 
1 139 TYR n 
1 140 GLN n 
1 141 ILE n 
1 142 LEU n 
1 143 ARG n 
1 144 GLY n 
1 145 LEU n 
1 146 LYS n 
1 147 TYR n 
1 148 ILE n 
1 149 HIS n 
1 150 SER n 
1 151 ALA n 
1 152 ASP n 
1 153 ILE n 
1 154 ILE n 
1 155 HIS n 
1 156 ARG n 
1 157 ASP n 
1 158 LEU n 
1 159 LYS n 
1 160 PRO n 
1 161 SER n 
1 162 ASN n 
1 163 LEU n 
1 164 ALA n 
1 165 VAL n 
1 166 ASN n 
1 167 GLU n 
1 168 ASP n 
1 169 CYS n 
1 170 GLU n 
1 171 LEU n 
1 172 LYS n 
1 173 ILE n 
1 174 LEU n 
1 175 ASP n 
1 176 PHE n 
1 177 GLY n 
1 178 LEU n 
1 179 ALA n 
1 180 ARG n 
1 181 HIS n 
1 182 THR n 
1 183 ASP n 
1 184 ASP n 
1 185 GLU n 
1 186 MET n 
1 187 THR n 
1 188 GLY n 
1 189 TYR n 
1 190 VAL n 
1 191 ALA n 
1 192 THR n 
1 193 ARG n 
1 194 TRP n 
1 195 TYR n 
1 196 ARG n 
1 197 ALA n 
1 198 PRO n 
1 199 GLU n 
1 200 ILE n 
1 201 MET n 
1 202 LEU n 
1 203 ASN n 
1 204 TRP n 
1 205 MET n 
1 206 HIS n 
1 207 TYR n 
1 208 ASN n 
1 209 GLN n 
1 210 THR n 
1 211 VAL n 
1 212 ASP n 
1 213 ILE n 
1 214 TRP n 
1 215 SER n 
1 216 VAL n 
1 217 GLY n 
1 218 CYS n 
1 219 ILE n 
1 220 MET n 
1 221 ALA n 
1 222 GLU n 
1 223 LEU n 
1 224 LEU n 
1 225 THR n 
1 226 GLY n 
1 227 ARG n 
1 228 THR n 
1 229 LEU n 
1 230 PHE n 
1 231 PRO n 
1 232 GLY n 
1 233 THR n 
1 234 ASP n 
1 235 HIS n 
1 236 ILE n 
1 237 ASP n 
1 238 GLN n 
1 239 LEU n 
1 240 LYS n 
1 241 LEU n 
1 242 ILE n 
1 243 LEU n 
1 244 ARG n 
1 245 LEU n 
1 246 VAL n 
1 247 GLY n 
1 248 THR n 
1 249 PRO n 
1 250 GLY n 
1 251 ALA n 
1 252 GLU n 
1 253 LEU n 
1 254 LEU n 
1 255 LYS n 
1 256 LYS n 
1 257 ILE n 
1 258 SER n 
1 259 SER n 
1 260 GLU n 
1 261 SER n 
1 262 ALA n 
1 263 ARG n 
1 264 ASN n 
1 265 TYR n 
1 266 ILE n 
1 267 GLN n 
1 268 SER n 
1 269 LEU n 
1 270 ALA n 
1 271 GLN n 
1 272 MET n 
1 273 PRO n 
1 274 LYS n 
1 275 MET n 
1 276 ASN n 
1 277 PHE n 
1 278 ALA n 
1 279 ASN n 
1 280 VAL n 
1 281 PHE n 
1 282 ILE n 
1 283 GLY n 
1 284 ALA n 
1 285 ASN n 
1 286 PRO n 
1 287 LEU n 
1 288 ALA n 
1 289 VAL n 
1 290 ASP n 
1 291 LEU n 
1 292 LEU n 
1 293 GLU n 
1 294 LYS n 
1 295 MET n 
1 296 LEU n 
1 297 VAL n 
1 298 LEU n 
1 299 ASP n 
1 300 SER n 
1 301 ASP n 
1 302 LYS n 
1 303 ARG n 
1 304 ILE n 
1 305 THR n 
1 306 ALA n 
1 307 ALA n 
1 308 GLN n 
1 309 ALA n 
1 310 LEU n 
1 311 ALA n 
1 312 HIS n 
1 313 ALA n 
1 314 TYR n 
1 315 PHE n 
1 316 ALA n 
1 317 GLN n 
1 318 TYR n 
1 319 HIS n 
1 320 ASP n 
1 321 PRO n 
1 322 ASP n 
1 323 ASP n 
1 324 GLU n 
1 325 PRO n 
1 326 VAL n 
1 327 ALA n 
1 328 ASP n 
1 329 PRO n 
1 330 TYR n 
1 331 ASP n 
1 332 GLN n 
1 333 SER n 
1 334 PHE n 
1 335 GLU n 
1 336 SER n 
1 337 ARG n 
1 338 ASP n 
1 339 LEU n 
1 340 LEU n 
1 341 ILE n 
1 342 ASP n 
1 343 GLU n 
1 344 TRP n 
1 345 LYS n 
1 346 SER n 
1 347 LEU n 
1 348 THR n 
1 349 TYR n 
1 350 ASP n 
1 351 GLU n 
1 352 VAL n 
1 353 ILE n 
1 354 SER n 
1 355 PHE n 
1 356 VAL n 
1 357 PRO n 
1 358 PRO n 
1 359 PRO n 
1 360 LEU n 
1 361 ASP n 
1 362 GLN n 
1 363 GLU n 
1 364 GLU n 
1 365 MET n 
1 366 GLU n 
1 367 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                   367 
_entity_src_gen.gene_src_common_name               'house mouse' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Mapk14, Crk1, Csbp1, Csbp2' 
_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      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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 
BOG D-saccharide        n 'octyl beta-D-glucopyranoside' 
'Beta-Octylglucoside; octyl beta-D-glucoside; octyl D-glucoside; octyl glucoside' 'C14 H28 O6'          292.369 
CYS 'L-peptide linking' y CYSTEINE ?                                                                                 
'C3 H7 N O2 S'        121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                                                                                 
'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                                                                                 
'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE ?                                                                                 'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE ?                                                                                 
'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER ?                                                                                 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                                                                                 
'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE ?                                                                                 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE ?                                                                                 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE ?                                                                                 
'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                                                                                 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE ?                                                                                 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE ?                                                                                 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE ?                                                                                 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                                                                                 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE ?                                                                                 'C9 H11 N O3' 
181.189 
VAL 'L-peptide linking' y VALINE ?                                                                                 'C5 H11 N O2' 
117.146 
WHE non-polymer         . 
'(4P)-4-{6-[(azetidin-1-yl)methyl]-5-(2-chloro-6-fluoroanilino)-1H-indazol-1-yl}-N-methylthiophene-2-carboxamide' ? 
'C23 H21 Cl F N5 O S' 469.962 
# 
_pdbx_chem_comp_identifier.comp_id           BOG 
_pdbx_chem_comp_identifier.type              'IUPAC CARBOHYDRATE SYMBOL' 
_pdbx_chem_comp_identifier.program           PDB-CARE 
_pdbx_chem_comp_identifier.program_version   1.0 
_pdbx_chem_comp_identifier.identifier        b-octylglucoside 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -6  ?   ?   ?   A . n 
A 1 2   ALA 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   HIS 8   1   ?   ?   ?   A . n 
A 1 9   SER 9   2   ?   ?   ?   A . n 
A 1 10  GLN 10  3   ?   ?   ?   A . n 
A 1 11  GLU 11  4   ?   ?   ?   A . n 
A 1 12  ARG 12  5   5   ARG ARG A . n 
A 1 13  PRO 13  6   6   PRO PRO A . n 
A 1 14  THR 14  7   7   THR THR A . n 
A 1 15  PHE 15  8   8   PHE PHE A . n 
A 1 16  TYR 16  9   9   TYR TYR A . n 
A 1 17  ARG 17  10  10  ARG ARG A . n 
A 1 18  GLN 18  11  11  GLN GLN A . n 
A 1 19  GLU 19  12  12  GLU GLU A . n 
A 1 20  LEU 20  13  13  LEU LEU A . n 
A 1 21  ASN 21  14  14  ASN ASN A . n 
A 1 22  LYS 22  15  15  LYS LYS A . n 
A 1 23  THR 23  16  16  THR THR A . n 
A 1 24  ILE 24  17  17  ILE ILE A . n 
A 1 25  TRP 25  18  18  TRP TRP A . n 
A 1 26  GLU 26  19  19  GLU GLU A . n 
A 1 27  VAL 27  20  20  VAL VAL A . n 
A 1 28  PRO 28  21  21  PRO PRO A . n 
A 1 29  GLU 29  22  22  GLU GLU A . n 
A 1 30  ARG 30  23  23  ARG ARG A . n 
A 1 31  TYR 31  24  24  TYR TYR A . n 
A 1 32  GLN 32  25  25  GLN GLN A . n 
A 1 33  ASN 33  26  26  ASN ASN A . n 
A 1 34  LEU 34  27  27  LEU LEU A . n 
A 1 35  SER 35  28  28  SER SER A . n 
A 1 36  PRO 36  29  29  PRO PRO A . n 
A 1 37  VAL 37  30  30  VAL VAL A . n 
A 1 38  GLY 38  31  31  GLY GLY A . n 
A 1 39  SER 39  32  32  SER SER A . n 
A 1 40  GLY 40  33  33  GLY GLY A . n 
A 1 41  ALA 41  34  34  ALA ALA A . n 
A 1 42  TYR 42  35  35  TYR TYR A . n 
A 1 43  GLY 43  36  36  GLY GLY A . n 
A 1 44  SER 44  37  37  SER SER A . n 
A 1 45  VAL 45  38  38  VAL VAL A . n 
A 1 46  CYS 46  39  39  CYS CYS A . n 
A 1 47  ALA 47  40  40  ALA ALA A . n 
A 1 48  ALA 48  41  41  ALA ALA A . n 
A 1 49  PHE 49  42  42  PHE PHE A . n 
A 1 50  ASP 50  43  43  ASP ASP A . n 
A 1 51  THR 51  44  44  THR THR A . n 
A 1 52  LYS 52  45  45  LYS LYS A . n 
A 1 53  THR 53  46  46  THR THR A . n 
A 1 54  GLY 54  47  47  GLY GLY A . n 
A 1 55  HIS 55  48  48  HIS HIS A . n 
A 1 56  ARG 56  49  49  ARG ARG A . n 
A 1 57  VAL 57  50  50  VAL VAL A . n 
A 1 58  ALA 58  51  51  ALA ALA A . n 
A 1 59  VAL 59  52  52  VAL VAL A . n 
A 1 60  LYS 60  53  53  LYS LYS A . n 
A 1 61  LYS 61  54  54  LYS LYS A . n 
A 1 62  LEU 62  55  55  LEU LEU A . n 
A 1 63  SER 63  56  56  SER SER A . n 
A 1 64  ARG 64  57  57  ARG ARG A . n 
A 1 65  PRO 65  58  58  PRO PRO A . n 
A 1 66  PHE 66  59  59  PHE PHE A . n 
A 1 67  GLN 67  60  60  GLN GLN A . n 
A 1 68  SER 68  61  61  SER SER A . n 
A 1 69  ILE 69  62  62  ILE ILE A . n 
A 1 70  ILE 70  63  63  ILE ILE A . n 
A 1 71  HIS 71  64  64  HIS HIS A . n 
A 1 72  ALA 72  65  65  ALA ALA A . n 
A 1 73  LYS 73  66  66  LYS LYS A . n 
A 1 74  ARG 74  67  67  ARG ARG A . n 
A 1 75  THR 75  68  68  THR THR A . n 
A 1 76  TYR 76  69  69  TYR TYR A . n 
A 1 77  ARG 77  70  70  ARG ARG A . n 
A 1 78  GLU 78  71  71  GLU GLU A . n 
A 1 79  LEU 79  72  72  LEU LEU A . n 
A 1 80  ARG 80  73  73  ARG ARG A . n 
A 1 81  LEU 81  74  74  LEU LEU A . n 
A 1 82  LEU 82  75  75  LEU LEU A . n 
A 1 83  LYS 83  76  76  LYS LYS A . n 
A 1 84  HIS 84  77  77  HIS HIS A . n 
A 1 85  MET 85  78  78  MET MET A . n 
A 1 86  LYS 86  79  79  LYS LYS A . n 
A 1 87  HIS 87  80  80  HIS HIS A . n 
A 1 88  GLU 88  81  81  GLU GLU A . n 
A 1 89  ASN 89  82  82  ASN ASN A . n 
A 1 90  VAL 90  83  83  VAL VAL A . n 
A 1 91  ILE 91  84  84  ILE ILE A . n 
A 1 92  GLY 92  85  85  GLY GLY A . n 
A 1 93  LEU 93  86  86  LEU LEU A . n 
A 1 94  LEU 94  87  87  LEU LEU A . n 
A 1 95  ASP 95  88  88  ASP ASP A . n 
A 1 96  VAL 96  89  89  VAL VAL A . n 
A 1 97  PHE 97  90  90  PHE PHE A . n 
A 1 98  THR 98  91  91  THR THR A . n 
A 1 99  PRO 99  92  92  PRO PRO A . n 
A 1 100 ALA 100 93  93  ALA ALA A . n 
A 1 101 ARG 101 94  94  ARG ARG A . n 
A 1 102 SER 102 95  95  SER SER A . n 
A 1 103 LEU 103 96  96  LEU LEU A . n 
A 1 104 GLU 104 97  97  GLU GLU A . n 
A 1 105 GLU 105 98  98  GLU GLU A . n 
A 1 106 PHE 106 99  99  PHE PHE A . n 
A 1 107 ASN 107 100 100 ASN ASN A . n 
A 1 108 ASP 108 101 101 ASP ASP A . n 
A 1 109 VAL 109 102 102 VAL VAL A . n 
A 1 110 TYR 110 103 103 TYR TYR A . n 
A 1 111 LEU 111 104 104 LEU LEU A . n 
A 1 112 VAL 112 105 105 VAL VAL A . n 
A 1 113 THR 113 106 106 THR THR A . n 
A 1 114 HIS 114 107 107 HIS HIS A . n 
A 1 115 LEU 115 108 108 LEU LEU A . n 
A 1 116 MET 116 109 109 MET MET A . n 
A 1 117 GLY 117 110 110 GLY GLY A . n 
A 1 118 ALA 118 111 111 ALA ALA A . n 
A 1 119 ASP 119 112 112 ASP ASP A . n 
A 1 120 LEU 120 113 113 LEU LEU A . n 
A 1 121 ASN 121 114 114 ASN ASN A . n 
A 1 122 ASN 122 115 115 ASN ASN A . n 
A 1 123 ILE 123 116 116 ILE ILE A . n 
A 1 124 VAL 124 117 117 VAL VAL A . n 
A 1 125 LYS 125 118 118 LYS LYS A . n 
A 1 126 CYS 126 119 119 CYS CYS A . n 
A 1 127 GLN 127 120 120 GLN GLN A . n 
A 1 128 LYS 128 121 121 LYS LYS A . n 
A 1 129 LEU 129 122 122 LEU LEU A . n 
A 1 130 THR 130 123 123 THR THR A . n 
A 1 131 ASP 131 124 124 ASP ASP A . n 
A 1 132 ASP 132 125 125 ASP ASP A . n 
A 1 133 HIS 133 126 126 HIS HIS A . n 
A 1 134 VAL 134 127 127 VAL VAL A . n 
A 1 135 GLN 135 128 128 GLN GLN A . n 
A 1 136 PHE 136 129 129 PHE PHE A . n 
A 1 137 LEU 137 130 130 LEU LEU A . n 
A 1 138 ILE 138 131 131 ILE ILE A . n 
A 1 139 TYR 139 132 132 TYR TYR A . n 
A 1 140 GLN 140 133 133 GLN GLN A . n 
A 1 141 ILE 141 134 134 ILE ILE A . n 
A 1 142 LEU 142 135 135 LEU LEU A . n 
A 1 143 ARG 143 136 136 ARG ARG A . n 
A 1 144 GLY 144 137 137 GLY GLY A . n 
A 1 145 LEU 145 138 138 LEU LEU A . n 
A 1 146 LYS 146 139 139 LYS LYS A . n 
A 1 147 TYR 147 140 140 TYR TYR A . n 
A 1 148 ILE 148 141 141 ILE ILE A . n 
A 1 149 HIS 149 142 142 HIS HIS A . n 
A 1 150 SER 150 143 143 SER SER A . n 
A 1 151 ALA 151 144 144 ALA ALA A . n 
A 1 152 ASP 152 145 145 ASP ASP A . n 
A 1 153 ILE 153 146 146 ILE ILE A . n 
A 1 154 ILE 154 147 147 ILE ILE A . n 
A 1 155 HIS 155 148 148 HIS HIS A . n 
A 1 156 ARG 156 149 149 ARG ARG A . n 
A 1 157 ASP 157 150 150 ASP ASP A . n 
A 1 158 LEU 158 151 151 LEU LEU A . n 
A 1 159 LYS 159 152 152 LYS LYS A . n 
A 1 160 PRO 160 153 153 PRO PRO A . n 
A 1 161 SER 161 154 154 SER SER A . n 
A 1 162 ASN 162 155 155 ASN ASN A . n 
A 1 163 LEU 163 156 156 LEU LEU A . n 
A 1 164 ALA 164 157 157 ALA ALA A . n 
A 1 165 VAL 165 158 158 VAL VAL A . n 
A 1 166 ASN 166 159 159 ASN ASN A . n 
A 1 167 GLU 167 160 160 GLU GLU A . n 
A 1 168 ASP 168 161 161 ASP ASP A . n 
A 1 169 CYS 169 162 162 CYS CYS A . n 
A 1 170 GLU 170 163 163 GLU GLU A . n 
A 1 171 LEU 171 164 164 LEU LEU A . n 
A 1 172 LYS 172 165 165 LYS LYS A . n 
A 1 173 ILE 173 166 166 ILE ILE A . n 
A 1 174 LEU 174 167 167 LEU LEU A . n 
A 1 175 ASP 175 168 168 ASP ASP A . n 
A 1 176 PHE 176 169 169 PHE PHE A . n 
A 1 177 GLY 177 170 170 GLY GLY A . n 
A 1 178 LEU 178 171 171 LEU LEU A . n 
A 1 179 ALA 179 172 172 ALA ALA A . n 
A 1 180 ARG 180 173 173 ARG ARG A . n 
A 1 181 HIS 181 174 174 HIS HIS A . n 
A 1 182 THR 182 175 ?   ?   ?   A . n 
A 1 183 ASP 183 176 ?   ?   ?   A . n 
A 1 184 ASP 184 177 ?   ?   ?   A . n 
A 1 185 GLU 185 178 ?   ?   ?   A . n 
A 1 186 MET 186 179 ?   ?   ?   A . n 
A 1 187 THR 187 180 ?   ?   ?   A . n 
A 1 188 GLY 188 181 ?   ?   ?   A . n 
A 1 189 TYR 189 182 ?   ?   ?   A . n 
A 1 190 VAL 190 183 183 VAL VAL A . n 
A 1 191 ALA 191 184 184 ALA ALA A . n 
A 1 192 THR 192 185 185 THR THR A . n 
A 1 193 ARG 193 186 186 ARG ARG A . n 
A 1 194 TRP 194 187 187 TRP TRP A . n 
A 1 195 TYR 195 188 188 TYR TYR A . n 
A 1 196 ARG 196 189 189 ARG ARG A . n 
A 1 197 ALA 197 190 190 ALA ALA A . n 
A 1 198 PRO 198 191 191 PRO PRO A . n 
A 1 199 GLU 199 192 192 GLU GLU A . n 
A 1 200 ILE 200 193 193 ILE ILE A . n 
A 1 201 MET 201 194 194 MET MET A . n 
A 1 202 LEU 202 195 195 LEU LEU A . n 
A 1 203 ASN 203 196 196 ASN ASN A . n 
A 1 204 TRP 204 197 197 TRP TRP A . n 
A 1 205 MET 205 198 198 MET MET A . n 
A 1 206 HIS 206 199 199 HIS HIS A . n 
A 1 207 TYR 207 200 200 TYR TYR A . n 
A 1 208 ASN 208 201 201 ASN ASN A . n 
A 1 209 GLN 209 202 202 GLN GLN A . n 
A 1 210 THR 210 203 203 THR THR A . n 
A 1 211 VAL 211 204 204 VAL VAL A . n 
A 1 212 ASP 212 205 205 ASP ASP A . n 
A 1 213 ILE 213 206 206 ILE ILE A . n 
A 1 214 TRP 214 207 207 TRP TRP A . n 
A 1 215 SER 215 208 208 SER SER A . n 
A 1 216 VAL 216 209 209 VAL VAL A . n 
A 1 217 GLY 217 210 210 GLY GLY A . n 
A 1 218 CYS 218 211 211 CYS CYS A . n 
A 1 219 ILE 219 212 212 ILE ILE A . n 
A 1 220 MET 220 213 213 MET MET A . n 
A 1 221 ALA 221 214 214 ALA ALA A . n 
A 1 222 GLU 222 215 215 GLU GLU A . n 
A 1 223 LEU 223 216 216 LEU LEU A . n 
A 1 224 LEU 224 217 217 LEU LEU A . n 
A 1 225 THR 225 218 218 THR THR A . n 
A 1 226 GLY 226 219 219 GLY GLY A . n 
A 1 227 ARG 227 220 220 ARG ARG A . n 
A 1 228 THR 228 221 221 THR THR A . n 
A 1 229 LEU 229 222 222 LEU LEU A . n 
A 1 230 PHE 230 223 223 PHE PHE A . n 
A 1 231 PRO 231 224 224 PRO PRO A . n 
A 1 232 GLY 232 225 225 GLY GLY A . n 
A 1 233 THR 233 226 226 THR THR A . n 
A 1 234 ASP 234 227 227 ASP ASP A . n 
A 1 235 HIS 235 228 228 HIS HIS A . n 
A 1 236 ILE 236 229 229 ILE ILE A . n 
A 1 237 ASP 237 230 230 ASP ASP A . n 
A 1 238 GLN 238 231 231 GLN GLN A . n 
A 1 239 LEU 239 232 232 LEU LEU A . n 
A 1 240 LYS 240 233 233 LYS LYS A . n 
A 1 241 LEU 241 234 234 LEU LEU A . n 
A 1 242 ILE 242 235 235 ILE ILE A . n 
A 1 243 LEU 243 236 236 LEU LEU A . n 
A 1 244 ARG 244 237 237 ARG ARG A . n 
A 1 245 LEU 245 238 238 LEU LEU A . n 
A 1 246 VAL 246 239 239 VAL VAL A . n 
A 1 247 GLY 247 240 240 GLY GLY A . n 
A 1 248 THR 248 241 241 THR THR A . n 
A 1 249 PRO 249 242 242 PRO PRO A . n 
A 1 250 GLY 250 243 243 GLY GLY A . n 
A 1 251 ALA 251 244 244 ALA ALA A . n 
A 1 252 GLU 252 245 245 GLU GLU A . n 
A 1 253 LEU 253 246 246 LEU LEU A . n 
A 1 254 LEU 254 247 247 LEU LEU A . n 
A 1 255 LYS 255 248 248 LYS LYS A . n 
A 1 256 LYS 256 249 249 LYS LYS A . n 
A 1 257 ILE 257 250 250 ILE ILE A . n 
A 1 258 SER 258 251 251 SER SER A . n 
A 1 259 SER 259 252 252 SER SER A . n 
A 1 260 GLU 260 253 253 GLU GLU A . n 
A 1 261 SER 261 254 254 SER SER A . n 
A 1 262 ALA 262 255 255 ALA ALA A . n 
A 1 263 ARG 263 256 256 ARG ARG A . n 
A 1 264 ASN 264 257 257 ASN ASN A . n 
A 1 265 TYR 265 258 258 TYR TYR A . n 
A 1 266 ILE 266 259 259 ILE ILE A . n 
A 1 267 GLN 267 260 260 GLN GLN A . n 
A 1 268 SER 268 261 261 SER SER A . n 
A 1 269 LEU 269 262 262 LEU LEU A . n 
A 1 270 ALA 270 263 263 ALA ALA A . n 
A 1 271 GLN 271 264 264 GLN GLN A . n 
A 1 272 MET 272 265 265 MET MET A . n 
A 1 273 PRO 273 266 266 PRO PRO A . n 
A 1 274 LYS 274 267 267 LYS LYS A . n 
A 1 275 MET 275 268 268 MET MET A . n 
A 1 276 ASN 276 269 269 ASN ASN A . n 
A 1 277 PHE 277 270 270 PHE PHE A . n 
A 1 278 ALA 278 271 271 ALA ALA A . n 
A 1 279 ASN 279 272 272 ASN ASN A . n 
A 1 280 VAL 280 273 273 VAL VAL A . n 
A 1 281 PHE 281 274 274 PHE PHE A . n 
A 1 282 ILE 282 275 275 ILE ILE A . n 
A 1 283 GLY 283 276 276 GLY GLY A . n 
A 1 284 ALA 284 277 277 ALA ALA A . n 
A 1 285 ASN 285 278 278 ASN ASN A . n 
A 1 286 PRO 286 279 279 PRO PRO A . n 
A 1 287 LEU 287 280 280 LEU LEU A . n 
A 1 288 ALA 288 281 281 ALA ALA A . n 
A 1 289 VAL 289 282 282 VAL VAL A . n 
A 1 290 ASP 290 283 283 ASP ASP A . n 
A 1 291 LEU 291 284 284 LEU LEU A . n 
A 1 292 LEU 292 285 285 LEU LEU A . n 
A 1 293 GLU 293 286 286 GLU GLU A . n 
A 1 294 LYS 294 287 287 LYS LYS A . n 
A 1 295 MET 295 288 288 MET MET A . n 
A 1 296 LEU 296 289 289 LEU LEU A . n 
A 1 297 VAL 297 290 290 VAL VAL A . n 
A 1 298 LEU 298 291 291 LEU LEU A . n 
A 1 299 ASP 299 292 292 ASP ASP A . n 
A 1 300 SER 300 293 293 SER SER A . n 
A 1 301 ASP 301 294 294 ASP ASP A . n 
A 1 302 LYS 302 295 295 LYS LYS A . n 
A 1 303 ARG 303 296 296 ARG ARG A . n 
A 1 304 ILE 304 297 297 ILE ILE A . n 
A 1 305 THR 305 298 298 THR THR A . n 
A 1 306 ALA 306 299 299 ALA ALA A . n 
A 1 307 ALA 307 300 300 ALA ALA A . n 
A 1 308 GLN 308 301 301 GLN GLN A . n 
A 1 309 ALA 309 302 302 ALA ALA A . n 
A 1 310 LEU 310 303 303 LEU LEU A . n 
A 1 311 ALA 311 304 304 ALA ALA A . n 
A 1 312 HIS 312 305 305 HIS HIS A . n 
A 1 313 ALA 313 306 306 ALA ALA A . n 
A 1 314 TYR 314 307 307 TYR TYR A . n 
A 1 315 PHE 315 308 308 PHE PHE A . n 
A 1 316 ALA 316 309 309 ALA ALA A . n 
A 1 317 GLN 317 310 310 GLN GLN A . n 
A 1 318 TYR 318 311 311 TYR TYR A . n 
A 1 319 HIS 319 312 312 HIS HIS A . n 
A 1 320 ASP 320 313 313 ASP ASP A . n 
A 1 321 PRO 321 314 314 PRO PRO A . n 
A 1 322 ASP 322 315 315 ASP ASP A . n 
A 1 323 ASP 323 316 316 ASP ASP A . n 
A 1 324 GLU 324 317 317 GLU GLU A . n 
A 1 325 PRO 325 318 318 PRO PRO A . n 
A 1 326 VAL 326 319 319 VAL VAL A . n 
A 1 327 ALA 327 320 320 ALA ALA A . n 
A 1 328 ASP 328 321 321 ASP ASP A . n 
A 1 329 PRO 329 322 322 PRO PRO A . n 
A 1 330 TYR 330 323 323 TYR TYR A . n 
A 1 331 ASP 331 324 324 ASP ASP A . n 
A 1 332 GLN 332 325 325 GLN GLN A . n 
A 1 333 SER 333 326 326 SER SER A . n 
A 1 334 PHE 334 327 327 PHE PHE A . n 
A 1 335 GLU 335 328 328 GLU GLU A . n 
A 1 336 SER 336 329 329 SER SER A . n 
A 1 337 ARG 337 330 330 ARG ARG A . n 
A 1 338 ASP 338 331 331 ASP ASP A . n 
A 1 339 LEU 339 332 332 LEU LEU A . n 
A 1 340 LEU 340 333 333 LEU LEU A . n 
A 1 341 ILE 341 334 334 ILE ILE A . n 
A 1 342 ASP 342 335 335 ASP ASP A . n 
A 1 343 GLU 343 336 336 GLU GLU A . n 
A 1 344 TRP 344 337 337 TRP TRP A . n 
A 1 345 LYS 345 338 338 LYS LYS A . n 
A 1 346 SER 346 339 339 SER SER A . n 
A 1 347 LEU 347 340 340 LEU LEU A . n 
A 1 348 THR 348 341 341 THR THR A . n 
A 1 349 TYR 349 342 342 TYR TYR A . n 
A 1 350 ASP 350 343 343 ASP ASP A . n 
A 1 351 GLU 351 344 344 GLU GLU A . n 
A 1 352 VAL 352 345 345 VAL VAL A . n 
A 1 353 ILE 353 346 346 ILE ILE A . n 
A 1 354 SER 354 347 347 SER SER A . n 
A 1 355 PHE 355 348 348 PHE PHE A . n 
A 1 356 VAL 356 349 349 VAL VAL A . n 
A 1 357 PRO 357 350 350 PRO PRO A . n 
A 1 358 PRO 358 351 351 PRO PRO A . n 
A 1 359 PRO 359 352 352 PRO PRO A . n 
A 1 360 LEU 360 353 353 LEU LEU A . n 
A 1 361 ASP 361 354 354 ASP ASP A . n 
A 1 362 GLN 362 355 355 GLN GLN A . n 
A 1 363 GLU 363 356 356 GLU GLU A . n 
A 1 364 GLU 364 357 357 GLU GLU A . n 
A 1 365 MET 365 358 358 MET MET A . n 
A 1 366 GLU 366 359 359 GLU GLU A . n 
A 1 367 SER 367 360 360 SER SER A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WHE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WHE 
_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 WHE 1   401 401 WHE 21G A . 
C 3 BOG 1   402 501 BOG BOG A . 
D 3 BOG 1   403 601 BOG BOG A . 
E 4 HOH 1   501 328 HOH HOH A . 
E 4 HOH 2   502 260 HOH HOH A . 
E 4 HOH 3   503 220 HOH HOH A . 
E 4 HOH 4   504 274 HOH HOH A . 
E 4 HOH 5   505 194 HOH HOH A . 
E 4 HOH 6   506 144 HOH HOH A . 
E 4 HOH 7   507 286 HOH HOH A . 
E 4 HOH 8   508 267 HOH HOH A . 
E 4 HOH 9   509 157 HOH HOH A . 
E 4 HOH 10  510 227 HOH HOH A . 
E 4 HOH 11  511 68  HOH HOH A . 
E 4 HOH 12  512 46  HOH HOH A . 
E 4 HOH 13  513 141 HOH HOH A . 
E 4 HOH 14  514 69  HOH HOH A . 
E 4 HOH 15  515 9   HOH HOH A . 
E 4 HOH 16  516 361 HOH HOH A . 
E 4 HOH 17  517 228 HOH HOH A . 
E 4 HOH 18  518 126 HOH HOH A . 
E 4 HOH 19  519 308 HOH HOH A . 
E 4 HOH 20  520 305 HOH HOH A . 
E 4 HOH 21  521 355 HOH HOH A . 
E 4 HOH 22  522 104 HOH HOH A . 
E 4 HOH 23  523 129 HOH HOH A . 
E 4 HOH 24  524 21  HOH HOH A . 
E 4 HOH 25  525 258 HOH HOH A . 
E 4 HOH 26  526 257 HOH HOH A . 
E 4 HOH 27  527 88  HOH HOH A . 
E 4 HOH 28  528 139 HOH HOH A . 
E 4 HOH 29  529 322 HOH HOH A . 
E 4 HOH 30  530 115 HOH HOH A . 
E 4 HOH 31  531 128 HOH HOH A . 
E 4 HOH 32  532 38  HOH HOH A . 
E 4 HOH 33  533 114 HOH HOH A . 
E 4 HOH 34  534 191 HOH HOH A . 
E 4 HOH 35  535 294 HOH HOH A . 
E 4 HOH 36  536 121 HOH HOH A . 
E 4 HOH 37  537 22  HOH HOH A . 
E 4 HOH 38  538 264 HOH HOH A . 
E 4 HOH 39  539 158 HOH HOH A . 
E 4 HOH 40  540 64  HOH HOH A . 
E 4 HOH 41  541 4   HOH HOH A . 
E 4 HOH 42  542 98  HOH HOH A . 
E 4 HOH 43  543 113 HOH HOH A . 
E 4 HOH 44  544 155 HOH HOH A . 
E 4 HOH 45  545 329 HOH HOH A . 
E 4 HOH 46  546 161 HOH HOH A . 
E 4 HOH 47  547 57  HOH HOH A . 
E 4 HOH 48  548 19  HOH HOH A . 
E 4 HOH 49  549 28  HOH HOH A . 
E 4 HOH 50  550 13  HOH HOH A . 
E 4 HOH 51  551 241 HOH HOH A . 
E 4 HOH 52  552 148 HOH HOH A . 
E 4 HOH 53  553 31  HOH HOH A . 
E 4 HOH 54  554 310 HOH HOH A . 
E 4 HOH 55  555 122 HOH HOH A . 
E 4 HOH 56  556 15  HOH HOH A . 
E 4 HOH 57  557 248 HOH HOH A . 
E 4 HOH 58  558 190 HOH HOH A . 
E 4 HOH 59  559 83  HOH HOH A . 
E 4 HOH 60  560 263 HOH HOH A . 
E 4 HOH 61  561 91  HOH HOH A . 
E 4 HOH 62  562 342 HOH HOH A . 
E 4 HOH 63  563 102 HOH HOH A . 
E 4 HOH 64  564 283 HOH HOH A . 
E 4 HOH 65  565 238 HOH HOH A . 
E 4 HOH 66  566 184 HOH HOH A . 
E 4 HOH 67  567 11  HOH HOH A . 
E 4 HOH 68  568 319 HOH HOH A . 
E 4 HOH 69  569 60  HOH HOH A . 
E 4 HOH 70  570 218 HOH HOH A . 
E 4 HOH 71  571 23  HOH HOH A . 
E 4 HOH 72  572 59  HOH HOH A . 
E 4 HOH 73  573 100 HOH HOH A . 
E 4 HOH 74  574 124 HOH HOH A . 
E 4 HOH 75  575 256 HOH HOH A . 
E 4 HOH 76  576 108 HOH HOH A . 
E 4 HOH 77  577 117 HOH HOH A . 
E 4 HOH 78  578 75  HOH HOH A . 
E 4 HOH 79  579 145 HOH HOH A . 
E 4 HOH 80  580 55  HOH HOH A . 
E 4 HOH 81  581 170 HOH HOH A . 
E 4 HOH 82  582 101 HOH HOH A . 
E 4 HOH 83  583 105 HOH HOH A . 
E 4 HOH 84  584 270 HOH HOH A . 
E 4 HOH 85  585 334 HOH HOH A . 
E 4 HOH 86  586 247 HOH HOH A . 
E 4 HOH 87  587 311 HOH HOH A . 
E 4 HOH 88  588 315 HOH HOH A . 
E 4 HOH 89  589 47  HOH HOH A . 
E 4 HOH 90  590 281 HOH HOH A . 
E 4 HOH 91  591 245 HOH HOH A . 
E 4 HOH 92  592 44  HOH HOH A . 
E 4 HOH 93  593 67  HOH HOH A . 
E 4 HOH 94  594 211 HOH HOH A . 
E 4 HOH 95  595 78  HOH HOH A . 
E 4 HOH 96  596 26  HOH HOH A . 
E 4 HOH 97  597 187 HOH HOH A . 
E 4 HOH 98  598 74  HOH HOH A . 
E 4 HOH 99  599 171 HOH HOH A . 
E 4 HOH 100 600 37  HOH HOH A . 
E 4 HOH 101 601 77  HOH HOH A . 
E 4 HOH 102 602 172 HOH HOH A . 
E 4 HOH 103 603 204 HOH HOH A . 
E 4 HOH 104 604 16  HOH HOH A . 
E 4 HOH 105 605 97  HOH HOH A . 
E 4 HOH 106 606 95  HOH HOH A . 
E 4 HOH 107 607 156 HOH HOH A . 
E 4 HOH 108 608 41  HOH HOH A . 
E 4 HOH 109 609 5   HOH HOH A . 
E 4 HOH 110 610 303 HOH HOH A . 
E 4 HOH 111 611 66  HOH HOH A . 
E 4 HOH 112 612 133 HOH HOH A . 
E 4 HOH 113 613 169 HOH HOH A . 
E 4 HOH 114 614 61  HOH HOH A . 
E 4 HOH 115 615 25  HOH HOH A . 
E 4 HOH 116 616 3   HOH HOH A . 
E 4 HOH 117 617 73  HOH HOH A . 
E 4 HOH 118 618 312 HOH HOH A . 
E 4 HOH 119 619 49  HOH HOH A . 
E 4 HOH 120 620 40  HOH HOH A . 
E 4 HOH 121 621 32  HOH HOH A . 
E 4 HOH 122 622 1   HOH HOH A . 
E 4 HOH 123 623 360 HOH HOH A . 
E 4 HOH 124 624 255 HOH HOH A . 
E 4 HOH 125 625 182 HOH HOH A . 
E 4 HOH 126 626 103 HOH HOH A . 
E 4 HOH 127 627 269 HOH HOH A . 
E 4 HOH 128 628 152 HOH HOH A . 
E 4 HOH 129 629 317 HOH HOH A . 
E 4 HOH 130 630 71  HOH HOH A . 
E 4 HOH 131 631 39  HOH HOH A . 
E 4 HOH 132 632 192 HOH HOH A . 
E 4 HOH 133 633 7   HOH HOH A . 
E 4 HOH 134 634 143 HOH HOH A . 
E 4 HOH 135 635 24  HOH HOH A . 
E 4 HOH 136 636 318 HOH HOH A . 
E 4 HOH 137 637 76  HOH HOH A . 
E 4 HOH 138 638 212 HOH HOH A . 
E 4 HOH 139 639 340 HOH HOH A . 
E 4 HOH 140 640 119 HOH HOH A . 
E 4 HOH 141 641 51  HOH HOH A . 
E 4 HOH 142 642 291 HOH HOH A . 
E 4 HOH 143 643 30  HOH HOH A . 
E 4 HOH 144 644 276 HOH HOH A . 
E 4 HOH 145 645 2   HOH HOH A . 
E 4 HOH 146 646 8   HOH HOH A . 
E 4 HOH 147 647 222 HOH HOH A . 
E 4 HOH 148 648 206 HOH HOH A . 
E 4 HOH 149 649 43  HOH HOH A . 
E 4 HOH 150 650 368 HOH HOH A . 
E 4 HOH 151 651 300 HOH HOH A . 
E 4 HOH 152 652 65  HOH HOH A . 
E 4 HOH 153 653 53  HOH HOH A . 
E 4 HOH 154 654 12  HOH HOH A . 
E 4 HOH 155 655 250 HOH HOH A . 
E 4 HOH 156 656 14  HOH HOH A . 
E 4 HOH 157 657 336 HOH HOH A . 
E 4 HOH 158 658 89  HOH HOH A . 
E 4 HOH 159 659 175 HOH HOH A . 
E 4 HOH 160 660 50  HOH HOH A . 
E 4 HOH 161 661 106 HOH HOH A . 
E 4 HOH 162 662 52  HOH HOH A . 
E 4 HOH 163 663 96  HOH HOH A . 
E 4 HOH 164 664 235 HOH HOH A . 
E 4 HOH 165 665 331 HOH HOH A . 
E 4 HOH 166 666 354 HOH HOH A . 
E 4 HOH 167 667 146 HOH HOH A . 
E 4 HOH 168 668 70  HOH HOH A . 
E 4 HOH 169 669 10  HOH HOH A . 
E 4 HOH 170 670 345 HOH HOH A . 
E 4 HOH 171 671 29  HOH HOH A . 
E 4 HOH 172 672 20  HOH HOH A . 
E 4 HOH 173 673 93  HOH HOH A . 
E 4 HOH 174 674 243 HOH HOH A . 
E 4 HOH 175 675 34  HOH HOH A . 
E 4 HOH 176 676 231 HOH HOH A . 
E 4 HOH 177 677 27  HOH HOH A . 
E 4 HOH 178 678 127 HOH HOH A . 
E 4 HOH 179 679 352 HOH HOH A . 
E 4 HOH 180 680 118 HOH HOH A . 
E 4 HOH 181 681 45  HOH HOH A . 
E 4 HOH 182 682 85  HOH HOH A . 
E 4 HOH 183 683 225 HOH HOH A . 
E 4 HOH 184 684 282 HOH HOH A . 
E 4 HOH 185 685 216 HOH HOH A . 
E 4 HOH 186 686 266 HOH HOH A . 
E 4 HOH 187 687 335 HOH HOH A . 
E 4 HOH 188 688 232 HOH HOH A . 
E 4 HOH 189 689 63  HOH HOH A . 
E 4 HOH 190 690 237 HOH HOH A . 
E 4 HOH 191 691 163 HOH HOH A . 
E 4 HOH 192 692 109 HOH HOH A . 
E 4 HOH 193 693 357 HOH HOH A . 
E 4 HOH 194 694 48  HOH HOH A . 
E 4 HOH 195 695 56  HOH HOH A . 
E 4 HOH 196 696 99  HOH HOH A . 
E 4 HOH 197 697 131 HOH HOH A . 
E 4 HOH 198 698 316 HOH HOH A . 
E 4 HOH 199 699 150 HOH HOH A . 
E 4 HOH 200 700 42  HOH HOH A . 
E 4 HOH 201 701 207 HOH HOH A . 
E 4 HOH 202 702 189 HOH HOH A . 
E 4 HOH 203 703 87  HOH HOH A . 
E 4 HOH 204 704 301 HOH HOH A . 
E 4 HOH 205 705 62  HOH HOH A . 
E 4 HOH 206 706 178 HOH HOH A . 
E 4 HOH 207 707 136 HOH HOH A . 
E 4 HOH 208 708 289 HOH HOH A . 
E 4 HOH 209 709 323 HOH HOH A . 
E 4 HOH 210 710 253 HOH HOH A . 
E 4 HOH 211 711 137 HOH HOH A . 
E 4 HOH 212 712 346 HOH HOH A . 
E 4 HOH 213 713 84  HOH HOH A . 
E 4 HOH 214 714 180 HOH HOH A . 
E 4 HOH 215 715 36  HOH HOH A . 
E 4 HOH 216 716 271 HOH HOH A . 
E 4 HOH 217 717 72  HOH HOH A . 
E 4 HOH 218 718 159 HOH HOH A . 
E 4 HOH 219 719 324 HOH HOH A . 
E 4 HOH 220 720 224 HOH HOH A . 
E 4 HOH 221 721 168 HOH HOH A . 
E 4 HOH 222 722 261 HOH HOH A . 
E 4 HOH 223 723 233 HOH HOH A . 
E 4 HOH 224 724 94  HOH HOH A . 
E 4 HOH 225 725 366 HOH HOH A . 
E 4 HOH 226 726 208 HOH HOH A . 
E 4 HOH 227 727 166 HOH HOH A . 
E 4 HOH 228 728 230 HOH HOH A . 
E 4 HOH 229 729 214 HOH HOH A . 
E 4 HOH 230 730 17  HOH HOH A . 
E 4 HOH 231 731 160 HOH HOH A . 
E 4 HOH 232 732 6   HOH HOH A . 
E 4 HOH 233 733 153 HOH HOH A . 
E 4 HOH 234 734 223 HOH HOH A . 
E 4 HOH 235 735 262 HOH HOH A . 
E 4 HOH 236 736 226 HOH HOH A . 
E 4 HOH 237 737 350 HOH HOH A . 
E 4 HOH 238 738 273 HOH HOH A . 
E 4 HOH 239 739 217 HOH HOH A . 
E 4 HOH 240 740 33  HOH HOH A . 
E 4 HOH 241 741 167 HOH HOH A . 
E 4 HOH 242 742 246 HOH HOH A . 
E 4 HOH 243 743 302 HOH HOH A . 
E 4 HOH 244 744 120 HOH HOH A . 
E 4 HOH 245 745 112 HOH HOH A . 
E 4 HOH 246 746 268 HOH HOH A . 
E 4 HOH 247 747 244 HOH HOH A . 
E 4 HOH 248 748 234 HOH HOH A . 
E 4 HOH 249 749 213 HOH HOH A . 
E 4 HOH 250 750 288 HOH HOH A . 
E 4 HOH 251 751 90  HOH HOH A . 
E 4 HOH 252 752 79  HOH HOH A . 
E 4 HOH 253 753 205 HOH HOH A . 
E 4 HOH 254 754 296 HOH HOH A . 
E 4 HOH 255 755 365 HOH HOH A . 
E 4 HOH 256 756 304 HOH HOH A . 
E 4 HOH 257 757 278 HOH HOH A . 
E 4 HOH 258 758 343 HOH HOH A . 
E 4 HOH 259 759 111 HOH HOH A . 
E 4 HOH 260 760 333 HOH HOH A . 
E 4 HOH 261 761 179 HOH HOH A . 
E 4 HOH 262 762 309 HOH HOH A . 
E 4 HOH 263 763 154 HOH HOH A . 
E 4 HOH 264 764 162 HOH HOH A . 
E 4 HOH 265 765 326 HOH HOH A . 
E 4 HOH 266 766 193 HOH HOH A . 
E 4 HOH 267 767 259 HOH HOH A . 
E 4 HOH 268 768 299 HOH HOH A . 
E 4 HOH 269 769 277 HOH HOH A . 
E 4 HOH 270 770 209 HOH HOH A . 
E 4 HOH 271 771 338 HOH HOH A . 
E 4 HOH 272 772 292 HOH HOH A . 
E 4 HOH 273 773 314 HOH HOH A . 
E 4 HOH 274 774 198 HOH HOH A . 
E 4 HOH 275 775 200 HOH HOH A . 
E 4 HOH 276 776 280 HOH HOH A . 
E 4 HOH 277 777 313 HOH HOH A . 
E 4 HOH 278 778 240 HOH HOH A . 
E 4 HOH 279 779 295 HOH HOH A . 
E 4 HOH 280 780 236 HOH HOH A . 
E 4 HOH 281 781 177 HOH HOH A . 
E 4 HOH 282 782 140 HOH HOH A . 
E 4 HOH 283 783 203 HOH HOH A . 
E 4 HOH 284 784 298 HOH HOH A . 
E 4 HOH 285 785 307 HOH HOH A . 
E 4 HOH 286 786 275 HOH HOH A . 
E 4 HOH 287 787 134 HOH HOH A . 
E 4 HOH 288 788 164 HOH HOH A . 
E 4 HOH 289 789 125 HOH HOH A . 
E 4 HOH 290 790 215 HOH HOH A . 
E 4 HOH 291 791 18  HOH HOH A . 
E 4 HOH 292 792 202 HOH HOH A . 
E 4 HOH 293 793 252 HOH HOH A . 
E 4 HOH 294 794 320 HOH HOH A . 
E 4 HOH 295 795 356 HOH HOH A . 
E 4 HOH 296 796 123 HOH HOH A . 
E 4 HOH 297 797 188 HOH HOH A . 
E 4 HOH 298 798 219 HOH HOH A . 
E 4 HOH 299 799 132 HOH HOH A . 
E 4 HOH 300 800 185 HOH HOH A . 
E 4 HOH 301 801 279 HOH HOH A . 
E 4 HOH 302 802 344 HOH HOH A . 
E 4 HOH 303 803 174 HOH HOH A . 
E 4 HOH 304 804 347 HOH HOH A . 
E 4 HOH 305 805 110 HOH HOH A . 
E 4 HOH 306 806 86  HOH HOH A . 
E 4 HOH 307 807 130 HOH HOH A . 
E 4 HOH 308 808 142 HOH HOH A . 
E 4 HOH 309 809 287 HOH HOH A . 
E 4 HOH 310 810 210 HOH HOH A . 
E 4 HOH 311 811 196 HOH HOH A . 
E 4 HOH 312 812 54  HOH HOH A . 
E 4 HOH 313 813 107 HOH HOH A . 
E 4 HOH 314 814 284 HOH HOH A . 
E 4 HOH 315 815 362 HOH HOH A . 
E 4 HOH 316 816 239 HOH HOH A . 
E 4 HOH 317 817 183 HOH HOH A . 
E 4 HOH 318 818 369 HOH HOH A . 
E 4 HOH 319 819 201 HOH HOH A . 
E 4 HOH 320 820 81  HOH HOH A . 
E 4 HOH 321 821 116 HOH HOH A . 
E 4 HOH 322 822 199 HOH HOH A . 
E 4 HOH 323 823 353 HOH HOH A . 
E 4 HOH 324 824 367 HOH HOH A . 
E 4 HOH 325 825 221 HOH HOH A . 
E 4 HOH 326 826 339 HOH HOH A . 
E 4 HOH 327 827 332 HOH HOH A . 
E 4 HOH 328 828 82  HOH HOH A . 
E 4 HOH 329 829 173 HOH HOH A . 
E 4 HOH 330 830 254 HOH HOH A . 
E 4 HOH 331 831 321 HOH HOH A . 
E 4 HOH 332 832 325 HOH HOH A . 
E 4 HOH 333 833 337 HOH HOH A . 
E 4 HOH 334 834 165 HOH HOH A . 
E 4 HOH 335 835 80  HOH HOH A . 
E 4 HOH 336 836 135 HOH HOH A . 
E 4 HOH 337 837 285 HOH HOH A . 
E 4 HOH 338 838 195 HOH HOH A . 
E 4 HOH 339 839 176 HOH HOH A . 
E 4 HOH 340 840 35  HOH HOH A . 
E 4 HOH 341 841 358 HOH HOH A . 
E 4 HOH 342 842 341 HOH HOH A . 
E 4 HOH 343 843 351 HOH HOH A . 
E 4 HOH 344 844 249 HOH HOH A . 
E 4 HOH 345 845 186 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VWM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.120 
_cell.length_a_esd                 ? 
_cell.length_b                     70.780 
_cell.length_b_esd                 ? 
_cell.length_c                     77.050 
_cell.length_c_esd                 ? 
_cell.volume                       360591.966 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8VWM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8VWM 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.49 
_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' 
_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    'PEG 4000, Na cacodylate, n-octyl-b-D-glucoside (b-OG)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-09-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.995 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.995 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          19.82 
_reflns.entry_id                                       8VWM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.93 
_reflns.d_resolution_low                               40.8 
_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                                     27450 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.1 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.93 
_reflns_shell.d_res_low                                     1.98 
_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                             1796 
_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                                  0.904 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.74 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8VWM 
_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                            1.94 
_refine.ls_d_res_low                             38.52 
_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                     27240 
_refine.ls_number_reflns_R_free                  1243 
_refine.ls_number_reflns_R_work                  25997 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.53 
_refine.ls_percent_reflns_R_free                 4.56 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1769 
_refine.ls_R_factor_R_free                       0.2215 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1749 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 19.8638 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2041 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.94 
_refine_hist.d_res_low                        38.52 
_refine_hist.number_atoms_solvent             345 
_refine_hist.number_atoms_total               3228 
_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        2811 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.0076  ? 2952 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9146  ? 4004 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0598  ? 446  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0079  ? 504  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.4375 ? 1095 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.94 2.02  . . 152 2719 95.70  . . . . 0.2224 . . . . . . . . . . . 0.2904 
'X-RAY DIFFRACTION' 2.02 2.11  . . 130 2849 100.00 . . . . 0.1719 . . . . . . . . . . . 0.2558 
'X-RAY DIFFRACTION' 2.11 2.22  . . 146 2858 100.00 . . . . 0.1663 . . . . . . . . . . . 0.2088 
'X-RAY DIFFRACTION' 2.22 2.36  . . 152 2872 100.00 . . . . 0.1713 . . . . . . . . . . . 0.2086 
'X-RAY DIFFRACTION' 2.36 2.54  . . 130 2868 100.00 . . . . 0.1791 . . . . . . . . . . . 0.2709 
'X-RAY DIFFRACTION' 2.54 2.80  . . 115 2895 100.00 . . . . 0.1825 . . . . . . . . . . . 0.2380 
'X-RAY DIFFRACTION' 2.80 3.20  . . 130 2926 100.00 . . . . 0.1812 . . . . . . . . . . . 0.2206 
'X-RAY DIFFRACTION' 3.20 4.04  . . 156 2930 100.00 . . . . 0.1616 . . . . . . . . . . . 0.2005 
'X-RAY DIFFRACTION' 4.04 38.52 . . 132 3080 100.00 . . . . 0.1727 . . . . . . . . . . . 0.2024 
# 
_struct.entry_id                     8VWM 
_struct.title                        
'A structural study of selectivity mechanisms for JNK3 and p38 alpha with indazole scaffold probing compounds' 
_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        8VWM 
_struct_keywords.text            'C-Jun terminal kinase 3, JNK3, p38 alpha, Kinase, selectivity, 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 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MK14_MOUSE 
_struct_ref.pdbx_db_accession          P47811 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHE
NVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNED
CELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGT
PGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVAD
PYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8VWM 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 9 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 367 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P47811 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  360 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       360 
# 
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 8VWM MET A 1 ? UNP P47811 ? ? 'initiating methionine' -6 1 
1 8VWM ALA A 2 ? UNP P47811 ? ? 'expression tag'        -5 2 
1 8VWM HIS A 3 ? UNP P47811 ? ? 'expression tag'        -4 3 
1 8VWM HIS A 4 ? UNP P47811 ? ? 'expression tag'        -3 4 
1 8VWM HIS A 5 ? UNP P47811 ? ? 'expression tag'        -2 5 
1 8VWM HIS A 6 ? UNP P47811 ? ? 'expression tag'        -1 6 
1 8VWM HIS A 7 ? UNP P47811 ? ? 'expression tag'        0  7 
1 8VWM HIS A 8 ? UNP P47811 ? ? 'expression tag'        1  8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 68  ? MET A 85  ? SER A 61  MET A 78  1 ? 18 
HELX_P HELX_P2  AA2 LEU A 120 ? GLN A 127 ? LEU A 113 GLN A 120 1 ? 8  
HELX_P HELX_P3  AA3 THR A 130 ? ALA A 151 ? THR A 123 ALA A 144 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 159 ? SER A 161 ? LYS A 152 SER A 154 5 ? 3  
HELX_P HELX_P5  AA5 ALA A 197 ? LEU A 202 ? ALA A 190 LEU A 195 1 ? 6  
HELX_P HELX_P6  AA6 GLN A 209 ? GLY A 226 ? GLN A 202 GLY A 219 1 ? 18 
HELX_P HELX_P7  AA7 ASP A 234 ? GLY A 247 ? ASP A 227 GLY A 240 1 ? 14 
HELX_P HELX_P8  AA8 GLY A 250 ? LYS A 255 ? GLY A 243 LYS A 248 1 ? 6  
HELX_P HELX_P9  AA9 SER A 259 ? LEU A 269 ? SER A 252 LEU A 262 1 ? 11 
HELX_P HELX_P10 AB1 ASN A 276 ? PHE A 281 ? ASN A 269 PHE A 274 1 ? 6  
HELX_P HELX_P11 AB2 ASN A 285 ? LEU A 296 ? ASN A 278 LEU A 289 1 ? 12 
HELX_P HELX_P12 AB3 ASP A 299 ? ARG A 303 ? ASP A 292 ARG A 296 5 ? 5  
HELX_P HELX_P13 AB4 THR A 305 ? ALA A 311 ? THR A 298 ALA A 304 1 ? 7  
HELX_P HELX_P14 AB5 HIS A 312 ? ALA A 316 ? HIS A 305 ALA A 309 5 ? 5  
HELX_P HELX_P15 AB6 GLN A 332 ? ARG A 337 ? GLN A 325 ARG A 330 5 ? 6  
HELX_P HELX_P16 AB7 LEU A 340 ? PHE A 355 ? LEU A 333 PHE A 348 1 ? 16 
HELX_P HELX_P17 AB8 ASP A 361 ? MET A 365 ? ASP A 354 MET A 358 5 ? 5  
# 
_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 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? 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 PHE A 15  ? LEU A 20  ? PHE A 8   LEU A 13  
AA1 2 THR A 23  ? PRO A 28  ? THR A 16  PRO A 21  
AA2 1 TYR A 31  ? GLY A 40  ? TYR A 24  GLY A 33  
AA2 2 GLY A 43  ? ASP A 50  ? GLY A 36  ASP A 43  
AA2 3 ARG A 56  ? LYS A 61  ? ARG A 49  LYS A 54  
AA2 4 TYR A 110 ? HIS A 114 ? TYR A 103 HIS A 107 
AA2 5 ASP A 95  ? PHE A 97  ? ASP A 88  PHE A 90  
AA3 1 ALA A 118 ? ASP A 119 ? ALA A 111 ASP A 112 
AA3 2 LEU A 163 ? VAL A 165 ? LEU A 156 VAL A 158 
AA3 3 LEU A 171 ? ILE A 173 ? LEU A 164 ILE A 166 
# 
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 GLN A 18  ? N GLN A 11  O TRP A 25  ? O TRP A 18  
AA2 1 2 N SER A 35  ? N SER A 28  O ALA A 47  ? O ALA A 40  
AA2 2 3 N SER A 44  ? N SER A 37  O LYS A 61  ? O LYS A 54  
AA2 3 4 N LYS A 60  ? N LYS A 53  O LEU A 111 ? O LEU A 104 
AA2 4 5 O VAL A 112 ? O VAL A 105 N ASP A 95  ? N ASP A 88  
AA3 1 2 N ALA A 118 ? N ALA A 111 O VAL A 165 ? O VAL A 158 
AA3 2 3 N ALA A 164 ? N ALA A 157 O LYS A 172 ? O LYS A 165 
# 
_pdbx_entry_details.entry_id                   8VWM 
_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 704 ? ? 2.02 
2 1 O A HOH 744 ? ? O A HOH 758 ? ? 2.03 
3 1 O A HOH 517 ? ? O A HOH 672 ? ? 2.19 
4 1 O A HOH 709 ? ? O A HOH 827 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? 37.19   49.72   
2 1 ARG A 149 ? ? 85.50   -8.91   
3 1 ASP A 150 ? ? -148.89 48.68   
4 1 ASN A 159 ? ? -103.40 -168.76 
5 1 LEU A 167 ? ? -105.37 -136.33 
6 1 MET A 198 ? ? 87.12   -17.78  
7 1 PHE A 274 ? ? -99.65  34.90   
8 1 LEU A 289 ? ? -96.74  58.07   
9 1 GLU A 359 ? ? -105.43 -112.98 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -6  ? A MET 1   
2  1 Y 1 A ALA -5  ? A ALA 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 HIS 1   ? A HIS 8   
9  1 Y 1 A SER 2   ? A SER 9   
10 1 Y 1 A GLN 3   ? A GLN 10  
11 1 Y 1 A GLU 4   ? A GLU 11  
12 1 Y 1 A THR 175 ? A THR 182 
13 1 Y 1 A ASP 176 ? A ASP 183 
14 1 Y 1 A ASP 177 ? A ASP 184 
15 1 Y 1 A GLU 178 ? A GLU 185 
16 1 Y 1 A MET 179 ? A MET 186 
17 1 Y 1 A THR 180 ? A THR 187 
18 1 Y 1 A GLY 181 ? A GLY 188 
19 1 Y 1 A TYR 182 ? A TYR 189 
# 
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  
BOG C1     C  N R 74  
BOG O1     O  N N 75  
BOG C2     C  N R 76  
BOG O2     O  N N 77  
BOG C3     C  N S 78  
BOG O3     O  N N 79  
BOG C4     C  N S 80  
BOG O4     O  N N 81  
BOG C5     C  N R 82  
BOG O5     O  N N 83  
BOG C6     C  N N 84  
BOG O6     O  N N 85  
BOG "C1'"  C  N N 86  
BOG "C2'"  C  N N 87  
BOG "C3'"  C  N N 88  
BOG "C4'"  C  N N 89  
BOG "C5'"  C  N N 90  
BOG "C6'"  C  N N 91  
BOG "C7'"  C  N N 92  
BOG "C8'"  C  N N 93  
BOG H1     H  N N 94  
BOG H2     H  N N 95  
BOG HO2    H  N N 96  
BOG H3     H  N N 97  
BOG HO3    H  N N 98  
BOG H4     H  N N 99  
BOG HO4    H  N N 100 
BOG H5     H  N N 101 
BOG H61    H  N N 102 
BOG H62    H  N N 103 
BOG HO6    H  N N 104 
BOG "H1'1" H  N N 105 
BOG "H1'2" H  N N 106 
BOG "H2'1" H  N N 107 
BOG "H2'2" H  N N 108 
BOG "H3'1" H  N N 109 
BOG "H3'2" H  N N 110 
BOG "H4'1" H  N N 111 
BOG "H4'2" H  N N 112 
BOG "H5'1" H  N N 113 
BOG "H5'2" H  N N 114 
BOG "H6'1" H  N N 115 
BOG "H6'2" H  N N 116 
BOG "H7'1" H  N N 117 
BOG "H7'2" H  N N 118 
BOG "H8'1" H  N N 119 
BOG "H8'2" H  N N 120 
BOG "H8'3" H  N N 121 
CYS N      N  N N 122 
CYS CA     C  N R 123 
CYS C      C  N N 124 
CYS O      O  N N 125 
CYS CB     C  N N 126 
CYS SG     S  N N 127 
CYS OXT    O  N N 128 
CYS H      H  N N 129 
CYS H2     H  N N 130 
CYS HA     H  N N 131 
CYS HB2    H  N N 132 
CYS HB3    H  N N 133 
CYS HG     H  N N 134 
CYS HXT    H  N N 135 
GLN N      N  N N 136 
GLN CA     C  N S 137 
GLN C      C  N N 138 
GLN O      O  N N 139 
GLN CB     C  N N 140 
GLN CG     C  N N 141 
GLN CD     C  N N 142 
GLN OE1    O  N N 143 
GLN NE2    N  N N 144 
GLN OXT    O  N N 145 
GLN H      H  N N 146 
GLN H2     H  N N 147 
GLN HA     H  N N 148 
GLN HB2    H  N N 149 
GLN HB3    H  N N 150 
GLN HG2    H  N N 151 
GLN HG3    H  N N 152 
GLN HE21   H  N N 153 
GLN HE22   H  N N 154 
GLN HXT    H  N N 155 
GLU N      N  N N 156 
GLU CA     C  N S 157 
GLU C      C  N N 158 
GLU O      O  N N 159 
GLU CB     C  N N 160 
GLU CG     C  N N 161 
GLU CD     C  N N 162 
GLU OE1    O  N N 163 
GLU OE2    O  N N 164 
GLU OXT    O  N N 165 
GLU H      H  N N 166 
GLU H2     H  N N 167 
GLU HA     H  N N 168 
GLU HB2    H  N N 169 
GLU HB3    H  N N 170 
GLU HG2    H  N N 171 
GLU HG3    H  N N 172 
GLU HE2    H  N N 173 
GLU HXT    H  N N 174 
GLY N      N  N N 175 
GLY CA     C  N N 176 
GLY C      C  N N 177 
GLY O      O  N N 178 
GLY OXT    O  N N 179 
GLY H      H  N N 180 
GLY H2     H  N N 181 
GLY HA2    H  N N 182 
GLY HA3    H  N N 183 
GLY HXT    H  N N 184 
HIS N      N  N N 185 
HIS CA     C  N S 186 
HIS C      C  N N 187 
HIS O      O  N N 188 
HIS CB     C  N N 189 
HIS CG     C  Y N 190 
HIS ND1    N  Y N 191 
HIS CD2    C  Y N 192 
HIS CE1    C  Y N 193 
HIS NE2    N  Y N 194 
HIS OXT    O  N N 195 
HIS H      H  N N 196 
HIS H2     H  N N 197 
HIS HA     H  N N 198 
HIS HB2    H  N N 199 
HIS HB3    H  N N 200 
HIS HD1    H  N N 201 
HIS HD2    H  N N 202 
HIS HE1    H  N N 203 
HIS HE2    H  N N 204 
HIS HXT    H  N N 205 
HOH O      O  N N 206 
HOH H1     H  N N 207 
HOH H2     H  N N 208 
ILE N      N  N N 209 
ILE CA     C  N S 210 
ILE C      C  N N 211 
ILE O      O  N N 212 
ILE CB     C  N S 213 
ILE CG1    C  N N 214 
ILE CG2    C  N N 215 
ILE CD1    C  N N 216 
ILE OXT    O  N N 217 
ILE H      H  N N 218 
ILE H2     H  N N 219 
ILE HA     H  N N 220 
ILE HB     H  N N 221 
ILE HG12   H  N N 222 
ILE HG13   H  N N 223 
ILE HG21   H  N N 224 
ILE HG22   H  N N 225 
ILE HG23   H  N N 226 
ILE HD11   H  N N 227 
ILE HD12   H  N N 228 
ILE HD13   H  N N 229 
ILE HXT    H  N N 230 
LEU N      N  N N 231 
LEU CA     C  N S 232 
LEU C      C  N N 233 
LEU O      O  N N 234 
LEU CB     C  N N 235 
LEU CG     C  N N 236 
LEU CD1    C  N N 237 
LEU CD2    C  N N 238 
LEU OXT    O  N N 239 
LEU H      H  N N 240 
LEU H2     H  N N 241 
LEU HA     H  N N 242 
LEU HB2    H  N N 243 
LEU HB3    H  N N 244 
LEU HG     H  N N 245 
LEU HD11   H  N N 246 
LEU HD12   H  N N 247 
LEU HD13   H  N N 248 
LEU HD21   H  N N 249 
LEU HD22   H  N N 250 
LEU HD23   H  N N 251 
LEU HXT    H  N N 252 
LYS N      N  N N 253 
LYS CA     C  N S 254 
LYS C      C  N N 255 
LYS O      O  N N 256 
LYS CB     C  N N 257 
LYS CG     C  N N 258 
LYS CD     C  N N 259 
LYS CE     C  N N 260 
LYS NZ     N  N N 261 
LYS OXT    O  N N 262 
LYS H      H  N N 263 
LYS H2     H  N N 264 
LYS HA     H  N N 265 
LYS HB2    H  N N 266 
LYS HB3    H  N N 267 
LYS HG2    H  N N 268 
LYS HG3    H  N N 269 
LYS HD2    H  N N 270 
LYS HD3    H  N N 271 
LYS HE2    H  N N 272 
LYS HE3    H  N N 273 
LYS HZ1    H  N N 274 
LYS HZ2    H  N N 275 
LYS HZ3    H  N N 276 
LYS HXT    H  N N 277 
MET N      N  N N 278 
MET CA     C  N S 279 
MET C      C  N N 280 
MET O      O  N N 281 
MET CB     C  N N 282 
MET CG     C  N N 283 
MET SD     S  N N 284 
MET CE     C  N N 285 
MET OXT    O  N N 286 
MET H      H  N N 287 
MET H2     H  N N 288 
MET HA     H  N N 289 
MET HB2    H  N N 290 
MET HB3    H  N N 291 
MET HG2    H  N N 292 
MET HG3    H  N N 293 
MET HE1    H  N N 294 
MET HE2    H  N N 295 
MET HE3    H  N N 296 
MET HXT    H  N N 297 
PHE N      N  N N 298 
PHE CA     C  N S 299 
PHE C      C  N N 300 
PHE O      O  N N 301 
PHE CB     C  N N 302 
PHE CG     C  Y N 303 
PHE CD1    C  Y N 304 
PHE CD2    C  Y N 305 
PHE CE1    C  Y N 306 
PHE CE2    C  Y N 307 
PHE CZ     C  Y N 308 
PHE OXT    O  N N 309 
PHE H      H  N N 310 
PHE H2     H  N N 311 
PHE HA     H  N N 312 
PHE HB2    H  N N 313 
PHE HB3    H  N N 314 
PHE HD1    H  N N 315 
PHE HD2    H  N N 316 
PHE HE1    H  N N 317 
PHE HE2    H  N N 318 
PHE HZ     H  N N 319 
PHE HXT    H  N N 320 
PRO N      N  N N 321 
PRO CA     C  N S 322 
PRO C      C  N N 323 
PRO O      O  N N 324 
PRO CB     C  N N 325 
PRO CG     C  N N 326 
PRO CD     C  N N 327 
PRO OXT    O  N N 328 
PRO H      H  N N 329 
PRO HA     H  N N 330 
PRO HB2    H  N N 331 
PRO HB3    H  N N 332 
PRO HG2    H  N N 333 
PRO HG3    H  N N 334 
PRO HD2    H  N N 335 
PRO HD3    H  N N 336 
PRO HXT    H  N N 337 
SER N      N  N N 338 
SER CA     C  N S 339 
SER C      C  N N 340 
SER O      O  N N 341 
SER CB     C  N N 342 
SER OG     O  N N 343 
SER OXT    O  N N 344 
SER H      H  N N 345 
SER H2     H  N N 346 
SER HA     H  N N 347 
SER HB2    H  N N 348 
SER HB3    H  N N 349 
SER HG     H  N N 350 
SER HXT    H  N N 351 
THR N      N  N N 352 
THR CA     C  N S 353 
THR C      C  N N 354 
THR O      O  N N 355 
THR CB     C  N R 356 
THR OG1    O  N N 357 
THR CG2    C  N N 358 
THR OXT    O  N N 359 
THR H      H  N N 360 
THR H2     H  N N 361 
THR HA     H  N N 362 
THR HB     H  N N 363 
THR HG1    H  N N 364 
THR HG21   H  N N 365 
THR HG22   H  N N 366 
THR HG23   H  N N 367 
THR HXT    H  N N 368 
TRP N      N  N N 369 
TRP CA     C  N S 370 
TRP C      C  N N 371 
TRP O      O  N N 372 
TRP CB     C  N N 373 
TRP CG     C  Y N 374 
TRP CD1    C  Y N 375 
TRP CD2    C  Y N 376 
TRP NE1    N  Y N 377 
TRP CE2    C  Y N 378 
TRP CE3    C  Y N 379 
TRP CZ2    C  Y N 380 
TRP CZ3    C  Y N 381 
TRP CH2    C  Y N 382 
TRP OXT    O  N N 383 
TRP H      H  N N 384 
TRP H2     H  N N 385 
TRP HA     H  N N 386 
TRP HB2    H  N N 387 
TRP HB3    H  N N 388 
TRP HD1    H  N N 389 
TRP HE1    H  N N 390 
TRP HE3    H  N N 391 
TRP HZ2    H  N N 392 
TRP HZ3    H  N N 393 
TRP HH2    H  N N 394 
TRP HXT    H  N N 395 
TYR N      N  N N 396 
TYR CA     C  N S 397 
TYR C      C  N N 398 
TYR O      O  N N 399 
TYR CB     C  N N 400 
TYR CG     C  Y N 401 
TYR CD1    C  Y N 402 
TYR CD2    C  Y N 403 
TYR CE1    C  Y N 404 
TYR CE2    C  Y N 405 
TYR CZ     C  Y N 406 
TYR OH     O  N N 407 
TYR OXT    O  N N 408 
TYR H      H  N N 409 
TYR H2     H  N N 410 
TYR HA     H  N N 411 
TYR HB2    H  N N 412 
TYR HB3    H  N N 413 
TYR HD1    H  N N 414 
TYR HD2    H  N N 415 
TYR HE1    H  N N 416 
TYR HE2    H  N N 417 
TYR HH     H  N N 418 
TYR HXT    H  N N 419 
VAL N      N  N N 420 
VAL CA     C  N S 421 
VAL C      C  N N 422 
VAL O      O  N N 423 
VAL CB     C  N N 424 
VAL CG1    C  N N 425 
VAL CG2    C  N N 426 
VAL OXT    O  N N 427 
VAL H      H  N N 428 
VAL H2     H  N N 429 
VAL HA     H  N N 430 
VAL HB     H  N N 431 
VAL HG11   H  N N 432 
VAL HG12   H  N N 433 
VAL HG13   H  N N 434 
VAL HG21   H  N N 435 
VAL HG22   H  N N 436 
VAL HG23   H  N N 437 
VAL HXT    H  N N 438 
WHE C1     C  Y N 439 
WHE C2     C  Y N 440 
WHE C3     C  Y N 441 
WHE C5     C  Y N 442 
WHE C6     C  Y N 443 
WHE C7     C  Y N 444 
WHE N4     N  N N 445 
WHE C8     C  Y N 446 
WHE C11    C  Y N 447 
WHE C13    C  Y N 448 
WHE C14    C  Y N 449 
WHE C15    C  Y N 450 
WHE C18    C  N N 451 
WHE C20    C  N N 452 
WHE C22    C  N N 453 
WHE C23    C  N N 454 
WHE C10    C  Y N 455 
WHE C12    C  Y N 456 
WHE C16    C  Y N 457 
WHE C17    C  Y N 458 
WHE C19    C  N N 459 
WHE C21    C  N N 460 
WHE C4     C  Y N 461 
WHE C9     C  Y N 462 
WHE F1     F  N N 463 
WHE N1     N  Y N 464 
WHE N2     N  Y N 465 
WHE N3     N  N N 466 
WHE N5     N  N N 467 
WHE O1     O  N N 468 
WHE S1     S  Y N 469 
WHE CL1    CL N N 470 
WHE H2     H  N N 471 
WHE H10    H  N N 472 
WHE H3     H  N N 473 
WHE H5     H  N N 474 
WHE H7     H  N N 475 
WHE H8     H  N N 476 
WHE H14    H  N N 477 
WHE H15    H  N N 478 
WHE H18    H  N N 479 
WHE H19    H  N N 480 
WHE H20    H  N N 481 
WHE H21    H  N N 482 
WHE H6     H  N N 483 
WHE H9     H  N N 484 
WHE H13    H  N N 485 
WHE H11    H  N N 486 
WHE H12    H  N N 487 
WHE H16    H  N N 488 
WHE H17    H  N N 489 
WHE H1     H  N N 490 
WHE H4     H  N N 491 
# 
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  
BOG C1    O1     sing N N 70  
BOG C1    C2     sing N N 71  
BOG C1    O5     sing N N 72  
BOG C1    H1     sing N N 73  
BOG O1    "C1'"  sing N N 74  
BOG C2    O2     sing N N 75  
BOG C2    C3     sing N N 76  
BOG C2    H2     sing N N 77  
BOG O2    HO2    sing N N 78  
BOG C3    O3     sing N N 79  
BOG C3    C4     sing N N 80  
BOG C3    H3     sing N N 81  
BOG O3    HO3    sing N N 82  
BOG C4    O4     sing N N 83  
BOG C4    C5     sing N N 84  
BOG C4    H4     sing N N 85  
BOG O4    HO4    sing N N 86  
BOG C5    O5     sing N N 87  
BOG C5    C6     sing N N 88  
BOG C5    H5     sing N N 89  
BOG C6    O6     sing N N 90  
BOG C6    H61    sing N N 91  
BOG C6    H62    sing N N 92  
BOG O6    HO6    sing N N 93  
BOG "C1'" "C2'"  sing N N 94  
BOG "C1'" "H1'1" sing N N 95  
BOG "C1'" "H1'2" sing N N 96  
BOG "C2'" "C3'"  sing N N 97  
BOG "C2'" "H2'1" sing N N 98  
BOG "C2'" "H2'2" sing N N 99  
BOG "C3'" "C4'"  sing N N 100 
BOG "C3'" "H3'1" sing N N 101 
BOG "C3'" "H3'2" sing N N 102 
BOG "C4'" "C5'"  sing N N 103 
BOG "C4'" "H4'1" sing N N 104 
BOG "C4'" "H4'2" sing N N 105 
BOG "C5'" "C6'"  sing N N 106 
BOG "C5'" "H5'1" sing N N 107 
BOG "C5'" "H5'2" sing N N 108 
BOG "C6'" "C7'"  sing N N 109 
BOG "C6'" "H6'1" sing N N 110 
BOG "C6'" "H6'2" sing N N 111 
BOG "C7'" "C8'"  sing N N 112 
BOG "C7'" "H7'1" sing N N 113 
BOG "C7'" "H7'2" sing N N 114 
BOG "C8'" "H8'1" sing N N 115 
BOG "C8'" "H8'2" sing N N 116 
BOG "C8'" "H8'3" sing N N 117 
CYS N     CA     sing N N 118 
CYS N     H      sing N N 119 
CYS N     H2     sing N N 120 
CYS CA    C      sing N N 121 
CYS CA    CB     sing N N 122 
CYS CA    HA     sing N N 123 
CYS C     O      doub N N 124 
CYS C     OXT    sing N N 125 
CYS CB    SG     sing N N 126 
CYS CB    HB2    sing N N 127 
CYS CB    HB3    sing N N 128 
CYS SG    HG     sing N N 129 
CYS OXT   HXT    sing N N 130 
GLN N     CA     sing N N 131 
GLN N     H      sing N N 132 
GLN N     H2     sing N N 133 
GLN CA    C      sing N N 134 
GLN CA    CB     sing N N 135 
GLN CA    HA     sing N N 136 
GLN C     O      doub N N 137 
GLN C     OXT    sing N N 138 
GLN CB    CG     sing N N 139 
GLN CB    HB2    sing N N 140 
GLN CB    HB3    sing N N 141 
GLN CG    CD     sing N N 142 
GLN CG    HG2    sing N N 143 
GLN CG    HG3    sing N N 144 
GLN CD    OE1    doub N N 145 
GLN CD    NE2    sing N N 146 
GLN NE2   HE21   sing N N 147 
GLN NE2   HE22   sing N N 148 
GLN OXT   HXT    sing N N 149 
GLU N     CA     sing N N 150 
GLU N     H      sing N N 151 
GLU N     H2     sing N N 152 
GLU CA    C      sing N N 153 
GLU CA    CB     sing N N 154 
GLU CA    HA     sing N N 155 
GLU C     O      doub N N 156 
GLU C     OXT    sing N N 157 
GLU CB    CG     sing N N 158 
GLU CB    HB2    sing N N 159 
GLU CB    HB3    sing N N 160 
GLU CG    CD     sing N N 161 
GLU CG    HG2    sing N N 162 
GLU CG    HG3    sing N N 163 
GLU CD    OE1    doub N N 164 
GLU CD    OE2    sing N N 165 
GLU OE2   HE2    sing N N 166 
GLU OXT   HXT    sing N N 167 
GLY N     CA     sing N N 168 
GLY N     H      sing N N 169 
GLY N     H2     sing N N 170 
GLY CA    C      sing N N 171 
GLY CA    HA2    sing N N 172 
GLY CA    HA3    sing N N 173 
GLY C     O      doub N N 174 
GLY C     OXT    sing N N 175 
GLY OXT   HXT    sing N N 176 
HIS N     CA     sing N N 177 
HIS N     H      sing N N 178 
HIS N     H2     sing N N 179 
HIS CA    C      sing N N 180 
HIS CA    CB     sing N N 181 
HIS CA    HA     sing N N 182 
HIS C     O      doub N N 183 
HIS C     OXT    sing N N 184 
HIS CB    CG     sing N N 185 
HIS CB    HB2    sing N N 186 
HIS CB    HB3    sing N N 187 
HIS CG    ND1    sing Y N 188 
HIS CG    CD2    doub Y N 189 
HIS ND1   CE1    doub Y N 190 
HIS ND1   HD1    sing N N 191 
HIS CD2   NE2    sing Y N 192 
HIS CD2   HD2    sing N N 193 
HIS CE1   NE2    sing Y N 194 
HIS CE1   HE1    sing N N 195 
HIS NE2   HE2    sing N N 196 
HIS OXT   HXT    sing N N 197 
HOH O     H1     sing N N 198 
HOH O     H2     sing N N 199 
ILE N     CA     sing N N 200 
ILE N     H      sing N N 201 
ILE N     H2     sing N N 202 
ILE CA    C      sing N N 203 
ILE CA    CB     sing N N 204 
ILE CA    HA     sing N N 205 
ILE C     O      doub N N 206 
ILE C     OXT    sing N N 207 
ILE CB    CG1    sing N N 208 
ILE CB    CG2    sing N N 209 
ILE CB    HB     sing N N 210 
ILE CG1   CD1    sing N N 211 
ILE CG1   HG12   sing N N 212 
ILE CG1   HG13   sing N N 213 
ILE CG2   HG21   sing N N 214 
ILE CG2   HG22   sing N N 215 
ILE CG2   HG23   sing N N 216 
ILE CD1   HD11   sing N N 217 
ILE CD1   HD12   sing N N 218 
ILE CD1   HD13   sing N N 219 
ILE OXT   HXT    sing N N 220 
LEU N     CA     sing N N 221 
LEU N     H      sing N N 222 
LEU N     H2     sing N N 223 
LEU CA    C      sing N N 224 
LEU CA    CB     sing N N 225 
LEU CA    HA     sing N N 226 
LEU C     O      doub N N 227 
LEU C     OXT    sing N N 228 
LEU CB    CG     sing N N 229 
LEU CB    HB2    sing N N 230 
LEU CB    HB3    sing N N 231 
LEU CG    CD1    sing N N 232 
LEU CG    CD2    sing N N 233 
LEU CG    HG     sing N N 234 
LEU CD1   HD11   sing N N 235 
LEU CD1   HD12   sing N N 236 
LEU CD1   HD13   sing N N 237 
LEU CD2   HD21   sing N N 238 
LEU CD2   HD22   sing N N 239 
LEU CD2   HD23   sing N N 240 
LEU OXT   HXT    sing N N 241 
LYS N     CA     sing N N 242 
LYS N     H      sing N N 243 
LYS N     H2     sing N N 244 
LYS CA    C      sing N N 245 
LYS CA    CB     sing N N 246 
LYS CA    HA     sing N N 247 
LYS C     O      doub N N 248 
LYS C     OXT    sing N N 249 
LYS CB    CG     sing N N 250 
LYS CB    HB2    sing N N 251 
LYS CB    HB3    sing N N 252 
LYS CG    CD     sing N N 253 
LYS CG    HG2    sing N N 254 
LYS CG    HG3    sing N N 255 
LYS CD    CE     sing N N 256 
LYS CD    HD2    sing N N 257 
LYS CD    HD3    sing N N 258 
LYS CE    NZ     sing N N 259 
LYS CE    HE2    sing N N 260 
LYS CE    HE3    sing N N 261 
LYS NZ    HZ1    sing N N 262 
LYS NZ    HZ2    sing N N 263 
LYS NZ    HZ3    sing N N 264 
LYS OXT   HXT    sing N N 265 
MET N     CA     sing N N 266 
MET N     H      sing N N 267 
MET N     H2     sing N N 268 
MET CA    C      sing N N 269 
MET CA    CB     sing N N 270 
MET CA    HA     sing N N 271 
MET C     O      doub N N 272 
MET C     OXT    sing N N 273 
MET CB    CG     sing N N 274 
MET CB    HB2    sing N N 275 
MET CB    HB3    sing N N 276 
MET CG    SD     sing N N 277 
MET CG    HG2    sing N N 278 
MET CG    HG3    sing N N 279 
MET SD    CE     sing N N 280 
MET CE    HE1    sing N N 281 
MET CE    HE2    sing N N 282 
MET CE    HE3    sing N N 283 
MET OXT   HXT    sing N N 284 
PHE N     CA     sing N N 285 
PHE N     H      sing N N 286 
PHE N     H2     sing N N 287 
PHE CA    C      sing N N 288 
PHE CA    CB     sing N N 289 
PHE CA    HA     sing N N 290 
PHE C     O      doub N N 291 
PHE C     OXT    sing N N 292 
PHE CB    CG     sing N N 293 
PHE CB    HB2    sing N N 294 
PHE CB    HB3    sing N N 295 
PHE CG    CD1    doub Y N 296 
PHE CG    CD2    sing Y N 297 
PHE CD1   CE1    sing Y N 298 
PHE CD1   HD1    sing N N 299 
PHE CD2   CE2    doub Y N 300 
PHE CD2   HD2    sing N N 301 
PHE CE1   CZ     doub Y N 302 
PHE CE1   HE1    sing N N 303 
PHE CE2   CZ     sing Y N 304 
PHE CE2   HE2    sing N N 305 
PHE CZ    HZ     sing N N 306 
PHE OXT   HXT    sing N N 307 
PRO N     CA     sing N N 308 
PRO N     CD     sing N N 309 
PRO N     H      sing N N 310 
PRO CA    C      sing N N 311 
PRO CA    CB     sing N N 312 
PRO CA    HA     sing N N 313 
PRO C     O      doub N N 314 
PRO C     OXT    sing N N 315 
PRO CB    CG     sing N N 316 
PRO CB    HB2    sing N N 317 
PRO CB    HB3    sing N N 318 
PRO CG    CD     sing N N 319 
PRO CG    HG2    sing N N 320 
PRO CG    HG3    sing N N 321 
PRO CD    HD2    sing N N 322 
PRO CD    HD3    sing N N 323 
PRO OXT   HXT    sing N N 324 
SER N     CA     sing N N 325 
SER N     H      sing N N 326 
SER N     H2     sing N N 327 
SER CA    C      sing N N 328 
SER CA    CB     sing N N 329 
SER CA    HA     sing N N 330 
SER C     O      doub N N 331 
SER C     OXT    sing N N 332 
SER CB    OG     sing N N 333 
SER CB    HB2    sing N N 334 
SER CB    HB3    sing N N 335 
SER OG    HG     sing N N 336 
SER OXT   HXT    sing N N 337 
THR N     CA     sing N N 338 
THR N     H      sing N N 339 
THR N     H2     sing N N 340 
THR CA    C      sing N N 341 
THR CA    CB     sing N N 342 
THR CA    HA     sing N N 343 
THR C     O      doub N N 344 
THR C     OXT    sing N N 345 
THR CB    OG1    sing N N 346 
THR CB    CG2    sing N N 347 
THR CB    HB     sing N N 348 
THR OG1   HG1    sing N N 349 
THR CG2   HG21   sing N N 350 
THR CG2   HG22   sing N N 351 
THR CG2   HG23   sing N N 352 
THR OXT   HXT    sing N N 353 
TRP N     CA     sing N N 354 
TRP N     H      sing N N 355 
TRP N     H2     sing N N 356 
TRP CA    C      sing N N 357 
TRP CA    CB     sing N N 358 
TRP CA    HA     sing N N 359 
TRP C     O      doub N N 360 
TRP C     OXT    sing N N 361 
TRP CB    CG     sing N N 362 
TRP CB    HB2    sing N N 363 
TRP CB    HB3    sing N N 364 
TRP CG    CD1    doub Y N 365 
TRP CG    CD2    sing Y N 366 
TRP CD1   NE1    sing Y N 367 
TRP CD1   HD1    sing N N 368 
TRP CD2   CE2    doub Y N 369 
TRP CD2   CE3    sing Y N 370 
TRP NE1   CE2    sing Y N 371 
TRP NE1   HE1    sing N N 372 
TRP CE2   CZ2    sing Y N 373 
TRP CE3   CZ3    doub Y N 374 
TRP CE3   HE3    sing N N 375 
TRP CZ2   CH2    doub Y N 376 
TRP CZ2   HZ2    sing N N 377 
TRP CZ3   CH2    sing Y N 378 
TRP CZ3   HZ3    sing N N 379 
TRP CH2   HH2    sing N N 380 
TRP OXT   HXT    sing N N 381 
TYR N     CA     sing N N 382 
TYR N     H      sing N N 383 
TYR N     H2     sing N N 384 
TYR CA    C      sing N N 385 
TYR CA    CB     sing N N 386 
TYR CA    HA     sing N N 387 
TYR C     O      doub N N 388 
TYR C     OXT    sing N N 389 
TYR CB    CG     sing N N 390 
TYR CB    HB2    sing N N 391 
TYR CB    HB3    sing N N 392 
TYR CG    CD1    doub Y N 393 
TYR CG    CD2    sing Y N 394 
TYR CD1   CE1    sing Y N 395 
TYR CD1   HD1    sing N N 396 
TYR CD2   CE2    doub Y N 397 
TYR CD2   HD2    sing N N 398 
TYR CE1   CZ     doub Y N 399 
TYR CE1   HE1    sing N N 400 
TYR CE2   CZ     sing Y N 401 
TYR CE2   HE2    sing N N 402 
TYR CZ    OH     sing N N 403 
TYR OH    HH     sing N N 404 
TYR OXT   HXT    sing N N 405 
VAL N     CA     sing N N 406 
VAL N     H      sing N N 407 
VAL N     H2     sing N N 408 
VAL CA    C      sing N N 409 
VAL CA    CB     sing N N 410 
VAL CA    HA     sing N N 411 
VAL C     O      doub N N 412 
VAL C     OXT    sing N N 413 
VAL CB    CG1    sing N N 414 
VAL CB    CG2    sing N N 415 
VAL CB    HB     sing N N 416 
VAL CG1   HG11   sing N N 417 
VAL CG1   HG12   sing N N 418 
VAL CG1   HG13   sing N N 419 
VAL CG2   HG21   sing N N 420 
VAL CG2   HG22   sing N N 421 
VAL CG2   HG23   sing N N 422 
VAL OXT   HXT    sing N N 423 
WHE C19   N4     sing N N 424 
WHE N4    C18    sing N N 425 
WHE C18   O1     doub N N 426 
WHE C18   C16    sing N N 427 
WHE C15   C16    doub Y N 428 
WHE C15   C1     sing Y N 429 
WHE C16   S1     sing Y N 430 
WHE N2    C4     doub Y N 431 
WHE N2    N1     sing Y N 432 
WHE C4    C3     sing Y N 433 
WHE C1    N1     sing N N 434 
WHE C1    C17    doub Y N 435 
WHE S1    C17    sing Y N 436 
WHE N1    C2     sing Y N 437 
WHE C3    C2     doub Y N 438 
WHE C3    C8     sing Y N 439 
WHE C2    C5     sing Y N 440 
WHE C8    C7     doub Y N 441 
WHE C5    C6     doub Y N 442 
WHE F1    C14    sing N N 443 
WHE C7    C6     sing Y N 444 
WHE C7    N3     sing N N 445 
WHE C13   C14    doub Y N 446 
WHE C13   C12    sing Y N 447 
WHE C6    C20    sing N N 448 
WHE C14   C9     sing Y N 449 
WHE C12   C11    doub Y N 450 
WHE C9    N3     sing N N 451 
WHE C9    C10    doub Y N 452 
WHE C11   C10    sing Y N 453 
WHE C10   CL1    sing N N 454 
WHE C21   N5     sing N N 455 
WHE C21   C22    sing N N 456 
WHE C20   N5     sing N N 457 
WHE N5    C23    sing N N 458 
WHE C22   C23    sing N N 459 
WHE C5    H2     sing N N 460 
WHE N4    H10    sing N N 461 
WHE C8    H3     sing N N 462 
WHE C11   H5     sing N N 463 
WHE C13   H7     sing N N 464 
WHE C15   H8     sing N N 465 
WHE C20   H14    sing N N 466 
WHE C20   H15    sing N N 467 
WHE C22   H18    sing N N 468 
WHE C22   H19    sing N N 469 
WHE C23   H20    sing N N 470 
WHE C23   H21    sing N N 471 
WHE C12   H6     sing N N 472 
WHE C17   H9     sing N N 473 
WHE C19   H13    sing N N 474 
WHE C19   H11    sing N N 475 
WHE C19   H12    sing N N 476 
WHE C21   H16    sing N N 477 
WHE C21   H17    sing N N 478 
WHE C4    H1     sing N N 479 
WHE N3    H4     sing N N 480 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Institute on Aging (NIH/NIA)' 
_pdbx_audit_support.country                'United States' 
_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   4KIN 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8VWM 
_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]   0.015124 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014128 
_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]   0.012979 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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      . ARG A 1 12  ? -41.80700 11.82100  -26.09600 1.000 42.64913 ? 5   ARG A N      1 
ATOM   2    C  CA     . ARG A 1 12  ? -41.17900 10.69100  -25.41900 1.000 35.56993 ? 5   ARG A CA     1 
ATOM   3    C  C      . ARG A 1 12  ? -41.37800 9.42100   -26.24900 1.000 38.91237 ? 5   ARG A C      1 
ATOM   4    O  O      . ARG A 1 12  ? -42.51800 9.05700   -26.56800 1.000 39.07060 ? 5   ARG A O      1 
ATOM   5    C  CB     . ARG A 1 12  ? -41.78600 10.49600  -24.02900 1.000 38.86829 ? 5   ARG A CB     1 
ATOM   6    C  CG     . ARG A 1 12  ? -41.41900 9.18400   -23.35600 1.000 34.25090 ? 5   ARG A CG     1 
ATOM   7    C  CD     . ARG A 1 12  ? -42.18100 8.97100   -22.03900 1.000 37.09001 ? 5   ARG A CD     1 
ATOM   8    N  NE     . ARG A 1 12  ? -41.62600 7.86100   -21.27000 1.000 38.95314 ? 5   ARG A NE     1 
ATOM   9    C  CZ     . ARG A 1 12  ? -42.22000 6.68400   -21.13100 1.000 38.89112 ? 5   ARG A CZ     1 
ATOM   10   N  NH1    . ARG A 1 12  ? -43.35400 6.40700   -21.75100 1.000 45.16513 ? 5   ARG A NH1    1 
ATOM   11   N  NH2    . ARG A 1 12  ? -41.63900 5.74800   -20.38900 1.000 33.52946 ? 5   ARG A NH2    1 
ATOM   12   N  N      . PRO A 1 13  ? -40.29200 8.73900   -26.62900 1.000 31.79125 ? 6   PRO A N      1 
ATOM   13   C  CA     . PRO A 1 13  ? -40.43800 7.44900   -27.31900 1.000 27.65666 ? 6   PRO A CA     1 
ATOM   14   C  C      . PRO A 1 13  ? -41.22600 6.46400   -26.47500 1.000 28.73248 ? 6   PRO A C      1 
ATOM   15   O  O      . PRO A 1 13  ? -41.37500 6.61600   -25.26200 1.000 27.00836 ? 6   PRO A O      1 
ATOM   16   C  CB     . PRO A 1 13  ? -38.98700 6.97400   -27.50400 1.000 26.81333 ? 6   PRO A CB     1 
ATOM   17   C  CG     . PRO A 1 13  ? -38.19500 7.78500   -26.51300 1.000 31.43365 ? 6   PRO A CG     1 
ATOM   18   C  CD     . PRO A 1 13  ? -38.88100 9.12300   -26.49000 1.000 38.13047 ? 6   PRO A CD     1 
ATOM   19   N  N      . THR A 1 14  ? -41.74300 5.44200   -27.14400 1.000 28.08007 ? 7   THR A N      1 
ATOM   20   C  CA     . THR A 1 14  ? -42.33100 4.30800   -26.44700 1.000 27.96875 ? 7   THR A CA     1 
ATOM   21   C  C      . THR A 1 14  ? -41.22500 3.36300   -25.99400 1.000 23.56815 ? 7   THR A C      1 
ATOM   22   O  O      . THR A 1 14  ? -40.31800 3.03100   -26.76400 1.000 20.94152 ? 7   THR A O      1 
ATOM   23   C  CB     . THR A 1 14  ? -43.32800 3.56200   -27.34800 1.000 30.39879 ? 7   THR A CB     1 
ATOM   24   O  OG1    . THR A 1 14  ? -44.29900 4.49700   -27.84800 1.000 34.18440 ? 7   THR A OG1    1 
ATOM   25   C  CG2    . THR A 1 14  ? -44.01500 2.43200   -26.60200 1.000 28.67370 ? 7   THR A CG2    1 
ATOM   26   N  N      . PHE A 1 15  ? -41.30400 2.93400   -24.74200 1.000 22.73810 ? 8   PHE A N      1 
ATOM   27   C  CA     . PHE A 1 15  ? -40.33000 2.03600   -24.14700 1.000 21.51602 ? 8   PHE A CA     1 
ATOM   28   C  C      . PHE A 1 15  ? -40.88100 0.62000   -24.17700 1.000 20.84578 ? 8   PHE A C      1 
ATOM   29   O  O      . PHE A 1 15  ? -42.09600 0.40800   -24.15400 1.000 25.12242 ? 8   PHE A O      1 
ATOM   30   C  CB     . PHE A 1 15  ? -40.02600 2.45000   -22.70400 1.000 22.73248 ? 8   PHE A CB     1 
ATOM   31   C  CG     . PHE A 1 15  ? -39.10000 3.62800   -22.59300 1.000 21.30473 ? 8   PHE A CG     1 
ATOM   32   C  CD1    . PHE A 1 15  ? -39.54700 4.89500   -22.91300 1.000 20.38087 ? 8   PHE A CD1    1 
ATOM   33   C  CD2    . PHE A 1 15  ? -37.79100 3.46800   -22.15400 1.000 21.19585 ? 8   PHE A CD2    1 
ATOM   34   C  CE1    . PHE A 1 15  ? -38.70900 5.99700   -22.82000 1.000 26.06239 ? 8   PHE A CE1    1 
ATOM   35   C  CE2    . PHE A 1 15  ? -36.95100 4.56100   -22.04900 1.000 22.49706 ? 8   PHE A CE2    1 
ATOM   36   C  CZ     . PHE A 1 15  ? -37.40800 5.83200   -22.39400 1.000 19.34250 ? 8   PHE A CZ     1 
ATOM   37   N  N      . TYR A 1 16  ? -39.98400 -0.35300  -24.24100 1.000 16.26601 ? 9   TYR A N      1 
ATOM   38   C  CA     . TYR A 1 16  ? -40.36100 -1.74800  -24.07500 1.000 20.20989 ? 9   TYR A CA     1 
ATOM   39   C  C      . TYR A 1 16  ? -39.40700 -2.40100  -23.09300 1.000 24.93757 ? 9   TYR A C      1 
ATOM   40   O  O      . TYR A 1 16  ? -38.30500 -1.89700  -22.84200 1.000 19.72472 ? 9   TYR A O      1 
ATOM   41   C  CB     . TYR A 1 16  ? -40.40100 -2.48600  -25.42200 1.000 22.67962 ? 9   TYR A CB     1 
ATOM   42   C  CG     . TYR A 1 16  ? -39.06300 -2.88200  -26.01200 1.000 19.66174 ? 9   TYR A CG     1 
ATOM   43   C  CD1    . TYR A 1 16  ? -38.31300 -1.95500  -26.74600 1.000 20.47590 ? 9   TYR A CD1    1 
ATOM   44   C  CD2    . TYR A 1 16  ? -38.58100 -4.18600  -25.91500 1.000 23.37508 ? 9   TYR A CD2    1 
ATOM   45   C  CE1    . TYR A 1 16  ? -37.09100 -2.30300  -27.32300 1.000 15.84028 ? 9   TYR A CE1    1 
ATOM   46   C  CE2    . TYR A 1 16  ? -37.36300 -4.54800  -26.49900 1.000 23.05643 ? 9   TYR A CE2    1 
ATOM   47   C  CZ     . TYR A 1 16  ? -36.62400 -3.60100  -27.19900 1.000 18.81516 ? 9   TYR A CZ     1 
ATOM   48   O  OH     . TYR A 1 16  ? -35.41400 -3.95900  -27.78000 1.000 20.79225 ? 9   TYR A OH     1 
ATOM   49   N  N      . ARG A 1 17  ? -39.84700 -3.51100  -22.50000 1.000 21.14836 ? 10  ARG A N      1 
ATOM   50   C  CA     . ARG A 1 17  ? -39.04200 -4.16100  -21.47700 1.000 24.70287 ? 10  ARG A CA     1 
ATOM   51   C  C      . ARG A 1 17  ? -38.65700 -5.55500  -21.93600 1.000 29.21907 ? 10  ARG A C      1 
ATOM   52   O  O      . ARG A 1 17  ? -39.44400 -6.24300  -22.59000 1.000 28.57339 ? 10  ARG A O      1 
ATOM   53   C  CB     . ARG A 1 17  ? -39.75400 -4.25300  -20.12400 1.000 29.08211 ? 10  ARG A CB     1 
ATOM   54   C  CG     . ARG A 1 17  ? -40.00200 -2.88800  -19.51000 1.000 34.15370 ? 10  ARG A CG     1 
ATOM   55   C  CD     . ARG A 1 17  ? -40.75200 -2.96000  -18.19300 1.000 45.13721 ? 10  ARG A CD     1 
ATOM   56   N  NE     . ARG A 1 17  ? -40.72700 -4.31000  -17.64600 1.000 42.69392 ? 10  ARG A NE     1 
ATOM   57   C  CZ     . ARG A 1 17  ? -40.79000 -4.58200  -16.35000 1.000 45.94914 ? 10  ARG A CZ     1 
ATOM   58   N  NH1    . ARG A 1 17  ? -40.80900 -3.61600  -15.44400 1.000 40.12297 ? 10  ARG A NH1    1 
ATOM   59   N  NH2    . ARG A 1 17  ? -40.78800 -5.85200  -15.95200 1.000 46.19409 ? 10  ARG A NH2    1 
ATOM   60   N  N      . GLN A 1 18  ? -37.43400 -5.94800  -21.60100 1.000 23.27627 ? 11  GLN A N      1 
ATOM   61   C  CA     . GLN A 1 18  ? -36.87700 -7.24300  -21.95600 1.000 28.56426 ? 11  GLN A CA     1 
ATOM   62   C  C      . GLN A 1 18  ? -35.85400 -7.60800  -20.89400 1.000 36.05393 ? 11  GLN A C      1 
ATOM   63   O  O      . GLN A 1 18  ? -35.16500 -6.73100  -20.36500 1.000 32.71793 ? 11  GLN A O      1 
ATOM   64   C  CB     . GLN A 1 18  ? -36.24800 -7.20200  -23.35200 1.000 31.15402 ? 11  GLN A CB     1 
ATOM   65   C  CG     . GLN A 1 18  ? -35.08200 -8.14400  -23.55700 1.000 35.85517 ? 11  GLN A CG     1 
ATOM   66   C  CD     . GLN A 1 18  ? -34.83700 -8.45300  -25.01600 1.000 38.20588 ? 11  GLN A CD     1 
ATOM   67   O  OE1    . GLN A 1 18  ? -34.73800 -7.55200  -25.85300 1.000 43.64233 ? 11  GLN A OE1    1 
ATOM   68   N  NE2    . GLN A 1 18  ? -34.77500 -9.73900  -25.33800 1.000 47.35980 ? 11  GLN A NE2    1 
ATOM   69   N  N      . GLU A 1 19  ? -35.76500 -8.88900  -20.55500 1.000 30.94005 ? 12  GLU A N      1 
ATOM   70   C  CA     . GLU A 1 19  ? -34.81000 -9.31700  -19.54400 1.000 31.72230 ? 12  GLU A CA     1 
ATOM   71   C  C      . GLU A 1 19  ? -33.68800 -10.10900 -20.21300 1.000 35.33507 ? 12  GLU A C      1 
ATOM   72   O  O      . GLU A 1 19  ? -33.94800 -10.96800 -21.06500 1.000 37.98885 ? 12  GLU A O      1 
ATOM   73   C  CB     . GLU A 1 19  ? -35.49600 -10.12700 -18.43700 1.000 39.14804 ? 12  GLU A CB     1 
ATOM   74   C  CG     . GLU A 1 19  ? -34.59500 -11.12900 -17.74900 1.000 39.29759 ? 12  GLU A CG     1 
ATOM   75   C  CD     . GLU A 1 19  ? -35.35500 -12.16000 -16.92600 1.000 41.56513 ? 12  GLU A CD     1 
ATOM   76   O  OE1    . GLU A 1 19  ? -36.50700 -11.89500 -16.51800 1.000 38.92191 ? 12  GLU A OE1    1 
ATOM   77   O  OE2    . GLU A 1 19  ? -34.76300 -13.22200 -16.64200 1.000 38.25207 ? 12  GLU A OE2    1 
ATOM   78   N  N      . LEU A 1 20  ? -32.44500 -9.78800  -19.84600 1.000 34.07808 ? 13  LEU A N      1 
ATOM   79   C  CA     . LEU A 1 20  ? -31.24200 -10.41300 -20.38000 1.000 38.37704 ? 13  LEU A CA     1 
ATOM   80   C  C      . LEU A 1 20  ? -30.30900 -10.73200 -19.22500 1.000 41.78856 ? 13  LEU A C      1 
ATOM   81   O  O      . LEU A 1 20  ? -30.08600 -9.88400  -18.35700 1.000 39.26797 ? 13  LEU A O      1 
ATOM   82   C  CB     . LEU A 1 20  ? -30.51500 -9.49600  -21.37600 1.000 41.27189 ? 13  LEU A CB     1 
ATOM   83   C  CG     . LEU A 1 20  ? -31.30300 -8.98600  -22.58100 1.000 37.52846 ? 13  LEU A CG     1 
ATOM   84   C  CD1    . LEU A 1 20  ? -30.79900 -7.60700  -22.99700 1.000 39.25468 ? 13  LEU A CD1    1 
ATOM   85   C  CD2    . LEU A 1 20  ? -31.22300 -9.96100  -23.73900 1.000 37.98008 ? 13  LEU A CD2    1 
ATOM   86   N  N      . ASN A 1 21  ? -29.76000 -11.94800 -19.22100 1.000 44.51082 ? 14  ASN A N      1 
ATOM   87   C  CA     . ASN A 1 21  ? -28.87700 -12.41100 -18.14300 1.000 47.40233 ? 14  ASN A CA     1 
ATOM   88   C  C      . ASN A 1 21  ? -29.35300 -11.88900 -16.78800 1.000 43.15926 ? 14  ASN A C      1 
ATOM   89   O  O      . ASN A 1 21  ? -28.59800 -11.29900 -16.01100 1.000 41.71145 ? 14  ASN A O      1 
ATOM   90   C  CB     . ASN A 1 21  ? -27.42100 -12.00500 -18.40000 1.000 47.19217 ? 14  ASN A CB     1 
ATOM   91   C  CG     . ASN A 1 21  ? -26.81500 -12.68300 -19.62600 1.000 58.08160 ? 14  ASN A CG     1 
ATOM   92   O  OD1    . ASN A 1 21  ? -27.50200 -13.37300 -20.38400 1.000 55.95940 ? 14  ASN A OD1    1 
ATOM   93   N  ND2    . ASN A 1 21  ? -25.51700 -12.46800 -19.83300 1.000 62.62875 ? 14  ASN A ND2    1 
ATOM   94   N  N      . LYS A 1 22  ? -30.64600 -12.07900 -16.52500 1.000 44.21954 ? 15  LYS A N      1 
ATOM   95   C  CA     . LYS A 1 22  ? -31.28100 -11.81400 -15.23700 1.000 41.96857 ? 15  LYS A CA     1 
ATOM   96   C  C      . LYS A 1 22  ? -31.44800 -10.32900 -14.92900 1.000 43.59984 ? 15  LYS A C      1 
ATOM   97   O  O      . LYS A 1 22  ? -31.96700 -9.99700  -13.85400 1.000 48.40291 ? 15  LYS A O      1 
ATOM   98   C  CB     . LYS A 1 22  ? -30.51800 -12.47900 -14.07900 1.000 44.00070 ? 15  LYS A CB     1 
ATOM   99   C  CG     . LYS A 1 22  ? -30.91800 -13.93400 -13.79300 1.000 46.35459 ? 15  LYS A CG     1 
ATOM   100  C  CD     . LYS A 1 22  ? -32.33500 -14.04500 -13.23800 1.000 43.96382 ? 15  LYS A CD     1 
ATOM   101  C  CE     . LYS A 1 22  ? -33.38300 -14.02500 -14.33200 1.000 40.41419 ? 15  LYS A CE     1 
ATOM   102  N  NZ     . LYS A 1 22  ? -34.71100 -14.53000 -13.85800 1.000 41.69889 ? 15  LYS A NZ     1 
ATOM   103  N  N      . THR A 1 23  ? -31.03700 -9.42400  -15.81500 1.000 39.49360 ? 16  THR A N      1 
ATOM   104  C  CA     . THR A 1 23  ? -31.24500 -7.99300  -15.60900 1.000 42.07924 ? 16  THR A CA     1 
ATOM   105  C  C      . THR A 1 23  ? -32.30900 -7.47600  -16.57400 1.000 33.62054 ? 16  THR A C      1 
ATOM   106  O  O      . THR A 1 23  ? -32.35700 -7.88300  -17.74000 1.000 31.31634 ? 16  THR A O      1 
ATOM   107  C  CB     . THR A 1 23  ? -29.94700 -7.18400  -15.78700 1.000 42.27820 ? 16  THR A CB     1 
ATOM   108  O  OG1    . THR A 1 23  ? -29.68200 -6.98800  -17.18300 1.000 45.83790 ? 16  THR A OG1    1 
ATOM   109  C  CG2    . THR A 1 23  ? -28.75400 -7.88000  -15.12800 1.000 39.28278 ? 16  THR A CG2    1 
ATOM   110  N  N      . ILE A 1 24  ? -33.14800 -6.57400  -16.08300 1.000 29.82892 ? 17  ILE A N      1 
ATOM   111  C  CA     . ILE A 1 24  ? -34.26600 -6.04200  -16.84900 1.000 34.60941 ? 17  ILE A CA     1 
ATOM   112  C  C      . ILE A 1 24  ? -33.83100 -4.78300  -17.58500 1.000 29.90208 ? 17  ILE A C      1 
ATOM   113  O  O      . ILE A 1 24  ? -33.27400 -3.85400  -16.98300 1.000 24.55571 ? 17  ILE A O      1 
ATOM   114  C  CB     . ILE A 1 24  ? -35.46500 -5.74900  -15.93600 1.000 28.86089 ? 17  ILE A CB     1 
ATOM   115  C  CG1    . ILE A 1 24  ? -35.90400 -7.01700  -15.19900 1.000 34.72663 ? 17  ILE A CG1    1 
ATOM   116  C  CG2    . ILE A 1 24  ? -36.61300 -5.14900  -16.74500 1.000 36.42886 ? 17  ILE A CG2    1 
ATOM   117  C  CD1    . ILE A 1 24  ? -35.59500 -8.30900  -15.93200 1.000 40.34813 ? 17  ILE A CD1    1 
ATOM   118  N  N      . TRP A 1 25  ? -34.10700 -4.74000  -18.88600 1.000 25.55572 ? 18  TRP A N      1 
ATOM   119  C  CA     . TRP A 1 25  ? -33.76300 -3.59900  -19.72400 1.000 22.42004 ? 18  TRP A CA     1 
ATOM   120  C  C      . TRP A 1 25  ? -35.05900 -2.95300  -20.19800 1.000 23.71373 ? 18  TRP A C      1 
ATOM   121  O  O      . TRP A 1 25  ? -35.90300 -3.62600  -20.80000 1.000 24.82329 ? 18  TRP A O      1 
ATOM   122  C  CB     . TRP A 1 25  ? -32.88000 -4.03400  -20.90000 1.000 24.14893 ? 18  TRP A CB     1 
ATOM   123  C  CG     . TRP A 1 25  ? -31.48200 -4.41500  -20.47500 1.000 29.67673 ? 18  TRP A CG     1 
ATOM   124  C  CD1    . TRP A 1 25  ? -31.10700 -5.57100  -19.85100 1.000 35.15519 ? 18  TRP A CD1    1 
ATOM   125  C  CD2    . TRP A 1 25  ? -30.28500 -3.62600  -20.60500 1.000 23.45504 ? 18  TRP A CD2    1 
ATOM   126  N  NE1    . TRP A 1 25  ? -29.75300 -5.56500  -19.60200 1.000 35.82101 ? 18  TRP A NE1    1 
ATOM   127  C  CE2    . TRP A 1 25  ? -29.22400 -4.38200  -20.04900 1.000 31.61347 ? 18  TRP A CE2    1 
ATOM   128  C  CE3    . TRP A 1 25  ? -30.00800 -2.36100  -21.14000 1.000 21.13180 ? 18  TRP A CE3    1 
ATOM   129  C  CZ2    . TRP A 1 25  ? -27.90300 -3.91700  -20.02000 1.000 24.15605 ? 18  TRP A CZ2    1 
ATOM   130  C  CZ3    . TRP A 1 25  ? -28.69400 -1.90000  -21.11200 1.000 17.08120 ? 18  TRP A CZ3    1 
ATOM   131  C  CH2    . TRP A 1 25  ? -27.66200 -2.67700  -20.55300 1.000 19.85867 ? 18  TRP A CH2    1 
ATOM   132  N  N      . GLU A 1 26  ? -35.22700 -1.66000  -19.90300 1.000 19.74419 ? 19  GLU A N      1 
ATOM   133  C  CA     . GLU A 1 26  ? -36.35700 -0.85300  -20.36900 1.000 19.34264 ? 19  GLU A CA     1 
ATOM   134  C  C      . GLU A 1 26  ? -35.82200 0.20900   -21.32400 1.000 20.37689 ? 19  GLU A C      1 
ATOM   135  O  O      . GLU A 1 26  ? -35.21100 1.18200   -20.87500 1.000 19.46455 ? 19  GLU A O      1 
ATOM   136  C  CB     . GLU A 1 26  ? -37.06200 -0.17600  -19.19400 1.000 23.96229 ? 19  GLU A CB     1 
ATOM   137  C  CG     . GLU A 1 26  ? -37.69000 -1.12600  -18.20300 1.000 31.45522 ? 19  GLU A CG     1 
ATOM   138  C  CD     . GLU A 1 26  ? -38.57800 -0.40000  -17.21100 1.000 39.02218 ? 19  GLU A CD     1 
ATOM   139  O  OE1    . GLU A 1 26  ? -38.03700 0.21200   -16.25800 1.000 35.48197 ? 19  GLU A OE1    1 
ATOM   140  O  OE2    . GLU A 1 26  ? -39.81100 -0.41900  -17.40000 1.000 40.97331 ? 19  GLU A OE2    1 
ATOM   141  N  N      . VAL A 1 27  ? -36.07300 0.06400   -22.62200 1.000 17.41790 ? 20  VAL A N      1 
ATOM   142  C  CA     . VAL A 1 27  ? -35.41800 0.94800   -23.59200 1.000 18.28612 ? 20  VAL A CA     1 
ATOM   143  C  C      . VAL A 1 27  ? -36.42200 1.38500   -24.64900 1.000 18.63256 ? 20  VAL A C      1 
ATOM   144  O  O      . VAL A 1 27  ? -37.48000 0.76400   -24.81900 1.000 18.66483 ? 20  VAL A O      1 
ATOM   145  C  CB     . VAL A 1 27  ? -34.21100 0.26200   -24.26200 1.000 16.85940 ? 20  VAL A CB     1 
ATOM   146  C  CG1    . VAL A 1 27  ? -33.17600 -0.13200  -23.19600 1.000 16.18427 ? 20  VAL A CG1    1 
ATOM   147  C  CG2    . VAL A 1 27  ? -34.64700 -0.93900  -25.10600 1.000 14.81979 ? 20  VAL A CG2    1 
ATOM   148  N  N      . PRO A 1 28  ? -36.11600 2.46800   -25.37300 1.000 12.65594 ? 21  PRO A N      1 
ATOM   149  C  CA     . PRO A 1 28  ? -36.97300 2.87400   -26.49800 1.000 19.12573 ? 21  PRO A CA     1 
ATOM   150  C  C      . PRO A 1 28  ? -37.01100 1.82600   -27.60200 1.000 19.69327 ? 21  PRO A C      1 
ATOM   151  O  O      . PRO A 1 28  ? -36.00600 1.17500   -27.89900 1.000 17.34292 ? 21  PRO A O      1 
ATOM   152  C  CB     . PRO A 1 28  ? -36.30500 4.15500   -27.00300 1.000 18.58561 ? 21  PRO A CB     1 
ATOM   153  C  CG     . PRO A 1 28  ? -35.60500 4.71100   -25.80500 1.000 18.81620 ? 21  PRO A CG     1 
ATOM   154  C  CD     . PRO A 1 28  ? -35.12300 3.50300   -25.03500 1.000 15.20816 ? 21  PRO A CD     1 
ATOM   155  N  N      . GLU A 1 29  ? -38.18000 1.72300   -28.25700 1.000 16.85771 ? 22  GLU A N      1 
ATOM   156  C  CA     . GLU A 1 29  ? -38.37000 0.76700   -29.35200 1.000 13.88302 ? 22  GLU A CA     1 
ATOM   157  C  C      . GLU A 1 29  ? -37.27800 0.87700   -30.40600 1.000 15.76099 ? 22  GLU A C      1 
ATOM   158  O  O      . GLU A 1 29  ? -36.93300 -0.12300  -31.04900 1.000 16.76444 ? 22  GLU A O      1 
ATOM   159  C  CB     . GLU A 1 29  ? -39.74500 0.97400   -30.00000 1.000 17.74004 ? 22  GLU A CB     1 
ATOM   160  C  CG     . GLU A 1 29  ? -40.91100 0.74200   -29.04100 1.000 25.09073 ? 22  GLU A CG     1 
ATOM   161  C  CD     . GLU A 1 29  ? -42.27400 1.01500   -29.67300 1.000 26.94109 ? 22  GLU A CD     1 
ATOM   162  O  OE1    . GLU A 1 29  ? -42.37600 1.96700   -30.48200 1.000 22.79639 ? 22  GLU A OE1    1 
ATOM   163  O  OE2    . GLU A 1 29  ? -43.23900 0.28200   -29.33500 1.000 22.34637 ? 22  GLU A OE2    1 
ATOM   164  N  N      . ARG A 1 30  ? -36.70900 2.06900   -30.59100 1.000 16.25514 ? 23  ARG A N      1 
ATOM   165  C  CA     . ARG A 1 30  ? -35.69700 2.22000   -31.63100 1.000 18.69226 ? 23  ARG A CA     1 
ATOM   166  C  C      . ARG A 1 30  ? -34.53600 1.24600   -31.44600 1.000 16.86432 ? 23  ARG A C      1 
ATOM   167  O  O      . ARG A 1 30  ? -33.89500 0.86200   -32.43100 1.000 17.65537 ? 23  ARG A O      1 
ATOM   168  C  CB     . ARG A 1 30  ? -35.18500 3.66600   -31.69500 1.000 19.79003 ? 23  ARG A CB     1 
ATOM   169  C  CG     . ARG A 1 30  ? -34.04800 3.99500   -30.73900 1.000 21.64438 ? 23  ARG A CG     1 
ATOM   170  C  CD     . ARG A 1 30  ? -33.72200 5.50700   -30.69200 1.000 20.00122 ? 23  ARG A CD     1 
ATOM   171  N  NE     . ARG A 1 30  ? -32.55600 5.81900   -31.51600 1.000 21.31764 ? 23  ARG A NE     1 
ATOM   172  C  CZ     . ARG A 1 30  ? -32.00100 7.01900   -31.62200 1.000 24.79020 ? 23  ARG A CZ     1 
ATOM   173  N  NH1    . ARG A 1 30  ? -32.52000 8.08000   -31.01400 1.000 23.88470 ? 23  ARG A NH1    1 
ATOM   174  N  NH2    . ARG A 1 30  ? -30.87200 7.15000   -32.31300 1.000 21.14348 ? 23  ARG A NH2    1 
ATOM   175  N  N      . TYR A 1 31  ? -34.26200 0.81300   -30.21300 1.000 15.20774 ? 24  TYR A N      1 
ATOM   176  C  CA     . TYR A 1 31  ? -33.14200 -0.09200  -29.94200 1.000 17.83223 ? 24  TYR A CA     1 
ATOM   177  C  C      . TYR A 1 31  ? -33.64000 -1.53900  -29.92300 1.000 14.55431 ? 24  TYR A C      1 
ATOM   178  O  O      . TYR A 1 31  ? -34.36800 -1.93700  -29.00600 1.000 17.18036 ? 24  TYR A O      1 
ATOM   179  C  CB     . TYR A 1 31  ? -32.46400 0.28200   -28.62100 1.000 13.92616 ? 24  TYR A CB     1 
ATOM   180  C  CG     . TYR A 1 31  ? -31.91000 1.70100   -28.61300 1.000 15.61313 ? 24  TYR A CG     1 
ATOM   181  C  CD1    . TYR A 1 31  ? -30.88100 2.06400   -29.46800 1.000 11.43039 ? 24  TYR A CD1    1 
ATOM   182  C  CD2    . TYR A 1 31  ? -32.43000 2.67300   -27.76600 1.000 15.14748 ? 24  TYR A CD2    1 
ATOM   183  C  CE1    . TYR A 1 31  ? -30.38200 3.36600   -29.49000 1.000 13.99210 ? 24  TYR A CE1    1 
ATOM   184  C  CE2    . TYR A 1 31  ? -31.93200 3.98100   -27.77200 1.000 15.26141 ? 24  TYR A CE2    1 
ATOM   185  C  CZ     . TYR A 1 31  ? -30.90500 4.31500   -28.63900 1.000 18.30665 ? 24  TYR A CZ     1 
ATOM   186  O  OH     . TYR A 1 31  ? -30.39100 5.61000   -28.66800 1.000 16.71982 ? 24  TYR A OH     1 
ATOM   187  N  N      . GLN A 1 32  ? -33.23300 -2.32500  -30.92300 1.000 14.16517 ? 25  GLN A N      1 
ATOM   188  C  CA     . GLN A 1 32  ? -33.64500 -3.71700  -31.07500 1.000 17.72016 ? 25  GLN A CA     1 
ATOM   189  C  C      . GLN A 1 32  ? -32.44900 -4.65000  -30.93100 1.000 19.20626 ? 25  GLN A C      1 
ATOM   190  O  O      . GLN A 1 32  ? -31.29800 -4.21300  -30.82600 1.000 17.52271 ? 25  GLN A O      1 
ATOM   191  C  CB     . GLN A 1 32  ? -34.31200 -3.95800  -32.43700 1.000 20.25149 ? 25  GLN A CB     1 
ATOM   192  C  CG     . GLN A 1 32  ? -35.59000 -3.18200  -32.63500 1.000 17.26386 ? 25  GLN A CG     1 
ATOM   193  C  CD     . GLN A 1 32  ? -36.73200 -3.76700  -31.80500 1.000 18.76694 ? 25  GLN A CD     1 
ATOM   194  O  OE1    . GLN A 1 32  ? -37.02500 -4.97200  -31.87800 1.000 17.00626 ? 25  GLN A OE1    1 
ATOM   195  N  NE2    . GLN A 1 32  ? -37.39300 -2.91600  -31.03000 1.000 16.09811 ? 25  GLN A NE2    1 
ATOM   196  N  N      . ASN A 1 33  ? -32.73000 -5.95900  -30.93200 1.000 19.91552 ? 26  ASN A N      1 
ATOM   197  C  CA     . ASN A 1 33  ? -31.68500 -6.98500  -30.94700 1.000 19.53299 ? 26  ASN A CA     1 
ATOM   198  C  C      . ASN A 1 33  ? -30.69900 -6.82200  -29.78800 1.000 18.00409 ? 26  ASN A C      1 
ATOM   199  O  O      . ASN A 1 33  ? -29.48400 -6.87300  -29.97600 1.000 21.31228 ? 26  ASN A O      1 
ATOM   200  C  CB     . ASN A 1 33  ? -30.93700 -6.99300  -32.29100 1.000 21.28045 ? 26  ASN A CB     1 
ATOM   201  C  CG     . ASN A 1 33  ? -31.86400 -6.89300  -33.50300 1.000 32.75900 ? 26  ASN A CG     1 
ATOM   202  O  OD1    . ASN A 1 33  ? -31.82400 -5.92000  -34.26500 1.000 28.45580 ? 26  ASN A OD1    1 
ATOM   203  N  ND2    . ASN A 1 33  ? -32.65900 -7.94000  -33.72100 1.000 29.87937 ? 26  ASN A ND2    1 
ATOM   204  N  N      . LEU A 1 34  ? -31.22200 -6.63500  -28.57800 1.000 18.29516 ? 27  LEU A N      1 
ATOM   205  C  CA     . LEU A 1 34  ? -30.34800 -6.51600  -27.41200 1.000 22.22289 ? 27  LEU A CA     1 
ATOM   206  C  C      . LEU A 1 34  ? -29.63600 -7.83800  -27.13000 1.000 27.24896 ? 27  LEU A C      1 
ATOM   207  O  O      . LEU A 1 34  ? -30.28400 -8.88400  -26.98900 1.000 23.41807 ? 27  LEU A O      1 
ATOM   208  C  CB     . LEU A 1 34  ? -31.16300 -6.09000  -26.19000 1.000 26.49959 ? 27  LEU A CB     1 
ATOM   209  C  CG     . LEU A 1 34  ? -31.33100 -4.58600  -25.95100 1.000 27.30396 ? 27  LEU A CG     1 
ATOM   210  C  CD1    . LEU A 1 34  ? -32.09700 -3.97000  -27.09600 1.000 22.49159 ? 27  LEU A CD1    1 
ATOM   211  C  CD2    . LEU A 1 34  ? -32.07500 -4.35100  -24.64200 1.000 30.78104 ? 27  LEU A CD2    1 
ATOM   212  N  N      . SER A 1 35  ? -28.29900 -7.79500  -27.04400 1.000 21.58118 ? 28  SER A N      1 
ATOM   213  C  CA     . SER A 1 35  ? -27.49300 -8.95200  -26.66400 1.000 24.38305 ? 28  SER A CA     1 
ATOM   214  C  C      . SER A 1 35  ? -26.42400 -8.48500  -25.68700 1.000 29.81924 ? 28  SER A C      1 
ATOM   215  O  O      . SER A 1 35  ? -25.80900 -7.43500  -25.90500 1.000 25.34119 ? 28  SER A O      1 
ATOM   216  C  CB     . SER A 1 35  ? -26.82000 -9.62500  -27.87800 1.000 28.86590 ? 28  SER A CB     1 
ATOM   217  O  OG     . SER A 1 35  ? -26.50700 -8.67600  -28.87100 1.000 33.39682 ? 28  SER A OG     1 
ATOM   218  N  N      . PRO A 1 36  ? -26.17300 -9.23600  -24.61800 1.000 43.27476 ? 29  PRO A N      1 
ATOM   219  C  CA     . PRO A 1 36  ? -25.37400 -8.71000  -23.50500 1.000 44.23609 ? 29  PRO A CA     1 
ATOM   220  C  C      . PRO A 1 36  ? -23.87700 -8.84300  -23.75500 1.000 43.47609 ? 29  PRO A C      1 
ATOM   221  O  O      . PRO A 1 36  ? -23.33900 -9.95000  -23.82800 1.000 55.85052 ? 29  PRO A O      1 
ATOM   222  C  CB     . PRO A 1 36  ? -25.84000 -9.56700  -22.32100 1.000 47.80808 ? 29  PRO A CB     1 
ATOM   223  C  CG     . PRO A 1 36  ? -26.12800 -10.90100 -22.95100 1.000 51.37908 ? 29  PRO A CG     1 
ATOM   224  C  CD     . PRO A 1 36  ? -26.56500 -10.63900 -24.39200 1.000 45.04921 ? 29  PRO A CD     1 
ATOM   225  N  N      . VAL A 1 37  ? -23.20200 -7.69500  -23.87900 1.000 38.29645 ? 30  VAL A N      1 
ATOM   226  C  CA     . VAL A 1 37  ? -21.74900 -7.67800  -24.03000 1.000 36.62030 ? 30  VAL A CA     1 
ATOM   227  C  C      . VAL A 1 37  ? -21.07300 -8.11700  -22.73700 1.000 40.28035 ? 30  VAL A C      1 
ATOM   228  O  O      . VAL A 1 37  ? -20.10900 -8.89300  -22.75600 1.000 35.47612 ? 30  VAL A O      1 
ATOM   229  C  CB     . VAL A 1 37  ? -21.27000 -6.27900  -24.46300 1.000 32.90539 ? 30  VAL A CB     1 
ATOM   230  C  CG1    . VAL A 1 37  ? -19.80200 -6.31300  -24.88000 1.000 31.93800 ? 30  VAL A CG1    1 
ATOM   231  C  CG2    . VAL A 1 37  ? -22.14700 -5.73900  -25.58200 1.000 27.02336 ? 30  VAL A CG2    1 
ATOM   232  N  N      . GLY A 1 38  ? -21.55900 -7.63800  -21.59700 1.000 36.13876 ? 31  GLY A N      1 
ATOM   233  C  CA     . GLY A 1 38  ? -20.91500 -7.97700  -20.34100 1.000 44.35266 ? 31  GLY A CA     1 
ATOM   234  C  C      . GLY A 1 38  ? -21.68400 -7.45100  -19.15100 1.000 49.82489 ? 31  GLY A C      1 
ATOM   235  O  O      . GLY A 1 38  ? -22.62200 -6.65600  -19.27800 1.000 38.50433 ? 31  GLY A O      1 
ATOM   236  N  N      . SER A 1 39  ? -21.25700 -7.90900  -17.97700 1.000 54.58794 ? 32  SER A N      1 
ATOM   237  C  CA     . SER A 1 39  ? -21.88800 -7.53900  -16.72100 1.000 61.86790 ? 32  SER A CA     1 
ATOM   238  C  C      . SER A 1 39  ? -20.80500 -7.33800  -15.67600 1.000 69.89729 ? 32  SER A C      1 
ATOM   239  O  O      . SER A 1 39  ? -19.94400 -8.20400  -15.49600 1.000 70.11419 ? 32  SER A O      1 
ATOM   240  C  CB     . SER A 1 39  ? -22.88200 -8.61100  -16.25900 1.000 61.81658 ? 32  SER A CB     1 
ATOM   241  O  OG     . SER A 1 39  ? -24.14000 -8.03300  -15.95200 1.000 60.47735 ? 32  SER A OG     1 
ATOM   242  N  N      . GLY A 1 40  ? -20.84600 -6.19500  -15.00100 1.000 70.06260 ? 33  GLY A N      1 
ATOM   243  C  CA     . GLY A 1 40  ? -19.90300 -5.91500  -13.93600 1.000 76.31666 ? 33  GLY A CA     1 
ATOM   244  C  C      . GLY A 1 40  ? -20.54400 -5.02000  -12.90100 1.000 84.97151 ? 33  GLY A C      1 
ATOM   245  O  O      . GLY A 1 40  ? -21.57100 -4.37900  -13.15100 1.000 86.03283 ? 33  GLY A O      1 
ATOM   246  N  N      . ALA A 1 41  ? -19.93300 -4.99700  -11.71400 1.000 91.82436 ? 34  ALA A N      1 
ATOM   247  C  CA     . ALA A 1 41  ? -20.39900 -4.08200  -10.67900 1.000 95.82846 ? 34  ALA A CA     1 
ATOM   248  C  C      . ALA A 1 41  ? -20.32100 -2.63500  -11.15300 1.000 93.57939 ? 34  ALA A C      1 
ATOM   249  O  O      . ALA A 1 41  ? -21.12700 -1.79600  -10.73300 1.000 94.62921 ? 34  ALA A O      1 
ATOM   250  C  CB     . ALA A 1 41  ? -19.58500 -4.28100  -9.40100  1.000 91.09512 ? 34  ALA A CB     1 
ATOM   251  N  N      . TYR A 1 42  ? -19.36200 -2.33200  -12.03200 1.000 87.28173 ? 35  TYR A N      1 
ATOM   252  C  CA     . TYR A 1 42  ? -19.26100 -1.00400  -12.63100 1.000 81.95266 ? 35  TYR A CA     1 
ATOM   253  C  C      . TYR A 1 42  ? -20.46500 -0.67800  -13.51400 1.000 79.34241 ? 35  TYR A C      1 
ATOM   254  O  O      . TYR A 1 42  ? -20.83900 0.49500   -13.64400 1.000 75.36199 ? 35  TYR A O      1 
ATOM   255  C  CB     . TYR A 1 42  ? -17.97300 -0.91700  -13.45000 1.000 80.51641 ? 35  TYR A CB     1 
ATOM   256  C  CG     . TYR A 1 42  ? -18.03100 -1.83700  -14.64500 1.000 79.01309 ? 35  TYR A CG     1 
ATOM   257  C  CD1    . TYR A 1 42  ? -17.84500 -3.20800  -14.49500 1.000 78.87950 ? 35  TYR A CD1    1 
ATOM   258  C  CD2    . TYR A 1 42  ? -18.32500 -1.35000  -15.91200 1.000 71.81527 ? 35  TYR A CD2    1 
ATOM   259  C  CE1    . TYR A 1 42  ? -17.92000 -4.06700  -15.57600 1.000 74.55226 ? 35  TYR A CE1    1 
ATOM   260  C  CE2    . TYR A 1 42  ? -18.40500 -2.20600  -17.00100 1.000 64.82609 ? 35  TYR A CE2    1 
ATOM   261  C  CZ     . TYR A 1 42  ? -18.19900 -3.56400  -16.82500 1.000 64.44078 ? 35  TYR A CZ     1 
ATOM   262  O  OH     . TYR A 1 42  ? -18.27700 -4.43200  -17.89000 1.000 57.19748 ? 35  TYR A OH     1 
ATOM   263  N  N      . GLY A 1 43  ? -21.06800 -1.68500  -14.14000 1.000 75.11270 ? 36  GLY A N      1 
ATOM   264  C  CA     . GLY A 1 43  ? -22.22100 -1.45400  -14.99600 1.000 62.50542 ? 36  GLY A CA     1 
ATOM   265  C  C      . GLY A 1 43  ? -22.62000 -2.72200  -15.72500 1.000 58.47551 ? 36  GLY A C      1 
ATOM   266  O  O      . GLY A 1 43  ? -21.87900 -3.71200  -15.75200 1.000 62.78415 ? 36  GLY A O      1 
ATOM   267  N  N      . SER A 1 44  ? -23.81700 -2.67300  -16.30800 1.000 38.92716 ? 37  SER A N      1 
ATOM   268  C  CA     . SER A 1 44  ? -24.33600 -3.73300  -17.16600 1.000 32.13298 ? 37  SER A CA     1 
ATOM   269  C  C      . SER A 1 44  ? -24.46200 -3.20000  -18.58900 1.000 21.07986 ? 37  SER A C      1 
ATOM   270  O  O      . SER A 1 44  ? -25.02500 -2.12400  -18.79800 1.000 17.09784 ? 37  SER A O      1 
ATOM   271  C  CB     . SER A 1 44  ? -25.69000 -4.22300  -16.65400 1.000 37.55116 ? 37  SER A CB     1 
ATOM   272  O  OG     . SER A 1 44  ? -25.86700 -5.59500  -16.95800 1.000 54.18719 ? 37  SER A OG     1 
ATOM   273  N  N      . VAL A 1 45  ? -23.95200 -3.94900  -19.56200 1.000 20.72063 ? 38  VAL A N      1 
ATOM   274  C  CA     . VAL A 1 45  ? -23.79200 -3.44700  -20.92100 1.000 18.10199 ? 38  VAL A CA     1 
ATOM   275  C  C      . VAL A 1 45  ? -24.36000 -4.45900  -21.90000 1.000 21.71403 ? 38  VAL A C      1 
ATOM   276  O  O      . VAL A 1 45  ? -24.08500 -5.66100  -21.79300 1.000 19.27590 ? 38  VAL A O      1 
ATOM   277  C  CB     . VAL A 1 45  ? -22.30400 -3.16600  -21.24400 1.000 19.53385 ? 38  VAL A CB     1 
ATOM   278  C  CG1    . VAL A 1 45  ? -22.13300 -2.67800  -22.68000 1.000 16.56731 ? 38  VAL A CG1    1 
ATOM   279  C  CG2    . VAL A 1 45  ? -21.72900 -2.13300  -20.28000 1.000 18.99385 ? 38  VAL A CG2    1 
ATOM   280  N  N      . CYS A 1 46  ? -25.11200 -3.97300  -22.88700 1.000 16.36451 ? 39  CYS A N      1 
ATOM   281  C  CA     . CYS A 1 46  ? -25.48500 -4.82700  -24.00300 1.000 19.07730 ? 39  CYS A CA     1 
ATOM   282  C  C      . CYS A 1 46  ? -25.21200 -4.10600  -25.31500 1.000 20.03809 ? 39  CYS A C      1 
ATOM   283  O  O      . CYS A 1 46  ? -25.11800 -2.87400  -25.37100 1.000 16.48530 ? 39  CYS A O      1 
ATOM   284  C  CB     . CYS A 1 46  ? -26.95900 -5.22700  -23.96200 1.000 25.07479 ? 39  CYS A CB     1 
ATOM   285  S  SG     . CYS A 1 46  ? -28.03400 -3.85800  -24.30500 1.000 30.53396 ? 39  CYS A SG     1 
ATOM   286  N  N      . ALA A 1 47  ? -25.11500 -4.90100  -26.37300 1.000 15.67809 ? 40  ALA A N      1 
ATOM   287  C  CA     . ALA A 1 47  ? -25.13700 -4.39100  -27.72700 1.000 16.71742 ? 40  ALA A CA     1 
ATOM   288  C  C      . ALA A 1 47  ? -26.58000 -4.34600  -28.23300 1.000 18.94772 ? 40  ALA A C      1 
ATOM   289  O  O      . ALA A 1 47  ? -27.43200 -5.13600  -27.81000 1.000 16.70699 ? 40  ALA A O      1 
ATOM   290  C  CB     . ALA A 1 47  ? -24.27200 -5.26600  -28.62800 1.000 18.02156 ? 40  ALA A CB     1 
ATOM   291  N  N      . ALA A 1 48  ? -26.85100 -3.38900  -29.12300 1.000 16.09227 ? 41  ALA A N      1 
ATOM   292  C  CA     . ALA A 1 48  ? -28.18100 -3.22900  -29.70300 1.000 13.92425 ? 41  ALA A CA     1 
ATOM   293  C  C      . ALA A 1 48  ? -28.02600 -2.68700  -31.11200 1.000 16.52785 ? 41  ALA A C      1 
ATOM   294  O  O      . ALA A 1 48  ? -26.96500 -2.16700  -31.48600 1.000 15.34412 ? 41  ALA A O      1 
ATOM   295  C  CB     . ALA A 1 48  ? -29.07000 -2.28800  -28.87800 1.000 16.21337 ? 41  ALA A CB     1 
ATOM   296  N  N      . PHE A 1 49  ? -29.09600 -2.81400  -31.89400 1.000 12.36024 ? 42  PHE A N      1 
ATOM   297  C  CA     . PHE A 1 49  ? -29.14400 -2.25000  -33.24000 1.000 14.99189 ? 42  PHE A CA     1 
ATOM   298  C  C      . PHE A 1 49  ? -30.07100 -1.03800  -33.19400 1.000 16.49979 ? 42  PHE A C      1 
ATOM   299  O  O      . PHE A 1 49  ? -31.22900 -1.16100  -32.77600 1.000 16.58328 ? 42  PHE A O      1 
ATOM   300  C  CB     . PHE A 1 49  ? -29.63500 -3.28600  -34.26200 1.000 16.45061 ? 42  PHE A CB     1 
ATOM   301  C  CG     . PHE A 1 49  ? -29.81600 -2.72200  -35.64900 1.000 19.64431 ? 42  PHE A CG     1 
ATOM   302  C  CD1    . PHE A 1 49  ? -28.70800 -2.48900  -36.45200 1.000 20.30208 ? 42  PHE A CD1    1 
ATOM   303  C  CD2    . PHE A 1 49  ? -31.07800 -2.41100  -36.15200 1.000 19.81486 ? 42  PHE A CD2    1 
ATOM   304  C  CE1    . PHE A 1 49  ? -28.85100 -1.95600  -37.74300 1.000 21.47350 ? 42  PHE A CE1    1 
ATOM   305  C  CE2    . PHE A 1 49  ? -31.21900 -1.89500  -37.44100 1.000 21.55382 ? 42  PHE A CE2    1 
ATOM   306  C  CZ     . PHE A 1 49  ? -30.10600 -1.66500  -38.22900 1.000 18.01111 ? 42  PHE A CZ     1 
ATOM   307  N  N      . ASP A 1 50  ? -29.55300 0.13500   -33.57300 1.000 14.58505 ? 43  ASP A N      1 
ATOM   308  C  CA     . ASP A 1 50  ? -30.31500 1.38200   -33.49600 1.000 14.10274 ? 43  ASP A CA     1 
ATOM   309  C  C      . ASP A 1 50  ? -31.05900 1.52900   -34.81400 1.000 18.49669 ? 43  ASP A C      1 
ATOM   310  O  O      . ASP A 1 50  ? -30.47800 1.93400   -35.82600 1.000 15.85854 ? 43  ASP A O      1 
ATOM   311  C  CB     . ASP A 1 50  ? -29.39800 2.57200   -33.20900 1.000 18.33772 ? 43  ASP A CB     1 
ATOM   312  C  CG     . ASP A 1 50  ? -30.11900 3.92400   -33.28700 1.000 19.64568 ? 43  ASP A CG     1 
ATOM   313  O  OD1    . ASP A 1 50  ? -31.35800 3.95500   -33.40500 1.000 20.52847 ? 43  ASP A OD1    1 
ATOM   314  O  OD2    . ASP A 1 50  ? -29.43400 4.97000   -33.18100 1.000 20.81081 ? 43  ASP A OD2    1 
ATOM   315  N  N      . THR A 1 51  ? -32.34700 1.15900   -34.81000 1.000 20.00362 ? 44  THR A N      1 
ATOM   316  C  CA     . THR A 1 51  ? -33.12500 1.15000   -36.04600 1.000 18.26565 ? 44  THR A CA     1 
ATOM   317  C  C      . THR A 1 51  ? -33.28300 2.54000   -36.64800 1.000 20.57801 ? 44  THR A C      1 
ATOM   318  O  O      . THR A 1 51  ? -33.69700 2.65400   -37.80900 1.000 20.57584 ? 44  THR A O      1 
ATOM   319  C  CB     . THR A 1 51  ? -34.50200 0.53100   -35.80700 1.000 19.76083 ? 44  THR A CB     1 
ATOM   320  O  OG1    . THR A 1 51  ? -35.18700 1.27600   -34.79800 1.000 19.62649 ? 44  THR A OG1    1 
ATOM   321  C  CG2    . THR A 1 51  ? -34.36800 -0.92200  -35.35300 1.000 17.37893 ? 44  THR A CG2    1 
ATOM   322  N  N      . LYS A 1 52  ? -32.96300 3.59700   -35.89600 1.000 20.24203 ? 45  LYS A N      1 
ATOM   323  C  CA     . LYS A 1 52  ? -33.05700 4.95800   -36.41200 1.000 16.51120 ? 45  LYS A CA     1 
ATOM   324  C  C      . LYS A 1 52  ? -31.83400 5.38500   -37.21300 1.000 23.35137 ? 45  LYS A C      1 
ATOM   325  O  O      . LYS A 1 52  ? -31.94200 6.29900   -38.03900 1.000 22.70921 ? 45  LYS A O      1 
ATOM   326  C  CB     . LYS A 1 52  ? -33.25700 5.95900   -35.26900 1.000 20.39477 ? 45  LYS A CB     1 
ATOM   327  C  CG     . LYS A 1 52  ? -33.57400 7.38300   -35.74300 1.000 27.27422 ? 45  LYS A CG     1 
ATOM   328  C  CD     . LYS A 1 52  ? -33.67000 8.37300   -34.56400 1.000 31.24607 ? 45  LYS A CD     1 
ATOM   329  C  CE     . LYS A 1 52  ? -34.89400 9.29500   -34.66200 1.000 39.13639 ? 45  LYS A CE     1 
ATOM   330  N  NZ     . LYS A 1 52  ? -35.22900 9.97300   -33.36300 1.000 44.66697 ? 45  LYS A NZ     1 
ATOM   331  N  N      . THR A 1 53  ? -30.67400 4.77100   -36.98300 1.000 19.68787 ? 46  THR A N      1 
ATOM   332  C  CA     . THR A 1 53  ? -29.45800 5.16200   -37.68100 1.000 18.83923 ? 46  THR A CA     1 
ATOM   333  C  C      . THR A 1 53  ? -28.85700 4.05700   -38.53000 1.000 20.51794 ? 46  THR A C      1 
ATOM   334  O  O      . THR A 1 53  ? -27.94700 4.33900   -39.32000 1.000 18.68204 ? 46  THR A O      1 
ATOM   335  C  CB     . THR A 1 53  ? -28.38300 5.62300   -36.68600 1.000 23.60017 ? 46  THR A CB     1 
ATOM   336  O  OG1    . THR A 1 53  ? -27.98900 4.50600   -35.88400 1.000 19.54131 ? 46  THR A OG1    1 
ATOM   337  C  CG2    . THR A 1 53  ? -28.91400 6.72500   -35.78500 1.000 22.78815 ? 46  THR A CG2    1 
ATOM   338  N  N      . GLY A 1 54  ? -29.29900 2.81300   -38.36100 1.000 15.43186 ? 47  GLY A N      1 
ATOM   339  C  CA     . GLY A 1 54  ? -28.68700 1.69600   -39.04600 1.000 17.72670 ? 47  GLY A CA     1 
ATOM   340  C  C      . GLY A 1 54  ? -27.36200 1.24300   -38.47900 1.000 21.12782 ? 47  GLY A C      1 
ATOM   341  O  O      . GLY A 1 54  ? -26.66000 0.46600   -39.14200 1.000 22.27147 ? 47  GLY A O      1 
ATOM   342  N  N      . HIS A 1 55  ? -27.00800 1.67600   -37.26900 1.000 20.41811 ? 48  HIS A N      1 
ATOM   343  C  CA     . HIS A 1 55  ? -25.71500 1.37600   -36.66300 1.000 24.86492 ? 48  HIS A CA     1 
ATOM   344  C  C      . HIS A 1 55  ? -25.91400 0.57700   -35.37900 1.000 19.60362 ? 48  HIS A C      1 
ATOM   345  O  O      . HIS A 1 55  ? -26.95800 0.66900   -34.73000 1.000 15.41141 ? 48  HIS A O      1 
ATOM   346  C  CB     . HIS A 1 55  ? -24.95100 2.67400   -36.34400 1.000 23.59559 ? 48  HIS A CB     1 
ATOM   347  C  CG     . HIS A 1 55  ? -24.34800 3.32000   -37.55100 1.000 33.71022 ? 48  HIS A CG     1 
ATOM   348  N  ND1    . HIS A 1 55  ? -23.74500 2.59800   -38.56000 1.000 32.49500 ? 48  HIS A ND1    1 
ATOM   349  C  CD2    . HIS A 1 55  ? -24.31400 4.61600   -37.94200 1.000 34.03362 ? 48  HIS A CD2    1 
ATOM   350  C  CE1    . HIS A 1 55  ? -23.33500 3.42600   -39.50500 1.000 38.84449 ? 48  HIS A CE1    1 
ATOM   351  N  NE2    . HIS A 1 55  ? -23.67000 4.65500   -39.15600 1.000 39.25657 ? 48  HIS A NE2    1 
ATOM   352  N  N      . ARG A 1 56  ? -24.89200 -0.19700  -35.01300 1.000 14.70967 ? 49  ARG A N      1 
ATOM   353  C  CA     . ARG A 1 56  ? -24.92100 -0.94100  -33.76500 1.000 15.36907 ? 49  ARG A CA     1 
ATOM   354  C  C      . ARG A 1 56  ? -24.45000 -0.03200  -32.63500 1.000 14.46194 ? 49  ARG A C      1 
ATOM   355  O  O      . ARG A 1 56  ? -23.55600 0.79800   -32.82700 1.000 16.16899 ? 49  ARG A O      1 
ATOM   356  C  CB     . ARG A 1 56  ? -24.02400 -2.18100  -33.85900 1.000 21.94627 ? 49  ARG A CB     1 
ATOM   357  C  CG     . ARG A 1 56  ? -24.67900 -3.40700  -34.52900 1.000 28.14248 ? 49  ARG A CG     1 
ATOM   358  C  CD     . ARG A 1 56  ? -24.24000 -4.73600  -33.84400 1.000 34.74614 ? 49  ARG A CD     1 
ATOM   359  N  NE     . ARG A 1 56  ? -25.15200 -5.13600  -32.76600 1.000 35.61764 ? 49  ARG A NE     1 
ATOM   360  C  CZ     . ARG A 1 56  ? -26.09900 -6.06600  -32.87800 1.000 42.17738 ? 49  ARG A CZ     1 
ATOM   361  N  NH1    . ARG A 1 56  ? -26.27000 -6.74900  -34.00300 1.000 48.42193 ? 49  ARG A NH1    1 
ATOM   362  N  NH2    . ARG A 1 56  ? -26.89100 -6.32300  -31.83300 1.000 28.15063 ? 49  ARG A NH2    1 
ATOM   363  N  N      . VAL A 1 57  ? -25.04300 -0.19400  -31.45400 1.000 12.89860 ? 50  VAL A N      1 
ATOM   364  C  CA     . VAL A 1 57  ? -24.72800 0.66100   -30.31500 1.000 10.54289 ? 50  VAL A CA     1 
ATOM   365  C  C      . VAL A 1 57  ? -24.40400 -0.19900  -29.10000 1.000 13.60339 ? 50  VAL A C      1 
ATOM   366  O  O      . VAL A 1 57  ? -24.79400 -1.36600  -29.00600 1.000 13.03766 ? 50  VAL A O      1 
ATOM   367  C  CB     . VAL A 1 57  ? -25.86800 1.65600   -29.97000 1.000 13.26521 ? 50  VAL A CB     1 
ATOM   368  C  CG1    . VAL A 1 57  ? -26.06400 2.67600   -31.11400 1.000 13.24355 ? 50  VAL A CG1    1 
ATOM   369  C  CG2    . VAL A 1 57  ? -27.17500 0.89600   -29.67400 1.000 14.26025 ? 50  VAL A CG2    1 
ATOM   370  N  N      . ALA A 1 58  ? -23.65700 0.39700   -28.17300 1.000 12.69142 ? 51  ALA A N      1 
ATOM   371  C  CA     . ALA A 1 58  ? -23.43600 -0.14900  -26.84300 1.000 12.39374 ? 51  ALA A CA     1 
ATOM   372  C  C      . ALA A 1 58  ? -24.29900 0.63400   -25.87300 1.000 14.46520 ? 51  ALA A C      1 
ATOM   373  O  O      . ALA A 1 58  ? -24.27900 1.87100   -25.88100 1.000 12.05456 ? 51  ALA A O      1 
ATOM   374  C  CB     . ALA A 1 58  ? -21.96400 -0.06100  -26.42500 1.000 13.21657 ? 51  ALA A CB     1 
ATOM   375  N  N      . VAL A 1 59  ? -25.04700 -0.08300  -25.03700 1.000 11.80980 ? 52  VAL A N      1 
ATOM   376  C  CA     . VAL A 1 59  ? -25.97100 0.52800   -24.09200 1.000 11.20625 ? 52  VAL A CA     1 
ATOM   377  C  C      . VAL A 1 59  ? -25.56100 0.09900   -22.69600 1.000 14.31866 ? 52  VAL A C      1 
ATOM   378  O  O      . VAL A 1 59  ? -25.48300 -1.10300  -22.41300 1.000 15.30511 ? 52  VAL A O      1 
ATOM   379  C  CB     . VAL A 1 59  ? -27.42700 0.13000   -24.38100 1.000 13.69390 ? 52  VAL A CB     1 
ATOM   380  C  CG1    . VAL A 1 59  ? -28.38000 0.90800   -23.45800 1.000 13.13295 ? 52  VAL A CG1    1 
ATOM   381  C  CG2    . VAL A 1 59  ? -27.74500 0.33700   -25.87700 1.000 10.56320 ? 52  VAL A CG2    1 
ATOM   382  N  N      . LYS A 1 60  ? -25.30900 1.06900   -21.82100 1.000 14.04453 ? 53  LYS A N      1 
ATOM   383  C  CA     . LYS A 1 60  ? -24.89400 0.78100   -20.45400 1.000 15.91001 ? 53  LYS A CA     1 
ATOM   384  C  C      . LYS A 1 60  ? -25.98400 1.21500   -19.48300 1.000 15.53886 ? 53  LYS A C      1 
ATOM   385  O  O      . LYS A 1 60  ? -26.46000 2.36100   -19.52500 1.000 18.57383 ? 53  LYS A O      1 
ATOM   386  C  CB     . LYS A 1 60  ? -23.56200 1.46700   -20.11700 1.000 14.39929 ? 53  LYS A CB     1 
ATOM   387  C  CG     . LYS A 1 60  ? -23.26400 1.52500   -18.62500 1.000 18.17470 ? 53  LYS A CG     1 
ATOM   388  C  CD     . LYS A 1 60  ? -21.78900 1.28100   -18.33000 1.000 28.54122 ? 53  LYS A CD     1 
ATOM   389  C  CE     . LYS A 1 60  ? -21.00600 2.57200   -18.30300 1.000 21.92761 ? 53  LYS A CE     1 
ATOM   390  N  NZ     . LYS A 1 60  ? -19.94200 2.55800   -17.25000 1.000 21.17242 ? 53  LYS A NZ     1 
ATOM   391  N  N      . LYS A 1 61  ? -26.39500 0.30100   -18.61700 1.000 17.84776 ? 54  LYS A N      1 
ATOM   392  C  CA     . LYS A 1 61  ? -27.39300 0.62500   -17.60300 1.000 17.23195 ? 54  LYS A CA     1 
ATOM   393  C  C      . LYS A 1 61  ? -26.67200 0.87200   -16.27900 1.000 19.39736 ? 54  LYS A C      1 
ATOM   394  O  O      . LYS A 1 61  ? -25.88800 0.03400   -15.82600 1.000 17.35855 ? 54  LYS A O      1 
ATOM   395  C  CB     . LYS A 1 61  ? -28.43100 -0.49500  -17.48600 1.000 17.70047 ? 54  LYS A CB     1 
ATOM   396  C  CG     . LYS A 1 61  ? -29.55800 -0.23700  -16.46700 1.000 21.38688 ? 54  LYS A CG     1 
ATOM   397  C  CD     . LYS A 1 61  ? -30.58600 -1.38100  -16.48100 1.000 21.55429 ? 54  LYS A CD     1 
ATOM   398  C  CE     . LYS A 1 61  ? -31.61200 -1.26400  -15.34400 1.000 23.16985 ? 54  LYS A CE     1 
ATOM   399  N  NZ     . LYS A 1 61  ? -32.08800 -2.59300  -14.82500 1.000 25.63666 ? 54  LYS A NZ     1 
ATOM   400  N  N      . LEU A 1 62  ? -26.91300 2.02900   -15.67600 1.000 20.78046 ? 55  LEU A N      1 
ATOM   401  C  CA     . LEU A 1 62  ? -26.33900 2.30000   -14.36700 1.000 24.96139 ? 55  LEU A CA     1 
ATOM   402  C  C      . LEU A 1 62  ? -27.08700 1.49700   -13.30700 1.000 29.21322 ? 55  LEU A C      1 
ATOM   403  O  O      . LEU A 1 62  ? -28.31800 1.53800   -13.24100 1.000 30.59110 ? 55  LEU A O      1 
ATOM   404  C  CB     . LEU A 1 62  ? -26.40200 3.79700   -14.06600 1.000 21.12884 ? 55  LEU A CB     1 
ATOM   405  C  CG     . LEU A 1 62  ? -25.58400 4.69300   -14.99500 1.000 24.79704 ? 55  LEU A CG     1 
ATOM   406  C  CD1    . LEU A 1 62  ? -25.12300 5.94000   -14.26800 1.000 24.24900 ? 55  LEU A CD1    1 
ATOM   407  C  CD2    . LEU A 1 62  ? -24.36200 3.91500   -15.50900 1.000 22.95755 ? 55  LEU A CD2    1 
ATOM   408  N  N      . SER A 1 63  ? -26.34000 0.76300   -12.47900 1.000 38.39016 ? 56  SER A N      1 
ATOM   409  C  CA     . SER A 1 63  ? -26.93200 -0.04100  -11.41400 1.000 43.57615 ? 56  SER A CA     1 
ATOM   410  C  C      . SER A 1 63  ? -27.01300 0.74400   -10.10900 1.000 38.75417 ? 56  SER A C      1 
ATOM   411  O  O      . SER A 1 63  ? -26.03500 1.37200   -9.69400  1.000 37.89107 ? 56  SER A O      1 
ATOM   412  C  CB     . SER A 1 63  ? -26.12300 -1.32300  -11.19600 1.000 47.35533 ? 56  SER A CB     1 
ATOM   413  O  OG     . SER A 1 63  ? -24.73600 -1.05400  -11.05900 1.000 55.84435 ? 56  SER A OG     1 
ATOM   414  N  N      . ARG A 1 64  ? -28.18300 0.69500   -9.45900  1.000 39.20430 ? 57  ARG A N      1 
ATOM   415  C  CA     . ARG A 1 64  ? -28.40100 1.31000   -8.15300  1.000 45.00512 ? 57  ARG A CA     1 
ATOM   416  C  C      . ARG A 1 64  ? -27.97000 2.78100   -8.13600  1.000 37.29291 ? 57  ARG A C      1 
ATOM   417  O  O      . ARG A 1 64  ? -27.30000 3.22000   -7.20200  1.000 37.77388 ? 57  ARG A O      1 
ATOM   418  C  CB     . ARG A 1 64  ? -27.67300 0.54900   -7.05100  1.000 43.72752 ? 57  ARG A CB     1 
ATOM   419  C  CG     . ARG A 1 64  ? -28.06400 -0.90600  -6.81200  1.000 54.37449 ? 57  ARG A CG     1 
ATOM   420  C  CD     . ARG A 1 64  ? -29.50300 -1.18800  -7.19400  1.000 59.03105 ? 57  ARG A CD     1 
ATOM   421  N  NE     . ARG A 1 64  ? -30.39500 -0.94000  -6.06500  1.000 59.21432 ? 57  ARG A NE     1 
ATOM   422  C  CZ     . ARG A 1 64  ? -30.71900 -1.84200  -5.14800  1.000 57.47112 ? 57  ARG A CZ     1 
ATOM   423  N  NH1    . ARG A 1 64  ? -30.19900 -3.05900  -5.16200  1.000 64.18564 ? 57  ARG A NH1    1 
ATOM   424  N  NH2    . ARG A 1 64  ? -31.58200 -1.51500  -4.19100  1.000 47.87078 ? 57  ARG A NH2    1 
ATOM   425  N  N      . PRO A 1 65  ? -28.34800 3.56200   -9.15500  1.000 32.60090 ? 58  PRO A N      1 
ATOM   426  C  CA     . PRO A 1 65  ? -27.71000 4.87700   -9.32000  1.000 26.38648 ? 58  PRO A CA     1 
ATOM   427  C  C      . PRO A 1 65  ? -27.85600 5.78700   -8.11600  1.000 26.32681 ? 58  PRO A C      1 
ATOM   428  O  O      . PRO A 1 65  ? -26.94100 6.56900   -7.84100  1.000 23.10004 ? 58  PRO A O      1 
ATOM   429  C  CB     . PRO A 1 65  ? -28.41400 5.45500   -10.56200 1.000 29.29023 ? 58  PRO A CB     1 
ATOM   430  C  CG     . PRO A 1 65  ? -29.71300 4.71400   -10.64000 1.000 28.69462 ? 58  PRO A CG     1 
ATOM   431  C  CD     . PRO A 1 65  ? -29.39600 3.33100   -10.16200 1.000 34.81891 ? 58  PRO A CD     1 
ATOM   432  N  N      . PHE A 1 66  ? -28.96300 5.70700   -7.37900  1.000 24.47702 ? 59  PHE A N      1 
ATOM   433  C  CA     . PHE A 1 66  ? -29.24900 6.63100   -6.28500  1.000 24.11638 ? 59  PHE A CA     1 
ATOM   434  C  C      . PHE A 1 66  ? -29.43900 5.89900   -4.95700  1.000 27.45200 ? 59  PHE A C      1 
ATOM   435  O  O      . PHE A 1 66  ? -30.15100 6.37000   -4.06800  1.000 26.75453 ? 59  PHE A O      1 
ATOM   436  C  CB     . PHE A 1 66  ? -30.46700 7.48600   -6.63600  1.000 23.40894 ? 59  PHE A CB     1 
ATOM   437  C  CG     . PHE A 1 66  ? -30.35800 8.14200   -7.98600  1.000 25.81987 ? 59  PHE A CG     1 
ATOM   438  C  CD1    . PHE A 1 66  ? -29.26500 8.94100   -8.29100  1.000 24.03821 ? 59  PHE A CD1    1 
ATOM   439  C  CD2    . PHE A 1 66  ? -31.30400 7.91000   -8.97200  1.000 27.08290 ? 59  PHE A CD2    1 
ATOM   440  C  CE1    . PHE A 1 66  ? -29.13900 9.53100   -9.54600  1.000 22.58358 ? 59  PHE A CE1    1 
ATOM   441  C  CE2    . PHE A 1 66  ? -31.18200 8.49300   -10.23300 1.000 26.09833 ? 59  PHE A CE2    1 
ATOM   442  C  CZ     . PHE A 1 66  ? -30.09900 9.30800   -10.51700 1.000 19.76941 ? 59  PHE A CZ     1 
ATOM   443  N  N      . GLN A 1 67  ? -28.77800 4.75500   -4.79900  1.000 26.23424 ? 60  GLN A N      1 
ATOM   444  C  CA     . GLN A 1 67  ? -28.97000 3.94000   -3.60300  1.000 34.13572 ? 60  GLN A CA     1 
ATOM   445  C  C      . GLN A 1 67  ? -28.26200 4.52500   -2.38500  1.000 30.05496 ? 60  GLN A C      1 
ATOM   446  O  O      . GLN A 1 67  ? -28.66600 4.24800   -1.25000  1.000 31.56658 ? 60  GLN A O      1 
ATOM   447  C  CB     . GLN A 1 67  ? -28.49800 2.50800   -3.88900  1.000 33.43722 ? 60  GLN A CB     1 
ATOM   448  C  CG     . GLN A 1 67  ? -28.42900 1.56300   -2.68400  1.000 40.91102 ? 60  GLN A CG     1 
ATOM   449  C  CD     . GLN A 1 67  ? -27.35600 0.50000   -2.85000  1.000 41.09879 ? 60  GLN A CD     1 
ATOM   450  O  OE1    . GLN A 1 67  ? -26.27400 0.77400   -3.36600  1.000 42.33501 ? 60  GLN A OE1    1 
ATOM   451  N  NE2    . GLN A 1 67  ? -27.66000 -0.72500  -2.43400  1.000 44.04243 ? 60  GLN A NE2    1 
ATOM   452  N  N      . SER A 1 68  ? -27.24800 5.35700   -2.60200  1.000 24.04634 ? 61  SER A N      1 
ATOM   453  C  CA     . SER A 1 68  ? -26.43900 5.93700   -1.54000  1.000 24.33887 ? 61  SER A CA     1 
ATOM   454  C  C      . SER A 1 68  ? -25.89400 7.26800   -2.03600  1.000 29.24905 ? 61  SER A C      1 
ATOM   455  O  O      . SER A 1 68  ? -25.94100 7.56500   -3.23100  1.000 23.24917 ? 61  SER A O      1 
ATOM   456  C  CB     . SER A 1 68  ? -25.31700 4.97600   -1.13500  1.000 27.09360 ? 61  SER A CB     1 
ATOM   457  O  OG     . SER A 1 68  ? -24.15000 5.21000   -1.90200  1.000 26.65614 ? 61  SER A OG     1 
ATOM   458  N  N      . ILE A 1 69  ? -25.42000 8.09400   -1.10300  1.000 23.73769 ? 62  ILE A N      1 
ATOM   459  C  CA     . ILE A 1 69  ? -24.93800 9.41100   -1.50100  1.000 27.61399 ? 62  ILE A CA     1 
ATOM   460  C  C      . ILE A 1 69  ? -23.75500 9.24200   -2.44200  1.000 23.23153 ? 62  ILE A C      1 
ATOM   461  O  O      . ILE A 1 69  ? -23.61200 9.96500   -3.44200  1.000 18.97172 ? 62  ILE A O      1 
ATOM   462  C  CB     . ILE A 1 69  ? -24.54900 10.24000  -0.26600  1.000 29.41182 ? 62  ILE A CB     1 
ATOM   463  C  CG1    . ILE A 1 69  ? -25.74300 11.02800  0.25700   1.000 37.47543 ? 62  ILE A CG1    1 
ATOM   464  C  CG2    . ILE A 1 69  ? -23.48000 11.25400  -0.64900  1.000 31.33458 ? 62  ILE A CG2    1 
ATOM   465  C  CD1    . ILE A 1 69  ? -25.43400 11.79100  1.54100   1.000 39.47774 ? 62  ILE A CD1    1 
ATOM   466  N  N      . ILE A 1 70  ? -22.90600 8.25700   -2.14200  1.000 22.95053 ? 63  ILE A N      1 
ATOM   467  C  CA     . ILE A 1 70  ? -21.71900 7.99000   -2.95000  1.000 25.10443 ? 63  ILE A CA     1 
ATOM   468  C  C      . ILE A 1 70  ? -22.12400 7.55800   -4.35800  1.000 22.31269 ? 63  ILE A C      1 
ATOM   469  O  O      . ILE A 1 70  ? -21.62300 8.09000   -5.35600  1.000 19.72599 ? 63  ILE A O      1 
ATOM   470  C  CB     . ILE A 1 70  ? -20.84000 6.93000   -2.25600  1.000 27.59019 ? 63  ILE A CB     1 
ATOM   471  C  CG1    . ILE A 1 70  ? -20.21600 7.49100   -0.97900  1.000 33.84480 ? 63  ILE A CG1    1 
ATOM   472  C  CG2    . ILE A 1 70  ? -19.74700 6.43400   -3.18300  1.000 32.02945 ? 63  ILE A CG2    1 
ATOM   473  C  CD1    . ILE A 1 70  ? -19.73200 8.90000   -1.10400  1.000 33.82197 ? 63  ILE A CD1    1 
ATOM   474  N  N      . HIS A 1 71  ? -23.04600 6.59600   -4.45700  1.000 20.18750 ? 64  HIS A N      1 
ATOM   475  C  CA     . HIS A 1 71  ? -23.54200 6.16800   -5.77000  1.000 20.92962 ? 64  HIS A CA     1 
ATOM   476  C  C      . HIS A 1 71  ? -24.21700 7.31300   -6.52000  1.000 17.29113 ? 64  HIS A C      1 
ATOM   477  O  O      . HIS A 1 71  ? -24.07600 7.43600   -7.74200  1.000 18.59384 ? 64  HIS A O      1 
ATOM   478  C  CB     . HIS A 1 71  ? -24.54200 5.01900   -5.62400  1.000 24.26101 ? 64  HIS A CB     1 
ATOM   479  C  CG     . HIS A 1 71  ? -23.92100 3.66500   -5.49200  1.000 30.29105 ? 64  HIS A CG     1 
ATOM   480  N  ND1    . HIS A 1 71  ? -24.66700 2.50700   -5.52900  1.000 41.91235 ? 64  HIS A ND1    1 
ATOM   481  C  CD2    . HIS A 1 71  ? -22.64200 3.28000   -5.27000  1.000 38.00199 ? 64  HIS A CD2    1 
ATOM   482  C  CE1    . HIS A 1 71  ? -23.87200 1.46600   -5.36000  1.000 37.95059 ? 64  HIS A CE1    1 
ATOM   483  N  NE2    . HIS A 1 71  ? -22.63800 1.90800   -5.19600  1.000 33.06877 ? 64  HIS A NE2    1 
ATOM   484  N  N      . ALA A 1 72  ? -25.00500 8.13300   -5.82400  1.000 16.52919 ? 65  ALA A N      1 
ATOM   485  C  CA     . ALA A 1 72  ? -25.71300 9.20600   -6.51800  1.000 19.62816 ? 65  ALA A CA     1 
ATOM   486  C  C      . ALA A 1 72  ? -24.72900 10.21500  -7.10600  1.000 16.75101 ? 65  ALA A C      1 
ATOM   487  O  O      . ALA A 1 72  ? -24.87400 10.65700  -8.25300  1.000 17.08878 ? 65  ALA A O      1 
ATOM   488  C  CB     . ALA A 1 72  ? -26.68900 9.90200   -5.56500  1.000 19.29683 ? 65  ALA A CB     1 
ATOM   489  N  N      . LYS A 1 73  ? -23.72800 10.60100  -6.31900  1.000 15.09284 ? 66  LYS A N      1 
ATOM   490  C  CA     . LYS A 1 73  ? -22.69500 11.51000  -6.80000  1.000 15.17870 ? 66  LYS A CA     1 
ATOM   491  C  C      . LYS A 1 73  ? -21.90600 10.88100  -7.93700  1.000 17.13184 ? 66  LYS A C      1 
ATOM   492  O  O      . LYS A 1 73  ? -21.51500 11.56500  -8.89000  1.000 15.38147 ? 66  LYS A O      1 
ATOM   493  C  CB     . LYS A 1 73  ? -21.75500 11.88300  -5.65200  1.000 15.97202 ? 66  LYS A CB     1 
ATOM   494  C  CG     . LYS A 1 73  ? -20.64800 12.87600  -6.04600  1.000 20.59357 ? 66  LYS A CG     1 
ATOM   495  C  CD     . LYS A 1 73  ? -20.12400 13.66000  -4.84000  1.000 21.29734 ? 66  LYS A CD     1 
ATOM   496  C  CE     . LYS A 1 73  ? -19.15700 14.76900  -5.26200  1.000 21.28524 ? 66  LYS A CE     1 
ATOM   497  N  NZ     . LYS A 1 73  ? -18.25900 15.16300  -4.12900  1.000 21.32359 ? 66  LYS A NZ     1 
ATOM   498  N  N      . ARG A 1 74  ? -21.65200 9.57400   -7.84600  1.000 16.98014 ? 67  ARG A N      1 
ATOM   499  C  CA     . ARG A 1 74  ? -20.92200 8.87800   -8.90300  1.000 21.95326 ? 67  ARG A CA     1 
ATOM   500  C  C      . ARG A 1 74  ? -21.72900 8.80100   -10.19500 1.000 17.59534 ? 67  ARG A C      1 
ATOM   501  O  O      . ARG A 1 74  ? -21.15300 8.84100   -11.29100 1.000 14.06170 ? 67  ARG A O      1 
ATOM   502  C  CB     . ARG A 1 74  ? -20.55400 7.48000   -8.42300  1.000 21.27605 ? 67  ARG A CB     1 
ATOM   503  C  CG     . ARG A 1 74  ? -19.90200 6.62400   -9.46900  1.000 22.45260 ? 67  ARG A CG     1 
ATOM   504  C  CD     . ARG A 1 74  ? -19.70700 5.21900   -8.93700  1.000 29.08880 ? 67  ARG A CD     1 
ATOM   505  N  NE     . ARG A 1 74  ? -18.90300 5.24100   -7.72200  1.000 36.18319 ? 67  ARG A NE     1 
ATOM   506  C  CZ     . ARG A 1 74  ? -18.89200 4.28400   -6.80100  1.000 38.87733 ? 67  ARG A CZ     1 
ATOM   507  N  NH1    . ARG A 1 74  ? -19.64400 3.20100   -6.92000  1.000 36.26231 ? 67  ARG A NH1    1 
ATOM   508  N  NH2    . ARG A 1 74  ? -18.10000 4.41700   -5.73800  1.000 36.03837 ? 67  ARG A NH2    1 
ATOM   509  N  N      . THR A 1 75  ? -23.05200 8.66500   -10.08000 1.000 14.13136 ? 68  THR A N      1 
ATOM   510  C  CA     . THR A 1 75  ? -23.92200 8.71900   -11.25100 1.000 14.57346 ? 68  THR A CA     1 
ATOM   511  C  C      . THR A 1 75  ? -23.82300 10.08100  -11.93800 1.000 15.60622 ? 68  THR A C      1 
ATOM   512  O  O      . THR A 1 75  ? -23.56900 10.17300  -13.14500 1.000 14.32233 ? 68  THR A O      1 
ATOM   513  C  CB     . THR A 1 75  ? -25.35900 8.41000   -10.81900 1.000 19.04218 ? 68  THR A CB     1 
ATOM   514  O  OG1    . THR A 1 75  ? -25.42600 7.05700   -10.33300 1.000 18.32846 ? 68  THR A OG1    1 
ATOM   515  C  CG2    . THR A 1 75  ? -26.35800 8.63300   -11.96100 1.000 17.46124 ? 68  THR A CG2    1 
ATOM   516  N  N      . TYR A 1 76  ? -23.99900 11.15500  -11.17100 1.000 12.48264 ? 69  TYR A N      1 
ATOM   517  C  CA     . TYR A 1 76  ? -23.83700 12.50300  -11.70600 1.000 14.25582 ? 69  TYR A CA     1 
ATOM   518  C  C      . TYR A 1 76  ? -22.46300 12.69000  -12.34100 1.000 13.01092 ? 69  TYR A C      1 
ATOM   519  O  O      . TYR A 1 76  ? -22.34100 13.27700  -13.42200 1.000 11.89361 ? 69  TYR A O      1 
ATOM   520  C  CB     . TYR A 1 76  ? -24.03600 13.52900  -10.58200 1.000 13.23893 ? 69  TYR A CB     1 
ATOM   521  C  CG     . TYR A 1 76  ? -23.98700 14.97600  -11.02900 1.000 12.87063 ? 69  TYR A CG     1 
ATOM   522  C  CD1    . TYR A 1 76  ? -25.01700 15.52700  -11.76400 1.000 14.59809 ? 69  TYR A CD1    1 
ATOM   523  C  CD2    . TYR A 1 76  ? -22.90800 15.79600  -10.69100 1.000 13.94621 ? 69  TYR A CD2    1 
ATOM   524  C  CE1    . TYR A 1 76  ? -24.99100 16.84500  -12.16600 1.000 15.05538 ? 69  TYR A CE1    1 
ATOM   525  C  CE2    . TYR A 1 76  ? -22.87100 17.11700  -11.08500 1.000 13.58192 ? 69  TYR A CE2    1 
ATOM   526  C  CZ     . TYR A 1 76  ? -23.92600 17.63700  -11.81600 1.000 15.05787 ? 69  TYR A CZ     1 
ATOM   527  O  OH     . TYR A 1 76  ? -23.90100 18.94700  -12.23200 1.000 19.70747 ? 69  TYR A OH     1 
ATOM   528  N  N      . ARG A 1 77  ? -21.41600 12.19600  -11.67400 1.000 13.68657 ? 70  ARG A N      1 
ATOM   529  C  CA     . ARG A 1 77  ? -20.05200 12.38700  -12.16500 1.000 13.51886 ? 70  ARG A CA     1 
ATOM   530  C  C      . ARG A 1 77  ? -19.87900 11.76000  -13.54200 1.000 15.59820 ? 70  ARG A C      1 
ATOM   531  O  O      . ARG A 1 77  ? -19.30500 12.37700  -14.45000 1.000 11.48550 ? 70  ARG A O      1 
ATOM   532  C  CB     . ARG A 1 77  ? -19.05300 11.79900  -11.15200 1.000 13.85690 ? 70  ARG A CB     1 
ATOM   533  C  CG     . ARG A 1 77  ? -17.65700 11.59900  -11.69000 1.000 14.07786 ? 70  ARG A CG     1 
ATOM   534  C  CD     . ARG A 1 77  ? -16.67400 10.93400  -10.70400 1.000 17.61538 ? 70  ARG A CD     1 
ATOM   535  N  NE     . ARG A 1 77  ? -16.64000 11.56600  -9.38000  1.000 16.72853 ? 70  ARG A NE     1 
ATOM   536  C  CZ     . ARG A 1 77  ? -17.10400 11.02200  -8.25900  1.000 22.66363 ? 70  ARG A CZ     1 
ATOM   537  N  NH1    . ARG A 1 77  ? -17.50500 9.75600   -8.21200  1.000 17.25853 ? 70  ARG A NH1    1 
ATOM   538  N  NH2    . ARG A 1 77  ? -17.13500 11.75400  -7.14700  1.000 23.25821 ? 70  ARG A NH2    1 
ATOM   539  N  N      . GLU A 1 78  ? -20.38700 10.53700  -13.72800 1.000 13.34233 ? 71  GLU A N      1 
ATOM   540  C  CA     . GLU A 1 78  ? -20.16900 9.86600   -15.00700 1.000 13.56392 ? 71  GLU A CA     1 
ATOM   541  C  C      . GLU A 1 78  ? -20.97400 10.53300  -16.11700 1.000 13.87343 ? 71  GLU A C      1 
ATOM   542  O  O      . GLU A 1 78  ? -20.48800 10.67900  -17.24900 1.000 12.99103 ? 71  GLU A O      1 
ATOM   543  C  CB     . GLU A 1 78  ? -20.51000 8.37700   -14.90600 1.000 11.81096 ? 71  GLU A CB     1 
ATOM   544  C  CG     . GLU A 1 78  ? -20.39600 7.64400   -16.27800 1.000 17.31541 ? 71  GLU A CG     1 
ATOM   545  C  CD     . GLU A 1 78  ? -20.50500 6.13200   -16.17500 1.000 14.16362 ? 71  GLU A CD     1 
ATOM   546  O  OE1    . GLU A 1 78  ? -21.14000 5.64600   -15.22100 1.000 15.77207 ? 71  GLU A OE1    1 
ATOM   547  O  OE2    . GLU A 1 78  ? -19.97000 5.42300   -17.05000 1.000 20.56054 ? 71  GLU A OE2    1 
ATOM   548  N  N      . LEU A 1 79  ? -22.20300 10.96800  -15.82500 1.000 12.91474 ? 72  LEU A N      1 
ATOM   549  C  CA     . LEU A 1 79  ? -22.98200 11.58700  -16.89600 1.000 11.70095 ? 72  LEU A CA     1 
ATOM   550  C  C      . LEU A 1 79  ? -22.37600 12.93200  -17.28700 1.000 12.32278 ? 72  LEU A C      1 
ATOM   551  O  O      . LEU A 1 79  ? -22.27100 13.25100  -18.47700 1.000 11.25906 ? 72  LEU A O      1 
ATOM   552  C  CB     . LEU A 1 79  ? -24.45200 11.72700  -16.47300 1.000 12.49237 ? 72  LEU A CB     1 
ATOM   553  C  CG     . LEU A 1 79  ? -25.41500 12.51800  -17.37200 1.000 13.95096 ? 72  LEU A CG     1 
ATOM   554  C  CD1    . LEU A 1 79  ? -25.43700 11.91100  -18.78500 1.000 16.56819 ? 72  LEU A CD1    1 
ATOM   555  C  CD2    . LEU A 1 79  ? -26.84600 12.55500  -16.78300 1.000 12.86075 ? 72  LEU A CD2    1 
ATOM   556  N  N      . ARG A 1 80  ? -21.95600 13.73300  -16.30200 1.000 10.86665 ? 73  ARG A N      1 
ATOM   557  C  CA     . ARG A 1 80  ? -21.30300 15.00800  -16.62500 1.000 10.80498 ? 73  ARG A CA     1 
ATOM   558  C  C      . ARG A 1 80  ? -20.05400 14.77900  -17.46800 1.000 13.23900 ? 73  ARG A C      1 
ATOM   559  O  O      . ARG A 1 80  ? -19.82700 15.47300  -18.46900 1.000 11.04090 ? 73  ARG A O      1 
ATOM   560  C  CB     . ARG A 1 80  ? -20.94000 15.77400  -15.34600 1.000 13.57543 ? 73  ARG A CB     1 
ATOM   561  C  CG     . ARG A 1 80  ? -22.15200 16.33400  -14.59100 1.000 13.58181 ? 73  ARG A CG     1 
ATOM   562  C  CD     . ARG A 1 80  ? -22.69600 17.62000  -15.24500 1.000 14.76297 ? 73  ARG A CD     1 
ATOM   563  N  NE     . ARG A 1 80  ? -21.60800 18.48900  -15.69000 1.000 15.39570 ? 73  ARG A NE     1 
ATOM   564  C  CZ     . ARG A 1 80  ? -21.00100 19.37500  -14.91700 1.000 19.01368 ? 73  ARG A CZ     1 
ATOM   565  N  NH1    . ARG A 1 80  ? -21.34900 19.54100  -13.65000 1.000 19.70665 ? 73  ARG A NH1    1 
ATOM   566  N  NH2    . ARG A 1 80  ? -20.01500 20.11000  -15.42200 1.000 21.70200 ? 73  ARG A NH2    1 
ATOM   567  N  N      . LEU A 1 81  ? -19.21900 13.81600  -17.06000 1.000 11.74179 ? 74  LEU A N      1 
ATOM   568  C  CA     . LEU A 1 81  ? -18.00600 13.50200  -17.81300 1.000 17.59620 ? 74  LEU A CA     1 
ATOM   569  C  C      . LEU A 1 81  ? -18.34700 13.12600  -19.24700 1.000 14.33923 ? 74  LEU A C      1 
ATOM   570  O  O      . LEU A 1 81  ? -17.81700 13.70100  -20.20500 1.000 13.81595 ? 74  LEU A O      1 
ATOM   571  C  CB     . LEU A 1 81  ? -17.25600 12.35100  -17.14200 1.000 14.49206 ? 74  LEU A CB     1 
ATOM   572  C  CG     . LEU A 1 81  ? -16.22000 12.64200  -16.06200 1.000 23.99699 ? 74  LEU A CG     1 
ATOM   573  C  CD1    . LEU A 1 81  ? -15.75500 11.31900  -15.42000 1.000 23.02987 ? 74  LEU A CD1    1 
ATOM   574  C  CD2    . LEU A 1 81  ? -15.05100 13.44700  -16.62100 1.000 22.50746 ? 74  LEU A CD2    1 
ATOM   575  N  N      . LEU A 1 82  ? -19.24600 12.15800  -19.41000 1.000 11.86719 ? 75  LEU A N      1 
ATOM   576  C  CA     . LEU A 1 82  ? -19.53800 11.63100  -20.73400 1.000 12.68963 ? 75  LEU A CA     1 
ATOM   577  C  C      . LEU A 1 82  ? -20.21400 12.68600  -21.60900 1.000 12.56409 ? 75  LEU A C      1 
ATOM   578  O  O      . LEU A 1 82  ? -19.94900 12.76300  -22.81400 1.000 12.69971 ? 75  LEU A O      1 
ATOM   579  C  CB     . LEU A 1 82  ? -20.41100 10.38100  -20.59000 1.000 13.89292 ? 75  LEU A CB     1 
ATOM   580  C  CG     . LEU A 1 82  ? -19.64900 9.18900   -19.96800 1.000 18.31548 ? 75  LEU A CG     1 
ATOM   581  C  CD1    . LEU A 1 82  ? -20.24300 7.86700   -20.36100 1.000 21.42621 ? 75  LEU A CD1    1 
ATOM   582  C  CD2    . LEU A 1 82  ? -18.18300 9.21000   -20.38300 1.000 17.11442 ? 75  LEU A CD2    1 
ATOM   583  N  N      . LYS A 1 83  ? -21.07900 13.51600  -21.02900 1.000 10.50445 ? 76  LYS A N      1 
ATOM   584  C  CA     . LYS A 1 83  ? -21.63100 14.61900  -21.80500 1.000 11.74601 ? 76  LYS A CA     1 
ATOM   585  C  C      . LYS A 1 83  ? -20.56000 15.59000  -22.28500 1.000 12.08706 ? 76  LYS A C      1 
ATOM   586  O  O      . LYS A 1 83  ? -20.77400 16.27200  -23.29400 1.000 14.56059 ? 76  LYS A O      1 
ATOM   587  C  CB     . LYS A 1 83  ? -22.71600 15.35900  -20.99800 1.000 12.45965 ? 76  LYS A CB     1 
ATOM   588  C  CG     . LYS A 1 83  ? -24.00700 14.56200  -20.84700 1.000 12.05727 ? 76  LYS A CG     1 
ATOM   589  C  CD     . LYS A 1 83  ? -25.09700 15.37200  -20.09900 1.000 13.62188 ? 76  LYS A CD     1 
ATOM   590  C  CE     . LYS A 1 83  ? -25.80300 16.40700  -20.96400 1.000 15.61297 ? 76  LYS A CE     1 
ATOM   591  N  NZ     . LYS A 1 83  ? -26.67000 17.30600  -20.12300 1.000 15.26041 ? 76  LYS A NZ     1 
ATOM   592  N  N      . HIS A 1 84  ? -19.39400 15.64600  -21.63000 1.000 12.63269 ? 77  HIS A N      1 
ATOM   593  C  CA     . HIS A 1 84  ? -18.39100 16.64400  -22.01600 1.000 11.30389 ? 77  HIS A CA     1 
ATOM   594  C  C      . HIS A 1 84  ? -17.51900 16.17600  -23.17700 1.000 14.36665 ? 77  HIS A C      1 
ATOM   595  O  O      . HIS A 1 84  ? -17.01000 17.00000  -23.95000 1.000 12.38881 ? 77  HIS A O      1 
ATOM   596  C  CB     . HIS A 1 84  ? -17.48700 16.97500  -20.82900 1.000 13.28403 ? 77  HIS A CB     1 
ATOM   597  C  CG     . HIS A 1 84  ? -16.68600 18.22500  -21.03000 1.000 13.21602 ? 77  HIS A CG     1 
ATOM   598  N  ND1    . HIS A 1 84  ? -17.26300 19.47300  -21.14000 1.000 15.86631 ? 77  HIS A ND1    1 
ATOM   599  C  CD2    . HIS A 1 84  ? -15.36000 18.40500  -21.24900 1.000 14.39647 ? 77  HIS A CD2    1 
ATOM   600  C  CE1    . HIS A 1 84  ? -16.32000 20.37500  -21.35000 1.000 14.80203 ? 77  HIS A CE1    1 
ATOM   601  N  NE2    . HIS A 1 84  ? -15.15700 19.75500  -21.41700 1.000 17.12939 ? 77  HIS A NE2    1 
ATOM   602  N  N      . MET A 1 85  ? -17.33600 14.86400  -23.30000 1.000 12.01094 ? 78  MET A N      1 
ATOM   603  C  CA     . MET A 1 85  ? -16.35800 14.25100  -24.19900 1.000 14.35078 ? 78  MET A CA     1 
ATOM   604  C  C      . MET A 1 85  ? -16.81600 14.38000  -25.65000 1.000 13.49221 ? 78  MET A C      1 
ATOM   605  O  O      . MET A 1 85  ? -17.75900 13.70000  -26.07800 1.000 12.94340 ? 78  MET A O      1 
ATOM   606  C  CB     . MET A 1 85  ? -16.19700 12.78000  -23.82200 1.000 12.71258 ? 78  MET A CB     1 
ATOM   607  C  CG     . MET A 1 85  ? -15.34500 12.46000  -22.58600 1.000 14.19382 ? 78  MET A CG     1 
ATOM   608  S  SD     . MET A 1 85  ? -13.96300 13.53500  -22.16600 1.000 14.06431 ? 78  MET A SD     1 
ATOM   609  C  CE     . MET A 1 85  ? -13.70500 13.19200  -20.44500 1.000 21.08843 ? 78  MET A CE     1 
ATOM   610  N  N      . LYS A 1 86  ? -16.08100 15.18700  -26.44000 1.000 13.90960 ? 79  LYS A N      1 
ATOM   611  C  CA     . LYS A 1 86  ? -16.34100 15.39200  -27.87600 1.000 15.32006 ? 79  LYS A CA     1 
ATOM   612  C  C      . LYS A 1 86  ? -15.00300 15.29300  -28.60500 1.000 13.80476 ? 79  LYS A C      1 
ATOM   613  O  O      . LYS A 1 86  ? -14.40200 16.31600  -28.94400 1.000 12.55251 ? 79  LYS A O      1 
ATOM   614  C  CB     . LYS A 1 86  ? -16.99100 16.74900  -28.13400 1.000 18.51360 ? 79  LYS A CB     1 
ATOM   615  C  CG     . LYS A 1 86  ? -18.29400 17.03100  -27.41700 1.000 21.96005 ? 79  LYS A CG     1 
ATOM   616  C  CD     . LYS A 1 86  ? -19.21300 15.85000  -27.44900 1.000 28.34924 ? 79  LYS A CD     1 
ATOM   617  C  CE     . LYS A 1 86  ? -20.66700 16.33200  -27.46100 1.000 35.46155 ? 79  LYS A CE     1 
ATOM   618  N  NZ     . LYS A 1 86  ? -20.89800 17.46500  -26.50700 1.000 38.18703 ? 79  LYS A NZ     1 
ATOM   619  N  N      . HIS A 1 87  ? -14.53800 14.06800  -28.83600 1.000 11.19395 ? 80  HIS A N      1 
ATOM   620  C  CA     . HIS A 1 87  ? -13.21600 13.84700  -29.42500 1.000 12.38770 ? 80  HIS A CA     1 
ATOM   621  C  C      . HIS A 1 87  ? -13.22400 12.50000  -30.13500 1.000 11.00888 ? 80  HIS A C      1 
ATOM   622  O  O      . HIS A 1 87  ? -13.77700 11.53300  -29.60700 1.000 12.97176 ? 80  HIS A O      1 
ATOM   623  C  CB     . HIS A 1 87  ? -12.12300 13.86200  -28.34200 1.000 11.49548 ? 80  HIS A CB     1 
ATOM   624  C  CG     . HIS A 1 87  ? -10.72500 13.81500  -28.88100 1.000 10.10251 ? 80  HIS A CG     1 
ATOM   625  N  ND1    . HIS A 1 87  ? -10.13900 12.64200  -29.31400 1.000 10.05456 ? 80  HIS A ND1    1 
ATOM   626  C  CD2    . HIS A 1 87  ? -9.77500  14.77500  -28.99300 1.000 9.57093  ? 80  HIS A CD2    1 
ATOM   627  C  CE1    . HIS A 1 87  ? -8.90300  12.89200  -29.71100 1.000 11.87665 ? 80  HIS A CE1    1 
ATOM   628  N  NE2    . HIS A 1 87  ? -8.65600  14.17700  -29.52400 1.000 13.81104 ? 80  HIS A NE2    1 
ATOM   629  N  N      . GLU A 1 88  ? -12.56500 12.43900  -31.30200 1.000 13.35714 ? 81  GLU A N      1 
ATOM   630  C  CA     . GLU A 1 88  ? -12.57000 11.23400  -32.13600 1.000 14.63703 ? 81  GLU A CA     1 
ATOM   631  C  C      . GLU A 1 88  ? -12.09400 9.99200   -31.40000 1.000 16.31043 ? 81  GLU A C      1 
ATOM   632  O  O      . GLU A 1 88  ? -12.54600 8.88700   -31.72000 1.000 17.86778 ? 81  GLU A O      1 
ATOM   633  C  CB     . GLU A 1 88  ? -11.69400 11.44500  -33.38100 1.000 12.96864 ? 81  GLU A CB     1 
ATOM   634  C  CG     . GLU A 1 88  ? -12.05000 12.67600  -34.20300 1.000 22.53928 ? 81  GLU A CG     1 
ATOM   635  C  CD     . GLU A 1 88  ? -11.24800 12.76400  -35.49800 1.000 28.98902 ? 81  GLU A CD     1 
ATOM   636  O  OE1    . GLU A 1 88  ? -10.05100 12.39600  -35.46200 1.000 20.86746 ? 81  GLU A OE1    1 
ATOM   637  O  OE2    . GLU A 1 88  ? -11.80000 13.20400  -36.53400 1.000 33.55266 ? 81  GLU A OE2    1 
ATOM   638  N  N      . ASN A 1 89  ? -11.14400 10.12800  -30.47300 1.000 10.71903 ? 82  ASN A N      1 
ATOM   639  C  CA     . ASN A 1 89  ? -10.53700 8.97400   -29.80700 1.000 11.78718 ? 82  ASN A CA     1 
ATOM   640  C  C      . ASN A 1 89  ? -11.07200 8.76800   -28.39200 1.000 11.13157 ? 82  ASN A C      1 
ATOM   641  O  O      . ASN A 1 89  ? -10.47000 8.02700   -27.60400 1.000 9.69014  ? 82  ASN A O      1 
ATOM   642  C  CB     . ASN A 1 89  ? -9.01300  9.12000   -29.76600 1.000 9.90557  ? 82  ASN A CB     1 
ATOM   643  C  CG     . ASN A 1 89  ? -8.39000  9.21300   -31.15800 1.000 11.67164 ? 82  ASN A CG     1 
ATOM   644  O  OD1    . ASN A 1 89  ? -7.72500  10.18800  -31.47300 1.000 13.92734 ? 82  ASN A OD1    1 
ATOM   645  N  ND2    . ASN A 1 89  ? -8.59600  8.18700   -31.98400 1.000 11.08635 ? 82  ASN A ND2    1 
ATOM   646  N  N      . VAL A 1 90  ? -12.19400 9.38900   -28.05400 1.000 10.13853 ? 83  VAL A N      1 
ATOM   647  C  CA     . VAL A 1 90  ? -12.79600 9.22100   -26.73400 1.000 11.43976 ? 83  VAL A CA     1 
ATOM   648  C  C      . VAL A 1 90  ? -14.27100 8.88800   -26.92500 1.000 10.83122 ? 83  VAL A C      1 
ATOM   649  O  O      . VAL A 1 90  ? -14.92600 9.41200   -27.83400 1.000 12.56629 ? 83  VAL A O      1 
ATOM   650  C  CB     . VAL A 1 90  ? -12.63200 10.47400  -25.84400 1.000 10.04288 ? 83  VAL A CB     1 
ATOM   651  C  CG1    . VAL A 1 90  ? -13.24500 10.23400  -24.45700 1.000 11.62303 ? 83  VAL A CG1    1 
ATOM   652  C  CG2    . VAL A 1 90  ? -11.15000 10.89800  -25.72000 1.000 7.96345  ? 83  VAL A CG2    1 
ATOM   653  N  N      . ILE A 1 91  ? -14.79000 8.02300   -26.05800 1.000 11.52141 ? 84  ILE A N      1 
ATOM   654  C  CA     . ILE A 1 91  ? -16.19900 7.65400   -26.11900 1.000 14.33173 ? 84  ILE A CA     1 
ATOM   655  C  C      . ILE A 1 91  ? -17.06800 8.90300   -26.11200 1.000 17.02047 ? 84  ILE A C      1 
ATOM   656  O  O      . ILE A 1 91  ? -16.83900 9.83200   -25.32900 1.000 14.95260 ? 84  ILE A O      1 
ATOM   657  C  CB     . ILE A 1 91  ? -16.54000 6.68900   -24.96500 1.000 15.33495 ? 84  ILE A CB     1 
ATOM   658  C  CG1    . ILE A 1 91  ? -17.93000 6.10200   -25.17400 1.000 18.23693 ? 84  ILE A CG1    1 
ATOM   659  C  CG2    . ILE A 1 91  ? -16.34700 7.33000   -23.57100 1.000 13.15265 ? 84  ILE A CG2    1 
ATOM   660  C  CD1    . ILE A 1 91  ? -17.96000 5.21400   -26.43900 1.000 28.41190 ? 84  ILE A CD1    1 
ATOM   661  N  N      . GLY A 1 92  ? -18.04100 8.95000   -27.02400 1.000 15.07133 ? 85  GLY A N      1 
ATOM   662  C  CA     . GLY A 1 92  ? -18.99700 10.04400  -27.07900 1.000 20.60873 ? 85  GLY A CA     1 
ATOM   663  C  C      . GLY A 1 92  ? -20.41700 9.53100   -26.92000 1.000 17.48297 ? 85  GLY A C      1 
ATOM   664  O  O      . GLY A 1 92  ? -20.73400 8.41000   -27.31700 1.000 16.55186 ? 85  GLY A O      1 
ATOM   665  N  N      . LEU A 1 93  ? -21.27900 10.35700  -26.32600 1.000 12.38735 ? 86  LEU A N      1 
ATOM   666  C  CA     . LEU A 1 93  ? -22.63000 9.91700   -25.99500 1.000 12.78747 ? 86  LEU A CA     1 
ATOM   667  C  C      . LEU A 1 93  ? -23.52900 10.15900  -27.20000 1.000 17.38864 ? 86  LEU A C      1 
ATOM   668  O  O      . LEU A 1 93  ? -23.65200 11.30200  -27.65900 1.000 16.66413 ? 86  LEU A O      1 
ATOM   669  C  CB     . LEU A 1 93  ? -23.18200 10.66600  -24.78000 1.000 12.57143 ? 86  LEU A CB     1 
ATOM   670  C  CG     . LEU A 1 93  ? -22.97800 10.04100  -23.39300 1.000 18.28488 ? 86  LEU A CG     1 
ATOM   671  C  CD1    . LEU A 1 93  ? -23.55500 10.97500  -22.30000 1.000 14.67763 ? 86  LEU A CD1    1 
ATOM   672  C  CD2    . LEU A 1 93  ? -23.44300 8.58800   -23.24400 1.000 15.04370 ? 86  LEU A CD2    1 
ATOM   673  N  N      . LEU A 1 94  ? -24.17000 9.10000   -27.69300 1.000 15.41968 ? 87  LEU A N      1 
ATOM   674  C  CA     . LEU A 1 94  ? -25.21100 9.26600   -28.70500 1.000 12.80426 ? 87  LEU A CA     1 
ATOM   675  C  C      . LEU A 1 94  ? -26.59800 9.48800   -28.12500 1.000 16.91112 ? 87  LEU A C      1 
ATOM   676  O  O      . LEU A 1 94  ? -27.45300 10.07200  -28.80400 1.000 15.11603 ? 87  LEU A O      1 
ATOM   677  C  CB     . LEU A 1 94  ? -25.27200 8.04800   -29.62800 1.000 16.04115 ? 87  LEU A CB     1 
ATOM   678  C  CG     . LEU A 1 94  ? -23.98200 7.64000   -30.31300 1.000 18.91162 ? 87  LEU A CG     1 
ATOM   679  C  CD1    . LEU A 1 94  ? -24.22600 6.33900   -31.09100 1.000 18.08209 ? 87  LEU A CD1    1 
ATOM   680  C  CD2    . LEU A 1 94  ? -23.61000 8.76800   -31.25400 1.000 20.43590 ? 87  LEU A CD2    1 
ATOM   681  N  N      . ASP A 1 95  ? -26.84300 9.04200   -26.89600 1.000 15.49493 ? 88  ASP A N      1 
ATOM   682  C  CA     . ASP A 1 95  ? -28.17400 9.13800   -26.31900 1.000 16.33378 ? 88  ASP A CA     1 
ATOM   683  C  C      . ASP A 1 95  ? -28.04700 8.86600   -24.82800 1.000 15.51494 ? 88  ASP A C      1 
ATOM   684  O  O      . ASP A 1 95  ? -27.12700 8.17200   -24.39100 1.000 13.03737 ? 88  ASP A O      1 
ATOM   685  C  CB     . ASP A 1 95  ? -29.13000 8.15900   -27.03300 1.000 16.74366 ? 88  ASP A CB     1 
ATOM   686  C  CG     . ASP A 1 95  ? -30.60300 8.34500   -26.65100 1.000 20.28049 ? 88  ASP A CG     1 
ATOM   687  O  OD1    . ASP A 1 95  ? -30.98300 9.45900   -26.21600 1.000 15.55403 ? 88  ASP A OD1    1 
ATOM   688  O  OD2    . ASP A 1 95  ? -31.40600 7.41900   -26.94500 1.000 19.85656 ? 88  ASP A OD2    1 
ATOM   689  N  N      . VAL A 1 96  ? -28.91900 9.50300   -24.05200 1.000 13.19843 ? 89  VAL A N      1 
ATOM   690  C  CA     . VAL A 1 96  ? -29.06500 9.28000   -22.61400 1.000 14.82183 ? 89  VAL A CA     1 
ATOM   691  C  C      . VAL A 1 96  ? -30.56000 9.25600   -22.34700 1.000 14.21344 ? 89  VAL A C      1 
ATOM   692  O  O      . VAL A 1 96  ? -31.27500 10.13900  -22.82600 1.000 14.11643 ? 89  VAL A O      1 
ATOM   693  C  CB     . VAL A 1 96  ? -28.42000 10.39400  -21.76200 1.000 15.87388 ? 89  VAL A CB     1 
ATOM   694  C  CG1    . VAL A 1 96  ? -28.48800 10.02700  -20.26100 1.000 14.61786 ? 89  VAL A CG1    1 
ATOM   695  C  CG2    . VAL A 1 96  ? -27.00200 10.68300  -22.20500 1.000 15.86262 ? 89  VAL A CG2    1 
ATOM   696  N  N      . PHE A 1 97  ? -31.03400 8.27900   -21.58300 1.000 13.53733 ? 90  PHE A N      1 
ATOM   697  C  CA     . PHE A 1 97  ? -32.48300 8.16000   -21.45000 1.000 19.59872 ? 90  PHE A CA     1 
ATOM   698  C  C      . PHE A 1 97  ? -32.84600 7.44500   -20.16100 1.000 16.47300 ? 90  PHE A C      1 
ATOM   699  O  O      . PHE A 1 97  ? -32.02700 6.73500   -19.55800 1.000 15.99316 ? 90  PHE A O      1 
ATOM   700  C  CB     . PHE A 1 97  ? -33.10400 7.47400   -22.69600 1.000 15.13319 ? 90  PHE A CB     1 
ATOM   701  C  CG     . PHE A 1 97  ? -32.75800 6.00100   -22.85300 1.000 14.70143 ? 90  PHE A CG     1 
ATOM   702  C  CD1    . PHE A 1 97  ? -33.36200 5.03200   -22.07200 1.000 15.19348 ? 90  PHE A CD1    1 
ATOM   703  C  CD2    . PHE A 1 97  ? -31.85500 5.59300   -23.83400 1.000 15.78928 ? 90  PHE A CD2    1 
ATOM   704  C  CE1    . PHE A 1 97  ? -33.04700 3.68300   -22.22500 1.000 14.57322 ? 90  PHE A CE1    1 
ATOM   705  C  CE2    . PHE A 1 97  ? -31.52600 4.25400   -23.99400 1.000 13.38717 ? 90  PHE A CE2    1 
ATOM   706  C  CZ     . PHE A 1 97  ? -32.13400 3.29200   -23.19800 1.000 16.38239 ? 90  PHE A CZ     1 
ATOM   707  N  N      . THR A 1 98  ? -34.08900 7.67300   -19.72700 1.000 14.64010 ? 91  THR A N      1 
ATOM   708  C  CA     . THR A 1 98  ? -34.66800 6.98100   -18.58600 1.000 16.30790 ? 91  THR A CA     1 
ATOM   709  C  C      . THR A 1 98  ? -36.12300 6.67000   -18.92300 1.000 18.77510 ? 91  THR A C      1 
ATOM   710  O  O      . THR A 1 98  ? -36.78600 7.46300   -19.60700 1.000 18.09350 ? 91  THR A O      1 
ATOM   711  C  CB     . THR A 1 98  ? -34.59100 7.79300   -17.28400 1.000 17.18191 ? 91  THR A CB     1 
ATOM   712  O  OG1    . THR A 1 98  ? -35.30500 7.10700   -16.24300 1.000 21.37833 ? 91  THR A OG1    1 
ATOM   713  C  CG2    . THR A 1 98  ? -35.19300 9.18300   -17.45100 1.000 17.49418 ? 91  THR A CG2    1 
ATOM   714  N  N      . PRO A 1 99  ? -36.63500 5.51800   -18.49500 1.000 21.59720 ? 92  PRO A N      1 
ATOM   715  C  CA     . PRO A 1 99  ? -38.06200 5.22900   -18.72600 1.000 23.04742 ? 92  PRO A CA     1 
ATOM   716  C  C      . PRO A 1 99  ? -38.98800 6.10300   -17.89300 1.000 26.89033 ? 92  PRO A C      1 
ATOM   717  O  O      . PRO A 1 99  ? -40.15700 6.25200   -18.25100 1.000 25.74925 ? 92  PRO A O      1 
ATOM   718  C  CB     . PRO A 1 99  ? -38.18900 3.74700   -18.34200 1.000 25.34437 ? 92  PRO A CB     1 
ATOM   719  C  CG     . PRO A 1 99  ? -37.03600 3.51200   -17.40100 1.000 27.54952 ? 92  PRO A CG     1 
ATOM   720  C  CD     . PRO A 1 99  ? -35.92400 4.39400   -17.85900 1.000 18.79119 ? 92  PRO A CD     1 
ATOM   721  N  N      . ALA A 1 100 ? -38.49300 6.70000   -16.81000 1.000 30.39890 ? 93  ALA A N      1 
ATOM   722  C  CA     . ALA A 1 100 ? -39.31200 7.54900   -15.95000 1.000 29.46817 ? 93  ALA A CA     1 
ATOM   723  C  C      . ALA A 1 100 ? -39.81000 8.78900   -16.68500 1.000 30.79786 ? 93  ALA A C      1 
ATOM   724  O  O      . ALA A 1 100 ? -39.08600 9.38300   -17.48900 1.000 28.19835 ? 93  ALA A O      1 
ATOM   725  C  CB     . ALA A 1 100 ? -38.49400 7.97200   -14.73000 1.000 27.48556 ? 93  ALA A CB     1 
ATOM   726  N  N      . ARG A 1 101 ? -41.05000 9.20500   -16.39400 1.000 35.21774 ? 94  ARG A N      1 
ATOM   727  C  CA     . ARG A 1 101 ? -41.57400 10.45600  -16.94400 1.000 34.30844 ? 94  ARG A CA     1 
ATOM   728  C  C      . ARG A 1 101 ? -41.62200 11.58600  -15.92600 1.000 33.11369 ? 94  ARG A C      1 
ATOM   729  O  O      . ARG A 1 101 ? -42.12700 12.66500  -16.24000 1.000 38.85720 ? 94  ARG A O      1 
ATOM   730  C  CB     . ARG A 1 101 ? -42.96300 10.26900  -17.55700 1.000 40.81384 ? 94  ARG A CB     1 
ATOM   731  C  CG     . ARG A 1 101 ? -43.19500 8.93600   -18.22700 1.000 39.57311 ? 94  ARG A CG     1 
ATOM   732  C  CD     . ARG A 1 101 ? -44.62400 8.85900   -18.73900 1.000 49.10976 ? 94  ARG A CD     1 
ATOM   733  N  NE     . ARG A 1 101 ? -45.00000 7.52200   -19.18100 1.000 49.03681 ? 94  ARG A NE     1 
ATOM   734  C  CZ     . ARG A 1 101 ? -45.00900 6.45000   -18.40100 1.000 54.76846 ? 94  ARG A CZ     1 
ATOM   735  N  NH1    . ARG A 1 101 ? -44.62400 6.51100   -17.13400 1.000 51.65534 ? 94  ARG A NH1    1 
ATOM   736  N  NH2    . ARG A 1 101 ? -45.41800 5.28700   -18.90200 1.000 56.28000 ? 94  ARG A NH2    1 
ATOM   737  N  N      . SER A 1 102 ? -41.08600 11.37300  -14.73000 1.000 33.78412 ? 95  SER A N      1 
ATOM   738  C  CA     . SER A 1 102 ? -41.10400 12.37000  -13.67200 1.000 34.56991 ? 95  SER A CA     1 
ATOM   739  C  C      . SER A 1 102 ? -39.86200 12.19600  -12.81300 1.000 25.64560 ? 95  SER A C      1 
ATOM   740  O  O      . SER A 1 102 ? -39.28400 11.11000  -12.74700 1.000 26.19256 ? 95  SER A O      1 
ATOM   741  C  CB     . SER A 1 102 ? -42.39000 12.24800  -12.84200 1.000 30.34337 ? 95  SER A CB     1 
ATOM   742  O  OG     . SER A 1 102 ? -42.19700 11.39700  -11.72100 1.000 34.35464 ? 95  SER A OG     1 
ATOM   743  N  N      . LEU A 1 103 ? -39.44600 13.28100  -12.16300 1.000 27.62044 ? 96  LEU A N      1 
ATOM   744  C  CA     . LEU A 1 103 ? -38.26900 13.19800  -11.30500 1.000 28.87023 ? 96  LEU A CA     1 
ATOM   745  C  C      . LEU A 1 103 ? -38.50200 12.25100  -10.13300 1.000 26.89961 ? 96  LEU A C      1 
ATOM   746  O  O      . LEU A 1 103 ? -37.57300 11.56700  -9.68600  1.000 25.96930 ? 96  LEU A O      1 
ATOM   747  C  CB     . LEU A 1 103 ? -37.88000 14.59100  -10.80600 1.000 24.02802 ? 96  LEU A CB     1 
ATOM   748  C  CG     . LEU A 1 103 ? -37.06000 14.63400  -9.52000  1.000 28.55787 ? 96  LEU A CG     1 
ATOM   749  C  CD1    . LEU A 1 103 ? -35.62500 14.26500  -9.82700  1.000 24.88842 ? 96  LEU A CD1    1 
ATOM   750  C  CD2    . LEU A 1 103 ? -37.12600 16.02300  -8.88600  1.000 24.45228 ? 96  LEU A CD2    1 
ATOM   751  N  N      . GLU A 1 104 ? -39.73100 12.18400  -9.62500  1.000 33.87108 ? 97  GLU A N      1 
ATOM   752  C  CA     . GLU A 1 104 ? -40.01900 11.27600  -8.51900  1.000 35.13240 ? 97  GLU A CA     1 
ATOM   753  C  C      . GLU A 1 104 ? -40.09700 9.81800   -8.94600  1.000 31.79871 ? 97  GLU A C      1 
ATOM   754  O  O      . GLU A 1 104 ? -39.87700 8.93500   -8.11300  1.000 37.73027 ? 97  GLU A O      1 
ATOM   755  C  CB     . GLU A 1 104 ? -41.30200 11.70700  -7.80400  1.000 36.35674 ? 97  GLU A CB     1 
ATOM   756  C  CG     . GLU A 1 104 ? -42.38300 12.16500  -8.74600  1.000 40.00219 ? 97  GLU A CG     1 
ATOM   757  C  CD     . GLU A 1 104 ? -42.21200 13.64200  -9.09300  1.000 46.14286 ? 97  GLU A CD     1 
ATOM   758  O  OE1    . GLU A 1 104 ? -41.30200 14.28300  -8.52300  1.000 52.77417 ? 97  GLU A OE1    1 
ATOM   759  O  OE2    . GLU A 1 104 ? -42.95200 14.16100  -9.95500  1.000 55.29574 ? 97  GLU A OE2    1 
ATOM   760  N  N      . GLU A 1 105 ? -40.37500 9.54200   -10.21200 1.000 29.79851 ? 98  GLU A N      1 
ATOM   761  C  CA     . GLU A 1 105 ? -40.31100 8.18400   -10.73300 1.000 28.96380 ? 98  GLU A CA     1 
ATOM   762  C  C      . GLU A 1 105 ? -38.89400 7.79500   -11.14900 1.000 29.16110 ? 98  GLU A C      1 
ATOM   763  O  O      . GLU A 1 105 ? -38.61700 6.61100   -11.37000 1.000 26.80022 ? 98  GLU A O      1 
ATOM   764  C  CB     . GLU A 1 105 ? -41.27600 8.06800   -11.91800 1.000 33.17581 ? 98  GLU A CB     1 
ATOM   765  C  CG     . GLU A 1 105 ? -41.23200 6.78000   -12.71100 1.000 38.87438 ? 98  GLU A CG     1 
ATOM   766  C  CD     . GLU A 1 105 ? -42.43500 6.64000   -13.64900 1.000 39.39503 ? 98  GLU A CD     1 
ATOM   767  O  OE1    . GLU A 1 105 ? -42.66300 7.54300   -14.48900 1.000 35.28684 ? 98  GLU A OE1    1 
ATOM   768  O  OE2    . GLU A 1 105 ? -43.14700 5.62100   -13.54800 1.000 49.16829 ? 98  GLU A OE2    1 
ATOM   769  N  N      . PHE A 1 106 ? -37.99600 8.76800   -11.22500 1.000 29.60900 ? 99  PHE A N      1 
ATOM   770  C  CA     . PHE A 1 106 ? -36.68200 8.59600   -11.83500 1.000 26.33810 ? 99  PHE A CA     1 
ATOM   771  C  C      . PHE A 1 106 ? -35.80800 7.69700   -10.96500 1.000 22.82872 ? 99  PHE A C      1 
ATOM   772  O  O      . PHE A 1 106 ? -35.50700 8.04600   -9.82100  1.000 27.87478 ? 99  PHE A O      1 
ATOM   773  C  CB     . PHE A 1 106 ? -36.07200 9.98600   -12.00400 1.000 23.72887 ? 99  PHE A CB     1 
ATOM   774  C  CG     . PHE A 1 106 ? -34.67000 10.01200  -12.53600 1.000 24.47868 ? 99  PHE A CG     1 
ATOM   775  C  CD1    . PHE A 1 106 ? -34.30800 9.25700   -13.64400 1.000 19.54940 ? 99  PHE A CD1    1 
ATOM   776  C  CD2    . PHE A 1 106 ? -33.72700 10.86000  -11.96200 1.000 20.34742 ? 99  PHE A CD2    1 
ATOM   777  C  CE1    . PHE A 1 106 ? -33.01800 9.31100   -14.13900 1.000 20.73840 ? 99  PHE A CE1    1 
ATOM   778  C  CE2    . PHE A 1 106 ? -32.44400 10.91800  -12.45900 1.000 20.46380 ? 99  PHE A CE2    1 
ATOM   779  C  CZ     . PHE A 1 106 ? -32.08700 10.15100  -13.54800 1.000 16.93658 ? 99  PHE A CZ     1 
ATOM   780  N  N      . ASN A 1 107 ? -35.41800 6.51900   -11.48500 1.000 21.36525 ? 100 ASN A N      1 
ATOM   781  C  CA     . ASN A 1 107 ? -34.49900 5.68200   -10.71600 1.000 24.78912 ? 100 ASN A CA     1 
ATOM   782  C  C      . ASN A 1 107 ? -33.55600 4.81000   -11.55000 1.000 30.90234 ? 100 ASN A C      1 
ATOM   783  O  O      . ASN A 1 107 ? -32.84900 3.98100   -10.96300 1.000 28.28424 ? 100 ASN A O      1 
ATOM   784  C  CB     . ASN A 1 107 ? -35.28100 4.78700   -9.73600  1.000 32.50031 ? 100 ASN A CB     1 
ATOM   785  C  CG     . ASN A 1 107 ? -34.45500 4.40000   -8.50700  1.000 36.92882 ? 100 ASN A CG     1 
ATOM   786  O  OD1    . ASN A 1 107 ? -33.99700 5.26300   -7.74700  1.000 43.24213 ? 100 ASN A OD1    1 
ATOM   787  N  ND2    . ASN A 1 107 ? -34.27300 3.10100   -8.30400  1.000 40.73232 ? 100 ASN A ND2    1 
ATOM   788  N  N      . ASP A 1 108 ? -33.51200 4.94000   -12.87900 1.000 24.72257 ? 101 ASP A N      1 
ATOM   789  C  CA     . ASP A 1 108 ? -32.49000 4.28500   -13.69200 1.000 24.46198 ? 101 ASP A CA     1 
ATOM   790  C  C      . ASP A 1 108 ? -31.97900 5.24900   -14.74800 1.000 20.20736 ? 101 ASP A C      1 
ATOM   791  O  O      . ASP A 1 108 ? -32.67600 6.18200   -15.15000 1.000 19.55881 ? 101 ASP A O      1 
ATOM   792  C  CB     . ASP A 1 108 ? -32.97700 3.01000   -14.39900 1.000 25.44448 ? 101 ASP A CB     1 
ATOM   793  C  CG     . ASP A 1 108 ? -33.50300 1.97400   -13.44800 1.000 30.45859 ? 101 ASP A CG     1 
ATOM   794  O  OD1    . ASP A 1 108 ? -32.67700 1.35000   -12.74700 1.000 31.36486 ? 101 ASP A OD1    1 
ATOM   795  O  OD2    . ASP A 1 108 ? -34.73300 1.77300   -13.41100 1.000 33.40400 ? 101 ASP A OD2    1 
ATOM   796  N  N      . VAL A 1 109 ? -30.75500 4.99600   -15.20900 1.000 16.46662 ? 102 VAL A N      1 
ATOM   797  C  CA     . VAL A 1 109 ? -30.10700 5.83700   -16.20900 1.000 17.70821 ? 102 VAL A CA     1 
ATOM   798  C  C      . VAL A 1 109 ? -29.44700 4.91700   -17.22600 1.000 15.88274 ? 102 VAL A C      1 
ATOM   799  O  O      . VAL A 1 109 ? -28.74300 3.97300   -16.84700 1.000 16.28683 ? 102 VAL A O      1 
ATOM   800  C  CB     . VAL A 1 109 ? -29.05800 6.78400   -15.58600 1.000 20.63638 ? 102 VAL A CB     1 
ATOM   801  C  CG1    . VAL A 1 109 ? -28.33900 7.59900   -16.68100 1.000 16.82706 ? 102 VAL A CG1    1 
ATOM   802  C  CG2    . VAL A 1 109 ? -29.68800 7.68000   -14.52800 1.000 22.75846 ? 102 VAL A CG2    1 
ATOM   803  N  N      . TYR A 1 110 ? -29.67800 5.18400   -18.50300 1.000 16.13456 ? 103 TYR A N      1 
ATOM   804  C  CA     . TYR A 1 110 ? -29.10400 4.40600   -19.59400 1.000 13.27454 ? 103 TYR A CA     1 
ATOM   805  C  C      . TYR A 1 110 ? -28.25100 5.31100   -20.47100 1.000 13.17101 ? 103 TYR A C      1 
ATOM   806  O  O      . TYR A 1 110 ? -28.68200 6.40400   -20.82900 1.000 14.49647 ? 103 TYR A O      1 
ATOM   807  C  CB     . TYR A 1 110 ? -30.19900 3.79200   -20.45300 1.000 14.69450 ? 103 TYR A CB     1 
ATOM   808  C  CG     . TYR A 1 110 ? -30.99900 2.71300   -19.77100 1.000 16.73948 ? 103 TYR A CG     1 
ATOM   809  C  CD1    . TYR A 1 110 ? -32.10100 3.04100   -18.99500 1.000 15.95049 ? 103 TYR A CD1    1 
ATOM   810  C  CD2    . TYR A 1 110 ? -30.70700 1.37100   -19.96800 1.000 16.80853 ? 103 TYR A CD2    1 
ATOM   811  C  CE1    . TYR A 1 110 ? -32.86300 2.05400   -18.37400 1.000 17.95554 ? 103 TYR A CE1    1 
ATOM   812  C  CE2    . TYR A 1 110 ? -31.46700 0.38000   -19.36200 1.000 15.84393 ? 103 TYR A CE2    1 
ATOM   813  C  CZ     . TYR A 1 110 ? -32.54200 0.72800   -18.57200 1.000 17.96091 ? 103 TYR A CZ     1 
ATOM   814  O  OH     . TYR A 1 110 ? -33.30500 -0.25500  -17.97900 1.000 16.50175 ? 103 TYR A OH     1 
ATOM   815  N  N      . LEU A 1 111 ? -27.06300 4.82900   -20.85500 1.000 13.96972 ? 104 LEU A N      1 
ATOM   816  C  CA     . LEU A 1 111 ? -26.12100 5.57400   -21.68700 1.000 12.49247 ? 104 LEU A CA     1 
ATOM   817  C  C      . LEU A 1 111 ? -25.84700 4.80500   -22.98100 1.000 11.49406 ? 104 LEU A C      1 
ATOM   818  O  O      . LEU A 1 111 ? -25.65900 3.58500   -22.95100 1.000 15.41330 ? 104 LEU A O      1 
ATOM   819  C  CB     . LEU A 1 111 ? -24.81100 5.78700   -20.94100 1.000 12.44714 ? 104 LEU A CB     1 
ATOM   820  C  CG     . LEU A 1 111 ? -24.91100 6.25700   -19.48900 1.000 15.30301 ? 104 LEU A CG     1 
ATOM   821  C  CD1    . LEU A 1 111 ? -23.54000 6.35400   -18.86800 1.000 16.47415 ? 104 LEU A CD1    1 
ATOM   822  C  CD2    . LEU A 1 111 ? -25.51500 7.63600   -19.50200 1.000 14.50922 ? 104 LEU A CD2    1 
ATOM   823  N  N      . VAL A 1 112 ? -25.78900 5.52500   -24.11300 1.000 11.91002 ? 105 VAL A N      1 
ATOM   824  C  CA     . VAL A 1 112 ? -25.62600 4.91600   -25.43500 1.000 12.53863 ? 105 VAL A CA     1 
ATOM   825  C  C      . VAL A 1 112 ? -24.42800 5.51600   -26.16400 1.000 14.09449 ? 105 VAL A C      1 
ATOM   826  O  O      . VAL A 1 112 ? -24.25100 6.74000   -26.19300 1.000 12.84406 ? 105 VAL A O      1 
ATOM   827  C  CB     . VAL A 1 112 ? -26.88400 5.09000   -26.31300 1.000 11.63956 ? 105 VAL A CB     1 
ATOM   828  C  CG1    . VAL A 1 112 ? -26.74400 4.23600   -27.60200 1.000 12.30933 ? 105 VAL A CG1    1 
ATOM   829  C  CG2    . VAL A 1 112 ? -28.14500 4.72200   -25.54900 1.000 13.14463 ? 105 VAL A CG2    1 
ATOM   830  N  N      . THR A 1 113 ? -23.64900 4.65200   -26.81400 1.000 11.87777 ? 106 THR A N      1 
ATOM   831  C  CA     . THR A 1 113 ? -22.52600 5.07800   -27.63600 1.000 12.53654 ? 106 THR A CA     1 
ATOM   832  C  C      . THR A 1 113 ? -22.39800 4.11100   -28.80900 1.000 14.03980 ? 106 THR A C      1 
ATOM   833  O  O      . THR A 1 113 ? -23.11400 3.11000   -28.89400 1.000 11.57773 ? 106 THR A O      1 
ATOM   834  C  CB     . THR A 1 113 ? -21.23400 5.15200   -26.81500 1.000 14.23057 ? 106 THR A CB     1 
ATOM   835  O  OG1    . THR A 1 113 ? -20.23400 5.84400   -27.57800 1.000 16.53568 ? 106 THR A OG1    1 
ATOM   836  C  CG2    . THR A 1 113 ? -20.74900 3.75500   -26.48300 1.000 12.62913 ? 106 THR A CG2    1 
ATOM   837  N  N      . HIS A 1 114 ? -21.48600 4.42100   -29.72600 1.000 15.76734 ? 107 HIS A N      1 
ATOM   838  C  CA     . HIS A 1 114 ? -21.31500 3.56700   -30.89100 1.000 17.29931 ? 107 HIS A CA     1 
ATOM   839  C  C      . HIS A 1 114 ? -20.64000 2.26200   -30.48200 1.000 16.71920 ? 107 HIS A C      1 
ATOM   840  O  O      . HIS A 1 114 ? -19.70300 2.25200   -29.68300 1.000 15.11020 ? 107 HIS A O      1 
ATOM   841  C  CB     . HIS A 1 114 ? -20.49300 4.27500   -31.97200 1.000 19.47060 ? 107 HIS A CB     1 
ATOM   842  C  CG     . HIS A 1 114 ? -20.30800 3.45800   -33.21800 1.000 23.04672 ? 107 HIS A CG     1 
ATOM   843  N  ND1    . HIS A 1 114 ? -21.33500 3.21100   -34.10900 1.000 27.56784 ? 107 HIS A ND1    1 
ATOM   844  C  CD2    . HIS A 1 114 ? -19.22400 2.80900   -33.70700 1.000 26.51681 ? 107 HIS A CD2    1 
ATOM   845  C  CE1    . HIS A 1 114 ? -20.88500 2.45600   -35.09800 1.000 28.57150 ? 107 HIS A CE1    1 
ATOM   846  N  NE2    . HIS A 1 114 ? -19.60800 2.19700   -34.87700 1.000 25.20597 ? 107 HIS A NE2    1 
ATOM   847  N  N      . LEU A 1 115 ? -21.14300 1.15100   -31.00500 1.000 11.50120 ? 108 LEU A N      1 
ATOM   848  C  CA     . LEU A 1 115 ? -20.57600 -0.14900  -30.66100 1.000 13.94438 ? 108 LEU A CA     1 
ATOM   849  C  C      . LEU A 1 115 ? -19.28100 -0.33100  -31.44300 1.000 16.12017 ? 108 LEU A C      1 
ATOM   850  O  O      . LEU A 1 115 ? -19.29600 -0.27500  -32.67900 1.000 13.74774 ? 108 LEU A O      1 
ATOM   851  C  CB     . LEU A 1 115 ? -21.54700 -1.28200  -30.99400 1.000 13.72065 ? 108 LEU A CB     1 
ATOM   852  C  CG     . LEU A 1 115 ? -21.07900 -2.69700  -30.62700 1.000 15.20423 ? 108 LEU A CG     1 
ATOM   853  C  CD1    . LEU A 1 115 ? -20.95700 -2.81900  -29.11400 1.000 12.03334 ? 108 LEU A CD1    1 
ATOM   854  C  CD2    . LEU A 1 115 ? -21.96400 -3.81000  -31.20800 1.000 15.80913 ? 108 LEU A CD2    1 
ATOM   855  N  N      . MET A 1 116 ? -18.17200 -0.56200  -30.74100 1.000 12.56761 ? 109 MET A N      1 
ATOM   856  C  CA     . MET A 1 116 ? -16.92600 -0.69400  -31.47300 1.000 14.69865 ? 109 MET A CA     1 
ATOM   857  C  C      . MET A 1 116 ? -16.77000 -2.16200  -31.89200 1.000 14.70257 ? 109 MET A C      1 
ATOM   858  O  O      . MET A 1 116 ? -17.57100 -3.01100  -31.51000 1.000 16.91966 ? 109 MET A O      1 
ATOM   859  C  CB     . MET A 1 116 ? -15.75600 -0.25200  -30.58100 1.000 16.48511 ? 109 MET A CB     1 
ATOM   860  C  CG     . MET A 1 116 ? -15.90100 1.22100   -30.17600 1.000 16.43685 ? 109 MET A CG     1 
ATOM   861  S  SD     . MET A 1 116 ? -15.81600 2.39900   -31.51300 1.000 18.24520 ? 109 MET A SD     1 
ATOM   862  C  CE     . MET A 1 116 ? -14.24000 2.07000   -32.23100 1.000 18.36869 ? 109 MET A CE     1 
ATOM   863  N  N      . GLY A 1 117 ? -15.72600 -2.47100  -32.66700 1.000 16.04780 ? 110 GLY A N      1 
ATOM   864  C  CA     . GLY A 1 117 ? -15.55500 -3.82200  -33.18900 1.000 17.56651 ? 110 GLY A CA     1 
ATOM   865  C  C      . GLY A 1 117 ? -14.92200 -4.85500  -32.25800 1.000 18.27984 ? 110 GLY A C      1 
ATOM   866  O  O      . GLY A 1 117 ? -15.33200 -6.02500  -32.24200 1.000 18.06946 ? 110 GLY A O      1 
ATOM   867  N  N      . ALA A 1 118 ? -13.90100 -4.45400  -31.50300 1.000 14.96047 ? 111 ALA A N      1 
ATOM   868  C  CA     . ALA A 1 118 ? -13.22400 -5.35200  -30.57500 1.000 15.87896 ? 111 ALA A CA     1 
ATOM   869  C  C      . ALA A 1 118 ? -12.44100 -4.52500  -29.56700 1.000 17.58407 ? 111 ALA A C      1 
ATOM   870  O  O      . ALA A 1 118 ? -11.95600 -3.44100  -29.89600 1.000 14.77551 ? 111 ALA A O      1 
ATOM   871  C  CB     . ALA A 1 118 ? -12.27100 -6.30700  -31.30600 1.000 19.90816 ? 111 ALA A CB     1 
ATOM   872  N  N      . ASP A 1 119 ? -12.27900 -5.05700  -28.34800 1.000 13.93069 ? 112 ASP A N      1 
ATOM   873  C  CA     . ASP A 1 119 ? -11.41200 -4.34700  -27.41500 1.000 16.09318 ? 112 ASP A CA     1 
ATOM   874  C  C      . ASP A 1 119 ? -9.96700  -4.83000  -27.57900 1.000 20.90605 ? 112 ASP A C      1 
ATOM   875  O  O      . ASP A 1 119 ? -9.67100  -5.72900  -28.37800 1.000 17.70479 ? 112 ASP A O      1 
ATOM   876  C  CB     . ASP A 1 119 ? -11.90600 -4.46800  -25.96700 1.000 15.00446 ? 112 ASP A CB     1 
ATOM   877  C  CG     . ASP A 1 119 ? -11.86800 -5.89100  -25.41300 1.000 18.89327 ? 112 ASP A CG     1 
ATOM   878  O  OD1    . ASP A 1 119 ? -10.89900 -6.62300  -25.66800 1.000 16.95355 ? 112 ASP A OD1    1 
ATOM   879  O  OD2    . ASP A 1 119 ? -12.77100 -6.22800  -24.61400 1.000 18.08530 ? 112 ASP A OD2    1 
ATOM   880  N  N      . LEU A 1 120 ? -9.04400  -4.21600  -26.82800 1.000 15.40394 ? 113 LEU A N      1 
ATOM   881  C  CA     . LEU A 1 120 ? -7.62900  -4.52300  -27.01800 1.000 16.68983 ? 113 LEU A CA     1 
ATOM   882  C  C      . LEU A 1 120 ? -7.23200  -5.86200  -26.41200 1.000 18.63832 ? 113 LEU A C      1 
ATOM   883  O  O      . LEU A 1 120 ? -6.16200  -6.37700  -26.74400 1.000 23.43161 ? 113 LEU A O      1 
ATOM   884  C  CB     . LEU A 1 120 ? -6.74800  -3.41700  -26.42600 1.000 19.92808 ? 113 LEU A CB     1 
ATOM   885  C  CG     . LEU A 1 120 ? -6.56600  -2.11800  -27.20200 1.000 22.60562 ? 113 LEU A CG     1 
ATOM   886  C  CD1    . LEU A 1 120 ? -5.23900  -1.44400  -26.86400 1.000 18.16054 ? 113 LEU A CD1    1 
ATOM   887  C  CD2    . LEU A 1 120 ? -6.68200  -2.37300  -28.69000 1.000 26.84039 ? 113 LEU A CD2    1 
ATOM   888  N  N      . ASN A 1 121 ? -8.03300  -6.42700  -25.51200 1.000 17.65434 ? 114 ASN A N      1 
ATOM   889  C  CA     . ASN A 1 121 ? -7.75300  -7.80000  -25.10400 1.000 23.01495 ? 114 ASN A CA     1 
ATOM   890  C  C      . ASN A 1 121 ? -7.91500  -8.74700  -26.28100 1.000 28.79895 ? 114 ASN A C      1 
ATOM   891  O  O      . ASN A 1 121 ? -7.08000  -9.63300  -26.49800 1.000 32.22308 ? 114 ASN A O      1 
ATOM   892  C  CB     . ASN A 1 121 ? -8.65000  -8.23100  -23.94100 1.000 24.07495 ? 114 ASN A CB     1 
ATOM   893  C  CG     . ASN A 1 121 ? -8.19400  -7.66100  -22.60900 1.000 23.61706 ? 114 ASN A CG     1 
ATOM   894  O  OD1    . ASN A 1 121 ? -7.00600  -7.69700  -22.27700 1.000 20.23180 ? 114 ASN A OD1    1 
ATOM   895  N  ND2    . ASN A 1 121 ? -9.13500  -7.14200  -21.83500 1.000 23.15229 ? 114 ASN A ND2    1 
ATOM   896  N  N      . ASN A 1 122 ? -8.96000  -8.55000  -27.08000 1.000 24.45487 ? 115 ASN A N      1 
ATOM   897  C  CA     . ASN A 1 122 ? -9.20800  -9.47400  -28.18100 1.000 27.51034 ? 115 ASN A CA     1 
ATOM   898  C  C      . ASN A 1 122 ? -8.25000  -9.22200  -29.33900 1.000 36.34091 ? 115 ASN A C      1 
ATOM   899  O  O      . ASN A 1 122 ? -7.83300  -10.16600 -30.01800 1.000 40.57663 ? 115 ASN A O      1 
ATOM   900  C  CB     . ASN A 1 122 ? -10.66000 -9.36400  -28.63300 1.000 31.73078 ? 115 ASN A CB     1 
ATOM   901  C  CG     . ASN A 1 122 ? -11.60300 -9.04600  -27.48400 1.000 34.66562 ? 115 ASN A CG     1 
ATOM   902  O  OD1    . ASN A 1 122 ? -11.43000 -9.49300  -26.34000 1.000 36.22429 ? 115 ASN A OD1    1 
ATOM   903  N  ND2    . ASN A 1 122 ? -12.58900 -8.22600  -27.77600 1.000 35.93496 ? 115 ASN A ND2    1 
ATOM   904  N  N      . ILE A 1 123 ? -7.87500  -7.96300  -29.58300 1.000 32.85514 ? 116 ILE A N      1 
ATOM   905  C  CA     . ILE A 1 123 ? -6.84100  -7.69900  -30.58500 1.000 37.21603 ? 116 ILE A CA     1 
ATOM   906  C  C      . ILE A 1 123 ? -5.54000  -8.40000  -30.20300 1.000 42.00196 ? 116 ILE A C      1 
ATOM   907  O  O      . ILE A 1 123 ? -4.90500  -9.05400  -31.03600 1.000 43.12469 ? 116 ILE A O      1 
ATOM   908  C  CB     . ILE A 1 123 ? -6.63500  -6.18600  -30.77600 1.000 35.24812 ? 116 ILE A CB     1 
ATOM   909  C  CG1    . ILE A 1 123 ? -7.88900  -5.54800  -31.38700 1.000 30.29960 ? 116 ILE A CG1    1 
ATOM   910  C  CG2    . ILE A 1 123 ? -5.40100  -5.92000  -31.62200 1.000 33.88000 ? 116 ILE A CG2    1 
ATOM   911  C  CD1    . ILE A 1 123 ? -8.60900  -6.45300  -32.36100 1.000 32.65585 ? 116 ILE A CD1    1 
ATOM   912  N  N      . VAL A 1 124 ? -5.13000  -8.28300  -28.93300 1.000 37.67791 ? 117 VAL A N      1 
ATOM   913  C  CA     . VAL A 1 124 ? -3.85400  -8.85000  -28.49400 1.000 42.47823 ? 117 VAL A CA     1 
ATOM   914  C  C      . VAL A 1 124 ? -3.88200  -10.37200 -28.57500 1.000 42.96392 ? 117 VAL A C      1 
ATOM   915  O  O      . VAL A 1 124 ? -2.87300  -11.01300 -28.89500 1.000 45.71476 ? 117 VAL A O      1 
ATOM   916  C  CB     . VAL A 1 124 ? -3.51900  -8.36200  -27.07100 1.000 36.39286 ? 117 VAL A CB     1 
ATOM   917  C  CG1    . VAL A 1 124 ? -2.38400  -9.18800  -26.46500 1.000 31.67982 ? 117 VAL A CG1    1 
ATOM   918  C  CG2    . VAL A 1 124 ? -3.15700  -6.89000  -27.08700 1.000 35.41314 ? 117 VAL A CG2    1 
ATOM   919  N  N      . LYS A 1 125 ? -5.03300  -10.97600 -28.27600 1.000 46.50810 ? 118 LYS A N      1 
ATOM   920  C  CA     . LYS A 1 125 ? -5.16600  -12.42300 -28.38800 1.000 53.47817 ? 118 LYS A CA     1 
ATOM   921  C  C      . LYS A 1 125 ? -5.35500  -12.83700 -29.84500 1.000 59.30749 ? 118 LYS A C      1 
ATOM   922  O  O      . LYS A 1 125 ? -4.90100  -13.91200 -30.24500 1.000 61.54095 ? 118 LYS A O      1 
ATOM   923  C  CB     . LYS A 1 125 ? -6.33500  -12.89400 -27.50700 1.000 51.69915 ? 118 LYS A CB     1 
ATOM   924  C  CG     . LYS A 1 125 ? -7.02100  -14.24000 -27.83500 1.000 62.46609 ? 118 LYS A CG     1 
ATOM   925  C  CD     . LYS A 1 125 ? -6.03900  -15.33300 -28.25600 1.000 67.53827 ? 118 LYS A CD     1 
ATOM   926  C  CE     . LYS A 1 125 ? -6.47300  -16.71600 -27.76400 1.000 61.44355 ? 118 LYS A CE     1 
ATOM   927  N  NZ     . LYS A 1 125 ? -5.39200  -17.74300 -27.88400 1.000 54.93609 ? 118 LYS A NZ     1 
ATOM   928  N  N      . CYS A 1 126 ? -5.98200  -11.98800 -30.66200 1.000 56.08483 ? 119 CYS A N      1 
ATOM   929  C  CA     . CYS A 1 126 ? -6.24600  -12.37100 -32.04700 1.000 62.42575 ? 119 CYS A CA     1 
ATOM   930  C  C      . CYS A 1 126 ? -4.98000  -12.34200 -32.89400 1.000 61.86183 ? 119 CYS A C      1 
ATOM   931  O  O      . CYS A 1 126 ? -4.78400  -13.22000 -33.74300 1.000 66.35297 ? 119 CYS A O      1 
ATOM   932  C  CB     . CYS A 1 126 ? -7.32100  -11.47700 -32.66900 1.000 64.10378 ? 119 CYS A CB     1 
ATOM   933  S  SG     . CYS A 1 126 ? -9.01200  -11.97300 -32.26800 1.000 83.55459 ? 119 CYS A SG     1 
ATOM   934  N  N      . GLN A 1 127 ? -4.10900  -11.35300 -32.69100 1.000 66.97609 ? 120 GLN A N      1 
ATOM   935  C  CA     . GLN A 1 127 ? -2.94100  -11.26800 -33.55000 1.000 65.68609 ? 120 GLN A CA     1 
ATOM   936  C  C      . GLN A 1 127 ? -1.74500  -10.65700 -32.84900 1.000 64.67609 ? 120 GLN A C      1 
ATOM   937  O  O      . GLN A 1 127 ? -1.87300  -9.91100  -31.87600 1.000 59.04609 ? 120 GLN A O      1 
ATOM   938  C  CB     . GLN A 1 127 ? -3.21900  -10.47300 -34.82700 1.000 66.47609 ? 120 GLN A CB     1 
ATOM   939  C  CG     . GLN A 1 127 ? -2.45600  -11.05500 -35.99100 1.000 65.08609 ? 120 GLN A CG     1 
ATOM   940  C  CD     . GLN A 1 127 ? -3.21500  -12.16300 -36.68700 1.000 62.00609 ? 120 GLN A CD     1 
ATOM   941  O  OE1    . GLN A 1 127 ? -4.42500  -12.28000 -36.55000 1.000 58.64609 ? 120 GLN A OE1    1 
ATOM   942  N  NE2    . GLN A 1 127 ? -2.47700  -13.02800 -37.37300 1.000 65.31609 ? 120 GLN A NE2    1 
ATOM   943  N  N      . LYS A 1 128 ? -0.57200  -11.00600 -33.36700 1.000 50.23046 ? 121 LYS A N      1 
ATOM   944  C  CA     . LYS A 1 128 ? 0.64900   -10.29600 -33.03200 1.000 45.67026 ? 121 LYS A CA     1 
ATOM   945  C  C      . LYS A 1 128 ? 0.70100   -9.02700  -33.86600 1.000 48.68628 ? 121 LYS A C      1 
ATOM   946  O  O      . LYS A 1 128 ? 0.37200   -9.03700  -35.05200 1.000 40.41351 ? 121 LYS A O      1 
ATOM   947  C  CB     . LYS A 1 128 ? 1.87900   -11.16700 -33.31000 1.000 46.27752 ? 121 LYS A CB     1 
ATOM   948  C  CG     . LYS A 1 128 ? 3.17300   -10.61300 -32.73400 1.000 45.07729 ? 121 LYS A CG     1 
ATOM   949  C  CD     . LYS A 1 128 ? 2.97500   -10.16800 -31.28500 1.000 39.41924 ? 121 LYS A CD     1 
ATOM   950  C  CE     . LYS A 1 128 ? 4.16100   -9.39100  -30.73300 1.000 34.80716 ? 121 LYS A CE     1 
ATOM   951  N  NZ     . LYS A 1 128 ? 5.30000   -10.26800 -30.36000 1.000 43.33170 ? 121 LYS A NZ     1 
ATOM   952  N  N      . LEU A 1 129 ? 1.09900   -7.93600  -33.23600 1.000 40.18029 ? 122 LEU A N      1 
ATOM   953  C  CA     . LEU A 1 129 ? 0.93600   -6.60800  -33.79700 1.000 28.55789 ? 122 LEU A CA     1 
ATOM   954  C  C      . LEU A 1 129 ? 2.25800   -6.14900  -34.39600 1.000 23.61443 ? 122 LEU A C      1 
ATOM   955  O  O      . LEU A 1 129 ? 3.31700   -6.35900  -33.80500 1.000 24.65722 ? 122 LEU A O      1 
ATOM   956  C  CB     . LEU A 1 129 ? 0.47500   -5.64500  -32.69900 1.000 25.75906 ? 122 LEU A CB     1 
ATOM   957  C  CG     . LEU A 1 129 ? -1.02600  -5.67900  -32.44100 1.000 25.45234 ? 122 LEU A CG     1 
ATOM   958  C  CD1    . LEU A 1 129 ? -1.39300  -4.79000  -31.24900 1.000 23.55954 ? 122 LEU A CD1    1 
ATOM   959  C  CD2    . LEU A 1 129 ? -1.81900  -5.28800  -33.68700 1.000 30.46496 ? 122 LEU A CD2    1 
ATOM   960  N  N      . THR A 1 130 ? 2.19800   -5.55500  -35.58600 1.000 24.27133 ? 123 THR A N      1 
ATOM   961  C  CA     . THR A 1 130 ? 3.40800   -4.99600  -36.16000 1.000 20.41409 ? 123 THR A CA     1 
ATOM   962  C  C      . THR A 1 130 ? 3.74900   -3.68700  -35.45800 1.000 19.92023 ? 123 THR A C      1 
ATOM   963  O  O      . THR A 1 130 ? 2.94100   -3.12600  -34.71600 1.000 18.76987 ? 123 THR A O      1 
ATOM   964  C  CB     . THR A 1 130 ? 3.25200   -4.75700  -37.66300 1.000 24.05257 ? 123 THR A CB     1 
ATOM   965  O  OG1    . THR A 1 130 ? 2.57200   -3.51900  -37.89400 1.000 22.29758 ? 123 THR A OG1    1 
ATOM   966  C  CG2    . THR A 1 130 ? 2.48000   -5.91100  -38.32900 1.000 29.42154 ? 123 THR A CG2    1 
ATOM   967  N  N      . ASP A 1 131 ? 4.97100   -3.19600  -35.69900 1.000 16.61363 ? 124 ASP A N      1 
ATOM   968  C  CA     . ASP A 1 131 ? 5.39800   -1.97000  -35.02900 1.000 20.20573 ? 124 ASP A CA     1 
ATOM   969  C  C      . ASP A 1 131 ? 4.55500   -0.78800  -35.48700 1.000 17.61842 ? 124 ASP A C      1 
ATOM   970  O  O      . ASP A 1 131 ? 4.24900   0.11000   -34.69300 1.000 14.76942 ? 124 ASP A O      1 
ATOM   971  C  CB     . ASP A 1 131 ? 6.87300   -1.69100  -35.29700 1.000 20.54535 ? 124 ASP A CB     1 
ATOM   972  C  CG     . ASP A 1 131 ? 7.40300   -0.54100  -34.46800 1.000 20.36240 ? 124 ASP A CG     1 
ATOM   973  O  OD1    . ASP A 1 131 ? 7.20200   -0.53500  -33.22600 1.000 16.50386 ? 124 ASP A OD1    1 
ATOM   974  O  OD2    . ASP A 1 131 ? 8.01800   0.36600   -35.06700 1.000 18.65856 ? 124 ASP A OD2    1 
ATOM   975  N  N      . ASP A 1 132 ? 4.19400   -0.76600  -36.77600 1.000 15.82006 ? 125 ASP A N      1 
ATOM   976  C  CA     . ASP A 1 132 ? 3.27700   0.24300   -37.28500 1.000 20.83293 ? 125 ASP A CA     1 
ATOM   977  C  C      . ASP A 1 132 ? 1.95300   0.22700   -36.53400 1.000 17.86055 ? 125 ASP A C      1 
ATOM   978  O  O      . ASP A 1 132 ? 1.42400   1.28700   -36.19100 1.000 15.65420 ? 125 ASP A O      1 
ATOM   979  C  CB     . ASP A 1 132 ? 3.01200   0.02600   -38.77200 1.000 21.64478 ? 125 ASP A CB     1 
ATOM   980  C  CG     . ASP A 1 132 ? 2.20400   1.15500   -39.38400 1.000 28.36905 ? 125 ASP A CG     1 
ATOM   981  O  OD1    . ASP A 1 132 ? 2.44700   2.34300   -39.04800 1.000 26.60407 ? 125 ASP A OD1    1 
ATOM   982  O  OD2    . ASP A 1 132 ? 1.27300   0.84300   -40.15700 1.000 38.11695 ? 125 ASP A OD2    1 
ATOM   983  N  N      . HIS A 1 133 ? 1.37100   -0.96400  -36.33600 1.000 16.82610 ? 126 HIS A N      1 
ATOM   984  C  CA     . HIS A 1 133 ? 0.13900   -1.07300  -35.55900 1.000 19.56759 ? 126 HIS A CA     1 
ATOM   985  C  C      . HIS A 1 133 ? 0.31700   -0.46700  -34.17900 1.000 14.88156 ? 126 HIS A C      1 
ATOM   986  O  O      . HIS A 1 133 ? -0.52800  0.30600   -33.71800 1.000 13.96904 ? 126 HIS A O      1 
ATOM   987  C  CB     . HIS A 1 133 ? -0.29200  -2.53500  -35.41100 1.000 20.18268 ? 126 HIS A CB     1 
ATOM   988  C  CG     . HIS A 1 133 ? -0.89400  -3.13200  -36.64100 1.000 27.02161 ? 126 HIS A CG     1 
ATOM   989  N  ND1    . HIS A 1 133 ? -0.44300  -4.31300  -37.19000 1.000 32.21007 ? 126 HIS A ND1    1 
ATOM   990  C  CD2    . HIS A 1 133 ? -1.94800  -2.74400  -37.39700 1.000 32.86904 ? 126 HIS A CD2    1 
ATOM   991  C  CE1    . HIS A 1 133 ? -1.17800  -4.61300  -38.24700 1.000 34.85062 ? 126 HIS A CE1    1 
ATOM   992  N  NE2    . HIS A 1 133 ? -2.09600  -3.67500  -38.39600 1.000 32.91159 ? 126 HIS A NE2    1 
ATOM   993  N  N      . VAL A 1 134 ? 1.40400   -0.83400  -33.49000 1.000 14.02224 ? 127 VAL A N      1 
ATOM   994  C  CA     . VAL A 1 134 ? 1.63400   -0.31600  -32.14100 1.000 13.75287 ? 127 VAL A CA     1 
ATOM   995  C  C      . VAL A 1 134 ? 1.73400   1.21100   -32.17100 1.000 14.00169 ? 127 VAL A C      1 
ATOM   996  O  O      . VAL A 1 134 ? 1.15500   1.90400   -31.32300 1.000 12.79271 ? 127 VAL A O      1 
ATOM   997  C  CB     . VAL A 1 134 ? 2.89100   -0.96000  -31.51400 1.000 13.98548 ? 127 VAL A CB     1 
ATOM   998  C  CG1    . VAL A 1 134 ? 3.22500   -0.31100  -30.17200 1.000 12.38865 ? 127 VAL A CG1    1 
ATOM   999  C  CG2    . VAL A 1 134 ? 2.71900   -2.47300  -31.34100 1.000 14.24166 ? 127 VAL A CG2    1 
ATOM   1000 N  N      . GLN A 1 135 ? 2.46000   1.76300   -33.15400 1.000 15.24311 ? 128 GLN A N      1 
ATOM   1001 C  CA     . GLN A 1 135 ? 2.54700   3.22100   -33.29300 1.000 12.10496 ? 128 GLN A CA     1 
ATOM   1002 C  C      . GLN A 1 135 ? 1.16200   3.85100   -33.39900 1.000 13.05793 ? 128 GLN A C      1 
ATOM   1003 O  O      . GLN A 1 135 ? 0.86000   4.85500   -32.73900 1.000 12.97604 ? 128 GLN A O      1 
ATOM   1004 C  CB     . GLN A 1 135 ? 3.36300   3.61500   -34.53600 1.000 13.41741 ? 128 GLN A CB     1 
ATOM   1005 C  CG     . GLN A 1 135 ? 4.86500   3.30200   -34.50200 1.000 14.31703 ? 128 GLN A CG     1 
ATOM   1006 C  CD     . GLN A 1 135 ? 5.54300   3.56400   -35.86600 1.000 21.17927 ? 128 GLN A CD     1 
ATOM   1007 O  OE1    . GLN A 1 135 ? 5.04100   4.33800   -36.69900 1.000 20.54502 ? 128 GLN A OE1    1 
ATOM   1008 N  NE2    . GLN A 1 135 ? 6.64200   2.86500   -36.11500 1.000 17.86345 ? 128 GLN A NE2    1 
ATOM   1009 N  N      . PHE A 1 136 ? 0.32000   3.29600   -34.27000 1.000 12.97816 ? 129 PHE A N      1 
ATOM   1010 C  CA     . PHE A 1 136 ? -0.98600  3.90000   -34.51900 1.000 14.32519 ? 129 PHE A CA     1 
ATOM   1011 C  C      . PHE A 1 136 ? -1.89400  3.78600   -33.30100 1.000 13.15992 ? 129 PHE A C      1 
ATOM   1012 O  O      . PHE A 1 136 ? -2.59500  4.74300   -32.94800 1.000 12.40504 ? 129 PHE A O      1 
ATOM   1013 C  CB     . PHE A 1 136 ? -1.62800  3.24000   -35.73700 1.000 15.88329 ? 129 PHE A CB     1 
ATOM   1014 C  CG     . PHE A 1 136 ? -2.87400  3.92600   -36.21700 1.000 15.29861 ? 129 PHE A CG     1 
ATOM   1015 C  CD1    . PHE A 1 136 ? -2.94200  5.30500   -36.29100 1.000 18.14062 ? 129 PHE A CD1    1 
ATOM   1016 C  CD2    . PHE A 1 136 ? -3.97800  3.18300   -36.60800 1.000 15.78773 ? 129 PHE A CD2    1 
ATOM   1017 C  CE1    . PHE A 1 136 ? -4.09300  5.93500   -36.74900 1.000 17.89094 ? 129 PHE A CE1    1 
ATOM   1018 C  CE2    . PHE A 1 136 ? -5.13200  3.80700   -37.06600 1.000 19.49191 ? 129 PHE A CE2    1 
ATOM   1019 C  CZ     . PHE A 1 136 ? -5.18500  5.18000   -37.13900 1.000 17.50039 ? 129 PHE A CZ     1 
ATOM   1020 N  N      . LEU A 1 137 ? -1.90800  2.62300   -32.65000 1.000 12.06134 ? 130 LEU A N      1 
ATOM   1021 C  CA     . LEU A 1 137 ? -2.77700  2.45300   -31.49300 1.000 11.83400 ? 130 LEU A CA     1 
ATOM   1022 C  C      . LEU A 1 137 ? -2.34300  3.35400   -30.33700 1.000 10.36568 ? 130 LEU A C      1 
ATOM   1023 O  O      . LEU A 1 137 ? -3.16900  4.06400   -29.74600 1.000 12.18949 ? 130 LEU A O      1 
ATOM   1024 C  CB     . LEU A 1 137 ? -2.79000  0.99000   -31.05700 1.000 13.90740 ? 130 LEU A CB     1 
ATOM   1025 C  CG     . LEU A 1 137 ? -3.39200  0.00200   -32.04800 1.000 13.53773 ? 130 LEU A CG     1 
ATOM   1026 C  CD1    . LEU A 1 137 ? -3.06600  -1.38900  -31.59700 1.000 13.36744 ? 130 LEU A CD1    1 
ATOM   1027 C  CD2    . LEU A 1 137 ? -4.89500  0.20300   -32.11800 1.000 14.72574 ? 130 LEU A CD2    1 
ATOM   1028 N  N      . ILE A 1 138 ? -1.05500  3.32900   -29.97900 1.000 10.73570 ? 131 ILE A N      1 
ATOM   1029 C  CA     . ILE A 1 138 ? -0.62100  4.16200   -28.85400 1.000 11.40067 ? 131 ILE A CA     1 
ATOM   1030 C  C      . ILE A 1 138 ? -0.76400  5.63700   -29.21500 1.000 12.23318 ? 131 ILE A C      1 
ATOM   1031 O  O      . ILE A 1 138 ? -1.15100  6.45400   -28.37100 1.000 11.08362 ? 131 ILE A O      1 
ATOM   1032 C  CB     . ILE A 1 138 ? 0.81700   3.82400   -28.40600 1.000 9.22512  ? 131 ILE A CB     1 
ATOM   1033 C  CG1    . ILE A 1 138 ? 0.99100   2.33300   -28.04100 1.000 9.24866  ? 131 ILE A CG1    1 
ATOM   1034 C  CG2    . ILE A 1 138 ? 1.21600   4.70600   -27.17900 1.000 10.11173 ? 131 ILE A CG2    1 
ATOM   1035 C  CD1    . ILE A 1 138 ? -0.00300  1.79000   -27.00500 1.000 12.29952 ? 131 ILE A CD1    1 
ATOM   1036 N  N      . TYR A 1 139 ? -0.49000  6.00000   -30.47700 1.000 10.36897 ? 132 TYR A N      1 
ATOM   1037 C  CA     . TYR A 1 139 ? -0.69000  7.38800   -30.90000 1.000 10.42673 ? 132 TYR A CA     1 
ATOM   1038 C  C      . TYR A 1 139 ? -2.10900  7.85000   -30.59000 1.000 10.08822 ? 132 TYR A C      1 
ATOM   1039 O  O      . TYR A 1 139 ? -2.32300  8.94000   -30.05000 1.000 11.27639 ? 132 TYR A O      1 
ATOM   1040 C  CB     . TYR A 1 139 ? -0.40900  7.56600   -32.39600 1.000 10.52181 ? 132 TYR A CB     1 
ATOM   1041 C  CG     . TYR A 1 139 ? -0.85500  8.94100   -32.89600 1.000 13.52259 ? 132 TYR A CG     1 
ATOM   1042 C  CD1    . TYR A 1 139 ? -0.09100  10.07700  -32.62200 1.000 13.99344 ? 132 TYR A CD1    1 
ATOM   1043 C  CD2    . TYR A 1 139 ? -2.05400  9.11000   -33.58200 1.000 10.00337 ? 132 TYR A CD2    1 
ATOM   1044 C  CE1    . TYR A 1 139 ? -0.48700  11.33000  -33.04700 1.000 12.37230 ? 132 TYR A CE1    1 
ATOM   1045 C  CE2    . TYR A 1 139 ? -2.46900  10.38400  -34.01700 1.000 10.77753 ? 132 TYR A CE2    1 
ATOM   1046 C  CZ     . TYR A 1 139 ? -1.67500  11.48300  -33.73400 1.000 13.59958 ? 132 TYR A CZ     1 
ATOM   1047 O  OH     . TYR A 1 139 ? -2.03300  12.75800  -34.11600 1.000 13.61155 ? 132 TYR A OH     1 
ATOM   1048 N  N      . GLN A 1 140 ? -3.09900  7.02700   -30.93500 1.000 10.80647 ? 133 GLN A N      1 
ATOM   1049 C  CA     . GLN A 1 140 ? -4.49400  7.42000   -30.74700 1.000 9.45093  ? 133 GLN A CA     1 
ATOM   1050 C  C      . GLN A 1 140 ? -4.88200  7.50600   -29.27500 1.000 9.73046  ? 133 GLN A C      1 
ATOM   1051 O  O      . GLN A 1 140 ? -5.68300  8.36900   -28.89200 1.000 8.33746  ? 133 GLN A O      1 
ATOM   1052 C  CB     . GLN A 1 140 ? -5.40300  6.43600   -31.47300 1.000 9.74743  ? 133 GLN A CB     1 
ATOM   1053 C  CG     . GLN A 1 140 ? -5.37900  6.60000   -32.97600 1.000 11.27630 ? 133 GLN A CG     1 
ATOM   1054 C  CD     . GLN A 1 140 ? -6.21500  5.53200   -33.61500 1.000 14.65520 ? 133 GLN A CD     1 
ATOM   1055 O  OE1    . GLN A 1 140 ? -7.40600  5.73000   -33.87400 1.000 13.07023 ? 133 GLN A OE1    1 
ATOM   1056 N  NE2    . GLN A 1 140 ? -5.60700  4.37200   -33.85400 1.000 12.17486 ? 133 GLN A NE2    1 
ATOM   1057 N  N      . ILE A 1 141 ? -4.36900  6.59400   -28.44300 1.000 8.22396  ? 134 ILE A N      1 
ATOM   1058 C  CA     . ILE A 1 141 ? -4.60500  6.70300   -27.00200 1.000 10.41713 ? 134 ILE A CA     1 
ATOM   1059 C  C      . ILE A 1 141 ? -4.08700  8.04000   -26.48500 1.000 10.57324 ? 134 ILE A C      1 
ATOM   1060 O  O      . ILE A 1 141 ? -4.78600  8.75100   -25.75500 1.000 9.40234  ? 134 ILE A O      1 
ATOM   1061 C  CB     . ILE A 1 141 ? -3.97200  5.52000   -26.24300 1.000 10.66693 ? 134 ILE A CB     1 
ATOM   1062 C  CG1    . ILE A 1 141 ? -4.64900  4.19400   -26.62500 1.000 9.30650  ? 134 ILE A CG1    1 
ATOM   1063 C  CG2    . ILE A 1 141 ? -4.03300  5.74100   -24.72100 1.000 9.39354  ? 134 ILE A CG2    1 
ATOM   1064 C  CD1    . ILE A 1 141 ? -3.84300  2.94300   -26.24100 1.000 10.87885 ? 134 ILE A CD1    1 
ATOM   1065 N  N      . LEU A 1 142 ? -2.85000  8.39800   -26.86200 1.000 9.21364  ? 135 LEU A N      1 
ATOM   1066 C  CA     . LEU A 1 142 ? -2.23200  9.64000   -26.40500 1.000 11.31357 ? 135 LEU A CA     1 
ATOM   1067 C  C      . LEU A 1 142 ? -2.96100  10.85900  -26.94300 1.000 10.33304 ? 135 LEU A C      1 
ATOM   1068 O  O      . LEU A 1 142 ? -3.03500  11.89000  -26.25700 1.000 11.43315 ? 135 LEU A O      1 
ATOM   1069 C  CB     . LEU A 1 142 ? -0.76900  9.66600   -26.83700 1.000 8.51291  ? 135 LEU A CB     1 
ATOM   1070 C  CG     . LEU A 1 142 ? 0.12200   8.66000   -26.09000 1.000 10.54554 ? 135 LEU A CG     1 
ATOM   1071 C  CD1    . LEU A 1 142 ? 1.51500   8.61500   -26.70200 1.000 10.31537 ? 135 LEU A CD1    1 
ATOM   1072 C  CD2    . LEU A 1 142 ? 0.22700   9.09900   -24.62300 1.000 7.59846  ? 135 LEU A CD2    1 
ATOM   1073 N  N      . ARG A 1 143 ? -3.49300  10.76600  -28.16500 1.000 9.22331  ? 136 ARG A N      1 
ATOM   1074 C  CA     . ARG A 1 143 ? -4.27500  11.86400  -28.73200 1.000 9.00152  ? 136 ARG A CA     1 
ATOM   1075 C  C      . ARG A 1 143 ? -5.55200  12.09000  -27.92500 1.000 9.41726  ? 136 ARG A C      1 
ATOM   1076 O  O      . ARG A 1 143 ? -5.89000  13.22600  -27.56300 1.000 8.43056  ? 136 ARG A O      1 
ATOM   1077 C  CB     . ARG A 1 143 ? -4.62200  11.55800  -30.19300 1.000 9.78696  ? 136 ARG A CB     1 
ATOM   1078 C  CG     . ARG A 1 143 ? -5.30000  12.70700  -30.94300 1.000 8.70861  ? 136 ARG A CG     1 
ATOM   1079 C  CD     . ARG A 1 143 ? -5.24800  12.45100  -32.45000 1.000 15.42830 ? 136 ARG A CD     1 
ATOM   1080 N  NE     . ARG A 1 143 ? -6.00900  13.44000  -33.21100 1.000 11.44088 ? 136 ARG A NE     1 
ATOM   1081 C  CZ     . ARG A 1 143 ? -7.22900  13.25500  -33.69600 1.000 18.59290 ? 136 ARG A CZ     1 
ATOM   1082 N  NH1    . ARG A 1 143 ? -7.89200  12.12100  -33.50600 1.000 16.29284 ? 136 ARG A NH1    1 
ATOM   1083 N  NH2    . ARG A 1 143 ? -7.79600  14.22500  -34.41300 1.000 21.05971 ? 136 ARG A NH2    1 
ATOM   1084 N  N      . GLY A 1 144 ? -6.28500  11.01000  -27.64100 1.000 10.71754 ? 137 GLY A N      1 
ATOM   1085 C  CA     . GLY A 1 144 ? -7.44000  11.12600  -26.75500 1.000 8.47121  ? 137 GLY A CA     1 
ATOM   1086 C  C      . GLY A 1 144 ? -7.05200  11.59500  -25.36400 1.000 9.65765  ? 137 GLY A C      1 
ATOM   1087 O  O      . GLY A 1 144 ? -7.75400  12.40500  -24.75100 1.000 9.75708  ? 137 GLY A O      1 
ATOM   1088 N  N      . LEU A 1 145 ? -5.90800  11.12400  -24.86400 1.000 9.16353  ? 138 LEU A N      1 
ATOM   1089 C  CA     . LEU A 1 145 ? -5.47500  11.48900  -23.51600 1.000 10.37932 ? 138 LEU A CA     1 
ATOM   1090 C  C      . LEU A 1 145 ? -5.10400  12.96500  -23.43200 1.000 10.60641 ? 138 LEU A C      1 
ATOM   1091 O  O      . LEU A 1 145 ? -5.35200  13.61300  -22.40700 1.000 10.56575 ? 138 LEU A O      1 
ATOM   1092 C  CB     . LEU A 1 145 ? -4.28000  10.63000  -23.09300 1.000 12.27678 ? 138 LEU A CB     1 
ATOM   1093 C  CG     . LEU A 1 145 ? -4.04000  10.37700  -21.60100 1.000 13.41547 ? 138 LEU A CG     1 
ATOM   1094 C  CD1    . LEU A 1 145 ? -5.32800  9.95100   -20.84200 1.000 12.67745 ? 138 LEU A CD1    1 
ATOM   1095 C  CD2    . LEU A 1 145 ? -2.85600  9.39500   -21.34700 1.000 10.97894 ? 138 LEU A CD2    1 
ATOM   1096 N  N      . LYS A 1 146 ? -4.45000  13.50000  -24.47400 1.000 7.93335  ? 139 LYS A N      1 
ATOM   1097 C  CA     . LYS A 1 146 ? -4.13600  14.93000  -24.47300 1.000 10.64851 ? 139 LYS A CA     1 
ATOM   1098 C  C      . LYS A 1 146 ? -5.41400  15.74100  -24.29700 1.000 9.66608  ? 139 LYS A C      1 
ATOM   1099 O  O      . LYS A 1 146 ? -5.46600  16.69300  -23.51000 1.000 9.55989  ? 139 LYS A O      1 
ATOM   1100 C  CB     . LYS A 1 146 ? -3.40600  15.32400  -25.77100 1.000 11.08659 ? 139 LYS A CB     1 
ATOM   1101 C  CG     . LYS A 1 146 ? -3.05700  16.82800  -25.85900 1.000 11.63933 ? 139 LYS A CG     1 
ATOM   1102 C  CD     . LYS A 1 146 ? -2.96800  17.34800  -27.31400 1.000 10.11649 ? 139 LYS A CD     1 
ATOM   1103 C  CE     . LYS A 1 146 ? -2.53900  18.81700  -27.39100 1.000 13.00745 ? 139 LYS A CE     1 
ATOM   1104 N  NZ     . LYS A 1 146 ? -2.30300  19.22900  -28.81300 1.000 10.68072 ? 139 LYS A NZ     1 
ATOM   1105 N  N      . TYR A 1 147 ? -6.47500  15.33000  -24.98900 1.000 9.42331  ? 140 TYR A N      1 
ATOM   1106 C  CA     . TYR A 1 147 ? -7.76300  16.00200  -24.87900 1.000 10.59096 ? 140 TYR A CA     1 
ATOM   1107 C  C      . TYR A 1 147 ? -8.33700  15.86700  -23.47000 1.000 10.66933 ? 140 TYR A C      1 
ATOM   1108 O  O      . TYR A 1 147 ? -8.78000  16.85300  -22.87000 1.000 8.96854  ? 140 TYR A O      1 
ATOM   1109 C  CB     . TYR A 1 147 ? -8.71600  15.41700  -25.93200 1.000 9.96035  ? 140 TYR A CB     1 
ATOM   1110 C  CG     . TYR A 1 147 ? -10.15000 15.88200  -25.84100 1.000 12.30646 ? 140 TYR A CG     1 
ATOM   1111 C  CD1    . TYR A 1 147 ? -11.07200 15.19900  -25.05500 1.000 11.25830 ? 140 TYR A CD1    1 
ATOM   1112 C  CD2    . TYR A 1 147 ? -10.58700 17.01400  -26.54600 1.000 12.78768 ? 140 TYR A CD2    1 
ATOM   1113 C  CE1    . TYR A 1 147 ? -12.39900 15.62400  -24.95600 1.000 10.69571 ? 140 TYR A CE1    1 
ATOM   1114 C  CE2    . TYR A 1 147 ? -11.91700 17.45200  -26.45500 1.000 10.34518 ? 140 TYR A CE2    1 
ATOM   1115 C  CZ     . TYR A 1 147 ? -12.82000 16.73800  -25.66100 1.000 12.81245 ? 140 TYR A CZ     1 
ATOM   1116 O  OH     . TYR A 1 147 ? -14.14700 17.12600  -25.54600 1.000 9.57766  ? 140 TYR A OH     1 
ATOM   1117 N  N      . ILE A 1 148 ? -8.33600  14.64400  -22.92100 1.000 9.98148  ? 141 ILE A N      1 
ATOM   1118 C  CA     . ILE A 1 148 ? -8.87300  14.44000  -21.57000 1.000 7.71096  ? 141 ILE A CA     1 
ATOM   1119 C  C      . ILE A 1 148 ? -8.09200  15.28200  -20.56300 1.000 10.03111 ? 141 ILE A C      1 
ATOM   1120 O  O      . ILE A 1 148 ? -8.67000  15.98900  -19.72200 1.000 9.04854  ? 141 ILE A O      1 
ATOM   1121 C  CB     . ILE A 1 148 ? -8.85200  12.94500  -21.18700 1.000 8.94537  ? 141 ILE A CB     1 
ATOM   1122 C  CG1    . ILE A 1 148 ? -9.84700  12.13800  -22.04400 1.000 10.34694 ? 141 ILE A CG1    1 
ATOM   1123 C  CG2    . ILE A 1 148 ? -9.16400  12.76700  -19.68700 1.000 8.07220  ? 141 ILE A CG2    1 
ATOM   1124 C  CD1    . ILE A 1 148 ? -9.52000  10.64000  -22.07500 1.000 12.58803 ? 141 ILE A CD1    1 
ATOM   1125 N  N      . HIS A 1 149 ? -6.76100  15.20200  -20.61300 1.000 8.12005  ? 142 HIS A N      1 
ATOM   1126 C  CA     . HIS A 1 149 ? -5.97800  15.93900  -19.62600 1.000 8.10171  ? 142 HIS A CA     1 
ATOM   1127 C  C      . HIS A 1 149 ? -6.14700  17.44100  -19.80600 1.000 9.83782  ? 142 HIS A C      1 
ATOM   1128 O  O      . HIS A 1 149 ? -6.05000  18.19400  -18.82900 1.000 9.42268  ? 142 HIS A O      1 
ATOM   1129 C  CB     . HIS A 1 149 ? -4.49500  15.56200  -19.69800 1.000 8.19786  ? 142 HIS A CB     1 
ATOM   1130 C  CG     . HIS A 1 149 ? -4.19200  14.17100  -19.20900 1.000 12.61239 ? 142 HIS A CG     1 
ATOM   1131 N  ND1    . HIS A 1 149 ? -2.99600  13.54000  -19.47500 1.000 11.74650 ? 142 HIS A ND1    1 
ATOM   1132 C  CD2    . HIS A 1 149 ? -4.93500  13.28600  -18.49600 1.000 10.86401 ? 142 HIS A CD2    1 
ATOM   1133 C  CE1    . HIS A 1 149 ? -3.00200  12.33600  -18.92400 1.000 11.45040 ? 142 HIS A CE1    1 
ATOM   1134 N  NE2    . HIS A 1 149 ? -4.17300  12.15000  -18.34100 1.000 11.25279 ? 142 HIS A NE2    1 
ATOM   1135 N  N      . SER A 1 150 ? -6.43600  17.90100  -21.03100 1.000 10.24842 ? 143 SER A N      1 
ATOM   1136 C  CA     . SER A 1 150 ? -6.61100  19.34100  -21.23200 1.000 12.85362 ? 143 SER A CA     1 
ATOM   1137 C  C      . SER A 1 150 ? -7.87000  19.86700  -20.55100 1.000 12.40350 ? 143 SER A C      1 
ATOM   1138 O  O      . SER A 1 150 ? -7.98000  21.07800  -20.32700 1.000 13.12006 ? 143 SER A O      1 
ATOM   1139 C  CB     . SER A 1 150 ? -6.62700  19.68800  -22.72700 1.000 12.88946 ? 143 SER A CB     1 
ATOM   1140 O  OG     . SER A 1 150 ? -7.87600  19.35700  -23.33300 1.000 11.12009 ? 143 SER A OG     1 
ATOM   1141 N  N      . ALA A 1 151 ? -8.79700  18.99100  -20.17900 1.000 12.40368 ? 144 ALA A N      1 
ATOM   1142 C  CA     . ALA A 1 151 ? -9.96000  19.39900  -19.40400 1.000 11.92043 ? 144 ALA A CA     1 
ATOM   1143 C  C      . ALA A 1 151 ? -9.73300  19.26900  -17.90300 1.000 12.96087 ? 144 ALA A C      1 
ATOM   1144 O  O      . ALA A 1 151 ? -10.69000 19.38600  -17.13100 1.000 13.92586 ? 144 ALA A O      1 
ATOM   1145 C  CB     . ALA A 1 151 ? -11.18500 18.58200  -19.82500 1.000 11.13092 ? 144 ALA A CB     1 
ATOM   1146 N  N      . ASP A 1 152 ? -8.49500  19.03000  -17.48100 1.000 11.96673 ? 145 ASP A N      1 
ATOM   1147 C  CA     . ASP A 1 152 ? -8.15600  18.81100  -16.07600 1.000 14.20814 ? 145 ASP A CA     1 
ATOM   1148 C  C      . ASP A 1 152 ? -8.89700  17.59600  -15.51600 1.000 13.99513 ? 145 ASP A C      1 
ATOM   1149 O  O      . ASP A 1 152 ? -9.39000  17.61100  -14.38600 1.000 14.08162 ? 145 ASP A O      1 
ATOM   1150 C  CB     . ASP A 1 152 ? -8.42700  20.06200  -15.23100 1.000 14.57895 ? 145 ASP A CB     1 
ATOM   1151 C  CG     . ASP A 1 152 ? -7.64400  20.05600  -13.91400 1.000 20.27594 ? 145 ASP A CG     1 
ATOM   1152 O  OD1    . ASP A 1 152 ? -6.63700  19.32400  -13.83200 1.000 15.53291 ? 145 ASP A OD1    1 
ATOM   1153 O  OD2    . ASP A 1 152 ? -8.02900  20.77300  -12.96200 1.000 23.05777 ? 145 ASP A OD2    1 
ATOM   1154 N  N      . ILE A 1 153 ? -9.00000  16.55100  -16.33500 1.000 10.22332 ? 146 ILE A N      1 
ATOM   1155 C  CA     . ILE A 1 153 ? -9.57700  15.26200  -15.95700 1.000 9.91818  ? 146 ILE A CA     1 
ATOM   1156 C  C      . ILE A 1 153 ? -8.45800  14.22700  -15.96800 1.000 13.55889 ? 146 ILE A C      1 
ATOM   1157 O  O      . ILE A 1 153 ? -7.58800  14.26500  -16.84000 1.000 11.70145 ? 146 ILE A O      1 
ATOM   1158 C  CB     . ILE A 1 153 ? -10.70100 14.83400  -16.93000 1.000 10.65645 ? 146 ILE A CB     1 
ATOM   1159 C  CG1    . ILE A 1 153 ? -11.86800 15.82800  -16.90800 1.000 14.83704 ? 146 ILE A CG1    1 
ATOM   1160 C  CG2    . ILE A 1 153 ? -11.20700 13.41800  -16.59400 1.000 12.63890 ? 146 ILE A CG2    1 
ATOM   1161 C  CD1    . ILE A 1 153 ? -12.87100 15.60700  -18.05100 1.000 14.28170 ? 146 ILE A CD1    1 
ATOM   1162 N  N      . ILE A 1 154 ? -8.47600  13.30500  -15.00400 1.000 11.21106 ? 147 ILE A N      1 
ATOM   1163 C  CA     . ILE A 1 154 ? -7.63100  12.11700  -15.02800 1.000 9.43420  ? 147 ILE A CA     1 
ATOM   1164 C  C      . ILE A 1 154 ? -8.53200  10.93700  -15.35700 1.000 11.66246 ? 147 ILE A C      1 
ATOM   1165 O  O      . ILE A 1 154 ? -9.56700  10.75200  -14.69900 1.000 12.16415 ? 147 ILE A O      1 
ATOM   1166 C  CB     . ILE A 1 154 ? -6.91700  11.90900  -13.67600 1.000 13.08480 ? 147 ILE A CB     1 
ATOM   1167 C  CG1    . ILE A 1 154 ? -6.08700  13.14100  -13.27600 1.000 12.97773 ? 147 ILE A CG1    1 
ATOM   1168 C  CG2    . ILE A 1 154 ? -6.04400  10.66100  -13.69100 1.000 10.82748 ? 147 ILE A CG2    1 
ATOM   1169 C  CD1    . ILE A 1 154 ? -5.36800  12.96800  -11.91100 1.000 17.86842 ? 147 ILE A CD1    1 
ATOM   1170 N  N      . HIS A 1 155 ? -8.14100  10.11600  -16.34800 1.000 6.87228  ? 148 HIS A N      1 
ATOM   1171 C  CA     . HIS A 1 155 ? -9.00500  8.98600   -16.71600 1.000 9.74496  ? 148 HIS A CA     1 
ATOM   1172 C  C      . HIS A 1 155 ? -9.10900  7.97000   -15.58000 1.000 8.74171  ? 148 HIS A C      1 
ATOM   1173 O  O      . HIS A 1 155 ? -10.21900 7.57400   -15.18700 1.000 11.17551 ? 148 HIS A O      1 
ATOM   1174 C  CB     . HIS A 1 155 ? -8.52300  8.28800   -17.99500 1.000 11.05396 ? 148 HIS A CB     1 
ATOM   1175 C  CG     . HIS A 1 155 ? -9.48400  7.25200   -18.50300 1.000 11.52686 ? 148 HIS A CG     1 
ATOM   1176 N  ND1    . HIS A 1 155 ? -9.54000  5.97100   -17.99600 1.000 12.71458 ? 148 HIS A ND1    1 
ATOM   1177 C  CD2    . HIS A 1 155 ? -10.43200 7.31100   -19.47400 1.000 10.60576 ? 148 HIS A CD2    1 
ATOM   1178 C  CE1    . HIS A 1 155 ? -10.47400 5.28300   -18.63000 1.000 11.96650 ? 148 HIS A CE1    1 
ATOM   1179 N  NE2    . HIS A 1 155 ? -11.03800 6.07400   -19.52800 1.000 8.46488  ? 148 HIS A NE2    1 
ATOM   1180 N  N      . ARG A 1 156 ? -7.96000  7.50200   -15.08200 1.000 10.85530 ? 149 ARG A N      1 
ATOM   1181 C  CA     . ARG A 1 156 ? -7.73700  6.69600   -13.88300 1.000 12.95847 ? 149 ARG A CA     1 
ATOM   1182 C  C      . ARG A 1 156 ? -7.90100  5.20900   -14.13100 1.000 11.67785 ? 149 ARG A C      1 
ATOM   1183 O  O      . ARG A 1 156 ? -7.59300  4.41700   -13.23300 1.000 10.71371 ? 149 ARG A O      1 
ATOM   1184 C  CB     . ARG A 1 156 ? -8.65600  7.07400   -12.70000 1.000 14.61142 ? 149 ARG A CB     1 
ATOM   1185 C  CG     . ARG A 1 156 ? -8.47400  8.47600   -12.16500 1.000 18.02360 ? 149 ARG A CG     1 
ATOM   1186 C  CD     . ARG A 1 156 ? -9.20100  8.65300   -10.83000 1.000 25.37658 ? 149 ARG A CD     1 
ATOM   1187 N  NE     . ARG A 1 156 ? -8.89800  9.92800   -10.18000 1.000 30.92563 ? 149 ARG A NE     1 
ATOM   1188 C  CZ     . ARG A 1 156 ? -9.30300  11.10600  -10.63200 1.000 26.37134 ? 149 ARG A CZ     1 
ATOM   1189 N  NH1    . ARG A 1 156 ? -10.01600 11.20900  -11.74400 1.000 22.87374 ? 149 ARG A NH1    1 
ATOM   1190 N  NH2    . ARG A 1 156 ? -8.99000  12.20600  -9.95100  1.000 21.56627 ? 149 ARG A NH2    1 
ATOM   1191 N  N      . ASP A 1 157 ? -8.38600  4.78200   -15.29000 1.000 10.73941 ? 150 ASP A N      1 
ATOM   1192 C  CA     . ASP A 1 157 ? -8.58800  3.35700   -15.47800 1.000 10.74648 ? 150 ASP A CA     1 
ATOM   1193 C  C      . ASP A 1 157 ? -8.39400  2.96600   -16.94500 1.000 10.55208 ? 150 ASP A C      1 
ATOM   1194 O  O      . ASP A 1 157 ? -9.20300  2.24800   -17.53200 1.000 11.17274 ? 150 ASP A O      1 
ATOM   1195 C  CB     . ASP A 1 157 ? -9.96600  2.95000   -14.95700 1.000 11.82880 ? 150 ASP A CB     1 
ATOM   1196 C  CG     . ASP A 1 157 ? -10.08500 1.44600   -14.75000 1.000 17.14639 ? 150 ASP A CG     1 
ATOM   1197 O  OD1    . ASP A 1 157 ? -9.02400  0.77800   -14.63800 1.000 13.70496 ? 150 ASP A OD1    1 
ATOM   1198 O  OD2    . ASP A 1 157 ? -11.23100 0.95100   -14.72600 1.000 13.72397 ? 150 ASP A OD2    1 
ATOM   1199 N  N      . LEU A 1 158 ? -7.29600  3.41700   -17.54700 1.000 10.08520 ? 151 LEU A N      1 
ATOM   1200 C  CA     . LEU A 1 158 ? -6.90300  2.92000   -18.86100 1.000 10.37424 ? 151 LEU A CA     1 
ATOM   1201 C  C      . LEU A 1 158 ? -6.43500  1.47600   -18.72600 1.000 13.27215 ? 151 LEU A C      1 
ATOM   1202 O  O      . LEU A 1 158 ? -5.59700  1.15900   -17.87400 1.000 11.19961 ? 151 LEU A O      1 
ATOM   1203 C  CB     . LEU A 1 158 ? -5.78500  3.78100   -19.46700 1.000 7.92872  ? 151 LEU A CB     1 
ATOM   1204 C  CG     . LEU A 1 158 ? -6.14300  5.22300   -19.79300 1.000 10.42493 ? 151 LEU A CG     1 
ATOM   1205 C  CD1    . LEU A 1 158 ? -4.88200  6.02800   -20.19300 1.000 9.72718  ? 151 LEU A CD1    1 
ATOM   1206 C  CD2    . LEU A 1 158 ? -7.20600  5.26700   -20.90300 1.000 10.64290 ? 151 LEU A CD2    1 
ATOM   1207 N  N      . LYS A 1 159 ? -6.99900  0.60500   -19.55400 1.000 11.35476 ? 152 LYS A N      1 
ATOM   1208 C  CA     . LYS A 1 159 ? -6.67800  -0.81600  -19.58300 1.000 10.41884 ? 152 LYS A CA     1 
ATOM   1209 C  C      . LYS A 1 159 ? -7.26800  -1.40100  -20.86800 1.000 9.53497  ? 152 LYS A C      1 
ATOM   1210 O  O      . LYS A 1 159 ? -8.17700  -0.80700  -21.45700 1.000 9.61788  ? 152 LYS A O      1 
ATOM   1211 C  CB     . LYS A 1 159 ? -7.24500  -1.54900  -18.35600 1.000 10.39355 ? 152 LYS A CB     1 
ATOM   1212 C  CG     . LYS A 1 159 ? -8.76300  -1.42700  -18.23300 1.000 13.35392 ? 152 LYS A CG     1 
ATOM   1213 C  CD     . LYS A 1 159 ? -9.24600  -2.06100  -16.91800 1.000 13.84506 ? 152 LYS A CD     1 
ATOM   1214 C  CE     . LYS A 1 159 ? -10.74000 -1.86700  -16.73700 1.000 18.98638 ? 152 LYS A CE     1 
ATOM   1215 N  NZ     . LYS A 1 159 ? -11.16300 -2.25000  -15.36400 1.000 20.34773 ? 152 LYS A NZ     1 
ATOM   1216 N  N      . PRO A 1 160 ? -6.76500  -2.54900  -21.31700 1.000 9.63188  ? 153 PRO A N      1 
ATOM   1217 C  CA     . PRO A 1 160 ? -7.21200  -3.06100  -22.63000 1.000 11.23419 ? 153 PRO A CA     1 
ATOM   1218 C  C      . PRO A 1 160 ? -8.72800  -3.20400  -22.75300 1.000 12.08128 ? 153 PRO A C      1 
ATOM   1219 O  O      . PRO A 1 160 ? -9.28000  -2.92700  -23.82400 1.000 12.72168 ? 153 PRO A O      1 
ATOM   1220 C  CB     . PRO A 1 160 ? -6.48700  -4.40600  -22.73700 1.000 10.94945 ? 153 PRO A CB     1 
ATOM   1221 C  CG     . PRO A 1 160 ? -5.23500  -4.20400  -21.90500 1.000 12.46130 ? 153 PRO A CG     1 
ATOM   1222 C  CD     . PRO A 1 160 ? -5.68500  -3.36900  -20.73300 1.000 11.25064 ? 153 PRO A CD     1 
ATOM   1223 N  N      . SER A 1 161 ? -9.43200  -3.60800  -21.69000 1.000 9.25884  ? 154 SER A N      1 
ATOM   1224 C  CA     . SER A 1 161 ? -10.88200 -3.77300  -21.82200 1.000 11.92184 ? 154 SER A CA     1 
ATOM   1225 C  C      . SER A 1 161 ? -11.60200 -2.44100  -21.96800 1.000 16.18882 ? 154 SER A C      1 
ATOM   1226 O  O      . SER A 1 161 ? -12.77400 -2.41900  -22.38600 1.000 11.88316 ? 154 SER A O      1 
ATOM   1227 C  CB     . SER A 1 161 ? -11.44800 -4.54000  -20.62900 1.000 15.45522 ? 154 SER A CB     1 
ATOM   1228 O  OG     . SER A 1 161 ? -11.18000 -3.86500  -19.41200 1.000 16.93950 ? 154 SER A OG     1 
ATOM   1229 N  N      . ASN A 1 162 ? -10.93400 -1.33400  -21.62600 1.000 10.19932 ? 155 ASN A N      1 
ATOM   1230 C  CA     . ASN A 1 162 ? -11.48500 0.00600   -21.78200 1.000 10.47041 ? 155 ASN A CA     1 
ATOM   1231 C  C      . ASN A 1 162 ? -10.94600 0.70500   -23.02000 1.000 11.81410 ? 155 ASN A C      1 
ATOM   1232 O  O      . ASN A 1 162 ? -10.95000 1.93800   -23.06900 1.000 10.60789 ? 155 ASN A O      1 
ATOM   1233 C  CB     . ASN A 1 162 ? -11.18200 0.85800   -20.53900 1.000 9.56311  ? 155 ASN A CB     1 
ATOM   1234 C  CG     . ASN A 1 162 ? -12.18400 0.65600   -19.40400 1.000 14.20220 ? 155 ASN A CG     1 
ATOM   1235 O  OD1    . ASN A 1 162 ? -13.32200 0.20500   -19.60900 1.000 14.42897 ? 155 ASN A OD1    1 
ATOM   1236 N  ND2    . ASN A 1 162 ? -11.76100 1.01300   -18.18500 1.000 11.57918 ? 155 ASN A ND2    1 
ATOM   1237 N  N      . LEU A 1 163 ? -10.46700 -0.05200  -24.01100 1.000 11.15169 ? 156 LEU A N      1 
ATOM   1238 C  CA     . LEU A 1 163 ? -9.97700  0.49300   -25.27100 1.000 11.58523 ? 156 LEU A CA     1 
ATOM   1239 C  C      . LEU A 1 163 ? -10.50900 -0.37400  -26.39500 1.000 13.30789 ? 156 LEU A C      1 
ATOM   1240 O  O      . LEU A 1 163 ? -10.39200 -1.60200  -26.33600 1.000 11.36696 ? 156 LEU A O      1 
ATOM   1241 C  CB     . LEU A 1 163 ? -8.43200  0.53800   -25.31600 1.000 11.24432 ? 156 LEU A CB     1 
ATOM   1242 C  CG     . LEU A 1 163 ? -7.76500  1.38700   -24.22600 1.000 11.48893 ? 156 LEU A CG     1 
ATOM   1243 C  CD1    . LEU A 1 163 ? -6.30300  0.98300   -23.99600 1.000 10.22958 ? 156 LEU A CD1    1 
ATOM   1244 C  CD2    . LEU A 1 163 ? -7.87100  2.87000   -24.60400 1.000 9.34479  ? 156 LEU A CD2    1 
ATOM   1245 N  N      . ALA A 1 164 ? -11.09000 0.24700   -27.41900 1.000 10.25642 ? 157 ALA A N      1 
ATOM   1246 C  CA     . ALA A 1 164 ? -11.68600 -0.56400  -28.47300 1.000 12.86172 ? 157 ALA A CA     1 
ATOM   1247 C  C      . ALA A 1 164 ? -11.45200 0.08000   -29.82600 1.000 14.31784 ? 157 ALA A C      1 
ATOM   1248 O  O      . ALA A 1 164 ? -11.25300 1.28800   -29.93200 1.000 10.14154 ? 157 ALA A O      1 
ATOM   1249 C  CB     . ALA A 1 164 ? -13.19200 -0.79700  -28.21400 1.000 9.51734  ? 157 ALA A CB     1 
ATOM   1250 N  N      . VAL A 1 165 ? -11.45500 -0.76000  -30.86500 1.000 13.33436 ? 158 VAL A N      1 
ATOM   1251 C  CA     . VAL A 1 165 ? -11.09800 -0.35400  -32.21600 1.000 15.90656 ? 158 VAL A CA     1 
ATOM   1252 C  C      . VAL A 1 165 ? -12.16700 -0.83100  -33.19300 1.000 18.14395 ? 158 VAL A C      1 
ATOM   1253 O  O      . VAL A 1 165 ? -12.97300 -1.71600  -32.89100 1.000 13.23973 ? 158 VAL A O      1 
ATOM   1254 C  CB     . VAL A 1 165 ? -9.71300  -0.89800  -32.63900 1.000 15.96340 ? 158 VAL A CB     1 
ATOM   1255 C  CG1    . VAL A 1 165 ? -8.61200  -0.41900  -31.68000 1.000 15.43519 ? 158 VAL A CG1    1 
ATOM   1256 C  CG2    . VAL A 1 165 ? -9.74000  -2.41200  -32.64700 1.000 19.83105 ? 158 VAL A CG2    1 
ATOM   1257 N  N      . ASN A 1 166 ? -12.16600 -0.21400  -34.38400 1.000 17.21177 ? 159 ASN A N      1 
ATOM   1258 C  CA     . ASN A 1 166 ? -12.99200 -0.65800  -35.49200 1.000 20.33882 ? 159 ASN A CA     1 
ATOM   1259 C  C      . ASN A 1 166 ? -12.12200 -1.41000  -36.50800 1.000 22.70389 ? 159 ASN A C      1 
ATOM   1260 O  O      . ASN A 1 166 ? -10.95800 -1.74000  -36.24800 1.000 20.18630 ? 159 ASN A O      1 
ATOM   1261 C  CB     . ASN A 1 166 ? -13.74500 0.53200   -36.10900 1.000 20.44104 ? 159 ASN A CB     1 
ATOM   1262 C  CG     . ASN A 1 166 ? -12.82900 1.52300   -36.82400 1.000 24.88148 ? 159 ASN A CG     1 
ATOM   1263 O  OD1    . ASN A 1 166 ? -11.67000 1.22300   -37.13900 1.000 19.96016 ? 159 ASN A OD1    1 
ATOM   1264 N  ND2    . ASN A 1 166 ? -13.35800 2.71500   -37.09400 1.000 23.98374 ? 159 ASN A ND2    1 
ATOM   1265 N  N      . GLU A 1 167 ? -12.68000 -1.68300  -37.69400 1.000 24.25462 ? 160 GLU A N      1 
ATOM   1266 C  CA     . GLU A 1 167 ? -11.93800 -2.49500  -38.65600 1.000 27.01971 ? 160 GLU A CA     1 
ATOM   1267 C  C      . GLU A 1 167 ? -10.73300 -1.76300  -39.23400 1.000 28.89734 ? 160 GLU A C      1 
ATOM   1268 O  O      . GLU A 1 167 ? -9.84700  -2.40500  -39.81600 1.000 27.28512 ? 160 GLU A O      1 
ATOM   1269 C  CB     . GLU A 1 167 ? -12.85700 -2.94900  -39.79500 1.000 33.19795 ? 160 GLU A CB     1 
ATOM   1270 C  CG     . GLU A 1 167 ? -13.30900 -1.83200  -40.68900 1.000 30.52403 ? 160 GLU A CG     1 
ATOM   1271 C  CD     . GLU A 1 167 ? -14.18200 -2.32500  -41.81900 1.000 44.05563 ? 160 GLU A CD     1 
ATOM   1272 O  OE1    . GLU A 1 167 ? -14.85100 -3.36500  -41.63800 1.000 42.42602 ? 160 GLU A OE1    1 
ATOM   1273 O  OE2    . GLU A 1 167 ? -14.18400 -1.67600  -42.89000 1.000 44.76853 ? 160 GLU A OE2    1 
ATOM   1274 N  N      . ASP A 1 168 ? -10.68700 -0.43800  -39.10800 1.000 22.30578 ? 161 ASP A N      1 
ATOM   1275 C  CA     . ASP A 1 168 ? -9.55700  0.34900   -39.58000 1.000 22.38010 ? 161 ASP A CA     1 
ATOM   1276 C  C      . ASP A 1 168 ? -8.53900  0.62300   -38.47800 1.000 23.10841 ? 161 ASP A C      1 
ATOM   1277 O  O      . ASP A 1 168 ? -7.65400  1.46200   -38.65700 1.000 24.12033 ? 161 ASP A O      1 
ATOM   1278 C  CB     . ASP A 1 168 ? -10.05600 1.66300   -40.18600 1.000 24.91864 ? 161 ASP A CB     1 
ATOM   1279 C  CG     . ASP A 1 168 ? -10.92400 1.44500   -41.42500 1.000 29.16797 ? 161 ASP A CG     1 
ATOM   1280 O  OD1    . ASP A 1 168 ? -10.84000 0.36000   -42.05500 1.000 27.31545 ? 161 ASP A OD1    1 
ATOM   1281 O  OD2    . ASP A 1 168 ? -11.68100 2.36800   -41.77800 1.000 30.59565 ? 161 ASP A OD2    1 
ATOM   1282 N  N      . CYS A 1 169 ? -8.64100  -0.08000  -37.35000 1.000 21.33343 ? 162 CYS A N      1 
ATOM   1283 C  CA     . CYS A 1 169 ? -7.81300  0.14600   -36.16900 1.000 18.60433 ? 162 CYS A CA     1 
ATOM   1284 C  C      . CYS A 1 169 ? -7.97100  1.55900   -35.61200 1.000 18.85796 ? 162 CYS A C      1 
ATOM   1285 O  O      . CYS A 1 169 ? -7.05700  2.07400   -34.96100 1.000 15.31714 ? 162 CYS A O      1 
ATOM   1286 C  CB     . CYS A 1 169 ? -6.33000  -0.14400  -36.44900 1.000 23.61717 ? 162 CYS A CB     1 
ATOM   1287 S  SG     . CYS A 1 169 ? -5.97000  -1.76500  -37.26500 1.000 39.21080 ? 162 CYS A SG     1 
ATOM   1288 N  N      . GLU A 1 170 ? -9.09900  2.22000   -35.86800 1.000 13.16558 ? 163 GLU A N      1 
ATOM   1289 C  CA     . GLU A 1 170 ? -9.38200  3.49400   -35.21500 1.000 17.01844 ? 163 GLU A CA     1 
ATOM   1290 C  C      . GLU A 1 170 ? -9.87200  3.22400   -33.80100 1.000 14.91516 ? 163 GLU A C      1 
ATOM   1291 O  O      . GLU A 1 170 ? -10.74600 2.37800   -33.59500 1.000 15.75956 ? 163 GLU A O      1 
ATOM   1292 C  CB     . GLU A 1 170 ? -10.41900 4.28800   -35.99900 1.000 17.71416 ? 163 GLU A CB     1 
ATOM   1293 C  CG     . GLU A 1 170 ? -9.84800  4.82300   -37.30200 1.000 20.69690 ? 163 GLU A CG     1 
ATOM   1294 C  CD     . GLU A 1 170 ? -10.91100 5.29500   -38.27800 1.000 26.38695 ? 163 GLU A CD     1 
ATOM   1295 O  OE1    . GLU A 1 170 ? -12.11700 5.07200   -38.03600 1.000 27.50309 ? 163 GLU A OE1    1 
ATOM   1296 O  OE2    . GLU A 1 170 ? -10.52300 5.88500   -39.30100 1.000 28.49621 ? 163 GLU A OE2    1 
ATOM   1297 N  N      . LEU A 1 171 ? -9.32500  3.94600   -32.83300 1.000 11.10842 ? 164 LEU A N      1 
ATOM   1298 C  CA     . LEU A 1 171 ? -9.43000  3.56700   -31.43200 1.000 13.20086 ? 164 LEU A CA     1 
ATOM   1299 C  C      . LEU A 1 171 ? -10.24200 4.57900   -30.63200 1.000 9.86919  ? 164 LEU A C      1 
ATOM   1300 O  O      . LEU A 1 171 ? -10.17200 5.78400   -30.87800 1.000 10.78882 ? 164 LEU A O      1 
ATOM   1301 C  CB     . LEU A 1 171 ? -8.03000  3.44100   -30.83400 1.000 12.50948 ? 164 LEU A CB     1 
ATOM   1302 C  CG     . LEU A 1 171 ? -7.92900  3.14200   -29.35100 1.000 11.47241 ? 164 LEU A CG     1 
ATOM   1303 C  CD1    . LEU A 1 171 ? -6.71900  2.23400   -29.10800 1.000 10.87017 ? 164 LEU A CD1    1 
ATOM   1304 C  CD2    . LEU A 1 171 ? -7.85800  4.45600   -28.52800 1.000 9.29880  ? 164 LEU A CD2    1 
ATOM   1305 N  N      . LYS A 1 172 ? -10.98900 4.08500   -29.64300 1.000 11.33728 ? 165 LYS A N      1 
ATOM   1306 C  CA     . LYS A 1 172 ? -11.68700 4.95200   -28.70300 1.000 12.13051 ? 165 LYS A CA     1 
ATOM   1307 C  C      . LYS A 1 172 ? -11.35800 4.53100   -27.27900 1.000 10.30552 ? 165 LYS A C      1 
ATOM   1308 O  O      . LYS A 1 172 ? -11.30700 3.33300   -26.97100 1.000 11.74755 ? 165 LYS A O      1 
ATOM   1309 C  CB     . LYS A 1 172 ? -13.21800 4.92400   -28.93300 1.000 11.74864 ? 165 LYS A CB     1 
ATOM   1310 C  CG     . LYS A 1 172 ? -13.62600 5.66200   -30.22600 1.000 15.83792 ? 165 LYS A CG     1 
ATOM   1311 C  CD     . LYS A 1 172 ? -14.96200 6.38100   -30.09700 1.000 25.07980 ? 165 LYS A CD     1 
ATOM   1312 C  CE     . LYS A 1 172 ? -15.16100 7.43800   -31.21400 1.000 28.84917 ? 165 LYS A CE     1 
ATOM   1313 N  NZ     . LYS A 1 172 ? -15.51300 8.83000   -30.66400 1.000 22.92980 ? 165 LYS A NZ     1 
ATOM   1314 N  N      . ILE A 1 173 ? -11.11500 5.53000   -26.41800 1.000 10.08303 ? 166 ILE A N      1 
ATOM   1315 C  CA     . ILE A 1 173 ? -10.97200 5.32200   -24.97900 1.000 7.08199  ? 166 ILE A CA     1 
ATOM   1316 C  C      . ILE A 1 173 ? -12.36900 5.22700   -24.37500 1.000 10.95664 ? 166 ILE A C      1 
ATOM   1317 O  O      . ILE A 1 173 ? -13.20800 6.09800   -24.61800 1.000 10.84509 ? 166 ILE A O      1 
ATOM   1318 C  CB     . ILE A 1 173 ? -10.17900 6.48500   -24.34900 1.000 8.24135  ? 166 ILE A CB     1 
ATOM   1319 C  CG1    . ILE A 1 173 ? -8.74200  6.54900   -24.91200 1.000 9.79531  ? 166 ILE A CG1    1 
ATOM   1320 C  CG2    . ILE A 1 173 ? -10.22100 6.42800   -22.81600 1.000 8.16876  ? 166 ILE A CG2    1 
ATOM   1321 C  CD1    . ILE A 1 173 ? -8.03500  7.85400   -24.54700 1.000 10.88817 ? 166 ILE A CD1    1 
ATOM   1322 N  N      . LEU A 1 174 ? -12.62800 4.17900   -23.58400 1.000 8.99926  ? 167 LEU A N      1 
ATOM   1323 C  CA     . LEU A 1 174 ? -13.97600 3.99100   -23.04900 1.000 11.77648 ? 167 LEU A CA     1 
ATOM   1324 C  C      . LEU A 1 174 ? -14.07300 4.34900   -21.56400 1.000 12.40527 ? 167 LEU A C      1 
ATOM   1325 O  O      . LEU A 1 174 ? -13.52800 5.37300   -21.13600 1.000 13.83986 ? 167 LEU A O      1 
ATOM   1326 C  CB     . LEU A 1 174 ? -14.45100 2.55400   -23.27900 1.000 11.26833 ? 167 LEU A CB     1 
ATOM   1327 C  CG     . LEU A 1 174 ? -14.25500 2.01500   -24.69900 1.000 9.72718  ? 167 LEU A CG     1 
ATOM   1328 C  CD1    . LEU A 1 174 ? -14.70400 0.55500   -24.77100 1.000 10.94056 ? 167 LEU A CD1    1 
ATOM   1329 C  CD2    . LEU A 1 174 ? -15.00800 2.87000   -25.71200 1.000 11.27411 ? 167 LEU A CD2    1 
ATOM   1330 N  N      . ASP A 1 175 ? -14.76400 3.50700   -20.78300 1.000 10.61582 ? 168 ASP A N      1 
ATOM   1331 C  CA     . ASP A 1 175 ? -15.25500 3.87800   -19.45100 1.000 12.87664 ? 168 ASP A CA     1 
ATOM   1332 C  C      . ASP A 1 175 ? -14.17100 4.53600   -18.60500 1.000 14.02193 ? 168 ASP A C      1 
ATOM   1333 O  O      . ASP A 1 175 ? -13.07700 3.99500   -18.46400 1.000 12.38616 ? 168 ASP A O      1 
ATOM   1334 C  CB     . ASP A 1 175 ? -15.76800 2.63400   -18.70900 1.000 13.54243 ? 168 ASP A CB     1 
ATOM   1335 C  CG     . ASP A 1 175 ? -16.83700 1.87500   -19.48100 1.000 14.87997 ? 168 ASP A CG     1 
ATOM   1336 O  OD1    . ASP A 1 175 ? -16.62400 1.53500   -20.66500 1.000 15.43260 ? 168 ASP A OD1    1 
ATOM   1337 O  OD2    . ASP A 1 175 ? -17.89300 1.59800   -18.88600 1.000 16.90942 ? 168 ASP A OD2    1 
ATOM   1338 N  N      . PHE A 1 176 ? -14.52200 5.65800   -17.97600 1.000 12.00638 ? 169 PHE A N      1 
ATOM   1339 C  CA     . PHE A 1 176 ? -13.62000 6.40500   -17.10600 1.000 11.80729 ? 169 PHE A CA     1 
ATOM   1340 C  C      . PHE A 1 176 ? -13.59400 5.81700   -15.70100 1.000 12.74655 ? 169 PHE A C      1 
ATOM   1341 O  O      . PHE A 1 176 ? -14.56700 5.21400   -15.24700 1.000 13.36531 ? 169 PHE A O      1 
ATOM   1342 C  CB     . PHE A 1 176 ? -14.05200 7.87500   -17.01700 1.000 12.00036 ? 169 PHE A CB     1 
ATOM   1343 C  CG     . PHE A 1 176 ? -13.66100 8.69900   -18.22100 1.000 12.50098 ? 169 PHE A CG     1 
ATOM   1344 C  CD1    . PHE A 1 176 ? -14.14800 8.38100   -19.48800 1.000 15.90002 ? 169 PHE A CD1    1 
ATOM   1345 C  CD2    . PHE A 1 176 ? -12.81900 9.79000   -18.08700 1.000 13.94638 ? 169 PHE A CD2    1 
ATOM   1346 C  CE1    . PHE A 1 176 ? -13.78700 9.12400   -20.60900 1.000 14.97063 ? 169 PHE A CE1    1 
ATOM   1347 C  CE2    . PHE A 1 176 ? -12.44600 10.54200  -19.20800 1.000 12.59594 ? 169 PHE A CE2    1 
ATOM   1348 C  CZ     . PHE A 1 176 ? -12.92900 10.20800  -20.46300 1.000 13.46808 ? 169 PHE A CZ     1 
ATOM   1349 N  N      . GLY A 1 177 ? -12.46800 6.00100   -15.01300 1.000 12.82578 ? 170 GLY A N      1 
ATOM   1350 C  CA     . GLY A 1 177 ? -12.37600 5.61200   -13.61500 1.000 12.75644 ? 170 GLY A CA     1 
ATOM   1351 C  C      . GLY A 1 177 ? -13.17900 6.58100   -12.75800 1.000 14.55421 ? 170 GLY A C      1 
ATOM   1352 O  O      . GLY A 1 177 ? -12.95800 7.80200   -12.81700 1.000 15.38190 ? 170 GLY A O      1 
ATOM   1353 N  N      . LEU A 1 178 ? -14.13200 6.06800   -11.98900 1.000 13.50388 ? 171 LEU A N      1 
ATOM   1354 C  CA     . LEU A 1 178 ? -15.03000 6.93400   -11.24100 1.000 17.89421 ? 171 LEU A CA     1 
ATOM   1355 C  C      . LEU A 1 178 ? -14.72000 7.00700   -9.75200  1.000 22.11778 ? 171 LEU A C      1 
ATOM   1356 O  O      . LEU A 1 178 ? -15.40900 7.73300   -9.02800  1.000 21.84698 ? 171 LEU A O      1 
ATOM   1357 C  CB     . LEU A 1 178 ? -16.47700 6.48200   -11.44600 1.000 17.04351 ? 171 LEU A CB     1 
ATOM   1358 C  CG     . LEU A 1 178 ? -16.86800 6.40000   -12.92400 1.000 17.52064 ? 171 LEU A CG     1 
ATOM   1359 C  CD1    . LEU A 1 178 ? -18.25900 5.81600   -13.08200 1.000 14.18796 ? 171 LEU A CD1    1 
ATOM   1360 C  CD2    . LEU A 1 178 ? -16.78500 7.79200   -13.52600 1.000 11.77034 ? 171 LEU A CD2    1 
ATOM   1361 N  N      . ALA A 1 179 ? -13.71600 6.28700   -9.26900  1.000 18.90766 ? 172 ALA A N      1 
ATOM   1362 C  CA     . ALA A 1 179 ? -13.36300 6.38300   -7.86000  1.000 26.39958 ? 172 ALA A CA     1 
ATOM   1363 C  C      . ALA A 1 179 ? -12.55400 7.65000   -7.61100  1.000 27.95444 ? 172 ALA A C      1 
ATOM   1364 O  O      . ALA A 1 179 ? -11.72800 8.04900   -8.44000  1.000 25.63229 ? 172 ALA A O      1 
ATOM   1365 C  CB     . ALA A 1 179 ? -12.57700 5.15300   -7.40400  1.000 26.86136 ? 172 ALA A CB     1 
ATOM   1366 N  N      . ARG A 1 180 ? -12.81800 8.29100   -6.47300  1.000 31.32781 ? 173 ARG A N      1 
ATOM   1367 C  CA     . ARG A 1 180 ? -12.11500 9.48600   -6.02100  1.000 37.47121 ? 173 ARG A CA     1 
ATOM   1368 C  C      . ARG A 1 180 ? -11.78700 9.33800   -4.53700  1.000 46.77319 ? 173 ARG A C      1 
ATOM   1369 O  O      . ARG A 1 180 ? -12.26900 8.42600   -3.85800  1.000 47.82871 ? 173 ARG A O      1 
ATOM   1370 C  CB     . ARG A 1 180 ? -12.94100 10.76000  -6.26000  1.000 29.74297 ? 173 ARG A CB     1 
ATOM   1371 C  CG     . ARG A 1 180 ? -13.40900 10.96900  -7.69800  1.000 23.55617 ? 173 ARG A CG     1 
ATOM   1372 C  CD     . ARG A 1 180 ? -12.33100 11.62500  -8.55400  1.000 26.62496 ? 173 ARG A CD     1 
ATOM   1373 N  NE     . ARG A 1 180 ? -12.81400 11.97600  -9.88800  1.000 27.57597 ? 173 ARG A NE     1 
ATOM   1374 C  CZ     . ARG A 1 180 ? -12.93900 11.10200  -10.88100 1.000 25.28476 ? 173 ARG A CZ     1 
ATOM   1375 N  NH1    . ARG A 1 180 ? -12.67000 9.81400   -10.70600 1.000 23.41154 ? 173 ARG A NH1    1 
ATOM   1376 N  NH2    . ARG A 1 180 ? -13.34200 11.53000  -12.07300 1.000 22.07058 ? 173 ARG A NH2    1 
ATOM   1377 N  N      . HIS A 1 181 ? -10.96100 10.25100  -4.02900  1.000 47.50940 ? 174 HIS A N      1 
ATOM   1378 C  CA     . HIS A 1 181 ? -10.51300 10.20700  -2.63500  1.000 55.29093 ? 174 HIS A CA     1 
ATOM   1379 C  C      . HIS A 1 181 ? -9.75500  8.91800   -2.34200  1.000 57.95391 ? 174 HIS A C      1 
ATOM   1380 O  O      . HIS A 1 181 ? -10.13400 8.15700   -1.45200  1.000 59.63162 ? 174 HIS A O      1 
ATOM   1381 C  CB     . HIS A 1 181 ? -11.69600 10.33500  -1.67200  1.000 55.31952 ? 174 HIS A CB     1 
ATOM   1382 C  CG     . HIS A 1 181 ? -12.76700 11.26100  -2.15500  1.000 58.82029 ? 174 HIS A CG     1 
ATOM   1383 N  ND1    . HIS A 1 181 ? -12.60100 12.62900  -2.20500  1.000 60.99488 ? 174 HIS A ND1    1 
ATOM   1384 C  CD2    . HIS A 1 181 ? -14.01400 11.01500  -2.62300  1.000 56.68668 ? 174 HIS A CD2    1 
ATOM   1385 C  CE1    . HIS A 1 181 ? -13.70200 13.18600  -2.67800  1.000 63.15147 ? 174 HIS A CE1    1 
ATOM   1386 N  NE2    . HIS A 1 181 ? -14.57500 12.22800  -2.94000  1.000 61.46897 ? 174 HIS A NE2    1 
ATOM   1387 N  N      . VAL A 1 190 ? -12.50300 -8.25000  -10.47900 1.000 54.74776 ? 183 VAL A N      1 
ATOM   1388 C  CA     . VAL A 1 190 ? -13.55400 -7.25800  -10.66600 1.000 47.13310 ? 183 VAL A CA     1 
ATOM   1389 C  C      . VAL A 1 190 ? -12.98200 -5.99000  -11.30300 1.000 50.30406 ? 183 VAL A C      1 
ATOM   1390 O  O      . VAL A 1 190 ? -13.57500 -5.43600  -12.23100 1.000 53.04937 ? 183 VAL A O      1 
ATOM   1391 C  CB     . VAL A 1 190 ? -14.26600 -6.92800  -9.33000  1.000 50.73974 ? 183 VAL A CB     1 
ATOM   1392 C  CG1    . VAL A 1 190 ? -15.09100 -8.12000  -8.85600  1.000 48.18765 ? 183 VAL A CG1    1 
ATOM   1393 C  CG2    . VAL A 1 190 ? -13.26300 -6.49100  -8.26700  1.000 47.86843 ? 183 VAL A CG2    1 
ATOM   1394 N  N      . ALA A 1 191 ? -11.82800 -5.53500  -10.80800 1.000 40.87031 ? 184 ALA A N      1 
ATOM   1395 C  CA     . ALA A 1 191 ? -11.18300 -4.31800  -11.31400 1.000 39.31297 ? 184 ALA A CA     1 
ATOM   1396 C  C      . ALA A 1 191 ? -9.67600  -4.55700  -11.33400 1.000 28.43526 ? 184 ALA A C      1 
ATOM   1397 O  O      . ALA A 1 191 ? -9.01100  -4.45100  -10.29900 1.000 26.48140 ? 184 ALA A O      1 
ATOM   1398 C  CB     . ALA A 1 191 ? -11.53700 -3.10400  -10.46300 1.000 37.60809 ? 184 ALA A CB     1 
ATOM   1399 N  N      . THR A 1 192 ? -9.14200  -4.86100  -12.51200 1.000 25.11208 ? 185 THR A N      1 
ATOM   1400 C  CA     . THR A 1 192 ? -7.75400  -5.29100  -12.60100 1.000 21.46569 ? 185 THR A CA     1 
ATOM   1401 C  C      . THR A 1 192 ? -6.81400  -4.19900  -12.10100 1.000 20.31299 ? 185 THR A C      1 
ATOM   1402 O  O      . THR A 1 192 ? -7.05700  -3.00300  -12.29600 1.000 17.88477 ? 185 THR A O      1 
ATOM   1403 C  CB     . THR A 1 192 ? -7.39600  -5.67300  -14.03400 1.000 20.54788 ? 185 THR A CB     1 
ATOM   1404 O  OG1    . THR A 1 192 ? -6.07000  -6.20800  -14.05400 1.000 20.34107 ? 185 THR A OG1    1 
ATOM   1405 C  CG2    . THR A 1 192 ? -7.44400  -4.45100  -14.94700 1.000 20.63109 ? 185 THR A CG2    1 
ATOM   1406 N  N      . ARG A 1 193 ? -5.75500  -4.63100  -11.42100 1.000 16.46786 ? 186 ARG A N      1 
ATOM   1407 C  CA     . ARG A 1 193 ? -4.65500  -3.78900  -10.97000 1.000 19.20429 ? 186 ARG A CA     1 
ATOM   1408 C  C      . ARG A 1 193 ? -3.51100  -3.73000  -11.96900 1.000 15.59971 ? 186 ARG A C      1 
ATOM   1409 O  O      . ARG A 1 193 ? -2.53300  -3.00700  -11.73300 1.000 13.00109 ? 186 ARG A O      1 
ATOM   1410 C  CB     . ARG A 1 193 ? -4.06200  -4.33200  -9.67000  1.000 20.86463 ? 186 ARG A CB     1 
ATOM   1411 C  CG     . ARG A 1 193 ? -4.86900  -4.18500  -8.44400  1.000 29.08742 ? 186 ARG A CG     1 
ATOM   1412 C  CD     . ARG A 1 193 ? -4.07000  -4.80500  -7.29500  1.000 22.53974 ? 186 ARG A CD     1 
ATOM   1413 N  NE     . ARG A 1 193 ? -4.92800  -5.05000  -6.15000  1.000 21.96332 ? 186 ARG A NE     1 
ATOM   1414 C  CZ     . ARG A 1 193 ? -5.52600  -6.20500  -5.90600  1.000 25.80860 ? 186 ARG A CZ     1 
ATOM   1415 N  NH1    . ARG A 1 193 ? -5.34500  -7.26000  -6.69200  1.000 19.69739 ? 186 ARG A NH1    1 
ATOM   1416 N  NH2    . ARG A 1 193 ? -6.32000  -6.30800  -4.84600  1.000 30.21886 ? 186 ARG A NH2    1 
ATOM   1417 N  N      . TRP A 1 194 ? -3.58500  -4.49900  -13.05200 1.000 12.48793 ? 187 TRP A N      1 
ATOM   1418 C  CA     . TRP A 1 194 ? -2.39400  -4.72500  -13.86500 1.000 12.70883 ? 187 TRP A CA     1 
ATOM   1419 C  C      . TRP A 1 194 ? -1.86400  -3.44900  -14.51100 1.000 13.09788 ? 187 TRP A C      1 
ATOM   1420 O  O      . TRP A 1 194 ? -0.66200  -3.37100  -14.81300 1.000 12.74271 ? 187 TRP A O      1 
ATOM   1421 C  CB     . TRP A 1 194 ? -2.68500  -5.78900  -14.92400 1.000 14.17305 ? 187 TRP A CB     1 
ATOM   1422 C  CG     . TRP A 1 194 ? -2.87400  -7.16300  -14.32600 1.000 14.60565 ? 187 TRP A CG     1 
ATOM   1423 C  CD1    . TRP A 1 194 ? -2.65500  -7.54100  -13.02600 1.000 16.31230 ? 187 TRP A CD1    1 
ATOM   1424 C  CD2    . TRP A 1 194 ? -3.32200  -8.33300  -15.01300 1.000 17.65172 ? 187 TRP A CD2    1 
ATOM   1425 N  NE1    . TRP A 1 194 ? -2.93800  -8.88700  -12.86600 1.000 14.72996 ? 187 TRP A NE1    1 
ATOM   1426 C  CE2    . TRP A 1 194 ? -3.35100  -9.39100  -14.07200 1.000 17.13366 ? 187 TRP A CE2    1 
ATOM   1427 C  CE3    . TRP A 1 194 ? -3.68800  -8.59400  -16.34100 1.000 17.24212 ? 187 TRP A CE3    1 
ATOM   1428 C  CZ2    . TRP A 1 194 ? -3.73200  -10.68800 -14.41900 1.000 17.26116 ? 187 TRP A CZ2    1 
ATOM   1429 C  CZ3    . TRP A 1 194 ? -4.07500  -9.88800  -16.68200 1.000 21.96094 ? 187 TRP A CZ3    1 
ATOM   1430 C  CH2    . TRP A 1 194 ? -4.09200  -10.91800 -15.72200 1.000 23.23446 ? 187 TRP A CH2    1 
ATOM   1431 N  N      . TYR A 1 195 ? -2.72500  -2.45400  -14.74700 1.000 11.89910 ? 188 TYR A N      1 
ATOM   1432 C  CA     . TYR A 1 195 ? -2.36200  -1.23600  -15.47500 1.000 13.09623 ? 188 TYR A CA     1 
ATOM   1433 C  C      . TYR A 1 195 ? -2.31300  -0.01000  -14.56900 1.000 12.73299 ? 188 TYR A C      1 
ATOM   1434 O  O      . TYR A 1 195 ? -2.11400  1.11100   -15.05700 1.000 10.73430 ? 188 TYR A O      1 
ATOM   1435 C  CB     . TYR A 1 195 ? -3.34100  -1.03800  -16.64500 1.000 10.92940 ? 188 TYR A CB     1 
ATOM   1436 C  CG     . TYR A 1 195 ? -3.41800  -2.31100  -17.45400 1.000 9.62707  ? 188 TYR A CG     1 
ATOM   1437 C  CD1    . TYR A 1 195 ? -4.32400  -3.31800  -17.12900 1.000 13.92085 ? 188 TYR A CD1    1 
ATOM   1438 C  CD2    . TYR A 1 195 ? -2.50700  -2.55000  -18.48000 1.000 10.82090 ? 188 TYR A CD2    1 
ATOM   1439 C  CE1    . TYR A 1 195 ? -4.34800  -4.53900  -17.83700 1.000 11.28359 ? 188 TYR A CE1    1 
ATOM   1440 C  CE2    . TYR A 1 195 ? -2.52700  -3.75700  -19.19300 1.000 10.39491 ? 188 TYR A CE2    1 
ATOM   1441 C  CZ     . TYR A 1 195 ? -3.44600  -4.74200  -18.85500 1.000 11.71624 ? 188 TYR A CZ     1 
ATOM   1442 O  OH     . TYR A 1 195 ? -3.46300  -5.93300  -19.56900 1.000 14.19805 ? 188 TYR A OH     1 
ATOM   1443 N  N      . ARG A 1 196 ? -2.44300  -0.21300  -13.26500 1.000 12.39158 ? 189 ARG A N      1 
ATOM   1444 C  CA     . ARG A 1 196 ? -2.59200  0.86900   -12.30200 1.000 12.10591 ? 189 ARG A CA     1 
ATOM   1445 C  C      . ARG A 1 196 ? -1.23400  1.40300   -11.82900 1.000 13.05844 ? 189 ARG A C      1 
ATOM   1446 O  O      . ARG A 1 196 ? -0.31300  0.63200   -11.53100 1.000 13.10760 ? 189 ARG A O      1 
ATOM   1447 C  CB     . ARG A 1 196 ? -3.42500  0.36300   -11.11800 1.000 13.94407 ? 189 ARG A CB     1 
ATOM   1448 C  CG     . ARG A 1 196 ? -3.63200  1.39600   -10.01500 1.000 18.24586 ? 189 ARG A CG     1 
ATOM   1449 C  CD     . ARG A 1 196 ? -4.67900  0.95900   -8.99000  1.000 29.24343 ? 189 ARG A CD     1 
ATOM   1450 N  NE     . ARG A 1 196 ? -5.87400  0.36100   -9.57700  1.000 33.47951 ? 189 ARG A NE     1 
ATOM   1451 C  CZ     . ARG A 1 196 ? -6.63200  -0.54400  -8.96600  1.000 36.83760 ? 189 ARG A CZ     1 
ATOM   1452 N  NH1    . ARG A 1 196 ? -6.35600  -0.96600  -7.73900  1.000 36.34941 ? 189 ARG A NH1    1 
ATOM   1453 N  NH2    . ARG A 1 196 ? -7.69700  -1.03400  -9.59600  1.000 34.89989 ? 189 ARG A NH2    1 
ATOM   1454 N  N      . ALA A 1 197 ? -1.11800  2.73600   -11.75500 1.000 13.58715 ? 190 ALA A N      1 
ATOM   1455 C  CA     . ALA A 1 197 ? 0.12300   3.36300   -11.29700 1.000 11.84111 ? 190 ALA A CA     1 
ATOM   1456 C  C      . ALA A 1 197 ? 0.38900   3.01200   -9.83500  1.000 12.62959 ? 190 ALA A C      1 
ATOM   1457 O  O      . ALA A 1 197 ? -0.54100  2.97700   -9.02000  1.000 12.58592 ? 190 ALA A O      1 
ATOM   1458 C  CB     . ALA A 1 197 ? 0.05100   4.88300   -11.44100 1.000 12.31263 ? 190 ALA A CB     1 
ATOM   1459 N  N      . PRO A 1 198 ? 1.64200   2.76000   -9.46500  1.000 13.50069 ? 191 PRO A N      1 
ATOM   1460 C  CA     . PRO A 1 198 ? 1.89800   2.32400   -8.08300  1.000 17.34392 ? 191 PRO A CA     1 
ATOM   1461 C  C      . PRO A 1 198 ? 1.37600   3.29800   -7.03900  1.000 15.77786 ? 191 PRO A C      1 
ATOM   1462 O  O      . PRO A 1 198 ? 0.92900   2.85700   -5.97300  1.000 17.20772 ? 191 PRO A O      1 
ATOM   1463 C  CB     . PRO A 1 198 ? 3.42700   2.17600   -8.03300  1.000 15.28273 ? 191 PRO A CB     1 
ATOM   1464 C  CG     . PRO A 1 198 ? 3.94300   2.99900   -9.19000  1.000 15.91086 ? 191 PRO A CG     1 
ATOM   1465 C  CD     . PRO A 1 198 ? 2.88300   2.89400   -10.25200 1.000 12.92031 ? 191 PRO A CD     1 
ATOM   1466 N  N      . GLU A 1 199 ? 1.37100   4.60300   -7.31800  1.000 15.40509 ? 192 GLU A N      1 
ATOM   1467 C  CA     . GLU A 1 199 ? 0.99400   5.55600   -6.27400  1.000 17.31170 ? 192 GLU A CA     1 
ATOM   1468 C  C      . GLU A 1 199 ? -0.49900  5.48000   -5.98600  1.000 21.21978 ? 192 GLU A C      1 
ATOM   1469 O  O      . GLU A 1 199 ? -0.93800  5.77300   -4.86400  1.000 21.49224 ? 192 GLU A O      1 
ATOM   1470 C  CB     . GLU A 1 199 ? 1.39500   6.98200   -6.68500  1.000 18.63553 ? 192 GLU A CB     1 
ATOM   1471 C  CG     . GLU A 1 199 ? 0.76800   7.42900   -7.99600  1.000 15.50730 ? 192 GLU A CG     1 
ATOM   1472 C  CD     . GLU A 1 199 ? 1.72400   7.30100   -9.17100  1.000 14.31911 ? 192 GLU A CD     1 
ATOM   1473 O  OE1    . GLU A 1 199 ? 2.46300   6.29500   -9.22200  1.000 12.65279 ? 192 GLU A OE1    1 
ATOM   1474 O  OE2    . GLU A 1 199 ? 1.67900   8.16200   -10.07300 1.000 14.18942 ? 192 GLU A OE2    1 
ATOM   1475 N  N      . ILE A 1 200 ? -1.30000  5.08300   -6.97500  1.000 17.49274 ? 193 ILE A N      1 
ATOM   1476 C  CA     . ILE A 1 200 ? -2.72100  4.87700   -6.70500  1.000 19.09807 ? 193 ILE A CA     1 
ATOM   1477 C  C      . ILE A 1 200 ? -2.88900  3.72000   -5.73000  1.000 26.85550 ? 193 ILE A C      1 
ATOM   1478 O  O      . ILE A 1 200 ? -3.59600  3.82600   -4.71900  1.000 25.80482 ? 193 ILE A O      1 
ATOM   1479 C  CB     . ILE A 1 200 ? -3.49800  4.63900   -8.00800  1.000 20.87458 ? 193 ILE A CB     1 
ATOM   1480 C  CG1    . ILE A 1 200 ? -3.48600  5.90600   -8.85400  1.000 24.07129 ? 193 ILE A CG1    1 
ATOM   1481 C  CG2    . ILE A 1 200 ? -4.94500  4.23600   -7.69400  1.000 28.66752 ? 193 ILE A CG2    1 
ATOM   1482 C  CD1    . ILE A 1 200 ? -4.66100  6.01900   -9.76600  1.000 23.85415 ? 193 ILE A CD1    1 
ATOM   1483 N  N      . MET A 1 201 ? -2.18000  2.62100   -5.98400  1.000 20.14549 ? 194 MET A N      1 
ATOM   1484 C  CA     . MET A 1 201 ? -2.28200  1.47300   -5.09600  1.000 20.75078 ? 194 MET A CA     1 
ATOM   1485 C  C      . MET A 1 201 ? -1.76000  1.77700   -3.70100  1.000 22.72001 ? 194 MET A C      1 
ATOM   1486 O  O      . MET A 1 201 ? -2.11900  1.06800   -2.75600  1.000 24.07158 ? 194 MET A O      1 
ATOM   1487 C  CB     . MET A 1 201 ? -1.52300  0.30000   -5.69200  1.000 17.83677 ? 194 MET A CB     1 
ATOM   1488 C  CG     . MET A 1 201 ? -2.29400  -0.37100  -6.81200  1.000 23.12972 ? 194 MET A CG     1 
ATOM   1489 S  SD     . MET A 1 201 ? -1.31700  -1.65500  -7.60600  1.000 21.65184 ? 194 MET A SD     1 
ATOM   1490 C  CE     . MET A 1 201 ? 0.12100   -0.77600  -8.15200  1.000 17.18443 ? 194 MET A CE     1 
ATOM   1491 N  N      . LEU A 1 202 ? -0.93200  2.81100   -3.54700  1.000 19.19659 ? 195 LEU A N      1 
ATOM   1492 C  CA     . LEU A 1 202 ? -0.29200  3.11700   -2.27100  1.000 19.19572 ? 195 LEU A CA     1 
ATOM   1493 C  C      . LEU A 1 202 ? -0.91200  4.31700   -1.55800  1.000 22.22358 ? 195 LEU A C      1 
ATOM   1494 O  O      . LEU A 1 202 ? -0.29800  4.86000   -0.63300  1.000 27.11668 ? 195 LEU A O      1 
ATOM   1495 C  CB     . LEU A 1 202 ? 1.20300   3.34700   -2.47400  1.000 19.80644 ? 195 LEU A CB     1 
ATOM   1496 C  CG     . LEU A 1 202 ? 2.02200   2.07200   -2.67800  1.000 23.09221 ? 195 LEU A CG     1 
ATOM   1497 C  CD1    . LEU A 1 202 ? 3.49100   2.41700   -2.85200  1.000 29.76782 ? 195 LEU A CD1    1 
ATOM   1498 C  CD2    . LEU A 1 202 ? 1.82200   1.15200   -1.46400  1.000 23.08537 ? 195 LEU A CD2    1 
ATOM   1499 N  N      . ASN A 1 203 ? -2.09500  4.75200   -1.97600  1.000 21.44500 ? 196 ASN A N      1 
ATOM   1500 C  CA     . ASN A 1 203 ? -2.84400  5.78100   -1.25500  1.000 30.04186 ? 196 ASN A CA     1 
ATOM   1501 C  C      . ASN A 1 203 ? -2.09500  7.11300   -1.18200  1.000 31.73729 ? 196 ASN A C      1 
ATOM   1502 O  O      . ASN A 1 203 ? -2.17600  7.82400   -0.18000  1.000 31.72556 ? 196 ASN A O      1 
ATOM   1503 C  CB     . ASN A 1 203 ? -3.19600  5.28800   0.15300   1.000 28.46022 ? 196 ASN A CB     1 
ATOM   1504 C  CG     . ASN A 1 203 ? -4.22100  6.16800   0.83700   1.000 33.03630 ? 196 ASN A CG     1 
ATOM   1505 O  OD1    . ASN A 1 203 ? -5.28700  6.44400   0.28600   1.000 37.12586 ? 196 ASN A OD1    1 
ATOM   1506 N  ND2    . ASN A 1 203 ? -3.90600  6.60300   2.05700   1.000 34.29480 ? 196 ASN A ND2    1 
ATOM   1507 N  N      . TRP A 1 204 ? -1.36200  7.47500   -2.24500  1.000 24.38641 ? 197 TRP A N      1 
ATOM   1508 C  CA     . TRP A 1 204 ? -0.60700  8.72700   -2.18800  1.000 30.08943 ? 197 TRP A CA     1 
ATOM   1509 C  C      . TRP A 1 204 ? -1.52400  9.93400   -2.04300  1.000 33.44145 ? 197 TRP A C      1 
ATOM   1510 O  O      . TRP A 1 204 ? -1.15900  10.91900  -1.39300  1.000 34.52379 ? 197 TRP A O      1 
ATOM   1511 C  CB     . TRP A 1 204 ? 0.27300   8.90000   -3.40900  1.000 28.81473 ? 197 TRP A CB     1 
ATOM   1512 C  CG     . TRP A 1 204 ? 1.62800   9.43800   -3.11100  1.000 24.85361 ? 197 TRP A CG     1 
ATOM   1513 C  CD1    . TRP A 1 204 ? 1.97400   10.75500  -2.95900  1.000 28.62153 ? 197 TRP A CD1    1 
ATOM   1514 C  CD2    . TRP A 1 204 ? 2.84800   8.69400   -3.03800  1.000 23.62967 ? 197 TRP A CD2    1 
ATOM   1515 N  NE1    . TRP A 1 204 ? 3.33100   10.86900  -2.75600  1.000 27.93417 ? 197 TRP A NE1    1 
ATOM   1516 C  CE2    . TRP A 1 204 ? 3.89100   9.61700   -2.80400  1.000 25.40514 ? 197 TRP A CE2    1 
ATOM   1517 C  CE3    . TRP A 1 204 ? 3.16000   7.33400   -3.12500  1.000 26.49961 ? 197 TRP A CE3    1 
ATOM   1518 C  CZ2    . TRP A 1 204 ? 5.22100   9.22000   -2.66000  1.000 26.27757 ? 197 TRP A CZ2    1 
ATOM   1519 C  CZ3    . TRP A 1 204 ? 4.48100   6.94700   -2.98200  1.000 25.84228 ? 197 TRP A CZ3    1 
ATOM   1520 C  CH2    . TRP A 1 204 ? 5.49000   7.88400   -2.75500  1.000 27.21745 ? 197 TRP A CH2    1 
ATOM   1521 N  N      . MET A 1 205 ? -2.70000  9.89900   -2.66300  1.000 32.25241 ? 198 MET A N      1 
ATOM   1522 C  CA     . MET A 1 205 ? -3.74200  10.86300  -2.32000  1.000 43.33733 ? 198 MET A CA     1 
ATOM   1523 C  C      . MET A 1 205 ? -3.66800  12.17400  -3.08900  1.000 45.05297 ? 198 MET A C      1 
ATOM   1524 O  O      . MET A 1 205 ? -4.65000  12.91900  -3.12700  1.000 54.59862 ? 198 MET A O      1 
ATOM   1525 C  CB     . MET A 1 205 ? -3.71300  11.14700  -0.81400  1.000 49.09667 ? 198 MET A CB     1 
ATOM   1526 C  CG     . MET A 1 205 ? -5.07700  11.45600  -0.23700  1.000 56.57532 ? 198 MET A CG     1 
ATOM   1527 S  SD     . MET A 1 205 ? -6.37700  10.48700  -1.01500  1.000 73.98970 ? 198 MET A SD     1 
ATOM   1528 C  CE     . MET A 1 205 ? -6.47200  9.07900   0.08300   1.000 58.08483 ? 198 MET A CE     1 
ATOM   1529 N  N      . HIS A 1 206 ? -2.52700  12.47400  -3.69300  1.000 38.22609 ? 199 HIS A N      1 
ATOM   1530 C  CA     . HIS A 1 206 ? -2.43500  13.53400  -4.68800  1.000 38.67673 ? 199 HIS A CA     1 
ATOM   1531 C  C      . HIS A 1 206 ? -1.93900  12.86100  -5.95400  1.000 42.10114 ? 199 HIS A C      1 
ATOM   1532 O  O      . HIS A 1 206 ? -0.82400  12.33500  -5.96800  1.000 49.56238 ? 199 HIS A O      1 
ATOM   1533 C  CB     . HIS A 1 206 ? -1.46100  14.65000  -4.28900  1.000 40.47252 ? 199 HIS A CB     1 
ATOM   1534 C  CG     . HIS A 1 206 ? -0.60100  14.33300  -3.10300  1.000 47.81952 ? 199 HIS A CG     1 
ATOM   1535 N  ND1    . HIS A 1 206 ? -1.10600  14.16500  -1.83200  1.000 50.77656 ? 199 HIS A ND1    1 
ATOM   1536 C  CD2    . HIS A 1 206 ? 0.74200   14.17900  -2.99600  1.000 43.80761 ? 199 HIS A CD2    1 
ATOM   1537 C  CE1    . HIS A 1 206 ? -0.11500  13.91200  -0.99500  1.000 47.97230 ? 199 HIS A CE1    1 
ATOM   1538 N  NE2    . HIS A 1 206 ? 1.01700   13.91500  -1.67600  1.000 45.67544 ? 199 HIS A NE2    1 
ATOM   1539 N  N      . TYR A 1 207 ? -2.76500  12.82400  -6.99200  1.000 29.79716 ? 200 TYR A N      1 
ATOM   1540 C  CA     . TYR A 1 207 ? -2.40800  12.08900  -8.20000  1.000 23.75250 ? 200 TYR A CA     1 
ATOM   1541 C  C      . TYR A 1 207 ? -2.13200  13.06800  -9.32400  1.000 23.30832 ? 200 TYR A C      1 
ATOM   1542 O  O      . TYR A 1 207 ? -2.85700  14.05200  -9.49000  1.000 26.49870 ? 200 TYR A O      1 
ATOM   1543 C  CB     . TYR A 1 207 ? -3.49600  11.07900  -8.59300  1.000 24.66866 ? 200 TYR A CB     1 
ATOM   1544 C  CG     . TYR A 1 207 ? -3.61700  10.03500  -7.51800  1.000 24.50773 ? 200 TYR A CG     1 
ATOM   1545 C  CD1    . TYR A 1 207 ? -2.48800  9.40300   -7.04100  1.000 28.65611 ? 200 TYR A CD1    1 
ATOM   1546 C  CD2    . TYR A 1 207 ? -4.84300  9.73200   -6.93300  1.000 25.48323 ? 200 TYR A CD2    1 
ATOM   1547 C  CE1    . TYR A 1 207 ? -2.56400  8.46900   -6.03400  1.000 28.49968 ? 200 TYR A CE1    1 
ATOM   1548 C  CE2    . TYR A 1 207 ? -4.93100  8.78900   -5.92000  1.000 28.33128 ? 200 TYR A CE2    1 
ATOM   1549 C  CZ     . TYR A 1 207 ? -3.77900  8.16600   -5.47300  1.000 27.04923 ? 200 TYR A CZ     1 
ATOM   1550 O  OH     . TYR A 1 207 ? -3.81600  7.23200   -4.46400  1.000 30.94329 ? 200 TYR A OH     1 
ATOM   1551 N  N      . ASN A 1 208 ? -1.04500  12.81600  -10.04000 1.000 24.14031 ? 201 ASN A N      1 
ATOM   1552 C  CA     . ASN A 1 208 ? -0.69100  13.51000  -11.26600 1.000 22.38636 ? 201 ASN A CA     1 
ATOM   1553 C  C      . ASN A 1 208 ? -1.49600  12.91200  -12.41400 1.000 20.86852 ? 201 ASN A C      1 
ATOM   1554 O  O      . ASN A 1 208 ? -1.88300  11.73500  -12.38100 1.000 13.82446 ? 201 ASN A O      1 
ATOM   1555 C  CB     . ASN A 1 208 ? 0.81400   13.34700  -11.50400 1.000 18.20518 ? 201 ASN A CB     1 
ATOM   1556 C  CG     . ASN A 1 208 ? 1.36700   14.25000  -12.58500 1.000 28.74718 ? 201 ASN A CG     1 
ATOM   1557 O  OD1    . ASN A 1 208 ? 0.98300   14.18000  -13.75500 1.000 29.57181 ? 201 ASN A OD1    1 
ATOM   1558 N  ND2    . ASN A 1 208 ? 2.30500   15.11100  -12.19000 1.000 34.54174 ? 201 ASN A ND2    1 
ATOM   1559 N  N      . GLN A 1 209 ? -1.75000  13.72900  -13.44100 1.000 19.03061 ? 202 GLN A N      1 
ATOM   1560 C  CA     . GLN A 1 209 ? -2.31100  13.16400  -14.65700 1.000 18.20282 ? 202 GLN A CA     1 
ATOM   1561 C  C      . GLN A 1 209 ? -1.42900  12.04600  -15.18900 1.000 16.39781 ? 202 GLN A C      1 
ATOM   1562 O  O      . GLN A 1 209 ? -1.91700  11.19500  -15.94200 1.000 11.97904 ? 202 GLN A O      1 
ATOM   1563 C  CB     . GLN A 1 209 ? -2.48800  14.25700  -15.71700 1.000 14.98311 ? 202 GLN A CB     1 
ATOM   1564 C  CG     . GLN A 1 209 ? -3.47800  15.35500  -15.26900 1.000 17.48248 ? 202 GLN A CG     1 
ATOM   1565 C  CD     . GLN A 1 209 ? -3.71800  16.39800  -16.34000 1.000 16.18299 ? 202 GLN A CD     1 
ATOM   1566 O  OE1    . GLN A 1 209 ? -2.78200  16.86700  -16.97100 1.000 17.92870 ? 202 GLN A OE1    1 
ATOM   1567 N  NE2    . GLN A 1 209 ? -4.98100  16.79100  -16.52100 1.000 18.57568 ? 202 GLN A NE2    1 
ATOM   1568 N  N      . THR A 1 210 ? -0.13900  12.01500  -14.80700 1.000 14.56131 ? 203 THR A N      1 
ATOM   1569 C  CA     . THR A 1 210 ? 0.73200   10.95600  -15.31700 1.000 13.07571 ? 203 THR A CA     1 
ATOM   1570 C  C      . THR A 1 210 ? 0.43200   9.58500   -14.71200 1.000 13.39792 ? 203 THR A C      1 
ATOM   1571 O  O      . THR A 1 210 ? 1.11900   8.62100   -15.08400 1.000 9.80037  ? 203 THR A O      1 
ATOM   1572 C  CB     . THR A 1 210 ? 2.22200   11.25800  -15.09500 1.000 16.10642 ? 203 THR A CB     1 
ATOM   1573 O  OG1    . THR A 1 210 ? 2.47400   11.52500  -13.71500 1.000 16.37453 ? 203 THR A OG1    1 
ATOM   1574 C  CG2    . THR A 1 210 ? 2.68800   12.46700  -15.95200 1.000 18.72437 ? 203 THR A CG2    1 
ATOM   1575 N  N      . VAL A 1 211 ? -0.55200  9.43000   -13.81700 1.000 10.50828 ? 204 VAL A N      1 
ATOM   1576 C  CA     . VAL A 1 211 ? -0.97100  8.05900   -13.52800 1.000 11.20866 ? 204 VAL A CA     1 
ATOM   1577 C  C      . VAL A 1 211 ? -1.47400  7.40400   -14.80400 1.000 9.50520  ? 204 VAL A C      1 
ATOM   1578 O  O      . VAL A 1 211 ? -1.28400  6.19800   -15.00900 1.000 10.50600 ? 204 VAL A O      1 
ATOM   1579 C  CB     . VAL A 1 211 ? -2.03900  7.98200   -12.41600 1.000 13.24380 ? 204 VAL A CB     1 
ATOM   1580 C  CG1    . VAL A 1 211 ? -1.47400  8.47600   -11.07900 1.000 11.93398 ? 204 VAL A CG1    1 
ATOM   1581 C  CG2    . VAL A 1 211 ? -3.30200  8.71600   -12.82600 1.000 12.67600 ? 204 VAL A CG2    1 
ATOM   1582 N  N      . ASP A 1 212 ? -2.12300  8.18600   -15.68300 1.000 10.41719 ? 205 ASP A N      1 
ATOM   1583 C  CA     . ASP A 1 212 ? -2.61300  7.63500   -16.94500 1.000 9.32538  ? 205 ASP A CA     1 
ATOM   1584 C  C      . ASP A 1 212 ? -1.45400  7.25400   -17.85900 1.000 10.13942 ? 205 ASP A C      1 
ATOM   1585 O  O      . ASP A 1 212 ? -1.55200  6.29100   -18.63700 1.000 6.37389  ? 205 ASP A O      1 
ATOM   1586 C  CB     . ASP A 1 212 ? -3.51700  8.65200   -17.65800 1.000 8.99799  ? 205 ASP A CB     1 
ATOM   1587 C  CG     . ASP A 1 212 ? -4.89500  8.82600   -16.98300 1.000 10.09897 ? 205 ASP A CG     1 
ATOM   1588 O  OD1    . ASP A 1 212 ? -5.34200  7.93000   -16.23600 1.000 7.44769  ? 205 ASP A OD1    1 
ATOM   1589 O  OD2    . ASP A 1 212 ? -5.49800  9.90300   -17.17600 1.000 10.17105 ? 205 ASP A OD2    1 
ATOM   1590 N  N      . ILE A 1 213 ? -0.36300  8.02700   -17.81000 1.000 8.37608  ? 206 ILE A N      1 
ATOM   1591 C  CA     . ILE A 1 213 ? 0.81100   7.71500   -18.62400 1.000 8.59581  ? 206 ILE A CA     1 
ATOM   1592 C  C      . ILE A 1 213 ? 1.41800   6.38200   -18.19800 1.000 10.29011 ? 206 ILE A C      1 
ATOM   1593 O  O      . ILE A 1 213 ? 1.86000   5.59600   -19.04400 1.000 11.48535 ? 206 ILE A O      1 
ATOM   1594 C  CB     . ILE A 1 213 ? 1.84200   8.85900   -18.56100 1.000 8.96485  ? 206 ILE A CB     1 
ATOM   1595 C  CG1    . ILE A 1 213 ? 1.29200   10.14100  -19.20200 1.000 10.48322 ? 206 ILE A CG1    1 
ATOM   1596 C  CG2    . ILE A 1 213 ? 3.17100   8.43200   -19.21700 1.000 10.54785 ? 206 ILE A CG2    1 
ATOM   1597 C  CD1    . ILE A 1 213 ? 0.88600   9.97800   -20.68400 1.000 12.12777 ? 206 ILE A CD1    1 
ATOM   1598 N  N      . TRP A 1 214 ? 1.44000   6.09100   -16.89000 1.000 9.54681  ? 207 TRP A N      1 
ATOM   1599 C  CA     . TRP A 1 214 ? 1.88000   4.76500   -16.45100 1.000 10.26750 ? 207 TRP A CA     1 
ATOM   1600 C  C      . TRP A 1 214 ? 1.05600   3.68600   -17.14100 1.000 8.83543  ? 207 TRP A C      1 
ATOM   1601 O  O      . TRP A 1 214 ? 1.60000   2.74600   -17.73900 1.000 9.38692  ? 207 TRP A O      1 
ATOM   1602 C  CB     . TRP A 1 214 ? 1.75900   4.64200   -14.92700 1.000 8.89796  ? 207 TRP A CB     1 
ATOM   1603 C  CG     . TRP A 1 214 ? 2.19800   3.28100   -14.42800 1.000 9.97959  ? 207 TRP A CG     1 
ATOM   1604 C  CD1    . TRP A 1 214 ? 1.44900   2.14300   -14.32600 1.000 9.50363  ? 207 TRP A CD1    1 
ATOM   1605 C  CD2    . TRP A 1 214 ? 3.52500   2.92700   -14.03400 1.000 10.67990 ? 207 TRP A CD2    1 
ATOM   1606 N  NE1    . TRP A 1 214 ? 2.22900   1.10200   -13.86400 1.000 12.34219 ? 207 TRP A NE1    1 
ATOM   1607 C  CE2    . TRP A 1 214 ? 3.50800   1.56800   -13.66900 1.000 12.59855 ? 207 TRP A CE2    1 
ATOM   1608 C  CE3    . TRP A 1 214 ? 4.72000   3.65100   -13.90600 1.000 13.57340 ? 207 TRP A CE3    1 
ATOM   1609 C  CZ2    . TRP A 1 214 ? 4.64800   0.90900   -13.21300 1.000 9.73429  ? 207 TRP A CZ2    1 
ATOM   1610 C  CZ3    . TRP A 1 214 ? 5.85000   2.99800   -13.46600 1.000 11.90239 ? 207 TRP A CZ3    1 
ATOM   1611 C  CH2    . TRP A 1 214 ? 5.81200   1.64000   -13.12300 1.000 11.84085 ? 207 TRP A CH2    1 
ATOM   1612 N  N      . SER A 1 215 ? -0.27200  3.83000   -17.09300 1.000 8.03243  ? 208 SER A N      1 
ATOM   1613 C  CA     . SER A 1 215 ? -1.14700  2.85200   -17.72900 1.000 9.27536  ? 208 SER A CA     1 
ATOM   1614 C  C      . SER A 1 215 ? -0.84400  2.70500   -19.21800 1.000 9.17000  ? 208 SER A C      1 
ATOM   1615 O  O      . SER A 1 215 ? -0.82600  1.57900   -19.74200 1.000 9.31165  ? 208 SER A O      1 
ATOM   1616 C  CB     . SER A 1 215 ? -2.61800  3.22900   -17.51100 1.000 9.62348  ? 208 SER A CB     1 
ATOM   1617 O  OG     . SER A 1 215 ? -2.87500  3.49300   -16.12600 1.000 9.11548  ? 208 SER A OG     1 
ATOM   1618 N  N      . VAL A 1 216 ? -0.63000  3.82500   -19.92500 1.000 8.37307  ? 209 VAL A N      1 
ATOM   1619 C  CA     . VAL A 1 216 ? -0.28800  3.72900   -21.34300 1.000 8.27099  ? 209 VAL A CA     1 
ATOM   1620 C  C      . VAL A 1 216 ? 0.97900   2.91100   -21.53000 1.000 9.30652  ? 209 VAL A C      1 
ATOM   1621 O  O      . VAL A 1 216 ? 1.08700   2.11100   -22.46700 1.000 9.02609  ? 209 VAL A O      1 
ATOM   1622 C  CB     . VAL A 1 216 ? -0.13800  5.12000   -21.98300 1.000 9.86065  ? 209 VAL A CB     1 
ATOM   1623 C  CG1    . VAL A 1 216 ? 0.29600   4.95600   -23.46200 1.000 9.87929  ? 209 VAL A CG1    1 
ATOM   1624 C  CG2    . VAL A 1 216 ? -1.45600  5.89700   -21.87800 1.000 6.56045  ? 209 VAL A CG2    1 
ATOM   1625 N  N      . GLY A 1 217 ? 1.98400   3.14000   -20.68400 1.000 9.33382  ? 210 GLY A N      1 
ATOM   1626 C  CA     . GLY A 1 217 ? 3.22200   2.38800   -20.81800 1.000 10.65923 ? 210 GLY A CA     1 
ATOM   1627 C  C      . GLY A 1 217 ? 3.00400   0.89500   -20.66100 1.000 11.71471 ? 210 GLY A C      1 
ATOM   1628 O  O      . GLY A 1 217 ? 3.56500   0.09300   -21.41500 1.000 9.34833  ? 210 GLY A O      1 
ATOM   1629 N  N      . CYS A 1 218 ? 2.16500   0.50500   -19.69200 1.000 8.35302  ? 211 CYS A N      1 
ATOM   1630 C  CA     . CYS A 1 218 ? 1.86000   -0.90400  -19.46800 1.000 8.67721  ? 211 CYS A CA     1 
ATOM   1631 C  C      . CYS A 1 218 ? 1.17200   -1.50500  -20.68900 1.000 9.44027  ? 211 CYS A C      1 
ATOM   1632 O  O      . CYS A 1 218 ? 1.44000   -2.65400  -21.07500 1.000 9.51049  ? 211 CYS A O      1 
ATOM   1633 C  CB     . CYS A 1 218 ? 0.94500   -1.01600  -18.24000 1.000 8.98112  ? 211 CYS A CB     1 
ATOM   1634 S  SG     . CYS A 1 218 ? 1.82700   -0.78200  -16.69200 1.000 8.89815  ? 211 CYS A SG     1 
ATOM   1635 N  N      . ILE A 1 219 ? 0.24300   -0.74500  -21.27800 1.000 9.47256  ? 212 ILE A N      1 
ATOM   1636 C  CA     . ILE A 1 219 ? -0.49100  -1.19100  -22.45500 1.000 10.90601 ? 212 ILE A CA     1 
ATOM   1637 C  C      . ILE A 1 219 ? 0.45100   -1.33500  -23.64600 1.000 10.39871 ? 212 ILE A C      1 
ATOM   1638 O  O      . ILE A 1 219 ? 0.45900   -2.36200  -24.32500 1.000 12.65358 ? 212 ILE A O      1 
ATOM   1639 C  CB     . ILE A 1 219 ? -1.64200  -0.20900  -22.76300 1.000 10.77005 ? 212 ILE A CB     1 
ATOM   1640 C  CG1    . ILE A 1 219 ? -2.72600  -0.28000  -21.69000 1.000 9.91144  ? 212 ILE A CG1    1 
ATOM   1641 C  CG2    . ILE A 1 219 ? -2.26800  -0.51900  -24.12400 1.000 8.30083  ? 212 ILE A CG2    1 
ATOM   1642 C  CD1    . ILE A 1 219 ? -3.48900  1.04600   -21.46200 1.000 12.45870 ? 212 ILE A CD1    1 
ATOM   1643 N  N      . MET A 1 220 ? 1.23400   -0.29100  -23.93200 1.000 9.34217  ? 213 MET A N      1 
ATOM   1644 C  CA     . MET A 1 220 ? 2.26400   -0.34100  -24.98100 1.000 10.74330 ? 213 MET A CA     1 
ATOM   1645 C  C      . MET A 1 220 ? 3.13900   -1.59000  -24.88400 1.000 13.35434 ? 213 MET A C      1 
ATOM   1646 O  O      . MET A 1 220 ? 3.34900   -2.31100  -25.87100 1.000 12.40317 ? 213 MET A O      1 
ATOM   1647 C  CB     . MET A 1 220 ? 3.17600   0.88600   -24.83500 1.000 8.98228  ? 213 MET A CB     1 
ATOM   1648 C  CG     . MET A 1 220 ? 4.30800   0.92900   -25.85800 1.000 11.20202 ? 213 MET A CG     1 
ATOM   1649 S  SD     . MET A 1 220 ? 4.67300   2.63500   -26.35500 1.000 12.96208 ? 213 MET A SD     1 
ATOM   1650 C  CE     . MET A 1 220 ? 6.25900   2.32200   -27.19700 1.000 12.32204 ? 213 MET A CE     1 
ATOM   1651 N  N      . ALA A 1 221 ? 3.71500   -1.81800  -23.71200 1.000 10.98195 ? 214 ALA A N      1 
ATOM   1652 C  CA     . ALA A 1 221 ? 4.53800   -3.01200  -23.50900 1.000 10.24175 ? 214 ALA A CA     1 
ATOM   1653 C  C      . ALA A 1 221 ? 3.81700   -4.28800  -23.97500 1.000 12.30892 ? 214 ALA A C      1 
ATOM   1654 O  O      . ALA A 1 221 ? 4.35300   -5.10000  -24.75700 1.000 12.98564 ? 214 ALA A O      1 
ATOM   1655 C  CB     . ALA A 1 221 ? 4.90900   -3.11500  -22.02400 1.000 9.92375  ? 214 ALA A CB     1 
ATOM   1656 N  N      . GLU A 1 222 ? 2.56700   -4.44200  -23.53600 1.000 10.23103 ? 215 GLU A N      1 
ATOM   1657 C  CA     . GLU A 1 222 ? 1.76800   -5.61300  -23.89100 1.000 12.14695 ? 215 GLU A CA     1 
ATOM   1658 C  C      . GLU A 1 222 ? 1.48900   -5.69600  -25.38500 1.000 12.93951 ? 215 GLU A C      1 
ATOM   1659 O  O      . GLU A 1 222 ? 1.48300   -6.79400  -25.96000 1.000 13.58570 ? 215 GLU A O      1 
ATOM   1660 C  CB     . GLU A 1 222 ? 0.44400   -5.59600  -23.12500 1.000 14.24997 ? 215 GLU A CB     1 
ATOM   1661 C  CG     . GLU A 1 222 ? -0.39600  -6.86700  -23.26800 1.000 12.24478 ? 215 GLU A CG     1 
ATOM   1662 C  CD     . GLU A 1 222 ? -1.46400  -6.97300  -22.19000 1.000 19.96159 ? 215 GLU A CD     1 
ATOM   1663 O  OE1    . GLU A 1 222 ? -1.39500  -6.21600  -21.18000 1.000 12.68489 ? 215 GLU A OE1    1 
ATOM   1664 O  OE2    . GLU A 1 222 ? -2.34700  -7.84700  -22.32200 1.000 19.96058 ? 215 GLU A OE2    1 
ATOM   1665 N  N      . LEU A 1 223 ? 1.19900   -4.56100  -26.02500 1.000 11.33635 ? 216 LEU A N      1 
ATOM   1666 C  CA     . LEU A 1 223 ? 1.02800   -4.59600  -27.47700 1.000 16.19840 ? 216 LEU A CA     1 
ATOM   1667 C  C      . LEU A 1 223 ? 2.30500   -5.05100  -28.17000 1.000 16.95694 ? 216 LEU A C      1 
ATOM   1668 O  O      . LEU A 1 223 ? 2.24300   -5.71900  -29.21400 1.000 16.66310 ? 216 LEU A O      1 
ATOM   1669 C  CB     . LEU A 1 223 ? 0.59400   -3.23200  -28.00200 1.000 13.42752 ? 216 LEU A CB     1 
ATOM   1670 C  CG     . LEU A 1 223 ? -0.73000  -2.66400  -27.48500 1.000 13.49946 ? 216 LEU A CG     1 
ATOM   1671 C  CD1    . LEU A 1 223 ? -1.05400  -1.37800  -28.23800 1.000 15.11479 ? 216 LEU A CD1    1 
ATOM   1672 C  CD2    . LEU A 1 223 ? -1.86300  -3.67300  -27.61500 1.000 15.43217 ? 216 LEU A CD2    1 
ATOM   1673 N  N      . LEU A 1 224 ? 3.47500   -4.68200  -27.62700 1.000 13.21145 ? 217 LEU A N      1 
ATOM   1674 C  CA     . LEU A 1 224 ? 4.71500   -5.07600  -28.30000 1.000 14.65678 ? 217 LEU A CA     1 
ATOM   1675 C  C      . LEU A 1 224 ? 5.08000   -6.53600  -28.06400 1.000 19.29061 ? 217 LEU A C      1 
ATOM   1676 O  O      . LEU A 1 224 ? 5.54200   -7.21600  -28.98500 1.000 21.76157 ? 217 LEU A O      1 
ATOM   1677 C  CB     . LEU A 1 224 ? 5.90100   -4.19100  -27.90400 1.000 14.18685 ? 217 LEU A CB     1 
ATOM   1678 C  CG     . LEU A 1 224 ? 5.86300   -2.69700  -28.21100 1.000 14.52878 ? 217 LEU A CG     1 
ATOM   1679 C  CD1    . LEU A 1 224 ? 6.63600   -1.95400  -27.17500 1.000 12.56056 ? 217 LEU A CD1    1 
ATOM   1680 C  CD2    . LEU A 1 224 ? 6.39900   -2.42300  -29.63500 1.000 13.87072 ? 217 LEU A CD2    1 
ATOM   1681 N  N      . THR A 1 225 ? 4.90200   -7.04100  -26.84600 1.000 15.50808 ? 218 THR A N      1 
ATOM   1682 C  CA     . THR A 1 225 ? 5.30200   -8.40900  -26.54700 1.000 16.36025 ? 218 THR A CA     1 
ATOM   1683 C  C      . THR A 1 225 ? 4.16600   -9.40800  -26.66200 1.000 19.16682 ? 218 THR A C      1 
ATOM   1684 O  O      . THR A 1 225 ? 4.43100   -10.61100 -26.77400 1.000 19.19418 ? 218 THR A O      1 
ATOM   1685 C  CB     . THR A 1 225 ? 5.84400   -8.48800  -25.12700 1.000 14.76719 ? 218 THR A CB     1 
ATOM   1686 O  OG1    . THR A 1 225 ? 4.74300   -8.29400  -24.23700 1.000 14.93559 ? 218 THR A OG1    1 
ATOM   1687 C  CG2    . THR A 1 225 ? 6.86200   -7.36700  -24.89300 1.000 16.19059 ? 218 THR A CG2    1 
ATOM   1688 N  N      . GLY A 1 226 ? 2.91400   -8.94200  -26.63200 1.000 16.18968 ? 219 GLY A N      1 
ATOM   1689 C  CA     . GLY A 1 226 ? 1.76600   -9.81000  -26.47600 1.000 17.90389 ? 219 GLY A CA     1 
ATOM   1690 C  C      . GLY A 1 226 ? 1.56600   -10.36100 -25.08000 1.000 19.52786 ? 219 GLY A C      1 
ATOM   1691 O  O      . GLY A 1 226 ? 0.71600   -11.23500 -24.89700 1.000 18.98658 ? 219 GLY A O      1 
ATOM   1692 N  N      . ARG A 1 227 ? 2.30700   -9.88200  -24.08200 1.000 14.95836 ? 220 ARG A N      1 
ATOM   1693 C  CA     . ARG A 1 227 ? 2.22900   -10.45600 -22.74300 1.000 15.73756 ? 220 ARG A CA     1 
ATOM   1694 C  C      . ARG A 1 227 ? 2.01500   -9.33600  -21.73000 1.000 14.77832 ? 220 ARG A C      1 
ATOM   1695 O  O      . ARG A 1 227 ? 2.60900   -8.26500  -21.85600 1.000 11.87352 ? 220 ARG A O      1 
ATOM   1696 C  CB     . ARG A 1 227 ? 3.51500   -11.21200 -22.42500 1.000 19.21983 ? 220 ARG A CB     1 
ATOM   1697 C  CG     . ARG A 1 227 ? 3.83100   -12.23000 -23.50500 1.000 22.03872 ? 220 ARG A CG     1 
ATOM   1698 C  CD     . ARG A 1 227 ? 4.96600   -13.16200 -23.17800 1.000 24.41571 ? 220 ARG A CD     1 
ATOM   1699 N  NE     . ARG A 1 227 ? 5.24900   -13.22200 -21.75700 1.000 28.13975 ? 220 ARG A NE     1 
ATOM   1700 C  CZ     . ARG A 1 227 ? 4.91300   -14.24800 -20.98500 1.000 32.19870 ? 220 ARG A CZ     1 
ATOM   1701 N  NH1    . ARG A 1 227 ? 4.23500   -15.28600 -21.46400 1.000 31.56578 ? 220 ARG A NH1    1 
ATOM   1702 N  NH2    . ARG A 1 227 ? 5.26000   -14.23200 -19.70200 1.000 31.28810 ? 220 ARG A NH2    1 
ATOM   1703 N  N      . THR A 1 228 ? 1.16500   -9.58300  -20.73200 1.000 11.87733 ? 221 THR A N      1 
ATOM   1704 C  CA     . THR A 1 228 ? 0.99800   -8.61400  -19.65100 1.000 14.08115 ? 221 THR A CA     1 
ATOM   1705 C  C      . THR A 1 228 ? 2.34300   -8.27000  -19.01900 1.000 14.02839 ? 221 THR A C      1 
ATOM   1706 O  O      . THR A 1 228 ? 3.12700   -9.15900  -18.67100 1.000 13.30349 ? 221 THR A O      1 
ATOM   1707 C  CB     . THR A 1 228 ? 0.03600   -9.15100  -18.59000 1.000 14.77628 ? 221 THR A CB     1 
ATOM   1708 O  OG1    . THR A 1 228 ? -1.08000  -9.76800  -19.24100 1.000 13.39830 ? 221 THR A OG1    1 
ATOM   1709 C  CG2    . THR A 1 228 ? -0.43700  -8.02900  -17.65600 1.000 12.71505 ? 221 THR A CG2    1 
ATOM   1710 N  N      . LEU A 1 229 ? 2.59900   -6.96400  -18.86200 1.000 11.76437 ? 222 LEU A N      1 
ATOM   1711 C  CA     . LEU A 1 229 ? 3.87200   -6.51200  -18.30000 1.000 13.25302 ? 222 LEU A CA     1 
ATOM   1712 C  C      . LEU A 1 229 ? 3.97100   -6.84400  -16.82000 1.000 10.16045 ? 222 LEU A C      1 
ATOM   1713 O  O      . LEU A 1 229 ? 4.97100   -7.42100  -16.36700 1.000 10.15612 ? 222 LEU A O      1 
ATOM   1714 C  CB     . LEU A 1 229 ? 4.05000   -5.00700  -18.52500 1.000 11.54618 ? 222 LEU A CB     1 
ATOM   1715 C  CG     . LEU A 1 229 ? 5.37100   -4.45900  -17.95200 1.000 11.81557 ? 222 LEU A CG     1 
ATOM   1716 C  CD1    . LEU A 1 229 ? 6.54200   -5.24800  -18.49900 1.000 12.32307 ? 222 LEU A CD1    1 
ATOM   1717 C  CD2    . LEU A 1 229 ? 5.54700   -2.95200  -18.26300 1.000 14.43411 ? 222 LEU A CD2    1 
ATOM   1718 N  N      . PHE A 1 230 ? 2.93900   -6.49300  -16.04800 1.000 9.20860  ? 223 PHE A N      1 
ATOM   1719 C  CA     . PHE A 1 230 ? 2.91800   -6.67500  -14.59200 1.000 10.50932 ? 223 PHE A CA     1 
ATOM   1720 C  C      . PHE A 1 230 ? 1.63600   -7.41000  -14.19200 1.000 11.74418 ? 223 PHE A C      1 
ATOM   1721 O  O      . PHE A 1 230 ? 0.69100   -6.79400  -13.68300 1.000 11.19193 ? 223 PHE A O      1 
ATOM   1722 C  CB     . PHE A 1 230 ? 2.97500   -5.32100  -13.87300 1.000 9.37203  ? 223 PHE A CB     1 
ATOM   1723 C  CG     . PHE A 1 230 ? 4.18100   -4.46800  -14.20200 1.000 11.63419 ? 223 PHE A CG     1 
ATOM   1724 C  CD1    . PHE A 1 230 ? 5.46600   -4.91600  -13.97200 1.000 10.36865 ? 223 PHE A CD1    1 
ATOM   1725 C  CD2    . PHE A 1 230 ? 4.00200   -3.17600  -14.70500 1.000 9.98182  ? 223 PHE A CD2    1 
ATOM   1726 C  CE1    . PHE A 1 230 ? 6.56100   -4.10400  -14.23800 1.000 12.84541 ? 223 PHE A CE1    1 
ATOM   1727 C  CE2    . PHE A 1 230 ? 5.08500   -2.35500  -14.96700 1.000 12.20291 ? 223 PHE A CE2    1 
ATOM   1728 C  CZ     . PHE A 1 230 ? 6.37900   -2.83200  -14.74000 1.000 11.16544 ? 223 PHE A CZ     1 
ATOM   1729 N  N      . PRO A 1 231 ? 1.56100   -8.74400  -14.41600 1.000 13.50140 ? 224 PRO A N      1 
ATOM   1730 C  CA     . PRO A 1 231 ? 0.32200   -9.47600  -14.03200 1.000 13.07363 ? 224 PRO A CA     1 
ATOM   1731 C  C      . PRO A 1 231 ? 0.34600   -9.95400  -12.58400 1.000 14.32512 ? 224 PRO A C      1 
ATOM   1732 O  O      . PRO A 1 231 ? 0.47800   -11.14700 -12.27900 1.000 15.77367 ? 224 PRO A O      1 
ATOM   1733 C  CB     . PRO A 1 231 ? 0.30000   -10.64000 -15.02800 1.000 13.30911 ? 224 PRO A CB     1 
ATOM   1734 C  CG     . PRO A 1 231 ? 1.75600   -10.92900 -15.32100 1.000 15.10098 ? 224 PRO A CG     1 
ATOM   1735 C  CD     . PRO A 1 231 ? 2.48000   -9.56900  -15.22400 1.000 11.81351 ? 224 PRO A CD     1 
ATOM   1736 N  N      . GLY A 1 232 ? 0.22400   -9.01100  -11.64900 1.000 10.26681 ? 225 GLY A N      1 
ATOM   1737 C  CA     . GLY A 1 232 ? 0.29700   -9.36600  -10.24600 1.000 9.38036  ? 225 GLY A CA     1 
ATOM   1738 C  C      . GLY A 1 232 ? -0.89400  -10.20400 -9.82300  1.000 10.71864 ? 225 GLY A C      1 
ATOM   1739 O  O      . GLY A 1 232 ? -1.99900  -10.06600 -10.34500 1.000 12.97966 ? 225 GLY A O      1 
ATOM   1740 N  N      . THR A 1 233 ? -0.64900  -11.11500 -8.87800  1.000 10.30406 ? 226 THR A N      1 
ATOM   1741 C  CA     . THR A 1 233 ? -1.71300  -11.96700 -8.34100  1.000 13.69535 ? 226 THR A CA     1 
ATOM   1742 C  C      . THR A 1 233 ? -2.56600  -11.25400 -7.30700  1.000 14.83133 ? 226 THR A C      1 
ATOM   1743 O  O      . THR A 1 233 ? -3.69100  -11.68700 -7.04100  1.000 14.81370 ? 226 THR A O      1 
ATOM   1744 C  CB     . THR A 1 233 ? -1.13300  -13.19700 -7.65900  1.000 13.26198 ? 226 THR A CB     1 
ATOM   1745 O  OG1    . THR A 1 233 ? -0.31900  -12.74800 -6.56500  1.000 12.99928 ? 226 THR A OG1    1 
ATOM   1746 C  CG2    . THR A 1 233 ? -0.30300  -14.05900 -8.64600  1.000 12.03472 ? 226 THR A CG2    1 
ATOM   1747 N  N      . ASP A 1 234 ? -2.03100  -10.21600 -6.68400  1.000 9.83908  ? 227 ASP A N      1 
ATOM   1748 C  CA     . ASP A 1 234 ? -2.72600  -9.49100  -5.62700  1.000 15.68143 ? 227 ASP A CA     1 
ATOM   1749 C  C      . ASP A 1 234 ? -2.02800  -8.14200  -5.47300  1.000 16.23479 ? 227 ASP A C      1 
ATOM   1750 O  O      . ASP A 1 234 ? -1.14400  -7.78900  -6.26100  1.000 12.48355 ? 227 ASP A O      1 
ATOM   1751 C  CB     . ASP A 1 234 ? -2.77700  -10.31400 -4.32400  1.000 15.52189 ? 227 ASP A CB     1 
ATOM   1752 C  CG     . ASP A 1 234 ? -1.38900  -10.64700 -3.76300  1.000 15.98601 ? 227 ASP A CG     1 
ATOM   1753 O  OD1    . ASP A 1 234 ? -0.40900  -9.94000  -4.10300  1.000 14.00548 ? 227 ASP A OD1    1 
ATOM   1754 O  OD2    . ASP A 1 234 ? -1.28200  -11.61000 -2.95900  1.000 13.78689 ? 227 ASP A OD2    1 
ATOM   1755 N  N      . HIS A 1 235 ? -2.42700  -7.38000  -4.45600  1.000 15.59526 ? 228 HIS A N      1 
ATOM   1756 C  CA     . HIS A 1 235 ? -1.91400  -6.02200  -4.30800  1.000 16.85697 ? 228 HIS A CA     1 
ATOM   1757 C  C      . HIS A 1 235 ? -0.39700  -6.00600  -4.12000  1.000 13.85018 ? 228 HIS A C      1 
ATOM   1758 O  O      . HIS A 1 235 ? 0.31600   -5.25100  -4.79300  1.000 14.34386 ? 228 HIS A O      1 
ATOM   1759 C  CB     . HIS A 1 235 ? -2.62400  -5.33500  -3.13900  1.000 17.28113 ? 228 HIS A CB     1 
ATOM   1760 C  CG     . HIS A 1 235 ? -1.96200  -4.07600  -2.68000  1.000 15.03299 ? 228 HIS A CG     1 
ATOM   1761 N  ND1    . HIS A 1 235 ? -2.34600  -2.83000  -3.12600  1.000 18.45480 ? 228 HIS A ND1    1 
ATOM   1762 C  CD2    . HIS A 1 235 ? -0.95600  -3.86700  -1.79500  1.000 17.59129 ? 228 HIS A CD2    1 
ATOM   1763 C  CE1    . HIS A 1 235 ? -1.59900  -1.90600  -2.54500  1.000 15.57193 ? 228 HIS A CE1    1 
ATOM   1764 N  NE2    . HIS A 1 235 ? -0.74900  -2.50900  -1.73000  1.000 17.96597 ? 228 HIS A NE2    1 
ATOM   1765 N  N      . ILE A 1 236 ? 0.12500   -6.82400  -3.19800  1.000 12.58984 ? 229 ILE A N      1 
ATOM   1766 C  CA     . ILE A 1 236 ? 1.54700   -6.71500  -2.89600  1.000 13.06232 ? 229 ILE A CA     1 
ATOM   1767 C  C      . ILE A 1 236 ? 2.38100   -7.32200  -4.02100  1.000 13.35347 ? 229 ILE A C      1 
ATOM   1768 O  O      . ILE A 1 236 ? 3.47400   -6.83100  -4.33000  1.000 11.79375 ? 229 ILE A O      1 
ATOM   1769 C  CB     . ILE A 1 236 ? 1.86300   -7.34400  -1.52100  1.000 14.52761 ? 229 ILE A CB     1 
ATOM   1770 C  CG1    . ILE A 1 236 ? 3.24200   -6.88100  -1.06000  1.000 17.94088 ? 229 ILE A CG1    1 
ATOM   1771 C  CG2    . ILE A 1 236 ? 1.75700   -8.86900  -1.55700  1.000 14.70030 ? 229 ILE A CG2    1 
ATOM   1772 C  CD1    . ILE A 1 236 ? 3.35600   -5.36300  -0.98000  1.000 23.32629 ? 229 ILE A CD1    1 
ATOM   1773 N  N      . ASP A 1 237 ? 1.87300   -8.37300  -4.66100  1.000 11.55256 ? 230 ASP A N      1 
ATOM   1774 C  CA     . ASP A 1 237 ? 2.54900   -8.96000  -5.81500  1.000 15.28492 ? 230 ASP A CA     1 
ATOM   1775 C  C      . ASP A 1 237 ? 2.65800   -7.95800  -6.96200  1.000 13.46472 ? 230 ASP A C      1 
ATOM   1776 O  O      . ASP A 1 237 ? 3.68100   -7.90000  -7.65700  1.000 14.33531 ? 230 ASP A O      1 
ATOM   1777 C  CB     . ASP A 1 237 ? 1.79400   -10.21300 -6.26400  1.000 13.76071 ? 230 ASP A CB     1 
ATOM   1778 C  CG     . ASP A 1 237 ? 2.60400   -11.08100 -7.20100  1.000 13.05835 ? 230 ASP A CG     1 
ATOM   1779 O  OD1    . ASP A 1 237 ? 3.71400   -11.50600 -6.81400  1.000 14.93484 ? 230 ASP A OD1    1 
ATOM   1780 O  OD2    . ASP A 1 237 ? 2.11700   -11.32300 -8.32300  1.000 10.73280 ? 230 ASP A OD2    1 
ATOM   1781 N  N      . GLN A 1 238 ? 1.60900   -7.17000  -7.18200  1.000 12.40586 ? 231 GLN A N      1 
ATOM   1782 C  CA     . GLN A 1 238 ? 1.65500   -6.14400  -8.21700  1.000 12.50546 ? 231 GLN A CA     1 
ATOM   1783 C  C      . GLN A 1 238 ? 2.82500   -5.19200  -7.98600  1.000 12.96247 ? 231 GLN A C      1 
ATOM   1784 O  O      . GLN A 1 238 ? 3.60700   -4.90100  -8.90400  1.000 11.61917 ? 231 GLN A O      1 
ATOM   1785 C  CB     . GLN A 1 238 ? 0.32900   -5.38300  -8.24100  1.000 11.10019 ? 231 GLN A CB     1 
ATOM   1786 C  CG     . GLN A 1 238 ? 0.21600   -4.43700  -9.42600  1.000 11.53132 ? 231 GLN A CG     1 
ATOM   1787 C  CD     . GLN A 1 238 ? 0.07200   -5.19700  -10.74000 1.000 13.81020 ? 231 GLN A CD     1 
ATOM   1788 O  OE1    . GLN A 1 238 ? -0.48300  -6.30300  -10.77200 1.000 12.85113 ? 231 GLN A OE1    1 
ATOM   1789 N  NE2    . GLN A 1 238 ? 0.57100   -4.60700  -11.83400 1.000 13.01088 ? 231 GLN A NE2    1 
ATOM   1790 N  N      . LEU A 1 239 ? 2.98000   -4.72000  -6.75100  1.000 11.89788 ? 232 LEU A N      1 
ATOM   1791 C  CA     . LEU A 1 239 ? 4.09000   -3.82600  -6.43400  1.000 13.48721 ? 232 LEU A CA     1 
ATOM   1792 C  C      . LEU A 1 239 ? 5.43600   -4.53800  -6.55500  1.000 12.35512 ? 232 LEU A C      1 
ATOM   1793 O  O      . LEU A 1 239 ? 6.42200   -3.94600  -7.01100  1.000 11.40729 ? 232 LEU A O      1 
ATOM   1794 C  CB     . LEU A 1 239 ? 3.90800   -3.26800  -5.02000  1.000 14.17052 ? 232 LEU A CB     1 
ATOM   1795 C  CG     . LEU A 1 239 ? 2.73700   -2.29500  -4.88900  1.000 12.50028 ? 232 LEU A CG     1 
ATOM   1796 C  CD1    . LEU A 1 239 ? 2.38300   -2.07900  -3.41900  1.000 20.41768 ? 232 LEU A CD1    1 
ATOM   1797 C  CD2    . LEU A 1 239 ? 3.08000   -0.97800  -5.57700  1.000 16.58022 ? 232 LEU A CD2    1 
ATOM   1798 N  N      . LYS A 1 240 ? 5.50200   -5.80300  -6.12900  1.000 13.13010 ? 233 LYS A N      1 
ATOM   1799 C  CA     . LYS A 1 240 ? 6.73800   -6.57300  -6.27100  1.000 12.58771 ? 233 LYS A CA     1 
ATOM   1800 C  C      . LYS A 1 240 ? 7.18900   -6.62600  -7.72400  1.000 12.69887 ? 233 LYS A C      1 
ATOM   1801 O  O      . LYS A 1 240 ? 8.36500   -6.40000  -8.03700  1.000 16.66056 ? 233 LYS A O      1 
ATOM   1802 C  CB     . LYS A 1 240 ? 6.53900   -7.99400  -5.73300  1.000 16.59699 ? 233 LYS A CB     1 
ATOM   1803 C  CG     . LYS A 1 240 ? 6.80700   -8.12600  -4.24400  1.000 23.22296 ? 233 LYS A CG     1 
ATOM   1804 C  CD     . LYS A 1 240 ? 5.92500   -9.20600  -3.59100  1.000 28.79041 ? 233 LYS A CD     1 
ATOM   1805 C  CE     . LYS A 1 240 ? 6.52200   -10.60300 -3.73000  1.000 29.55079 ? 233 LYS A CE     1 
ATOM   1806 N  NZ     . LYS A 1 240 ? 5.91900   -11.57900 -2.74500  1.000 27.47021 ? 233 LYS A NZ     1 
ATOM   1807 N  N      . LEU A 1 241 ? 6.27200   -6.96800  -8.62700  1.000 12.42383 ? 234 LEU A N      1 
ATOM   1808 C  CA     . LEU A 1 241 ? 6.61800   -7.05600  -10.04300 1.000 13.18144 ? 234 LEU A CA     1 
ATOM   1809 C  C      . LEU A 1 241 ? 7.04400   -5.70400  -10.60100 1.000 12.61926 ? 234 LEU A C      1 
ATOM   1810 O  O      . LEU A 1 241 ? 7.97800   -5.62300  -11.40500 1.000 13.44926 ? 234 LEU A O      1 
ATOM   1811 C  CB     . LEU A 1 241 ? 5.43500   -7.61300  -10.82800 1.000 12.03127 ? 234 LEU A CB     1 
ATOM   1812 C  CG     . LEU A 1 241 ? 4.95200   -9.01300  -10.44900 1.000 13.27704 ? 234 LEU A CG     1 
ATOM   1813 C  CD1    . LEU A 1 241 ? 3.87800   -9.46600  -11.43800 1.000 11.81991 ? 234 LEU A CD1    1 
ATOM   1814 C  CD2    . LEU A 1 241 ? 6.12000   -10.02600 -10.39200 1.000 11.65972 ? 234 LEU A CD2    1 
ATOM   1815 N  N      . ILE A 1 242 ? 6.36500   -4.62900  -10.19300 1.000 12.64627 ? 235 ILE A N      1 
ATOM   1816 C  CA     . ILE A 1 242 ? 6.72000   -3.29500  -10.68300 1.000 11.94352 ? 235 ILE A CA     1 
ATOM   1817 C  C      . ILE A 1 242 ? 8.15300   -2.95600  -10.29600 1.000 13.90215 ? 235 ILE A C      1 
ATOM   1818 O  O      . ILE A 1 242 ? 8.96600   -2.54800  -11.13900 1.000 13.87421 ? 235 ILE A O      1 
ATOM   1819 C  CB     . ILE A 1 242 ? 5.73000   -2.24800  -10.13800 1.000 11.59238 ? 235 ILE A CB     1 
ATOM   1820 C  CG1    . ILE A 1 242 ? 4.37800   -2.34300  -10.86400 1.000 11.51185 ? 235 ILE A CG1    1 
ATOM   1821 C  CG2    . ILE A 1 242 ? 6.34700   -0.84000  -10.20100 1.000 11.16573 ? 235 ILE A CG2    1 
ATOM   1822 C  CD1    . ILE A 1 242 ? 3.25900   -1.48100  -10.23600 1.000 12.59669 ? 235 ILE A CD1    1 
ATOM   1823 N  N      . LEU A 1 243 ? 8.49100   -3.13100  -9.00600  1.000 12.16706 ? 236 LEU A N      1 
ATOM   1824 C  CA     . LEU A 1 243 ? 9.82000   -2.75900  -8.52400  1.000 13.30265 ? 236 LEU A CA     1 
ATOM   1825 C  C      . LEU A 1 243 ? 10.91900  -3.58600  -9.18600  1.000 15.81421 ? 236 LEU A C      1 
ATOM   1826 O  O      . LEU A 1 243 ? 12.05600  -3.11700  -9.31100  1.000 13.39465 ? 236 LEU A O      1 
ATOM   1827 C  CB     . LEU A 1 243 ? 9.90800   -2.91700  -7.00400  1.000 14.21220 ? 236 LEU A CB     1 
ATOM   1828 C  CG     . LEU A 1 243 ? 9.04800   -1.95500  -6.17400  1.000 15.39261 ? 236 LEU A CG     1 
ATOM   1829 C  CD1    . LEU A 1 243 ? 9.39900   -2.06300  -4.69900  1.000 21.99582 ? 236 LEU A CD1    1 
ATOM   1830 C  CD2    . LEU A 1 243 ? 9.17800   -0.49800  -6.67200  1.000 20.73557 ? 236 LEU A CD2    1 
ATOM   1831 N  N      . ARG A 1 244 ? 10.62000  -4.81800  -9.58800  1.000 12.76805 ? 237 ARG A N      1 
ATOM   1832 C  CA     . ARG A 1 244 ? 11.64900  -5.62100  -10.24900 1.000 17.86210 ? 237 ARG A CA     1 
ATOM   1833 C  C      . ARG A 1 244 ? 12.04400  -5.03300  -11.59500 1.000 19.03126 ? 237 ARG A C      1 
ATOM   1834 O  O      . ARG A 1 244 ? 13.20900  -5.15900  -12.01000 1.000 17.09488 ? 237 ARG A O      1 
ATOM   1835 C  CB     . ARG A 1 244 ? 11.18100  -7.06500  -10.42400 1.000 18.98711 ? 237 ARG A CB     1 
ATOM   1836 C  CG     . ARG A 1 244 ? 11.19200  -7.83400  -9.11300  1.000 23.77941 ? 237 ARG A CG     1 
ATOM   1837 C  CD     . ARG A 1 244 ? 10.63000  -9.21600  -9.28100  1.000 27.27602 ? 237 ARG A CD     1 
ATOM   1838 N  NE     . ARG A 1 244 ? 11.50100  -10.06400 -10.08900 1.000 28.04729 ? 237 ARG A NE     1 
ATOM   1839 C  CZ     . ARG A 1 244 ? 11.20900  -11.31500 -10.41400 1.000 27.09899 ? 237 ARG A CZ     1 
ATOM   1840 N  NH1    . ARG A 1 244 ? 10.08700  -11.88700 -10.01000 1.000 24.55347 ? 237 ARG A NH1    1 
ATOM   1841 N  NH2    . ARG A 1 244 ? 12.05800  -12.00500 -11.17200 1.000 25.77116 ? 237 ARG A NH2    1 
ATOM   1842 N  N      . LEU A 1 245 ? 11.10600  -4.38200  -12.29000 1.000 15.63623 ? 238 LEU A N      1 
ATOM   1843 C  CA     . LEU A 1 245 ? 11.45600  -3.78800  -13.57700 1.000 15.92154 ? 238 LEU A CA     1 
ATOM   1844 C  C      . LEU A 1 245 ? 12.10300  -2.42200  -13.40700 1.000 17.97231 ? 238 LEU A C      1 
ATOM   1845 O  O      . LEU A 1 245 ? 13.16800  -2.16100  -13.97600 1.000 17.29094 ? 238 LEU A O      1 
ATOM   1846 C  CB     . LEU A 1 245 ? 10.22600  -3.66800  -14.48400 1.000 15.70586 ? 238 LEU A CB     1 
ATOM   1847 C  CG     . LEU A 1 245 ? 10.54500  -2.99600  -15.83500 1.000 18.95053 ? 238 LEU A CG     1 
ATOM   1848 C  CD1    . LEU A 1 245 ? 11.27100  -3.95000  -16.78100 1.000 18.89792 ? 238 LEU A CD1    1 
ATOM   1849 C  CD2    . LEU A 1 245 ? 9.32300   -2.38100  -16.51900 1.000 13.06466 ? 238 LEU A CD2    1 
ATOM   1850 N  N      . VAL A 1 246 ? 11.46200  -1.52400  -12.65200 1.000 13.23948 ? 239 VAL A N      1 
ATOM   1851 C  CA     . VAL A 1 246 ? 11.90400  -0.14200  -12.60100 1.000 14.02272 ? 239 VAL A CA     1 
ATOM   1852 C  C      . VAL A 1 246 ? 12.83300  0.12300   -11.43200 1.000 21.68802 ? 239 VAL A C      1 
ATOM   1853 O  O      . VAL A 1 246 ? 13.35800  1.23500   -11.31400 1.000 21.29699 ? 239 VAL A O      1 
ATOM   1854 C  CB     . VAL A 1 246 ? 10.70500  0.83200   -12.57700 1.000 19.69971 ? 239 VAL A CB     1 
ATOM   1855 C  CG1    . VAL A 1 246 ? 9.77300   0.53900   -13.75100 1.000 15.78987 ? 239 VAL A CG1    1 
ATOM   1856 C  CG2    . VAL A 1 246 ? 9.93300   0.73800   -11.24500 1.000 16.78200 ? 239 VAL A CG2    1 
ATOM   1857 N  N      . GLY A 1 247 ? 13.07600  -0.86700  -10.58500 1.000 16.56667 ? 240 GLY A N      1 
ATOM   1858 C  CA     . GLY A 1 247 ? 14.01300  -0.72600  -9.49300  1.000 18.74590 ? 240 GLY A CA     1 
ATOM   1859 C  C      . GLY A 1 247 ? 13.38400  -0.12900  -8.24600  1.000 23.42612 ? 240 GLY A C      1 
ATOM   1860 O  O      . GLY A 1 247 ? 12.32900  0.50300   -8.27900  1.000 18.64062 ? 240 GLY A O      1 
ATOM   1861 N  N      . THR A 1 248 ? 14.05800  -0.35500  -7.12100  1.000 22.97587 ? 241 THR A N      1 
ATOM   1862 C  CA     . THR A 1 248 ? 13.65300  0.27200   -5.87400  1.000 24.86776 ? 241 THR A CA     1 
ATOM   1863 C  C      . THR A 1 248 ? 13.87500  1.78900   -5.95200  1.000 25.33306 ? 241 THR A C      1 
ATOM   1864 O  O      . THR A 1 248 ? 14.75100  2.25900   -6.68400  1.000 21.42491 ? 241 THR A O      1 
ATOM   1865 C  CB     . THR A 1 248 ? 14.44000  -0.32400  -4.71200  1.000 29.76830 ? 241 THR A CB     1 
ATOM   1866 O  OG1    . THR A 1 248 ? 15.80500  -0.47100  -5.10500  1.000 33.49969 ? 241 THR A OG1    1 
ATOM   1867 C  CG2    . THR A 1 248 ? 13.90900  -1.70100  -4.36300  1.000 31.04234 ? 241 THR A CG2    1 
ATOM   1868 N  N      . PRO A 1 249 ? 13.08500  2.57400   -5.21400  1.000 23.03929 ? 242 PRO A N      1 
ATOM   1869 C  CA     . PRO A 1 249 ? 13.13100  4.03800   -5.36000  1.000 19.64826 ? 242 PRO A CA     1 
ATOM   1870 C  C      . PRO A 1 249 ? 14.52700  4.62800   -5.17000  1.000 27.10382 ? 242 PRO A C      1 
ATOM   1871 O  O      . PRO A 1 249 ? 15.30700  4.18500   -4.32200  1.000 23.42707 ? 242 PRO A O      1 
ATOM   1872 C  CB     . PRO A 1 249 ? 12.16800  4.52200   -4.27200  1.000 22.16213 ? 242 PRO A CB     1 
ATOM   1873 C  CG     . PRO A 1 249 ? 11.19900  3.38900   -4.11200  1.000 17.29482 ? 242 PRO A CG     1 
ATOM   1874 C  CD     . PRO A 1 249 ? 11.97800  2.13600   -4.34200  1.000 23.07014 ? 242 PRO A CD     1 
ATOM   1875 N  N      . GLY A 1 250 ? 14.82700  5.66900   -5.97100  1.000 22.91028 ? 243 GLY A N      1 
ATOM   1876 C  CA     . GLY A 1 250 ? 16.09900  6.36000   -5.89700  1.000 26.72066 ? 243 GLY A CA     1 
ATOM   1877 C  C      . GLY A 1 250 ? 16.11100  7.43800   -4.81900  1.000 28.37844 ? 243 GLY A C      1 
ATOM   1878 O  O      . GLY A 1 250 ? 15.08800  7.77600   -4.22900  1.000 24.84954 ? 243 GLY A O      1 
ATOM   1879 N  N      . ALA A 1 251 ? 17.30400  7.98400   -4.55700  1.000 29.49659 ? 244 ALA A N      1 
ATOM   1880 C  CA     . ALA A 1 251 ? 17.43000  8.96900   -3.48600  1.000 25.62665 ? 244 ALA A CA     1 
ATOM   1881 C  C      . ALA A 1 251 ? 16.51700  10.16500  -3.72700  1.000 26.48786 ? 244 ALA A C      1 
ATOM   1882 O  O      . ALA A 1 251 ? 15.87900  10.66200  -2.79100  1.000 26.54038 ? 244 ALA A O      1 
ATOM   1883 C  CB     . ALA A 1 251 ? 18.88700  9.41600   -3.33900  1.000 26.22939 ? 244 ALA A CB     1 
ATOM   1884 N  N      . GLU A 1 252 ? 16.41800  10.63000  -4.98000  1.000 23.61319 ? 245 GLU A N      1 
ATOM   1885 C  CA     . GLU A 1 252 ? 15.59500  11.80400  -5.26200  1.000 26.22770 ? 245 GLU A CA     1 
ATOM   1886 C  C      . GLU A 1 252 ? 14.12500  11.53800  -4.96300  1.000 24.02538 ? 245 GLU A C      1 
ATOM   1887 O  O      . GLU A 1 252 ? 13.40000  12.44100  -4.53000  1.000 24.11259 ? 245 GLU A O      1 
ATOM   1888 C  CB     . GLU A 1 252 ? 15.78000  12.25600  -6.71000  1.000 24.85283 ? 245 GLU A CB     1 
ATOM   1889 C  CG     . GLU A 1 252 ? 17.08900  13.01400  -6.93600  1.000 35.89190 ? 245 GLU A CG     1 
ATOM   1890 C  CD     . GLU A 1 252 ? 17.45700  13.92700  -5.76100  1.000 44.63265 ? 245 GLU A CD     1 
ATOM   1891 O  OE1    . GLU A 1 252 ? 17.01300  15.09600  -5.76000  1.000 49.66760 ? 245 GLU A OE1    1 
ATOM   1892 O  OE2    . GLU A 1 252 ? 18.19100  13.48400  -4.83900  1.000 43.14001 ? 245 GLU A OE2    1 
ATOM   1893 N  N      . LEU A 1 253 ? 13.66200  10.31100  -5.20900  1.000 25.79760 ? 246 LEU A N      1 
ATOM   1894 C  CA     . LEU A 1 253 ? 12.29400  9.94900   -4.85600  1.000 23.98078 ? 246 LEU A CA     1 
ATOM   1895 C  C      . LEU A 1 253 ? 12.13800  9.77700   -3.34900  1.000 19.96021 ? 246 LEU A C      1 
ATOM   1896 O  O      . LEU A 1 253 ? 11.17000  10.27100  -2.76500  1.000 20.46205 ? 246 LEU A O      1 
ATOM   1897 C  CB     . LEU A 1 253 ? 11.88800  8.67100   -5.59500  1.000 24.56896 ? 246 LEU A CB     1 
ATOM   1898 C  CG     . LEU A 1 253 ? 10.45100  8.16100   -5.44800  1.000 21.83701 ? 246 LEU A CG     1 
ATOM   1899 C  CD1    . LEU A 1 253 ? 9.42400   9.27500   -5.61300  1.000 20.83182 ? 246 LEU A CD1    1 
ATOM   1900 C  CD2    . LEU A 1 253 ? 10.20200  7.02400   -6.43900  1.000 18.73486 ? 246 LEU A CD2    1 
ATOM   1901 N  N      . LEU A 1 254 ? 13.08600  9.09100   -2.70200  1.000 22.74724 ? 247 LEU A N      1 
ATOM   1902 C  CA     . LEU A 1 254 ? 13.01000  8.89600   -1.25800  1.000 23.98901 ? 247 LEU A CA     1 
ATOM   1903 C  C      . LEU A 1 254 ? 12.91100  10.22400  -0.52200  1.000 25.68150 ? 247 LEU A C      1 
ATOM   1904 O  O      . LEU A 1 254 ? 12.35100  10.28200  0.57800   1.000 21.63775 ? 247 LEU A O      1 
ATOM   1905 C  CB     . LEU A 1 254 ? 14.22700  8.11700   -0.75900  1.000 25.46909 ? 247 LEU A CB     1 
ATOM   1906 C  CG     . LEU A 1 254 ? 14.22700  6.59600   -0.94500  1.000 32.99023 ? 247 LEU A CG     1 
ATOM   1907 C  CD1    . LEU A 1 254 ? 15.33500  5.96300   -0.12600  1.000 34.83055 ? 247 LEU A CD1    1 
ATOM   1908 C  CD2    . LEU A 1 254 ? 12.89300  5.99200   -0.56000  1.000 29.56658 ? 247 LEU A CD2    1 
ATOM   1909 N  N      . LYS A 1 255 ? 13.43500  11.29500  -1.12400  1.000 22.33173 ? 248 LYS A N      1 
ATOM   1910 C  CA     . LYS A 1 255 ? 13.41400  12.61100  -0.49900  1.000 24.33035 ? 248 LYS A CA     1 
ATOM   1911 C  C      . LYS A 1 255 ? 11.99200  13.10300  -0.28800  1.000 23.86004 ? 248 LYS A C      1 
ATOM   1912 O  O      . LYS A 1 255 ? 11.75000  13.96400  0.56500   1.000 18.67245 ? 248 LYS A O      1 
ATOM   1913 C  CB     . LYS A 1 255 ? 14.17100  13.61100  -1.37700  1.000 22.93724 ? 248 LYS A CB     1 
ATOM   1914 C  CG     . LYS A 1 255 ? 15.64400  13.79100  -1.05900  1.000 30.05336 ? 248 LYS A CG     1 
ATOM   1915 C  CD     . LYS A 1 255 ? 16.13600  15.10000  -1.66800  1.000 33.43301 ? 248 LYS A CD     1 
ATOM   1916 C  CE     . LYS A 1 255 ? 17.62300  15.06500  -2.01000  1.000 43.83251 ? 248 LYS A CE     1 
ATOM   1917 N  NZ     . LYS A 1 255 ? 18.04500  16.30400  -2.76000  1.000 39.80997 ? 248 LYS A NZ     1 
ATOM   1918 N  N      . LYS A 1 256 ? 11.05200  12.60900  -1.08800  1.000 19.43532 ? 249 LYS A N      1 
ATOM   1919 C  CA     . LYS A 1 256 ? 9.68900   13.11200  -1.08700  1.000 17.61013 ? 249 LYS A CA     1 
ATOM   1920 C  C      . LYS A 1 256 ? 8.75000   12.29500  -0.20300  1.000 17.38481 ? 249 LYS A C      1 
ATOM   1921 O  O      . LYS A 1 256 ? 7.55400   12.60100  -0.14500  1.000 17.84278 ? 249 LYS A O      1 
ATOM   1922 C  CB     . LYS A 1 256 ? 9.16200   13.14200  -2.52300  1.000 20.13697 ? 249 LYS A CB     1 
ATOM   1923 C  CG     . LYS A 1 256 ? 9.97300   14.06900  -3.43900  1.000 21.00865 ? 249 LYS A CG     1 
ATOM   1924 C  CD     . LYS A 1 256 ? 9.28200   14.23200  -4.77700  1.000 27.78349 ? 249 LYS A CD     1 
ATOM   1925 C  CE     . LYS A 1 256 ? 10.25800  14.10700  -5.92000  1.000 23.92919 ? 249 LYS A CE     1 
ATOM   1926 N  NZ     . LYS A 1 256 ? 9.54000   13.90400  -7.20600  1.000 29.39299 ? 249 LYS A NZ     1 
ATOM   1927 N  N      . ILE A 1 257 ? 9.25500   11.27900  0.48800   1.000 16.49911 ? 250 ILE A N      1 
ATOM   1928 C  CA     . ILE A 1 257 ? 8.42700   10.38600  1.29600   1.000 17.48091 ? 250 ILE A CA     1 
ATOM   1929 C  C      . ILE A 1 257 ? 8.57900   10.78700  2.76300   1.000 17.85551 ? 250 ILE A C      1 
ATOM   1930 O  O      . ILE A 1 257 ? 9.64500   10.61900  3.36300   1.000 19.27901 ? 250 ILE A O      1 
ATOM   1931 C  CB     . ILE A 1 257 ? 8.79400   8.91300   1.07100   1.000 17.64931 ? 250 ILE A CB     1 
ATOM   1932 C  CG1    . ILE A 1 257 ? 8.40600   8.49000   -0.34700  1.000 15.86071 ? 250 ILE A CG1    1 
ATOM   1933 C  CG2    . ILE A 1 257 ? 8.11400   8.02600   2.11400   1.000 18.39547 ? 250 ILE A CG2    1 
ATOM   1934 C  CD1    . ILE A 1 257 ? 8.97400   7.12800   -0.77900  1.000 16.81565 ? 250 ILE A CD1    1 
ATOM   1935 N  N      . SER A 1 258 ? 7.49300   11.28700  3.35600   1.000 16.49028 ? 251 SER A N      1 
ATOM   1936 C  CA     . SER A 1 258 ? 7.55900   11.83700  4.71000   1.000 20.19897 ? 251 SER A CA     1 
ATOM   1937 C  C      . SER A 1 258 ? 7.78100   10.75600  5.76500   1.000 21.38536 ? 251 SER A C      1 
ATOM   1938 O  O      . SER A 1 258 ? 8.57900   10.94000  6.69500   1.000 22.69420 ? 251 SER A O      1 
ATOM   1939 C  CB     . SER A 1 258 ? 6.27500   12.60000  5.01800   1.000 21.05398 ? 251 SER A CB     1 
ATOM   1940 O  OG     . SER A 1 258 ? 6.38700   13.24800  6.26300   1.000 23.97995 ? 251 SER A OG     1 
ATOM   1941 N  N      . SER A 1 259 ? 7.06900   9.63900   5.66200   1.000 16.48178 ? 252 SER A N      1 
ATOM   1942 C  CA     . SER A 1 259 ? 7.05200   8.63900   6.72900   1.000 19.10179 ? 252 SER A CA     1 
ATOM   1943 C  C      . SER A 1 259 ? 8.39800   7.92200   6.86100   1.000 19.93262 ? 252 SER A C      1 
ATOM   1944 O  O      . SER A 1 259 ? 8.86700   7.27700   5.91300   1.000 19.52645 ? 252 SER A O      1 
ATOM   1945 C  CB     . SER A 1 259 ? 5.94700   7.62000   6.46500   1.000 17.74356 ? 252 SER A CB     1 
ATOM   1946 O  OG     . SER A 1 259 ? 6.17000   6.45700   7.23900   1.000 18.81625 ? 252 SER A OG     1 
ATOM   1947 N  N      . GLU A 1 260 ? 8.99200   7.98800   8.06100   1.000 17.52341 ? 253 GLU A N      1 
ATOM   1948 C  CA     . GLU A 1 260 ? 10.26800  7.31400   8.29600   1.000 17.49899 ? 253 GLU A CA     1 
ATOM   1949 C  C      . GLU A 1 260 ? 10.11900  5.79600   8.26200   1.000 18.95461 ? 253 GLU A C      1 
ATOM   1950 O  O      . GLU A 1 260 ? 11.03500  5.09100   7.81500   1.000 19.24748 ? 253 GLU A O      1 
ATOM   1951 C  CB     . GLU A 1 260 ? 10.88300  7.75800   9.63200   1.000 22.10455 ? 253 GLU A CB     1 
ATOM   1952 C  CG     . GLU A 1 260 ? 11.01100  9.27400   9.78400   1.000 28.37769 ? 253 GLU A CG     1 
ATOM   1953 C  CD     . GLU A 1 260 ? 11.60600  9.69000   11.13100  1.000 34.00109 ? 253 GLU A CD     1 
ATOM   1954 O  OE1    . GLU A 1 260 ? 11.68700  8.83100   12.04000  1.000 37.52222 ? 253 GLU A OE1    1 
ATOM   1955 O  OE2    . GLU A 1 260 ? 11.99300  10.87400  11.26800  1.000 37.53281 ? 253 GLU A OE2    1 
ATOM   1956 N  N      . SER A 1 261 ? 8.98400   5.26600   8.73500   1.000 17.23251 ? 254 SER A N      1 
ATOM   1957 C  CA     . SER A 1 261 ? 8.79400   3.81600   8.70300   1.000 18.38457 ? 254 SER A CA     1 
ATOM   1958 C  C      . SER A 1 261 ? 8.64200   3.31900   7.27400   1.000 18.19889 ? 254 SER A C      1 
ATOM   1959 O  O      . SER A 1 261 ? 9.13300   2.23600   6.93200   1.000 19.97166 ? 254 SER A O      1 
ATOM   1960 C  CB     . SER A 1 261 ? 7.58300   3.41400   9.54700   1.000 18.10165 ? 254 SER A CB     1 
ATOM   1961 O  OG     . SER A 1 261 ? 6.43700   4.18100   9.20500   1.000 18.86185 ? 254 SER A OG     1 
ATOM   1962 N  N      . ALA A 1 262 ? 7.97400   4.10300   6.42200   1.000 15.64916 ? 255 ALA A N      1 
ATOM   1963 C  CA     . ALA A 1 262 ? 7.86300   3.72900   5.01600   1.000 18.57477 ? 255 ALA A CA     1 
ATOM   1964 C  C      . ALA A 1 262 ? 9.23400   3.70900   4.35300   1.000 16.23975 ? 255 ALA A C      1 
ATOM   1965 O  O      . ALA A 1 262 ? 9.56700   2.77000   3.62100   1.000 15.71834 ? 255 ALA A O      1 
ATOM   1966 C  CB     . ALA A 1 262 ? 6.91200   4.68000   4.28900   1.000 16.48768 ? 255 ALA A CB     1 
ATOM   1967 N  N      . ARG A 1 263 ? 10.04600  4.74500   4.60400   1.000 16.58486 ? 256 ARG A N      1 
ATOM   1968 C  CA     . ARG A 1 263 ? 11.40400  4.76900   4.07000   1.000 14.49581 ? 256 ARG A CA     1 
ATOM   1969 C  C      . ARG A 1 263 ? 12.22600  3.60800   4.61200   1.000 18.96881 ? 256 ARG A C      1 
ATOM   1970 O  O      . ARG A 1 263 ? 12.96400  2.95400   3.86600   1.000 17.34972 ? 256 ARG A O      1 
ATOM   1971 C  CB     . ARG A 1 263 ? 12.07700  6.10700   4.39900   1.000 18.23760 ? 256 ARG A CB     1 
ATOM   1972 C  CG     . ARG A 1 263 ? 11.40200  7.32600   3.78000   1.000 20.96235 ? 256 ARG A CG     1 
ATOM   1973 C  CD     . ARG A 1 263 ? 12.36300  8.52400   3.69700   1.000 18.61769 ? 256 ARG A CD     1 
ATOM   1974 N  NE     . ARG A 1 263 ? 13.00100  8.81800   4.97900   1.000 23.67578 ? 256 ARG A NE     1 
ATOM   1975 C  CZ     . ARG A 1 263 ? 12.42900  9.50200   5.96400   1.000 27.10685 ? 256 ARG A CZ     1 
ATOM   1976 N  NH1    . ARG A 1 263 ? 11.19500  9.97300   5.85900   1.000 23.61663 ? 256 ARG A NH1    1 
ATOM   1977 N  NH2    . ARG A 1 263 ? 13.11000  9.71600   7.08600   1.000 32.12559 ? 256 ARG A NH2    1 
ATOM   1978 N  N      . ASN A 1 264 ? 12.11400  3.33500   5.91600   1.000 20.03665 ? 257 ASN A N      1 
ATOM   1979 C  CA     . ASN A 1 264 ? 12.87100  2.22700   6.48900   1.000 21.37321 ? 257 ASN A CA     1 
ATOM   1980 C  C      . ASN A 1 264 ? 12.46000  0.91400   5.83600   1.000 22.23255 ? 257 ASN A C      1 
ATOM   1981 O  O      . ASN A 1 264 ? 13.31200  0.09200   5.47500   1.000 21.56870 ? 257 ASN A O      1 
ATOM   1982 C  CB     . ASN A 1 264 ? 12.66700  2.16200   8.00300   1.000 19.12667 ? 257 ASN A CB     1 
ATOM   1983 C  CG     . ASN A 1 264 ? 13.47700  1.05400   8.65300   1.000 28.84869 ? 257 ASN A CG     1 
ATOM   1984 O  OD1    . ASN A 1 264 ? 14.70200  1.10500   8.65500   1.000 23.26287 ? 257 ASN A OD1    1 
ATOM   1985 N  ND2    . ASN A 1 264 ? 12.79700  0.03100   9.17900   1.000 24.30412 ? 257 ASN A ND2    1 
ATOM   1986 N  N      . TYR A 1 265 ? 11.15400  0.70900   5.64200   1.000 20.66859 ? 258 TYR A N      1 
ATOM   1987 C  CA     . TYR A 1 265 ? 10.72200  -0.51300  4.97300   1.000 21.66722 ? 258 TYR A CA     1 
ATOM   1988 C  C      . TYR A 1 265 ? 11.34500  -0.62300  3.58900   1.000 23.09272 ? 258 TYR A C      1 
ATOM   1989 O  O      . TYR A 1 265 ? 11.90300  -1.66600  3.22800   1.000 23.19255 ? 258 TYR A O      1 
ATOM   1990 C  CB     . TYR A 1 265 ? 9.19600   -0.58800  4.87300   1.000 23.23229 ? 258 TYR A CB     1 
ATOM   1991 C  CG     . TYR A 1 265 ? 8.76900   -1.80100  4.08100   1.000 26.54562 ? 258 TYR A CG     1 
ATOM   1992 C  CD1    . TYR A 1 265 ? 8.64700   -3.05000  4.68600   1.000 32.75989 ? 258 TYR A CD1    1 
ATOM   1993 C  CD2    . TYR A 1 265 ? 8.50800   -1.70500  2.71600   1.000 28.66717 ? 258 TYR A CD2    1 
ATOM   1994 C  CE1    . TYR A 1 265 ? 8.27100   -4.17400  3.94400   1.000 33.90966 ? 258 TYR A CE1    1 
ATOM   1995 C  CE2    . TYR A 1 265 ? 8.13300   -2.81000  1.97900   1.000 25.56170 ? 258 TYR A CE2    1 
ATOM   1996 C  CZ     . TYR A 1 265 ? 8.01500   -4.04100  2.59500   1.000 33.14061 ? 258 TYR A CZ     1 
ATOM   1997 O  OH     . TYR A 1 265 ? 7.63400   -5.14100  1.85500   1.000 37.42267 ? 258 TYR A OH     1 
ATOM   1998 N  N      . ILE A 1 266 ? 11.26200  0.45000   2.79400   1.000 20.20719 ? 259 ILE A N      1 
ATOM   1999 C  CA     . ILE A 1 266 ? 11.86600  0.42900   1.46100   1.000 20.07113 ? 259 ILE A CA     1 
ATOM   2000 C  C      . ILE A 1 266 ? 13.35400  0.08500   1.53800   1.000 20.25364 ? 259 ILE A C      1 
ATOM   2001 O  O      . ILE A 1 266 ? 13.85400  -0.75200  0.77700   1.000 20.06429 ? 259 ILE A O      1 
ATOM   2002 C  CB     . ILE A 1 266 ? 11.63800  1.76700   0.72700   1.000 17.98550 ? 259 ILE A CB     1 
ATOM   2003 C  CG1    . ILE A 1 266 ? 10.18600  1.92300   0.26500   1.000 21.38004 ? 259 ILE A CG1    1 
ATOM   2004 C  CG2    . ILE A 1 266 ? 12.59600  1.88600   -0.46100  1.000 19.35583 ? 259 ILE A CG2    1 
ATOM   2005 C  CD1    . ILE A 1 266 ? 9.61900   3.32400   0.42400   1.000 20.59869 ? 259 ILE A CD1    1 
ATOM   2006 N  N      . GLN A 1 267 ? 14.09500  0.74800   2.42700   1.000 19.12457 ? 260 GLN A N      1 
ATOM   2007 C  CA     . GLN A 1 267 ? 15.52300  0.46200   2.48500   1.000 21.87456 ? 260 GLN A CA     1 
ATOM   2008 C  C      . GLN A 1 267 ? 15.80600  -0.94300  2.98800   1.000 21.06743 ? 260 GLN A C      1 
ATOM   2009 O  O      . GLN A 1 267 ? 16.91300  -1.44800  2.77200   1.000 23.38310 ? 260 GLN A O      1 
ATOM   2010 C  CB     . GLN A 1 267 ? 16.25900  1.47900   3.36600   1.000 21.85714 ? 260 GLN A CB     1 
ATOM   2011 C  CG     . GLN A 1 267 ? 16.08900  2.90900   2.94500   1.000 25.14245 ? 260 GLN A CG     1 
ATOM   2012 C  CD     . GLN A 1 267 ? 16.85000  3.85000   3.86900   1.000 41.74615 ? 260 GLN A CD     1 
ATOM   2013 O  OE1    . GLN A 1 267 ? 17.63000  3.40700   4.71800   1.000 35.10674 ? 260 GLN A OE1    1 
ATOM   2014 N  NE2    . GLN A 1 267 ? 16.61900  5.15000   3.71500   1.000 43.77778 ? 260 GLN A NE2    1 
ATOM   2015 N  N      . SER A 1 268 ? 14.82900  -1.58600  3.63700   1.000 19.51229 ? 261 SER A N      1 
ATOM   2016 C  CA     . SER A 1 268 ? 15.00400  -2.95400  4.11700   1.000 22.14725 ? 261 SER A CA     1 
ATOM   2017 C  C      . SER A 1 268 ? 14.81600  -3.99900  3.02400   1.000 28.25466 ? 261 SER A C      1 
ATOM   2018 O  O      . SER A 1 268 ? 15.19800  -5.16100  3.22500   1.000 25.62999 ? 261 SER A O      1 
ATOM   2019 C  CB     . SER A 1 268 ? 14.03100  -3.23300  5.26100   1.000 27.65574 ? 261 SER A CB     1 
ATOM   2020 O  OG     . SER A 1 268 ? 12.83300  -3.79100  4.75200   1.000 31.49206 ? 261 SER A OG     1 
ATOM   2021 N  N      . LEU A 1 269 ? 14.23300  -3.62700  1.88600   1.000 26.71991 ? 262 LEU A N      1 
ATOM   2022 C  CA     . LEU A 1 269 ? 14.12300  -4.56500  0.77800   1.000 30.08025 ? 262 LEU A CA     1 
ATOM   2023 C  C      . LEU A 1 269 ? 15.48700  -4.79300  0.13800   1.000 30.86488 ? 262 LEU A C      1 
ATOM   2024 O  O      . LEU A 1 269 ? 16.39600  -3.96200  0.23000   1.000 28.36790 ? 262 LEU A O      1 
ATOM   2025 C  CB     . LEU A 1 269 ? 13.12700  -4.06200  -0.27400  1.000 29.44969 ? 262 LEU A CB     1 
ATOM   2026 C  CG     . LEU A 1 269 ? 11.74600  -3.64200  0.23000   1.000 28.18256 ? 262 LEU A CG     1 
ATOM   2027 C  CD1    . LEU A 1 269 ? 11.04700  -2.73300  -0.77800  1.000 30.64735 ? 262 LEU A CD1    1 
ATOM   2028 C  CD2    . LEU A 1 269 ? 10.89900  -4.85400  0.55600   1.000 30.15538 ? 262 LEU A CD2    1 
ATOM   2029 N  N      . ALA A 1 270 ? 15.63200  -5.94900  -0.50600  1.000 34.38759 ? 263 ALA A N      1 
ATOM   2030 C  CA     . ALA A 1 270 ? 16.76900  -6.14200  -1.39600  1.000 31.76879 ? 263 ALA A CA     1 
ATOM   2031 C  C      . ALA A 1 270 ? 16.75200  -5.04800  -2.45600  1.000 32.31832 ? 263 ALA A C      1 
ATOM   2032 O  O      . ALA A 1 270 ? 15.77700  -4.91300  -3.20100  1.000 37.93877 ? 263 ALA A O      1 
ATOM   2033 C  CB     . ALA A 1 270 ? 16.71500  -7.52600  -2.04100  1.000 40.50684 ? 263 ALA A CB     1 
ATOM   2034 N  N      . GLN A 1 271 ? 17.81200  -4.24400  -2.49700  1.000 29.70449 ? 264 GLN A N      1 
ATOM   2035 C  CA     . GLN A 1 271 ? 17.87500  -3.12700  -3.42800  1.000 37.44105 ? 264 GLN A CA     1 
ATOM   2036 C  C      . GLN A 1 271 ? 17.99000  -3.63600  -4.86600  1.000 37.34833 ? 264 GLN A C      1 
ATOM   2037 O  O      . GLN A 1 271 ? 18.94700  -4.33500  -5.21600  1.000 38.38905 ? 264 GLN A O      1 
ATOM   2038 C  CB     . GLN A 1 271 ? 19.04600  -2.21800  -3.06000  1.000 34.73062 ? 264 GLN A CB     1 
ATOM   2039 C  CG     . GLN A 1 271 ? 18.84600  -1.45000  -1.73900  1.000 39.33337 ? 264 GLN A CG     1 
ATOM   2040 C  CD     . GLN A 1 271 ? 17.43200  -0.92000  -1.56500  1.000 32.67372 ? 264 GLN A CD     1 
ATOM   2041 O  OE1    . GLN A 1 271 ? 17.00100  -0.03900  -2.29600  1.000 36.26998 ? 264 GLN A OE1    1 
ATOM   2042 N  NE2    . GLN A 1 271 ? 16.68800  -1.49400  -0.62100  1.000 32.63700 ? 264 GLN A NE2    1 
ATOM   2043 N  N      . MET A 1 272 ? 17.02000  -3.26500  -5.70100  1.000 37.44176 ? 265 MET A N      1 
ATOM   2044 C  CA     . MET A 1 272 ? 16.94700  -3.70700  -7.08300  1.000 34.93249 ? 265 MET A CA     1 
ATOM   2045 C  C      . MET A 1 272 ? 17.26800  -2.54800  -8.00600  1.000 28.98705 ? 265 MET A C      1 
ATOM   2046 O  O      . MET A 1 272 ? 16.67600  -1.46900  -7.86300  1.000 28.97243 ? 265 MET A O      1 
ATOM   2047 C  CB     . MET A 1 272 ? 15.54700  -4.24600  -7.38800  1.000 37.39275 ? 265 MET A CB     1 
ATOM   2048 C  CG     . MET A 1 272 ? 15.10600  -5.33400  -6.43000  1.000 42.88337 ? 265 MET A CG     1 
ATOM   2049 S  SD     . MET A 1 272 ? 13.98600  -6.52400  -7.16900  1.000 52.79205 ? 265 MET A SD     1 
ATOM   2050 C  CE     . MET A 1 272 ? 14.97900  -8.02100  -7.15700  1.000 48.31951 ? 265 MET A CE     1 
ATOM   2051 N  N      . PRO A 1 273 ? 18.20300  -2.71700  -8.93300  1.000 32.57149 ? 266 PRO A N      1 
ATOM   2052 C  CA     . PRO A 1 273 ? 18.42800  -1.68900  -9.94700  1.000 32.93755 ? 266 PRO A CA     1 
ATOM   2053 C  C      . PRO A 1 273 ? 17.30000  -1.71200  -10.96500 1.000 29.95291 ? 266 PRO A C      1 
ATOM   2054 O  O      . PRO A 1 273 ? 16.62100  -2.72400  -11.15300 1.000 31.42641 ? 266 PRO A O      1 
ATOM   2055 C  CB     . PRO A 1 273 ? 19.75300  -2.11300  -10.59200 1.000 32.55736 ? 266 PRO A CB     1 
ATOM   2056 C  CG     . PRO A 1 273 ? 19.75600  -3.60200  -10.43900 1.000 29.10090 ? 266 PRO A CG     1 
ATOM   2057 C  CD     . PRO A 1 273 ? 19.09100  -3.87800  -9.11400  1.000 37.74269 ? 266 PRO A CD     1 
ATOM   2058 N  N      . LYS A 1 274 ? 17.09500  -0.58700  -11.63800 1.000 26.51045 ? 267 LYS A N      1 
ATOM   2059 C  CA     . LYS A 1 274 ? 16.14400  -0.63000  -12.73700 1.000 29.90592 ? 267 LYS A CA     1 
ATOM   2060 C  C      . LYS A 1 274 ? 16.74900  -1.46200  -13.85600 1.000 31.56336 ? 267 LYS A C      1 
ATOM   2061 O  O      . LYS A 1 274 ? 17.94700  -1.36000  -14.14100 1.000 29.71466 ? 267 LYS A O      1 
ATOM   2062 C  CB     . LYS A 1 274 ? 15.77200  0.76600   -13.23900 1.000 33.62920 ? 267 LYS A CB     1 
ATOM   2063 C  CG     . LYS A 1 274 ? 16.81700  1.48100   -14.05700 1.000 36.10786 ? 267 LYS A CG     1 
ATOM   2064 C  CD     . LYS A 1 274 ? 16.30000  2.85000   -14.47300 1.000 34.65048 ? 267 LYS A CD     1 
ATOM   2065 C  CE     . LYS A 1 274 ? 15.06400  2.73000   -15.35900 1.000 36.66166 ? 267 LYS A CE     1 
ATOM   2066 N  NZ     . LYS A 1 274 ? 15.34500  1.91400   -16.58800 1.000 34.91023 ? 267 LYS A NZ     1 
ATOM   2067 N  N      . MET A 1 275 ? 15.94000  -2.33800  -14.44400 1.000 23.28791 ? 268 MET A N      1 
ATOM   2068 C  CA     . MET A 1 275 ? 16.44800  -3.15000  -15.53800 1.000 21.62126 ? 268 MET A CA     1 
ATOM   2069 C  C      . MET A 1 275 ? 16.67900  -2.28600  -16.76800 1.000 22.76594 ? 268 MET A C      1 
ATOM   2070 O  O      . MET A 1 275 ? 16.16400  -1.16900  -16.88600 1.000 24.17148 ? 268 MET A O      1 
ATOM   2071 C  CB     . MET A 1 275 ? 15.48800  -4.30000  -15.85600 1.000 18.79782 ? 268 MET A CB     1 
ATOM   2072 C  CG     . MET A 1 275 ? 15.38800  -5.31800  -14.73900 1.000 20.93639 ? 268 MET A CG     1 
ATOM   2073 S  SD     . MET A 1 275 ? 14.20300  -6.61000  -15.12000 1.000 24.16740 ? 268 MET A SD     1 
ATOM   2074 C  CE     . MET A 1 275 ? 14.26300  -7.58700  -13.61600 1.000 22.72852 ? 268 MET A CE     1 
ATOM   2075 N  N      . ASN A 1 276 ? 17.47300  -2.80500  -17.69300 1.000 21.34270 ? 269 ASN A N      1 
ATOM   2076 C  CA     . ASN A 1 276 ? 17.76300  -2.06300  -18.91200 1.000 23.88223 ? 269 ASN A CA     1 
ATOM   2077 C  C      . ASN A 1 276 ? 16.64700  -2.40100  -19.89600 1.000 18.10447 ? 269 ASN A C      1 
ATOM   2078 O  O      . ASN A 1 276 ? 16.53200  -3.54500  -20.33600 1.000 20.16816 ? 269 ASN A O      1 
ATOM   2079 C  CB     . ASN A 1 276 ? 19.14200  -2.43000  -19.45200 1.000 29.35420 ? 269 ASN A CB     1 
ATOM   2080 C  CG     . ASN A 1 276 ? 19.27600  -2.16700  -20.93500 1.000 28.48188 ? 269 ASN A CG     1 
ATOM   2081 O  OD1    . ASN A 1 276 ? 18.87700  -1.10600  -21.41700 1.000 37.48564 ? 269 ASN A OD1    1 
ATOM   2082 N  ND2    . ASN A 1 276 ? 19.84300  -3.12100  -21.66700 1.000 35.72276 ? 269 ASN A ND2    1 
ATOM   2083 N  N      . PHE A 1 277 ? 15.78200  -1.42600  -20.19500 1.000 17.48385 ? 270 PHE A N      1 
ATOM   2084 C  CA     . PHE A 1 277 ? 14.61500  -1.72800  -21.01400 1.000 18.43455 ? 270 PHE A CA     1 
ATOM   2085 C  C      . PHE A 1 277 ? 15.02000  -2.28300  -22.37500 1.000 15.80616 ? 270 PHE A C      1 
ATOM   2086 O  O      . PHE A 1 277 ? 14.25900  -3.03900  -22.98800 1.000 16.30599 ? 270 PHE A O      1 
ATOM   2087 C  CB     . PHE A 1 277 ? 13.75100  -0.48100  -21.19600 1.000 18.76297 ? 270 PHE A CB     1 
ATOM   2088 C  CG     . PHE A 1 277 ? 12.85800  -0.17000  -20.02200 1.000 19.51714 ? 270 PHE A CG     1 
ATOM   2089 C  CD1    . PHE A 1 277 ? 13.26400  -0.45900  -18.72200 1.000 20.64746 ? 270 PHE A CD1    1 
ATOM   2090 C  CD2    . PHE A 1 277 ? 11.63600  0.44000   -20.21900 1.000 16.37368 ? 270 PHE A CD2    1 
ATOM   2091 C  CE1    . PHE A 1 277 ? 12.44400  -0.16100  -17.64100 1.000 18.54497 ? 270 PHE A CE1    1 
ATOM   2092 C  CE2    . PHE A 1 277 ? 10.82300  0.74900   -19.15800 1.000 15.35381 ? 270 PHE A CE2    1 
ATOM   2093 C  CZ     . PHE A 1 277 ? 11.22600  0.46000   -17.86700 1.000 18.08105 ? 270 PHE A CZ     1 
ATOM   2094 N  N      . ALA A 1 278 ? 16.19700  -1.89600  -22.88100 1.000 16.52799 ? 271 ALA A N      1 
ATOM   2095 C  CA     . ALA A 1 278 ? 16.65000  -2.42400  -24.16600 1.000 20.40549 ? 271 ALA A CA     1 
ATOM   2096 C  C      . ALA A 1 278 ? 16.80000  -3.94000  -24.11400 1.000 20.42967 ? 271 ALA A C      1 
ATOM   2097 O  O      . ALA A 1 278 ? 16.50900  -4.63500  -25.09600 1.000 21.82129 ? 271 ALA A O      1 
ATOM   2098 C  CB     . ALA A 1 278 ? 17.97100  -1.75500  -24.57700 1.000 20.56896 ? 271 ALA A CB     1 
ATOM   2099 N  N      . ASN A 1 279 ? 17.22900  -4.47800  -22.97300 1.000 20.91846 ? 272 ASN A N      1 
ATOM   2100 C  CA     . ASN A 1 279 ? 17.31900  -5.93000  -22.88000 1.000 24.37457 ? 272 ASN A CA     1 
ATOM   2101 C  C      . ASN A 1 279 ? 15.95400  -6.55400  -22.62700 1.000 25.94738 ? 272 ASN A C      1 
ATOM   2102 O  O      . ASN A 1 279 ? 15.64400  -7.61100  -23.19200 1.000 20.85090 ? 272 ASN A O      1 
ATOM   2103 C  CB     . ASN A 1 279 ? 18.31300  -6.32900  -21.79200 1.000 28.45407 ? 272 ASN A CB     1 
ATOM   2104 C  CG     . ASN A 1 279 ? 19.72800  -5.91400  -22.13600 1.000 37.90842 ? 272 ASN A CG     1 
ATOM   2105 O  OD1    . ASN A 1 279 ? 20.40300  -5.22800  -21.35900 1.000 41.25402 ? 272 ASN A OD1    1 
ATOM   2106 N  ND2    . ASN A 1 279 ? 20.18200  -6.31500  -23.31800 1.000 33.24063 ? 272 ASN A ND2    1 
ATOM   2107 N  N      . VAL A 1 280 ? 15.11700  -5.88900  -21.81800 1.000 20.09260 ? 273 VAL A N      1 
ATOM   2108 C  CA     . VAL A 1 280 ? 13.79000  -6.41800  -21.49500 1.000 19.50280 ? 273 VAL A CA     1 
ATOM   2109 C  C      . VAL A 1 280 ? 12.93200  -6.54500  -22.74800 1.000 21.36876 ? 273 VAL A C      1 
ATOM   2110 O  O      . VAL A 1 280 ? 12.25400  -7.55800  -22.95900 1.000 20.04459 ? 273 VAL A O      1 
ATOM   2111 C  CB     . VAL A 1 280 ? 13.09500  -5.52700  -20.44800 1.000 20.01090 ? 273 VAL A CB     1 
ATOM   2112 C  CG1    . VAL A 1 280 ? 11.70200  -6.06900  -20.13300 1.000 17.74621 ? 273 VAL A CG1    1 
ATOM   2113 C  CG2    . VAL A 1 280 ? 13.94600  -5.43100  -19.18300 1.000 18.19050 ? 273 VAL A CG2    1 
ATOM   2114 N  N      . PHE A 1 281 ? 12.89800  -5.49800  -23.57000 1.000 16.50603 ? 274 PHE A N      1 
ATOM   2115 C  CA     . PHE A 1 281 ? 12.08400  -5.47000  -24.78500 1.000 17.66812 ? 274 PHE A CA     1 
ATOM   2116 C  C      . PHE A 1 281 ? 12.90200  -5.77400  -26.03400 1.000 19.49513 ? 274 PHE A C      1 
ATOM   2117 O  O      . PHE A 1 281 ? 12.63500  -5.22100  -27.10700 1.000 17.88076 ? 274 PHE A O      1 
ATOM   2118 C  CB     . PHE A 1 281 ? 11.38400  -4.11600  -24.88900 1.000 14.59482 ? 274 PHE A CB     1 
ATOM   2119 C  CG     . PHE A 1 281 ? 10.45200  -3.85100  -23.75000 1.000 15.33552 ? 274 PHE A CG     1 
ATOM   2120 C  CD1    . PHE A 1 281 ? 9.31900   -4.63100  -23.57900 1.000 17.08477 ? 274 PHE A CD1    1 
ATOM   2121 C  CD2    . PHE A 1 281 ? 10.79100  -2.95000  -22.76100 1.000 18.95621 ? 274 PHE A CD2    1 
ATOM   2122 C  CE1    . PHE A 1 281 ? 8.46000   -4.42300  -22.51300 1.000 19.58439 ? 274 PHE A CE1    1 
ATOM   2123 C  CE2    . PHE A 1 281 ? 9.95800   -2.75300  -21.67200 1.000 18.34715 ? 274 PHE A CE2    1 
ATOM   2124 C  CZ     . PHE A 1 281 ? 8.78800   -3.48700  -21.55200 1.000 17.23231 ? 274 PHE A CZ     1 
ATOM   2125 N  N      . ILE A 1 282 ? 13.89500  -6.65700  -25.91200 1.000 18.25720 ? 275 ILE A N      1 
ATOM   2126 C  CA     . ILE A 1 282 ? 14.77600  -7.02700  -27.02000 1.000 21.15766 ? 275 ILE A CA     1 
ATOM   2127 C  C      . ILE A 1 282 ? 13.96500  -7.30100  -28.28700 1.000 17.73144 ? 275 ILE A C      1 
ATOM   2128 O  O      . ILE A 1 282 ? 13.01000  -8.08100  -28.27200 1.000 21.29033 ? 275 ILE A O      1 
ATOM   2129 C  CB     . ILE A 1 282 ? 15.63000  -8.25200  -26.63200 1.000 25.26628 ? 275 ILE A CB     1 
ATOM   2130 C  CG1    . ILE A 1 282 ? 16.78500  -8.46900  -27.62500 1.000 30.86604 ? 275 ILE A CG1    1 
ATOM   2131 C  CG2    . ILE A 1 282 ? 14.75400  -9.48900  -26.55900 1.000 24.16598 ? 275 ILE A CG2    1 
ATOM   2132 C  CD1    . ILE A 1 282 ? 17.53300  -7.21100  -28.01800 1.000 33.42008 ? 275 ILE A CD1    1 
ATOM   2133 N  N      . GLY A 1 283 ? 14.33800  -6.66100  -29.39100 1.000 20.50681 ? 276 GLY A N      1 
ATOM   2134 C  CA     . GLY A 1 283 ? 13.67100  -6.83700  -30.66000 1.000 26.01269 ? 276 GLY A CA     1 
ATOM   2135 C  C      . GLY A 1 283 ? 12.70900  -5.72400  -31.02000 1.000 27.13200 ? 276 GLY A C      1 
ATOM   2136 O  O      . GLY A 1 283 ? 12.35900  -5.57900  -32.20000 1.000 26.42254 ? 276 GLY A O      1 
ATOM   2137 N  N      . ALA A 1 284 ? 12.27900  -4.93300  -30.04400 1.000 20.07474 ? 277 ALA A N      1 
ATOM   2138 C  CA     . ALA A 1 284 ? 11.37100  -3.83200  -30.34300 1.000 19.98528 ? 277 ALA A CA     1 
ATOM   2139 C  C      . ALA A 1 284 ? 12.11400  -2.69100  -31.03700 1.000 17.63530 ? 277 ALA A C      1 
ATOM   2140 O  O      . ALA A 1 284 ? 13.34200  -2.57700  -30.98300 1.000 19.13906 ? 277 ALA A O      1 
ATOM   2141 C  CB     . ALA A 1 284 ? 10.71000  -3.31100  -29.06600 1.000 15.15998 ? 277 ALA A CB     1 
ATOM   2142 N  N      . ASN A 1 285 ? 11.34500  -1.83600  -31.69000 1.000 18.15577 ? 278 ASN A N      1 
ATOM   2143 C  CA     . ASN A 1 285 ? 11.85700  -0.58500  -32.22600 1.000 17.48990 ? 278 ASN A CA     1 
ATOM   2144 C  C      . ASN A 1 285 ? 12.59100  0.19400   -31.13100 1.000 17.66550 ? 278 ASN A C      1 
ATOM   2145 O  O      . ASN A 1 285 ? 11.99800  0.48600   -30.07900 1.000 18.91185 ? 278 ASN A O      1 
ATOM   2146 C  CB     . ASN A 1 285 ? 10.68100  0.22100   -32.78300 1.000 18.14617 ? 278 ASN A CB     1 
ATOM   2147 C  CG     . ASN A 1 285 ? 11.10500  1.47100   -33.53700 1.000 18.58569 ? 278 ASN A CG     1 
ATOM   2148 O  OD1    . ASN A 1 285 ? 12.19800  2.01600   -33.33400 1.000 15.51063 ? 278 ASN A OD1    1 
ATOM   2149 N  ND2    . ASN A 1 285 ? 10.21700  1.94100   -34.41800 1.000 17.96051 ? 278 ASN A ND2    1 
ATOM   2150 N  N      . PRO A 1 286 ? 13.86600  0.52700   -31.32300 1.000 17.27699 ? 279 PRO A N      1 
ATOM   2151 C  CA     . PRO A 1 286 ? 14.57800  1.30600   -30.29100 1.000 17.19158 ? 279 PRO A CA     1 
ATOM   2152 C  C      . PRO A 1 286 ? 13.85400  2.57700   -29.86900 1.000 14.98556 ? 279 PRO A C      1 
ATOM   2153 O  O      . PRO A 1 286 ? 13.92700  2.97500   -28.69700 1.000 16.15766 ? 279 PRO A O      1 
ATOM   2154 C  CB     . PRO A 1 286 ? 15.92300  1.62000   -30.97100 1.000 18.66614 ? 279 PRO A CB     1 
ATOM   2155 C  CG     . PRO A 1 286 ? 16.12400  0.48600   -31.91900 1.000 20.66325 ? 279 PRO A CG     1 
ATOM   2156 C  CD     . PRO A 1 286 ? 14.75000  0.13000   -32.43700 1.000 22.62130 ? 279 PRO A CD     1 
ATOM   2157 N  N      . LEU A 1 287 ? 13.17100  3.24300   -30.80000 1.000 15.41493 ? 280 LEU A N      1 
ATOM   2158 C  CA     . LEU A 1 287 ? 12.35500  4.39800   -30.42800 1.000 14.39706 ? 280 LEU A CA     1 
ATOM   2159 C  C      . LEU A 1 287 ? 11.20700  4.00200   -29.50900 1.000 14.41626 ? 280 LEU A C      1 
ATOM   2160 O  O      . LEU A 1 287 ? 10.82100  4.77700   -28.62400 1.000 15.05760 ? 280 LEU A O      1 
ATOM   2161 C  CB     . LEU A 1 287 ? 11.80500  5.08000   -31.68000 1.000 14.64043 ? 280 LEU A CB     1 
ATOM   2162 C  CG     . LEU A 1 287 ? 12.80500  5.92900   -32.47200 1.000 17.53288 ? 280 LEU A CG     1 
ATOM   2163 C  CD1    . LEU A 1 287 ? 12.12100  6.56200   -33.67300 1.000 18.69950 ? 280 LEU A CD1    1 
ATOM   2164 C  CD2    . LEU A 1 287 ? 13.42600  6.99800   -31.56400 1.000 18.39133 ? 280 LEU A CD2    1 
ATOM   2165 N  N      . ALA A 1 288 ? 10.60200  2.82700   -29.74200 1.000 13.46097 ? 281 ALA A N      1 
ATOM   2166 C  CA     . ALA A 1 288 ? 9.55900   2.36000   -28.82800 1.000 14.46917 ? 281 ALA A CA     1 
ATOM   2167 C  C      . ALA A 1 288 ? 10.12000  2.13700   -27.42700 1.000 15.30098 ? 281 ALA A C      1 
ATOM   2168 O  O      . ALA A 1 288 ? 9.46000   2.45100   -26.42200 1.000 14.03169 ? 281 ALA A O      1 
ATOM   2169 C  CB     . ALA A 1 288 ? 8.92000   1.07700   -29.36000 1.000 12.63563 ? 281 ALA A CB     1 
ATOM   2170 N  N      . VAL A 1 289 ? 11.34000  1.60400   -27.33900 1.000 13.04236 ? 282 VAL A N      1 
ATOM   2171 C  CA     . VAL A 1 289 ? 11.94800  1.36300   -26.03000 1.000 15.37536 ? 282 VAL A CA     1 
ATOM   2172 C  C      . VAL A 1 289 ? 12.23300  2.67900   -25.31500 1.000 13.99910 ? 282 VAL A C      1 
ATOM   2173 O  O      . VAL A 1 289 ? 12.03400  2.79000   -24.10300 1.000 13.32951 ? 282 VAL A O      1 
ATOM   2174 C  CB     . VAL A 1 289 ? 13.22400  0.51000   -26.17100 1.000 16.40903 ? 282 VAL A CB     1 
ATOM   2175 C  CG1    . VAL A 1 289 ? 13.88800  0.33000   -24.80700 1.000 17.02717 ? 282 VAL A CG1    1 
ATOM   2176 C  CG2    . VAL A 1 289 ? 12.90900  -0.83900  -26.78500 1.000 16.86155 ? 282 VAL A CG2    1 
ATOM   2177 N  N      . ASP A 1 290 ? 12.71400  3.69100   -26.04600 1.000 15.66740 ? 283 ASP A N      1 
ATOM   2178 C  CA     . ASP A 1 290 ? 12.94800  5.01400   -25.45700 1.000 15.12145 ? 283 ASP A CA     1 
ATOM   2179 C  C      . ASP A 1 290 ? 11.66500  5.60300   -24.87000 1.000 14.92016 ? 283 ASP A C      1 
ATOM   2180 O  O      . ASP A 1 290 ? 11.66200  6.14400   -23.75100 1.000 14.42067 ? 283 ASP A O      1 
ATOM   2181 C  CB     . ASP A 1 290 ? 13.52200  5.95000   -26.52200 1.000 16.60817 ? 283 ASP A CB     1 
ATOM   2182 C  CG     . ASP A 1 290 ? 13.81400  7.34200   -25.97900 1.000 18.98240 ? 283 ASP A CG     1 
ATOM   2183 O  OD1    . ASP A 1 290 ? 14.80400  7.50600   -25.23500 1.000 23.60063 ? 283 ASP A OD1    1 
ATOM   2184 O  OD2    . ASP A 1 290 ? 13.06500  8.28100   -26.30700 1.000 18.09415 ? 283 ASP A OD2    1 
ATOM   2185 N  N      . LEU A 1 291 ? 10.56000  5.51700   -25.61800 1.000 12.97327 ? 284 LEU A N      1 
ATOM   2186 C  CA     . LEU A 1 291 ? 9.30800   6.06400   -25.10800 1.000 13.68689 ? 284 LEU A CA     1 
ATOM   2187 C  C      . LEU A 1 291 ? 8.87100   5.32900   -23.84900 1.000 13.39762 ? 284 LEU A C      1 
ATOM   2188 O  O      . LEU A 1 291 ? 8.44700   5.95800   -22.87500 1.000 14.58771 ? 284 LEU A O      1 
ATOM   2189 C  CB     . LEU A 1 291 ? 8.22400   5.99900   -26.18400 1.000 13.63833 ? 284 LEU A CB     1 
ATOM   2190 C  CG     . LEU A 1 291 ? 6.90400   6.69100   -25.80700 1.000 13.46484 ? 284 LEU A CG     1 
ATOM   2191 C  CD1    . LEU A 1 291 ? 7.14600   8.17500   -25.46400 1.000 13.28569 ? 284 LEU A CD1    1 
ATOM   2192 C  CD2    . LEU A 1 291 ? 5.82500   6.51700   -26.89700 1.000 10.32741 ? 284 LEU A CD2    1 
ATOM   2193 N  N      . LEU A 1 292 ? 8.99300   3.99200   -23.83800 1.000 13.71790 ? 285 LEU A N      1 
ATOM   2194 C  CA     . LEU A 1 292 ? 8.60100   3.21500   -22.66000 1.000 12.64668 ? 285 LEU A CA     1 
ATOM   2195 C  C      . LEU A 1 292 ? 9.41000   3.61900   -21.43600 1.000 13.50000 ? 285 LEU A C      1 
ATOM   2196 O  O      . LEU A 1 292 ? 8.88000   3.68600   -20.31800 1.000 13.98866 ? 285 LEU A O      1 
ATOM   2197 C  CB     . LEU A 1 292 ? 8.78500   1.71200   -22.92400 1.000 12.49285 ? 285 LEU A CB     1 
ATOM   2198 C  CG     . LEU A 1 292 ? 7.67000   1.04200   -23.71800 1.000 11.92769 ? 285 LEU A CG     1 
ATOM   2199 C  CD1    . LEU A 1 292 ? 8.10500   -0.35900  -24.17900 1.000 14.95959 ? 285 LEU A CD1    1 
ATOM   2200 C  CD2    . LEU A 1 292 ? 6.37900   0.95600   -22.88600 1.000 12.98526 ? 285 LEU A CD2    1 
ATOM   2201 N  N      . GLU A 1 293 ? 10.71200  3.83300   -21.61400 1.000 11.99862 ? 286 GLU A N      1 
ATOM   2202 C  CA     . GLU A 1 293 ? 11.52500  4.31500   -20.50700 1.000 13.81250 ? 286 GLU A CA     1 
ATOM   2203 C  C      . GLU A 1 293 ? 11.02900  5.66300   -19.99600 1.000 15.67791 ? 286 GLU A C      1 
ATOM   2204 O  O      . GLU A 1 293 ? 11.20100  5.98300   -18.81300 1.000 18.25205 ? 286 GLU A O      1 
ATOM   2205 C  CB     . GLU A 1 293 ? 12.99900  4.41700   -20.92500 1.000 16.80461 ? 286 GLU A CB     1 
ATOM   2206 C  CG     . GLU A 1 293 ? 13.76800  3.15500   -20.62400 1.000 23.75850 ? 286 GLU A CG     1 
ATOM   2207 C  CD     . GLU A 1 293 ? 15.14600  3.13500   -21.23600 1.000 38.22333 ? 286 GLU A CD     1 
ATOM   2208 O  OE1    . GLU A 1 293 ? 15.39600  3.91600   -22.18500 1.000 36.90983 ? 286 GLU A OE1    1 
ATOM   2209 O  OE2    . GLU A 1 293 ? 15.97300  2.31500   -20.77500 1.000 41.73869 ? 286 GLU A OE2    1 
ATOM   2210 N  N      . LYS A 1 294 ? 10.41800  6.46400   -20.85600 1.000 12.17444 ? 287 LYS A N      1 
ATOM   2211 C  CA     . LYS A 1 294 ? 9.97700   7.78300   -20.43200 1.000 14.29261 ? 287 LYS A CA     1 
ATOM   2212 C  C      . LYS A 1 294 ? 8.60900   7.73300   -19.77300 1.000 15.52802 ? 287 LYS A C      1 
ATOM   2213 O  O      . LYS A 1 294 ? 8.22400   8.69200   -19.10500 1.000 11.57157 ? 287 LYS A O      1 
ATOM   2214 C  CB     . LYS A 1 294 ? 9.97100   8.74000   -21.63100 1.000 15.08603 ? 287 LYS A CB     1 
ATOM   2215 C  CG     . LYS A 1 294 ? 11.38400  9.11600   -22.11400 1.000 19.33888 ? 287 LYS A CG     1 
ATOM   2216 C  CD     . LYS A 1 294 ? 11.32700  10.20800  -23.18600 1.000 22.53200 ? 287 LYS A CD     1 
ATOM   2217 C  CE     . LYS A 1 294 ? 12.60800  10.32900  -23.99600 1.000 29.00505 ? 287 LYS A CE     1 
ATOM   2218 N  NZ     . LYS A 1 294 ? 13.78600  10.02700  -23.16400 1.000 25.48868 ? 287 LYS A NZ     1 
ATOM   2219 N  N      . MET A 1 295 ? 7.89500   6.61900   -19.92800 1.000 11.12203 ? 288 MET A N      1 
ATOM   2220 C  CA     . MET A 1 295 ? 6.54200   6.42300   -19.43900 1.000 12.99542 ? 288 MET A CA     1 
ATOM   2221 C  C      . MET A 1 295 ? 6.55200   5.68900   -18.10700 1.000 11.64791 ? 288 MET A C      1 
ATOM   2222 O  O      . MET A 1 295 ? 5.80600   6.06300   -17.19600 1.000 12.68167 ? 288 MET A O      1 
ATOM   2223 C  CB     . MET A 1 295 ? 5.77600   5.59400   -20.46600 1.000 10.03788 ? 288 MET A CB     1 
ATOM   2224 C  CG     . MET A 1 295 ? 5.50500   6.31700   -21.77200 1.000 11.25536 ? 288 MET A CG     1 
ATOM   2225 S  SD     . MET A 1 295 ? 4.20500   5.49000   -22.68900 1.000 17.77005 ? 288 MET A SD     1 
ATOM   2226 C  CE     . MET A 1 295 ? 3.64900   6.84000   -23.67700 1.000 17.72209 ? 288 MET A CE     1 
ATOM   2227 N  N      . LEU A 1 296 ? 7.37800   4.64400   -18.00000 1.000 12.01210 ? 289 LEU A N      1 
ATOM   2228 C  CA     . LEU A 1 296 ? 7.41100   3.74100   -16.84500 1.000 13.03030 ? 289 LEU A CA     1 
ATOM   2229 C  C      . LEU A 1 296 ? 8.51800   4.15200   -15.87000 1.000 14.97644 ? 289 LEU A C      1 
ATOM   2230 O  O      . LEU A 1 296 ? 9.45100   3.40500   -15.56100 1.000 18.53320 ? 289 LEU A O      1 
ATOM   2231 C  CB     . LEU A 1 296 ? 7.58800   2.29800   -17.31400 1.000 12.88377 ? 289 LEU A CB     1 
ATOM   2232 C  CG     . LEU A 1 296 ? 6.44600   1.78800   -18.19500 1.000 12.73954 ? 289 LEU A CG     1 
ATOM   2233 C  CD1    . LEU A 1 296 ? 6.70600   0.36500   -18.74900 1.000 9.93373  ? 289 LEU A CD1    1 
ATOM   2234 C  CD2    . LEU A 1 296 ? 5.09600   1.89200   -17.46300 1.000 12.94233 ? 289 LEU A CD2    1 
ATOM   2235 N  N      . VAL A 1 297 ? 8.41100   5.38700   -15.41400 1.000 14.29032 ? 290 VAL A N      1 
ATOM   2236 C  CA     . VAL A 1 297 ? 9.28800   5.94300   -14.39400 1.000 16.99863 ? 290 VAL A CA     1 
ATOM   2237 C  C      . VAL A 1 297 ? 8.52100   5.94100   -13.08500 1.000 16.58511 ? 290 VAL A C      1 
ATOM   2238 O  O      . VAL A 1 297 ? 7.35100   6.34400   -13.04300 1.000 15.32264 ? 290 VAL A O      1 
ATOM   2239 C  CB     . VAL A 1 297 ? 9.74400   7.36500   -14.76400 1.000 19.34060 ? 290 VAL A CB     1 
ATOM   2240 C  CG1    . VAL A 1 297 ? 10.76200  7.88200   -13.75500 1.000 20.29538 ? 290 VAL A CG1    1 
ATOM   2241 C  CG2    . VAL A 1 297 ? 10.33600  7.38500   -16.16800 1.000 21.64607 ? 290 VAL A CG2    1 
ATOM   2242 N  N      . LEU A 1 298 ? 9.16300   5.46700   -12.01700 1.000 13.83853 ? 291 LEU A N      1 
ATOM   2243 C  CA     . LEU A 1 298 ? 8.47800   5.37300   -10.73300 1.000 15.84281 ? 291 LEU A CA     1 
ATOM   2244 C  C      . LEU A 1 298 ? 7.99900   6.74700   -10.27700 1.000 14.22353 ? 291 LEU A C      1 
ATOM   2245 O  O      . LEU A 1 298 ? 6.82400   6.93700   -9.94000  1.000 13.79515 ? 291 LEU A O      1 
ATOM   2246 C  CB     . LEU A 1 298 ? 9.42100   4.74600   -9.70200  1.000 20.53528 ? 291 LEU A CB     1 
ATOM   2247 C  CG     . LEU A 1 298 ? 8.84300   3.94900   -8.53800  1.000 24.45617 ? 291 LEU A CG     1 
ATOM   2248 C  CD1    . LEU A 1 298 ? 7.66500   3.09100   -8.99700  1.000 17.39375 ? 291 LEU A CD1    1 
ATOM   2249 C  CD2    . LEU A 1 298 ? 9.92600   3.11100   -7.85000  1.000 23.48474 ? 291 LEU A CD2    1 
ATOM   2250 N  N      . ASP A 1 299 ? 8.90100   7.72400   -10.27700 1.000 12.20022 ? 292 ASP A N      1 
ATOM   2251 C  CA     . ASP A 1 299 ? 8.56700   9.09300   -9.88000  1.000 17.94766 ? 292 ASP A CA     1 
ATOM   2252 C  C      . ASP A 1 299 ? 7.59500   9.70400   -10.89100 1.000 15.49872 ? 292 ASP A C      1 
ATOM   2253 O  O      . ASP A 1 299 ? 7.97200   9.94800   -12.04000 1.000 15.66645 ? 292 ASP A O      1 
ATOM   2254 C  CB     . ASP A 1 299 ? 9.85500   9.90800   -9.79400  1.000 16.54725 ? 292 ASP A CB     1 
ATOM   2255 C  CG     . ASP A 1 299 ? 9.65400   11.25000  -9.14200  1.000 20.61663 ? 292 ASP A CG     1 
ATOM   2256 O  OD1    . ASP A 1 299 ? 8.48900   11.68300  -9.01700  1.000 17.92426 ? 292 ASP A OD1    1 
ATOM   2257 O  OD2    . ASP A 1 299 ? 10.66500  11.86400  -8.74800  1.000 22.76466 ? 292 ASP A OD2    1 
ATOM   2258 N  N      . SER A 1 300 ? 6.35000   9.97000   -10.47000 1.000 14.39639 ? 293 SER A N      1 
ATOM   2259 C  CA     . SER A 1 300 ? 5.33800   10.47600  -11.40200 1.000 14.99214 ? 293 SER A CA     1 
ATOM   2260 C  C      . SER A 1 300 ? 5.70100   11.84700  -11.95300 1.000 19.32972 ? 293 SER A C      1 
ATOM   2261 O  O      . SER A 1 300 ? 5.28900   12.19700  -13.06800 1.000 16.11549 ? 293 SER A O      1 
ATOM   2262 C  CB     . SER A 1 300 ? 3.96000   10.52700  -10.73000 1.000 16.53324 ? 293 SER A CB     1 
ATOM   2263 O  OG     . SER A 1 300 ? 3.88400   11.55300  -9.74700  1.000 18.22780 ? 293 SER A OG     1 
ATOM   2264 N  N      . ASP A 1 301 ? 6.47700   12.62900  -11.20100 1.000 15.94221 ? 294 ASP A N      1 
ATOM   2265 C  CA     . ASP A 1 301 ? 6.91100   13.94100  -11.66400 1.000 19.66506 ? 294 ASP A CA     1 
ATOM   2266 C  C      . ASP A 1 301 ? 7.84700   13.85500  -12.86600 1.000 15.96643 ? 294 ASP A C      1 
ATOM   2267 O  O      . ASP A 1 301 ? 7.99200   14.84500  -13.59600 1.000 20.86821 ? 294 ASP A O      1 
ATOM   2268 C  CB     . ASP A 1 301 ? 7.61800   14.69500  -10.53200 1.000 23.27636 ? 294 ASP A CB     1 
ATOM   2269 C  CG     . ASP A 1 301 ? 6.70200   14.98200  -9.35100  1.000 26.69636 ? 294 ASP A CG     1 
ATOM   2270 O  OD1    . ASP A 1 301 ? 5.53300   15.37800  -9.56900  1.000 30.73684 ? 294 ASP A OD1    1 
ATOM   2271 O  OD2    . ASP A 1 301 ? 7.16900   14.83800  -8.19900  1.000 31.65545 ? 294 ASP A OD2    1 
ATOM   2272 N  N      . LYS A 1 302 ? 8.48400   12.70600  -13.08600 1.000 16.17893 ? 295 LYS A N      1 
ATOM   2273 C  CA     . LYS A 1 302 ? 9.46500   12.53400  -14.15300 1.000 14.37573 ? 295 LYS A CA     1 
ATOM   2274 C  C      . LYS A 1 302 ? 8.91300   11.82200  -15.37500 1.000 16.36117 ? 295 LYS A C      1 
ATOM   2275 O  O      . LYS A 1 302 ? 9.65400   11.62900  -16.34600 1.000 13.92714 ? 295 LYS A O      1 
ATOM   2276 C  CB     . LYS A 1 302 ? 10.68400  11.75700  -13.63700 1.000 14.52741 ? 295 LYS A CB     1 
ATOM   2277 C  CG     . LYS A 1 302 ? 11.27000  12.31200  -12.34500 1.000 21.19773 ? 295 LYS A CG     1 
ATOM   2278 C  CD     . LYS A 1 302 ? 11.84300  13.68400  -12.54700 1.000 25.83897 ? 295 LYS A CD     1 
ATOM   2279 C  CE     . LYS A 1 302 ? 12.82600  14.02100  -11.41600 1.000 35.23664 ? 295 LYS A CE     1 
ATOM   2280 N  NZ     . LYS A 1 302 ? 13.86100  15.00200  -11.85200 1.000 38.50182 ? 295 LYS A NZ     1 
ATOM   2281 N  N      . ARG A 1 303 ? 7.64800   11.41100  -15.35400 1.000 13.26642 ? 296 ARG A N      1 
ATOM   2282 C  CA     . ARG A 1 303 ? 7.05300   10.74900  -16.50600 1.000 14.71758 ? 296 ARG A CA     1 
ATOM   2283 C  C      . ARG A 1 303 ? 6.71700   11.76900  -17.59400 1.000 12.56444 ? 296 ARG A C      1 
ATOM   2284 O  O      . ARG A 1 303 ? 6.38300   12.91600  -17.30800 1.000 11.12412 ? 296 ARG A O      1 
ATOM   2285 C  CB     . ARG A 1 303 ? 5.77300   10.01800  -16.08900 1.000 15.98281 ? 296 ARG A CB     1 
ATOM   2286 C  CG     . ARG A 1 303 ? 6.00100   8.78800   -15.22800 1.000 14.64071 ? 296 ARG A CG     1 
ATOM   2287 C  CD     . ARG A 1 303 ? 4.67700   8.29400   -14.66700 1.000 11.49223 ? 296 ARG A CD     1 
ATOM   2288 N  NE     . ARG A 1 303 ? 4.89000   7.47800   -13.47200 1.000 10.52718 ? 296 ARG A NE     1 
ATOM   2289 C  CZ     . ARG A 1 303 ? 3.97500   7.27300   -12.53200 1.000 12.14622 ? 296 ARG A CZ     1 
ATOM   2290 N  NH1    . ARG A 1 303 ? 2.72900   7.70800   -12.67000 1.000 10.96675 ? 296 ARG A NH1    1 
ATOM   2291 N  NH2    . ARG A 1 303 ? 4.31900   6.61700   -11.42200 1.000 11.40761 ? 296 ARG A NH2    1 
ATOM   2292 N  N      . ILE A 1 304 ? 6.77400   11.32000  -18.85300 1.000 11.71679 ? 297 ILE A N      1 
ATOM   2293 C  CA     . ILE A 1 304 ? 6.41700   12.16000  -19.99500 1.000 9.71499  ? 297 ILE A CA     1 
ATOM   2294 C  C      . ILE A 1 304 ? 4.91400   12.46700  -19.98800 1.000 11.41532 ? 297 ILE A C      1 
ATOM   2295 O  O      . ILE A 1 304 ? 4.09400   11.63000  -19.58700 1.000 10.75012 ? 297 ILE A O      1 
ATOM   2296 C  CB     . ILE A 1 304 ? 6.86800   11.44300  -21.28400 1.000 11.49221 ? 297 ILE A CB     1 
ATOM   2297 C  CG1    . ILE A 1 304 ? 6.79500   12.35900  -22.49900 1.000 11.19229 ? 297 ILE A CG1    1 
ATOM   2298 C  CG2    . ILE A 1 304 ? 6.06800   10.13000  -21.51700 1.000 12.72105 ? 297 ILE A CG2    1 
ATOM   2299 C  CD1    . ILE A 1 304 ? 7.58200   11.82200  -23.67100 1.000 13.49539 ? 297 ILE A CD1    1 
ATOM   2300 N  N      . THR A 1 305 ? 4.53700   13.67700  -20.42700 1.000 10.77303 ? 298 THR A N      1 
ATOM   2301 C  CA     . THR A 1 305 ? 3.12000   14.02000  -20.55000 1.000 12.33015 ? 298 THR A CA     1 
ATOM   2302 C  C      . THR A 1 305 ? 2.54700   13.52100  -21.87500 1.000 10.50632 ? 298 THR A C      1 
ATOM   2303 O  O      . THR A 1 305 ? 3.27000   13.14400  -22.79900 1.000 10.92318 ? 298 THR A O      1 
ATOM   2304 C  CB     . THR A 1 305 ? 2.89100   15.53400  -20.44500 1.000 11.97237 ? 298 THR A CB     1 
ATOM   2305 O  OG1    . THR A 1 305 ? 3.39400   16.16800  -21.63200 1.000 9.03800  ? 298 THR A OG1    1 
ATOM   2306 C  CG2    . THR A 1 305 ? 3.60400   16.11000  -19.21100 1.000 13.83568 ? 298 THR A CG2    1 
ATOM   2307 N  N      . ALA A 1 306 ? 1.21400   13.53000  -21.97700 1.000 9.75672  ? 299 ALA A N      1 
ATOM   2308 C  CA     . ALA A 1 306 ? 0.59500   13.12500  -23.23600 1.000 12.65987 ? 299 ALA A CA     1 
ATOM   2309 C  C      . ALA A 1 306 ? 1.07300   14.00600  -24.39200 1.000 12.94224 ? 299 ALA A C      1 
ATOM   2310 O  O      . ALA A 1 306 ? 1.43400   13.50500  -25.46400 1.000 11.16777 ? 299 ALA A O      1 
ATOM   2311 C  CB     . ALA A 1 306 ? -0.93300  13.17100  -23.11900 1.000 10.74203 ? 299 ALA A CB     1 
ATOM   2312 N  N      . ALA A 1 307 ? 1.04700   15.33000  -24.20100 1.000 9.99226  ? 300 ALA A N      1 
ATOM   2313 C  CA     . ALA A 1 307 ? 1.46800   16.24400  -25.26700 1.000 12.11696 ? 300 ALA A CA     1 
ATOM   2314 C  C      . ALA A 1 307 ? 2.92700   16.01700  -25.65400 1.000 13.67044 ? 300 ALA A C      1 
ATOM   2315 O  O      . ALA A 1 307 ? 3.26800   15.98600  -26.84500 1.000 13.71759 ? 300 ALA A O      1 
ATOM   2316 C  CB     . ALA A 1 307 ? 1.24400   17.70300  -24.83700 1.000 10.22095 ? 300 ALA A CB     1 
ATOM   2317 N  N      . GLN A 1 308 ? 3.80800   15.86000  -24.66100 1.000 14.41001 ? 301 GLN A N      1 
ATOM   2318 C  CA     . GLN A 1 308 ? 5.20500   15.57200  -24.96400 1.000 12.15774 ? 301 GLN A CA     1 
ATOM   2319 C  C      . GLN A 1 308 ? 5.34000   14.26500  -25.72700 1.000 14.01149 ? 301 GLN A C      1 
ATOM   2320 O  O      . GLN A 1 308 ? 6.13200   14.16900  -26.67600 1.000 12.24209 ? 301 GLN A O      1 
ATOM   2321 C  CB     . GLN A 1 308 ? 6.03000   15.51500  -23.68200 1.000 11.91412 ? 301 GLN A CB     1 
ATOM   2322 C  CG     . GLN A 1 308 ? 6.19100   16.86300  -23.01800 1.000 12.45456 ? 301 GLN A CG     1 
ATOM   2323 C  CD     . GLN A 1 308 ? 6.69800   16.76000  -21.59800 1.000 18.28514 ? 301 GLN A CD     1 
ATOM   2324 O  OE1    . GLN A 1 308 ? 6.72800   15.67500  -21.00600 1.000 12.65210 ? 301 GLN A OE1    1 
ATOM   2325 N  NE2    . GLN A 1 308 ? 7.12100   17.89100  -21.04500 1.000 19.64047 ? 301 GLN A NE2    1 
ATOM   2326 N  N      . ALA A 1 309 ? 4.58200   13.24300  -25.32300 1.000 11.00523 ? 302 ALA A N      1 
ATOM   2327 C  CA     . ALA A 1 309 ? 4.71900   11.93600  -25.96300 1.000 13.28377 ? 302 ALA A CA     1 
ATOM   2328 C  C      . ALA A 1 309 ? 4.27800   11.99300  -27.42000 1.000 13.38935 ? 302 ALA A C      1 
ATOM   2329 O  O      . ALA A 1 309 ? 4.88000   11.33900  -28.28500 1.000 14.82449 ? 302 ALA A O      1 
ATOM   2330 C  CB     . ALA A 1 309 ? 3.92500   10.88400  -25.17500 1.000 10.83425 ? 302 ALA A CB     1 
ATOM   2331 N  N      . LEU A 1 310 ? 3.24600   12.78800  -27.72000 1.000 11.52804 ? 303 LEU A N      1 
ATOM   2332 C  CA     . LEU A 1 310 ? 2.78200   12.89500  -29.10600 1.000 13.05881 ? 303 LEU A CA     1 
ATOM   2333 C  C      . LEU A 1 310 ? 3.86500   13.46200  -30.02600 1.000 14.48636 ? 303 LEU A C      1 
ATOM   2334 O  O      . LEU A 1 310 ? 3.86100   13.19100  -31.23600 1.000 13.03130 ? 303 LEU A O      1 
ATOM   2335 C  CB     . LEU A 1 310 ? 1.51700   13.76300  -29.17600 1.000 11.57521 ? 303 LEU A CB     1 
ATOM   2336 C  CG     . LEU A 1 310 ? 0.18100   13.15900  -28.70500 1.000 11.71242 ? 303 LEU A CG     1 
ATOM   2337 C  CD1    . LEU A 1 310 ? -0.90000  14.25800  -28.44800 1.000 7.91576  ? 303 LEU A CD1    1 
ATOM   2338 C  CD2    . LEU A 1 310 ? -0.35500  12.12500  -29.72200 1.000 10.45222 ? 303 LEU A CD2    1 
ATOM   2339 N  N      . ALA A 1 311 ? 4.78000   14.26700  -29.49000 1.000 13.00401 ? 304 ALA A N      1 
ATOM   2340 C  CA     . ALA A 1 311 ? 5.87800   14.82000  -30.28200 1.000 15.07503 ? 304 ALA A CA     1 
ATOM   2341 C  C      . ALA A 1 311 ? 7.12500   13.93200  -30.29300 1.000 18.49550 ? 304 ALA A C      1 
ATOM   2342 O  O      . ALA A 1 311 ? 8.15200   14.32700  -30.86100 1.000 17.40962 ? 304 ALA A O      1 
ATOM   2343 C  CB     . ALA A 1 311 ? 6.24800   16.21900  -29.76500 1.000 14.59768 ? 304 ALA A CB     1 
ATOM   2344 N  N      . HIS A 1 312 ? 7.06800   12.76000  -29.66700 1.000 15.03651 ? 305 HIS A N      1 
ATOM   2345 C  CA     . HIS A 1 312 ? 8.19600   11.83900  -29.64700 1.000 15.40294 ? 305 HIS A CA     1 
ATOM   2346 C  C      . HIS A 1 312 ? 8.40300   11.24500  -31.04200 1.000 14.14143 ? 305 HIS A C      1 
ATOM   2347 O  O      . HIS A 1 312 ? 7.45100   11.01100  -31.78700 1.000 15.39313 ? 305 HIS A O      1 
ATOM   2348 C  CB     . HIS A 1 312 ? 7.94000   10.74200  -28.60400 1.000 14.47757 ? 305 HIS A CB     1 
ATOM   2349 C  CG     . HIS A 1 312 ? 9.10000   9.81700   -28.36900 1.000 15.50653 ? 305 HIS A CG     1 
ATOM   2350 N  ND1    . HIS A 1 312 ? 9.42500   8.79400   -29.23600 1.000 14.04666 ? 305 HIS A ND1    1 
ATOM   2351 C  CD2    . HIS A 1 312 ? 9.99000   9.74200   -27.35100 1.000 13.25577 ? 305 HIS A CD2    1 
ATOM   2352 C  CE1    . HIS A 1 312 ? 10.47400  8.13800   -28.76700 1.000 14.77215 ? 305 HIS A CE1    1 
ATOM   2353 N  NE2    . HIS A 1 312 ? 10.83200  8.68600   -27.61900 1.000 14.42096 ? 305 HIS A NE2    1 
ATOM   2354 N  N      . ALA A 1 313 ? 9.66600   11.02200  -31.40500 1.000 16.82410 ? 306 ALA A N      1 
ATOM   2355 C  CA     . ALA A 1 313 ? 9.98200   10.54800  -32.75400 1.000 17.31878 ? 306 ALA A CA     1 
ATOM   2356 C  C      . ALA A 1 313 ? 9.30900   9.21500   -33.09000 1.000 17.40392 ? 306 ALA A C      1 
ATOM   2357 O  O      . ALA A 1 313 ? 9.19100   8.86700   -34.27100 1.000 18.51498 ? 306 ALA A O      1 
ATOM   2358 C  CB     . ALA A 1 313 ? 11.49800  10.43000  -32.92000 1.000 18.36291 ? 306 ALA A CB     1 
ATOM   2359 N  N      . TYR A 1 314 ? 8.84900   8.46300   -32.09600 1.000 14.27065 ? 307 TYR A N      1 
ATOM   2360 C  CA     . TYR A 1 314 ? 8.19600   7.18600   -32.39800 1.000 13.93696 ? 307 TYR A CA     1 
ATOM   2361 C  C      . TYR A 1 314 ? 6.91300   7.39400   -33.19300 1.000 15.05500 ? 307 TYR A C      1 
ATOM   2362 O  O      . TYR A 1 314 ? 6.50700   6.50700   -33.95800 1.000 13.86944 ? 307 TYR A O      1 
ATOM   2363 C  CB     . TYR A 1 314 ? 7.90800   6.42500   -31.09500 1.000 13.90687 ? 307 TYR A CB     1 
ATOM   2364 C  CG     . TYR A 1 314 ? 7.30500   5.03100   -31.24100 1.000 12.30640 ? 307 TYR A CG     1 
ATOM   2365 C  CD1    . TYR A 1 314 ? 7.95400   4.04000   -31.98400 1.000 15.94587 ? 307 TYR A CD1    1 
ATOM   2366 C  CD2    . TYR A 1 314 ? 6.09600   4.70200   -30.62600 1.000 12.69563 ? 307 TYR A CD2    1 
ATOM   2367 C  CE1    . TYR A 1 314 ? 7.42600   2.76500   -32.10400 1.000 14.88811 ? 307 TYR A CE1    1 
ATOM   2368 C  CE2    . TYR A 1 314 ? 5.55000   3.41700   -30.73900 1.000 13.76792 ? 307 TYR A CE2    1 
ATOM   2369 C  CZ     . TYR A 1 314 ? 6.22400   2.45800   -31.48300 1.000 15.59752 ? 307 TYR A CZ     1 
ATOM   2370 O  OH     . TYR A 1 314 ? 5.71200   1.19100   -31.61600 1.000 14.39697 ? 307 TYR A OH     1 
ATOM   2371 N  N      . PHE A 1 315 ? 6.26200   8.55400   -33.04700 1.000 14.17158 ? 308 PHE A N      1 
ATOM   2372 C  CA     . PHE A 1 315 ? 5.00300   8.82800   -33.73600 1.000 12.94422 ? 308 PHE A CA     1 
ATOM   2373 C  C      . PHE A 1 315 ? 5.16400   9.73700   -34.95400 1.000 13.79064 ? 308 PHE A C      1 
ATOM   2374 O  O      . PHE A 1 315 ? 4.17400   10.30500  -35.43400 1.000 13.65206 ? 308 PHE A O      1 
ATOM   2375 C  CB     . PHE A 1 315 ? 3.98700   9.42300   -32.76100 1.000 12.15223 ? 308 PHE A CB     1 
ATOM   2376 C  CG     . PHE A 1 315 ? 3.76400   8.56200   -31.55000 1.000 12.33204 ? 308 PHE A CG     1 
ATOM   2377 C  CD1    . PHE A 1 315 ? 3.16400   7.31300   -31.68100 1.000 10.89592 ? 308 PHE A CD1    1 
ATOM   2378 C  CD2    . PHE A 1 315 ? 4.15500   8.99800   -30.29400 1.000 11.13654 ? 308 PHE A CD2    1 
ATOM   2379 C  CE1    . PHE A 1 315 ? 2.95100   6.50500   -30.57800 1.000 14.13015 ? 308 PHE A CE1    1 
ATOM   2380 C  CE2    . PHE A 1 315 ? 3.95600   8.18900   -29.18000 1.000 11.63677 ? 308 PHE A CE2    1 
ATOM   2381 C  CZ     . PHE A 1 315 ? 3.37200   6.94500   -29.31900 1.000 9.46825  ? 308 PHE A CZ     1 
ATOM   2382 N  N      . ALA A 1 316 ? 6.37700   9.85600   -35.49200 1.000 16.00988 ? 309 ALA A N      1 
ATOM   2383 C  CA     . ALA A 1 316 ? 6.59000   10.78600  -36.59900 1.000 19.01537 ? 309 ALA A CA     1 
ATOM   2384 C  C      . ALA A 1 316 ? 5.62400   10.54500  -37.75600 1.000 17.57714 ? 309 ALA A C      1 
ATOM   2385 O  O      . ALA A 1 316 ? 5.20800   11.49900  -38.42200 1.000 17.28565 ? 309 ALA A O      1 
ATOM   2386 C  CB     . ALA A 1 316 ? 8.03700   10.69400  -37.09800 1.000 21.39155 ? 309 ALA A CB     1 
ATOM   2387 N  N      . GLN A 1 317 ? 5.25400   9.28800   -38.01400 1.000 19.53224 ? 310 GLN A N      1 
ATOM   2388 C  CA     . GLN A 1 317 ? 4.38700   9.00000   -39.15200 1.000 19.89154 ? 310 GLN A CA     1 
ATOM   2389 C  C      . GLN A 1 317 ? 2.95700   9.48000   -38.93300 1.000 19.97898 ? 310 GLN A C      1 
ATOM   2390 O  O      . GLN A 1 317 ? 2.22100   9.64700   -39.91100 1.000 14.17876 ? 310 GLN A O      1 
ATOM   2391 C  CB     . GLN A 1 317 ? 4.37700   7.49900   -39.47400 1.000 22.40224 ? 310 GLN A CB     1 
ATOM   2392 C  CG     . GLN A 1 317 ? 5.77300   6.92900   -39.75300 1.000 31.18983 ? 310 GLN A CG     1 
ATOM   2393 C  CD     . GLN A 1 317 ? 6.55000   7.74400   -40.78700 1.000 41.30095 ? 310 GLN A CD     1 
ATOM   2394 O  OE1    . GLN A 1 317 ? 6.03500   8.08400   -41.86600 1.000 39.36562 ? 310 GLN A OE1    1 
ATOM   2395 N  NE2    . GLN A 1 317 ? 7.79000   8.08000   -40.45100 1.000 41.71619 ? 310 GLN A NE2    1 
ATOM   2396 N  N      . TYR A 1 318 ? 2.55800   9.74100   -37.68200 1.000 14.54307 ? 311 TYR A N      1 
ATOM   2397 C  CA     . TYR A 1 318 ? 1.17000   10.04400  -37.35400 1.000 13.90709 ? 311 TYR A CA     1 
ATOM   2398 C  C      . TYR A 1 318 ? 0.94300   11.41400  -36.72600 1.000 14.60606 ? 311 TYR A C      1 
ATOM   2399 O  O      . TYR A 1 318 ? -0.18700  11.90900  -36.78400 1.000 14.42433 ? 311 TYR A O      1 
ATOM   2400 C  CB     . TYR A 1 318 ? 0.59800   8.97200   -36.40500 1.000 14.55600 ? 311 TYR A CB     1 
ATOM   2401 C  CG     . TYR A 1 318 ? 0.54700   7.61900   -37.06600 1.000 16.39041 ? 311 TYR A CG     1 
ATOM   2402 C  CD1    . TYR A 1 318 ? -0.41300  7.33800   -38.03500 1.000 19.05697 ? 311 TYR A CD1    1 
ATOM   2403 C  CD2    . TYR A 1 318 ? 1.48600   6.63800   -36.76800 1.000 18.80419 ? 311 TYR A CD2    1 
ATOM   2404 C  CE1    . TYR A 1 318 ? -0.44100  6.09800   -38.68500 1.000 21.83890 ? 311 TYR A CE1    1 
ATOM   2405 C  CE2    . TYR A 1 318 ? 1.45600   5.40200   -37.40000 1.000 17.90866 ? 311 TYR A CE2    1 
ATOM   2406 C  CZ     . TYR A 1 318 ? 0.49600   5.14200   -38.36000 1.000 21.10321 ? 311 TYR A CZ     1 
ATOM   2407 O  OH     . TYR A 1 318 ? 0.47500   3.92300   -38.98800 1.000 20.86442 ? 311 TYR A OH     1 
ATOM   2408 N  N      . HIS A 1 319 ? 1.97100   12.02900  -36.14000 1.000 11.45876 ? 312 HIS A N      1 
ATOM   2409 C  CA     . HIS A 1 319 ? 1.83600   13.27700  -35.38800 1.000 14.38949 ? 312 HIS A CA     1 
ATOM   2410 C  C      . HIS A 1 319 ? 1.46300   14.44100  -36.29700 1.000 17.31089 ? 312 HIS A C      1 
ATOM   2411 O  O      . HIS A 1 319 ? 2.12400   14.68100  -37.30600 1.000 13.58361 ? 312 HIS A O      1 
ATOM   2412 C  CB     . HIS A 1 319 ? 3.16100   13.57500  -34.68400 1.000 14.65013 ? 312 HIS A CB     1 
ATOM   2413 C  CG     . HIS A 1 319 ? 3.20200   14.86900  -33.92700 1.000 15.54418 ? 312 HIS A CG     1 
ATOM   2414 N  ND1    . HIS A 1 319 ? 2.23400   15.24100  -33.01600 1.000 12.65392 ? 312 HIS A ND1    1 
ATOM   2415 C  CD2    . HIS A 1 319 ? 4.14500   15.84100  -33.88700 1.000 16.54881 ? 312 HIS A CD2    1 
ATOM   2416 C  CE1    . HIS A 1 319 ? 2.56600   16.39700  -32.47100 1.000 14.06593 ? 312 HIS A CE1    1 
ATOM   2417 N  NE2    . HIS A 1 319 ? 3.71900   16.78400  -32.98500 1.000 15.30485 ? 312 HIS A NE2    1 
ATOM   2418 N  N      . ASP A 1 320 ? 0.43000   15.18900  -35.90800 1.000 15.41246 ? 313 ASP A N      1 
ATOM   2419 C  CA     . ASP A 1 320 ? 0.03100   16.42300  -36.58500 1.000 12.50055 ? 313 ASP A CA     1 
ATOM   2420 C  C      . ASP A 1 320 ? -0.33600  17.45600  -35.52200 1.000 12.63381 ? 313 ASP A C      1 
ATOM   2421 O  O      . ASP A 1 320 ? -1.43300  17.39000  -34.94400 1.000 15.20265 ? 313 ASP A O      1 
ATOM   2422 C  CB     . ASP A 1 320 ? -1.14500  16.18900  -37.52900 1.000 15.60979 ? 313 ASP A CB     1 
ATOM   2423 C  CG     . ASP A 1 320 ? -1.54800  17.45300  -38.28700 1.000 18.13593 ? 313 ASP A CG     1 
ATOM   2424 O  OD1    . ASP A 1 320 ? -1.02200  18.54200  -37.96500 1.000 15.76367 ? 313 ASP A OD1    1 
ATOM   2425 O  OD2    . ASP A 1 320 ? -2.40400  17.35200  -39.19900 1.000 17.83226 ? 313 ASP A OD2    1 
ATOM   2426 N  N      . PRO A 1 321 ? 0.54100   18.43000  -35.25100 1.000 11.38441 ? 314 PRO A N      1 
ATOM   2427 C  CA     . PRO A 1 321 ? 0.25500   19.39600  -34.17200 1.000 12.42956 ? 314 PRO A CA     1 
ATOM   2428 C  C      . PRO A 1 321 ? -1.00200  20.21400  -34.40200 1.000 15.28198 ? 314 PRO A C      1 
ATOM   2429 O  O      . PRO A 1 321 ? -1.51700  20.82500  -33.45100 1.000 14.37994 ? 314 PRO A O      1 
ATOM   2430 C  CB     . PRO A 1 321 ? 1.50800   20.28600  -34.15900 1.000 13.88017 ? 314 PRO A CB     1 
ATOM   2431 C  CG     . PRO A 1 321 ? 2.06300   20.18500  -35.54300 1.000 16.46239 ? 314 PRO A CG     1 
ATOM   2432 C  CD     . PRO A 1 321 ? 1.80200   18.74900  -35.95100 1.000 15.07485 ? 314 PRO A CD     1 
ATOM   2433 N  N      . ASP A 1 322 ? -1.50600  20.26800  -35.63300 1.000 10.82586 ? 315 ASP A N      1 
ATOM   2434 C  CA     . ASP A 1 322 ? -2.72300  21.00700  -35.92800 1.000 14.13207 ? 315 ASP A CA     1 
ATOM   2435 C  C      . ASP A 1 322 ? -3.95500  20.11800  -35.96300 1.000 16.17664 ? 315 ASP A C      1 
ATOM   2436 O  O      . ASP A 1 322 ? -5.04300  20.59000  -36.30700 1.000 15.14190 ? 315 ASP A O      1 
ATOM   2437 C  CB     . ASP A 1 322 ? -2.56000  21.75800  -37.24900 1.000 19.34902 ? 315 ASP A CB     1 
ATOM   2438 C  CG     . ASP A 1 322 ? -1.37100  22.68600  -37.22000 1.000 19.32476 ? 315 ASP A CG     1 
ATOM   2439 O  OD1    . ASP A 1 322 ? -1.13300  23.26600  -36.13800 1.000 15.56498 ? 315 ASP A OD1    1 
ATOM   2440 O  OD2    . ASP A 1 322 ? -0.65900  22.79400  -38.24200 1.000 19.39147 ? 315 ASP A OD2    1 
ATOM   2441 N  N      . ASP A 1 323 ? -3.82200  18.84600  -35.60300 1.000 14.41764 ? 316 ASP A N      1 
ATOM   2442 C  CA     . ASP A 1 323 ? -4.99200  17.97300  -35.52500 1.000 15.06490 ? 316 ASP A CA     1 
ATOM   2443 C  C      . ASP A 1 323 ? -4.91200  17.08800  -34.28200 1.000 16.46508 ? 316 ASP A C      1 
ATOM   2444 O  O      . ASP A 1 323 ? -5.18500  15.88700  -34.33500 1.000 15.77454 ? 316 ASP A O      1 
ATOM   2445 C  CB     . ASP A 1 323 ? -5.13700  17.13400  -36.79400 1.000 15.89069 ? 316 ASP A CB     1 
ATOM   2446 C  CG     . ASP A 1 323 ? -6.47700  16.42100  -36.86600 1.000 19.99804 ? 316 ASP A CG     1 
ATOM   2447 O  OD1    . ASP A 1 323 ? -7.46200  16.90500  -36.25800 1.000 21.07206 ? 316 ASP A OD1    1 
ATOM   2448 O  OD2    . ASP A 1 323 ? -6.53700  15.36700  -37.51600 1.000 20.87553 ? 316 ASP A OD2    1 
ATOM   2449 N  N      . GLU A 1 324 ? -4.54500  17.68700  -33.14600 1.000 11.15805 ? 317 GLU A N      1 
ATOM   2450 C  CA     . GLU A 1 324 ? -4.52700  17.02200  -31.84300 1.000 15.18464 ? 317 GLU A CA     1 
ATOM   2451 C  C      . GLU A 1 324 ? -5.26400  17.94300  -30.86800 1.000 10.44230 ? 317 GLU A C      1 
ATOM   2452 O  O      . GLU A 1 324 ? -4.65900  18.56500  -29.98900 1.000 11.90849 ? 317 GLU A O      1 
ATOM   2453 C  CB     . GLU A 1 324 ? -3.08500  16.71400  -31.42100 1.000 9.86155  ? 317 GLU A CB     1 
ATOM   2454 C  CG     . GLU A 1 324 ? -2.48700  15.59100  -32.32400 1.000 10.23434 ? 317 GLU A CG     1 
ATOM   2455 C  CD     . GLU A 1 324 ? -0.96300  15.47600  -32.29500 1.000 13.30837 ? 317 GLU A CD     1 
ATOM   2456 O  OE1    . GLU A 1 324 ? -0.29900  16.21800  -31.54500 1.000 13.32239 ? 317 GLU A OE1    1 
ATOM   2457 O  OE2    . GLU A 1 324 ? -0.42600  14.62700  -33.05100 1.000 13.33257 ? 317 GLU A OE2    1 
ATOM   2458 N  N      . PRO A 1 325 ? -6.58200  18.04700  -31.01100 1.000 12.98753 ? 318 PRO A N      1 
ATOM   2459 C  CA     . PRO A 1 325 ? -7.33400  19.12400  -30.35600 1.000 13.67287 ? 318 PRO A CA     1 
ATOM   2460 C  C      . PRO A 1 325 ? -7.47800  18.92200  -28.85400 1.000 13.93787 ? 318 PRO A C      1 
ATOM   2461 O  O      . PRO A 1 325 ? -7.29200  17.83200  -28.31200 1.000 13.32212 ? 318 PRO A O      1 
ATOM   2462 C  CB     . PRO A 1 325 ? -8.70300  19.06800  -31.04700 1.000 12.43754 ? 318 PRO A CB     1 
ATOM   2463 C  CG     . PRO A 1 325 ? -8.81600  17.68000  -31.57700 1.000 16.82010 ? 318 PRO A CG     1 
ATOM   2464 C  CD     . PRO A 1 325 ? -7.42000  17.24100  -31.92200 1.000 14.33826 ? 318 PRO A CD     1 
ATOM   2465 N  N      . VAL A 1 326 ? -7.83500  20.01000  -28.18200 1.000 10.77184 ? 319 VAL A N      1 
ATOM   2466 C  CA     . VAL A 1 326 ? -7.98800  20.02600  -26.73500 1.000 10.86180 ? 319 VAL A CA     1 
ATOM   2467 C  C      . VAL A 1 326 ? -9.45000  20.32600  -26.39900 1.000 13.11668 ? 319 VAL A C      1 
ATOM   2468 O  O      . VAL A 1 326 ? -10.25000 20.66500  -27.26900 1.000 11.23736 ? 319 VAL A O      1 
ATOM   2469 C  CB     . VAL A 1 326 ? -7.03000  21.02700  -26.08100 1.000 15.24599 ? 319 VAL A CB     1 
ATOM   2470 C  CG1    . VAL A 1 326 ? -5.60600  20.61700  -26.40600 1.000 19.35323 ? 319 VAL A CG1    1 
ATOM   2471 C  CG2    . VAL A 1 326 ? -7.29900  22.43700  -26.60700 1.000 17.83478 ? 319 VAL A CG2    1 
ATOM   2472 N  N      . ALA A 1 327 ? -9.80500  20.14600  -25.12900 1.000 11.43997 ? 320 ALA A N      1 
ATOM   2473 C  CA     . ALA A 1 327 ? -11.20300 20.19400  -24.70600 1.000 12.79290 ? 320 ALA A CA     1 
ATOM   2474 C  C      . ALA A 1 327 ? -11.62400 21.59700  -24.28300 1.000 13.92644 ? 320 ALA A C      1 
ATOM   2475 O  O      . ALA A 1 327 ? -10.80300 22.40300  -23.84500 1.000 11.61502 ? 320 ALA A O      1 
ATOM   2476 C  CB     . ALA A 1 327 ? -11.44000 19.24000  -23.53500 1.000 11.23523 ? 320 ALA A CB     1 
ATOM   2477 N  N      . ASP A 1 328 ? -12.92200 21.87400  -24.41000 1.000 13.50417 ? 321 ASP A N      1 
ATOM   2478 C  CA     . ASP A 1 328 ? -13.50600 23.02500  -23.73300 1.000 16.10222 ? 321 ASP A CA     1 
ATOM   2479 C  C      . ASP A 1 328 ? -13.31400 22.88900  -22.22200 1.000 14.15885 ? 321 ASP A C      1 
ATOM   2480 O  O      . ASP A 1 328 ? -13.22100 21.77100  -21.69900 1.000 12.78876 ? 321 ASP A O      1 
ATOM   2481 C  CB     . ASP A 1 328 ? -14.99800 23.12600  -24.02700 1.000 15.13846 ? 321 ASP A CB     1 
ATOM   2482 C  CG     . ASP A 1 328 ? -15.29200 23.53900  -25.44300 1.000 20.68671 ? 321 ASP A CG     1 
ATOM   2483 O  OD1    . ASP A 1 328 ? -14.37700 24.00900  -26.14600 1.000 21.61626 ? 321 ASP A OD1    1 
ATOM   2484 O  OD2    . ASP A 1 328 ? -16.45800 23.37400  -25.85600 1.000 25.37199 ? 321 ASP A OD2    1 
ATOM   2485 N  N      . PRO A 1 329 ? -13.28700 24.00300  -21.49100 1.000 17.60923 ? 322 PRO A N      1 
ATOM   2486 C  CA     . PRO A 1 329 ? -13.18200 23.91000  -20.03300 1.000 16.09718 ? 322 PRO A CA     1 
ATOM   2487 C  C      . PRO A 1 329 ? -14.34500 23.12700  -19.44200 1.000 15.77943 ? 322 PRO A C      1 
ATOM   2488 O  O      . PRO A 1 329 ? -15.49200 23.22800  -19.89200 1.000 15.70180 ? 322 PRO A O      1 
ATOM   2489 C  CB     . PRO A 1 329 ? -13.19400 25.37700  -19.58600 1.000 23.21532 ? 322 PRO A CB     1 
ATOM   2490 C  CG     . PRO A 1 329 ? -12.65900 26.12900  -20.77800 1.000 21.19853 ? 322 PRO A CG     1 
ATOM   2491 C  CD     . PRO A 1 329 ? -13.26500 25.40500  -21.94900 1.000 19.83807 ? 322 PRO A CD     1 
ATOM   2492 N  N      . TYR A 1 330 ? -14.02100 22.33300  -18.42600 1.000 16.65888 ? 323 TYR A N      1 
ATOM   2493 C  CA     . TYR A 1 330 ? -14.92600 21.40000  -17.77000 1.000 14.35433 ? 323 TYR A CA     1 
ATOM   2494 C  C      . TYR A 1 330 ? -15.12800 21.86900  -16.33500 1.000 16.18560 ? 323 TYR A C      1 
ATOM   2495 O  O      . TYR A 1 330 ? -14.17200 21.89400  -15.55500 1.000 18.61198 ? 323 TYR A O      1 
ATOM   2496 C  CB     . TYR A 1 330 ? -14.33600 19.99100  -17.78800 1.000 14.15703 ? 323 TYR A CB     1 
ATOM   2497 C  CG     . TYR A 1 330 ? -15.17700 18.95200  -17.11200 1.000 14.43145 ? 323 TYR A CG     1 
ATOM   2498 C  CD1    . TYR A 1 330 ? -16.51300 18.78500  -17.46000 1.000 16.70439 ? 323 TYR A CD1    1 
ATOM   2499 C  CD2    . TYR A 1 330 ? -14.64000 18.11600  -16.14500 1.000 15.48469 ? 323 TYR A CD2    1 
ATOM   2500 C  CE1    . TYR A 1 330 ? -17.29900 17.81900  -16.84500 1.000 16.60878 ? 323 TYR A CE1    1 
ATOM   2501 C  CE2    . TYR A 1 330 ? -15.42200 17.15200  -15.51900 1.000 18.00809 ? 323 TYR A CE2    1 
ATOM   2502 C  CZ     . TYR A 1 330 ? -16.74500 17.00700  -15.88600 1.000 17.21555 ? 323 TYR A CZ     1 
ATOM   2503 O  OH     . TYR A 1 330 ? -17.52600 16.05600  -15.27500 1.000 21.85611 ? 323 TYR A OH     1 
ATOM   2504 N  N      . ASP A 1 331 ? -16.36500 22.21500  -15.98400 1.000 16.91660 ? 324 ASP A N      1 
ATOM   2505 C  CA     . ASP A 1 331 ? -16.70700 22.69200  -14.63500 1.000 16.65731 ? 324 ASP A CA     1 
ATOM   2506 C  C      . ASP A 1 331 ? -16.90700 21.48800  -13.72000 1.000 15.32517 ? 324 ASP A C      1 
ATOM   2507 O  O      . ASP A 1 331 ? -17.98800 20.89000  -13.68000 1.000 17.44767 ? 324 ASP A O      1 
ATOM   2508 C  CB     . ASP A 1 331 ? -17.94500 23.58600  -14.71000 1.000 17.10174 ? 324 ASP A CB     1 
ATOM   2509 C  CG     . ASP A 1 331 ? -18.55300 23.91700  -13.35200 1.000 21.08849 ? 324 ASP A CG     1 
ATOM   2510 O  OD1    . ASP A 1 331 ? -17.97900 23.56600  -12.30000 1.000 17.04076 ? 324 ASP A OD1    1 
ATOM   2511 O  OD2    . ASP A 1 331 ? -19.61000 24.59800  -13.35500 1.000 23.75831 ? 324 ASP A OD2    1 
ATOM   2512 N  N      . GLN A 1 332 ? -15.87600 21.12700  -12.95700 1.000 13.32207 ? 325 GLN A N      1 
ATOM   2513 C  CA     . GLN A 1 332 ? -16.02200 20.06100  -11.97000 1.000 19.33508 ? 325 GLN A CA     1 
ATOM   2514 C  C      . GLN A 1 332 ? -16.06100 20.59000  -10.54200 1.000 18.56251 ? 325 GLN A C      1 
ATOM   2515 O  O      . GLN A 1 332 ? -15.65500 19.89800  -9.60600  1.000 21.33887 ? 325 GLN A O      1 
ATOM   2516 C  CB     . GLN A 1 332 ? -14.94200 18.99100  -12.11300 1.000 24.63350 ? 325 GLN A CB     1 
ATOM   2517 C  CG     . GLN A 1 332 ? -13.57200 19.44200  -12.44800 1.000 26.86640 ? 325 GLN A CG     1 
ATOM   2518 C  CD     . GLN A 1 332 ? -12.72900 18.25500  -12.91100 1.000 32.44767 ? 325 GLN A CD     1 
ATOM   2519 O  OE1    . GLN A 1 332 ? -13.13400 17.09600  -12.73800 1.000 29.14235 ? 325 GLN A OE1    1 
ATOM   2520 N  NE2    . GLN A 1 332 ? -11.61100 18.52900  -13.55400 1.000 25.60503 ? 325 GLN A NE2    1 
ATOM   2521 N  N      . SER A 1 333 ? -16.60300 21.79300  -10.35600 1.000 18.77582 ? 326 SER A N      1 
ATOM   2522 C  CA     . SER A 1 333 ? -16.79600 22.31800  -9.01000  1.000 18.93138 ? 326 SER A CA     1 
ATOM   2523 C  C      . SER A 1 333 ? -17.70300 21.42400  -8.16400  1.000 18.69101 ? 326 SER A C      1 
ATOM   2524 O  O      . SER A 1 333 ? -17.64400 21.49100  -6.93000  1.000 17.68386 ? 326 SER A O      1 
ATOM   2525 C  CB     . SER A 1 333 ? -17.35800 23.74400  -9.09500  1.000 18.59187 ? 326 SER A CB     1 
ATOM   2526 O  OG     . SER A 1 333 ? -18.65600 23.77300  -9.66500  1.000 17.43359 ? 326 SER A OG     1 
ATOM   2527 N  N      . PHE A 1 334 ? -18.52700 20.57900  -8.79300  1.000 17.05992 ? 327 PHE A N      1 
ATOM   2528 C  CA     . PHE A 1 334 ? -19.38200 19.67100  -8.03800  1.000 19.23841 ? 327 PHE A CA     1 
ATOM   2529 C  C      . PHE A 1 334 ? -18.59100 18.66000  -7.21500  1.000 17.55774 ? 327 PHE A C      1 
ATOM   2530 O  O      . PHE A 1 334 ? -19.10400 18.15800  -6.20500  1.000 17.25793 ? 327 PHE A O      1 
ATOM   2531 C  CB     . PHE A 1 334 ? -20.33500 18.95300  -8.99300  1.000 17.78531 ? 327 PHE A CB     1 
ATOM   2532 C  CG     . PHE A 1 334 ? -19.69500 17.82200  -9.75600  1.000 17.44761 ? 327 PHE A CG     1 
ATOM   2533 C  CD1    . PHE A 1 334 ? -19.69800 16.53100  -9.24500  1.000 19.89226 ? 327 PHE A CD1    1 
ATOM   2534 C  CD2    . PHE A 1 334 ? -19.11100 18.05100  -11.00300 1.000 15.91198 ? 327 PHE A CD2    1 
ATOM   2535 C  CE1    . PHE A 1 334 ? -19.10600 15.48300  -9.96100  1.000 19.25492 ? 327 PHE A CE1    1 
ATOM   2536 C  CE2    . PHE A 1 334 ? -18.52400 17.00800  -11.71700 1.000 17.35758 ? 327 PHE A CE2    1 
ATOM   2537 C  CZ     . PHE A 1 334 ? -18.52800 15.72900  -11.19300 1.000 15.23462 ? 327 PHE A CZ     1 
ATOM   2538 N  N      . GLU A 1 335 ? -17.35600 18.34800  -7.61800  1.000 15.66608 ? 328 GLU A N      1 
ATOM   2539 C  CA     . GLU A 1 335 ? -16.57200 17.34300  -6.90300  1.000 14.58050 ? 328 GLU A CA     1 
ATOM   2540 C  C      . GLU A 1 335 ? -16.31200 17.77200  -5.46000  1.000 17.78068 ? 328 GLU A C      1 
ATOM   2541 O  O      . GLU A 1 335 ? -16.12600 16.92100  -4.58500  1.000 19.93183 ? 328 GLU A O      1 
ATOM   2542 C  CB     . GLU A 1 335 ? -15.24700 17.07600  -7.63300  1.000 17.77463 ? 328 GLU A CB     1 
ATOM   2543 C  CG     . GLU A 1 335 ? -15.37500 16.28700  -8.96900  1.000 15.41141 ? 328 GLU A CG     1 
ATOM   2544 C  CD     . GLU A 1 335 ? -15.78700 14.84200  -8.76300  1.000 19.87199 ? 328 GLU A CD     1 
ATOM   2545 O  OE1    . GLU A 1 335 ? -16.12700 14.47600  -7.61100  1.000 14.39867 ? 328 GLU A OE1    1 
ATOM   2546 O  OE2    . GLU A 1 335 ? -15.77700 14.07100  -9.75200  1.000 16.85754 ? 328 GLU A OE2    1 
ATOM   2547 N  N      . SER A 1 336 ? -16.31200 19.08300  -5.19700  1.000 18.50407 ? 329 SER A N      1 
ATOM   2548 C  CA     . SER A 1 336 ? -16.14200 19.65100  -3.85800  1.000 23.55556 ? 329 SER A CA     1 
ATOM   2549 C  C      . SER A 1 336 ? -17.43300 19.71800  -3.04900  1.000 25.76333 ? 329 SER A C      1 
ATOM   2550 O  O      . SER A 1 336 ? -17.39000 20.15400  -1.88900  1.000 26.75036 ? 329 SER A O      1 
ATOM   2551 C  CB     . SER A 1 336 ? -15.57200 21.06800  -3.96100  1.000 20.95881 ? 329 SER A CB     1 
ATOM   2552 O  OG     . SER A 1 336 ? -14.26000 21.04700  -4.47800  1.000 30.00128 ? 329 SER A OG     1 
ATOM   2553 N  N      . ARG A 1 337 ? -18.57300 19.33700  -3.62000  1.000 19.55828 ? 330 ARG A N      1 
ATOM   2554 C  CA     . ARG A 1 337 ? -19.86000 19.55300  -2.96900  1.000 19.63696 ? 330 ARG A CA     1 
ATOM   2555 C  C      . ARG A 1 337 ? -20.25200 18.36900  -2.09600  1.000 24.24578 ? 330 ARG A C      1 
ATOM   2556 O  O      . ARG A 1 337 ? -20.01000 17.20900  -2.44400  1.000 23.18110 ? 330 ARG A O      1 
ATOM   2557 C  CB     . ARG A 1 337 ? -20.96600 19.79800  -4.00000  1.000 20.55405 ? 330 ARG A CB     1 
ATOM   2558 C  CG     . ARG A 1 337 ? -20.73600 20.98500  -4.89800  1.000 26.72664 ? 330 ARG A CG     1 
ATOM   2559 C  CD     . ARG A 1 337 ? -21.27800 22.25700  -4.28200  1.000 26.00448 ? 330 ARG A CD     1 
ATOM   2560 N  NE     . ARG A 1 337 ? -20.32000 22.88700  -3.38300  1.000 26.89857 ? 330 ARG A NE     1 
ATOM   2561 C  CZ     . ARG A 1 337 ? -19.15800 23.40100  -3.76200  1.000 27.87779 ? 330 ARG A CZ     1 
ATOM   2562 N  NH1    . ARG A 1 337 ? -18.75500 23.34300  -5.01800  1.000 24.71528 ? 330 ARG A NH1    1 
ATOM   2563 N  NH2    . ARG A 1 337 ? -18.38500 24.00200  -2.85700  1.000 25.71782 ? 330 ARG A NH2    1 
ATOM   2564 N  N      . ASP A 1 338 ? -20.89500 18.67100  -0.97500  1.000 20.38055 ? 331 ASP A N      1 
ATOM   2565 C  CA     . ASP A 1 338 ? -21.47400 17.66800  -0.09000  1.000 21.03432 ? 331 ASP A CA     1 
ATOM   2566 C  C      . ASP A 1 338 ? -22.97100 17.96700  -0.06800  1.000 21.65437 ? 331 ASP A C      1 
ATOM   2567 O  O      . ASP A 1 338 ? -23.41900 18.85900  0.65700   1.000 17.98627 ? 331 ASP A O      1 
ATOM   2568 C  CB     . ASP A 1 338 ? -20.84800 17.73900  1.30400   1.000 26.56253 ? 331 ASP A CB     1 
ATOM   2569 C  CG     . ASP A 1 338 ? -19.49300 17.03300  1.37300   1.000 34.96569 ? 331 ASP A CG     1 
ATOM   2570 O  OD1    . ASP A 1 338 ? -19.27100 16.05600  0.62300   1.000 34.61058 ? 331 ASP A OD1    1 
ATOM   2571 O  OD2    . ASP A 1 338 ? -18.64000 17.47000  2.17200   1.000 41.72257 ? 331 ASP A OD2    1 
ATOM   2572 N  N      . LEU A 1 339 ? -23.73600 17.25200  -0.88700  1.000 20.83097 ? 332 LEU A N      1 
ATOM   2573 C  CA     . LEU A 1 339 ? -25.14400 17.54600  -1.11900  1.000 17.31178 ? 332 LEU A CA     1 
ATOM   2574 C  C      . LEU A 1 339 ? -26.01400 16.36800  -0.70400  1.000 21.54490 ? 332 LEU A C      1 
ATOM   2575 O  O      . LEU A 1 339 ? -25.53400 15.25100  -0.49900  1.000 22.67796 ? 332 LEU A O      1 
ATOM   2576 C  CB     . LEU A 1 339 ? -25.40000 17.87400  -2.59700  1.000 18.28321 ? 332 LEU A CB     1 
ATOM   2577 C  CG     . LEU A 1 339 ? -24.56900 18.99400  -3.23900  1.000 20.80476 ? 332 LEU A CG     1 
ATOM   2578 C  CD1    . LEU A 1 339 ? -24.95900 19.15500  -4.70700  1.000 17.50220 ? 332 LEU A CD1    1 
ATOM   2579 C  CD2    . LEU A 1 339 ? -24.76400 20.31300  -2.49000  1.000 19.03115 ? 332 LEU A CD2    1 
ATOM   2580 N  N      . LEU A 1 340 ? -27.31900 16.62300  -0.61900  1.000 20.68917 ? 333 LEU A N      1 
ATOM   2581 C  CA     . LEU A 1 340 ? -28.26100 15.58500  -0.22500  1.000 22.86516 ? 333 LEU A CA     1 
ATOM   2582 C  C      . LEU A 1 340 ? -28.57600 14.66500  -1.40000  1.000 27.22424 ? 333 LEU A C      1 
ATOM   2583 O  O      . LEU A 1 340 ? -28.44200 15.04000  -2.57100  1.000 20.94875 ? 333 LEU A O      1 
ATOM   2584 C  CB     . LEU A 1 340 ? -29.54700 16.19100  0.33900   1.000 30.06445 ? 333 LEU A CB     1 
ATOM   2585 C  CG     . LEU A 1 340 ? -29.32900 17.03900  1.59500   1.000 31.52240 ? 333 LEU A CG     1 
ATOM   2586 C  CD1    . LEU A 1 340 ? -30.56100 17.87000  1.93100   1.000 34.39487 ? 333 LEU A CD1    1 
ATOM   2587 C  CD2    . LEU A 1 340 ? -28.92100 16.15500  2.74300   1.000 33.78339 ? 333 LEU A CD2    1 
ATOM   2588 N  N      . ILE A 1 341 ? -28.95300 13.42800  -1.06400  1.000 25.96074 ? 334 ILE A N      1 
ATOM   2589 C  CA     . ILE A 1 341 ? -29.21600 12.41300  -2.08300  1.000 26.15758 ? 334 ILE A CA     1 
ATOM   2590 C  C      . ILE A 1 341 ? -30.20200 12.94700  -3.10900  1.000 25.93162 ? 334 ILE A C      1 
ATOM   2591 O  O      . ILE A 1 341 ? -30.01200 12.79200  -4.32200  1.000 21.50540 ? 334 ILE A O      1 
ATOM   2592 C  CB     . ILE A 1 341 ? -29.74100 11.11800  -1.43700  1.000 33.98801 ? 334 ILE A CB     1 
ATOM   2593 C  CG1    . ILE A 1 341 ? -29.70000 9.97300   -2.43900  1.000 31.43311 ? 334 ILE A CG1    1 
ATOM   2594 C  CG2    . ILE A 1 341 ? -31.19000 11.28400  -1.00400  1.000 37.98162 ? 334 ILE A CG2    1 
ATOM   2595 C  CD1    . ILE A 1 341 ? -28.47100 9.10700   -2.28700  1.000 34.51924 ? 334 ILE A CD1    1 
ATOM   2596 N  N      . ASP A 1 342 ? -31.26900 13.59900  -2.63300  1.000 23.01644 ? 335 ASP A N      1 
ATOM   2597 C  CA     . ASP A 1 342 ? -32.28700 14.10100  -3.54500  1.000 24.42157 ? 335 ASP A CA     1 
ATOM   2598 C  C      . ASP A 1 342 ? -31.73200 15.18700  -4.44800  1.000 22.84270 ? 335 ASP A C      1 
ATOM   2599 O  O      . ASP A 1 342 ? -32.24400 15.39400  -5.55900  1.000 20.76941 ? 335 ASP A O      1 
ATOM   2600 C  CB     . ASP A 1 342 ? -33.49000 14.64000  -2.77500  1.000 27.05778 ? 335 ASP A CB     1 
ATOM   2601 C  CG     . ASP A 1 342 ? -34.41600 13.53900  -2.28200  1.000 35.83801 ? 335 ASP A CG     1 
ATOM   2602 O  OD1    . ASP A 1 342 ? -34.40800 12.42600  -2.86200  1.000 35.45889 ? 335 ASP A OD1    1 
ATOM   2603 O  OD2    . ASP A 1 342 ? -35.17000 13.79900  -1.32000  1.000 47.39213 ? 335 ASP A OD2    1 
ATOM   2604 N  N      . GLU A 1 343 ? -30.69600 15.89800  -3.98900  1.000 20.16471 ? 336 GLU A N      1 
ATOM   2605 C  CA     . GLU A 1 343 ? -30.10000 16.93800  -4.81900  1.000 21.28006 ? 336 GLU A CA     1 
ATOM   2606 C  C      . GLU A 1 343 ? -29.27900 16.32200  -5.94500  1.000 20.36372 ? 336 GLU A C      1 
ATOM   2607 O  O      . GLU A 1 343 ? -29.41500 16.71900  -7.10800  1.000 15.73050 ? 336 GLU A O      1 
ATOM   2608 C  CB     . GLU A 1 343 ? -29.23700 17.88500  -3.97700  1.000 22.04518 ? 336 GLU A CB     1 
ATOM   2609 C  CG     . GLU A 1 343 ? -30.04000 18.88900  -3.16800  1.000 25.98531 ? 336 GLU A CG     1 
ATOM   2610 C  CD     . GLU A 1 343 ? -29.17700 19.82400  -2.31600  1.000 27.52207 ? 336 GLU A CD     1 
ATOM   2611 O  OE1    . GLU A 1 343 ? -28.44900 19.35500  -1.39400  1.000 24.98723 ? 336 GLU A OE1    1 
ATOM   2612 O  OE2    . GLU A 1 343 ? -29.22100 21.04200  -2.59300  1.000 27.03980 ? 336 GLU A OE2    1 
ATOM   2613 N  N      . TRP A 1 344 ? -28.40200 15.36200  -5.61400  1.000 18.24207 ? 337 TRP A N      1 
ATOM   2614 C  CA     . TRP A 1 344 ? -27.65200 14.68100  -6.67100  1.000 20.23966 ? 337 TRP A CA     1 
ATOM   2615 C  C      . TRP A 1 344 ? -28.60000 14.07500  -7.70300  1.000 18.78298 ? 337 TRP A C      1 
ATOM   2616 O  O      . TRP A 1 344 ? -28.34900 14.15300  -8.91500  1.000 19.72084 ? 337 TRP A O      1 
ATOM   2617 C  CB     . TRP A 1 344 ? -26.73200 13.60500  -6.08000  1.000 19.05309 ? 337 TRP A CB     1 
ATOM   2618 C  CG     . TRP A 1 344 ? -25.51600 14.14300  -5.31600  1.000 19.28643 ? 337 TRP A CG     1 
ATOM   2619 C  CD1    . TRP A 1 344 ? -25.18100 13.87900  -4.01600  1.000 18.19722 ? 337 TRP A CD1    1 
ATOM   2620 C  CD2    . TRP A 1 344 ? -24.49600 15.02300  -5.81900  1.000 17.84360 ? 337 TRP A CD2    1 
ATOM   2621 N  NE1    . TRP A 1 344 ? -24.01800 14.54100  -3.67600  1.000 17.56378 ? 337 TRP A NE1    1 
ATOM   2622 C  CE2    . TRP A 1 344 ? -23.58100 15.25100  -4.76400  1.000 18.01697 ? 337 TRP A CE2    1 
ATOM   2623 C  CE3    . TRP A 1 344 ? -24.27800 15.65500  -7.05400  1.000 15.65911 ? 337 TRP A CE3    1 
ATOM   2624 C  CZ2    . TRP A 1 344 ? -22.46000 16.06500  -4.90800  1.000 15.59242 ? 337 TRP A CZ2    1 
ATOM   2625 C  CZ3    . TRP A 1 344 ? -23.15900 16.46600  -7.19300  1.000 16.55107 ? 337 TRP A CZ3    1 
ATOM   2626 C  CH2    . TRP A 1 344 ? -22.26300 16.66000  -6.12700  1.000 17.22738 ? 337 TRP A CH2    1 
ATOM   2627 N  N      . LYS A 1 345 ? -29.70700 13.48700  -7.24100  1.000 18.45376 ? 338 LYS A N      1 
ATOM   2628 C  CA     . LYS A 1 345 ? -30.67500 12.89400  -8.16100  1.000 21.16890 ? 338 LYS A CA     1 
ATOM   2629 C  C      . LYS A 1 345 ? -31.30900 13.94500  -9.05800  1.000 20.31759 ? 338 LYS A C      1 
ATOM   2630 O  O      . LYS A 1 345 ? -31.48900 13.71900  -10.26300 1.000 19.20059 ? 338 LYS A O      1 
ATOM   2631 C  CB     . LYS A 1 345 ? -31.75300 12.14800  -7.37700  1.000 19.54212 ? 338 LYS A CB     1 
ATOM   2632 C  CG     . LYS A 1 345 ? -32.77000 11.42800  -8.25600  1.000 23.03978 ? 338 LYS A CG     1 
ATOM   2633 C  CD     . LYS A 1 345 ? -33.63100 10.48500  -7.43700  1.000 26.80951 ? 338 LYS A CD     1 
ATOM   2634 C  CE     . LYS A 1 345 ? -35.07100 10.96400  -7.39300  1.000 36.76307 ? 338 LYS A CE     1 
ATOM   2635 N  NZ     . LYS A 1 345 ? -36.02400 9.89900   -7.84200  1.000 35.81463 ? 338 LYS A NZ     1 
ATOM   2636 N  N      . SER A 1 346 ? -31.67200 15.09500  -8.48000  1.000 18.92293 ? 339 SER A N      1 
ATOM   2637 C  CA     . SER A 1 346 ? -32.30400 16.15600  -9.25000  1.000 18.90868 ? 339 SER A CA     1 
ATOM   2638 C  C      . SER A 1 346 ? -31.34300 16.73700  -10.27900 1.000 20.38992 ? 339 SER A C      1 
ATOM   2639 O  O      . SER A 1 346 ? -31.74100 17.03900  -11.41200 1.000 17.61251 ? 339 SER A O      1 
ATOM   2640 C  CB     . SER A 1 346 ? -32.81000 17.25000  -8.31200  1.000 21.23259 ? 339 SER A CB     1 
ATOM   2641 O  OG     . SER A 1 346 ? -33.58400 18.19200  -9.03300  1.000 31.00910 ? 339 SER A OG     1 
ATOM   2642 N  N      . LEU A 1 347 ? -30.06900 16.89000  -9.90700  1.000 18.29734 ? 340 LEU A N      1 
ATOM   2643 C  CA     . LEU A 1 347 ? -29.07300 17.38000  -10.85900 1.000 14.21545 ? 340 LEU A CA     1 
ATOM   2644 C  C      . LEU A 1 347 ? -28.87600 16.39300  -12.00500 1.000 13.67571 ? 340 LEU A C      1 
ATOM   2645 O  O      . LEU A 1 347 ? -28.72900 16.79200  -13.16700 1.000 17.16846 ? 340 LEU A O      1 
ATOM   2646 C  CB     . LEU A 1 347 ? -27.74900 17.63200  -10.13400 1.000 18.01407 ? 340 LEU A CB     1 
ATOM   2647 C  CG     . LEU A 1 347 ? -27.72900 18.76900  -9.10100  1.000 16.25075 ? 340 LEU A CG     1 
ATOM   2648 C  CD1    . LEU A 1 347 ? -26.47800 18.68400  -8.20300  1.000 17.80068 ? 340 LEU A CD1    1 
ATOM   2649 C  CD2    . LEU A 1 347 ? -27.80900 20.12600  -9.78200  1.000 20.70500 ? 340 LEU A CD2    1 
ATOM   2650 N  N      . THR A 1 348 ? -28.85200 15.09700  -11.69700 1.000 13.14690 ? 341 THR A N      1 
ATOM   2651 C  CA     . THR A 1 348 ? -28.70700 14.09500  -12.75300 1.000 18.52958 ? 341 THR A CA     1 
ATOM   2652 C  C      . THR A 1 348 ? -29.89600 14.13700  -13.70200 1.000 18.26122 ? 341 THR A C      1 
ATOM   2653 O  O      . THR A 1 348 ? -29.73000 14.13100  -14.93000 1.000 14.82516 ? 341 THR A O      1 
ATOM   2654 C  CB     . THR A 1 348 ? -28.54900 12.70600  -12.13100 1.000 16.53430 ? 341 THR A CB     1 
ATOM   2655 O  OG1    . THR A 1 348 ? -27.43700 12.72300  -11.23800 1.000 15.22203 ? 341 THR A OG1    1 
ATOM   2656 C  CG2    . THR A 1 348 ? -28.30800 11.64900  -13.20700 1.000 16.41819 ? 341 THR A CG2    1 
ATOM   2657 N  N      . TYR A 1 349 ? -31.11000 14.21100  -13.14400 1.000 13.93362 ? 342 TYR A N      1 
ATOM   2658 C  CA     . TYR A 1 349 ? -32.31300 14.30200  -13.96500 1.000 15.48036 ? 342 TYR A CA     1 
ATOM   2659 C  C      . TYR A 1 349 ? -32.25100 15.49900  -14.90700 1.000 17.52357 ? 342 TYR A C      1 
ATOM   2660 O  O      . TYR A 1 349 ? -32.55000 15.37700  -16.10200 1.000 18.12166 ? 342 TYR A O      1 
ATOM   2661 C  CB     . TYR A 1 349 ? -33.54700 14.36900  -13.05800 1.000 17.34729 ? 342 TYR A CB     1 
ATOM   2662 C  CG     . TYR A 1 349 ? -34.86800 14.22000  -13.79600 1.000 18.23440 ? 342 TYR A CG     1 
ATOM   2663 C  CD1    . TYR A 1 349 ? -35.20300 13.02800  -14.42300 1.000 17.85472 ? 342 TYR A CD1    1 
ATOM   2664 C  CD2    . TYR A 1 349 ? -35.77800 15.27100  -13.85700 1.000 20.96031 ? 342 TYR A CD2    1 
ATOM   2665 C  CE1    . TYR A 1 349 ? -36.41400 12.88000  -15.09500 1.000 20.89543 ? 342 TYR A CE1    1 
ATOM   2666 C  CE2    . TYR A 1 349 ? -36.99200 15.13300  -14.52400 1.000 24.41399 ? 342 TYR A CE2    1 
ATOM   2667 C  CZ     . TYR A 1 349 ? -37.29900 13.93000  -15.14100 1.000 24.80069 ? 342 TYR A CZ     1 
ATOM   2668 O  OH     . TYR A 1 349 ? -38.49400 13.77700  -15.80900 1.000 26.71360 ? 342 TYR A OH     1 
ATOM   2669 N  N      . ASP A 1 350 ? -31.84400 16.66800  -14.39400 1.000 16.94217 ? 343 ASP A N      1 
ATOM   2670 C  CA     . ASP A 1 350 ? -31.69700 17.84600  -15.24900 1.000 19.17875 ? 343 ASP A CA     1 
ATOM   2671 C  C      . ASP A 1 350 ? -30.75100 17.57800  -16.41500 1.000 19.77623 ? 343 ASP A C      1 
ATOM   2672 O  O      . ASP A 1 350 ? -30.97900 18.05200  -17.53600 1.000 17.22077 ? 343 ASP A O      1 
ATOM   2673 C  CB     . ASP A 1 350 ? -31.15500 19.03500  -14.45300 1.000 21.75919 ? 343 ASP A CB     1 
ATOM   2674 C  CG     . ASP A 1 350 ? -32.12500 19.55200  -13.42400 1.000 29.94681 ? 343 ASP A CG     1 
ATOM   2675 O  OD1    . ASP A 1 350 ? -33.34000 19.30000  -13.56500 1.000 29.31316 ? 343 ASP A OD1    1 
ATOM   2676 O  OD2    . ASP A 1 350 ? -31.64600 20.20800  -12.46900 1.000 34.11995 ? 343 ASP A OD2    1 
ATOM   2677 N  N      . GLU A 1 351 ? -29.65000 16.87100  -16.15100 1.000 17.76785 ? 344 GLU A N      1 
ATOM   2678 C  CA     . GLU A 1 351 ? -28.68400 16.57100  -17.20600 1.000 17.16198 ? 344 GLU A CA     1 
ATOM   2679 C  C      . GLU A 1 351 ? -29.23300 15.55900  -18.20700 1.000 15.99642 ? 344 GLU A C      1 
ATOM   2680 O  O      . GLU A 1 351 ? -28.89000 15.61900  -19.39400 1.000 20.10681 ? 344 GLU A O      1 
ATOM   2681 C  CB     . GLU A 1 351 ? -27.37500 16.06900  -16.57800 1.000 19.05284 ? 344 GLU A CB     1 
ATOM   2682 C  CG     . GLU A 1 351 ? -26.62500 17.14100  -15.76000 1.000 14.00777 ? 344 GLU A CG     1 
ATOM   2683 C  CD     . GLU A 1 351 ? -25.92800 18.18600  -16.63700 1.000 19.46045 ? 344 GLU A CD     1 
ATOM   2684 O  OE1    . GLU A 1 351 ? -25.65500 17.89600  -17.81800 1.000 15.98704 ? 344 GLU A OE1    1 
ATOM   2685 O  OE2    . GLU A 1 351 ? -25.63000 19.29500  -16.13600 1.000 19.05859 ? 344 GLU A OE2    1 
ATOM   2686 N  N      . VAL A 1 352 ? -30.07400 14.62500  -17.75900 1.000 17.53171 ? 345 VAL A N      1 
ATOM   2687 C  CA     . VAL A 1 352 ? -30.74900 13.72300  -18.69400 1.000 18.75470 ? 345 VAL A CA     1 
ATOM   2688 C  C      . VAL A 1 352 ? -31.64000 14.52900  -19.62800 1.000 22.27627 ? 345 VAL A C      1 
ATOM   2689 O  O      . VAL A 1 352 ? -31.55900 14.41000  -20.86100 1.000 17.63997 ? 345 VAL A O      1 
ATOM   2690 C  CB     . VAL A 1 352 ? -31.54700 12.64600  -17.92900 1.000 18.19469 ? 345 VAL A CB     1 
ATOM   2691 C  CG1    . VAL A 1 352 ? -32.39500 11.81700  -18.88600 1.000 19.34070 ? 345 VAL A CG1    1 
ATOM   2692 C  CG2    . VAL A 1 352 ? -30.61600 11.74100  -17.13100 1.000 14.06550 ? 345 VAL A CG2    1 
ATOM   2693 N  N      . ILE A 1 353 ? -32.45000 15.42400  -19.04900 1.000 20.97718 ? 346 ILE A N      1 
ATOM   2694 C  CA     . ILE A 1 353 ? -33.40300 16.21800  -19.81800 1.000 21.50886 ? 346 ILE A CA     1 
ATOM   2695 C  C      . ILE A 1 353 ? -32.71300 17.15900  -20.79000 1.000 22.92991 ? 346 ILE A C      1 
ATOM   2696 O  O      . ILE A 1 353 ? -33.23500 17.42200  -21.88200 1.000 22.80795 ? 346 ILE A O      1 
ATOM   2697 C  CB     . ILE A 1 353 ? -34.32200 17.01900  -18.87700 1.000 26.39764 ? 346 ILE A CB     1 
ATOM   2698 C  CG1    . ILE A 1 353 ? -35.28900 16.11200  -18.14600 1.000 31.52863 ? 346 ILE A CG1    1 
ATOM   2699 C  CG2    . ILE A 1 353 ? -35.10500 18.04300  -19.66600 1.000 29.76533 ? 346 ILE A CG2    1 
ATOM   2700 C  CD1    . ILE A 1 353 ? -35.70400 16.69300  -16.84700 1.000 29.11119 ? 346 ILE A CD1    1 
ATOM   2701 N  N      . SER A 1 354 ? -31.56000 17.71500  -20.42100 1.000 24.55657 ? 347 SER A N      1 
ATOM   2702 C  CA     . SER A 1 354 ? -30.92700 18.69700  -21.29200 1.000 24.09121 ? 347 SER A CA     1 
ATOM   2703 C  C      . SER A 1 354 ? -30.06700 18.07400  -22.38900 1.000 26.65466 ? 347 SER A C      1 
ATOM   2704 O  O      . SER A 1 354 ? -29.61400 18.80400  -23.28300 1.000 23.81667 ? 347 SER A O      1 
ATOM   2705 C  CB     . SER A 1 354 ? -30.06300 19.66200  -20.47700 1.000 24.11063 ? 347 SER A CB     1 
ATOM   2706 O  OG     . SER A 1 354 ? -29.05600 18.95400  -19.78400 1.000 19.94270 ? 347 SER A OG     1 
ATOM   2707 N  N      . PHE A 1 355 ? -29.82300 16.76400  -22.34800 1.000 22.64982 ? 348 PHE A N      1 
ATOM   2708 C  CA     . PHE A 1 355 ? -28.93400 16.14100  -23.32200 1.000 19.61507 ? 348 PHE A CA     1 
ATOM   2709 C  C      . PHE A 1 355 ? -29.39900 16.42600  -24.74800 1.000 20.60582 ? 348 PHE A C      1 
ATOM   2710 O  O      . PHE A 1 355 ? -30.57600 16.25900  -25.07500 1.000 22.45785 ? 348 PHE A O      1 
ATOM   2711 C  CB     . PHE A 1 355 ? -28.86300 14.62700  -23.10200 1.000 20.70958 ? 348 PHE A CB     1 
ATOM   2712 C  CG     . PHE A 1 355 ? -28.06300 13.91900  -24.15800 1.000 22.34928 ? 348 PHE A CG     1 
ATOM   2713 C  CD1    . PHE A 1 355 ? -26.66700 13.96900  -24.13800 1.000 17.69046 ? 348 PHE A CD1    1 
ATOM   2714 C  CD2    . PHE A 1 355 ? -28.69800 13.24100  -25.20000 1.000 21.77986 ? 348 PHE A CD2    1 
ATOM   2715 C  CE1    . PHE A 1 355 ? -25.91300 13.34100  -25.13600 1.000 19.21881 ? 348 PHE A CE1    1 
ATOM   2716 C  CE2    . PHE A 1 355 ? -27.94700 12.61100  -26.20100 1.000 17.82136 ? 348 PHE A CE2    1 
ATOM   2717 C  CZ     . PHE A 1 355 ? -26.55700 12.65600  -26.16600 1.000 16.72498 ? 348 PHE A CZ     1 
ATOM   2718 N  N      . VAL A 1 356 ? -28.45700 16.82000  -25.60200 1.000 19.45776 ? 349 VAL A N      1 
ATOM   2719 C  CA     . VAL A 1 356 ? -28.70500 17.05700  -27.02000 1.000 24.00789 ? 349 VAL A CA     1 
ATOM   2720 C  C      . VAL A 1 356 ? -27.85100 16.08600  -27.82700 1.000 22.21711 ? 349 VAL A C      1 
ATOM   2721 O  O      . VAL A 1 356 ? -26.62000 16.12400  -27.73300 1.000 21.44262 ? 349 VAL A O      1 
ATOM   2722 C  CB     . VAL A 1 356 ? -28.40000 18.50800  -27.42500 1.000 25.67648 ? 349 VAL A CB     1 
ATOM   2723 C  CG1    . VAL A 1 356 ? -28.47100 18.67200  -28.94200 1.000 26.74713 ? 349 VAL A CG1    1 
ATOM   2724 C  CG2    . VAL A 1 356 ? -29.36900 19.47000  -26.73100 1.000 25.88793 ? 349 VAL A CG2    1 
ATOM   2725 N  N      . PRO A 1 357 ? -28.44700 15.22700  -28.65900 1.000 23.57923 ? 350 PRO A N      1 
ATOM   2726 C  CA     . PRO A 1 357 ? -27.64600 14.25600  -29.39300 1.000 22.47320 ? 350 PRO A CA     1 
ATOM   2727 C  C      . PRO A 1 357 ? -26.77800 14.95000  -30.42900 1.000 27.17987 ? 350 PRO A C      1 
ATOM   2728 O  O      . PRO A 1 357 ? -27.15400 16.00400  -30.96800 1.000 24.19816 ? 350 PRO A O      1 
ATOM   2729 C  CB     . PRO A 1 357 ? -28.70000 13.35400  -30.05600 1.000 23.62201 ? 350 PRO A CB     1 
ATOM   2730 C  CG     . PRO A 1 357 ? -29.89900 14.18600  -30.16400 1.000 26.71772 ? 350 PRO A CG     1 
ATOM   2731 C  CD     . PRO A 1 357 ? -29.88200 15.11700  -28.98200 1.000 25.00575 ? 350 PRO A CD     1 
ATOM   2732 N  N      . PRO A 1 358 ? -25.60300 14.40900  -30.72500 1.000 22.37949 ? 351 PRO A N      1 
ATOM   2733 C  CA     . PRO A 1 358 ? -24.77300 15.01000  -31.75100 1.000 25.66291 ? 351 PRO A CA     1 
ATOM   2734 C  C      . PRO A 1 358 ? -25.45800 14.90100  -33.10000 1.000 25.53457 ? 351 PRO A C      1 
ATOM   2735 O  O      . PRO A 1 358 ? -26.36100 14.06900  -33.28600 1.000 28.43569 ? 351 PRO A O      1 
ATOM   2736 C  CB     . PRO A 1 358 ? -23.48100 14.18000  -31.69700 1.000 30.61101 ? 351 PRO A CB     1 
ATOM   2737 C  CG     . PRO A 1 358 ? -23.90100 12.86900  -31.17900 1.000 27.95779 ? 351 PRO A CG     1 
ATOM   2738 C  CD     . PRO A 1 358 ? -25.04400 13.13900  -30.22800 1.000 26.71148 ? 351 PRO A CD     1 
ATOM   2739 N  N      . PRO A 1 359 ? -25.09200 15.73900  -34.05900 1.000 31.22016 ? 352 PRO A N      1 
ATOM   2740 C  CA     . PRO A 1 359 ? -25.66000 15.58700  -35.40000 1.000 32.11371 ? 352 PRO A CA     1 
ATOM   2741 C  C      . PRO A 1 359 ? -25.12600 14.32600  -36.05700 1.000 31.44453 ? 352 PRO A C      1 
ATOM   2742 O  O      . PRO A 1 359 ? -24.10500 13.76200  -35.65200 1.000 30.02110 ? 352 PRO A O      1 
ATOM   2743 C  CB     . PRO A 1 359 ? -25.19600 16.84500  -36.14000 1.000 32.77075 ? 352 PRO A CB     1 
ATOM   2744 C  CG     . PRO A 1 359 ? -23.97000 17.31200  -35.39700 1.000 39.24876 ? 352 PRO A CG     1 
ATOM   2745 C  CD     . PRO A 1 359 ? -23.96000 16.68100  -34.02000 1.000 31.26982 ? 352 PRO A CD     1 
ATOM   2746 N  N      . LEU A 1 360 ? -25.85500 13.86600  -37.07000 1.000 32.94591 ? 353 LEU A N      1 
ATOM   2747 C  CA     . LEU A 1 360 ? -25.31900 12.83200  -37.94000 1.000 32.71538 ? 353 LEU A CA     1 
ATOM   2748 C  C      . LEU A 1 360 ? -24.03800 13.32800  -38.59500 1.000 35.47033 ? 353 LEU A C      1 
ATOM   2749 O  O      . LEU A 1 360 ? -23.92400 14.50000  -38.96700 1.000 38.95880 ? 353 LEU A O      1 
ATOM   2750 C  CB     . LEU A 1 360 ? -26.33500 12.45100  -39.02100 1.000 33.37453 ? 353 LEU A CB     1 
ATOM   2751 C  CG     . LEU A 1 360 ? -27.62900 11.72000  -38.65100 1.000 34.71023 ? 353 LEU A CG     1 
ATOM   2752 C  CD1    . LEU A 1 360 ? -28.57600 11.68000  -39.85600 1.000 32.53889 ? 353 LEU A CD1    1 
ATOM   2753 C  CD2    . LEU A 1 360 ? -27.32400 10.31500  -38.16000 1.000 33.49379 ? 353 LEU A CD2    1 
ATOM   2754 N  N      . ASP A 1 361 ? -23.06700 12.43000  -38.73200 1.000 39.02026 ? 354 ASP A N      1 
ATOM   2755 C  CA     . ASP A 1 361 ? -21.88700 12.73300  -39.53000 1.000 38.43023 ? 354 ASP A CA     1 
ATOM   2756 C  C      . ASP A 1 361 ? -22.28400 13.00400  -40.97900 1.000 40.82419 ? 354 ASP A C      1 
ATOM   2757 O  O      . ASP A 1 361 ? -23.24100 12.42500  -41.50600 1.000 36.02234 ? 354 ASP A O      1 
ATOM   2758 C  CB     . ASP A 1 361 ? -20.89200 11.57900  -39.45600 1.000 41.37051 ? 354 ASP A CB     1 
ATOM   2759 C  CG     . ASP A 1 361 ? -20.16000 11.53800  -38.13800 1.000 52.46459 ? 354 ASP A CG     1 
ATOM   2760 O  OD1    . ASP A 1 361 ? -20.21300 12.56000  -37.41500 1.000 51.33533 ? 354 ASP A OD1    1 
ATOM   2761 O  OD2    . ASP A 1 361 ? -19.54900 10.49400  -37.81800 1.000 57.89398 ? 354 ASP A OD2    1 
ATOM   2762 N  N      . GLN A 1 362 ? -21.54100 13.90400  -41.62800 1.000 37.73992 ? 355 GLN A N      1 
ATOM   2763 C  CA     . GLN A 1 362 ? -21.85200 14.22300  -43.01800 1.000 41.21951 ? 355 GLN A CA     1 
ATOM   2764 C  C      . GLN A 1 362 ? -21.83300 12.96700  -43.88100 1.000 39.79689 ? 355 GLN A C      1 
ATOM   2765 O  O      . GLN A 1 362 ? -22.71600 12.77300  -44.73000 1.000 41.48402 ? 355 GLN A O      1 
ATOM   2766 C  CB     . GLN A 1 362 ? -20.87600 15.27500  -43.54400 1.000 40.53046 ? 355 GLN A CB     1 
ATOM   2767 C  CG     . GLN A 1 362 ? -21.02300 16.62000  -42.84300 1.000 41.89942 ? 355 GLN A CG     1 
ATOM   2768 C  CD     . GLN A 1 362 ? -21.66800 17.67500  -43.73100 1.000 49.47518 ? 355 GLN A CD     1 
ATOM   2769 O  OE1    . GLN A 1 362 ? -22.66400 17.41400  -44.41000 1.000 45.37012 ? 355 GLN A OE1    1 
ATOM   2770 N  NE2    . GLN A 1 362 ? -21.10000 18.87800  -43.72600 1.000 51.68564 ? 355 GLN A NE2    1 
ATOM   2771 N  N      . GLU A 1 363 ? -20.86200 12.07800  -43.64400 1.000 38.84993 ? 356 GLU A N      1 
ATOM   2772 C  CA     . GLU A 1 363 ? -20.76200 10.84200  -44.41900 1.000 39.36619 ? 356 GLU A CA     1 
ATOM   2773 C  C      . GLU A 1 363 ? -22.04200 10.01900  -44.35100 1.000 36.56963 ? 356 GLU A C      1 
ATOM   2774 O  O      . GLU A 1 363 ? -22.31800 9.23500   -45.26500 1.000 37.74368 ? 356 GLU A O      1 
ATOM   2775 C  CB     . GLU A 1 363 ? -19.58100 10.00200  -43.92700 1.000 41.52553 ? 356 GLU A CB     1 
ATOM   2776 C  CG     . GLU A 1 363 ? -18.22200 10.50000  -44.38900 1.000 50.66478 ? 356 GLU A CG     1 
ATOM   2777 C  CD     . GLU A 1 363 ? -17.55100 11.40900  -43.37100 1.000 57.48845 ? 356 GLU A CD     1 
ATOM   2778 O  OE1    . GLU A 1 363 ? -17.87600 12.61600  -43.33900 1.000 56.26003 ? 356 GLU A OE1    1 
ATOM   2779 O  OE2    . GLU A 1 363 ? -16.69700 10.91400  -42.60100 1.000 65.73156 ? 356 GLU A OE2    1 
ATOM   2780 N  N      . GLU A 1 364 ? -22.82500 10.16800  -43.27600 1.000 37.52648 ? 357 GLU A N      1 
ATOM   2781 C  CA     . GLU A 1 364 ? -24.06800 9.41800   -43.08800 1.000 37.02927 ? 357 GLU A CA     1 
ATOM   2782 C  C      . GLU A 1 364 ? -25.21000 9.89200   -43.98300 1.000 36.60021 ? 357 GLU A C      1 
ATOM   2783 O  O      . GLU A 1 364 ? -26.22600 9.19300   -44.07900 1.000 33.28654 ? 357 GLU A O      1 
ATOM   2784 C  CB     . GLU A 1 364 ? -24.52200 9.49800   -41.62100 1.000 34.96491 ? 357 GLU A CB     1 
ATOM   2785 C  CG     . GLU A 1 364 ? -23.65300 8.77700   -40.59000 1.000 37.71474 ? 357 GLU A CG     1 
ATOM   2786 C  CD     . GLU A 1 364 ? -23.33200 7.33100   -40.98100 1.000 48.40620 ? 357 GLU A CD     1 
ATOM   2787 O  OE1    . GLU A 1 364 ? -24.26900 6.61000   -41.40300 1.000 44.14221 ? 357 GLU A OE1    1 
ATOM   2788 O  OE2    . GLU A 1 364 ? -22.16500 6.89700   -40.81300 1.000 49.52708 ? 357 GLU A OE2    1 
ATOM   2789 N  N      . MET A 1 365 ? -25.08300 11.05300  -44.61700 1.000 34.74117 ? 358 MET A N      1 
ATOM   2790 C  CA     . MET A 1 365 ? -26.15500 11.67300  -45.37800 1.000 29.70390 ? 358 MET A CA     1 
ATOM   2791 C  C      . MET A 1 365 ? -25.72200 11.81600  -46.83500 1.000 30.57119 ? 358 MET A C      1 
ATOM   2792 O  O      . MET A 1 365 ? -24.53600 11.72000  -47.16200 1.000 32.88772 ? 358 MET A O      1 
ATOM   2793 C  CB     . MET A 1 365 ? -26.53100 13.03100  -44.75700 1.000 32.65613 ? 358 MET A CB     1 
ATOM   2794 C  CG     . MET A 1 365 ? -27.07000 12.92500  -43.31000 1.000 36.70554 ? 358 MET A CG     1 
ATOM   2795 S  SD     . MET A 1 365 ? -27.25800 14.51200  -42.45700 1.000 36.16545 ? 358 MET A SD     1 
ATOM   2796 C  CE     . MET A 1 365 ? -25.58900 15.16000  -42.59600 1.000 37.04878 ? 358 MET A CE     1 
ATOM   2797 N  N      . GLU A 1 366 ? -26.69100 12.03300  -47.72900 1.000 36.95790 ? 359 GLU A N      1 
ATOM   2798 C  CA     . GLU A 1 366 ? -26.36500 11.89000  -49.14800 1.000 35.21022 ? 359 GLU A CA     1 
ATOM   2799 C  C      . GLU A 1 366 ? -26.24100 13.23200  -49.87300 1.000 44.49464 ? 359 GLU A C      1 
ATOM   2800 O  O      . GLU A 1 366 ? -25.30600 13.99100  -49.59400 1.000 51.86804 ? 359 GLU A O      1 
ATOM   2801 C  CB     . GLU A 1 366 ? -27.38900 10.97700  -49.82400 1.000 29.56429 ? 359 GLU A CB     1 
ATOM   2802 C  CG     . GLU A 1 366 ? -27.51400 9.62100   -49.15000 1.000 30.04292 ? 359 GLU A CG     1 
ATOM   2803 C  CD     . GLU A 1 366 ? -26.94000 8.44800   -49.95600 1.000 27.52437 ? 359 GLU A CD     1 
ATOM   2804 O  OE1    . GLU A 1 366 ? -26.53300 8.62300   -51.12800 1.000 22.85427 ? 359 GLU A OE1    1 
ATOM   2805 O  OE2    . GLU A 1 366 ? -26.95300 7.32700   -49.41100 1.000 23.15980 ? 359 GLU A OE2    1 
ATOM   2806 N  N      . SER A 1 367 ? -27.14600 13.54400  -50.80600 1.000 38.01943 ? 360 SER A N      1 
ATOM   2807 C  CA     . SER A 1 367 ? -26.90900 14.68400  -51.71100 1.000 42.01499 ? 360 SER A CA     1 
ATOM   2808 C  C      . SER A 1 367 ? -27.31300 16.03800  -51.10000 1.000 33.56080 ? 360 SER A C      1 
ATOM   2809 O  O      . SER A 1 367 ? -28.42800 16.20100  -50.60000 1.000 35.50414 ? 360 SER A O      1 
ATOM   2810 C  CB     . SER A 1 367 ? -27.62700 14.46600  -53.06100 1.000 25.27537 ? 360 SER A CB     1 
ATOM   2811 O  OG     . SER A 1 367 ? -28.86600 15.16300  -53.13400 1.000 20.28111 ? 360 SER A OG     1 
HETATM 2812 C  C1     . WHE B 2 .   ? -17.34200 -2.83400  -27.00600 1.000 15.81018 ? 401 WHE A C1     1 
HETATM 2813 C  C2     . WHE B 2 .   ? -18.03000 -0.98500  -25.49100 1.000 12.80791 ? 401 WHE A C2     1 
HETATM 2814 C  C3     . WHE B 2 .   ? -18.39800 0.36500   -25.68200 1.000 13.54765 ? 401 WHE A C3     1 
HETATM 2815 C  C5     . WHE B 2 .   ? -18.02100 -1.53600  -24.22500 1.000 13.47188 ? 401 WHE A C5     1 
HETATM 2816 C  C6     . WHE B 2 .   ? -18.29900 -0.73700  -23.10300 1.000 13.83256 ? 401 WHE A C6     1 
HETATM 2817 C  C7     . WHE B 2 .   ? -18.71300 0.59400   -23.29700 1.000 12.76575 ? 401 WHE A C7     1 
HETATM 2818 N  N4     . WHE B 2 .   ? -17.95000 -5.63200  -30.50700 1.000 27.83778 ? 401 WHE A N4     1 
HETATM 2819 C  C8     . WHE B 2 .   ? -18.73800 1.15900   -24.58500 1.000 13.80257 ? 401 WHE A C8     1 
HETATM 2820 C  C11    . WHE B 2 .   ? -20.93400 4.74400   -22.33900 1.000 16.03395 ? 401 WHE A C11    1 
HETATM 2821 C  C13    . WHE B 2 .   ? -22.34100 3.03000   -23.30100 1.000 15.56194 ? 401 WHE A C13    1 
HETATM 2822 C  C14    . WHE B 2 .   ? -21.38000 2.05500   -23.03800 1.000 16.29188 ? 401 WHE A C14    1 
HETATM 2823 C  C15    . WHE B 2 .   ? -17.29500 -3.49100  -28.39800 1.000 17.38689 ? 401 WHE A C15    1 
HETATM 2824 C  C18    . WHE B 2 .   ? -17.36300 -5.92700  -29.20500 1.000 24.54638 ? 401 WHE A C18    1 
HETATM 2825 C  C20    . WHE B 2 .   ? -18.17600 -1.30100  -21.66000 1.000 14.99607 ? 401 WHE A C20    1 
HETATM 2826 C  C22    . WHE B 2 .   ? -15.64400 -2.27200  -20.45600 1.000 18.35921 ? 401 WHE A C22    1 
HETATM 2827 C  C23    . WHE B 2 .   ? -16.06000 -1.56500  -21.75500 1.000 16.49307 ? 401 WHE A C23    1 
HETATM 2828 C  C10    . WHE B 2 .   ? -19.96500 3.76900   -22.09400 1.000 18.06612 ? 401 WHE A C10    1 
HETATM 2829 C  C12    . WHE B 2 .   ? -22.12500 4.36600   -22.94800 1.000 15.29073 ? 401 WHE A C12    1 
HETATM 2830 C  C16    . WHE B 2 .   ? -16.97500 -4.78400  -28.26800 1.000 19.98868 ? 401 WHE A C16    1 
HETATM 2831 C  C17    . WHE B 2 .   ? -16.40400 -3.39900  -26.22900 1.000 19.23419 ? 401 WHE A C17    1 
HETATM 2832 C  C19    . WHE B 2 .   ? -18.32100 -6.72200  -31.41500 1.000 28.13453 ? 401 WHE A C19    1 
HETATM 2833 C  C21    . WHE B 2 .   ? -16.96800 -1.67000  -19.94700 1.000 20.22397 ? 401 WHE A C21    1 
HETATM 2834 C  C4     . WHE B 2 .   ? -18.30000 0.58000   -27.15500 1.000 14.72189 ? 401 WHE A C4     1 
HETATM 2835 C  C9     . WHE B 2 .   ? -20.18000 2.43600   -22.43300 1.000 13.19831 ? 401 WHE A C9     1 
HETATM 2836 F  F1     . WHE B 2 .   ? -21.61000 0.74400   -23.36900 1.000 11.52755 ? 401 WHE A F1     1 
HETATM 2837 N  N1     . WHE B 2 .   ? -17.78200 -1.45600  -26.76500 1.000 13.44107 ? 401 WHE A N1     1 
HETATM 2838 N  N2     . WHE B 2 .   ? -17.92300 -0.58900  -27.72200 1.000 12.86541 ? 401 WHE A N2     1 
HETATM 2839 N  N3     . WHE B 2 .   ? -19.14700 1.42300   -22.17600 1.000 10.83321 ? 401 WHE A N3     1 
HETATM 2840 N  N5     . WHE B 2 .   ? -17.03400 -1.03600  -21.08600 1.000 15.61130 ? 401 WHE A N5     1 
HETATM 2841 O  O1     . WHE B 2 .   ? -17.16700 -7.04900  -28.84200 1.000 25.60534 ? 401 WHE A O1     1 
HETATM 2842 S  S1     . WHE B 2 .   ? -15.93800 -5.05200  -26.80400 1.000 22.08379 ? 401 WHE A S1     1 
HETATM 2843 CL CL1    . WHE B 2 .   ? -18.42500 4.23900   -21.33900 1.000 20.35299 ? 401 WHE A CL1    1 
HETATM 2844 H  H2     . WHE B 2 .   ? -17.82900 -2.43800  -24.11500 1.000 16.16625 ? 401 WHE A H2     1 
HETATM 2845 H  H10    . WHE B 2 .   ? -18.07900 -4.80800  -30.74500 1.000 33.40534 ? 401 WHE A H10    1 
HETATM 2846 H  H3     . WHE B 2 .   ? -18.97700 2.04900   -24.70400 1.000 16.56308 ? 401 WHE A H3     1 
HETATM 2847 H  H5     . WHE B 2 .   ? -20.78500 5.62900   -22.10000 1.000 19.24074 ? 401 WHE A H5     1 
HETATM 2848 H  H7     . WHE B 2 .   ? -23.13600 2.78900   -23.71600 1.000 18.67433 ? 401 WHE A H7     1 
HETATM 2849 H  H8     . WHE B 2 .   ? -17.46300 -3.05700  -29.20300 1.000 20.86427 ? 401 WHE A H8     1 
HETATM 2850 H  H14    . WHE B 2 .   ? -18.27900 -2.23300  -21.69600 1.000 17.99529 ? 401 WHE A H14    1 
HETATM 2851 H  H15    . WHE B 2 .   ? -18.86200 -0.93000  -21.13700 1.000 17.99529 ? 401 WHE A H15    1 
HETATM 2852 H  H18    . WHE B 2 .   ? -14.88200 -1.90000  -20.05200 1.000 22.03105 ? 401 WHE A H18    1 
HETATM 2853 H  H19    . WHE B 2 .   ? -15.65600 -3.20900  -20.51700 1.000 22.03105 ? 401 WHE A H19    1 
HETATM 2854 H  H20    . WHE B 2 .   ? -15.42900 -0.93300  -22.04600 1.000 19.79168 ? 401 WHE A H20    1 
HETATM 2855 H  H21    . WHE B 2 .   ? -16.35200 -2.16100  -22.41900 1.000 19.79168 ? 401 WHE A H21    1 
HETATM 2856 H  H6     . WHE B 2 .   ? -22.78000 5.00300   -23.12100 1.000 18.34888 ? 401 WHE A H6     1 
HETATM 2857 H  H9     . WHE B 2 .   ? -16.03600 -2.98900  -25.48000 1.000 23.08102 ? 401 WHE A H9     1 
HETATM 2858 H  H13    . WHE B 2 .   ? -18.58700 -7.47000  -30.91300 1.000 33.76144 ? 401 WHE A H13    1 
HETATM 2859 H  H11    . WHE B 2 .   ? -17.58400 -6.94900  -31.95000 1.000 33.76144 ? 401 WHE A H11    1 
HETATM 2860 H  H12    . WHE B 2 .   ? -19.03200 -6.44400  -31.96200 1.000 33.76144 ? 401 WHE A H12    1 
HETATM 2861 H  H16    . WHE B 2 .   ? -17.64700 -2.31000  -19.84300 1.000 24.26876 ? 401 WHE A H16    1 
HETATM 2862 H  H17    . WHE B 2 .   ? -16.85300 -1.09600  -19.21300 1.000 24.26876 ? 401 WHE A H17    1 
HETATM 2863 H  H1     . WHE B 2 .   ? -18.46900 1.37700   -27.60400 1.000 17.66627 ? 401 WHE A H1     1 
HETATM 2864 H  H4     . WHE B 2 .   ? -18.80700 1.32000   -21.38400 1.000 12.99985 ? 401 WHE A H4     1 
HETATM 2865 C  C1     . BOG C 3 .   ? 2.58100   8.93600   1.08000   1.000 25.45707 ? 402 BOG A C1     1 
HETATM 2866 O  O1     . BOG C 3 .   ? 2.98200   7.62600   1.35700   1.000 25.07139 ? 402 BOG A O1     1 
HETATM 2867 C  C2     . BOG C 3 .   ? 1.40200   9.28000   1.99000   1.000 25.46130 ? 402 BOG A C2     1 
HETATM 2868 O  O2     . BOG C 3 .   ? 0.42300   8.29400   1.81600   1.000 23.61723 ? 402 BOG A O2     1 
HETATM 2869 C  C3     . BOG C 3 .   ? 0.88000   10.68700  1.71100   1.000 27.86570 ? 402 BOG A C3     1 
HETATM 2870 O  O3     . BOG C 3 .   ? -0.05300  11.01400  2.70500   1.000 26.84193 ? 402 BOG A O3     1 
HETATM 2871 C  C4     . BOG C 3 .   ? 2.10500   11.60000  1.77600   1.000 27.46064 ? 402 BOG A C4     1 
HETATM 2872 O  O4     . BOG C 3 .   ? 1.71200   12.89700  1.42200   1.000 24.93818 ? 402 BOG A O4     1 
HETATM 2873 C  C5     . BOG C 3 .   ? 3.22500   11.09000  0.85000   1.000 21.17250 ? 402 BOG A C5     1 
HETATM 2874 O  O5     . BOG C 3 .   ? 3.64400   9.82200   1.28900   1.000 21.99465 ? 402 BOG A O5     1 
HETATM 2875 C  C6     . BOG C 3 .   ? 4.43300   12.03100  0.86300   1.000 23.58623 ? 402 BOG A C6     1 
HETATM 2876 O  O6     . BOG C 3 .   ? 5.01700   11.96800  2.13200   1.000 20.59973 ? 402 BOG A O6     1 
HETATM 2877 C  "C1'"  . BOG C 3 .   ? 3.85800   7.06100   0.42500   1.000 27.95743 ? 402 BOG A "C1'"  1 
HETATM 2878 C  "C2'"  . BOG C 3 .   ? 4.64500   5.96100   1.12500   1.000 28.37865 ? 402 BOG A "C2'"  1 
HETATM 2879 C  "C3'"  . BOG C 3 .   ? 5.26800   5.06200   0.06900   1.000 32.04988 ? 402 BOG A "C3'"  1 
HETATM 2880 C  "C4'"  . BOG C 3 .   ? 4.69500   3.68500   0.33500   1.000 31.33698 ? 402 BOG A "C4'"  1 
HETATM 2881 C  "C5'"  . BOG C 3 .   ? 5.77000   2.82100   0.97500   1.000 33.94129 ? 402 BOG A "C5'"  1 
HETATM 2882 C  "C6'"  . BOG C 3 .   ? 5.07300   1.79600   1.86000   1.000 31.95124 ? 402 BOG A "C6'"  1 
HETATM 2883 C  "C7'"  . BOG C 3 .   ? 6.08700   1.04900   2.71300   1.000 31.64697 ? 402 BOG A "C7'"  1 
HETATM 2884 C  "C8'"  . BOG C 3 .   ? 5.45100   0.76700   4.07700   1.000 20.20769 ? 402 BOG A "C8'"  1 
HETATM 2885 H  H1     . BOG C 3 .   ? 2.31000   9.01500   0.15200   1.000 30.54848 ? 402 BOG A H1     1 
HETATM 2886 H  H2     . BOG C 3 .   ? 1.67900   9.28700   2.92000   1.000 30.55355 ? 402 BOG A H2     1 
HETATM 2887 H  HO2    . BOG C 3 .   ? 0.33900   8.10000   0.99100   1.000 28.34067 ? 402 BOG A HO2    1 
HETATM 2888 H  H3     . BOG C 3 .   ? 0.44000   10.77100  0.85000   1.000 33.43884 ? 402 BOG A H3     1 
HETATM 2889 H  HO3    . BOG C 3 .   ? 0.35000   11.28400  3.40400   1.000 32.21031 ? 402 BOG A HO3    1 
HETATM 2890 H  H4     . BOG C 3 .   ? 2.46300   11.60200  2.67700   1.000 32.95277 ? 402 BOG A H4     1 
HETATM 2891 H  HO4    . BOG C 3 .   ? 1.77300   12.98700  0.57900   1.000 29.92582 ? 402 BOG A HO4    1 
HETATM 2892 H  H5     . BOG C 3 .   ? 2.87300   11.04700  -0.05300  1.000 25.40700 ? 402 BOG A H5     1 
HETATM 2893 H  H61    . BOG C 3 .   ? 4.14500   12.93800  0.67800   1.000 28.30347 ? 402 BOG A H61    1 
HETATM 2894 H  H62    . BOG C 3 .   ? 5.07500   11.75200  0.19100   1.000 28.30347 ? 402 BOG A H62    1 
HETATM 2895 H  HO6    . BOG C 3 .   ? 5.68300   12.48800  2.15900   1.000 24.71968 ? 402 BOG A HO6    1 
HETATM 2896 H  "H1'1" . BOG C 3 .   ? 4.46600   7.74000   0.09200   1.000 33.54892 ? 402 BOG A "H1'1" 1 
HETATM 2897 H  "H1'2" . BOG C 3 .   ? 3.35500   6.68700   -0.31500  1.000 33.54892 ? 402 BOG A "H1'2" 1 
HETATM 2898 H  "H2'1" . BOG C 3 .   ? 4.05000   5.44100   1.68700   1.000 34.05439 ? 402 BOG A "H2'1" 1 
HETATM 2899 H  "H2'2" . BOG C 3 .   ? 5.34300   6.35500   1.67100   1.000 34.05439 ? 402 BOG A "H2'2" 1 
HETATM 2900 H  "H3'1" . BOG C 3 .   ? 5.02800   5.36500   -0.82100  1.000 38.45986 ? 402 BOG A "H3'1" 1 
HETATM 2901 H  "H3'2" . BOG C 3 .   ? 6.23400   5.05200   0.15800   1.000 38.45986 ? 402 BOG A "H3'2" 1 
HETATM 2902 H  "H4'1" . BOG C 3 .   ? 4.40900   3.28400   -0.50100  1.000 37.60438 ? 402 BOG A "H4'1" 1 
HETATM 2903 H  "H4'2" . BOG C 3 .   ? 3.93600   3.75800   0.93400   1.000 37.60438 ? 402 BOG A "H4'2" 1 
HETATM 2904 H  "H5'1" . BOG C 3 .   ? 6.36100   3.37300   1.51100   1.000 40.72955 ? 402 BOG A "H5'1" 1 
HETATM 2905 H  "H5'2" . BOG C 3 .   ? 6.28400   2.37000   0.28700   1.000 40.72955 ? 402 BOG A "H5'2" 1 
HETATM 2906 H  "H6'1" . BOG C 3 .   ? 4.59900   1.16100   1.30000   1.000 38.34149 ? 402 BOG A "H6'1" 1 
HETATM 2907 H  "H6'2" . BOG C 3 .   ? 4.44200   2.25100   2.43900   1.000 38.34149 ? 402 BOG A "H6'2" 1 
HETATM 2908 H  "H7'1" . BOG C 3 .   ? 6.88200   1.59200   2.82800   1.000 37.97636 ? 402 BOG A "H7'1" 1 
HETATM 2909 H  "H7'2" . BOG C 3 .   ? 6.32500   0.21300   2.28300   1.000 37.97636 ? 402 BOG A "H7'2" 1 
HETATM 2910 H  "H8'1" . BOG C 3 .   ? 6.08900   0.30300   4.64100   1.000 24.24923 ? 402 BOG A "H8'1" 1 
HETATM 2911 H  "H8'2" . BOG C 3 .   ? 5.19800   1.60500   4.49500   1.000 24.24923 ? 402 BOG A "H8'2" 1 
HETATM 2912 H  "H8'3" . BOG C 3 .   ? 4.66300   0.21400   3.95800   1.000 24.24923 ? 402 BOG A "H8'3" 1 
HETATM 2913 C  C1     . BOG D 3 .   ? 5.12400   10.54900  -6.84600  1.000 19.99935 ? 403 BOG A C1     1 
HETATM 2914 O  O1     . BOG D 3 .   ? 5.63000   9.58900   -7.73400  1.000 14.74006 ? 403 BOG A O1     1 
HETATM 2915 C  C2     . BOG D 3 .   ? 5.94200   11.84000  -6.87900  1.000 17.19853 ? 403 BOG A C2     1 
HETATM 2916 O  O2     . BOG D 3 .   ? 7.25900   11.55200  -6.49300  1.000 17.99069 ? 403 BOG A O2     1 
HETATM 2917 C  C3     . BOG D 3 .   ? 5.37900   12.87600  -5.91400  1.000 22.89240 ? 403 BOG A C3     1 
HETATM 2918 O  O3     . BOG D 3 .   ? 6.02800   14.10700  -6.09000  1.000 23.12195 ? 403 BOG A O3     1 
HETATM 2919 C  C4     . BOG D 3 .   ? 3.90300   13.05300  -6.23300  1.000 25.36925 ? 403 BOG A C4     1 
HETATM 2920 O  O4     . BOG D 3 .   ? 3.29100   13.87700  -5.26800  1.000 22.29110 ? 403 BOG A O4     1 
HETATM 2921 C  C5     . BOG D 3 .   ? 3.21000   11.69100  -6.30000  1.000 22.68939 ? 403 BOG A C5     1 
HETATM 2922 O  O5     . BOG D 3 .   ? 3.80500   10.81000  -7.21000  1.000 21.33729 ? 403 BOG A O5     1 
HETATM 2923 C  C6     . BOG D 3 .   ? 1.79200   12.00800  -6.78000  1.000 23.61390 ? 403 BOG A C6     1 
HETATM 2924 O  O6     . BOG D 3 .   ? 0.90300   10.98700  -6.45600  1.000 28.31581 ? 403 BOG A O6     1 
HETATM 2925 C  "C1'"  . BOG D 3 .   ? 5.13400   8.29700   -7.48800  1.000 19.40004 ? 403 BOG A "C1'"  1 
HETATM 2926 C  "C2'"  . BOG D 3 .   ? 6.10700   7.49200   -6.61700  1.000 19.04287 ? 403 BOG A "C2'"  1 
HETATM 2927 C  "C3'"  . BOG D 3 .   ? 5.60600   6.05100   -6.49900  1.000 18.90334 ? 403 BOG A "C3'"  1 
HETATM 2928 C  "C4'"  . BOG D 3 .   ? 6.62400   5.21100   -5.72600  1.000 21.85790 ? 403 BOG A "C4'"  1 
HETATM 2929 C  "C5'"  . BOG D 3 .   ? 5.96200   3.95500   -5.16000  1.000 27.95936 ? 403 BOG A "C5'"  1 
HETATM 2930 C  "C6'"  . BOG D 3 .   ? 7.00600   2.84100   -5.02400  1.000 31.16048 ? 403 BOG A "C6'"  1 
HETATM 2931 C  "C7'"  . BOG D 3 .   ? 6.65200   1.97300   -3.82000  1.000 33.72802 ? 403 BOG A "C7'"  1 
HETATM 2932 C  "C8'"  . BOG D 3 .   ? 7.85900   1.16300   -3.35300  1.000 33.01747 ? 403 BOG A "C8'"  1 
HETATM 2933 H  H1     . BOG D 3 .   ? 5.17500   10.20500  -5.94000  1.000 23.99922 ? 403 BOG A H1     1 
HETATM 2934 H  H2     . BOG D 3 .   ? 5.90900   12.19900  -7.77900  1.000 20.63824 ? 403 BOG A H2     1 
HETATM 2935 H  HO2    . BOG D 3 .   ? 7.58300   10.94500  -6.99000  1.000 21.58883 ? 403 BOG A HO2    1 
HETATM 2936 H  H3     . BOG D 3 .   ? 5.51000   12.57900  -5.00000  1.000 27.47088 ? 403 BOG A H3     1 
HETATM 2937 H  HO3    . BOG D 3 .   ? 6.75800   13.99200  -6.51800  1.000 27.74634 ? 403 BOG A HO3    1 
HETATM 2938 H  H4     . BOG D 3 .   ? 3.81800   13.48200  -7.09900  1.000 30.44310 ? 403 BOG A H4     1 
HETATM 2939 H  HO4    . BOG D 3 .   ? 3.05800   13.42800  -4.58100  1.000 26.74931 ? 403 BOG A HO4    1 
HETATM 2940 H  H5     . BOG D 3 .   ? 3.25500   11.25100  -5.43700  1.000 27.22727 ? 403 BOG A H5     1 
HETATM 2941 H  H61    . BOG D 3 .   ? 1.80300   12.12300  -7.74300  1.000 28.33668 ? 403 BOG A H61    1 
HETATM 2942 H  H62    . BOG D 3 .   ? 1.49400   12.83100  -6.36000  1.000 28.33668 ? 403 BOG A H62    1 
HETATM 2943 H  HO6    . BOG D 3 .   ? 1.32900   10.34800  -6.09000  1.000 33.97897 ? 403 BOG A HO6    1 
HETATM 2944 H  "H1'1" . BOG D 3 .   ? 5.01100   7.83800   -8.33400  1.000 23.28004 ? 403 BOG A "H1'1" 1 
HETATM 2945 H  "H1'2" . BOG D 3 .   ? 4.28100   8.36600   -7.03100  1.000 23.28004 ? 403 BOG A "H1'2" 1 
HETATM 2946 H  "H2'1" . BOG D 3 .   ? 6.15800   7.89000   -5.73400  1.000 22.85144 ? 403 BOG A "H2'1" 1 
HETATM 2947 H  "H2'2" . BOG D 3 .   ? 6.98700   7.49600   -7.02500  1.000 22.85144 ? 403 BOG A "H2'2" 1 
HETATM 2948 H  "H3'1" . BOG D 3 .   ? 4.75800   6.04300   -6.02800  1.000 22.68401 ? 403 BOG A "H3'1" 1 
HETATM 2949 H  "H3'2" . BOG D 3 .   ? 5.48700   5.67800   -7.38600  1.000 22.68401 ? 403 BOG A "H3'2" 1 
HETATM 2950 H  "H4'1" . BOG D 3 .   ? 6.98500   5.73800   -4.99600  1.000 26.22947 ? 403 BOG A "H4'1" 1 
HETATM 2951 H  "H4'2" . BOG D 3 .   ? 7.34300   4.95100   -6.32300  1.000 26.22947 ? 403 BOG A "H4'2" 1 
HETATM 2952 H  "H5'1" . BOG D 3 .   ? 5.25600   3.66500   -5.75800  1.000 33.55124 ? 403 BOG A "H5'1" 1 
HETATM 2953 H  "H5'2" . BOG D 3 .   ? 5.58600   4.15300   -4.28800  1.000 33.55124 ? 403 BOG A "H5'2" 1 
HETATM 2954 H  "H6'1" . BOG D 3 .   ? 7.88400   3.23300   -4.89500  1.000 37.39257 ? 403 BOG A "H6'1" 1 
HETATM 2955 H  "H6'2" . BOG D 3 .   ? 7.00800   2.29800   -5.82700  1.000 37.39257 ? 403 BOG A "H6'2" 1 
HETATM 2956 H  "H7'1" . BOG D 3 .   ? 5.93900   1.36400   -4.06800  1.000 40.47362 ? 403 BOG A "H7'1" 1 
HETATM 2957 H  "H7'2" . BOG D 3 .   ? 6.35300   2.54300   -3.09500  1.000 40.47362 ? 403 BOG A "H7'2" 1 
HETATM 2958 H  "H8'1" . BOG D 3 .   ? 7.56600   0.46600   -2.74400  1.000 39.62097 ? 403 BOG A "H8'1" 1 
HETATM 2959 H  "H8'2" . BOG D 3 .   ? 8.29500   0.75900   -4.12000  1.000 39.62097 ? 403 BOG A "H8'2" 1 
HETATM 2960 H  "H8'3" . BOG D 3 .   ? 8.48500   1.74800   -2.89700  1.000 39.62097 ? 403 BOG A "H8'3" 1 
HETATM 2961 O  O      . HOH E 4 .   ? -40.38000 0.84600   -19.14300 1.000 36.01123 ? 501 HOH A O      1 
HETATM 2962 O  O      . HOH E 4 .   ? -14.97300 -5.16000  -13.99400 1.000 48.92224 ? 502 HOH A O      1 
HETATM 2963 O  O      . HOH E 4 .   ? 14.91200  2.64200   -2.68900  1.000 31.74127 ? 503 HOH A O      1 
HETATM 2964 O  O      . HOH E 4 .   ? -5.70000  -10.57900 -24.93700 1.000 36.41496 ? 504 HOH A O      1 
HETATM 2965 O  O      . HOH E 4 .   ? -23.03100 0.94700   -12.85800 1.000 45.18448 ? 505 HOH A O      1 
HETATM 2966 O  O      . HOH E 4 .   ? 11.80400  3.09300   -15.20900 1.000 23.12560 ? 506 HOH A O      1 
HETATM 2967 O  O      . HOH E 4 .   ? -44.06200 7.92000   -25.11900 1.000 42.11721 ? 507 HOH A O      1 
HETATM 2968 O  O      . HOH E 4 .   ? -25.23600 16.00800  -48.28600 1.000 39.32922 ? 508 HOH A O      1 
HETATM 2969 O  O      . HOH E 4 .   ? 4.47600   3.67600   -39.25400 1.000 27.03270 ? 509 HOH A O      1 
HETATM 2970 O  O      . HOH E 4 .   ? 11.698    -5.529    6.040     1.000 41.06912 ? 510 HOH A O      1 
HETATM 2971 O  O      . HOH E 4 .   ? 0.18900   20.21400  -39.28800 1.000 21.89908 ? 511 HOH A O      1 
HETATM 2972 O  O      . HOH E 4 .   ? -34.92700 0.35300   -16.21100 1.000 22.24385 ? 512 HOH A O      1 
HETATM 2973 O  O      . HOH E 4 .   ? -19.38800 9.18800   -5.42800  1.000 29.56695 ? 513 HOH A O      1 
HETATM 2974 O  O      . HOH E 4 .   ? 3.72000   -11.48600 -3.91400  1.000 19.79437 ? 514 HOH A O      1 
HETATM 2975 O  O      . HOH E 4 .   ? -0.12400  17.74600  -29.55200 1.000 14.88173 ? 515 HOH A O      1 
HETATM 2976 O  O      . HOH E 4 .   ? -23.70600 3.96100   -33.71000 1.000 25.34666 ? 516 HOH A O      1 
HETATM 2977 O  O      . HOH E 4 .   ? 0.11300   -1.83000  -11.19300 1.000 23.61915 ? 517 HOH A O      1 
HETATM 2978 O  O      . HOH E 4 .   ? -34.26800 -6.52600  -28.10900 1.000 24.88750 ? 518 HOH A O      1 
HETATM 2979 O  O      . HOH E 4 .   ? -6.64000  20.83500  -10.84200 1.000 38.33717 ? 519 HOH A O      1 
HETATM 2980 O  O      . HOH E 4 .   ? 3.97000   16.68400  -8.05200  1.000 39.72232 ? 520 HOH A O      1 
HETATM 2981 O  O      . HOH E 4 .   ? 15.17600  8.28200   7.45500   1.000 37.36897 ? 521 HOH A O      1 
HETATM 2982 O  O      . HOH E 4 .   ? -3.33300  -8.87400  -20.20100 1.000 25.05406 ? 522 HOH A O      1 
HETATM 2983 O  O      . HOH E 4 .   ? -31.08800 11.48300  -27.78500 1.000 27.77521 ? 523 HOH A O      1 
HETATM 2984 O  O      . HOH E 4 .   ? -25.94100 19.88200  -13.65600 1.000 16.89835 ? 524 HOH A O      1 
HETATM 2985 O  O      . HOH E 4 .   ? -36.08500 -3.74700  -23.36300 1.000 29.31274 ? 525 HOH A O      1 
HETATM 2986 O  O      . HOH E 4 .   ? -32.47400 -5.84300  -13.69800 1.000 34.84691 ? 526 HOH A O      1 
HETATM 2987 O  O      . HOH E 4 .   ? 13.20100  2.95900   -9.38200  1.000 29.35101 ? 527 HOH A O      1 
HETATM 2988 O  O      . HOH E 4 .   ? 10.23500  -6.65600  -6.25300  1.000 25.52212 ? 528 HOH A O      1 
HETATM 2989 O  O      . HOH E 4 .   ? 5.58300   6.88100   -36.46100 1.000 26.49217 ? 529 HOH A O      1 
HETATM 2990 O  O      . HOH E 4 .   ? -8.51300  22.84700  -22.66800 1.000 22.77231 ? 530 HOH A O      1 
HETATM 2991 O  O      . HOH E 4 .   ? -10.47600 21.66400  -12.72300 1.000 31.72507 ? 531 HOH A O      1 
HETATM 2992 O  O      . HOH E 4 .   ? -13.52700 1.66800   -15.76100 1.000 19.01417 ? 532 HOH A O      1 
HETATM 2993 O  O      . HOH E 4 .   ? -19.61000 14.43800  -1.41100  1.000 25.50593 ? 533 HOH A O      1 
HETATM 2994 O  O      . HOH E 4 .   ? -17.49900 13.27000  -2.48300  1.000 35.69990 ? 534 HOH A O      1 
HETATM 2995 O  O      . HOH E 4 .   ? 3.23700   14.11100  -9.95300  1.000 30.20159 ? 535 HOH A O      1 
HETATM 2996 O  O      . HOH E 4 .   ? -34.64600 14.63200  -6.30200  1.000 23.15988 ? 536 HOH A O      1 
HETATM 2997 O  O      . HOH E 4 .   ? 3.51300   18.77400  -21.32000 1.000 14.74463 ? 537 HOH A O      1 
HETATM 2998 O  O      . HOH E 4 .   ? -26.39600 5.05000   -33.86300 1.000 26.61187 ? 538 HOH A O      1 
HETATM 2999 O  O      . HOH E 4 .   ? -26.75300 6.57800   -40.02200 1.000 29.89910 ? 539 HOH A O      1 
HETATM 3000 O  O      . HOH E 4 .   ? 8.67400   14.84000  -26.83000 1.000 23.27295 ? 540 HOH A O      1 
HETATM 3001 O  O      . HOH E 4 .   ? -0.65800  14.63600  -20.01500 1.000 10.30344 ? 541 HOH A O      1 
HETATM 3002 O  O      . HOH E 4 .   ? 10.16000  10.55500  -18.70200 1.000 18.04362 ? 542 HOH A O      1 
HETATM 3003 O  O      . HOH E 4 .   ? 15.33100  -10.11300 -22.41000 1.000 23.45349 ? 543 HOH A O      1 
HETATM 3004 O  O      . HOH E 4 .   ? 8.98900   0.15700   -37.51400 1.000 31.14353 ? 544 HOH A O      1 
HETATM 3005 O  O      . HOH E 4 .   ? -44.260   -0.883    -24.951   1.000 34.48234 ? 545 HOH A O      1 
HETATM 3006 O  O      . HOH E 4 .   ? -30.35200 21.96400  -4.80200  1.000 28.47614 ? 546 HOH A O      1 
HETATM 3007 O  O      . HOH E 4 .   ? -23.90800 5.03400   -11.12100 1.000 24.26265 ? 547 HOH A O      1 
HETATM 3008 O  O      . HOH E 4 .   ? -6.17100  16.73800  -13.49400 1.000 16.26745 ? 548 HOH A O      1 
HETATM 3009 O  O      . HOH E 4 .   ? -31.28500 8.33400   -39.60500 1.000 15.71400 ? 549 HOH A O      1 
HETATM 3010 O  O      . HOH E 4 .   ? 5.11400   -13.38300 -8.05600  1.000 13.77054 ? 550 HOH A O      1 
HETATM 3011 O  O      . HOH E 4 .   ? -11.80600 20.76700  -14.97100 1.000 21.67854 ? 551 HOH A O      1 
HETATM 3012 O  O      . HOH E 4 .   ? -1.55600  16.34700  -13.02600 1.000 26.22037 ? 552 HOH A O      1 
HETATM 3013 O  O      . HOH E 4 .   ? 6.10000   -8.90300  -14.47100 1.000 15.42908 ? 553 HOH A O      1 
HETATM 3014 O  O      . HOH E 4 .   ? -32.77300 12.33300  -22.95000 1.000 35.57880 ? 554 HOH A O      1 
HETATM 3015 O  O      . HOH E 4 .   ? -22.45700 13.64900  -27.28900 1.000 24.31020 ? 555 HOH A O      1 
HETATM 3016 O  O      . HOH E 4 .   ? -20.32000 12.95600  -25.44100 1.000 14.34801 ? 556 HOH A O      1 
HETATM 3017 O  O      . HOH E 4 .   ? 5.53200   -6.26800  -31.47400 1.000 31.29268 ? 557 HOH A O      1 
HETATM 3018 O  O      . HOH E 4 .   ? 5.83800   14.88000  -15.59100 1.000 30.22781 ? 558 HOH A O      1 
HETATM 3019 O  O      . HOH E 4 .   ? 1.21300   24.62200  -38.75900 1.000 23.02006 ? 559 HOH A O      1 
HETATM 3020 O  O      . HOH E 4 .   ? -35.25500 16.35100  -0.53900  1.000 44.79636 ? 560 HOH A O      1 
HETATM 3021 O  O      . HOH E 4 .   ? -20.54200 3.06700   -14.29900 1.000 25.65267 ? 561 HOH A O      1 
HETATM 3022 O  O      . HOH E 4 .   ? -2.73200  16.20400  -1.24300  1.000 48.36065 ? 562 HOH A O      1 
HETATM 3023 O  O      . HOH E 4 .   ? -44.65300 3.33200   -30.80000 1.000 27.56013 ? 563 HOH A O      1 
HETATM 3024 O  O      . HOH E 4 .   ? -37.63700 -13.98200 -15.28600 1.000 40.92686 ? 564 HOH A O      1 
HETATM 3025 O  O      . HOH E 4 .   ? -16.58100 25.13200  -21.43100 1.000 32.23492 ? 565 HOH A O      1 
HETATM 3026 O  O      . HOH E 4 .   ? -25.61300 18.74100  2.19200   1.000 28.91195 ? 566 HOH A O      1 
HETATM 3027 O  O      . HOH E 4 .   ? -16.94800 19.62900  -24.47200 1.000 13.64645 ? 567 HOH A O      1 
HETATM 3028 O  O      . HOH E 4 .   ? -2.14300  22.75200  -40.47800 1.000 31.04300 ? 568 HOH A O      1 
HETATM 3029 O  O      . HOH E 4 .   ? -3.95200  -8.10100  -8.82900  1.000 22.08774 ? 569 HOH A O      1 
HETATM 3030 O  O      . HOH E 4 .   ? -32.60500 -14.18100 -17.92200 1.000 35.32532 ? 570 HOH A O      1 
HETATM 3031 O  O      . HOH E 4 .   ? -12.13100 10.05000  -14.29900 1.000 15.32326 ? 571 HOH A O      1 
HETATM 3032 O  O      . HOH E 4 .   ? -8.45100  19.17700  -35.21500 1.000 21.39333 ? 572 HOH A O      1 
HETATM 3033 O  O      . HOH E 4 .   ? -14.54700 -0.52300  -17.32800 1.000 24.07117 ? 573 HOH A O      1 
HETATM 3034 O  O      . HOH E 4 .   ? -15.43100 2.81800   -14.36500 1.000 26.21123 ? 574 HOH A O      1 
HETATM 3035 O  O      . HOH E 4 .   ? -6.07900  -7.05000  -19.83000 1.000 22.22254 ? 575 HOH A O      1 
HETATM 3036 O  O      . HOH E 4 .   ? -38.50100 11.96000  -18.03300 1.000 35.33818 ? 576 HOH A O      1 
HETATM 3037 O  O      . HOH E 4 .   ? 17.81100  4.42200   -3.34100  1.000 33.67624 ? 577 HOH A O      1 
HETATM 3038 O  O      . HOH E 4 .   ? 8.73100   -2.48000  -32.13900 1.000 19.96440 ? 578 HOH A O      1 
HETATM 3039 O  O      . HOH E 4 .   ? -9.77800  15.70900  -36.97600 1.000 34.53352 ? 579 HOH A O      1 
HETATM 3040 O  O      . HOH E 4 .   ? -1.43700  -12.30300 -18.36700 1.000 22.79559 ? 580 HOH A O      1 
HETATM 3041 O  O      . HOH E 4 .   ? -5.44600  -1.67600  -14.01700 1.000 18.01159 ? 581 HOH A O      1 
HETATM 3042 O  O      . HOH E 4 .   ? 2.15500   -13.26800 -12.38300 1.000 16.54219 ? 582 HOH A O      1 
HETATM 3043 O  O      . HOH E 4 .   ? -19.54900 19.99700  -19.79000 1.000 24.79713 ? 583 HOH A O      1 
HETATM 3044 O  O      . HOH E 4 .   ? -7.92800  5.97900   -40.07000 1.000 42.72496 ? 584 HOH A O      1 
HETATM 3045 O  O      . HOH E 4 .   ? -14.98500 -7.64600  -23.96000 1.000 40.94206 ? 585 HOH A O      1 
HETATM 3046 O  O      . HOH E 4 .   ? -14.55500 14.26400  -5.41300  1.000 35.53040 ? 586 HOH A O      1 
HETATM 3047 O  O      . HOH E 4 .   ? 12.58600  4.50600   -17.00400 1.000 22.39813 ? 587 HOH A O      1 
HETATM 3048 O  O      . HOH E 4 .   ? 1.41300   -8.13300  -30.14200 1.000 36.12389 ? 588 HOH A O      1 
HETATM 3049 O  O      . HOH E 4 .   ? -15.13500 14.70200  -12.31600 1.000 21.83297 ? 589 HOH A O      1 
HETATM 3050 O  O      . HOH E 4 .   ? -6.80200  -7.66000  -16.23200 1.000 28.83618 ? 590 HOH A O      1 
HETATM 3051 O  O      . HOH E 4 .   ? 4.28600   16.22700  -37.89600 1.000 31.91761 ? 591 HOH A O      1 
HETATM 3052 O  O      . HOH E 4 .   ? 0.59300   10.70300  -9.51100  1.000 17.12506 ? 592 HOH A O      1 
HETATM 3053 O  O      . HOH E 4 .   ? -11.87600 -7.73200  -22.51900 1.000 21.41665 ? 593 HOH A O      1 
HETATM 3054 O  O      . HOH E 4 .   ? -4.64000  -2.69700  -4.79600  1.000 21.73752 ? 594 HOH A O      1 
HETATM 3055 O  O      . HOH E 4 .   ? 15.72100  -5.26500  -10.70000 1.000 30.78346 ? 595 HOH A O      1 
HETATM 3056 O  O      . HOH E 4 .   ? 5.75400   12.60400  -33.22200 1.000 17.22093 ? 596 HOH A O      1 
HETATM 3057 O  O      . HOH E 4 .   ? -28.48200 6.44900   -30.43800 1.000 26.75450 ? 597 HOH A O      1 
HETATM 3058 O  O      . HOH E 4 .   ? -28.66200 9.47100   -31.18500 1.000 22.89139 ? 598 HOH A O      1 
HETATM 3059 O  O      . HOH E 4 .   ? -43.05900 -1.62700  -27.37900 1.000 25.52197 ? 599 HOH A O      1 
HETATM 3060 O  O      . HOH E 4 .   ? 5.959     14.756    -0.717    1.000 21.51258 ? 600 HOH A O      1 
HETATM 3061 O  O      . HOH E 4 .   ? 19.12200  -0.35900  1.56700   1.000 31.46228 ? 601 HOH A O      1 
HETATM 3062 O  O      . HOH E 4 .   ? -22.36900 14.64900  -1.48500  1.000 21.81873 ? 602 HOH A O      1 
HETATM 3063 O  O      . HOH E 4 .   ? -13.27100 -4.19700  -17.66400 1.000 32.80849 ? 603 HOH A O      1 
HETATM 3064 O  O      . HOH E 4 .   ? 5.04100   -6.97800  -21.79600 1.000 16.46847 ? 604 HOH A O      1 
HETATM 3065 O  O      . HOH E 4 .   ? 1.55600   16.15900  -15.58400 1.000 28.84122 ? 605 HOH A O      1 
HETATM 3066 O  O      . HOH E 4 .   ? 14.218    3.389     -34.612   1.000 23.40655 ? 606 HOH A O      1 
HETATM 3067 O  O      . HOH E 4 .   ? 15.38000  -4.11900  -29.65700 1.000 28.27372 ? 607 HOH A O      1 
HETATM 3068 O  O      . HOH E 4 .   ? -14.52200 19.84700  -25.81800 1.000 14.71663 ? 608 HOH A O      1 
HETATM 3069 O  O      . HOH E 4 .   ? 0.66400   -4.88700  -19.64700 1.000 11.78846 ? 609 HOH A O      1 
HETATM 3070 O  O      . HOH E 4 .   ? -4.34600  13.87000  -38.28400 1.000 35.19991 ? 610 HOH A O      1 
HETATM 3071 O  O      . HOH E 4 .   ? -23.38700 18.75000  -19.14900 1.000 19.22056 ? 611 HOH A O      1 
HETATM 3072 O  O      . HOH E 4 .   ? 16.61000  9.58200   -24.96100 1.000 37.49331 ? 612 HOH A O      1 
HETATM 3073 O  O      . HOH E 4 .   ? -6.14700  15.51600  -29.29800 1.000 11.47110 ? 613 HOH A O      1 
HETATM 3074 O  O      . HOH E 4 .   ? 9.72200   13.35100  7.43200   1.000 25.44536 ? 614 HOH A O      1 
HETATM 3075 O  O      . HOH E 4 .   ? -5.30700  2.87300   -13.49100 1.000 15.32881 ? 615 HOH A O      1 
HETATM 3076 O  O      . HOH E 4 .   ? 0.99100   -4.68000  -16.84000 1.000 8.49791  ? 616 HOH A O      1 
HETATM 3077 O  O      . HOH E 4 .   ? -39.07200 8.82300   -20.40800 1.000 28.35536 ? 617 HOH A O      1 
HETATM 3078 O  O      . HOH E 4 .   ? -34.19200 -5.34600  -35.61100 1.000 29.31651 ? 618 HOH A O      1 
HETATM 3079 O  O      . HOH E 4 .   ? 3.04200   -11.94200 -18.68500 1.000 18.23766 ? 619 HOH A O      1 
HETATM 3080 O  O      . HOH E 4 .   ? -21.82700 6.23500   -12.58700 1.000 16.64837 ? 620 HOH A O      1 
HETATM 3081 O  O      . HOH E 4 .   ? -14.52800 -4.26100  -23.53900 1.000 15.06261 ? 621 HOH A O      1 
HETATM 3082 O  O      . HOH E 4 .   ? -2.98000  4.20500   -13.23000 1.000 11.23200 ? 622 HOH A O      1 
HETATM 3083 O  O      . HOH E 4 .   ? -32.44600 20.42400  -17.69600 1.000 28.95622 ? 623 HOH A O      1 
HETATM 3084 O  O      . HOH E 4 .   ? 2.97600   -3.09100  -40.62500 1.000 40.54245 ? 624 HOH A O      1 
HETATM 3085 O  O      . HOH E 4 .   ? -31.56200 20.04800  -9.55900  1.000 33.45992 ? 625 HOH A O      1 
HETATM 3086 O  O      . HOH E 4 .   ? 12.42000  12.37100  7.62500   1.000 29.32928 ? 626 HOH A O      1 
HETATM 3087 O  O      . HOH E 4 .   ? -23.12900 7.72600   0.59400   1.000 35.66530 ? 627 HOH A O      1 
HETATM 3088 O  O      . HOH E 4 .   ? -17.23900 6.16300   -17.54500 1.000 23.01049 ? 628 HOH A O      1 
HETATM 3089 O  O      . HOH E 4 .   ? -5.22800  14.92800  -8.28800  1.000 34.05741 ? 629 HOH A O      1 
HETATM 3090 O  O      . HOH E 4 .   ? -43.47100 3.85000   -22.88500 1.000 23.42935 ? 630 HOH A O      1 
HETATM 3091 O  O      . HOH E 4 .   ? -9.36200  -1.62300  -13.23500 1.000 18.35818 ? 631 HOH A O      1 
HETATM 3092 O  O      . HOH E 4 .   ? -23.87100 15.88400  -27.24400 1.000 30.79163 ? 632 HOH A O      1 
HETATM 3093 O  O      . HOH E 4 .   ? 3.06800   -13.39400 -9.95800  1.000 11.85794 ? 633 HOH A O      1 
HETATM 3094 O  O      . HOH E 4 .   ? 9.09800   15.10400  -19.61800 1.000 24.84092 ? 634 HOH A O      1 
HETATM 3095 O  O      . HOH E 4 .   ? -6.22300  0.83700   -15.15800 1.000 12.45896 ? 635 HOH A O      1 
HETATM 3096 O  O      . HOH E 4 .   ? -15.16500 18.60200  -30.38200 1.000 29.17480 ? 636 HOH A O      1 
HETATM 3097 O  O      . HOH E 4 .   ? -0.15400  16.30200  -17.78200 1.000 17.20146 ? 637 HOH A O      1 
HETATM 3098 O  O      . HOH E 4 .   ? -41.04600 4.39600   -30.01600 1.000 27.36438 ? 638 HOH A O      1 
HETATM 3099 O  O      . HOH E 4 .   ? -4.13400  19.34100  -40.17100 1.000 31.43124 ? 639 HOH A O      1 
HETATM 3100 O  O      . HOH E 4 .   ? 16.56800  0.52800   10.67600  1.000 24.79947 ? 640 HOH A O      1 
HETATM 3101 O  O      . HOH E 4 .   ? -36.422   -6.562    -34.119   1.000 18.91532 ? 641 HOH A O      1 
HETATM 3102 O  O      . HOH E 4 .   ? -16.85400 11.32900  -4.32500  1.000 34.93748 ? 642 HOH A O      1 
HETATM 3103 O  O      . HOH E 4 .   ? -11.99600 17.19800  -30.11500 1.000 14.83454 ? 643 HOH A O      1 
HETATM 3104 O  O      . HOH E 4 .   ? -31.11400 3.95700   -6.86100  1.000 33.84258 ? 644 HOH A O      1 
HETATM 3105 O  O      . HOH E 4 .   ? -5.34600  5.10900   -16.23300 1.000 9.21965  ? 645 HOH A O      1 
HETATM 3106 O  O      . HOH E 4 .   ? -16.18300 11.93700  -27.77700 1.000 11.34780 ? 646 HOH A O      1 
HETATM 3107 O  O      . HOH E 4 .   ? -34.54900 -1.92000  -13.61500 1.000 30.28558 ? 647 HOH A O      1 
HETATM 3108 O  O      . HOH E 4 .   ? -27.58300 -1.32700  -41.12300 1.000 29.22698 ? 648 HOH A O      1 
HETATM 3109 O  O      . HOH E 4 .   ? 11.85600  11.92700  -29.86300 1.000 18.07849 ? 649 HOH A O      1 
HETATM 3110 O  O      . HOH E 4 .   ? -32.67100 14.37900  -24.79000 1.000 38.02398 ? 650 HOH A O      1 
HETATM 3111 O  O      . HOH E 4 .   ? 3.41600   -13.23200 -27.12000 1.000 31.76703 ? 651 HOH A O      1 
HETATM 3112 O  O      . HOH E 4 .   ? 7.02400   6.64300   10.47800  1.000 23.44137 ? 652 HOH A O      1 
HETATM 3113 O  O      . HOH E 4 .   ? -4.47500  -8.12700  -2.64400  1.000 26.53329 ? 653 HOH A O      1 
HETATM 3114 O  O      . HOH E 4 .   ? -20.95500 18.07300  -18.54400 1.000 12.20825 ? 654 HOH A O      1 
HETATM 3115 O  O      . HOH E 4 .   ? -22.199   21.076    -45.141   1.000 37.06359 ? 655 HOH A O      1 
HETATM 3116 O  O      . HOH E 4 .   ? -4.22700  20.50400  -32.67800 1.000 16.10931 ? 656 HOH A O      1 
HETATM 3117 O  O      . HOH E 4 .   ? -7.55900  3.24000   -10.65000 1.000 40.17958 ? 657 HOH A O      1 
HETATM 3118 O  O      . HOH E 4 .   ? -10.15800 13.88900  -12.67200 1.000 19.48334 ? 658 HOH A O      1 
HETATM 3119 O  O      . HOH E 4 .   ? -31.516   14.163    -52.919   1.000 26.42349 ? 659 HOH A O      1 
HETATM 3120 O  O      . HOH E 4 .   ? -19.99000 21.13100  -11.67800 1.000 16.67549 ? 660 HOH A O      1 
HETATM 3121 O  O      . HOH E 4 .   ? -14.49700 25.87400  -28.28800 1.000 32.77267 ? 661 HOH A O      1 
HETATM 3122 O  O      . HOH E 4 .   ? -34.23800 7.68300   -26.97600 1.000 19.25032 ? 662 HOH A O      1 
HETATM 3123 O  O      . HOH E 4 .   ? 16.21400  -3.26600  -27.57200 1.000 31.12274 ? 663 HOH A O      1 
HETATM 3124 O  O      . HOH E 4 .   ? 14.71300  9.08100   -7.54900  1.000 23.87321 ? 664 HOH A O      1 
HETATM 3125 O  O      . HOH E 4 .   ? 13.67700  6.00400   8.34400   1.000 30.28603 ? 665 HOH A O      1 
HETATM 3126 O  O      . HOH E 4 .   ? -15.44800 -2.23100  -38.05700 1.000 40.90184 ? 666 HOH A O      1 
HETATM 3127 O  O      . HOH E 4 .   ? 13.47300  -7.81300  -0.49200  1.000 38.61436 ? 667 HOH A O      1 
HETATM 3128 O  O      . HOH E 4 .   ? 3.84900   13.64300  -2.32800  1.000 27.36221 ? 668 HOH A O      1 
HETATM 3129 O  O      . HOH E 4 .   ? -3.05600  17.85500  -22.51200 1.000 10.29710 ? 669 HOH A O      1 
HETATM 3130 O  O      . HOH E 4 .   ? -13.99000 20.91700  -7.31900  1.000 30.06918 ? 670 HOH A O      1 
HETATM 3131 O  O      . HOH E 4 .   ? 7.89100   -12.94200 -8.51400  1.000 16.24698 ? 671 HOH A O      1 
HETATM 3132 O  O      . HOH E 4 .   ? 0.87400   -1.55700  -13.22400 1.000 14.87222 ? 672 HOH A O      1 
HETATM 3133 O  O      . HOH E 4 .   ? -38.04200 4.55700   -30.13500 1.000 23.77298 ? 673 HOH A O      1 
HETATM 3134 O  O      . HOH E 4 .   ? -18.43200 21.76400  -24.55000 1.000 33.80134 ? 674 HOH A O      1 
HETATM 3135 O  O      . HOH E 4 .   ? 4.80100   9.19400   3.83800   1.000 16.98025 ? 675 HOH A O      1 
HETATM 3136 O  O      . HOH E 4 .   ? -20.33200 -1.75400  -34.91000 1.000 32.65641 ? 676 HOH A O      1 
HETATM 3137 O  O      . HOH E 4 .   ? -11.82300 19.93400  -29.55600 1.000 16.09473 ? 677 HOH A O      1 
HETATM 3138 O  O      . HOH E 4 .   ? 5.73500   14.18000  -37.50200 1.000 31.34338 ? 678 HOH A O      1 
HETATM 3139 O  O      . HOH E 4 .   ? 16.88700  10.45500  -0.09600  1.000 32.31078 ? 679 HOH A O      1 
HETATM 3140 O  O      . HOH E 4 .   ? -11.54300 6.76300   -33.39800 1.000 27.10040 ? 680 HOH A O      1 
HETATM 3141 O  O      . HOH E 4 .   ? -25.79700 17.52900  -24.70100 1.000 21.05756 ? 681 HOH A O      1 
HETATM 3142 O  O      . HOH E 4 .   ? 8.52800   -7.77200  -13.27000 1.000 22.29076 ? 682 HOH A O      1 
HETATM 3143 O  O      . HOH E 4 .   ? -6.56200  -3.71700  -3.56900  1.000 38.69576 ? 683 HOH A O      1 
HETATM 3144 O  O      . HOH E 4 .   ? -17.11200 3.88700   -15.65800 1.000 25.86873 ? 684 HOH A O      1 
HETATM 3145 O  O      . HOH E 4 .   ? 13.26000  10.73300  -9.37700  1.000 28.77786 ? 685 HOH A O      1 
HETATM 3146 O  O      . HOH E 4 .   ? 7.07400   -11.71100 -26.28400 1.000 31.86680 ? 686 HOH A O      1 
HETATM 3147 O  O      . HOH E 4 .   ? -32.72900 18.18800  -24.75700 1.000 39.65502 ? 687 HOH A O      1 
HETATM 3148 O  O      . HOH E 4 .   ? -17.127   24.780    -18.054   1.000 31.21128 ? 688 HOH A O      1 
HETATM 3149 O  O      . HOH E 4 .   ? 2.57400   17.73000  -29.06700 1.000 18.56073 ? 689 HOH A O      1 
HETATM 3150 O  O      . HOH E 4 .   ? 5.867     15.876    -3.786    1.000 38.69615 ? 690 HOH A O      1 
HETATM 3151 O  O      . HOH E 4 .   ? 8.46500   3.37300   -38.33600 1.000 38.31565 ? 691 HOH A O      1 
HETATM 3152 O  O      . HOH E 4 .   ? -13.64300 22.96900  -12.57100 1.000 24.80998 ? 692 HOH A O      1 
HETATM 3153 O  O      . HOH E 4 .   ? -23.20100 9.82000   -37.42400 1.000 43.49256 ? 693 HOH A O      1 
HETATM 3154 O  O      . HOH E 4 .   ? 0.41500   -12.39900 -20.47100 1.000 22.22208 ? 694 HOH A O      1 
HETATM 3155 O  O      . HOH E 4 .   ? 7.07000   -4.81000  -36.94400 1.000 27.03985 ? 695 HOH A O      1 
HETATM 3156 O  O      . HOH E 4 .   ? -34.90900 17.71600  -11.60100 1.000 25.54009 ? 696 HOH A O      1 
HETATM 3157 O  O      . HOH E 4 .   ? -42.34800 -4.90400  -23.17000 1.000 27.82927 ? 697 HOH A O      1 
HETATM 3158 O  O      . HOH E 4 .   ? 7.63700   17.81800  -18.15100 1.000 37.05975 ? 698 HOH A O      1 
HETATM 3159 O  O      . HOH E 4 .   ? -18.72700 21.60800  -17.64300 1.000 26.05605 ? 699 HOH A O      1 
HETATM 3160 O  O      . HOH E 4 .   ? 11.80100  7.27700   -10.61000 1.000 18.48566 ? 700 HOH A O      1 
HETATM 3161 O  O      . HOH E 4 .   ? -40.74300 15.87400  -12.76500 1.000 34.37690 ? 701 HOH A O      1 
HETATM 3162 O  O      . HOH E 4 .   ? -10.90200 -5.20000  -15.30900 1.000 33.13209 ? 702 HOH A O      1 
HETATM 3163 O  O      . HOH E 4 .   ? 13.34900  6.34000   -8.45400  1.000 26.29336 ? 703 HOH A O      1 
HETATM 3164 O  O      . HOH E 4 .   ? -3.17900  13.09500  -36.83200 1.000 34.38260 ? 704 HOH A O      1 
HETATM 3165 O  O      . HOH E 4 .   ? -26.48800 19.44100  -22.17900 1.000 24.23310 ? 705 HOH A O      1 
HETATM 3166 O  O      . HOH E 4 .   ? 16.236    2.143     -27.025   1.000 28.20430 ? 706 HOH A O      1 
HETATM 3167 O  O      . HOH E 4 .   ? 18.30300  -5.63700  -17.30500 1.000 30.88717 ? 707 HOH A O      1 
HETATM 3168 O  O      . HOH E 4 .   ? -23.63700 11.00900  -34.61300 1.000 35.93729 ? 708 HOH A O      1 
HETATM 3169 O  O      . HOH E 4 .   ? -25.87300 7.48200   1.78200   1.000 39.75218 ? 709 HOH A O      1 
HETATM 3170 O  O      . HOH E 4 .   ? -26.72900 -3.50800  -1.88200  1.000 40.72025 ? 710 HOH A O      1 
HETATM 3171 O  O      . HOH E 4 .   ? -18.09400 7.29000   -29.50800 1.000 25.12353 ? 711 HOH A O      1 
HETATM 3172 O  O      . HOH E 4 .   ? -30.52700 -2.55600  -1.59500  1.000 43.30306 ? 712 HOH A O      1 
HETATM 3173 O  O      . HOH E 4 .   ? -11.44600 15.07700  -32.16000 1.000 22.03418 ? 713 HOH A O      1 
HETATM 3174 O  O      . HOH E 4 .   ? -1.81100  -13.06300 -12.04000 1.000 21.81586 ? 714 HOH A O      1 
HETATM 3175 O  O      . HOH E 4 .   ? -11.21500 22.63500  -17.41700 1.000 17.62308 ? 715 HOH A O      1 
HETATM 3176 O  O      . HOH E 4 .   ? -9.50700  -8.12600  -10.54200 1.000 34.65184 ? 716 HOH A O      1 
HETATM 3177 O  O      . HOH E 4 .   ? -36.46900 4.96900   -13.83400 1.000 22.87515 ? 717 HOH A O      1 
HETATM 3178 O  O      . HOH E 4 .   ? 10.02300  4.44100   -36.07400 1.000 25.07383 ? 718 HOH A O      1 
HETATM 3179 O  O      . HOH E 4 .   ? 12.91100  -10.47900 -22.64700 1.000 31.67644 ? 719 HOH A O      1 
HETATM 3180 O  O      . HOH E 4 .   ? 11.13600  8.85200   -36.58200 1.000 33.02385 ? 720 HOH A O      1 
HETATM 3181 O  O      . HOH E 4 .   ? -31.01700 10.70000  -30.93200 1.000 35.43730 ? 721 HOH A O      1 
HETATM 3182 O  O      . HOH E 4 .   ? -16.36100 16.48100  -0.07100  1.000 45.48557 ? 722 HOH A O      1 
HETATM 3183 O  O      . HOH E 4 .   ? -35.26300 9.99500   -21.26600 1.000 19.88288 ? 723 HOH A O      1 
HETATM 3184 O  O      . HOH E 4 .   ? -14.72100 3.09700   -12.04800 1.000 20.56251 ? 724 HOH A O      1 
HETATM 3185 O  O      . HOH E 4 .   ? -0.832    -1.325    -39.905   1.000 41.10842 ? 725 HOH A O      1 
HETATM 3186 O  O      . HOH E 4 .   ? -23.04800 14.77300  1.17400   1.000 35.74807 ? 726 HOH A O      1 
HETATM 3187 O  O      . HOH E 4 .   ? 5.83600   -1.90400  -39.06900 1.000 27.92082 ? 727 HOH A O      1 
HETATM 3188 O  O      . HOH E 4 .   ? -15.00600 -8.67600  -30.78600 1.000 35.91577 ? 728 HOH A O      1 
HETATM 3189 O  O      . HOH E 4 .   ? -27.59000 21.13800  -18.25100 1.000 37.92866 ? 729 HOH A O      1 
HETATM 3190 O  O      . HOH E 4 .   ? -8.24900  -5.12100  -19.32000 1.000 15.04843 ? 730 HOH A O      1 
HETATM 3191 O  O      . HOH E 4 .   ? 4.02600   16.21400  -14.47400 1.000 41.22863 ? 731 HOH A O      1 
HETATM 3192 O  O      . HOH E 4 .   ? -0.59200  16.61900  -21.95400 1.000 9.99504  ? 732 HOH A O      1 
HETATM 3193 O  O      . HOH E 4 .   ? -1.63900  -10.79100 -22.81400 1.000 27.71082 ? 733 HOH A O      1 
HETATM 3194 O  O      . HOH E 4 .   ? 15.71700  12.19700  -24.15700 1.000 42.03030 ? 734 HOH A O      1 
HETATM 3195 O  O      . HOH E 4 .   ? -5.98800  21.03200  -39.19500 1.000 35.83499 ? 735 HOH A O      1 
HETATM 3196 O  O      . HOH E 4 .   ? 11.99500  4.27100   -12.23900 1.000 30.36814 ? 736 HOH A O      1 
HETATM 3197 O  O      . HOH E 4 .   ? -25.22600 18.26100  -29.47200 1.000 31.41854 ? 737 HOH A O      1 
HETATM 3198 O  O      . HOH E 4 .   ? -9.52600  -4.46100  -35.94500 1.000 35.25277 ? 738 HOH A O      1 
HETATM 3199 O  O      . HOH E 4 .   ? -22.95700 -0.36900  -38.91400 1.000 34.49622 ? 739 HOH A O      1 
HETATM 3200 O  O      . HOH E 4 .   ? -23.67700 15.99400  -24.35100 1.000 20.96450 ? 740 HOH A O      1 
HETATM 3201 O  O      . HOH E 4 .   ? -9.06900  18.44000  -11.18600 1.000 31.73555 ? 741 HOH A O      1 
HETATM 3202 O  O      . HOH E 4 .   ? -14.17100 -2.61800  -16.12500 1.000 42.90284 ? 742 HOH A O      1 
HETATM 3203 O  O      . HOH E 4 .   ? 13.95600  -2.74500  10.02600  1.000 37.42996 ? 743 HOH A O      1 
HETATM 3204 O  O      . HOH E 4 .   ? 9.18900   6.46000   -36.29800 1.000 36.40201 ? 744 HOH A O      1 
HETATM 3205 O  O      . HOH E 4 .   ? 21.73300  -3.29000  -24.19400 1.000 35.53930 ? 745 HOH A O      1 
HETATM 3206 O  O      . HOH E 4 .   ? -34.94400 9.95600   -0.95700  1.000 43.69606 ? 746 HOH A O      1 
HETATM 3207 O  O      . HOH E 4 .   ? -28.32800 19.91900  -13.45200 1.000 29.52922 ? 747 HOH A O      1 
HETATM 3208 O  O      . HOH E 4 .   ? 3.094     -16.077   -18.287   1.000 24.35978 ? 748 HOH A O      1 
HETATM 3209 O  O      . HOH E 4 .   ? -8.01400  8.46400   -35.38000 1.000 24.93907 ? 749 HOH A O      1 
HETATM 3210 O  O      . HOH E 4 .   ? -8.11600  -3.52200  -6.99600  1.000 36.98352 ? 750 HOH A O      1 
HETATM 3211 O  O      . HOH E 4 .   ? -23.01800 4.54700   -8.65400  1.000 31.02758 ? 751 HOH A O      1 
HETATM 3212 O  O      . HOH E 4 .   ? -20.45600 7.34100   -30.57000 1.000 24.14365 ? 752 HOH A O      1 
HETATM 3213 O  O      . HOH E 4 .   ? 15.671    3.911     7.222     1.000 36.10539 ? 753 HOH A O      1 
HETATM 3214 O  O      . HOH E 4 .   ? -0.79100  17.32400  -2.65200  1.000 47.75207 ? 754 HOH A O      1 
HETATM 3215 O  O      . HOH E 4 .   ? -16.69800 -1.60500  -35.68600 1.000 38.07418 ? 755 HOH A O      1 
HETATM 3216 O  O      . HOH E 4 .   ? -11.44100 -10.55100 -23.22500 1.000 38.83426 ? 756 HOH A O      1 
HETATM 3217 O  O      . HOH E 4 .   ? 8.69100   -6.56300  -29.80700 1.000 28.77077 ? 757 HOH A O      1 
HETATM 3218 O  O      . HOH E 4 .   ? 8.84300   5.85800   -38.20600 1.000 40.65850 ? 758 HOH A O      1 
HETATM 3219 O  O      . HOH E 4 .   ? -8.30900  15.87800  -11.74600 1.000 19.83505 ? 759 HOH A O      1 
HETATM 3220 O  O      . HOH E 4 .   ? 9.72400   -7.49600  -27.90500 1.000 36.74224 ? 760 HOH A O      1 
HETATM 3221 O  O      . HOH E 4 .   ? -6.98600  21.34900  -33.67200 1.000 27.43131 ? 761 HOH A O      1 
HETATM 3222 O  O      . HOH E 4 .   ? 23.274    -6.982    -21.205   1.000 44.35189 ? 762 HOH A O      1 
HETATM 3223 O  O      . HOH E 4 .   ? -39.20200 4.56300   -14.29500 1.000 33.53622 ? 763 HOH A O      1 
HETATM 3224 O  O      . HOH E 4 .   ? -35.46000 8.09900   -29.33800 1.000 34.28927 ? 764 HOH A O      1 
HETATM 3225 O  O      . HOH E 4 .   ? 3.13400   -13.68300 -17.07800 1.000 31.85928 ? 765 HOH A O      1 
HETATM 3226 O  O      . HOH E 4 .   ? 9.59300   -8.93900  -21.27600 1.000 37.54014 ? 766 HOH A O      1 
HETATM 3227 O  O      . HOH E 4 .   ? -36.59200 13.08300  -5.44900  1.000 40.03281 ? 767 HOH A O      1 
HETATM 3228 O  O      . HOH E 4 .   ? -22.27900 6.52200   -34.48700 1.000 33.14041 ? 768 HOH A O      1 
HETATM 3229 O  O      . HOH E 4 .   ? -16.78400 15.11600  -31.28700 1.000 35.81474 ? 769 HOH A O      1 
HETATM 3230 O  O      . HOH E 4 .   ? 11.041    3.897     11.222    1.000 33.48560 ? 770 HOH A O      1 
HETATM 3231 O  O      . HOH E 4 .   ? -36.88900 4.38000   -34.97900 1.000 38.28010 ? 771 HOH A O      1 
HETATM 3232 O  O      . HOH E 4 .   ? 20.37500  1.69300   3.14100   1.000 34.75749 ? 772 HOH A O      1 
HETATM 3233 O  O      . HOH E 4 .   ? -14.47700 19.89400  -28.54800 1.000 26.37264 ? 773 HOH A O      1 
HETATM 3234 O  O      . HOH E 4 .   ? -28.986   15.609    -47.092   1.000 30.26050 ? 774 HOH A O      1 
HETATM 3235 O  O      . HOH E 4 .   ? 4.82800   8.21900   10.09300  1.000 34.89703 ? 775 HOH A O      1 
HETATM 3236 O  O      . HOH E 4 .   ? 19.72000  -4.63600  1.56900   1.000 36.80176 ? 776 HOH A O      1 
HETATM 3237 O  O      . HOH E 4 .   ? -9.54600  -6.55700  -17.53300 1.000 34.73798 ? 777 HOH A O      1 
HETATM 3238 O  O      . HOH E 4 .   ? 2.50800   21.11400  -39.02200 1.000 35.62280 ? 778 HOH A O      1 
HETATM 3239 O  O      . HOH E 4 .   ? -21.37100 7.34200   -37.18400 1.000 45.81220 ? 779 HOH A O      1 
HETATM 3240 O  O      . HOH E 4 .   ? -13.60300 5.10800   -34.28400 1.000 33.10169 ? 780 HOH A O      1 
HETATM 3241 O  O      . HOH E 4 .   ? -23.216   21.705    -9.835    1.000 32.36502 ? 781 HOH A O      1 
HETATM 3242 O  O      . HOH E 4 .   ? 0.56000   -14.73700 -21.71300 1.000 29.33903 ? 782 HOH A O      1 
HETATM 3243 O  O      . HOH E 4 .   ? 9.219     6.084     12.650    1.000 31.53035 ? 783 HOH A O      1 
HETATM 3244 O  O      . HOH E 4 .   ? 10.477    -2.746    -35.220   1.000 31.15353 ? 784 HOH A O      1 
HETATM 3245 O  O      . HOH E 4 .   ? 8.21400   -8.09000  -0.43300  1.000 39.03969 ? 785 HOH A O      1 
HETATM 3246 O  O      . HOH E 4 .   ? -14.85500 15.15300  -32.66000 1.000 30.67318 ? 786 HOH A O      1 
HETATM 3247 O  O      . HOH E 4 .   ? 4.62000   19.88700  -18.98400 1.000 23.32210 ? 787 HOH A O      1 
HETATM 3248 O  O      . HOH E 4 .   ? -27.847   5.161     2.362     1.000 39.19641 ? 788 HOH A O      1 
HETATM 3249 O  O      . HOH E 4 .   ? -3.99600  16.64600  -12.05300 1.000 28.81177 ? 789 HOH A O      1 
HETATM 3250 O  O      . HOH E 4 .   ? -12.73300 9.49600   -36.57000 1.000 37.69085 ? 790 HOH A O      1 
HETATM 3251 O  O      . HOH E 4 .   ? 0.78300   18.90500  -21.02500 1.000 15.15587 ? 791 HOH A O      1 
HETATM 3252 O  O      . HOH E 4 .   ? 19.40400  -4.03100  -27.53300 1.000 32.65235 ? 792 HOH A O      1 
HETATM 3253 O  O      . HOH E 4 .   ? -37.19500 9.38400   -22.89800 1.000 34.03838 ? 793 HOH A O      1 
HETATM 3254 O  O      . HOH E 4 .   ? -31.90800 2.55200   -4.46800  1.000 44.01754 ? 794 HOH A O      1 
HETATM 3255 O  O      . HOH E 4 .   ? -30.72000 -0.30600  -0.13500  1.000 39.65516 ? 795 HOH A O      1 
HETATM 3256 O  O      . HOH E 4 .   ? -17.78800 12.26400  -30.11100 1.000 29.94596 ? 796 HOH A O      1 
HETATM 3257 O  O      . HOH E 4 .   ? -25.38200 7.29400   -34.91100 1.000 30.75226 ? 797 HOH A O      1 
HETATM 3258 O  O      . HOH E 4 .   ? -10.74100 8.53500   -36.07400 1.000 34.10399 ? 798 HOH A O      1 
HETATM 3259 O  O      . HOH E 4 .   ? -24.70100 19.36600  -26.40600 1.000 34.01930 ? 799 HOH A O      1 
HETATM 3260 O  O      . HOH E 4 .   ? 3.16100   10.49800  5.55600   1.000 26.44110 ? 800 HOH A O      1 
HETATM 3261 O  O      . HOH E 4 .   ? 13.78100  10.47800  -29.69100 1.000 33.94267 ? 801 HOH A O      1 
HETATM 3262 O  O      . HOH E 4 .   ? 1.61200   24.50000  -41.12500 1.000 39.80322 ? 802 HOH A O      1 
HETATM 3263 O  O      . HOH E 4 .   ? 9.151     -12.839   -6.154    1.000 32.76824 ? 803 HOH A O      1 
HETATM 3264 O  O      . HOH E 4 .   ? 12.71300  10.10900  -18.60100 1.000 34.75616 ? 804 HOH A O      1 
HETATM 3265 O  O      . HOH E 4 .   ? 11.543    -13.956   -6.785    1.000 28.57561 ? 805 HOH A O      1 
HETATM 3266 O  O      . HOH E 4 .   ? -17.12400 -4.81400  -22.69700 1.000 26.13540 ? 806 HOH A O      1 
HETATM 3267 O  O      . HOH E 4 .   ? -23.338   21.893    -42.043   1.000 24.95572 ? 807 HOH A O      1 
HETATM 3268 O  O      . HOH E 4 .   ? 0.66000   18.80900  -18.21200 1.000 20.91023 ? 808 HOH A O      1 
HETATM 3269 O  O      . HOH E 4 .   ? -6.60400  -11.80700 -22.67400 1.000 46.86609 ? 809 HOH A O      1 
HETATM 3270 O  O      . HOH E 4 .   ? -36.858   -13.628   -22.390   1.000 34.30281 ? 810 HOH A O      1 
HETATM 3271 O  O      . HOH E 4 .   ? -4.99100  -10.92600 -20.48800 1.000 29.79753 ? 811 HOH A O      1 
HETATM 3272 O  O      . HOH E 4 .   ? 7.25700   14.01900  -34.96000 1.000 20.61710 ? 812 HOH A O      1 
HETATM 3273 O  O      . HOH E 4 .   ? 10.36600  12.86200  -20.42200 1.000 29.66884 ? 813 HOH A O      1 
HETATM 3274 O  O      . HOH E 4 .   ? -39.12800 -13.07700 -13.41100 1.000 41.03816 ? 814 HOH A O      1 
HETATM 3275 O  O      . HOH E 4 .   ? -18.60200 10.92800  -2.68700  1.000 41.53598 ? 815 HOH A O      1 
HETATM 3276 O  O      . HOH E 4 .   ? -36.63000 11.81400  -19.95300 1.000 37.18404 ? 816 HOH A O      1 
HETATM 3277 O  O      . HOH E 4 .   ? 7.85400   -5.16700  -31.89700 1.000 34.05257 ? 817 HOH A O      1 
HETATM 3278 O  O      . HOH E 4 .   ? -20.21700 13.13100  -29.49600 1.000 37.76130 ? 818 HOH A O      1 
HETATM 3279 O  O      . HOH E 4 .   ? -23.55700 19.79800  -21.61100 1.000 30.86092 ? 819 HOH A O      1 
HETATM 3280 O  O      . HOH E 4 .   ? 6.340     -11.318   -15.236   1.000 21.55788 ? 820 HOH A O      1 
HETATM 3281 O  O      . HOH E 4 .   ? 11.03200  12.50000  -25.35800 1.000 22.12966 ? 821 HOH A O      1 
HETATM 3282 O  O      . HOH E 4 .   ? -3.96500  -12.99900 -19.51600 1.000 30.38536 ? 822 HOH A O      1 
HETATM 3283 O  O      . HOH E 4 .   ? 6.61000   -3.75100  -2.14500  1.000 34.97642 ? 823 HOH A O      1 
HETATM 3284 O  O      . HOH E 4 .   ? -9.248    25.708    -21.452   1.000 36.66342 ? 824 HOH A O      1 
HETATM 3285 O  O      . HOH E 4 .   ? -13.25000 -7.92200  -20.58200 1.000 36.16899 ? 825 HOH A O      1 
HETATM 3286 O  O      . HOH E 4 .   ? -37.26200 6.09400   -33.51700 1.000 41.58498 ? 826 HOH A O      1 
HETATM 3287 O  O      . HOH E 4 .   ? -27.893   7.769     2.579     1.000 49.18784 ? 827 HOH A O      1 
HETATM 3288 O  O      . HOH E 4 .   ? 7.34000   -8.33700  -20.61700 1.000 20.30101 ? 828 HOH A O      1 
HETATM 3289 O  O      . HOH E 4 .   ? -37.20400 6.80300   -30.82300 1.000 31.22711 ? 829 HOH A O      1 
HETATM 3290 O  O      . HOH E 4 .   ? -33.23700 8.11500   -1.21400  1.000 38.59050 ? 830 HOH A O      1 
HETATM 3291 O  O      . HOH E 4 .   ? -46.37300 3.57500   -23.88600 1.000 41.70190 ? 831 HOH A O      1 
HETATM 3292 O  O      . HOH E 4 .   ? -4.32500  22.25200  -23.45000 1.000 29.42541 ? 832 HOH A O      1 
HETATM 3293 O  O      . HOH E 4 .   ? -19.759   24.934    -17.940   1.000 32.53868 ? 833 HOH A O      1 
HETATM 3294 O  O      . HOH E 4 .   ? 10.89200  13.60900  -23.13600 1.000 26.90897 ? 834 HOH A O      1 
HETATM 3295 O  O      . HOH E 4 .   ? -20.76500 7.68900   -33.01400 1.000 25.05706 ? 835 HOH A O      1 
HETATM 3296 O  O      . HOH E 4 .   ? -11.19400 19.00800  -34.40800 1.000 33.73350 ? 836 HOH A O      1 
HETATM 3297 O  O      . HOH E 4 .   ? -41.84200 6.37800   -31.98200 1.000 43.88087 ? 837 HOH A O      1 
HETATM 3298 O  O      . HOH E 4 .   ? 11.34000  13.49700  -27.52100 1.000 36.37286 ? 838 HOH A O      1 
HETATM 3299 O  O      . HOH E 4 .   ? 13.21600  9.11200   -11.58700 1.000 27.91279 ? 839 HOH A O      1 
HETATM 3300 O  O      . HOH E 4 .   ? -33.169   14.192    -54.839   1.000 20.39013 ? 840 HOH A O      1 
HETATM 3301 O  O      . HOH E 4 .   ? -11.38400 17.56400  -38.86500 1.000 47.52522 ? 841 HOH A O      1 
HETATM 3302 O  O      . HOH E 4 .   ? -2.53900  20.48500  -23.64400 1.000 30.77539 ? 842 HOH A O      1 
HETATM 3303 O  O      . HOH E 4 .   ? -38.288   1.663     -39.275   1.000 37.78921 ? 843 HOH A O      1 
HETATM 3304 O  O      . HOH E 4 .   ? -16.62700 27.76700  -21.43100 1.000 33.87582 ? 844 HOH A O      1 
HETATM 3305 O  O      . HOH E 4 .   ? 13.83800  10.06400  -14.05600 1.000 32.38277 ? 845 HOH A O      1 
# 
