data_5O6H
# 
_entry.id   5O6H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.295 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5O6H         
WWPDB D_1200005268 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Same protein in complex with inhibitor IMP-1088' 5MU6 unspecified 
PDB .                                                 5O6J unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5O6H 
_pdbx_database_status.recvd_initial_deposition_date   2017-06-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Brannigan, J.A.' 1 0000-0001-6597-8972 
'Wilkinson, A.J.' 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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1755-4349 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                599 
_citation.page_last                 606 
_citation.title                     
'Fragment-derived inhibitors of human N-myristoyltransferase block capsid assembly and replication of the common cold virus.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41557-018-0039-2 
_citation.pdbx_database_id_PubMed   29760414 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Mousnier, A.'            1  
primary 'Bell, A.S.'              2  
primary 'Swieboda, D.P.'          3  
primary 'Morales-Sanfrutos, J.'   4  
primary 'Perez-Dorado, I.'        5  
primary 'Brannigan, J.A.'         6  
primary 'Newman, J.'              7  
primary 'Ritzefeld, M.'           8  
primary 'Hutton, J.A.'            9  
primary 'Guedan, A.'              10 
primary 'Asfor, A.S.'             11 
primary 'Robinson, S.W.'          12 
primary 'Hopkins-Navratilova, I.' 13 
primary 'Wilkinson, A.J.'         14 
primary 'Johnston, S.L.'          15 
primary 'Leatherbarrow, R.J.'     16 
primary 'Tuthill, T.J.'           17 
primary 'Solari, R.'              18 
primary 'Tate, E.W.'              19 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5O6H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     79.138 
_cell.length_a_esd                 ? 
_cell.length_b                     178.852 
_cell.length_b_esd                 ? 
_cell.length_c                     58.465 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5O6H 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'Glycylpeptide N-tetradecanoyltransferase 1' 45453.348 2    2.3.1.97 ? ? ? 
2 non-polymer syn TETRADECANOYL-COA 977.890   2    ?        ? ? ? 
3 non-polymer syn 'PHOSPHATE ION' 94.971    8    ?        ? ? ? 
4 non-polymer syn 
'1-[5-[4-fluoranyl-2-[2-(1,3,5-trimethylpyrazol-4-yl)ethoxy]phenyl]-2~{H}-indazol-3-yl]-~{N},~{N}-dimethyl-methanamine' 421.510   
2    ?        ? ? ? 
5 non-polymer syn 'MAGNESIUM ION' 24.305    2    ?        ? ? ? 
6 non-polymer syn GLYCEROL 92.094    3    ?        ? ? ? 
7 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    1    ?        ? ? ? 
8 water       nat water 18.015    1018 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Myristoyl-CoA:protein N-myristoyltransferase 1,Type I N-myristoyltransferase,Peptide N-myristoyltransferase 1' 
# 
_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       
;GPHMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDD
NMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIR
EITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKD
IPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNV
HTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPHMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDD
NMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIR
EITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKD
IPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNV
HTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   HIS n 
1 4   MET n 
1 5   GLU n 
1 6   GLU n 
1 7   ALA n 
1 8   SER n 
1 9   LYS n 
1 10  ARG n 
1 11  SER n 
1 12  TYR n 
1 13  GLN n 
1 14  PHE n 
1 15  TRP n 
1 16  ASP n 
1 17  THR n 
1 18  GLN n 
1 19  PRO n 
1 20  VAL n 
1 21  PRO n 
1 22  LYS n 
1 23  LEU n 
1 24  GLY n 
1 25  GLU n 
1 26  VAL n 
1 27  VAL n 
1 28  ASN n 
1 29  THR n 
1 30  HIS n 
1 31  GLY n 
1 32  PRO n 
1 33  VAL n 
1 34  GLU n 
1 35  PRO n 
1 36  ASP n 
1 37  LYS n 
1 38  ASP n 
1 39  ASN n 
1 40  ILE n 
1 41  ARG n 
1 42  GLN n 
1 43  GLU n 
1 44  PRO n 
1 45  TYR n 
1 46  THR n 
1 47  LEU n 
1 48  PRO n 
1 49  GLN n 
1 50  GLY n 
1 51  PHE n 
1 52  THR n 
1 53  TRP n 
1 54  ASP n 
1 55  ALA n 
1 56  LEU n 
1 57  ASP n 
1 58  LEU n 
1 59  GLY n 
1 60  ASP n 
1 61  ARG n 
1 62  GLY n 
1 63  VAL n 
1 64  LEU n 
1 65  LYS n 
1 66  GLU n 
1 67  LEU n 
1 68  TYR n 
1 69  THR n 
1 70  LEU n 
1 71  LEU n 
1 72  ASN n 
1 73  GLU n 
1 74  ASN n 
1 75  TYR n 
1 76  VAL n 
1 77  GLU n 
1 78  ASP n 
1 79  ASP n 
1 80  ASP n 
1 81  ASN n 
1 82  MET n 
1 83  PHE n 
1 84  ARG n 
1 85  PHE n 
1 86  ASP n 
1 87  TYR n 
1 88  SER n 
1 89  PRO n 
1 90  GLU n 
1 91  PHE n 
1 92  LEU n 
1 93  LEU n 
1 94  TRP n 
1 95  ALA n 
1 96  LEU n 
1 97  ARG n 
1 98  PRO n 
1 99  PRO n 
1 100 GLY n 
1 101 TRP n 
1 102 LEU n 
1 103 PRO n 
1 104 GLN n 
1 105 TRP n 
1 106 HIS n 
1 107 CYS n 
1 108 GLY n 
1 109 VAL n 
1 110 ARG n 
1 111 VAL n 
1 112 VAL n 
1 113 SER n 
1 114 SER n 
1 115 ARG n 
1 116 LYS n 
1 117 LEU n 
1 118 VAL n 
1 119 GLY n 
1 120 PHE n 
1 121 ILE n 
1 122 SER n 
1 123 ALA n 
1 124 ILE n 
1 125 PRO n 
1 126 ALA n 
1 127 ASN n 
1 128 ILE n 
1 129 HIS n 
1 130 ILE n 
1 131 TYR n 
1 132 ASP n 
1 133 THR n 
1 134 GLU n 
1 135 LYS n 
1 136 LYS n 
1 137 MET n 
1 138 VAL n 
1 139 GLU n 
1 140 ILE n 
1 141 ASN n 
1 142 PHE n 
1 143 LEU n 
1 144 CYS n 
1 145 VAL n 
1 146 HIS n 
1 147 LYS n 
1 148 LYS n 
1 149 LEU n 
1 150 ARG n 
1 151 SER n 
1 152 LYS n 
1 153 ARG n 
1 154 VAL n 
1 155 ALA n 
1 156 PRO n 
1 157 VAL n 
1 158 LEU n 
1 159 ILE n 
1 160 ARG n 
1 161 GLU n 
1 162 ILE n 
1 163 THR n 
1 164 ARG n 
1 165 ARG n 
1 166 VAL n 
1 167 HIS n 
1 168 LEU n 
1 169 GLU n 
1 170 GLY n 
1 171 ILE n 
1 172 PHE n 
1 173 GLN n 
1 174 ALA n 
1 175 VAL n 
1 176 TYR n 
1 177 THR n 
1 178 ALA n 
1 179 GLY n 
1 180 VAL n 
1 181 VAL n 
1 182 LEU n 
1 183 PRO n 
1 184 LYS n 
1 185 PRO n 
1 186 VAL n 
1 187 GLY n 
1 188 THR n 
1 189 CYS n 
1 190 ARG n 
1 191 TYR n 
1 192 TRP n 
1 193 HIS n 
1 194 ARG n 
1 195 SER n 
1 196 LEU n 
1 197 ASN n 
1 198 PRO n 
1 199 ARG n 
1 200 LYS n 
1 201 LEU n 
1 202 ILE n 
1 203 GLU n 
1 204 VAL n 
1 205 LYS n 
1 206 PHE n 
1 207 SER n 
1 208 HIS n 
1 209 LEU n 
1 210 SER n 
1 211 ARG n 
1 212 ASN n 
1 213 MET n 
1 214 THR n 
1 215 MET n 
1 216 GLN n 
1 217 ARG n 
1 218 THR n 
1 219 MET n 
1 220 LYS n 
1 221 LEU n 
1 222 TYR n 
1 223 ARG n 
1 224 LEU n 
1 225 PRO n 
1 226 GLU n 
1 227 THR n 
1 228 PRO n 
1 229 LYS n 
1 230 THR n 
1 231 ALA n 
1 232 GLY n 
1 233 LEU n 
1 234 ARG n 
1 235 PRO n 
1 236 MET n 
1 237 GLU n 
1 238 THR n 
1 239 LYS n 
1 240 ASP n 
1 241 ILE n 
1 242 PRO n 
1 243 VAL n 
1 244 VAL n 
1 245 HIS n 
1 246 GLN n 
1 247 LEU n 
1 248 LEU n 
1 249 THR n 
1 250 ARG n 
1 251 TYR n 
1 252 LEU n 
1 253 LYS n 
1 254 GLN n 
1 255 PHE n 
1 256 HIS n 
1 257 LEU n 
1 258 THR n 
1 259 PRO n 
1 260 VAL n 
1 261 MET n 
1 262 SER n 
1 263 GLN n 
1 264 GLU n 
1 265 GLU n 
1 266 VAL n 
1 267 GLU n 
1 268 HIS n 
1 269 TRP n 
1 270 PHE n 
1 271 TYR n 
1 272 PRO n 
1 273 GLN n 
1 274 GLU n 
1 275 ASN n 
1 276 ILE n 
1 277 ILE n 
1 278 ASP n 
1 279 THR n 
1 280 PHE n 
1 281 VAL n 
1 282 VAL n 
1 283 GLU n 
1 284 ASN n 
1 285 ALA n 
1 286 ASN n 
1 287 GLY n 
1 288 GLU n 
1 289 VAL n 
1 290 THR n 
1 291 ASP n 
1 292 PHE n 
1 293 LEU n 
1 294 SER n 
1 295 PHE n 
1 296 TYR n 
1 297 THR n 
1 298 LEU n 
1 299 PRO n 
1 300 SER n 
1 301 THR n 
1 302 ILE n 
1 303 MET n 
1 304 ASN n 
1 305 HIS n 
1 306 PRO n 
1 307 THR n 
1 308 HIS n 
1 309 LYS n 
1 310 SER n 
1 311 LEU n 
1 312 LYS n 
1 313 ALA n 
1 314 ALA n 
1 315 TYR n 
1 316 SER n 
1 317 PHE n 
1 318 TYR n 
1 319 ASN n 
1 320 VAL n 
1 321 HIS n 
1 322 THR n 
1 323 GLN n 
1 324 THR n 
1 325 PRO n 
1 326 LEU n 
1 327 LEU n 
1 328 ASP n 
1 329 LEU n 
1 330 MET n 
1 331 SER n 
1 332 ASP n 
1 333 ALA n 
1 334 LEU n 
1 335 VAL n 
1 336 LEU n 
1 337 ALA n 
1 338 LYS n 
1 339 MET n 
1 340 LYS n 
1 341 GLY n 
1 342 PHE n 
1 343 ASP n 
1 344 VAL n 
1 345 PHE n 
1 346 ASN n 
1 347 ALA n 
1 348 LEU n 
1 349 ASP n 
1 350 LEU n 
1 351 MET n 
1 352 GLU n 
1 353 ASN n 
1 354 LYS n 
1 355 THR n 
1 356 PHE n 
1 357 LEU n 
1 358 GLU n 
1 359 LYS n 
1 360 LEU n 
1 361 LYS n 
1 362 PHE n 
1 363 GLY n 
1 364 ILE n 
1 365 GLY n 
1 366 ASP n 
1 367 GLY n 
1 368 ASN n 
1 369 LEU n 
1 370 GLN n 
1 371 TYR n 
1 372 TYR n 
1 373 LEU n 
1 374 TYR n 
1 375 ASN n 
1 376 TRP n 
1 377 LYS n 
1 378 CYS n 
1 379 PRO n 
1 380 SER n 
1 381 MET n 
1 382 GLY n 
1 383 ALA n 
1 384 GLU n 
1 385 LYS n 
1 386 VAL n 
1 387 GLY n 
1 388 LEU n 
1 389 VAL n 
1 390 LEU n 
1 391 GLN 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                   391 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'NMT1, NMT' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              pRareS 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NMT1_HUMAN 
_struct_ref.pdbx_db_accession          P30419 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMF
RFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREIT
RRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPV
VHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQ
TPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ
;
_struct_ref.pdbx_align_begin           109 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5O6H A 4 ? 391 ? P30419 109 ? 496 ? 109 496 
2 1 5O6H B 4 ? 391 ? P30419 109 ? 496 ? 109 496 
# 
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 5O6H GLY A 1 ? UNP P30419 ? ? 'expression tag' 106 1 
1 5O6H PRO A 2 ? UNP P30419 ? ? 'expression tag' 107 2 
1 5O6H HIS A 3 ? UNP P30419 ? ? 'expression tag' 108 3 
2 5O6H GLY B 1 ? UNP P30419 ? ? 'expression tag' 106 4 
2 5O6H PRO B 2 ? UNP P30419 ? ? 'expression tag' 107 5 
2 5O6H HIS B 3 ? UNP P30419 ? ? 'expression tag' 108 6 
# 
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 
9M2 non-polymer         . 
'1-[5-[4-fluoranyl-2-[2-(1,3,5-trimethylpyrazol-4-yl)ethoxy]phenyl]-2~{H}-indazol-3-yl]-~{N},~{N}-dimethyl-methanamine' ? 
'C24 H28 F N5 O'      421.510 
ALA 'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'          133.103 
CYS 'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE' ?                               'C2 H6 O S'           78.133  
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  
GOL non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'            92.094  
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 
MG  non-polymer         . 'MAGNESIUM ION' ?                               'Mg 2'                24.305  
MYA non-polymer         . TETRADECANOYL-COA MYRISTOYL-COA                   'C35 H62 N7 O17 P3 S' 977.890 
PHE 'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'         165.189 
PO4 non-polymer         . 'PHOSPHATE ION' ?                               'O4 P -3'             94.971  
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 
# 
_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                   5O6H 
_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            2.28 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         45.95 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.4M Sodium phosphate buffer, 17.5% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_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_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-13 
# 
_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   0.9200 
_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                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9200 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            9.7 
_reflns.entry_id                         5O6H 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.29 
_reflns.d_resolution_low                 89 
_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                       206823 
_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             99.1 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.2 
_reflns.pdbx_Rmerge_I_obs                0.062 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            14.7 
_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                  0.039 
_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_R_split                     ? 
# 
_reflns_shell.d_res_high                  1.29 
_reflns_shell.d_res_low                   1.31 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.6 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           9516 
_reflns_shell.percent_possible_all        93.1 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.651 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             3.4 
_reflns_shell.pdbx_Rsym_value             ? 
_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             0.595 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.697 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            1.70 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.57 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.13 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               17.134 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.973 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 5O6H 
_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                            1.29 
_refine.ls_d_res_low                             55 
_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                     195765 
_refine.ls_number_reflns_R_free                  10300 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.68 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16533 
_refine.ls_R_factor_R_free                       0.19348 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16384 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      4c2y 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.047 
_refine.pdbx_overall_ESU_R_Free                  0.051 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             0.965 
_refine.overall_SU_ML                            0.040 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        6272 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         252 
_refine_hist.number_atoms_solvent             1018 
_refine_hist.number_atoms_total               7542 
_refine_hist.d_res_high                       1.29 
_refine_hist.d_res_low                        55 
# 
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' ? 0.028  0.019  7038  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.498  1.998  9647  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.437  5.000  859   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 37.518 23.934 333   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.050 15.000 1219  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.794 15.000 43    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.175  0.200  1032  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.021  5353  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.685  1.364  3164  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.483  2.051  3977  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.823  1.643  3874  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.269  20.019 11007 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.290 
_refine_ls_shell.d_res_low                        1.323 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             714 
_refine_ls_shell.number_reflns_R_work             13037 
_refine_ls_shell.percent_reflns_obs               89.74 
_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                  0.277 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.264 
_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_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5O6H 
_struct.title                        'Human NMT1 in complex with myristoyl-CoA and inhibitor IMP-917' 
_struct.pdbx_descriptor              'Glycylpeptide N-tetradecanoyltransferase 1 (E.C.2.3.1.97)' 
_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        5O6H 
_struct_keywords.text            'Myristoyl, transferase, inhibitor' 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 7 ? 
K N N 2 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 4 ? 
R N N 5 ? 
S N N 6 ? 
T N N 6 ? 
U N N 8 ? 
V N N 8 ? 
# 
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 PHE A 14  ? GLN A 18  ? PHE A 119 GLN A 123 5 ? 5  
HELX_P HELX_P2  AA2 ASP A 60  ? TYR A 75  ? ASP A 165 TYR A 180 1 ? 16 
HELX_P HELX_P3  AA3 SER A 88  ? ARG A 97  ? SER A 193 ARG A 202 1 ? 10 
HELX_P HELX_P4  AA4 LEU A 102 ? GLN A 104 ? LEU A 207 GLN A 209 5 ? 3  
HELX_P HELX_P5  AA5 LYS A 147 ? ARG A 150 ? LYS A 252 ARG A 255 5 ? 4  
HELX_P HELX_P6  AA6 VAL A 154 ? LEU A 168 ? VAL A 259 LEU A 273 1 ? 15 
HELX_P HELX_P7  AA7 ASN A 197 ? VAL A 204 ? ASN A 302 VAL A 309 1 ? 8  
HELX_P HELX_P8  AA8 THR A 214 ? ARG A 223 ? THR A 319 ARG A 328 1 ? 10 
HELX_P HELX_P9  AA9 GLU A 237 ? LYS A 239 ? GLU A 342 LYS A 344 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 240 ? LYS A 253 ? ASP A 345 LYS A 358 1 ? 14 
HELX_P HELX_P11 AB2 SER A 262 ? TYR A 271 ? SER A 367 TYR A 376 1 ? 10 
HELX_P HELX_P12 AB3 PRO A 325 ? LYS A 340 ? PRO A 430 LYS A 445 1 ? 16 
HELX_P HELX_P13 AB4 GLU A 352 ? PHE A 356 ? GLU A 457 PHE A 461 5 ? 5  
HELX_P HELX_P14 AB5 GLY A 382 ? VAL A 386 ? GLY A 487 VAL A 491 5 ? 5  
HELX_P HELX_P15 AB6 PHE B 14  ? GLN B 18  ? PHE B 119 GLN B 123 5 ? 5  
HELX_P HELX_P16 AB7 ASP B 60  ? TYR B 75  ? ASP B 165 TYR B 180 1 ? 16 
HELX_P HELX_P17 AB8 SER B 88  ? ARG B 97  ? SER B 193 ARG B 202 1 ? 10 
HELX_P HELX_P18 AB9 LEU B 102 ? GLN B 104 ? LEU B 207 GLN B 209 5 ? 3  
HELX_P HELX_P19 AC1 LYS B 147 ? ARG B 150 ? LYS B 252 ARG B 255 5 ? 4  
HELX_P HELX_P20 AC2 ARG B 153 ? LEU B 168 ? ARG B 258 LEU B 273 1 ? 16 
HELX_P HELX_P21 AC3 ASN B 197 ? VAL B 204 ? ASN B 302 VAL B 309 1 ? 8  
HELX_P HELX_P22 AC4 THR B 214 ? ARG B 223 ? THR B 319 ARG B 328 1 ? 10 
HELX_P HELX_P23 AC5 GLU B 237 ? LYS B 239 ? GLU B 342 LYS B 344 5 ? 3  
HELX_P HELX_P24 AC6 ASP B 240 ? LYS B 253 ? ASP B 345 LYS B 358 1 ? 14 
HELX_P HELX_P25 AC7 SER B 262 ? TYR B 271 ? SER B 367 TYR B 376 1 ? 10 
HELX_P HELX_P26 AC8 PRO B 325 ? LYS B 340 ? PRO B 430 LYS B 445 1 ? 16 
HELX_P HELX_P27 AC9 GLU B 352 ? PHE B 356 ? GLU B 457 PHE B 461 5 ? 5  
HELX_P HELX_P28 AD1 GLY B 382 ? VAL B 386 ? GLY B 487 VAL B 491 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1 metalc ? ? A LEU 149 O   ? ? ? 1_555 H MG . MG ? ? A LEU 254  A MG 2006 1_555 ? ? ? ? ? ? ? 2.756 ? 
metalc2 metalc ? ? B LEU 149 O   ? ? ? 1_555 R MG . MG ? ? B LEU 254  B MG 2008 1_555 ? ? ? ? ? ? ? 2.834 ? 
metalc3 metalc ? ? C MYA .   O1A ? ? ? 1_555 H MG . MG ? ? A MYA 2001 A MG 2006 1_555 ? ? ? ? ? ? ? 2.884 ? 
metalc4 metalc ? ? K MYA .   O1A ? ? ? 1_555 R MG . MG ? ? B MYA 2001 B MG 2008 1_555 ? ? ? ? ? ? ? 2.869 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 183 A . ? PRO 288 A LYS 184 A ? LYS 289 A 1 -13.88 
2 PRO 183 B . ? PRO 288 B LYS 184 B ? LYS 289 B 1 -18.86 
3 PRO 183 B . ? PRO 288 B LYS 184 B ? LYS 289 B 1 -19.70 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 12 ? 
AA2 ? 4  ? 
AA3 ? 3  ? 
AA4 ? 11 ? 
AA5 ? 11 ? 
AA6 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? parallel      
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? parallel      
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA4 1  2  ? anti-parallel 
AA4 2  3  ? anti-parallel 
AA4 3  4  ? anti-parallel 
AA4 4  5  ? parallel      
AA4 5  6  ? anti-parallel 
AA4 6  7  ? anti-parallel 
AA4 7  8  ? anti-parallel 
AA4 8  9  ? parallel      
AA4 9  10 ? anti-parallel 
AA5 1  2  ? anti-parallel 
AA5 2  3  ? anti-parallel 
AA5 3  4  ? anti-parallel 
AA5 4  5  ? parallel      
AA5 5  6  ? anti-parallel 
AA5 6  7  ? anti-parallel 
AA5 7  8  ? anti-parallel 
AA5 8  9  ? parallel      
AA5 9  10 ? anti-parallel 
AA6 1  2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  PHE A 51  ? ALA A 55  ? PHE A 156 ALA A 160 
AA1 2  HIS A 106 ? VAL A 111 ? HIS A 211 VAL A 216 
AA1 3  LEU A 117 ? ILE A 130 ? LEU A 222 ILE A 235 
AA1 4  THR A 133 ? VAL A 145 ? THR A 238 VAL A 250 
AA1 5  ALA A 174 ? ALA A 178 ? ALA A 279 ALA A 283 
AA1 6  GLY A 363 ? TYR A 374 ? GLY A 468 TYR A 479 
AA1 7  GLY A 187 ? SER A 195 ? GLY A 292 SER A 300 
AA1 8  VAL A 344 ? LEU A 348 ? VAL A 449 LEU A 453 
AA1 9  ALA A 313 ? SER A 316 ? ALA A 418 SER A 421 
AA1 10 VAL A 289 ? THR A 297 ? VAL A 394 THR A 402 
AA1 11 ILE A 277 ? GLU A 283 ? ILE A 382 GLU A 388 
AA1 12 LEU A 233 ? PRO A 235 ? LEU A 338 PRO A 340 
AA2 1  PHE A 51  ? ALA A 55  ? PHE A 156 ALA A 160 
AA2 2  HIS A 106 ? VAL A 111 ? HIS A 211 VAL A 216 
AA2 3  LEU A 117 ? ILE A 130 ? LEU A 222 ILE A 235 
AA2 4  LEU A 257 ? VAL A 260 ? LEU A 362 VAL A 365 
AA3 1  PHE A 83  ? PHE A 85  ? PHE A 188 PHE A 190 
AA3 2  SER A 300 ? ILE A 302 ? SER A 405 ILE A 407 
AA3 3  SER A 310 ? LEU A 311 ? SER A 415 LEU A 416 
AA4 1  PHE B 51  ? ALA B 55  ? PHE B 156 ALA B 160 
AA4 2  HIS B 106 ? VAL B 111 ? HIS B 211 VAL B 216 
AA4 3  LEU B 117 ? ILE B 130 ? LEU B 222 ILE B 235 
AA4 4  THR B 133 ? VAL B 145 ? THR B 238 VAL B 250 
AA4 5  ALA B 174 ? ALA B 178 ? ALA B 279 ALA B 283 
AA4 6  GLY B 363 ? TYR B 374 ? GLY B 468 TYR B 479 
AA4 7  GLY B 187 ? SER B 195 ? GLY B 292 SER B 300 
AA4 8  VAL B 344 ? LEU B 348 ? VAL B 449 LEU B 453 
AA4 9  ALA B 313 ? SER B 316 ? ALA B 418 SER B 421 
AA4 10 VAL B 289 ? THR B 297 ? VAL B 394 THR B 402 
AA4 11 LEU B 257 ? VAL B 260 ? LEU B 362 VAL B 365 
AA5 1  LEU B 233 ? PRO B 235 ? LEU B 338 PRO B 340 
AA5 2  ILE B 277 ? GLU B 283 ? ILE B 382 GLU B 388 
AA5 3  VAL B 289 ? THR B 297 ? VAL B 394 THR B 402 
AA5 4  ALA B 313 ? SER B 316 ? ALA B 418 SER B 421 
AA5 5  VAL B 344 ? LEU B 348 ? VAL B 449 LEU B 453 
AA5 6  GLY B 187 ? SER B 195 ? GLY B 292 SER B 300 
AA5 7  GLY B 363 ? TYR B 374 ? GLY B 468 TYR B 479 
AA5 8  ALA B 174 ? ALA B 178 ? ALA B 279 ALA B 283 
AA5 9  THR B 133 ? VAL B 145 ? THR B 238 VAL B 250 
AA5 10 LEU B 117 ? ILE B 130 ? LEU B 222 ILE B 235 
AA5 11 VAL B 320 ? HIS B 321 ? VAL B 425 HIS B 426 
AA6 1  PHE B 83  ? PHE B 85  ? PHE B 188 PHE B 190 
AA6 2  SER B 300 ? ILE B 302 ? SER B 405 ILE B 407 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N THR A 52  ? N THR A 157 O ARG A 110 ? O ARG A 215 
AA1 2  3  N VAL A 109 ? N VAL A 214 O VAL A 118 ? O VAL A 223 
AA1 3  4  N ALA A 126 ? N ALA A 231 O MET A 137 ? O MET A 242 
AA1 4  5  N VAL A 138 ? N VAL A 243 O VAL A 175 ? O VAL A 280 
AA1 5  6  N ALA A 178 ? N ALA A 283 O GLN A 370 ? O GLN A 475 
AA1 6  7  O LEU A 369 ? O LEU A 474 N CYS A 189 ? N CYS A 294 
AA1 7  8  N TRP A 192 ? N TRP A 297 O ALA A 347 ? O ALA A 452 
AA1 8  9  O ASN A 346 ? O ASN A 451 N ALA A 314 ? N ALA A 419 
AA1 9  10 O TYR A 315 ? O TYR A 420 N TYR A 296 ? N TYR A 401 
AA1 10 11 O LEU A 293 ? O LEU A 398 N PHE A 280 ? N PHE A 385 
AA1 11 12 O VAL A 281 ? O VAL A 386 N ARG A 234 ? N ARG A 339 
AA2 1  2  N THR A 52  ? N THR A 157 O ARG A 110 ? O ARG A 215 
AA2 2  3  N VAL A 109 ? N VAL A 214 O VAL A 118 ? O VAL A 223 
AA2 3  4  N HIS A 129 ? N HIS A 234 O THR A 258 ? O THR A 363 
AA3 1  2  N ARG A 84  ? N ARG A 189 O THR A 301 ? O THR A 406 
AA3 2  3  N SER A 300 ? N SER A 405 O LEU A 311 ? O LEU A 416 
AA4 1  2  N THR B 52  ? N THR B 157 O ARG B 110 ? O ARG B 215 
AA4 2  3  N VAL B 109 ? N VAL B 214 O VAL B 118 ? O VAL B 223 
AA4 3  4  N ALA B 126 ? N ALA B 231 O MET B 137 ? O MET B 242 
AA4 4  5  N VAL B 138 ? N VAL B 243 O VAL B 175 ? O VAL B 280 
AA4 5  6  N ALA B 178 ? N ALA B 283 O GLN B 370 ? O GLN B 475 
AA4 6  7  O TYR B 371 ? O TYR B 476 N GLY B 187 ? N GLY B 292 
AA4 7  8  N TRP B 192 ? N TRP B 297 O ALA B 347 ? O ALA B 452 
AA4 8  9  O ASN B 346 ? O ASN B 451 N ALA B 314 ? N ALA B 419 
AA4 9  10 O TYR B 315 ? O TYR B 420 N TYR B 296 ? N TYR B 401 
AA5 1  2  N ARG B 234 ? N ARG B 339 O VAL B 281 ? O VAL B 386 
AA5 2  3  N ASP B 278 ? N ASP B 383 O PHE B 295 ? O PHE B 400 
AA5 3  4  N TYR B 296 ? N TYR B 401 O TYR B 315 ? O TYR B 420 
AA5 4  5  N ALA B 314 ? N ALA B 419 O ASN B 346 ? O ASN B 451 
AA5 5  6  O ALA B 347 ? O ALA B 452 N TRP B 192 ? N TRP B 297 
AA5 6  7  N GLY B 187 ? N GLY B 292 O TYR B 371 ? O TYR B 476 
AA5 7  8  O GLN B 370 ? O GLN B 475 N ALA B 178 ? N ALA B 283 
AA5 8  9  O VAL B 175 ? O VAL B 280 N VAL B 138 ? N VAL B 243 
AA5 9  10 O MET B 137 ? O MET B 242 N ALA B 126 ? N ALA B 231 
AA6 1  2  N ARG B 84  ? N ARG B 189 O THR B 301 ? O THR B 406 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A MYA 2001 ? 34 'binding site for residue MYA A 2001' 
AC2 Software A PO4 2002 ? 8  'binding site for residue PO4 A 2002' 
AC3 Software A PO4 2003 ? 10 'binding site for residue PO4 A 2003' 
AC4 Software A PO4 2004 ? 9  'binding site for residue PO4 A 2004' 
AC5 Software A 9M2 2005 ? 15 'binding site for residue 9M2 A 2005' 
AC6 Software A MG  2006 ? 6  'binding site for residue MG A 2006'  
AC7 Software A GOL 2007 ? 10 'binding site for residue GOL A 2007' 
AC8 Software A DMS 2008 ? 4  'binding site for residue DMS A 2008' 
AC9 Software B MYA 2001 ? 35 'binding site for residue MYA B 2001' 
AD1 Software B PO4 2002 ? 9  'binding site for residue PO4 B 2002' 
AD2 Software B PO4 2003 ? 11 'binding site for residue PO4 B 2003' 
AD3 Software B PO4 2004 ? 8  'binding site for residue PO4 B 2004' 
AD4 Software B PO4 2005 ? 5  'binding site for residue PO4 B 2005' 
AD5 Software B PO4 2006 ? 5  'binding site for residue PO4 B 2006' 
AD6 Software B 9M2 2007 ? 16 'binding site for residue 9M2 B 2007' 
AD7 Software B MG  2008 ? 6  'binding site for residue MG B 2008'  
AD8 Software B GOL 2009 ? 10 'binding site for residue GOL B 2009' 
AD9 Software B GOL 2010 ? 6  'binding site for residue GOL B 2010' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 34 TYR A 12  ? TYR A 117  . ? 1_555 ? 
2   AC1 34 GLN A 13  ? GLN A 118  . ? 1_555 ? 
3   AC1 34 PHE A 14  ? PHE A 119  . ? 1_555 ? 
4   AC1 34 TRP A 15  ? TRP A 120  . ? 1_555 ? 
5   AC1 34 ASN A 74  ? ASN A 179  . ? 1_555 ? 
6   AC1 34 TYR A 75  ? TYR A 180  . ? 1_555 ? 
7   AC1 34 VAL A 76  ? VAL A 181  . ? 1_555 ? 
8   AC1 34 ASN A 141 ? ASN A 246  . ? 1_555 ? 
9   AC1 34 PHE A 142 ? PHE A 247  . ? 1_555 ? 
10  AC1 34 LEU A 143 ? LEU A 248  . ? 1_555 ? 
11  AC1 34 CYS A 144 ? CYS A 249  . ? 1_555 ? 
12  AC1 34 VAL A 145 ? VAL A 250  . ? 1_555 ? 
13  AC1 34 ARG A 150 ? ARG A 255  . ? 1_555 ? 
14  AC1 34 SER A 151 ? SER A 256  . ? 1_555 ? 
15  AC1 34 LYS A 152 ? LYS A 257  . ? 1_555 ? 
16  AC1 34 ARG A 153 ? ARG A 258  . ? 1_555 ? 
17  AC1 34 VAL A 154 ? VAL A 259  . ? 1_555 ? 
18  AC1 34 ALA A 155 ? ALA A 260  . ? 1_555 ? 
19  AC1 34 PRO A 156 ? PRO A 261  . ? 1_555 ? 
20  AC1 34 THR A 163 ? THR A 268  . ? 1_555 ? 
21  AC1 34 VAL A 166 ? VAL A 271  . ? 1_555 ? 
22  AC1 34 PHE A 172 ? PHE A 277  . ? 1_555 ? 
23  AC1 34 TYR A 176 ? TYR A 281  . ? 1_555 ? 
24  AC1 34 THR A 177 ? THR A 282  . ? 1_555 ? 
25  AC1 34 LEU A 182 ? LEU A 287  . ? 1_555 ? 
26  AC1 34 TYR A 374 ? TYR A 479  . ? 1_555 ? 
27  AC1 34 MG  H .   ? MG  A 2006 . ? 1_555 ? 
28  AC1 34 HOH U .   ? HOH A 2130 . ? 1_555 ? 
29  AC1 34 HOH U .   ? HOH A 2199 . ? 1_555 ? 
30  AC1 34 HOH U .   ? HOH A 2203 . ? 1_555 ? 
31  AC1 34 HOH U .   ? HOH A 2274 . ? 1_555 ? 
32  AC1 34 HOH U .   ? HOH A 2320 . ? 1_555 ? 
33  AC1 34 HOH U .   ? HOH A 2388 . ? 1_555 ? 
34  AC1 34 HOH U .   ? HOH A 2391 . ? 1_555 ? 
35  AC2 8  GLU A 34  ? GLU A 139  . ? 1_555 ? 
36  AC2 8  LYS A 37  ? LYS A 142  . ? 1_555 ? 
37  AC2 8  HOH U .   ? HOH A 2156 . ? 1_555 ? 
38  AC2 8  HOH U .   ? HOH A 2174 . ? 1_555 ? 
39  AC2 8  HOH U .   ? HOH A 2188 . ? 1_555 ? 
40  AC2 8  HOH U .   ? HOH A 2237 . ? 1_555 ? 
41  AC2 8  HOH U .   ? HOH A 2242 . ? 1_555 ? 
42  AC2 8  HOH U .   ? HOH A 2350 . ? 1_555 ? 
43  AC3 10 TYR A 45  ? TYR A 150  . ? 1_555 ? 
44  AC3 10 THR A 46  ? THR A 151  . ? 1_555 ? 
45  AC3 10 VAL A 157 ? VAL A 262  . ? 1_555 ? 
46  AC3 10 ARG A 160 ? ARG A 265  . ? 1_555 ? 
47  AC3 10 ALA A 231 ? ALA A 336  . ? 1_556 ? 
48  AC3 10 GLY A 232 ? GLY A 337  . ? 1_556 ? 
49  AC3 10 LEU A 233 ? LEU A 338  . ? 1_556 ? 
50  AC3 10 DMS J .   ? DMS A 2008 . ? 1_555 ? 
51  AC3 10 HOH U .   ? HOH A 2116 . ? 1_555 ? 
52  AC3 10 HOH U .   ? HOH A 2152 . ? 1_556 ? 
53  AC4 9  GLN A 13  ? GLN A 118  . ? 1_555 ? 
54  AC4 9  PHE A 14  ? PHE A 119  . ? 1_555 ? 
55  AC4 9  ARG A 153 ? ARG A 258  . ? 1_555 ? 
56  AC4 9  PRO A 156 ? PRO A 261  . ? 1_555 ? 
57  AC4 9  ARG A 160 ? ARG A 265  . ? 1_555 ? 
58  AC4 9  LYS A 229 ? LYS A 334  . ? 1_556 ? 
59  AC4 9  HOH U .   ? HOH A 2119 . ? 1_555 ? 
60  AC4 9  HOH U .   ? HOH A 2163 . ? 1_555 ? 
61  AC4 9  HOH U .   ? HOH A 2434 . ? 1_555 ? 
62  AC5 15 VAL A 76  ? VAL A 181  . ? 1_555 ? 
63  AC5 15 PHE A 83  ? PHE A 188  . ? 1_555 ? 
64  AC5 15 PHE A 85  ? PHE A 190  . ? 1_555 ? 
65  AC5 15 TYR A 87  ? TYR A 192  . ? 1_555 ? 
66  AC5 15 ASN A 141 ? ASN A 246  . ? 1_555 ? 
67  AC5 15 THR A 177 ? THR A 282  . ? 1_555 ? 
68  AC5 15 TYR A 191 ? TYR A 296  . ? 1_555 ? 
69  AC5 15 SER A 300 ? SER A 405  . ? 1_555 ? 
70  AC5 15 TYR A 315 ? TYR A 420  . ? 1_555 ? 
71  AC5 15 ASN A 346 ? ASN A 451  . ? 1_555 ? 
72  AC5 15 ALA A 347 ? ALA A 452  . ? 1_555 ? 
73  AC5 15 LEU A 390 ? LEU A 495  . ? 1_555 ? 
74  AC5 15 GLN A 391 ? GLN A 496  . ? 1_555 ? 
75  AC5 15 HOH U .   ? HOH A 2138 . ? 1_555 ? 
76  AC5 15 HOH U .   ? HOH A 2317 . ? 1_555 ? 
77  AC6 6  LEU A 149 ? LEU A 254  . ? 1_555 ? 
78  AC6 6  SER A 151 ? SER A 256  . ? 1_555 ? 
79  AC6 6  LYS A 152 ? LYS A 257  . ? 1_555 ? 
80  AC6 6  ARG A 153 ? ARG A 258  . ? 1_555 ? 
81  AC6 6  VAL A 154 ? VAL A 259  . ? 1_555 ? 
82  AC6 6  MYA C .   ? MYA A 2001 . ? 1_555 ? 
83  AC7 10 PRO A 21  ? PRO A 126  . ? 1_555 ? 
84  AC7 10 LYS A 184 ? LYS A 289  . ? 1_555 ? 
85  AC7 10 VAL A 186 ? VAL A 291  . ? 1_555 ? 
86  AC7 10 TYR A 372 ? TYR A 477  . ? 1_555 ? 
87  AC7 10 LEU A 373 ? LEU A 478  . ? 1_555 ? 
88  AC7 10 TRP A 376 ? TRP A 481  . ? 1_555 ? 
89  AC7 10 LYS A 377 ? LYS A 482  . ? 1_555 ? 
90  AC7 10 CYS A 378 ? CYS A 483  . ? 1_555 ? 
91  AC7 10 SER A 380 ? SER A 485  . ? 1_555 ? 
92  AC7 10 HOH U .   ? HOH A 2145 . ? 1_555 ? 
93  AC8 4  LEU A 233 ? LEU A 338  . ? 1_556 ? 
94  AC8 4  PO4 E .   ? PO4 A 2003 . ? 1_555 ? 
95  AC8 4  HOH U .   ? HOH A 2187 . ? 1_555 ? 
96  AC8 4  HOH U .   ? HOH A 2342 . ? 1_555 ? 
97  AC9 35 ARG B 10  ? ARG B 115  . ? 1_555 ? 
98  AC9 35 TYR B 12  ? TYR B 117  . ? 1_555 ? 
99  AC9 35 GLN B 13  ? GLN B 118  . ? 1_555 ? 
100 AC9 35 PHE B 14  ? PHE B 119  . ? 1_555 ? 
101 AC9 35 TRP B 15  ? TRP B 120  . ? 1_555 ? 
102 AC9 35 ASN B 74  ? ASN B 179  . ? 1_555 ? 
103 AC9 35 TYR B 75  ? TYR B 180  . ? 1_555 ? 
104 AC9 35 VAL B 76  ? VAL B 181  . ? 1_555 ? 
105 AC9 35 ASN B 141 ? ASN B 246  . ? 1_555 ? 
106 AC9 35 PHE B 142 ? PHE B 247  . ? 1_555 ? 
107 AC9 35 LEU B 143 ? LEU B 248  . ? 1_555 ? 
108 AC9 35 CYS B 144 ? CYS B 249  . ? 1_555 ? 
109 AC9 35 VAL B 145 ? VAL B 250  . ? 1_555 ? 
110 AC9 35 ARG B 150 ? ARG B 255  . ? 1_555 ? 
111 AC9 35 SER B 151 ? SER B 256  . ? 1_555 ? 
112 AC9 35 LYS B 152 ? LYS B 257  . ? 1_555 ? 
113 AC9 35 ARG B 153 ? ARG B 258  . ? 1_555 ? 
114 AC9 35 VAL B 154 ? VAL B 259  . ? 1_555 ? 
115 AC9 35 ALA B 155 ? ALA B 260  . ? 1_555 ? 
116 AC9 35 PRO B 156 ? PRO B 261  . ? 1_555 ? 
117 AC9 35 THR B 163 ? THR B 268  . ? 1_555 ? 
118 AC9 35 VAL B 166 ? VAL B 271  . ? 1_555 ? 
119 AC9 35 PHE B 172 ? PHE B 277  . ? 1_555 ? 
120 AC9 35 THR B 177 ? THR B 282  . ? 1_555 ? 
121 AC9 35 LEU B 182 ? LEU B 287  . ? 1_555 ? 
122 AC9 35 TYR B 374 ? TYR B 479  . ? 1_555 ? 
123 AC9 35 MG  R .   ? MG  B 2008 . ? 1_555 ? 
124 AC9 35 HOH V .   ? HOH B 2145 . ? 1_555 ? 
125 AC9 35 HOH V .   ? HOH B 2160 . ? 1_555 ? 
126 AC9 35 HOH V .   ? HOH B 2212 . ? 1_555 ? 
127 AC9 35 HOH V .   ? HOH B 2287 . ? 1_555 ? 
128 AC9 35 HOH V .   ? HOH B 2311 . ? 1_555 ? 
129 AC9 35 HOH V .   ? HOH B 2371 . ? 1_555 ? 
130 AC9 35 HOH V .   ? HOH B 2411 . ? 1_555 ? 
131 AC9 35 HOH V .   ? HOH B 2471 . ? 1_555 ? 
132 AD1 9  GLU B 34  ? GLU B 139  . ? 1_555 ? 
133 AD1 9  LYS B 37  ? LYS B 142  . ? 1_555 ? 
134 AD1 9  HOH V .   ? HOH B 2108 . ? 1_555 ? 
135 AD1 9  HOH V .   ? HOH B 2190 . ? 1_555 ? 
136 AD1 9  HOH V .   ? HOH B 2205 . ? 1_555 ? 
137 AD1 9  HOH V .   ? HOH B 2275 . ? 1_555 ? 
138 AD1 9  HOH V .   ? HOH B 2284 . ? 1_555 ? 
139 AD1 9  HOH V .   ? HOH B 2307 . ? 1_555 ? 
140 AD1 9  HOH V .   ? HOH B 2315 . ? 1_555 ? 
141 AD2 11 TYR B 45  ? TYR B 150  . ? 1_555 ? 
142 AD2 11 THR B 46  ? THR B 151  . ? 1_555 ? 
143 AD2 11 VAL B 157 ? VAL B 262  . ? 1_555 ? 
144 AD2 11 ARG B 160 ? ARG B 265  . ? 1_555 ? 
145 AD2 11 ALA B 231 ? ALA B 336  . ? 1_554 ? 
146 AD2 11 GLY B 232 ? GLY B 337  . ? 1_554 ? 
147 AD2 11 LEU B 233 ? LEU B 338  . ? 1_554 ? 
148 AD2 11 GOL T .   ? GOL B 2010 . ? 1_554 ? 
149 AD2 11 HOH V .   ? HOH B 2115 . ? 1_555 ? 
150 AD2 11 HOH V .   ? HOH B 2126 . ? 1_555 ? 
151 AD2 11 HOH V .   ? HOH B 2324 . ? 1_555 ? 
152 AD3 8  GLN B 13  ? GLN B 118  . ? 1_555 ? 
153 AD3 8  PHE B 14  ? PHE B 119  . ? 1_555 ? 
154 AD3 8  ARG B 153 ? ARG B 258  . ? 1_555 ? 
155 AD3 8  PRO B 156 ? PRO B 261  . ? 1_555 ? 
156 AD3 8  ARG B 160 ? ARG B 265  . ? 1_555 ? 
157 AD3 8  LYS B 229 ? LYS B 334  . ? 1_554 ? 
158 AD3 8  HOH V .   ? HOH B 2104 . ? 1_555 ? 
159 AD3 8  HOH V .   ? HOH B 2399 . ? 1_555 ? 
160 AD4 5  ARG B 61  ? ARG B 166  . ? 1_555 ? 
161 AD4 5  LYS B 65  ? LYS B 170  . ? 1_555 ? 
162 AD4 5  ARG B 250 ? ARG B 355  . ? 4_555 ? 
163 AD4 5  HOH V .   ? HOH B 2144 . ? 1_555 ? 
164 AD4 5  HOH V .   ? HOH B 2421 . ? 1_555 ? 
165 AD5 5  GLU B 267 ? GLU B 372  . ? 1_555 ? 
166 AD5 5  HIS B 268 ? HIS B 373  . ? 1_555 ? 
167 AD5 5  HOH V .   ? HOH B 2129 . ? 1_555 ? 
168 AD5 5  HOH V .   ? HOH B 2292 . ? 1_555 ? 
169 AD5 5  HOH V .   ? HOH B 2422 . ? 1_555 ? 
170 AD6 16 VAL B 76  ? VAL B 181  . ? 1_555 ? 
171 AD6 16 PHE B 83  ? PHE B 188  . ? 1_555 ? 
172 AD6 16 PHE B 85  ? PHE B 190  . ? 1_555 ? 
173 AD6 16 TYR B 87  ? TYR B 192  . ? 1_555 ? 
174 AD6 16 ASN B 141 ? ASN B 246  . ? 1_555 ? 
175 AD6 16 THR B 177 ? THR B 282  . ? 1_555 ? 
176 AD6 16 TYR B 191 ? TYR B 296  . ? 1_555 ? 
177 AD6 16 SER B 300 ? SER B 405  . ? 1_555 ? 
178 AD6 16 TYR B 315 ? TYR B 420  . ? 1_555 ? 
179 AD6 16 ASN B 346 ? ASN B 451  . ? 1_555 ? 
180 AD6 16 ALA B 347 ? ALA B 452  . ? 1_555 ? 
181 AD6 16 LEU B 348 ? LEU B 453  . ? 1_555 ? 
182 AD6 16 LEU B 390 ? LEU B 495  . ? 1_555 ? 
183 AD6 16 GLN B 391 ? GLN B 496  . ? 1_555 ? 
184 AD6 16 HOH V .   ? HOH B 2131 . ? 1_555 ? 
185 AD6 16 HOH V .   ? HOH B 2258 . ? 1_555 ? 
186 AD7 6  LEU B 149 ? LEU B 254  . ? 1_555 ? 
187 AD7 6  SER B 151 ? SER B 256  . ? 1_555 ? 
188 AD7 6  LYS B 152 ? LYS B 257  . ? 1_555 ? 
189 AD7 6  ARG B 153 ? ARG B 258  . ? 1_555 ? 
190 AD7 6  VAL B 154 ? VAL B 259  . ? 1_555 ? 
191 AD7 6  MYA K .   ? MYA B 2001 . ? 1_555 ? 
192 AD8 10 PRO B 21  ? PRO B 126  . ? 1_555 ? 
193 AD8 10 LYS B 184 ? LYS B 289  . ? 1_555 ? 
194 AD8 10 PRO B 185 ? PRO B 290  . ? 1_555 ? 
195 AD8 10 VAL B 186 ? VAL B 291  . ? 1_555 ? 
196 AD8 10 TYR B 372 ? TYR B 477  . ? 1_555 ? 
197 AD8 10 LEU B 373 ? LEU B 478  . ? 1_555 ? 
198 AD8 10 TRP B 376 ? TRP B 481  . ? 1_555 ? 
199 AD8 10 LYS B 377 ? LYS B 482  . ? 1_555 ? 
200 AD8 10 CYS B 378 ? CYS B 483  . ? 1_555 ? 
201 AD8 10 SER B 380 ? SER B 485  . ? 1_555 ? 
202 AD9 6  LEU B 233 ? LEU B 338  . ? 1_555 ? 
203 AD9 6  PRO B 235 ? PRO B 340  . ? 1_555 ? 
204 AD9 6  PHE B 280 ? PHE B 385  . ? 1_555 ? 
205 AD9 6  PO4 M .   ? PO4 B 2003 . ? 1_556 ? 
206 AD9 6  HOH V .   ? HOH B 2465 . ? 1_555 ? 
207 AD9 6  HOH V .   ? HOH B 2477 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5O6H 
_atom_sites.fract_transf_matrix[1][1]   0.012636 
_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]   0.005591 
_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]   0.017104 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ARG A 1 10  ? -32.629 -0.602  -0.985  1.00 59.79 ? 115  ARG A N   1 
ATOM   2    C  CA  . ARG A 1 10  ? -31.948 -0.737  0.324   1.00 60.61 ? 115  ARG A CA  1 
ATOM   3    C  C   . ARG A 1 10  ? -32.118 0.591   1.110   1.00 54.85 ? 115  ARG A C   1 
ATOM   4    O  O   . ARG A 1 10  ? -33.191 1.213   1.021   1.00 64.56 ? 115  ARG A O   1 
ATOM   5    C  CB  . ARG A 1 10  ? -30.485 -1.233  0.122   1.00 66.84 ? 115  ARG A CB  1 
ATOM   6    C  CG  . ARG A 1 10  ? -29.498 -0.341  -0.663  1.00 77.08 ? 115  ARG A CG  1 
ATOM   7    C  CD  . ARG A 1 10  ? -29.831 -0.098  -2.133  1.00 78.91 ? 115  ARG A CD  1 
ATOM   8    N  NE  . ARG A 1 10  ? -29.893 -1.325  -2.940  1.00 83.99 ? 115  ARG A NE  1 
ATOM   9    C  CZ  . ARG A 1 10  ? -30.268 -1.395  -4.227  1.00 85.31 ? 115  ARG A CZ  1 
ATOM   10   N  NH1 . ARG A 1 10  ? -30.636 -0.300  -4.920  1.00 76.77 ? 115  ARG A NH1 1 
ATOM   11   N  NH2 . ARG A 1 10  ? -30.276 -2.583  -4.831  1.00 78.59 ? 115  ARG A NH2 1 
ATOM   12   N  N   . SER A 1 11  ? -31.108 1.021   1.876   1.00 42.56 ? 116  SER A N   1 
ATOM   13   C  CA  . SER A 1 11  ? -31.040 2.391   2.477   1.00 35.34 ? 116  SER A CA  1 
ATOM   14   C  C   . SER A 1 11  ? -29.734 2.988   1.896   1.00 29.69 ? 116  SER A C   1 
ATOM   15   O  O   . SER A 1 11  ? -28.940 2.241   1.366   1.00 27.27 ? 116  SER A O   1 
ATOM   16   C  CB  . SER A 1 11  ? -30.942 2.300   3.997   1.00 37.92 ? 116  SER A CB  1 
ATOM   17   O  OG  . SER A 1 11  ? -29.682 1.735   4.314   1.00 38.16 ? 116  SER A OG  1 
ATOM   18   N  N   . TYR A 1 12  ? -29.547 4.301   1.942   1.00 24.45 ? 117  TYR A N   1 
ATOM   19   C  CA  . TYR A 1 12  ? -28.338 4.956   1.423   1.00 19.60 ? 117  TYR A CA  1 
ATOM   20   C  C   . TYR A 1 12  ? -27.882 5.927   2.492   1.00 17.90 ? 117  TYR A C   1 
ATOM   21   O  O   . TYR A 1 12  ? -28.449 7.017   2.752   1.00 17.49 ? 117  TYR A O   1 
ATOM   22   C  CB  . TYR A 1 12  ? -28.690 5.753   0.135   1.00 20.20 ? 117  TYR A CB  1 
ATOM   23   C  CG  . TYR A 1 12  ? -28.936 4.908   -1.091  1.00 20.89 ? 117  TYR A CG  1 
ATOM   24   C  CD1 . TYR A 1 12  ? -27.885 4.708   -1.992  1.00 21.35 ? 117  TYR A CD1 1 
ATOM   25   C  CD2 . TYR A 1 12  ? -30.193 4.416   -1.403  1.00 21.57 ? 117  TYR A CD2 1 
ATOM   26   C  CE1 . TYR A 1 12  ? -28.047 3.994   -3.185  1.00 22.27 ? 117  TYR A CE1 1 
ATOM   27   C  CE2 . TYR A 1 12  ? -30.374 3.696   -2.605  1.00 24.94 ? 117  TYR A CE2 1 
ATOM   28   C  CZ  . TYR A 1 12  ? -29.298 3.457   -3.451  1.00 24.12 ? 117  TYR A CZ  1 
ATOM   29   O  OH  . TYR A 1 12  ? -29.545 2.763   -4.632  1.00 28.05 ? 117  TYR A OH  1 
ATOM   30   N  N   . GLN A 1 13  ? -26.901 5.468   3.272   1.00 17.41 ? 118  GLN A N   1 
ATOM   31   C  CA  . GLN A 1 13  ? -26.467 6.238   4.430   1.00 18.86 ? 118  GLN A CA  1 
ATOM   32   C  C   . GLN A 1 13  ? -26.163 7.716   4.197   1.00 17.77 ? 118  GLN A C   1 
ATOM   33   O  O   . GLN A 1 13  ? -26.531 8.598   4.944   1.00 19.28 ? 118  GLN A O   1 
ATOM   34   C  CB  . GLN A 1 13  ? -25.264 5.541   5.117   1.00 20.66 ? 118  GLN A CB  1 
ATOM   35   C  CG  . GLN A 1 13  ? -24.743 6.309   6.341   1.00 24.19 ? 118  GLN A CG  1 
ATOM   36   C  CD  . GLN A 1 13  ? -23.594 5.535   7.049   1.00 29.05 ? 118  GLN A CD  1 
ATOM   37   O  OE1 . GLN A 1 13  ? -22.387 5.817   6.842   1.00 30.91 ? 118  GLN A OE1 1 
ATOM   38   N  NE2 . GLN A 1 13  ? -23.974 4.468   7.746   1.00 32.74 ? 118  GLN A NE2 1 
ATOM   39   N  N   . PHE A 1 14  ? -25.499 7.968   3.044   1.00 15.87 ? 119  PHE A N   1 
ATOM   40   C  CA  . PHE A 1 14  ? -25.279 9.374   2.632   1.00 16.51 ? 119  PHE A CA  1 
ATOM   41   C  C   . PHE A 1 14  ? -26.457 9.938   1.797   1.00 13.27 ? 119  PHE A C   1 
ATOM   42   O  O   . PHE A 1 14  ? -26.982 10.992  2.123   1.00 13.31 ? 119  PHE A O   1 
ATOM   43   C  CB  . PHE A 1 14  ? -23.980 9.473   1.827   1.00 16.81 ? 119  PHE A CB  1 
ATOM   44   C  CG  . PHE A 1 14  ? -23.805 10.840  1.192   1.00 15.74 ? 119  PHE A CG  1 
ATOM   45   C  CD1 . PHE A 1 14  ? -23.647 11.965  2.006   1.00 15.45 ? 119  PHE A CD1 1 
ATOM   46   C  CD2 . PHE A 1 14  ? -23.756 10.990  -0.212  1.00 15.40 ? 119  PHE A CD2 1 
ATOM   47   C  CE1 . PHE A 1 14  ? -23.460 13.257  1.404   1.00 17.58 ? 119  PHE A CE1 1 
ATOM   48   C  CE2 . PHE A 1 14  ? -23.627 12.260  -0.810  1.00 15.63 ? 119  PHE A CE2 1 
ATOM   49   C  CZ  . PHE A 1 14  ? -23.490 13.365  -0.006  1.00 15.65 ? 119  PHE A CZ  1 
ATOM   50   N  N   . TRP A 1 15  ? -26.865 9.233   0.755   1.00 14.35 ? 120  TRP A N   1 
ATOM   51   C  CA  . TRP A 1 15  ? -27.815 9.879   -0.179  1.00 13.81 ? 120  TRP A CA  1 
ATOM   52   C  C   . TRP A 1 15  ? -29.198 10.121  0.414   1.00 13.61 ? 120  TRP A C   1 
ATOM   53   O  O   . TRP A 1 15  ? -29.911 11.038  0.021   1.00 13.35 ? 120  TRP A O   1 
ATOM   54   C  CB  . TRP A 1 15  ? -27.938 9.113   -1.516  1.00 12.84 ? 120  TRP A CB  1 
ATOM   55   C  CG  . TRP A 1 15  ? -26.726 9.394   -2.401  1.00 12.90 ? 120  TRP A CG  1 
ATOM   56   C  CD1 . TRP A 1 15  ? -25.707 8.592   -2.661  1.00 13.12 ? 120  TRP A CD1 1 
ATOM   57   C  CD2 . TRP A 1 15  ? -26.529 10.622  -3.090  1.00 12.60 ? 120  TRP A CD2 1 
ATOM   58   N  NE1 . TRP A 1 15  ? -24.769 9.263   -3.540  1.00 13.45 ? 120  TRP A NE1 1 
ATOM   59   C  CE2 . TRP A 1 15  ? -25.284 10.501  -3.782  1.00 12.87 ? 120  TRP A CE2 1 
ATOM   60   C  CE3 . TRP A 1 15  ? -27.274 11.835  -3.132  1.00 12.94 ? 120  TRP A CE3 1 
ATOM   61   C  CZ2 . TRP A 1 15  ? -24.759 11.539  -4.552  1.00 11.47 ? 120  TRP A CZ2 1 
ATOM   62   C  CZ3 . TRP A 1 15  ? -26.797 12.853  -3.885  1.00 12.67 ? 120  TRP A CZ3 1 
ATOM   63   C  CH2 . TRP A 1 15  ? -25.523 12.713  -4.542  1.00 12.83 ? 120  TRP A CH2 1 
ATOM   64   N  N   . ASP A 1 16  ? -29.507 9.362   1.495   1.00 14.74 ? 121  ASP A N   1 
ATOM   65   C  CA  . ASP A 1 16  ? -30.827 9.607   2.168   1.00 14.69 ? 121  ASP A CA  1 
ATOM   66   C  C   . ASP A 1 16  ? -30.882 10.958  2.899   1.00 16.15 ? 121  ASP A C   1 
ATOM   67   O  O   . ASP A 1 16  ? -31.949 11.516  3.155   1.00 17.37 ? 121  ASP A O   1 
ATOM   68   C  CB  . ASP A 1 16  ? -31.101 8.455   3.192   1.00 18.88 ? 121  ASP A CB  1 
ATOM   69   C  CG  . ASP A 1 16  ? -31.540 7.174   2.549   1.00 23.98 ? 121  ASP A CG  1 
ATOM   70   O  OD1 . ASP A 1 16  ? -31.865 7.128   1.353   1.00 26.29 ? 121  ASP A OD1 1 
ATOM   71   O  OD2 . ASP A 1 16  ? -31.525 6.136   3.284   1.00 27.39 ? 121  ASP A OD2 1 
ATOM   72   N  N   . THR A 1 17  ? -29.676 11.553  3.163   1.00 15.14 ? 122  THR A N   1 
ATOM   73   C  CA  . THR A 1 17  ? -29.579 12.836  3.794   1.00 14.85 ? 122  THR A CA  1 
ATOM   74   C  C   . THR A 1 17  ? -29.648 13.998  2.808   1.00 13.80 ? 122  THR A C   1 
ATOM   75   O  O   . THR A 1 17  ? -29.694 15.156  3.255   1.00 14.98 ? 122  THR A O   1 
ATOM   76   C  CB  . THR A 1 17  ? -28.240 13.042  4.606   1.00 15.03 ? 122  THR A CB  1 
ATOM   77   O  OG1 . THR A 1 17  ? -27.125 13.169  3.704   1.00 15.87 ? 122  THR A OG1 1 
ATOM   78   C  CG2 . THR A 1 17  ? -27.969 11.789  5.573   1.00 16.98 ? 122  THR A CG2 1 
ATOM   79   N  N   . GLN A 1 18  ? -29.631 13.699  1.504   1.00 12.60 ? 123  GLN A N   1 
ATOM   80   C  CA  . GLN A 1 18  ? -29.436 14.770  0.466   1.00 12.71 ? 123  GLN A CA  1 
ATOM   81   C  C   . GLN A 1 18  ? -30.775 15.226  -0.136  1.00 12.93 ? 123  GLN A C   1 
ATOM   82   O  O   . GLN A 1 18  ? -31.738 14.415  -0.143  1.00 13.87 ? 123  GLN A O   1 
ATOM   83   C  CB  . GLN A 1 18  ? -28.490 14.233  -0.654  1.00 13.50 ? 123  GLN A CB  1 
ATOM   84   C  CG  . GLN A 1 18  ? -27.068 13.940  -0.040  1.00 12.54 ? 123  GLN A CG  1 
ATOM   85   C  CD  . GLN A 1 18  ? -26.399 15.228  0.435   1.00 12.51 ? 123  GLN A CD  1 
ATOM   86   O  OE1 . GLN A 1 18  ? -26.050 16.109  -0.388  1.00 13.08 ? 123  GLN A OE1 1 
ATOM   87   N  NE2 . GLN A 1 18  ? -26.300 15.430  1.753   1.00 12.87 ? 123  GLN A NE2 1 
ATOM   88   N  N   . PRO A 1 19  ? -30.808 16.435  -0.713  1.00 13.01 ? 124  PRO A N   1 
ATOM   89   C  CA  . PRO A 1 19  ? -32.025 16.963  -1.330  1.00 13.52 ? 124  PRO A CA  1 
ATOM   90   C  C   . PRO A 1 19  ? -32.203 16.336  -2.739  1.00 13.10 ? 124  PRO A C   1 
ATOM   91   O  O   . PRO A 1 19  ? -32.030 17.067  -3.767  1.00 14.33 ? 124  PRO A O   1 
ATOM   92   C  CB  . PRO A 1 19  ? -31.814 18.465  -1.298  1.00 14.41 ? 124  PRO A CB  1 
ATOM   93   C  CG  . PRO A 1 19  ? -30.256 18.594  -1.463  1.00 14.32 ? 124  PRO A CG  1 
ATOM   94   C  CD  . PRO A 1 19  ? -29.781 17.500  -0.523  1.00 13.44 ? 124  PRO A CD  1 
ATOM   95   N  N   . VAL A 1 20  ? -32.532 15.053  -2.753  1.00 13.09 ? 125  VAL A N   1 
ATOM   96   C  CA  . VAL A 1 20  ? -32.810 14.316  -3.971  1.00 13.18 ? 125  VAL A CA  1 
ATOM   97   C  C   . VAL A 1 20  ? -34.081 13.497  -3.621  1.00 17.47 ? 125  VAL A C   1 
ATOM   98   O  O   . VAL A 1 20  ? -34.230 13.101  -2.442  1.00 15.85 ? 125  VAL A O   1 
ATOM   99   C  CB  . VAL A 1 20  ? -31.658 13.445  -4.507  1.00 14.47 ? 125  VAL A CB  1 
ATOM   100  C  CG1 . VAL A 1 20  ? -30.461 14.363  -4.917  1.00 13.56 ? 125  VAL A CG1 1 
ATOM   101  C  CG2 . VAL A 1 20  ? -31.225 12.412  -3.446  1.00 15.42 ? 125  VAL A CG2 1 
ATOM   102  N  N   . PRO A 1 21  ? -34.887 13.117  -4.618  1.00 15.74 ? 126  PRO A N   1 
ATOM   103  C  CA  . PRO A 1 21  ? -36.087 12.264  -4.356  1.00 17.23 ? 126  PRO A CA  1 
ATOM   104  C  C   . PRO A 1 21  ? -35.636 10.876  -3.961  1.00 17.67 ? 126  PRO A C   1 
ATOM   105  O  O   . PRO A 1 21  ? -34.565 10.359  -4.323  1.00 18.19 ? 126  PRO A O   1 
ATOM   106  C  CB  . PRO A 1 21  ? -36.812 12.249  -5.717  1.00 16.36 ? 126  PRO A CB  1 
ATOM   107  C  CG  . PRO A 1 21  ? -36.289 13.411  -6.495  1.00 19.98 ? 126  PRO A CG  1 
ATOM   108  C  CD  . PRO A 1 21  ? -34.843 13.509  -6.034  1.00 16.13 ? 126  PRO A CD  1 
ATOM   109  N  N   . LYS A 1 22  ? -36.481 10.181  -3.172  1.00 22.23 ? 127  LYS A N   1 
ATOM   110  C  CA  A LYS A 1 22  ? -36.195 8.807   -2.851  0.50 22.50 ? 127  LYS A CA  1 
ATOM   111  C  CA  B LYS A 1 22  ? -36.208 8.795   -2.847  0.50 22.75 ? 127  LYS A CA  1 
ATOM   112  C  C   . LYS A 1 22  ? -36.395 7.862   -4.057  1.00 22.50 ? 127  LYS A C   1 
ATOM   113  O  O   . LYS A 1 22  ? -37.196 8.138   -4.902  1.00 24.23 ? 127  LYS A O   1 
ATOM   114  C  CB  A LYS A 1 22  ? -37.112 8.373   -1.694  0.50 23.76 ? 127  LYS A CB  1 
ATOM   115  C  CB  B LYS A 1 22  ? -37.157 8.308   -1.730  0.50 23.97 ? 127  LYS A CB  1 
ATOM   116  C  CG  A LYS A 1 22  ? -36.943 9.243   -0.449  0.50 29.47 ? 127  LYS A CG  1 
ATOM   117  C  CG  B LYS A 1 22  ? -37.116 9.116   -0.436  0.50 30.95 ? 127  LYS A CG  1 
ATOM   118  C  CD  A LYS A 1 22  ? -35.562 9.031   0.158   0.50 29.65 ? 127  LYS A CD  1 
ATOM   119  C  CD  B LYS A 1 22  ? -37.275 8.206   0.789   0.50 30.07 ? 127  LYS A CD  1 
ATOM   120  C  CE  A LYS A 1 22  ? -35.405 9.461   1.618   0.50 28.39 ? 127  LYS A CE  1 
ATOM   121  C  CE  B LYS A 1 22  ? -37.701 8.967   2.052   0.50 33.81 ? 127  LYS A CE  1 
ATOM   122  N  NZ  A LYS A 1 22  ? -34.719 10.780  1.708   0.50 28.12 ? 127  LYS A NZ  1 
ATOM   123  N  NZ  B LYS A 1 22  ? -37.863 8.079   3.247   0.50 34.69 ? 127  LYS A NZ  1 
ATOM   124  N  N   . LEU A 1 23  ? -35.648 6.792   -4.115  1.00 23.48 ? 128  LEU A N   1 
ATOM   125  C  CA  . LEU A 1 23  ? -35.932 5.743   -5.114  1.00 27.95 ? 128  LEU A CA  1 
ATOM   126  C  C   . LEU A 1 23  ? -37.355 5.218   -4.916  1.00 29.66 ? 128  LEU A C   1 
ATOM   127  O  O   . LEU A 1 23  ? -37.792 4.946   -3.794  1.00 35.83 ? 128  LEU A O   1 
ATOM   128  C  CB  . LEU A 1 23  ? -34.993 4.578   -4.934  1.00 24.17 ? 128  LEU A CB  1 
ATOM   129  C  CG  . LEU A 1 23  ? -33.641 4.539   -5.604  1.00 28.00 ? 128  LEU A CG  1 
ATOM   130  C  CD1 . LEU A 1 23  ? -33.021 3.139   -5.452  1.00 28.34 ? 128  LEU A CD1 1 
ATOM   131  C  CD2 . LEU A 1 23  ? -33.731 4.838   -7.141  1.00 25.43 ? 128  LEU A CD2 1 
ATOM   132  N  N   . GLY A 1 24  ? -38.121 5.118   -5.981  1.00 36.94 ? 129  GLY A N   1 
ATOM   133  C  CA  . GLY A 1 24  ? -39.493 4.670   -5.804  1.00 43.23 ? 129  GLY A CA  1 
ATOM   134  C  C   . GLY A 1 24  ? -40.479 5.784   -5.487  1.00 49.87 ? 129  GLY A C   1 
ATOM   135  O  O   . GLY A 1 24  ? -41.684 5.555   -5.498  1.00 49.70 ? 129  GLY A O   1 
ATOM   136  N  N   . GLU A 1 25  ? -39.979 6.997   -5.240  1.00 46.65 ? 130  GLU A N   1 
ATOM   137  C  CA  . GLU A 1 25  ? -40.829 8.175   -4.992  1.00 43.84 ? 130  GLU A CA  1 
ATOM   138  C  C   . GLU A 1 25  ? -41.567 8.535   -6.295  1.00 42.23 ? 130  GLU A C   1 
ATOM   139  O  O   . GLU A 1 25  ? -40.957 8.660   -7.351  1.00 40.68 ? 130  GLU A O   1 
ATOM   140  C  CB  . GLU A 1 25  ? -39.975 9.375   -4.497  1.00 40.98 ? 130  GLU A CB  1 
ATOM   141  C  CG  . GLU A 1 25  ? -40.757 10.571  -3.931  1.00 42.90 ? 130  GLU A CG  1 
ATOM   142  C  CD  . GLU A 1 25  ? -39.877 11.734  -3.461  1.00 37.22 ? 130  GLU A CD  1 
ATOM   143  O  OE1 . GLU A 1 25  ? -38.901 11.542  -2.741  1.00 34.88 ? 130  GLU A OE1 1 
ATOM   144  O  OE2 . GLU A 1 25  ? -40.246 12.872  -3.764  1.00 48.43 ? 130  GLU A OE2 1 
ATOM   145  N  N   . VAL A 1 26  ? -42.887 8.693   -6.225  1.00 41.04 ? 131  VAL A N   1 
ATOM   146  C  CA  A VAL A 1 26  ? -43.676 9.158   -7.376  0.50 39.92 ? 131  VAL A CA  1 
ATOM   147  C  CA  B VAL A 1 26  ? -43.623 9.146   -7.404  0.50 38.79 ? 131  VAL A CA  1 
ATOM   148  C  C   . VAL A 1 26  ? -43.536 10.675  -7.481  1.00 37.81 ? 131  VAL A C   1 
ATOM   149  O  O   . VAL A 1 26  ? -43.949 11.377  -6.570  1.00 36.64 ? 131  VAL A O   1 
ATOM   150  C  CB  A VAL A 1 26  ? -45.203 8.769   -7.260  0.50 42.50 ? 131  VAL A CB  1 
ATOM   151  C  CB  B VAL A 1 26  ? -45.116 8.682   -7.413  0.50 41.36 ? 131  VAL A CB  1 
ATOM   152  C  CG1 A VAL A 1 26  ? -45.837 9.252   -5.946  0.50 41.07 ? 131  VAL A CG1 1 
ATOM   153  C  CG1 B VAL A 1 26  ? -45.566 8.413   -8.850  0.50 37.69 ? 131  VAL A CG1 1 
ATOM   154  C  CG2 A VAL A 1 26  ? -46.002 9.262   -8.467  0.50 38.99 ? 131  VAL A CG2 1 
ATOM   155  C  CG2 B VAL A 1 26  ? -45.319 7.447   -6.522  0.50 36.77 ? 131  VAL A CG2 1 
ATOM   156  N  N   . VAL A 1 27  ? -42.959 11.182  -8.580  1.00 36.01 ? 132  VAL A N   1 
ATOM   157  C  CA  . VAL A 1 27  ? -42.864 12.623  -8.748  1.00 33.92 ? 132  VAL A CA  1 
ATOM   158  C  C   . VAL A 1 27  ? -43.809 13.197  -9.818  1.00 35.08 ? 132  VAL A C   1 
ATOM   159  O  O   . VAL A 1 27  ? -43.669 12.902  -11.012 1.00 42.51 ? 132  VAL A O   1 
ATOM   160  C  CB  . VAL A 1 27  ? -41.420 13.093  -9.078  1.00 30.10 ? 132  VAL A CB  1 
ATOM   161  C  CG1 . VAL A 1 27  ? -41.474 14.602  -9.197  1.00 27.99 ? 132  VAL A CG1 1 
ATOM   162  C  CG2 . VAL A 1 27  ? -40.409 12.621  -8.053  1.00 30.57 ? 132  VAL A CG2 1 
ATOM   163  N  N   . ASN A 1 28  ? -44.712 14.072  -9.391  1.00 39.92 ? 133  ASN A N   1 
ATOM   164  C  CA  . ASN A 1 28  ? -45.703 14.730  -10.261 1.00 46.67 ? 133  ASN A CA  1 
ATOM   165  C  C   . ASN A 1 28  ? -45.471 16.224  -10.420 1.00 48.22 ? 133  ASN A C   1 
ATOM   166  O  O   . ASN A 1 28  ? -46.204 16.877  -11.185 1.00 61.88 ? 133  ASN A O   1 
ATOM   167  C  CB  . ASN A 1 28  ? -47.109 14.564  -9.651  1.00 51.65 ? 133  ASN A CB  1 
ATOM   168  C  CG  . ASN A 1 28  ? -47.534 13.104  -9.544  1.00 57.63 ? 133  ASN A CG  1 
ATOM   169  O  OD1 . ASN A 1 28  ? -47.493 12.359  -10.536 1.00 62.26 ? 133  ASN A OD1 1 
ATOM   170  N  ND2 . ASN A 1 28  ? -47.945 12.687  -8.346  1.00 59.39 ? 133  ASN A ND2 1 
ATOM   171  N  N   . THR A 1 29  ? -44.483 16.774  -9.685  1.00 36.76 ? 134  THR A N   1 
ATOM   172  C  CA  . THR A 1 29  ? -44.282 18.236  -9.596  1.00 32.90 ? 134  THR A CA  1 
ATOM   173  C  C   . THR A 1 29  ? -42.877 18.550  -10.167 1.00 30.02 ? 134  THR A C   1 
ATOM   174  O  O   . THR A 1 29  ? -42.175 17.595  -10.517 1.00 27.37 ? 134  THR A O   1 
ATOM   175  C  CB  . THR A 1 29  ? -44.358 18.709  -8.132  1.00 36.04 ? 134  THR A CB  1 
ATOM   176  O  OG1 . THR A 1 29  ? -43.380 18.008  -7.383  1.00 36.04 ? 134  THR A OG1 1 
ATOM   177  C  CG2 . THR A 1 29  ? -45.819 18.451  -7.553  1.00 36.60 ? 134  THR A CG2 1 
ATOM   178  N  N   . HIS A 1 30  ? -42.577 19.830  -10.367 1.00 25.43 ? 135  HIS A N   1 
ATOM   179  C  CA  . HIS A 1 30  ? -41.234 20.283  -10.880 1.00 24.82 ? 135  HIS A CA  1 
ATOM   180  C  C   . HIS A 1 30  ? -40.765 21.395  -9.947  1.00 27.70 ? 135  HIS A C   1 
ATOM   181  O  O   . HIS A 1 30  ? -41.536 22.342  -9.709  1.00 32.47 ? 135  HIS A O   1 
ATOM   182  C  CB  . HIS A 1 30  ? -41.304 20.850  -12.336 1.00 25.93 ? 135  HIS A CB  1 
ATOM   183  C  CG  . HIS A 1 30  ? -42.081 19.994  -13.301 1.00 25.62 ? 135  HIS A CG  1 
ATOM   184  N  ND1 . HIS A 1 30  ? -41.500 19.302  -14.350 1.00 28.17 ? 135  HIS A ND1 1 
ATOM   185  C  CD2 . HIS A 1 30  ? -43.413 19.716  -13.348 1.00 28.87 ? 135  HIS A CD2 1 
ATOM   186  C  CE1 . HIS A 1 30  ? -42.444 18.610  -14.981 1.00 28.00 ? 135  HIS A CE1 1 
ATOM   187  N  NE2 . HIS A 1 30  ? -43.609 18.845  -14.386 1.00 29.51 ? 135  HIS A NE2 1 
ATOM   188  N  N   . GLY A 1 31  ? -39.532 21.298  -9.404  1.00 20.61 ? 136  GLY A N   1 
ATOM   189  C  CA  . GLY A 1 31  ? -38.999 22.387  -8.675  1.00 19.78 ? 136  GLY A CA  1 
ATOM   190  C  C   . GLY A 1 31  ? -37.922 21.941  -7.657  1.00 16.60 ? 136  GLY A C   1 
ATOM   191  O  O   . GLY A 1 31  ? -37.568 20.741  -7.560  1.00 17.27 ? 136  GLY A O   1 
ATOM   192  N  N   . PRO A 1 32  ? -37.360 22.881  -6.925  1.00 16.57 ? 137  PRO A N   1 
ATOM   193  C  CA  . PRO A 1 32  ? -36.293 22.472  -6.022  1.00 17.22 ? 137  PRO A CA  1 
ATOM   194  C  C   . PRO A 1 32  ? -36.738 21.606  -4.885  1.00 17.18 ? 137  PRO A C   1 
ATOM   195  O  O   . PRO A 1 32  ? -37.933 21.649  -4.441  1.00 19.89 ? 137  PRO A O   1 
ATOM   196  C  CB  . PRO A 1 32  ? -35.731 23.794  -5.480  1.00 17.24 ? 137  PRO A CB  1 
ATOM   197  C  CG  . PRO A 1 32  ? -36.797 24.821  -5.686  1.00 24.10 ? 137  PRO A CG  1 
ATOM   198  C  CD  . PRO A 1 32  ? -37.670 24.358  -6.836  1.00 18.03 ? 137  PRO A CD  1 
ATOM   199  N  N   . VAL A 1 33  ? -35.897 20.730  -4.404  1.00 15.52 ? 138  VAL A N   1 
ATOM   200  C  CA  . VAL A 1 33  ? -36.213 19.925  -3.228  1.00 15.66 ? 138  VAL A CA  1 
ATOM   201  C  C   . VAL A 1 33  ? -36.174 20.770  -1.970  1.00 18.09 ? 138  VAL A C   1 
ATOM   202  O  O   . VAL A 1 33  ? -37.003 20.577  -1.096  1.00 20.99 ? 138  VAL A O   1 
ATOM   203  C  CB  . VAL A 1 33  ? -35.255 18.683  -3.123  1.00 17.70 ? 138  VAL A CB  1 
ATOM   204  C  CG1 . VAL A 1 33  ? -35.496 17.923  -1.793  1.00 17.63 ? 138  VAL A CG1 1 
ATOM   205  C  CG2 . VAL A 1 33  ? -35.505 17.736  -4.349  1.00 17.37 ? 138  VAL A CG2 1 
ATOM   206  N  N   . GLU A 1 34  ? -35.222 21.698  -1.900  1.00 17.87 ? 139  GLU A N   1 
ATOM   207  C  CA  . GLU A 1 34  ? -35.115 22.666  -0.750  1.00 19.81 ? 139  GLU A CA  1 
ATOM   208  C  C   . GLU A 1 34  ? -34.725 24.046  -1.341  1.00 19.97 ? 139  GLU A C   1 
ATOM   209  O  O   . GLU A 1 34  ? -34.199 24.162  -2.426  1.00 20.00 ? 139  GLU A O   1 
ATOM   210  C  CB  . GLU A 1 34  ? -34.066 22.126  0.271   1.00 20.63 ? 139  GLU A CB  1 
ATOM   211  C  CG  . GLU A 1 34  ? -32.590 22.138  -0.247  1.00 19.08 ? 139  GLU A CG  1 
ATOM   212  C  CD  . GLU A 1 34  ? -31.506 21.604  0.680   1.00 18.38 ? 139  GLU A CD  1 
ATOM   213  O  OE1 . GLU A 1 34  ? -30.328 21.977  0.449   1.00 16.70 ? 139  GLU A OE1 1 
ATOM   214  O  OE2 . GLU A 1 34  ? -31.828 20.815  1.565   1.00 19.30 ? 139  GLU A OE2 1 
ATOM   215  N  N   . PRO A 1 35  ? -34.894 25.163  -0.524  1.00 24.01 ? 140  PRO A N   1 
ATOM   216  C  CA  . PRO A 1 35  ? -34.574 26.506  -1.046  1.00 24.56 ? 140  PRO A CA  1 
ATOM   217  C  C   . PRO A 1 35  ? -33.120 26.871  -1.242  1.00 24.85 ? 140  PRO A C   1 
ATOM   218  O  O   . PRO A 1 35  ? -32.170 26.152  -0.780  1.00 28.43 ? 140  PRO A O   1 
ATOM   219  C  CB  . PRO A 1 35  ? -35.266 27.473  -0.060  1.00 29.64 ? 140  PRO A CB  1 
ATOM   220  C  CG  . PRO A 1 35  ? -35.916 26.638  0.970   1.00 27.21 ? 140  PRO A CG  1 
ATOM   221  C  CD  . PRO A 1 35  ? -35.595 25.173  0.749   1.00 23.33 ? 140  PRO A CD  1 
ATOM   222  N  N   . ASP A 1 36  ? -32.857 27.917  -1.986  1.00 24.86 ? 141  ASP A N   1 
ATOM   223  C  CA  A ASP A 1 36  ? -31.548 28.490  -2.068  0.50 19.95 ? 141  ASP A CA  1 
ATOM   224  C  CA  B ASP A 1 36  ? -31.525 28.381  -1.993  0.50 23.63 ? 141  ASP A CA  1 
ATOM   225  C  C   . ASP A 1 36  ? -31.105 28.843  -0.613  1.00 23.43 ? 141  ASP A C   1 
ATOM   226  O  O   . ASP A 1 36  ? -31.933 29.229  0.250   1.00 23.65 ? 141  ASP A O   1 
ATOM   227  C  CB  A ASP A 1 36  ? -31.485 29.747  -2.993  0.50 17.45 ? 141  ASP A CB  1 
ATOM   228  C  CB  B ASP A 1 36  ? -31.362 29.362  -3.123  0.50 26.91 ? 141  ASP A CB  1 
ATOM   229  C  CG  A ASP A 1 36  ? -31.725 29.438  -4.538  0.50 14.11 ? 141  ASP A CG  1 
ATOM   230  C  CG  B ASP A 1 36  ? -31.966 28.782  -4.339  0.50 28.16 ? 141  ASP A CG  1 
ATOM   231  O  OD1 A ASP A 1 36  ? -31.740 28.240  -5.070  0.50 14.21 ? 141  ASP A OD1 1 
ATOM   232  O  OD1 B ASP A 1 36  ? -32.298 27.567  -4.179  0.50 19.96 ? 141  ASP A OD1 1 
ATOM   233  O  OD2 A ASP A 1 36  ? -31.589 30.391  -5.305  0.50 15.87 ? 141  ASP A OD2 1 
ATOM   234  O  OD2 B ASP A 1 36  ? -32.076 29.434  -5.388  0.50 37.01 ? 141  ASP A OD2 1 
ATOM   235  N  N   . LYS A 1 37  ? -29.813 28.717  -0.343  1.00 20.05 ? 142  LYS A N   1 
ATOM   236  C  CA  . LYS A 1 37  ? -29.378 28.950  1.049   1.00 20.99 ? 142  LYS A CA  1 
ATOM   237  C  C   . LYS A 1 37  ? -28.938 30.344  1.162   1.00 21.02 ? 142  LYS A C   1 
ATOM   238  O  O   . LYS A 1 37  ? -28.230 30.812  0.322   1.00 23.05 ? 142  LYS A O   1 
ATOM   239  C  CB  . LYS A 1 37  ? -28.174 28.007  1.334   1.00 18.70 ? 142  LYS A CB  1 
ATOM   240  C  CG  . LYS A 1 37  ? -28.685 26.596  1.518   1.00 18.27 ? 142  LYS A CG  1 
ATOM   241  C  CD  . LYS A 1 37  ? -27.485 25.609  1.785   1.00 17.80 ? 142  LYS A CD  1 
ATOM   242  C  CE  . LYS A 1 37  ? -27.944 24.168  1.939   1.00 15.43 ? 142  LYS A CE  1 
ATOM   243  N  NZ  . LYS A 1 37  ? -29.069 24.058  2.936   1.00 17.57 ? 142  LYS A NZ  1 
ATOM   244  N  N   . ASP A 1 38  ? -29.286 31.045  2.258   1.00 20.36 ? 143  ASP A N   1 
ATOM   245  C  CA  A ASP A 1 38  ? -28.618 32.398  2.206   0.50 21.06 ? 143  ASP A CA  1 
ATOM   246  C  CA  B ASP A 1 38  ? -28.819 32.389  2.508   0.50 19.72 ? 143  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 38  ? -27.525 32.529  3.296   1.00 18.13 ? 143  ASP A C   1 
ATOM   248  O  O   . ASP A 1 38  ? -26.987 33.624  3.456   1.00 16.88 ? 143  ASP A O   1 
ATOM   249  C  CB  A ASP A 1 38  ? -29.604 33.561  2.182   0.50 24.85 ? 143  ASP A CB  1 
ATOM   250  C  CB  B ASP A 1 38  ? -29.943 33.135  3.127   0.50 18.81 ? 143  ASP A CB  1 
ATOM   251  C  CG  A ASP A 1 38  ? -30.622 33.386  3.248   0.50 26.94 ? 143  ASP A CG  1 
ATOM   252  C  CG  B ASP A 1 38  ? -30.884 33.663  2.017   0.50 22.33 ? 143  ASP A CG  1 
ATOM   253  O  OD1 A ASP A 1 38  ? -30.209 32.781  4.219   0.50 21.17 ? 143  ASP A OD1 1 
ATOM   254  O  OD1 B ASP A 1 38  ? -30.585 33.453  0.792   0.50 26.90 ? 143  ASP A OD1 1 
ATOM   255  O  OD2 A ASP A 1 38  ? -31.819 33.713  3.119   0.50 30.17 ? 143  ASP A OD2 1 
ATOM   256  O  OD2 B ASP A 1 38  ? -31.855 34.326  2.351   0.50 27.77 ? 143  ASP A OD2 1 
ATOM   257  N  N   . ASN A 1 39  ? -27.144 31.382  3.921   1.00 15.87 ? 144  ASN A N   1 
ATOM   258  C  CA  A ASN A 1 39  ? -25.878 31.368  4.629   0.50 14.66 ? 144  ASN A CA  1 
ATOM   259  C  CA  B ASN A 1 39  ? -25.941 31.273  4.786   0.50 14.43 ? 144  ASN A CA  1 
ATOM   260  C  C   . ASN A 1 39  ? -25.298 29.962  4.331   1.00 10.24 ? 144  ASN A C   1 
ATOM   261  O  O   . ASN A 1 39  ? -25.987 28.951  4.405   1.00 12.23 ? 144  ASN A O   1 
ATOM   262  C  CB  A ASN A 1 39  ? -26.051 31.678  6.129   0.50 16.98 ? 144  ASN A CB  1 
ATOM   263  C  CB  B ASN A 1 39  ? -26.273 31.047  6.298   0.50 14.66 ? 144  ASN A CB  1 
ATOM   264  C  CG  A ASN A 1 39  ? -27.157 30.875  6.770   0.50 17.43 ? 144  ASN A CG  1 
ATOM   265  C  CG  B ASN A 1 39  ? -26.848 32.220  6.951   0.50 18.29 ? 144  ASN A CG  1 
ATOM   266  O  OD1 A ASN A 1 39  ? -27.061 30.556  7.970   0.50 22.33 ? 144  ASN A OD1 1 
ATOM   267  O  OD1 B ASN A 1 39  ? -26.147 33.022  7.535   0.50 21.44 ? 144  ASN A OD1 1 
ATOM   268  N  ND2 A ASN A 1 39  ? -28.190 30.512  6.019   0.50 18.47 ? 144  ASN A ND2 1 
ATOM   269  N  ND2 B ASN A 1 39  ? -28.094 32.365  6.771   0.50 18.73 ? 144  ASN A ND2 1 
ATOM   270  N  N   . ILE A 1 40  ? -24.013 30.038  3.929   1.00 11.35 ? 145  ILE A N   1 
ATOM   271  C  CA  A ILE A 1 40  ? -23.357 28.777  3.543   0.50 10.62 ? 145  ILE A CA  1 
ATOM   272  C  CA  B ILE A 1 40  ? -23.255 28.831  3.448   0.50 10.91 ? 145  ILE A CA  1 
ATOM   273  C  C   . ILE A 1 40  ? -22.102 28.612  4.428   1.00 9.91  ? 145  ILE A C   1 
ATOM   274  O  O   . ILE A 1 40  ? -21.355 29.529  4.749   1.00 10.36 ? 145  ILE A O   1 
ATOM   275  C  CB  A ILE A 1 40  ? -23.015 28.797  2.046   0.50 10.21 ? 145  ILE A CB  1 
ATOM   276  C  CB  B ILE A 1 40  ? -22.632 29.073  2.023   0.50 10.42 ? 145  ILE A CB  1 
ATOM   277  C  CG1 A ILE A 1 40  ? -24.281 28.977  1.149   0.50 11.20 ? 145  ILE A CG1 1 
ATOM   278  C  CG1 B ILE A 1 40  ? -23.703 29.515  1.006   0.50 11.95 ? 145  ILE A CG1 1 
ATOM   279  C  CG2 A ILE A 1 40  ? -22.193 27.560  1.650   0.50 10.61 ? 145  ILE A CG2 1 
ATOM   280  C  CG2 B ILE A 1 40  ? -21.854 27.807  1.571   0.50 10.41 ? 145  ILE A CG2 1 
ATOM   281  C  CD1 A ILE A 1 40  ? -24.101 29.758  -0.084  0.50 16.02 ? 145  ILE A CD1 1 
ATOM   282  C  CD1 B ILE A 1 40  ? -24.884 28.591  1.004   0.50 14.06 ? 145  ILE A CD1 1 
ATOM   283  N  N   . ARG A 1 41  ? -21.915 27.326  4.808   1.00 10.55 ? 146  ARG A N   1 
ATOM   284  C  CA  A ARG A 1 41  ? -20.732 26.861  5.591   0.50 10.73 ? 146  ARG A CA  1 
ATOM   285  C  CA  B ARG A 1 41  ? -20.790 26.913  5.624   0.50 11.64 ? 146  ARG A CA  1 
ATOM   286  C  C   . ARG A 1 41  ? -19.428 27.417  5.050   1.00 10.32 ? 146  ARG A C   1 
ATOM   287  O  O   . ARG A 1 41  ? -19.117 27.133  3.859   1.00 10.71 ? 146  ARG A O   1 
ATOM   288  C  CB  A ARG A 1 41  ? -20.626 25.332  5.534   0.50 10.98 ? 146  ARG A CB  1 
ATOM   289  C  CB  B ARG A 1 41  ? -20.897 25.396  5.725   0.50 12.84 ? 146  ARG A CB  1 
ATOM   290  C  CG  A ARG A 1 41  ? -19.467 24.697  6.391   0.50 9.18  ? 146  ARG A CG  1 
ATOM   291  C  CG  B ARG A 1 41  ? -19.922 24.725  6.692   0.50 13.24 ? 146  ARG A CG  1 
ATOM   292  C  CD  A ARG A 1 41  ? -19.726 23.168  6.270   0.50 9.41  ? 146  ARG A CD  1 
ATOM   293  C  CD  B ARG A 1 41  ? -19.859 23.225  6.453   0.50 13.84 ? 146  ARG A CD  1 
ATOM   294  N  NE  A ARG A 1 41  ? -19.730 22.422  7.542   0.50 10.04 ? 146  ARG A NE  1 
ATOM   295  N  NE  B ARG A 1 41  ? -18.501 22.874  6.781   0.50 15.71 ? 146  ARG A NE  1 
ATOM   296  C  CZ  A ARG A 1 41  ? -18.626 21.999  8.125   0.50 9.39  ? 146  ARG A CZ  1 
ATOM   297  C  CZ  B ARG A 1 41  ? -18.180 22.078  7.776   0.50 14.29 ? 146  ARG A CZ  1 
ATOM   298  N  NH1 A ARG A 1 41  ? -17.466 22.305  7.592   0.50 9.16  ? 146  ARG A NH1 1 
ATOM   299  N  NH1 B ARG A 1 41  ? -19.160 21.557  8.555   0.50 17.21 ? 146  ARG A NH1 1 
ATOM   300  N  NH2 A ARG A 1 41  ? -18.689 21.263  9.252   0.50 9.85  ? 146  ARG A NH2 1 
ATOM   301  N  NH2 B ARG A 1 41  ? -16.861 21.854  7.984   0.50 16.02 ? 146  ARG A NH2 1 
ATOM   302  N  N   . GLN A 1 42  ? -18.640 28.150  5.808   1.00 10.22 ? 147  GLN A N   1 
ATOM   303  C  CA  . GLN A 1 42  ? -17.358 28.709  5.361   1.00 11.36 ? 147  GLN A CA  1 
ATOM   304  C  C   . GLN A 1 42  ? -16.186 27.818  5.413   1.00 12.64 ? 147  GLN A C   1 
ATOM   305  O  O   . GLN A 1 42  ? -15.210 28.042  4.633   1.00 16.51 ? 147  GLN A O   1 
ATOM   306  C  CB  . GLN A 1 42  ? -16.965 29.989  6.115   1.00 11.96 ? 147  GLN A CB  1 
ATOM   307  C  CG  . GLN A 1 42  ? -18.010 31.086  5.875   1.00 14.30 ? 147  GLN A CG  1 
ATOM   308  C  CD  . GLN A 1 42  ? -17.538 32.417  6.389   1.00 19.02 ? 147  GLN A CD  1 
ATOM   309  O  OE1 . GLN A 1 42  ? -17.128 33.239  5.538   1.00 24.18 ? 147  GLN A OE1 1 
ATOM   310  N  NE2 . GLN A 1 42  ? -17.488 32.565  7.687   1.00 18.82 ? 147  GLN A NE2 1 
ATOM   311  N  N   . GLU A 1 43  ? -16.321 26.816  6.255   1.00 13.36 ? 148  GLU A N   1 
ATOM   312  C  CA  . GLU A 1 43  ? -15.107 25.907  6.437   1.00 14.89 ? 148  GLU A CA  1 
ATOM   313  C  C   . GLU A 1 43  ? -15.258 24.629  5.617   1.00 11.50 ? 148  GLU A C   1 
ATOM   314  O  O   . GLU A 1 43  ? -16.304 24.023  5.546   1.00 11.42 ? 148  GLU A O   1 
ATOM   315  C  CB  . GLU A 1 43  ? -15.067 25.529  7.837   1.00 17.47 ? 148  GLU A CB  1 
ATOM   316  C  CG  . GLU A 1 43  ? -14.993 26.825  8.720   1.00 20.69 ? 148  GLU A CG  1 
ATOM   317  C  CD  . GLU A 1 43  ? -16.411 27.327  9.111   1.00 21.26 ? 148  GLU A CD  1 
ATOM   318  O  OE1 . GLU A 1 43  ? -17.469 26.695  8.894   1.00 18.58 ? 148  GLU A OE1 1 
ATOM   319  O  OE2 . GLU A 1 43  ? -16.406 28.418  9.719   1.00 24.03 ? 148  GLU A OE2 1 
ATOM   320  N  N   . PRO A 1 44  ? -14.125 24.206  5.085   1.00 12.64 ? 149  PRO A N   1 
ATOM   321  C  CA  . PRO A 1 44  ? -14.122 22.955  4.375   1.00 12.10 ? 149  PRO A CA  1 
ATOM   322  C  C   . PRO A 1 44  ? -14.516 21.786  5.269   1.00 11.21 ? 149  PRO A C   1 
ATOM   323  O  O   . PRO A 1 44  ? -14.295 21.795  6.531   1.00 11.72 ? 149  PRO A O   1 
ATOM   324  C  CB  . PRO A 1 44  ? -12.662 22.767  3.937   1.00 13.34 ? 149  PRO A CB  1 
ATOM   325  C  CG  . PRO A 1 44  ? -12.065 24.166  3.928   1.00 15.28 ? 149  PRO A CG  1 
ATOM   326  C  CD  . PRO A 1 44  ? -12.844 24.915  5.013   1.00 14.96 ? 149  PRO A CD  1 
ATOM   327  N  N   . TYR A 1 45  ? -15.126 20.757  4.698   1.00 10.79 ? 150  TYR A N   1 
ATOM   328  C  CA  . TYR A 1 45  ? -15.387 19.486  5.415   1.00 10.80 ? 150  TYR A CA  1 
ATOM   329  C  C   . TYR A 1 45  ? -14.027 18.822  5.738   1.00 12.93 ? 150  TYR A C   1 
ATOM   330  O  O   . TYR A 1 45  ? -13.038 19.093  5.183   1.00 13.46 ? 150  TYR A O   1 
ATOM   331  C  CB  . TYR A 1 45  ? -16.294 18.585  4.560   1.00 11.56 ? 150  TYR A CB  1 
ATOM   332  C  CG  . TYR A 1 45  ? -17.730 19.088  4.551   1.00 10.81 ? 150  TYR A CG  1 
ATOM   333  C  CD1 . TYR A 1 45  ? -18.230 19.834  3.494   1.00 10.59 ? 150  TYR A CD1 1 
ATOM   334  C  CD2 . TYR A 1 45  ? -18.560 18.821  5.632   1.00 11.66 ? 150  TYR A CD2 1 
ATOM   335  C  CE1 . TYR A 1 45  ? -19.506 20.321  3.523   1.00 10.91 ? 150  TYR A CE1 1 
ATOM   336  C  CE2 . TYR A 1 45  ? -19.855 19.337  5.697   1.00 11.70 ? 150  TYR A CE2 1 
ATOM   337  C  CZ  . TYR A 1 45  ? -20.321 20.102  4.631   1.00 10.97 ? 150  TYR A CZ  1 
ATOM   338  O  OH  . TYR A 1 45  ? -21.635 20.526  4.692   1.00 11.94 ? 150  TYR A OH  1 
ATOM   339  N  N   . THR A 1 46  ? -14.130 17.976  6.758   1.00 14.10 ? 151  THR A N   1 
ATOM   340  C  CA  . THR A 1 46  ? -12.889 17.296  7.267   1.00 15.51 ? 151  THR A CA  1 
ATOM   341  C  C   . THR A 1 46  ? -12.651 15.972  6.627   1.00 13.32 ? 151  THR A C   1 
ATOM   342  O  O   . THR A 1 46  ? -13.469 15.109  6.626   1.00 16.07 ? 151  THR A O   1 
ATOM   343  C  CB  . THR A 1 46  ? -13.090 17.046  8.846   1.00 15.72 ? 151  THR A CB  1 
ATOM   344  O  OG1 . THR A 1 46  ? -13.229 18.375  9.430   1.00 19.40 ? 151  THR A OG1 1 
ATOM   345  C  CG2 . THR A 1 46  ? -11.870 16.327  9.450   1.00 21.70 ? 151  THR A CG2 1 
ATOM   346  N  N   . LEU A 1 47  ? -11.446 15.784  6.103   1.00 14.35 ? 152  LEU A N   1 
ATOM   347  C  CA  . LEU A 1 47  ? -11.025 14.473  5.579   1.00 15.44 ? 152  LEU A CA  1 
ATOM   348  C  C   . LEU A 1 47  ? -10.494 13.554  6.741   1.00 15.37 ? 152  LEU A C   1 
ATOM   349  O  O   . LEU A 1 47  ? -10.132 14.118  7.758   1.00 15.96 ? 152  LEU A O   1 
ATOM   350  C  CB  . LEU A 1 47  ? -9.911  14.698  4.576   1.00 15.64 ? 152  LEU A CB  1 
ATOM   351  C  CG  . LEU A 1 47  ? -10.480 15.307  3.211   1.00 14.26 ? 152  LEU A CG  1 
ATOM   352  C  CD1 . LEU A 1 47  ? -9.308  15.980  2.516   1.00 14.17 ? 152  LEU A CD1 1 
ATOM   353  C  CD2 . LEU A 1 47  ? -10.998 14.218  2.292   1.00 15.64 ? 152  LEU A CD2 1 
ATOM   354  N  N   . PRO A 1 48  ? -10.355 12.231  6.425   1.00 15.72 ? 153  PRO A N   1 
ATOM   355  C  CA  . PRO A 1 48  ? -9.671  11.403  7.489   1.00 17.61 ? 153  PRO A CA  1 
ATOM   356  C  C   . PRO A 1 48  ? -8.255  11.895  7.745   1.00 18.31 ? 153  PRO A C   1 
ATOM   357  O  O   . PRO A 1 48  ? -7.583  12.581  6.948   1.00 17.36 ? 153  PRO A O   1 
ATOM   358  C  CB  . PRO A 1 48  ? -9.658  10.011  6.859   1.00 18.54 ? 153  PRO A CB  1 
ATOM   359  C  CG  . PRO A 1 48  ? -10.887 10.013  5.915   1.00 19.30 ? 153  PRO A CG  1 
ATOM   360  C  CD  . PRO A 1 48  ? -10.874 11.432  5.321   1.00 18.13 ? 153  PRO A CD  1 
ATOM   361  N  N   . GLN A 1 49  ? -7.727  11.521  8.940   1.00 18.32 ? 154  GLN A N   1 
ATOM   362  C  CA  . GLN A 1 49  ? -6.467  11.993  9.349   1.00 19.88 ? 154  GLN A CA  1 
ATOM   363  C  C   . GLN A 1 49  ? -5.341  11.571  8.323   1.00 16.89 ? 154  GLN A C   1 
ATOM   364  O  O   . GLN A 1 49  ? -5.369  10.412  7.879   1.00 19.94 ? 154  GLN A O   1 
ATOM   365  C  CB  . GLN A 1 49  ? -6.201  11.402  10.773  1.00 25.18 ? 154  GLN A CB  1 
ATOM   366  C  CG  . GLN A 1 49  ? -5.268  12.283  11.571  1.00 39.33 ? 154  GLN A CG  1 
ATOM   367  C  CD  . GLN A 1 49  ? -3.820  11.949  11.362  1.00 48.23 ? 154  GLN A CD  1 
ATOM   368  O  OE1 . GLN A 1 49  ? -3.473  10.798  11.051  1.00 60.29 ? 154  GLN A OE1 1 
ATOM   369  N  NE2 . GLN A 1 49  ? -2.941  12.960  11.536  1.00 52.52 ? 154  GLN A NE2 1 
ATOM   370  N  N   . GLY A 1 50  ? -4.477  12.473  8.032   1.00 16.94 ? 155  GLY A N   1 
ATOM   371  C  CA  . GLY A 1 50  ? -3.359  12.229  7.104   1.00 17.74 ? 155  GLY A CA  1 
ATOM   372  C  C   . GLY A 1 50  ? -3.651  12.657  5.685   1.00 17.90 ? 155  GLY A C   1 
ATOM   373  O  O   . GLY A 1 50  ? -2.738  12.491  4.823   1.00 19.06 ? 155  GLY A O   1 
ATOM   374  N  N   . PHE A 1 51  ? -4.881  13.182  5.427   1.00 15.20 ? 156  PHE A N   1 
ATOM   375  C  CA  . PHE A 1 51  ? -5.211  13.620  4.014   1.00 14.05 ? 156  PHE A CA  1 
ATOM   376  C  C   . PHE A 1 51  ? -5.578  15.078  4.089   1.00 15.71 ? 156  PHE A C   1 
ATOM   377  O  O   . PHE A 1 51  ? -6.098  15.566  5.121   1.00 17.41 ? 156  PHE A O   1 
ATOM   378  C  CB  . PHE A 1 51  ? -6.372  12.793  3.475   1.00 15.58 ? 156  PHE A CB  1 
ATOM   379  C  CG  . PHE A 1 51  ? -6.075  11.316  3.424   1.00 16.38 ? 156  PHE A CG  1 
ATOM   380  C  CD1 . PHE A 1 51  ? -6.550  10.409  4.460   1.00 20.10 ? 156  PHE A CD1 1 
ATOM   381  C  CD2 . PHE A 1 51  ? -5.383  10.796  2.345   1.00 16.15 ? 156  PHE A CD2 1 
ATOM   382  C  CE1 . PHE A 1 51  ? -6.231  9.055   4.379   1.00 20.09 ? 156  PHE A CE1 1 
ATOM   383  C  CE2 . PHE A 1 51  ? -5.061  9.439   2.300   1.00 17.30 ? 156  PHE A CE2 1 
ATOM   384  C  CZ  . PHE A 1 51  ? -5.494  8.562   3.298   1.00 19.86 ? 156  PHE A CZ  1 
ATOM   385  N  N   . THR A 1 52  ? -5.370  15.805  2.994   1.00 14.11 ? 157  THR A N   1 
ATOM   386  C  CA  . THR A 1 52  ? -5.664  17.238  2.986   1.00 14.40 ? 157  THR A CA  1 
ATOM   387  C  C   . THR A 1 52  ? -6.295  17.611  1.595   1.00 12.92 ? 157  THR A C   1 
ATOM   388  O  O   . THR A 1 52  ? -5.955  16.966  0.545   1.00 13.04 ? 157  THR A O   1 
ATOM   389  C  CB  . THR A 1 52  ? -4.355  18.057  3.190   1.00 18.83 ? 157  THR A CB  1 
ATOM   390  O  OG1 . THR A 1 52  ? -4.698  19.487  3.265   1.00 21.86 ? 157  THR A OG1 1 
ATOM   391  C  CG2 . THR A 1 52  ? -3.314  17.838  2.098   1.00 18.84 ? 157  THR A CG2 1 
ATOM   392  N  N   . TRP A 1 53  ? -7.036  18.682  1.524   1.00 11.03 ? 158  TRP A N   1 
ATOM   393  C  CA  . TRP A 1 53  ? -7.537  19.263  0.293   1.00 10.49 ? 158  TRP A CA  1 
ATOM   394  C  C   . TRP A 1 53  ? -6.421  19.916  -0.420  1.00 10.93 ? 158  TRP A C   1 
ATOM   395  O  O   . TRP A 1 53  ? -5.519  20.551  0.197   1.00 13.56 ? 158  TRP A O   1 
ATOM   396  C  CB  . TRP A 1 53  ? -8.602  20.338  0.551   1.00 10.70 ? 158  TRP A CB  1 
ATOM   397  C  CG  . TRP A 1 53  ? -9.839  19.787  1.258   1.00 10.37 ? 158  TRP A CG  1 
ATOM   398  C  CD1 . TRP A 1 53  ? -10.248 20.141  2.552   1.00 11.72 ? 158  TRP A CD1 1 
ATOM   399  C  CD2 . TRP A 1 53  ? -10.797 18.847  0.778   1.00 9.76  ? 158  TRP A CD2 1 
ATOM   400  N  NE1 . TRP A 1 53  ? -11.390 19.429  2.882   1.00 11.71 ? 158  TRP A NE1 1 
ATOM   401  C  CE2 . TRP A 1 53  ? -11.769 18.667  1.798   1.00 10.42 ? 158  TRP A CE2 1 
ATOM   402  C  CE3 . TRP A 1 53  ? -10.931 18.150  -0.449  1.00 10.40 ? 158  TRP A CE3 1 
ATOM   403  C  CZ2 . TRP A 1 53  ? -12.829 17.750  1.674   1.00 10.44 ? 158  TRP A CZ2 1 
ATOM   404  C  CZ3 . TRP A 1 53  ? -11.997 17.286  -0.592  1.00 11.06 ? 158  TRP A CZ3 1 
ATOM   405  C  CH2 . TRP A 1 53  ? -12.918 17.067  0.459   1.00 10.06 ? 158  TRP A CH2 1 
ATOM   406  N  N   . ASP A 1 54  ? -6.464  19.955  -1.773  1.00 11.08 ? 159  ASP A N   1 
ATOM   407  C  CA  . ASP A 1 54  ? -5.604  20.824  -2.586  1.00 10.72 ? 159  ASP A CA  1 
ATOM   408  C  C   . ASP A 1 54  ? -6.306  21.117  -3.867  1.00 10.95 ? 159  ASP A C   1 
ATOM   409  O  O   . ASP A 1 54  ? -6.714  20.154  -4.575  1.00 12.87 ? 159  ASP A O   1 
ATOM   410  C  CB  . ASP A 1 54  ? -4.262  20.102  -2.923  1.00 11.87 ? 159  ASP A CB  1 
ATOM   411  C  CG  . ASP A 1 54  ? -3.227  20.984  -3.476  1.00 13.88 ? 159  ASP A CG  1 
ATOM   412  O  OD1 . ASP A 1 54  ? -3.263  22.233  -3.237  1.00 18.40 ? 159  ASP A OD1 1 
ATOM   413  O  OD2 . ASP A 1 54  ? -2.295  20.564  -4.189  1.00 14.49 ? 159  ASP A OD2 1 
ATOM   414  N  N   . ALA A 1 55  ? -6.503  22.387  -4.194  1.00 11.39 ? 160  ALA A N   1 
ATOM   415  C  CA  . ALA A 1 55  ? -7.084  22.754  -5.487  1.00 11.82 ? 160  ALA A CA  1 
ATOM   416  C  C   . ALA A 1 55  ? -6.024  22.646  -6.565  1.00 13.82 ? 160  ALA A C   1 
ATOM   417  O  O   . ALA A 1 55  ? -4.857  23.096  -6.429  1.00 16.82 ? 160  ALA A O   1 
ATOM   418  C  CB  . ALA A 1 55  ? -7.600  24.213  -5.437  1.00 14.50 ? 160  ALA A CB  1 
ATOM   419  N  N   . LEU A 1 56  ? -6.320  21.907  -7.606  1.00 10.70 ? 161  LEU A N   1 
ATOM   420  C  CA  . LEU A 1 56  ? -5.322  21.523  -8.597  1.00 11.89 ? 161  LEU A CA  1 
ATOM   421  C  C   . LEU A 1 56  ? -5.258  22.509  -9.734  1.00 10.83 ? 161  LEU A C   1 
ATOM   422  O  O   . LEU A 1 56  ? -6.291  22.718  -10.413 1.00 12.38 ? 161  LEU A O   1 
ATOM   423  C  CB  . LEU A 1 56  ? -5.607  20.129  -9.180  1.00 11.22 ? 161  LEU A CB  1 
ATOM   424  C  CG  . LEU A 1 56  ? -5.708  18.990  -8.168  1.00 10.81 ? 161  LEU A CG  1 
ATOM   425  C  CD1 . LEU A 1 56  ? -5.751  17.663  -8.942  1.00 12.83 ? 161  LEU A CD1 1 
ATOM   426  C  CD2 . LEU A 1 56  ? -4.473  19.004  -7.170  1.00 12.25 ? 161  LEU A CD2 1 
ATOM   427  N  N   . ASP A 1 57  ? -4.111  23.174  -9.947  1.00 10.18 ? 162  ASP A N   1 
ATOM   428  C  CA  . ASP A 1 57  ? -3.899  24.081  -11.094 1.00 10.37 ? 162  ASP A CA  1 
ATOM   429  C  C   . ASP A 1 57  ? -3.527  23.226  -12.324 1.00 11.18 ? 162  ASP A C   1 
ATOM   430  O  O   . ASP A 1 57  ? -2.383  22.801  -12.533 1.00 11.69 ? 162  ASP A O   1 
ATOM   431  C  CB  . ASP A 1 57  ? -2.798  25.067  -10.745 1.00 11.48 ? 162  ASP A CB  1 
ATOM   432  C  CG  . ASP A 1 57  ? -2.545  25.998  -11.874 1.00 13.40 ? 162  ASP A CG  1 
ATOM   433  O  OD1 . ASP A 1 57  ? -3.126  25.960  -12.933 1.00 12.49 ? 162  ASP A OD1 1 
ATOM   434  O  OD2 . ASP A 1 57  ? -1.506  26.779  -11.742 1.00 17.30 ? 162  ASP A OD2 1 
ATOM   435  N  N   . LEU A 1 58  ? -4.534  22.990  -13.151 1.00 10.73 ? 163  LEU A N   1 
ATOM   436  C  CA  . LEU A 1 58  ? -4.314  22.128  -14.312 1.00 10.99 ? 163  LEU A CA  1 
ATOM   437  C  C   . LEU A 1 58  ? -3.570  22.790  -15.398 1.00 12.14 ? 163  LEU A C   1 
ATOM   438  O  O   . LEU A 1 58  ? -3.183  22.122  -16.369 1.00 12.58 ? 163  LEU A O   1 
ATOM   439  C  CB  . LEU A 1 58  ? -5.714  21.574  -14.836 1.00 11.23 ? 163  LEU A CB  1 
ATOM   440  C  CG  . LEU A 1 58  ? -6.540  20.897  -13.759 1.00 13.26 ? 163  LEU A CG  1 
ATOM   441  C  CD1 . LEU A 1 58  ? -7.811  20.377  -14.434 1.00 14.64 ? 163  LEU A CD1 1 
ATOM   442  C  CD2 . LEU A 1 58  ? -5.807  19.690  -13.139 1.00 14.07 ? 163  LEU A CD2 1 
ATOM   443  N  N   . GLY A 1 59  ? -3.330  24.106  -15.299 1.00 12.18 ? 164  GLY A N   1 
ATOM   444  C  CA  . GLY A 1 59  ? -2.398  24.818  -16.182 1.00 12.88 ? 164  GLY A CA  1 
ATOM   445  C  C   . GLY A 1 59  ? -0.952  24.505  -15.829 1.00 13.25 ? 164  GLY A C   1 
ATOM   446  O  O   . GLY A 1 59  ? -0.071  24.947  -16.609 1.00 14.99 ? 164  GLY A O   1 
ATOM   447  N  N   . ASP A 1 60  ? -0.671  23.884  -14.709 1.00 12.59 ? 165  ASP A N   1 
ATOM   448  C  CA  . ASP A 1 60  ? 0.708   23.433  -14.384 1.00 13.12 ? 165  ASP A CA  1 
ATOM   449  C  C   . ASP A 1 60  ? 0.881   22.018  -14.938 1.00 13.63 ? 165  ASP A C   1 
ATOM   450  O  O   . ASP A 1 60  ? 0.097   21.090  -14.584 1.00 12.79 ? 165  ASP A O   1 
ATOM   451  C  CB  . ASP A 1 60  ? 0.888   23.479  -12.868 1.00 14.04 ? 165  ASP A CB  1 
ATOM   452  C  CG  . ASP A 1 60  ? 2.229   22.972  -12.482 1.00 15.47 ? 165  ASP A CG  1 
ATOM   453  O  OD1 . ASP A 1 60  ? 3.112   23.843  -12.263 1.00 18.79 ? 165  ASP A OD1 1 
ATOM   454  O  OD2 . ASP A 1 60  ? 2.529   21.777  -12.409 1.00 15.41 ? 165  ASP A OD2 1 
ATOM   455  N  N   . ARG A 1 61  ? 1.902   21.810  -15.772 1.00 14.12 ? 166  ARG A N   1 
ATOM   456  C  CA  A ARG A 1 61  ? 1.986   20.520  -16.452 0.50 14.81 ? 166  ARG A CA  1 
ATOM   457  C  CA  B ARG A 1 61  ? 2.058   20.539  -16.460 0.50 16.09 ? 166  ARG A CA  1 
ATOM   458  C  C   . ARG A 1 61  ? 2.216   19.382  -15.468 1.00 14.23 ? 166  ARG A C   1 
ATOM   459  O  O   . ARG A 1 61  ? 1.662   18.255  -15.667 1.00 14.44 ? 166  ARG A O   1 
ATOM   460  C  CB  A ARG A 1 61  ? 3.142   20.601  -17.477 0.50 17.90 ? 166  ARG A CB  1 
ATOM   461  C  CB  B ARG A 1 61  ? 3.310   20.679  -17.394 0.50 20.55 ? 166  ARG A CB  1 
ATOM   462  C  CG  A ARG A 1 61  ? 3.422   19.328  -18.255 0.50 20.39 ? 166  ARG A CG  1 
ATOM   463  C  CG  B ARG A 1 61  ? 3.080   21.587  -18.622 0.50 28.35 ? 166  ARG A CG  1 
ATOM   464  C  CD  A ARG A 1 61  ? 4.692   19.569  -19.085 0.50 26.19 ? 166  ARG A CD  1 
ATOM   465  C  CD  B ARG A 1 61  ? 4.310   22.443  -19.000 0.50 36.27 ? 166  ARG A CD  1 
ATOM   466  N  NE  A ARG A 1 61  ? 5.613   18.445  -18.967 0.50 32.55 ? 166  ARG A NE  1 
ATOM   467  N  NE  B ARG A 1 61  ? 5.360   21.760  -19.750 0.50 40.25 ? 166  ARG A NE  1 
ATOM   468  C  CZ  A ARG A 1 61  ? 6.914   18.579  -18.743 0.50 34.09 ? 166  ARG A CZ  1 
ATOM   469  C  CZ  B ARG A 1 61  ? 6.479   22.365  -20.146 0.50 42.20 ? 166  ARG A CZ  1 
ATOM   470  N  NH1 A ARG A 1 61  ? 7.455   19.792  -18.651 0.50 36.85 ? 166  ARG A NH1 1 
ATOM   471  N  NH1 B ARG A 1 61  ? 6.665   23.638  -19.843 0.50 47.01 ? 166  ARG A NH1 1 
ATOM   472  N  NH2 A ARG A 1 61  ? 7.672   17.499  -18.659 0.50 39.65 ? 166  ARG A NH2 1 
ATOM   473  N  NH2 B ARG A 1 61  ? 7.416   21.711  -20.826 0.50 43.98 ? 166  ARG A NH2 1 
ATOM   474  N  N   . GLY A 1 62  ? 2.988   19.615  -14.406 1.00 14.00 ? 167  GLY A N   1 
ATOM   475  C  CA  . GLY A 1 62  ? 3.247   18.561  -13.442 1.00 13.76 ? 167  GLY A CA  1 
ATOM   476  C  C   . GLY A 1 62  ? 1.980   18.150  -12.690 1.00 11.88 ? 167  GLY A C   1 
ATOM   477  O  O   . GLY A 1 62  ? 1.715   16.945  -12.496 1.00 12.21 ? 167  GLY A O   1 
ATOM   478  N  N   . VAL A 1 63  ? 1.141   19.143  -12.339 1.00 11.24 ? 168  VAL A N   1 
ATOM   479  C  CA  . VAL A 1 63  ? -0.090  18.805  -11.580 1.00 11.29 ? 168  VAL A CA  1 
ATOM   480  C  C   . VAL A 1 63  ? -1.080  18.116  -12.518 1.00 10.40 ? 168  VAL A C   1 
ATOM   481  O  O   . VAL A 1 63  ? -1.793  17.149  -12.118 1.00 10.64 ? 168  VAL A O   1 
ATOM   482  C  CB  . VAL A 1 63  ? -0.727  20.102  -10.970 1.00 10.70 ? 168  VAL A CB  1 
ATOM   483  C  CG1 . VAL A 1 63  ? -2.110  19.821  -10.346 1.00 12.28 ? 168  VAL A CG1 1 
ATOM   484  C  CG2 . VAL A 1 63  ? 0.227   20.695  -9.925  1.00 12.83 ? 168  VAL A CG2 1 
ATOM   485  N  N   . LEU A 1 64  ? -1.180  18.597  -13.767 1.00 10.49 ? 169  LEU A N   1 
ATOM   486  C  CA  . LEU A 1 64  ? -2.083  17.905  -14.715 1.00 10.74 ? 169  LEU A CA  1 
ATOM   487  C  C   . LEU A 1 64  ? -1.654  16.431  -14.932 1.00 11.06 ? 169  LEU A C   1 
ATOM   488  O  O   . LEU A 1 64  ? -2.510  15.552  -14.980 1.00 11.29 ? 169  LEU A O   1 
ATOM   489  C  CB  . LEU A 1 64  ? -2.112  18.673  -16.093 1.00 11.60 ? 169  LEU A CB  1 
ATOM   490  C  CG  . LEU A 1 64  ? -2.992  18.056  -17.198 1.00 12.33 ? 169  LEU A CG  1 
ATOM   491  C  CD1 . LEU A 1 64  ? -4.434  17.960  -16.753 1.00 14.27 ? 169  LEU A CD1 1 
ATOM   492  C  CD2 . LEU A 1 64  ? -2.732  18.877  -18.465 1.00 13.43 ? 169  LEU A CD2 1 
ATOM   493  N  N   . LYS A 1 65  ? -0.339  16.215  -14.988 1.00 11.62 ? 170  LYS A N   1 
ATOM   494  C  CA  . LYS A 1 65  ? 0.090   14.848  -15.107 1.00 12.48 ? 170  LYS A CA  1 
ATOM   495  C  C   . LYS A 1 65  ? -0.176  14.000  -13.886 1.00 10.27 ? 170  LYS A C   1 
ATOM   496  O  O   . LYS A 1 65  ? -0.506  12.808  -14.022 1.00 12.17 ? 170  LYS A O   1 
ATOM   497  C  CB  . LYS A 1 65  ? 1.621   14.844  -15.432 1.00 12.84 ? 170  LYS A CB  1 
ATOM   498  C  CG  . LYS A 1 65  ? 2.184   13.435  -15.803 1.00 15.40 ? 170  LYS A CG  1 
ATOM   499  C  CD  . LYS A 1 65  ? 1.594   12.893  -17.146 1.00 18.97 ? 170  LYS A CD  1 
ATOM   500  C  CE  . LYS A 1 65  ? 1.974   11.425  -17.448 1.00 19.01 ? 170  LYS A CE  1 
ATOM   501  N  NZ  . LYS A 1 65  ? 3.458   11.312  -17.779 1.00 20.54 ? 170  LYS A NZ  1 
ATOM   502  N  N   . GLU A 1 66  ? -0.160  14.593  -12.673 1.00 11.24 ? 171  GLU A N   1 
ATOM   503  C  CA  . GLU A 1 66  ? -0.606  13.838  -11.464 1.00 10.05 ? 171  GLU A CA  1 
ATOM   504  C  C   . GLU A 1 66  ? -2.046  13.415  -11.592 1.00 10.20 ? 171  GLU A C   1 
ATOM   505  O  O   . GLU A 1 66  ? -2.398  12.297  -11.178 1.00 10.25 ? 171  GLU A O   1 
ATOM   506  C  CB  . GLU A 1 66  ? -0.362  14.612  -10.173 1.00 9.91  ? 171  GLU A CB  1 
ATOM   507  C  CG  . GLU A 1 66  ? 1.099   14.926  -9.808  1.00 11.80 ? 171  GLU A CG  1 
ATOM   508  C  CD  . GLU A 1 66  ? 1.147   15.641  -8.500  1.00 11.88 ? 171  GLU A CD  1 
ATOM   509  O  OE1 . GLU A 1 66  ? 1.122   16.911  -8.542  1.00 13.50 ? 171  GLU A OE1 1 
ATOM   510  O  OE2 . GLU A 1 66  ? 1.151   14.947  -7.482  1.00 14.18 ? 171  GLU A OE2 1 
ATOM   511  N  N   . LEU A 1 67  ? -2.917  14.356  -12.099 1.00 10.19 ? 172  LEU A N   1 
ATOM   512  C  CA  . LEU A 1 67  ? -4.344  13.977  -12.246 1.00 9.80  ? 172  LEU A CA  1 
ATOM   513  C  C   . LEU A 1 67  ? -4.480  12.900  -13.300 1.00 8.93  ? 172  LEU A C   1 
ATOM   514  O  O   . LEU A 1 67  ? -5.271  11.926  -13.065 1.00 9.21  ? 172  LEU A O   1 
ATOM   515  C  CB  . LEU A 1 67  ? -5.194  15.290  -12.583 1.00 9.73  ? 172  LEU A CB  1 
ATOM   516  C  CG  . LEU A 1 67  ? -6.665  14.880  -12.809 1.00 9.19  ? 172  LEU A CG  1 
ATOM   517  C  CD1 . LEU A 1 67  ? -7.327  14.379  -11.558 1.00 10.21 ? 172  LEU A CD1 1 
ATOM   518  C  CD2 . LEU A 1 67  ? -7.368  16.214  -13.331 1.00 10.81 ? 172  LEU A CD2 1 
ATOM   519  N  N   . TYR A 1 68  ? -3.820  13.099  -14.421 1.00 9.67  ? 173  TYR A N   1 
ATOM   520  C  CA  . TYR A 1 68  ? -3.864  12.053  -15.478 1.00 8.98  ? 173  TYR A CA  1 
ATOM   521  C  C   . TYR A 1 68  ? -3.474  10.636  -14.874 1.00 9.08  ? 173  TYR A C   1 
ATOM   522  O  O   . TYR A 1 68  ? -4.185  9.674   -15.157 1.00 9.87  ? 173  TYR A O   1 
ATOM   523  C  CB  . TYR A 1 68  ? -2.753  12.403  -16.528 1.00 10.68 ? 173  TYR A CB  1 
ATOM   524  C  CG  . TYR A 1 68  ? -2.520  11.217  -17.429 1.00 10.93 ? 173  TYR A CG  1 
ATOM   525  C  CD1 . TYR A 1 68  ? -3.433  10.911  -18.449 1.00 10.75 ? 173  TYR A CD1 1 
ATOM   526  C  CD2 . TYR A 1 68  ? -1.390  10.370  -17.223 1.00 12.16 ? 173  TYR A CD2 1 
ATOM   527  C  CE1 . TYR A 1 68  ? -3.336  9.697   -19.201 1.00 11.76 ? 173  TYR A CE1 1 
ATOM   528  C  CE2 . TYR A 1 68  ? -1.258  9.214   -17.979 1.00 11.49 ? 173  TYR A CE2 1 
ATOM   529  C  CZ  . TYR A 1 68  ? -2.204  8.885   -18.919 1.00 10.71 ? 173  TYR A CZ  1 
ATOM   530  O  OH  . TYR A 1 68  ? -2.128  7.652   -19.666 1.00 12.10 ? 173  TYR A OH  1 
ATOM   531  N  N   . THR A 1 69  ? -2.422  10.596  -14.016 1.00 10.29 ? 174  THR A N   1 
ATOM   532  C  CA  . THR A 1 69  ? -2.007  9.296   -13.423 1.00 11.10 ? 174  THR A CA  1 
ATOM   533  C  C   . THR A 1 69  ? -3.003  8.745   -12.456 1.00 9.94  ? 174  THR A C   1 
ATOM   534  O  O   . THR A 1 69  ? -3.356  7.546   -12.467 1.00 10.96 ? 174  THR A O   1 
ATOM   535  C  CB  . THR A 1 69  ? -0.614  9.480   -12.896 1.00 12.16 ? 174  THR A CB  1 
ATOM   536  O  OG1 . THR A 1 69  ? 0.274   9.640   -14.019 1.00 15.53 ? 174  THR A OG1 1 
ATOM   537  C  CG2 . THR A 1 69  ? -0.184  8.211   -12.124 1.00 13.04 ? 174  THR A CG2 1 
ATOM   538  N  N   . LEU A 1 70  ? -3.604  9.616   -11.591 1.00 10.00 ? 175  LEU A N   1 
ATOM   539  C  CA  . LEU A 1 70  ? -4.623  9.157   -10.681 1.00 9.44  ? 175  LEU A CA  1 
ATOM   540  C  C   . LEU A 1 70  ? -5.766  8.483   -11.443 1.00 9.16  ? 175  LEU A C   1 
ATOM   541  O  O   . LEU A 1 70  ? -6.229  7.416   -11.083 1.00 10.48 ? 175  LEU A O   1 
ATOM   542  C  CB  . LEU A 1 70  ? -5.213  10.383  -9.843  1.00 10.14 ? 175  LEU A CB  1 
ATOM   543  C  CG  . LEU A 1 70  ? -6.429  10.010  -9.040  1.00 9.35  ? 175  LEU A CG  1 
ATOM   544  C  CD1 . LEU A 1 70  ? -6.053  9.224   -7.780  1.00 11.99 ? 175  LEU A CD1 1 
ATOM   545  C  CD2 . LEU A 1 70  ? -7.163  11.285  -8.580  1.00 11.53 ? 175  LEU A CD2 1 
ATOM   546  N  N   . LEU A 1 71  ? -6.250  9.203   -12.527 1.00 9.15  ? 176  LEU A N   1 
ATOM   547  C  CA  . LEU A 1 71  ? -7.409  8.630   -13.249 1.00 9.15  ? 176  LEU A CA  1 
ATOM   548  C  C   . LEU A 1 71  ? -6.987  7.386   -14.086 1.00 9.53  ? 176  LEU A C   1 
ATOM   549  O  O   . LEU A 1 71  ? -7.737  6.422   -14.139 1.00 9.96  ? 176  LEU A O   1 
ATOM   550  C  CB  . LEU A 1 71  ? -8.026  9.729   -14.164 1.00 9.17  ? 176  LEU A CB  1 
ATOM   551  C  CG  . LEU A 1 71  ? -8.513  10.992  -13.355 1.00 9.35  ? 176  LEU A CG  1 
ATOM   552  C  CD1 . LEU A 1 71  ? -8.962  12.041  -14.411 1.00 10.30 ? 176  LEU A CD1 1 
ATOM   553  C  CD2 . LEU A 1 71  ? -9.712  10.655  -12.463 1.00 11.14 ? 176  LEU A CD2 1 
ATOM   554  N  N   . ASN A 1 72  ? -5.800  7.468   -14.687 1.00 9.90  ? 177  ASN A N   1 
ATOM   555  C  CA  . ASN A 1 72  ? -5.367  6.319   -15.478 1.00 9.71  ? 177  ASN A CA  1 
ATOM   556  C  C   . ASN A 1 72  ? -5.313  5.052   -14.615 1.00 10.36 ? 177  ASN A C   1 
ATOM   557  O  O   . ASN A 1 72  ? -5.629  3.959   -15.129 1.00 11.00 ? 177  ASN A O   1 
ATOM   558  C  CB  . ASN A 1 72  ? -3.992  6.630   -16.060 1.00 10.08 ? 177  ASN A CB  1 
ATOM   559  C  CG  . ASN A 1 72  ? -3.349  5.379   -16.652 1.00 10.52 ? 177  ASN A CG  1 
ATOM   560  O  OD1 . ASN A 1 72  ? -2.686  4.640   -15.893 1.00 13.37 ? 177  ASN A OD1 1 
ATOM   561  N  ND2 . ASN A 1 72  ? -3.497  5.134   -17.884 1.00 11.13 ? 177  ASN A ND2 1 
ATOM   562  N  N   . GLU A 1 73  ? -4.963  5.162   -13.319 1.00 10.07 ? 178  GLU A N   1 
ATOM   563  C  CA  . GLU A 1 73  ? -4.756  4.027   -12.470 1.00 10.30 ? 178  GLU A CA  1 
ATOM   564  C  C   . GLU A 1 73  ? -5.991  3.699   -11.700 1.00 11.30 ? 178  GLU A C   1 
ATOM   565  O  O   . GLU A 1 73  ? -6.097  2.524   -11.188 1.00 12.39 ? 178  GLU A O   1 
ATOM   566  C  CB  . GLU A 1 73  ? -3.558  4.243   -11.578 1.00 13.29 ? 178  GLU A CB  1 
ATOM   567  C  CG  . GLU A 1 73  ? -2.266  4.221   -12.423 1.00 14.17 ? 178  GLU A CG  1 
ATOM   568  C  CD  . GLU A 1 73  ? -1.019  4.584   -11.671 1.00 15.73 ? 178  GLU A CD  1 
ATOM   569  O  OE1 . GLU A 1 73  ? -1.052  4.964   -10.442 1.00 16.18 ? 178  GLU A OE1 1 
ATOM   570  O  OE2 . GLU A 1 73  ? 0.077   4.461   -12.297 1.00 19.51 ? 178  GLU A OE2 1 
ATOM   571  N  N   . ASN A 1 74  ? -6.945  4.619   -11.497 1.00 10.98 ? 179  ASN A N   1 
ATOM   572  C  CA  . ASN A 1 74  ? -8.003  4.430   -10.514 1.00 10.84 ? 179  ASN A CA  1 
ATOM   573  C  C   . ASN A 1 74  ? -9.395  4.868   -10.923 1.00 9.70  ? 179  ASN A C   1 
ATOM   574  O  O   . ASN A 1 74  ? -10.320 4.815   -10.115 1.00 10.63 ? 179  ASN A O   1 
ATOM   575  C  CB  . ASN A 1 74  ? -7.695  5.212   -9.164  1.00 10.96 ? 179  ASN A CB  1 
ATOM   576  C  CG  . ASN A 1 74  ? -6.305  4.895   -8.632  1.00 10.37 ? 179  ASN A CG  1 
ATOM   577  O  OD1 . ASN A 1 74  ? -6.191  3.858   -7.866  1.00 11.13 ? 179  ASN A OD1 1 
ATOM   578  N  ND2 . ASN A 1 74  ? -5.315  5.677   -8.929  1.00 10.71 ? 179  ASN A ND2 1 
ATOM   579  N  N   . TYR A 1 75  ? -9.568  5.213   -12.218 1.00 10.07 ? 180  TYR A N   1 
ATOM   580  C  CA  . TYR A 1 75  ? -10.894 5.709   -12.668 1.00 10.41 ? 180  TYR A CA  1 
ATOM   581  C  C   . TYR A 1 75  ? -11.781 4.610   -13.154 1.00 10.19 ? 180  TYR A C   1 
ATOM   582  O  O   . TYR A 1 75  ? -11.562 3.384   -12.796 1.00 11.74 ? 180  TYR A O   1 
ATOM   583  C  CB  . TYR A 1 75  ? -10.729 6.866   -13.645 1.00 11.00 ? 180  TYR A CB  1 
ATOM   584  C  CG  . TYR A 1 75  ? -11.933 7.792   -13.745 1.00 9.50  ? 180  TYR A CG  1 
ATOM   585  C  CD1 . TYR A 1 75  ? -12.608 8.278   -12.606 1.00 9.76  ? 180  TYR A CD1 1 
ATOM   586  C  CD2 . TYR A 1 75  ? -12.401 8.159   -15.015 1.00 10.48 ? 180  TYR A CD2 1 
ATOM   587  C  CE1 . TYR A 1 75  ? -13.744 9.164   -12.744 1.00 9.26  ? 180  TYR A CE1 1 
ATOM   588  C  CE2 . TYR A 1 75  ? -13.525 9.004   -15.168 1.00 9.95  ? 180  TYR A CE2 1 
ATOM   589  C  CZ  . TYR A 1 75  ? -14.182 9.452   -14.027 1.00 9.07  ? 180  TYR A CZ  1 
ATOM   590  O  OH  . TYR A 1 75  ? -15.321 10.268  -14.115 1.00 9.61  ? 180  TYR A OH  1 
ATOM   591  N  N   . VAL A 1 76  ? -12.836 4.880   -13.896 1.00 9.94  ? 181  VAL A N   1 
ATOM   592  C  CA  . VAL A 1 76  ? -13.933 3.925   -14.202 1.00 10.70 ? 181  VAL A CA  1 
ATOM   593  C  C   . VAL A 1 76  ? -13.434 2.758   -15.064 1.00 10.49 ? 181  VAL A C   1 
ATOM   594  O  O   . VAL A 1 76  ? -12.691 2.917   -16.048 1.00 11.20 ? 181  VAL A O   1 
ATOM   595  C  CB  . VAL A 1 76  ? -15.054 4.635   -14.977 1.00 11.48 ? 181  VAL A CB  1 
ATOM   596  C  CG1 . VAL A 1 76  ? -16.230 3.692   -15.345 1.00 13.49 ? 181  VAL A CG1 1 
ATOM   597  C  CG2 . VAL A 1 76  ? -15.590 5.918   -14.226 1.00 12.99 ? 181  VAL A CG2 1 
ATOM   598  N  N   . GLU A 1 77  ? -13.852 1.565   -14.570 1.00 11.17 ? 182  GLU A N   1 
ATOM   599  C  CA  . GLU A 1 77  ? -13.668 0.290   -15.326 1.00 11.66 ? 182  GLU A CA  1 
ATOM   600  C  C   . GLU A 1 77  ? -15.007 -0.174  -15.803 1.00 11.39 ? 182  GLU A C   1 
ATOM   601  O  O   . GLU A 1 77  ? -16.077 0.164   -15.298 1.00 13.12 ? 182  GLU A O   1 
ATOM   602  C  CB  . GLU A 1 77  ? -13.046 -0.781  -14.367 1.00 11.92 ? 182  GLU A CB  1 
ATOM   603  C  CG  . GLU A 1 77  ? -11.644 -0.339  -13.949 1.00 11.62 ? 182  GLU A CG  1 
ATOM   604  C  CD  . GLU A 1 77  ? -10.968 -1.249  -12.919 1.00 13.49 ? 182  GLU A CD  1 
ATOM   605  O  OE1 . GLU A 1 77  ? -9.855  -0.914  -12.438 1.00 14.40 ? 182  GLU A OE1 1 
ATOM   606  O  OE2 . GLU A 1 77  ? -11.566 -2.338  -12.649 1.00 15.18 ? 182  GLU A OE2 1 
ATOM   607  N  N   . ASP A 1 78  ? -15.025 -1.019  -16.854 1.00 12.07 ? 183  ASP A N   1 
ATOM   608  C  CA  . ASP A 1 78  ? -16.284 -1.655  -17.272 1.00 13.63 ? 183  ASP A CA  1 
ATOM   609  C  C   . ASP A 1 78  ? -16.724 -2.696  -16.229 1.00 14.37 ? 183  ASP A C   1 
ATOM   610  O  O   . ASP A 1 78  ? -15.999 -3.003  -15.276 1.00 15.02 ? 183  ASP A O   1 
ATOM   611  C  CB  . ASP A 1 78  ? -16.096 -2.446  -18.602 1.00 15.08 ? 183  ASP A CB  1 
ATOM   612  C  CG  . ASP A 1 78  ? -15.105 -3.638  -18.391 1.00 16.09 ? 183  ASP A CG  1 
ATOM   613  O  OD1 . ASP A 1 78  ? -13.962 -3.510  -17.911 1.00 14.37 ? 183  ASP A OD1 1 
ATOM   614  O  OD2 . ASP A 1 78  ? -15.596 -4.806  -18.701 1.00 21.01 ? 183  ASP A OD2 1 
ATOM   615  N  N   . ASP A 1 79  ? -17.926 -3.232  -16.448 1.00 16.60 ? 184  ASP A N   1 
ATOM   616  C  CA  . ASP A 1 79  ? -18.512 -4.117  -15.450 1.00 18.86 ? 184  ASP A CA  1 
ATOM   617  C  C   . ASP A 1 79  ? -17.789 -5.466  -15.315 1.00 21.88 ? 184  ASP A C   1 
ATOM   618  O  O   . ASP A 1 79  ? -18.074 -6.196  -14.329 1.00 23.49 ? 184  ASP A O   1 
ATOM   619  C  CB  . ASP A 1 79  ? -19.984 -4.389  -15.768 1.00 23.94 ? 184  ASP A CB  1 
ATOM   620  C  CG  . ASP A 1 79  ? -20.912 -3.212  -15.462 1.00 34.09 ? 184  ASP A CG  1 
ATOM   621  O  OD1 . ASP A 1 79  ? -20.467 -2.223  -14.796 1.00 35.54 ? 184  ASP A OD1 1 
ATOM   622  O  OD2 . ASP A 1 79  ? -22.083 -3.272  -15.951 1.00 37.19 ? 184  ASP A OD2 1 
ATOM   623  N  N   . ASP A 1 80  ? -16.950 -5.848  -16.259 1.00 17.53 ? 185  ASP A N   1 
ATOM   624  C  CA  . ASP A 1 80  ? -16.035 -7.024  -16.093 1.00 18.67 ? 185  ASP A CA  1 
ATOM   625  C  C   . ASP A 1 80  ? -14.619 -6.775  -15.652 1.00 18.47 ? 185  ASP A C   1 
ATOM   626  O  O   . ASP A 1 80  ? -13.749 -7.706  -15.582 1.00 18.84 ? 185  ASP A O   1 
ATOM   627  C  CB  . ASP A 1 80  ? -15.990 -7.803  -17.408 1.00 21.19 ? 185  ASP A CB  1 
ATOM   628  C  CG  . ASP A 1 80  ? -17.209 -8.626  -17.651 1.00 29.71 ? 185  ASP A CG  1 
ATOM   629  O  OD1 . ASP A 1 80  ? -17.734 -9.255  -16.719 1.00 38.67 ? 185  ASP A OD1 1 
ATOM   630  O  OD2 . ASP A 1 80  ? -17.589 -8.683  -18.812 1.00 40.38 ? 185  ASP A OD2 1 
ATOM   631  N  N   . ASN A 1 81  ? -14.304 -5.543  -15.248 1.00 16.24 ? 186  ASN A N   1 
ATOM   632  C  CA  . ASN A 1 81  ? -12.977 -5.228  -14.797 1.00 13.46 ? 186  ASN A CA  1 
ATOM   633  C  C   . ASN A 1 81  ? -11.885 -5.636  -15.771 1.00 15.78 ? 186  ASN A C   1 
ATOM   634  O  O   . ASN A 1 81  ? -10.784 -6.158  -15.392 1.00 16.61 ? 186  ASN A O   1 
ATOM   635  C  CB  . ASN A 1 81  ? -12.638 -5.795  -13.350 1.00 16.14 ? 186  ASN A CB  1 
ATOM   636  C  CG  . ASN A 1 81  ? -13.670 -5.441  -12.354 1.00 18.60 ? 186  ASN A CG  1 
ATOM   637  O  OD1 . ASN A 1 81  ? -14.509 -6.304  -11.948 1.00 22.96 ? 186  ASN A OD1 1 
ATOM   638  N  ND2 . ASN A 1 81  ? -13.740 -4.133  -11.988 1.00 17.71 ? 186  ASN A ND2 1 
ATOM   639  N  N   . MET A 1 82  ? -12.108 -5.281  -17.048 1.00 13.56 ? 187  MET A N   1 
ATOM   640  C  CA  . MET A 1 82  ? -11.129 -5.587  -18.108 1.00 13.96 ? 187  MET A CA  1 
ATOM   641  C  C   . MET A 1 82  ? -10.542 -4.324  -18.787 1.00 12.18 ? 187  MET A C   1 
ATOM   642  O  O   . MET A 1 82  ? -9.428  -4.372  -19.360 1.00 12.34 ? 187  MET A O   1 
ATOM   643  C  CB  . MET A 1 82  ? -11.785 -6.373  -19.180 1.00 16.83 ? 187  MET A CB  1 
ATOM   644  C  CG  . MET A 1 82  ? -12.127 -7.790  -18.646 1.00 18.50 ? 187  MET A CG  1 
ATOM   645  S  SD  . MET A 1 82  ? -12.981 -8.802  -19.836 1.00 24.05 ? 187  MET A SD  1 
ATOM   646  C  CE  . MET A 1 82  ? -11.788 -9.004  -21.136 1.00 26.49 ? 187  MET A CE  1 
ATOM   647  N  N   . PHE A 1 83  ? -11.308 -3.206  -18.715 1.00 11.27 ? 188  PHE A N   1 
ATOM   648  C  CA  . PHE A 1 83  ? -10.895 -1.934  -19.440 1.00 10.44 ? 188  PHE A CA  1 
ATOM   649  C  C   . PHE A 1 83  ? -11.121 -0.803  -18.440 1.00 10.18 ? 188  PHE A C   1 
ATOM   650  O  O   . PHE A 1 83  ? -12.111 -0.807  -17.709 1.00 12.40 ? 188  PHE A O   1 
ATOM   651  C  CB  . PHE A 1 83  ? -11.871 -1.741  -20.709 1.00 11.96 ? 188  PHE A CB  1 
ATOM   652  C  CG  . PHE A 1 83  ? -11.845 -2.935  -21.629 1.00 12.93 ? 188  PHE A CG  1 
ATOM   653  C  CD1 . PHE A 1 83  ? -10.755 -3.144  -22.468 1.00 14.80 ? 188  PHE A CD1 1 
ATOM   654  C  CD2 . PHE A 1 83  ? -12.911 -3.828  -21.567 1.00 16.87 ? 188  PHE A CD2 1 
ATOM   655  C  CE1 . PHE A 1 83  ? -10.708 -4.320  -23.337 1.00 16.00 ? 188  PHE A CE1 1 
ATOM   656  C  CE2 . PHE A 1 83  ? -12.865 -5.000  -22.449 1.00 18.05 ? 188  PHE A CE2 1 
ATOM   657  C  CZ  . PHE A 1 83  ? -11.731 -5.214  -23.213 1.00 17.34 ? 188  PHE A CZ  1 
ATOM   658  N  N   . ARG A 1 84  ? -10.198 0.164   -18.517 1.00 10.51 ? 189  ARG A N   1 
ATOM   659  C  CA  . ARG A 1 84  ? -10.250 1.341   -17.597 1.00 10.64 ? 189  ARG A CA  1 
ATOM   660  C  C   . ARG A 1 84  ? -10.062 2.608   -18.478 1.00 11.41 ? 189  ARG A C   1 
ATOM   661  O  O   . ARG A 1 84  ? -9.139  2.656   -19.288 1.00 10.81 ? 189  ARG A O   1 
ATOM   662  C  CB  . ARG A 1 84  ? -9.152  1.265   -16.553 1.00 11.07 ? 189  ARG A CB  1 
ATOM   663  C  CG  . ARG A 1 84  ? -9.370  2.376   -15.465 1.00 11.21 ? 189  ARG A CG  1 
ATOM   664  C  CD  . ARG A 1 84  ? -8.613  1.993   -14.133 1.00 14.24 ? 189  ARG A CD  1 
ATOM   665  N  NE  . ARG A 1 84  ? -7.194  1.653   -14.357 1.00 15.50 ? 189  ARG A NE  1 
ATOM   666  C  CZ  . ARG A 1 84  ? -6.605  0.486   -14.039 1.00 15.38 ? 189  ARG A CZ  1 
ATOM   667  N  NH1 . ARG A 1 84  ? -5.309  0.442   -14.306 1.00 16.67 ? 189  ARG A NH1 1 
ATOM   668  N  NH2 . ARG A 1 84  ? -7.298  -0.517  -13.463 1.00 15.94 ? 189  ARG A NH2 1 
ATOM   669  N  N   . PHE A 1 85  ? -10.914 3.631   -18.272 1.00 10.70 ? 190  PHE A N   1 
ATOM   670  C  CA  . PHE A 1 85  ? -10.715 4.815   -19.139 1.00 10.47 ? 190  PHE A CA  1 
ATOM   671  C  C   . PHE A 1 85  ? -9.326  5.378   -18.941 1.00 9.44  ? 190  PHE A C   1 
ATOM   672  O  O   . PHE A 1 85  ? -8.747  5.376   -17.826 1.00 9.75  ? 190  PHE A O   1 
ATOM   673  C  CB  . PHE A 1 85  ? -11.735 5.930   -18.774 1.00 10.22 ? 190  PHE A CB  1 
ATOM   674  C  CG  . PHE A 1 85  ? -13.146 5.654   -19.167 1.00 9.93  ? 190  PHE A CG  1 
ATOM   675  C  CD1 . PHE A 1 85  ? -14.205 6.079   -18.341 1.00 10.73 ? 190  PHE A CD1 1 
ATOM   676  C  CD2 . PHE A 1 85  ? -13.479 5.032   -20.404 1.00 11.52 ? 190  PHE A CD2 1 
ATOM   677  C  CE1 . PHE A 1 85  ? -15.541 5.864   -18.661 1.00 12.42 ? 190  PHE A CE1 1 
ATOM   678  C  CE2 . PHE A 1 85  ? -14.799 4.864   -20.710 1.00 11.88 ? 190  PHE A CE2 1 
ATOM   679  C  CZ  . PHE A 1 85  ? -15.867 5.239   -19.882 1.00 12.67 ? 190  PHE A CZ  1 
ATOM   680  N  N   . ASP A 1 86  ? -8.791  5.942   -20.045 1.00 9.42  ? 191  ASP A N   1 
ATOM   681  C  CA  . ASP A 1 86  ? -7.520  6.531   -20.078 1.00 8.79  ? 191  ASP A CA  1 
ATOM   682  C  C   . ASP A 1 86  ? -7.552  7.948   -20.744 1.00 10.54 ? 191  ASP A C   1 
ATOM   683  O  O   . ASP A 1 86  ? -6.978  8.216   -21.815 1.00 9.87  ? 191  ASP A O   1 
ATOM   684  C  CB  . ASP A 1 86  ? -6.540  5.601   -20.933 1.00 10.15 ? 191  ASP A CB  1 
ATOM   685  C  CG  . ASP A 1 86  ? -5.141  6.082   -20.903 1.00 10.27 ? 191  ASP A CG  1 
ATOM   686  O  OD1 . ASP A 1 86  ? -4.647  6.769   -19.953 1.00 11.85 ? 191  ASP A OD1 1 
ATOM   687  O  OD2 . ASP A 1 86  ? -4.398  5.803   -21.940 1.00 12.37 ? 191  ASP A OD2 1 
ATOM   688  N  N   . TYR A 1 87  ? -8.249  8.870   -20.030 1.00 9.29  ? 192  TYR A N   1 
ATOM   689  C  CA  . TYR A 1 87  ? -8.382  10.263  -20.554 1.00 8.91  ? 192  TYR A CA  1 
ATOM   690  C  C   . TYR A 1 87  ? -6.986  10.871  -20.665 1.00 8.06  ? 192  TYR A C   1 
ATOM   691  O  O   . TYR A 1 87  ? -6.185  10.847  -19.726 1.00 10.15 ? 192  TYR A O   1 
ATOM   692  C  CB  . TYR A 1 87  ? -9.125  11.073  -19.504 1.00 9.44  ? 192  TYR A CB  1 
ATOM   693  C  CG  . TYR A 1 87  ? -10.613 10.769  -19.399 1.00 7.93  ? 192  TYR A CG  1 
ATOM   694  C  CD1 . TYR A 1 87  ? -11.139 9.786   -18.518 1.00 8.74  ? 192  TYR A CD1 1 
ATOM   695  C  CD2 . TYR A 1 87  ? -11.580 11.497  -20.191 1.00 9.55  ? 192  TYR A CD2 1 
ATOM   696  C  CE1 . TYR A 1 87  ? -12.482 9.489   -18.449 1.00 9.60  ? 192  TYR A CE1 1 
ATOM   697  C  CE2 . TYR A 1 87  ? -12.912 11.202  -20.078 1.00 8.73  ? 192  TYR A CE2 1 
ATOM   698  C  CZ  . TYR A 1 87  ? -13.387 10.216  -19.195 1.00 8.77  ? 192  TYR A CZ  1 
ATOM   699  O  OH  . TYR A 1 87  ? -14.711 9.911   -18.971 1.00 9.83  ? 192  TYR A OH  1 
ATOM   700  N  N   . SER A 1 88  ? -6.723  11.520  -21.827 1.00 8.98  ? 193  SER A N   1 
ATOM   701  C  CA  . SER A 1 88  ? -5.388  12.117  -21.983 1.00 8.23  ? 193  SER A CA  1 
ATOM   702  C  C   . SER A 1 88  ? -5.292  13.441  -21.182 1.00 9.25  ? 193  SER A C   1 
ATOM   703  O  O   . SER A 1 88  ? -6.323  14.086  -20.892 1.00 9.21  ? 193  SER A O   1 
ATOM   704  C  CB  . SER A 1 88  ? -5.059  12.404  -23.441 1.00 9.87  ? 193  SER A CB  1 
ATOM   705  O  OG  . SER A 1 88  ? -5.883  13.499  -23.922 1.00 10.72 ? 193  SER A OG  1 
ATOM   706  N  N   . PRO A 1 89  ? -4.090  13.928  -20.907 1.00 8.84  ? 194  PRO A N   1 
ATOM   707  C  CA  . PRO A 1 89  ? -3.983  15.209  -20.292 1.00 10.38 ? 194  PRO A CA  1 
ATOM   708  C  C   . PRO A 1 89  ? -4.665  16.343  -21.077 1.00 9.41  ? 194  PRO A C   1 
ATOM   709  O  O   . PRO A 1 89  ? -5.397  17.179  -20.445 1.00 9.21  ? 194  PRO A O   1 
ATOM   710  C  CB  . PRO A 1 89  ? -2.457  15.482  -20.238 1.00 10.59 ? 194  PRO A CB  1 
ATOM   711  C  CG  . PRO A 1 89  ? -1.864  14.056  -20.140 1.00 10.09 ? 194  PRO A CG  1 
ATOM   712  C  CD  . PRO A 1 89  ? -2.762  13.278  -21.116 1.00 10.37 ? 194  PRO A CD  1 
ATOM   713  N  N   A GLU A 1 90  ? -4.508  16.401  -22.379 0.50 9.62  ? 195  GLU A N   1 
ATOM   714  N  N   B GLU A 1 90  ? -4.542  16.381  -22.367 0.50 9.49  ? 195  GLU A N   1 
ATOM   715  C  CA  A GLU A 1 90  ? -5.137  17.481  -23.161 0.50 9.44  ? 195  GLU A CA  1 
ATOM   716  C  CA  B GLU A 1 90  ? -5.128  17.474  -23.126 0.50 9.29  ? 195  GLU A CA  1 
ATOM   717  C  C   A GLU A 1 90  ? -6.643  17.289  -23.222 0.50 9.34  ? 195  GLU A C   1 
ATOM   718  C  C   B GLU A 1 90  ? -6.638  17.287  -23.195 0.50 9.22  ? 195  GLU A C   1 
ATOM   719  O  O   A GLU A 1 90  ? -7.399  18.313  -23.267 0.50 10.13 ? 195  GLU A O   1 
ATOM   720  O  O   B GLU A 1 90  ? -7.390  18.306  -23.194 0.50 9.85  ? 195  GLU A O   1 
ATOM   721  C  CB  A GLU A 1 90  ? -4.603  17.637  -24.605 0.50 10.92 ? 195  GLU A CB  1 
ATOM   722  C  CB  B GLU A 1 90  ? -4.544  17.518  -24.527 0.50 10.82 ? 195  GLU A CB  1 
ATOM   723  C  CG  A GLU A 1 90  ? -4.563  16.405  -25.519 0.50 14.93 ? 195  GLU A CG  1 
ATOM   724  C  CG  B GLU A 1 90  ? -3.014  17.776  -24.489 0.50 13.97 ? 195  GLU A CG  1 
ATOM   725  C  CD  A GLU A 1 90  ? -3.998  16.638  -26.967 0.50 16.83 ? 195  GLU A CD  1 
ATOM   726  C  CD  B GLU A 1 90  ? -2.176  16.480  -24.247 0.50 16.74 ? 195  GLU A CD  1 
ATOM   727  O  OE1 A GLU A 1 90  ? -3.665  17.775  -27.382 0.50 21.50 ? 195  GLU A OE1 1 
ATOM   728  O  OE1 B GLU A 1 90  ? -2.643  15.305  -24.294 0.50 15.85 ? 195  GLU A OE1 1 
ATOM   729  O  OE2 A GLU A 1 90  ? -3.975  15.687  -27.720 0.50 13.70 ? 195  GLU A OE2 1 
ATOM   730  O  OE2 B GLU A 1 90  ? -0.973  16.702  -23.944 0.50 24.48 ? 195  GLU A OE2 1 
ATOM   731  N  N   . PHE A 1 91  ? -7.159  16.041  -23.187 1.00 9.01  ? 196  PHE A N   1 
ATOM   732  C  CA  . PHE A 1 91  ? -8.569  15.851  -23.076 1.00 8.75  ? 196  PHE A CA  1 
ATOM   733  C  C   . PHE A 1 91  ? -9.064  16.388  -21.761 1.00 8.32  ? 196  PHE A C   1 
ATOM   734  O  O   . PHE A 1 91  ? -10.144 17.040  -21.675 1.00 8.99  ? 196  PHE A O   1 
ATOM   735  C  CB  . PHE A 1 91  ? -8.954  14.337  -23.221 1.00 9.14  ? 196  PHE A CB  1 
ATOM   736  C  CG  . PHE A 1 91  ? -10.430 14.047  -23.300 1.00 7.98  ? 196  PHE A CG  1 
ATOM   737  C  CD1 . PHE A 1 91  ? -10.989 13.502  -24.471 1.00 9.50  ? 196  PHE A CD1 1 
ATOM   738  C  CD2 . PHE A 1 91  ? -11.305 14.227  -22.219 1.00 9.03  ? 196  PHE A CD2 1 
ATOM   739  C  CE1 . PHE A 1 91  ? -12.315 13.163  -24.559 1.00 9.41  ? 196  PHE A CE1 1 
ATOM   740  C  CE2 . PHE A 1 91  ? -12.654 13.942  -22.312 1.00 8.42  ? 196  PHE A CE2 1 
ATOM   741  C  CZ  . PHE A 1 91  ? -13.160 13.374  -23.469 1.00 8.95  ? 196  PHE A CZ  1 
ATOM   742  N  N   . LEU A 1 92  ? -8.363  16.093  -20.662 1.00 8.66  ? 197  LEU A N   1 
ATOM   743  C  CA  . LEU A 1 92  ? -8.790  16.607  -19.327 1.00 8.53  ? 197  LEU A CA  1 
ATOM   744  C  C   . LEU A 1 92  ? -8.866  18.148  -19.341 1.00 8.50  ? 197  LEU A C   1 
ATOM   745  O  O   . LEU A 1 92  ? -9.818  18.691  -18.749 1.00 9.11  ? 197  LEU A O   1 
ATOM   746  C  CB  . LEU A 1 92  ? -7.828  16.085  -18.244 1.00 8.65  ? 197  LEU A CB  1 
ATOM   747  C  CG  . LEU A 1 92  ? -7.988  14.541  -17.993 1.00 8.86  ? 197  LEU A CG  1 
ATOM   748  C  CD1 . LEU A 1 92  ? -6.850  14.106  -17.108 1.00 11.11 ? 197  LEU A CD1 1 
ATOM   749  C  CD2 . LEU A 1 92  ? -9.309  14.168  -17.386 1.00 10.52 ? 197  LEU A CD2 1 
ATOM   750  N  N   . LEU A 1 93  ? -7.935  18.812  -19.996 1.00 8.55  ? 198  LEU A N   1 
ATOM   751  C  CA  . LEU A 1 93  ? -8.044  20.282  -20.073 1.00 9.49  ? 198  LEU A CA  1 
ATOM   752  C  C   . LEU A 1 93  ? -9.250  20.669  -20.859 1.00 9.75  ? 198  LEU A C   1 
ATOM   753  O  O   . LEU A 1 93  ? -9.927  21.706  -20.455 1.00 10.38 ? 198  LEU A O   1 
ATOM   754  C  CB  . LEU A 1 93  ? -6.827  20.892  -20.772 1.00 12.46 ? 198  LEU A CB  1 
ATOM   755  C  CG  . LEU A 1 93  ? -5.614  20.898  -19.939 1.00 13.27 ? 198  LEU A CG  1 
ATOM   756  C  CD1 . LEU A 1 93  ? -4.432  21.317  -20.841 1.00 16.09 ? 198  LEU A CD1 1 
ATOM   757  C  CD2 . LEU A 1 93  ? -5.690  21.927  -18.767 1.00 17.13 ? 198  LEU A CD2 1 
ATOM   758  N  N   . TRP A 1 94  ? -9.614  19.995  -21.945 1.00 8.67  ? 199  TRP A N   1 
ATOM   759  C  CA  . TRP A 1 94  ? -10.866 20.318  -22.663 1.00 8.70  ? 199  TRP A CA  1 
ATOM   760  C  C   . TRP A 1 94  ? -12.082 20.097  -21.781 1.00 9.57  ? 199  TRP A C   1 
ATOM   761  O  O   . TRP A 1 94  ? -13.007 20.959  -21.735 1.00 10.26 ? 199  TRP A O   1 
ATOM   762  C  CB  . TRP A 1 94  ? -10.937 19.351  -23.925 1.00 9.56  ? 199  TRP A CB  1 
ATOM   763  C  CG  . TRP A 1 94  ? -12.176 19.459  -24.741 1.00 8.73  ? 199  TRP A CG  1 
ATOM   764  C  CD1 . TRP A 1 94  ? -12.591 20.644  -25.492 1.00 8.86  ? 199  TRP A CD1 1 
ATOM   765  C  CD2 . TRP A 1 94  ? -13.152 18.447  -25.017 1.00 8.33  ? 199  TRP A CD2 1 
ATOM   766  N  NE1 . TRP A 1 94  ? -13.708 20.295  -26.176 1.00 8.55  ? 199  TRP A NE1 1 
ATOM   767  C  CE2 . TRP A 1 94  ? -14.084 18.978  -25.959 1.00 8.22  ? 199  TRP A CE2 1 
ATOM   768  C  CE3 . TRP A 1 94  ? -13.279 17.067  -24.622 1.00 9.81  ? 199  TRP A CE3 1 
ATOM   769  C  CZ2 . TRP A 1 94  ? -15.189 18.276  -26.407 1.00 8.44  ? 199  TRP A CZ2 1 
ATOM   770  C  CZ3 . TRP A 1 94  ? -14.296 16.332  -25.092 1.00 9.97  ? 199  TRP A CZ3 1 
ATOM   771  C  CH2 . TRP A 1 94  ? -15.306 16.940  -25.974 1.00 9.41  ? 199  TRP A CH2 1 
ATOM   772  N  N   . ALA A 1 95  ? -12.146 19.031  -21.003 1.00 8.38  ? 200  ALA A N   1 
ATOM   773  C  CA  . ALA A 1 95  ? -13.360 18.726  -20.240 1.00 8.70  ? 200  ALA A CA  1 
ATOM   774  C  C   . ALA A 1 95  ? -13.443 19.612  -18.964 1.00 8.24  ? 200  ALA A C   1 
ATOM   775  O  O   . ALA A 1 95  ? -14.548 19.846  -18.476 1.00 10.05 ? 200  ALA A O   1 
ATOM   776  C  CB  . ALA A 1 95  ? -13.287 17.234  -19.805 1.00 9.10  ? 200  ALA A CB  1 
ATOM   777  N  N   . LEU A 1 96  ? -12.301 20.043  -18.418 1.00 8.30  ? 201  LEU A N   1 
ATOM   778  C  CA  . LEU A 1 96  ? -12.243 20.680  -17.094 1.00 8.72  ? 201  LEU A CA  1 
ATOM   779  C  C   . LEU A 1 96  ? -12.062 22.177  -17.151 1.00 8.98  ? 201  LEU A C   1 
ATOM   780  O  O   . LEU A 1 96  ? -12.345 22.869  -16.129 1.00 9.43  ? 201  LEU A O   1 
ATOM   781  C  CB  . LEU A 1 96  ? -11.213 19.982  -16.246 1.00 9.61  ? 201  LEU A CB  1 
ATOM   782  C  CG  . LEU A 1 96  ? -11.608 18.544  -15.820 1.00 9.31  ? 201  LEU A CG  1 
ATOM   783  C  CD1 . LEU A 1 96  ? -10.347 17.834  -15.250 1.00 10.22 ? 201  LEU A CD1 1 
ATOM   784  C  CD2 . LEU A 1 96  ? -12.702 18.560  -14.777 1.00 11.52 ? 201  LEU A CD2 1 
ATOM   785  N  N   . ARG A 1 97  ? -11.582 22.727  -18.294 1.00 9.73  ? 202  ARG A N   1 
ATOM   786  C  CA  . ARG A 1 97  ? -11.494 24.185  -18.433 1.00 9.07  ? 202  ARG A CA  1 
ATOM   787  C  C   . ARG A 1 97  ? -12.326 24.738  -19.568 1.00 9.33  ? 202  ARG A C   1 
ATOM   788  O  O   . ARG A 1 97  ? -11.788 25.519  -20.428 1.00 10.52 ? 202  ARG A O   1 
ATOM   789  C  CB  . ARG A 1 97  ? -10.024 24.618  -18.546 1.00 9.29  ? 202  ARG A CB  1 
ATOM   790  C  CG  . ARG A 1 97  ? -9.211  24.526  -17.216 1.00 11.34 ? 202  ARG A CG  1 
ATOM   791  C  CD  . ARG A 1 97  ? -7.805  25.178  -17.406 1.00 13.28 ? 202  ARG A CD  1 
ATOM   792  N  NE  . ARG A 1 97  ? -7.147  25.360  -16.080 1.00 13.89 ? 202  ARG A NE  1 
ATOM   793  C  CZ  . ARG A 1 97  ? -6.065  26.125  -15.967 1.00 13.62 ? 202  ARG A CZ  1 
ATOM   794  N  NH1 . ARG A 1 97  ? -5.536  26.682  -17.051 1.00 17.03 ? 202  ARG A NH1 1 
ATOM   795  N  NH2 . ARG A 1 97  ? -5.577  26.383  -14.801 1.00 17.44 ? 202  ARG A NH2 1 
ATOM   796  N  N   . PRO A 1 98  ? -13.637 24.440  -19.621 1.00 8.54  ? 203  PRO A N   1 
ATOM   797  C  CA  . PRO A 1 98  ? -14.539 25.105  -20.560 1.00 9.25  ? 203  PRO A CA  1 
ATOM   798  C  C   . PRO A 1 98  ? -14.819 26.523  -20.048 1.00 10.46 ? 203  PRO A C   1 
ATOM   799  O  O   . PRO A 1 98  ? -14.432 26.919  -18.932 1.00 9.64  ? 203  PRO A O   1 
ATOM   800  C  CB  . PRO A 1 98  ? -15.821 24.310  -20.433 1.00 9.88  ? 203  PRO A CB  1 
ATOM   801  C  CG  . PRO A 1 98  ? -15.790 23.873  -18.971 1.00 9.26  ? 203  PRO A CG  1 
ATOM   802  C  CD  . PRO A 1 98  ? -14.367 23.547  -18.691 1.00 10.30 ? 203  PRO A CD  1 
ATOM   803  N  N   . PRO A 1 99  ? -15.539 27.333  -20.837 1.00 9.56  ? 204  PRO A N   1 
ATOM   804  C  CA  . PRO A 1 99  ? -15.876 28.699  -20.379 1.00 10.43 ? 204  PRO A CA  1 
ATOM   805  C  C   . PRO A 1 99  ? -16.546 28.694  -19.034 1.00 9.92  ? 204  PRO A C   1 
ATOM   806  O  O   . PRO A 1 99  ? -17.459 27.940  -18.731 1.00 11.91 ? 204  PRO A O   1 
ATOM   807  C  CB  . PRO A 1 99  ? -16.859 29.176  -21.525 1.00 10.55 ? 204  PRO A CB  1 
ATOM   808  C  CG  . PRO A 1 99  ? -16.287 28.496  -22.749 1.00 10.75 ? 204  PRO A CG  1 
ATOM   809  C  CD  . PRO A 1 99  ? -15.966 27.050  -22.237 1.00 10.03 ? 204  PRO A CD  1 
ATOM   810  N  N   . GLY A 1 100 ? -16.003 29.584  -18.167 1.00 10.38 ? 205  GLY A N   1 
ATOM   811  C  CA  . GLY A 1 100 ? -16.561 29.761  -16.794 1.00 12.69 ? 205  GLY A CA  1 
ATOM   812  C  C   . GLY A 1 100 ? -15.952 28.777  -15.783 1.00 10.90 ? 205  GLY A C   1 
ATOM   813  O  O   . GLY A 1 100 ? -16.342 28.852  -14.579 1.00 10.85 ? 205  GLY A O   1 
ATOM   814  N  N   . TRP A 1 101 ? -14.958 27.942  -16.138 1.00 10.55 ? 206  TRP A N   1 
ATOM   815  C  CA  . TRP A 1 101 ? -14.343 27.101  -15.098 1.00 9.52  ? 206  TRP A CA  1 
ATOM   816  C  C   . TRP A 1 101 ? -13.764 27.943  -13.990 1.00 9.38  ? 206  TRP A C   1 
ATOM   817  O  O   . TRP A 1 101 ? -13.305 29.090  -14.202 1.00 9.98  ? 206  TRP A O   1 
ATOM   818  C  CB  . TRP A 1 101 ? -13.243 26.258  -15.776 1.00 9.86  ? 206  TRP A CB  1 
ATOM   819  C  CG  . TRP A 1 101 ? -11.995 26.993  -16.188 1.00 9.26  ? 206  TRP A CG  1 
ATOM   820  C  CD1 . TRP A 1 101 ? -11.765 27.564  -17.425 1.00 10.30 ? 206  TRP A CD1 1 
ATOM   821  C  CD2 . TRP A 1 101 ? -10.864 27.305  -15.381 1.00 9.95  ? 206  TRP A CD2 1 
ATOM   822  N  NE1 . TRP A 1 101 ? -10.525 28.204  -17.431 1.00 10.97 ? 206  TRP A NE1 1 
ATOM   823  C  CE2 . TRP A 1 101 ? -9.970  28.079  -16.192 1.00 10.29 ? 206  TRP A CE2 1 
ATOM   824  C  CE3 . TRP A 1 101 ? -10.453 26.942  -14.074 1.00 11.71 ? 206  TRP A CE3 1 
ATOM   825  C  CZ2 . TRP A 1 101 ? -8.712  28.527  -15.705 1.00 11.27 ? 206  TRP A CZ2 1 
ATOM   826  C  CZ3 . TRP A 1 101 ? -9.229  27.431  -13.593 1.00 12.65 ? 206  TRP A CZ3 1 
ATOM   827  C  CH2 . TRP A 1 101 ? -8.398  28.192  -14.401 1.00 11.95 ? 206  TRP A CH2 1 
ATOM   828  N  N   . LEU A 1 102 ? -13.772 27.356  -12.797 1.00 9.01  ? 207  LEU A N   1 
ATOM   829  C  CA  . LEU A 1 102 ? -13.239 28.013  -11.542 1.00 10.37 ? 207  LEU A CA  1 
ATOM   830  C  C   . LEU A 1 102 ? -12.223 27.170  -10.902 1.00 9.96  ? 207  LEU A C   1 
ATOM   831  O  O   . LEU A 1 102 ? -12.379 25.906  -10.809 1.00 9.58  ? 207  LEU A O   1 
ATOM   832  C  CB  . LEU A 1 102 ? -14.410 28.260  -10.545 1.00 10.16 ? 207  LEU A CB  1 
ATOM   833  C  CG  . LEU A 1 102 ? -15.464 29.227  -11.039 1.00 10.53 ? 207  LEU A CG  1 
ATOM   834  C  CD1 . LEU A 1 102 ? -16.546 29.417  -9.967  1.00 11.71 ? 207  LEU A CD1 1 
ATOM   835  C  CD2 . LEU A 1 102 ? -14.864 30.618  -11.413 1.00 13.35 ? 207  LEU A CD2 1 
ATOM   836  N  N   . PRO A 1 103 ? -11.112 27.748  -10.388 1.00 9.60  ? 208  PRO A N   1 
ATOM   837  C  CA  . PRO A 1 103 ? -10.068 26.910  -9.789  1.00 11.10 ? 208  PRO A CA  1 
ATOM   838  C  C   . PRO A 1 103 ? -10.481 26.136  -8.554  1.00 10.59 ? 208  PRO A C   1 
ATOM   839  O  O   . PRO A 1 103 ? -9.977  24.991  -8.362  1.00 10.95 ? 208  PRO A O   1 
ATOM   840  C  CB  . PRO A 1 103 ? -8.943  27.953  -9.451  1.00 12.23 ? 208  PRO A CB  1 
ATOM   841  C  CG  . PRO A 1 103 ? -9.672  29.245  -9.357  1.00 14.48 ? 208  PRO A CG  1 
ATOM   842  C  CD  . PRO A 1 103 ? -10.756 29.197  -10.442 1.00 11.93 ? 208  PRO A CD  1 
ATOM   843  N  N   . GLN A 1 104 ? -11.362 26.673  -7.748  1.00 9.65  ? 209  GLN A N   1 
ATOM   844  C  CA  A GLN A 1 104 ? -11.738 25.951  -6.531  0.50 9.87  ? 209  GLN A CA  1 
ATOM   845  C  CA  B GLN A 1 104 ? -11.751 25.939  -6.510  0.50 10.70 ? 209  GLN A CA  1 
ATOM   846  C  C   . GLN A 1 104 ? -12.613 24.729  -6.827  1.00 10.05 ? 209  GLN A C   1 
ATOM   847  O  O   . GLN A 1 104 ? -12.878 23.898  -5.949  1.00 10.94 ? 209  GLN A O   1 
ATOM   848  C  CB  A GLN A 1 104 ? -12.520 26.931  -5.630  0.50 11.10 ? 209  GLN A CB  1 
ATOM   849  C  CB  B GLN A 1 104 ? -12.606 26.838  -5.566  0.50 13.01 ? 209  GLN A CB  1 
ATOM   850  C  CG  A GLN A 1 104 ? -13.735 27.592  -6.256  0.50 10.62 ? 209  GLN A CG  1 
ATOM   851  C  CG  B GLN A 1 104 ? -11.833 27.665  -4.526  0.50 15.81 ? 209  GLN A CG  1 
ATOM   852  C  CD  A GLN A 1 104 ? -13.568 28.943  -6.890  0.50 10.54 ? 209  GLN A CD  1 
ATOM   853  C  CD  B GLN A 1 104 ? -11.308 26.798  -3.327  0.50 16.56 ? 209  GLN A CD  1 
ATOM   854  O  OE1 A GLN A 1 104 ? -12.628 29.220  -7.601  0.50 6.25  ? 209  GLN A OE1 1 
ATOM   855  O  OE1 B GLN A 1 104 ? -12.067 26.355  -2.313  0.50 15.59 ? 209  GLN A OE1 1 
ATOM   856  N  NE2 A GLN A 1 104 ? -14.545 29.834  -6.493  0.50 14.39 ? 209  GLN A NE2 1 
ATOM   857  N  NE2 B GLN A 1 104 ? -9.967  26.556  -3.423  0.50 15.32 ? 209  GLN A NE2 1 
ATOM   858  N  N   . TRP A 1 105 ? -13.075 24.637  -8.097  1.00 8.33  ? 210  TRP A N   1 
ATOM   859  C  CA  . TRP A 1 105 ? -13.943 23.529  -8.476  1.00 8.61  ? 210  TRP A CA  1 
ATOM   860  C  C   . TRP A 1 105 ? -13.104 22.373  -9.103  1.00 8.99  ? 210  TRP A C   1 
ATOM   861  O  O   . TRP A 1 105 ? -13.694 21.392  -9.632  1.00 9.34  ? 210  TRP A O   1 
ATOM   862  C  CB  . TRP A 1 105 ? -14.971 24.001  -9.450  1.00 9.08  ? 210  TRP A CB  1 
ATOM   863  C  CG  . TRP A 1 105 ? -16.076 24.832  -8.833  1.00 8.56  ? 210  TRP A CG  1 
ATOM   864  C  CD1 . TRP A 1 105 ? -16.272 25.123  -7.523  1.00 8.90  ? 210  TRP A CD1 1 
ATOM   865  C  CD2 . TRP A 1 105 ? -17.146 25.482  -9.566  1.00 8.89  ? 210  TRP A CD2 1 
ATOM   866  N  NE1 . TRP A 1 105 ? -17.431 25.931  -7.365  1.00 9.93  ? 210  TRP A NE1 1 
ATOM   867  C  CE2 . TRP A 1 105 ? -17.980 26.158  -8.611  1.00 9.42  ? 210  TRP A CE2 1 
ATOM   868  C  CE3 . TRP A 1 105 ? -17.426 25.595  -10.942 1.00 9.97  ? 210  TRP A CE3 1 
ATOM   869  C  CZ2 . TRP A 1 105 ? -19.096 26.903  -8.988  1.00 10.58 ? 210  TRP A CZ2 1 
ATOM   870  C  CZ3 . TRP A 1 105 ? -18.547 26.360  -11.315 1.00 10.50 ? 210  TRP A CZ3 1 
ATOM   871  C  CH2 . TRP A 1 105 ? -19.383 27.008  -10.351 1.00 10.78 ? 210  TRP A CH2 1 
ATOM   872  N  N   . HIS A 1 106 ? -11.773 22.434  -9.045  1.00 8.66  ? 211  HIS A N   1 
ATOM   873  C  CA  . HIS A 1 106 ? -10.868 21.310  -9.419  1.00 8.59  ? 211  HIS A CA  1 
ATOM   874  C  C   . HIS A 1 106 ? -10.306 20.797  -8.070  1.00 8.95  ? 211  HIS A C   1 
ATOM   875  O  O   . HIS A 1 106 ? -9.248  21.232  -7.606  1.00 9.85  ? 211  HIS A O   1 
ATOM   876  C  CB  . HIS A 1 106 ? -9.775  21.801  -10.357 1.00 8.90  ? 211  HIS A CB  1 
ATOM   877  C  CG  . HIS A 1 106 ? -10.324 22.239  -11.684 1.00 8.58  ? 211  HIS A CG  1 
ATOM   878  N  ND1 . HIS A 1 106 ? -9.661  23.038  -12.584 1.00 10.19 ? 211  HIS A ND1 1 
ATOM   879  C  CD2 . HIS A 1 106 ? -11.540 21.950  -12.255 1.00 8.48  ? 211  HIS A CD2 1 
ATOM   880  C  CE1 . HIS A 1 106 ? -10.448 23.225  -13.641 1.00 9.46  ? 211  HIS A CE1 1 
ATOM   881  N  NE2 . HIS A 1 106 ? -11.578 22.587  -13.489 1.00 8.64  ? 211  HIS A NE2 1 
ATOM   882  N  N   . CYS A 1 107 ? -11.071 19.955  -7.410  1.00 8.85  ? 212  CYS A N   1 
ATOM   883  C  CA  . CYS A 1 107 ? -10.910 19.692  -5.968  1.00 9.69  ? 212  CYS A CA  1 
ATOM   884  C  C   . CYS A 1 107 ? -10.141 18.347  -5.764  1.00 9.05  ? 212  CYS A C   1 
ATOM   885  O  O   . CYS A 1 107 ? -10.741 17.294  -5.830  1.00 9.39  ? 212  CYS A O   1 
ATOM   886  C  CB  . CYS A 1 107 ? -12.305 19.636  -5.347  1.00 8.95  ? 212  CYS A CB  1 
ATOM   887  S  SG  . CYS A 1 107 ? -12.331 19.349  -3.566  1.00 12.78 ? 212  CYS A SG  1 
ATOM   888  N  N   . GLY A 1 108 ? -8.870  18.488  -5.419  1.00 9.10  ? 213  GLY A N   1 
ATOM   889  C  CA  . GLY A 1 108 ? -8.032  17.297  -5.143  1.00 9.59  ? 213  GLY A CA  1 
ATOM   890  C  C   . GLY A 1 108 ? -7.940  16.964  -3.689  1.00 9.91  ? 213  GLY A C   1 
ATOM   891  O  O   . GLY A 1 108 ? -8.177  17.825  -2.775  1.00 10.07 ? 213  GLY A O   1 
ATOM   892  N  N   . VAL A 1 109 ? -7.506  15.725  -3.414  1.00 10.58 ? 214  VAL A N   1 
ATOM   893  C  CA  . VAL A 1 109 ? -7.168  15.237  -2.066  1.00 9.80  ? 214  VAL A CA  1 
ATOM   894  C  C   . VAL A 1 109 ? -5.733  14.621  -2.142  1.00 11.39 ? 214  VAL A C   1 
ATOM   895  O  O   . VAL A 1 109 ? -5.462  13.798  -3.049  1.00 10.50 ? 214  VAL A O   1 
ATOM   896  C  CB  . VAL A 1 109 ? -8.127  14.148  -1.627  1.00 11.07 ? 214  VAL A CB  1 
ATOM   897  C  CG1 . VAL A 1 109 ? -7.674  13.546  -0.247  1.00 12.54 ? 214  VAL A CG1 1 
ATOM   898  C  CG2 . VAL A 1 109 ? -9.571  14.682  -1.561  1.00 14.98 ? 214  VAL A CG2 1 
ATOM   899  N  N   . ARG A 1 110 ? -4.841  15.079  -1.259  1.00 11.13 ? 215  ARG A N   1 
ATOM   900  C  CA  . ARG A 1 110 ? -3.442  14.564  -1.209  1.00 10.71 ? 215  ARG A CA  1 
ATOM   901  C  C   . ARG A 1 110 ? -3.157  13.925  0.171   1.00 11.52 ? 215  ARG A C   1 
ATOM   902  O  O   . ARG A 1 110 ? -3.747  14.292  1.204   1.00 12.63 ? 215  ARG A O   1 
ATOM   903  C  CB  . ARG A 1 110 ? -2.435  15.658  -1.437  1.00 11.38 ? 215  ARG A CB  1 
ATOM   904  C  CG  . ARG A 1 110 ? -2.512  16.262  -2.868  1.00 12.36 ? 215  ARG A CG  1 
ATOM   905  C  CD  . ARG A 1 110 ? -1.463  17.338  -3.031  1.00 12.46 ? 215  ARG A CD  1 
ATOM   906  N  NE  . ARG A 1 110 ? -1.419  17.906  -4.393  1.00 12.69 ? 215  ARG A NE  1 
ATOM   907  C  CZ  . ARG A 1 110 ? -0.818  17.379  -5.417  1.00 11.53 ? 215  ARG A CZ  1 
ATOM   908  N  NH1 . ARG A 1 110 ? -0.200  16.190  -5.330  1.00 12.69 ? 215  ARG A NH1 1 
ATOM   909  N  NH2 . ARG A 1 110 ? -0.802  17.972  -6.605  1.00 12.95 ? 215  ARG A NH2 1 
ATOM   910  N  N   . VAL A 1 111 ? -2.271  12.950  0.124   1.00 12.51 ? 216  VAL A N   1 
ATOM   911  C  CA  . VAL A 1 111 ? -1.642  12.433  1.395   1.00 13.35 ? 216  VAL A CA  1 
ATOM   912  C  C   . VAL A 1 111 ? -0.713  13.578  1.910   1.00 13.48 ? 216  VAL A C   1 
ATOM   913  O  O   . VAL A 1 111 ? 0.118   14.131  1.207   1.00 14.36 ? 216  VAL A O   1 
ATOM   914  C  CB  . VAL A 1 111 ? -0.846  11.197  1.031   1.00 12.70 ? 216  VAL A CB  1 
ATOM   915  C  CG1 . VAL A 1 111 ? -0.234  10.672  2.400   1.00 14.62 ? 216  VAL A CG1 1 
ATOM   916  C  CG2 . VAL A 1 111 ? -1.759  10.131  0.391   1.00 14.86 ? 216  VAL A CG2 1 
ATOM   917  N  N   . VAL A 1 112 ? -0.887  13.924  3.207   1.00 15.31 ? 217  VAL A N   1 
ATOM   918  C  CA  . VAL A 1 112 ? -0.161  15.087  3.761   1.00 18.46 ? 217  VAL A CA  1 
ATOM   919  C  C   . VAL A 1 112 ? 1.409   14.862  3.691   1.00 17.90 ? 217  VAL A C   1 
ATOM   920  O  O   . VAL A 1 112 ? 2.093   15.794  3.313   1.00 20.69 ? 217  VAL A O   1 
ATOM   921  C  CB  . VAL A 1 112 ? -0.542  15.357  5.210   1.00 19.12 ? 217  VAL A CB  1 
ATOM   922  C  CG1 . VAL A 1 112 ? 0.376   16.400  5.850   1.00 21.11 ? 217  VAL A CG1 1 
ATOM   923  C  CG2 . VAL A 1 112 ? -1.944  15.989  5.263   1.00 18.84 ? 217  VAL A CG2 1 
ATOM   924  N  N   . SER A 1 113 ? 1.817   13.648  4.024   1.00 19.27 ? 218  SER A N   1 
ATOM   925  C  CA  . SER A 1 113 ? 3.298   13.378  4.170   1.00 19.98 ? 218  SER A CA  1 
ATOM   926  C  C   . SER A 1 113 ? 3.913   13.234  2.795   1.00 21.52 ? 218  SER A C   1 
ATOM   927  O  O   . SER A 1 113 ? 4.828   13.996  2.461   1.00 24.59 ? 218  SER A O   1 
ATOM   928  C  CB  . SER A 1 113 ? 3.494   12.123  5.032   1.00 22.68 ? 218  SER A CB  1 
ATOM   929  O  OG  . SER A 1 113 ? 2.980   10.963  4.439   1.00 21.68 ? 218  SER A OG  1 
ATOM   930  N  N   . SER A 1 114 ? 3.369   12.376  1.906   1.00 17.33 ? 219  SER A N   1 
ATOM   931  C  CA  . SER A 1 114 ? 4.050   12.116  0.653   1.00 16.82 ? 219  SER A CA  1 
ATOM   932  C  C   . SER A 1 114 ? 3.607   13.083  -0.441  1.00 16.31 ? 219  SER A C   1 
ATOM   933  O  O   . SER A 1 114 ? 4.278   13.058  -1.468  1.00 17.27 ? 219  SER A O   1 
ATOM   934  C  CB  . SER A 1 114 ? 3.749   10.744  0.110   1.00 18.49 ? 219  SER A CB  1 
ATOM   935  O  OG  . SER A 1 114 ? 2.270   10.612  -0.072  1.00 17.26 ? 219  SER A OG  1 
ATOM   936  N  N   . ARG A 1 115 ? 2.474   13.786  -0.234  1.00 16.77 ? 220  ARG A N   1 
ATOM   937  C  CA  . ARG A 1 115 ? 1.826   14.660  -1.252  1.00 16.53 ? 220  ARG A CA  1 
ATOM   938  C  C   . ARG A 1 115 ? 1.125   13.849  -2.344  1.00 14.86 ? 220  ARG A C   1 
ATOM   939  O  O   . ARG A 1 115 ? 0.580   14.503  -3.274  1.00 14.90 ? 220  ARG A O   1 
ATOM   940  C  CB  . ARG A 1 115 ? 2.811   15.682  -1.927  1.00 15.95 ? 220  ARG A CB  1 
ATOM   941  C  CG  . ARG A 1 115 ? 3.579   16.562  -0.917  1.00 19.00 ? 220  ARG A CG  1 
ATOM   942  C  CD  . ARG A 1 115 ? 2.667   17.004  0.214   1.00 20.63 ? 220  ARG A CD  1 
ATOM   943  N  NE  . ARG A 1 115 ? 1.647   17.946  -0.271  1.00 20.87 ? 220  ARG A NE  1 
ATOM   944  C  CZ  . ARG A 1 115 ? 0.725   18.519  0.510   1.00 22.86 ? 220  ARG A CZ  1 
ATOM   945  N  NH1 . ARG A 1 115 ? 0.702   18.250  1.839   1.00 24.11 ? 220  ARG A NH1 1 
ATOM   946  N  NH2 . ARG A 1 115 ? -0.139  19.402  -0.007  1.00 18.90 ? 220  ARG A NH2 1 
ATOM   947  N  N   . LYS A 1 116 ? 1.075   12.528  -2.274  1.00 14.35 ? 221  LYS A N   1 
ATOM   948  C  CA  . LYS A 1 116 ? 0.483   11.730  -3.385  1.00 14.03 ? 221  LYS A CA  1 
ATOM   949  C  C   . LYS A 1 116 ? -0.993  12.166  -3.551  1.00 11.09 ? 221  LYS A C   1 
ATOM   950  O  O   . LYS A 1 116 ? -1.771  12.233  -2.601  1.00 12.34 ? 221  LYS A O   1 
ATOM   951  C  CB  . LYS A 1 116 ? 0.584   10.224  -3.115  1.00 14.49 ? 221  LYS A CB  1 
ATOM   952  C  CG  . LYS A 1 116 ? 0.039   9.341   -4.232  1.00 16.59 ? 221  LYS A CG  1 
ATOM   953  C  CD  . LYS A 1 116 ? 0.084   7.875   -3.827  1.00 19.70 ? 221  LYS A CD  1 
ATOM   954  C  CE  . LYS A 1 116 ? -0.437  6.985   -4.944  1.00 22.64 ? 221  LYS A CE  1 
ATOM   955  N  NZ  . LYS A 1 116 ? 0.260   7.129   -6.274  1.00 25.55 ? 221  LYS A NZ  1 
ATOM   956  N  N   . LEU A 1 117 ? -1.317  12.355  -4.834  1.00 11.53 ? 222  LEU A N   1 
ATOM   957  C  CA  . LEU A 1 117 ? -2.745  12.632  -5.182  1.00 11.96 ? 222  LEU A CA  1 
ATOM   958  C  C   . LEU A 1 117 ? -3.574  11.368  -5.061  1.00 10.62 ? 222  LEU A C   1 
ATOM   959  O  O   . LEU A 1 117 ? -3.250  10.367  -5.800  1.00 11.74 ? 222  LEU A O   1 
ATOM   960  C  CB  . LEU A 1 117 ? -2.809  13.257  -6.605  1.00 11.54 ? 222  LEU A CB  1 
ATOM   961  C  CG  . LEU A 1 117 ? -4.240  13.727  -7.002  1.00 9.99  ? 222  LEU A CG  1 
ATOM   962  C  CD1 . LEU A 1 117 ? -4.726  14.973  -6.199  1.00 11.94 ? 222  LEU A CD1 1 
ATOM   963  C  CD2 . LEU A 1 117 ? -4.187  14.105  -8.517  1.00 11.83 ? 222  LEU A CD2 1 
ATOM   964  N  N   . VAL A 1 118 ? -4.621  11.374  -4.264  1.00 10.43 ? 223  VAL A N   1 
ATOM   965  C  CA  . VAL A 1 118 ? -5.394  10.165  -4.003  1.00 11.17 ? 223  VAL A CA  1 
ATOM   966  C  C   . VAL A 1 118 ? -6.900  10.327  -4.167  1.00 10.40 ? 223  VAL A C   1 
ATOM   967  O  O   . VAL A 1 118 ? -7.674  9.410   -4.014  1.00 10.64 ? 223  VAL A O   1 
ATOM   968  C  CB  . VAL A 1 118 ? -5.134  9.540   -2.614  1.00 11.65 ? 223  VAL A CB  1 
ATOM   969  C  CG1 . VAL A 1 118 ? -3.656  8.997   -2.595  1.00 13.24 ? 223  VAL A CG1 1 
ATOM   970  C  CG2 . VAL A 1 118 ? -5.392  10.537  -1.501  1.00 11.82 ? 223  VAL A CG2 1 
ATOM   971  N  N   . GLY A 1 119 ? -7.326  11.575  -4.518  1.00 10.74 ? 224  GLY A N   1 
ATOM   972  C  CA  . GLY A 1 119 ? -8.805  11.757  -4.727  1.00 10.19 ? 224  GLY A CA  1 
ATOM   973  C  C   . GLY A 1 119 ? -9.008  13.037  -5.592  1.00 8.94  ? 224  GLY A C   1 
ATOM   974  O  O   . GLY A 1 119 ? -8.140  13.919  -5.628  1.00 9.31  ? 224  GLY A O   1 
ATOM   975  N  N   . PHE A 1 120 ? -10.168 13.047  -6.250  1.00 8.49  ? 225  PHE A N   1 
ATOM   976  C  CA  . PHE A 1 120 ? -10.524 14.257  -7.053  1.00 8.30  ? 225  PHE A CA  1 
ATOM   977  C  C   . PHE A 1 120 ? -12.019 14.229  -7.241  1.00 7.67  ? 225  PHE A C   1 
ATOM   978  O  O   . PHE A 1 120 ? -12.693 13.210  -7.225  1.00 8.22  ? 225  PHE A O   1 
ATOM   979  C  CB  . PHE A 1 120 ? -9.815  14.174  -8.447  1.00 9.21  ? 225  PHE A CB  1 
ATOM   980  C  CG  . PHE A 1 120 ? -10.009 15.446  -9.291  1.00 8.71  ? 225  PHE A CG  1 
ATOM   981  C  CD1 . PHE A 1 120 ? -9.294  16.618  -8.949  1.00 9.02  ? 225  PHE A CD1 1 
ATOM   982  C  CD2 . PHE A 1 120 ? -10.815 15.408  -10.456 1.00 8.76  ? 225  PHE A CD2 1 
ATOM   983  C  CE1 . PHE A 1 120 ? -9.430  17.753  -9.737  1.00 8.52  ? 225  PHE A CE1 1 
ATOM   984  C  CE2 . PHE A 1 120 ? -10.928 16.525  -11.243 1.00 8.93  ? 225  PHE A CE2 1 
ATOM   985  C  CZ  . PHE A 1 120 ? -10.221 17.674  -10.922 1.00 9.23  ? 225  PHE A CZ  1 
ATOM   986  N  N   . ILE A 1 121 ? -12.526 15.481  -7.413  1.00 8.39  ? 226  ILE A N   1 
ATOM   987  C  CA  . ILE A 1 121 ? -13.904 15.672  -7.919  1.00 8.13  ? 226  ILE A CA  1 
ATOM   988  C  C   . ILE A 1 121 ? -13.916 17.082  -8.573  1.00 7.81  ? 226  ILE A C   1 
ATOM   989  O  O   . ILE A 1 121 ? -13.076 17.911  -8.239  1.00 8.51  ? 226  ILE A O   1 
ATOM   990  C  CB  . ILE A 1 121 ? -14.968 15.605  -6.797  1.00 8.14  ? 226  ILE A CB  1 
ATOM   991  C  CG1 . ILE A 1 121 ? -16.415 15.537  -7.377  1.00 9.54  ? 226  ILE A CG1 1 
ATOM   992  C  CG2 . ILE A 1 121 ? -14.854 16.756  -5.796  1.00 9.70  ? 226  ILE A CG2 1 
ATOM   993  C  CD1 . ILE A 1 121 ? -17.513 15.112  -6.340  1.00 10.79 ? 226  ILE A CD1 1 
ATOM   994  N  N   . SER A 1 122 ? -14.793 17.248  -9.574  1.00 8.23  ? 227  SER A N   1 
ATOM   995  C  CA  . SER A 1 122 ? -14.868 18.522  -10.303 1.00 7.98  ? 227  SER A CA  1 
ATOM   996  C  C   . SER A 1 122 ? -16.298 18.971  -10.510 1.00 7.56  ? 227  SER A C   1 
ATOM   997  O  O   . SER A 1 122 ? -17.186 18.145  -10.658 1.00 8.07  ? 227  SER A O   1 
ATOM   998  C  CB  . SER A 1 122 ? -14.107 18.466  -11.611 1.00 8.49  ? 227  SER A CB  1 
ATOM   999  O  OG  . SER A 1 122 ? -14.794 17.638  -12.546 1.00 10.25 ? 227  SER A OG  1 
ATOM   1000 N  N   . ALA A 1 123 ? -16.387 20.299  -10.666 1.00 8.56  ? 228  ALA A N   1 
ATOM   1001 C  CA  . ALA A 1 123 ? -17.593 20.957  -11.164 1.00 7.93  ? 228  ALA A CA  1 
ATOM   1002 C  C   . ALA A 1 123 ? -17.225 21.899  -12.291 1.00 8.19  ? 228  ALA A C   1 
ATOM   1003 O  O   . ALA A 1 123 ? -16.167 22.570  -12.228 1.00 8.24  ? 228  ALA A O   1 
ATOM   1004 C  CB  . ALA A 1 123 ? -18.241 21.808  -10.039 1.00 8.00  ? 228  ALA A CB  1 
ATOM   1005 N  N   . ILE A 1 124 ? -18.094 21.966  -13.345 1.00 7.89  ? 229  ILE A N   1 
ATOM   1006 C  CA  . ILE A 1 124 ? -17.972 23.010  -14.365 1.00 8.31  ? 229  ILE A CA  1 
ATOM   1007 C  C   . ILE A 1 124 ? -19.376 23.618  -14.500 1.00 8.27  ? 229  ILE A C   1 
ATOM   1008 O  O   . ILE A 1 124 ? -20.371 22.949  -14.281 1.00 8.39  ? 229  ILE A O   1 
ATOM   1009 C  CB  . ILE A 1 124 ? -17.477 22.432  -15.763 1.00 8.76  ? 229  ILE A CB  1 
ATOM   1010 C  CG1 . ILE A 1 124 ? -18.368 21.288  -16.251 1.00 8.73  ? 229  ILE A CG1 1 
ATOM   1011 C  CG2 . ILE A 1 124 ? -16.039 22.024  -15.669 1.00 9.37  ? 229  ILE A CG2 1 
ATOM   1012 C  CD1 . ILE A 1 124 ? -18.107 20.952  -17.733 1.00 9.51  ? 229  ILE A CD1 1 
ATOM   1013 N  N   . PRO A 1 125 ? -19.477 24.932  -14.780 1.00 8.65  ? 230  PRO A N   1 
ATOM   1014 C  CA  . PRO A 1 125 ? -20.814 25.545  -14.921 1.00 9.06  ? 230  PRO A CA  1 
ATOM   1015 C  C   . PRO A 1 125 ? -21.507 25.121  -16.158 1.00 9.64  ? 230  PRO A C   1 
ATOM   1016 O  O   . PRO A 1 125 ? -20.853 24.943  -17.201 1.00 11.36 ? 230  PRO A O   1 
ATOM   1017 C  CB  . PRO A 1 125 ? -20.457 27.045  -14.951 1.00 10.49 ? 230  PRO A CB  1 
ATOM   1018 C  CG  . PRO A 1 125 ? -19.092 27.122  -15.572 1.00 10.90 ? 230  PRO A CG  1 
ATOM   1019 C  CD  . PRO A 1 125 ? -18.372 25.849  -15.117 1.00 9.17  ? 230  PRO A CD  1 
ATOM   1020 N  N   . ALA A 1 126 ? -22.847 25.076  -16.137 1.00 9.24  ? 231  ALA A N   1 
ATOM   1021 C  CA  . ALA A 1 126 ? -23.616 24.823  -17.386 1.00 10.56 ? 231  ALA A CA  1 
ATOM   1022 C  C   . ALA A 1 126 ? -25.017 25.344  -17.204 1.00 10.78 ? 231  ALA A C   1 
ATOM   1023 O  O   . ALA A 1 126 ? -25.619 25.142  -16.115 1.00 12.58 ? 231  ALA A O   1 
ATOM   1024 C  CB  . ALA A 1 126 ? -23.651 23.337  -17.685 1.00 12.67 ? 231  ALA A CB  1 
ATOM   1025 N  N   . ASN A 1 127 ? -25.547 25.974  -18.217 1.00 10.71 ? 232  ASN A N   1 
ATOM   1026 C  CA  . ASN A 1 127 ? -26.990 26.275  -18.216 1.00 12.79 ? 232  ASN A CA  1 
ATOM   1027 C  C   . ASN A 1 127 ? -27.750 25.062  -18.733 1.00 10.56 ? 232  ASN A C   1 
ATOM   1028 O  O   . ASN A 1 127 ? -27.382 24.469  -19.783 1.00 11.62 ? 232  ASN A O   1 
ATOM   1029 C  CB  . ASN A 1 127 ? -27.211 27.507  -19.091 1.00 14.14 ? 232  ASN A CB  1 
ATOM   1030 C  CG  . ASN A 1 127 ? -26.785 28.771  -18.292 1.00 18.02 ? 232  ASN A CG  1 
ATOM   1031 O  OD1 . ASN A 1 127 ? -27.360 29.147  -17.264 1.00 20.69 ? 232  ASN A OD1 1 
ATOM   1032 N  ND2 . ASN A 1 127 ? -25.622 29.304  -18.667 1.00 23.97 ? 232  ASN A ND2 1 
ATOM   1033 N  N   . ILE A 1 128 ? -28.722 24.614  -17.968 1.00 10.88 ? 233  ILE A N   1 
ATOM   1034 C  CA  . ILE A 1 128 ? -29.471 23.377  -18.266 1.00 10.62 ? 233  ILE A CA  1 
ATOM   1035 C  C   . ILE A 1 128 ? -30.959 23.647  -18.430 1.00 11.38 ? 233  ILE A C   1 
ATOM   1036 O  O   . ILE A 1 128 ? -31.547 24.346  -17.595 1.00 13.80 ? 233  ILE A O   1 
ATOM   1037 C  CB  . ILE A 1 128 ? -29.240 22.354  -17.083 1.00 11.13 ? 233  ILE A CB  1 
ATOM   1038 C  CG1 . ILE A 1 128 ? -27.784 21.947  -16.989 1.00 11.96 ? 233  ILE A CG1 1 
ATOM   1039 C  CG2 . ILE A 1 128 ? -30.109 21.084  -17.179 1.00 12.95 ? 233  ILE A CG2 1 
ATOM   1040 C  CD1 . ILE A 1 128 ? -27.123 21.184  -18.217 1.00 12.23 ? 233  ILE A CD1 1 
ATOM   1041 N  N   . HIS A 1 129 ? -31.497 23.087  -19.507 1.00 11.52 ? 234  HIS A N   1 
ATOM   1042 C  CA  A HIS A 1 129 ? -32.926 23.130  -19.763 0.50 12.34 ? 234  HIS A CA  1 
ATOM   1043 C  CA  B HIS A 1 129 ? -32.935 23.133  -19.720 0.50 13.19 ? 234  HIS A CA  1 
ATOM   1044 C  C   . HIS A 1 129 ? -33.510 21.781  -19.318 1.00 12.90 ? 234  HIS A C   1 
ATOM   1045 O  O   . HIS A 1 129 ? -33.130 20.706  -19.846 1.00 12.88 ? 234  HIS A O   1 
ATOM   1046 C  CB  A HIS A 1 129 ? -33.088 23.338  -21.283 0.50 12.51 ? 234  HIS A CB  1 
ATOM   1047 C  CB  B HIS A 1 129 ? -33.237 23.448  -21.191 0.50 15.42 ? 234  HIS A CB  1 
ATOM   1048 C  CG  A HIS A 1 129 ? -34.457 23.837  -21.699 0.50 15.88 ? 234  HIS A CG  1 
ATOM   1049 C  CG  B HIS A 1 129 ? -34.659 23.928  -21.430 0.50 20.22 ? 234  HIS A CG  1 
ATOM   1050 N  ND1 A HIS A 1 129 ? -34.755 24.167  -23.009 0.50 17.71 ? 234  HIS A ND1 1 
ATOM   1051 N  ND1 B HIS A 1 129 ? -34.990 25.264  -21.534 0.50 26.01 ? 234  HIS A ND1 1 
ATOM   1052 C  CD2 A HIS A 1 129 ? -35.590 24.065  -20.985 0.50 16.13 ? 234  HIS A CD2 1 
ATOM   1053 C  CD2 B HIS A 1 129 ? -35.824 23.246  -21.591 0.50 20.71 ? 234  HIS A CD2 1 
ATOM   1054 C  CE1 A HIS A 1 129 ? -36.014 24.564  -23.085 0.50 15.08 ? 234  HIS A CE1 1 
ATOM   1055 C  CE1 B HIS A 1 129 ? -36.288 25.393  -21.772 0.50 26.34 ? 234  HIS A CE1 1 
ATOM   1056 N  NE2 A HIS A 1 129 ? -36.552 24.513  -21.880 0.50 18.38 ? 234  HIS A NE2 1 
ATOM   1057 N  NE2 B HIS A 1 129 ? -36.817 24.182  -21.832 0.50 26.01 ? 234  HIS A NE2 1 
ATOM   1058 N  N   . ILE A 1 130 ? -34.421 21.840  -18.354 1.00 12.99 ? 235  ILE A N   1 
ATOM   1059 C  CA  . ILE A 1 130 ? -35.071 20.653  -17.818 1.00 13.08 ? 235  ILE A CA  1 
ATOM   1060 C  C   . ILE A 1 130 ? -36.619 20.926  -17.874 1.00 12.15 ? 235  ILE A C   1 
ATOM   1061 O  O   . ILE A 1 130 ? -37.109 21.799  -17.207 1.00 14.18 ? 235  ILE A O   1 
ATOM   1062 C  CB  . ILE A 1 130 ? -34.555 20.302  -16.355 1.00 13.10 ? 235  ILE A CB  1 
ATOM   1063 C  CG1 . ILE A 1 130 ? -35.344 19.115  -15.802 1.00 13.57 ? 235  ILE A CG1 1 
ATOM   1064 C  CG2 . ILE A 1 130 ? -34.530 21.525  -15.393 1.00 13.31 ? 235  ILE A CG2 1 
ATOM   1065 C  CD1 . ILE A 1 130 ? -35.157 17.789  -16.558 1.00 13.88 ? 235  ILE A CD1 1 
ATOM   1066 N  N   . TYR A 1 131 ? -37.275 20.186  -18.763 1.00 12.60 ? 236  TYR A N   1 
ATOM   1067 C  CA  . TYR A 1 131 ? -38.714 20.442  -19.101 1.00 15.61 ? 236  TYR A CA  1 
ATOM   1068 C  C   . TYR A 1 131 ? -38.898 21.881  -19.412 1.00 17.69 ? 236  TYR A C   1 
ATOM   1069 O  O   . TYR A 1 131 ? -38.202 22.331  -20.327 1.00 19.12 ? 236  TYR A O   1 
ATOM   1070 C  CB  . TYR A 1 131 ? -39.642 19.874  -17.993 1.00 15.32 ? 236  TYR A CB  1 
ATOM   1071 C  CG  . TYR A 1 131 ? -39.567 18.387  -17.863 1.00 14.94 ? 236  TYR A CG  1 
ATOM   1072 C  CD1 . TYR A 1 131 ? -40.170 17.541  -18.849 1.00 15.83 ? 236  TYR A CD1 1 
ATOM   1073 C  CD2 . TYR A 1 131 ? -38.901 17.776  -16.790 1.00 16.55 ? 236  TYR A CD2 1 
ATOM   1074 C  CE1 . TYR A 1 131 ? -40.144 16.181  -18.723 1.00 16.02 ? 236  TYR A CE1 1 
ATOM   1075 C  CE2 . TYR A 1 131 ? -38.876 16.417  -16.634 1.00 16.59 ? 236  TYR A CE2 1 
ATOM   1076 C  CZ  . TYR A 1 131 ? -39.526 15.592  -17.591 1.00 16.74 ? 236  TYR A CZ  1 
ATOM   1077 O  OH  . TYR A 1 131 ? -39.495 14.267  -17.521 1.00 17.63 ? 236  TYR A OH  1 
ATOM   1078 N  N   . ASP A 1 132 ? -39.680 22.656  -18.685 1.00 16.93 ? 237  ASP A N   1 
ATOM   1079 C  CA  . ASP A 1 132 ? -39.987 24.022  -19.011 1.00 17.69 ? 237  ASP A CA  1 
ATOM   1080 C  C   . ASP A 1 132 ? -39.148 25.054  -18.250 1.00 17.69 ? 237  ASP A C   1 
ATOM   1081 O  O   . ASP A 1 132 ? -39.474 26.269  -18.260 1.00 23.79 ? 237  ASP A O   1 
ATOM   1082 C  CB  . ASP A 1 132 ? -41.496 24.349  -18.748 1.00 23.35 ? 237  ASP A CB  1 
ATOM   1083 C  CG  . ASP A 1 132 ? -42.430 23.370  -19.464 1.00 36.85 ? 237  ASP A CG  1 
ATOM   1084 O  OD1 . ASP A 1 132 ? -42.216 23.094  -20.676 1.00 32.24 ? 237  ASP A OD1 1 
ATOM   1085 O  OD2 . ASP A 1 132 ? -43.380 22.835  -18.810 1.00 48.06 ? 237  ASP A OD2 1 
ATOM   1086 N  N   . THR A 1 133 ? -38.067 24.638  -17.574 1.00 18.06 ? 238  THR A N   1 
ATOM   1087 C  CA  . THR A 1 133 ? -37.259 25.544  -16.808 1.00 18.30 ? 238  THR A CA  1 
ATOM   1088 C  C   . THR A 1 133 ? -35.812 25.557  -17.357 1.00 14.53 ? 238  THR A C   1 
ATOM   1089 O  O   . THR A 1 133 ? -35.305 24.479  -17.687 1.00 17.50 ? 238  THR A O   1 
ATOM   1090 C  CB  . THR A 1 133 ? -37.213 25.029  -15.336 1.00 20.11 ? 238  THR A CB  1 
ATOM   1091 O  OG1 . THR A 1 133 ? -38.589 25.150  -14.858 1.00 25.53 ? 238  THR A OG1 1 
ATOM   1092 C  CG2 . THR A 1 133 ? -36.266 25.856  -14.455 1.00 25.40 ? 238  THR A CG2 1 
ATOM   1093 N  N   . GLU A 1 134 ? -35.200 26.704  -17.431 1.00 15.77 ? 239  GLU A N   1 
ATOM   1094 C  CA  A GLU A 1 134 ? -33.759 26.785  -17.669 0.50 17.18 ? 239  GLU A CA  1 
ATOM   1095 C  CA  B GLU A 1 134 ? -33.741 26.808  -17.647 0.50 17.75 ? 239  GLU A CA  1 
ATOM   1096 C  C   . GLU A 1 134 ? -33.160 27.248  -16.328 1.00 17.42 ? 239  GLU A C   1 
ATOM   1097 O  O   . GLU A 1 134 ? -33.704 28.213  -15.658 1.00 20.65 ? 239  GLU A O   1 
ATOM   1098 C  CB  A GLU A 1 134 ? -33.493 27.729  -18.838 0.50 18.86 ? 239  GLU A CB  1 
ATOM   1099 C  CB  B GLU A 1 134 ? -33.464 27.842  -18.709 0.50 20.33 ? 239  GLU A CB  1 
ATOM   1100 C  CG  A GLU A 1 134 ? -32.027 27.724  -19.179 0.50 18.91 ? 239  GLU A CG  1 
ATOM   1101 C  CG  B GLU A 1 134 ? -33.733 27.298  -20.074 0.50 23.22 ? 239  GLU A CG  1 
ATOM   1102 C  CD  A GLU A 1 134 ? -31.579 28.688  -20.245 0.50 25.16 ? 239  GLU A CD  1 
ATOM   1103 C  CD  B GLU A 1 134 ? -33.065 28.097  -21.183 0.50 28.72 ? 239  GLU A CD  1 
ATOM   1104 O  OE1 A GLU A 1 134 ? -32.310 28.920  -21.254 0.50 28.13 ? 239  GLU A OE1 1 
ATOM   1105 O  OE1 B GLU A 1 134 ? -32.371 29.122  -20.899 0.50 34.19 ? 239  GLU A OE1 1 
ATOM   1106 O  OE2 A GLU A 1 134 ? -30.433 29.142  -20.106 0.50 24.28 ? 239  GLU A OE2 1 
ATOM   1107 O  OE2 B GLU A 1 134 ? -33.301 27.709  -22.331 0.50 26.54 ? 239  GLU A OE2 1 
ATOM   1108 N  N   . LYS A 1 135 ? -32.124 26.511  -15.859 1.00 16.41 ? 240  LYS A N   1 
ATOM   1109 C  CA  . LYS A 1 135 ? -31.453 26.999  -14.605 1.00 19.36 ? 240  LYS A CA  1 
ATOM   1110 C  C   . LYS A 1 135 ? -29.924 26.938  -14.850 1.00 16.07 ? 240  LYS A C   1 
ATOM   1111 O  O   . LYS A 1 135 ? -29.430 26.036  -15.493 1.00 12.69 ? 240  LYS A O   1 
ATOM   1112 C  CB  . LYS A 1 135 ? -31.790 26.167  -13.373 1.00 24.05 ? 240  LYS A CB  1 
ATOM   1113 C  CG  . LYS A 1 135 ? -31.780 27.176  -12.137 1.00 29.93 ? 240  LYS A CG  1 
ATOM   1114 C  CD  . LYS A 1 135 ? -32.938 26.923  -11.150 1.00 24.02 ? 240  LYS A CD  1 
ATOM   1115 C  CE  . LYS A 1 135 ? -33.177 28.070  -10.125 1.00 25.81 ? 240  LYS A CE  1 
ATOM   1116 N  NZ  . LYS A 1 135 ? -32.599 27.675  -8.800  1.00 33.97 ? 240  LYS A NZ  1 
ATOM   1117 N  N   . LYS A 1 136 ? -29.200 27.834  -14.199 1.00 16.04 ? 241  LYS A N   1 
ATOM   1118 C  CA  . LYS A 1 136 ? -27.693 27.728  -14.150 1.00 13.55 ? 241  LYS A CA  1 
ATOM   1119 C  C   . LYS A 1 136 ? -27.463 26.635  -13.143 1.00 13.79 ? 241  LYS A C   1 
ATOM   1120 O  O   . LYS A 1 136 ? -27.960 26.645  -11.999 1.00 15.71 ? 241  LYS A O   1 
ATOM   1121 C  CB  . LYS A 1 136 ? -27.165 29.066  -13.591 1.00 16.22 ? 241  LYS A CB  1 
ATOM   1122 C  CG  . LYS A 1 136 ? -25.689 29.056  -13.228 1.00 17.17 ? 241  LYS A CG  1 
ATOM   1123 C  CD  . LYS A 1 136 ? -24.920 28.641  -14.435 1.00 19.35 ? 241  LYS A CD  1 
ATOM   1124 C  CE  . LYS A 1 136 ? -23.455 28.916  -14.215 1.00 21.88 ? 241  LYS A CE  1 
ATOM   1125 N  NZ  . LYS A 1 136 ? -23.091 30.311  -13.718 1.00 21.74 ? 241  LYS A NZ  1 
ATOM   1126 N  N   . MET A 1 137 ? -26.650 25.677  -13.527 1.00 10.10 ? 242  MET A N   1 
ATOM   1127 C  CA  . MET A 1 137 ? -26.310 24.497  -12.730 1.00 9.72  ? 242  MET A CA  1 
ATOM   1128 C  C   . MET A 1 137 ? -24.779 24.293  -12.814 1.00 8.90  ? 242  MET A C   1 
ATOM   1129 O  O   . MET A 1 137 ? -24.058 25.067  -13.450 1.00 9.35  ? 242  MET A O   1 
ATOM   1130 C  CB  . MET A 1 137 ? -26.947 23.213  -13.280 1.00 11.04 ? 242  MET A CB  1 
ATOM   1131 C  CG  . MET A 1 137 ? -28.456 23.348  -13.243 1.00 12.35 ? 242  MET A CG  1 
ATOM   1132 S  SD  . MET A 1 137 ? -29.218 21.685  -13.340 1.00 13.95 ? 242  MET A SD  1 
ATOM   1133 C  CE  . MET A 1 137 ? -30.925 22.059  -13.484 1.00 19.12 ? 242  MET A CE  1 
ATOM   1134 N  N   . VAL A 1 138 ? -24.282 23.218  -12.188 1.00 8.90  ? 243  VAL A N   1 
ATOM   1135 C  CA  . VAL A 1 138 ? -22.966 22.690  -12.517 1.00 9.53  ? 243  VAL A CA  1 
ATOM   1136 C  C   . VAL A 1 138 ? -23.151 21.254  -12.998 1.00 9.24  ? 243  VAL A C   1 
ATOM   1137 O  O   . VAL A 1 138 ? -24.154 20.600  -12.657 1.00 9.19  ? 243  VAL A O   1 
ATOM   1138 C  CB  . VAL A 1 138 ? -21.981 22.689  -11.327 1.00 8.49  ? 243  VAL A CB  1 
ATOM   1139 C  CG1 . VAL A 1 138 ? -21.627 24.155  -10.966 1.00 8.72  ? 243  VAL A CG1 1 
ATOM   1140 C  CG2 . VAL A 1 138 ? -22.523 21.957  -10.108 1.00 9.24  ? 243  VAL A CG2 1 
ATOM   1141 N  N   . GLU A 1 139 ? -22.120 20.766  -13.719 1.00 8.28  ? 244  GLU A N   1 
ATOM   1142 C  CA  . GLU A 1 139 ? -21.981 19.358  -14.084 1.00 8.79  ? 244  GLU A CA  1 
ATOM   1143 C  C   . GLU A 1 139 ? -20.866 18.812  -13.212 1.00 8.69  ? 244  GLU A C   1 
ATOM   1144 O  O   . GLU A 1 139 ? -19.784 19.359  -13.160 1.00 8.79  ? 244  GLU A O   1 
ATOM   1145 C  CB  . GLU A 1 139 ? -21.602 19.180  -15.544 1.00 10.29 ? 244  GLU A CB  1 
ATOM   1146 C  CG  . GLU A 1 139 ? -22.740 19.691  -16.483 1.00 12.53 ? 244  GLU A CG  1 
ATOM   1147 C  CD  . GLU A 1 139 ? -22.416 19.800  -17.950 1.00 15.92 ? 244  GLU A CD  1 
ATOM   1148 O  OE1 . GLU A 1 139 ? -21.307 19.371  -18.257 1.00 22.09 ? 244  GLU A OE1 1 
ATOM   1149 O  OE2 . GLU A 1 139 ? -23.491 20.013  -18.689 1.00 15.90 ? 244  GLU A OE2 1 
ATOM   1150 N  N   . ILE A 1 140 ? -21.175 17.701  -12.537 1.00 8.88  ? 245  ILE A N   1 
ATOM   1151 C  CA  . ILE A 1 140 ? -20.190 17.034  -11.645 1.00 8.65  ? 245  ILE A CA  1 
ATOM   1152 C  C   . ILE A 1 140 ? -19.587 15.854  -12.406 1.00 8.50  ? 245  ILE A C   1 
ATOM   1153 O  O   . ILE A 1 140 ? -20.354 15.087  -13.013 1.00 9.97  ? 245  ILE A O   1 
ATOM   1154 C  CB  . ILE A 1 140 ? -20.768 16.610  -10.296 1.00 8.86  ? 245  ILE A CB  1 
ATOM   1155 C  CG1 . ILE A 1 140 ? -21.420 17.811  -9.569  1.00 9.66  ? 245  ILE A CG1 1 
ATOM   1156 C  CG2 . ILE A 1 140 ? -19.717 15.906  -9.481  1.00 10.14 ? 245  ILE A CG2 1 
ATOM   1157 C  CD1 . ILE A 1 140 ? -20.411 18.932  -9.278  1.00 9.58  ? 245  ILE A CD1 1 
ATOM   1158 N  N   . ASN A 1 141 ? -18.285 15.737  -12.380 1.00 8.60  ? 246  ASN A N   1 
ATOM   1159 C  CA  . ASN A 1 141 ? -17.591 14.706  -13.181 1.00 8.83  ? 246  ASN A CA  1 
ATOM   1160 C  C   . ASN A 1 141 ? -16.254 14.418  -12.530 1.00 8.55  ? 246  ASN A C   1 
ATOM   1161 O  O   . ASN A 1 141 ? -15.744 15.204  -11.695 1.00 8.82  ? 246  ASN A O   1 
ATOM   1162 C  CB  . ASN A 1 141 ? -17.521 15.158  -14.654 1.00 10.41 ? 246  ASN A CB  1 
ATOM   1163 C  CG  . ASN A 1 141 ? -17.469 14.034  -15.668 1.00 10.00 ? 246  ASN A CG  1 
ATOM   1164 O  OD1 . ASN A 1 141 ? -17.133 12.876  -15.337 1.00 10.24 ? 246  ASN A OD1 1 
ATOM   1165 N  ND2 . ASN A 1 141 ? -17.793 14.370  -16.933 1.00 11.75 ? 246  ASN A ND2 1 
ATOM   1166 N  N   . PHE A 1 142 ? -15.627 13.314  -12.921 1.00 8.23  ? 247  PHE A N   1 
ATOM   1167 C  CA  . PHE A 1 142 ? -14.277 12.933  -12.519 1.00 8.78  ? 247  PHE A CA  1 
ATOM   1168 C  C   . PHE A 1 142 ? -14.113 12.728  -10.997 1.00 8.10  ? 247  PHE A C   1 
ATOM   1169 O  O   . PHE A 1 142 ? -13.035 12.922  -10.455 1.00 9.66  ? 247  PHE A O   1 
ATOM   1170 C  CB  . PHE A 1 142 ? -13.221 13.924  -13.102 1.00 9.07  ? 247  PHE A CB  1 
ATOM   1171 C  CG  . PHE A 1 142 ? -13.280 13.973  -14.590 1.00 9.01  ? 247  PHE A CG  1 
ATOM   1172 C  CD1 . PHE A 1 142 ? -13.863 15.058  -15.229 1.00 9.49  ? 247  PHE A CD1 1 
ATOM   1173 C  CD2 . PHE A 1 142 ? -12.717 12.911  -15.392 1.00 10.05 ? 247  PHE A CD2 1 
ATOM   1174 C  CE1 . PHE A 1 142 ? -13.959 15.084  -16.625 1.00 10.05 ? 247  PHE A CE1 1 
ATOM   1175 C  CE2 . PHE A 1 142 ? -12.805 12.931  -16.768 1.00 9.97  ? 247  PHE A CE2 1 
ATOM   1176 C  CZ  . PHE A 1 142 ? -13.430 14.047  -17.428 1.00 10.23 ? 247  PHE A CZ  1 
ATOM   1177 N  N   . LEU A 1 143 ? -15.202 12.254  -10.364 1.00 9.01  ? 248  LEU A N   1 
ATOM   1178 C  CA  . LEU A 1 143 ? -15.086 11.797  -8.953  1.00 7.79  ? 248  LEU A CA  1 
ATOM   1179 C  C   . LEU A 1 143 ? -14.254 10.510  -8.928  1.00 8.35  ? 248  LEU A C   1 
ATOM   1180 O  O   . LEU A 1 143 ? -14.578 9.518   -9.661  1.00 9.22  ? 248  LEU A O   1 
ATOM   1181 C  CB  . LEU A 1 143 ? -16.477 11.529  -8.401  1.00 8.03  ? 248  LEU A CB  1 
ATOM   1182 C  CG  . LEU A 1 143 ? -16.582 10.741  -7.077  1.00 8.39  ? 248  LEU A CG  1 
ATOM   1183 C  CD1 . LEU A 1 143 ? -15.811 11.421  -5.945  1.00 10.98 ? 248  LEU A CD1 1 
ATOM   1184 C  CD2 . LEU A 1 143 ? -18.007 10.430  -6.699  1.00 11.02 ? 248  LEU A CD2 1 
ATOM   1185 N  N   . CYS A 1 144 ? -13.170 10.545  -8.165  1.00 9.19  ? 249  CYS A N   1 
ATOM   1186 C  CA  . CYS A 1 144 ? -12.260 9.366   -8.136  1.00 8.81  ? 249  CYS A CA  1 
ATOM   1187 C  C   . CYS A 1 144 ? -11.638 9.285   -6.790  1.00 9.57  ? 249  CYS A C   1 
ATOM   1188 O  O   . CYS A 1 144 ? -11.094 10.279  -6.285  1.00 10.41 ? 249  CYS A O   1 
ATOM   1189 C  CB  . CYS A 1 144 ? -11.194 9.550   -9.250  1.00 9.16  ? 249  CYS A CB  1 
ATOM   1190 S  SG  . CYS A 1 144 ? -10.048 8.140   -9.354  1.00 11.41 ? 249  CYS A SG  1 
ATOM   1191 N  N   . VAL A 1 145 ? -11.659 8.070   -6.199  1.00 9.64  ? 250  VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 145 ? -10.872 7.759   -4.962  1.00 10.87 ? 250  VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 145 ? -9.871  6.657   -5.339  1.00 10.83 ? 250  VAL A C   1 
ATOM   1194 O  O   . VAL A 1 145 ? -10.252 5.652   -6.000  1.00 11.43 ? 250  VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 145 ? -11.864 7.333   -3.853  1.00 11.03 ? 250  VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 145 ? -11.122 6.755   -2.628  1.00 13.04 ? 250  VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 145 ? -12.638 8.585   -3.404  1.00 11.54 ? 250  VAL A CG2 1 
ATOM   1198 N  N   . HIS A 1 146 ? -8.620  6.825   -4.901  1.00 11.32 ? 251  HIS A N   1 
ATOM   1199 C  CA  . HIS A 1 146 ? -7.600  5.817   -5.184  1.00 12.03 ? 251  HIS A CA  1 
ATOM   1200 C  C   . HIS A 1 146 ? -8.084  4.387   -4.715  1.00 12.98 ? 251  HIS A C   1 
ATOM   1201 O  O   . HIS A 1 146 ? -8.748  4.253   -3.690  1.00 13.04 ? 251  HIS A O   1 
ATOM   1202 C  CB  . HIS A 1 146 ? -6.356  6.189   -4.429  1.00 12.31 ? 251  HIS A CB  1 
ATOM   1203 C  CG  . HIS A 1 146 ? -5.142  5.457   -4.870  1.00 12.41 ? 251  HIS A CG  1 
ATOM   1204 N  ND1 . HIS A 1 146 ? -4.882  4.132   -4.478  1.00 15.05 ? 251  HIS A ND1 1 
ATOM   1205 C  CD2 . HIS A 1 146 ? -4.124  5.876   -5.644  1.00 13.41 ? 251  HIS A CD2 1 
ATOM   1206 C  CE1 . HIS A 1 146 ? -3.701  3.827   -5.019  1.00 15.07 ? 251  HIS A CE1 1 
ATOM   1207 N  NE2 . HIS A 1 146 ? -3.235  4.811   -5.737  1.00 15.78 ? 251  HIS A NE2 1 
ATOM   1208 N  N   . LYS A 1 147 ? -7.718  3.371   -5.498  1.00 12.89 ? 252  LYS A N   1 
ATOM   1209 C  CA  . LYS A 1 147 ? -8.099  2.005   -5.123  1.00 13.88 ? 252  LYS A CA  1 
ATOM   1210 C  C   . LYS A 1 147 ? -7.721  1.586   -3.683  1.00 14.01 ? 252  LYS A C   1 
ATOM   1211 O  O   . LYS A 1 147 ? -8.536  0.837   -3.056  1.00 16.64 ? 252  LYS A O   1 
ATOM   1212 C  CB  . LYS A 1 147 ? -7.440  1.022   -6.120  1.00 14.75 ? 252  LYS A CB  1 
ATOM   1213 C  CG  . LYS A 1 147 ? -8.078  1.068   -7.478  1.00 14.91 ? 252  LYS A CG  1 
ATOM   1214 C  CD  . LYS A 1 147 ? -7.275  0.142   -8.456  1.00 17.54 ? 252  LYS A CD  1 
ATOM   1215 C  CE  . LYS A 1 147 ? -7.953  0.107   -9.834  1.00 19.62 ? 252  LYS A CE  1 
ATOM   1216 N  NZ  . LYS A 1 147 ? -8.916  -1.022  -9.821  1.00 21.63 ? 252  LYS A NZ  1 
ATOM   1217 N  N   . LYS A 1 148 ? -6.629  2.131   -3.158  1.00 15.22 ? 253  LYS A N   1 
ATOM   1218 C  CA  . LYS A 1 148 ? -6.188  1.702   -1.791  1.00 17.01 ? 253  LYS A CA  1 
ATOM   1219 C  C   . LYS A 1 148 ? -7.030  2.409   -0.719  1.00 20.02 ? 253  LYS A C   1 
ATOM   1220 O  O   . LYS A 1 148 ? -7.033  2.030   0.464   1.00 19.41 ? 253  LYS A O   1 
ATOM   1221 C  CB  . LYS A 1 148 ? -4.723  2.040   -1.582  1.00 19.72 ? 253  LYS A CB  1 
ATOM   1222 C  CG  . LYS A 1 148 ? -3.751  1.127   -2.403  1.00 27.00 ? 253  LYS A CG  1 
ATOM   1223 C  CD  . LYS A 1 148 ? -3.649  -0.299  -1.779  1.00 38.55 ? 253  LYS A CD  1 
ATOM   1224 C  CE  . LYS A 1 148 ? -2.825  -1.343  -2.581  1.00 47.28 ? 253  LYS A CE  1 
ATOM   1225 N  NZ  . LYS A 1 148 ? -1.580  -1.806  -1.869  1.00 58.26 ? 253  LYS A NZ  1 
ATOM   1226 N  N   . LEU A 1 149 ? -7.817  3.421   -1.089  1.00 15.64 ? 254  LEU A N   1 
ATOM   1227 C  CA  . LEU A 1 149 ? -8.717  4.152   -0.174  1.00 16.66 ? 254  LEU A CA  1 
ATOM   1228 C  C   . LEU A 1 149 ? -10.198 3.837   -0.331  1.00 15.50 ? 254  LEU A C   1 
ATOM   1229 O  O   . LEU A 1 149 ? -11.023 4.546   0.271   1.00 15.67 ? 254  LEU A O   1 
ATOM   1230 C  CB  . LEU A 1 149 ? -8.507  5.641   -0.402  1.00 19.51 ? 254  LEU A CB  1 
ATOM   1231 C  CG  . LEU A 1 149 ? -7.447  6.507   0.274   1.00 30.59 ? 254  LEU A CG  1 
ATOM   1232 C  CD1 . LEU A 1 149 ? -6.012  6.128   0.033   1.00 33.57 ? 254  LEU A CD1 1 
ATOM   1233 C  CD2 . LEU A 1 149 ? -7.709  7.972   0.036   1.00 23.77 ? 254  LEU A CD2 1 
ATOM   1234 N  N   . ARG A 1 150 ? -10.598 2.822   -1.087  1.00 14.73 ? 255  ARG A N   1 
ATOM   1235 C  CA  . ARG A 1 150 ? -11.977 2.526   -1.377  1.00 15.36 ? 255  ARG A CA  1 
ATOM   1236 C  C   . ARG A 1 150 ? -12.765 2.042   -0.132  1.00 16.87 ? 255  ARG A C   1 
ATOM   1237 O  O   . ARG A 1 150 ? -12.156 1.319   0.731   1.00 18.34 ? 255  ARG A O   1 
ATOM   1238 C  CB  . ARG A 1 150 ? -12.074 1.452   -2.495  1.00 14.88 ? 255  ARG A CB  1 
ATOM   1239 C  CG  . ARG A 1 150 ? -11.570 1.990   -3.891  1.00 13.95 ? 255  ARG A CG  1 
ATOM   1240 C  CD  . ARG A 1 150 ? -12.586 2.943   -4.557  1.00 12.85 ? 255  ARG A CD  1 
ATOM   1241 N  NE  . ARG A 1 150 ? -12.054 3.465   -5.815  1.00 12.99 ? 255  ARG A NE  1 
ATOM   1242 C  CZ  . ARG A 1 150 ? -11.853 2.742   -6.910  1.00 13.04 ? 255  ARG A CZ  1 
ATOM   1243 N  NH1 . ARG A 1 150 ? -12.340 1.472   -7.060  1.00 15.77 ? 255  ARG A NH1 1 
ATOM   1244 N  NH2 . ARG A 1 150 ? -11.257 3.273   -7.919  1.00 13.74 ? 255  ARG A NH2 1 
ATOM   1245 N  N   . SER A 1 151 ? -14.055 2.268   -0.120  1.00 16.44 ? 256  SER A N   1 
ATOM   1246 C  CA  . SER A 1 151 ? -14.990 1.782   0.867   1.00 16.32 ? 256  SER A CA  1 
ATOM   1247 C  C   . SER A 1 151 ? -14.653 2.331   2.248   1.00 17.05 ? 256  SER A C   1 
ATOM   1248 O  O   . SER A 1 151 ? -14.881 1.579   3.241   1.00 21.17 ? 256  SER A O   1 
ATOM   1249 C  CB  . SER A 1 151 ? -15.053 0.221   0.808   1.00 19.17 ? 256  SER A CB  1 
ATOM   1250 O  OG  . SER A 1 151 ? -15.469 -0.211  -0.471  1.00 20.26 ? 256  SER A OG  1 
ATOM   1251 N  N   . LYS A 1 152 ? -14.093 3.518   2.363   1.00 17.15 ? 257  LYS A N   1 
ATOM   1252 C  CA  . LYS A 1 152 ? -13.805 4.188   3.637   1.00 15.81 ? 257  LYS A CA  1 
ATOM   1253 C  C   . LYS A 1 152 ? -14.635 5.503   3.750   1.00 16.83 ? 257  LYS A C   1 
ATOM   1254 O  O   . LYS A 1 152 ? -14.325 6.352   4.592   1.00 18.99 ? 257  LYS A O   1 
ATOM   1255 C  CB  . LYS A 1 152 ? -12.394 4.586   3.663   1.00 17.75 ? 257  LYS A CB  1 
ATOM   1256 C  CG  . LYS A 1 152 ? -11.523 3.365   3.658   1.00 21.95 ? 257  LYS A CG  1 
ATOM   1257 C  CD  . LYS A 1 152 ? -10.055 3.759   3.700   1.00 23.41 ? 257  LYS A CD  1 
ATOM   1258 C  CE  . LYS A 1 152 ? -9.094  2.540   3.687   1.00 31.01 ? 257  LYS A CE  1 
ATOM   1259 N  NZ  . LYS A 1 152 ? -9.493  1.456   4.678   1.00 36.77 ? 257  LYS A NZ  1 
ATOM   1260 N  N   . ARG A 1 153 ? -15.679 5.653   2.914   1.00 16.99 ? 258  ARG A N   1 
ATOM   1261 C  CA  . ARG A 1 153 ? -16.623 6.816   2.952   1.00 17.73 ? 258  ARG A CA  1 
ATOM   1262 C  C   . ARG A 1 153 ? -15.867 8.103   2.725   1.00 16.66 ? 258  ARG A C   1 
ATOM   1263 O  O   . ARG A 1 153 ? -16.295 9.162   3.253   1.00 17.34 ? 258  ARG A O   1 
ATOM   1264 C  CB  . ARG A 1 153 ? -17.415 6.915   4.275   1.00 18.26 ? 258  ARG A CB  1 
ATOM   1265 C  CG  . ARG A 1 153 ? -17.766 5.641   4.992   1.00 27.86 ? 258  ARG A CG  1 
ATOM   1266 C  CD  . ARG A 1 153 ? -18.815 4.950   4.226   1.00 28.52 ? 258  ARG A CD  1 
ATOM   1267 N  NE  . ARG A 1 153 ? -19.948 5.830   3.973   1.00 36.56 ? 258  ARG A NE  1 
ATOM   1268 C  CZ  . ARG A 1 153 ? -21.028 5.464   3.251   1.00 36.43 ? 258  ARG A CZ  1 
ATOM   1269 N  NH1 . ARG A 1 153 ? -21.136 4.222   2.727   1.00 31.03 ? 258  ARG A NH1 1 
ATOM   1270 N  NH2 . ARG A 1 153 ? -21.974 6.363   3.046   1.00 29.56 ? 258  ARG A NH2 1 
ATOM   1271 N  N   . VAL A 1 154 ? -14.865 8.116   1.888   1.00 13.80 ? 259  VAL A N   1 
ATOM   1272 C  CA  . VAL A 1 154 ? -14.216 9.337   1.380   1.00 13.24 ? 259  VAL A CA  1 
ATOM   1273 C  C   . VAL A 1 154 ? -15.098 10.005  0.288   1.00 13.43 ? 259  VAL A C   1 
ATOM   1274 O  O   . VAL A 1 154 ? -15.127 11.257  0.214   1.00 14.05 ? 259  VAL A O   1 
ATOM   1275 C  CB  . VAL A 1 154 ? -12.803 9.071   0.802   1.00 14.22 ? 259  VAL A CB  1 
ATOM   1276 C  CG1 . VAL A 1 154 ? -12.172 10.332  0.211   1.00 15.79 ? 259  VAL A CG1 1 
ATOM   1277 C  CG2 . VAL A 1 154 ? -11.923 8.526   1.961   1.00 18.00 ? 259  VAL A CG2 1 
ATOM   1278 N  N   . ALA A 1 155 ? -15.790 9.224   -0.555  1.00 11.84 ? 260  ALA A N   1 
ATOM   1279 C  CA  . ALA A 1 155 ? -16.602 9.846   -1.655  1.00 12.57 ? 260  ALA A CA  1 
ATOM   1280 C  C   . ALA A 1 155 ? -17.652 10.822  -1.096  1.00 12.32 ? 260  ALA A C   1 
ATOM   1281 O  O   . ALA A 1 155 ? -17.761 11.914  -1.671  1.00 11.33 ? 260  ALA A O   1 
ATOM   1282 C  CB  . ALA A 1 155 ? -17.209 8.762   -2.560  1.00 10.69 ? 260  ALA A CB  1 
ATOM   1283 N  N   . PRO A 1 156 ? -18.402 10.506  -0.025  1.00 11.14 ? 261  PRO A N   1 
ATOM   1284 C  CA  . PRO A 1 156 ? -19.354 11.517  0.480   1.00 11.22 ? 261  PRO A CA  1 
ATOM   1285 C  C   . PRO A 1 156 ? -18.693 12.788  0.934   1.00 10.59 ? 261  PRO A C   1 
ATOM   1286 O  O   . PRO A 1 156 ? -19.372 13.860  0.850   1.00 11.11 ? 261  PRO A O   1 
ATOM   1287 C  CB  . PRO A 1 156 ? -20.083 10.766  1.637   1.00 12.14 ? 261  PRO A CB  1 
ATOM   1288 C  CG  . PRO A 1 156 ? -19.989 9.295   1.181   1.00 12.80 ? 261  PRO A CG  1 
ATOM   1289 C  CD  . PRO A 1 156 ? -18.584 9.177   0.670   1.00 11.51 ? 261  PRO A CD  1 
ATOM   1290 N  N   . VAL A 1 157 ? -17.462 12.723  1.409   1.00 8.88  ? 262  VAL A N   1 
ATOM   1291 C  CA  . VAL A 1 157 ? -16.779 13.977  1.849   1.00 10.07 ? 262  VAL A CA  1 
ATOM   1292 C  C   . VAL A 1 157 ? -16.463 14.836  0.601   1.00 9.46  ? 262  VAL A C   1 
ATOM   1293 O  O   . VAL A 1 157 ? -16.680 16.049  0.584   1.00 9.97  ? 262  VAL A O   1 
ATOM   1294 C  CB  . VAL A 1 157 ? -15.493 13.700  2.655   1.00 10.58 ? 262  VAL A CB  1 
ATOM   1295 C  CG1 . VAL A 1 157 ? -14.883 15.011  3.152   1.00 12.12 ? 262  VAL A CG1 1 
ATOM   1296 C  CG2 . VAL A 1 157 ? -15.771 12.730  3.828   1.00 12.48 ? 262  VAL A CG2 1 
ATOM   1297 N  N   . LEU A 1 158 ? -15.968 14.211  -0.484  1.00 9.23  ? 263  LEU A N   1 
ATOM   1298 C  CA  . LEU A 1 158 ? -15.716 14.948  -1.742  1.00 9.36  ? 263  LEU A CA  1 
ATOM   1299 C  C   . LEU A 1 158 ? -17.032 15.482  -2.289  1.00 8.89  ? 263  LEU A C   1 
ATOM   1300 O  O   . LEU A 1 158 ? -17.021 16.637  -2.764  1.00 9.28  ? 263  LEU A O   1 
ATOM   1301 C  CB  . LEU A 1 158 ? -15.110 13.929  -2.778  1.00 9.97  ? 263  LEU A CB  1 
ATOM   1302 C  CG  . LEU A 1 158 ? -13.602 13.740  -2.686  1.00 10.86 ? 263  LEU A CG  1 
ATOM   1303 C  CD1 . LEU A 1 158 ? -13.194 12.388  -3.412  1.00 12.79 ? 263  LEU A CD1 1 
ATOM   1304 C  CD2 . LEU A 1 158 ? -12.795 14.842  -3.360  1.00 13.53 ? 263  LEU A CD2 1 
ATOM   1305 N  N   . ILE A 1 159 ? -18.163 14.788  -2.183  1.00 8.71  ? 264  ILE A N   1 
ATOM   1306 C  CA  . ILE A 1 159 ? -19.430 15.269  -2.733  1.00 8.89  ? 264  ILE A CA  1 
ATOM   1307 C  C   . ILE A 1 159 ? -19.896 16.476  -1.898  1.00 8.87  ? 264  ILE A C   1 
ATOM   1308 O  O   . ILE A 1 159 ? -20.291 17.513  -2.442  1.00 9.36  ? 264  ILE A O   1 
ATOM   1309 C  CB  . ILE A 1 159 ? -20.446 14.129  -2.812  1.00 9.60  ? 264  ILE A CB  1 
ATOM   1310 C  CG1 . ILE A 1 159 ? -20.031 13.088  -3.866  1.00 10.85 ? 264  ILE A CG1 1 
ATOM   1311 C  CG2 . ILE A 1 159 ? -21.834 14.697  -3.112  1.00 10.25 ? 264  ILE A CG2 1 
ATOM   1312 C  CD1 . ILE A 1 159 ? -20.814 11.747  -3.735  1.00 10.47 ? 264  ILE A CD1 1 
ATOM   1313 N  N   . ARG A 1 160 ? -19.846 16.357  -0.557  1.00 9.08  ? 265  ARG A N   1 
ATOM   1314 C  CA  . ARG A 1 160 ? -20.261 17.507  0.279   1.00 9.00  ? 265  ARG A CA  1 
ATOM   1315 C  C   . ARG A 1 160 ? -19.334 18.694  0.067   1.00 8.08  ? 265  ARG A C   1 
ATOM   1316 O  O   . ARG A 1 160 ? -19.888 19.832  0.034   1.00 8.86  ? 265  ARG A O   1 
ATOM   1317 C  CB  . ARG A 1 160 ? -20.223 17.072  1.816   1.00 11.06 ? 265  ARG A CB  1 
ATOM   1318 C  CG  . ARG A 1 160 ? -21.327 16.136  2.181   1.00 13.77 ? 265  ARG A CG  1 
ATOM   1319 C  CD  . ARG A 1 160 ? -21.276 16.041  3.729   1.00 14.37 ? 265  ARG A CD  1 
ATOM   1320 N  NE  . ARG A 1 160 ? -20.143 15.397  4.443   1.00 18.90 ? 265  ARG A NE  1 
ATOM   1321 C  CZ  . ARG A 1 160 ? -20.049 14.062  4.619   1.00 18.72 ? 265  ARG A CZ  1 
ATOM   1322 N  NH1 . ARG A 1 160 ? -19.100 13.537  5.419   1.00 22.57 ? 265  ARG A NH1 1 
ATOM   1323 N  NH2 . ARG A 1 160 ? -20.961 13.286  3.999   1.00 19.81 ? 265  ARG A NH2 1 
ATOM   1324 N  N   . GLU A 1 161 ? -18.024 18.484  -0.103  1.00 8.72  ? 266  GLU A N   1 
ATOM   1325 C  CA  . GLU A 1 161 ? -17.119 19.605  -0.275  1.00 8.56  ? 266  GLU A CA  1 
ATOM   1326 C  C   . GLU A 1 161 ? -17.345 20.319  -1.606  1.00 8.40  ? 266  GLU A C   1 
ATOM   1327 O  O   . GLU A 1 161 ? -17.392 21.566  -1.664  1.00 8.63  ? 266  GLU A O   1 
ATOM   1328 C  CB  . GLU A 1 161 ? -15.700 19.188  -0.095  1.00 9.15  ? 266  GLU A CB  1 
ATOM   1329 C  CG  . GLU A 1 161 ? -14.669 20.274  -0.210  1.00 9.34  ? 266  GLU A CG  1 
ATOM   1330 C  CD  . GLU A 1 161 ? -14.787 21.432  0.803   1.00 9.20  ? 266  GLU A CD  1 
ATOM   1331 O  OE1 . GLU A 1 161 ? -15.574 21.344  1.800   1.00 9.93  ? 266  GLU A OE1 1 
ATOM   1332 O  OE2 . GLU A 1 161 ? -14.056 22.415  0.606   1.00 9.53  ? 266  GLU A OE2 1 
ATOM   1333 N  N   . ILE A 1 162 ? -17.564 19.585  -2.737  1.00 8.44  ? 267  ILE A N   1 
ATOM   1334 C  CA  . ILE A 1 162 ? -17.812 20.291  -3.985  1.00 7.84  ? 267  ILE A CA  1 
ATOM   1335 C  C   . ILE A 1 162 ? -19.192 20.962  -3.854  1.00 7.85  ? 267  ILE A C   1 
ATOM   1336 O  O   . ILE A 1 162 ? -19.370 22.050  -4.437  1.00 8.11  ? 267  ILE A O   1 
ATOM   1337 C  CB  . ILE A 1 162 ? -17.666 19.324  -5.221  1.00 7.59  ? 267  ILE A CB  1 
ATOM   1338 C  CG1 . ILE A 1 162 ? -17.464 20.151  -6.507  1.00 8.70  ? 267  ILE A CG1 1 
ATOM   1339 C  CG2 . ILE A 1 162 ? -18.911 18.428  -5.426  1.00 9.41  ? 267  ILE A CG2 1 
ATOM   1340 C  CD1 . ILE A 1 162 ? -16.150 20.953  -6.541  1.00 9.88  ? 267  ILE A CD1 1 
ATOM   1341 N  N   . THR A 1 163 ? -20.169 20.333  -3.186  1.00 8.06  ? 268  THR A N   1 
ATOM   1342 C  CA  . THR A 1 163 ? -21.459 21.001  -3.024  1.00 8.72  ? 268  THR A CA  1 
ATOM   1343 C  C   . THR A 1 163 ? -21.306 22.333  -2.319  1.00 8.52  ? 268  THR A C   1 
ATOM   1344 O  O   . THR A 1 163 ? -21.897 23.321  -2.782  1.00 8.22  ? 268  THR A O   1 
ATOM   1345 C  CB  . THR A 1 163 ? -22.412 20.110  -2.229  1.00 8.36  ? 268  THR A CB  1 
ATOM   1346 O  OG1 . THR A 1 163 ? -22.642 18.873  -2.945  1.00 10.27 ? 268  THR A OG1 1 
ATOM   1347 C  CG2 . THR A 1 163 ? -23.755 20.772  -2.068  1.00 9.53  ? 268  THR A CG2 1 
ATOM   1348 N  N   . ARG A 1 164 ? -20.561 22.383  -1.212  1.00 8.39  ? 269  ARG A N   1 
ATOM   1349 C  CA  . ARG A 1 164 ? -20.322 23.627  -0.501  1.00 8.05  ? 269  ARG A CA  1 
ATOM   1350 C  C   . ARG A 1 164 ? -19.716 24.655  -1.410  1.00 8.73  ? 269  ARG A C   1 
ATOM   1351 O  O   . ARG A 1 164 ? -20.115 25.856  -1.378  1.00 8.74  ? 269  ARG A O   1 
ATOM   1352 C  CB  . ARG A 1 164 ? -19.472 23.239  0.715   1.00 8.30  ? 269  ARG A CB  1 
ATOM   1353 C  CG  . ARG A 1 164 ? -19.329 24.383  1.768   1.00 8.94  ? 269  ARG A CG  1 
ATOM   1354 C  CD  . ARG A 1 164 ? -18.202 23.981  2.760   1.00 9.79  ? 269  ARG A CD  1 
ATOM   1355 N  NE  . ARG A 1 164 ? -16.858 23.953  2.219   1.00 9.27  ? 269  ARG A NE  1 
ATOM   1356 C  CZ  . ARG A 1 164 ? -16.139 25.048  2.069   1.00 8.76  ? 269  ARG A CZ  1 
ATOM   1357 N  NH1 . ARG A 1 164 ? -16.605 26.262  2.427   1.00 10.41 ? 269  ARG A NH1 1 
ATOM   1358 N  NH2 . ARG A 1 164 ? -14.907 24.947  1.580   1.00 11.14 ? 269  ARG A NH2 1 
ATOM   1359 N  N   . ARG A 1 165 ? -18.613 24.275  -2.140  1.00 8.71  ? 270  ARG A N   1 
ATOM   1360 C  CA  . ARG A 1 165 ? -17.954 25.268  -2.997  1.00 7.82  ? 270  ARG A CA  1 
ATOM   1361 C  C   . ARG A 1 165 ? -18.829 25.750  -4.105  1.00 8.31  ? 270  ARG A C   1 
ATOM   1362 O  O   . ARG A 1 165 ? -18.636 26.888  -4.597  1.00 8.98  ? 270  ARG A O   1 
ATOM   1363 C  CB  . ARG A 1 165 ? -16.644 24.596  -3.579  1.00 8.18  ? 270  ARG A CB  1 
ATOM   1364 C  CG  . ARG A 1 165 ? -15.619 24.259  -2.478  1.00 9.16  ? 270  ARG A CG  1 
ATOM   1365 C  CD  . ARG A 1 165 ? -14.395 23.618  -3.101  1.00 10.64 ? 270  ARG A CD  1 
ATOM   1366 N  NE  . ARG A 1 165 ? -13.487 23.115  -2.040  1.00 10.34 ? 270  ARG A NE  1 
ATOM   1367 C  CZ  . ARG A 1 165 ? -12.290 22.739  -2.246  1.00 12.75 ? 270  ARG A CZ  1 
ATOM   1368 N  NH1 . ARG A 1 165 ? -11.721 22.855  -3.457  1.00 14.66 ? 270  ARG A NH1 1 
ATOM   1369 N  NH2 . ARG A 1 165 ? -11.580 22.193  -1.263  1.00 14.49 ? 270  ARG A NH2 1 
ATOM   1370 N  N   . VAL A 1 166 ? -19.768 24.940  -4.591  1.00 8.11  ? 271  VAL A N   1 
ATOM   1371 C  CA  . VAL A 1 166 ? -20.687 25.411  -5.624  1.00 9.09  ? 271  VAL A CA  1 
ATOM   1372 C  C   . VAL A 1 166 ? -21.719 26.353  -4.952  1.00 9.18  ? 271  VAL A C   1 
ATOM   1373 O  O   . VAL A 1 166 ? -22.070 27.401  -5.548  1.00 9.03  ? 271  VAL A O   1 
ATOM   1374 C  CB  . VAL A 1 166 ? -21.304 24.169  -6.353  1.00 8.30  ? 271  VAL A CB  1 
ATOM   1375 C  CG1 . VAL A 1 166 ? -22.502 24.581  -7.223  1.00 9.07  ? 271  VAL A CG1 1 
ATOM   1376 C  CG2 . VAL A 1 166 ? -20.276 23.429  -7.176  1.00 9.04  ? 271  VAL A CG2 1 
ATOM   1377 N  N   . HIS A 1 167 ? -22.221 25.966  -3.793  1.00 8.69  ? 272  HIS A N   1 
ATOM   1378 C  CA  . HIS A 1 167 ? -23.168 26.888  -3.093  1.00 8.62  ? 272  HIS A CA  1 
ATOM   1379 C  C   . HIS A 1 167 ? -22.529 28.238  -2.821  1.00 8.74  ? 272  HIS A C   1 
ATOM   1380 O  O   . HIS A 1 167 ? -23.263 29.267  -2.921  1.00 10.50 ? 272  HIS A O   1 
ATOM   1381 C  CB  . HIS A 1 167 ? -23.478 26.235  -1.698  1.00 9.55  ? 272  HIS A CB  1 
ATOM   1382 C  CG  . HIS A 1 167 ? -24.468 25.141  -1.780  1.00 9.40  ? 272  HIS A CG  1 
ATOM   1383 N  ND1 . HIS A 1 167 ? -24.730 24.314  -0.685  1.00 9.73  ? 272  HIS A ND1 1 
ATOM   1384 C  CD2 . HIS A 1 167 ? -25.265 24.689  -2.783  1.00 9.19  ? 272  HIS A CD2 1 
ATOM   1385 C  CE1 . HIS A 1 167 ? -25.669 23.437  -1.018  1.00 10.00 ? 272  HIS A CE1 1 
ATOM   1386 N  NE2 . HIS A 1 167 ? -26.024 23.639  -2.298  1.00 10.26 ? 272  HIS A NE2 1 
ATOM   1387 N  N   . LEU A 1 168 ? -21.263 28.356  -2.544  1.00 8.94  ? 273  LEU A N   1 
ATOM   1388 C  CA  . LEU A 1 168 ? -20.661 29.677  -2.300  1.00 8.32  ? 273  LEU A CA  1 
ATOM   1389 C  C   . LEU A 1 168 ? -20.764 30.558  -3.523  1.00 9.72  ? 273  LEU A C   1 
ATOM   1390 O  O   . LEU A 1 168 ? -20.741 31.799  -3.376  1.00 10.74 ? 273  LEU A O   1 
ATOM   1391 C  CB  . LEU A 1 168 ? -19.175 29.510  -1.949  1.00 9.03  ? 273  LEU A CB  1 
ATOM   1392 C  CG  . LEU A 1 168 ? -18.906 28.882  -0.554  1.00 9.69  ? 273  LEU A CG  1 
ATOM   1393 C  CD1 . LEU A 1 168 ? -17.424 28.609  -0.435  1.00 12.12 ? 273  LEU A CD1 1 
ATOM   1394 C  CD2 . LEU A 1 168 ? -19.322 29.885  0.575   1.00 11.85 ? 273  LEU A CD2 1 
ATOM   1395 N  N   . GLU A 1 169 ? -20.839 29.954  -4.727  1.00 9.03  ? 274  GLU A N   1 
ATOM   1396 C  CA  . GLU A 1 169 ? -20.923 30.707  -5.981  1.00 11.08 ? 274  GLU A CA  1 
ATOM   1397 C  C   . GLU A 1 169 ? -22.414 30.907  -6.275  1.00 10.47 ? 274  GLU A C   1 
ATOM   1398 O  O   . GLU A 1 169 ? -22.679 31.436  -7.429  1.00 13.53 ? 274  GLU A O   1 
ATOM   1399 C  CB  . GLU A 1 169 ? -20.203 29.946  -7.110  1.00 11.79 ? 274  GLU A CB  1 
ATOM   1400 C  CG  . GLU A 1 169 ? -18.744 29.862  -6.848  1.00 13.20 ? 274  GLU A CG  1 
ATOM   1401 C  CD  . GLU A 1 169 ? -17.997 31.183  -6.887  1.00 18.88 ? 274  GLU A CD  1 
ATOM   1402 O  OE1 . GLU A 1 169 ? -18.488 32.076  -7.633  1.00 20.44 ? 274  GLU A OE1 1 
ATOM   1403 O  OE2 . GLU A 1 169 ? -16.940 31.122  -6.237  1.00 25.53 ? 274  GLU A OE2 1 
ATOM   1404 N  N   . GLY A 1 170 ? -23.380 30.567  -5.458  1.00 11.91 ? 275  GLY A N   1 
ATOM   1405 C  CA  . GLY A 1 170 ? -24.797 30.903  -5.674  1.00 12.69 ? 275  GLY A CA  1 
ATOM   1406 C  C   . GLY A 1 170 ? -25.581 29.924  -6.549  1.00 15.12 ? 275  GLY A C   1 
ATOM   1407 O  O   . GLY A 1 170 ? -26.647 30.291  -7.063  1.00 16.52 ? 275  GLY A O   1 
ATOM   1408 N  N   . ILE A 1 171 ? -25.017 28.712  -6.712  1.00 11.10 ? 276  ILE A N   1 
ATOM   1409 C  CA  . ILE A 1 171 ? -25.639 27.663  -7.571  1.00 10.06 ? 276  ILE A CA  1 
ATOM   1410 C  C   . ILE A 1 171 ? -26.181 26.601  -6.661  1.00 9.32  ? 276  ILE A C   1 
ATOM   1411 O  O   . ILE A 1 171 ? -25.437 26.091  -5.776  1.00 9.36  ? 276  ILE A O   1 
ATOM   1412 C  CB  . ILE A 1 171 ? -24.622 27.163  -8.550  1.00 9.55  ? 276  ILE A CB  1 
ATOM   1413 C  CG1 . ILE A 1 171 ? -24.236 28.344  -9.549  1.00 11.27 ? 276  ILE A CG1 1 
ATOM   1414 C  CG2 . ILE A 1 171 ? -25.160 25.943  -9.344  1.00 10.82 ? 276  ILE A CG2 1 
ATOM   1415 C  CD1 . ILE A 1 171 ? -23.012 27.966  -10.459 1.00 13.72 ? 276  ILE A CD1 1 
ATOM   1416 N  N   . PHE A 1 172 ? -27.411 26.138  -6.894  1.00 9.74  ? 277  PHE A N   1 
ATOM   1417 C  CA  . PHE A 1 172 ? -28.111 25.217  -5.991  1.00 10.49 ? 277  PHE A CA  1 
ATOM   1418 C  C   . PHE A 1 172 ? -28.625 23.946  -6.644  1.00 9.81  ? 277  PHE A C   1 
ATOM   1419 O  O   . PHE A 1 172 ? -29.209 23.101  -5.974  1.00 10.36 ? 277  PHE A O   1 
ATOM   1420 C  CB  . PHE A 1 172 ? -29.234 25.957  -5.191  1.00 11.76 ? 277  PHE A CB  1 
ATOM   1421 C  CG  . PHE A 1 172 ? -28.645 27.035  -4.285  1.00 13.21 ? 277  PHE A CG  1 
ATOM   1422 C  CD1 . PHE A 1 172 ? -28.015 26.589  -3.072  1.00 15.89 ? 277  PHE A CD1 1 
ATOM   1423 C  CD2 . PHE A 1 172 ? -28.421 28.374  -4.781  1.00 15.64 ? 277  PHE A CD2 1 
ATOM   1424 C  CE1 . PHE A 1 172 ? -27.383 27.570  -2.284  1.00 19.09 ? 277  PHE A CE1 1 
ATOM   1425 C  CE2 . PHE A 1 172 ? -27.760 29.362  -3.950  1.00 17.22 ? 277  PHE A CE2 1 
ATOM   1426 C  CZ  . PHE A 1 172 ? -27.192 28.875  -2.756  1.00 19.62 ? 277  PHE A CZ  1 
ATOM   1427 N  N   . GLN A 1 173 ? -28.370 23.744  -7.957  1.00 10.53 ? 278  GLN A N   1 
ATOM   1428 C  CA  . GLN A 1 173 ? -28.703 22.510  -8.687  1.00 9.93  ? 278  GLN A CA  1 
ATOM   1429 C  C   . GLN A 1 173 ? -27.475 22.005  -9.429  1.00 9.16  ? 278  GLN A C   1 
ATOM   1430 O  O   . GLN A 1 173 ? -26.585 22.800  -9.821  1.00 10.60 ? 278  GLN A O   1 
ATOM   1431 C  CB  . GLN A 1 173 ? -29.843 22.783  -9.689  1.00 11.04 ? 278  GLN A CB  1 
ATOM   1432 C  CG  . GLN A 1 173 ? -31.249 22.815  -9.042  1.00 12.27 ? 278  GLN A CG  1 
ATOM   1433 C  CD  . GLN A 1 173 ? -31.573 24.114  -8.317  1.00 11.98 ? 278  GLN A CD  1 
ATOM   1434 O  OE1 . GLN A 1 173 ? -31.098 25.206  -8.642  1.00 14.09 ? 278  GLN A OE1 1 
ATOM   1435 N  NE2 . GLN A 1 173 ? -32.373 23.981  -7.246  1.00 11.83 ? 278  GLN A NE2 1 
ATOM   1436 N  N   . ALA A 1 174 ? -27.453 20.714  -9.657  1.00 9.34  ? 279  ALA A N   1 
ATOM   1437 C  CA  . ALA A 1 174 ? -26.402 20.040  -10.462 1.00 9.03  ? 279  ALA A CA  1 
ATOM   1438 C  C   . ALA A 1 174 ? -26.949 18.967  -11.315 1.00 9.60  ? 279  ALA A C   1 
ATOM   1439 O  O   . ALA A 1 174 ? -28.060 18.418  -11.021 1.00 9.89  ? 279  ALA A O   1 
ATOM   1440 C  CB  . ALA A 1 174 ? -25.276 19.483  -9.598  1.00 9.13  ? 279  ALA A CB  1 
ATOM   1441 N  N   . VAL A 1 175 ? -26.244 18.607  -12.382 1.00 9.23  ? 280  VAL A N   1 
ATOM   1442 C  CA  . VAL A 1 175 ? -26.542 17.430  -13.176 1.00 9.52  ? 280  VAL A CA  1 
ATOM   1443 C  C   . VAL A 1 175 ? -25.333 16.542  -13.160 1.00 8.79  ? 280  VAL A C   1 
ATOM   1444 O  O   . VAL A 1 175 ? -24.165 17.010  -13.142 1.00 9.79  ? 280  VAL A O   1 
ATOM   1445 C  CB  . VAL A 1 175 ? -26.972 17.791  -14.605 1.00 9.60  ? 280  VAL A CB  1 
ATOM   1446 C  CG1 . VAL A 1 175 ? -25.891 18.529  -15.408 1.00 12.04 ? 280  VAL A CG1 1 
ATOM   1447 C  CG2 . VAL A 1 175 ? -27.465 16.590  -15.368 1.00 11.75 ? 280  VAL A CG2 1 
ATOM   1448 N  N   . TYR A 1 176 ? -25.499 15.217  -13.181 1.00 9.95  ? 281  TYR A N   1 
ATOM   1449 C  CA  . TYR A 1 176 ? -24.394 14.273  -13.155 1.00 10.43 ? 281  TYR A CA  1 
ATOM   1450 C  C   . TYR A 1 176 ? -24.911 12.945  -13.744 1.00 11.00 ? 281  TYR A C   1 
ATOM   1451 O  O   . TYR A 1 176 ? -26.114 12.662  -13.731 1.00 11.56 ? 281  TYR A O   1 
ATOM   1452 C  CB  . TYR A 1 176 ? -23.825 14.131  -11.714 1.00 11.24 ? 281  TYR A CB  1 
ATOM   1453 C  CG  . TYR A 1 176 ? -24.826 13.846  -10.613 1.00 11.49 ? 281  TYR A CG  1 
ATOM   1454 C  CD1 . TYR A 1 176 ? -24.932 12.549  -10.077 1.00 10.67 ? 281  TYR A CD1 1 
ATOM   1455 C  CD2 . TYR A 1 176 ? -25.635 14.894  -10.070 1.00 12.62 ? 281  TYR A CD2 1 
ATOM   1456 C  CE1 . TYR A 1 176 ? -25.806 12.299  -9.032  1.00 12.20 ? 281  TYR A CE1 1 
ATOM   1457 C  CE2 . TYR A 1 176 ? -26.537 14.619  -9.063  1.00 13.53 ? 281  TYR A CE2 1 
ATOM   1458 C  CZ  . TYR A 1 176 ? -26.626 13.344  -8.552  1.00 13.00 ? 281  TYR A CZ  1 
ATOM   1459 O  OH  . TYR A 1 176 ? -27.599 13.141  -7.554  1.00 15.59 ? 281  TYR A OH  1 
ATOM   1460 N  N   . THR A 1 177 ? -23.954 12.136  -14.166 1.00 11.32 ? 282  THR A N   1 
ATOM   1461 C  CA  . THR A 1 177 ? -24.214 10.744  -14.664 1.00 11.01 ? 282  THR A CA  1 
ATOM   1462 C  C   . THR A 1 177 ? -23.332 9.823   -13.868 1.00 15.16 ? 282  THR A C   1 
ATOM   1463 O  O   . THR A 1 177 ? -22.256 10.174  -13.364 1.00 14.56 ? 282  THR A O   1 
ATOM   1464 C  CB  . THR A 1 177 ? -23.922 10.603  -16.173 1.00 12.26 ? 282  THR A CB  1 
ATOM   1465 O  OG1 . THR A 1 177 ? -22.505 10.846  -16.439 1.00 13.66 ? 282  THR A OG1 1 
ATOM   1466 C  CG2 . THR A 1 177 ? -24.757 11.523  -17.022 1.00 13.04 ? 282  THR A CG2 1 
ATOM   1467 N  N   . ALA A 1 178 ? -23.796 8.562   -13.765 1.00 12.95 ? 283  ALA A N   1 
ATOM   1468 C  CA  . ALA A 1 178 ? -23.030 7.480   -13.155 1.00 13.53 ? 283  ALA A CA  1 
ATOM   1469 C  C   . ALA A 1 178 ? -23.587 6.173   -13.609 1.00 13.69 ? 283  ALA A C   1 
ATOM   1470 O  O   . ALA A 1 178 ? -24.751 6.038   -13.982 1.00 13.58 ? 283  ALA A O   1 
ATOM   1471 C  CB  . ALA A 1 178 ? -23.087 7.544   -11.610 1.00 15.23 ? 283  ALA A CB  1 
ATOM   1472 N  N   . GLY A 1 179 ? -22.679 5.172   -13.569 1.00 13.93 ? 284  GLY A N   1 
ATOM   1473 C  CA  . GLY A 1 179 ? -23.137 3.761   -13.931 1.00 14.45 ? 284  GLY A CA  1 
ATOM   1474 C  C   . GLY A 1 179 ? -23.854 3.113   -12.786 1.00 17.94 ? 284  GLY A C   1 
ATOM   1475 O  O   . GLY A 1 179 ? -24.494 2.079   -13.047 1.00 24.58 ? 284  GLY A O   1 
ATOM   1476 N  N   . VAL A 1 180 ? -23.855 3.649   -11.578 1.00 18.13 ? 285  VAL A N   1 
ATOM   1477 C  CA  . VAL A 1 180 ? -24.594 3.041   -10.451 1.00 18.47 ? 285  VAL A CA  1 
ATOM   1478 C  C   . VAL A 1 180 ? -25.943 3.657   -10.168 1.00 18.40 ? 285  VAL A C   1 
ATOM   1479 O  O   . VAL A 1 180 ? -26.195 4.824   -10.552 1.00 16.58 ? 285  VAL A O   1 
ATOM   1480 C  CB  . VAL A 1 180 ? -23.703 3.054   -9.224  1.00 21.69 ? 285  VAL A CB  1 
ATOM   1481 C  CG1 . VAL A 1 180 ? -22.450 2.243   -9.548  1.00 26.05 ? 285  VAL A CG1 1 
ATOM   1482 C  CG2 . VAL A 1 180 ? -23.388 4.471   -8.742  1.00 21.83 ? 285  VAL A CG2 1 
ATOM   1483 N  N   . VAL A 1 181 ? -26.895 2.888   -9.611  1.00 16.78 ? 286  VAL A N   1 
ATOM   1484 C  CA  . VAL A 1 181 ? -28.175 3.369   -9.211  1.00 17.32 ? 286  VAL A CA  1 
ATOM   1485 C  C   . VAL A 1 181 ? -28.125 4.033   -7.870  1.00 18.95 ? 286  VAL A C   1 
ATOM   1486 O  O   . VAL A 1 181 ? -27.710 3.401   -6.840  1.00 21.23 ? 286  VAL A O   1 
ATOM   1487 C  CB  . VAL A 1 181 ? -29.234 2.200   -9.180  1.00 19.98 ? 286  VAL A CB  1 
ATOM   1488 C  CG1 . VAL A 1 181 ? -30.580 2.688   -8.659  1.00 19.50 ? 286  VAL A CG1 1 
ATOM   1489 C  CG2 . VAL A 1 181 ? -29.373 1.575   -10.555 1.00 21.50 ? 286  VAL A CG2 1 
ATOM   1490 N  N   . LEU A 1 182 ? -28.543 5.281   -7.822  1.00 17.40 ? 287  LEU A N   1 
ATOM   1491 C  CA  . LEU A 1 182 ? -28.652 6.192   -6.635  1.00 17.54 ? 287  LEU A CA  1 
ATOM   1492 C  C   . LEU A 1 182 ? -30.006 6.812   -6.615  1.00 15.91 ? 287  LEU A C   1 
ATOM   1493 O  O   . LEU A 1 182 ? -30.658 6.893   -7.687  1.00 15.57 ? 287  LEU A O   1 
ATOM   1494 C  CB  . LEU A 1 182 ? -27.585 7.287   -6.744  1.00 17.71 ? 287  LEU A CB  1 
ATOM   1495 C  CG  . LEU A 1 182 ? -26.143 6.878   -7.074  1.00 16.61 ? 287  LEU A CG  1 
ATOM   1496 C  CD1 . LEU A 1 182 ? -25.303 8.100   -7.399  1.00 17.60 ? 287  LEU A CD1 1 
ATOM   1497 C  CD2 . LEU A 1 182 ? -25.474 6.116   -5.904  1.00 18.14 ? 287  LEU A CD2 1 
ATOM   1498 N  N   . PRO A 1 183 ? -30.472 7.340   -5.479  1.00 15.07 ? 288  PRO A N   1 
ATOM   1499 C  CA  . PRO A 1 183 ? -31.666 8.147   -5.479  1.00 15.19 ? 288  PRO A CA  1 
ATOM   1500 C  C   . PRO A 1 183 ? -31.394 9.441   -6.296  1.00 16.00 ? 288  PRO A C   1 
ATOM   1501 O  O   . PRO A 1 183 ? -30.456 10.187  -5.951  1.00 16.31 ? 288  PRO A O   1 
ATOM   1502 C  CB  . PRO A 1 183 ? -31.895 8.525   -3.976  1.00 16.52 ? 288  PRO A CB  1 
ATOM   1503 C  CG  . PRO A 1 183 ? -30.998 7.535   -3.260  1.00 19.78 ? 288  PRO A CG  1 
ATOM   1504 C  CD  . PRO A 1 183 ? -29.866 7.228   -4.123  1.00 19.39 ? 288  PRO A CD  1 
ATOM   1505 N  N   . LYS A 1 184 ? -32.165 9.775   -7.318  1.00 14.18 ? 289  LYS A N   1 
ATOM   1506 C  CA  . LYS A 1 184 ? -33.173 8.944   -8.049  1.00 14.52 ? 289  LYS A CA  1 
ATOM   1507 C  C   . LYS A 1 184 ? -32.924 9.301   -9.562  1.00 12.79 ? 289  LYS A C   1 
ATOM   1508 O  O   . LYS A 1 184 ? -32.949 10.483  -9.883  1.00 13.57 ? 289  LYS A O   1 
ATOM   1509 C  CB  . LYS A 1 184 ? -34.587 9.425   -7.673  1.00 15.61 ? 289  LYS A CB  1 
ATOM   1510 C  CG  . LYS A 1 184 ? -35.606 8.581   -8.469  1.00 16.98 ? 289  LYS A CG  1 
ATOM   1511 C  CD  . LYS A 1 184 ? -37.045 8.992   -8.281  1.00 20.21 ? 289  LYS A CD  1 
ATOM   1512 C  CE  . LYS A 1 184 ? -37.865 7.869   -8.986  1.00 25.81 ? 289  LYS A CE  1 
ATOM   1513 N  NZ  . LYS A 1 184 ? -39.000 8.507   -9.706  1.00 35.17 ? 289  LYS A NZ  1 
ATOM   1514 N  N   . PRO A 1 185 ? -32.721 8.315   -10.421 1.00 13.29 ? 290  PRO A N   1 
ATOM   1515 C  CA  . PRO A 1 185 ? -32.442 8.683   -11.861 1.00 11.82 ? 290  PRO A CA  1 
ATOM   1516 C  C   . PRO A 1 185 ? -33.576 9.471   -12.468 1.00 14.37 ? 290  PRO A C   1 
ATOM   1517 O  O   . PRO A 1 185 ? -34.813 9.149   -12.287 1.00 16.04 ? 290  PRO A O   1 
ATOM   1518 C  CB  . PRO A 1 185 ? -32.301 7.327   -12.564 1.00 13.82 ? 290  PRO A CB  1 
ATOM   1519 C  CG  . PRO A 1 185 ? -31.946 6.367   -11.463 1.00 16.29 ? 290  PRO A CG  1 
ATOM   1520 C  CD  . PRO A 1 185 ? -32.697 6.841   -10.250 1.00 13.96 ? 290  PRO A CD  1 
ATOM   1521 N  N   . VAL A 1 186 ? -33.215 10.521  -13.234 1.00 12.70 ? 291  VAL A N   1 
ATOM   1522 C  CA  . VAL A 1 186 ? -34.174 11.203  -14.098 1.00 13.71 ? 291  VAL A CA  1 
ATOM   1523 C  C   . VAL A 1 186 ? -34.290 10.518  -15.433 1.00 14.19 ? 291  VAL A C   1 
ATOM   1524 O  O   . VAL A 1 186 ? -35.250 10.795  -16.156 1.00 15.91 ? 291  VAL A O   1 
ATOM   1525 C  CB  . VAL A 1 186 ? -33.861 12.741  -14.205 1.00 13.59 ? 291  VAL A CB  1 
ATOM   1526 C  CG1 . VAL A 1 186 ? -32.618 13.017  -15.028 1.00 13.69 ? 291  VAL A CG1 1 
ATOM   1527 C  CG2 . VAL A 1 186 ? -35.039 13.571  -14.734 1.00 16.98 ? 291  VAL A CG2 1 
ATOM   1528 N  N   . GLY A 1 187 ? -33.290 9.739   -15.787 1.00 13.43 ? 292  GLY A N   1 
ATOM   1529 C  CA  . GLY A 1 187 ? -33.355 8.947   -17.088 1.00 14.39 ? 292  GLY A CA  1 
ATOM   1530 C  C   . GLY A 1 187 ? -32.302 7.912   -17.005 1.00 13.24 ? 292  GLY A C   1 
ATOM   1531 O  O   . GLY A 1 187 ? -31.313 8.018   -16.224 1.00 15.12 ? 292  GLY A O   1 
ATOM   1532 N  N   . THR A 1 188 ? -32.462 6.811   -17.735 1.00 13.71 ? 293  THR A N   1 
ATOM   1533 C  CA  . THR A 1 188 ? -31.600 5.663   -17.728 1.00 13.45 ? 293  THR A CA  1 
ATOM   1534 C  C   . THR A 1 188 ? -31.296 5.332   -19.166 1.00 14.33 ? 293  THR A C   1 
ATOM   1535 O  O   . THR A 1 188 ? -32.224 5.029   -19.961 1.00 16.23 ? 293  THR A O   1 
ATOM   1536 C  CB  . THR A 1 188 ? -32.317 4.433   -17.073 1.00 14.97 ? 293  THR A CB  1 
ATOM   1537 O  OG1 . THR A 1 188 ? -32.636 4.810   -15.689 1.00 16.34 ? 293  THR A OG1 1 
ATOM   1538 C  CG2 . THR A 1 188 ? -31.376 3.226   -17.044 1.00 17.10 ? 293  THR A CG2 1 
ATOM   1539 N  N   . CYS A 1 189 ? -29.987 5.302   -19.514 1.00 13.21 ? 294  CYS A N   1 
ATOM   1540 C  CA  . CYS A 1 189 ? -29.552 5.014   -20.879 1.00 13.84 ? 294  CYS A CA  1 
ATOM   1541 C  C   . CYS A 1 189 ? -28.682 3.810   -21.000 1.00 17.28 ? 294  CYS A C   1 
ATOM   1542 O  O   . CYS A 1 189 ? -27.892 3.559   -20.143 1.00 22.73 ? 294  CYS A O   1 
ATOM   1543 C  CB  . CYS A 1 189 ? -28.717 6.273   -21.345 1.00 16.35 ? 294  CYS A CB  1 
ATOM   1544 S  SG  . CYS A 1 189 ? -29.667 7.745   -21.583 1.00 17.89 ? 294  CYS A SG  1 
ATOM   1545 N  N   . ARG A 1 190 ? -28.909 2.967   -22.000 1.00 15.85 ? 295  ARG A N   1 
ATOM   1546 C  CA  . ARG A 1 190 ? -28.032 1.868   -22.258 1.00 15.30 ? 295  ARG A CA  1 
ATOM   1547 C  C   . ARG A 1 190 ? -26.933 2.296   -23.235 1.00 12.71 ? 295  ARG A C   1 
ATOM   1548 O  O   . ARG A 1 190 ? -27.288 2.981   -24.230 1.00 14.85 ? 295  ARG A O   1 
ATOM   1549 C  CB  . ARG A 1 190 ? -28.827 0.738   -22.947 1.00 19.43 ? 295  ARG A CB  1 
ATOM   1550 C  CG  . ARG A 1 190 ? -29.728 -0.089  -21.982 1.00 21.87 ? 295  ARG A CG  1 
ATOM   1551 C  CD  . ARG A 1 190 ? -29.004 -0.984  -21.009 1.00 23.31 ? 295  ARG A CD  1 
ATOM   1552 N  NE  . ARG A 1 190 ? -28.329 -2.191  -21.489 1.00 22.21 ? 295  ARG A NE  1 
ATOM   1553 C  CZ  . ARG A 1 190 ? -28.892 -3.401  -21.646 1.00 25.56 ? 295  ARG A CZ  1 
ATOM   1554 N  NH1 . ARG A 1 190 ? -30.197 -3.555  -21.474 1.00 26.39 ? 295  ARG A NH1 1 
ATOM   1555 N  NH2 . ARG A 1 190 ? -28.196 -4.421  -22.106 1.00 26.21 ? 295  ARG A NH2 1 
ATOM   1556 N  N   . TYR A 1 191 ? -25.689 1.861   -23.033 1.00 12.39 ? 296  TYR A N   1 
ATOM   1557 C  CA  . TYR A 1 191 ? -24.639 2.051   -24.030 1.00 12.77 ? 296  TYR A CA  1 
ATOM   1558 C  C   . TYR A 1 191 ? -24.601 0.868   -24.994 1.00 13.60 ? 296  TYR A C   1 
ATOM   1559 O  O   . TYR A 1 191 ? -24.811 -0.320  -24.610 1.00 15.22 ? 296  TYR A O   1 
ATOM   1560 C  CB  . TYR A 1 191 ? -23.271 2.392   -23.387 1.00 12.70 ? 296  TYR A CB  1 
ATOM   1561 C  CG  . TYR A 1 191 ? -22.912 1.619   -22.141 1.00 13.74 ? 296  TYR A CG  1 
ATOM   1562 C  CD1 . TYR A 1 191 ? -23.112 2.184   -20.882 1.00 14.85 ? 296  TYR A CD1 1 
ATOM   1563 C  CD2 . TYR A 1 191 ? -22.293 0.358   -22.208 1.00 17.27 ? 296  TYR A CD2 1 
ATOM   1564 C  CE1 . TYR A 1 191 ? -22.762 1.561   -19.653 1.00 17.76 ? 296  TYR A CE1 1 
ATOM   1565 C  CE2 . TYR A 1 191 ? -21.932 -0.346  -20.987 1.00 19.02 ? 296  TYR A CE2 1 
ATOM   1566 C  CZ  . TYR A 1 191 ? -22.193 0.296   -19.739 1.00 19.34 ? 296  TYR A CZ  1 
ATOM   1567 O  OH  . TYR A 1 191 ? -21.825 -0.304  -18.500 1.00 20.07 ? 296  TYR A OH  1 
ATOM   1568 N  N   . TRP A 1 192 ? -24.208 1.188   -26.210 1.00 11.63 ? 297  TRP A N   1 
ATOM   1569 C  CA  . TRP A 1 192 ? -24.005 0.218   -27.355 1.00 11.72 ? 297  TRP A CA  1 
ATOM   1570 C  C   . TRP A 1 192 ? -22.693 0.419   -27.963 1.00 12.91 ? 297  TRP A C   1 
ATOM   1571 O  O   . TRP A 1 192 ? -22.061 1.559   -27.814 1.00 12.35 ? 297  TRP A O   1 
ATOM   1572 C  CB  . TRP A 1 192 ? -25.091 0.542   -28.395 1.00 13.04 ? 297  TRP A CB  1 
ATOM   1573 C  CG  . TRP A 1 192 ? -26.509 0.252   -27.986 1.00 13.05 ? 297  TRP A CG  1 
ATOM   1574 C  CD1 . TRP A 1 192 ? -27.252 0.829   -27.009 1.00 13.62 ? 297  TRP A CD1 1 
ATOM   1575 C  CD2 . TRP A 1 192 ? -27.406 -0.693  -28.667 1.00 14.83 ? 297  TRP A CD2 1 
ATOM   1576 N  NE1 . TRP A 1 192 ? -28.558 0.245   -26.973 1.00 16.05 ? 297  TRP A NE1 1 
ATOM   1577 C  CE2 . TRP A 1 192 ? -28.629 -0.649  -28.031 1.00 16.10 ? 297  TRP A CE2 1 
ATOM   1578 C  CE3 . TRP A 1 192 ? -27.234 -1.540  -29.793 1.00 16.78 ? 297  TRP A CE3 1 
ATOM   1579 C  CZ2 . TRP A 1 192 ? -29.750 -1.452  -28.460 1.00 17.63 ? 297  TRP A CZ2 1 
ATOM   1580 C  CZ3 . TRP A 1 192 ? -28.284 -2.351  -30.190 1.00 17.11 ? 297  TRP A CZ3 1 
ATOM   1581 C  CH2 . TRP A 1 192 ? -29.531 -2.249  -29.557 1.00 18.46 ? 297  TRP A CH2 1 
ATOM   1582 N  N   . HIS A 1 193 ? -22.169 -0.525  -28.742 1.00 13.32 ? 298  HIS A N   1 
ATOM   1583 C  CA  . HIS A 1 193 ? -20.868 -0.423  -29.348 1.00 11.09 ? 298  HIS A CA  1 
ATOM   1584 C  C   . HIS A 1 193 ? -20.959 -0.824  -30.821 1.00 12.86 ? 298  HIS A C   1 
ATOM   1585 O  O   . HIS A 1 193 ? -21.764 -1.719  -31.123 1.00 15.84 ? 298  HIS A O   1 
ATOM   1586 C  CB  . HIS A 1 193 ? -19.824 -1.333  -28.649 1.00 13.55 ? 298  HIS A CB  1 
ATOM   1587 C  CG  . HIS A 1 193 ? -20.343 -2.712  -28.415 1.00 14.92 ? 298  HIS A CG  1 
ATOM   1588 N  ND1 . HIS A 1 193 ? -20.924 -3.090  -27.240 1.00 16.62 ? 298  HIS A ND1 1 
ATOM   1589 C  CD2 . HIS A 1 193 ? -20.401 -3.795  -29.261 1.00 16.34 ? 298  HIS A CD2 1 
ATOM   1590 C  CE1 . HIS A 1 193 ? -21.358 -4.352  -27.338 1.00 18.25 ? 298  HIS A CE1 1 
ATOM   1591 N  NE2 . HIS A 1 193 ? -21.037 -4.795  -28.545 1.00 18.96 ? 298  HIS A NE2 1 
ATOM   1592 N  N   . ARG A 1 194 ? -20.081 -0.324  -31.646 1.00 12.64 ? 299  ARG A N   1 
ATOM   1593 C  CA  . ARG A 1 194 ? -20.079 -0.677  -33.125 1.00 11.29 ? 299  ARG A CA  1 
ATOM   1594 C  C   . ARG A 1 194 ? -18.655 -1.019  -33.390 1.00 11.53 ? 299  ARG A C   1 
ATOM   1595 O  O   . ARG A 1 194 ? -17.683 -0.203  -33.362 1.00 12.90 ? 299  ARG A O   1 
ATOM   1596 C  CB  . ARG A 1 194 ? -20.588 0.543   -33.970 1.00 13.25 ? 299  ARG A CB  1 
ATOM   1597 C  CG  . ARG A 1 194 ? -21.238 0.043   -35.332 1.00 13.73 ? 299  ARG A CG  1 
ATOM   1598 C  CD  . ARG A 1 194 ? -20.187 -0.609  -36.260 1.00 14.25 ? 299  ARG A CD  1 
ATOM   1599 N  NE  . ARG A 1 194 ? -20.861 -0.836  -37.564 1.00 13.84 ? 299  ARG A NE  1 
ATOM   1600 C  CZ  . ARG A 1 194 ? -20.208 -1.332  -38.606 1.00 14.48 ? 299  ARG A CZ  1 
ATOM   1601 N  NH1 . ARG A 1 194 ? -18.955 -1.692  -38.585 1.00 13.37 ? 299  ARG A NH1 1 
ATOM   1602 N  NH2 . ARG A 1 194 ? -20.965 -1.432  -39.734 1.00 16.04 ? 299  ARG A NH2 1 
ATOM   1603 N  N   . SER A 1 195 ? -18.409 -2.328  -33.748 1.00 12.53 ? 300  SER A N   1 
ATOM   1604 C  CA  A SER A 1 195 ? -17.054 -2.811  -34.010 0.50 12.57 ? 300  SER A CA  1 
ATOM   1605 C  CA  B SER A 1 195 ? -17.118 -2.826  -34.000 0.50 12.27 ? 300  SER A CA  1 
ATOM   1606 C  C   . SER A 1 195 ? -16.479 -2.176  -35.248 1.00 12.13 ? 300  SER A C   1 
ATOM   1607 O  O   . SER A 1 195 ? -17.159 -2.173  -36.353 1.00 13.96 ? 300  SER A O   1 
ATOM   1608 C  CB  A SER A 1 195 ? -17.065 -4.342  -34.282 0.50 13.72 ? 300  SER A CB  1 
ATOM   1609 C  CB  B SER A 1 195 ? -17.323 -4.339  -34.287 0.50 12.89 ? 300  SER A CB  1 
ATOM   1610 O  OG  A SER A 1 195 ? -17.544 -4.973  -33.124 0.50 15.17 ? 300  SER A OG  1 
ATOM   1611 O  OG  B SER A 1 195 ? -16.049 -4.882  -34.429 0.50 14.12 ? 300  SER A OG  1 
ATOM   1612 N  N   . LEU A 1 196 ? -15.258 -1.691  -35.149 1.00 12.26 ? 301  LEU A N   1 
ATOM   1613 C  CA  . LEU A 1 196 ? -14.561 -1.164  -36.309 1.00 14.13 ? 301  LEU A CA  1 
ATOM   1614 C  C   . LEU A 1 196 ? -13.400 -2.034  -36.679 1.00 14.51 ? 301  LEU A C   1 
ATOM   1615 O  O   . LEU A 1 196 ? -13.101 -2.223  -37.867 1.00 18.42 ? 301  LEU A O   1 
ATOM   1616 C  CB  . LEU A 1 196 ? -14.104 0.324   -36.116 1.00 13.99 ? 301  LEU A CB  1 
ATOM   1617 C  CG  . LEU A 1 196 ? -15.240 1.267   -35.761 1.00 14.48 ? 301  LEU A CG  1 
ATOM   1618 C  CD1 . LEU A 1 196 ? -14.571 2.588   -35.394 1.00 14.57 ? 301  LEU A CD1 1 
ATOM   1619 C  CD2 . LEU A 1 196 ? -16.280 1.522   -36.846 1.00 17.45 ? 301  LEU A CD2 1 
ATOM   1620 N  N   . ASN A 1 197 ? -12.727 -2.597  -35.698 1.00 14.77 ? 302  ASN A N   1 
ATOM   1621 C  CA  . ASN A 1 197 ? -11.558 -3.493  -35.917 1.00 14.68 ? 302  ASN A CA  1 
ATOM   1622 C  C   . ASN A 1 197 ? -11.846 -4.822  -35.122 1.00 16.66 ? 302  ASN A C   1 
ATOM   1623 O  O   . ASN A 1 197 ? -11.324 -5.080  -34.025 1.00 15.17 ? 302  ASN A O   1 
ATOM   1624 C  CB  . ASN A 1 197 ? -10.356 -2.843  -35.357 1.00 16.23 ? 302  ASN A CB  1 
ATOM   1625 C  CG  . ASN A 1 197 ? -9.066  -3.647  -35.451 1.00 21.69 ? 302  ASN A CG  1 
ATOM   1626 O  OD1 . ASN A 1 197 ? -9.041  -4.815  -35.907 1.00 27.35 ? 302  ASN A OD1 1 
ATOM   1627 N  ND2 . ASN A 1 197 ? -7.956  -3.032  -34.988 1.00 23.99 ? 302  ASN A ND2 1 
ATOM   1628 N  N   . PRO A 1 198 ? -12.744 -5.698  -35.664 1.00 17.64 ? 303  PRO A N   1 
ATOM   1629 C  CA  . PRO A 1 198 ? -13.142 -6.889  -34.924 1.00 17.80 ? 303  PRO A CA  1 
ATOM   1630 C  C   . PRO A 1 198 ? -12.068 -7.860  -34.580 1.00 20.57 ? 303  PRO A C   1 
ATOM   1631 O  O   . PRO A 1 198 ? -12.194 -8.424  -33.454 1.00 19.55 ? 303  PRO A O   1 
ATOM   1632 C  CB  . PRO A 1 198 ? -14.313 -7.464  -35.775 1.00 20.50 ? 303  PRO A CB  1 
ATOM   1633 C  CG  . PRO A 1 198 ? -14.107 -6.882  -37.168 1.00 19.63 ? 303  PRO A CG  1 
ATOM   1634 C  CD  . PRO A 1 198 ? -13.538 -5.533  -36.921 1.00 17.87 ? 303  PRO A CD  1 
ATOM   1635 N  N   . ARG A 1 199 ? -11.027 -8.038  -35.392 1.00 20.83 ? 304  ARG A N   1 
ATOM   1636 C  CA  A ARG A 1 199 ? -9.883  -8.939  -35.059 0.50 23.59 ? 304  ARG A CA  1 
ATOM   1637 C  CA  B ARG A 1 199 ? -9.880  -8.934  -35.064 0.50 23.13 ? 304  ARG A CA  1 
ATOM   1638 C  C   . ARG A 1 199 ? -9.286  -8.512  -33.705 1.00 21.17 ? 304  ARG A C   1 
ATOM   1639 O  O   . ARG A 1 199 ? -9.131  -9.339  -32.809 1.00 21.06 ? 304  ARG A O   1 
ATOM   1640 C  CB  A ARG A 1 199 ? -8.774  -8.896  -36.121 0.50 26.76 ? 304  ARG A CB  1 
ATOM   1641 C  CB  B ARG A 1 199 ? -8.787  -8.867  -36.140 0.50 25.38 ? 304  ARG A CB  1 
ATOM   1642 C  CG  A ARG A 1 199 ? -7.474  -9.643  -35.761 0.50 33.51 ? 304  ARG A CG  1 
ATOM   1643 C  CG  B ARG A 1 199 ? -7.579  -9.804  -35.970 0.50 30.94 ? 304  ARG A CG  1 
ATOM   1644 C  CD  A ARG A 1 199 ? -7.134  -10.759 -36.737 0.50 37.06 ? 304  ARG A CD  1 
ATOM   1645 C  CD  B ARG A 1 199 ? -6.726  -9.766  -37.246 0.50 31.57 ? 304  ARG A CD  1 
ATOM   1646 N  NE  A ARG A 1 199 ? -7.438  -12.074 -36.186 0.50 36.46 ? 304  ARG A NE  1 
ATOM   1647 N  NE  B ARG A 1 199 ? -7.473  -10.410 -38.321 0.50 32.89 ? 304  ARG A NE  1 
ATOM   1648 C  CZ  A ARG A 1 199 ? -7.832  -13.096 -36.923 0.50 32.40 ? 304  ARG A CZ  1 
ATOM   1649 C  CZ  B ARG A 1 199 ? -7.279  -10.208 -39.624 0.50 37.89 ? 304  ARG A CZ  1 
ATOM   1650 N  NH1 A ARG A 1 199 ? -7.974  -12.953 -38.222 0.50 32.81 ? 304  ARG A NH1 1 
ATOM   1651 N  NH1 B ARG A 1 199 ? -6.383  -9.327  -40.037 0.50 32.09 ? 304  ARG A NH1 1 
ATOM   1652 N  NH2 A ARG A 1 199 ? -8.085  -14.246 -36.354 0.50 36.06 ? 304  ARG A NH2 1 
ATOM   1653 N  NH2 B ARG A 1 199 ? -8.003  -10.877 -40.517 0.50 39.25 ? 304  ARG A NH2 1 
ATOM   1654 N  N   . LYS A 1 200 ? -8.963  -7.213  -33.526 1.00 19.25 ? 305  LYS A N   1 
ATOM   1655 C  CA  . LYS A 1 200 ? -8.396  -6.757  -32.246 1.00 18.54 ? 305  LYS A CA  1 
ATOM   1656 C  C   . LYS A 1 200 ? -9.463  -6.845  -31.135 1.00 14.76 ? 305  LYS A C   1 
ATOM   1657 O  O   . LYS A 1 200 ? -9.054  -7.279  -30.001 1.00 17.63 ? 305  LYS A O   1 
ATOM   1658 C  CB  . LYS A 1 200 ? -7.886  -5.276  -32.394 1.00 17.11 ? 305  LYS A CB  1 
ATOM   1659 C  CG  . LYS A 1 200 ? -7.376  -4.691  -31.046 1.00 19.81 ? 305  LYS A CG  1 
ATOM   1660 C  CD  . LYS A 1 200 ? -6.568  -3.391  -31.249 1.00 18.61 ? 305  LYS A CD  1 
ATOM   1661 C  CE  . LYS A 1 200 ? -6.296  -2.739  -29.861 1.00 16.94 ? 305  LYS A CE  1 
ATOM   1662 N  NZ  . LYS A 1 200 ? -5.769  -1.355  -30.127 1.00 19.66 ? 305  LYS A NZ  1 
ATOM   1663 N  N   . LEU A 1 201 ? -10.741 -6.462  -31.358 1.00 15.05 ? 306  LEU A N   1 
ATOM   1664 C  CA  . LEU A 1 201 ? -11.742 -6.503  -30.316 1.00 15.81 ? 306  LEU A CA  1 
ATOM   1665 C  C   . LEU A 1 201 ? -11.938 -7.951  -29.754 1.00 17.35 ? 306  LEU A C   1 
ATOM   1666 O  O   . LEU A 1 201 ? -12.144 -8.188  -28.565 1.00 16.70 ? 306  LEU A O   1 
ATOM   1667 C  CB  . LEU A 1 201 ? -13.100 -5.977  -30.722 1.00 15.61 ? 306  LEU A CB  1 
ATOM   1668 C  CG  . LEU A 1 201 ? -13.163 -4.463  -31.116 1.00 15.96 ? 306  LEU A CG  1 
ATOM   1669 C  CD1 . LEU A 1 201 ? -14.617 -4.052  -31.490 1.00 16.73 ? 306  LEU A CD1 1 
ATOM   1670 C  CD2 . LEU A 1 201 ? -12.748 -3.580  -29.927 1.00 16.68 ? 306  LEU A CD2 1 
ATOM   1671 N  N   . ILE A 1 202 ? -11.884 -8.936  -30.668 1.00 18.91 ? 307  ILE A N   1 
ATOM   1672 C  CA  . ILE A 1 202 ? -11.996 -10.352 -30.252 1.00 19.72 ? 307  ILE A CA  1 
ATOM   1673 C  C   . ILE A 1 202 ? -10.702 -10.812 -29.571 1.00 16.99 ? 307  ILE A C   1 
ATOM   1674 O  O   . ILE A 1 202 ? -10.924 -11.439 -28.495 1.00 20.09 ? 307  ILE A O   1 
ATOM   1675 C  CB  . ILE A 1 202 ? -12.324 -11.187 -31.490 1.00 18.63 ? 307  ILE A CB  1 
ATOM   1676 C  CG1 . ILE A 1 202 ? -13.764 -10.948 -31.929 1.00 19.79 ? 307  ILE A CG1 1 
ATOM   1677 C  CG2 . ILE A 1 202 ? -12.129 -12.712 -31.162 1.00 20.54 ? 307  ILE A CG2 1 
ATOM   1678 C  CD1 . ILE A 1 202 ? -14.153 -11.544 -33.317 1.00 21.16 ? 307  ILE A CD1 1 
ATOM   1679 N  N   . GLU A 1 203 ? -9.494  -10.406 -29.990 1.00 19.36 ? 308  GLU A N   1 
ATOM   1680 C  CA  A GLU A 1 203 ? -8.189  -10.728 -29.310 0.50 20.20 ? 308  GLU A CA  1 
ATOM   1681 C  CA  B GLU A 1 203 ? -8.253  -10.750 -29.358 0.50 22.34 ? 308  GLU A CA  1 
ATOM   1682 C  C   . GLU A 1 203 ? -8.149  -10.251 -27.890 1.00 20.78 ? 308  GLU A C   1 
ATOM   1683 O  O   . GLU A 1 203 ? -7.732  -10.967 -26.994 1.00 23.35 ? 308  GLU A O   1 
ATOM   1684 C  CB  A GLU A 1 203 ? -6.917  -10.183 -29.966 0.50 17.92 ? 308  GLU A CB  1 
ATOM   1685 C  CB  B GLU A 1 203 ? -7.088  -10.356 -30.262 0.50 24.56 ? 308  GLU A CB  1 
ATOM   1686 C  CG  A GLU A 1 203 ? -5.572  -10.863 -29.558 0.50 20.19 ? 308  GLU A CG  1 
ATOM   1687 C  CG  B GLU A 1 203 ? -6.566  -11.547 -31.117 0.50 28.90 ? 308  GLU A CG  1 
ATOM   1688 C  CD  A GLU A 1 203 ? -4.825  -10.282 -28.327 0.50 20.01 ? 308  GLU A CD  1 
ATOM   1689 C  CD  B GLU A 1 203 ? -6.809  -11.528 -32.647 0.50 31.52 ? 308  GLU A CD  1 
ATOM   1690 O  OE1 A GLU A 1 203 ? -3.842  -10.905 -27.867 0.50 22.05 ? 308  GLU A OE1 1 
ATOM   1691 O  OE1 B GLU A 1 203 ? -5.871  -11.118 -33.374 0.50 29.68 ? 308  GLU A OE1 1 
ATOM   1692 O  OE2 A GLU A 1 203 ? -5.155  -9.200  -27.811 0.50 19.26 ? 308  GLU A OE2 1 
ATOM   1693 O  OE2 B GLU A 1 203 ? -7.904  -11.975 -33.147 0.50 26.62 ? 308  GLU A OE2 1 
ATOM   1694 N  N   . VAL A 1 204 ? -8.570  -9.014  -27.655 1.00 19.11 ? 309  VAL A N   1 
ATOM   1695 C  CA  . VAL A 1 204 ? -8.556  -8.424  -26.288 1.00 20.45 ? 309  VAL A CA  1 
ATOM   1696 C  C   . VAL A 1 204 ? -9.815  -8.767  -25.471 1.00 18.78 ? 309  VAL A C   1 
ATOM   1697 O  O   . VAL A 1 204 ? -9.991  -8.300  -24.300 1.00 22.00 ? 309  VAL A O   1 
ATOM   1698 C  CB  . VAL A 1 204 ? -8.274  -6.900  -26.351 1.00 18.69 ? 309  VAL A CB  1 
ATOM   1699 C  CG1 . VAL A 1 204 ? -7.041  -6.635  -27.194 1.00 20.32 ? 309  VAL A CG1 1 
ATOM   1700 C  CG2 . VAL A 1 204 ? -9.522  -6.095  -26.847 1.00 16.35 ? 309  VAL A CG2 1 
ATOM   1701 N  N   . LYS A 1 205 ? -10.744 -9.545  -26.021 1.00 17.64 ? 310  LYS A N   1 
ATOM   1702 C  CA  . LYS A 1 205 ? -11.975 -9.985  -25.412 1.00 17.63 ? 310  LYS A CA  1 
ATOM   1703 C  C   . LYS A 1 205 ? -12.921 -8.887  -24.992 1.00 18.37 ? 310  LYS A C   1 
ATOM   1704 O  O   . LYS A 1 205 ? -13.800 -9.068  -24.140 1.00 19.92 ? 310  LYS A O   1 
ATOM   1705 C  CB  . LYS A 1 205 ? -11.663 -10.893 -24.190 1.00 27.51 ? 310  LYS A CB  1 
ATOM   1706 C  CG  . LYS A 1 205 ? -10.452 -11.762 -24.482 1.00 36.72 ? 310  LYS A CG  1 
ATOM   1707 C  CD  . LYS A 1 205 ? -10.891 -13.142 -24.760 1.00 41.92 ? 310  LYS A CD  1 
ATOM   1708 C  CE  . LYS A 1 205 ? -10.639 -13.834 -23.453 1.00 42.43 ? 310  LYS A CE  1 
ATOM   1709 N  NZ  . LYS A 1 205 ? -9.823  -14.998 -23.857 1.00 54.00 ? 310  LYS A NZ  1 
ATOM   1710 N  N   . PHE A 1 206 ? -12.862 -7.797  -25.796 1.00 17.50 ? 311  PHE A N   1 
ATOM   1711 C  CA  . PHE A 1 206 ? -13.970 -6.869  -25.752 1.00 17.05 ? 311  PHE A CA  1 
ATOM   1712 C  C   . PHE A 1 206 ? -15.193 -7.488  -26.398 1.00 15.19 ? 311  PHE A C   1 
ATOM   1713 O  O   . PHE A 1 206 ? -16.295 -7.287  -25.996 1.00 17.36 ? 311  PHE A O   1 
ATOM   1714 C  CB  . PHE A 1 206 ? -13.538 -5.554  -26.526 1.00 16.33 ? 311  PHE A CB  1 
ATOM   1715 C  CG  . PHE A 1 206 ? -14.617 -4.503  -26.576 1.00 16.96 ? 311  PHE A CG  1 
ATOM   1716 C  CD1 . PHE A 1 206 ? -14.531 -3.412  -25.679 1.00 18.22 ? 311  PHE A CD1 1 
ATOM   1717 C  CD2 . PHE A 1 206 ? -15.595 -4.497  -27.558 1.00 17.20 ? 311  PHE A CD2 1 
ATOM   1718 C  CE1 . PHE A 1 206 ? -15.492 -2.377  -25.773 1.00 18.65 ? 311  PHE A CE1 1 
ATOM   1719 C  CE2 . PHE A 1 206 ? -16.617 -3.567  -27.568 1.00 19.34 ? 311  PHE A CE2 1 
ATOM   1720 C  CZ  . PHE A 1 206 ? -16.539 -2.469  -26.693 1.00 19.40 ? 311  PHE A CZ  1 
ATOM   1721 N  N   . SER A 1 207 ? -14.909 -8.230  -27.510 1.00 17.67 ? 312  SER A N   1 
ATOM   1722 C  CA  . SER A 1 207 ? -15.974 -8.916  -28.294 1.00 21.23 ? 312  SER A CA  1 
ATOM   1723 C  C   . SER A 1 207 ? -15.701 -10.407 -28.217 1.00 20.38 ? 312  SER A C   1 
ATOM   1724 O  O   . SER A 1 207 ? -14.582 -10.793 -27.892 1.00 20.56 ? 312  SER A O   1 
ATOM   1725 C  CB  . SER A 1 207 ? -15.856 -8.527  -29.797 1.00 19.32 ? 312  SER A CB  1 
ATOM   1726 O  OG  . SER A 1 207 ? -16.130 -7.119  -29.925 1.00 21.39 ? 312  SER A OG  1 
ATOM   1727 N  N   . HIS A 1 208 ? -16.706 -11.165 -28.640 1.00 23.23 ? 313  HIS A N   1 
ATOM   1728 C  CA  . HIS A 1 208 ? -16.479 -12.638 -28.856 1.00 23.82 ? 313  HIS A CA  1 
ATOM   1729 C  C   . HIS A 1 208 ? -16.856 -12.952 -30.291 1.00 24.74 ? 313  HIS A C   1 
ATOM   1730 O  O   . HIS A 1 208 ? -17.723 -12.292 -30.862 1.00 26.53 ? 313  HIS A O   1 
ATOM   1731 C  CB  . HIS A 1 208 ? -17.228 -13.542 -27.822 1.00 30.57 ? 313  HIS A CB  1 
ATOM   1732 C  CG  . HIS A 1 208 ? -18.717 -13.539 -27.954 1.00 41.91 ? 313  HIS A CG  1 
ATOM   1733 N  ND1 . HIS A 1 208 ? -19.527 -12.636 -27.288 1.00 46.73 ? 313  HIS A ND1 1 
ATOM   1734 C  CD2 . HIS A 1 208 ? -19.553 -14.333 -28.674 1.00 46.36 ? 313  HIS A CD2 1 
ATOM   1735 C  CE1 . HIS A 1 208 ? -20.795 -12.855 -27.612 1.00 52.98 ? 313  HIS A CE1 1 
ATOM   1736 N  NE2 . HIS A 1 208 ? -20.837 -13.877 -28.453 1.00 52.46 ? 313  HIS A NE2 1 
ATOM   1737 N  N   . LEU A 1 209 ? -16.191 -13.973 -30.825 1.00 24.78 ? 314  LEU A N   1 
ATOM   1738 C  CA  . LEU A 1 209 ? -16.509 -14.480 -32.172 1.00 26.61 ? 314  LEU A CA  1 
ATOM   1739 C  C   . LEU A 1 209 ? -17.772 -15.292 -32.056 1.00 25.32 ? 314  LEU A C   1 
ATOM   1740 O  O   . LEU A 1 209 ? -17.878 -16.192 -31.181 1.00 29.95 ? 314  LEU A O   1 
ATOM   1741 C  CB  . LEU A 1 209 ? -15.305 -15.338 -32.694 1.00 24.68 ? 314  LEU A CB  1 
ATOM   1742 C  CG  . LEU A 1 209 ? -15.492 -15.831 -34.169 1.00 25.30 ? 314  LEU A CG  1 
ATOM   1743 C  CD1 . LEU A 1 209 ? -15.329 -14.685 -35.189 1.00 25.45 ? 314  LEU A CD1 1 
ATOM   1744 C  CD2 . LEU A 1 209 ? -14.460 -16.906 -34.393 1.00 29.39 ? 314  LEU A CD2 1 
ATOM   1745 N  N   . SER A 1 210 ? -18.771 -14.961 -32.876 1.00 27.27 ? 315  SER A N   1 
ATOM   1746 C  CA  . SER A 1 210 ? -20.038 -15.664 -32.924 1.00 27.78 ? 315  SER A CA  1 
ATOM   1747 C  C   . SER A 1 210 ? -19.813 -17.169 -33.245 1.00 26.90 ? 315  SER A C   1 
ATOM   1748 O  O   . SER A 1 210 ? -19.020 -17.484 -34.105 1.00 25.91 ? 315  SER A O   1 
ATOM   1749 C  CB  . SER A 1 210 ? -20.964 -15.061 -33.985 1.00 28.53 ? 315  SER A CB  1 
ATOM   1750 O  OG  . SER A 1 210 ? -22.168 -15.765 -34.024 1.00 28.70 ? 315  SER A OG  1 
ATOM   1751 N  N   . ARG A 1 211 ? -20.569 -18.050 -32.575 1.00 29.03 ? 316  ARG A N   1 
ATOM   1752 C  CA  . ARG A 1 211 ? -20.565 -19.510 -32.969 1.00 28.84 ? 316  ARG A CA  1 
ATOM   1753 C  C   . ARG A 1 211 ? -21.154 -19.739 -34.345 1.00 29.39 ? 316  ARG A C   1 
ATOM   1754 O  O   . ARG A 1 211 ? -20.952 -20.829 -34.931 1.00 27.29 ? 316  ARG A O   1 
ATOM   1755 C  CB  . ARG A 1 211 ? -21.393 -20.346 -31.977 1.00 31.55 ? 316  ARG A CB  1 
ATOM   1756 C  CG  . ARG A 1 211 ? -20.893 -20.227 -30.577 1.00 38.81 ? 316  ARG A CG  1 
ATOM   1757 C  CD  . ARG A 1 211 ? -21.808 -21.078 -29.685 1.00 45.78 ? 316  ARG A CD  1 
ATOM   1758 N  NE  . ARG A 1 211 ? -23.247 -20.938 -29.969 1.00 53.94 ? 316  ARG A NE  1 
ATOM   1759 C  CZ  . ARG A 1 211 ? -24.131 -20.435 -29.110 1.00 70.09 ? 316  ARG A CZ  1 
ATOM   1760 N  NH1 . ARG A 1 211 ? -25.415 -20.348 -29.449 1.00 70.65 ? 316  ARG A NH1 1 
ATOM   1761 N  NH2 . ARG A 1 211 ? -23.731 -20.019 -27.905 1.00 73.69 ? 316  ARG A NH2 1 
ATOM   1762 N  N   . ASN A 1 212 ? -21.883 -18.759 -34.867 1.00 24.97 ? 317  ASN A N   1 
ATOM   1763 C  CA  . ASN A 1 212 ? -22.464 -18.839 -36.173 1.00 23.18 ? 317  ASN A CA  1 
ATOM   1764 C  C   . ASN A 1 212 ? -21.783 -17.997 -37.267 1.00 24.14 ? 317  ASN A C   1 
ATOM   1765 O  O   . ASN A 1 212 ? -22.420 -17.766 -38.344 1.00 21.92 ? 317  ASN A O   1 
ATOM   1766 C  CB  . ASN A 1 212 ? -23.978 -18.479 -36.144 1.00 24.65 ? 317  ASN A CB  1 
ATOM   1767 C  CG  . ASN A 1 212 ? -24.774 -19.336 -35.141 1.00 28.46 ? 317  ASN A CG  1 
ATOM   1768 O  OD1 . ASN A 1 212 ? -24.574 -20.563 -35.019 1.00 29.16 ? 317  ASN A OD1 1 
ATOM   1769 N  ND2 . ASN A 1 212 ? -25.611 -18.653 -34.319 1.00 34.49 ? 317  ASN A ND2 1 
ATOM   1770 N  N   . MET A 1 213 ? -20.562 -17.524 -36.982 1.00 23.26 ? 318  MET A N   1 
ATOM   1771 C  CA  . MET A 1 213 ? -19.827 -16.748 -38.004 1.00 20.97 ? 318  MET A CA  1 
ATOM   1772 C  C   . MET A 1 213 ? -18.405 -17.042 -37.893 1.00 18.97 ? 318  MET A C   1 
ATOM   1773 O  O   . MET A 1 213 ? -17.854 -17.071 -36.803 1.00 24.86 ? 318  MET A O   1 
ATOM   1774 C  CB  . MET A 1 213 ? -19.961 -15.213 -37.831 1.00 20.38 ? 318  MET A CB  1 
ATOM   1775 C  CG  . MET A 1 213 ? -21.347 -14.731 -38.039 1.00 23.65 ? 318  MET A CG  1 
ATOM   1776 S  SD  . MET A 1 213 ? -21.387 -12.877 -38.154 1.00 31.62 ? 318  MET A SD  1 
ATOM   1777 C  CE  . MET A 1 213 ? -20.312 -12.569 -39.412 1.00 28.69 ? 318  MET A CE  1 
ATOM   1778 N  N   . THR A 1 214 ? -17.753 -17.195 -39.027 1.00 19.05 ? 319  THR A N   1 
ATOM   1779 C  CA  . THR A 1 214 ? -16.328 -17.322 -39.021 1.00 18.27 ? 319  THR A CA  1 
ATOM   1780 C  C   . THR A 1 214 ? -15.734 -15.866 -38.799 1.00 21.69 ? 319  THR A C   1 
ATOM   1781 O  O   . THR A 1 214 ? -16.424 -14.805 -38.956 1.00 18.83 ? 319  THR A O   1 
ATOM   1782 C  CB  . THR A 1 214 ? -15.779 -17.802 -40.381 1.00 19.94 ? 319  THR A CB  1 
ATOM   1783 O  OG1 . THR A 1 214 ? -16.128 -16.890 -41.420 1.00 20.49 ? 319  THR A OG1 1 
ATOM   1784 C  CG2 . THR A 1 214 ? -16.342 -19.255 -40.771 1.00 20.60 ? 319  THR A CG2 1 
ATOM   1785 N  N   . MET A 1 215 ? -14.442 -15.841 -38.548 1.00 19.95 ? 320  MET A N   1 
ATOM   1786 C  CA  . MET A 1 215 ? -13.694 -14.552 -38.520 1.00 23.63 ? 320  MET A CA  1 
ATOM   1787 C  C   . MET A 1 215 ? -13.809 -13.838 -39.834 1.00 23.53 ? 320  MET A C   1 
ATOM   1788 O  O   . MET A 1 215 ? -14.056 -12.623 -39.828 1.00 22.17 ? 320  MET A O   1 
ATOM   1789 C  CB  . MET A 1 215 ? -12.240 -14.802 -38.118 1.00 23.77 ? 320  MET A CB  1 
ATOM   1790 C  CG  . MET A 1 215 ? -11.411 -13.522 -37.890 1.00 24.83 ? 320  MET A CG  1 
ATOM   1791 S  SD  . MET A 1 215 ? -12.065 -12.359 -36.605 1.00 28.13 ? 320  MET A SD  1 
ATOM   1792 C  CE  . MET A 1 215 ? -11.490 -13.243 -35.143 1.00 30.96 ? 320  MET A CE  1 
ATOM   1793 N  N   . GLN A 1 216 ? -13.727 -14.559 -40.996 1.00 21.38 ? 321  GLN A N   1 
ATOM   1794 C  CA  . GLN A 1 216 ? -13.836 -13.980 -42.306 1.00 23.76 ? 321  GLN A CA  1 
ATOM   1795 C  C   . GLN A 1 216 ? -15.135 -13.255 -42.432 1.00 20.73 ? 321  GLN A C   1 
ATOM   1796 O  O   . GLN A 1 216 ? -15.220 -12.116 -42.894 1.00 21.07 ? 321  GLN A O   1 
ATOM   1797 C  CB  . GLN A 1 216 ? -13.845 -15.184 -43.291 1.00 27.51 ? 321  GLN A CB  1 
ATOM   1798 C  CG  . GLN A 1 216 ? -13.634 -14.865 -44.734 1.00 34.64 ? 321  GLN A CG  1 
ATOM   1799 C  CD  . GLN A 1 216 ? -13.294 -16.139 -45.493 1.00 40.10 ? 321  GLN A CD  1 
ATOM   1800 O  OE1 . GLN A 1 216 ? -12.295 -16.839 -45.203 1.00 48.71 ? 321  GLN A OE1 1 
ATOM   1801 N  NE2 . GLN A 1 216 ? -14.155 -16.488 -46.406 1.00 28.12 ? 321  GLN A NE2 1 
ATOM   1802 N  N   . ARG A 1 217 ? -16.206 -13.890 -42.060 1.00 18.99 ? 322  ARG A N   1 
ATOM   1803 C  CA  . ARG A 1 217 ? -17.545 -13.387 -42.241 1.00 21.28 ? 322  ARG A CA  1 
ATOM   1804 C  C   . ARG A 1 217 ? -17.691 -12.129 -41.315 1.00 20.01 ? 322  ARG A C   1 
ATOM   1805 O  O   . ARG A 1 217 ? -18.421 -11.200 -41.669 1.00 18.55 ? 322  ARG A O   1 
ATOM   1806 C  CB  . ARG A 1 217 ? -18.536 -14.461 -41.748 1.00 22.50 ? 322  ARG A CB  1 
ATOM   1807 C  CG  . ARG A 1 217 ? -20.012 -14.092 -41.597 1.00 27.06 ? 322  ARG A CG  1 
ATOM   1808 C  CD  . ARG A 1 217 ? -20.575 -13.430 -42.826 1.00 30.27 ? 322  ARG A CD  1 
ATOM   1809 N  NE  . ARG A 1 217 ? -21.895 -12.891 -42.570 1.00 32.81 ? 322  ARG A NE  1 
ATOM   1810 C  CZ  . ARG A 1 217 ? -22.361 -11.783 -43.152 1.00 38.94 ? 322  ARG A CZ  1 
ATOM   1811 N  NH1 . ARG A 1 217 ? -21.592 -11.110 -43.996 1.00 45.50 ? 322  ARG A NH1 1 
ATOM   1812 N  NH2 . ARG A 1 217 ? -23.596 -11.342 -42.882 1.00 40.77 ? 322  ARG A NH2 1 
ATOM   1813 N  N   . THR A 1 218 ? -17.124 -12.230 -40.113 1.00 18.30 ? 323  THR A N   1 
ATOM   1814 C  CA  . THR A 1 218 ? -17.269 -11.109 -39.106 1.00 16.95 ? 323  THR A CA  1 
ATOM   1815 C  C   . THR A 1 218 ? -16.516 -9.909  -39.656 1.00 19.35 ? 323  THR A C   1 
ATOM   1816 O  O   . THR A 1 218 ? -17.068 -8.779  -39.553 1.00 18.23 ? 323  THR A O   1 
ATOM   1817 C  CB  . THR A 1 218 ? -16.654 -11.550 -37.797 1.00 18.63 ? 323  THR A CB  1 
ATOM   1818 O  OG1 . THR A 1 218 ? -17.392 -12.657 -37.276 1.00 19.36 ? 323  THR A OG1 1 
ATOM   1819 C  CG2 . THR A 1 218 ? -16.864 -10.391 -36.708 1.00 17.18 ? 323  THR A CG2 1 
ATOM   1820 N  N   . MET A 1 219 ? -15.333 -10.093 -40.221 1.00 18.31 ? 324  MET A N   1 
ATOM   1821 C  CA  A MET A 1 219 ? -14.616 -8.946  -40.828 0.50 19.80 ? 324  MET A CA  1 
ATOM   1822 C  CA  B MET A 1 219 ? -14.615 -8.947  -40.859 0.50 20.02 ? 324  MET A CA  1 
ATOM   1823 C  C   . MET A 1 219 ? -15.432 -8.338  -41.967 1.00 22.51 ? 324  MET A C   1 
ATOM   1824 O  O   . MET A 1 219 ? -15.555 -7.111  -42.076 1.00 19.43 ? 324  MET A O   1 
ATOM   1825 C  CB  A MET A 1 219 ? -13.140 -9.245  -41.144 0.50 22.43 ? 324  MET A CB  1 
ATOM   1826 C  CB  B MET A 1 219 ? -13.233 -9.317  -41.346 0.50 23.29 ? 324  MET A CB  1 
ATOM   1827 C  CG  A MET A 1 219 ? -12.225 -9.155  -39.919 0.50 25.16 ? 324  MET A CG  1 
ATOM   1828 C  CG  B MET A 1 219 ? -12.653 -10.436 -40.544 0.50 28.95 ? 324  MET A CG  1 
ATOM   1829 S  SD  A MET A 1 219 ? -10.499 -9.546  -40.366 0.50 36.49 ? 324  MET A SD  1 
ATOM   1830 S  SD  B MET A 1 219 ? -10.946 -10.152 -40.377 0.50 34.76 ? 324  MET A SD  1 
ATOM   1831 C  CE  A MET A 1 219 ? -10.808 -11.049 -41.303 0.50 25.97 ? 324  MET A CE  1 
ATOM   1832 C  CE  B MET A 1 219 ? -11.301 -8.753  -39.306 0.50 21.68 ? 324  MET A CE  1 
ATOM   1833 N  N   . LYS A 1 220 ? -16.100 -9.176  -42.764 1.00 19.95 ? 325  LYS A N   1 
ATOM   1834 C  CA  . LYS A 1 220 ? -16.939 -8.704  -43.797 1.00 22.55 ? 325  LYS A CA  1 
ATOM   1835 C  C   . LYS A 1 220 ? -18.235 -7.979  -43.306 1.00 21.78 ? 325  LYS A C   1 
ATOM   1836 O  O   . LYS A 1 220 ? -18.593 -6.868  -43.805 1.00 20.48 ? 325  LYS A O   1 
ATOM   1837 C  CB  . LYS A 1 220 ? -17.242 -9.889  -44.795 1.00 26.81 ? 325  LYS A CB  1 
ATOM   1838 C  CG  . LYS A 1 220 ? -17.817 -9.457  -46.132 1.00 40.15 ? 325  LYS A CG  1 
ATOM   1839 C  CD  . LYS A 1 220 ? -19.304 -9.814  -46.235 1.00 50.96 ? 325  LYS A CD  1 
ATOM   1840 C  CE  . LYS A 1 220 ? -19.605 -11.110 -47.033 1.00 58.13 ? 325  LYS A CE  1 
ATOM   1841 N  NZ  . LYS A 1 220 ? -19.770 -12.415 -46.268 1.00 59.72 ? 325  LYS A NZ  1 
ATOM   1842 N  N   . LEU A 1 221 ? -18.878 -8.528  -42.277 1.00 18.81 ? 326  LEU A N   1 
ATOM   1843 C  CA  . LEU A 1 221 ? -20.089 -7.939  -41.658 1.00 19.69 ? 326  LEU A CA  1 
ATOM   1844 C  C   . LEU A 1 221 ? -19.772 -6.444  -41.224 1.00 16.85 ? 326  LEU A C   1 
ATOM   1845 O  O   . LEU A 1 221 ? -20.576 -5.580  -41.506 1.00 20.64 ? 326  LEU A O   1 
ATOM   1846 C  CB  . LEU A 1 221 ? -20.466 -8.755  -40.435 1.00 23.20 ? 326  LEU A CB  1 
ATOM   1847 C  CG  . LEU A 1 221 ? -21.643 -8.262  -39.603 1.00 26.41 ? 326  LEU A CG  1 
ATOM   1848 C  CD1 . LEU A 1 221 ? -22.970 -8.361  -40.366 1.00 27.99 ? 326  LEU A CD1 1 
ATOM   1849 C  CD2 . LEU A 1 221 ? -21.649 -8.986  -38.260 1.00 29.86 ? 326  LEU A CD2 1 
ATOM   1850 N  N   . TYR A 1 222 ? -18.627 -6.236  -40.629 1.00 16.56 ? 327  TYR A N   1 
ATOM   1851 C  CA  . TYR A 1 222 ? -18.321 -4.840  -40.076 1.00 17.32 ? 327  TYR A CA  1 
ATOM   1852 C  C   . TYR A 1 222 ? -17.553 -4.020  -41.035 1.00 19.10 ? 327  TYR A C   1 
ATOM   1853 O  O   . TYR A 1 222 ? -17.285 -2.847  -40.681 1.00 17.02 ? 327  TYR A O   1 
ATOM   1854 C  CB  . TYR A 1 222 ? -17.584 -5.036  -38.722 1.00 16.41 ? 327  TYR A CB  1 
ATOM   1855 C  CG  . TYR A 1 222 ? -18.477 -5.612  -37.646 1.00 16.72 ? 327  TYR A CG  1 
ATOM   1856 C  CD1 . TYR A 1 222 ? -19.676 -5.029  -37.302 1.00 19.28 ? 327  TYR A CD1 1 
ATOM   1857 C  CD2 . TYR A 1 222 ? -18.101 -6.822  -36.993 1.00 18.04 ? 327  TYR A CD2 1 
ATOM   1858 C  CE1 . TYR A 1 222 ? -20.499 -5.554  -36.322 1.00 19.15 ? 327  TYR A CE1 1 
ATOM   1859 C  CE2 . TYR A 1 222 ? -18.921 -7.344  -35.956 1.00 18.40 ? 327  TYR A CE2 1 
ATOM   1860 C  CZ  . TYR A 1 222 ? -20.106 -6.762  -35.649 1.00 23.23 ? 327  TYR A CZ  1 
ATOM   1861 O  OH  . TYR A 1 222 ? -20.985 -7.268  -34.659 1.00 25.68 ? 327  TYR A OH  1 
ATOM   1862 N  N   . ARG A 1 223 ? -17.110 -4.510  -42.202 1.00 17.35 ? 328  ARG A N   1 
ATOM   1863 C  CA  . ARG A 1 223 ? -16.352 -3.678  -43.121 1.00 18.64 ? 328  ARG A CA  1 
ATOM   1864 C  C   . ARG A 1 223 ? -17.134 -2.443  -43.597 1.00 16.76 ? 328  ARG A C   1 
ATOM   1865 O  O   . ARG A 1 223 ? -18.305 -2.486  -43.841 1.00 17.79 ? 328  ARG A O   1 
ATOM   1866 C  CB  . ARG A 1 223 ? -15.956 -4.547  -44.382 1.00 19.81 ? 328  ARG A CB  1 
ATOM   1867 C  CG  . ARG A 1 223 ? -14.954 -3.790  -45.295 1.00 23.86 ? 328  ARG A CG  1 
ATOM   1868 C  CD  . ARG A 1 223 ? -14.343 -4.799  -46.321 1.00 29.80 ? 328  ARG A CD  1 
ATOM   1869 N  NE  . ARG A 1 223 ? -13.487 -5.752  -45.570 1.00 37.22 ? 328  ARG A NE  1 
ATOM   1870 C  CZ  . ARG A 1 223 ? -13.632 -7.097  -45.565 1.00 46.99 ? 328  ARG A CZ  1 
ATOM   1871 N  NH1 . ARG A 1 223 ? -14.567 -7.699  -46.323 1.00 48.40 ? 328  ARG A NH1 1 
ATOM   1872 N  NH2 . ARG A 1 223 ? -12.792 -7.855  -44.843 1.00 46.28 ? 328  ARG A NH2 1 
ATOM   1873 N  N   . LEU A 1 224 ? -16.401 -1.329  -43.709 1.00 16.37 ? 329  LEU A N   1 
ATOM   1874 C  CA  . LEU A 1 224 ? -16.997 -0.055  -44.099 1.00 17.15 ? 329  LEU A CA  1 
ATOM   1875 C  C   . LEU A 1 224 ? -16.315 0.486   -45.360 1.00 17.68 ? 329  LEU A C   1 
ATOM   1876 O  O   . LEU A 1 224 ? -15.091 0.249   -45.580 1.00 19.94 ? 329  LEU A O   1 
ATOM   1877 C  CB  . LEU A 1 224 ? -16.804 0.946   -42.889 1.00 16.63 ? 329  LEU A CB  1 
ATOM   1878 C  CG  . LEU A 1 224 ? -17.667 0.631   -41.675 1.00 16.88 ? 329  LEU A CG  1 
ATOM   1879 C  CD1 . LEU A 1 224 ? -16.966 1.358   -40.439 1.00 19.46 ? 329  LEU A CD1 1 
ATOM   1880 C  CD2 . LEU A 1 224 ? -19.095 1.052   -41.857 1.00 17.99 ? 329  LEU A CD2 1 
ATOM   1881 N  N   . PRO A 1 225 ? -17.033 1.405   -46.063 1.00 19.82 ? 330  PRO A N   1 
ATOM   1882 C  CA  . PRO A 1 225 ? -16.404 2.138   -47.156 1.00 22.61 ? 330  PRO A CA  1 
ATOM   1883 C  C   . PRO A 1 225 ? -15.167 2.913   -46.724 1.00 20.98 ? 330  PRO A C   1 
ATOM   1884 O  O   . PRO A 1 225 ? -15.050 3.290   -45.523 1.00 19.45 ? 330  PRO A O   1 
ATOM   1885 C  CB  . PRO A 1 225 ? -17.511 3.117   -47.561 1.00 23.10 ? 330  PRO A CB  1 
ATOM   1886 C  CG  . PRO A 1 225 ? -18.814 2.544   -47.139 1.00 27.07 ? 330  PRO A CG  1 
ATOM   1887 C  CD  . PRO A 1 225 ? -18.464 1.744   -45.900 1.00 20.29 ? 330  PRO A CD  1 
ATOM   1888 N  N   . GLU A 1 226 ? -14.246 3.196   -47.646 1.00 21.11 ? 331  GLU A N   1 
ATOM   1889 C  CA  . GLU A 1 226 ? -13.051 3.909   -47.348 1.00 22.56 ? 331  GLU A CA  1 
ATOM   1890 C  C   . GLU A 1 226 ? -13.257 5.448   -47.186 1.00 23.41 ? 331  GLU A C   1 
ATOM   1891 O  O   . GLU A 1 226 ? -12.424 6.149   -46.591 1.00 26.99 ? 331  GLU A O   1 
ATOM   1892 C  CB  . GLU A 1 226 ? -12.021 3.657   -48.434 1.00 34.21 ? 331  GLU A CB  1 
ATOM   1893 C  CG  . GLU A 1 226 ? -11.482 2.208   -48.493 1.00 40.64 ? 331  GLU A CG  1 
ATOM   1894 C  CD  . GLU A 1 226 ? -10.745 1.897   -49.834 1.00 49.47 ? 331  GLU A CD  1 
ATOM   1895 O  OE1 . GLU A 1 226 ? -10.473 2.797   -50.696 1.00 45.56 ? 331  GLU A OE1 1 
ATOM   1896 O  OE2 . GLU A 1 226 ? -10.422 0.709   -50.030 1.00 61.07 ? 331  GLU A OE2 1 
ATOM   1897 N  N   . THR A 1 227 ? -14.361 5.965   -47.723 1.00 19.56 ? 332  THR A N   1 
ATOM   1898 C  CA  . THR A 1 227 ? -14.643 7.409   -47.615 1.00 21.17 ? 332  THR A CA  1 
ATOM   1899 C  C   . THR A 1 227 ? -16.128 7.572   -47.328 1.00 17.72 ? 332  THR A C   1 
ATOM   1900 O  O   . THR A 1 227 ? -16.991 6.745   -47.653 1.00 18.65 ? 332  THR A O   1 
ATOM   1901 C  CB  . THR A 1 227 ? -14.224 8.276   -48.857 1.00 27.05 ? 332  THR A CB  1 
ATOM   1902 O  OG1 . THR A 1 227 ? -14.853 7.766   -49.973 1.00 28.01 ? 332  THR A OG1 1 
ATOM   1903 C  CG2 . THR A 1 227 ? -12.732 8.302   -49.096 1.00 31.16 ? 332  THR A CG2 1 
ATOM   1904 N  N   . PRO A 1 228 ? -16.491 8.683   -46.680 1.00 18.35 ? 333  PRO A N   1 
ATOM   1905 C  CA  . PRO A 1 228 ? -17.902 8.801   -46.344 1.00 17.72 ? 333  PRO A CA  1 
ATOM   1906 C  C   . PRO A 1 228 ? -18.880 9.018   -47.509 1.00 18.09 ? 333  PRO A C   1 
ATOM   1907 O  O   . PRO A 1 228 ? -18.394 9.547   -48.539 1.00 25.59 ? 333  PRO A O   1 
ATOM   1908 C  CB  . PRO A 1 228 ? -17.907 10.074  -45.416 1.00 20.61 ? 333  PRO A CB  1 
ATOM   1909 C  CG  . PRO A 1 228 ? -16.513 10.246  -44.972 1.00 22.56 ? 333  PRO A CG  1 
ATOM   1910 C  CD  . PRO A 1 228 ? -15.620 9.720   -46.086 1.00 20.48 ? 333  PRO A CD  1 
ATOM   1911 N  N   . LYS A 1 229 ? -20.116 8.609   -47.333 1.00 18.87 ? 334  LYS A N   1 
ATOM   1912 C  CA  . LYS A 1 229 ? -21.063 8.771   -48.469 1.00 24.56 ? 334  LYS A CA  1 
ATOM   1913 C  C   . LYS A 1 229 ? -21.615 10.190  -48.660 1.00 23.38 ? 334  LYS A C   1 
ATOM   1914 O  O   . LYS A 1 229 ? -21.931 10.556  -49.818 1.00 23.57 ? 334  LYS A O   1 
ATOM   1915 C  CB  . LYS A 1 229 ? -22.165 7.744   -48.239 1.00 28.69 ? 334  LYS A CB  1 
ATOM   1916 C  CG  . LYS A 1 229 ? -23.498 8.199   -47.775 1.00 45.37 ? 334  LYS A CG  1 
ATOM   1917 C  CD  . LYS A 1 229 ? -23.876 7.416   -46.528 1.00 50.66 ? 334  LYS A CD  1 
ATOM   1918 C  CE  . LYS A 1 229 ? -24.336 6.000   -46.850 1.00 56.04 ? 334  LYS A CE  1 
ATOM   1919 N  NZ  . LYS A 1 229 ? -25.578 6.101   -47.665 1.00 62.99 ? 334  LYS A NZ  1 
ATOM   1920 N  N   . THR A 1 230 ? -21.756 11.013  -47.606 1.00 18.01 ? 335  THR A N   1 
ATOM   1921 C  CA  . THR A 1 230 ? -22.608 12.246  -47.790 1.00 15.33 ? 335  THR A CA  1 
ATOM   1922 C  C   . THR A 1 230 ? -21.752 13.258  -48.463 1.00 15.31 ? 335  THR A C   1 
ATOM   1923 O  O   . THR A 1 230 ? -20.609 13.565  -48.083 1.00 17.33 ? 335  THR A O   1 
ATOM   1924 C  CB  . THR A 1 230 ? -23.002 12.763  -46.393 1.00 15.32 ? 335  THR A CB  1 
ATOM   1925 O  OG1 . THR A 1 230 ? -23.762 11.753  -45.737 1.00 16.60 ? 335  THR A OG1 1 
ATOM   1926 C  CG2 . THR A 1 230 ? -23.885 14.058  -46.578 1.00 15.92 ? 335  THR A CG2 1 
ATOM   1927 N  N   . ALA A 1 231 ? -22.318 13.880  -49.569 1.00 14.30 ? 336  ALA A N   1 
ATOM   1928 C  CA  . ALA A 1 231 ? -21.657 14.927  -50.222 1.00 14.37 ? 336  ALA A CA  1 
ATOM   1929 C  C   . ALA A 1 231 ? -21.419 16.117  -49.328 1.00 14.24 ? 336  ALA A C   1 
ATOM   1930 O  O   . ALA A 1 231 ? -22.338 16.524  -48.576 1.00 15.34 ? 336  ALA A O   1 
ATOM   1931 C  CB  . ALA A 1 231 ? -22.462 15.336  -51.455 1.00 16.16 ? 336  ALA A CB  1 
ATOM   1932 N  N   . GLY A 1 232 ? -20.285 16.773  -49.554 1.00 11.85 ? 337  GLY A N   1 
ATOM   1933 C  CA  . GLY A 1 232 ? -19.976 18.047  -48.899 1.00 12.86 ? 337  GLY A CA  1 
ATOM   1934 C  C   . GLY A 1 232 ? -19.616 17.978  -47.451 1.00 11.52 ? 337  GLY A C   1 
ATOM   1935 O  O   . GLY A 1 232 ? -19.550 19.068  -46.802 1.00 12.46 ? 337  GLY A O   1 
ATOM   1936 N  N   . LEU A 1 233 ? -19.303 16.797  -46.924 1.00 11.02 ? 338  LEU A N   1 
ATOM   1937 C  CA  A LEU A 1 233 ? -18.818 16.645  -45.544 0.50 10.60 ? 338  LEU A CA  1 
ATOM   1938 C  CA  B LEU A 1 233 ? -18.761 16.620  -45.553 0.50 11.41 ? 338  LEU A CA  1 
ATOM   1939 C  C   . LEU A 1 233 ? -17.379 17.168  -45.420 1.00 11.55 ? 338  LEU A C   1 
ATOM   1940 O  O   . LEU A 1 233 ? -16.460 16.919  -46.274 1.00 14.89 ? 338  LEU A O   1 
ATOM   1941 C  CB  A LEU A 1 233 ? -18.869 15.131  -45.178 0.50 11.53 ? 338  LEU A CB  1 
ATOM   1942 C  CB  B LEU A 1 233 ? -18.613 15.107  -45.264 0.50 13.54 ? 338  LEU A CB  1 
ATOM   1943 C  CG  A LEU A 1 233 ? -18.774 14.760  -43.712 0.50 9.94  ? 338  LEU A CG  1 
ATOM   1944 C  CG  B LEU A 1 233 ? -19.889 14.578  -44.663 0.50 13.74 ? 338  LEU A CG  1 
ATOM   1945 C  CD1 A LEU A 1 233 ? -19.950 15.293  -42.872 0.50 11.04 ? 338  LEU A CD1 1 
ATOM   1946 C  CD1 B LEU A 1 233 ? -19.840 13.079  -44.723 0.50 15.41 ? 338  LEU A CD1 1 
ATOM   1947 C  CD2 A LEU A 1 233 ? -18.758 13.236  -43.676 0.50 10.92 ? 338  LEU A CD2 1 
ATOM   1948 C  CD2 B LEU A 1 233 ? -20.008 15.018  -43.168 0.50 15.48 ? 338  LEU A CD2 1 
ATOM   1949 N  N   . ARG A 1 234 ? -17.089 17.927  -44.349 1.00 9.78  ? 339  ARG A N   1 
ATOM   1950 C  CA  . ARG A 1 234 ? -15.764 18.445  -44.148 1.00 10.06 ? 339  ARG A CA  1 
ATOM   1951 C  C   . ARG A 1 234 ? -15.610 18.778  -42.636 1.00 9.06  ? 339  ARG A C   1 
ATOM   1952 O  O   . ARG A 1 234 ? -16.622 19.011  -41.963 1.00 10.85 ? 339  ARG A O   1 
ATOM   1953 C  CB  . ARG A 1 234 ? -15.481 19.717  -44.996 1.00 9.69  ? 339  ARG A CB  1 
ATOM   1954 C  CG  . ARG A 1 234 ? -16.517 20.829  -44.740 1.00 11.00 ? 339  ARG A CG  1 
ATOM   1955 C  CD  . ARG A 1 234 ? -16.055 22.161  -45.387 1.00 11.62 ? 339  ARG A CD  1 
ATOM   1956 N  NE  . ARG A 1 234 ? -17.031 23.266  -45.203 1.00 11.01 ? 339  ARG A NE  1 
ATOM   1957 C  CZ  . ARG A 1 234 ? -17.169 23.981  -44.077 1.00 10.35 ? 339  ARG A CZ  1 
ATOM   1958 N  NH1 . ARG A 1 234 ? -16.436 23.767  -42.992 1.00 9.73  ? 339  ARG A NH1 1 
ATOM   1959 N  NH2 . ARG A 1 234 ? -18.104 24.924  -44.075 1.00 10.58 ? 339  ARG A NH2 1 
ATOM   1960 N  N   . PRO A 1 235 ? -14.387 18.927  -42.140 1.00 9.22  ? 340  PRO A N   1 
ATOM   1961 C  CA  . PRO A 1 235 ? -14.278 19.358  -40.699 1.00 9.49  ? 340  PRO A CA  1 
ATOM   1962 C  C   . PRO A 1 235 ? -14.870 20.733  -40.505 1.00 9.09  ? 340  PRO A C   1 
ATOM   1963 O  O   . PRO A 1 235 ? -14.765 21.631  -41.374 1.00 10.02 ? 340  PRO A O   1 
ATOM   1964 C  CB  . PRO A 1 235 ? -12.756 19.446  -40.520 1.00 10.07 ? 340  PRO A CB  1 
ATOM   1965 C  CG  . PRO A 1 235 ? -12.159 18.373  -41.450 1.00 11.09 ? 340  PRO A CG  1 
ATOM   1966 C  CD  . PRO A 1 235 ? -13.067 18.546  -42.723 1.00 10.99 ? 340  PRO A CD  1 
ATOM   1967 N  N   . MET A 1 236 ? -15.403 20.932  -39.310 1.00 9.13  ? 341  MET A N   1 
ATOM   1968 C  CA  . MET A 1 236 ? -15.849 22.255  -38.852 1.00 8.04  ? 341  MET A CA  1 
ATOM   1969 C  C   . MET A 1 236 ? -14.623 23.184  -38.759 1.00 9.24  ? 341  MET A C   1 
ATOM   1970 O  O   . MET A 1 236 ? -13.499 22.839  -38.350 1.00 10.63 ? 341  MET A O   1 
ATOM   1971 C  CB  . MET A 1 236 ? -16.393 22.062  -37.462 1.00 9.13  ? 341  MET A CB  1 
ATOM   1972 C  CG  . MET A 1 236 ? -16.992 23.362  -36.863 1.00 9.31  ? 341  MET A CG  1 
ATOM   1973 S  SD  . MET A 1 236 ? -17.382 23.112  -35.108 1.00 9.91  ? 341  MET A SD  1 
ATOM   1974 C  CE  . MET A 1 236 ? -17.817 24.807  -34.701 1.00 10.79 ? 341  MET A CE  1 
ATOM   1975 N  N   . GLU A 1 237 ? -14.880 24.448  -39.194 1.00 9.08  ? 342  GLU A N   1 
ATOM   1976 C  CA  . GLU A 1 237 ? -13.931 25.544  -39.177 1.00 9.42  ? 342  GLU A CA  1 
ATOM   1977 C  C   . GLU A 1 237 ? -14.497 26.701  -38.320 1.00 9.10  ? 342  GLU A C   1 
ATOM   1978 O  O   . GLU A 1 237 ? -15.681 26.747  -37.982 1.00 9.32  ? 342  GLU A O   1 
ATOM   1979 C  CB  . GLU A 1 237 ? -13.652 26.073  -40.607 1.00 10.70 ? 342  GLU A CB  1 
ATOM   1980 C  CG  . GLU A 1 237 ? -13.068 24.947  -41.522 1.00 12.25 ? 342  GLU A CG  1 
ATOM   1981 C  CD  . GLU A 1 237 ? -12.835 25.456  -42.940 1.00 14.79 ? 342  GLU A CD  1 
ATOM   1982 O  OE1 . GLU A 1 237 ? -12.854 26.698  -43.197 1.00 21.61 ? 342  GLU A OE1 1 
ATOM   1983 O  OE2 . GLU A 1 237 ? -12.701 24.591  -43.795 1.00 16.59 ? 342  GLU A OE2 1 
ATOM   1984 N  N   . THR A 1 238 ? -13.616 27.703  -38.132 1.00 10.08 ? 343  THR A N   1 
ATOM   1985 C  CA  . THR A 1 238 ? -14.063 28.874  -37.320 1.00 10.57 ? 343  THR A CA  1 
ATOM   1986 C  C   . THR A 1 238 ? -15.272 29.589  -37.931 1.00 10.09 ? 343  THR A C   1 
ATOM   1987 O  O   . THR A 1 238 ? -16.214 29.941  -37.179 1.00 10.97 ? 343  THR A O   1 
ATOM   1988 C  CB  . THR A 1 238 ? -12.868 29.886  -37.274 1.00 11.61 ? 343  THR A CB  1 
ATOM   1989 O  OG1 . THR A 1 238 ? -11.810 29.209  -36.594 1.00 13.86 ? 343  THR A OG1 1 
ATOM   1990 C  CG2 . THR A 1 238 ? -13.189 31.171  -36.490 1.00 12.25 ? 343  THR A CG2 1 
ATOM   1991 N  N   . LYS A 1 239 ? -15.365 29.653  -39.269 1.00 11.21 ? 344  LYS A N   1 
ATOM   1992 C  CA  . LYS A 1 239 ? -16.519 30.327  -39.879 1.00 10.07 ? 344  LYS A CA  1 
ATOM   1993 C  C   . LYS A 1 239 ? -17.819 29.599  -39.635 1.00 10.60 ? 344  LYS A C   1 
ATOM   1994 O  O   . LYS A 1 239 ? -18.900 30.168  -39.825 1.00 12.10 ? 344  LYS A O   1 
ATOM   1995 C  CB  . LYS A 1 239 ? -16.310 30.433  -41.399 1.00 12.74 ? 344  LYS A CB  1 
ATOM   1996 C  CG  . LYS A 1 239 ? -16.253 29.109  -42.128 1.00 11.72 ? 344  LYS A CG  1 
ATOM   1997 C  CD  . LYS A 1 239 ? -15.862 29.410  -43.631 1.00 16.16 ? 344  LYS A CD  1 
ATOM   1998 C  CE  . LYS A 1 239 ? -15.997 28.119  -44.312 1.00 19.75 ? 344  LYS A CE  1 
ATOM   1999 N  NZ  . LYS A 1 239 ? -15.399 28.092  -45.730 1.00 25.77 ? 344  LYS A NZ  1 
ATOM   2000 N  N   . ASP A 1 240 ? -17.753 28.326  -39.204 1.00 9.33  ? 345  ASP A N   1 
ATOM   2001 C  CA  . ASP A 1 240 ? -18.996 27.565  -38.984 1.00 9.01  ? 345  ASP A CA  1 
ATOM   2002 C  C   . ASP A 1 240 ? -19.504 27.677  -37.525 1.00 8.92  ? 345  ASP A C   1 
ATOM   2003 O  O   . ASP A 1 240 ? -20.547 27.076  -37.228 1.00 9.58  ? 345  ASP A O   1 
ATOM   2004 C  CB  . ASP A 1 240 ? -18.706 26.031  -39.192 1.00 9.78  ? 345  ASP A CB  1 
ATOM   2005 C  CG  . ASP A 1 240 ? -18.189 25.736  -40.551 1.00 11.48 ? 345  ASP A CG  1 
ATOM   2006 O  OD1 . ASP A 1 240 ? -18.731 26.256  -41.573 1.00 10.67 ? 345  ASP A OD1 1 
ATOM   2007 O  OD2 . ASP A 1 240 ? -17.210 24.985  -40.681 1.00 10.27 ? 345  ASP A OD2 1 
ATOM   2008 N  N   . ILE A 1 241 ? -18.773 28.368  -36.634 1.00 9.86  ? 346  ILE A N   1 
ATOM   2009 C  CA  . ILE A 1 241 ? -19.221 28.390  -35.210 1.00 9.50  ? 346  ILE A CA  1 
ATOM   2010 C  C   . ILE A 1 241 ? -20.705 28.920  -35.060 1.00 9.67  ? 346  ILE A C   1 
ATOM   2011 O  O   . ILE A 1 241 ? -21.470 28.263  -34.359 1.00 9.26  ? 346  ILE A O   1 
ATOM   2012 C  CB  . ILE A 1 241 ? -18.221 29.184  -34.385 1.00 9.76  ? 346  ILE A CB  1 
ATOM   2013 C  CG1 . ILE A 1 241 ? -16.879 28.342  -34.226 1.00 10.64 ? 346  ILE A CG1 1 
ATOM   2014 C  CG2 . ILE A 1 241 ? -18.796 29.489  -32.999 1.00 11.90 ? 346  ILE A CG2 1 
ATOM   2015 C  CD1 . ILE A 1 241 ? -15.725 29.206  -33.784 1.00 12.20 ? 346  ILE A CD1 1 
ATOM   2016 N  N   . PRO A 1 242 ? -21.095 30.017  -35.759 1.00 9.62  ? 347  PRO A N   1 
ATOM   2017 C  CA  . PRO A 1 242 ? -22.464 30.492  -35.562 1.00 9.91  ? 347  PRO A CA  1 
ATOM   2018 C  C   . PRO A 1 242 ? -23.514 29.502  -36.043 1.00 10.03 ? 347  PRO A C   1 
ATOM   2019 O  O   . PRO A 1 242 ? -24.459 29.212  -35.335 1.00 9.78  ? 347  PRO A O   1 
ATOM   2020 C  CB  . PRO A 1 242 ? -22.460 31.815  -36.362 1.00 9.46  ? 347  PRO A CB  1 
ATOM   2021 C  CG  . PRO A 1 242 ? -21.050 32.295  -36.371 1.00 9.71  ? 347  PRO A CG  1 
ATOM   2022 C  CD  . PRO A 1 242 ? -20.243 30.971  -36.510 1.00 9.99  ? 347  PRO A CD  1 
ATOM   2023 N  N   . VAL A 1 243 ? -23.305 28.921  -37.255 1.00 10.43 ? 348  VAL A N   1 
ATOM   2024 C  CA  . VAL A 1 243 ? -24.330 28.030  -37.747 1.00 10.59 ? 348  VAL A CA  1 
ATOM   2025 C  C   . VAL A 1 243 ? -24.370 26.711  -36.940 1.00 9.80  ? 348  VAL A C   1 
ATOM   2026 O  O   . VAL A 1 243 ? -25.483 26.175  -36.754 1.00 9.63  ? 348  VAL A O   1 
ATOM   2027 C  CB  . VAL A 1 243 ? -24.164 27.794  -39.291 1.00 10.63 ? 348  VAL A CB  1 
ATOM   2028 C  CG1 . VAL A 1 243 ? -22.972 26.895  -39.603 1.00 11.58 ? 348  VAL A CG1 1 
ATOM   2029 C  CG2 . VAL A 1 243 ? -25.373 27.059  -39.829 1.00 11.89 ? 348  VAL A CG2 1 
ATOM   2030 N  N   . VAL A 1 244 ? -23.205 26.206  -36.455 1.00 10.39 ? 349  VAL A N   1 
ATOM   2031 C  CA  . VAL A 1 244 ? -23.296 25.033  -35.550 1.00 10.06 ? 349  VAL A CA  1 
ATOM   2032 C  C   . VAL A 1 244 ? -24.088 25.383  -34.281 1.00 9.14  ? 349  VAL A C   1 
ATOM   2033 O  O   . VAL A 1 244 ? -24.903 24.592  -33.840 1.00 9.73  ? 349  VAL A O   1 
ATOM   2034 C  CB  . VAL A 1 244 ? -21.863 24.544  -35.281 1.00 9.54  ? 349  VAL A CB  1 
ATOM   2035 C  CG1 . VAL A 1 244 ? -21.794 23.528  -34.145 1.00 9.87  ? 349  VAL A CG1 1 
ATOM   2036 C  CG2 . VAL A 1 244 ? -21.274 23.896  -36.616 1.00 10.35 ? 349  VAL A CG2 1 
ATOM   2037 N  N   . HIS A 1 245 ? -23.846 26.589  -33.730 1.00 8.65  ? 350  HIS A N   1 
ATOM   2038 C  CA  . HIS A 1 245 ? -24.634 27.011  -32.603 1.00 9.38  ? 350  HIS A CA  1 
ATOM   2039 C  C   . HIS A 1 245 ? -26.097 27.087  -32.921 1.00 9.20  ? 350  HIS A C   1 
ATOM   2040 O  O   . HIS A 1 245 ? -26.916 26.554  -32.141 1.00 10.12 ? 350  HIS A O   1 
ATOM   2041 C  CB  . HIS A 1 245 ? -24.096 28.378  -32.114 1.00 10.98 ? 350  HIS A CB  1 
ATOM   2042 C  CG  . HIS A 1 245 ? -24.935 28.924  -30.987 1.00 10.73 ? 350  HIS A CG  1 
ATOM   2043 N  ND1 . HIS A 1 245 ? -26.004 29.787  -31.186 1.00 15.44 ? 350  HIS A ND1 1 
ATOM   2044 C  CD2 . HIS A 1 245 ? -24.946 28.663  -29.649 1.00 12.94 ? 350  HIS A CD2 1 
ATOM   2045 C  CE1 . HIS A 1 245 ? -26.549 30.131  -30.011 1.00 16.11 ? 350  HIS A CE1 1 
ATOM   2046 N  NE2 . HIS A 1 245 ? -25.921 29.468  -29.063 1.00 14.95 ? 350  HIS A NE2 1 
ATOM   2047 N  N   . GLN A 1 246 ? -26.479 27.666  -34.088 1.00 9.07  ? 351  GLN A N   1 
ATOM   2048 C  CA  . GLN A 1 246 ? -27.904 27.731  -34.461 1.00 10.30 ? 351  GLN A CA  1 
ATOM   2049 C  C   . GLN A 1 246 ? -28.509 26.359  -34.619 1.00 9.76  ? 351  GLN A C   1 
ATOM   2050 O  O   . GLN A 1 246 ? -29.616 26.036  -34.101 1.00 11.67 ? 351  GLN A O   1 
ATOM   2051 C  CB  . GLN A 1 246 ? -27.966 28.551  -35.744 1.00 11.55 ? 351  GLN A CB  1 
ATOM   2052 C  CG  . GLN A 1 246 ? -29.413 28.602  -36.337 1.00 13.61 ? 351  GLN A CG  1 
ATOM   2053 C  CD  . GLN A 1 246 ? -29.441 29.432  -37.632 1.00 20.41 ? 351  GLN A CD  1 
ATOM   2054 O  OE1 . GLN A 1 246 ? -28.588 29.371  -38.457 1.00 19.34 ? 351  GLN A OE1 1 
ATOM   2055 N  NE2 . GLN A 1 246 ? -30.436 30.275  -37.716 1.00 30.85 ? 351  GLN A NE2 1 
ATOM   2056 N  N   . LEU A 1 247 ? -27.821 25.477  -35.364 1.00 10.11 ? 352  LEU A N   1 
ATOM   2057 C  CA  . LEU A 1 247 ? -28.346 24.128  -35.631 1.00 10.13 ? 352  LEU A CA  1 
ATOM   2058 C  C   . LEU A 1 247 ? -28.563 23.361  -34.314 1.00 10.28 ? 352  LEU A C   1 
ATOM   2059 O  O   . LEU A 1 247 ? -29.590 22.728  -34.121 1.00 10.75 ? 352  LEU A O   1 
ATOM   2060 C  CB  . LEU A 1 247 ? -27.378 23.354  -36.554 1.00 10.67 ? 352  LEU A CB  1 
ATOM   2061 C  CG  . LEU A 1 247 ? -27.413 23.841  -38.042 1.00 10.82 ? 352  LEU A CG  1 
ATOM   2062 C  CD1 . LEU A 1 247 ? -26.178 23.247  -38.776 1.00 12.15 ? 352  LEU A CD1 1 
ATOM   2063 C  CD2 . LEU A 1 247 ? -28.681 23.377  -38.775 1.00 14.36 ? 352  LEU A CD2 1 
ATOM   2064 N  N   . LEU A 1 248 ? -27.521 23.443  -33.424 1.00 10.37 ? 353  LEU A N   1 
ATOM   2065 C  CA  . LEU A 1 248 ? -27.636 22.665  -32.154 1.00 11.12 ? 353  LEU A CA  1 
ATOM   2066 C  C   . LEU A 1 248 ? -28.798 23.212  -31.279 1.00 9.32  ? 353  LEU A C   1 
ATOM   2067 O  O   . LEU A 1 248 ? -29.596 22.429  -30.763 1.00 10.92 ? 353  LEU A O   1 
ATOM   2068 C  CB  . LEU A 1 248 ? -26.298 22.777  -31.390 1.00 11.27 ? 353  LEU A CB  1 
ATOM   2069 C  CG  . LEU A 1 248 ? -26.247 22.028  -30.048 1.00 10.43 ? 353  LEU A CG  1 
ATOM   2070 C  CD1 . LEU A 1 248 ? -26.337 20.495  -30.272 1.00 12.22 ? 353  LEU A CD1 1 
ATOM   2071 C  CD2 . LEU A 1 248 ? -24.996 22.378  -29.241 1.00 12.96 ? 353  LEU A CD2 1 
ATOM   2072 N  N   . THR A 1 249 ? -28.872 24.548  -31.196 1.00 10.72 ? 354  THR A N   1 
ATOM   2073 C  CA  . THR A 1 249 ? -29.891 25.130  -30.309 1.00 12.33 ? 354  THR A CA  1 
ATOM   2074 C  C   . THR A 1 249 ? -31.297 24.736  -30.749 1.00 12.09 ? 354  THR A C   1 
ATOM   2075 O  O   . THR A 1 249 ? -32.156 24.340  -29.972 1.00 13.81 ? 354  THR A O   1 
ATOM   2076 C  CB  . THR A 1 249 ? -29.698 26.643  -30.302 1.00 13.23 ? 354  THR A CB  1 
ATOM   2077 O  OG1 . THR A 1 249 ? -28.387 26.988  -29.777 1.00 14.62 ? 354  THR A OG1 1 
ATOM   2078 C  CG2 . THR A 1 249 ? -30.825 27.356  -29.411 1.00 17.12 ? 354  THR A CG2 1 
ATOM   2079 N  N   . ARG A 1 250 ? -31.539 24.815  -32.074 1.00 11.88 ? 355  ARG A N   1 
ATOM   2080 C  CA  . ARG A 1 250 ? -32.865 24.421  -32.643 1.00 14.06 ? 355  ARG A CA  1 
ATOM   2081 C  C   . ARG A 1 250 ? -33.147 22.971  -32.439 1.00 13.14 ? 355  ARG A C   1 
ATOM   2082 O  O   . ARG A 1 250 ? -34.298 22.593  -32.068 1.00 14.76 ? 355  ARG A O   1 
ATOM   2083 C  CB  . ARG A 1 250 ? -32.999 24.859  -34.121 1.00 14.24 ? 355  ARG A CB  1 
ATOM   2084 C  CG  . ARG A 1 250 ? -33.037 26.407  -34.214 1.00 17.83 ? 355  ARG A CG  1 
ATOM   2085 C  CD  . ARG A 1 250 ? -33.112 26.872  -35.655 1.00 23.21 ? 355  ARG A CD  1 
ATOM   2086 N  NE  . ARG A 1 250 ? -32.925 28.320  -35.595 1.00 33.73 ? 355  ARG A NE  1 
ATOM   2087 C  CZ  . ARG A 1 250 ? -33.036 29.147  -36.634 1.00 40.40 ? 355  ARG A CZ  1 
ATOM   2088 N  NH1 . ARG A 1 250 ? -33.381 28.632  -37.828 1.00 42.96 ? 355  ARG A NH1 1 
ATOM   2089 N  NH2 . ARG A 1 250 ? -32.807 30.490  -36.451 1.00 38.10 ? 355  ARG A NH2 1 
ATOM   2090 N  N   . TYR A 1 251 ? -32.152 22.087  -32.717 1.00 12.24 ? 356  TYR A N   1 
ATOM   2091 C  CA  . TYR A 1 251 ? -32.322 20.657  -32.636 1.00 11.41 ? 356  TYR A CA  1 
ATOM   2092 C  C   . TYR A 1 251 ? -32.622 20.164  -31.210 1.00 11.36 ? 356  TYR A C   1 
ATOM   2093 O  O   . TYR A 1 251 ? -33.398 19.214  -31.010 1.00 12.69 ? 356  TYR A O   1 
ATOM   2094 C  CB  . TYR A 1 251 ? -31.063 19.963  -33.214 1.00 11.43 ? 356  TYR A CB  1 
ATOM   2095 C  CG  . TYR A 1 251 ? -31.120 18.493  -33.176 1.00 11.98 ? 356  TYR A CG  1 
ATOM   2096 C  CD1 . TYR A 1 251 ? -31.841 17.816  -34.151 1.00 13.45 ? 356  TYR A CD1 1 
ATOM   2097 C  CD2 . TYR A 1 251 ? -30.499 17.727  -32.157 1.00 12.25 ? 356  TYR A CD2 1 
ATOM   2098 C  CE1 . TYR A 1 251 ? -31.941 16.435  -34.185 1.00 13.68 ? 356  TYR A CE1 1 
ATOM   2099 C  CE2 . TYR A 1 251 ? -30.569 16.343  -32.146 1.00 12.25 ? 356  TYR A CE2 1 
ATOM   2100 C  CZ  . TYR A 1 251 ? -31.327 15.669  -33.131 1.00 13.86 ? 356  TYR A CZ  1 
ATOM   2101 O  OH  . TYR A 1 251 ? -31.421 14.308  -33.032 1.00 16.64 ? 356  TYR A OH  1 
ATOM   2102 N  N   . LEU A 1 252 ? -32.035 20.822  -30.208 1.00 11.52 ? 357  LEU A N   1 
ATOM   2103 C  CA  . LEU A 1 252 ? -32.165 20.314  -28.827 1.00 12.03 ? 357  LEU A CA  1 
ATOM   2104 C  C   . LEU A 1 252 ? -33.495 20.651  -28.215 1.00 12.93 ? 357  LEU A C   1 
ATOM   2105 O  O   . LEU A 1 252 ? -33.867 20.014  -27.218 1.00 12.95 ? 357  LEU A O   1 
ATOM   2106 C  CB  . LEU A 1 252 ? -31.009 20.934  -27.974 1.00 12.49 ? 357  LEU A CB  1 
ATOM   2107 C  CG  . LEU A 1 252 ? -29.662 20.299  -28.208 1.00 11.06 ? 357  LEU A CG  1 
ATOM   2108 C  CD1 . LEU A 1 252 ? -28.642 21.121  -27.339 1.00 12.63 ? 357  LEU A CD1 1 
ATOM   2109 C  CD2 . LEU A 1 252 ? -29.590 18.821  -27.892 1.00 12.03 ? 357  LEU A CD2 1 
ATOM   2110 N  N   . LYS A 1 253 ? -34.311 21.539  -28.859 1.00 13.07 ? 358  LYS A N   1 
ATOM   2111 C  CA  . LYS A 1 253 ? -35.613 21.909  -28.261 1.00 15.49 ? 358  LYS A CA  1 
ATOM   2112 C  C   . LYS A 1 253 ? -36.591 20.716  -28.131 1.00 14.85 ? 358  LYS A C   1 
ATOM   2113 O  O   . LYS A 1 253 ? -37.433 20.801  -27.217 1.00 16.84 ? 358  LYS A O   1 
ATOM   2114 C  CB  . LYS A 1 253 ? -36.258 23.013  -29.151 1.00 16.20 ? 358  LYS A CB  1 
ATOM   2115 C  CG  . LYS A 1 253 ? -35.556 24.375  -28.994 1.00 20.36 ? 358  LYS A CG  1 
ATOM   2116 C  CD  . LYS A 1 253 ? -36.187 25.428  -29.914 1.00 27.26 ? 358  LYS A CD  1 
ATOM   2117 C  CE  . LYS A 1 253 ? -35.509 26.793  -29.826 1.00 37.66 ? 358  LYS A CE  1 
ATOM   2118 N  NZ  . LYS A 1 253 ? -35.685 27.540  -31.119 1.00 39.59 ? 358  LYS A NZ  1 
ATOM   2119 N  N   . GLN A 1 254 ? -36.436 19.638  -28.905 1.00 12.48 ? 359  GLN A N   1 
ATOM   2120 C  CA  . GLN A 1 254 ? -37.311 18.531  -28.914 1.00 14.60 ? 359  GLN A CA  1 
ATOM   2121 C  C   . GLN A 1 254 ? -37.103 17.609  -27.698 1.00 15.54 ? 359  GLN A C   1 
ATOM   2122 O  O   . GLN A 1 254 ? -37.926 16.692  -27.435 1.00 17.22 ? 359  GLN A O   1 
ATOM   2123 C  CB  . GLN A 1 254 ? -37.214 17.743  -30.187 1.00 16.51 ? 359  GLN A CB  1 
ATOM   2124 C  CG  . GLN A 1 254 ? -35.930 16.970  -30.297 1.00 15.27 ? 359  GLN A CG  1 
ATOM   2125 C  CD  . GLN A 1 254 ? -35.701 16.443  -31.696 1.00 15.77 ? 359  GLN A CD  1 
ATOM   2126 O  OE1 . GLN A 1 254 ? -36.367 15.459  -32.108 1.00 21.80 ? 359  GLN A OE1 1 
ATOM   2127 N  NE2 . GLN A 1 254 ? -34.835 17.074  -32.463 1.00 15.88 ? 359  GLN A NE2 1 
ATOM   2128 N  N   . PHE A 1 255 ? -36.000 17.807  -26.917 1.00 13.31 ? 360  PHE A N   1 
ATOM   2129 C  CA  . PHE A 1 255 ? -35.688 16.879  -25.787 1.00 13.36 ? 360  PHE A CA  1 
ATOM   2130 C  C   . PHE A 1 255 ? -36.057 17.541  -24.468 1.00 12.84 ? 360  PHE A C   1 
ATOM   2131 O  O   . PHE A 1 255 ? -36.355 18.754  -24.497 1.00 15.95 ? 360  PHE A O   1 
ATOM   2132 C  CB  . PHE A 1 255 ? -34.200 16.452  -25.841 1.00 12.06 ? 360  PHE A CB  1 
ATOM   2133 C  CG  . PHE A 1 255 ? -33.800 15.916  -27.195 1.00 12.69 ? 360  PHE A CG  1 
ATOM   2134 C  CD1 . PHE A 1 255 ? -34.308 14.754  -27.707 1.00 12.47 ? 360  PHE A CD1 1 
ATOM   2135 C  CD2 . PHE A 1 255 ? -32.931 16.608  -28.008 1.00 11.95 ? 360  PHE A CD2 1 
ATOM   2136 C  CE1 . PHE A 1 255 ? -34.004 14.250  -28.944 1.00 13.05 ? 360  PHE A CE1 1 
ATOM   2137 C  CE2 . PHE A 1 255 ? -32.558 16.133  -29.263 1.00 14.04 ? 360  PHE A CE2 1 
ATOM   2138 C  CZ  . PHE A 1 255 ? -33.111 14.957  -29.797 1.00 13.45 ? 360  PHE A CZ  1 
ATOM   2139 N  N   . HIS A 1 256 ? -36.053 16.805  -23.353 1.00 13.04 ? 361  HIS A N   1 
ATOM   2140 C  CA  . HIS A 1 256 ? -36.407 17.329  -22.065 1.00 12.79 ? 361  HIS A CA  1 
ATOM   2141 C  C   . HIS A 1 256 ? -35.305 17.642  -21.076 1.00 12.15 ? 361  HIS A C   1 
ATOM   2142 O  O   . HIS A 1 256 ? -35.597 18.271  -20.059 1.00 13.61 ? 361  HIS A O   1 
ATOM   2143 C  CB  . HIS A 1 256 ? -37.493 16.449  -21.396 1.00 14.75 ? 361  HIS A CB  1 
ATOM   2144 C  CG  . HIS A 1 256 ? -38.825 16.417  -22.155 1.00 19.60 ? 361  HIS A CG  1 
ATOM   2145 N  ND1 . HIS A 1 256 ? -39.412 17.534  -22.691 1.00 21.81 ? 361  HIS A ND1 1 
ATOM   2146 C  CD2 . HIS A 1 256 ? -39.689 15.397  -22.334 1.00 21.23 ? 361  HIS A CD2 1 
ATOM   2147 C  CE1 . HIS A 1 256 ? -40.583 17.181  -23.236 1.00 27.56 ? 361  HIS A CE1 1 
ATOM   2148 N  NE2 . HIS A 1 256 ? -40.753 15.880  -23.052 1.00 26.05 ? 361  HIS A NE2 1 
ATOM   2149 N  N   . LEU A 1 257 ? -34.087 17.136  -21.370 1.00 11.44 ? 362  LEU A N   1 
ATOM   2150 C  CA  . LEU A 1 257 ? -32.918 17.521  -20.534 1.00 11.12 ? 362  LEU A CA  1 
ATOM   2151 C  C   . LEU A 1 257 ? -31.784 17.839  -21.535 1.00 10.03 ? 362  LEU A C   1 
ATOM   2152 O  O   . LEU A 1 257 ? -31.361 16.946  -22.248 1.00 11.47 ? 362  LEU A O   1 
ATOM   2153 C  CB  . LEU A 1 257 ? -32.546 16.280  -19.664 1.00 12.08 ? 362  LEU A CB  1 
ATOM   2154 C  CG  . LEU A 1 257 ? -31.219 16.545  -18.852 1.00 11.54 ? 362  LEU A CG  1 
ATOM   2155 C  CD1 . LEU A 1 257 ? -31.254 17.723  -17.921 1.00 12.01 ? 362  LEU A CD1 1 
ATOM   2156 C  CD2 . LEU A 1 257 ? -30.901 15.257  -18.058 1.00 13.18 ? 362  LEU A CD2 1 
ATOM   2157 N  N   . THR A 1 258 ? -31.410 19.099  -21.586 1.00 10.60 ? 363  THR A N   1 
ATOM   2158 C  CA  . THR A 1 258 ? -30.392 19.523  -22.602 1.00 10.29 ? 363  THR A CA  1 
ATOM   2159 C  C   . THR A 1 258 ? -29.540 20.626  -22.031 1.00 10.49 ? 363  THR A C   1 
ATOM   2160 O  O   . THR A 1 258 ? -29.920 21.340  -21.111 1.00 11.47 ? 363  THR A O   1 
ATOM   2161 C  CB  . THR A 1 258 ? -31.117 20.130  -23.878 1.00 11.50 ? 363  THR A CB  1 
ATOM   2162 O  OG1 . THR A 1 258 ? -31.860 21.306  -23.558 1.00 16.13 ? 363  THR A OG1 1 
ATOM   2163 C  CG2 . THR A 1 258 ? -32.090 19.148  -24.496 1.00 13.33 ? 363  THR A CG2 1 
ATOM   2164 N  N   . PRO A 1 259 ? -28.338 20.824  -22.599 1.00 10.03 ? 364  PRO A N   1 
ATOM   2165 C  CA  . PRO A 1 259 ? -27.599 22.048  -22.282 1.00 10.65 ? 364  PRO A CA  1 
ATOM   2166 C  C   . PRO A 1 259 ? -28.126 23.213  -23.107 1.00 10.82 ? 364  PRO A C   1 
ATOM   2167 O  O   . PRO A 1 259 ? -28.727 23.004  -24.173 1.00 12.71 ? 364  PRO A O   1 
ATOM   2168 C  CB  . PRO A 1 259 ? -26.150 21.672  -22.759 1.00 11.39 ? 364  PRO A CB  1 
ATOM   2169 C  CG  . PRO A 1 259 ? -26.417 20.784  -24.039 1.00 10.86 ? 364  PRO A CG  1 
ATOM   2170 C  CD  . PRO A 1 259 ? -27.641 19.943  -23.595 1.00 11.24 ? 364  PRO A CD  1 
ATOM   2171 N  N   . VAL A 1 260 ? -27.836 24.411  -22.617 1.00 10.53 ? 365  VAL A N   1 
ATOM   2172 C  CA  . VAL A 1 260 ? -28.074 25.656  -23.359 1.00 11.20 ? 365  VAL A CA  1 
ATOM   2173 C  C   . VAL A 1 260 ? -26.715 26.260  -23.513 1.00 10.80 ? 365  VAL A C   1 
ATOM   2174 O  O   . VAL A 1 260 ? -26.124 26.788  -22.522 1.00 12.71 ? 365  VAL A O   1 
ATOM   2175 C  CB  . VAL A 1 260 ? -29.073 26.553  -22.621 1.00 12.30 ? 365  VAL A CB  1 
ATOM   2176 C  CG1 . VAL A 1 260 ? -29.302 27.857  -23.407 1.00 15.98 ? 365  VAL A CG1 1 
ATOM   2177 C  CG2 . VAL A 1 260 ? -30.435 25.783  -22.423 1.00 16.06 ? 365  VAL A CG2 1 
ATOM   2178 N  N   . MET A 1 261 ? -26.136 26.216  -24.698 1.00 10.86 ? 366  MET A N   1 
ATOM   2179 C  CA  . MET A 1 261 ? -24.725 26.679  -24.891 1.00 9.99  ? 366  MET A CA  1 
ATOM   2180 C  C   . MET A 1 261 ? -24.685 28.044  -25.545 1.00 10.02 ? 366  MET A C   1 
ATOM   2181 O  O   . MET A 1 261 ? -25.357 28.293  -26.578 1.00 12.35 ? 366  MET A O   1 
ATOM   2182 C  CB  . MET A 1 261 ? -24.024 25.683  -25.822 1.00 10.04 ? 366  MET A CB  1 
ATOM   2183 C  CG  . MET A 1 261 ? -23.789 24.312  -25.198 1.00 11.05 ? 366  MET A CG  1 
ATOM   2184 S  SD  . MET A 1 261 ? -22.699 23.350  -26.265 1.00 11.81 ? 366  MET A SD  1 
ATOM   2185 C  CE  . MET A 1 261 ? -22.797 21.816  -25.373 1.00 16.71 ? 366  MET A CE  1 
ATOM   2186 N  N   . SER A 1 262 ? -23.811 28.898  -25.047 1.00 8.83  ? 367  SER A N   1 
ATOM   2187 C  CA  . SER A 1 262 ? -23.494 30.136  -25.761 1.00 8.51  ? 367  SER A CA  1 
ATOM   2188 C  C   . SER A 1 262 ? -22.624 29.863  -27.021 1.00 8.44  ? 367  SER A C   1 
ATOM   2189 O  O   . SER A 1 262 ? -22.112 28.711  -27.213 1.00 9.18  ? 367  SER A O   1 
ATOM   2190 C  CB  . SER A 1 262 ? -22.643 31.026  -24.823 1.00 9.43  ? 367  SER A CB  1 
ATOM   2191 O  OG  . SER A 1 262 ? -21.318 30.435  -24.676 1.00 9.09  ? 367  SER A OG  1 
ATOM   2192 N  N   . GLN A 1 263 ? -22.427 30.842  -27.855 1.00 7.86  ? 368  GLN A N   1 
ATOM   2193 C  CA  . GLN A 1 263 ? -21.581 30.667  -29.010 1.00 8.63  ? 368  GLN A CA  1 
ATOM   2194 C  C   . GLN A 1 263 ? -20.129 30.352  -28.552 1.00 8.85  ? 368  GLN A C   1 
ATOM   2195 O  O   . GLN A 1 263 ? -19.453 29.533  -29.263 1.00 9.51  ? 368  GLN A O   1 
ATOM   2196 C  CB  . GLN A 1 263 ? -21.752 31.882  -29.944 1.00 9.58  ? 368  GLN A CB  1 
ATOM   2197 C  CG  . GLN A 1 263 ? -21.051 31.654  -31.318 1.00 9.21  ? 368  GLN A CG  1 
ATOM   2198 C  CD  . GLN A 1 263 ? -21.586 32.653  -32.333 1.00 8.75  ? 368  GLN A CD  1 
ATOM   2199 O  OE1 . GLN A 1 263 ? -22.799 32.632  -32.671 1.00 9.32  ? 368  GLN A OE1 1 
ATOM   2200 N  NE2 . GLN A 1 263 ? -20.676 33.500  -32.848 1.00 9.08  ? 368  GLN A NE2 1 
ATOM   2201 N  N   . GLU A 1 264 ? -19.641 30.952  -27.493 1.00 8.82  ? 369  GLU A N   1 
ATOM   2202 C  CA  . GLU A 1 264 ? -18.318 30.563  -26.994 1.00 9.80  ? 369  GLU A CA  1 
ATOM   2203 C  C   . GLU A 1 264 ? -18.262 29.135  -26.503 1.00 8.70  ? 369  GLU A C   1 
ATOM   2204 O  O   . GLU A 1 264 ? -17.232 28.438  -26.728 1.00 9.03  ? 369  GLU A O   1 
ATOM   2205 C  CB  . GLU A 1 264 ? -17.849 31.498  -25.867 1.00 11.27 ? 369  GLU A CB  1 
ATOM   2206 C  CG  . GLU A 1 264 ? -17.613 32.886  -26.456 1.00 16.51 ? 369  GLU A CG  1 
ATOM   2207 C  CD  . GLU A 1 264 ? -16.397 33.007  -27.365 1.00 20.15 ? 369  GLU A CD  1 
ATOM   2208 O  OE1 . GLU A 1 264 ? -15.457 32.209  -27.197 1.00 26.53 ? 369  GLU A OE1 1 
ATOM   2209 O  OE2 . GLU A 1 264 ? -16.470 33.909  -28.274 1.00 23.48 ? 369  GLU A OE2 1 
ATOM   2210 N  N   . GLU A 1 265 ? -19.331 28.651  -25.854 1.00 8.11  ? 370  GLU A N   1 
ATOM   2211 C  CA  . GLU A 1 265 ? -19.304 27.242  -25.426 1.00 7.94  ? 370  GLU A CA  1 
ATOM   2212 C  C   . GLU A 1 265 ? -19.394 26.323  -26.628 1.00 8.67  ? 370  GLU A C   1 
ATOM   2213 O  O   . GLU A 1 265 ? -18.730 25.267  -26.589 1.00 8.24  ? 370  GLU A O   1 
ATOM   2214 C  CB  . GLU A 1 265 ? -20.534 27.005  -24.500 1.00 8.78  ? 370  GLU A CB  1 
ATOM   2215 C  CG  . GLU A 1 265 ? -20.303 27.578  -23.087 1.00 8.93  ? 370  GLU A CG  1 
ATOM   2216 C  CD  . GLU A 1 265 ? -21.552 27.498  -22.270 1.00 11.02 ? 370  GLU A CD  1 
ATOM   2217 O  OE1 . GLU A 1 265 ? -22.582 27.992  -22.643 1.00 10.75 ? 370  GLU A OE1 1 
ATOM   2218 O  OE2 . GLU A 1 265 ? -21.502 26.912  -21.128 1.00 12.85 ? 370  GLU A OE2 1 
ATOM   2219 N  N   . VAL A 1 266 ? -20.125 26.693  -27.689 1.00 8.07  ? 371  VAL A N   1 
ATOM   2220 C  CA  . VAL A 1 266 ? -20.124 25.823  -28.897 1.00 8.18  ? 371  VAL A CA  1 
ATOM   2221 C  C   . VAL A 1 266 ? -18.722 25.820  -29.511 1.00 8.23  ? 371  VAL A C   1 
ATOM   2222 O  O   . VAL A 1 266 ? -18.255 24.703  -29.905 1.00 8.55  ? 371  VAL A O   1 
ATOM   2223 C  CB  . VAL A 1 266 ? -21.200 26.348  -29.892 1.00 8.62  ? 371  VAL A CB  1 
ATOM   2224 C  CG1 . VAL A 1 266 ? -21.000 25.728  -31.306 1.00 10.51 ? 371  VAL A CG1 1 
ATOM   2225 C  CG2 . VAL A 1 266 ? -22.572 25.978  -29.396 1.00 11.75 ? 371  VAL A CG2 1 
ATOM   2226 N  N   . GLU A 1 267 ? -17.989 26.917  -29.537 1.00 8.58  ? 372  GLU A N   1 
ATOM   2227 C  CA  A GLU A 1 267 ? -16.665 26.851  -30.048 0.50 8.22  ? 372  GLU A CA  1 
ATOM   2228 C  CA  B GLU A 1 267 ? -16.609 26.882  -30.008 0.50 8.74  ? 372  GLU A CA  1 
ATOM   2229 C  C   . GLU A 1 267 ? -15.834 25.875  -29.152 1.00 8.46  ? 372  GLU A C   1 
ATOM   2230 O  O   . GLU A 1 267 ? -15.087 25.014  -29.698 1.00 8.28  ? 372  GLU A O   1 
ATOM   2231 C  CB  A GLU A 1 267 ? -16.063 28.247  -30.097 0.50 8.51  ? 372  GLU A CB  1 
ATOM   2232 C  CB  B GLU A 1 267 ? -15.901 28.244  -29.879 0.50 10.02 ? 372  GLU A CB  1 
ATOM   2233 C  CG  A GLU A 1 267 ? -14.575 28.203  -30.370 0.50 9.75  ? 372  GLU A CG  1 
ATOM   2234 C  CG  B GLU A 1 267 ? -14.488 28.254  -30.490 0.50 12.32 ? 372  GLU A CG  1 
ATOM   2235 C  CD  A GLU A 1 267 ? -13.937 29.565  -30.370 0.50 11.08 ? 372  GLU A CD  1 
ATOM   2236 C  CD  B GLU A 1 267 ? -13.368 27.679  -29.587 0.50 15.14 ? 372  GLU A CD  1 
ATOM   2237 O  OE1 A GLU A 1 267 ? -14.628 30.597  -30.383 0.50 11.72 ? 372  GLU A OE1 1 
ATOM   2238 O  OE1 B GLU A 1 267 ? -13.447 27.722  -28.340 0.50 16.46 ? 372  GLU A OE1 1 
ATOM   2239 O  OE2 A GLU A 1 267 ? -12.706 29.687  -30.410 0.50 15.41 ? 372  GLU A OE2 1 
ATOM   2240 O  OE2 B GLU A 1 267 ? -12.350 27.171  -30.157 0.50 19.70 ? 372  GLU A OE2 1 
ATOM   2241 N  N   . HIS A 1 268 ? -15.944 25.959  -27.829 1.00 7.80  ? 373  HIS A N   1 
ATOM   2242 C  CA  . HIS A 1 268 ? -15.134 25.085  -26.976 1.00 8.13  ? 373  HIS A CA  1 
ATOM   2243 C  C   . HIS A 1 268 ? -15.479 23.633  -27.179 1.00 7.81  ? 373  HIS A C   1 
ATOM   2244 O  O   . HIS A 1 268 ? -14.518 22.775  -27.335 1.00 7.54  ? 373  HIS A O   1 
ATOM   2245 C  CB  . HIS A 1 268 ? -15.330 25.499  -25.495 1.00 8.01  ? 373  HIS A CB  1 
ATOM   2246 C  CG  . HIS A 1 268 ? -14.499 24.624  -24.583 1.00 7.66  ? 373  HIS A CG  1 
ATOM   2247 N  ND1 . HIS A 1 268 ? -13.185 24.914  -24.415 1.00 9.97  ? 373  HIS A ND1 1 
ATOM   2248 C  CD2 . HIS A 1 268 ? -14.778 23.475  -23.922 1.00 8.33  ? 373  HIS A CD2 1 
ATOM   2249 C  CE1 . HIS A 1 268 ? -12.626 23.975  -23.625 1.00 9.54  ? 373  HIS A CE1 1 
ATOM   2250 N  NE2 . HIS A 1 268 ? -13.567 23.109  -23.314 1.00 9.09  ? 373  HIS A NE2 1 
ATOM   2251 N  N   . TRP A 1 269 ? -16.736 23.312  -27.183 1.00 7.68  ? 374  TRP A N   1 
ATOM   2252 C  CA  . TRP A 1 269 ? -17.140 21.875  -27.187 1.00 7.67  ? 374  TRP A CA  1 
ATOM   2253 C  C   . TRP A 1 269 ? -17.040 21.228  -28.568 1.00 7.57  ? 374  TRP A C   1 
ATOM   2254 O  O   . TRP A 1 269 ? -16.930 19.974  -28.625 1.00 9.12  ? 374  TRP A O   1 
ATOM   2255 C  CB  . TRP A 1 269 ? -18.544 21.702  -26.631 1.00 9.06  ? 374  TRP A CB  1 
ATOM   2256 C  CG  . TRP A 1 269 ? -18.618 22.001  -25.147 1.00 8.08  ? 374  TRP A CG  1 
ATOM   2257 C  CD1 . TRP A 1 269 ? -19.390 22.963  -24.528 1.00 9.03  ? 374  TRP A CD1 1 
ATOM   2258 C  CD2 . TRP A 1 269 ? -17.865 21.382  -24.088 1.00 8.07  ? 374  TRP A CD2 1 
ATOM   2259 N  NE1 . TRP A 1 269 ? -19.180 22.955  -23.162 1.00 8.98  ? 374  TRP A NE1 1 
ATOM   2260 C  CE2 . TRP A 1 269 ? -18.203 22.034  -22.871 1.00 8.71  ? 374  TRP A CE2 1 
ATOM   2261 C  CE3 . TRP A 1 269 ? -16.903 20.339  -24.066 1.00 8.72  ? 374  TRP A CE3 1 
ATOM   2262 C  CZ2 . TRP A 1 269 ? -17.736 21.637  -21.608 1.00 9.76  ? 374  TRP A CZ2 1 
ATOM   2263 C  CZ3 . TRP A 1 269 ? -16.329 19.983  -22.830 1.00 9.17  ? 374  TRP A CZ3 1 
ATOM   2264 C  CH2 . TRP A 1 269 ? -16.736 20.637  -21.633 1.00 10.36 ? 374  TRP A CH2 1 
ATOM   2265 N  N   . PHE A 1 270 ? -17.003 21.993  -29.693 1.00 7.14  ? 375  PHE A N   1 
ATOM   2266 C  CA  . PHE A 1 270 ? -17.058 21.397  -30.999 1.00 7.69  ? 375  PHE A CA  1 
ATOM   2267 C  C   . PHE A 1 270 ? -15.920 21.720  -31.890 1.00 8.11  ? 375  PHE A C   1 
ATOM   2268 O  O   . PHE A 1 270 ? -15.631 20.932  -32.839 1.00 8.71  ? 375  PHE A O   1 
ATOM   2269 C  CB  . PHE A 1 270 ? -18.396 21.734  -31.725 1.00 8.31  ? 375  PHE A CB  1 
ATOM   2270 C  CG  . PHE A 1 270 ? -19.596 21.189  -31.008 1.00 8.61  ? 375  PHE A CG  1 
ATOM   2271 C  CD1 . PHE A 1 270 ? -19.974 19.834  -31.212 1.00 9.03  ? 375  PHE A CD1 1 
ATOM   2272 C  CD2 . PHE A 1 270 ? -20.332 22.013  -30.144 1.00 8.30  ? 375  PHE A CD2 1 
ATOM   2273 C  CE1 . PHE A 1 270 ? -21.054 19.310  -30.520 1.00 9.23  ? 375  PHE A CE1 1 
ATOM   2274 C  CE2 . PHE A 1 270 ? -21.427 21.476  -29.467 1.00 8.78  ? 375  PHE A CE2 1 
ATOM   2275 C  CZ  . PHE A 1 270 ? -21.799 20.122  -29.622 1.00 9.13  ? 375  PHE A CZ  1 
ATOM   2276 N  N   . TYR A 1 271 ? -15.189 22.797  -31.691 1.00 7.92  ? 376  TYR A N   1 
ATOM   2277 C  CA  . TYR A 1 271 ? -14.114 23.127  -32.640 1.00 8.69  ? 376  TYR A CA  1 
ATOM   2278 C  C   . TYR A 1 271 ? -13.084 22.011  -32.638 1.00 8.40  ? 376  TYR A C   1 
ATOM   2279 O  O   . TYR A 1 271 ? -12.640 21.597  -31.549 1.00 8.84  ? 376  TYR A O   1 
ATOM   2280 C  CB  . TYR A 1 271 ? -13.475 24.493  -32.291 1.00 9.31  ? 376  TYR A CB  1 
ATOM   2281 C  CG  . TYR A 1 271 ? -12.537 24.922  -33.332 1.00 9.63  ? 376  TYR A CG  1 
ATOM   2282 C  CD1 . TYR A 1 271 ? -12.934 25.481  -34.520 1.00 10.79 ? 376  TYR A CD1 1 
ATOM   2283 C  CD2 . TYR A 1 271 ? -11.198 24.799  -33.107 1.00 11.53 ? 376  TYR A CD2 1 
ATOM   2284 C  CE1 . TYR A 1 271 ? -12.002 25.914  -35.487 1.00 11.39 ? 376  TYR A CE1 1 
ATOM   2285 C  CE2 . TYR A 1 271 ? -10.197 25.246  -34.049 1.00 12.79 ? 376  TYR A CE2 1 
ATOM   2286 C  CZ  . TYR A 1 271 ? -10.632 25.785  -35.245 1.00 13.12 ? 376  TYR A CZ  1 
ATOM   2287 O  OH  . TYR A 1 271 ? -9.750  26.237  -36.215 1.00 14.26 ? 376  TYR A OH  1 
ATOM   2288 N  N   . PRO A 1 272 ? -12.702 21.453  -33.788 1.00 8.57  ? 377  PRO A N   1 
ATOM   2289 C  CA  . PRO A 1 272 ? -11.856 20.215  -33.714 1.00 8.48  ? 377  PRO A CA  1 
ATOM   2290 C  C   . PRO A 1 272 ? -10.558 20.413  -33.042 1.00 9.81  ? 377  PRO A C   1 
ATOM   2291 O  O   . PRO A 1 272 ? -9.810  21.406  -33.281 1.00 10.42 ? 377  PRO A O   1 
ATOM   2292 C  CB  . PRO A 1 272 ? -11.655 19.889  -35.185 1.00 10.07 ? 377  PRO A CB  1 
ATOM   2293 C  CG  . PRO A 1 272 ? -12.923 20.382  -35.857 1.00 9.29  ? 377  PRO A CG  1 
ATOM   2294 C  CD  . PRO A 1 272 ? -13.135 21.730  -35.174 1.00 8.82  ? 377  PRO A CD  1 
ATOM   2295 N  N   . GLN A 1 273 ? -10.216 19.361  -32.236 1.00 9.66  ? 378  GLN A N   1 
ATOM   2296 C  CA  . GLN A 1 273 ? -8.859  19.261  -31.623 1.00 10.14 ? 378  GLN A CA  1 
ATOM   2297 C  C   . GLN A 1 273 ? -8.418  17.839  -31.833 1.00 11.05 ? 378  GLN A C   1 
ATOM   2298 O  O   . GLN A 1 273 ? -9.091  16.900  -31.362 1.00 10.04 ? 378  GLN A O   1 
ATOM   2299 C  CB  . GLN A 1 273 ? -8.836  19.599  -30.133 1.00 10.09 ? 378  GLN A CB  1 
ATOM   2300 C  CG  . GLN A 1 273 ? -9.167  21.070  -29.794 1.00 10.23 ? 378  GLN A CG  1 
ATOM   2301 C  CD  . GLN A 1 273 ? -9.078  21.314  -28.275 1.00 12.63 ? 378  GLN A CD  1 
ATOM   2302 O  OE1 . GLN A 1 273 ? -10.030 21.814  -27.649 1.00 15.00 ? 378  GLN A OE1 1 
ATOM   2303 N  NE2 . GLN A 1 273 ? -7.975  20.960  -27.629 1.00 11.31 ? 378  GLN A NE2 1 
ATOM   2304 N  N   . GLU A 1 274 ? -7.268  17.600  -32.546 1.00 11.29 ? 379  GLU A N   1 
ATOM   2305 C  CA  C GLU A 1 274 ? -6.943  16.201  -32.907 0.44 13.04 ? 379  GLU A CA  1 
ATOM   2306 C  CA  D GLU A 1 274 ? -6.853  16.237  -32.872 0.56 12.65 ? 379  GLU A CA  1 
ATOM   2307 C  C   . GLU A 1 274 ? -6.757  15.354  -31.605 1.00 12.03 ? 379  GLU A C   1 
ATOM   2308 O  O   . GLU A 1 274 ? -6.203  15.831  -30.570 1.00 12.90 ? 379  GLU A O   1 
ATOM   2309 C  CB  C GLU A 1 274 ? -5.715  16.169  -33.872 0.44 14.80 ? 379  GLU A CB  1 
ATOM   2310 C  CB  D GLU A 1 274 ? -5.480  16.362  -33.540 0.56 13.03 ? 379  GLU A CB  1 
ATOM   2311 C  CG  C GLU A 1 274 ? -5.628  14.954  -34.880 0.44 21.00 ? 379  GLU A CG  1 
ATOM   2312 C  CG  D GLU A 1 274 ? -5.028  15.013  -34.091 0.56 15.46 ? 379  GLU A CG  1 
ATOM   2313 C  CD  C GLU A 1 274 ? -6.661  14.948  -36.047 0.44 22.42 ? 379  GLU A CD  1 
ATOM   2314 C  CD  D GLU A 1 274 ? -3.831  15.060  -34.990 0.56 19.67 ? 379  GLU A CD  1 
ATOM   2315 O  OE1 C GLU A 1 274 ? -6.731  15.928  -36.916 0.44 19.24 ? 379  GLU A OE1 1 
ATOM   2316 O  OE1 D GLU A 1 274 ? -3.092  16.050  -35.032 0.56 22.14 ? 379  GLU A OE1 1 
ATOM   2317 O  OE2 C GLU A 1 274 ? -7.422  13.915  -36.149 0.44 24.46 ? 379  GLU A OE2 1 
ATOM   2318 O  OE2 D GLU A 1 274 ? -3.626  13.983  -35.617 0.56 27.37 ? 379  GLU A OE2 1 
ATOM   2319 N  N   . ASN A 1 275 ? -7.276  14.170  -31.724 1.00 11.70 ? 380  ASN A N   1 
ATOM   2320 C  CA  . ASN A 1 275 ? -7.210  13.187  -30.546 1.00 12.61 ? 380  ASN A CA  1 
ATOM   2321 C  C   . ASN A 1 275 ? -7.966  13.607  -29.318 1.00 11.05 ? 380  ASN A C   1 
ATOM   2322 O  O   . ASN A 1 275 ? -7.818  13.054  -28.226 1.00 11.14 ? 380  ASN A O   1 
ATOM   2323 C  CB  . ASN A 1 275 ? -5.703  12.898  -30.149 1.00 15.94 ? 380  ASN A CB  1 
ATOM   2324 C  CG  . ASN A 1 275 ? -4.851  12.436  -31.373 1.00 20.31 ? 380  ASN A CG  1 
ATOM   2325 O  OD1 . ASN A 1 275 ? -5.341  11.614  -32.132 1.00 22.63 ? 380  ASN A OD1 1 
ATOM   2326 N  ND2 . ASN A 1 275 ? -3.701  13.099  -31.617 1.00 24.22 ? 380  ASN A ND2 1 
ATOM   2327 N  N   . ILE A 1 276 ? -8.941  14.528  -29.515 1.00 10.44 ? 381  ILE A N   1 
ATOM   2328 C  CA  . ILE A 1 276 ? -9.828  14.957  -28.402 1.00 9.92  ? 381  ILE A CA  1 
ATOM   2329 C  C   . ILE A 1 276 ? -11.282 14.983  -28.914 1.00 7.70  ? 381  ILE A C   1 
ATOM   2330 O  O   . ILE A 1 276 ? -12.135 14.288  -28.449 1.00 8.49  ? 381  ILE A O   1 
ATOM   2331 C  CB  . ILE A 1 276 ? -9.492  16.332  -27.856 1.00 10.14 ? 381  ILE A CB  1 
ATOM   2332 C  CG1 . ILE A 1 276 ? -8.040  16.340  -27.324 1.00 10.47 ? 381  ILE A CG1 1 
ATOM   2333 C  CG2 . ILE A 1 276 ? -10.500 16.724  -26.738 1.00 10.15 ? 381  ILE A CG2 1 
ATOM   2334 C  CD1 . ILE A 1 276 ? -7.515  17.686  -26.801 1.00 11.77 ? 381  ILE A CD1 1 
ATOM   2335 N  N   . ILE A 1 277 ? -11.502 15.900  -29.916 1.00 8.33  ? 382  ILE A N   1 
ATOM   2336 C  CA  . ILE A 1 277 ? -12.866 16.128  -30.383 1.00 8.77  ? 382  ILE A CA  1 
ATOM   2337 C  C   . ILE A 1 277 ? -12.841 16.305  -31.919 1.00 8.21  ? 382  ILE A C   1 
ATOM   2338 O  O   . ILE A 1 277 ? -12.038 17.096  -32.436 1.00 8.91  ? 382  ILE A O   1 
ATOM   2339 C  CB  . ILE A 1 277 ? -13.542 17.342  -29.635 1.00 8.15  ? 382  ILE A CB  1 
ATOM   2340 C  CG1 . ILE A 1 277 ? -14.977 17.675  -30.216 1.00 8.75  ? 382  ILE A CG1 1 
ATOM   2341 C  CG2 . ILE A 1 277 ? -12.666 18.642  -29.608 1.00 9.32  ? 382  ILE A CG2 1 
ATOM   2342 C  CD1 . ILE A 1 277 ? -16.065 16.646  -30.004 1.00 10.67 ? 382  ILE A CD1 1 
ATOM   2343 N  N   . ASP A 1 278 ? -13.772 15.663  -32.596 1.00 8.44  ? 383  ASP A N   1 
ATOM   2344 C  CA  . ASP A 1 278 ? -13.903 15.800  -34.075 1.00 9.42  ? 383  ASP A CA  1 
ATOM   2345 C  C   . ASP A 1 278 ? -15.333 16.222  -34.314 1.00 9.26  ? 383  ASP A C   1 
ATOM   2346 O  O   . ASP A 1 278 ? -16.304 15.634  -33.782 1.00 9.22  ? 383  ASP A O   1 
ATOM   2347 C  CB  . ASP A 1 278 ? -13.729 14.375  -34.731 1.00 9.31  ? 383  ASP A CB  1 
ATOM   2348 C  CG  . ASP A 1 278 ? -12.250 14.111  -34.925 1.00 10.95 ? 383  ASP A CG  1 
ATOM   2349 O  OD1 . ASP A 1 278 ? -11.589 14.735  -35.802 1.00 11.69 ? 383  ASP A OD1 1 
ATOM   2350 O  OD2 . ASP A 1 278 ? -11.662 13.393  -34.098 1.00 12.68 ? 383  ASP A OD2 1 
ATOM   2351 N  N   . THR A 1 279 ? -15.488 17.224  -35.233 1.00 9.42  ? 384  THR A N   1 
ATOM   2352 C  CA  . THR A 1 279 ? -16.821 17.674  -35.685 1.00 9.41  ? 384  THR A CA  1 
ATOM   2353 C  C   . THR A 1 279 ? -16.730 17.883  -37.186 1.00 8.49  ? 384  THR A C   1 
ATOM   2354 O  O   . THR A 1 279 ? -15.756 18.546  -37.651 1.00 9.02  ? 384  THR A O   1 
ATOM   2355 C  CB  . THR A 1 279 ? -17.223 18.998  -35.001 1.00 8.97  ? 384  THR A CB  1 
ATOM   2356 O  OG1 . THR A 1 279 ? -17.215 18.823  -33.569 1.00 9.38  ? 384  THR A OG1 1 
ATOM   2357 C  CG2 . THR A 1 279 ? -18.624 19.451  -35.430 1.00 9.95  ? 384  THR A CG2 1 
ATOM   2358 N  N   . PHE A 1 280 ? -17.650 17.271  -37.893 1.00 8.54  ? 385  PHE A N   1 
ATOM   2359 C  CA  . PHE A 1 280 ? -17.754 17.409  -39.356 1.00 9.24  ? 385  PHE A CA  1 
ATOM   2360 C  C   . PHE A 1 280 ? -19.120 17.971  -39.679 1.00 8.93  ? 385  PHE A C   1 
ATOM   2361 O  O   . PHE A 1 280 ? -20.140 17.590  -39.149 1.00 10.08 ? 385  PHE A O   1 
ATOM   2362 C  CB  . PHE A 1 280 ? -17.539 16.046  -40.103 1.00 10.32 ? 385  PHE A CB  1 
ATOM   2363 C  CG  . PHE A 1 280 ? -16.096 15.582  -40.127 1.00 10.93 ? 385  PHE A CG  1 
ATOM   2364 C  CD1 . PHE A 1 280 ? -15.308 15.596  -41.338 1.00 13.55 ? 385  PHE A CD1 1 
ATOM   2365 C  CD2 . PHE A 1 280 ? -15.516 15.092  -38.974 1.00 14.29 ? 385  PHE A CD2 1 
ATOM   2366 C  CE1 . PHE A 1 280 ? -13.983 15.115  -41.324 1.00 14.29 ? 385  PHE A CE1 1 
ATOM   2367 C  CE2 . PHE A 1 280 ? -14.152 14.693  -39.008 1.00 14.93 ? 385  PHE A CE2 1 
ATOM   2368 C  CZ  . PHE A 1 280 ? -13.436 14.742  -40.167 1.00 14.81 ? 385  PHE A CZ  1 
ATOM   2369 N  N   . VAL A 1 281 ? -19.086 18.985  -40.588 1.00 9.50  ? 386  VAL A N   1 
ATOM   2370 C  CA  . VAL A 1 281 ? -20.287 19.646  -41.044 1.00 9.25  ? 386  VAL A CA  1 
ATOM   2371 C  C   . VAL A 1 281 ? -20.601 19.209  -42.522 1.00 10.40 ? 386  VAL A C   1 
ATOM   2372 O  O   . VAL A 1 281 ? -19.710 18.787  -43.241 1.00 10.75 ? 386  VAL A O   1 
ATOM   2373 C  CB  . VAL A 1 281 ? -20.207 21.185  -40.999 1.00 9.31  ? 386  VAL A CB  1 
ATOM   2374 C  CG1 . VAL A 1 281 ? -19.911 21.703  -39.565 1.00 10.71 ? 386  VAL A CG1 1 
ATOM   2375 C  CG2 . VAL A 1 281 ? -19.064 21.712  -41.883 1.00 11.52 ? 386  VAL A CG2 1 
ATOM   2376 N  N   . VAL A 1 282 ? -21.886 19.271  -42.863 1.00 9.57  ? 387  VAL A N   1 
ATOM   2377 C  CA  . VAL A 1 282 ? -22.306 19.022  -44.305 1.00 9.78  ? 387  VAL A CA  1 
ATOM   2378 C  C   . VAL A 1 282 ? -22.573 20.417  -44.878 1.00 10.18 ? 387  VAL A C   1 
ATOM   2379 O  O   . VAL A 1 282 ? -23.465 21.168  -44.390 1.00 11.27 ? 387  VAL A O   1 
ATOM   2380 C  CB  . VAL A 1 282 ? -23.566 18.193  -44.353 1.00 10.87 ? 387  VAL A CB  1 
ATOM   2381 C  CG1 . VAL A 1 282 ? -24.057 18.041  -45.823 1.00 11.06 ? 387  VAL A CG1 1 
ATOM   2382 C  CG2 . VAL A 1 282 ? -23.340 16.798  -43.745 1.00 12.25 ? 387  VAL A CG2 1 
ATOM   2383 N  N   . GLU A 1 283 ? -21.811 20.777  -45.887 1.00 10.18 ? 388  GLU A N   1 
ATOM   2384 C  CA  . GLU A 1 283 ? -21.975 22.045  -46.637 1.00 10.49 ? 388  GLU A CA  1 
ATOM   2385 C  C   . GLU A 1 283 ? -22.530 21.777  -48.050 1.00 11.35 ? 388  GLU A C   1 
ATOM   2386 O  O   . GLU A 1 283 ? -21.837 21.060  -48.828 1.00 13.13 ? 388  GLU A O   1 
ATOM   2387 C  CB  . GLU A 1 283 ? -20.710 22.792  -46.717 1.00 11.21 ? 388  GLU A CB  1 
ATOM   2388 C  CG  . GLU A 1 283 ? -20.867 24.095  -47.545 1.00 10.12 ? 388  GLU A CG  1 
ATOM   2389 C  CD  . GLU A 1 283 ? -19.580 24.753  -47.798 1.00 11.55 ? 388  GLU A CD  1 
ATOM   2390 O  OE1 . GLU A 1 283 ? -19.614 25.754  -48.702 1.00 12.28 ? 388  GLU A OE1 1 
ATOM   2391 O  OE2 . GLU A 1 283 ? -18.432 24.511  -47.360 1.00 12.95 ? 388  GLU A OE2 1 
ATOM   2392 N  N   . ASN A 1 284 ? -23.759 22.193  -48.279 1.00 12.12 ? 389  ASN A N   1 
ATOM   2393 C  CA  . ASN A 1 284 ? -24.459 21.823  -49.525 1.00 13.02 ? 389  ASN A CA  1 
ATOM   2394 C  C   . ASN A 1 284 ? -23.960 22.641  -50.763 1.00 10.68 ? 389  ASN A C   1 
ATOM   2395 O  O   . ASN A 1 284 ? -22.974 23.379  -50.763 1.00 10.93 ? 389  ASN A O   1 
ATOM   2396 C  CB  . ASN A 1 284 ? -26.012 21.934  -49.322 1.00 14.14 ? 389  ASN A CB  1 
ATOM   2397 C  CG  . ASN A 1 284 ? -26.492 23.320  -49.217 1.00 14.58 ? 389  ASN A CG  1 
ATOM   2398 O  OD1 . ASN A 1 284 ? -25.785 24.277  -49.532 1.00 13.52 ? 389  ASN A OD1 1 
ATOM   2399 N  ND2 . ASN A 1 284 ? -27.749 23.457  -48.772 1.00 16.93 ? 389  ASN A ND2 1 
ATOM   2400 N  N   . ALA A 1 285 ? -24.679 22.392  -51.874 1.00 12.01 ? 390  ALA A N   1 
ATOM   2401 C  CA  . ALA A 1 285 ? -24.307 22.930  -53.212 1.00 10.99 ? 390  ALA A CA  1 
ATOM   2402 C  C   . ALA A 1 285 ? -24.452 24.442  -53.245 1.00 11.27 ? 390  ALA A C   1 
ATOM   2403 O  O   . ALA A 1 285 ? -23.916 25.116  -54.127 1.00 11.18 ? 390  ALA A O   1 
ATOM   2404 C  CB  . ALA A 1 285 ? -25.170 22.246  -54.233 1.00 12.49 ? 390  ALA A CB  1 
ATOM   2405 N  N   . ASN A 1 286 ? -25.241 24.973  -52.311 1.00 11.42 ? 391  ASN A N   1 
ATOM   2406 C  CA  . ASN A 1 286 ? -25.432 26.386  -52.126 1.00 11.54 ? 391  ASN A CA  1 
ATOM   2407 C  C   . ASN A 1 286 ? -24.460 27.037  -51.135 1.00 12.68 ? 391  ASN A C   1 
ATOM   2408 O  O   . ASN A 1 286 ? -24.511 28.276  -50.951 1.00 13.90 ? 391  ASN A O   1 
ATOM   2409 C  CB  . ASN A 1 286 ? -26.910 26.685  -51.627 1.00 14.63 ? 391  ASN A CB  1 
ATOM   2410 C  CG  . ASN A 1 286 ? -27.936 26.438  -52.702 1.00 20.01 ? 391  ASN A CG  1 
ATOM   2411 O  OD1 . ASN A 1 286 ? -27.994 25.424  -53.257 1.00 20.75 ? 391  ASN A OD1 1 
ATOM   2412 N  ND2 . ASN A 1 286 ? -28.665 27.477  -53.051 1.00 23.94 ? 391  ASN A ND2 1 
ATOM   2413 N  N   . GLY A 1 287 ? -23.548 26.252  -50.513 1.00 12.10 ? 392  GLY A N   1 
ATOM   2414 C  CA  . GLY A 1 287 ? -22.702 26.788  -49.507 1.00 12.95 ? 392  GLY A CA  1 
ATOM   2415 C  C   . GLY A 1 287 ? -23.243 26.803  -48.088 1.00 11.86 ? 392  GLY A C   1 
ATOM   2416 O  O   . GLY A 1 287 ? -22.583 27.422  -47.237 1.00 14.85 ? 392  GLY A O   1 
ATOM   2417 N  N   . GLU A 1 288 ? -24.377 26.228  -47.895 1.00 11.89 ? 393  GLU A N   1 
ATOM   2418 C  CA  A GLU A 1 288 ? -25.126 26.314  -46.565 0.50 12.04 ? 393  GLU A CA  1 
ATOM   2419 C  CA  B GLU A 1 288 ? -25.006 26.349  -46.552 0.50 12.40 ? 393  GLU A CA  1 
ATOM   2420 C  C   . GLU A 1 288 ? -24.693 25.061  -45.780 1.00 12.40 ? 393  GLU A C   1 
ATOM   2421 O  O   . GLU A 1 288 ? -24.776 23.958  -46.281 1.00 11.19 ? 393  GLU A O   1 
ATOM   2422 C  CB  A GLU A 1 288 ? -26.687 26.258  -46.736 0.50 14.59 ? 393  GLU A CB  1 
ATOM   2423 C  CB  B GLU A 1 288 ? -26.505 26.501  -46.711 0.50 15.75 ? 393  GLU A CB  1 
ATOM   2424 C  CG  A GLU A 1 288 ? -27.530 26.637  -45.468 0.50 17.03 ? 393  GLU A CG  1 
ATOM   2425 C  CG  B GLU A 1 288 ? -26.892 27.723  -47.532 0.50 19.08 ? 393  GLU A CG  1 
ATOM   2426 C  CD  A GLU A 1 288 ? -29.072 26.336  -45.566 0.50 20.16 ? 393  GLU A CD  1 
ATOM   2427 C  CD  B GLU A 1 288 ? -28.217 27.661  -48.290 0.50 22.54 ? 393  GLU A CD  1 
ATOM   2428 O  OE1 A GLU A 1 288 ? -29.630 26.056  -46.617 0.50 26.34 ? 393  GLU A OE1 1 
ATOM   2429 O  OE1 B GLU A 1 288 ? -28.640 28.788  -48.781 0.50 24.15 ? 393  GLU A OE1 1 
ATOM   2430 O  OE2 A GLU A 1 288 ? -29.711 26.288  -44.538 0.50 20.31 ? 393  GLU A OE2 1 
ATOM   2431 O  OE2 B GLU A 1 288 ? -28.783 26.531  -48.524 0.50 19.41 ? 393  GLU A OE2 1 
ATOM   2432 N  N   . VAL A 1 289 ? -24.399 25.261  -44.483 1.00 11.57 ? 394  VAL A N   1 
ATOM   2433 C  CA  . VAL A 1 289 ? -24.219 24.096  -43.565 1.00 10.92 ? 394  VAL A CA  1 
ATOM   2434 C  C   . VAL A 1 289 ? -25.553 23.671  -43.016 1.00 10.55 ? 394  VAL A C   1 
ATOM   2435 O  O   . VAL A 1 289 ? -26.289 24.509  -42.378 1.00 12.65 ? 394  VAL A O   1 
ATOM   2436 C  CB  . VAL A 1 289 ? -23.242 24.506  -42.426 1.00 10.80 ? 394  VAL A CB  1 
ATOM   2437 C  CG1 . VAL A 1 289 ? -23.210 23.444  -41.325 1.00 11.78 ? 394  VAL A CG1 1 
ATOM   2438 C  CG2 . VAL A 1 289 ? -21.842 24.788  -42.962 1.00 14.60 ? 394  VAL A CG2 1 
ATOM   2439 N  N   . THR A 1 290 ? -25.921 22.419  -43.202 1.00 10.15 ? 395  THR A N   1 
ATOM   2440 C  CA  . THR A 1 290 ? -27.238 21.933  -42.840 1.00 11.48 ? 395  THR A CA  1 
ATOM   2441 C  C   . THR A 1 290 ? -27.254 20.798  -41.786 1.00 11.30 ? 395  THR A C   1 
ATOM   2442 O  O   . THR A 1 290 ? -28.293 20.418  -41.296 1.00 12.93 ? 395  THR A O   1 
ATOM   2443 C  CB  . THR A 1 290 ? -27.912 21.351  -44.120 1.00 12.62 ? 395  THR A CB  1 
ATOM   2444 O  OG1 . THR A 1 290 ? -27.045 20.380  -44.746 1.00 12.64 ? 395  THR A OG1 1 
ATOM   2445 C  CG2 . THR A 1 290 ? -28.168 22.545  -45.164 1.00 14.17 ? 395  THR A CG2 1 
ATOM   2446 N  N   . ASP A 1 291 ? -26.081 20.221  -41.518 1.00 9.87  ? 396  ASP A N   1 
ATOM   2447 C  CA  . ASP A 1 291 ? -26.000 19.082  -40.559 1.00 10.91 ? 396  ASP A CA  1 
ATOM   2448 C  C   . ASP A 1 291 ? -24.588 19.092  -39.986 1.00 10.65 ? 396  ASP A C   1 
ATOM   2449 O  O   . ASP A 1 291 ? -23.681 19.620  -40.557 1.00 10.41 ? 396  ASP A O   1 
ATOM   2450 C  CB  . ASP A 1 291 ? -26.134 17.722  -41.360 1.00 10.71 ? 396  ASP A CB  1 
ATOM   2451 C  CG  . ASP A 1 291 ? -27.424 17.684  -42.269 1.00 11.36 ? 396  ASP A CG  1 
ATOM   2452 O  OD1 . ASP A 1 291 ? -27.178 18.026  -43.499 1.00 13.40 ? 396  ASP A OD1 1 
ATOM   2453 O  OD2 . ASP A 1 291 ? -28.551 17.376  -41.796 1.00 13.20 ? 396  ASP A OD2 1 
ATOM   2454 N  N   . PHE A 1 292 ? -24.464 18.388  -38.825 1.00 9.77  ? 397  PHE A N   1 
ATOM   2455 C  CA  . PHE A 1 292 ? -23.090 18.099  -38.353 1.00 10.38 ? 397  PHE A CA  1 
ATOM   2456 C  C   . PHE A 1 292 ? -23.137 16.841  -37.488 1.00 9.19  ? 397  PHE A C   1 
ATOM   2457 O  O   . PHE A 1 292 ? -24.124 16.508  -36.904 1.00 10.33 ? 397  PHE A O   1 
ATOM   2458 C  CB  . PHE A 1 292 ? -22.458 19.289  -37.603 1.00 9.54  ? 397  PHE A CB  1 
ATOM   2459 C  CG  . PHE A 1 292 ? -23.022 19.596  -36.247 1.00 9.70  ? 397  PHE A CG  1 
ATOM   2460 C  CD1 . PHE A 1 292 ? -22.563 18.928  -35.119 1.00 10.91 ? 397  PHE A CD1 1 
ATOM   2461 C  CD2 . PHE A 1 292 ? -24.010 20.609  -36.088 1.00 9.75  ? 397  PHE A CD2 1 
ATOM   2462 C  CE1 . PHE A 1 292 ? -22.995 19.248  -33.827 1.00 10.51 ? 397  PHE A CE1 1 
ATOM   2463 C  CE2 . PHE A 1 292 ? -24.466 20.893  -34.834 1.00 11.13 ? 397  PHE A CE2 1 
ATOM   2464 C  CZ  . PHE A 1 292 ? -23.985 20.211  -33.701 1.00 12.10 ? 397  PHE A CZ  1 
ATOM   2465 N  N   . LEU A 1 293 ? -21.958 16.207  -37.438 1.00 9.17  ? 398  LEU A N   1 
ATOM   2466 C  CA  . LEU A 1 293 ? -21.768 15.036  -36.527 1.00 9.74  ? 398  LEU A CA  1 
ATOM   2467 C  C   . LEU A 1 293 ? -20.536 15.348  -35.688 1.00 9.28  ? 398  LEU A C   1 
ATOM   2468 O  O   . LEU A 1 293 ? -19.629 16.119  -36.064 1.00 9.16  ? 398  LEU A O   1 
ATOM   2469 C  CB  . LEU A 1 293 ? -21.525 13.751  -37.397 1.00 10.18 ? 398  LEU A CB  1 
ATOM   2470 C  CG  . LEU A 1 293 ? -20.262 13.754  -38.269 1.00 9.63  ? 398  LEU A CG  1 
ATOM   2471 C  CD1 . LEU A 1 293 ? -18.978 13.189  -37.559 1.00 11.26 ? 398  LEU A CD1 1 
ATOM   2472 C  CD2 . LEU A 1 293 ? -20.506 12.933  -39.579 1.00 11.64 ? 398  LEU A CD2 1 
ATOM   2473 N  N   . SER A 1 294 ? -20.465 14.706  -34.493 1.00 9.28  ? 399  SER A N   1 
ATOM   2474 C  CA  . SER A 1 294 ? -19.291 14.926  -33.629 1.00 8.75  ? 399  SER A CA  1 
ATOM   2475 C  C   . SER A 1 294 ? -19.071 13.641  -32.748 1.00 7.60  ? 399  SER A C   1 
ATOM   2476 O  O   . SER A 1 294 ? -20.018 12.976  -32.397 1.00 8.88  ? 399  SER A O   1 
ATOM   2477 C  CB  . SER A 1 294 ? -19.413 16.211  -32.754 1.00 8.87  ? 399  SER A CB  1 
ATOM   2478 O  OG  . SER A 1 294 ? -20.554 16.145  -31.872 1.00 9.65  ? 399  SER A OG  1 
ATOM   2479 N  N   . PHE A 1 295 ? -17.800 13.475  -32.427 1.00 8.63  ? 400  PHE A N   1 
ATOM   2480 C  CA  . PHE A 1 295 ? -17.469 12.346  -31.489 1.00 7.98  ? 400  PHE A CA  1 
ATOM   2481 C  C   . PHE A 1 295 ? -16.170 12.674  -30.826 1.00 8.16  ? 400  PHE A C   1 
ATOM   2482 O  O   . PHE A 1 295 ? -15.291 13.376  -31.421 1.00 8.96  ? 400  PHE A O   1 
ATOM   2483 C  CB  . PHE A 1 295 ? -17.418 10.974  -32.323 1.00 10.90 ? 400  PHE A CB  1 
ATOM   2484 C  CG  . PHE A 1 295 ? -16.466 10.999  -33.509 1.00 10.05 ? 400  PHE A CG  1 
ATOM   2485 C  CD1 . PHE A 1 295 ? -15.077 10.741  -33.380 1.00 10.06 ? 400  PHE A CD1 1 
ATOM   2486 C  CD2 . PHE A 1 295 ? -16.992 11.194  -34.793 1.00 10.26 ? 400  PHE A CD2 1 
ATOM   2487 C  CE1 . PHE A 1 295 ? -14.246 10.713  -34.470 1.00 11.22 ? 400  PHE A CE1 1 
ATOM   2488 C  CE2 . PHE A 1 295 ? -16.160 11.133  -35.918 1.00 11.29 ? 400  PHE A CE2 1 
ATOM   2489 C  CZ  . PHE A 1 295 ? -14.816 10.889  -35.764 1.00 11.06 ? 400  PHE A CZ  1 
ATOM   2490 N  N   . TYR A 1 296 ? -16.042 12.243  -29.579 1.00 8.99  ? 401  TYR A N   1 
ATOM   2491 C  CA  . TYR A 1 296 ? -14.817 12.511  -28.827 1.00 9.34  ? 401  TYR A CA  1 
ATOM   2492 C  C   . TYR A 1 296 ? -13.932 11.249  -28.663 1.00 8.53  ? 401  TYR A C   1 
ATOM   2493 O  O   . TYR A 1 296 ? -14.477 10.114  -28.867 1.00 8.95  ? 401  TYR A O   1 
ATOM   2494 C  CB  . TYR A 1 296 ? -15.082 13.202  -27.434 1.00 9.51  ? 401  TYR A CB  1 
ATOM   2495 C  CG  . TYR A 1 296 ? -15.931 12.427  -26.448 1.00 9.04  ? 401  TYR A CG  1 
ATOM   2496 C  CD1 . TYR A 1 296 ? -15.379 11.435  -25.600 1.00 9.18  ? 401  TYR A CD1 1 
ATOM   2497 C  CD2 . TYR A 1 296 ? -17.308 12.698  -26.358 1.00 11.05 ? 401  TYR A CD2 1 
ATOM   2498 C  CE1 . TYR A 1 296 ? -16.242 10.777  -24.657 1.00 10.46 ? 401  TYR A CE1 1 
ATOM   2499 C  CE2 . TYR A 1 296 ? -18.126 12.026  -25.441 1.00 12.34 ? 401  TYR A CE2 1 
ATOM   2500 C  CZ  . TYR A 1 296 ? -17.565 11.074  -24.610 1.00 11.37 ? 401  TYR A CZ  1 
ATOM   2501 O  OH  . TYR A 1 296 ? -18.385 10.345  -23.714 1.00 14.73 ? 401  TYR A OH  1 
ATOM   2502 N  N   . THR A 1 297 ? -12.675 11.461  -28.440 1.00 8.79  ? 402  THR A N   1 
ATOM   2503 C  CA  . THR A 1 297 ? -11.641 10.357  -28.393 1.00 9.22  ? 402  THR A CA  1 
ATOM   2504 C  C   . THR A 1 297 ? -11.319 10.006  -26.948 1.00 9.40  ? 402  THR A C   1 
ATOM   2505 O  O   . THR A 1 297 ? -10.904 10.877  -26.166 1.00 10.08 ? 402  THR A O   1 
ATOM   2506 C  CB  . THR A 1 297 ? -10.351 10.948  -29.022 1.00 9.47  ? 402  THR A CB  1 
ATOM   2507 O  OG1 . THR A 1 297 ? -10.532 11.219  -30.426 1.00 10.52 ? 402  THR A OG1 1 
ATOM   2508 C  CG2 . THR A 1 297 ? -9.124  9.940   -28.935 1.00 11.45 ? 402  THR A CG2 1 
ATOM   2509 N  N   . LEU A 1 298 ? -11.552 8.719   -26.571 1.00 9.36  ? 403  LEU A N   1 
ATOM   2510 C  CA  . LEU A 1 298 ? -11.336 8.358   -25.144 1.00 9.03  ? 403  LEU A CA  1 
ATOM   2511 C  C   . LEU A 1 298 ? -10.841 6.851   -25.179 1.00 9.23  ? 403  LEU A C   1 
ATOM   2512 O  O   . LEU A 1 298 ? -11.709 5.951   -25.312 1.00 9.82  ? 403  LEU A O   1 
ATOM   2513 C  CB  . LEU A 1 298 ? -12.634 8.513   -24.349 1.00 9.90  ? 403  LEU A CB  1 
ATOM   2514 C  CG  . LEU A 1 298 ? -12.599 7.985   -22.893 1.00 9.89  ? 403  LEU A CG  1 
ATOM   2515 C  CD1 . LEU A 1 298 ? -11.397 8.505   -22.146 1.00 10.44 ? 403  LEU A CD1 1 
ATOM   2516 C  CD2 . LEU A 1 298 ? -13.910 8.317   -22.223 1.00 11.33 ? 403  LEU A CD2 1 
ATOM   2517 N  N   . PRO A 1 299 ? -9.517  6.681   -25.136 1.00 9.42  ? 404  PRO A N   1 
ATOM   2518 C  CA  . PRO A 1 299 ? -9.049  5.255   -25.128 1.00 9.83  ? 404  PRO A CA  1 
ATOM   2519 C  C   . PRO A 1 299 ? -9.328  4.616   -23.797 1.00 10.75 ? 404  PRO A C   1 
ATOM   2520 O  O   . PRO A 1 299 ? -9.485  5.303   -22.741 1.00 10.74 ? 404  PRO A O   1 
ATOM   2521 C  CB  . PRO A 1 299 ? -7.589  5.377   -25.366 1.00 11.20 ? 404  PRO A CB  1 
ATOM   2522 C  CG  . PRO A 1 299 ? -7.151  6.800   -24.858 1.00 12.27 ? 404  PRO A CG  1 
ATOM   2523 C  CD  . PRO A 1 299 ? -8.445  7.644   -25.082 1.00 11.01 ? 404  PRO A CD  1 
ATOM   2524 N  N   . SER A 1 300 ? -9.319  3.261   -23.771 1.00 11.65 ? 405  SER A N   1 
ATOM   2525 C  CA  . SER A 1 300 ? -9.340  2.465   -22.500 1.00 11.36 ? 405  SER A CA  1 
ATOM   2526 C  C   . SER A 1 300 ? -8.064  1.637   -22.395 1.00 12.29 ? 405  SER A C   1 
ATOM   2527 O  O   . SER A 1 300 ? -7.665  0.980   -23.392 1.00 13.93 ? 405  SER A O   1 
ATOM   2528 C  CB  . SER A 1 300 ? -10.533 1.605   -22.366 1.00 12.90 ? 405  SER A CB  1 
ATOM   2529 O  OG  . SER A 1 300 ? -11.756 2.390   -22.049 1.00 14.56 ? 405  SER A OG  1 
ATOM   2530 N  N   . THR A 1 301 ? -7.470  1.671   -21.259 1.00 11.40 ? 406  THR A N   1 
ATOM   2531 C  CA  . THR A 1 301 ? -6.369  0.677   -20.915 1.00 10.70 ? 406  THR A CA  1 
ATOM   2532 C  C   . THR A 1 301 ? -6.965  -0.702  -20.835 1.00 10.72 ? 406  THR A C   1 
ATOM   2533 O  O   . THR A 1 301 ? -8.022  -0.945  -20.322 1.00 11.50 ? 406  THR A O   1 
ATOM   2534 C  CB  . THR A 1 301 ? -5.851  1.044   -19.547 1.00 11.17 ? 406  THR A CB  1 
ATOM   2535 O  OG1 . THR A 1 301 ? -5.266  2.351   -19.633 1.00 12.90 ? 406  THR A OG1 1 
ATOM   2536 C  CG2 . THR A 1 301 ? -4.740  0.047   -19.117 1.00 13.96 ? 406  THR A CG2 1 
ATOM   2537 N  N   . ILE A 1 302 ? -6.231  -1.617  -21.518 1.00 11.48 ? 407  ILE A N   1 
ATOM   2538 C  CA  . ILE A 1 302 ? -6.600  -3.071  -21.510 1.00 12.90 ? 407  ILE A CA  1 
ATOM   2539 C  C   . ILE A 1 302 ? -5.833  -3.708  -20.356 1.00 12.24 ? 407  ILE A C   1 
ATOM   2540 O  O   . ILE A 1 302 ? -4.628  -3.857  -20.455 1.00 13.80 ? 407  ILE A O   1 
ATOM   2541 C  CB  . ILE A 1 302 ? -6.286  -3.704  -22.897 1.00 13.38 ? 407  ILE A CB  1 
ATOM   2542 C  CG1 . ILE A 1 302 ? -6.988  -2.926  -24.053 1.00 13.62 ? 407  ILE A CG1 1 
ATOM   2543 C  CG2 . ILE A 1 302 ? -6.790  -5.161  -22.850 1.00 14.57 ? 407  ILE A CG2 1 
ATOM   2544 C  CD1 . ILE A 1 302 ? -6.623  -3.482  -25.447 1.00 17.63 ? 407  ILE A CD1 1 
ATOM   2545 N  N   . MET A 1 303 ? -6.524  -3.905  -19.254 1.00 12.87 ? 408  MET A N   1 
ATOM   2546 C  CA  . MET A 1 303 ? -5.857  -4.211  -17.980 1.00 15.24 ? 408  MET A CA  1 
ATOM   2547 C  C   . MET A 1 303 ? -5.090  -5.551  -18.041 1.00 17.02 ? 408  MET A C   1 
ATOM   2548 O  O   . MET A 1 303 ? -5.625  -6.546  -18.511 1.00 14.63 ? 408  MET A O   1 
ATOM   2549 C  CB  . MET A 1 303 ? -6.925  -4.161  -16.854 1.00 17.59 ? 408  MET A CB  1 
ATOM   2550 C  CG  . MET A 1 303 ? -7.614  -2.677  -16.663 1.00 17.34 ? 408  MET A CG  1 
ATOM   2551 S  SD  . MET A 1 303 ? -9.154  -2.903  -15.714 1.00 16.60 ? 408  MET A SD  1 
ATOM   2552 C  CE  . MET A 1 303 ? -8.691  -3.822  -14.228 1.00 15.28 ? 408  MET A CE  1 
ATOM   2553 N  N   . ASN A 1 304 ? -3.825  -5.461  -17.609 1.00 16.18 ? 409  ASN A N   1 
ATOM   2554 C  CA  . ASN A 1 304 ? -2.963  -6.680  -17.407 1.00 16.92 ? 409  ASN A CA  1 
ATOM   2555 C  C   . ASN A 1 304 ? -2.775  -7.490  -18.680 1.00 19.38 ? 409  ASN A C   1 
ATOM   2556 O  O   . ASN A 1 304 ? -2.481  -8.685  -18.598 1.00 20.35 ? 409  ASN A O   1 
ATOM   2557 C  CB  . ASN A 1 304 ? -3.461  -7.622  -16.254 1.00 18.93 ? 409  ASN A CB  1 
ATOM   2558 C  CG  . ASN A 1 304 ? -3.801  -6.844  -14.998 1.00 20.23 ? 409  ASN A CG  1 
ATOM   2559 O  OD1 . ASN A 1 304 ? -5.033  -6.701  -14.629 1.00 26.44 ? 409  ASN A OD1 1 
ATOM   2560 N  ND2 . ASN A 1 304 ? -2.782  -6.200  -14.431 1.00 20.30 ? 409  ASN A ND2 1 
ATOM   2561 N  N   . HIS A 1 305 ? -2.845  -6.870  -19.868 1.00 16.84 ? 410  HIS A N   1 
ATOM   2562 C  CA  . HIS A 1 305 ? -2.759  -7.672  -21.075 1.00 15.79 ? 410  HIS A CA  1 
ATOM   2563 C  C   . HIS A 1 305 ? -1.355  -7.622  -21.641 1.00 15.55 ? 410  HIS A C   1 
ATOM   2564 O  O   . HIS A 1 305 ? -0.798  -6.550  -21.760 1.00 15.51 ? 410  HIS A O   1 
ATOM   2565 C  CB  . HIS A 1 305 ? -3.749  -7.021  -22.119 1.00 17.87 ? 410  HIS A CB  1 
ATOM   2566 C  CG  . HIS A 1 305 ? -4.139  -7.933  -23.237 1.00 18.48 ? 410  HIS A CG  1 
ATOM   2567 N  ND1 . HIS A 1 305 ? -4.794  -9.137  -23.038 1.00 20.33 ? 410  HIS A ND1 1 
ATOM   2568 C  CD2 . HIS A 1 305 ? -3.966  -7.794  -24.564 1.00 21.48 ? 410  HIS A CD2 1 
ATOM   2569 C  CE1 . HIS A 1 305 ? -5.004  -9.707  -24.216 1.00 21.43 ? 410  HIS A CE1 1 
ATOM   2570 N  NE2 . HIS A 1 305 ? -4.495  -8.922  -25.152 1.00 23.79 ? 410  HIS A NE2 1 
ATOM   2571 N  N   . PRO A 1 306 ? -0.765  -8.800  -22.010 1.00 15.70 ? 411  PRO A N   1 
ATOM   2572 C  CA  . PRO A 1 306 ? 0.623   -8.701  -22.444 1.00 15.24 ? 411  PRO A CA  1 
ATOM   2573 C  C   . PRO A 1 306 ? 0.892   -8.026  -23.789 1.00 13.50 ? 411  PRO A C   1 
ATOM   2574 O  O   . PRO A 1 306 ? 1.965   -7.478  -23.941 1.00 15.16 ? 411  PRO A O   1 
ATOM   2575 C  CB  . PRO A 1 306 ? 1.052   -10.233 -22.569 1.00 16.35 ? 411  PRO A CB  1 
ATOM   2576 C  CG  . PRO A 1 306 ? 0.110   -10.916 -21.565 1.00 16.43 ? 411  PRO A CG  1 
ATOM   2577 C  CD  . PRO A 1 306 ? -1.213  -10.151 -21.639 1.00 17.83 ? 411  PRO A CD  1 
ATOM   2578 N  N   . THR A 1 307 ? -0.062  -8.124  -24.718 1.00 16.19 ? 412  THR A N   1 
ATOM   2579 C  CA  . THR A 1 307 ? 0.188   -7.680  -26.129 1.00 18.23 ? 412  THR A CA  1 
ATOM   2580 C  C   . THR A 1 307 ? -0.442  -6.291  -26.320 1.00 20.36 ? 412  THR A C   1 
ATOM   2581 O  O   . THR A 1 307 ? 0.214   -5.319  -26.021 1.00 22.20 ? 412  THR A O   1 
ATOM   2582 C  CB  . THR A 1 307 ? -0.423  -8.710  -27.132 1.00 18.56 ? 412  THR A CB  1 
ATOM   2583 O  OG1 . THR A 1 307 ? -1.799  -8.912  -26.820 1.00 25.36 ? 412  THR A OG1 1 
ATOM   2584 C  CG2 . THR A 1 307 ? 0.297   -10.103 -27.024 1.00 24.21 ? 412  THR A CG2 1 
ATOM   2585 N  N   . HIS A 1 308 ? -1.700  -6.211  -26.676 1.00 21.82 ? 413  HIS A N   1 
ATOM   2586 C  CA  . HIS A 1 308 ? -2.344  -4.894  -26.928 1.00 17.98 ? 413  HIS A CA  1 
ATOM   2587 C  C   . HIS A 1 308 ? -2.583  -4.218  -25.545 1.00 15.38 ? 413  HIS A C   1 
ATOM   2588 O  O   . HIS A 1 308 ? -3.040  -4.834  -24.617 1.00 16.28 ? 413  HIS A O   1 
ATOM   2589 C  CB  . HIS A 1 308 ? -3.721  -5.087  -27.620 1.00 20.30 ? 413  HIS A CB  1 
ATOM   2590 C  CG  . HIS A 1 308 ? -3.641  -5.629  -29.041 1.00 23.20 ? 413  HIS A CG  1 
ATOM   2591 N  ND1 . HIS A 1 308 ? -3.019  -4.934  -30.070 1.00 25.08 ? 413  HIS A ND1 1 
ATOM   2592 C  CD2 . HIS A 1 308 ? -4.124  -6.780  -29.561 1.00 25.10 ? 413  HIS A CD2 1 
ATOM   2593 C  CE1 . HIS A 1 308 ? -3.122  -5.677  -31.182 1.00 27.34 ? 413  HIS A CE1 1 
ATOM   2594 N  NE2 . HIS A 1 308 ? -3.810  -6.780  -30.893 1.00 23.59 ? 413  HIS A NE2 1 
ATOM   2595 N  N   . LYS A 1 309 ? -2.188  -2.960  -25.479 1.00 14.55 ? 414  LYS A N   1 
ATOM   2596 C  CA  . LYS A 1 309 ? -2.258  -2.219  -24.219 1.00 11.91 ? 414  LYS A CA  1 
ATOM   2597 C  C   . LYS A 1 309 ? -3.440  -1.222  -24.156 1.00 12.39 ? 414  LYS A C   1 
ATOM   2598 O  O   . LYS A 1 309 ? -3.890  -0.896  -23.009 1.00 12.17 ? 414  LYS A O   1 
ATOM   2599 C  CB  . LYS A 1 309 ? -0.994  -1.471  -24.062 1.00 13.57 ? 414  LYS A CB  1 
ATOM   2600 C  CG  . LYS A 1 309 ? 0.310   -2.369  -24.055 1.00 14.48 ? 414  LYS A CG  1 
ATOM   2601 C  CD  . LYS A 1 309 ? 0.305   -3.373  -22.851 1.00 12.90 ? 414  LYS A CD  1 
ATOM   2602 C  CE  . LYS A 1 309 ? 1.654   -4.162  -22.959 1.00 13.53 ? 414  LYS A CE  1 
ATOM   2603 N  NZ  . LYS A 1 309 ? 1.721   -5.094  -21.810 1.00 13.53 ? 414  LYS A NZ  1 
ATOM   2604 N  N   . SER A 1 310 ? -3.979  -0.836  -25.305 1.00 14.15 ? 415  SER A N   1 
ATOM   2605 C  CA  . SER A 1 310 ? -4.915  0.334   -25.351 1.00 13.68 ? 415  SER A CA  1 
ATOM   2606 C  C   . SER A 1 310 ? -5.968  -0.019  -26.407 1.00 14.48 ? 415  SER A C   1 
ATOM   2607 O  O   . SER A 1 310 ? -5.649  -0.572  -27.494 1.00 17.24 ? 415  SER A O   1 
ATOM   2608 C  CB  . SER A 1 310 ? -4.129  1.573   -25.643 1.00 17.28 ? 415  SER A CB  1 
ATOM   2609 O  OG  . SER A 1 310 ? -5.116  2.714   -25.615 1.00 19.96 ? 415  SER A OG  1 
ATOM   2610 N  N   . LEU A 1 311 ? -7.238  0.186   -26.067 1.00 12.48 ? 416  LEU A N   1 
ATOM   2611 C  CA  . LEU A 1 311 ? -8.393  0.126   -26.955 1.00 15.11 ? 416  LEU A CA  1 
ATOM   2612 C  C   . LEU A 1 311 ? -8.717  1.573   -27.439 1.00 13.27 ? 416  LEU A C   1 
ATOM   2613 O  O   . LEU A 1 311 ? -8.908  2.471   -26.577 1.00 13.56 ? 416  LEU A O   1 
ATOM   2614 C  CB  . LEU A 1 311 ? -9.608  -0.386  -26.149 1.00 18.45 ? 416  LEU A CB  1 
ATOM   2615 C  CG  . LEU A 1 311 ? -10.989 -0.349  -26.753 1.00 18.36 ? 416  LEU A CG  1 
ATOM   2616 C  CD1 . LEU A 1 311 ? -10.928 -1.521  -27.754 1.00 21.39 ? 416  LEU A CD1 1 
ATOM   2617 C  CD2 . LEU A 1 311 ? -12.179 -0.520  -25.783 1.00 22.94 ? 416  LEU A CD2 1 
ATOM   2618 N  N   . LYS A 1 312 ? -8.646  1.816   -28.715 1.00 12.85 ? 417  LYS A N   1 
ATOM   2619 C  CA  A LYS A 1 312 ? -8.915  3.160   -29.305 0.70 14.17 ? 417  LYS A CA  1 
ATOM   2620 C  CA  B LYS A 1 312 ? -8.921  3.134   -29.285 0.30 12.64 ? 417  LYS A CA  1 
ATOM   2621 C  C   . LYS A 1 312 ? -10.409 3.295   -29.562 1.00 12.50 ? 417  LYS A C   1 
ATOM   2622 O  O   . LYS A 1 312 ? -11.004 2.590   -30.395 1.00 13.37 ? 417  LYS A O   1 
ATOM   2623 C  CB  A LYS A 1 312 ? -8.063  3.533   -30.576 0.70 17.20 ? 417  LYS A CB  1 
ATOM   2624 C  CB  B LYS A 1 312 ? -8.083  3.338   -30.539 0.30 13.09 ? 417  LYS A CB  1 
ATOM   2625 C  CG  A LYS A 1 312 ? -8.218  5.033   -30.991 0.70 24.17 ? 417  LYS A CG  1 
ATOM   2626 C  CG  B LYS A 1 312 ? -6.603  3.044   -30.309 0.30 12.08 ? 417  LYS A CG  1 
ATOM   2627 C  CD  A LYS A 1 312 ? -7.441  5.681   -32.179 0.70 27.47 ? 417  LYS A CD  1 
ATOM   2628 C  CD  B LYS A 1 312 ? -6.036  3.712   -29.073 0.30 16.27 ? 417  LYS A CD  1 
ATOM   2629 C  CE  A LYS A 1 312 ? -7.779  7.152   -32.338 0.70 25.27 ? 417  LYS A CE  1 
ATOM   2630 C  CE  B LYS A 1 312 ? -5.738  5.180   -29.267 0.30 17.67 ? 417  LYS A CE  1 
ATOM   2631 N  NZ  A LYS A 1 312 ? -6.822  7.827   -33.252 0.70 32.68 ? 417  LYS A NZ  1 
ATOM   2632 N  NZ  B LYS A 1 312 ? -5.111  5.661   -28.025 0.30 16.67 ? 417  LYS A NZ  1 
ATOM   2633 N  N   . ALA A 1 313 ? -11.127 4.134   -28.747 1.00 10.80 ? 418  ALA A N   1 
ATOM   2634 C  CA  . ALA A 1 313 ? -12.584 4.200   -28.789 1.00 11.10 ? 418  ALA A CA  1 
ATOM   2635 C  C   . ALA A 1 313 ? -12.977 5.685   -29.085 1.00 11.05 ? 418  ALA A C   1 
ATOM   2636 O  O   . ALA A 1 313 ? -12.434 6.605   -28.482 1.00 10.64 ? 418  ALA A O   1 
ATOM   2637 C  CB  . ALA A 1 313 ? -13.179 3.754   -27.421 1.00 11.13 ? 418  ALA A CB  1 
ATOM   2638 N  N   . ALA A 1 314 ? -13.998 5.780   -29.925 1.00 10.79 ? 419  ALA A N   1 
ATOM   2639 C  CA  . ALA A 1 314 ? -14.664 7.067   -30.229 1.00 10.39 ? 419  ALA A CA  1 
ATOM   2640 C  C   . ALA A 1 314 ? -16.023 6.976   -29.605 1.00 10.83 ? 419  ALA A C   1 
ATOM   2641 O  O   . ALA A 1 314 ? -16.690 5.930   -29.505 1.00 11.28 ? 419  ALA A O   1 
ATOM   2642 C  CB  . ALA A 1 314 ? -14.762 7.231   -31.736 1.00 10.98 ? 419  ALA A CB  1 
ATOM   2643 N  N   . TYR A 1 315 ? -16.527 8.133   -29.074 1.00 9.59  ? 420  TYR A N   1 
ATOM   2644 C  CA  . TYR A 1 315 ? -17.802 8.242   -28.424 1.00 9.29  ? 420  TYR A CA  1 
ATOM   2645 C  C   . TYR A 1 315 ? -18.685 9.297   -29.115 1.00 9.07  ? 420  TYR A C   1 
ATOM   2646 O  O   . TYR A 1 315 ? -18.282 10.468  -29.248 1.00 9.51  ? 420  TYR A O   1 
ATOM   2647 C  CB  . TYR A 1 315 ? -17.645 8.653   -26.933 1.00 8.96  ? 420  TYR A CB  1 
ATOM   2648 C  CG  . TYR A 1 315 ? -17.052 7.550   -26.086 1.00 9.18  ? 420  TYR A CG  1 
ATOM   2649 C  CD1 . TYR A 1 315 ? -17.893 6.830   -25.244 1.00 9.54  ? 420  TYR A CD1 1 
ATOM   2650 C  CD2 . TYR A 1 315 ? -15.687 7.239   -26.186 1.00 9.33  ? 420  TYR A CD2 1 
ATOM   2651 C  CE1 . TYR A 1 315 ? -17.362 5.741   -24.484 1.00 11.35 ? 420  TYR A CE1 1 
ATOM   2652 C  CE2 . TYR A 1 315 ? -15.132 6.132   -25.491 1.00 10.03 ? 420  TYR A CE2 1 
ATOM   2653 C  CZ  . TYR A 1 315 ? -16.013 5.427   -24.705 1.00 10.92 ? 420  TYR A CZ  1 
ATOM   2654 O  OH  . TYR A 1 315 ? -15.533 4.275   -23.971 1.00 13.73 ? 420  TYR A OH  1 
ATOM   2655 N  N   . SER A 1 316 ? -19.855 8.884   -29.562 1.00 9.67  ? 421  SER A N   1 
ATOM   2656 C  CA  . SER A 1 316 ? -20.853 9.828   -30.128 1.00 10.13 ? 421  SER A CA  1 
ATOM   2657 C  C   . SER A 1 316 ? -21.133 10.967  -29.161 1.00 10.22 ? 421  SER A C   1 
ATOM   2658 O  O   . SER A 1 316 ? -21.326 10.737  -27.974 1.00 10.58 ? 421  SER A O   1 
ATOM   2659 C  CB  . SER A 1 316 ? -22.129 8.999   -30.408 1.00 10.33 ? 421  SER A CB  1 
ATOM   2660 O  OG  . SER A 1 316 ? -23.122 9.796   -31.067 1.00 10.67 ? 421  SER A OG  1 
ATOM   2661 N  N   . PHE A 1 317 ? -21.170 12.194  -29.724 1.00 9.17  ? 422  PHE A N   1 
ATOM   2662 C  CA  . PHE A 1 317 ? -21.325 13.392  -28.900 1.00 8.84  ? 422  PHE A CA  1 
ATOM   2663 C  C   . PHE A 1 317 ? -22.678 13.993  -29.236 1.00 8.69  ? 422  PHE A C   1 
ATOM   2664 O  O   . PHE A 1 317 ? -23.707 13.488  -28.806 1.00 11.00 ? 422  PHE A O   1 
ATOM   2665 C  CB  . PHE A 1 317 ? -20.076 14.264  -29.060 1.00 9.17  ? 422  PHE A CB  1 
ATOM   2666 C  CG  . PHE A 1 317 ? -19.956 15.406  -28.069 1.00 8.89  ? 422  PHE A CG  1 
ATOM   2667 C  CD1 . PHE A 1 317 ? -20.199 15.204  -26.662 1.00 9.81  ? 422  PHE A CD1 1 
ATOM   2668 C  CD2 . PHE A 1 317 ? -19.493 16.642  -28.513 1.00 9.43  ? 422  PHE A CD2 1 
ATOM   2669 C  CE1 . PHE A 1 317 ? -20.041 16.302  -25.789 1.00 9.23  ? 422  PHE A CE1 1 
ATOM   2670 C  CE2 . PHE A 1 317 ? -19.318 17.706  -27.605 1.00 9.92  ? 422  PHE A CE2 1 
ATOM   2671 C  CZ  . PHE A 1 317 ? -19.587 17.534  -26.258 1.00 9.58  ? 422  PHE A CZ  1 
ATOM   2672 N  N   . TYR A 1 318 ? -22.718 15.054  -30.057 1.00 9.07  ? 423  TYR A N   1 
ATOM   2673 C  CA  . TYR A 1 318 ? -24.010 15.629  -30.570 1.00 9.53  ? 423  TYR A CA  1 
ATOM   2674 C  C   . TYR A 1 318 ? -24.046 15.537  -32.089 1.00 9.85  ? 423  TYR A C   1 
ATOM   2675 O  O   . TYR A 1 318 ? -23.094 15.910  -32.777 1.00 10.09 ? 423  TYR A O   1 
ATOM   2676 C  CB  . TYR A 1 318 ? -24.238 17.068  -30.124 1.00 9.96  ? 423  TYR A CB  1 
ATOM   2677 C  CG  . TYR A 1 318 ? -24.350 17.198  -28.588 1.00 9.72  ? 423  TYR A CG  1 
ATOM   2678 C  CD1 . TYR A 1 318 ? -25.613 17.175  -27.977 1.00 10.09 ? 423  TYR A CD1 1 
ATOM   2679 C  CD2 . TYR A 1 318 ? -23.241 17.414  -27.825 1.00 9.54  ? 423  TYR A CD2 1 
ATOM   2680 C  CE1 . TYR A 1 318 ? -25.734 17.366  -26.614 1.00 9.79  ? 423  TYR A CE1 1 
ATOM   2681 C  CE2 . TYR A 1 318 ? -23.368 17.593  -26.413 1.00 9.27  ? 423  TYR A CE2 1 
ATOM   2682 C  CZ  . TYR A 1 318 ? -24.642 17.536  -25.866 1.00 9.14  ? 423  TYR A CZ  1 
ATOM   2683 O  OH  . TYR A 1 318 ? -24.753 17.688  -24.436 1.00 10.26 ? 423  TYR A OH  1 
ATOM   2684 N  N   . ASN A 1 319 ? -25.168 15.014  -32.618 1.00 9.55  ? 424  ASN A N   1 
ATOM   2685 C  CA  . ASN A 1 319 ? -25.333 14.814  -34.062 1.00 9.73  ? 424  ASN A CA  1 
ATOM   2686 C  C   . ASN A 1 319 ? -26.628 15.510  -34.422 1.00 11.57 ? 424  ASN A C   1 
ATOM   2687 O  O   . ASN A 1 319 ? -27.687 15.188  -33.885 1.00 13.19 ? 424  ASN A O   1 
ATOM   2688 C  CB  . ASN A 1 319 ? -25.365 13.285  -34.348 1.00 11.40 ? 424  ASN A CB  1 
ATOM   2689 C  CG  . ASN A 1 319 ? -24.037 12.651  -33.988 1.00 9.15  ? 424  ASN A CG  1 
ATOM   2690 O  OD1 . ASN A 1 319 ? -23.014 12.945  -34.543 1.00 10.53 ? 424  ASN A OD1 1 
ATOM   2691 N  ND2 . ASN A 1 319 ? -24.105 11.782  -32.961 1.00 10.09 ? 424  ASN A ND2 1 
ATOM   2692 N  N   . VAL A 1 320 ? -26.531 16.460  -35.338 1.00 10.40 ? 425  VAL A N   1 
ATOM   2693 C  CA  . VAL A 1 320 ? -27.691 17.316  -35.709 1.00 11.08 ? 425  VAL A CA  1 
ATOM   2694 C  C   . VAL A 1 320 ? -27.949 17.129  -37.203 1.00 11.44 ? 425  VAL A C   1 
ATOM   2695 O  O   . VAL A 1 320 ? -27.086 17.358  -38.017 1.00 11.16 ? 425  VAL A O   1 
ATOM   2696 C  CB  . VAL A 1 320 ? -27.452 18.786  -35.378 1.00 11.31 ? 425  VAL A CB  1 
ATOM   2697 C  CG1 . VAL A 1 320 ? -28.616 19.643  -35.936 1.00 13.60 ? 425  VAL A CG1 1 
ATOM   2698 C  CG2 . VAL A 1 320 ? -27.337 18.986  -33.870 1.00 12.84 ? 425  VAL A CG2 1 
ATOM   2699 N  N   . HIS A 1 321 ? -29.240 16.770  -37.505 1.00 12.67 ? 426  HIS A N   1 
ATOM   2700 C  CA  . HIS A 1 321 ? -29.626 16.550  -38.980 1.00 12.76 ? 426  HIS A CA  1 
ATOM   2701 C  C   . HIS A 1 321 ? -30.786 17.454  -39.221 1.00 12.91 ? 426  HIS A C   1 
ATOM   2702 O  O   . HIS A 1 321 ? -31.733 17.579  -38.399 1.00 14.33 ? 426  HIS A O   1 
ATOM   2703 C  CB  . HIS A 1 321 ? -29.980 15.084  -39.240 1.00 12.79 ? 426  HIS A CB  1 
ATOM   2704 C  CG  . HIS A 1 321 ? -31.182 14.638  -38.476 1.00 15.28 ? 426  HIS A CG  1 
ATOM   2705 N  ND1 . HIS A 1 321 ? -32.459 14.620  -39.017 1.00 15.46 ? 426  HIS A ND1 1 
ATOM   2706 C  CD2 . HIS A 1 321 ? -31.329 14.240  -37.181 1.00 15.18 ? 426  HIS A CD2 1 
ATOM   2707 C  CE1 . HIS A 1 321 ? -33.324 14.222  -38.097 1.00 18.08 ? 426  HIS A CE1 1 
ATOM   2708 N  NE2 . HIS A 1 321 ? -32.657 13.990  -36.970 1.00 17.11 ? 426  HIS A NE2 1 
ATOM   2709 N  N   . THR A 1 322 ? -30.718 18.160  -40.399 1.00 13.08 ? 427  THR A N   1 
ATOM   2710 C  CA  . THR A 1 322 ? -31.900 18.942  -40.941 1.00 13.79 ? 427  THR A CA  1 
ATOM   2711 C  C   . THR A 1 322 ? -32.124 18.542  -42.426 1.00 15.85 ? 427  THR A C   1 
ATOM   2712 O  O   . THR A 1 322 ? -33.273 18.771  -42.883 1.00 17.23 ? 427  THR A O   1 
ATOM   2713 C  CB  . THR A 1 322 ? -31.858 20.439  -40.861 1.00 13.60 ? 427  THR A CB  1 
ATOM   2714 O  OG1 . THR A 1 322 ? -30.863 20.994  -41.753 1.00 14.58 ? 427  THR A OG1 1 
ATOM   2715 C  CG2 . THR A 1 322 ? -31.502 20.842  -39.398 1.00 15.63 ? 427  THR A CG2 1 
ATOM   2716 N  N   . GLN A 1 323 ? -31.097 18.123  -43.140 1.00 14.05 ? 428  GLN A N   1 
ATOM   2717 C  CA  . GLN A 1 323 ? -31.303 17.725  -44.583 1.00 16.41 ? 428  GLN A CA  1 
ATOM   2718 C  C   . GLN A 1 323 ? -30.704 16.365  -44.892 1.00 18.07 ? 428  GLN A C   1 
ATOM   2719 O  O   . GLN A 1 323 ? -31.156 15.730  -45.814 1.00 25.40 ? 428  GLN A O   1 
ATOM   2720 C  CB  . GLN A 1 323 ? -30.569 18.744  -45.463 1.00 17.50 ? 428  GLN A CB  1 
ATOM   2721 C  CG  . GLN A 1 323 ? -31.251 20.119  -45.368 1.00 21.29 ? 428  GLN A CG  1 
ATOM   2722 C  CD  . GLN A 1 323 ? -32.752 20.130  -45.828 1.00 26.14 ? 428  GLN A CD  1 
ATOM   2723 O  OE1 . GLN A 1 323 ? -33.183 19.295  -46.603 1.00 30.64 ? 428  GLN A OE1 1 
ATOM   2724 N  NE2 . GLN A 1 323 ? -33.502 21.100  -45.360 1.00 30.59 ? 428  GLN A NE2 1 
ATOM   2725 N  N   . THR A 1 324 ? -29.678 15.885  -44.197 1.00 15.42 ? 429  THR A N   1 
ATOM   2726 C  CA  . THR A 1 324 ? -29.094 14.595  -44.408 1.00 15.75 ? 429  THR A CA  1 
ATOM   2727 C  C   . THR A 1 324 ? -29.761 13.658  -43.426 1.00 16.34 ? 429  THR A C   1 
ATOM   2728 O  O   . THR A 1 324 ? -29.955 13.997  -42.251 1.00 14.97 ? 429  THR A O   1 
ATOM   2729 C  CB  . THR A 1 324 ? -27.637 14.670  -44.042 1.00 13.35 ? 429  THR A CB  1 
ATOM   2730 O  OG1 . THR A 1 324 ? -26.994 15.693  -44.829 1.00 15.38 ? 429  THR A OG1 1 
ATOM   2731 C  CG2 . THR A 1 324 ? -26.883 13.295  -44.270 1.00 14.64 ? 429  THR A CG2 1 
ATOM   2732 N  N   . PRO A 1 325 ? -30.194 12.440  -43.864 1.00 15.33 ? 430  PRO A N   1 
ATOM   2733 C  CA  . PRO A 1 325 ? -30.841 11.559  -42.888 1.00 15.73 ? 430  PRO A CA  1 
ATOM   2734 C  C   . PRO A 1 325 ? -29.869 11.235  -41.751 1.00 16.27 ? 430  PRO A C   1 
ATOM   2735 O  O   . PRO A 1 325 ? -28.652 11.001  -42.042 1.00 15.22 ? 430  PRO A O   1 
ATOM   2736 C  CB  . PRO A 1 325 ? -31.092 10.253  -43.703 1.00 18.93 ? 430  PRO A CB  1 
ATOM   2737 C  CG  . PRO A 1 325 ? -31.263 10.821  -45.137 1.00 19.76 ? 430  PRO A CG  1 
ATOM   2738 C  CD  . PRO A 1 325 ? -30.218 11.945  -45.243 1.00 17.73 ? 430  PRO A CD  1 
ATOM   2739 N  N   . LEU A 1 326 ? -30.392 11.137  -40.547 1.00 17.52 ? 431  LEU A N   1 
ATOM   2740 C  CA  . LEU A 1 326 ? -29.550 10.751  -39.428 1.00 16.95 ? 431  LEU A CA  1 
ATOM   2741 C  C   . LEU A 1 326 ? -28.800 9.414   -39.642 1.00 16.21 ? 431  LEU A C   1 
ATOM   2742 O  O   . LEU A 1 326 ? -27.619 9.312   -39.311 1.00 15.72 ? 431  LEU A O   1 
ATOM   2743 C  CB  . LEU A 1 326 ? -30.352 10.714  -38.126 1.00 15.86 ? 431  LEU A CB  1 
ATOM   2744 C  CG  . LEU A 1 326 ? -29.587 10.361  -36.860 1.00 16.05 ? 431  LEU A CG  1 
ATOM   2745 C  CD1 . LEU A 1 326 ? -28.382 11.307  -36.544 1.00 15.84 ? 431  LEU A CD1 1 
ATOM   2746 C  CD2 . LEU A 1 326 ? -30.564 10.312  -35.697 1.00 15.74 ? 431  LEU A CD2 1 
ATOM   2747 N  N   . LEU A 1 327 ? -29.464 8.437   -40.289 1.00 19.03 ? 432  LEU A N   1 
ATOM   2748 C  CA  . LEU A 1 327 ? -28.824 7.161   -40.528 1.00 18.15 ? 432  LEU A CA  1 
ATOM   2749 C  C   . LEU A 1 327 ? -27.575 7.384   -41.351 1.00 17.43 ? 432  LEU A C   1 
ATOM   2750 O  O   . LEU A 1 327 ? -26.516 6.762   -41.104 1.00 17.21 ? 432  LEU A O   1 
ATOM   2751 C  CB  . LEU A 1 327 ? -29.815 6.267   -41.297 1.00 19.24 ? 432  LEU A CB  1 
ATOM   2752 C  CG  . LEU A 1 327 ? -29.450 4.850   -41.504 1.00 21.63 ? 432  LEU A CG  1 
ATOM   2753 C  CD1 . LEU A 1 327 ? -29.434 4.076   -40.171 1.00 21.27 ? 432  LEU A CD1 1 
ATOM   2754 C  CD2 . LEU A 1 327 ? -30.624 4.358   -42.397 1.00 24.79 ? 432  LEU A CD2 1 
ATOM   2755 N  N   . ASP A 1 328 ? -27.626 8.267   -42.387 1.00 15.97 ? 433  ASP A N   1 
ATOM   2756 C  CA  . ASP A 1 328 ? -26.433 8.452   -43.229 1.00 16.57 ? 433  ASP A CA  1 
ATOM   2757 C  C   . ASP A 1 328 ? -25.300 9.222   -42.489 1.00 16.36 ? 433  ASP A C   1 
ATOM   2758 O  O   . ASP A 1 328 ? -24.128 8.963   -42.674 1.00 14.71 ? 433  ASP A O   1 
ATOM   2759 C  CB  . ASP A 1 328 ? -26.757 9.237   -44.557 1.00 19.97 ? 433  ASP A CB  1 
ATOM   2760 C  CG  . ASP A 1 328 ? -27.741 8.515   -45.439 1.00 24.50 ? 433  ASP A CG  1 
ATOM   2761 O  OD1 . ASP A 1 328 ? -28.143 9.170   -46.399 1.00 24.82 ? 433  ASP A OD1 1 
ATOM   2762 O  OD2 . ASP A 1 328 ? -28.101 7.359   -45.190 1.00 27.29 ? 433  ASP A OD2 1 
ATOM   2763 N  N   . LEU A 1 329 ? -25.745 10.255  -41.715 1.00 15.91 ? 434  LEU A N   1 
ATOM   2764 C  CA  . LEU A 1 329 ? -24.763 10.955  -40.885 1.00 16.04 ? 434  LEU A CA  1 
ATOM   2765 C  C   . LEU A 1 329 ? -24.003 10.030  -39.955 1.00 14.39 ? 434  LEU A C   1 
ATOM   2766 O  O   . LEU A 1 329 ? -22.797 10.145  -39.822 1.00 13.76 ? 434  LEU A O   1 
ATOM   2767 C  CB  . LEU A 1 329 ? -25.495 12.018  -40.044 1.00 18.69 ? 434  LEU A CB  1 
ATOM   2768 C  CG  . LEU A 1 329 ? -24.890 13.283  -39.708 1.00 23.16 ? 434  LEU A CG  1 
ATOM   2769 C  CD1 . LEU A 1 329 ? -24.425 14.059  -40.978 1.00 21.63 ? 434  LEU A CD1 1 
ATOM   2770 C  CD2 . LEU A 1 329 ? -25.933 14.079  -38.845 1.00 21.84 ? 434  LEU A CD2 1 
ATOM   2771 N  N   . MET A 1 330 ? -24.714 9.089   -39.325 1.00 13.57 ? 435  MET A N   1 
ATOM   2772 C  CA  . MET A 1 330 ? -24.072 8.117   -38.402 1.00 13.93 ? 435  MET A CA  1 
ATOM   2773 C  C   . MET A 1 330 ? -23.193 7.138   -39.136 1.00 13.91 ? 435  MET A C   1 
ATOM   2774 O  O   . MET A 1 330 ? -22.112 6.807   -38.728 1.00 12.76 ? 435  MET A O   1 
ATOM   2775 C  CB  . MET A 1 330 ? -25.086 7.481   -37.470 1.00 14.14 ? 435  MET A CB  1 
ATOM   2776 C  CG  . MET A 1 330 ? -25.743 8.529   -36.585 1.00 12.81 ? 435  MET A CG  1 
ATOM   2777 S  SD  . MET A 1 330 ? -24.668 9.672   -35.657 1.00 15.48 ? 435  MET A SD  1 
ATOM   2778 C  CE  . MET A 1 330 ? -23.688 8.532   -34.691 1.00 15.01 ? 435  MET A CE  1 
ATOM   2779 N  N   . SER A 1 331 ? -23.622 6.703   -40.350 1.00 13.75 ? 436  SER A N   1 
ATOM   2780 C  CA  A SER A 1 331 ? -22.727 5.907   -41.179 0.50 14.70 ? 436  SER A CA  1 
ATOM   2781 C  CA  B SER A 1 331 ? -22.726 5.932   -41.229 0.50 14.71 ? 436  SER A CA  1 
ATOM   2782 C  C   . SER A 1 331 ? -21.392 6.626   -41.497 1.00 12.34 ? 436  SER A C   1 
ATOM   2783 O  O   . SER A 1 331 ? -20.288 6.064   -41.484 1.00 13.27 ? 436  SER A O   1 
ATOM   2784 C  CB  A SER A 1 331 ? -23.449 5.477   -42.466 0.50 15.82 ? 436  SER A CB  1 
ATOM   2785 C  CB  B SER A 1 331 ? -23.438 5.619   -42.563 0.50 16.12 ? 436  SER A CB  1 
ATOM   2786 O  OG  A SER A 1 331 ? -22.566 4.712   -43.226 0.50 17.32 ? 436  SER A OG  1 
ATOM   2787 O  OG  B SER A 1 331 ? -24.436 4.670   -42.291 0.50 16.74 ? 436  SER A OG  1 
ATOM   2788 N  N   . ASP A 1 332 ? -21.516 7.948   -41.805 1.00 12.63 ? 437  ASP A N   1 
ATOM   2789 C  CA  A ASP A 1 332 ? -20.391 8.858   -42.065 0.50 13.57 ? 437  ASP A CA  1 
ATOM   2790 C  CA  B ASP A 1 332 ? -20.280 8.677   -42.100 0.50 14.45 ? 437  ASP A CA  1 
ATOM   2791 C  C   . ASP A 1 332 ? -19.434 8.867   -40.857 1.00 11.41 ? 437  ASP A C   1 
ATOM   2792 O  O   . ASP A 1 332 ? -18.242 8.794   -40.978 1.00 11.93 ? 437  ASP A O   1 
ATOM   2793 C  CB  A ASP A 1 332 ? -20.892 10.333  -42.288 0.50 11.68 ? 437  ASP A CB  1 
ATOM   2794 C  CB  B ASP A 1 332 ? -20.500 10.002  -42.854 0.50 16.15 ? 437  ASP A CB  1 
ATOM   2795 C  CG  A ASP A 1 332 ? -21.744 10.521  -43.545 0.50 13.31 ? 437  ASP A CG  1 
ATOM   2796 C  CG  B ASP A 1 332 ? -20.682 9.755   -44.359 0.50 15.08 ? 437  ASP A CG  1 
ATOM   2797 O  OD1 A ASP A 1 332 ? -21.608 9.825   -44.585 0.50 12.32 ? 437  ASP A OD1 1 
ATOM   2798 O  OD1 B ASP A 1 332 ? -20.430 8.608   -44.858 0.50 18.09 ? 437  ASP A OD1 1 
ATOM   2799 O  OD2 A ASP A 1 332 ? -22.547 11.458  -43.516 0.50 11.02 ? 437  ASP A OD2 1 
ATOM   2800 O  OD2 B ASP A 1 332 ? -21.128 10.666  -45.004 0.50 18.39 ? 437  ASP A OD2 1 
ATOM   2801 N  N   . ALA A 1 333 ? -20.061 9.011   -39.681 1.00 11.19 ? 438  ALA A N   1 
ATOM   2802 C  CA  . ALA A 1 333 ? -19.268 9.013   -38.423 1.00 11.63 ? 438  ALA A CA  1 
ATOM   2803 C  C   . ALA A 1 333 ? -18.442 7.728   -38.208 1.00 10.22 ? 438  ALA A C   1 
ATOM   2804 O  O   . ALA A 1 333 ? -17.285 7.783   -37.904 1.00 11.30 ? 438  ALA A O   1 
ATOM   2805 C  CB  . ALA A 1 333 ? -20.165 9.256   -37.193 1.00 11.76 ? 438  ALA A CB  1 
ATOM   2806 N  N   . LEU A 1 334 ? -19.128 6.588   -38.522 1.00 11.11 ? 439  LEU A N   1 
ATOM   2807 C  CA  . LEU A 1 334 ? -18.382 5.281   -38.411 1.00 11.52 ? 439  LEU A CA  1 
ATOM   2808 C  C   . LEU A 1 334 ? -17.246 5.185   -39.392 1.00 10.95 ? 439  LEU A C   1 
ATOM   2809 O  O   . LEU A 1 334 ? -16.159 4.785   -39.064 1.00 12.23 ? 439  LEU A O   1 
ATOM   2810 C  CB  . LEU A 1 334 ? -19.382 4.112   -38.667 1.00 12.35 ? 439  LEU A CB  1 
ATOM   2811 C  CG  . LEU A 1 334 ? -20.517 3.953   -37.671 1.00 12.45 ? 439  LEU A CG  1 
ATOM   2812 C  CD1 . LEU A 1 334 ? -21.404 2.785   -38.186 1.00 13.90 ? 439  LEU A CD1 1 
ATOM   2813 C  CD2 . LEU A 1 334 ? -20.057 3.646   -36.237 1.00 13.44 ? 439  LEU A CD2 1 
ATOM   2814 N  N   . VAL A 1 335 ? -17.479 5.656   -40.663 1.00 11.98 ? 440  VAL A N   1 
ATOM   2815 C  CA  . VAL A 1 335 ? -16.410 5.644   -41.651 1.00 11.77 ? 440  VAL A CA  1 
ATOM   2816 C  C   . VAL A 1 335 ? -15.232 6.455   -41.261 1.00 11.37 ? 440  VAL A C   1 
ATOM   2817 O  O   . VAL A 1 335 ? -14.086 6.133   -41.331 1.00 13.33 ? 440  VAL A O   1 
ATOM   2818 C  CB  . VAL A 1 335 ? -16.954 6.087   -43.069 1.00 12.46 ? 440  VAL A CB  1 
ATOM   2819 C  CG1 . VAL A 1 335 ? -15.824 6.396   -44.030 1.00 15.20 ? 440  VAL A CG1 1 
ATOM   2820 C  CG2 . VAL A 1 335 ? -17.895 4.989   -43.635 1.00 14.42 ? 440  VAL A CG2 1 
ATOM   2821 N  N   . LEU A 1 336 ? -15.562 7.717   -40.769 1.00 12.08 ? 441  LEU A N   1 
ATOM   2822 C  CA  . LEU A 1 336 ? -14.513 8.594   -40.338 1.00 12.23 ? 441  LEU A CA  1 
ATOM   2823 C  C   . LEU A 1 336 ? -13.656 8.089   -39.159 1.00 12.22 ? 441  LEU A C   1 
ATOM   2824 O  O   . LEU A 1 336 ? -12.450 8.206   -39.098 1.00 12.31 ? 441  LEU A O   1 
ATOM   2825 C  CB  . LEU A 1 336 ? -15.099 9.980   -39.986 1.00 11.76 ? 441  LEU A CB  1 
ATOM   2826 C  CG  . LEU A 1 336 ? -15.574 10.778  -41.185 1.00 13.43 ? 441  LEU A CG  1 
ATOM   2827 C  CD1 . LEU A 1 336 ? -16.574 11.899  -40.710 1.00 16.30 ? 441  LEU A CD1 1 
ATOM   2828 C  CD2 . LEU A 1 336 ? -14.433 11.382  -41.997 1.00 15.25 ? 441  LEU A CD2 1 
ATOM   2829 N  N   . ALA A 1 337 ? -14.409 7.511   -38.205 1.00 11.31 ? 442  ALA A N   1 
ATOM   2830 C  CA  . ALA A 1 337 ? -13.728 6.906   -37.027 1.00 12.21 ? 442  ALA A CA  1 
ATOM   2831 C  C   . ALA A 1 337 ? -12.762 5.748   -37.486 1.00 10.84 ? 442  ALA A C   1 
ATOM   2832 O  O   . ALA A 1 337 ? -11.606 5.677   -37.051 1.00 12.25 ? 442  ALA A O   1 
ATOM   2833 C  CB  . ALA A 1 337 ? -14.777 6.438   -36.019 1.00 12.91 ? 442  ALA A CB  1 
ATOM   2834 N  N   . LYS A 1 338 ? -13.281 4.905   -38.408 1.00 12.51 ? 443  LYS A N   1 
ATOM   2835 C  CA  . LYS A 1 338 ? -12.413 3.866   -38.910 1.00 14.49 ? 443  LYS A CA  1 
ATOM   2836 C  C   . LYS A 1 338 ? -11.221 4.429   -39.638 1.00 14.99 ? 443  LYS A C   1 
ATOM   2837 O  O   . LYS A 1 338 ? -10.081 3.981   -39.421 1.00 14.66 ? 443  LYS A O   1 
ATOM   2838 C  CB  . LYS A 1 338 ? -13.237 2.932   -39.863 1.00 15.51 ? 443  LYS A CB  1 
ATOM   2839 C  CG  . LYS A 1 338 ? -12.363 1.784   -40.537 1.00 17.24 ? 443  LYS A CG  1 
ATOM   2840 C  CD  . LYS A 1 338 ? -12.033 0.711   -39.494 1.00 18.91 ? 443  LYS A CD  1 
ATOM   2841 C  CE  . LYS A 1 338 ? -11.211 -0.510  -40.027 1.00 22.03 ? 443  LYS A CE  1 
ATOM   2842 N  NZ  . LYS A 1 338 ? -9.811  -0.135  -40.002 1.00 29.09 ? 443  LYS A NZ  1 
ATOM   2843 N  N   . MET A 1 339 ? -11.419 5.515   -40.441 1.00 12.97 ? 444  MET A N   1 
ATOM   2844 C  CA  . MET A 1 339 ? -10.257 6.109   -41.113 1.00 15.41 ? 444  MET A CA  1 
ATOM   2845 C  C   . MET A 1 339 ? -9.177  6.648   -40.172 1.00 15.31 ? 444  MET A C   1 
ATOM   2846 O  O   . MET A 1 339 ? -7.951  6.636   -40.427 1.00 17.48 ? 444  MET A O   1 
ATOM   2847 C  CB  . MET A 1 339 ? -10.664 7.276   -42.049 1.00 16.06 ? 444  MET A CB  1 
ATOM   2848 C  CG  . MET A 1 339 ? -11.558 6.853   -43.244 1.00 17.98 ? 444  MET A CG  1 
ATOM   2849 S  SD  . MET A 1 339 ? -12.430 8.330   -43.980 1.00 21.01 ? 444  MET A SD  1 
ATOM   2850 C  CE  . MET A 1 339 ? -11.087 9.437   -44.466 1.00 24.37 ? 444  MET A CE  1 
ATOM   2851 N  N   . LYS A 1 340 ? -9.668  7.142   -39.015 1.00 15.03 ? 445  LYS A N   1 
ATOM   2852 C  CA  . LYS A 1 340 ? -8.800  7.700   -38.002 1.00 14.43 ? 445  LYS A CA  1 
ATOM   2853 C  C   . LYS A 1 340 ? -8.175  6.645   -37.064 1.00 15.86 ? 445  LYS A C   1 
ATOM   2854 O  O   . LYS A 1 340 ? -7.410  7.050   -36.161 1.00 19.85 ? 445  LYS A O   1 
ATOM   2855 C  CB  . LYS A 1 340 ? -9.583  8.768   -37.145 1.00 14.28 ? 445  LYS A CB  1 
ATOM   2856 C  CG  . LYS A 1 340 ? -9.887  10.055  -37.976 1.00 15.57 ? 445  LYS A CG  1 
ATOM   2857 C  CD  . LYS A 1 340 ? -10.975 10.964  -37.313 1.00 17.12 ? 445  LYS A CD  1 
ATOM   2858 C  CE  . LYS A 1 340 ? -11.361 12.265  -38.064 1.00 21.21 ? 445  LYS A CE  1 
ATOM   2859 N  NZ  . LYS A 1 340 ? -10.180 13.218  -38.013 1.00 21.58 ? 445  LYS A NZ  1 
ATOM   2860 N  N   . GLY A 1 341 ? -8.412  5.371   -37.339 1.00 15.18 ? 446  GLY A N   1 
ATOM   2861 C  CA  . GLY A 1 341 ? -7.674  4.287   -36.587 1.00 15.02 ? 446  GLY A CA  1 
ATOM   2862 C  C   . GLY A 1 341 ? -8.410  3.850   -35.336 1.00 14.60 ? 446  GLY A C   1 
ATOM   2863 O  O   . GLY A 1 341 ? -7.850  3.106   -34.541 1.00 17.26 ? 446  GLY A O   1 
ATOM   2864 N  N   . PHE A 1 342 ? -9.677  4.236   -35.135 1.00 14.23 ? 447  PHE A N   1 
ATOM   2865 C  CA  . PHE A 1 342 ? -10.380 3.728   -33.936 1.00 12.03 ? 447  PHE A CA  1 
ATOM   2866 C  C   . PHE A 1 342 ? -10.652 2.244   -34.089 1.00 13.47 ? 447  PHE A C   1 
ATOM   2867 O  O   . PHE A 1 342 ? -10.933 1.735   -35.195 1.00 14.57 ? 447  PHE A O   1 
ATOM   2868 C  CB  . PHE A 1 342 ? -11.702 4.477   -33.687 1.00 11.40 ? 447  PHE A CB  1 
ATOM   2869 C  CG  . PHE A 1 342 ? -11.522 5.943   -33.230 1.00 12.45 ? 447  PHE A CG  1 
ATOM   2870 C  CD1 . PHE A 1 342 ? -11.329 6.183   -31.852 1.00 12.65 ? 447  PHE A CD1 1 
ATOM   2871 C  CD2 . PHE A 1 342 ? -11.424 7.018   -34.154 1.00 13.20 ? 447  PHE A CD2 1 
ATOM   2872 C  CE1 . PHE A 1 342 ? -11.139 7.509   -31.421 1.00 14.47 ? 447  PHE A CE1 1 
ATOM   2873 C  CE2 . PHE A 1 342 ? -11.279 8.337   -33.677 1.00 13.50 ? 447  PHE A CE2 1 
ATOM   2874 C  CZ  . PHE A 1 342 ? -11.119 8.558   -32.289 1.00 13.82 ? 447  PHE A CZ  1 
ATOM   2875 N  N   . ASP A 1 343 ? -10.789 1.566   -32.946 1.00 11.69 ? 448  ASP A N   1 
ATOM   2876 C  CA  . ASP A 1 343 ? -11.212 0.111   -32.886 1.00 11.45 ? 448  ASP A CA  1 
ATOM   2877 C  C   . ASP A 1 343 ? -12.673 -0.070  -32.731 1.00 12.69 ? 448  ASP A C   1 
ATOM   2878 O  O   . ASP A 1 343 ? -13.252 -1.106  -33.115 1.00 12.58 ? 448  ASP A O   1 
ATOM   2879 C  CB  . ASP A 1 343 ? -10.508 -0.579  -31.712 1.00 12.51 ? 448  ASP A CB  1 
ATOM   2880 C  CG  . ASP A 1 343 ? -9.017  -0.463  -31.787 1.00 13.33 ? 448  ASP A CG  1 
ATOM   2881 O  OD1 . ASP A 1 343 ? -8.278  -0.202  -30.810 1.00 14.51 ? 448  ASP A OD1 1 
ATOM   2882 O  OD2 . ASP A 1 343 ? -8.464  -0.694  -32.941 1.00 15.45 ? 448  ASP A OD2 1 
ATOM   2883 N  N   . VAL A 1 344 ? -13.411 0.865   -32.050 1.00 10.82 ? 449  VAL A N   1 
ATOM   2884 C  CA  . VAL A 1 344 ? -14.820 0.710   -31.697 1.00 10.50 ? 449  VAL A CA  1 
ATOM   2885 C  C   . VAL A 1 344 ? -15.436 2.135   -31.666 1.00 10.65 ? 449  VAL A C   1 
ATOM   2886 O  O   . VAL A 1 344 ? -14.716 3.078   -31.254 1.00 11.10 ? 449  VAL A O   1 
ATOM   2887 C  CB  . VAL A 1 344 ? -14.953 -0.100  -30.369 1.00 10.87 ? 449  VAL A CB  1 
ATOM   2888 C  CG1 . VAL A 1 344 ? -14.318 0.690   -29.142 1.00 12.01 ? 449  VAL A CG1 1 
ATOM   2889 C  CG2 . VAL A 1 344 ? -16.389 -0.491  -30.046 1.00 12.46 ? 449  VAL A CG2 1 
ATOM   2890 N  N   . PHE A 1 345 ? -16.691 2.237   -31.982 1.00 10.12 ? 450  PHE A N   1 
ATOM   2891 C  CA  . PHE A 1 345 ? -17.461 3.474   -31.809 1.00 10.04 ? 450  PHE A CA  1 
ATOM   2892 C  C   . PHE A 1 345 ? -18.562 3.176   -30.824 1.00 13.05 ? 450  PHE A C   1 
ATOM   2893 O  O   . PHE A 1 345 ? -19.380 2.240   -30.978 1.00 14.98 ? 450  PHE A O   1 
ATOM   2894 C  CB  . PHE A 1 345 ? -17.980 3.836   -33.233 1.00 11.84 ? 450  PHE A CB  1 
ATOM   2895 C  CG  . PHE A 1 345 ? -18.623 5.188   -33.271 1.00 10.88 ? 450  PHE A CG  1 
ATOM   2896 C  CD1 . PHE A 1 345 ? -17.918 6.284   -33.783 1.00 11.91 ? 450  PHE A CD1 1 
ATOM   2897 C  CD2 . PHE A 1 345 ? -19.920 5.351   -32.937 1.00 10.71 ? 450  PHE A CD2 1 
ATOM   2898 C  CE1 . PHE A 1 345 ? -18.574 7.611   -33.907 1.00 11.60 ? 450  PHE A CE1 1 
ATOM   2899 C  CE2 . PHE A 1 345 ? -20.576 6.633   -33.034 1.00 12.16 ? 450  PHE A CE2 1 
ATOM   2900 C  CZ  . PHE A 1 345 ? -19.909 7.710   -33.534 1.00 12.50 ? 450  PHE A CZ  1 
ATOM   2901 N  N   . ASN A 1 346 ? -18.704 4.035   -29.796 1.00 10.70 ? 451  ASN A N   1 
ATOM   2902 C  CA  . ASN A 1 346 ? -19.670 3.868   -28.708 1.00 11.92 ? 451  ASN A CA  1 
ATOM   2903 C  C   . ASN A 1 346 ? -20.775 4.891   -28.746 1.00 11.23 ? 451  ASN A C   1 
ATOM   2904 O  O   . ASN A 1 346 ? -20.476 6.075   -29.095 1.00 12.26 ? 451  ASN A O   1 
ATOM   2905 C  CB  . ASN A 1 346 ? -18.954 3.939   -27.354 1.00 12.49 ? 451  ASN A CB  1 
ATOM   2906 C  CG  . ASN A 1 346 ? -17.886 2.895   -27.238 1.00 14.06 ? 451  ASN A CG  1 
ATOM   2907 O  OD1 . ASN A 1 346 ? -18.183 1.724   -27.159 1.00 19.21 ? 451  ASN A OD1 1 
ATOM   2908 N  ND2 . ASN A 1 346 ? -16.647 3.295   -27.307 1.00 20.41 ? 451  ASN A ND2 1 
ATOM   2909 N  N   . ALA A 1 347 ? -21.983 4.546   -28.423 1.00 11.43 ? 452  ALA A N   1 
ATOM   2910 C  CA  . ALA A 1 347 ? -23.067 5.495   -28.348 1.00 10.85 ? 452  ALA A CA  1 
ATOM   2911 C  C   . ALA A 1 347 ? -24.100 5.093   -27.354 1.00 12.37 ? 452  ALA A C   1 
ATOM   2912 O  O   . ALA A 1 347 ? -24.263 3.858   -27.101 1.00 13.17 ? 452  ALA A O   1 
ATOM   2913 C  CB  . ALA A 1 347 ? -23.708 5.673   -29.759 1.00 12.30 ? 452  ALA A CB  1 
ATOM   2914 N  N   . LEU A 1 348 ? -24.806 6.023   -26.742 1.00 11.58 ? 453  LEU A N   1 
ATOM   2915 C  CA  . LEU A 1 348 ? -25.896 5.726   -25.843 1.00 11.21 ? 453  LEU A CA  1 
ATOM   2916 C  C   . LEU A 1 348 ? -27.221 5.689   -26.613 1.00 11.58 ? 453  LEU A C   1 
ATOM   2917 O  O   . LEU A 1 348 ? -27.277 6.175   -27.800 1.00 14.08 ? 453  LEU A O   1 
ATOM   2918 C  CB  . LEU A 1 348 ? -25.946 6.930   -24.801 1.00 12.32 ? 453  LEU A CB  1 
ATOM   2919 C  CG  . LEU A 1 348 ? -24.744 6.926   -23.823 1.00 12.77 ? 453  LEU A CG  1 
ATOM   2920 C  CD1 . LEU A 1 348 ? -24.616 8.327   -23.199 1.00 13.78 ? 453  LEU A CD1 1 
ATOM   2921 C  CD2 . LEU A 1 348 ? -24.928 5.843   -22.750 1.00 13.60 ? 453  LEU A CD2 1 
ATOM   2922 N  N   . ASP A 1 349 ? -28.270 5.216   -25.985 1.00 12.78 ? 454  ASP A N   1 
ATOM   2923 C  CA  . ASP A 1 349 ? -29.573 5.174   -26.658 1.00 12.63 ? 454  ASP A CA  1 
ATOM   2924 C  C   . ASP A 1 349 ? -30.439 6.344   -26.477 1.00 13.03 ? 454  ASP A C   1 
ATOM   2925 O  O   . ASP A 1 349 ? -31.669 6.334   -26.601 1.00 14.86 ? 454  ASP A O   1 
ATOM   2926 C  CB  . ASP A 1 349 ? -30.338 3.899   -26.229 1.00 13.94 ? 454  ASP A CB  1 
ATOM   2927 C  CG  . ASP A 1 349 ? -30.673 3.875   -24.746 1.00 15.79 ? 454  ASP A CG  1 
ATOM   2928 O  OD1 . ASP A 1 349 ? -30.254 4.778   -23.962 1.00 15.10 ? 454  ASP A OD1 1 
ATOM   2929 O  OD2 . ASP A 1 349 ? -31.373 2.877   -24.292 1.00 16.96 ? 454  ASP A OD2 1 
ATOM   2930 N  N   . LEU A 1 350 ? -29.788 7.511   -26.171 1.00 12.71 ? 455  LEU A N   1 
ATOM   2931 C  CA  . LEU A 1 350 ? -30.502 8.775   -25.945 1.00 12.48 ? 455  LEU A CA  1 
ATOM   2932 C  C   . LEU A 1 350 ? -30.794 9.560   -27.268 1.00 11.47 ? 455  LEU A C   1 
ATOM   2933 O  O   . LEU A 1 350 ? -30.426 9.082   -28.364 1.00 13.25 ? 455  LEU A O   1 
ATOM   2934 C  CB  . LEU A 1 350 ? -29.755 9.642   -24.877 1.00 13.28 ? 455  LEU A CB  1 
ATOM   2935 C  CG  . LEU A 1 350 ? -28.251 9.835   -25.066 1.00 13.43 ? 455  LEU A CG  1 
ATOM   2936 C  CD1 . LEU A 1 350 ? -27.869 10.350  -26.442 1.00 13.34 ? 455  LEU A CD1 1 
ATOM   2937 C  CD2 . LEU A 1 350 ? -27.732 10.799  -23.987 1.00 13.29 ? 455  LEU A CD2 1 
ATOM   2938 N  N   . MET A 1 351 ? -31.416 10.713  -27.175 1.00 12.75 ? 456  MET A N   1 
ATOM   2939 C  CA  . MET A 1 351 ? -31.822 11.489  -28.334 1.00 12.19 ? 456  MET A CA  1 
ATOM   2940 C  C   . MET A 1 351 ? -32.515 10.543  -29.369 1.00 14.27 ? 456  MET A C   1 
ATOM   2941 O  O   . MET A 1 351 ? -33.431 9.798   -28.932 1.00 14.00 ? 456  MET A O   1 
ATOM   2942 C  CB  . MET A 1 351 ? -30.711 12.354  -28.962 1.00 12.03 ? 456  MET A CB  1 
ATOM   2943 C  CG  . MET A 1 351 ? -30.343 13.450  -27.930 1.00 12.18 ? 456  MET A CG  1 
ATOM   2944 S  SD  . MET A 1 351 ? -28.973 14.584  -28.505 1.00 12.20 ? 456  MET A SD  1 
ATOM   2945 C  CE  . MET A 1 351 ? -27.475 13.636  -28.009 1.00 15.36 ? 456  MET A CE  1 
ATOM   2946 N  N   . GLU A 1 352 ? -32.184 10.654  -30.639 1.00 12.58 ? 457  GLU A N   1 
ATOM   2947 C  CA  . GLU A 1 352 ? -32.893 9.785   -31.658 1.00 13.19 ? 457  GLU A CA  1 
ATOM   2948 C  C   . GLU A 1 352 ? -32.012 8.605   -31.905 1.00 13.13 ? 457  GLU A C   1 
ATOM   2949 O  O   . GLU A 1 352 ? -32.164 7.930   -33.008 1.00 14.55 ? 457  GLU A O   1 
ATOM   2950 C  CB  . GLU A 1 352 ? -33.103 10.580  -32.941 1.00 13.08 ? 457  GLU A CB  1 
ATOM   2951 C  CG  . GLU A 1 352 ? -33.963 11.816  -32.732 1.00 13.82 ? 457  GLU A CG  1 
ATOM   2952 C  CD  . GLU A 1 352 ? -34.237 12.493  -34.051 1.00 17.77 ? 457  GLU A CD  1 
ATOM   2953 O  OE1 . GLU A 1 352 ? -33.445 13.376  -34.455 1.00 16.64 ? 457  GLU A OE1 1 
ATOM   2954 O  OE2 . GLU A 1 352 ? -35.118 11.998  -34.787 1.00 18.24 ? 457  GLU A OE2 1 
ATOM   2955 N  N   . ASN A 1 353 ? -31.081 8.224   -31.037 1.00 14.10 ? 458  ASN A N   1 
ATOM   2956 C  CA  . ASN A 1 353 ? -30.125 7.240   -31.398 1.00 13.34 ? 458  ASN A CA  1 
ATOM   2957 C  C   . ASN A 1 353 ? -30.713 5.804   -31.677 1.00 13.98 ? 458  ASN A C   1 
ATOM   2958 O  O   . ASN A 1 353 ? -30.120 5.035   -32.460 1.00 13.83 ? 458  ASN A O   1 
ATOM   2959 C  CB  . ASN A 1 353 ? -28.994 7.111   -30.331 1.00 13.13 ? 458  ASN A CB  1 
ATOM   2960 C  CG  . ASN A 1 353 ? -28.062 8.321   -30.372 1.00 13.09 ? 458  ASN A CG  1 
ATOM   2961 O  OD1 . ASN A 1 353 ? -28.258 9.291   -31.183 1.00 12.72 ? 458  ASN A OD1 1 
ATOM   2962 N  ND2 . ASN A 1 353 ? -27.004 8.288   -29.518 1.00 13.37 ? 458  ASN A ND2 1 
ATOM   2963 N  N   . LYS A 1 354 ? -31.810 5.497   -30.954 1.00 14.14 ? 459  LYS A N   1 
ATOM   2964 C  CA  . LYS A 1 354 ? -32.438 4.148   -31.219 1.00 14.53 ? 459  LYS A CA  1 
ATOM   2965 C  C   . LYS A 1 354 ? -32.894 4.030   -32.669 1.00 16.75 ? 459  LYS A C   1 
ATOM   2966 O  O   . LYS A 1 354 ? -33.025 2.859   -33.144 1.00 17.98 ? 459  LYS A O   1 
ATOM   2967 C  CB  . LYS A 1 354 ? -33.604 3.871   -30.292 1.00 15.64 ? 459  LYS A CB  1 
ATOM   2968 C  CG  . LYS A 1 354 ? -33.192 3.653   -28.813 1.00 17.61 ? 459  LYS A CG  1 
ATOM   2969 C  CD  . LYS A 1 354 ? -34.408 3.491   -27.911 1.00 20.34 ? 459  LYS A CD  1 
ATOM   2970 C  CE  . LYS A 1 354 ? -34.060 3.428   -26.418 1.00 20.22 ? 459  LYS A CE  1 
ATOM   2971 N  NZ  . LYS A 1 354 ? -35.295 3.117   -25.610 1.00 26.99 ? 459  LYS A NZ  1 
ATOM   2972 N  N   . THR A 1 355 ? -33.059 5.103   -33.414 1.00 15.02 ? 460  THR A N   1 
ATOM   2973 C  CA  . THR A 1 355 ? -33.493 5.011   -34.833 1.00 15.99 ? 460  THR A CA  1 
ATOM   2974 C  C   . THR A 1 355 ? -32.365 4.446   -35.666 1.00 17.48 ? 460  THR A C   1 
ATOM   2975 O  O   . THR A 1 355 ? -32.619 3.959   -36.800 1.00 22.05 ? 460  THR A O   1 
ATOM   2976 C  CB  . THR A 1 355 ? -33.997 6.336   -35.398 1.00 17.68 ? 460  THR A CB  1 
ATOM   2977 O  OG1 . THR A 1 355 ? -32.844 7.228   -35.562 1.00 18.71 ? 460  THR A OG1 1 
ATOM   2978 C  CG2 . THR A 1 355 ? -35.134 6.956   -34.587 1.00 16.70 ? 460  THR A CG2 1 
ATOM   2979 N  N   . PHE A 1 356 ? -31.115 4.387   -35.234 1.00 14.27 ? 461  PHE A N   1 
ATOM   2980 C  CA  . PHE A 1 356 ? -30.045 3.897   -36.047 1.00 14.95 ? 461  PHE A CA  1 
ATOM   2981 C  C   . PHE A 1 356 ? -29.176 2.776   -35.484 1.00 14.22 ? 461  PHE A C   1 
ATOM   2982 O  O   . PHE A 1 356 ? -28.379 2.180   -36.221 1.00 16.02 ? 461  PHE A O   1 
ATOM   2983 C  CB  . PHE A 1 356 ? -29.120 5.013   -36.568 1.00 14.78 ? 461  PHE A CB  1 
ATOM   2984 C  CG  . PHE A 1 356 ? -28.299 5.733   -35.476 1.00 14.51 ? 461  PHE A CG  1 
ATOM   2985 C  CD1 . PHE A 1 356 ? -27.189 5.101   -34.861 1.00 14.74 ? 461  PHE A CD1 1 
ATOM   2986 C  CD2 . PHE A 1 356 ? -28.747 7.004   -35.041 1.00 14.69 ? 461  PHE A CD2 1 
ATOM   2987 C  CE1 . PHE A 1 356 ? -26.469 5.784   -33.825 1.00 14.13 ? 461  PHE A CE1 1 
ATOM   2988 C  CE2 . PHE A 1 356 ? -28.029 7.664   -34.015 1.00 15.18 ? 461  PHE A CE2 1 
ATOM   2989 C  CZ  . PHE A 1 356 ? -26.919 7.065   -33.441 1.00 14.08 ? 461  PHE A CZ  1 
ATOM   2990 N  N   . LEU A 1 357 ? -29.222 2.553   -34.151 1.00 14.12 ? 462  LEU A N   1 
ATOM   2991 C  CA  . LEU A 1 357 ? -28.291 1.599   -33.507 1.00 14.66 ? 462  LEU A CA  1 
ATOM   2992 C  C   . LEU A 1 357 ? -28.294 0.223   -34.169 1.00 15.78 ? 462  LEU A C   1 
ATOM   2993 O  O   . LEU A 1 357 ? -27.269 -0.266  -34.544 1.00 16.51 ? 462  LEU A O   1 
ATOM   2994 C  CB  . LEU A 1 357 ? -28.557 1.530   -31.968 1.00 15.61 ? 462  LEU A CB  1 
ATOM   2995 C  CG  . LEU A 1 357 ? -28.146 2.860   -31.264 1.00 14.40 ? 462  LEU A CG  1 
ATOM   2996 C  CD1 . LEU A 1 357 ? -28.753 2.852   -29.859 1.00 17.48 ? 462  LEU A CD1 1 
ATOM   2997 C  CD2 . LEU A 1 357 ? -26.606 2.966   -31.148 1.00 15.50 ? 462  LEU A CD2 1 
ATOM   2998 N  N   . GLU A 1 358 ? -29.511 -0.376  -34.224 1.00 18.43 ? 463  GLU A N   1 
ATOM   2999 C  CA  . GLU A 1 358 ? -29.588 -1.756  -34.779 1.00 20.92 ? 463  GLU A CA  1 
ATOM   3000 C  C   . GLU A 1 358 ? -29.287 -1.751  -36.293 1.00 17.41 ? 463  GLU A C   1 
ATOM   3001 O  O   . GLU A 1 358 ? -28.493 -2.589  -36.725 1.00 18.32 ? 463  GLU A O   1 
ATOM   3002 C  CB  . GLU A 1 358 ? -31.002 -2.332  -34.564 1.00 22.72 ? 463  GLU A CB  1 
ATOM   3003 C  CG  . GLU A 1 358 ? -31.417 -2.599  -33.119 1.00 34.14 ? 463  GLU A CG  1 
ATOM   3004 C  CD  . GLU A 1 358 ? -31.028 -3.974  -32.593 1.00 46.77 ? 463  GLU A CD  1 
ATOM   3005 O  OE1 . GLU A 1 358 ? -30.102 -4.643  -33.161 1.00 58.27 ? 463  GLU A OE1 1 
ATOM   3006 O  OE2 . GLU A 1 358 ? -31.676 -4.367  -31.592 1.00 48.24 ? 463  GLU A OE2 1 
ATOM   3007 N  N   . LYS A 1 359 ? -29.764 -0.735  -37.007 1.00 17.23 ? 464  LYS A N   1 
ATOM   3008 C  CA  . LYS A 1 359 ? -29.557 -0.680  -38.478 1.00 17.52 ? 464  LYS A CA  1 
ATOM   3009 C  C   . LYS A 1 359 ? -28.105 -0.605  -38.874 1.00 18.73 ? 464  LYS A C   1 
ATOM   3010 O  O   . LYS A 1 359 ? -27.639 -1.181  -39.847 1.00 19.35 ? 464  LYS A O   1 
ATOM   3011 C  CB  . LYS A 1 359 ? -30.381 0.479   -39.075 1.00 21.50 ? 464  LYS A CB  1 
ATOM   3012 C  CG  . LYS A 1 359 ? -31.864 0.217   -39.087 1.00 27.50 ? 464  LYS A CG  1 
ATOM   3013 C  CD  . LYS A 1 359 ? -32.640 1.486   -39.523 1.00 30.28 ? 464  LYS A CD  1 
ATOM   3014 C  CE  . LYS A 1 359 ? -33.786 1.221   -40.467 1.00 42.79 ? 464  LYS A CE  1 
ATOM   3015 N  NZ  . LYS A 1 359 ? -35.053 1.465   -39.758 1.00 42.98 ? 464  LYS A NZ  1 
ATOM   3016 N  N   . LEU A 1 360 ? -27.305 0.113   -38.049 1.00 16.56 ? 465  LEU A N   1 
ATOM   3017 C  CA  . LEU A 1 360 ? -25.892 0.221   -38.306 1.00 13.83 ? 465  LEU A CA  1 
ATOM   3018 C  C   . LEU A 1 360 ? -24.999 -0.774  -37.605 1.00 14.41 ? 465  LEU A C   1 
ATOM   3019 O  O   . LEU A 1 360 ? -23.830 -0.605  -37.513 1.00 14.92 ? 465  LEU A O   1 
ATOM   3020 C  CB  . LEU A 1 360 ? -25.409 1.699   -37.939 1.00 14.55 ? 465  LEU A CB  1 
ATOM   3021 C  CG  . LEU A 1 360 ? -26.033 2.725   -38.817 1.00 15.01 ? 465  LEU A CG  1 
ATOM   3022 C  CD1 . LEU A 1 360 ? -25.472 4.132   -38.465 1.00 16.64 ? 465  LEU A CD1 1 
ATOM   3023 C  CD2 . LEU A 1 360 ? -25.829 2.483   -40.347 1.00 17.64 ? 465  LEU A CD2 1 
ATOM   3024 N  N   . LYS A 1 361 ? -25.594 -1.876  -37.146 1.00 14.51 ? 466  LYS A N   1 
ATOM   3025 C  CA  A LYS A 1 361 ? -24.776 -3.023  -36.670 0.50 14.50 ? 466  LYS A CA  1 
ATOM   3026 C  CA  B LYS A 1 361 ? -24.873 -3.035  -36.602 0.50 15.35 ? 466  LYS A CA  1 
ATOM   3027 C  C   . LYS A 1 361 ? -24.163 -2.763  -35.259 1.00 14.84 ? 466  LYS A C   1 
ATOM   3028 O  O   . LYS A 1 361 ? -23.204 -3.387  -34.939 1.00 16.05 ? 466  LYS A O   1 
ATOM   3029 C  CB  A LYS A 1 361 ? -23.700 -3.523  -37.688 0.50 15.81 ? 466  LYS A CB  1 
ATOM   3030 C  CB  B LYS A 1 361 ? -23.980 -3.710  -37.638 0.50 17.46 ? 466  LYS A CB  1 
ATOM   3031 C  CG  A LYS A 1 361 ? -24.236 -3.689  -39.127 0.50 15.45 ? 466  LYS A CG  1 
ATOM   3032 C  CG  B LYS A 1 361 ? -24.807 -4.072  -38.898 0.50 18.78 ? 466  LYS A CG  1 
ATOM   3033 C  CD  A LYS A 1 361 ? -23.226 -4.402  -39.997 0.50 17.44 ? 466  LYS A CD  1 
ATOM   3034 C  CD  B LYS A 1 361 ? -23.914 -4.634  -39.967 0.50 21.98 ? 466  LYS A CD  1 
ATOM   3035 C  CE  A LYS A 1 361 ? -23.752 -4.687  -41.403 0.50 17.88 ? 466  LYS A CE  1 
ATOM   3036 C  CE  B LYS A 1 361 ? -24.724 -5.371  -41.066 0.50 21.42 ? 466  LYS A CE  1 
ATOM   3037 N  NZ  A LYS A 1 361 ? -25.047 -4.091  -41.810 0.50 22.66 ? 466  LYS A NZ  1 
ATOM   3038 N  NZ  B LYS A 1 361 ? -23.863 -5.344  -42.274 0.50 24.45 ? 466  LYS A NZ  1 
ATOM   3039 N  N   . PHE A 1 362 ? -24.695 -1.835  -34.504 1.00 15.74 ? 467  PHE A N   1 
ATOM   3040 C  CA  . PHE A 1 362 ? -24.247 -1.730  -33.090 1.00 14.48 ? 467  PHE A CA  1 
ATOM   3041 C  C   . PHE A 1 362 ? -24.785 -2.967  -32.326 1.00 16.67 ? 467  PHE A C   1 
ATOM   3042 O  O   . PHE A 1 362 ? -25.872 -3.475  -32.644 1.00 17.50 ? 467  PHE A O   1 
ATOM   3043 C  CB  . PHE A 1 362 ? -24.873 -0.473  -32.402 1.00 14.74 ? 467  PHE A CB  1 
ATOM   3044 C  CG  . PHE A 1 362 ? -24.195 0.881   -32.781 1.00 13.16 ? 467  PHE A CG  1 
ATOM   3045 C  CD1 . PHE A 1 362 ? -23.425 1.597   -31.829 1.00 13.35 ? 467  PHE A CD1 1 
ATOM   3046 C  CD2 . PHE A 1 362 ? -24.433 1.478   -34.041 1.00 14.33 ? 467  PHE A CD2 1 
ATOM   3047 C  CE1 . PHE A 1 362 ? -22.835 2.843   -32.181 1.00 13.41 ? 467  PHE A CE1 1 
ATOM   3048 C  CE2 . PHE A 1 362 ? -23.860 2.705   -34.412 1.00 13.02 ? 467  PHE A CE2 1 
ATOM   3049 C  CZ  . PHE A 1 362 ? -23.045 3.428   -33.467 1.00 13.99 ? 467  PHE A CZ  1 
ATOM   3050 N  N   . GLY A 1 363 ? -24.099 -3.331  -31.274 1.00 16.15 ? 468  GLY A N   1 
ATOM   3051 C  CA  . GLY A 1 363 ? -24.537 -4.355  -30.340 1.00 15.68 ? 468  GLY A CA  1 
ATOM   3052 C  C   . GLY A 1 363 ? -24.719 -3.692  -28.961 1.00 16.57 ? 468  GLY A C   1 
ATOM   3053 O  O   . GLY A 1 363 ? -23.892 -2.773  -28.557 1.00 16.36 ? 468  GLY A O   1 
ATOM   3054 N  N   . ILE A 1 364 ? -25.677 -4.158  -28.178 1.00 16.68 ? 469  ILE A N   1 
ATOM   3055 C  CA  . ILE A 1 364 ? -25.999 -3.570  -26.895 1.00 16.81 ? 469  ILE A CA  1 
ATOM   3056 C  C   . ILE A 1 364 ? -24.940 -3.996  -25.884 1.00 16.52 ? 469  ILE A C   1 
ATOM   3057 O  O   . ILE A 1 364 ? -24.379 -5.111  -25.965 1.00 19.97 ? 469  ILE A O   1 
ATOM   3058 C  CB  . ILE A 1 364 ? -27.435 -3.929  -26.424 1.00 17.76 ? 469  ILE A CB  1 
ATOM   3059 C  CG1 . ILE A 1 364 ? -27.859 -2.921  -25.341 1.00 19.56 ? 469  ILE A CG1 1 
ATOM   3060 C  CG2 . ILE A 1 364 ? -27.537 -5.438  -25.990 1.00 19.05 ? 469  ILE A CG2 1 
ATOM   3061 C  CD1 . ILE A 1 364 ? -29.351 -2.906  -25.034 1.00 21.97 ? 469  ILE A CD1 1 
ATOM   3062 N  N   . GLY A 1 365 ? -24.493 -3.072  -25.026 1.00 17.07 ? 470  GLY A N   1 
ATOM   3063 C  CA  . GLY A 1 365 ? -23.566 -3.421  -23.943 1.00 16.95 ? 470  GLY A CA  1 
ATOM   3064 C  C   . GLY A 1 365 ? -24.204 -4.036  -22.721 1.00 19.93 ? 470  GLY A C   1 
ATOM   3065 O  O   . GLY A 1 365 ? -25.381 -4.427  -22.768 1.00 20.82 ? 470  GLY A O   1 
ATOM   3066 N  N   . ASP A 1 366 ? -23.435 -4.046  -21.631 1.00 18.09 ? 471  ASP A N   1 
ATOM   3067 C  CA  . ASP A 1 366 ? -23.939 -4.703  -20.469 1.00 21.14 ? 471  ASP A CA  1 
ATOM   3068 C  C   . ASP A 1 366 ? -24.469 -3.871  -19.318 1.00 26.46 ? 471  ASP A C   1 
ATOM   3069 O  O   . ASP A 1 366 ? -24.849 -4.432  -18.283 1.00 30.58 ? 471  ASP A O   1 
ATOM   3070 C  CB  . ASP A 1 366 ? -22.906 -5.739  -19.966 1.00 25.37 ? 471  ASP A CB  1 
ATOM   3071 C  CG  . ASP A 1 366 ? -21.609 -5.135  -19.628 1.00 32.78 ? 471  ASP A CG  1 
ATOM   3072 O  OD1 . ASP A 1 366 ? -21.463 -3.864  -19.743 1.00 34.56 ? 471  ASP A OD1 1 
ATOM   3073 O  OD2 . ASP A 1 366 ? -20.686 -5.917  -19.202 1.00 34.27 ? 471  ASP A OD2 1 
ATOM   3074 N  N   . GLY A 1 367 ? -24.385 -2.549  -19.389 1.00 24.72 ? 472  GLY A N   1 
ATOM   3075 C  CA  . GLY A 1 367 ? -24.803 -1.731  -18.238 1.00 23.20 ? 472  GLY A CA  1 
ATOM   3076 C  C   . GLY A 1 367 ? -25.499 -0.455  -18.712 1.00 18.70 ? 472  GLY A C   1 
ATOM   3077 O  O   . GLY A 1 367 ? -25.681 -0.223  -19.904 1.00 19.68 ? 472  GLY A O   1 
ATOM   3078 N  N   . ASN A 1 368 ? -25.829 0.363   -17.715 1.00 19.69 ? 473  ASN A N   1 
ATOM   3079 C  CA  A ASN A 1 368 ? -26.611 1.580   -17.796 0.50 18.81 ? 473  ASN A CA  1 
ATOM   3080 C  CA  B ASN A 1 368 ? -26.542 1.603   -17.986 0.50 18.44 ? 473  ASN A CA  1 
ATOM   3081 C  C   . ASN A 1 368 ? -25.675 2.793   -17.524 1.00 15.99 ? 473  ASN A C   1 
ATOM   3082 O  O   . ASN A 1 368 ? -24.778 2.668   -16.668 1.00 16.33 ? 473  ASN A O   1 
ATOM   3083 C  CB  A ASN A 1 368 ? -27.648 1.579   -16.647 0.50 20.09 ? 473  ASN A CB  1 
ATOM   3084 C  CB  B ASN A 1 368 ? -27.891 1.693   -17.250 0.50 19.09 ? 473  ASN A CB  1 
ATOM   3085 C  CG  A ASN A 1 368 ? -28.487 0.309   -16.569 0.50 21.31 ? 473  ASN A CG  1 
ATOM   3086 C  CG  B ASN A 1 368 ? -29.004 0.842   -17.855 0.50 21.95 ? 473  ASN A CG  1 
ATOM   3087 O  OD1 A ASN A 1 368 ? -28.874 -0.224  -17.598 0.50 24.03 ? 473  ASN A OD1 1 
ATOM   3088 O  OD1 B ASN A 1 368 ? -29.363 1.004   -18.996 0.50 22.20 ? 473  ASN A OD1 1 
ATOM   3089 N  ND2 A ASN A 1 368 ? -28.800 -0.145  -15.361 0.50 24.18 ? 473  ASN A ND2 1 
ATOM   3090 N  ND2 B ASN A 1 368 ? -29.653 0.063   -17.010 0.50 22.29 ? 473  ASN A ND2 1 
ATOM   3091 N  N   . LEU A 1 369 ? -25.990 3.907   -18.130 1.00 14.15 ? 474  LEU A N   1 
ATOM   3092 C  CA  . LEU A 1 369 ? -25.477 5.218   -17.641 1.00 12.65 ? 474  LEU A CA  1 
ATOM   3093 C  C   . LEU A 1 369 ? -26.771 5.934   -17.162 1.00 12.95 ? 474  LEU A C   1 
ATOM   3094 O  O   . LEU A 1 369 ? -27.673 6.206   -17.944 1.00 13.43 ? 474  LEU A O   1 
ATOM   3095 C  CB  . LEU A 1 369 ? -24.828 6.012   -18.772 1.00 13.92 ? 474  LEU A CB  1 
ATOM   3096 C  CG  . LEU A 1 369 ? -24.152 7.278   -18.187 1.00 12.48 ? 474  LEU A CG  1 
ATOM   3097 C  CD1 . LEU A 1 369 ? -22.912 6.984   -17.246 1.00 14.01 ? 474  LEU A CD1 1 
ATOM   3098 C  CD2 . LEU A 1 369 ? -23.760 8.254   -19.310 1.00 13.17 ? 474  LEU A CD2 1 
ATOM   3099 N  N   . GLN A 1 370 ? -26.860 6.177   -15.821 1.00 11.81 ? 475  GLN A N   1 
ATOM   3100 C  CA  A GLN A 1 370 ? -27.966 6.850   -15.205 0.50 11.68 ? 475  GLN A CA  1 
ATOM   3101 C  CA  B GLN A 1 370 ? -28.008 6.894   -15.261 0.50 12.90 ? 475  GLN A CA  1 
ATOM   3102 C  C   . GLN A 1 370 ? -27.719 8.375   -15.217 1.00 11.41 ? 475  GLN A C   1 
ATOM   3103 O  O   . GLN A 1 370 ? -26.584 8.813   -15.004 1.00 13.20 ? 475  GLN A O   1 
ATOM   3104 C  CB  A GLN A 1 370 ? -28.044 6.345   -13.742 0.50 10.63 ? 475  GLN A CB  1 
ATOM   3105 C  CB  B GLN A 1 370 ? -28.387 6.403   -13.837 0.50 14.05 ? 475  GLN A CB  1 
ATOM   3106 C  CG  A GLN A 1 370 ? -28.167 4.832   -13.494 0.50 10.61 ? 475  GLN A CG  1 
ATOM   3107 C  CG  B GLN A 1 370 ? -29.203 5.088   -13.847 0.50 17.79 ? 475  GLN A CG  1 
ATOM   3108 C  CD  A GLN A 1 370 ? -29.503 4.233   -13.921 0.50 12.51 ? 475  GLN A CD  1 
ATOM   3109 C  CD  B GLN A 1 370 ? -28.341 3.837   -13.918 0.50 17.13 ? 475  GLN A CD  1 
ATOM   3110 O  OE1 A GLN A 1 370 ? -29.658 3.000   -13.912 0.50 16.10 ? 475  GLN A OE1 1 
ATOM   3111 O  OE1 B GLN A 1 370 ? -27.127 3.811   -13.627 0.50 20.63 ? 475  GLN A OE1 1 
ATOM   3112 N  NE2 A GLN A 1 370 ? -30.443 5.024   -14.210 0.50 9.83  ? 475  GLN A NE2 1 
ATOM   3113 N  NE2 B GLN A 1 370 ? -28.989 2.741   -14.229 0.50 16.42 ? 475  GLN A NE2 1 
ATOM   3114 N  N   . TYR A 1 371 ? -28.784 9.184   -15.406 1.00 10.67 ? 476  TYR A N   1 
ATOM   3115 C  CA  . TYR A 1 371 ? -28.699 10.645  -15.337 1.00 11.62 ? 476  TYR A CA  1 
ATOM   3116 C  C   . TYR A 1 371 ? -29.407 11.097  -14.094 1.00 11.79 ? 476  TYR A C   1 
ATOM   3117 O  O   . TYR A 1 371 ? -30.505 10.568  -13.753 1.00 12.17 ? 476  TYR A O   1 
ATOM   3118 C  CB  . TYR A 1 371 ? -29.437 11.259  -16.580 1.00 12.90 ? 476  TYR A CB  1 
ATOM   3119 C  CG  . TYR A 1 371 ? -28.592 11.256  -17.801 1.00 11.56 ? 476  TYR A CG  1 
ATOM   3120 C  CD1 . TYR A 1 371 ? -28.013 12.435  -18.289 1.00 11.07 ? 476  TYR A CD1 1 
ATOM   3121 C  CD2 . TYR A 1 371 ? -28.276 10.038  -18.457 1.00 12.23 ? 476  TYR A CD2 1 
ATOM   3122 C  CE1 . TYR A 1 371 ? -27.214 12.433  -19.398 1.00 10.43 ? 476  TYR A CE1 1 
ATOM   3123 C  CE2 . TYR A 1 371 ? -27.419 10.030  -19.583 1.00 11.30 ? 476  TYR A CE2 1 
ATOM   3124 C  CZ  . TYR A 1 371 ? -26.896 11.258  -20.069 1.00 11.02 ? 476  TYR A CZ  1 
ATOM   3125 O  OH  . TYR A 1 371 ? -26.071 11.218  -21.189 1.00 11.58 ? 476  TYR A OH  1 
ATOM   3126 N  N   . TYR A 1 372 ? -28.867 12.101  -13.442 1.00 10.90 ? 477  TYR A N   1 
ATOM   3127 C  CA  . TYR A 1 372 ? -29.409 12.574  -12.153 1.00 11.31 ? 477  TYR A CA  1 
ATOM   3128 C  C   . TYR A 1 372 ? -29.372 14.100  -12.128 1.00 11.35 ? 477  TYR A C   1 
ATOM   3129 O  O   . TYR A 1 372 ? -28.548 14.769  -12.717 1.00 10.95 ? 477  TYR A O   1 
ATOM   3130 C  CB  . TYR A 1 372 ? -28.461 12.141  -11.000 1.00 12.13 ? 477  TYR A CB  1 
ATOM   3131 C  CG  . TYR A 1 372 ? -28.347 10.643  -10.818 1.00 12.22 ? 477  TYR A CG  1 
ATOM   3132 C  CD1 . TYR A 1 372 ? -29.353 9.976   -10.073 1.00 11.72 ? 477  TYR A CD1 1 
ATOM   3133 C  CD2 . TYR A 1 372 ? -27.309 9.923   -11.381 1.00 12.35 ? 477  TYR A CD2 1 
ATOM   3134 C  CE1 . TYR A 1 372 ? -29.296 8.603   -10.006 1.00 13.22 ? 477  TYR A CE1 1 
ATOM   3135 C  CE2 . TYR A 1 372 ? -27.213 8.514   -11.268 1.00 12.88 ? 477  TYR A CE2 1 
ATOM   3136 C  CZ  . TYR A 1 372 ? -28.244 7.919   -10.561 1.00 12.28 ? 477  TYR A CZ  1 
ATOM   3137 O  OH  . TYR A 1 372 ? -28.218 6.536   -10.421 1.00 14.04 ? 477  TYR A OH  1 
ATOM   3138 N  N   . LEU A 1 373 ? -30.330 14.639  -11.387 1.00 11.47 ? 478  LEU A N   1 
ATOM   3139 C  CA  . LEU A 1 373 ? -30.341 16.043  -10.946 1.00 10.97 ? 478  LEU A CA  1 
ATOM   3140 C  C   . LEU A 1 373 ? -30.204 16.109  -9.440  1.00 12.09 ? 478  LEU A C   1 
ATOM   3141 O  O   . LEU A 1 373 ? -30.847 15.284  -8.715  1.00 12.03 ? 478  LEU A O   1 
ATOM   3142 C  CB  . LEU A 1 373 ? -31.582 16.832  -11.385 1.00 11.85 ? 478  LEU A CB  1 
ATOM   3143 C  CG  . LEU A 1 373 ? -31.766 16.853  -12.919 1.00 12.20 ? 478  LEU A CG  1 
ATOM   3144 C  CD1 . LEU A 1 373 ? -33.182 17.349  -13.284 1.00 15.95 ? 478  LEU A CD1 1 
ATOM   3145 C  CD2 . LEU A 1 373 ? -30.699 17.676  -13.592 1.00 16.08 ? 478  LEU A CD2 1 
ATOM   3146 N  N   . TYR A 1 374 ? -29.410 17.072  -8.933  1.00 10.60 ? 479  TYR A N   1 
ATOM   3147 C  CA  . TYR A 1 374 ? -29.340 17.360  -7.475  1.00 10.73 ? 479  TYR A CA  1 
ATOM   3148 C  C   . TYR A 1 374 ? -30.228 18.541  -7.198  1.00 10.52 ? 479  TYR A C   1 
ATOM   3149 O  O   . TYR A 1 374 ? -30.087 19.603  -7.808  1.00 11.43 ? 479  TYR A O   1 
ATOM   3150 C  CB  . TYR A 1 374 ? -27.877 17.721  -7.168  1.00 10.59 ? 479  TYR A CB  1 
ATOM   3151 C  CG  . TYR A 1 374 ? -27.568 17.916  -5.645  1.00 9.47  ? 479  TYR A CG  1 
ATOM   3152 C  CD1 . TYR A 1 374 ? -27.201 16.808  -4.884  1.00 10.20 ? 479  TYR A CD1 1 
ATOM   3153 C  CD2 . TYR A 1 374 ? -27.718 19.140  -5.039  1.00 9.72  ? 479  TYR A CD2 1 
ATOM   3154 C  CE1 . TYR A 1 374 ? -26.895 16.944  -3.497  1.00 10.62 ? 479  TYR A CE1 1 
ATOM   3155 C  CE2 . TYR A 1 374 ? -27.462 19.345  -3.683  1.00 9.93  ? 479  TYR A CE2 1 
ATOM   3156 C  CZ  . TYR A 1 374 ? -27.009 18.250  -2.949  1.00 9.68  ? 479  TYR A CZ  1 
ATOM   3157 O  OH  . TYR A 1 374 ? -26.739 18.434  -1.589  1.00 10.65 ? 479  TYR A OH  1 
ATOM   3158 N  N   . ASN A 1 375 ? -31.085 18.403  -6.157  1.00 11.32 ? 480  ASN A N   1 
ATOM   3159 C  CA  . ASN A 1 375 ? -31.958 19.494  -5.666  1.00 11.28 ? 480  ASN A CA  1 
ATOM   3160 C  C   . ASN A 1 375 ? -32.975 19.952  -6.744  1.00 11.27 ? 480  ASN A C   1 
ATOM   3161 O  O   . ASN A 1 375 ? -33.259 21.140  -6.856  1.00 11.71 ? 480  ASN A O   1 
ATOM   3162 C  CB  . ASN A 1 375 ? -31.178 20.636  -5.011  1.00 12.00 ? 480  ASN A CB  1 
ATOM   3163 C  CG  . ASN A 1 375 ? -32.084 21.642  -4.308  1.00 11.62 ? 480  ASN A CG  1 
ATOM   3164 O  OD1 . ASN A 1 375 ? -33.061 21.138  -3.690  1.00 13.47 ? 480  ASN A OD1 1 
ATOM   3165 N  ND2 . ASN A 1 375 ? -31.697 22.873  -4.251  1.00 12.45 ? 480  ASN A ND2 1 
ATOM   3166 N  N   . TRP A 1 376 ? -33.446 18.985  -7.558  1.00 12.55 ? 481  TRP A N   1 
ATOM   3167 C  CA  . TRP A 1 376 ? -34.487 19.325  -8.529  1.00 12.51 ? 481  TRP A CA  1 
ATOM   3168 C  C   . TRP A 1 376 ? -35.400 18.137  -8.680  1.00 12.94 ? 481  TRP A C   1 
ATOM   3169 O  O   . TRP A 1 376 ? -34.964 17.076  -9.088  1.00 16.23 ? 481  TRP A O   1 
ATOM   3170 C  CB  . TRP A 1 376 ? -33.917 19.711  -9.890  1.00 12.74 ? 481  TRP A CB  1 
ATOM   3171 C  CG  . TRP A 1 376 ? -34.970 20.439  -10.777 1.00 12.51 ? 481  TRP A CG  1 
ATOM   3172 C  CD1 . TRP A 1 376 ? -35.735 19.863  -11.812 1.00 14.59 ? 481  TRP A CD1 1 
ATOM   3173 C  CD2 . TRP A 1 376 ? -35.389 21.798  -10.654 1.00 12.92 ? 481  TRP A CD2 1 
ATOM   3174 N  NE1 . TRP A 1 376 ? -36.562 20.831  -12.286 1.00 14.64 ? 481  TRP A NE1 1 
ATOM   3175 C  CE2 . TRP A 1 376 ? -36.398 22.002  -11.649 1.00 13.32 ? 481  TRP A CE2 1 
ATOM   3176 C  CE3 . TRP A 1 376 ? -35.053 22.887  -9.819  1.00 13.35 ? 481  TRP A CE3 1 
ATOM   3177 C  CZ2 . TRP A 1 376 ? -37.048 23.242  -11.805 1.00 13.49 ? 481  TRP A CZ2 1 
ATOM   3178 C  CZ3 . TRP A 1 376 ? -35.674 24.088  -9.999  1.00 14.22 ? 481  TRP A CZ3 1 
ATOM   3179 C  CH2 . TRP A 1 376 ? -36.643 24.276  -11.035 1.00 15.63 ? 481  TRP A CH2 1 
ATOM   3180 N  N   . LYS A 1 377 ? -36.673 18.339  -8.312  1.00 16.48 ? 482  LYS A N   1 
ATOM   3181 C  CA  A LYS A 1 377 ? -37.714 17.282  -8.427  0.50 17.52 ? 482  LYS A CA  1 
ATOM   3182 C  CA  B LYS A 1 377 ? -37.576 17.176  -8.499  0.50 17.94 ? 482  LYS A CA  1 
ATOM   3183 C  C   . LYS A 1 377 ? -38.428 17.383  -9.760  1.00 19.44 ? 482  LYS A C   1 
ATOM   3184 O  O   . LYS A 1 377 ? -38.898 18.489  -10.055 1.00 22.18 ? 482  LYS A O   1 
ATOM   3185 C  CB  A LYS A 1 377 ? -38.767 17.514  -7.332  0.50 19.12 ? 482  LYS A CB  1 
ATOM   3186 C  CB  B LYS A 1 377 ? -38.344 16.754  -7.214  0.50 21.53 ? 482  LYS A CB  1 
ATOM   3187 C  CG  A LYS A 1 377 ? -39.524 16.224  -6.984  0.50 20.75 ? 482  LYS A CG  1 
ATOM   3188 C  CG  B LYS A 1 377 ? -38.645 17.900  -6.285  0.50 22.27 ? 482  LYS A CG  1 
ATOM   3189 C  CD  A LYS A 1 377 ? -40.178 16.260  -5.609  0.50 23.10 ? 482  LYS A CD  1 
ATOM   3190 C  CD  B LYS A 1 377 ? -39.878 17.749  -5.393  0.50 24.42 ? 482  LYS A CD  1 
ATOM   3191 C  CE  A LYS A 1 377 ? -39.337 15.494  -4.620  0.50 27.17 ? 482  LYS A CE  1 
ATOM   3192 C  CE  B LYS A 1 377 ? -40.081 19.035  -4.601  0.50 27.84 ? 482  LYS A CE  1 
ATOM   3193 N  NZ  A LYS A 1 377 ? -40.043 15.264  -3.339  0.50 31.50 ? 482  LYS A NZ  1 
ATOM   3194 N  NZ  B LYS A 1 377 ? -40.220 20.239  -5.483  0.50 27.02 ? 482  LYS A NZ  1 
ATOM   3195 N  N   . CYS A 1 378 ? -38.543 16.297  -10.530 1.00 17.57 ? 483  CYS A N   1 
ATOM   3196 C  CA  . CYS A 1 378 ? -39.347 16.425  -11.777 1.00 17.29 ? 483  CYS A CA  1 
ATOM   3197 C  C   . CYS A 1 378 ? -39.643 14.944  -12.129 1.00 16.20 ? 483  CYS A C   1 
ATOM   3198 O  O   . CYS A 1 378 ? -38.977 14.033  -11.665 1.00 16.83 ? 483  CYS A O   1 
ATOM   3199 C  CB  . CYS A 1 378 ? -38.553 17.162  -12.909 1.00 17.13 ? 483  CYS A CB  1 
ATOM   3200 S  SG  . CYS A 1 378 ? -36.965 16.363  -13.303 1.00 16.70 ? 483  CYS A SG  1 
ATOM   3201 N  N   . PRO A 1 379 ? -40.580 14.727  -13.062 1.00 18.02 ? 484  PRO A N   1 
ATOM   3202 C  CA  . PRO A 1 379 ? -40.809 13.357  -13.503 1.00 17.94 ? 484  PRO A CA  1 
ATOM   3203 C  C   . PRO A 1 379 ? -39.597 12.781  -14.259 1.00 17.27 ? 484  PRO A C   1 
ATOM   3204 O  O   . PRO A 1 379 ? -38.859 13.570  -14.957 1.00 18.76 ? 484  PRO A O   1 
ATOM   3205 C  CB  . PRO A 1 379 ? -42.050 13.490  -14.422 1.00 18.75 ? 484  PRO A CB  1 
ATOM   3206 C  CG  . PRO A 1 379 ? -42.687 14.783  -14.052 1.00 19.11 ? 484  PRO A CG  1 
ATOM   3207 C  CD  . PRO A 1 379 ? -41.477 15.684  -13.742 1.00 18.52 ? 484  PRO A CD  1 
ATOM   3208 N  N   . SER A 1 380 ? -39.362 11.535  -14.135 1.00 15.97 ? 485  SER A N   1 
ATOM   3209 C  CA  . SER A 1 380 ? -38.386 10.864  -15.004 1.00 16.87 ? 485  SER A CA  1 
ATOM   3210 C  C   . SER A 1 380 ? -38.825 10.834  -16.484 1.00 17.76 ? 485  SER A C   1 
ATOM   3211 O  O   . SER A 1 380 ? -40.005 11.113  -16.807 1.00 20.14 ? 485  SER A O   1 
ATOM   3212 C  CB  . SER A 1 380 ? -37.976 9.522   -14.499 1.00 21.02 ? 485  SER A CB  1 
ATOM   3213 O  OG  . SER A 1 380 ? -39.116 8.628   -14.576 1.00 25.06 ? 485  SER A OG  1 
ATOM   3214 N  N   . MET A 1 381 ? -37.844 10.619  -17.381 1.00 15.18 ? 486  MET A N   1 
ATOM   3215 C  CA  . MET A 1 381 ? -38.158 10.636  -18.789 1.00 14.83 ? 486  MET A CA  1 
ATOM   3216 C  C   . MET A 1 381 ? -37.508 9.437   -19.442 1.00 13.98 ? 486  MET A C   1 
ATOM   3217 O  O   . MET A 1 381 ? -36.535 8.812   -18.942 1.00 16.35 ? 486  MET A O   1 
ATOM   3218 C  CB  . MET A 1 381 ? -37.571 11.955  -19.428 1.00 15.82 ? 486  MET A CB  1 
ATOM   3219 C  CG  . MET A 1 381 ? -36.005 12.002  -19.445 1.00 15.30 ? 486  MET A CG  1 
ATOM   3220 S  SD  . MET A 1 381 ? -35.466 13.661  -19.941 1.00 15.37 ? 486  MET A SD  1 
ATOM   3221 C  CE  . MET A 1 381 ? -35.863 14.619  -18.504 1.00 15.63 ? 486  MET A CE  1 
ATOM   3222 N  N   . GLY A 1 382 ? -38.062 9.068   -20.635 1.00 15.16 ? 487  GLY A N   1 
ATOM   3223 C  CA  . GLY A 1 382 ? -37.474 8.029   -21.465 1.00 15.49 ? 487  GLY A CA  1 
ATOM   3224 C  C   . GLY A 1 382 ? -36.098 8.450   -22.003 1.00 14.95 ? 487  GLY A C   1 
ATOM   3225 O  O   . GLY A 1 382 ? -35.835 9.665   -22.122 1.00 13.97 ? 487  GLY A O   1 
ATOM   3226 N  N   . ALA A 1 383 ? -35.317 7.475   -22.344 1.00 15.09 ? 488  ALA A N   1 
ATOM   3227 C  CA  . ALA A 1 383 ? -33.920 7.721   -22.904 1.00 15.24 ? 488  ALA A CA  1 
ATOM   3228 C  C   . ALA A 1 383 ? -34.005 8.621   -24.124 1.00 13.44 ? 488  ALA A C   1 
ATOM   3229 O  O   . ALA A 1 383 ? -33.164 9.503   -24.278 1.00 14.41 ? 488  ALA A O   1 
ATOM   3230 C  CB  . ALA A 1 383 ? -33.224 6.415   -23.231 1.00 15.87 ? 488  ALA A CB  1 
ATOM   3231 N  N   . GLU A 1 384 ? -35.054 8.544   -24.929 1.00 15.55 ? 489  GLU A N   1 
ATOM   3232 C  CA  A GLU A 1 384 ? -35.217 9.278   -26.186 0.50 14.61 ? 489  GLU A CA  1 
ATOM   3233 C  CA  B GLU A 1 384 ? -35.092 9.251   -26.183 0.50 13.58 ? 489  GLU A CA  1 
ATOM   3234 C  C   . GLU A 1 384 ? -35.420 10.743  -25.933 1.00 15.10 ? 489  GLU A C   1 
ATOM   3235 O  O   . GLU A 1 384 ? -35.311 11.608  -26.856 1.00 14.52 ? 489  GLU A O   1 
ATOM   3236 C  CB  A GLU A 1 384 ? -36.484 8.749   -26.981 0.50 17.05 ? 489  GLU A CB  1 
ATOM   3237 C  CB  B GLU A 1 384 ? -36.140 8.559   -27.115 0.50 14.69 ? 489  GLU A CB  1 
ATOM   3238 C  CG  A GLU A 1 384 ? -36.492 7.281   -27.416 0.50 18.29 ? 489  GLU A CG  1 
ATOM   3239 C  CG  B GLU A 1 384 ? -37.542 9.074   -26.799 0.50 15.28 ? 489  GLU A CG  1 
ATOM   3240 C  CD  A GLU A 1 384 ? -36.885 6.254   -26.298 0.50 19.23 ? 489  GLU A CD  1 
ATOM   3241 C  CD  B GLU A 1 384 ? -38.227 8.361   -25.640 0.50 17.44 ? 489  GLU A CD  1 
ATOM   3242 O  OE1 A GLU A 1 384 ? -37.012 6.571   -25.108 0.50 18.52 ? 489  GLU A OE1 1 
ATOM   3243 O  OE1 B GLU A 1 384 ? -37.651 7.402   -25.144 0.50 15.53 ? 489  GLU A OE1 1 
ATOM   3244 O  OE2 A GLU A 1 384 ? -37.011 5.073   -26.586 0.50 21.97 ? 489  GLU A OE2 1 
ATOM   3245 O  OE2 B GLU A 1 384 ? -39.315 8.736   -25.170 0.50 21.94 ? 489  GLU A OE2 1 
ATOM   3246 N  N   . LYS A 1 385 ? -35.718 11.117  -24.652 1.00 14.73 ? 490  LYS A N   1 
ATOM   3247 C  CA  . LYS A 1 385 ? -35.912 12.518  -24.322 1.00 14.85 ? 490  LYS A CA  1 
ATOM   3248 C  C   . LYS A 1 385 ? -34.692 13.115  -23.627 1.00 12.29 ? 490  LYS A C   1 
ATOM   3249 O  O   . LYS A 1 385 ? -34.731 14.298  -23.370 1.00 13.71 ? 490  LYS A O   1 
ATOM   3250 C  CB  . LYS A 1 385 ? -37.173 12.746  -23.440 1.00 17.25 ? 490  LYS A CB  1 
ATOM   3251 C  CG  . LYS A 1 385 ? -38.437 12.336  -24.275 1.00 20.50 ? 490  LYS A CG  1 
ATOM   3252 C  CD  . LYS A 1 385 ? -38.739 13.298  -25.347 1.00 26.42 ? 490  LYS A CD  1 
ATOM   3253 C  CE  . LYS A 1 385 ? -40.160 12.864  -25.780 1.00 31.82 ? 490  LYS A CE  1 
ATOM   3254 N  NZ  . LYS A 1 385 ? -40.421 13.463  -27.089 1.00 38.58 ? 490  LYS A NZ  1 
ATOM   3255 N  N   . VAL A 1 386 ? -33.716 12.263  -23.370 1.00 12.90 ? 491  VAL A N   1 
ATOM   3256 C  CA  . VAL A 1 386 ? -32.454 12.825  -22.735 1.00 12.16 ? 491  VAL A CA  1 
ATOM   3257 C  C   . VAL A 1 386 ? -31.634 13.417  -23.903 1.00 10.78 ? 491  VAL A C   1 
ATOM   3258 O  O   . VAL A 1 386 ? -31.370 12.704  -24.910 1.00 11.20 ? 491  VAL A O   1 
ATOM   3259 C  CB  . VAL A 1 386 ? -31.674 11.716  -22.059 1.00 12.59 ? 491  VAL A CB  1 
ATOM   3260 C  CG1 . VAL A 1 386 ? -30.317 12.246  -21.488 1.00 13.75 ? 491  VAL A CG1 1 
ATOM   3261 C  CG2 . VAL A 1 386 ? -32.498 11.115  -20.884 1.00 13.45 ? 491  VAL A CG2 1 
ATOM   3262 N  N   . GLY A 1 387 ? -31.187 14.691  -23.795 1.00 11.15 ? 492  GLY A N   1 
ATOM   3263 C  CA  . GLY A 1 387 ? -30.446 15.395  -24.836 1.00 11.32 ? 492  GLY A CA  1 
ATOM   3264 C  C   . GLY A 1 387 ? -29.160 16.043  -24.314 1.00 10.91 ? 492  GLY A C   1 
ATOM   3265 O  O   . GLY A 1 387 ? -28.850 17.177  -24.712 1.00 10.73 ? 492  GLY A O   1 
ATOM   3266 N  N   . LEU A 1 388 ? -28.446 15.283  -23.473 1.00 10.46 ? 493  LEU A N   1 
ATOM   3267 C  CA  . LEU A 1 388 ? -27.269 15.871  -22.805 1.00 10.38 ? 493  LEU A CA  1 
ATOM   3268 C  C   . LEU A 1 388 ? -26.227 14.752  -22.730 1.00 10.03 ? 493  LEU A C   1 
ATOM   3269 O  O   . LEU A 1 388 ? -26.582 13.613  -22.363 1.00 10.62 ? 493  LEU A O   1 
ATOM   3270 C  CB  . LEU A 1 388 ? -27.645 16.239  -21.367 1.00 11.36 ? 493  LEU A CB  1 
ATOM   3271 C  CG  . LEU A 1 388 ? -26.478 16.668  -20.463 1.00 10.06 ? 493  LEU A CG  1 
ATOM   3272 C  CD1 . LEU A 1 388 ? -25.859 17.969  -20.919 1.00 12.56 ? 493  LEU A CD1 1 
ATOM   3273 C  CD2 . LEU A 1 388 ? -26.994 16.802  -19.020 1.00 11.73 ? 493  LEU A CD2 1 
ATOM   3274 N  N   . VAL A 1 389 ? -24.984 15.038  -23.126 1.00 9.81  ? 494  VAL A N   1 
ATOM   3275 C  CA  . VAL A 1 389 ? -23.881 14.060  -23.123 1.00 10.19 ? 494  VAL A CA  1 
ATOM   3276 C  C   . VAL A 1 389 ? -22.742 14.613  -22.265 1.00 10.93 ? 494  VAL A C   1 
ATOM   3277 O  O   . VAL A 1 389 ? -22.291 15.737  -22.581 1.00 13.34 ? 494  VAL A O   1 
ATOM   3278 C  CB  . VAL A 1 389 ? -23.371 13.703  -24.541 1.00 10.26 ? 494  VAL A CB  1 
ATOM   3279 C  CG1 . VAL A 1 389 ? -22.201 12.720  -24.430 1.00 12.22 ? 494  VAL A CG1 1 
ATOM   3280 C  CG2 . VAL A 1 389 ? -24.549 13.131  -25.359 1.00 12.77 ? 494  VAL A CG2 1 
ATOM   3281 N  N   . LEU A 1 390 ? -22.313 13.888  -21.241 1.00 11.34 ? 495  LEU A N   1 
ATOM   3282 C  CA  . LEU A 1 390 ? -21.113 14.286  -20.404 1.00 11.31 ? 495  LEU A CA  1 
ATOM   3283 C  C   . LEU A 1 390 ? -19.938 13.381  -20.726 1.00 12.59 ? 495  LEU A C   1 
ATOM   3284 O  O   . LEU A 1 390 ? -20.144 12.160  -21.029 1.00 16.16 ? 495  LEU A O   1 
ATOM   3285 C  CB  . LEU A 1 390 ? -21.356 14.135  -18.898 1.00 12.00 ? 495  LEU A CB  1 
ATOM   3286 C  CG  . LEU A 1 390 ? -22.506 15.046  -18.364 1.00 14.53 ? 495  LEU A CG  1 
ATOM   3287 C  CD1 . LEU A 1 390 ? -22.476 14.943  -16.857 1.00 15.79 ? 495  LEU A CD1 1 
ATOM   3288 C  CD2 . LEU A 1 390 ? -22.614 16.477  -18.822 1.00 20.29 ? 495  LEU A CD2 1 
ATOM   3289 N  N   . GLN A 1 391 ? -18.739 13.908  -20.743 1.00 12.56 ? 496  GLN A N   1 
ATOM   3290 C  CA  . GLN A 1 391 ? -17.545 13.091  -21.119 1.00 12.25 ? 496  GLN A CA  1 
ATOM   3291 C  C   . GLN A 1 391 ? -17.222 12.080  -20.037 1.00 13.65 ? 496  GLN A C   1 
ATOM   3292 O  O   . GLN A 1 391 ? -16.521 11.080  -20.414 1.00 13.08 ? 496  GLN A O   1 
ATOM   3293 C  CB  . GLN A 1 391 ? -16.319 13.960  -21.266 1.00 15.33 ? 496  GLN A CB  1 
ATOM   3294 C  CG  . GLN A 1 391 ? -16.344 15.048  -22.411 1.00 16.73 ? 496  GLN A CG  1 
ATOM   3295 C  CD  . GLN A 1 391 ? -17.244 16.222  -22.144 1.00 16.31 ? 496  GLN A CD  1 
ATOM   3296 O  OE1 . GLN A 1 391 ? -17.655 16.541  -21.014 1.00 17.43 ? 496  GLN A OE1 1 
ATOM   3297 N  NE2 . GLN A 1 391 ? -17.614 16.936  -23.248 1.00 16.09 ? 496  GLN A NE2 1 
ATOM   3298 O  OXT . GLN A 1 391 ? -17.648 12.166  -18.840 1.00 11.46 ? 496  GLN A OXT 1 
ATOM   3299 N  N   . ARG B 1 10  ? -37.272 65.489  -30.031 1.00 71.13 ? 115  ARG B N   1 
ATOM   3300 C  CA  . ARG B 1 10  ? -36.005 64.707  -29.966 1.00 64.91 ? 115  ARG B CA  1 
ATOM   3301 C  C   . ARG B 1 10  ? -36.009 63.505  -30.919 1.00 70.72 ? 115  ARG B C   1 
ATOM   3302 O  O   . ARG B 1 10  ? -37.074 62.959  -31.239 1.00 81.41 ? 115  ARG B O   1 
ATOM   3303 C  CB  . ARG B 1 10  ? -35.745 64.221  -28.529 1.00 65.91 ? 115  ARG B CB  1 
ATOM   3304 C  CG  . ARG B 1 10  ? -34.833 65.102  -27.662 1.00 64.46 ? 115  ARG B CG  1 
ATOM   3305 C  CD  . ARG B 1 10  ? -33.458 65.392  -28.269 1.00 65.67 ? 115  ARG B CD  1 
ATOM   3306 N  NE  . ARG B 1 10  ? -32.732 64.175  -28.677 1.00 64.33 ? 115  ARG B NE  1 
ATOM   3307 C  CZ  . ARG B 1 10  ? -31.533 63.800  -28.238 1.00 61.01 ? 115  ARG B CZ  1 
ATOM   3308 N  NH1 . ARG B 1 10  ? -30.874 64.532  -27.358 1.00 59.12 ? 115  ARG B NH1 1 
ATOM   3309 N  NH2 . ARG B 1 10  ? -30.976 62.689  -28.709 1.00 58.02 ? 115  ARG B NH2 1 
ATOM   3310 N  N   . SER B 1 11  ? -34.821 63.116  -31.393 1.00 58.03 ? 116  SER B N   1 
ATOM   3311 C  CA  . SER B 1 11  ? -34.627 61.770  -31.952 1.00 45.79 ? 116  SER B CA  1 
ATOM   3312 C  C   . SER B 1 11  ? -33.227 61.227  -31.548 1.00 34.84 ? 116  SER B C   1 
ATOM   3313 O  O   . SER B 1 11  ? -32.303 61.973  -31.163 1.00 42.39 ? 116  SER B O   1 
ATOM   3314 C  CB  . SER B 1 11  ? -34.849 61.747  -33.459 1.00 43.85 ? 116  SER B CB  1 
ATOM   3315 O  OG  . SER B 1 11  ? -33.664 62.151  -34.101 1.00 46.71 ? 116  SER B OG  1 
ATOM   3316 N  N   . TYR B 1 12  ? -33.107 59.923  -31.570 1.00 28.17 ? 117  TYR B N   1 
ATOM   3317 C  CA  . TYR B 1 12  ? -31.877 59.252  -31.034 1.00 19.63 ? 117  TYR B CA  1 
ATOM   3318 C  C   . TYR B 1 12  ? -31.356 58.381  -32.152 1.00 15.17 ? 117  TYR B C   1 
ATOM   3319 O  O   . TYR B 1 12  ? -31.785 57.219  -32.301 1.00 15.37 ? 117  TYR B O   1 
ATOM   3320 C  CB  . TYR B 1 12  ? -32.249 58.426  -29.826 1.00 18.83 ? 117  TYR B CB  1 
ATOM   3321 C  CG  . TYR B 1 12  ? -32.531 59.201  -28.553 1.00 19.63 ? 117  TYR B CG  1 
ATOM   3322 C  CD1 . TYR B 1 12  ? -31.495 59.468  -27.636 1.00 19.25 ? 117  TYR B CD1 1 
ATOM   3323 C  CD2 . TYR B 1 12  ? -33.851 59.643  -28.234 1.00 20.14 ? 117  TYR B CD2 1 
ATOM   3324 C  CE1 . TYR B 1 12  ? -31.730 60.100  -26.406 1.00 20.39 ? 117  TYR B CE1 1 
ATOM   3325 C  CE2 . TYR B 1 12  ? -34.100 60.334  -26.996 1.00 21.63 ? 117  TYR B CE2 1 
ATOM   3326 C  CZ  . TYR B 1 12  ? -33.010 60.594  -26.138 1.00 20.59 ? 117  TYR B CZ  1 
ATOM   3327 O  OH  . TYR B 1 12  ? -33.230 61.186  -24.941 1.00 23.73 ? 117  TYR B OH  1 
ATOM   3328 N  N   . GLN B 1 13  ? -30.419 58.911  -32.944 1.00 14.99 ? 118  GLN B N   1 
ATOM   3329 C  CA  . GLN B 1 13  ? -29.983 58.207  -34.138 1.00 14.97 ? 118  GLN B CA  1 
ATOM   3330 C  C   . GLN B 1 13  ? -29.436 56.786  -33.835 1.00 13.76 ? 118  GLN B C   1 
ATOM   3331 O  O   . GLN B 1 13  ? -29.716 55.829  -34.601 1.00 15.53 ? 118  GLN B O   1 
ATOM   3332 C  CB  . GLN B 1 13  ? -28.853 59.007  -34.802 1.00 18.96 ? 118  GLN B CB  1 
ATOM   3333 C  CG  . GLN B 1 13  ? -28.273 58.371  -36.070 1.00 26.09 ? 118  GLN B CG  1 
ATOM   3334 C  CD  . GLN B 1 13  ? -27.188 59.220  -36.735 1.00 27.04 ? 118  GLN B CD  1 
ATOM   3335 O  OE1 . GLN B 1 13  ? -26.013 59.008  -36.530 1.00 33.21 ? 118  GLN B OE1 1 
ATOM   3336 N  NE2 . GLN B 1 13  ? -27.619 60.223  -37.493 1.00 32.77 ? 118  GLN B NE2 1 
ATOM   3337 N  N   . PHE B 1 14  ? -28.733 56.636  -32.707 1.00 13.48 ? 119  PHE B N   1 
ATOM   3338 C  CA  . PHE B 1 14  ? -28.262 55.273  -32.298 1.00 12.68 ? 119  PHE B CA  1 
ATOM   3339 C  C   . PHE B 1 14  ? -29.365 54.547  -31.484 1.00 11.44 ? 119  PHE B C   1 
ATOM   3340 O  O   . PHE B 1 14  ? -29.790 53.426  -31.821 1.00 11.67 ? 119  PHE B O   1 
ATOM   3341 C  CB  . PHE B 1 14  ? -26.979 55.379  -31.474 1.00 14.74 ? 119  PHE B CB  1 
ATOM   3342 C  CG  . PHE B 1 14  ? -26.615 54.052  -30.859 1.00 12.46 ? 119  PHE B CG  1 
ATOM   3343 C  CD1 . PHE B 1 14  ? -26.349 52.928  -31.677 1.00 12.70 ? 119  PHE B CD1 1 
ATOM   3344 C  CD2 . PHE B 1 14  ? -26.598 53.925  -29.438 1.00 13.34 ? 119  PHE B CD2 1 
ATOM   3345 C  CE1 . PHE B 1 14  ? -26.026 51.662  -31.073 1.00 13.81 ? 119  PHE B CE1 1 
ATOM   3346 C  CE2 . PHE B 1 14  ? -26.263 52.651  -28.892 1.00 13.61 ? 119  PHE B CE2 1 
ATOM   3347 C  CZ  . PHE B 1 14  ? -25.997 51.556  -29.665 1.00 12.75 ? 119  PHE B CZ  1 
ATOM   3348 N  N   . TRP B 1 15  ? -29.836 55.168  -30.421 1.00 11.08 ? 120  TRP B N   1 
ATOM   3349 C  CA  . TRP B 1 15  ? -30.699 54.457  -29.502 1.00 11.49 ? 120  TRP B CA  1 
ATOM   3350 C  C   . TRP B 1 15  ? -31.994 53.970  -30.111 1.00 10.13 ? 120  TRP B C   1 
ATOM   3351 O  O   . TRP B 1 15  ? -32.555 52.963  -29.723 1.00 11.42 ? 120  TRP B O   1 
ATOM   3352 C  CB  . TRP B 1 15  ? -30.916 55.244  -28.193 1.00 10.72 ? 120  TRP B CB  1 
ATOM   3353 C  CG  . TRP B 1 15  ? -29.717 55.062  -27.284 1.00 10.45 ? 120  TRP B CG  1 
ATOM   3354 C  CD1 . TRP B 1 15  ? -28.771 55.981  -26.986 1.00 11.86 ? 120  TRP B CD1 1 
ATOM   3355 C  CD2 . TRP B 1 15  ? -29.352 53.836  -26.628 1.00 9.55  ? 120  TRP B CD2 1 
ATOM   3356 N  NE1 . TRP B 1 15  ? -27.757 55.412  -26.149 1.00 11.07 ? 120  TRP B NE1 1 
ATOM   3357 C  CE2 . TRP B 1 15  ? -28.160 54.114  -25.894 1.00 11.09 ? 120  TRP B CE2 1 
ATOM   3358 C  CE3 . TRP B 1 15  ? -29.964 52.602  -26.532 1.00 9.05  ? 120  TRP B CE3 1 
ATOM   3359 C  CZ2 . TRP B 1 15  ? -27.514 53.118  -25.139 1.00 10.67 ? 120  TRP B CZ2 1 
ATOM   3360 C  CZ3 . TRP B 1 15  ? -29.284 51.601  -25.814 1.00 9.86  ? 120  TRP B CZ3 1 
ATOM   3361 C  CH2 . TRP B 1 15  ? -28.150 51.885  -25.117 1.00 10.24 ? 120  TRP B CH2 1 
ATOM   3362 N  N   . ASP B 1 16  ? -32.535 54.710  -31.115 1.00 11.47 ? 121  ASP B N   1 
ATOM   3363 C  CA  . ASP B 1 16  ? -33.794 54.285  -31.769 1.00 13.47 ? 121  ASP B CA  1 
ATOM   3364 C  C   . ASP B 1 16  ? -33.632 53.013  -32.551 1.00 13.52 ? 121  ASP B C   1 
ATOM   3365 O  O   . ASP B 1 16  ? -34.617 52.298  -32.846 1.00 14.33 ? 121  ASP B O   1 
ATOM   3366 C  CB  . ASP B 1 16  ? -34.251 55.377  -32.794 1.00 15.95 ? 121  ASP B CB  1 
ATOM   3367 C  CG  . ASP B 1 16  ? -34.782 56.671  -32.145 1.00 24.14 ? 121  ASP B CG  1 
ATOM   3368 O  OD1 . ASP B 1 16  ? -35.160 56.688  -30.972 1.00 25.43 ? 121  ASP B OD1 1 
ATOM   3369 O  OD2 . ASP B 1 16  ? -34.768 57.728  -32.907 1.00 27.11 ? 121  ASP B OD2 1 
ATOM   3370 N  N   . THR B 1 17  ? -32.383 52.528  -32.802 1.00 10.95 ? 122  THR B N   1 
ATOM   3371 C  CA  . THR B 1 17  ? -32.162 51.257  -33.493 1.00 12.11 ? 122  THR B CA  1 
ATOM   3372 C  C   . THR B 1 17  ? -32.031 50.102  -32.519 1.00 11.41 ? 122  THR B C   1 
ATOM   3373 O  O   . THR B 1 17  ? -31.900 48.966  -32.933 1.00 13.15 ? 122  THR B O   1 
ATOM   3374 C  CB  . THR B 1 17  ? -30.803 51.250  -34.276 1.00 13.40 ? 122  THR B CB  1 
ATOM   3375 O  OG1 . THR B 1 17  ? -29.643 51.276  -33.381 1.00 13.81 ? 122  THR B OG1 1 
ATOM   3376 C  CG2 . THR B 1 17  ? -30.710 52.472  -35.248 1.00 14.39 ? 122  THR B CG2 1 
ATOM   3377 N  N   . GLN B 1 18  ? -32.078 50.385  -31.219 1.00 11.21 ? 123  GLN B N   1 
ATOM   3378 C  CA  . GLN B 1 18  ? -31.741 49.338  -30.183 1.00 10.53 ? 123  GLN B CA  1 
ATOM   3379 C  C   . GLN B 1 18  ? -32.926 48.717  -29.580 1.00 10.98 ? 123  GLN B C   1 
ATOM   3380 O  O   . GLN B 1 18  ? -34.016 49.350  -29.566 1.00 11.39 ? 123  GLN B O   1 
ATOM   3381 C  CB  . GLN B 1 18  ? -30.820 49.997  -29.102 1.00 11.22 ? 123  GLN B CB  1 
ATOM   3382 C  CG  . GLN B 1 18  ? -29.472 50.495  -29.676 1.00 10.96 ? 123  GLN B CG  1 
ATOM   3383 C  CD  . GLN B 1 18  ? -28.634 49.326  -30.132 1.00 10.36 ? 123  GLN B CD  1 
ATOM   3384 O  OE1 . GLN B 1 18  ? -28.212 48.496  -29.290 1.00 11.76 ? 123  GLN B OE1 1 
ATOM   3385 N  NE2 . GLN B 1 18  ? -28.517 49.139  -31.427 1.00 12.04 ? 123  GLN B NE2 1 
ATOM   3386 N  N   . PRO B 1 19  ? -32.831 47.558  -28.978 1.00 10.28 ? 124  PRO B N   1 
ATOM   3387 C  CA  . PRO B 1 19  ? -33.954 46.829  -28.348 1.00 10.44 ? 124  PRO B CA  1 
ATOM   3388 C  C   . PRO B 1 19  ? -34.248 47.399  -26.955 1.00 10.92 ? 124  PRO B C   1 
ATOM   3389 O  O   . PRO B 1 19  ? -33.964 46.699  -25.897 1.00 11.04 ? 124  PRO B O   1 
ATOM   3390 C  CB  . PRO B 1 19  ? -33.505 45.315  -28.410 1.00 11.21 ? 124  PRO B CB  1 
ATOM   3391 C  CG  . PRO B 1 19  ? -31.986 45.460  -28.193 1.00 11.43 ? 124  PRO B CG  1 
ATOM   3392 C  CD  . PRO B 1 19  ? -31.670 46.629  -29.065 1.00 11.87 ? 124  PRO B CD  1 
ATOM   3393 N  N   . VAL B 1 20  ? -34.762 48.638  -26.920 1.00 10.76 ? 125  VAL B N   1 
ATOM   3394 C  CA  . VAL B 1 20  ? -35.136 49.326  -25.688 1.00 11.42 ? 125  VAL B CA  1 
ATOM   3395 C  C   . VAL B 1 20  ? -36.477 50.041  -26.017 1.00 13.49 ? 125  VAL B C   1 
ATOM   3396 O  O   . VAL B 1 20  ? -36.783 50.314  -27.200 1.00 15.83 ? 125  VAL B O   1 
ATOM   3397 C  CB  . VAL B 1 20  ? -34.078 50.382  -25.264 1.00 11.70 ? 125  VAL B CB  1 
ATOM   3398 C  CG1 . VAL B 1 20  ? -32.756 49.664  -24.847 1.00 13.03 ? 125  VAL B CG1 1 
ATOM   3399 C  CG2 . VAL B 1 20  ? -33.810 51.460  -26.337 1.00 13.37 ? 125  VAL B CG2 1 
ATOM   3400 N  N   . PRO B 1 21  ? -37.279 50.342  -25.008 1.00 12.79 ? 126  PRO B N   1 
ATOM   3401 C  CA  . PRO B 1 21  ? -38.544 51.106  -25.281 1.00 14.49 ? 126  PRO B CA  1 
ATOM   3402 C  C   . PRO B 1 21  ? -38.264 52.474  -25.715 1.00 14.23 ? 126  PRO B C   1 
ATOM   3403 O  O   . PRO B 1 21  ? -37.222 53.060  -25.502 1.00 16.66 ? 126  PRO B O   1 
ATOM   3404 C  CB  . PRO B 1 21  ? -39.257 51.053  -23.906 1.00 15.88 ? 126  PRO B CB  1 
ATOM   3405 C  CG  . PRO B 1 21  ? -38.515 49.955  -23.073 1.00 19.47 ? 126  PRO B CG  1 
ATOM   3406 C  CD  . PRO B 1 21  ? -37.077 49.983  -23.587 1.00 13.93 ? 126  PRO B CD  1 
ATOM   3407 N  N   . LYS B 1 22  ? -39.247 53.052  -26.487 1.00 17.90 ? 127  LYS B N   1 
ATOM   3408 C  CA  . LYS B 1 22  ? -39.126 54.482  -26.843 1.00 18.27 ? 127  LYS B CA  1 
ATOM   3409 C  C   . LYS B 1 22  ? -39.434 55.375  -25.644 1.00 21.09 ? 127  LYS B C   1 
ATOM   3410 O  O   . LYS B 1 22  ? -40.205 54.982  -24.738 1.00 20.43 ? 127  LYS B O   1 
ATOM   3411 C  CB  . LYS B 1 22  ? -40.139 54.831  -28.004 1.00 20.86 ? 127  LYS B CB  1 
ATOM   3412 C  CG  . LYS B 1 22  ? -40.120 53.734  -29.093 1.00 26.17 ? 127  LYS B CG  1 
ATOM   3413 C  CD  . LYS B 1 22  ? -38.882 53.816  -29.962 1.00 29.89 ? 127  LYS B CD  1 
ATOM   3414 C  CE  . LYS B 1 22  ? -38.848 52.676  -30.998 1.00 27.70 ? 127  LYS B CE  1 
ATOM   3415 N  NZ  . LYS B 1 22  ? -37.475 52.408  -31.541 1.00 24.42 ? 127  LYS B NZ  1 
ATOM   3416 N  N   . LEU B 1 23  ? -38.859 56.590  -25.630 1.00 21.59 ? 128  LEU B N   1 
ATOM   3417 C  CA  . LEU B 1 23  ? -39.248 57.586  -24.559 1.00 27.92 ? 128  LEU B CA  1 
ATOM   3418 C  C   . LEU B 1 23  ? -40.742 57.851  -24.626 1.00 29.64 ? 128  LEU B C   1 
ATOM   3419 O  O   . LEU B 1 23  ? -41.336 57.924  -25.705 1.00 31.86 ? 128  LEU B O   1 
ATOM   3420 C  CB  . LEU B 1 23  ? -38.548 58.869  -24.768 1.00 31.60 ? 128  LEU B CB  1 
ATOM   3421 C  CG  . LEU B 1 23  ? -37.187 59.082  -24.221 1.00 30.16 ? 128  LEU B CG  1 
ATOM   3422 C  CD1 . LEU B 1 23  ? -36.982 60.579  -24.431 1.00 29.37 ? 128  LEU B CD1 1 
ATOM   3423 C  CD2 . LEU B 1 23  ? -37.030 58.715  -22.697 1.00 25.75 ? 128  LEU B CD2 1 
ATOM   3424 N  N   . GLY B 1 24  ? -41.403 57.878  -23.496 1.00 39.49 ? 129  GLY B N   1 
ATOM   3425 C  CA  . GLY B 1 24  ? -42.861 58.062  -23.609 1.00 41.66 ? 129  GLY B CA  1 
ATOM   3426 C  C   . GLY B 1 24  ? -43.683 56.948  -24.249 1.00 43.71 ? 129  GLY B C   1 
ATOM   3427 O  O   . GLY B 1 24  ? -44.893 57.063  -24.361 1.00 44.53 ? 129  GLY B O   1 
ATOM   3428 N  N   . GLU B 1 25  ? -43.056 55.861  -24.688 1.00 33.33 ? 130  GLU B N   1 
ATOM   3429 C  CA  . GLU B 1 25  ? -43.780 54.621  -24.673 1.00 34.29 ? 130  GLU B CA  1 
ATOM   3430 C  C   . GLU B 1 25  ? -44.036 54.487  -23.163 1.00 32.28 ? 130  GLU B C   1 
ATOM   3431 O  O   . GLU B 1 25  ? -43.121 54.707  -22.329 1.00 33.98 ? 130  GLU B O   1 
ATOM   3432 C  CB  . GLU B 1 25  ? -42.907 53.470  -25.201 1.00 31.63 ? 130  GLU B CB  1 
ATOM   3433 C  CG  . GLU B 1 25  ? -43.546 52.115  -25.201 1.00 28.40 ? 130  GLU B CG  1 
ATOM   3434 C  CD  . GLU B 1 25  ? -42.691 51.048  -25.878 1.00 26.69 ? 130  GLU B CD  1 
ATOM   3435 O  OE1 . GLU B 1 25  ? -41.682 51.367  -26.544 1.00 26.06 ? 130  GLU B OE1 1 
ATOM   3436 O  OE2 . GLU B 1 25  ? -43.166 49.923  -25.810 1.00 28.65 ? 130  GLU B OE2 1 
ATOM   3437 N  N   . VAL B 1 26  ? -45.266 54.182  -22.779 1.00 27.36 ? 131  VAL B N   1 
ATOM   3438 C  CA  . VAL B 1 26  ? -45.547 53.839  -21.390 1.00 27.99 ? 131  VAL B CA  1 
ATOM   3439 C  C   . VAL B 1 26  ? -45.669 52.344  -21.364 1.00 26.95 ? 131  VAL B C   1 
ATOM   3440 O  O   . VAL B 1 26  ? -46.582 51.744  -21.931 1.00 27.13 ? 131  VAL B O   1 
ATOM   3441 C  CB  . VAL B 1 26  ? -46.805 54.591  -20.779 1.00 25.17 ? 131  VAL B CB  1 
ATOM   3442 C  CG1 . VAL B 1 26  ? -47.049 54.238  -19.277 1.00 26.77 ? 131  VAL B CG1 1 
ATOM   3443 C  CG2 . VAL B 1 26  ? -46.641 56.117  -20.902 1.00 29.31 ? 131  VAL B CG2 1 
ATOM   3444 N  N   . VAL B 1 27  ? -44.673 51.699  -20.756 1.00 25.91 ? 132  VAL B N   1 
ATOM   3445 C  CA  . VAL B 1 27  ? -44.565 50.205  -20.848 1.00 25.46 ? 132  VAL B CA  1 
ATOM   3446 C  C   . VAL B 1 27  ? -45.468 49.493  -19.831 1.00 23.97 ? 132  VAL B C   1 
ATOM   3447 O  O   . VAL B 1 27  ? -45.471 49.827  -18.648 1.00 24.64 ? 132  VAL B O   1 
ATOM   3448 C  CB  . VAL B 1 27  ? -43.120 49.809  -20.677 1.00 21.82 ? 132  VAL B CB  1 
ATOM   3449 C  CG1 . VAL B 1 27  ? -43.031 48.287  -20.623 1.00 21.63 ? 132  VAL B CG1 1 
ATOM   3450 C  CG2 . VAL B 1 27  ? -42.302 50.446  -21.808 1.00 24.64 ? 132  VAL B CG2 1 
ATOM   3451 N  N   . ASN B 1 28  ? -46.220 48.524  -20.246 1.00 22.45 ? 133  ASN B N   1 
ATOM   3452 C  CA  . ASN B 1 28  ? -46.981 47.638  -19.313 1.00 23.62 ? 133  ASN B CA  1 
ATOM   3453 C  C   . ASN B 1 28  ? -46.715 46.151  -19.318 1.00 27.77 ? 133  ASN B C   1 
ATOM   3454 O  O   . ASN B 1 28  ? -47.245 45.404  -18.456 1.00 32.80 ? 133  ASN B O   1 
ATOM   3455 C  CB  . ASN B 1 28  ? -48.486 47.957  -19.298 1.00 32.39 ? 133  ASN B CB  1 
ATOM   3456 C  CG  . ASN B 1 28  ? -48.733 49.377  -18.777 1.00 41.13 ? 133  ASN B CG  1 
ATOM   3457 O  OD1 . ASN B 1 28  ? -48.851 50.323  -19.581 1.00 51.01 ? 133  ASN B OD1 1 
ATOM   3458 N  ND2 . ASN B 1 28  ? -48.708 49.557  -17.440 1.00 45.02 ? 133  ASN B ND2 1 
ATOM   3459 N  N   . THR B 1 29  ? -45.768 45.695  -20.154 1.00 19.10 ? 134  THR B N   1 
ATOM   3460 C  CA  . THR B 1 29  ? -45.516 44.260  -20.255 1.00 17.60 ? 134  THR B CA  1 
ATOM   3461 C  C   . THR B 1 29  ? -44.174 43.941  -19.516 1.00 15.93 ? 134  THR B C   1 
ATOM   3462 O  O   . THR B 1 29  ? -43.579 44.894  -18.967 1.00 16.81 ? 134  THR B O   1 
ATOM   3463 C  CB  . THR B 1 29  ? -45.381 43.930  -21.781 1.00 17.05 ? 134  THR B CB  1 
ATOM   3464 O  OG1 . THR B 1 29  ? -44.522 44.882  -22.377 1.00 19.60 ? 134  THR B OG1 1 
ATOM   3465 C  CG2 . THR B 1 29  ? -46.834 43.958  -22.541 1.00 23.15 ? 134  THR B CG2 1 
ATOM   3466 N  N   . HIS B 1 30  ? -43.780 42.693  -19.550 1.00 15.94 ? 135  HIS B N   1 
ATOM   3467 C  CA  . HIS B 1 30  ? -42.444 42.334  -18.903 1.00 14.36 ? 135  HIS B CA  1 
ATOM   3468 C  C   . HIS B 1 30  ? -41.774 41.246  -19.757 1.00 14.89 ? 135  HIS B C   1 
ATOM   3469 O  O   . HIS B 1 30  ? -42.240 40.084  -19.770 1.00 18.81 ? 135  HIS B O   1 
ATOM   3470 C  CB  . HIS B 1 30  ? -42.629 41.689  -17.517 1.00 16.04 ? 135  HIS B CB  1 
ATOM   3471 C  CG  . HIS B 1 30  ? -43.358 42.547  -16.536 1.00 15.86 ? 135  HIS B CG  1 
ATOM   3472 N  ND1 . HIS B 1 30  ? -44.745 42.681  -16.554 1.00 18.23 ? 135  HIS B ND1 1 
ATOM   3473 C  CD2 . HIS B 1 30  ? -42.931 43.183  -15.417 1.00 15.95 ? 135  HIS B CD2 1 
ATOM   3474 C  CE1 . HIS B 1 30  ? -45.115 43.419  -15.517 1.00 17.20 ? 135  HIS B CE1 1 
ATOM   3475 N  NE2 . HIS B 1 30  ? -44.039 43.794  -14.838 1.00 19.46 ? 135  HIS B NE2 1 
ATOM   3476 N  N   . GLY B 1 31  ? -40.597 41.564  -20.320 1.00 13.84 ? 136  GLY B N   1 
ATOM   3477 C  CA  . GLY B 1 31  ? -39.929 40.510  -21.099 1.00 12.19 ? 136  GLY B CA  1 
ATOM   3478 C  C   . GLY B 1 31  ? -39.004 41.123  -22.147 1.00 10.95 ? 136  GLY B C   1 
ATOM   3479 O  O   . GLY B 1 31  ? -38.857 42.335  -22.255 1.00 11.46 ? 136  GLY B O   1 
ATOM   3480 N  N   . PRO B 1 32  ? -38.319 40.240  -22.897 1.00 11.13 ? 137  PRO B N   1 
ATOM   3481 C  CA  . PRO B 1 32  ? -37.340 40.732  -23.867 1.00 11.56 ? 137  PRO B CA  1 
ATOM   3482 C  C   . PRO B 1 32  ? -37.985 41.523  -24.979 1.00 11.26 ? 137  PRO B C   1 
ATOM   3483 O  O   . PRO B 1 32  ? -39.167 41.327  -25.343 1.00 11.36 ? 137  PRO B O   1 
ATOM   3484 C  CB  . PRO B 1 32  ? -36.675 39.470  -24.411 1.00 14.04 ? 137  PRO B CB  1 
ATOM   3485 C  CG  . PRO B 1 32  ? -37.602 38.344  -24.141 1.00 14.96 ? 137  PRO B CG  1 
ATOM   3486 C  CD  . PRO B 1 32  ? -38.358 38.766  -22.835 1.00 11.86 ? 137  PRO B CD  1 
ATOM   3487 N  N   . VAL B 1 33  ? -37.192 42.420  -25.551 1.00 11.11 ? 138  VAL B N   1 
ATOM   3488 C  CA  . VAL B 1 33  ? -37.645 43.230  -26.739 1.00 11.52 ? 138  VAL B CA  1 
ATOM   3489 C  C   . VAL B 1 33  ? -37.443 42.467  -28.023 1.00 12.60 ? 138  VAL B C   1 
ATOM   3490 O  O   . VAL B 1 33  ? -38.235 42.651  -29.012 1.00 14.67 ? 138  VAL B O   1 
ATOM   3491 C  CB  . VAL B 1 33  ? -36.930 44.600  -26.716 1.00 10.90 ? 138  VAL B CB  1 
ATOM   3492 C  CG1 . VAL B 1 33  ? -37.282 45.427  -27.951 1.00 12.83 ? 138  VAL B CG1 1 
ATOM   3493 C  CG2 . VAL B 1 33  ? -37.285 45.337  -25.399 1.00 13.94 ? 138  VAL B CG2 1 
ATOM   3494 N  N   . GLU B 1 34  ? -36.421 41.625  -28.102 1.00 11.91 ? 139  GLU B N   1 
ATOM   3495 C  CA  . GLU B 1 34  ? -36.076 40.867  -29.346 1.00 12.75 ? 139  GLU B CA  1 
ATOM   3496 C  C   . GLU B 1 34  ? -35.665 39.433  -28.920 1.00 13.98 ? 139  GLU B C   1 
ATOM   3497 O  O   . GLU B 1 34  ? -35.305 39.240  -27.807 1.00 13.89 ? 139  GLU B O   1 
ATOM   3498 C  CB  . GLU B 1 34  ? -35.007 41.607  -30.194 1.00 13.15 ? 139  GLU B CB  1 
ATOM   3499 C  CG  . GLU B 1 34  ? -33.621 41.551  -29.527 1.00 12.88 ? 139  GLU B CG  1 
ATOM   3500 C  CD  . GLU B 1 34  ? -32.572 42.368  -30.314 1.00 14.56 ? 139  GLU B CD  1 
ATOM   3501 O  OE1 . GLU B 1 34  ? -31.407 42.060  -30.093 1.00 15.74 ? 139  GLU B OE1 1 
ATOM   3502 O  OE2 . GLU B 1 34  ? -32.944 43.178  -31.184 1.00 16.89 ? 139  GLU B OE2 1 
ATOM   3503 N  N   . PRO B 1 35  ? -35.723 38.405  -29.915 1.00 14.31 ? 140  PRO B N   1 
ATOM   3504 C  CA  . PRO B 1 35  ? -35.384 37.043  -29.531 1.00 17.64 ? 140  PRO B CA  1 
ATOM   3505 C  C   . PRO B 1 35  ? -33.903 36.862  -29.212 1.00 15.38 ? 140  PRO B C   1 
ATOM   3506 O  O   . PRO B 1 35  ? -33.114 37.630  -29.879 1.00 16.90 ? 140  PRO B O   1 
ATOM   3507 C  CB  . PRO B 1 35  ? -35.676 36.261  -30.828 1.00 17.08 ? 140  PRO B CB  1 
ATOM   3508 C  CG  . PRO B 1 35  ? -35.805 37.215  -31.901 1.00 17.50 ? 140  PRO B CG  1 
ATOM   3509 C  CD  . PRO B 1 35  ? -36.243 38.570  -31.289 1.00 15.72 ? 140  PRO B CD  1 
ATOM   3510 N  N   . ASP B 1 36  ? -33.537 35.921  -28.379 1.00 15.15 ? 141  ASP B N   1 
ATOM   3511 C  CA  . ASP B 1 36  ? -32.068 35.596  -28.098 1.00 16.39 ? 141  ASP B CA  1 
ATOM   3512 C  C   . ASP B 1 36  ? -31.525 35.147  -29.424 1.00 16.97 ? 141  ASP B C   1 
ATOM   3513 O  O   . ASP B 1 36  ? -32.211 34.592  -30.291 1.00 17.87 ? 141  ASP B O   1 
ATOM   3514 C  CB  . ASP B 1 36  ? -31.932 34.511  -27.083 1.00 16.90 ? 141  ASP B CB  1 
ATOM   3515 C  CG  . ASP B 1 36  ? -32.257 34.904  -25.656 1.00 15.60 ? 141  ASP B CG  1 
ATOM   3516 O  OD1 . ASP B 1 36  ? -32.567 36.123  -25.446 1.00 17.11 ? 141  ASP B OD1 1 
ATOM   3517 O  OD2 . ASP B 1 36  ? -32.233 34.017  -24.820 1.00 18.40 ? 141  ASP B OD2 1 
ATOM   3518 N  N   . LYS B 1 37  ? -30.222 35.402  -29.651 1.00 16.05 ? 142  LYS B N   1 
ATOM   3519 C  CA  . LYS B 1 37  ? -29.650 35.182  -30.995 1.00 13.30 ? 142  LYS B CA  1 
ATOM   3520 C  C   . LYS B 1 37  ? -29.038 33.838  -31.195 1.00 15.29 ? 142  LYS B C   1 
ATOM   3521 O  O   . LYS B 1 37  ? -28.226 33.427  -30.399 1.00 17.21 ? 142  LYS B O   1 
ATOM   3522 C  CB  . LYS B 1 37  ? -28.568 36.295  -31.182 1.00 13.32 ? 142  LYS B CB  1 
ATOM   3523 C  CG  . LYS B 1 37  ? -29.189 37.699  -31.227 1.00 14.48 ? 142  LYS B CG  1 
ATOM   3524 C  CD  . LYS B 1 37  ? -28.143 38.813  -31.514 1.00 12.86 ? 142  LYS B CD  1 
ATOM   3525 C  CE  . LYS B 1 37  ? -28.794 40.195  -31.579 1.00 13.46 ? 142  LYS B CE  1 
ATOM   3526 N  NZ  . LYS B 1 37  ? -29.897 40.248  -32.586 1.00 14.86 ? 142  LYS B NZ  1 
ATOM   3527 N  N   . ASP B 1 38  ? -29.529 33.184  -32.227 1.00 14.21 ? 143  ASP B N   1 
ATOM   3528 C  CA  . ASP B 1 38  ? -29.012 31.850  -32.615 1.00 14.92 ? 143  ASP B CA  1 
ATOM   3529 C  C   . ASP B 1 38  ? -27.616 32.007  -33.259 1.00 12.36 ? 143  ASP B C   1 
ATOM   3530 O  O   . ASP B 1 38  ? -26.868 31.015  -33.325 1.00 11.95 ? 143  ASP B O   1 
ATOM   3531 C  CB  . ASP B 1 38  ? -29.991 31.251  -33.698 1.00 17.05 ? 143  ASP B CB  1 
ATOM   3532 C  CG  . ASP B 1 38  ? -31.164 30.489  -33.103 1.00 27.38 ? 143  ASP B CG  1 
ATOM   3533 O  OD1 . ASP B 1 38  ? -31.236 30.259  -31.882 1.00 26.98 ? 143  ASP B OD1 1 
ATOM   3534 O  OD2 . ASP B 1 38  ? -32.062 30.210  -33.891 1.00 30.58 ? 143  ASP B OD2 1 
ATOM   3535 N  N   . ASN B 1 39  ? -27.294 33.193  -33.844 1.00 11.43 ? 144  ASN B N   1 
ATOM   3536 C  CA  . ASN B 1 39  ? -26.033 33.419  -34.536 1.00 10.28 ? 144  ASN B CA  1 
ATOM   3537 C  C   . ASN B 1 39  ? -25.577 34.784  -34.071 1.00 9.21  ? 144  ASN B C   1 
ATOM   3538 O  O   . ASN B 1 39  ? -26.368 35.766  -34.130 1.00 9.65  ? 144  ASN B O   1 
ATOM   3539 C  CB  . ASN B 1 39  ? -26.202 33.487  -36.106 1.00 13.56 ? 144  ASN B CB  1 
ATOM   3540 C  CG  . ASN B 1 39  ? -26.764 32.257  -36.729 1.00 17.31 ? 144  ASN B CG  1 
ATOM   3541 O  OD1 . ASN B 1 39  ? -27.971 31.975  -36.596 1.00 24.75 ? 144  ASN B OD1 1 
ATOM   3542 N  ND2 . ASN B 1 39  ? -25.903 31.492  -37.389 1.00 21.49 ? 144  ASN B ND2 1 
ATOM   3543 N  N   . ILE B 1 40  ? -24.298 34.920  -33.707 1.00 8.63  ? 145  ILE B N   1 
ATOM   3544 C  CA  A ILE B 1 40  ? -23.740 36.191  -33.259 0.50 9.17  ? 145  ILE B CA  1 
ATOM   3545 C  CA  B ILE B 1 40  ? -23.755 36.203  -33.277 0.50 9.20  ? 145  ILE B CA  1 
ATOM   3546 C  C   . ILE B 1 40  ? -22.570 36.608  -34.161 1.00 9.09  ? 145  ILE B C   1 
ATOM   3547 O  O   . ILE B 1 40  ? -21.689 35.770  -34.494 1.00 8.83  ? 145  ILE B O   1 
ATOM   3548 C  CB  A ILE B 1 40  ? -23.247 36.114  -31.759 0.50 9.80  ? 145  ILE B CB  1 
ATOM   3549 C  CB  B ILE B 1 40  ? -23.371 36.174  -31.753 0.50 10.09 ? 145  ILE B CB  1 
ATOM   3550 C  CG1 A ILE B 1 40  ? -24.484 35.850  -30.778 0.50 12.57 ? 145  ILE B CG1 1 
ATOM   3551 C  CG1 B ILE B 1 40  ? -24.736 36.049  -30.878 0.50 12.46 ? 145  ILE B CG1 1 
ATOM   3552 C  CG2 A ILE B 1 40  ? -22.685 37.457  -31.316 0.50 9.53  ? 145  ILE B CG2 1 
ATOM   3553 C  CG2 B ILE B 1 40  ? -22.695 37.465  -31.322 0.50 9.61  ? 145  ILE B CG2 1 
ATOM   3554 C  CD1 A ILE B 1 40  ? -25.085 34.479  -30.813 0.50 14.78 ? 145  ILE B CD1 1 
ATOM   3555 C  CD1 B ILE B 1 40  ? -24.474 35.167  -29.695 0.50 15.38 ? 145  ILE B CD1 1 
ATOM   3556 N  N   . ARG B 1 41  ? -22.599 37.882  -34.584 1.00 9.35  ? 146  ARG B N   1 
ATOM   3557 C  CA  . ARG B 1 41  ? -21.510 38.454  -35.388 1.00 9.70  ? 146  ARG B CA  1 
ATOM   3558 C  C   . ARG B 1 41  ? -20.100 38.118  -34.783 1.00 9.12  ? 146  ARG B C   1 
ATOM   3559 O  O   . ARG B 1 41  ? -19.835 38.492  -33.636 1.00 8.96  ? 146  ARG B O   1 
ATOM   3560 C  CB  . ARG B 1 41  ? -21.744 40.012  -35.356 1.00 10.18 ? 146  ARG B CB  1 
ATOM   3561 C  CG  . ARG B 1 41  ? -20.781 40.759  -36.287 1.00 9.82  ? 146  ARG B CG  1 
ATOM   3562 C  CD  . ARG B 1 41  ? -21.088 42.267  -36.126 1.00 10.89 ? 146  ARG B CD  1 
ATOM   3563 N  NE  . ARG B 1 41  ? -21.095 43.006  -37.380 1.00 15.80 ? 146  ARG B NE  1 
ATOM   3564 C  CZ  . ARG B 1 41  ? -20.071 43.631  -37.901 1.00 13.05 ? 146  ARG B CZ  1 
ATOM   3565 N  NH1 . ARG B 1 41  ? -18.824 43.542  -37.389 1.00 13.09 ? 146  ARG B NH1 1 
ATOM   3566 N  NH2 . ARG B 1 41  ? -20.224 44.319  -38.986 1.00 13.63 ? 146  ARG B NH2 1 
ATOM   3567 N  N   . GLN B 1 42  ? -19.237 37.456  -35.590 1.00 9.26  ? 147  GLN B N   1 
ATOM   3568 C  CA  . GLN B 1 42  ? -17.934 37.112  -35.069 1.00 10.65 ? 147  GLN B CA  1 
ATOM   3569 C  C   . GLN B 1 42  ? -16.929 38.160  -35.147 1.00 11.17 ? 147  GLN B C   1 
ATOM   3570 O  O   . GLN B 1 42  ? -15.891 38.051  -34.433 1.00 13.75 ? 147  GLN B O   1 
ATOM   3571 C  CB  . GLN B 1 42  ? -17.399 35.851  -35.817 1.00 11.33 ? 147  GLN B CB  1 
ATOM   3572 C  CG  . GLN B 1 42  ? -18.341 34.577  -35.627 1.00 11.32 ? 147  GLN B CG  1 
ATOM   3573 C  CD  . GLN B 1 42  ? -17.629 33.373  -36.249 1.00 17.38 ? 147  GLN B CD  1 
ATOM   3574 O  OE1 . GLN B 1 42  ? -17.089 32.585  -35.397 1.00 21.06 ? 147  GLN B OE1 1 
ATOM   3575 N  NE2 . GLN B 1 42  ? -17.612 33.278  -37.543 1.00 16.00 ? 147  GLN B NE2 1 
ATOM   3576 N  N   . GLU B 1 43  ? -17.123 39.132  -36.006 1.00 10.99 ? 148  GLU B N   1 
ATOM   3577 C  CA  . GLU B 1 43  ? -16.095 40.213  -36.264 1.00 12.89 ? 148  GLU B CA  1 
ATOM   3578 C  C   . GLU B 1 43  ? -16.357 41.429  -35.416 1.00 10.79 ? 148  GLU B C   1 
ATOM   3579 O  O   . GLU B 1 43  ? -17.555 41.836  -35.317 1.00 9.85  ? 148  GLU B O   1 
ATOM   3580 C  CB  . GLU B 1 43  ? -16.167 40.649  -37.674 1.00 15.06 ? 148  GLU B CB  1 
ATOM   3581 C  CG  . GLU B 1 43  ? -15.868 39.425  -38.671 1.00 17.45 ? 148  GLU B CG  1 
ATOM   3582 C  CD  . GLU B 1 43  ? -17.143 38.607  -38.934 1.00 20.66 ? 148  GLU B CD  1 
ATOM   3583 O  OE1 . GLU B 1 43  ? -18.286 38.992  -38.610 1.00 15.70 ? 148  GLU B OE1 1 
ATOM   3584 O  OE2 . GLU B 1 43  ? -16.966 37.444  -39.375 1.00 23.17 ? 148  GLU B OE2 1 
ATOM   3585 N  N   . PRO B 1 44  ? -15.316 42.033  -34.879 1.00 10.54 ? 149  PRO B N   1 
ATOM   3586 C  CA  . PRO B 1 44  ? -15.543 43.292  -34.166 1.00 9.77  ? 149  PRO B CA  1 
ATOM   3587 C  C   . PRO B 1 44  ? -16.117 44.389  -35.051 1.00 9.07  ? 149  PRO B C   1 
ATOM   3588 O  O   . PRO B 1 44  ? -15.940 44.425  -36.273 1.00 11.32 ? 149  PRO B O   1 
ATOM   3589 C  CB  . PRO B 1 44  ? -14.096 43.686  -33.704 1.00 11.36 ? 149  PRO B CB  1 
ATOM   3590 C  CG  . PRO B 1 44  ? -13.348 42.337  -33.665 1.00 14.01 ? 149  PRO B CG  1 
ATOM   3591 C  CD  . PRO B 1 44  ? -13.921 41.563  -34.784 1.00 14.27 ? 149  PRO B CD  1 
ATOM   3592 N  N   . TYR B 1 45  ? -16.871 45.309  -34.418 1.00 9.02  ? 150  TYR B N   1 
ATOM   3593 C  CA  . TYR B 1 45  ? -17.283 46.493  -35.173 1.00 8.90  ? 150  TYR B CA  1 
ATOM   3594 C  C   . TYR B 1 45  ? -16.107 47.362  -35.527 1.00 9.74  ? 150  TYR B C   1 
ATOM   3595 O  O   . TYR B 1 45  ? -15.002 47.279  -34.973 1.00 12.02 ? 150  TYR B O   1 
ATOM   3596 C  CB  . TYR B 1 45  ? -18.313 47.284  -34.313 1.00 9.76  ? 150  TYR B CB  1 
ATOM   3597 C  CG  . TYR B 1 45  ? -19.632 46.547  -34.292 1.00 9.32  ? 150  TYR B CG  1 
ATOM   3598 C  CD1 . TYR B 1 45  ? -20.051 45.715  -33.254 1.00 9.14  ? 150  TYR B CD1 1 
ATOM   3599 C  CD2 . TYR B 1 45  ? -20.517 46.732  -35.356 1.00 10.21 ? 150  TYR B CD2 1 
ATOM   3600 C  CE1 . TYR B 1 45  ? -21.303 45.078  -33.293 1.00 10.01 ? 150  TYR B CE1 1 
ATOM   3601 C  CE2 . TYR B 1 45  ? -21.760 46.054  -35.426 1.00 10.64 ? 150  TYR B CE2 1 
ATOM   3602 C  CZ  . TYR B 1 45  ? -22.117 45.227  -34.361 1.00 9.01  ? 150  TYR B CZ  1 
ATOM   3603 O  OH  . TYR B 1 45  ? -23.340 44.569  -34.438 1.00 11.23 ? 150  TYR B OH  1 
ATOM   3604 N  N   . THR B 1 46  ? -16.343 48.167  -36.550 1.00 12.12 ? 151  THR B N   1 
ATOM   3605 C  CA  . THR B 1 46  ? -15.245 49.028  -37.082 1.00 13.02 ? 151  THR B CA  1 
ATOM   3606 C  C   . THR B 1 46  ? -15.245 50.387  -36.445 1.00 12.37 ? 151  THR B C   1 
ATOM   3607 O  O   . THR B 1 46  ? -16.239 51.144  -36.460 1.00 13.97 ? 151  THR B O   1 
ATOM   3608 C  CB  . THR B 1 46  ? -15.409 49.197  -38.576 1.00 14.73 ? 151  THR B CB  1 
ATOM   3609 O  OG1 . THR B 1 46  ? -15.420 47.917  -39.218 1.00 17.50 ? 151  THR B OG1 1 
ATOM   3610 C  CG2 . THR B 1 46  ? -14.201 49.993  -39.135 1.00 18.70 ? 151  THR B CG2 1 
ATOM   3611 N  N   . LEU B 1 47  ? -14.134 50.761  -35.832 1.00 12.41 ? 152  LEU B N   1 
ATOM   3612 C  CA  . LEU B 1 47  ? -13.917 52.136  -35.305 1.00 13.11 ? 152  LEU B CA  1 
ATOM   3613 C  C   . LEU B 1 47  ? -13.564 53.175  -36.393 1.00 12.33 ? 152  LEU B C   1 
ATOM   3614 O  O   . LEU B 1 47  ? -13.099 52.697  -37.420 1.00 14.51 ? 152  LEU B O   1 
ATOM   3615 C  CB  . LEU B 1 47  ? -12.758 52.018  -34.312 1.00 11.72 ? 152  LEU B CB  1 
ATOM   3616 C  CG  . LEU B 1 47  ? -13.233 51.391  -32.966 1.00 11.33 ? 152  LEU B CG  1 
ATOM   3617 C  CD1 . LEU B 1 47  ? -11.954 50.827  -32.273 1.00 12.53 ? 152  LEU B CD1 1 
ATOM   3618 C  CD2 . LEU B 1 47  ? -13.902 52.348  -32.026 1.00 13.22 ? 152  LEU B CD2 1 
ATOM   3619 N  N   . PRO B 1 48  ? -13.731 54.461  -36.104 1.00 12.29 ? 153  PRO B N   1 
ATOM   3620 C  CA  . PRO B 1 48  ? -13.247 55.441  -37.093 1.00 14.01 ? 153  PRO B CA  1 
ATOM   3621 C  C   . PRO B 1 48  ? -11.764 55.208  -37.436 1.00 14.75 ? 153  PRO B C   1 
ATOM   3622 O  O   . PRO B 1 48  ? -10.963 54.652  -36.605 1.00 15.41 ? 153  PRO B O   1 
ATOM   3623 C  CB  . PRO B 1 48  ? -13.463 56.784  -36.368 1.00 15.93 ? 153  PRO B CB  1 
ATOM   3624 C  CG  . PRO B 1 48  ? -14.618 56.556  -35.487 1.00 14.69 ? 153  PRO B CG  1 
ATOM   3625 C  CD  . PRO B 1 48  ? -14.364 55.089  -34.951 1.00 13.09 ? 153  PRO B CD  1 
ATOM   3626 N  N   . GLN B 1 49  ? -11.367 55.586  -38.681 1.00 16.32 ? 154  GLN B N   1 
ATOM   3627 C  CA  A GLN B 1 49  ? -9.966  55.385  -39.140 0.50 16.58 ? 154  GLN B CA  1 
ATOM   3628 C  CA  B GLN B 1 49  ? -9.977  55.359  -39.141 0.50 16.32 ? 154  GLN B CA  1 
ATOM   3629 C  C   . GLN B 1 49  ? -8.954  55.935  -38.125 1.00 13.74 ? 154  GLN B C   1 
ATOM   3630 O  O   . GLN B 1 49  ? -9.121  57.054  -37.643 1.00 17.27 ? 154  GLN B O   1 
ATOM   3631 C  CB  A GLN B 1 49  ? -9.699  56.082  -40.521 0.50 19.57 ? 154  GLN B CB  1 
ATOM   3632 C  CB  B GLN B 1 49  ? -9.761  55.973  -40.574 0.50 18.98 ? 154  GLN B CB  1 
ATOM   3633 C  CG  A GLN B 1 49  ? -8.394  55.620  -41.212 0.50 26.45 ? 154  GLN B CG  1 
ATOM   3634 C  CG  B GLN B 1 49  ? -8.300  56.079  -41.067 0.50 23.99 ? 154  GLN B CG  1 
ATOM   3635 C  CD  A GLN B 1 49  ? -7.129  56.395  -40.808 0.50 27.62 ? 154  GLN B CD  1 
ATOM   3636 C  CD  B GLN B 1 49  ? -7.619  54.726  -41.334 0.50 28.03 ? 154  GLN B CD  1 
ATOM   3637 O  OE1 A GLN B 1 49  ? -5.999  55.919  -40.981 0.50 33.14 ? 154  GLN B OE1 1 
ATOM   3638 O  OE1 B GLN B 1 49  ? -6.397  54.560  -41.140 0.50 32.18 ? 154  GLN B OE1 1 
ATOM   3639 N  NE2 A GLN B 1 49  ? -7.323  57.589  -40.229 0.50 28.39 ? 154  GLN B NE2 1 
ATOM   3640 N  NE2 B GLN B 1 49  ? -8.396  53.754  -41.773 0.50 27.43 ? 154  GLN B NE2 1 
ATOM   3641 N  N   . GLY B 1 50  ? -7.957  55.115  -37.869 1.00 15.79 ? 155  GLY B N   1 
ATOM   3642 C  CA  . GLY B 1 50  ? -6.877  55.543  -36.925 1.00 15.86 ? 155  GLY B CA  1 
ATOM   3643 C  C   . GLY B 1 50  ? -7.033  55.076  -35.488 1.00 11.73 ? 155  GLY B C   1 
ATOM   3644 O  O   . GLY B 1 50  ? -6.231  55.432  -34.666 1.00 12.46 ? 155  GLY B O   1 
ATOM   3645 N  N   . PHE B 1 51  ? -8.148  54.331  -35.197 1.00 12.06 ? 156  PHE B N   1 
ATOM   3646 C  CA  . PHE B 1 51  ? -8.403  53.811  -33.800 1.00 10.53 ? 156  PHE B CA  1 
ATOM   3647 C  C   . PHE B 1 51  ? -8.629  52.326  -33.924 1.00 10.05 ? 156  PHE B C   1 
ATOM   3648 O  O   . PHE B 1 51  ? -8.977  51.760  -34.969 1.00 11.46 ? 156  PHE B O   1 
ATOM   3649 C  CB  . PHE B 1 51  ? -9.653  54.481  -33.217 1.00 11.87 ? 156  PHE B CB  1 
ATOM   3650 C  CG  . PHE B 1 51  ? -9.472  55.987  -33.113 1.00 12.93 ? 156  PHE B CG  1 
ATOM   3651 C  CD1 . PHE B 1 51  ? -10.000 56.797  -34.130 1.00 16.39 ? 156  PHE B CD1 1 
ATOM   3652 C  CD2 . PHE B 1 51  ? -8.693  56.535  -32.161 1.00 12.08 ? 156  PHE B CD2 1 
ATOM   3653 C  CE1 . PHE B 1 51  ? -9.766  58.178  -34.113 1.00 16.73 ? 156  PHE B CE1 1 
ATOM   3654 C  CE2 . PHE B 1 51  ? -8.490  57.900  -32.101 1.00 14.12 ? 156  PHE B CE2 1 
ATOM   3655 C  CZ  . PHE B 1 51  ? -8.997  58.736  -33.087 1.00 15.13 ? 156  PHE B CZ  1 
ATOM   3656 N  N   . THR B 1 52  ? -8.296  51.610  -32.826 1.00 10.38 ? 157  THR B N   1 
ATOM   3657 C  CA  . THR B 1 52  ? -8.371  50.122  -32.832 1.00 10.66 ? 157  THR B CA  1 
ATOM   3658 C  C   . THR B 1 52  ? -8.716  49.620  -31.454 1.00 9.39  ? 157  THR B C   1 
ATOM   3659 O  O   . THR B 1 52  ? -8.486  50.308  -30.450 1.00 9.92  ? 157  THR B O   1 
ATOM   3660 C  CB  . THR B 1 52  ? -6.984  49.532  -33.335 1.00 12.85 ? 157  THR B CB  1 
ATOM   3661 O  OG1 . THR B 1 52  ? -7.193  48.131  -33.480 1.00 16.52 ? 157  THR B OG1 1 
ATOM   3662 C  CG2 . THR B 1 52  ? -5.847  49.820  -32.385 1.00 14.54 ? 157  THR B CG2 1 
ATOM   3663 N  N   . TRP B 1 53  ? -9.314  48.435  -31.383 1.00 9.26  ? 158  TRP B N   1 
ATOM   3664 C  CA  . TRP B 1 53  ? -9.599  47.799  -30.069 1.00 8.69  ? 158  TRP B CA  1 
ATOM   3665 C  C   . TRP B 1 53  ? -8.410  47.276  -29.396 1.00 9.23  ? 158  TRP B C   1 
ATOM   3666 O  O   . TRP B 1 53  ? -7.453  46.780  -30.075 1.00 11.23 ? 158  TRP B O   1 
ATOM   3667 C  CB  . TRP B 1 53  ? -10.534 46.580  -30.316 1.00 9.37  ? 158  TRP B CB  1 
ATOM   3668 C  CG  . TRP B 1 53  ? -11.827 46.916  -31.041 1.00 8.68  ? 158  TRP B CG  1 
ATOM   3669 C  CD1 . TRP B 1 53  ? -12.167 46.564  -32.317 1.00 9.42  ? 158  TRP B CD1 1 
ATOM   3670 C  CD2 . TRP B 1 53  ? -12.903 47.759  -30.530 1.00 8.16  ? 158  TRP B CD2 1 
ATOM   3671 N  NE1 . TRP B 1 53  ? -13.424 47.107  -32.650 1.00 9.88  ? 158  TRP B NE1 1 
ATOM   3672 C  CE2 . TRP B 1 53  ? -13.877 47.820  -31.548 1.00 8.66  ? 158  TRP B CE2 1 
ATOM   3673 C  CE3 . TRP B 1 53  ? -13.128 48.416  -29.308 1.00 8.85  ? 158  TRP B CE3 1 
ATOM   3674 C  CZ2 . TRP B 1 53  ? -15.075 48.590  -31.423 1.00 8.91  ? 158  TRP B CZ2 1 
ATOM   3675 C  CZ3 . TRP B 1 53  ? -14.293 49.176  -29.163 1.00 8.95  ? 158  TRP B CZ3 1 
ATOM   3676 C  CH2 . TRP B 1 53  ? -15.257 49.231  -30.238 1.00 9.15  ? 158  TRP B CH2 1 
ATOM   3677 N  N   . ASP B 1 54  ? -8.430  47.265  -28.093 1.00 9.65  ? 159  ASP B N   1 
ATOM   3678 C  CA  . ASP B 1 54  ? -7.377  46.538  -27.296 1.00 9.65  ? 159  ASP B CA  1 
ATOM   3679 C  C   . ASP B 1 54  ? -8.047  46.160  -25.967 1.00 10.71 ? 159  ASP B C   1 
ATOM   3680 O  O   . ASP B 1 54  ? -8.491  47.056  -25.223 1.00 10.84 ? 159  ASP B O   1 
ATOM   3681 C  CB  . ASP B 1 54  ? -6.169  47.392  -27.016 1.00 11.48 ? 159  ASP B CB  1 
ATOM   3682 C  CG  . ASP B 1 54  ? -4.991  46.561  -26.485 1.00 13.77 ? 159  ASP B CG  1 
ATOM   3683 O  OD1 . ASP B 1 54  ? -4.958  45.351  -26.696 1.00 17.66 ? 159  ASP B OD1 1 
ATOM   3684 O  OD2 . ASP B 1 54  ? -4.087  47.125  -25.850 1.00 13.80 ? 159  ASP B OD2 1 
ATOM   3685 N  N   . ALA B 1 55  ? -8.131  44.863  -25.650 1.00 10.76 ? 160  ALA B N   1 
ATOM   3686 C  CA  . ALA B 1 55  ? -8.636  44.454  -24.334 1.00 11.41 ? 160  ALA B CA  1 
ATOM   3687 C  C   . ALA B 1 55  ? -7.580  44.764  -23.276 1.00 13.32 ? 160  ALA B C   1 
ATOM   3688 O  O   . ALA B 1 55  ? -6.324  44.552  -23.486 1.00 14.54 ? 160  ALA B O   1 
ATOM   3689 C  CB  . ALA B 1 55  ? -8.891  42.982  -24.356 1.00 12.60 ? 160  ALA B CB  1 
ATOM   3690 N  N   . LEU B 1 56  ? -7.937  45.382  -22.177 1.00 10.52 ? 161  LEU B N   1 
ATOM   3691 C  CA  . LEU B 1 56  ? -6.984  45.896  -21.200 1.00 10.70 ? 161  LEU B CA  1 
ATOM   3692 C  C   . LEU B 1 56  ? -6.826  44.862  -20.086 1.00 11.72 ? 161  LEU B C   1 
ATOM   3693 O  O   . LEU B 1 56  ? -7.776  44.531  -19.347 1.00 11.36 ? 161  LEU B O   1 
ATOM   3694 C  CB  . LEU B 1 56  ? -7.493  47.231  -20.586 1.00 10.76 ? 161  LEU B CB  1 
ATOM   3695 C  CG  . LEU B 1 56  ? -7.699  48.378  -21.612 1.00 10.63 ? 161  LEU B CG  1 
ATOM   3696 C  CD1 . LEU B 1 56  ? -7.906  49.650  -20.853 1.00 10.32 ? 161  LEU B CD1 1 
ATOM   3697 C  CD2 . LEU B 1 56  ? -6.548  48.523  -22.655 1.00 11.97 ? 161  LEU B CD2 1 
ATOM   3698 N  N   . ASP B 1 57  ? -5.597  44.345  -19.930 1.00 12.10 ? 162  ASP B N   1 
ATOM   3699 C  CA  . ASP B 1 57  ? -5.278  43.465  -18.769 1.00 13.56 ? 162  ASP B CA  1 
ATOM   3700 C  C   . ASP B 1 57  ? -4.961  44.255  -17.572 1.00 12.52 ? 162  ASP B C   1 
ATOM   3701 O  O   . ASP B 1 57  ? -3.855  44.880  -17.441 1.00 12.95 ? 162  ASP B O   1 
ATOM   3702 C  CB  . ASP B 1 57  ? -4.024  42.624  -19.169 1.00 13.48 ? 162  ASP B CB  1 
ATOM   3703 C  CG  . ASP B 1 57  ? -3.635  41.653  -18.055 1.00 16.67 ? 162  ASP B CG  1 
ATOM   3704 O  OD1 . ASP B 1 57  ? -4.237  41.595  -16.991 1.00 15.04 ? 162  ASP B OD1 1 
ATOM   3705 O  OD2 . ASP B 1 57  ? -2.630  40.873  -18.315 1.00 21.10 ? 162  ASP B OD2 1 
ATOM   3706 N  N   . LEU B 1 58  ? -5.936  44.400  -16.691 1.00 12.05 ? 163  LEU B N   1 
ATOM   3707 C  CA  . LEU B 1 58  ? -5.784  45.247  -15.521 1.00 12.80 ? 163  LEU B CA  1 
ATOM   3708 C  C   . LEU B 1 58  ? -4.862  44.688  -14.408 1.00 13.09 ? 163  LEU B C   1 
ATOM   3709 O  O   . LEU B 1 58  ? -4.490  45.446  -13.520 1.00 13.48 ? 163  LEU B O   1 
ATOM   3710 C  CB  . LEU B 1 58  ? -7.196  45.629  -14.901 1.00 12.96 ? 163  LEU B CB  1 
ATOM   3711 C  CG  . LEU B 1 58  ? -8.144  46.269  -15.966 1.00 13.47 ? 163  LEU B CG  1 
ATOM   3712 C  CD1 . LEU B 1 58  ? -9.468  46.528  -15.208 1.00 14.68 ? 163  LEU B CD1 1 
ATOM   3713 C  CD2 . LEU B 1 58  ? -7.538  47.482  -16.635 1.00 14.14 ? 163  LEU B CD2 1 
ATOM   3714 N  N   . GLY B 1 59  ? -4.464  43.450  -14.642 1.00 13.37 ? 164  GLY B N   1 
ATOM   3715 C  CA  . GLY B 1 59  ? -3.386  42.792  -13.821 1.00 14.34 ? 164  GLY B CA  1 
ATOM   3716 C  C   . GLY B 1 59  ? -2.029  43.289  -14.279 1.00 18.90 ? 164  GLY B C   1 
ATOM   3717 O  O   . GLY B 1 59  ? -1.044  42.993  -13.540 1.00 21.21 ? 164  GLY B O   1 
ATOM   3718 N  N   . ASP B 1 60  ? -1.884  43.952  -15.442 1.00 14.99 ? 165  ASP B N   1 
ATOM   3719 C  CA  . ASP B 1 60  ? -0.631  44.527  -15.901 1.00 16.89 ? 165  ASP B CA  1 
ATOM   3720 C  C   . ASP B 1 60  ? -0.662  45.969  -15.295 1.00 18.04 ? 165  ASP B C   1 
ATOM   3721 O  O   . ASP B 1 60  ? -1.523  46.860  -15.682 1.00 16.05 ? 165  ASP B O   1 
ATOM   3722 C  CB  . ASP B 1 60  ? -0.597  44.466  -17.431 1.00 16.23 ? 165  ASP B CB  1 
ATOM   3723 C  CG  . ASP B 1 60  ? 0.613   45.181  -18.017 1.00 18.73 ? 165  ASP B CG  1 
ATOM   3724 O  OD1 . ASP B 1 60  ? 0.929   44.862  -19.151 1.00 23.77 ? 165  ASP B OD1 1 
ATOM   3725 O  OD2 . ASP B 1 60  ? 1.047   46.152  -17.514 1.00 18.50 ? 165  ASP B OD2 1 
ATOM   3726 N  N   . ARG B 1 61  ? 0.192   46.294  -14.331 1.00 18.00 ? 166  ARG B N   1 
ATOM   3727 C  CA  . ARG B 1 61  ? 0.171   47.498  -13.636 1.00 17.33 ? 166  ARG B CA  1 
ATOM   3728 C  C   . ARG B 1 61  ? 0.235   48.749  -14.564 1.00 15.54 ? 166  ARG B C   1 
ATOM   3729 O  O   . ARG B 1 61  ? -0.464  49.753  -14.320 1.00 15.82 ? 166  ARG B O   1 
ATOM   3730 C  CB  . ARG B 1 61  ? 1.399   47.546  -12.676 1.00 22.02 ? 166  ARG B CB  1 
ATOM   3731 C  CG  . ARG B 1 61  ? 1.478   48.818  -11.896 1.00 20.72 ? 166  ARG B CG  1 
ATOM   3732 C  CD  . ARG B 1 61  ? 0.308   48.975  -10.955 1.00 23.98 ? 166  ARG B CD  1 
ATOM   3733 N  NE  . ARG B 1 61  ? 0.427   50.254  -10.194 1.00 24.42 ? 166  ARG B NE  1 
ATOM   3734 C  CZ  . ARG B 1 61  ? -0.430  50.694  -9.255  1.00 27.90 ? 166  ARG B CZ  1 
ATOM   3735 N  NH1 . ARG B 1 61  ? -1.528  49.990  -8.877  1.00 24.11 ? 166  ARG B NH1 1 
ATOM   3736 N  NH2 . ARG B 1 61  ? -0.155  51.833  -8.645  1.00 32.74 ? 166  ARG B NH2 1 
ATOM   3737 N  N   . GLY B 1 62  ? 1.091   48.738  -15.595 1.00 15.88 ? 167  GLY B N   1 
ATOM   3738 C  CA  . GLY B 1 62  ? 1.212   49.890  -16.500 1.00 14.28 ? 167  GLY B CA  1 
ATOM   3739 C  C   . GLY B 1 62  ? -0.139  50.094  -17.274 1.00 13.50 ? 167  GLY B C   1 
ATOM   3740 O  O   . GLY B 1 62  ? -0.528  51.256  -17.438 1.00 13.77 ? 167  GLY B O   1 
ATOM   3741 N  N   . VAL B 1 63  ? -0.835  49.010  -17.597 1.00 13.05 ? 168  VAL B N   1 
ATOM   3742 C  CA  . VAL B 1 63  ? -2.162  49.162  -18.349 1.00 11.96 ? 168  VAL B CA  1 
ATOM   3743 C  C   . VAL B 1 63  ? -3.193  49.692  -17.341 1.00 12.51 ? 168  VAL B C   1 
ATOM   3744 O  O   . VAL B 1 63  ? -3.983  50.600  -17.726 1.00 12.39 ? 168  VAL B O   1 
ATOM   3745 C  CB  . VAL B 1 63  ? -2.553  47.811  -18.932 1.00 12.72 ? 168  VAL B CB  1 
ATOM   3746 C  CG1 . VAL B 1 63  ? -3.965  47.930  -19.584 1.00 12.80 ? 168  VAL B CG1 1 
ATOM   3747 C  CG2 . VAL B 1 63  ? -1.524  47.396  -20.050 1.00 14.63 ? 168  VAL B CG2 1 
ATOM   3748 N  N   . LEU B 1 64  ? -3.213  49.201  -16.112 1.00 11.62 ? 169  LEU B N   1 
ATOM   3749 C  CA  . LEU B 1 64  ? -4.147  49.768  -15.145 1.00 12.36 ? 169  LEU B CA  1 
ATOM   3750 C  C   . LEU B 1 64  ? -3.875  51.228  -14.976 1.00 13.12 ? 169  LEU B C   1 
ATOM   3751 O  O   . LEU B 1 64  ? -4.830  52.040  -14.862 1.00 12.04 ? 169  LEU B O   1 
ATOM   3752 C  CB  . LEU B 1 64  ? -4.011  48.992  -13.820 1.00 12.74 ? 169  LEU B CB  1 
ATOM   3753 C  CG  . LEU B 1 64  ? -4.880  49.523  -12.663 1.00 12.43 ? 169  LEU B CG  1 
ATOM   3754 C  CD1 . LEU B 1 64  ? -6.411  49.439  -13.009 1.00 14.11 ? 169  LEU B CD1 1 
ATOM   3755 C  CD2 . LEU B 1 64  ? -4.536  48.646  -11.395 1.00 13.87 ? 169  LEU B CD2 1 
ATOM   3756 N  N   . LYS B 1 65  ? -2.641  51.683  -14.890 1.00 12.96 ? 170  LYS B N   1 
ATOM   3757 C  CA  . LYS B 1 65  ? -2.364  53.094  -14.758 1.00 13.74 ? 170  LYS B CA  1 
ATOM   3758 C  C   . LYS B 1 65  ? -2.762  53.896  -15.999 1.00 12.29 ? 170  LYS B C   1 
ATOM   3759 O  O   . LYS B 1 65  ? -3.261  55.016  -15.835 1.00 12.27 ? 170  LYS B O   1 
ATOM   3760 C  CB  . LYS B 1 65  ? -0.858  53.337  -14.486 1.00 15.75 ? 170  LYS B CB  1 
ATOM   3761 C  CG  . LYS B 1 65  ? -0.363  52.907  -13.080 1.00 22.00 ? 170  LYS B CG  1 
ATOM   3762 C  CD  . LYS B 1 65  ? -1.204  53.483  -11.910 1.00 25.25 ? 170  LYS B CD  1 
ATOM   3763 C  CE  . LYS B 1 65  ? -1.310  55.035  -11.836 1.00 28.05 ? 170  LYS B CE  1 
ATOM   3764 N  NZ  . LYS B 1 65  ? 0.105   55.512  -11.483 1.00 29.22 ? 170  LYS B NZ  1 
ATOM   3765 N  N   . GLU B 1 66  ? -2.696  53.285  -17.198 1.00 11.67 ? 171  GLU B N   1 
ATOM   3766 C  CA  . GLU B 1 66  ? -3.215  53.974  -18.403 1.00 11.92 ? 171  GLU B CA  1 
ATOM   3767 C  C   . GLU B 1 66  ? -4.762  54.218  -18.295 1.00 11.18 ? 171  GLU B C   1 
ATOM   3768 O  O   . GLU B 1 66  ? -5.252  55.281  -18.657 1.00 11.80 ? 171  GLU B O   1 
ATOM   3769 C  CB  . GLU B 1 66  ? -2.973  53.216  -19.655 1.00 12.20 ? 171  GLU B CB  1 
ATOM   3770 C  CG  . GLU B 1 66  ? -1.465  53.204  -20.091 1.00 13.36 ? 171  GLU B CG  1 
ATOM   3771 C  CD  . GLU B 1 66  ? -1.362  52.444  -21.402 1.00 12.52 ? 171  GLU B CD  1 
ATOM   3772 O  OE1 . GLU B 1 66  ? -1.261  51.188  -21.409 1.00 14.22 ? 171  GLU B OE1 1 
ATOM   3773 O  OE2 . GLU B 1 66  ? -1.493  53.133  -22.476 1.00 13.43 ? 171  GLU B OE2 1 
ATOM   3774 N  N   . LEU B 1 67  ? -5.463  53.193  -17.804 1.00 10.82 ? 172  LEU B N   1 
ATOM   3775 C  CA  . LEU B 1 67  ? -6.916  53.368  -17.575 1.00 11.43 ? 172  LEU B CA  1 
ATOM   3776 C  C   . LEU B 1 67  ? -7.200  54.394  -16.498 1.00 10.94 ? 172  LEU B C   1 
ATOM   3777 O  O   . LEU B 1 67  ? -8.064  55.274  -16.673 1.00 10.45 ? 172  LEU B O   1 
ATOM   3778 C  CB  . LEU B 1 67  ? -7.604  52.019  -17.243 1.00 9.57  ? 172  LEU B CB  1 
ATOM   3779 C  CG  . LEU B 1 67  ? -9.127  52.164  -16.927 1.00 9.81  ? 172  LEU B CG  1 
ATOM   3780 C  CD1 . LEU B 1 67  ? -9.904  52.569  -18.193 1.00 10.97 ? 172  LEU B CD1 1 
ATOM   3781 C  CD2 . LEU B 1 67  ? -9.655  50.775  -16.437 1.00 10.82 ? 172  LEU B CD2 1 
ATOM   3782 N  N   . TYR B 1 68  ? -6.481  54.337  -15.340 1.00 10.37 ? 173  TYR B N   1 
ATOM   3783 C  CA  . TYR B 1 68  ? -6.631  55.356  -14.330 1.00 11.22 ? 173  TYR B CA  1 
ATOM   3784 C  C   . TYR B 1 68  ? -6.431  56.775  -14.897 1.00 11.53 ? 173  TYR B C   1 
ATOM   3785 O  O   . TYR B 1 68  ? -7.244  57.681  -14.605 1.00 10.85 ? 173  TYR B O   1 
ATOM   3786 C  CB  . TYR B 1 68  ? -5.500  55.066  -13.208 1.00 12.29 ? 173  TYR B CB  1 
ATOM   3787 C  CG  . TYR B 1 68  ? -5.310  56.285  -12.393 1.00 12.48 ? 173  TYR B CG  1 
ATOM   3788 C  CD1 . TYR B 1 68  ? -6.213  56.569  -11.312 1.00 13.15 ? 173  TYR B CD1 1 
ATOM   3789 C  CD2 . TYR B 1 68  ? -4.345  57.244  -12.685 1.00 13.86 ? 173  TYR B CD2 1 
ATOM   3790 C  CE1 . TYR B 1 68  ? -6.121  57.757  -10.554 1.00 14.08 ? 173  TYR B CE1 1 
ATOM   3791 C  CE2 . TYR B 1 68  ? -4.289  58.422  -11.937 1.00 14.93 ? 173  TYR B CE2 1 
ATOM   3792 C  CZ  . TYR B 1 68  ? -5.154  58.673  -10.905 1.00 15.34 ? 173  TYR B CZ  1 
ATOM   3793 O  OH  . TYR B 1 68  ? -5.134  59.859  -10.142 1.00 21.54 ? 173  TYR B OH  1 
ATOM   3794 N  N   . THR B 1 69  ? -5.417  56.959  -15.783 1.00 12.71 ? 174  THR B N   1 
ATOM   3795 C  CA  . THR B 1 69  ? -5.172  58.279  -16.365 1.00 12.72 ? 174  THR B CA  1 
ATOM   3796 C  C   . THR B 1 69  ? -6.289  58.709  -17.290 1.00 10.83 ? 174  THR B C   1 
ATOM   3797 O  O   . THR B 1 69  ? -6.761  59.854  -17.270 1.00 11.69 ? 174  THR B O   1 
ATOM   3798 C  CB  . THR B 1 69  ? -3.809  58.279  -17.075 1.00 13.50 ? 174  THR B CB  1 
ATOM   3799 O  OG1 . THR B 1 69  ? -2.828  57.999  -16.031 1.00 14.43 ? 174  THR B OG1 1 
ATOM   3800 C  CG2 . THR B 1 69  ? -3.522  59.659  -17.741 1.00 13.76 ? 174  THR B CG2 1 
ATOM   3801 N  N   . LEU B 1 70  ? -6.741  57.750  -18.176 1.00 10.56 ? 175  LEU B N   1 
ATOM   3802 C  CA  . LEU B 1 70  ? -7.856  58.108  -19.087 1.00 10.33 ? 175  LEU B CA  1 
ATOM   3803 C  C   . LEU B 1 70  ? -9.072  58.610  -18.262 1.00 9.41  ? 175  LEU B C   1 
ATOM   3804 O  O   . LEU B 1 70  ? -9.695  59.664  -18.624 1.00 10.24 ? 175  LEU B O   1 
ATOM   3805 C  CB  . LEU B 1 70  ? -8.288  56.871  -19.861 1.00 10.34 ? 175  LEU B CB  1 
ATOM   3806 C  CG  . LEU B 1 70  ? -9.574  57.135  -20.757 1.00 9.32  ? 175  LEU B CG  1 
ATOM   3807 C  CD1 . LEU B 1 70  ? -9.279  58.021  -21.987 1.00 11.29 ? 175  LEU B CD1 1 
ATOM   3808 C  CD2 . LEU B 1 70  ? -10.108 55.763  -21.192 1.00 10.04 ? 175  LEU B CD2 1 
ATOM   3809 N  N   . LEU B 1 71  ? -9.424  57.883  -17.192 1.00 9.61  ? 176  LEU B N   1 
ATOM   3810 C  CA  . LEU B 1 71  ? -10.634 58.269  -16.413 1.00 9.90  ? 176  LEU B CA  1 
ATOM   3811 C  C   . LEU B 1 71  ? -10.391 59.515  -15.610 1.00 9.91  ? 176  LEU B C   1 
ATOM   3812 O  O   . LEU B 1 71  ? -11.282 60.410  -15.522 1.00 10.02 ? 176  LEU B O   1 
ATOM   3813 C  CB  . LEU B 1 71  ? -11.077 57.096  -15.507 1.00 10.15 ? 176  LEU B CB  1 
ATOM   3814 C  CG  . LEU B 1 71  ? -11.445 55.779  -16.270 1.00 10.58 ? 176  LEU B CG  1 
ATOM   3815 C  CD1 . LEU B 1 71  ? -11.787 54.675  -15.273 1.00 10.73 ? 176  LEU B CD1 1 
ATOM   3816 C  CD2 . LEU B 1 71  ? -12.669 55.987  -17.214 1.00 11.74 ? 176  LEU B CD2 1 
ATOM   3817 N  N   . ASN B 1 72  ? -9.190  59.612  -15.013 1.00 10.29 ? 177  ASN B N   1 
ATOM   3818 C  CA  . ASN B 1 72  ? -8.898  60.815  -14.190 1.00 11.37 ? 177  ASN B CA  1 
ATOM   3819 C  C   . ASN B 1 72  ? -9.013  62.101  -15.048 1.00 11.57 ? 177  ASN B C   1 
ATOM   3820 O  O   . ASN B 1 72  ? -9.456  63.101  -14.522 1.00 12.01 ? 177  ASN B O   1 
ATOM   3821 C  CB  . ASN B 1 72  ? -7.467  60.669  -13.588 1.00 11.92 ? 177  ASN B CB  1 
ATOM   3822 C  CG  . ASN B 1 72  ? -6.960  61.962  -13.000 1.00 13.21 ? 177  ASN B CG  1 
ATOM   3823 O  OD1 . ASN B 1 72  ? -6.504  62.814  -13.744 1.00 15.20 ? 177  ASN B OD1 1 
ATOM   3824 N  ND2 . ASN B 1 72  ? -7.050  62.101  -11.690 1.00 14.67 ? 177  ASN B ND2 1 
ATOM   3825 N  N   . GLU B 1 73  ? -8.630  61.997  -16.318 1.00 11.23 ? 178  GLU B N   1 
ATOM   3826 C  CA  . GLU B 1 73  ? -8.603  63.174  -17.164 1.00 11.90 ? 178  GLU B CA  1 
ATOM   3827 C  C   . GLU B 1 73  ? -9.887  63.365  -17.927 1.00 10.78 ? 178  GLU B C   1 
ATOM   3828 O  O   . GLU B 1 73  ? -10.173 64.514  -18.403 1.00 12.20 ? 178  GLU B O   1 
ATOM   3829 C  CB  . GLU B 1 73  ? -7.388  63.072  -18.127 1.00 12.35 ? 178  GLU B CB  1 
ATOM   3830 C  CG  . GLU B 1 73  ? -6.092  63.200  -17.297 1.00 14.34 ? 178  GLU B CG  1 
ATOM   3831 C  CD  . GLU B 1 73  ? -4.774  63.096  -18.147 1.00 16.05 ? 178  GLU B CD  1 
ATOM   3832 O  OE1 . GLU B 1 73  ? -4.816  62.673  -19.311 1.00 17.49 ? 178  GLU B OE1 1 
ATOM   3833 O  OE2 . GLU B 1 73  ? -3.719  63.216  -17.463 1.00 19.95 ? 178  GLU B OE2 1 
ATOM   3834 N  N   . ASN B 1 74  ? -10.741 62.297  -18.140 1.00 10.63 ? 179  ASN B N   1 
ATOM   3835 C  CA  . ASN B 1 74  ? -11.796 62.398  -19.137 1.00 10.06 ? 179  ASN B CA  1 
ATOM   3836 C  C   . ASN B 1 74  ? -13.119 61.800  -18.702 1.00 9.75  ? 179  ASN B C   1 
ATOM   3837 O  O   . ASN B 1 74  ? -14.048 61.744  -19.500 1.00 10.74 ? 179  ASN B O   1 
ATOM   3838 C  CB  . ASN B 1 74  ? -11.386 61.621  -20.426 1.00 10.40 ? 179  ASN B CB  1 
ATOM   3839 C  CG  . ASN B 1 74  ? -10.061 62.159  -21.002 1.00 9.72  ? 179  ASN B CG  1 
ATOM   3840 O  OD1 . ASN B 1 74  ? -10.070 63.207  -21.742 1.00 12.62 ? 179  ASN B OD1 1 
ATOM   3841 N  ND2 . ASN B 1 74  ? -8.962  61.451  -20.729 1.00 11.67 ? 179  ASN B ND2 1 
ATOM   3842 N  N   . TYR B 1 75  ? -13.248 61.396  -17.417 1.00 9.84  ? 180  TYR B N   1 
ATOM   3843 C  CA  . TYR B 1 75  ? -14.516 60.737  -16.995 1.00 10.33 ? 180  TYR B CA  1 
ATOM   3844 C  C   . TYR B 1 75  ? -15.564 61.724  -16.475 1.00 9.97  ? 180  TYR B C   1 
ATOM   3845 O  O   . TYR B 1 75  ? -15.495 62.925  -16.818 1.00 11.22 ? 180  TYR B O   1 
ATOM   3846 C  CB  . TYR B 1 75  ? -14.170 59.584  -16.029 1.00 10.72 ? 180  TYR B CB  1 
ATOM   3847 C  CG  . TYR B 1 75  ? -15.313 58.533  -15.896 1.00 8.94  ? 180  TYR B CG  1 
ATOM   3848 C  CD1 . TYR B 1 75  ? -15.845 57.923  -17.056 1.00 9.14  ? 180  TYR B CD1 1 
ATOM   3849 C  CD2 . TYR B 1 75  ? -15.730 58.103  -14.644 1.00 9.65  ? 180  TYR B CD2 1 
ATOM   3850 C  CE1 . TYR B 1 75  ? -16.875 56.954  -16.938 1.00 9.72  ? 180  TYR B CE1 1 
ATOM   3851 C  CE2 . TYR B 1 75  ? -16.759 57.101  -14.511 1.00 10.04 ? 180  TYR B CE2 1 
ATOM   3852 C  CZ  . TYR B 1 75  ? -17.278 56.538  -15.662 1.00 10.03 ? 180  TYR B CZ  1 
ATOM   3853 O  OH  . TYR B 1 75  ? -18.292 55.600  -15.524 1.00 10.32 ? 180  TYR B OH  1 
ATOM   3854 N  N   . VAL B 1 76  ? -16.506 61.258  -15.645 1.00 10.81 ? 181  VAL B N   1 
ATOM   3855 C  CA  . VAL B 1 76  ? -17.763 62.041  -15.325 1.00 11.04 ? 181  VAL B CA  1 
ATOM   3856 C  C   . VAL B 1 76  ? -17.369 63.273  -14.491 1.00 10.64 ? 181  VAL B C   1 
ATOM   3857 O  O   . VAL B 1 76  ? -16.628 63.180  -13.483 1.00 11.43 ? 181  VAL B O   1 
ATOM   3858 C  CB  . VAL B 1 76  ? -18.700 61.090  -14.547 1.00 10.25 ? 181  VAL B CB  1 
ATOM   3859 C  CG1 . VAL B 1 76  ? -19.957 61.913  -14.019 1.00 12.98 ? 181  VAL B CG1 1 
ATOM   3860 C  CG2 . VAL B 1 76  ? -19.099 59.856  -15.392 1.00 12.54 ? 181  VAL B CG2 1 
ATOM   3861 N  N   . GLU B 1 77  ? -17.973 64.399  -14.901 1.00 11.84 ? 182  GLU B N   1 
ATOM   3862 C  CA  . GLU B 1 77  ? -17.940 65.685  -14.119 1.00 11.76 ? 182  GLU B CA  1 
ATOM   3863 C  C   . GLU B 1 77  ? -19.332 65.972  -13.585 1.00 12.75 ? 182  GLU B C   1 
ATOM   3864 O  O   . GLU B 1 77  ? -20.331 65.493  -14.131 1.00 12.91 ? 182  GLU B O   1 
ATOM   3865 C  CB  . GLU B 1 77  ? -17.480 66.817  -15.068 1.00 12.77 ? 182  GLU B CB  1 
ATOM   3866 C  CG  . GLU B 1 77  ? -16.068 66.538  -15.588 1.00 14.53 ? 182  GLU B CG  1 
ATOM   3867 C  CD  . GLU B 1 77  ? -15.536 67.500  -16.646 1.00 14.05 ? 182  GLU B CD  1 
ATOM   3868 O  OE1 . GLU B 1 77  ? -14.316 67.327  -17.024 1.00 14.72 ? 182  GLU B OE1 1 
ATOM   3869 O  OE2 . GLU B 1 77  ? -16.346 68.430  -17.013 1.00 15.75 ? 182  GLU B OE2 1 
ATOM   3870 N  N   . ASP B 1 78  ? -19.387 66.784  -12.536 1.00 12.80 ? 183  ASP B N   1 
ATOM   3871 C  CA  . ASP B 1 78  ? -20.724 67.230  -12.005 1.00 13.44 ? 183  ASP B CA  1 
ATOM   3872 C  C   . ASP B 1 78  ? -21.332 68.232  -13.025 1.00 13.99 ? 183  ASP B C   1 
ATOM   3873 O  O   . ASP B 1 78  ? -20.715 68.668  -14.045 1.00 13.70 ? 183  ASP B O   1 
ATOM   3874 C  CB  . ASP B 1 78  ? -20.611 67.902  -10.606 1.00 14.52 ? 183  ASP B CB  1 
ATOM   3875 C  CG  . ASP B 1 78  ? -19.898 69.179  -10.686 1.00 18.66 ? 183  ASP B CG  1 
ATOM   3876 O  OD1 . ASP B 1 78  ? -18.904 69.307  -11.359 1.00 15.74 ? 183  ASP B OD1 1 
ATOM   3877 O  OD2 . ASP B 1 78  ? -20.402 70.176  -10.090 1.00 26.82 ? 183  ASP B OD2 1 
ATOM   3878 N  N   . ASP B 1 79  ? -22.598 68.551  -12.778 1.00 15.58 ? 184  ASP B N   1 
ATOM   3879 C  CA  . ASP B 1 79  ? -23.302 69.459  -13.708 1.00 16.81 ? 184  ASP B CA  1 
ATOM   3880 C  C   . ASP B 1 79  ? -22.730 70.889  -13.662 1.00 16.69 ? 184  ASP B C   1 
ATOM   3881 O  O   . ASP B 1 79  ? -23.035 71.622  -14.635 1.00 21.69 ? 184  ASP B O   1 
ATOM   3882 C  CB  . ASP B 1 79  ? -24.791 69.432  -13.363 1.00 19.77 ? 184  ASP B CB  1 
ATOM   3883 C  CG  . ASP B 1 79  ? -25.539 68.163  -13.882 1.00 27.54 ? 184  ASP B CG  1 
ATOM   3884 O  OD1 . ASP B 1 79  ? -24.980 67.266  -14.560 1.00 31.73 ? 184  ASP B OD1 1 
ATOM   3885 O  OD2 . ASP B 1 79  ? -26.771 68.062  -13.623 1.00 33.41 ? 184  ASP B OD2 1 
ATOM   3886 N  N   . ASP B 1 80  ? -21.978 71.302  -12.675 1.00 16.69 ? 185  ASP B N   1 
ATOM   3887 C  CA  . ASP B 1 80  ? -21.281 72.663  -12.745 1.00 20.77 ? 185  ASP B CA  1 
ATOM   3888 C  C   . ASP B 1 80  ? -19.884 72.607  -13.434 1.00 18.34 ? 185  ASP B C   1 
ATOM   3889 O  O   . ASP B 1 80  ? -19.141 73.572  -13.438 1.00 18.18 ? 185  ASP B O   1 
ATOM   3890 C  CB  . ASP B 1 80  ? -21.101 73.244  -11.361 1.00 23.37 ? 185  ASP B CB  1 
ATOM   3891 C  CG  . ASP B 1 80  ? -22.402 73.780  -10.751 1.00 37.40 ? 185  ASP B CG  1 
ATOM   3892 O  OD1 . ASP B 1 80  ? -23.317 74.198  -11.505 1.00 35.97 ? 185  ASP B OD1 1 
ATOM   3893 O  OD2 . ASP B 1 80  ? -22.488 73.758  -9.479  1.00 44.86 ? 185  ASP B OD2 1 
ATOM   3894 N  N   . ASN B 1 81  ? -19.394 71.413  -13.848 1.00 16.41 ? 186  ASN B N   1 
ATOM   3895 C  CA  . ASN B 1 81  ? -18.071 71.217  -14.378 1.00 14.00 ? 186  ASN B CA  1 
ATOM   3896 C  C   . ASN B 1 81  ? -17.032 71.785  -13.418 1.00 16.06 ? 186  ASN B C   1 
ATOM   3897 O  O   . ASN B 1 81  ? -16.017 72.453  -13.803 1.00 16.94 ? 186  ASN B O   1 
ATOM   3898 C  CB  . ASN B 1 81  ? -17.923 71.886  -15.818 1.00 16.50 ? 186  ASN B CB  1 
ATOM   3899 C  CG  . ASN B 1 81  ? -18.940 71.398  -16.780 1.00 18.33 ? 186  ASN B CG  1 
ATOM   3900 O  OD1 . ASN B 1 81  ? -19.857 72.130  -17.145 1.00 19.98 ? 186  ASN B OD1 1 
ATOM   3901 N  ND2 . ASN B 1 81  ? -18.881 70.089  -17.132 1.00 16.51 ? 186  ASN B ND2 1 
ATOM   3902 N  N   . MET B 1 82  ? -17.177 71.426  -12.129 1.00 15.50 ? 187  MET B N   1 
ATOM   3903 C  CA  A MET B 1 82  ? -16.248 71.825  -11.083 0.50 17.15 ? 187  MET B CA  1 
ATOM   3904 C  CA  B MET B 1 82  ? -16.228 71.824  -11.102 0.50 16.48 ? 187  MET B CA  1 
ATOM   3905 C  C   . MET B 1 82  ? -15.434 70.651  -10.520 1.00 14.42 ? 187  MET B C   1 
ATOM   3906 O  O   . MET B 1 82  ? -14.303 70.809  -10.040 1.00 15.61 ? 187  MET B O   1 
ATOM   3907 C  CB  A MET B 1 82  ? -17.011 72.489  -9.944  0.50 19.72 ? 187  MET B CB  1 
ATOM   3908 C  CB  B MET B 1 82  ? -16.942 72.579  -9.985  0.50 18.34 ? 187  MET B CB  1 
ATOM   3909 C  CG  A MET B 1 82  ? -17.685 73.792  -10.355 0.50 24.31 ? 187  MET B CG  1 
ATOM   3910 C  CG  B MET B 1 82  ? -17.436 73.955  -10.465 0.50 20.02 ? 187  MET B CG  1 
ATOM   3911 S  SD  A MET B 1 82  ? -17.980 74.813  -8.917  0.50 29.87 ? 187  MET B SD  1 
ATOM   3912 S  SD  B MET B 1 82  ? -16.172 75.225  -10.436 0.50 24.90 ? 187  MET B SD  1 
ATOM   3913 C  CE  A MET B 1 82  ? -18.813 73.801  -7.721  0.50 24.95 ? 187  MET B CE  1 
ATOM   3914 C  CE  B MET B 1 82  ? -16.088 75.577  -8.702  0.50 29.78 ? 187  MET B CE  1 
ATOM   3915 N  N   . PHE B 1 83  ? -16.039 69.434  -10.606 1.00 12.57 ? 188  PHE B N   1 
ATOM   3916 C  CA  . PHE B 1 83  ? -15.451 68.238  -9.914  1.00 12.26 ? 188  PHE B CA  1 
ATOM   3917 C  C   . PHE B 1 83  ? -15.525 67.084  -10.958 1.00 11.54 ? 188  PHE B C   1 
ATOM   3918 O  O   . PHE B 1 83  ? -16.552 66.928  -11.646 1.00 12.78 ? 188  PHE B O   1 
ATOM   3919 C  CB  . PHE B 1 83  ? -16.308 67.886  -8.657  1.00 13.07 ? 188  PHE B CB  1 
ATOM   3920 C  CG  . PHE B 1 83  ? -16.324 68.998  -7.644  1.00 15.16 ? 188  PHE B CG  1 
ATOM   3921 C  CD1 . PHE B 1 83  ? -15.144 69.302  -6.979  1.00 16.69 ? 188  PHE B CD1 1 
ATOM   3922 C  CD2 . PHE B 1 83  ? -17.479 69.802  -7.548  1.00 18.25 ? 188  PHE B CD2 1 
ATOM   3923 C  CE1 . PHE B 1 83  ? -15.100 70.463  -6.100  1.00 18.76 ? 188  PHE B CE1 1 
ATOM   3924 C  CE2 . PHE B 1 83  ? -17.441 70.974  -6.679  1.00 18.24 ? 188  PHE B CE2 1 
ATOM   3925 C  CZ  . PHE B 1 83  ? -16.246 71.255  -6.055  1.00 18.14 ? 188  PHE B CZ  1 
ATOM   3926 N  N   . ARG B 1 84  ? -14.448 66.289  -10.954 1.00 12.17 ? 189  ARG B N   1 
ATOM   3927 C  CA  . ARG B 1 84  ? -14.417 65.116  -11.899 1.00 12.02 ? 189  ARG B CA  1 
ATOM   3928 C  C   . ARG B 1 84  ? -14.055 63.935  -11.047 1.00 11.95 ? 189  ARG B C   1 
ATOM   3929 O  O   . ARG B 1 84  ? -13.115 63.948  -10.235 1.00 12.79 ? 189  ARG B O   1 
ATOM   3930 C  CB  . ARG B 1 84  ? -13.363 65.380  -13.008 1.00 11.95 ? 189  ARG B CB  1 
ATOM   3931 C  CG  . ARG B 1 84  ? -13.444 64.214  -14.029 1.00 12.12 ? 189  ARG B CG  1 
ATOM   3932 C  CD  . ARG B 1 84  ? -12.521 64.268  -15.270 1.00 17.29 ? 189  ARG B CD  1 
ATOM   3933 N  NE  . ARG B 1 84  ? -12.165 65.497  -15.609 1.00 23.52 ? 189  ARG B NE  1 
ATOM   3934 C  CZ  . ARG B 1 84  ? -11.161 66.433  -15.482 1.00 18.01 ? 189  ARG B CZ  1 
ATOM   3935 N  NH1 . ARG B 1 84  ? -9.828  66.538  -15.166 1.00 20.68 ? 189  ARG B NH1 1 
ATOM   3936 N  NH2 . ARG B 1 84  ? -11.741 67.419  -15.954 1.00 15.64 ? 189  ARG B NH2 1 
ATOM   3937 N  N   . PHE B 1 85  ? -14.750 62.811  -11.240 1.00 10.50 ? 190  PHE B N   1 
ATOM   3938 C  CA  . PHE B 1 85  ? -14.407 61.603  -10.436 1.00 10.31 ? 190  PHE B CA  1 
ATOM   3939 C  C   . PHE B 1 85  ? -12.945 61.231  -10.598 1.00 11.16 ? 190  PHE B C   1 
ATOM   3940 O  O   . PHE B 1 85  ? -12.374 61.332  -11.716 1.00 11.76 ? 190  PHE B O   1 
ATOM   3941 C  CB  . PHE B 1 85  ? -15.285 60.392  -10.830 1.00 9.99  ? 190  PHE B CB  1 
ATOM   3942 C  CG  . PHE B 1 85  ? -16.707 60.423  -10.407 1.00 10.08 ? 190  PHE B CG  1 
ATOM   3943 C  CD1 . PHE B 1 85  ? -17.687 59.854  -11.217 1.00 11.02 ? 190  PHE B CD1 1 
ATOM   3944 C  CD2 . PHE B 1 85  ? -17.093 60.997  -9.172  1.00 10.46 ? 190  PHE B CD2 1 
ATOM   3945 C  CE1 . PHE B 1 85  ? -19.040 59.839  -10.829 1.00 11.35 ? 190  PHE B CE1 1 
ATOM   3946 C  CE2 . PHE B 1 85  ? -18.464 60.948  -8.756  1.00 11.42 ? 190  PHE B CE2 1 
ATOM   3947 C  CZ  . PHE B 1 85  ? -19.404 60.365  -9.592  1.00 11.15 ? 190  PHE B CZ  1 
ATOM   3948 N  N   . ASP B 1 86  ? -12.327 60.773  -9.502  1.00 11.05 ? 191  ASP B N   1 
ATOM   3949 C  CA  . ASP B 1 86  ? -10.935 60.376  -9.498  1.00 11.49 ? 191  ASP B CA  1 
ATOM   3950 C  C   . ASP B 1 86  ? -10.860 58.963  -8.863  1.00 11.53 ? 191  ASP B C   1 
ATOM   3951 O  O   . ASP B 1 86  ? -10.401 58.751  -7.739  1.00 11.75 ? 191  ASP B O   1 
ATOM   3952 C  CB  . ASP B 1 86  ? -10.111 61.409  -8.665  1.00 12.89 ? 191  ASP B CB  1 
ATOM   3953 C  CG  . ASP B 1 86  ? -8.641  61.077  -8.688  1.00 14.81 ? 191  ASP B CG  1 
ATOM   3954 O  OD1 . ASP B 1 86  ? -8.106  60.390  -9.586  1.00 15.57 ? 191  ASP B OD1 1 
ATOM   3955 O  OD2 . ASP B 1 86  ? -7.973  61.446  -7.666  1.00 18.20 ? 191  ASP B OD2 1 
ATOM   3956 N  N   . TYR B 1 87  ? -11.347 57.966  -9.615  1.00 10.25 ? 192  TYR B N   1 
ATOM   3957 C  CA  . TYR B 1 87  ? -11.274 56.560  -9.126  1.00 10.77 ? 192  TYR B CA  1 
ATOM   3958 C  C   . TYR B 1 87  ? -9.805  56.156  -8.973  1.00 11.72 ? 192  TYR B C   1 
ATOM   3959 O  O   . TYR B 1 87  ? -9.024  56.317  -9.919  1.00 11.44 ? 192  TYR B O   1 
ATOM   3960 C  CB  . TYR B 1 87  ? -11.982 55.638  -10.204 1.00 10.53 ? 192  TYR B CB  1 
ATOM   3961 C  CG  . TYR B 1 87  ? -13.481 55.744  -10.278 1.00 9.62  ? 192  TYR B CG  1 
ATOM   3962 C  CD1 . TYR B 1 87  ? -14.049 56.630  -11.180 1.00 10.06 ? 192  TYR B CD1 1 
ATOM   3963 C  CD2 . TYR B 1 87  ? -14.303 54.921  -9.518  1.00 9.37  ? 192  TYR B CD2 1 
ATOM   3964 C  CE1 . TYR B 1 87  ? -15.425 56.745  -11.265 1.00 10.48 ? 192  TYR B CE1 1 
ATOM   3965 C  CE2 . TYR B 1 87  ? -15.682 55.015  -9.608  1.00 9.39  ? 192  TYR B CE2 1 
ATOM   3966 C  CZ  . TYR B 1 87  ? -16.251 55.906  -10.516 1.00 10.29 ? 192  TYR B CZ  1 
ATOM   3967 O  OH  . TYR B 1 87  ? -17.623 55.994  -10.674 1.00 11.24 ? 192  TYR B OH  1 
ATOM   3968 N  N   . SER B 1 88  ? -9.464  55.514  -7.871  1.00 11.21 ? 193  SER B N   1 
ATOM   3969 C  CA  . SER B 1 88  ? -8.048  55.099  -7.715  1.00 11.28 ? 193  SER B CA  1 
ATOM   3970 C  C   . SER B 1 88  ? -7.813  53.803  -8.496  1.00 12.38 ? 193  SER B C   1 
ATOM   3971 O  O   . SER B 1 88  ? -8.737  53.012  -8.829  1.00 11.31 ? 193  SER B O   1 
ATOM   3972 C  CB  . SER B 1 88  ? -7.744  54.848  -6.241  1.00 11.37 ? 193  SER B CB  1 
ATOM   3973 O  OG  . SER B 1 88  ? -8.429  53.644  -5.786  1.00 11.33 ? 193  SER B OG  1 
ATOM   3974 N  N   . PRO B 1 89  ? -6.586  53.430  -8.818  1.00 11.35 ? 194  PRO B N   1 
ATOM   3975 C  CA  . PRO B 1 89  ? -6.318  52.147  -9.460  1.00 11.58 ? 194  PRO B CA  1 
ATOM   3976 C  C   . PRO B 1 89  ? -6.874  50.932  -8.683  1.00 10.67 ? 194  PRO B C   1 
ATOM   3977 O  O   . PRO B 1 89  ? -7.433  50.010  -9.262  1.00 10.70 ? 194  PRO B O   1 
ATOM   3978 C  CB  . PRO B 1 89  ? -4.757  52.074  -9.602  1.00 12.52 ? 194  PRO B CB  1 
ATOM   3979 C  CG  . PRO B 1 89  ? -4.374  53.535  -9.546  1.00 12.82 ? 194  PRO B CG  1 
ATOM   3980 C  CD  . PRO B 1 89  ? -5.339  54.251  -8.652  1.00 13.35 ? 194  PRO B CD  1 
ATOM   3981 N  N   . GLU B 1 90  ? -6.662  50.933  -7.342  1.00 12.28 ? 195  GLU B N   1 
ATOM   3982 C  CA  . GLU B 1 90  ? -7.171  49.794  -6.536  1.00 10.72 ? 195  GLU B CA  1 
ATOM   3983 C  C   . GLU B 1 90  ? -8.706  49.782  -6.499  1.00 9.87  ? 195  GLU B C   1 
ATOM   3984 O  O   . GLU B 1 90  ? -9.261  48.684  -6.475  1.00 9.81  ? 195  GLU B O   1 
ATOM   3985 C  CB  . GLU B 1 90  ? -6.586  49.893  -5.118  1.00 13.93 ? 195  GLU B CB  1 
ATOM   3986 C  CG  . GLU B 1 90  ? -5.030  49.792  -5.109  1.00 19.44 ? 195  GLU B CG  1 
ATOM   3987 C  CD  . GLU B 1 90  ? -4.328  51.088  -5.644  1.00 25.59 ? 195  GLU B CD  1 
ATOM   3988 O  OE1 . GLU B 1 90  ? -4.921  52.267  -5.559  1.00 21.16 ? 195  GLU B OE1 1 
ATOM   3989 O  OE2 . GLU B 1 90  ? -3.184  50.861  -6.206  1.00 30.77 ? 195  GLU B OE2 1 
ATOM   3990 N  N   . PHE B 1 91  ? -9.351  50.954  -6.497  1.00 9.60  ? 196  PHE B N   1 
ATOM   3991 C  CA  . PHE B 1 91  ? -10.797 50.960  -6.630  1.00 9.78  ? 196  PHE B CA  1 
ATOM   3992 C  C   . PHE B 1 91  ? -11.227 50.343  -7.983  1.00 9.15  ? 196  PHE B C   1 
ATOM   3993 O  O   . PHE B 1 91  ? -12.209 49.558  -8.024  1.00 9.55  ? 196  PHE B O   1 
ATOM   3994 C  CB  . PHE B 1 91  ? -11.380 52.398  -6.481  1.00 9.34  ? 196  PHE B CB  1 
ATOM   3995 C  CG  . PHE B 1 91  ? -12.864 52.462  -6.424  1.00 9.45  ? 196  PHE B CG  1 
ATOM   3996 C  CD1 . PHE B 1 91  ? -13.456 52.898  -5.248  1.00 9.80  ? 196  PHE B CD1 1 
ATOM   3997 C  CD2 . PHE B 1 91  ? -13.684 52.147  -7.508  1.00 10.09 ? 196  PHE B CD2 1 
ATOM   3998 C  CE1 . PHE B 1 91  ? -14.852 53.080  -5.132  1.00 10.89 ? 196  PHE B CE1 1 
ATOM   3999 C  CE2 . PHE B 1 91  ? -15.092 52.310  -7.414  1.00 9.72  ? 196  PHE B CE2 1 
ATOM   4000 C  CZ  . PHE B 1 91  ? -15.693 52.794  -6.214  1.00 10.44 ? 196  PHE B CZ  1 
ATOM   4001 N  N   . LEU B 1 92  ? -10.547 50.729  -9.062  1.00 8.61  ? 197  LEU B N   1 
ATOM   4002 C  CA  . LEU B 1 92  ? -10.915 50.184  -10.376 1.00 8.98  ? 197  LEU B CA  1 
ATOM   4003 C  C   . LEU B 1 92  ? -10.801 48.646  -10.373 1.00 8.85  ? 197  LEU B C   1 
ATOM   4004 O  O   . LEU B 1 92  ? -11.643 47.963  -10.941 1.00 9.65  ? 197  LEU B O   1 
ATOM   4005 C  CB  . LEU B 1 92  ? -10.030 50.809  -11.476 1.00 10.58 ? 197  LEU B CB  1 
ATOM   4006 C  CG  . LEU B 1 92  ? -10.298 52.295  -11.663 1.00 10.43 ? 197  LEU B CG  1 
ATOM   4007 C  CD1 . LEU B 1 92  ? -9.279  52.903  -12.630 1.00 12.34 ? 197  LEU B CD1 1 
ATOM   4008 C  CD2 . LEU B 1 92  ? -11.711 52.516  -12.297 1.00 11.63 ? 197  LEU B CD2 1 
ATOM   4009 N  N   . LEU B 1 93  ? -9.778  48.094  -9.689  1.00 10.91 ? 198  LEU B N   1 
ATOM   4010 C  CA  . LEU B 1 93  ? -9.711  46.619  -9.626  1.00 11.74 ? 198  LEU B CA  1 
ATOM   4011 C  C   . LEU B 1 93  ? -10.868 46.028  -8.842  1.00 10.85 ? 198  LEU B C   1 
ATOM   4012 O  O   . LEU B 1 93  ? -11.397 44.954  -9.243  1.00 11.11 ? 198  LEU B O   1 
ATOM   4013 C  CB  . LEU B 1 93  ? -8.391  46.128  -8.948  1.00 13.32 ? 198  LEU B CB  1 
ATOM   4014 C  CG  . LEU B 1 93  ? -7.143  46.356  -9.791  1.00 13.98 ? 198  LEU B CG  1 
ATOM   4015 C  CD1 . LEU B 1 93  ? -5.869  46.098  -8.931  1.00 17.46 ? 198  LEU B CD1 1 
ATOM   4016 C  CD2 . LEU B 1 93  ? -7.119  45.427  -11.034 1.00 15.55 ? 198  LEU B CD2 1 
ATOM   4017 N  N   . TRP B 1 94  ? -11.301 46.711  -7.779  1.00 9.70  ? 199  TRP B N   1 
ATOM   4018 C  CA  . TRP B 1 94  ? -12.476 46.248  -7.054  1.00 10.14 ? 199  TRP B CA  1 
ATOM   4019 C  C   . TRP B 1 94  ? -13.702 46.289  -7.969  1.00 9.85  ? 199  TRP B C   1 
ATOM   4020 O  O   . TRP B 1 94  ? -14.505 45.329  -7.969  1.00 10.15 ? 199  TRP B O   1 
ATOM   4021 C  CB  . TRP B 1 94  ? -12.665 47.150  -5.820  1.00 10.23 ? 199  TRP B CB  1 
ATOM   4022 C  CG  . TRP B 1 94  ? -13.896 46.916  -4.978  1.00 8.59  ? 199  TRP B CG  1 
ATOM   4023 C  CD1 . TRP B 1 94  ? -14.161 45.748  -4.224  1.00 10.11 ? 199  TRP B CD1 1 
ATOM   4024 C  CD2 . TRP B 1 94  ? -14.987 47.793  -4.690  1.00 9.58  ? 199  TRP B CD2 1 
ATOM   4025 N  NE1 . TRP B 1 94  ? -15.321 45.895  -3.532  1.00 10.38 ? 199  TRP B NE1 1 
ATOM   4026 C  CE2 . TRP B 1 94  ? -15.889 47.118  -3.788  1.00 8.99  ? 199  TRP B CE2 1 
ATOM   4027 C  CE3 . TRP B 1 94  ? -15.341 49.091  -5.097  1.00 9.28  ? 199  TRP B CE3 1 
ATOM   4028 C  CZ2 . TRP B 1 94  ? -17.060 47.706  -3.271  1.00 10.40 ? 199  TRP B CZ2 1 
ATOM   4029 C  CZ3 . TRP B 1 94  ? -16.548 49.662  -4.619  1.00 11.02 ? 199  TRP B CZ3 1 
ATOM   4030 C  CH2 . TRP B 1 94  ? -17.339 49.006  -3.679  1.00 10.04 ? 199  TRP B CH2 1 
ATOM   4031 N  N   . ALA B 1 95  ? -13.955 47.402  -8.682  1.00 9.21  ? 200  ALA B N   1 
ATOM   4032 C  CA  . ALA B 1 95  ? -15.190 47.525  -9.480  1.00 10.00 ? 200  ALA B CA  1 
ATOM   4033 C  C   . ALA B 1 95  ? -15.164 46.665  -10.742 1.00 9.74  ? 200  ALA B C   1 
ATOM   4034 O  O   . ALA B 1 95  ? -16.245 46.283  -11.194 1.00 10.64 ? 200  ALA B O   1 
ATOM   4035 C  CB  . ALA B 1 95  ? -15.384 48.985  -9.881  1.00 11.16 ? 200  ALA B CB  1 
ATOM   4036 N  N   . LEU B 1 96  ? -13.975 46.388  -11.284 1.00 9.06  ? 201  LEU B N   1 
ATOM   4037 C  CA  . LEU B 1 96  ? -13.873 45.771  -12.602 1.00 9.05  ? 201  LEU B CA  1 
ATOM   4038 C  C   . LEU B 1 96  ? -13.483 44.307  -12.590 1.00 9.07  ? 201  LEU B C   1 
ATOM   4039 O  O   . LEU B 1 96  ? -13.694 43.588  -13.581 1.00 9.56  ? 201  LEU B O   1 
ATOM   4040 C  CB  . LEU B 1 96  ? -12.887 46.536  -13.483 1.00 9.36  ? 201  LEU B CB  1 
ATOM   4041 C  CG  . LEU B 1 96  ? -13.457 47.894  -13.910 1.00 9.49  ? 201  LEU B CG  1 
ATOM   4042 C  CD1 . LEU B 1 96  ? -12.348 48.767  -14.448 1.00 9.80  ? 201  LEU B CD1 1 
ATOM   4043 C  CD2 . LEU B 1 96  ? -14.528 47.728  -14.973 1.00 11.65 ? 201  LEU B CD2 1 
ATOM   4044 N  N   . ARG B 1 97  ? -13.013 43.803  -11.440 1.00 9.98  ? 202  ARG B N   1 
ATOM   4045 C  CA  . ARG B 1 97  ? -12.621 42.374  -11.301 1.00 10.20 ? 202  ARG B CA  1 
ATOM   4046 C  C   . ARG B 1 97  ? -13.401 41.718  -10.162 1.00 10.70 ? 202  ARG B C   1 
ATOM   4047 O  O   . ARG B 1 97  ? -12.788 41.011  -9.332  1.00 11.20 ? 202  ARG B O   1 
ATOM   4048 C  CB  . ARG B 1 97  ? -11.103 42.104  -11.220 1.00 11.25 ? 202  ARG B CB  1 
ATOM   4049 C  CG  . ARG B 1 97  ? -10.349 42.358  -12.548 1.00 13.64 ? 202  ARG B CG  1 
ATOM   4050 C  CD  . ARG B 1 97  ? -8.866  41.891  -12.406 1.00 13.56 ? 202  ARG B CD  1 
ATOM   4051 N  NE  . ARG B 1 97  ? -8.208  41.782  -13.669 1.00 15.19 ? 202  ARG B NE  1 
ATOM   4052 C  CZ  . ARG B 1 97  ? -7.025  41.175  -13.821 1.00 16.12 ? 202  ARG B CZ  1 
ATOM   4053 N  NH1 . ARG B 1 97  ? -6.384  40.738  -12.720 1.00 17.64 ? 202  ARG B NH1 1 
ATOM   4054 N  NH2 . ARG B 1 97  ? -6.494  40.986  -14.985 1.00 17.23 ? 202  ARG B NH2 1 
ATOM   4055 N  N   . PRO B 1 98  ? -14.725 41.799  -10.097 1.00 9.42  ? 203  PRO B N   1 
ATOM   4056 C  CA  . PRO B 1 98  ? -15.529 41.020  -9.150  1.00 9.32  ? 203  PRO B CA  1 
ATOM   4057 C  C   . PRO B 1 98  ? -15.607 39.589  -9.652  1.00 9.56  ? 203  PRO B C   1 
ATOM   4058 O  O   . PRO B 1 98  ? -15.187 39.272  -10.795 1.00 10.14 ? 203  PRO B O   1 
ATOM   4059 C  CB  . PRO B 1 98  ? -16.961 41.700  -9.239  1.00 9.88  ? 203  PRO B CB  1 
ATOM   4060 C  CG  . PRO B 1 98  ? -17.028 42.122  -10.737 1.00 10.57 ? 203  PRO B CG  1 
ATOM   4061 C  CD  . PRO B 1 98  ? -15.600 42.602  -11.026 1.00 10.21 ? 203  PRO B CD  1 
ATOM   4062 N  N   . PRO B 1 99  ? -16.205 38.686  -8.896  1.00 10.45 ? 204  PRO B N   1 
ATOM   4063 C  CA  . PRO B 1 99  ? -16.342 37.268  -9.296  1.00 10.78 ? 204  PRO B CA  1 
ATOM   4064 C  C   . PRO B 1 99  ? -17.031 37.189  -10.671 1.00 11.49 ? 204  PRO B C   1 
ATOM   4065 O  O   . PRO B 1 99  ? -18.059 37.863  -10.950 1.00 12.33 ? 204  PRO B O   1 
ATOM   4066 C  CB  . PRO B 1 99  ? -17.286 36.681  -8.208  1.00 11.66 ? 204  PRO B CB  1 
ATOM   4067 C  CG  . PRO B 1 99  ? -16.908 37.495  -6.949  1.00 11.96 ? 204  PRO B CG  1 
ATOM   4068 C  CD  . PRO B 1 99  ? -16.653 38.895  -7.484  1.00 11.08 ? 204  PRO B CD  1 
ATOM   4069 N  N   . GLY B 1 100 ? -16.369 36.419  -11.543 1.00 11.77 ? 205  GLY B N   1 
ATOM   4070 C  CA  . GLY B 1 100 ? -16.905 36.191  -12.943 1.00 11.69 ? 205  GLY B CA  1 
ATOM   4071 C  C   . GLY B 1 100 ? -16.440 37.213  -13.934 1.00 10.65 ? 205  GLY B C   1 
ATOM   4072 O  O   . GLY B 1 100 ? -16.835 37.097  -15.114 1.00 11.16 ? 205  GLY B O   1 
ATOM   4073 N  N   . TRP B 1 101 ? -15.576 38.180  -13.591 1.00 9.16  ? 206  TRP B N   1 
ATOM   4074 C  CA  . TRP B 1 101 ? -15.078 39.092  -14.605 1.00 9.39  ? 206  TRP B CA  1 
ATOM   4075 C  C   . TRP B 1 101 ? -14.375 38.327  -15.758 1.00 8.67  ? 206  TRP B C   1 
ATOM   4076 O  O   . TRP B 1 101 ? -13.787 37.258  -15.572 1.00 10.13 ? 206  TRP B O   1 
ATOM   4077 C  CB  . TRP B 1 101 ? -14.084 40.088  -13.975 1.00 9.79  ? 206  TRP B CB  1 
ATOM   4078 C  CG  . TRP B 1 101 ? -12.782 39.486  -13.543 1.00 9.81  ? 206  TRP B CG  1 
ATOM   4079 C  CD1 . TRP B 1 101 ? -12.491 38.931  -12.308 1.00 11.49 ? 206  TRP B CD1 1 
ATOM   4080 C  CD2 . TRP B 1 101 ? -11.607 39.360  -14.359 1.00 10.89 ? 206  TRP B CD2 1 
ATOM   4081 N  NE1 . TRP B 1 101 ? -11.162 38.480  -12.319 1.00 12.00 ? 206  TRP B NE1 1 
ATOM   4082 C  CE2 . TRP B 1 101 ? -10.605 38.732  -13.556 1.00 12.67 ? 206  TRP B CE2 1 
ATOM   4083 C  CE3 . TRP B 1 101 ? -11.281 39.752  -15.680 1.00 11.95 ? 206  TRP B CE3 1 
ATOM   4084 C  CZ2 . TRP B 1 101 ? -9.316  38.439  -14.065 1.00 12.01 ? 206  TRP B CZ2 1 
ATOM   4085 C  CZ3 . TRP B 1 101 ? -10.017 39.528  -16.137 1.00 12.94 ? 206  TRP B CZ3 1 
ATOM   4086 C  CH2 . TRP B 1 101 ? -9.061  38.801  -15.348 1.00 13.47 ? 206  TRP B CH2 1 
ATOM   4087 N  N   . LEU B 1 102 ? -14.491 38.894  -16.931 1.00 8.96  ? 207  LEU B N   1 
ATOM   4088 C  CA  . LEU B 1 102 ? -13.905 38.333  -18.163 1.00 9.32  ? 207  LEU B CA  1 
ATOM   4089 C  C   . LEU B 1 102 ? -13.000 39.356  -18.816 1.00 10.07 ? 207  LEU B C   1 
ATOM   4090 O  O   . LEU B 1 102 ? -13.334 40.553  -18.911 1.00 9.03  ? 207  LEU B O   1 
ATOM   4091 C  CB  . LEU B 1 102 ? -14.988 37.904  -19.172 1.00 10.02 ? 207  LEU B CB  1 
ATOM   4092 C  CG  . LEU B 1 102 ? -15.922 36.789  -18.705 1.00 11.78 ? 207  LEU B CG  1 
ATOM   4093 C  CD1 . LEU B 1 102 ? -17.018 36.438  -19.750 1.00 11.96 ? 207  LEU B CD1 1 
ATOM   4094 C  CD2 . LEU B 1 102 ? -15.126 35.519  -18.286 1.00 15.03 ? 207  LEU B CD2 1 
ATOM   4095 N  N   . PRO B 1 103 ? -11.837 38.937  -19.338 1.00 10.76 ? 208  PRO B N   1 
ATOM   4096 C  CA  . PRO B 1 103 ? -10.919 39.873  -19.925 1.00 11.64 ? 208  PRO B CA  1 
ATOM   4097 C  C   . PRO B 1 103 ? -11.414 40.623  -21.179 1.00 9.38  ? 208  PRO B C   1 
ATOM   4098 O  O   . PRO B 1 103 ? -11.091 41.766  -21.404 1.00 10.56 ? 208  PRO B O   1 
ATOM   4099 C  CB  . PRO B 1 103 ? -9.672  38.967  -20.282 1.00 12.89 ? 208  PRO B CB  1 
ATOM   4100 C  CG  . PRO B 1 103 ? -10.166 37.639  -20.370 1.00 14.64 ? 208  PRO B CG  1 
ATOM   4101 C  CD  . PRO B 1 103 ? -11.278 37.518  -19.313 1.00 12.46 ? 208  PRO B CD  1 
ATOM   4102 N  N   . GLN B 1 104 ? -12.219 39.923  -21.984 1.00 10.29 ? 209  GLN B N   1 
ATOM   4103 C  CA  A GLN B 1 104 ? -12.741 40.542  -23.251 0.50 8.93  ? 209  GLN B CA  1 
ATOM   4104 C  CA  B GLN B 1 104 ? -12.684 40.599  -23.248 0.50 10.02 ? 209  GLN B CA  1 
ATOM   4105 C  C   . GLN B 1 104 ? -13.745 41.666  -22.899 1.00 9.32  ? 209  GLN B C   1 
ATOM   4106 O  O   . GLN B 1 104 ? -14.112 42.446  -23.804 1.00 10.39 ? 209  GLN B O   1 
ATOM   4107 C  CB  A GLN B 1 104 ? -13.443 39.507  -24.142 0.50 10.20 ? 209  GLN B CB  1 
ATOM   4108 C  CB  B GLN B 1 104 ? -13.281 39.627  -24.265 0.50 13.79 ? 209  GLN B CB  1 
ATOM   4109 C  CG  A GLN B 1 104 ? -14.519 38.707  -23.508 0.50 9.88  ? 209  GLN B CG  1 
ATOM   4110 C  CG  B GLN B 1 104 ? -12.274 38.747  -24.988 0.50 16.27 ? 209  GLN B CG  1 
ATOM   4111 C  CD  A GLN B 1 104 ? -14.083 37.382  -22.911 0.50 9.25  ? 209  GLN B CD  1 
ATOM   4112 C  CD  B GLN B 1 104 ? -10.947 39.483  -25.470 0.50 16.71 ? 209  GLN B CD  1 
ATOM   4113 O  OE1 A GLN B 1 104 ? -13.062 37.312  -22.233 0.50 8.70  ? 209  GLN B OE1 1 
ATOM   4114 O  OE1 B GLN B 1 104 ? -10.985 40.328  -26.383 0.50 20.26 ? 209  GLN B OE1 1 
ATOM   4115 N  NE2 A GLN B 1 104 ? -14.896 36.389  -23.054 0.50 12.60 ? 209  GLN B NE2 1 
ATOM   4116 N  NE2 B GLN B 1 104 ? -9.795  39.238  -24.720 0.50 18.94 ? 209  GLN B NE2 1 
ATOM   4117 N  N   . TRP B 1 105 ? -14.246 41.675  -21.646 1.00 9.26  ? 210  TRP B N   1 
ATOM   4118 C  CA  . TRP B 1 105 ? -15.224 42.695  -21.241 1.00 8.34  ? 210  TRP B CA  1 
ATOM   4119 C  C   . TRP B 1 105 ? -14.530 43.913  -20.658 1.00 8.87  ? 210  TRP B C   1 
ATOM   4120 O  O   . TRP B 1 105 ? -15.269 44.825  -20.157 1.00 8.73  ? 210  TRP B O   1 
ATOM   4121 C  CB  . TRP B 1 105 ? -16.229 42.066  -20.267 1.00 7.91  ? 210  TRP B CB  1 
ATOM   4122 C  CG  . TRP B 1 105 ? -17.124 41.072  -20.884 1.00 7.71  ? 210  TRP B CG  1 
ATOM   4123 C  CD1 . TRP B 1 105 ? -17.330 40.772  -22.239 1.00 8.22  ? 210  TRP B CD1 1 
ATOM   4124 C  CD2 . TRP B 1 105 ? -18.114 40.289  -20.165 1.00 7.16  ? 210  TRP B CD2 1 
ATOM   4125 N  NE1 . TRP B 1 105 ? -18.326 39.807  -22.377 1.00 8.03  ? 210  TRP B NE1 1 
ATOM   4126 C  CE2 . TRP B 1 105 ? -18.853 39.512  -21.111 1.00 7.18  ? 210  TRP B CE2 1 
ATOM   4127 C  CE3 . TRP B 1 105 ? -18.388 40.141  -18.802 1.00 8.65  ? 210  TRP B CE3 1 
ATOM   4128 C  CZ2 . TRP B 1 105 ? -19.836 38.641  -20.732 1.00 8.32  ? 210  TRP B CZ2 1 
ATOM   4129 C  CZ3 . TRP B 1 105 ? -19.359 39.240  -18.407 1.00 9.60  ? 210  TRP B CZ3 1 
ATOM   4130 C  CH2 . TRP B 1 105 ? -20.107 38.514  -19.393 1.00 8.79  ? 210  TRP B CH2 1 
ATOM   4131 N  N   . HIS B 1 106 ? -13.231 44.071  -20.708 1.00 8.39  ? 211  HIS B N   1 
ATOM   4132 C  CA  . HIS B 1 106 ? -12.505 45.297  -20.349 1.00 9.09  ? 211  HIS B CA  1 
ATOM   4133 C  C   . HIS B 1 106 ? -12.029 45.870  -21.677 1.00 10.00 ? 211  HIS B C   1 
ATOM   4134 O  O   . HIS B 1 106 ? -10.926 45.566  -22.156 1.00 10.17 ? 211  HIS B O   1 
ATOM   4135 C  CB  . HIS B 1 106 ? -11.332 44.962  -19.368 1.00 9.75  ? 211  HIS B CB  1 
ATOM   4136 C  CG  . HIS B 1 106 ? -11.813 44.423  -18.084 1.00 8.97  ? 211  HIS B CG  1 
ATOM   4137 N  ND1 . HIS B 1 106 ? -11.000 43.743  -17.195 1.00 11.16 ? 211  HIS B ND1 1 
ATOM   4138 C  CD2 . HIS B 1 106 ? -13.033 44.577  -17.484 1.00 9.24  ? 211  HIS B CD2 1 
ATOM   4139 C  CE1 . HIS B 1 106 ? -11.708 43.447  -16.138 1.00 11.51 ? 211  HIS B CE1 1 
ATOM   4140 N  NE2 . HIS B 1 106 ? -12.956 43.922  -16.264 1.00 10.07 ? 211  HIS B NE2 1 
ATOM   4141 N  N   . CYS B 1 107 ? -12.927 46.637  -22.324 1.00 8.20  ? 212  CYS B N   1 
ATOM   4142 C  CA  . CYS B 1 107 ? -12.782 46.857  -23.759 1.00 9.00  ? 212  CYS B CA  1 
ATOM   4143 C  C   . CYS B 1 107 ? -12.221 48.250  -24.025 1.00 8.27  ? 212  CYS B C   1 
ATOM   4144 O  O   . CYS B 1 107 ? -12.968 49.277  -23.907 1.00 8.82  ? 212  CYS B O   1 
ATOM   4145 C  CB  . CYS B 1 107 ? -14.209 46.689  -24.384 1.00 9.05  ? 212  CYS B CB  1 
ATOM   4146 S  SG  . CYS B 1 107 ? -14.286 47.027  -26.172 1.00 12.24 ? 212  CYS B SG  1 
ATOM   4147 N  N   . GLY B 1 108 ? -10.936 48.352  -24.365 1.00 8.99  ? 213  GLY B N   1 
ATOM   4148 C  CA  . GLY B 1 108 ? -10.302 49.633  -24.615 1.00 9.24  ? 213  GLY B CA  1 
ATOM   4149 C  C   . GLY B 1 108 ? -10.252 49.991  -26.118 1.00 9.02  ? 213  GLY B C   1 
ATOM   4150 O  O   . GLY B 1 108 ? -10.421 49.114  -27.014 1.00 9.44  ? 213  GLY B O   1 
ATOM   4151 N  N   . VAL B 1 109 ? -10.019 51.281  -26.347 1.00 8.64  ? 214  VAL B N   1 
ATOM   4152 C  CA  . VAL B 1 109 ? -9.818  51.814  -27.708 1.00 8.94  ? 214  VAL B CA  1 
ATOM   4153 C  C   . VAL B 1 109 ? -8.488  52.627  -27.638 1.00 9.17  ? 214  VAL B C   1 
ATOM   4154 O  O   . VAL B 1 109 ? -8.284  53.438  -26.767 1.00 9.11  ? 214  VAL B O   1 
ATOM   4155 C  CB  . VAL B 1 109 ? -10.919 52.796  -28.106 1.00 9.65  ? 214  VAL B CB  1 
ATOM   4156 C  CG1 . VAL B 1 109 ? -10.625 53.441  -29.474 1.00 10.04 ? 214  VAL B CG1 1 
ATOM   4157 C  CG2 . VAL B 1 109 ? -12.249 52.035  -28.133 1.00 11.54 ? 214  VAL B CG2 1 
ATOM   4158 N  N   . ARG B 1 110 ? -7.598  52.269  -28.579 1.00 9.12  ? 215  ARG B N   1 
ATOM   4159 C  CA  . ARG B 1 110 ? -6.295  52.963  -28.707 1.00 9.19  ? 215  ARG B CA  1 
ATOM   4160 C  C   . ARG B 1 110 ? -6.134  53.607  -30.036 1.00 9.36  ? 215  ARG B C   1 
ATOM   4161 O  O   . ARG B 1 110 ? -6.694  53.212  -31.071 1.00 10.36 ? 215  ARG B O   1 
ATOM   4162 C  CB  . ARG B 1 110 ? -5.083  52.001  -28.471 1.00 9.53  ? 215  ARG B CB  1 
ATOM   4163 C  CG  . ARG B 1 110 ? -5.049  51.484  -27.039 1.00 9.53  ? 215  ARG B CG  1 
ATOM   4164 C  CD  . ARG B 1 110 ? -3.885  50.477  -26.843 1.00 10.21 ? 215  ARG B CD  1 
ATOM   4165 N  NE  . ARG B 1 110 ? -3.792  49.902  -25.517 1.00 11.19 ? 215  ARG B NE  1 
ATOM   4166 C  CZ  . ARG B 1 110 ? -3.217  50.542  -24.477 1.00 9.93  ? 215  ARG B CZ  1 
ATOM   4167 N  NH1 . ARG B 1 110 ? -2.841  51.777  -24.575 1.00 11.73 ? 215  ARG B NH1 1 
ATOM   4168 N  NH2 . ARG B 1 110 ? -3.112  49.932  -23.279 1.00 11.91 ? 215  ARG B NH2 1 
ATOM   4169 N  N   . VAL B 1 111 ? -5.293  54.648  -30.078 1.00 9.63  ? 216  VAL B N   1 
ATOM   4170 C  CA  . VAL B 1 111 ? -4.893  55.263  -31.353 1.00 10.02 ? 216  VAL B CA  1 
ATOM   4171 C  C   . VAL B 1 111 ? -3.931  54.244  -32.028 1.00 10.51 ? 216  VAL B C   1 
ATOM   4172 O  O   . VAL B 1 111 ? -3.000  53.683  -31.410 1.00 11.03 ? 216  VAL B O   1 
ATOM   4173 C  CB  . VAL B 1 111 ? -4.161  56.568  -31.049 1.00 11.09 ? 216  VAL B CB  1 
ATOM   4174 C  CG1 . VAL B 1 111 ? -3.670  57.219  -32.385 1.00 13.40 ? 216  VAL B CG1 1 
ATOM   4175 C  CG2 . VAL B 1 111 ? -5.005  57.578  -30.235 1.00 12.12 ? 216  VAL B CG2 1 
ATOM   4176 N  N   . VAL B 1 112 ? -4.129  54.039  -33.328 1.00 10.90 ? 217  VAL B N   1 
ATOM   4177 C  CA  . VAL B 1 112 ? -3.324  53.027  -34.071 1.00 11.48 ? 217  VAL B CA  1 
ATOM   4178 C  C   . VAL B 1 112 ? -1.819  53.361  -34.054 1.00 11.29 ? 217  VAL B C   1 
ATOM   4179 O  O   . VAL B 1 112 ? -0.991  52.488  -33.757 1.00 11.98 ? 217  VAL B O   1 
ATOM   4180 C  CB  . VAL B 1 112 ? -3.822  52.862  -35.495 1.00 12.35 ? 217  VAL B CB  1 
ATOM   4181 C  CG1 . VAL B 1 112 ? -2.861  52.040  -36.390 1.00 13.12 ? 217  VAL B CG1 1 
ATOM   4182 C  CG2 . VAL B 1 112 ? -5.164  52.158  -35.485 1.00 12.68 ? 217  VAL B CG2 1 
ATOM   4183 N  N   . SER B 1 113 ? -1.512  54.610  -34.374 1.00 11.77 ? 218  SER B N   1 
ATOM   4184 C  CA  . SER B 1 113 ? -0.062  54.982  -34.505 1.00 13.32 ? 218  SER B CA  1 
ATOM   4185 C  C   . SER B 1 113 ? 0.655   55.065  -33.192 1.00 13.51 ? 218  SER B C   1 
ATOM   4186 O  O   . SER B 1 113 ? 1.783   54.527  -33.059 1.00 16.36 ? 218  SER B O   1 
ATOM   4187 C  CB  . SER B 1 113 ? 0.030   56.320  -35.281 1.00 14.33 ? 218  SER B CB  1 
ATOM   4188 O  OG  . SER B 1 113 ? -0.569  57.370  -34.555 1.00 19.82 ? 218  SER B OG  1 
ATOM   4189 N  N   . SER B 1 114 ? 0.099   55.759  -32.184 1.00 13.79 ? 219  SER B N   1 
ATOM   4190 C  CA  . SER B 1 114 ? 0.762   56.023  -30.936 1.00 14.36 ? 219  SER B CA  1 
ATOM   4191 C  C   . SER B 1 114 ? 0.432   55.014  -29.849 1.00 13.28 ? 219  SER B C   1 
ATOM   4192 O  O   . SER B 1 114 ? 1.135   54.991  -28.829 1.00 14.24 ? 219  SER B O   1 
ATOM   4193 C  CB  . SER B 1 114 ? 0.291   57.427  -30.474 1.00 15.57 ? 219  SER B CB  1 
ATOM   4194 O  OG  . SER B 1 114 ? -1.104  57.327  -30.056 1.00 14.55 ? 219  SER B OG  1 
ATOM   4195 N  N   . ARG B 1 115 ? -0.653  54.213  -30.019 1.00 12.40 ? 220  ARG B N   1 
ATOM   4196 C  CA  . ARG B 1 115 ? -1.157  53.303  -28.987 1.00 11.21 ? 220  ARG B CA  1 
ATOM   4197 C  C   . ARG B 1 115 ? -1.711  54.023  -27.777 1.00 11.47 ? 220  ARG B C   1 
ATOM   4198 O  O   . ARG B 1 115 ? -2.045  53.330  -26.798 1.00 12.39 ? 220  ARG B O   1 
ATOM   4199 C  CB  . ARG B 1 115 ? -0.091  52.237  -28.566 1.00 12.20 ? 220  ARG B CB  1 
ATOM   4200 C  CG  . ARG B 1 115 ? 0.446   51.465  -29.786 1.00 13.31 ? 220  ARG B CG  1 
ATOM   4201 C  CD  . ARG B 1 115 ? -0.615  50.581  -30.519 1.00 12.77 ? 220  ARG B CD  1 
ATOM   4202 N  NE  . ARG B 1 115 ? -1.166  49.580  -29.642 1.00 12.30 ? 220  ARG B NE  1 
ATOM   4203 C  CZ  . ARG B 1 115 ? -2.169  48.732  -29.929 1.00 12.20 ? 220  ARG B CZ  1 
ATOM   4204 N  NH1 . ARG B 1 115 ? -2.729  48.742  -31.120 1.00 13.04 ? 220  ARG B NH1 1 
ATOM   4205 N  NH2 . ARG B 1 115 ? -2.606  47.839  -29.017 1.00 14.08 ? 220  ARG B NH2 1 
ATOM   4206 N  N   . LYS B 1 116 ? -1.920  55.322  -27.836 1.00 11.35 ? 221  LYS B N   1 
ATOM   4207 C  CA  . LYS B 1 116 ? -2.507  56.057  -26.686 1.00 12.52 ? 221  LYS B CA  1 
ATOM   4208 C  C   . LYS B 1 116 ? -3.923  55.498  -26.386 1.00 10.49 ? 221  LYS B C   1 
ATOM   4209 O  O   . LYS B 1 116 ? -4.750  55.315  -27.328 1.00 11.27 ? 221  LYS B O   1 
ATOM   4210 C  CB  . LYS B 1 116 ? -2.604  57.530  -26.977 1.00 12.70 ? 221  LYS B CB  1 
ATOM   4211 C  CG  . LYS B 1 116 ? -3.258  58.372  -25.862 1.00 15.60 ? 221  LYS B CG  1 
ATOM   4212 C  CD  . LYS B 1 116 ? -3.250  59.859  -26.190 1.00 18.52 ? 221  LYS B CD  1 
ATOM   4213 C  CE  . LYS B 1 116 ? -3.809  60.716  -25.083 1.00 20.99 ? 221  LYS B CE  1 
ATOM   4214 N  NZ  . LYS B 1 116 ? -3.319  60.600  -23.665 1.00 25.08 ? 221  LYS B NZ  1 
ATOM   4215 N  N   . LEU B 1 117 ? -4.207  55.306  -25.095 1.00 10.92 ? 222  LEU B N   1 
ATOM   4216 C  CA  . LEU B 1 117 ? -5.593  54.866  -24.705 1.00 10.08 ? 222  LEU B CA  1 
ATOM   4217 C  C   . LEU B 1 117 ? -6.577  56.084  -24.752 1.00 10.57 ? 222  LEU B C   1 
ATOM   4218 O  O   . LEU B 1 117 ? -6.346  57.122  -24.099 1.00 11.17 ? 222  LEU B O   1 
ATOM   4219 C  CB  . LEU B 1 117 ? -5.541  54.291  -23.304 1.00 10.86 ? 222  LEU B CB  1 
ATOM   4220 C  CG  . LEU B 1 117 ? -6.893  53.658  -22.822 1.00 9.21  ? 222  LEU B CG  1 
ATOM   4221 C  CD1 . LEU B 1 117 ? -7.297  52.425  -23.614 1.00 11.32 ? 222  LEU B CD1 1 
ATOM   4222 C  CD2 . LEU B 1 117 ? -6.824  53.384  -21.334 1.00 12.02 ? 222  LEU B CD2 1 
ATOM   4223 N  N   . VAL B 1 118 ? -7.625  55.927  -25.572 1.00 9.50  ? 223  VAL B N   1 
ATOM   4224 C  CA  . VAL B 1 118 ? -8.539  57.079  -25.756 1.00 10.01 ? 223  VAL B CA  1 
ATOM   4225 C  C   . VAL B 1 118 ? -10.006 56.679  -25.534 1.00 9.66  ? 223  VAL B C   1 
ATOM   4226 O  O   . VAL B 1 118 ? -10.902 57.542  -25.673 1.00 9.79  ? 223  VAL B O   1 
ATOM   4227 C  CB  . VAL B 1 118 ? -8.351  57.693  -27.162 1.00 9.25  ? 223  VAL B CB  1 
ATOM   4228 C  CG1 . VAL B 1 118 ? -6.989  58.399  -27.225 1.00 11.32 ? 223  VAL B CG1 1 
ATOM   4229 C  CG2 . VAL B 1 118 ? -8.569  56.700  -28.280 1.00 10.43 ? 223  VAL B CG2 1 
ATOM   4230 N  N   . GLY B 1 119 ? -10.306 55.394  -25.226 1.00 10.54 ? 224  GLY B N   1 
ATOM   4231 C  CA  . GLY B 1 119 ? -11.686 55.034  -24.923 1.00 10.52 ? 224  GLY B CA  1 
ATOM   4232 C  C   . GLY B 1 119 ? -11.769 53.808  -24.111 1.00 9.04  ? 224  GLY B C   1 
ATOM   4233 O  O   . GLY B 1 119 ? -10.777 52.998  -24.116 1.00 8.87  ? 224  GLY B O   1 
ATOM   4234 N  N   . PHE B 1 120 ? -12.917 53.551  -23.479 1.00 8.54  ? 225  PHE B N   1 
ATOM   4235 C  CA  . PHE B 1 120 ? -13.098 52.308  -22.693 1.00 8.56  ? 225  PHE B CA  1 
ATOM   4236 C  C   . PHE B 1 120 ? -14.581 52.088  -22.472 1.00 8.17  ? 225  PHE B C   1 
ATOM   4237 O  O   . PHE B 1 120 ? -15.358 53.078  -22.464 1.00 8.48  ? 225  PHE B O   1 
ATOM   4238 C  CB  . PHE B 1 120 ? -12.436 52.499  -21.277 1.00 8.18  ? 225  PHE B CB  1 
ATOM   4239 C  CG  . PHE B 1 120 ? -12.397 51.202  -20.445 1.00 8.45  ? 225  PHE B CG  1 
ATOM   4240 C  CD1 . PHE B 1 120 ? -11.587 50.136  -20.805 1.00 8.64  ? 225  PHE B CD1 1 
ATOM   4241 C  CD2 . PHE B 1 120 ? -13.138 51.131  -19.283 1.00 9.41  ? 225  PHE B CD2 1 
ATOM   4242 C  CE1 . PHE B 1 120 ? -11.523 49.003  -20.001 1.00 9.21  ? 225  PHE B CE1 1 
ATOM   4243 C  CE2 . PHE B 1 120 ? -13.126 49.982  -18.470 1.00 9.02  ? 225  PHE B CE2 1 
ATOM   4244 C  CZ  . PHE B 1 120 ? -12.275 48.890  -18.812 1.00 9.79  ? 225  PHE B CZ  1 
ATOM   4245 N  N   . ILE B 1 121 ? -14.961 50.852  -22.287 1.00 8.01  ? 226  ILE B N   1 
ATOM   4246 C  CA  . ILE B 1 121 ? -16.297 50.471  -21.738 1.00 7.76  ? 226  ILE B CA  1 
ATOM   4247 C  C   . ILE B 1 121 ? -16.045 49.135  -21.040 1.00 7.69  ? 226  ILE B C   1 
ATOM   4248 O  O   . ILE B 1 121 ? -15.189 48.333  -21.457 1.00 8.52  ? 226  ILE B O   1 
ATOM   4249 C  CB  . ILE B 1 121 ? -17.349 50.423  -22.882 1.00 8.16  ? 226  ILE B CB  1 
ATOM   4250 C  CG1 . ILE B 1 121 ? -18.759 50.285  -22.250 1.00 8.54  ? 226  ILE B CG1 1 
ATOM   4251 C  CG2 . ILE B 1 121 ? -17.074 49.301  -23.883 1.00 9.35  ? 226  ILE B CG2 1 
ATOM   4252 C  CD1 . ILE B 1 121 ? -19.871 50.615  -23.306 1.00 9.55  ? 226  ILE B CD1 1 
ATOM   4253 N  N   . SER B 1 122 ? -16.914 48.805  -20.083 1.00 7.45  ? 227  SER B N   1 
ATOM   4254 C  CA  . SER B 1 122 ? -16.787 47.505  -19.392 1.00 8.14  ? 227  SER B CA  1 
ATOM   4255 C  C   . SER B 1 122 ? -18.113 46.866  -19.195 1.00 7.94  ? 227  SER B C   1 
ATOM   4256 O  O   . SER B 1 122 ? -19.133 47.546  -19.004 1.00 7.86  ? 227  SER B O   1 
ATOM   4257 C  CB  . SER B 1 122 ? -16.042 47.679  -18.061 1.00 9.28  ? 227  SER B CB  1 
ATOM   4258 O  OG  . SER B 1 122 ? -16.857 48.369  -17.141 1.00 10.06 ? 227  SER B OG  1 
ATOM   4259 N  N   . ALA B 1 123 ? -18.043 45.547  -19.045 1.00 7.66  ? 228  ALA B N   1 
ATOM   4260 C  CA  . ALA B 1 123 ? -19.188 44.729  -18.547 1.00 7.61  ? 228  ALA B CA  1 
ATOM   4261 C  C   . ALA B 1 123 ? -18.677 43.856  -17.411 1.00 7.93  ? 228  ALA B C   1 
ATOM   4262 O  O   . ALA B 1 123 ? -17.551 43.329  -17.489 1.00 8.54  ? 228  ALA B O   1 
ATOM   4263 C  CB  . ALA B 1 123 ? -19.753 43.820  -19.662 1.00 7.86  ? 228  ALA B CB  1 
ATOM   4264 N  N   . ILE B 1 124 ? -19.515 43.687  -16.370 1.00 7.57  ? 229  ILE B N   1 
ATOM   4265 C  CA  . ILE B 1 124 ? -19.293 42.666  -15.347 1.00 7.53  ? 229  ILE B CA  1 
ATOM   4266 C  C   . ILE B 1 124 ? -20.547 41.845  -15.182 1.00 8.34  ? 229  ILE B C   1 
ATOM   4267 O  O   . ILE B 1 124 ? -21.680 42.365  -15.406 1.00 9.09  ? 229  ILE B O   1 
ATOM   4268 C  CB  . ILE B 1 124 ? -18.841 43.228  -13.963 1.00 8.11  ? 229  ILE B CB  1 
ATOM   4269 C  CG1 . ILE B 1 124 ? -19.924 44.238  -13.415 1.00 7.85  ? 229  ILE B CG1 1 
ATOM   4270 C  CG2 . ILE B 1 124 ? -17.452 43.849  -14.090 1.00 9.30  ? 229  ILE B CG2 1 
ATOM   4271 C  CD1 . ILE B 1 124 ? -19.716 44.669  -11.936 1.00 10.01 ? 229  ILE B CD1 1 
ATOM   4272 N  N   . PRO B 1 125 ? -20.494 40.558  -14.882 1.00 8.39  ? 230  PRO B N   1 
ATOM   4273 C  CA  . PRO B 1 125 ? -21.722 39.746  -14.798 1.00 8.31  ? 230  PRO B CA  1 
ATOM   4274 C  C   . PRO B 1 125 ? -22.457 40.052  -13.493 1.00 9.79  ? 230  PRO B C   1 
ATOM   4275 O  O   . PRO B 1 125 ? -21.801 40.360  -12.443 1.00 10.70 ? 230  PRO B O   1 
ATOM   4276 C  CB  . PRO B 1 125 ? -21.157 38.302  -14.788 1.00 10.25 ? 230  PRO B CB  1 
ATOM   4277 C  CG  . PRO B 1 125 ? -19.839 38.443  -14.182 1.00 11.21 ? 230  PRO B CG  1 
ATOM   4278 C  CD  . PRO B 1 125 ? -19.285 39.759  -14.607 1.00 8.78  ? 230  PRO B CD  1 
ATOM   4279 N  N   . ALA B 1 126 ? -23.781 39.988  -13.507 1.00 9.34  ? 231  ALA B N   1 
ATOM   4280 C  CA  . ALA B 1 126 ? -24.566 40.125  -12.260 1.00 9.16  ? 231  ALA B CA  1 
ATOM   4281 C  C   . ALA B 1 126 ? -25.852 39.376  -12.382 1.00 10.41 ? 231  ALA B C   1 
ATOM   4282 O  O   . ALA B 1 126 ? -26.473 39.436  -13.471 1.00 10.97 ? 231  ALA B O   1 
ATOM   4283 C  CB  . ALA B 1 126 ? -24.814 41.633  -11.977 1.00 11.10 ? 231  ALA B CB  1 
ATOM   4284 N  N   . ASN B 1 127 ? -26.346 38.710  -11.375 1.00 10.10 ? 232  ASN B N   1 
ATOM   4285 C  CA  A ASN B 1 127 ? -27.707 38.211  -11.387 0.50 10.86 ? 232  ASN B CA  1 
ATOM   4286 C  CA  B ASN B 1 127 ? -27.693 38.150  -11.306 0.50 11.30 ? 232  ASN B CA  1 
ATOM   4287 C  C   . ASN B 1 127 ? -28.605 39.315  -10.906 1.00 10.18 ? 232  ASN B C   1 
ATOM   4288 O  O   . ASN B 1 127 ? -28.348 39.956  -9.837  1.00 10.79 ? 232  ASN B O   1 
ATOM   4289 C  CB  A ASN B 1 127 ? -27.779 36.969  -10.516 0.50 11.50 ? 232  ASN B CB  1 
ATOM   4290 C  CB  B ASN B 1 127 ? -27.687 37.068  -10.203 0.50 12.59 ? 232  ASN B CB  1 
ATOM   4291 C  CG  A ASN B 1 127 ? -27.157 35.776  -11.242 0.50 13.14 ? 232  ASN B CG  1 
ATOM   4292 C  CG  B ASN B 1 127 ? -28.780 36.045  -10.373 0.50 15.78 ? 232  ASN B CG  1 
ATOM   4293 O  OD1 A ASN B 1 127 ? -27.650 35.378  -12.236 0.50 13.16 ? 232  ASN B OD1 1 
ATOM   4294 O  OD1 B ASN B 1 127 ? -29.552 36.104  -11.344 0.50 16.68 ? 232  ASN B OD1 1 
ATOM   4295 N  ND2 A ASN B 1 127 ? -25.962 35.470  -10.900 0.50 18.17 ? 232  ASN B ND2 1 
ATOM   4296 N  ND2 B ASN B 1 127 ? -28.845 35.083  -9.447  0.50 18.81 ? 232  ASN B ND2 1 
ATOM   4297 N  N   . ILE B 1 128 ? -29.643 39.591  -11.674 1.00 10.11 ? 233  ILE B N   1 
ATOM   4298 C  CA  . ILE B 1 128 ? -30.494 40.744  -11.440 1.00 9.86  ? 233  ILE B CA  1 
ATOM   4299 C  C   . ILE B 1 128 ? -31.956 40.268  -11.210 1.00 10.95 ? 233  ILE B C   1 
ATOM   4300 O  O   . ILE B 1 128 ? -32.473 39.422  -11.979 1.00 13.10 ? 233  ILE B O   1 
ATOM   4301 C  CB  . ILE B 1 128 ? -30.453 41.707  -12.653 1.00 10.62 ? 233  ILE B CB  1 
ATOM   4302 C  CG1 . ILE B 1 128 ? -29.055 42.371  -12.756 1.00 9.94  ? 233  ILE B CG1 1 
ATOM   4303 C  CG2 . ILE B 1 128 ? -31.524 42.792  -12.559 1.00 12.10 ? 233  ILE B CG2 1 
ATOM   4304 C  CD1 . ILE B 1 128 ? -28.603 43.227  -11.526 1.00 12.49 ? 233  ILE B CD1 1 
ATOM   4305 N  N   . HIS B 1 129 ? -32.569 40.781  -10.159 1.00 10.46 ? 234  HIS B N   1 
ATOM   4306 C  CA  . HIS B 1 129 ? -34.009 40.530  -9.904  1.00 11.95 ? 234  HIS B CA  1 
ATOM   4307 C  C   . HIS B 1 129 ? -34.727 41.782  -10.413 1.00 11.45 ? 234  HIS B C   1 
ATOM   4308 O  O   . HIS B 1 129 ? -34.514 42.886  -9.921  1.00 11.28 ? 234  HIS B O   1 
ATOM   4309 C  CB  . HIS B 1 129 ? -34.147 40.320  -8.379  1.00 13.03 ? 234  HIS B CB  1 
ATOM   4310 C  CG  . HIS B 1 129 ? -35.447 39.708  -7.962  1.00 17.87 ? 234  HIS B CG  1 
ATOM   4311 N  ND1 . HIS B 1 129 ? -35.702 39.389  -6.643  1.00 21.04 ? 234  HIS B ND1 1 
ATOM   4312 C  CD2 . HIS B 1 129 ? -36.514 39.266  -8.678  1.00 20.34 ? 234  HIS B CD2 1 
ATOM   4313 C  CE1 . HIS B 1 129 ? -36.923 38.844  -6.546  1.00 24.95 ? 234  HIS B CE1 1 
ATOM   4314 N  NE2 . HIS B 1 129 ? -37.434 38.755  -7.764  1.00 21.43 ? 234  HIS B NE2 1 
ATOM   4315 N  N   . ILE B 1 130 ? -35.636 41.574  -11.385 1.00 11.28 ? 235  ILE B N   1 
ATOM   4316 C  CA  . ILE B 1 130 ? -36.433 42.697  -11.901 1.00 10.90 ? 235  ILE B CA  1 
ATOM   4317 C  C   . ILE B 1 130 ? -37.904 42.215  -11.888 1.00 11.22 ? 235  ILE B C   1 
ATOM   4318 O  O   . ILE B 1 130 ? -38.283 41.273  -12.596 1.00 12.02 ? 235  ILE B O   1 
ATOM   4319 C  CB  . ILE B 1 130 ? -35.949 43.103  -13.314 1.00 11.48 ? 235  ILE B CB  1 
ATOM   4320 C  CG1 . ILE B 1 130 ? -36.871 44.163  -13.939 1.00 11.98 ? 235  ILE B CG1 1 
ATOM   4321 C  CG2 . ILE B 1 130 ? -35.767 41.918  -14.312 1.00 11.04 ? 235  ILE B CG2 1 
ATOM   4322 C  CD1 . ILE B 1 130 ? -36.936 45.478  -13.134 1.00 13.37 ? 235  ILE B CD1 1 
ATOM   4323 N  N   . TYR B 1 131 ? -38.653 42.832  -10.980 1.00 12.14 ? 236  TYR B N   1 
ATOM   4324 C  CA  . TYR B 1 131 ? -40.068 42.355  -10.663 1.00 12.84 ? 236  TYR B CA  1 
ATOM   4325 C  C   . TYR B 1 131 ? -40.049 40.855  -10.431 1.00 15.38 ? 236  TYR B C   1 
ATOM   4326 O  O   . TYR B 1 131 ? -39.269 40.410  -9.551  1.00 17.29 ? 236  TYR B O   1 
ATOM   4327 C  CB  . TYR B 1 131 ? -41.044 42.824  -11.775 1.00 12.85 ? 236  TYR B CB  1 
ATOM   4328 C  CG  . TYR B 1 131 ? -41.205 44.264  -11.896 1.00 12.44 ? 236  TYR B CG  1 
ATOM   4329 C  CD1 . TYR B 1 131 ? -41.926 45.041  -10.944 1.00 14.91 ? 236  TYR B CD1 1 
ATOM   4330 C  CD2 . TYR B 1 131 ? -40.621 44.978  -12.948 1.00 12.80 ? 236  TYR B CD2 1 
ATOM   4331 C  CE1 . TYR B 1 131 ? -42.019 46.407  -11.075 1.00 13.21 ? 236  TYR B CE1 1 
ATOM   4332 C  CE2 . TYR B 1 131 ? -40.739 46.376  -13.072 1.00 11.76 ? 236  TYR B CE2 1 
ATOM   4333 C  CZ  . TYR B 1 131 ? -41.475 47.084  -12.134 1.00 13.21 ? 236  TYR B CZ  1 
ATOM   4334 O  OH  . TYR B 1 131 ? -41.614 48.407  -12.244 1.00 14.41 ? 236  TYR B OH  1 
ATOM   4335 N  N   . ASP B 1 132 ? -40.761 40.005  -11.190 1.00 14.53 ? 237  ASP B N   1 
ATOM   4336 C  CA  A ASP B 1 132 ? -40.843 38.571  -10.827 0.50 18.47 ? 237  ASP B CA  1 
ATOM   4337 C  CA  B ASP B 1 132 ? -40.896 38.556  -10.974 0.50 16.67 ? 237  ASP B CA  1 
ATOM   4338 C  C   . ASP B 1 132 ? -39.838 37.735  -11.615 1.00 20.18 ? 237  ASP B C   1 
ATOM   4339 O  O   . ASP B 1 132 ? -39.949 36.490  -11.639 1.00 24.29 ? 237  ASP B O   1 
ATOM   4340 C  CB  A ASP B 1 132 ? -42.325 38.012  -10.841 0.50 22.82 ? 237  ASP B CB  1 
ATOM   4341 C  CB  B ASP B 1 132 ? -42.318 38.043  -11.427 0.50 18.71 ? 237  ASP B CB  1 
ATOM   4342 C  CG  A ASP B 1 132 ? -43.256 38.780  -9.906  0.50 29.95 ? 237  ASP B CG  1 
ATOM   4343 C  CG  B ASP B 1 132 ? -42.625 38.314  -12.911 0.50 19.59 ? 237  ASP B CG  1 
ATOM   4344 O  OD1 A ASP B 1 132 ? -42.934 38.874  -8.689  0.50 32.71 ? 237  ASP B OD1 1 
ATOM   4345 O  OD1 B ASP B 1 132 ? -42.264 39.378  -13.532 0.50 21.76 ? 237  ASP B OD1 1 
ATOM   4346 O  OD2 A ASP B 1 132 ? -44.303 39.304  -10.373 0.50 36.04 ? 237  ASP B OD2 1 
ATOM   4347 O  OD2 B ASP B 1 132 ? -43.306 37.389  -13.440 0.50 27.30 ? 237  ASP B OD2 1 
ATOM   4348 N  N   . THR B 1 133 ? -38.832 38.343  -12.248 1.00 16.98 ? 238  THR B N   1 
ATOM   4349 C  CA  . THR B 1 133 ? -37.841 37.549  -12.986 1.00 16.60 ? 238  THR B CA  1 
ATOM   4350 C  C   . THR B 1 133 ? -36.446 37.704  -12.349 1.00 13.83 ? 238  THR B C   1 
ATOM   4351 O  O   . THR B 1 133 ? -36.093 38.838  -11.964 1.00 14.74 ? 238  THR B O   1 
ATOM   4352 C  CB  . THR B 1 133 ? -37.701 38.106  -14.409 1.00 19.38 ? 238  THR B CB  1 
ATOM   4353 O  OG1 . THR B 1 133 ? -38.892 37.780  -15.148 1.00 22.82 ? 238  THR B OG1 1 
ATOM   4354 C  CG2 . THR B 1 133 ? -36.509 37.585  -15.199 1.00 18.46 ? 238  THR B CG2 1 
ATOM   4355 N  N   . GLU B 1 134 ? -35.701 36.650  -12.231 1.00 13.71 ? 239  GLU B N   1 
ATOM   4356 C  CA  A GLU B 1 134 ? -34.277 36.762  -11.866 0.50 16.59 ? 239  GLU B CA  1 
ATOM   4357 C  CA  B GLU B 1 134 ? -34.261 36.750  -11.877 0.50 16.31 ? 239  GLU B CA  1 
ATOM   4358 C  C   . GLU B 1 134 ? -33.477 36.121  -12.963 1.00 17.74 ? 239  GLU B C   1 
ATOM   4359 O  O   . GLU B 1 134 ? -33.733 34.914  -13.348 1.00 21.17 ? 239  GLU B O   1 
ATOM   4360 C  CB  A GLU B 1 134 ? -34.008 35.986  -10.568 0.50 16.86 ? 239  GLU B CB  1 
ATOM   4361 C  CB  B GLU B 1 134 ? -33.908 35.956  -10.607 0.50 15.81 ? 239  GLU B CB  1 
ATOM   4362 C  CG  A GLU B 1 134 ? -32.585 35.991  -10.042 0.50 18.00 ? 239  GLU B CG  1 
ATOM   4363 C  CG  B GLU B 1 134 ? -34.534 36.568  -9.387  0.50 17.91 ? 239  GLU B CG  1 
ATOM   4364 C  CD  A GLU B 1 134 ? -32.446 34.983  -8.902  0.50 25.08 ? 239  GLU B CD  1 
ATOM   4365 C  CD  B GLU B 1 134 ? -34.130 35.999  -8.028  0.50 20.53 ? 239  GLU B CD  1 
ATOM   4366 O  OE1 A GLU B 1 134 ? -33.016 35.292  -7.827  0.50 28.98 ? 239  GLU B OE1 1 
ATOM   4367 O  OE1 B GLU B 1 134 ? -33.373 35.027  -7.996  0.50 25.82 ? 239  GLU B OE1 1 
ATOM   4368 O  OE2 A GLU B 1 134 ? -31.822 33.872  -9.072  0.50 28.26 ? 239  GLU B OE2 1 
ATOM   4369 O  OE2 B GLU B 1 134 ? -34.528 36.577  -7.005  0.50 21.44 ? 239  GLU B OE2 1 
ATOM   4370 N  N   . LYS B 1 135 ? -32.505 36.865  -13.454 1.00 16.84 ? 240  LYS B N   1 
ATOM   4371 C  CA  . LYS B 1 135 ? -31.750 36.319  -14.550 1.00 18.10 ? 240  LYS B CA  1 
ATOM   4372 C  C   . LYS B 1 135 ? -30.338 36.894  -14.559 1.00 14.43 ? 240  LYS B C   1 
ATOM   4373 O  O   . LYS B 1 135 ? -30.108 38.057  -14.126 1.00 12.32 ? 240  LYS B O   1 
ATOM   4374 C  CB  . LYS B 1 135 ? -32.403 36.996  -15.740 1.00 22.49 ? 240  LYS B CB  1 
ATOM   4375 C  CG  . LYS B 1 135 ? -32.198 36.233  -17.012 1.00 26.37 ? 240  LYS B CG  1 
ATOM   4376 C  CD  . LYS B 1 135 ? -33.067 36.778  -18.194 1.00 19.99 ? 240  LYS B CD  1 
ATOM   4377 C  CE  . LYS B 1 135 ? -32.435 36.004  -19.290 1.00 24.22 ? 240  LYS B CE  1 
ATOM   4378 N  NZ  . LYS B 1 135 ? -33.258 36.192  -20.491 1.00 20.21 ? 240  LYS B NZ  1 
ATOM   4379 N  N   . LYS B 1 136 ? -29.411 36.117  -15.132 1.00 15.20 ? 241  LYS B N   1 
ATOM   4380 C  CA  A LYS B 1 136 ? -28.055 36.543  -15.368 0.50 12.60 ? 241  LYS B CA  1 
ATOM   4381 C  CA  B LYS B 1 136 ? -28.035 36.582  -15.303 0.50 12.30 ? 241  LYS B CA  1 
ATOM   4382 C  C   . LYS B 1 136 ? -27.989 37.649  -16.385 1.00 11.13 ? 241  LYS B C   1 
ATOM   4383 O  O   . LYS B 1 136 ? -28.455 37.443  -17.495 1.00 12.31 ? 241  LYS B O   1 
ATOM   4384 C  CB  A LYS B 1 136 ? -27.293 35.292  -15.900 0.50 14.70 ? 241  LYS B CB  1 
ATOM   4385 C  CB  B LYS B 1 136 ? -27.055 35.349  -15.518 0.50 13.74 ? 241  LYS B CB  1 
ATOM   4386 C  CG  A LYS B 1 136 ? -25.952 35.689  -16.447 0.50 17.28 ? 241  LYS B CG  1 
ATOM   4387 C  CG  B LYS B 1 136 ? -25.647 35.734  -15.849 0.50 14.45 ? 241  LYS B CG  1 
ATOM   4388 C  CD  A LYS B 1 136 ? -25.128 36.420  -15.380 0.50 20.29 ? 241  LYS B CD  1 
ATOM   4389 C  CD  B LYS B 1 136 ? -24.868 36.474  -14.759 0.50 17.07 ? 241  LYS B CD  1 
ATOM   4390 C  CE  A LYS B 1 136 ? -23.646 36.190  -15.613 0.50 20.17 ? 241  LYS B CE  1 
ATOM   4391 C  CE  B LYS B 1 136 ? -24.831 35.671  -13.441 0.50 16.51 ? 241  LYS B CE  1 
ATOM   4392 N  NZ  A LYS B 1 136 ? -23.259 34.766  -15.911 0.50 20.68 ? 241  LYS B NZ  1 
ATOM   4393 N  NZ  B LYS B 1 136 ? -23.959 34.432  -13.445 0.50 17.52 ? 241  LYS B NZ  1 
ATOM   4394 N  N   . MET B 1 137 ? -27.395 38.827  -16.069 1.00 9.24  ? 242  MET B N   1 
ATOM   4395 C  CA  . MET B 1 137 ? -27.259 39.989  -16.941 1.00 8.79  ? 242  MET B CA  1 
ATOM   4396 C  C   . MET B 1 137 ? -25.788 40.421  -16.847 1.00 8.51  ? 242  MET B C   1 
ATOM   4397 O  O   . MET B 1 137 ? -24.984 39.776  -16.169 1.00 9.24  ? 242  MET B O   1 
ATOM   4398 C  CB  . MET B 1 137 ? -28.130 41.155  -16.501 1.00 9.98  ? 242  MET B CB  1 
ATOM   4399 C  CG  . MET B 1 137 ? -29.604 40.721  -16.443 1.00 11.13 ? 242  MET B CG  1 
ATOM   4400 S  SD  . MET B 1 137 ? -30.678 42.194  -16.372 1.00 12.93 ? 242  MET B SD  1 
ATOM   4401 C  CE  . MET B 1 137 ? -32.288 41.355  -16.250 1.00 16.46 ? 242  MET B CE  1 
ATOM   4402 N  N   . VAL B 1 138 ? -25.495 41.528  -17.489 1.00 8.08  ? 243  VAL B N   1 
ATOM   4403 C  CA  . VAL B 1 138 ? -24.271 42.271  -17.201 1.00 8.72  ? 243  VAL B CA  1 
ATOM   4404 C  C   . VAL B 1 138 ? -24.606 43.681  -16.703 1.00 8.13  ? 243  VAL B C   1 
ATOM   4405 O  O   . VAL B 1 138 ? -25.676 44.235  -17.033 1.00 9.24  ? 243  VAL B O   1 
ATOM   4406 C  CB  . VAL B 1 138 ? -23.280 42.388  -18.390 1.00 7.93  ? 243  VAL B CB  1 
ATOM   4407 C  CG1 . VAL B 1 138 ? -22.707 41.028  -18.739 1.00 9.20  ? 243  VAL B CG1 1 
ATOM   4408 C  CG2 . VAL B 1 138 ? -23.911 43.066  -19.606 1.00 8.87  ? 243  VAL B CG2 1 
ATOM   4409 N  N   . GLU B 1 139 ? -23.692 44.275  -15.956 1.00 7.95  ? 244  GLU B N   1 
ATOM   4410 C  CA  . GLU B 1 139 ? -23.730 45.713  -15.596 1.00 7.90  ? 244  GLU B CA  1 
ATOM   4411 C  C   . GLU B 1 139 ? -22.725 46.411  -16.458 1.00 8.96  ? 244  GLU B C   1 
ATOM   4412 O  O   . GLU B 1 139 ? -21.526 46.006  -16.519 1.00 8.72  ? 244  GLU B O   1 
ATOM   4413 C  CB  . GLU B 1 139 ? -23.343 45.899  -14.135 1.00 9.43  ? 244  GLU B CB  1 
ATOM   4414 C  CG  . GLU B 1 139 ? -24.471 45.335  -13.227 1.00 11.95 ? 244  GLU B CG  1 
ATOM   4415 C  CD  . GLU B 1 139 ? -24.164 45.182  -11.776 1.00 14.02 ? 244  GLU B CD  1 
ATOM   4416 O  OE1 . GLU B 1 139 ? -23.056 45.388  -11.409 1.00 19.22 ? 244  GLU B OE1 1 
ATOM   4417 O  OE2 . GLU B 1 139 ? -25.102 44.906  -10.992 1.00 14.27 ? 244  GLU B OE2 1 
ATOM   4418 N  N   . ILE B 1 140 ? -23.116 47.472  -17.161 1.00 8.42  ? 245  ILE B N   1 
ATOM   4419 C  CA  . ILE B 1 140 ? -22.207 48.258  -18.007 1.00 7.79  ? 245  ILE B CA  1 
ATOM   4420 C  C   . ILE B 1 140 ? -21.785 49.494  -17.283 1.00 8.64  ? 245  ILE B C   1 
ATOM   4421 O  O   . ILE B 1 140 ? -22.662 50.197  -16.669 1.00 8.98  ? 245  ILE B O   1 
ATOM   4422 C  CB  . ILE B 1 140 ? -22.877 48.634  -19.366 1.00 8.29  ? 245  ILE B CB  1 
ATOM   4423 C  CG1 . ILE B 1 140 ? -23.315 47.395  -20.104 1.00 8.61  ? 245  ILE B CG1 1 
ATOM   4424 C  CG2 . ILE B 1 140 ? -21.896 49.455  -20.230 1.00 8.72  ? 245  ILE B CG2 1 
ATOM   4425 C  CD1 . ILE B 1 140 ? -22.225 46.323  -20.367 1.00 10.04 ? 245  ILE B CD1 1 
ATOM   4426 N  N   . ASN B 1 141 ? -20.480 49.836  -17.273 1.00 8.36  ? 246  ASN B N   1 
ATOM   4427 C  CA  . ASN B 1 141 ? -19.996 50.944  -16.479 1.00 8.95  ? 246  ASN B CA  1 
ATOM   4428 C  C   . ASN B 1 141 ? -18.667 51.399  -17.126 1.00 8.61  ? 246  ASN B C   1 
ATOM   4429 O  O   . ASN B 1 141 ? -18.116 50.696  -17.990 1.00 9.32  ? 246  ASN B O   1 
ATOM   4430 C  CB  . ASN B 1 141 ? -19.745 50.481  -15.017 1.00 9.55  ? 246  ASN B CB  1 
ATOM   4431 C  CG  . ASN B 1 141 ? -19.942 51.582  -13.972 1.00 9.91  ? 246  ASN B CG  1 
ATOM   4432 O  OD1 . ASN B 1 141 ? -19.783 52.774  -14.310 1.00 10.26 ? 246  ASN B OD1 1 
ATOM   4433 N  ND2 . ASN B 1 141 ? -20.191 51.195  -12.745 1.00 11.49 ? 246  ASN B ND2 1 
ATOM   4434 N  N   . PHE B 1 142 ? -18.219 52.581  -16.712 1.00 8.41  ? 247  PHE B N   1 
ATOM   4435 C  CA  . PHE B 1 142 ? -16.913 53.114  -17.145 1.00 8.20  ? 247  PHE B CA  1 
ATOM   4436 C  C   . PHE B 1 142 ? -16.824 53.379  -18.630 1.00 9.45  ? 247  PHE B C   1 
ATOM   4437 O  O   . PHE B 1 142 ? -15.744 53.327  -19.217 1.00 10.82 ? 247  PHE B O   1 
ATOM   4438 C  CB  . PHE B 1 142 ? -15.717 52.290  -16.604 1.00 8.67  ? 247  PHE B CB  1 
ATOM   4439 C  CG  . PHE B 1 142 ? -15.765 52.221  -15.097 1.00 8.58  ? 247  PHE B CG  1 
ATOM   4440 C  CD1 . PHE B 1 142 ? -16.232 51.090  -14.475 1.00 8.90  ? 247  PHE B CD1 1 
ATOM   4441 C  CD2 . PHE B 1 142 ? -15.362 53.296  -14.312 1.00 9.34  ? 247  PHE B CD2 1 
ATOM   4442 C  CE1 . PHE B 1 142 ? -16.317 51.007  -13.052 1.00 10.77 ? 247  PHE B CE1 1 
ATOM   4443 C  CE2 . PHE B 1 142 ? -15.403 53.253  -12.894 1.00 10.47 ? 247  PHE B CE2 1 
ATOM   4444 C  CZ  . PHE B 1 142 ? -15.911 52.106  -12.260 1.00 11.09 ? 247  PHE B CZ  1 
ATOM   4445 N  N   . LEU B 1 143 ? -17.954 53.693  -19.275 1.00 8.82  ? 248  LEU B N   1 
ATOM   4446 C  CA  . LEU B 1 143 ? -17.929 54.189  -20.681 1.00 8.44  ? 248  LEU B CA  1 
ATOM   4447 C  C   . LEU B 1 143 ? -17.233 55.538  -20.691 1.00 8.37  ? 248  LEU B C   1 
ATOM   4448 O  O   . LEU B 1 143 ? -17.667 56.492  -19.998 1.00 9.05  ? 248  LEU B O   1 
ATOM   4449 C  CB  . LEU B 1 143 ? -19.354 54.279  -21.279 1.00 8.86  ? 248  LEU B CB  1 
ATOM   4450 C  CG  . LEU B 1 143 ? -19.494 55.065  -22.570 1.00 9.28  ? 248  LEU B CG  1 
ATOM   4451 C  CD1 . LEU B 1 143 ? -18.642 54.424  -23.734 1.00 10.01 ? 248  LEU B CD1 1 
ATOM   4452 C  CD2 . LEU B 1 143 ? -20.968 55.180  -22.958 1.00 10.38 ? 248  LEU B CD2 1 
ATOM   4453 N  N   . CYS B 1 144 ? -16.189 55.705  -21.495 1.00 8.66  ? 249  CYS B N   1 
ATOM   4454 C  CA  . CYS B 1 144 ? -15.392 56.973  -21.497 1.00 8.99  ? 249  CYS B CA  1 
ATOM   4455 C  C   . CYS B 1 144 ? -14.790 57.149  -22.851 1.00 9.62  ? 249  CYS B C   1 
ATOM   4456 O  O   . CYS B 1 144 ? -14.151 56.187  -23.376 1.00 8.96  ? 249  CYS B O   1 
ATOM   4457 C  CB  . CYS B 1 144 ? -14.314 56.905  -20.424 1.00 9.34  ? 249  CYS B CB  1 
ATOM   4458 S  SG  . CYS B 1 144 ? -13.366 58.453  -20.286 1.00 10.79 ? 249  CYS B SG  1 
ATOM   4459 N  N   . VAL B 1 145 ? -14.926 58.348  -23.436 1.00 9.55  ? 250  VAL B N   1 
ATOM   4460 C  CA  . VAL B 1 145 ? -14.218 58.730  -24.648 1.00 10.58 ? 250  VAL B CA  1 
ATOM   4461 C  C   . VAL B 1 145 ? -13.367 59.941  -24.300 1.00 10.62 ? 250  VAL B C   1 
ATOM   4462 O  O   . VAL B 1 145 ? -13.844 60.900  -23.622 1.00 11.04 ? 250  VAL B O   1 
ATOM   4463 C  CB  . VAL B 1 145 ? -15.196 59.042  -25.793 1.00 10.44 ? 250  VAL B CB  1 
ATOM   4464 C  CG1 . VAL B 1 145 ? -14.555 59.759  -27.003 1.00 12.50 ? 250  VAL B CG1 1 
ATOM   4465 C  CG2 . VAL B 1 145 ? -15.816 57.701  -26.297 1.00 11.00 ? 250  VAL B CG2 1 
ATOM   4466 N  N   . HIS B 1 146 ? -12.092 59.980  -24.696 1.00 10.76 ? 251  HIS B N   1 
ATOM   4467 C  CA  . HIS B 1 146 ? -11.205 61.115  -24.425 1.00 10.89 ? 251  HIS B CA  1 
ATOM   4468 C  C   . HIS B 1 146 ? -11.905 62.421  -24.889 1.00 10.01 ? 251  HIS B C   1 
ATOM   4469 O  O   . HIS B 1 146 ? -12.559 62.481  -25.952 1.00 11.19 ? 251  HIS B O   1 
ATOM   4470 C  CB  . HIS B 1 146 ? -9.908  60.855  -25.240 1.00 12.60 ? 251  HIS B CB  1 
ATOM   4471 C  CG  . HIS B 1 146 ? -8.760  61.722  -24.818 1.00 11.57 ? 251  HIS B CG  1 
ATOM   4472 N  ND1 . HIS B 1 146 ? -8.674  63.078  -25.161 1.00 16.21 ? 251  HIS B ND1 1 
ATOM   4473 C  CD2 . HIS B 1 146 ? -7.692  61.430  -24.039 1.00 13.38 ? 251  HIS B CD2 1 
ATOM   4474 C  CE1 . HIS B 1 146 ? -7.552  63.544  -24.622 1.00 16.36 ? 251  HIS B CE1 1 
ATOM   4475 N  NE2 . HIS B 1 146 ? -6.955  62.592  -23.926 1.00 15.68 ? 251  HIS B NE2 1 
ATOM   4476 N  N   . LYS B 1 147 ? -11.657 63.479  -24.109 1.00 11.72 ? 252  LYS B N   1 
ATOM   4477 C  CA  . LYS B 1 147 ? -12.200 64.806  -24.461 1.00 12.92 ? 252  LYS B CA  1 
ATOM   4478 C  C   . LYS B 1 147 ? -11.873 65.258  -25.887 1.00 13.92 ? 252  LYS B C   1 
ATOM   4479 O  O   . LYS B 1 147 ? -12.723 65.926  -26.472 1.00 14.89 ? 252  LYS B O   1 
ATOM   4480 C  CB  . LYS B 1 147 ? -11.651 65.862  -23.429 1.00 13.15 ? 252  LYS B CB  1 
ATOM   4481 C  CG  . LYS B 1 147 ? -12.373 65.733  -22.073 1.00 13.20 ? 252  LYS B CG  1 
ATOM   4482 C  CD  . LYS B 1 147 ? -11.666 66.570  -20.960 1.00 14.65 ? 252  LYS B CD  1 
ATOM   4483 C  CE  . LYS B 1 147 ? -12.365 66.548  -19.601 1.00 16.16 ? 252  LYS B CE  1 
ATOM   4484 N  NZ  . LYS B 1 147 ? -13.503 67.524  -19.673 1.00 17.24 ? 252  LYS B NZ  1 
ATOM   4485 N  N   . LYS B 1 148 ? -10.677 64.929  -26.403 1.00 12.84 ? 253  LYS B N   1 
ATOM   4486 C  CA  . LYS B 1 148 ? -10.325 65.377  -27.782 1.00 15.96 ? 253  LYS B CA  1 
ATOM   4487 C  C   . LYS B 1 148 ? -11.032 64.524  -28.839 1.00 18.65 ? 253  LYS B C   1 
ATOM   4488 O  O   . LYS B 1 148 ? -10.892 64.825  -30.051 1.00 19.93 ? 253  LYS B O   1 
ATOM   4489 C  CB  . LYS B 1 148 ? -8.791  65.238  -27.968 1.00 21.06 ? 253  LYS B CB  1 
ATOM   4490 C  CG  . LYS B 1 148 ? -8.069  66.243  -27.088 1.00 28.45 ? 253  LYS B CG  1 
ATOM   4491 C  CD  . LYS B 1 148 ? -8.174  67.671  -27.563 1.00 41.85 ? 253  LYS B CD  1 
ATOM   4492 C  CE  . LYS B 1 148 ? -7.334  68.588  -26.664 1.00 47.05 ? 253  LYS B CE  1 
ATOM   4493 N  NZ  . LYS B 1 148 ? -7.065  69.858  -27.392 1.00 51.28 ? 253  LYS B NZ  1 
ATOM   4494 N  N   . LEU B 1 149 ? -11.765 63.500  -28.482 1.00 14.55 ? 254  LEU B N   1 
ATOM   4495 C  CA  A LEU B 1 149 ? -12.431 62.584  -29.417 0.50 15.93 ? 254  LEU B CA  1 
ATOM   4496 C  CA  B LEU B 1 149 ? -12.414 62.557  -29.424 0.50 13.90 ? 254  LEU B CA  1 
ATOM   4497 C  C   . LEU B 1 149 ? -13.943 62.649  -29.295 1.00 13.69 ? 254  LEU B C   1 
ATOM   4498 O  O   . LEU B 1 149 ? -14.636 61.848  -29.861 1.00 13.07 ? 254  LEU B O   1 
ATOM   4499 C  CB  A LEU B 1 149 ? -11.978 61.182  -29.116 0.50 17.71 ? 254  LEU B CB  1 
ATOM   4500 C  CB  B LEU B 1 149 ? -11.895 61.140  -29.155 0.50 12.61 ? 254  LEU B CB  1 
ATOM   4501 C  CG  A LEU B 1 149 ? -10.655 60.810  -29.727 0.50 20.17 ? 254  LEU B CG  1 
ATOM   4502 C  CG  B LEU B 1 149 ? -12.197 59.913  -30.030 0.50 10.89 ? 254  LEU B CG  1 
ATOM   4503 C  CD1 A LEU B 1 149 ? -10.716 59.299  -29.702 0.50 22.69 ? 254  LEU B CD1 1 
ATOM   4504 C  CD1 B LEU B 1 149 ? -11.894 60.221  -31.514 0.50 11.62 ? 254  LEU B CD1 1 
ATOM   4505 C  CD2 A LEU B 1 149 ? -10.589 61.344  -31.132 0.50 20.98 ? 254  LEU B CD2 1 
ATOM   4506 C  CD2 B LEU B 1 149 ? -11.480 58.628  -29.625 0.50 10.71 ? 254  LEU B CD2 1 
ATOM   4507 N  N   . ARG B 1 150 ? -14.442 63.666  -28.542 1.00 13.60 ? 255  ARG B N   1 
ATOM   4508 C  CA  . ARG B 1 150 ? -15.885 63.761  -28.278 1.00 12.86 ? 255  ARG B CA  1 
ATOM   4509 C  C   . ARG B 1 150 ? -16.702 64.081  -29.521 1.00 13.84 ? 255  ARG B C   1 
ATOM   4510 O  O   . ARG B 1 150 ? -16.160 64.860  -30.396 1.00 15.85 ? 255  ARG B O   1 
ATOM   4511 C  CB  . ARG B 1 150 ? -16.241 64.756  -27.156 1.00 13.70 ? 255  ARG B CB  1 
ATOM   4512 C  CG  . ARG B 1 150 ? -15.606 64.343  -25.772 1.00 11.70 ? 255  ARG B CG  1 
ATOM   4513 C  CD  . ARG B 1 150 ? -16.513 63.264  -25.112 1.00 10.92 ? 255  ARG B CD  1 
ATOM   4514 N  NE  . ARG B 1 150 ? -15.915 62.863  -23.852 1.00 11.14 ? 255  ARG B NE  1 
ATOM   4515 C  CZ  . ARG B 1 150 ? -15.844 63.581  -22.735 1.00 11.49 ? 255  ARG B CZ  1 
ATOM   4516 N  NH1 . ARG B 1 150 ? -16.519 64.763  -22.633 1.00 12.36 ? 255  ARG B NH1 1 
ATOM   4517 N  NH2 . ARG B 1 150 ? -15.146 63.176  -21.685 1.00 11.41 ? 255  ARG B NH2 1 
ATOM   4518 N  N   . SER B 1 151 ? -17.984 63.697  -29.532 1.00 14.30 ? 256  SER B N   1 
ATOM   4519 C  CA  . SER B 1 151 ? -19.001 63.996  -30.574 1.00 14.89 ? 256  SER B CA  1 
ATOM   4520 C  C   . SER B 1 151 ? -18.554 63.493  -31.936 1.00 15.39 ? 256  SER B C   1 
ATOM   4521 O  O   . SER B 1 151 ? -18.794 64.135  -32.979 1.00 17.91 ? 256  SER B O   1 
ATOM   4522 C  CB  . SER B 1 151 ? -19.185 65.556  -30.545 1.00 15.67 ? 256  SER B CB  1 
ATOM   4523 O  OG  . SER B 1 151 ? -19.899 65.883  -29.339 1.00 20.06 ? 256  SER B OG  1 
ATOM   4524 N  N   . LYS B 1 152 ? -17.849 62.379  -31.981 1.00 14.55 ? 257  LYS B N   1 
ATOM   4525 C  CA  . LYS B 1 152 ? -17.424 61.748  -33.259 1.00 13.84 ? 257  LYS B CA  1 
ATOM   4526 C  C   . LYS B 1 152 ? -18.069 60.379  -33.345 1.00 14.67 ? 257  LYS B C   1 
ATOM   4527 O  O   . LYS B 1 152 ? -17.624 59.542  -34.188 1.00 15.98 ? 257  LYS B O   1 
ATOM   4528 C  CB  . LYS B 1 152 ? -15.897 61.635  -33.323 1.00 16.12 ? 257  LYS B CB  1 
ATOM   4529 C  CG  . LYS B 1 152 ? -15.122 62.959  -33.254 1.00 19.60 ? 257  LYS B CG  1 
ATOM   4530 C  CD  . LYS B 1 152 ? -14.919 63.514  -34.653 1.00 27.67 ? 257  LYS B CD  1 
ATOM   4531 C  CE  . LYS B 1 152 ? -13.909 64.708  -34.611 1.00 33.56 ? 257  LYS B CE  1 
ATOM   4532 N  NZ  . LYS B 1 152 ? -14.588 65.929  -34.132 1.00 37.40 ? 257  LYS B NZ  1 
ATOM   4533 N  N   . ARG B 1 153 ? -19.128 60.087  -32.539 1.00 13.70 ? 258  ARG B N   1 
ATOM   4534 C  CA  . ARG B 1 153 ? -19.949 58.831  -32.636 1.00 13.76 ? 258  ARG B CA  1 
ATOM   4535 C  C   . ARG B 1 153 ? -19.068 57.634  -32.330 1.00 14.60 ? 258  ARG B C   1 
ATOM   4536 O  O   . ARG B 1 153 ? -19.326 56.522  -32.877 1.00 15.01 ? 258  ARG B O   1 
ATOM   4537 C  CB  . ARG B 1 153 ? -20.534 58.604  -34.091 1.00 16.80 ? 258  ARG B CB  1 
ATOM   4538 C  CG  . ARG B 1 153 ? -21.222 59.836  -34.694 1.00 21.63 ? 258  ARG B CG  1 
ATOM   4539 C  CD  . ARG B 1 153 ? -22.277 60.311  -33.780 1.00 19.13 ? 258  ARG B CD  1 
ATOM   4540 N  NE  . ARG B 1 153 ? -23.395 59.327  -33.556 1.00 24.59 ? 258  ARG B NE  1 
ATOM   4541 C  CZ  . ARG B 1 153 ? -24.566 59.609  -32.938 1.00 26.29 ? 258  ARG B CZ  1 
ATOM   4542 N  NH1 . ARG B 1 153 ? -24.785 60.804  -32.413 1.00 24.58 ? 258  ARG B NH1 1 
ATOM   4543 N  NH2 . ARG B 1 153 ? -25.459 58.639  -32.752 1.00 23.38 ? 258  ARG B NH2 1 
ATOM   4544 N  N   . VAL B 1 154 ? -18.079 57.755  -31.482 1.00 12.43 ? 259  VAL B N   1 
ATOM   4545 C  CA  . VAL B 1 154 ? -17.314 56.604  -30.965 1.00 13.04 ? 259  VAL B CA  1 
ATOM   4546 C  C   . VAL B 1 154 ? -18.111 55.877  -29.916 1.00 10.79 ? 259  VAL B C   1 
ATOM   4547 O  O   . VAL B 1 154 ? -18.012 54.630  -29.848 1.00 12.18 ? 259  VAL B O   1 
ATOM   4548 C  CB  . VAL B 1 154 ? -15.949 57.021  -30.396 1.00 12.08 ? 259  VAL B CB  1 
ATOM   4549 C  CG1 . VAL B 1 154 ? -15.109 55.871  -29.800 1.00 14.17 ? 259  VAL B CG1 1 
ATOM   4550 C  CG2 . VAL B 1 154 ? -15.217 57.705  -31.612 1.00 15.80 ? 259  VAL B CG2 1 
ATOM   4551 N  N   . ALA B 1 155 ? -18.905 56.555  -29.085 1.00 12.06 ? 260  ALA B N   1 
ATOM   4552 C  CA  . ALA B 1 155 ? -19.639 55.833  -28.046 1.00 9.80  ? 260  ALA B CA  1 
ATOM   4553 C  C   . ALA B 1 155 ? -20.596 54.753  -28.561 1.00 11.04 ? 260  ALA B C   1 
ATOM   4554 O  O   . ALA B 1 155 ? -20.621 53.666  -27.985 1.00 9.93  ? 260  ALA B O   1 
ATOM   4555 C  CB  . ALA B 1 155 ? -20.380 56.863  -27.149 1.00 12.31 ? 260  ALA B CB  1 
ATOM   4556 N  N   . PRO B 1 156 ? -21.351 54.995  -29.656 1.00 10.10 ? 261  PRO B N   1 
ATOM   4557 C  CA  . PRO B 1 156 ? -22.239 53.909  -30.169 1.00 9.84  ? 261  PRO B CA  1 
ATOM   4558 C  C   . PRO B 1 156 ? -21.406 52.721  -30.618 1.00 9.88  ? 261  PRO B C   1 
ATOM   4559 O  O   . PRO B 1 156 ? -21.923 51.598  -30.499 1.00 9.31  ? 261  PRO B O   1 
ATOM   4560 C  CB  . PRO B 1 156 ? -22.964 54.541  -31.365 1.00 10.87 ? 261  PRO B CB  1 
ATOM   4561 C  CG  . PRO B 1 156 ? -23.075 56.032  -30.874 1.00 13.00 ? 261  PRO B CG  1 
ATOM   4562 C  CD  . PRO B 1 156 ? -21.698 56.342  -30.282 1.00 10.73 ? 261  PRO B CD  1 
ATOM   4563 N  N   . VAL B 1 157 ? -20.175 52.927  -31.112 1.00 9.22  ? 262  VAL B N   1 
ATOM   4564 C  CA  . VAL B 1 157 ? -19.355 51.754  -31.525 1.00 8.51  ? 262  VAL B CA  1 
ATOM   4565 C  C   . VAL B 1 157 ? -18.927 50.986  -30.254 1.00 8.66  ? 262  VAL B C   1 
ATOM   4566 O  O   . VAL B 1 157 ? -18.960 49.730  -30.266 1.00 8.54  ? 262  VAL B O   1 
ATOM   4567 C  CB  . VAL B 1 157 ? -18.141 52.201  -32.344 1.00 8.71  ? 262  VAL B CB  1 
ATOM   4568 C  CG1 . VAL B 1 157 ? -17.389 50.977  -32.872 1.00 10.32 ? 262  VAL B CG1 1 
ATOM   4569 C  CG2 . VAL B 1 157 ? -18.540 53.079  -33.563 1.00 10.99 ? 262  VAL B CG2 1 
ATOM   4570 N  N   . LEU B 1 158 ? -18.473 51.687  -29.192 1.00 8.45  ? 263  LEU B N   1 
ATOM   4571 C  CA  . LEU B 1 158 ? -18.171 51.008  -27.929 1.00 8.14  ? 263  LEU B CA  1 
ATOM   4572 C  C   . LEU B 1 158 ? -19.359 50.206  -27.440 1.00 7.55  ? 263  LEU B C   1 
ATOM   4573 O  O   . LEU B 1 158 ? -19.231 49.099  -26.943 1.00 8.40  ? 263  LEU B O   1 
ATOM   4574 C  CB  . LEU B 1 158 ? -17.722 52.022  -26.851 1.00 9.61  ? 263  LEU B CB  1 
ATOM   4575 C  CG  . LEU B 1 158 ? -16.235 52.429  -26.992 1.00 9.94  ? 263  LEU B CG  1 
ATOM   4576 C  CD1 . LEU B 1 158 ? -15.952 53.792  -26.317 1.00 11.51 ? 263  LEU B CD1 1 
ATOM   4577 C  CD2 . LEU B 1 158 ? -15.356 51.414  -26.182 1.00 11.31 ? 263  LEU B CD2 1 
ATOM   4578 N  N   . ILE B 1 159 ? -20.572 50.813  -27.526 1.00 8.27  ? 264  ILE B N   1 
ATOM   4579 C  CA  . ILE B 1 159 ? -21.747 50.133  -26.983 1.00 7.84  ? 264  ILE B CA  1 
ATOM   4580 C  C   . ILE B 1 159 ? -22.084 48.888  -27.829 1.00 8.29  ? 264  ILE B C   1 
ATOM   4581 O  O   . ILE B 1 159 ? -22.345 47.817  -27.255 1.00 8.84  ? 264  ILE B O   1 
ATOM   4582 C  CB  . ILE B 1 159 ? -22.968 51.117  -26.875 1.00 8.01  ? 264  ILE B CB  1 
ATOM   4583 C  CG1 . ILE B 1 159 ? -22.632 52.210  -25.834 1.00 8.73  ? 264  ILE B CG1 1 
ATOM   4584 C  CG2 . ILE B 1 159 ? -24.253 50.338  -26.545 1.00 9.15  ? 264  ILE B CG2 1 
ATOM   4585 C  CD1 . ILE B 1 159 ? -23.582 53.428  -25.963 1.00 9.51  ? 264  ILE B CD1 1 
ATOM   4586 N  N   . ARG B 1 160 ? -22.066 49.007  -29.142 1.00 7.84  ? 265  ARG B N   1 
ATOM   4587 C  CA  . ARG B 1 160 ? -22.312 47.831  -29.983 1.00 8.36  ? 265  ARG B CA  1 
ATOM   4588 C  C   . ARG B 1 160 ? -21.256 46.712  -29.786 1.00 7.76  ? 265  ARG B C   1 
ATOM   4589 O  O   . ARG B 1 160 ? -21.637 45.526  -29.753 1.00 8.26  ? 265  ARG B O   1 
ATOM   4590 C  CB  . ARG B 1 160 ? -22.370 48.155  -31.478 1.00 11.34 ? 265  ARG B CB  1 
ATOM   4591 C  CG  . ARG B 1 160 ? -23.525 49.009  -31.878 1.00 13.22 ? 265  ARG B CG  1 
ATOM   4592 C  CD  . ARG B 1 160 ? -23.543 49.178  -33.386 1.00 16.36 ? 265  ARG B CD  1 
ATOM   4593 N  NE  . ARG B 1 160 ? -22.523 49.960  -34.118 1.00 20.45 ? 265  ARG B NE  1 
ATOM   4594 C  CZ  . ARG B 1 160 ? -22.634 51.326  -34.273 1.00 20.19 ? 265  ARG B CZ  1 
ATOM   4595 N  NH1 . ARG B 1 160 ? -21.866 52.005  -35.109 1.00 20.80 ? 265  ARG B NH1 1 
ATOM   4596 N  NH2 . ARG B 1 160 ? -23.649 51.951  -33.687 1.00 20.75 ? 265  ARG B NH2 1 
ATOM   4597 N  N   . GLU B 1 161 ? -20.033 47.116  -29.603 1.00 7.79  ? 266  GLU B N   1 
ATOM   4598 C  CA  . GLU B 1 161 ? -18.972 46.096  -29.451 1.00 7.74  ? 266  GLU B CA  1 
ATOM   4599 C  C   . GLU B 1 161 ? -19.058 45.363  -28.126 1.00 7.92  ? 266  GLU B C   1 
ATOM   4600 O  O   . GLU B 1 161 ? -18.941 44.155  -28.081 1.00 8.38  ? 266  GLU B O   1 
ATOM   4601 C  CB  . GLU B 1 161 ? -17.616 46.783  -29.618 1.00 7.98  ? 266  GLU B CB  1 
ATOM   4602 C  CG  . GLU B 1 161 ? -16.426 45.787  -29.559 1.00 8.66  ? 266  GLU B CG  1 
ATOM   4603 C  CD  . GLU B 1 161 ? -16.402 44.689  -30.556 1.00 8.14  ? 266  GLU B CD  1 
ATOM   4604 O  OE1 . GLU B 1 161 ? -17.183 44.655  -31.534 1.00 8.94  ? 266  GLU B OE1 1 
ATOM   4605 O  OE2 . GLU B 1 161 ? -15.518 43.762  -30.306 1.00 9.44  ? 266  GLU B OE2 1 
ATOM   4606 N  N   . ILE B 1 162 ? -19.329 46.082  -27.011 1.00 7.62  ? 267  ILE B N   1 
ATOM   4607 C  CA  . ILE B 1 162 ? -19.487 45.399  -25.758 1.00 7.74  ? 267  ILE B CA  1 
ATOM   4608 C  C   . ILE B 1 162 ? -20.769 44.520  -25.824 1.00 7.15  ? 267  ILE B C   1 
ATOM   4609 O  O   . ILE B 1 162 ? -20.784 43.379  -25.287 1.00 7.73  ? 267  ILE B O   1 
ATOM   4610 C  CB  . ILE B 1 162 ? -19.473 46.303  -24.502 1.00 7.72  ? 267  ILE B CB  1 
ATOM   4611 C  CG1 . ILE B 1 162 ? -19.231 45.513  -23.185 1.00 8.30  ? 267  ILE B CG1 1 
ATOM   4612 C  CG2 . ILE B 1 162 ? -20.804 47.068  -24.312 1.00 9.32  ? 267  ILE B CG2 1 
ATOM   4613 C  CD1 . ILE B 1 162 ? -17.776 44.876  -23.159 1.00 10.98 ? 267  ILE B CD1 1 
ATOM   4614 N  N   . THR B 1 163 ? -21.799 44.974  -26.518 1.00 8.29  ? 268  THR B N   1 
ATOM   4615 C  CA  . THR B 1 163 ? -23.012 44.168  -26.661 1.00 7.64  ? 268  THR B CA  1 
ATOM   4616 C  C   . THR B 1 163 ? -22.686 42.869  -27.392 1.00 8.03  ? 268  THR B C   1 
ATOM   4617 O  O   . THR B 1 163 ? -23.107 41.777  -26.923 1.00 7.58  ? 268  THR B O   1 
ATOM   4618 C  CB  . THR B 1 163 ? -24.102 44.935  -27.461 1.00 7.56  ? 268  THR B CB  1 
ATOM   4619 O  OG1 . THR B 1 163 ? -24.493 46.135  -26.763 1.00 9.16  ? 268  THR B OG1 1 
ATOM   4620 C  CG2 . THR B 1 163 ? -25.314 44.071  -27.597 1.00 8.80  ? 268  THR B CG2 1 
ATOM   4621 N  N   . ARG B 1 164 ? -21.942 42.953  -28.486 1.00 8.00  ? 269  ARG B N   1 
ATOM   4622 C  CA  . ARG B 1 164 ? -21.569 41.728  -29.215 1.00 7.75  ? 269  ARG B CA  1 
ATOM   4623 C  C   . ARG B 1 164 ? -20.721 40.759  -28.334 1.00 7.84  ? 269  ARG B C   1 
ATOM   4624 O  O   . ARG B 1 164 ? -21.009 39.558  -28.354 1.00 7.93  ? 269  ARG B O   1 
ATOM   4625 C  CB  . ARG B 1 164 ? -20.759 42.229  -30.421 1.00 7.63  ? 269  ARG B CB  1 
ATOM   4626 C  CG  . ARG B 1 164 ? -20.439 41.112  -31.458 1.00 7.55  ? 269  ARG B CG  1 
ATOM   4627 C  CD  . ARG B 1 164 ? -19.400 41.643  -32.496 1.00 8.01  ? 269  ARG B CD  1 
ATOM   4628 N  NE  . ARG B 1 164 ? -18.081 41.848  -31.959 1.00 8.23  ? 269  ARG B NE  1 
ATOM   4629 C  CZ  . ARG B 1 164 ? -17.188 40.857  -31.792 1.00 8.10  ? 269  ARG B CZ  1 
ATOM   4630 N  NH1 . ARG B 1 164 ? -17.473 39.599  -32.160 1.00 8.88  ? 269  ARG B NH1 1 
ATOM   4631 N  NH2 . ARG B 1 164 ? -15.981 41.156  -31.319 1.00 9.23  ? 269  ARG B NH2 1 
ATOM   4632 N  N   . ARG B 1 165 ? -19.762 41.326  -27.574 1.00 7.63  ? 270  ARG B N   1 
ATOM   4633 C  CA  . ARG B 1 165 ? -18.944 40.444  -26.725 1.00 7.67  ? 270  ARG B CA  1 
ATOM   4634 C  C   . ARG B 1 165 ? -19.743 39.811  -25.602 1.00 7.28  ? 270  ARG B C   1 
ATOM   4635 O  O   . ARG B 1 165 ? -19.365 38.713  -25.148 1.00 9.02  ? 270  ARG B O   1 
ATOM   4636 C  CB  . ARG B 1 165 ? -17.802 41.279  -26.157 1.00 7.76  ? 270  ARG B CB  1 
ATOM   4637 C  CG  . ARG B 1 165 ? -16.808 41.774  -27.256 1.00 8.14  ? 270  ARG B CG  1 
ATOM   4638 C  CD  . ARG B 1 165 ? -15.677 42.602  -26.627 1.00 9.58  ? 270  ARG B CD  1 
ATOM   4639 N  NE  . ARG B 1 165 ? -14.831 43.148  -27.689 1.00 9.71  ? 270  ARG B NE  1 
ATOM   4640 C  CZ  . ARG B 1 165 ? -13.701 43.644  -27.521 1.00 10.78 ? 270  ARG B CZ  1 
ATOM   4641 N  NH1 . ARG B 1 165 ? -13.064 43.668  -26.336 1.00 14.44 ? 270  ARG B NH1 1 
ATOM   4642 N  NH2 . ARG B 1 165 ? -13.098 44.160  -28.588 1.00 15.00 ? 270  ARG B NH2 1 
ATOM   4643 N  N   . VAL B 1 166 ? -20.749 40.483  -25.090 1.00 7.19  ? 271  VAL B N   1 
ATOM   4644 C  CA  . VAL B 1 166 ? -21.637 39.876  -24.100 1.00 7.38  ? 271  VAL B CA  1 
ATOM   4645 C  C   . VAL B 1 166 ? -22.529 38.808  -24.717 1.00 7.59  ? 271  VAL B C   1 
ATOM   4646 O  O   . VAL B 1 166 ? -22.724 37.723  -24.178 1.00 7.60  ? 271  VAL B O   1 
ATOM   4647 C  CB  . VAL B 1 166 ? -22.427 41.055  -23.405 1.00 7.60  ? 271  VAL B CB  1 
ATOM   4648 C  CG1 . VAL B 1 166 ? -23.541 40.492  -22.498 1.00 8.13  ? 271  VAL B CG1 1 
ATOM   4649 C  CG2 . VAL B 1 166 ? -21.419 41.856  -22.569 1.00 8.15  ? 271  VAL B CG2 1 
ATOM   4650 N  N   . HIS B 1 167 ? -23.083 39.110  -25.922 1.00 7.74  ? 272  HIS B N   1 
ATOM   4651 C  CA  . HIS B 1 167 ? -23.927 38.097  -26.640 1.00 7.75  ? 272  HIS B CA  1 
ATOM   4652 C  C   . HIS B 1 167 ? -23.113 36.805  -26.895 1.00 7.79  ? 272  HIS B C   1 
ATOM   4653 O  O   . HIS B 1 167 ? -23.735 35.737  -26.800 1.00 8.48  ? 272  HIS B O   1 
ATOM   4654 C  CB  . HIS B 1 167 ? -24.302 38.713  -28.011 1.00 7.39  ? 272  HIS B CB  1 
ATOM   4655 C  CG  . HIS B 1 167 ? -25.443 39.680  -27.911 1.00 7.50  ? 272  HIS B CG  1 
ATOM   4656 N  ND1 . HIS B 1 167 ? -25.792 40.468  -29.006 1.00 8.54  ? 272  HIS B ND1 1 
ATOM   4657 C  CD2 . HIS B 1 167 ? -26.254 40.022  -26.887 1.00 8.07  ? 272  HIS B CD2 1 
ATOM   4658 C  CE1 . HIS B 1 167 ? -26.856 41.203  -28.651 1.00 8.44  ? 272  HIS B CE1 1 
ATOM   4659 N  NE2 . HIS B 1 167 ? -27.120 41.010  -27.369 1.00 8.11  ? 272  HIS B NE2 1 
ATOM   4660 N  N   . LEU B 1 168 ? -21.822 36.923  -27.184 1.00 7.82  ? 273  LEU B N   1 
ATOM   4661 C  CA  . LEU B 1 168 ? -21.031 35.676  -27.430 1.00 8.35  ? 273  LEU B CA  1 
ATOM   4662 C  C   . LEU B 1 168 ? -21.060 34.800  -26.225 1.00 8.28  ? 273  LEU B C   1 
ATOM   4663 O  O   . LEU B 1 168 ? -20.865 33.541  -26.368 1.00 8.80  ? 273  LEU B O   1 
ATOM   4664 C  CB  . LEU B 1 168 ? -19.625 36.088  -27.785 1.00 8.39  ? 273  LEU B CB  1 
ATOM   4665 C  CG  . LEU B 1 168 ? -19.414 36.669  -29.190 1.00 8.25  ? 273  LEU B CG  1 
ATOM   4666 C  CD1 . LEU B 1 168 ? -18.003 37.215  -29.309 1.00 10.94 ? 273  LEU B CD1 1 
ATOM   4667 C  CD2 . LEU B 1 168 ? -19.678 35.605  -30.276 1.00 9.58  ? 273  LEU B CD2 1 
ATOM   4668 N  N   . GLU B 1 169 ? -21.199 35.347  -24.994 1.00 8.07  ? 274  GLU B N   1 
ATOM   4669 C  CA  . GLU B 1 169 ? -21.252 34.566  -23.735 1.00 9.32  ? 274  GLU B CA  1 
ATOM   4670 C  C   . GLU B 1 169 ? -22.659 34.151  -23.393 1.00 9.54  ? 274  GLU B C   1 
ATOM   4671 O  O   . GLU B 1 169 ? -22.856 33.630  -22.266 1.00 11.16 ? 274  GLU B O   1 
ATOM   4672 C  CB  . GLU B 1 169 ? -20.624 35.326  -22.597 1.00 10.56 ? 274  GLU B CB  1 
ATOM   4673 C  CG  . GLU B 1 169 ? -19.168 35.737  -22.866 1.00 12.01 ? 274  GLU B CG  1 
ATOM   4674 C  CD  . GLU B 1 169 ? -18.207 34.585  -22.973 1.00 18.42 ? 274  GLU B CD  1 
ATOM   4675 O  OE1 . GLU B 1 169 ? -18.471 33.554  -22.233 1.00 18.16 ? 274  GLU B OE1 1 
ATOM   4676 O  OE2 . GLU B 1 169 ? -17.263 34.861  -23.760 1.00 22.57 ? 274  GLU B OE2 1 
ATOM   4677 N  N   . GLY B 1 170 ? -23.647 34.432  -24.246 1.00 9.62  ? 275  GLY B N   1 
ATOM   4678 C  CA  . GLY B 1 170 ? -24.990 33.873  -24.044 1.00 9.97  ? 275  GLY B CA  1 
ATOM   4679 C  C   . GLY B 1 170 ? -25.881 34.781  -23.201 1.00 10.38 ? 275  GLY B C   1 
ATOM   4680 O  O   . GLY B 1 170 ? -26.949 34.324  -22.754 1.00 11.81 ? 275  GLY B O   1 
ATOM   4681 N  N   . ILE B 1 171 ? -25.481 36.029  -22.947 1.00 8.50  ? 276  ILE B N   1 
ATOM   4682 C  CA  . ILE B 1 171 ? -26.232 36.991  -22.099 1.00 8.33  ? 276  ILE B CA  1 
ATOM   4683 C  C   . ILE B 1 171 ? -26.871 38.011  -23.038 1.00 7.85  ? 276  ILE B C   1 
ATOM   4684 O  O   . ILE B 1 171 ? -26.228 38.605  -23.882 1.00 8.31  ? 276  ILE B O   1 
ATOM   4685 C  CB  . ILE B 1 171 ? -25.263 37.606  -21.080 1.00 7.80  ? 276  ILE B CB  1 
ATOM   4686 C  CG1 . ILE B 1 171 ? -24.770 36.492  -20.108 1.00 10.13 ? 276  ILE B CG1 1 
ATOM   4687 C  CG2 . ILE B 1 171 ? -25.925 38.772  -20.302 1.00 9.30  ? 276  ILE B CG2 1 
ATOM   4688 C  CD1 . ILE B 1 171 ? -23.626 37.050  -19.194 1.00 12.73 ? 276  ILE B CD1 1 
ATOM   4689 N  N   . PHE B 1 172 ? -28.195 38.243  -22.784 1.00 8.36  ? 277  PHE B N   1 
ATOM   4690 C  CA  . PHE B 1 172 ? -28.955 39.070  -23.689 1.00 8.38  ? 277  PHE B CA  1 
ATOM   4691 C  C   . PHE B 1 172 ? -29.617 40.301  -23.012 1.00 8.31  ? 277  PHE B C   1 
ATOM   4692 O  O   . PHE B 1 172 ? -30.285 41.096  -23.711 1.00 8.51  ? 277  PHE B O   1 
ATOM   4693 C  CB  . PHE B 1 172 ? -29.974 38.236  -24.468 1.00 9.14  ? 277  PHE B CB  1 
ATOM   4694 C  CG  . PHE B 1 172 ? -29.275 37.303  -25.403 1.00 10.13 ? 277  PHE B CG  1 
ATOM   4695 C  CD1 . PHE B 1 172 ? -28.785 37.790  -26.591 1.00 11.07 ? 277  PHE B CD1 1 
ATOM   4696 C  CD2 . PHE B 1 172 ? -29.055 35.953  -25.005 1.00 11.10 ? 277  PHE B CD2 1 
ATOM   4697 C  CE1 . PHE B 1 172 ? -27.927 36.955  -27.406 1.00 12.68 ? 277  PHE B CE1 1 
ATOM   4698 C  CE2 . PHE B 1 172 ? -28.287 35.083  -25.896 1.00 11.55 ? 277  PHE B CE2 1 
ATOM   4699 C  CZ  . PHE B 1 172 ? -27.741 35.622  -27.057 1.00 12.37 ? 277  PHE B CZ  1 
ATOM   4700 N  N   . GLN B 1 173 ? -29.363 40.526  -21.756 1.00 7.90  ? 278  GLN B N   1 
ATOM   4701 C  CA  . GLN B 1 173 ? -29.891 41.729  -21.022 1.00 8.12  ? 278  GLN B CA  1 
ATOM   4702 C  C   . GLN B 1 173 ? -28.742 42.338  -20.255 1.00 8.24  ? 278  GLN B C   1 
ATOM   4703 O  O   . GLN B 1 173 ? -27.744 41.685  -19.829 1.00 8.94  ? 278  GLN B O   1 
ATOM   4704 C  CB  . GLN B 1 173 ? -30.972 41.337  -20.001 1.00 9.03  ? 278  GLN B CB  1 
ATOM   4705 C  CG  . GLN B 1 173 ? -32.402 41.139  -20.665 1.00 8.96  ? 278  GLN B CG  1 
ATOM   4706 C  CD  . GLN B 1 173 ? -32.562 39.780  -21.333 1.00 10.15 ? 278  GLN B CD  1 
ATOM   4707 O  OE1 . GLN B 1 173 ? -31.998 38.769  -20.850 1.00 11.38 ? 278  GLN B OE1 1 
ATOM   4708 N  NE2 . GLN B 1 173 ? -33.359 39.715  -22.425 1.00 10.02 ? 278  GLN B NE2 1 
ATOM   4709 N  N   . ALA B 1 174 ? -28.868 43.657  -20.065 1.00 9.02  ? 279  ALA B N   1 
ATOM   4710 C  CA  . ALA B 1 174 ? -27.925 44.468  -19.252 1.00 8.20  ? 279  ALA B CA  1 
ATOM   4711 C  C   . ALA B 1 174 ? -28.639 45.495  -18.387 1.00 8.78  ? 279  ALA B C   1 
ATOM   4712 O  O   . ALA B 1 174 ? -29.812 45.896  -18.732 1.00 9.08  ? 279  ALA B O   1 
ATOM   4713 C  CB  . ALA B 1 174 ? -26.884 45.205  -20.090 1.00 8.22  ? 279  ALA B CB  1 
ATOM   4714 N  N   . VAL B 1 175 ? -28.021 45.913  -17.314 1.00 8.52  ? 280  VAL B N   1 
ATOM   4715 C  CA  A VAL B 1 175 ? -28.530 47.052  -16.518 0.50 7.29  ? 280  VAL B CA  1 
ATOM   4716 C  CA  B VAL B 1 175 ? -28.504 47.078  -16.523 0.50 8.54  ? 280  VAL B CA  1 
ATOM   4717 C  C   . VAL B 1 175 ? -27.387 48.094  -16.521 1.00 8.07  ? 280  VAL B C   1 
ATOM   4718 O  O   . VAL B 1 175 ? -26.174 47.757  -16.583 1.00 9.29  ? 280  VAL B O   1 
ATOM   4719 C  CB  A VAL B 1 175 ? -28.921 46.542  -15.081 0.50 6.81  ? 280  VAL B CB  1 
ATOM   4720 C  CB  B VAL B 1 175 ? -28.728 46.688  -15.051 0.50 9.85  ? 280  VAL B CB  1 
ATOM   4721 C  CG1 A VAL B 1 175 ? -27.666 46.033  -14.332 0.50 5.29  ? 280  VAL B CG1 1 
ATOM   4722 C  CG1 B VAL B 1 175 ? -29.126 47.915  -14.228 0.50 11.77 ? 280  VAL B CG1 1 
ATOM   4723 C  CG2 A VAL B 1 175 ? -29.704 47.662  -14.325 0.50 7.65  ? 280  VAL B CG2 1 
ATOM   4724 C  CG2 B VAL B 1 175 ? -29.823 45.698  -14.963 0.50 11.92 ? 280  VAL B CG2 1 
ATOM   4725 N  N   . TYR B 1 176 ? -27.806 49.365  -16.549 1.00 8.64  ? 281  TYR B N   1 
ATOM   4726 C  CA  . TYR B 1 176 ? -26.795 50.430  -16.545 1.00 9.58  ? 281  TYR B CA  1 
ATOM   4727 C  C   . TYR B 1 176 ? -27.398 51.682  -15.943 1.00 10.22 ? 281  TYR B C   1 
ATOM   4728 O  O   . TYR B 1 176 ? -28.675 51.830  -15.943 1.00 10.49 ? 281  TYR B O   1 
ATOM   4729 C  CB  . TYR B 1 176 ? -26.273 50.735  -17.972 1.00 10.87 ? 281  TYR B CB  1 
ATOM   4730 C  CG  . TYR B 1 176 ? -27.311 50.877  -19.084 1.00 10.06 ? 281  TYR B CG  1 
ATOM   4731 C  CD1 . TYR B 1 176 ? -27.583 52.108  -19.672 1.00 10.30 ? 281  TYR B CD1 1 
ATOM   4732 C  CD2 . TYR B 1 176 ? -27.952 49.730  -19.609 1.00 11.90 ? 281  TYR B CD2 1 
ATOM   4733 C  CE1 . TYR B 1 176 ? -28.508 52.216  -20.682 1.00 10.89 ? 281  TYR B CE1 1 
ATOM   4734 C  CE2 . TYR B 1 176 ? -28.878 49.846  -20.595 1.00 11.51 ? 281  TYR B CE2 1 
ATOM   4735 C  CZ  . TYR B 1 176 ? -29.160 51.084  -21.156 1.00 12.36 ? 281  TYR B CZ  1 
ATOM   4736 O  OH  . TYR B 1 176 ? -30.096 51.207  -22.160 1.00 12.50 ? 281  TYR B OH  1 
ATOM   4737 N  N   . THR B 1 177 ? -26.543 52.602  -15.528 1.00 10.08 ? 282  THR B N   1 
ATOM   4738 C  CA  . THR B 1 177 ? -27.044 53.914  -14.996 1.00 11.02 ? 282  THR B CA  1 
ATOM   4739 C  C   . THR B 1 177 ? -26.339 54.974  -15.803 1.00 11.75 ? 282  THR B C   1 
ATOM   4740 O  O   . THR B 1 177 ? -25.184 54.733  -16.348 1.00 13.18 ? 282  THR B O   1 
ATOM   4741 C  CB  . THR B 1 177 ? -26.735 54.122  -13.530 1.00 12.34 ? 282  THR B CB  1 
ATOM   4742 O  OG1 . THR B 1 177 ? -25.307 54.127  -13.247 1.00 12.48 ? 282  THR B OG1 1 
ATOM   4743 C  CG2 . THR B 1 177 ? -27.416 53.109  -12.616 1.00 12.09 ? 282  THR B CG2 1 
ATOM   4744 N  N   . ALA B 1 178 ? -26.947 56.170  -15.935 1.00 11.27 ? 283  ALA B N   1 
ATOM   4745 C  CA  . ALA B 1 178 ? -26.310 57.294  -16.623 1.00 12.61 ? 283  ALA B CA  1 
ATOM   4746 C  C   . ALA B 1 178 ? -26.967 58.610  -16.105 1.00 13.12 ? 283  ALA B C   1 
ATOM   4747 O  O   . ALA B 1 178 ? -28.157 58.574  -15.670 1.00 12.70 ? 283  ALA B O   1 
ATOM   4748 C  CB  . ALA B 1 178 ? -26.391 57.225  -18.126 1.00 13.88 ? 283  ALA B CB  1 
ATOM   4749 N  N   . GLY B 1 179 ? -26.216 59.710  -16.176 1.00 13.61 ? 284  GLY B N   1 
ATOM   4750 C  CA  . GLY B 1 179 ? -26.834 61.025  -15.788 1.00 13.23 ? 284  GLY B CA  1 
ATOM   4751 C  C   . GLY B 1 179 ? -27.591 61.595  -16.924 1.00 15.63 ? 284  GLY B C   1 
ATOM   4752 O  O   . GLY B 1 179 ? -28.328 62.623  -16.650 1.00 25.25 ? 284  GLY B O   1 
ATOM   4753 N  N   . VAL B 1 180 ? -27.601 61.056  -18.148 1.00 14.02 ? 285  VAL B N   1 
ATOM   4754 C  CA  . VAL B 1 180 ? -28.388 61.665  -19.259 1.00 15.66 ? 285  VAL B CA  1 
ATOM   4755 C  C   . VAL B 1 180 ? -29.640 60.839  -19.474 1.00 15.49 ? 285  VAL B C   1 
ATOM   4756 O  O   . VAL B 1 180 ? -29.708 59.649  -19.131 1.00 14.44 ? 285  VAL B O   1 
ATOM   4757 C  CB  . VAL B 1 180 ? -27.524 61.715  -20.553 1.00 20.05 ? 285  VAL B CB  1 
ATOM   4758 C  CG1 . VAL B 1 180 ? -26.424 62.697  -20.383 1.00 21.18 ? 285  VAL B CG1 1 
ATOM   4759 C  CG2 . VAL B 1 180 ? -26.907 60.365  -20.933 1.00 18.14 ? 285  VAL B CG2 1 
ATOM   4760 N  N   . VAL B 1 181 ? -30.650 61.451  -20.110 1.00 14.87 ? 286  VAL B N   1 
ATOM   4761 C  CA  . VAL B 1 181 ? -31.882 60.772  -20.446 1.00 14.62 ? 286  VAL B CA  1 
ATOM   4762 C  C   . VAL B 1 181 ? -31.737 60.117  -21.817 1.00 14.87 ? 286  VAL B C   1 
ATOM   4763 O  O   . VAL B 1 181 ? -31.355 60.811  -22.858 1.00 16.84 ? 286  VAL B O   1 
ATOM   4764 C  CB  . VAL B 1 181 ? -33.023 61.813  -20.549 1.00 15.89 ? 286  VAL B CB  1 
ATOM   4765 C  CG1 . VAL B 1 181 ? -34.306 61.157  -21.028 1.00 17.63 ? 286  VAL B CG1 1 
ATOM   4766 C  CG2 . VAL B 1 181 ? -33.226 62.538  -19.215 1.00 20.92 ? 286  VAL B CG2 1 
ATOM   4767 N  N   . LEU B 1 182 ? -31.996 58.823  -21.828 1.00 13.69 ? 287  LEU B N   1 
ATOM   4768 C  CA  . LEU B 1 182 ? -31.965 57.996  -23.049 1.00 13.48 ? 287  LEU B CA  1 
ATOM   4769 C  C   . LEU B 1 182 ? -33.274 57.180  -23.049 1.00 13.99 ? 287  LEU B C   1 
ATOM   4770 O  O   . LEU B 1 182 ? -33.950 57.009  -22.036 1.00 13.83 ? 287  LEU B O   1 
ATOM   4771 C  CB  . LEU B 1 182 ? -30.793 56.971  -22.891 1.00 14.60 ? 287  LEU B CB  1 
ATOM   4772 C  CG  . LEU B 1 182 ? -29.467 57.558  -22.596 1.00 14.38 ? 287  LEU B CG  1 
ATOM   4773 C  CD1 . LEU B 1 182 ? -28.538 56.413  -22.145 1.00 14.23 ? 287  LEU B CD1 1 
ATOM   4774 C  CD2 . LEU B 1 182 ? -28.869 58.373  -23.753 1.00 14.96 ? 287  LEU B CD2 1 
ATOM   4775 N  N   . PRO B 1 183 ? -33.674 56.562  -24.201 1.00 13.33 ? 288  PRO B N   1 
ATOM   4776 C  CA  . PRO B 1 183 ? -34.777 55.660  -24.208 1.00 13.00 ? 288  PRO B CA  1 
ATOM   4777 C  C   . PRO B 1 183 ? -34.413 54.363  -23.415 1.00 13.55 ? 288  PRO B C   1 
ATOM   4778 O  O   . PRO B 1 183 ? -33.417 53.723  -23.757 1.00 14.55 ? 288  PRO B O   1 
ATOM   4779 C  CB  . PRO B 1 183 ? -35.018 55.343  -25.737 1.00 14.10 ? 288  PRO B CB  1 
ATOM   4780 C  CG  . PRO B 1 183 ? -34.247 56.443  -26.416 1.00 16.02 ? 288  PRO B CG  1 
ATOM   4781 C  CD  . PRO B 1 183 ? -33.089 56.768  -25.541 1.00 14.66 ? 288  PRO B CD  1 
ATOM   4782 N  N   . LYS B 1 184 ? -35.162 53.967  -22.394 1.00 12.46 ? 289  LYS B N   1 
ATOM   4783 C  CA  A LYS B 1 184 ? -36.150 54.752  -21.576 0.50 14.05 ? 289  LYS B CA  1 
ATOM   4784 C  CA  B LYS B 1 184 ? -36.127 54.758  -21.578 0.50 14.06 ? 289  LYS B CA  1 
ATOM   4785 C  C   . LYS B 1 184 ? -35.875 54.355  -20.093 1.00 13.55 ? 289  LYS B C   1 
ATOM   4786 O  O   . LYS B 1 184 ? -35.701 53.176  -19.786 1.00 12.63 ? 289  LYS B O   1 
ATOM   4787 C  CB  A LYS B 1 184 ? -37.577 54.290  -21.922 0.50 17.06 ? 289  LYS B CB  1 
ATOM   4788 C  CB  B LYS B 1 184 ? -37.537 54.308  -21.933 0.50 17.09 ? 289  LYS B CB  1 
ATOM   4789 C  CG  A LYS B 1 184 ? -38.707 54.943  -21.070 0.50 20.95 ? 289  LYS B CG  1 
ATOM   4790 C  CG  B LYS B 1 184 ? -38.630 54.999  -21.096 0.50 21.29 ? 289  LYS B CG  1 
ATOM   4791 C  CD  A LYS B 1 184 ? -40.009 54.106  -21.072 0.50 24.53 ? 289  LYS B CD  1 
ATOM   4792 C  CD  B LYS B 1 184 ? -39.922 54.205  -21.195 0.50 25.02 ? 289  LYS B CD  1 
ATOM   4793 C  CE  A LYS B 1 184 ? -41.078 54.580  -20.038 0.50 26.56 ? 289  LYS B CE  1 
ATOM   4794 C  CE  B LYS B 1 184 ? -41.035 54.826  -20.343 0.50 29.41 ? 289  LYS B CE  1 
ATOM   4795 N  NZ  A LYS B 1 184 ? -42.192 53.564  -19.694 0.50 23.17 ? 289  LYS B NZ  1 
ATOM   4796 N  NZ  B LYS B 1 184 ? -40.817 56.287  -20.128 0.50 28.99 ? 289  LYS B NZ  1 
ATOM   4797 N  N   . PRO B 1 185 ? -35.820 55.371  -19.198 1.00 11.99 ? 290  PRO B N   1 
ATOM   4798 C  CA  . PRO B 1 185 ? -35.478 54.991  -17.805 1.00 10.64 ? 290  PRO B CA  1 
ATOM   4799 C  C   . PRO B 1 185 ? -36.476 54.075  -17.194 1.00 12.15 ? 290  PRO B C   1 
ATOM   4800 O  O   . PRO B 1 185 ? -37.714 54.228  -17.387 1.00 13.13 ? 290  PRO B O   1 
ATOM   4801 C  CB  . PRO B 1 185 ? -35.459 56.307  -17.063 1.00 12.79 ? 290  PRO B CB  1 
ATOM   4802 C  CG  . PRO B 1 185 ? -35.134 57.365  -18.113 1.00 13.09 ? 290  PRO B CG  1 
ATOM   4803 C  CD  . PRO B 1 185 ? -35.907 56.851  -19.362 1.00 12.46 ? 290  PRO B CD  1 
ATOM   4804 N  N   . VAL B 1 186 ? -36.027 53.053  -16.474 1.00 10.75 ? 291  VAL B N   1 
ATOM   4805 C  CA  . VAL B 1 186 ? -36.930 52.261  -15.638 1.00 11.03 ? 291  VAL B CA  1 
ATOM   4806 C  C   . VAL B 1 186 ? -37.087 52.931  -14.244 1.00 10.82 ? 291  VAL B C   1 
ATOM   4807 O  O   . VAL B 1 186 ? -37.998 52.544  -13.475 1.00 13.55 ? 291  VAL B O   1 
ATOM   4808 C  CB  . VAL B 1 186 ? -36.384 50.810  -15.458 1.00 12.36 ? 291  VAL B CB  1 
ATOM   4809 C  CG1 . VAL B 1 186 ? -35.044 50.732  -14.659 1.00 14.19 ? 291  VAL B CG1 1 
ATOM   4810 C  CG2 . VAL B 1 186 ? -37.389 49.830  -14.981 1.00 14.63 ? 291  VAL B CG2 1 
ATOM   4811 N  N   . GLY B 1 187 ? -36.150 53.797  -13.887 1.00 10.41 ? 292  GLY B N   1 
ATOM   4812 C  CA  . GLY B 1 187 ? -36.296 54.549  -12.634 1.00 11.55 ? 292  GLY B CA  1 
ATOM   4813 C  C   . GLY B 1 187 ? -35.387 55.739  -12.693 1.00 11.14 ? 292  GLY B C   1 
ATOM   4814 O  O   . GLY B 1 187 ? -34.395 55.773  -13.428 1.00 11.83 ? 292  GLY B O   1 
ATOM   4815 N  N   . THR B 1 188 ? -35.778 56.808  -11.927 1.00 10.74 ? 293  THR B N   1 
ATOM   4816 C  CA  . THR B 1 188 ? -35.009 58.047  -11.927 1.00 11.50 ? 293  THR B CA  1 
ATOM   4817 C  C   . THR B 1 188 ? -34.726 58.458  -10.481 1.00 11.15 ? 293  THR B C   1 
ATOM   4818 O  O   . THR B 1 188 ? -35.678 58.661  -9.704  1.00 12.23 ? 293  THR B O   1 
ATOM   4819 C  CB  . THR B 1 188 ? -35.830 59.226  -12.566 1.00 10.88 ? 293  THR B CB  1 
ATOM   4820 O  OG1 . THR B 1 188 ? -36.103 58.821  -13.957 1.00 12.69 ? 293  THR B OG1 1 
ATOM   4821 C  CG2 . THR B 1 188 ? -35.063 60.451  -12.566 1.00 12.26 ? 293  THR B CG2 1 
ATOM   4822 N  N   . CYS B 1 189 ? -33.479 58.602  -10.131 1.00 10.96 ? 294  CYS B N   1 
ATOM   4823 C  CA  . CYS B 1 189 ? -33.066 58.921  -8.765  1.00 11.15 ? 294  CYS B CA  1 
ATOM   4824 C  C   . CYS B 1 189 ? -32.377 60.276  -8.694  1.00 13.33 ? 294  CYS B C   1 
ATOM   4825 O  O   . CYS B 1 189 ? -31.749 60.749  -9.693  1.00 18.06 ? 294  CYS B O   1 
ATOM   4826 C  CB  . CYS B 1 189 ? -32.025 57.865  -8.309  1.00 13.79 ? 294  CYS B CB  1 
ATOM   4827 S  SG  . CYS B 1 189 ? -32.798 56.280  -8.055  1.00 15.66 ? 294  CYS B SG  1 
ATOM   4828 N  N   . ARG B 1 190 ? -32.652 61.046  -7.668  1.00 11.47 ? 295  ARG B N   1 
ATOM   4829 C  CA  . ARG B 1 190 ? -31.876 62.220  -7.398  1.00 12.56 ? 295  ARG B CA  1 
ATOM   4830 C  C   . ARG B 1 190 ? -30.741 61.935  -6.406  1.00 11.74 ? 295  ARG B C   1 
ATOM   4831 O  O   . ARG B 1 190 ? -30.953 61.176  -5.392  1.00 12.69 ? 295  ARG B O   1 
ATOM   4832 C  CB  . ARG B 1 190 ? -32.763 63.332  -6.722  1.00 14.00 ? 295  ARG B CB  1 
ATOM   4833 C  CG  . ARG B 1 190 ? -33.815 63.900  -7.647  1.00 17.27 ? 295  ARG B CG  1 
ATOM   4834 C  CD  . ARG B 1 190 ? -33.221 64.916  -8.637  1.00 17.20 ? 295  ARG B CD  1 
ATOM   4835 N  NE  . ARG B 1 190 ? -32.702 66.198  -8.117  1.00 18.78 ? 295  ARG B NE  1 
ATOM   4836 C  CZ  . ARG B 1 190 ? -33.412 67.325  -7.986  1.00 21.75 ? 295  ARG B CZ  1 
ATOM   4837 N  NH1 . ARG B 1 190 ? -34.721 67.271  -8.187  1.00 20.18 ? 295  ARG B NH1 1 
ATOM   4838 N  NH2 . ARG B 1 190 ? -32.832 68.484  -7.597  1.00 21.96 ? 295  ARG B NH2 1 
ATOM   4839 N  N   . TYR B 1 191 ? -29.627 62.577  -6.555  1.00 10.85 ? 296  TYR B N   1 
ATOM   4840 C  CA  . TYR B 1 191 ? -28.570 62.501  -5.553  1.00 11.23 ? 296  TYR B CA  1 
ATOM   4841 C  C   . TYR B 1 191 ? -28.601 63.691  -4.577  1.00 11.71 ? 296  TYR B C   1 
ATOM   4842 O  O   . TYR B 1 191 ? -29.073 64.803  -4.970  1.00 12.53 ? 296  TYR B O   1 
ATOM   4843 C  CB  . TYR B 1 191 ? -27.152 62.353  -6.198  1.00 10.82 ? 296  TYR B CB  1 
ATOM   4844 C  CG  . TYR B 1 191 ? -26.902 63.159  -7.444  1.00 11.82 ? 296  TYR B CG  1 
ATOM   4845 C  CD1 . TYR B 1 191 ? -26.477 64.483  -7.397  1.00 14.33 ? 296  TYR B CD1 1 
ATOM   4846 C  CD2 . TYR B 1 191 ? -27.074 62.522  -8.714  1.00 12.99 ? 296  TYR B CD2 1 
ATOM   4847 C  CE1 . TYR B 1 191 ? -26.214 65.227  -8.610  1.00 15.75 ? 296  TYR B CE1 1 
ATOM   4848 C  CE2 . TYR B 1 191 ? -26.820 63.222  -9.909  1.00 15.02 ? 296  TYR B CE2 1 
ATOM   4849 C  CZ  . TYR B 1 191 ? -26.419 64.520  -9.832  1.00 14.92 ? 296  TYR B CZ  1 
ATOM   4850 O  OH  . TYR B 1 191 ? -26.124 65.209  -11.030 1.00 19.77 ? 296  TYR B OH  1 
ATOM   4851 N  N   . TRP B 1 192 ? -28.224 63.413  -3.352  1.00 10.55 ? 297  TRP B N   1 
ATOM   4852 C  CA  . TRP B 1 192 ? -28.184 64.357  -2.241  1.00 10.09 ? 297  TRP B CA  1 
ATOM   4853 C  C   . TRP B 1 192 ? -26.840 64.301  -1.614  1.00 10.66 ? 297  TRP B C   1 
ATOM   4854 O  O   . TRP B 1 192 ? -26.053 63.342  -1.738  1.00 10.78 ? 297  TRP B O   1 
ATOM   4855 C  CB  . TRP B 1 192 ? -29.256 63.919  -1.212  1.00 10.82 ? 297  TRP B CB  1 
ATOM   4856 C  CG  . TRP B 1 192 ? -30.672 64.062  -1.609  1.00 11.32 ? 297  TRP B CG  1 
ATOM   4857 C  CD1 . TRP B 1 192 ? -31.321 63.367  -2.617  1.00 12.00 ? 297  TRP B CD1 1 
ATOM   4858 C  CD2 . TRP B 1 192 ? -31.666 64.852  -0.932  1.00 12.19 ? 297  TRP B CD2 1 
ATOM   4859 N  NE1 . TRP B 1 192 ? -32.697 63.725  -2.612  1.00 12.62 ? 297  TRP B NE1 1 
ATOM   4860 C  CE2 . TRP B 1 192 ? -32.896 64.629  -1.571  1.00 12.27 ? 297  TRP B CE2 1 
ATOM   4861 C  CE3 . TRP B 1 192 ? -31.575 65.719  0.188   1.00 12.98 ? 297  TRP B CE3 1 
ATOM   4862 C  CZ2 . TRP B 1 192 ? -34.150 65.286  -1.157  1.00 13.04 ? 297  TRP B CZ2 1 
ATOM   4863 C  CZ3 . TRP B 1 192 ? -32.768 66.438  0.589   1.00 13.52 ? 297  TRP B CZ3 1 
ATOM   4864 C  CH2 . TRP B 1 192 ? -34.035 66.153  -0.059  1.00 13.27 ? 297  TRP B CH2 1 
ATOM   4865 N  N   . HIS B 1 193 ? -26.462 65.347  -0.871  1.00 11.22 ? 298  HIS B N   1 
ATOM   4866 C  CA  . HIS B 1 193 ? -25.163 65.460  -0.207  1.00 11.05 ? 298  HIS B CA  1 
ATOM   4867 C  C   . HIS B 1 193 ? -25.347 65.848  1.253   1.00 11.00 ? 298  HIS B C   1 
ATOM   4868 O  O   . HIS B 1 193 ? -26.294 66.616  1.598   1.00 12.84 ? 298  HIS B O   1 
ATOM   4869 C  CB  . HIS B 1 193 ? -24.225 66.478  -0.891  1.00 12.20 ? 298  HIS B CB  1 
ATOM   4870 C  CG  . HIS B 1 193 ? -24.898 67.771  -1.168  1.00 13.67 ? 298  HIS B CG  1 
ATOM   4871 N  ND1 . HIS B 1 193 ? -25.463 68.101  -2.383  1.00 15.57 ? 298  HIS B ND1 1 
ATOM   4872 C  CD2 . HIS B 1 193 ? -25.173 68.810  -0.335  1.00 16.73 ? 298  HIS B CD2 1 
ATOM   4873 C  CE1 . HIS B 1 193 ? -26.026 69.299  -2.287  1.00 16.72 ? 298  HIS B CE1 1 
ATOM   4874 N  NE2 . HIS B 1 193 ? -25.881 69.733  -1.063  1.00 18.73 ? 298  HIS B NE2 1 
ATOM   4875 N  N   . ARG B 1 194 ? -24.432 65.410  2.110   1.00 11.35 ? 299  ARG B N   1 
ATOM   4876 C  CA  . ARG B 1 194 ? -24.435 65.820  3.554   1.00 10.90 ? 299  ARG B CA  1 
ATOM   4877 C  C   . ARG B 1 194 ? -23.061 66.320  3.845   1.00 11.17 ? 299  ARG B C   1 
ATOM   4878 O  O   . ARG B 1 194 ? -22.041 65.648  3.800   1.00 11.44 ? 299  ARG B O   1 
ATOM   4879 C  CB  . ARG B 1 194 ? -24.790 64.601  4.447   1.00 10.54 ? 299  ARG B CB  1 
ATOM   4880 C  CG  . ARG B 1 194 ? -25.542 65.038  5.746   1.00 10.96 ? 299  ARG B CG  1 
ATOM   4881 C  CD  . ARG B 1 194 ? -24.627 65.718  6.778   1.00 12.45 ? 299  ARG B CD  1 
ATOM   4882 N  NE  . ARG B 1 194 ? -25.288 65.937  8.004   1.00 11.67 ? 299  ARG B NE  1 
ATOM   4883 C  CZ  . ARG B 1 194 ? -24.741 66.520  9.096   1.00 11.74 ? 299  ARG B CZ  1 
ATOM   4884 N  NH1 . ARG B 1 194 ? -23.522 66.988  9.059   1.00 11.95 ? 299  ARG B NH1 1 
ATOM   4885 N  NH2 . ARG B 1 194 ? -25.512 66.609  10.203  1.00 13.88 ? 299  ARG B NH2 1 
ATOM   4886 N  N   A SER B 1 195 ? -23.003 67.624  4.222   0.50 12.30 ? 300  SER B N   1 
ATOM   4887 N  N   B SER B 1 195 ? -23.019 67.611  4.240   0.50 12.84 ? 300  SER B N   1 
ATOM   4888 C  CA  A SER B 1 195 ? -21.732 68.256  4.567   0.50 12.38 ? 300  SER B CA  1 
ATOM   4889 C  CA  B SER B 1 195 ? -21.764 68.253  4.568   0.50 13.24 ? 300  SER B CA  1 
ATOM   4890 C  C   A SER B 1 195 ? -21.120 67.680  5.820   0.50 12.52 ? 300  SER B C   1 
ATOM   4891 C  C   B SER B 1 195 ? -21.123 67.681  5.824   0.50 13.09 ? 300  SER B C   1 
ATOM   4892 O  O   A SER B 1 195 ? -21.785 67.597  6.855   0.50 12.45 ? 300  SER B O   1 
ATOM   4893 O  O   B SER B 1 195 ? -21.776 67.591  6.865   0.50 13.04 ? 300  SER B O   1 
ATOM   4894 C  CB  A SER B 1 195 ? -21.981 69.768  4.816   0.50 12.98 ? 300  SER B CB  1 
ATOM   4895 C  CB  B SER B 1 195 ? -22.058 69.754  4.804   0.50 14.67 ? 300  SER B CB  1 
ATOM   4896 O  OG  A SER B 1 195 ? -22.372 70.395  3.626   0.50 12.01 ? 300  SER B OG  1 
ATOM   4897 O  OG  B SER B 1 195 ? -20.851 70.420  5.098   0.50 15.24 ? 300  SER B OG  1 
ATOM   4898 N  N   . LEU B 1 196 ? -19.845 67.301  5.734   1.00 13.11 ? 301  LEU B N   1 
ATOM   4899 C  CA  . LEU B 1 196 ? -19.073 66.812  6.879   1.00 13.52 ? 301  LEU B CA  1 
ATOM   4900 C  C   . LEU B 1 196 ? -18.030 67.862  7.229   1.00 14.76 ? 301  LEU B C   1 
ATOM   4901 O  O   . LEU B 1 196 ? -17.788 68.043  8.492   1.00 16.71 ? 301  LEU B O   1 
ATOM   4902 C  CB  . LEU B 1 196 ? -18.418 65.444  6.588   1.00 14.17 ? 301  LEU B CB  1 
ATOM   4903 C  CG  . LEU B 1 196 ? -19.366 64.336  6.108   1.00 12.81 ? 301  LEU B CG  1 
ATOM   4904 C  CD1 . LEU B 1 196 ? -18.541 63.086  5.718   1.00 13.77 ? 301  LEU B CD1 1 
ATOM   4905 C  CD2 . LEU B 1 196 ? -20.501 64.016  7.140   1.00 14.70 ? 301  LEU B CD2 1 
ATOM   4906 N  N   . ASN B 1 197 ? -17.380 68.501  6.249   1.00 15.07 ? 302  ASN B N   1 
ATOM   4907 C  CA  . ASN B 1 197 ? -16.361 69.549  6.539   1.00 16.38 ? 302  ASN B CA  1 
ATOM   4908 C  C   . ASN B 1 197 ? -16.782 70.764  5.775   1.00 16.01 ? 302  ASN B C   1 
ATOM   4909 O  O   . ASN B 1 197 ? -16.279 71.011  4.681   1.00 16.55 ? 302  ASN B O   1 
ATOM   4910 C  CB  . ASN B 1 197 ? -15.027 69.030  6.081   1.00 18.08 ? 302  ASN B CB  1 
ATOM   4911 C  CG  . ASN B 1 197 ? -13.848 69.920  6.427   1.00 25.07 ? 302  ASN B CG  1 
ATOM   4912 O  OD1 . ASN B 1 197 ? -14.004 71.101  6.731   1.00 26.16 ? 302  ASN B OD1 1 
ATOM   4913 N  ND2 . ASN B 1 197 ? -12.665 69.378  6.258   1.00 28.08 ? 302  ASN B ND2 1 
ATOM   4914 N  N   . PRO B 1 198 ? -17.753 71.549  6.292   1.00 15.24 ? 303  PRO B N   1 
ATOM   4915 C  CA  . PRO B 1 198 ? -18.327 72.685  5.560   1.00 17.55 ? 303  PRO B CA  1 
ATOM   4916 C  C   . PRO B 1 198 ? -17.200 73.721  5.227   1.00 18.40 ? 303  PRO B C   1 
ATOM   4917 O  O   . PRO B 1 198 ? -17.338 74.358  4.169   1.00 18.96 ? 303  PRO B O   1 
ATOM   4918 C  CB  . PRO B 1 198 ? -19.450 73.287  6.499   1.00 20.75 ? 303  PRO B CB  1 
ATOM   4919 C  CG  . PRO B 1 198 ? -19.193 72.572  7.788   1.00 19.76 ? 303  PRO B CG  1 
ATOM   4920 C  CD  . PRO B 1 198 ? -18.408 71.314  7.596   1.00 18.72 ? 303  PRO B CD  1 
ATOM   4921 N  N   . ARG B 1 199 ? -16.218 73.912  6.114   1.00 19.79 ? 304  ARG B N   1 
ATOM   4922 C  CA  . ARG B 1 199 ? -15.193 74.949  5.797   1.00 23.72 ? 304  ARG B CA  1 
ATOM   4923 C  C   . ARG B 1 199 ? -14.491 74.545  4.464   1.00 22.41 ? 304  ARG B C   1 
ATOM   4924 O  O   . ARG B 1 199 ? -14.383 75.391  3.576   1.00 21.22 ? 304  ARG B O   1 
ATOM   4925 C  CB  . ARG B 1 199 ? -14.193 75.125  6.927   1.00 28.47 ? 304  ARG B CB  1 
ATOM   4926 C  CG  . ARG B 1 199 ? -13.047 76.086  6.572   1.00 39.45 ? 304  ARG B CG  1 
ATOM   4927 C  CD  . ARG B 1 199 ? -11.935 76.007  7.616   1.00 48.72 ? 304  ARG B CD  1 
ATOM   4928 N  NE  . ARG B 1 199 ? -12.333 76.865  8.735   1.00 62.45 ? 304  ARG B NE  1 
ATOM   4929 C  CZ  . ARG B 1 199 ? -12.115 76.610  10.015  1.00 64.66 ? 304  ARG B CZ  1 
ATOM   4930 N  NH1 . ARG B 1 199 ? -11.507 75.479  10.389  1.00 64.92 ? 304  ARG B NH1 1 
ATOM   4931 N  NH2 . ARG B 1 199 ? -12.527 77.500  10.913  1.00 62.34 ? 304  ARG B NH2 1 
ATOM   4932 N  N   . LYS B 1 200 ? -14.088 73.264  4.323   1.00 20.87 ? 305  LYS B N   1 
ATOM   4933 C  CA  . LYS B 1 200 ? -13.480 72.820  3.068   1.00 22.35 ? 305  LYS B CA  1 
ATOM   4934 C  C   . LYS B 1 200 ? -14.491 72.894  1.894   1.00 18.75 ? 305  LYS B C   1 
ATOM   4935 O  O   . LYS B 1 200 ? -14.121 73.301  0.766   1.00 21.43 ? 305  LYS B O   1 
ATOM   4936 C  CB  . LYS B 1 200 ? -12.849 71.451  3.232   1.00 24.22 ? 305  LYS B CB  1 
ATOM   4937 C  CG  . LYS B 1 200 ? -12.466 70.807  1.879   1.00 28.11 ? 305  LYS B CG  1 
ATOM   4938 C  CD  . LYS B 1 200 ? -11.113 70.170  1.779   1.00 32.84 ? 305  LYS B CD  1 
ATOM   4939 C  CE  . LYS B 1 200 ? -10.942 69.506  0.372   1.00 26.32 ? 305  LYS B CE  1 
ATOM   4940 N  NZ  . LYS B 1 200 ? -10.452 68.092  0.561   1.00 31.39 ? 305  LYS B NZ  1 
ATOM   4941 N  N   . LEU B 1 201 ? -15.726 72.463  2.079   1.00 17.74 ? 306  LEU B N   1 
ATOM   4942 C  CA  . LEU B 1 201 ? -16.616 72.468  0.993   1.00 17.54 ? 306  LEU B CA  1 
ATOM   4943 C  C   . LEU B 1 201 ? -16.893 73.874  0.447   1.00 17.44 ? 306  LEU B C   1 
ATOM   4944 O  O   . LEU B 1 201 ? -17.146 74.105  -0.754  1.00 18.43 ? 306  LEU B O   1 
ATOM   4945 C  CB  . LEU B 1 201 ? -17.946 71.762  1.398   1.00 16.46 ? 306  LEU B CB  1 
ATOM   4946 C  CG  . LEU B 1 201 ? -17.802 70.248  1.774   1.00 15.60 ? 306  LEU B CG  1 
ATOM   4947 C  CD1 . LEU B 1 201 ? -19.207 69.749  2.147   1.00 15.38 ? 306  LEU B CD1 1 
ATOM   4948 C  CD2 . LEU B 1 201 ? -17.309 69.435  0.581   1.00 16.59 ? 306  LEU B CD2 1 
ATOM   4949 N  N   . ILE B 1 202 ? -16.958 74.851  1.360   1.00 20.86 ? 307  ILE B N   1 
ATOM   4950 C  CA  . ILE B 1 202 ? -17.115 76.231  0.921   1.00 21.67 ? 307  ILE B CA  1 
ATOM   4951 C  C   . ILE B 1 202 ? -15.869 76.747  0.217   1.00 18.68 ? 307  ILE B C   1 
ATOM   4952 O  O   . ILE B 1 202 ? -16.035 77.413  -0.812  1.00 20.87 ? 307  ILE B O   1 
ATOM   4953 C  CB  . ILE B 1 202 ? -17.542 77.098  2.158   1.00 20.91 ? 307  ILE B CB  1 
ATOM   4954 C  CG1 . ILE B 1 202 ? -18.993 76.745  2.506   1.00 22.22 ? 307  ILE B CG1 1 
ATOM   4955 C  CG2 . ILE B 1 202 ? -17.392 78.623  1.868   1.00 22.40 ? 307  ILE B CG2 1 
ATOM   4956 C  CD1 . ILE B 1 202 ? -19.427 77.108  3.945   1.00 23.64 ? 307  ILE B CD1 1 
ATOM   4957 N  N   . GLU B 1 203 ? -14.734 76.389  0.726   1.00 20.23 ? 308  GLU B N   1 
ATOM   4958 C  CA  . GLU B 1 203 ? -13.405 76.818  0.147   1.00 24.07 ? 308  GLU B CA  1 
ATOM   4959 C  C   . GLU B 1 203 ? -13.328 76.333  -1.300  1.00 29.30 ? 308  GLU B C   1 
ATOM   4960 O  O   . GLU B 1 203 ? -12.905 77.091  -2.178  1.00 28.90 ? 308  GLU B O   1 
ATOM   4961 C  CB  . GLU B 1 203 ? -12.292 76.216  0.914   1.00 26.16 ? 308  GLU B CB  1 
ATOM   4962 C  CG  . GLU B 1 203 ? -10.861 76.467  0.283   1.00 36.96 ? 308  GLU B CG  1 
ATOM   4963 C  CD  . GLU B 1 203 ? -9.832  75.703  1.074   1.00 42.61 ? 308  GLU B CD  1 
ATOM   4964 O  OE1 . GLU B 1 203 ? -9.777  76.000  2.285   1.00 46.10 ? 308  GLU B OE1 1 
ATOM   4965 O  OE2 . GLU B 1 203 ? -9.173  74.748  0.556   1.00 53.25 ? 308  GLU B OE2 1 
ATOM   4966 N  N   . VAL B 1 204 ? -13.750 75.085  -1.582  1.00 26.21 ? 309  VAL B N   1 
ATOM   4967 C  CA  . VAL B 1 204 ? -13.659 74.529  -2.948  1.00 26.63 ? 309  VAL B CA  1 
ATOM   4968 C  C   . VAL B 1 204 ? -14.860 74.787  -3.785  1.00 20.90 ? 309  VAL B C   1 
ATOM   4969 O  O   . VAL B 1 204 ? -14.911 74.323  -4.968  1.00 24.74 ? 309  VAL B O   1 
ATOM   4970 C  CB  . VAL B 1 204 ? -13.193 73.040  -2.983  1.00 23.07 ? 309  VAL B CB  1 
ATOM   4971 C  CG1 . VAL B 1 204 ? -11.920 72.909  -2.205  1.00 25.23 ? 309  VAL B CG1 1 
ATOM   4972 C  CG2 . VAL B 1 204 ? -14.256 72.108  -2.338  1.00 22.72 ? 309  VAL B CG2 1 
ATOM   4973 N  N   . LYS B 1 205 ? -15.811 75.558  -3.255  1.00 21.05 ? 310  LYS B N   1 
ATOM   4974 C  CA  . LYS B 1 205 ? -17.038 75.963  -3.909  1.00 19.43 ? 310  LYS B CA  1 
ATOM   4975 C  C   . LYS B 1 205 ? -18.025 74.791  -4.249  1.00 18.90 ? 310  LYS B C   1 
ATOM   4976 O  O   . LYS B 1 205 ? -18.905 74.922  -5.066  1.00 20.42 ? 310  LYS B O   1 
ATOM   4977 C  CB  . LYS B 1 205 ? -16.795 76.864  -5.157  1.00 28.23 ? 310  LYS B CB  1 
ATOM   4978 C  CG  . LYS B 1 205 ? -16.162 78.197  -4.751  1.00 33.46 ? 310  LYS B CG  1 
ATOM   4979 C  CD  . LYS B 1 205 ? -15.685 78.937  -6.007  1.00 42.06 ? 310  LYS B CD  1 
ATOM   4980 C  CE  . LYS B 1 205 ? -15.176 80.334  -5.684  1.00 43.48 ? 310  LYS B CE  1 
ATOM   4981 N  NZ  . LYS B 1 205 ? -14.146 80.310  -4.618  1.00 45.61 ? 310  LYS B NZ  1 
ATOM   4982 N  N   . PHE B 1 206 ? -17.876 73.694  -3.513  1.00 18.58 ? 311  PHE B N   1 
ATOM   4983 C  CA  . PHE B 1 206 ? -18.928 72.644  -3.535  1.00 19.53 ? 311  PHE B CA  1 
ATOM   4984 C  C   . PHE B 1 206 ? -20.200 73.191  -2.908  1.00 17.88 ? 311  PHE B C   1 
ATOM   4985 O  O   . PHE B 1 206 ? -21.299 72.934  -3.328  1.00 18.81 ? 311  PHE B O   1 
ATOM   4986 C  CB  . PHE B 1 206 ? -18.370 71.404  -2.754  1.00 17.05 ? 311  PHE B CB  1 
ATOM   4987 C  CG  . PHE B 1 206 ? -19.307 70.246  -2.733  1.00 17.27 ? 311  PHE B CG  1 
ATOM   4988 C  CD1 . PHE B 1 206 ? -19.116 69.173  -3.673  1.00 17.98 ? 311  PHE B CD1 1 
ATOM   4989 C  CD2 . PHE B 1 206 ? -20.363 70.193  -1.849  1.00 17.52 ? 311  PHE B CD2 1 
ATOM   4990 C  CE1 . PHE B 1 206 ? -19.992 68.067  -3.594  1.00 18.46 ? 311  PHE B CE1 1 
ATOM   4991 C  CE2 . PHE B 1 206 ? -21.242 69.116  -1.832  1.00 19.20 ? 311  PHE B CE2 1 
ATOM   4992 C  CZ  . PHE B 1 206 ? -21.071 68.084  -2.735  1.00 17.95 ? 311  PHE B CZ  1 
ATOM   4993 N  N   . SER B 1 207 ? -19.967 73.996  -1.849  1.00 20.07 ? 312  SER B N   1 
ATOM   4994 C  CA  . SER B 1 207 ? -21.045 74.630  -1.052  1.00 19.82 ? 312  SER B CA  1 
ATOM   4995 C  C   . SER B 1 207 ? -20.837 76.133  -1.075  1.00 22.45 ? 312  SER B C   1 
ATOM   4996 O  O   . SER B 1 207 ? -19.748 76.574  -1.379  1.00 22.06 ? 312  SER B O   1 
ATOM   4997 C  CB  . SER B 1 207 ? -20.994 74.176  0.369   1.00 21.44 ? 312  SER B CB  1 
ATOM   4998 O  OG  . SER B 1 207 ? -21.186 72.761  0.455   1.00 20.98 ? 312  SER B OG  1 
ATOM   4999 N  N   . HIS B 1 208 ? -21.911 76.820  -0.745  1.00 24.88 ? 313  HIS B N   1 
ATOM   5000 C  CA  . HIS B 1 208 ? -21.779 78.291  -0.513  1.00 26.81 ? 313  HIS B CA  1 
ATOM   5001 C  C   . HIS B 1 208 ? -22.304 78.630  0.892   1.00 26.61 ? 313  HIS B C   1 
ATOM   5002 O  O   . HIS B 1 208 ? -23.253 77.938  1.409   1.00 26.73 ? 313  HIS B O   1 
ATOM   5003 C  CB  . HIS B 1 208 ? -22.503 79.079  -1.620  1.00 29.32 ? 313  HIS B CB  1 
ATOM   5004 C  CG  . HIS B 1 208 ? -23.996 78.928  -1.598  1.00 40.05 ? 313  HIS B CG  1 
ATOM   5005 N  ND1 . HIS B 1 208 ? -24.672 78.020  -2.384  1.00 48.65 ? 313  HIS B ND1 1 
ATOM   5006 C  CD2 . HIS B 1 208 ? -24.949 79.584  -0.890  1.00 49.76 ? 313  HIS B CD2 1 
ATOM   5007 C  CE1 . HIS B 1 208 ? -25.974 78.115  -2.161  1.00 50.28 ? 313  HIS B CE1 1 
ATOM   5008 N  NE2 . HIS B 1 208 ? -26.169 79.054  -1.251  1.00 50.35 ? 313  HIS B NE2 1 
ATOM   5009 N  N   . LEU B 1 209 ? -21.684 79.665  1.479   1.00 29.30 ? 314  LEU B N   1 
ATOM   5010 C  CA  . LEU B 1 209 ? -22.103 80.232  2.773   1.00 32.37 ? 314  LEU B CA  1 
ATOM   5011 C  C   . LEU B 1 209 ? -23.474 80.833  2.621   1.00 38.14 ? 314  LEU B C   1 
ATOM   5012 O  O   . LEU B 1 209 ? -23.675 81.727  1.752   1.00 38.71 ? 314  LEU B O   1 
ATOM   5013 C  CB  . LEU B 1 209 ? -21.034 81.220  3.228   1.00 33.14 ? 314  LEU B CB  1 
ATOM   5014 C  CG  . LEU B 1 209 ? -20.820 81.527  4.697   1.00 38.10 ? 314  LEU B CG  1 
ATOM   5015 C  CD1 . LEU B 1 209 ? -20.783 80.285  5.605   1.00 35.42 ? 314  LEU B CD1 1 
ATOM   5016 C  CD2 . LEU B 1 209 ? -19.517 82.311  4.835   1.00 42.15 ? 314  LEU B CD2 1 
ATOM   5017 N  N   . SER B 1 210 ? -24.451 80.276  3.354   1.00 35.79 ? 315  SER B N   1 
ATOM   5018 C  CA  . SER B 1 210 ? -25.856 80.696  3.231   1.00 47.54 ? 315  SER B CA  1 
ATOM   5019 C  C   . SER B 1 210 ? -26.058 82.160  3.627   1.00 51.04 ? 315  SER B C   1 
ATOM   5020 O  O   . SER B 1 210 ? -25.204 82.776  4.320   1.00 46.25 ? 315  SER B O   1 
ATOM   5021 C  CB  . SER B 1 210 ? -26.806 79.810  4.033   0.50 47.03 ? 315  SER B CB  1 
ATOM   5022 O  OG  . SER B 1 210 ? -27.258 78.709  3.266   0.50 47.14 ? 315  SER B OG  1 
ATOM   5023 N  N   . ARG B 1 211 ? -27.160 82.714  3.098   1.00 54.36 ? 316  ARG B N   1 
ATOM   5024 C  CA  . ARG B 1 211 ? -27.615 84.075  3.397   1.00 49.32 ? 316  ARG B CA  1 
ATOM   5025 C  C   . ARG B 1 211 ? -27.912 83.989  4.884   1.00 45.09 ? 316  ARG B C   1 
ATOM   5026 O  O   . ARG B 1 211 ? -28.550 83.011  5.336   1.00 45.75 ? 316  ARG B O   1 
ATOM   5027 C  CB  . ARG B 1 211 ? -28.913 84.471  2.644   0.50 49.17 ? 316  ARG B CB  1 
ATOM   5028 C  CG  . ARG B 1 211 ? -29.327 83.595  1.463   0.50 49.84 ? 316  ARG B CG  1 
ATOM   5029 C  CD  . ARG B 1 211 ? -30.048 82.338  1.942   0.50 48.96 ? 316  ARG B CD  1 
ATOM   5030 N  NE  . ARG B 1 211 ? -29.360 81.126  1.495   0.50 45.56 ? 316  ARG B NE  1 
ATOM   5031 C  CZ  . ARG B 1 211 ? -29.342 80.720  0.236   0.50 43.73 ? 316  ARG B CZ  1 
ATOM   5032 N  NH1 . ARG B 1 211 ? -29.967 81.425  -0.704  0.50 39.42 ? 316  ARG B NH1 1 
ATOM   5033 N  NH2 . ARG B 1 211 ? -28.714 79.612  -0.077  0.50 44.28 ? 316  ARG B NH2 1 
ATOM   5034 N  N   . ASN B 1 212 ? -27.378 84.948  5.644   1.00 35.02 ? 317  ASN B N   1 
ATOM   5035 C  CA  . ASN B 1 212 ? -27.725 85.053  7.088   1.00 35.26 ? 317  ASN B CA  1 
ATOM   5036 C  C   . ASN B 1 212 ? -27.046 84.056  8.006   1.00 33.09 ? 317  ASN B C   1 
ATOM   5037 O  O   . ASN B 1 212 ? -27.448 83.913  9.189   1.00 27.30 ? 317  ASN B O   1 
ATOM   5038 C  CB  . ASN B 1 212 ? -29.262 85.075  7.325   1.00 41.20 ? 317  ASN B CB  1 
ATOM   5039 C  CG  . ASN B 1 212 ? -29.965 86.104  6.433   1.00 53.96 ? 317  ASN B CG  1 
ATOM   5040 O  OD1 . ASN B 1 212 ? -29.468 87.251  6.250   1.00 46.91 ? 317  ASN B OD1 1 
ATOM   5041 N  ND2 . ASN B 1 212 ? -31.119 85.699  5.836   1.00 52.42 ? 317  ASN B ND2 1 
ATOM   5042 N  N   . MET B 1 213 ? -26.013 83.363  7.514   1.00 30.55 ? 318  MET B N   1 
ATOM   5043 C  CA  . MET B 1 213 ? -25.277 82.411  8.424   1.00 26.42 ? 318  MET B CA  1 
ATOM   5044 C  C   . MET B 1 213 ? -23.811 82.667  8.322   1.00 25.73 ? 318  MET B C   1 
ATOM   5045 O  O   . MET B 1 213 ? -23.320 82.826  7.210   1.00 26.46 ? 318  MET B O   1 
ATOM   5046 C  CB  . MET B 1 213 ? -25.600 80.971  8.028   1.00 33.36 ? 318  MET B CB  1 
ATOM   5047 C  CG  . MET B 1 213 ? -25.637 79.964  9.152   1.00 37.74 ? 318  MET B CG  1 
ATOM   5048 S  SD  . MET B 1 213 ? -26.424 78.355  8.761   1.00 43.34 ? 318  MET B SD  1 
ATOM   5049 C  CE  . MET B 1 213 ? -27.413 78.954  7.410   1.00 33.44 ? 318  MET B CE  1 
ATOM   5050 N  N   . THR B 1 214 ? -23.125 82.768  9.452   1.00 20.67 ? 319  THR B N   1 
ATOM   5051 C  CA  . THR B 1 214 ? -21.693 82.857  9.507   1.00 22.47 ? 319  THR B CA  1 
ATOM   5052 C  C   . THR B 1 214 ? -21.072 81.454  9.262   1.00 21.96 ? 319  THR B C   1 
ATOM   5053 O  O   . THR B 1 214 ? -21.768 80.421  9.442   1.00 21.41 ? 319  THR B O   1 
ATOM   5054 C  CB  . THR B 1 214 ? -21.175 83.344  10.858  1.00 22.53 ? 319  THR B CB  1 
ATOM   5055 O  OG1 . THR B 1 214 ? -21.547 82.434  11.911  1.00 22.39 ? 319  THR B OG1 1 
ATOM   5056 C  CG2 . THR B 1 214 ? -21.781 84.821  11.226  1.00 21.88 ? 319  THR B CG2 1 
ATOM   5057 N  N   . MET B 1 215 ? -19.769 81.424  9.006   1.00 21.15 ? 320  MET B N   1 
ATOM   5058 C  CA  . MET B 1 215 ? -19.032 80.181  8.957   1.00 20.70 ? 320  MET B CA  1 
ATOM   5059 C  C   . MET B 1 215 ? -19.102 79.468  10.258  1.00 22.30 ? 320  MET B C   1 
ATOM   5060 O  O   . MET B 1 215 ? -19.287 78.224  10.281  1.00 23.09 ? 320  MET B O   1 
ATOM   5061 C  CB  . MET B 1 215 ? -17.558 80.450  8.590   1.00 21.13 ? 320  MET B CB  1 
ATOM   5062 C  CG  . MET B 1 215 ? -16.662 79.196  8.501   1.00 21.88 ? 320  MET B CG  1 
ATOM   5063 S  SD  . MET B 1 215 ? -17.227 78.057  7.150   1.00 27.56 ? 320  MET B SD  1 
ATOM   5064 C  CE  . MET B 1 215 ? -16.441 78.885  5.779   1.00 26.74 ? 320  MET B CE  1 
ATOM   5065 N  N   . GLN B 1 216 ? -19.053 80.176  11.392  1.00 21.73 ? 321  GLN B N   1 
ATOM   5066 C  CA  A GLN B 1 216 ? -19.144 79.581  12.710  0.50 19.74 ? 321  GLN B CA  1 
ATOM   5067 C  CA  B GLN B 1 216 ? -19.062 79.517  12.679  0.50 21.11 ? 321  GLN B CA  1 
ATOM   5068 C  C   . GLN B 1 216 ? -20.465 78.888  12.906  1.00 20.74 ? 321  GLN B C   1 
ATOM   5069 O  O   . GLN B 1 216 ? -20.557 77.728  13.416  1.00 19.22 ? 321  GLN B O   1 
ATOM   5070 C  CB  A GLN B 1 216 ? -19.084 80.711  13.746  0.50 19.48 ? 321  GLN B CB  1 
ATOM   5071 C  CB  B GLN B 1 216 ? -18.530 80.470  13.819  0.50 24.48 ? 321  GLN B CB  1 
ATOM   5072 C  CG  A GLN B 1 216 ? -18.796 80.238  15.142  0.50 20.69 ? 321  GLN B CG  1 
ATOM   5073 C  CG  B GLN B 1 216 ? -18.556 81.965  13.500  0.50 29.21 ? 321  GLN B CG  1 
ATOM   5074 C  CD  A GLN B 1 216 ? -18.439 81.408  16.029  0.50 23.28 ? 321  GLN B CD  1 
ATOM   5075 C  CD  B GLN B 1 216 ? -17.442 82.461  12.599  0.50 24.80 ? 321  GLN B CD  1 
ATOM   5076 O  OE1 A GLN B 1 216 ? -17.471 82.122  15.774  0.50 29.19 ? 321  GLN B OE1 1 
ATOM   5077 O  OE1 B GLN B 1 216 ? -16.287 82.437  12.980  0.50 34.05 ? 321  GLN B OE1 1 
ATOM   5078 N  NE2 A GLN B 1 216 ? -19.223 81.628  17.027  0.50 23.18 ? 321  GLN B NE2 1 
ATOM   5079 N  NE2 B GLN B 1 216 ? -17.782 82.929  11.441  0.50 20.78 ? 321  GLN B NE2 1 
ATOM   5080 N  N   . ARG B 1 217 ? -21.542 79.535  12.505  1.00 18.75 ? 322  ARG B N   1 
ATOM   5081 C  CA  . ARG B 1 217 ? -22.881 78.993  12.670  1.00 19.81 ? 322  ARG B CA  1 
ATOM   5082 C  C   . ARG B 1 217 ? -23.023 77.730  11.766  1.00 20.41 ? 322  ARG B C   1 
ATOM   5083 O  O   . ARG B 1 217 ? -23.710 76.779  12.154  1.00 19.75 ? 322  ARG B O   1 
ATOM   5084 C  CB  . ARG B 1 217 ? -23.999 80.047  12.413  1.00 19.85 ? 322  ARG B CB  1 
ATOM   5085 C  CG  . ARG B 1 217 ? -25.397 79.550  12.189  1.00 25.11 ? 322  ARG B CG  1 
ATOM   5086 C  CD  . ARG B 1 217 ? -25.887 79.104  13.507  1.00 27.25 ? 322  ARG B CD  1 
ATOM   5087 N  NE  . ARG B 1 217 ? -27.184 78.451  13.412  1.00 36.01 ? 322  ARG B NE  1 
ATOM   5088 C  CZ  . ARG B 1 217 ? -27.409 77.132  13.534  1.00 38.28 ? 322  ARG B CZ  1 
ATOM   5089 N  NH1 . ARG B 1 217 ? -26.401 76.241  13.689  1.00 34.59 ? 322  ARG B NH1 1 
ATOM   5090 N  NH2 . ARG B 1 217 ? -28.672 76.692  13.450  1.00 44.16 ? 322  ARG B NH2 1 
ATOM   5091 N  N   . THR B 1 218 ? -22.497 77.818  10.557  1.00 19.53 ? 323  THR B N   1 
ATOM   5092 C  CA  . THR B 1 218 ? -22.605 76.677  9.580   1.00 18.02 ? 323  THR B CA  1 
ATOM   5093 C  C   . THR B 1 218 ? -21.794 75.486  10.127  1.00 16.49 ? 323  THR B C   1 
ATOM   5094 O  O   . THR B 1 218 ? -22.305 74.351  10.063  1.00 16.85 ? 323  THR B O   1 
ATOM   5095 C  CB  . THR B 1 218 ? -22.050 77.162  8.259   1.00 18.68 ? 323  THR B CB  1 
ATOM   5096 O  OG1 . THR B 1 218 ? -22.826 78.272  7.772   1.00 22.10 ? 323  THR B OG1 1 
ATOM   5097 C  CG2 . THR B 1 218 ? -22.103 76.037  7.221   1.00 17.58 ? 323  THR B CG2 1 
ATOM   5098 N  N   . MET B 1 219 ? -20.625 75.693  10.703  1.00 18.05 ? 324  MET B N   1 
ATOM   5099 C  CA  . MET B 1 219 ? -19.855 74.587  11.310  1.00 18.86 ? 324  MET B CA  1 
ATOM   5100 C  C   . MET B 1 219 ? -20.656 73.970  12.437  1.00 18.87 ? 324  MET B C   1 
ATOM   5101 O  O   . MET B 1 219 ? -20.682 72.701  12.648  1.00 18.17 ? 324  MET B O   1 
ATOM   5102 C  CB  . MET B 1 219 ? -18.398 74.960  11.689  1.00 21.02 ? 324  MET B CB  1 
ATOM   5103 C  CG  . MET B 1 219 ? -17.523 75.205  10.450  1.00 25.58 ? 324  MET B CG  1 
ATOM   5104 S  SD  . MET B 1 219 ? -15.856 75.815  10.887  1.00 35.31 ? 324  MET B SD  1 
ATOM   5105 C  CE  . MET B 1 219 ? -16.228 77.086  12.079  1.00 40.77 ? 324  MET B CE  1 
ATOM   5106 N  N   . LYS B 1 220 ? -21.393 74.808  13.202  1.00 18.87 ? 325  LYS B N   1 
ATOM   5107 C  CA  . LYS B 1 220 ? -22.145 74.325  14.287  1.00 19.50 ? 325  LYS B CA  1 
ATOM   5108 C  C   . LYS B 1 220 ? -23.347 73.474  13.758  1.00 17.14 ? 325  LYS B C   1 
ATOM   5109 O  O   . LYS B 1 220 ? -23.676 72.386  14.334  1.00 19.66 ? 325  LYS B O   1 
ATOM   5110 C  CB  . LYS B 1 220 ? -22.629 75.587  15.106  1.00 22.39 ? 325  LYS B CB  1 
ATOM   5111 C  CG  . LYS B 1 220 ? -23.636 75.286  16.165  1.00 26.33 ? 325  LYS B CG  1 
ATOM   5112 C  CD  . LYS B 1 220 ? -24.006 76.631  16.836  1.00 28.88 ? 325  LYS B CD  1 
ATOM   5113 C  CE  . LYS B 1 220 ? -25.098 76.343  17.850  1.00 35.09 ? 325  LYS B CE  1 
ATOM   5114 N  NZ  . LYS B 1 220 ? -25.558 77.688  18.345  1.00 35.40 ? 325  LYS B NZ  1 
ATOM   5115 N  N   . LEU B 1 221 ? -24.058 73.959  12.730  1.00 18.11 ? 326  LEU B N   1 
ATOM   5116 C  CA  . LEU B 1 221 ? -25.195 73.269  12.171  1.00 18.97 ? 326  LEU B CA  1 
ATOM   5117 C  C   . LEU B 1 221 ? -24.848 71.834  11.755  1.00 16.70 ? 326  LEU B C   1 
ATOM   5118 O  O   . LEU B 1 221 ? -25.658 70.927  12.015  1.00 18.79 ? 326  LEU B O   1 
ATOM   5119 C  CB  . LEU B 1 221 ? -25.688 74.033  10.971  1.00 19.45 ? 326  LEU B CB  1 
ATOM   5120 C  CG  . LEU B 1 221 ? -26.855 73.443  10.129  1.00 22.62 ? 326  LEU B CG  1 
ATOM   5121 C  CD1 . LEU B 1 221 ? -28.127 73.292  10.936  1.00 22.30 ? 326  LEU B CD1 1 
ATOM   5122 C  CD2 . LEU B 1 221 ? -27.103 74.185  8.817   1.00 25.53 ? 326  LEU B CD2 1 
ATOM   5123 N  N   . TYR B 1 222 ? -23.674 71.714  11.119  1.00 16.17 ? 327  TYR B N   1 
ATOM   5124 C  CA  . TYR B 1 222 ? -23.307 70.362  10.575  1.00 14.51 ? 327  TYR B CA  1 
ATOM   5125 C  C   . TYR B 1 222 ? -22.494 69.550  11.490  1.00 16.58 ? 327  TYR B C   1 
ATOM   5126 O  O   . TYR B 1 222 ? -22.076 68.424  11.124  1.00 14.54 ? 327  TYR B O   1 
ATOM   5127 C  CB  . TYR B 1 222 ? -22.595 70.569  9.218   1.00 15.62 ? 327  TYR B CB  1 
ATOM   5128 C  CG  . TYR B 1 222 ? -23.538 71.068  8.191   1.00 14.39 ? 327  TYR B CG  1 
ATOM   5129 C  CD1 . TYR B 1 222 ? -24.641 70.271  7.807   1.00 15.47 ? 327  TYR B CD1 1 
ATOM   5130 C  CD2 . TYR B 1 222 ? -23.371 72.311  7.557   1.00 18.68 ? 327  TYR B CD2 1 
ATOM   5131 C  CE1 . TYR B 1 222 ? -25.598 70.717  6.897   1.00 16.95 ? 327  TYR B CE1 1 
ATOM   5132 C  CE2 . TYR B 1 222 ? -24.291 72.765  6.560   1.00 18.97 ? 327  TYR B CE2 1 
ATOM   5133 C  CZ  . TYR B 1 222 ? -25.401 71.968  6.237   1.00 19.55 ? 327  TYR B CZ  1 
ATOM   5134 O  OH  . TYR B 1 222 ? -26.405 72.429  5.362   1.00 22.70 ? 327  TYR B OH  1 
ATOM   5135 N  N   . ARG B 1 223 ? -22.161 70.020  12.738  1.00 17.47 ? 328  ARG B N   1 
ATOM   5136 C  CA  . ARG B 1 223 ? -21.180 69.253  13.595  1.00 16.53 ? 328  ARG B CA  1 
ATOM   5137 C  C   . ARG B 1 223 ? -21.826 67.912  13.980  1.00 14.80 ? 328  ARG B C   1 
ATOM   5138 O  O   . ARG B 1 223 ? -23.014 67.818  14.158  1.00 16.89 ? 328  ARG B O   1 
ATOM   5139 C  CB  . ARG B 1 223 ? -20.818 70.050  14.905  1.00 20.08 ? 328  ARG B CB  1 
ATOM   5140 C  CG  . ARG B 1 223 ? -19.637 69.531  15.684  1.00 24.71 ? 328  ARG B CG  1 
ATOM   5141 C  CD  . ARG B 1 223 ? -18.941 70.590  16.564  1.00 30.97 ? 328  ARG B CD  1 
ATOM   5142 N  NE  . ARG B 1 223 ? -18.369 71.687  15.741  1.00 38.68 ? 328  ARG B NE  1 
ATOM   5143 C  CZ  . ARG B 1 223 ? -18.596 72.988  15.995  1.00 39.04 ? 328  ARG B CZ  1 
ATOM   5144 N  NH1 . ARG B 1 223 ? -19.342 73.343  17.057  1.00 42.45 ? 328  ARG B NH1 1 
ATOM   5145 N  NH2 . ARG B 1 223 ? -18.084 73.921  15.210  1.00 33.35 ? 328  ARG B NH2 1 
ATOM   5146 N  N   . LEU B 1 224 ? -20.993 66.917  14.164  1.00 17.06 ? 329  LEU B N   1 
ATOM   5147 C  CA  . LEU B 1 224 ? -21.484 65.549  14.493  1.00 15.47 ? 329  LEU B CA  1 
ATOM   5148 C  C   . LEU B 1 224 ? -20.779 65.091  15.749  1.00 16.58 ? 329  LEU B C   1 
ATOM   5149 O  O   . LEU B 1 224 ? -19.658 65.493  15.984  1.00 17.54 ? 329  LEU B O   1 
ATOM   5150 C  CB  . LEU B 1 224 ? -21.091 64.600  13.289  1.00 16.04 ? 329  LEU B CB  1 
ATOM   5151 C  CG  . LEU B 1 224 ? -21.984 64.811  12.064  1.00 15.74 ? 329  LEU B CG  1 
ATOM   5152 C  CD1 . LEU B 1 224 ? -21.312 64.134  10.837  1.00 18.00 ? 329  LEU B CD1 1 
ATOM   5153 C  CD2 . LEU B 1 224 ? -23.375 64.296  12.273  1.00 18.13 ? 329  LEU B CD2 1 
ATOM   5154 N  N   . PRO B 1 225 ? -21.321 64.080  16.414  1.00 17.87 ? 330  PRO B N   1 
ATOM   5155 C  CA  . PRO B 1 225 ? -20.582 63.381  17.492  1.00 19.79 ? 330  PRO B CA  1 
ATOM   5156 C  C   . PRO B 1 225 ? -19.266 62.818  17.050  1.00 19.45 ? 330  PRO B C   1 
ATOM   5157 O  O   . PRO B 1 225 ? -19.078 62.504  15.846  1.00 17.91 ? 330  PRO B O   1 
ATOM   5158 C  CB  . PRO B 1 225 ? -21.566 62.287  17.917  1.00 22.15 ? 330  PRO B CB  1 
ATOM   5159 C  CG  . PRO B 1 225 ? -22.888 62.673  17.388  1.00 24.28 ? 330  PRO B CG  1 
ATOM   5160 C  CD  . PRO B 1 225 ? -22.628 63.478  16.162  1.00 18.75 ? 330  PRO B CD  1 
ATOM   5161 N  N   . GLU B 1 226 ? -18.293 62.624  17.947  1.00 19.29 ? 331  GLU B N   1 
ATOM   5162 C  CA  . GLU B 1 226 ? -17.016 62.049  17.602  1.00 21.64 ? 331  GLU B CA  1 
ATOM   5163 C  C   . GLU B 1 226 ? -17.001 60.514  17.468  1.00 23.14 ? 331  GLU B C   1 
ATOM   5164 O  O   . GLU B 1 226 ? -16.144 59.911  16.801  1.00 28.16 ? 331  GLU B O   1 
ATOM   5165 C  CB  . GLU B 1 226 ? -15.972 62.418  18.673  1.00 27.20 ? 331  GLU B CB  1 
ATOM   5166 C  CG  . GLU B 1 226 ? -15.321 63.788  18.427  1.00 33.51 ? 331  GLU B CG  1 
ATOM   5167 C  CD  . GLU B 1 226 ? -14.866 64.532  19.721  1.00 46.20 ? 331  GLU B CD  1 
ATOM   5168 O  OE1 . GLU B 1 226 ? -14.700 63.908  20.809  1.00 42.42 ? 331  GLU B OE1 1 
ATOM   5169 O  OE2 . GLU B 1 226 ? -14.678 65.778  19.668  1.00 53.03 ? 331  GLU B OE2 1 
ATOM   5170 N  N   . THR B 1 227 ? -17.987 59.888  18.030  1.00 19.80 ? 332  THR B N   1 
ATOM   5171 C  CA  . THR B 1 227 ? -18.130 58.442  17.940  1.00 21.33 ? 332  THR B CA  1 
ATOM   5172 C  C   . THR B 1 227 ? -19.587 58.103  17.670  1.00 17.91 ? 332  THR B C   1 
ATOM   5173 O  O   . THR B 1 227 ? -20.550 58.813  18.027  1.00 16.74 ? 332  THR B O   1 
ATOM   5174 C  CB  . THR B 1 227 ? -17.622 57.690  19.202  1.00 25.88 ? 332  THR B CB  1 
ATOM   5175 O  OG1 . THR B 1 227 ? -18.366 58.175  20.269  1.00 26.74 ? 332  THR B OG1 1 
ATOM   5176 C  CG2 . THR B 1 227 ? -16.134 58.078  19.454  1.00 24.12 ? 332  THR B CG2 1 
ATOM   5177 N  N   . PRO B 1 228 ? -19.814 56.943  16.998  1.00 18.37 ? 333  PRO B N   1 
ATOM   5178 C  CA  . PRO B 1 228 ? -21.197 56.618  16.681  1.00 19.39 ? 333  PRO B CA  1 
ATOM   5179 C  C   . PRO B 1 228 ? -21.993 56.240  17.924  1.00 18.84 ? 333  PRO B C   1 
ATOM   5180 O  O   . PRO B 1 228 ? -21.388 55.819  18.921  1.00 24.05 ? 333  PRO B O   1 
ATOM   5181 C  CB  . PRO B 1 228 ? -21.058 55.356  15.771  1.00 20.22 ? 333  PRO B CB  1 
ATOM   5182 C  CG  . PRO B 1 228 ? -19.639 55.189  15.486  1.00 23.83 ? 333  PRO B CG  1 
ATOM   5183 C  CD  . PRO B 1 228 ? -18.796 56.086  16.349  1.00 20.90 ? 333  PRO B CD  1 
ATOM   5184 N  N   . LYS B 1 229 ? -23.277 56.372  17.789  1.00 16.42 ? 334  LYS B N   1 
ATOM   5185 C  CA  . LYS B 1 229 ? -24.138 56.095  18.941  1.00 23.37 ? 334  LYS B CA  1 
ATOM   5186 C  C   . LYS B 1 229 ? -24.680 54.696  19.037  1.00 23.41 ? 334  LYS B C   1 
ATOM   5187 O  O   . LYS B 1 229 ? -24.966 54.263  20.156  1.00 21.25 ? 334  LYS B O   1 
ATOM   5188 C  CB  . LYS B 1 229 ? -25.284 57.017  18.882  1.00 25.21 ? 334  LYS B CB  1 
ATOM   5189 C  CG  . LYS B 1 229 ? -26.312 56.780  17.839  1.00 28.33 ? 334  LYS B CG  1 
ATOM   5190 C  CD  . LYS B 1 229 ? -27.367 57.832  18.066  1.00 36.11 ? 334  LYS B CD  1 
ATOM   5191 C  CE  . LYS B 1 229 ? -28.159 58.021  16.795  1.00 37.47 ? 334  LYS B CE  1 
ATOM   5192 N  NZ  . LYS B 1 229 ? -29.245 59.027  17.049  1.00 45.72 ? 334  LYS B NZ  1 
ATOM   5193 N  N   . THR B 1 230 ? -24.704 53.896  17.957  1.00 16.86 ? 335  THR B N   1 
ATOM   5194 C  CA  . THR B 1 230 ? -25.372 52.571  18.097  1.00 15.41 ? 335  THR B CA  1 
ATOM   5195 C  C   . THR B 1 230 ? -24.435 51.679  18.770  1.00 15.52 ? 335  THR B C   1 
ATOM   5196 O  O   . THR B 1 230 ? -23.265 51.541  18.392  1.00 15.91 ? 335  THR B O   1 
ATOM   5197 C  CB  . THR B 1 230 ? -25.704 52.019  16.691  1.00 13.58 ? 335  THR B CB  1 
ATOM   5198 O  OG1 . THR B 1 230 ? -26.679 52.889  16.036  1.00 15.82 ? 335  THR B OG1 1 
ATOM   5199 C  CG2 . THR B 1 230 ? -26.336 50.590  16.826  1.00 15.73 ? 335  THR B CG2 1 
ATOM   5200 N  N   . ALA B 1 231 ? -24.933 51.000  19.819  1.00 15.36 ? 336  ALA B N   1 
ATOM   5201 C  CA  . ALA B 1 231 ? -24.085 50.062  20.536  1.00 16.05 ? 336  ALA B CA  1 
ATOM   5202 C  C   . ALA B 1 231 ? -23.721 48.854  19.664  1.00 15.44 ? 336  ALA B C   1 
ATOM   5203 O  O   . ALA B 1 231 ? -24.578 48.367  18.848  1.00 16.47 ? 336  ALA B O   1 
ATOM   5204 C  CB  . ALA B 1 231 ? -24.784 49.540  21.797  1.00 18.50 ? 336  ALA B CB  1 
ATOM   5205 N  N   . GLY B 1 232 ? -22.514 48.407  19.799  1.00 13.08 ? 337  GLY B N   1 
ATOM   5206 C  CA  . GLY B 1 232 ? -22.064 47.171  19.152  1.00 11.17 ? 337  GLY B CA  1 
ATOM   5207 C  C   . GLY B 1 232 ? -21.628 47.318  17.723  1.00 11.19 ? 337  GLY B C   1 
ATOM   5208 O  O   . GLY B 1 232 ? -21.430 46.289  17.078  1.00 11.82 ? 337  GLY B O   1 
ATOM   5209 N  N   . LEU B 1 233 ? -21.443 48.524  17.222  1.00 9.99  ? 338  LEU B N   1 
ATOM   5210 C  CA  . LEU B 1 233 ? -20.995 48.750  15.832  1.00 10.39 ? 338  LEU B CA  1 
ATOM   5211 C  C   . LEU B 1 233 ? -19.532 48.432  15.710  1.00 11.95 ? 338  LEU B C   1 
ATOM   5212 O  O   . LEU B 1 233 ? -18.666 48.766  16.587  1.00 14.64 ? 338  LEU B O   1 
ATOM   5213 C  CB  . LEU B 1 233 ? -21.217 50.251  15.534  1.00 12.39 ? 338  LEU B CB  1 
ATOM   5214 C  CG  . LEU B 1 233 ? -21.320 50.604  14.056  1.00 16.24 ? 338  LEU B CG  1 
ATOM   5215 C  CD1 . LEU B 1 233 ? -22.494 50.005  13.280  1.00 14.69 ? 338  LEU B CD1 1 
ATOM   5216 C  CD2 . LEU B 1 233 ? -21.407 52.170  14.054  1.00 21.08 ? 338  LEU B CD2 1 
ATOM   5217 N  N   . ARG B 1 234 ? -19.152 47.712  14.658  1.00 10.53 ? 339  ARG B N   1 
ATOM   5218 C  CA  . ARG B 1 234 ? -17.746 47.362  14.466  1.00 10.33 ? 339  ARG B CA  1 
ATOM   5219 C  C   . ARG B 1 234 ? -17.536 47.077  12.954  1.00 10.76 ? 339  ARG B C   1 
ATOM   5220 O  O   . ARG B 1 234 ? -18.526 46.707  12.292  1.00 10.39 ? 339  ARG B O   1 
ATOM   5221 C  CB  . ARG B 1 234 ? -17.324 46.117  15.283  1.00 10.58 ? 339  ARG B CB  1 
ATOM   5222 C  CG  . ARG B 1 234 ? -18.201 44.890  15.051  1.00 10.38 ? 339  ARG B CG  1 
ATOM   5223 C  CD  . ARG B 1 234 ? -17.567 43.674  15.685  1.00 11.54 ? 339  ARG B CD  1 
ATOM   5224 N  NE  . ARG B 1 234 ? -18.410 42.480  15.547  1.00 11.01 ? 339  ARG B NE  1 
ATOM   5225 C  CZ  . ARG B 1 234 ? -18.434 41.747  14.385  1.00 9.77  ? 339  ARG B CZ  1 
ATOM   5226 N  NH1 . ARG B 1 234 ? -17.717 42.116  13.295  1.00 10.18 ? 339  ARG B NH1 1 
ATOM   5227 N  NH2 . ARG B 1 234 ? -19.179 40.633  14.352  1.00 9.99  ? 339  ARG B NH2 1 
ATOM   5228 N  N   . PRO B 1 235 ? -16.274 47.130  12.464  1.00 10.20 ? 340  PRO B N   1 
ATOM   5229 C  CA  . PRO B 1 235 ? -16.136 46.709  11.051  1.00 9.53  ? 340  PRO B CA  1 
ATOM   5230 C  C   . PRO B 1 235 ? -16.513 45.256  10.807  1.00 10.10 ? 340  PRO B C   1 
ATOM   5231 O  O   . PRO B 1 235 ? -16.315 44.355  11.679  1.00 10.24 ? 340  PRO B O   1 
ATOM   5232 C  CB  . PRO B 1 235 ? -14.622 46.856  10.845  1.00 10.70 ? 340  PRO B CB  1 
ATOM   5233 C  CG  . PRO B 1 235 ? -14.184 47.988  11.773  1.00 11.33 ? 340  PRO B CG  1 
ATOM   5234 C  CD  . PRO B 1 235 ? -15.032 47.657  13.045  1.00 11.25 ? 340  PRO B CD  1 
ATOM   5235 N  N   . MET B 1 236 ? -17.033 44.965  9.620   1.00 9.40  ? 341  MET B N   1 
ATOM   5236 C  CA  . MET B 1 236 ? -17.250 43.617  9.148   1.00 9.39  ? 341  MET B CA  1 
ATOM   5237 C  C   . MET B 1 236 ? -15.919 42.810  9.099   1.00 9.62  ? 341  MET B C   1 
ATOM   5238 O  O   . MET B 1 236 ? -14.880 43.361  8.687   1.00 10.84 ? 341  MET B O   1 
ATOM   5239 C  CB  . MET B 1 236 ? -17.802 43.755  7.722   1.00 10.52 ? 341  MET B CB  1 
ATOM   5240 C  CG  . MET B 1 236 ? -18.173 42.360  7.114   1.00 9.89  ? 341  MET B CG  1 
ATOM   5241 S  SD  . MET B 1 236 ? -18.659 42.569  5.403   1.00 10.93 ? 341  MET B SD  1 
ATOM   5242 C  CE  . MET B 1 236 ? -18.905 40.829  4.963   1.00 11.72 ? 341  MET B CE  1 
ATOM   5243 N  N   . GLU B 1 237 ? -16.044 41.568  9.523   1.00 10.21 ? 342  GLU B N   1 
ATOM   5244 C  CA  . GLU B 1 237 ? -14.939 40.632  9.506   1.00 11.49 ? 342  GLU B CA  1 
ATOM   5245 C  C   . GLU B 1 237 ? -15.353 39.401  8.676   1.00 11.65 ? 342  GLU B C   1 
ATOM   5246 O  O   . GLU B 1 237 ? -16.509 39.221  8.277   1.00 10.48 ? 342  GLU B O   1 
ATOM   5247 C  CB  . GLU B 1 237 ? -14.708 40.162  10.924  1.00 12.81 ? 342  GLU B CB  1 
ATOM   5248 C  CG  . GLU B 1 237 ? -14.148 41.346  11.775  1.00 14.62 ? 342  GLU B CG  1 
ATOM   5249 C  CD  . GLU B 1 237 ? -13.901 40.864  13.211  1.00 19.87 ? 342  GLU B CD  1 
ATOM   5250 O  OE1 . GLU B 1 237 ? -13.702 39.644  13.478  1.00 24.04 ? 342  GLU B OE1 1 
ATOM   5251 O  OE2 . GLU B 1 237 ? -13.928 41.746  14.096  1.00 19.08 ? 342  GLU B OE2 1 
ATOM   5252 N  N   . THR B 1 238 ? -14.335 38.509  8.426   1.00 11.59 ? 343  THR B N   1 
ATOM   5253 C  CA  . THR B 1 238 ? -14.609 37.300  7.620   1.00 12.27 ? 343  THR B CA  1 
ATOM   5254 C  C   . THR B 1 238 ? -15.712 36.464  8.201   1.00 10.52 ? 343  THR B C   1 
ATOM   5255 O  O   . THR B 1 238 ? -16.570 35.936  7.479   1.00 12.22 ? 343  THR B O   1 
ATOM   5256 C  CB  . THR B 1 238 ? -13.263 36.517  7.535   1.00 12.73 ? 343  THR B CB  1 
ATOM   5257 O  OG1 . THR B 1 238 ? -12.313 37.297  6.872   1.00 16.19 ? 343  THR B OG1 1 
ATOM   5258 C  CG2 . THR B 1 238 ? -13.451 35.175  6.758   1.00 15.53 ? 343  THR B CG2 1 
ATOM   5259 N  N   . LYS B 1 239 ? -15.782 36.370  9.547   1.00 11.11 ? 344  LYS B N   1 
ATOM   5260 C  CA  . LYS B 1 239 ? -16.834 35.582  10.141  1.00 12.52 ? 344  LYS B CA  1 
ATOM   5261 C  C   . LYS B 1 239 ? -18.276 36.047  9.905   1.00 11.57 ? 344  LYS B C   1 
ATOM   5262 O  O   . LYS B 1 239 ? -19.234 35.344  10.108  1.00 12.65 ? 344  LYS B O   1 
ATOM   5263 C  CB  . LYS B 1 239 ? -16.624 35.476  11.679  1.00 12.96 ? 344  LYS B CB  1 
ATOM   5264 C  CG  . LYS B 1 239 ? -16.798 36.814  12.408  1.00 13.19 ? 344  LYS B CG  1 
ATOM   5265 C  CD  . LYS B 1 239 ? -16.462 36.630  13.927  1.00 18.23 ? 344  LYS B CD  1 
ATOM   5266 C  CE  . LYS B 1 239 ? -16.393 37.998  14.498  1.00 20.79 ? 344  LYS B CE  1 
ATOM   5267 N  NZ  . LYS B 1 239 ? -16.032 38.055  16.018  1.00 25.14 ? 344  LYS B NZ  1 
ATOM   5268 N  N   . ASP B 1 240 ? -18.356 37.348  9.503   1.00 10.84 ? 345  ASP B N   1 
ATOM   5269 C  CA  . ASP B 1 240 ? -19.664 37.961  9.200   1.00 10.68 ? 345  ASP B CA  1 
ATOM   5270 C  C   . ASP B 1 240 ? -20.172 37.788  7.784   1.00 9.02  ? 345  ASP B C   1 
ATOM   5271 O  O   . ASP B 1 240 ? -21.324 38.226  7.494   1.00 11.06 ? 345  ASP B O   1 
ATOM   5272 C  CB  . ASP B 1 240 ? -19.617 39.504  9.470   1.00 11.25 ? 345  ASP B CB  1 
ATOM   5273 C  CG  . ASP B 1 240 ? -19.144 39.890  10.849  1.00 9.79  ? 345  ASP B CG  1 
ATOM   5274 O  OD1 . ASP B 1 240 ? -19.622 39.260  11.839  1.00 11.20 ? 345  ASP B OD1 1 
ATOM   5275 O  OD2 . ASP B 1 240 ? -18.281 40.794  10.949  1.00 10.91 ? 345  ASP B OD2 1 
ATOM   5276 N  N   . ILE B 1 241 ? -19.384 37.184  6.893   1.00 10.88 ? 346  ILE B N   1 
ATOM   5277 C  CA  . ILE B 1 241 ? -19.790 37.121  5.480   1.00 10.34 ? 346  ILE B CA  1 
ATOM   5278 C  C   . ILE B 1 241 ? -21.166 36.388  5.382   1.00 9.70  ? 346  ILE B C   1 
ATOM   5279 O  O   . ILE B 1 241 ? -22.021 36.889  4.640   1.00 9.94  ? 346  ILE B O   1 
ATOM   5280 C  CB  . ILE B 1 241 ? -18.675 36.498  4.643   1.00 11.22 ? 346  ILE B CB  1 
ATOM   5281 C  CG1 . ILE B 1 241 ? -17.494 37.452  4.512   1.00 11.93 ? 346  ILE B CG1 1 
ATOM   5282 C  CG2 . ILE B 1 241 ? -19.165 36.028  3.240   1.00 11.67 ? 346  ILE B CG2 1 
ATOM   5283 C  CD1 . ILE B 1 241 ? -16.193 36.744  4.049   1.00 12.86 ? 346  ILE B CD1 1 
ATOM   5284 N  N   . PRO B 1 242 ? -21.417 35.206  6.027   1.00 10.08 ? 347  PRO B N   1 
ATOM   5285 C  CA  . PRO B 1 242 ? -22.715 34.582  5.890   1.00 10.42 ? 347  PRO B CA  1 
ATOM   5286 C  C   . PRO B 1 242 ? -23.884 35.429  6.352   1.00 10.13 ? 347  PRO B C   1 
ATOM   5287 O  O   . PRO B 1 242 ? -24.867 35.560  5.638   1.00 11.02 ? 347  PRO B O   1 
ATOM   5288 C  CB  . PRO B 1 242 ? -22.601 33.251  6.615   1.00 11.24 ? 347  PRO B CB  1 
ATOM   5289 C  CG  . PRO B 1 242 ? -21.098 33.025  6.669   1.00 11.21 ? 347  PRO B CG  1 
ATOM   5290 C  CD  . PRO B 1 242 ? -20.443 34.371  6.794   1.00 10.53 ? 347  PRO B CD  1 
ATOM   5291 N  N   . VAL B 1 243 ? -23.751 36.055  7.550   1.00 10.54 ? 348  VAL B N   1 
ATOM   5292 C  CA  . VAL B 1 243 ? -24.919 36.859  8.043   1.00 10.67 ? 348  VAL B CA  1 
ATOM   5293 C  C   . VAL B 1 243 ? -25.152 38.135  7.244   1.00 9.33  ? 348  VAL B C   1 
ATOM   5294 O  O   . VAL B 1 243 ? -26.319 38.468  7.016   1.00 10.38 ? 348  VAL B O   1 
ATOM   5295 C  CB  . VAL B 1 243 ? -24.792 37.073  9.581   1.00 10.63 ? 348  VAL B CB  1 
ATOM   5296 C  CG1 . VAL B 1 243 ? -23.691 38.066  9.887   1.00 10.84 ? 348  VAL B CG1 1 
ATOM   5297 C  CG2 . VAL B 1 243 ? -26.119 37.622  10.114  1.00 12.73 ? 348  VAL B CG2 1 
ATOM   5298 N  N   . VAL B 1 244 ? -24.062 38.754  6.774   1.00 10.51 ? 349  VAL B N   1 
ATOM   5299 C  CA  . VAL B 1 244 ? -24.252 39.906  5.868   1.00 10.81 ? 349  VAL B CA  1 
ATOM   5300 C  C   . VAL B 1 244 ? -24.971 39.479  4.575   1.00 9.54  ? 349  VAL B C   1 
ATOM   5301 O  O   . VAL B 1 244 ? -25.902 40.130  4.153   1.00 11.04 ? 349  VAL B O   1 
ATOM   5302 C  CB  . VAL B 1 244 ? -22.911 40.569  5.576   1.00 9.73  ? 349  VAL B CB  1 
ATOM   5303 C  CG1 . VAL B 1 244 ? -23.006 41.630  4.466   1.00 10.48 ? 349  VAL B CG1 1 
ATOM   5304 C  CG2 . VAL B 1 244 ? -22.427 41.268  6.869   1.00 10.55 ? 349  VAL B CG2 1 
ATOM   5305 N  N   . HIS B 1 245 ? -24.578 38.296  4.032   1.00 9.87  ? 350  HIS B N   1 
ATOM   5306 C  CA  A HIS B 1 245 ? -25.339 37.750  2.861   0.50 10.50 ? 350  HIS B CA  1 
ATOM   5307 C  CA  B HIS B 1 245 ? -25.258 37.731  2.851   0.50 11.00 ? 350  HIS B CA  1 
ATOM   5308 C  C   . HIS B 1 245 ? -26.765 37.508  3.159   1.00 10.80 ? 350  HIS B C   1 
ATOM   5309 O  O   . HIS B 1 245 ? -27.659 37.918  2.394   1.00 11.86 ? 350  HIS B O   1 
ATOM   5310 C  CB  A HIS B 1 245 ? -24.751 36.443  2.359   0.50 11.03 ? 350  HIS B CB  1 
ATOM   5311 C  CB  B HIS B 1 245 ? -24.366 36.502  2.498   0.50 11.63 ? 350  HIS B CB  1 
ATOM   5312 C  CG  A HIS B 1 245 ? -25.518 35.820  1.238   0.50 9.91  ? 350  HIS B CG  1 
ATOM   5313 C  CG  B HIS B 1 245 ? -24.864 35.590  1.410   0.50 11.77 ? 350  HIS B CG  1 
ATOM   5314 N  ND1 A HIS B 1 245 ? -26.459 34.837  1.443   0.50 10.88 ? 350  HIS B ND1 1 
ATOM   5315 N  ND1 B HIS B 1 245 ? -25.765 35.912  0.408   0.50 14.13 ? 350  HIS B ND1 1 
ATOM   5316 C  CD2 A HIS B 1 245 ? -25.491 36.055  -0.102  0.50 11.08 ? 350  HIS B CD2 1 
ATOM   5317 C  CD2 B HIS B 1 245 ? -24.577 34.274  1.243   0.50 12.56 ? 350  HIS B CD2 1 
ATOM   5318 C  CE1 A HIS B 1 245 ? -26.971 34.474  0.270   0.50 12.09 ? 350  HIS B CE1 1 
ATOM   5319 C  CE1 B HIS B 1 245 ? -25.938 34.850  -0.364  0.50 11.69 ? 350  HIS B CE1 1 
ATOM   5320 N  NE2 A HIS B 1 245 ? -26.424 35.230  -0.669  0.50 12.19 ? 350  HIS B NE2 1 
ATOM   5321 N  NE2 B HIS B 1 245 ? -25.265 33.842  0.143   0.50 15.56 ? 350  HIS B NE2 1 
ATOM   5322 N  N   . GLN B 1 246 ? -27.075 36.883  4.306   1.00 10.91 ? 351  GLN B N   1 
ATOM   5323 C  CA  . GLN B 1 246 ? -28.474 36.631  4.669   1.00 11.19 ? 351  GLN B CA  1 
ATOM   5324 C  C   . GLN B 1 246 ? -29.270 37.940  4.834   1.00 10.83 ? 351  GLN B C   1 
ATOM   5325 O  O   . GLN B 1 246 ? -30.382 38.061  4.353   1.00 11.86 ? 351  GLN B O   1 
ATOM   5326 C  CB  . GLN B 1 246 ? -28.496 35.768  5.989   1.00 12.25 ? 351  GLN B CB  1 
ATOM   5327 C  CG  . GLN B 1 246 ? -29.920 35.479  6.438   1.00 14.74 ? 351  GLN B CG  1 
ATOM   5328 C  CD  . GLN B 1 246 ? -29.865 34.570  7.654   1.00 23.67 ? 351  GLN B CD  1 
ATOM   5329 O  OE1 . GLN B 1 246 ? -29.417 34.977  8.683   1.00 25.37 ? 351  GLN B OE1 1 
ATOM   5330 N  NE2 . GLN B 1 246 ? -30.044 33.235  7.414   1.00 30.34 ? 351  GLN B NE2 1 
ATOM   5331 N  N   . LEU B 1 247 ? -28.668 38.888  5.614   1.00 11.58 ? 352  LEU B N   1 
ATOM   5332 C  CA  . LEU B 1 247 ? -29.381 40.134  5.885   1.00 11.72 ? 352  LEU B CA  1 
ATOM   5333 C  C   . LEU B 1 247 ? -29.671 40.888  4.558   1.00 9.79  ? 352  LEU B C   1 
ATOM   5334 O  O   . LEU B 1 247 ? -30.799 41.370  4.386   1.00 10.96 ? 352  LEU B O   1 
ATOM   5335 C  CB  . LEU B 1 247 ? -28.525 41.032  6.795   1.00 12.04 ? 352  LEU B CB  1 
ATOM   5336 C  CG  . LEU B 1 247 ? -28.466 40.589  8.298   1.00 12.73 ? 352  LEU B CG  1 
ATOM   5337 C  CD1 . LEU B 1 247 ? -27.360 41.337  9.024   1.00 13.14 ? 352  LEU B CD1 1 
ATOM   5338 C  CD2 . LEU B 1 247 ? -29.807 40.897  8.973   1.00 15.99 ? 352  LEU B CD2 1 
ATOM   5339 N  N   . LEU B 1 248 ? -28.644 40.946  3.680   1.00 10.48 ? 353  LEU B N   1 
ATOM   5340 C  CA  . LEU B 1 248 ? -28.871 41.701  2.409   1.00 10.91 ? 353  LEU B CA  1 
ATOM   5341 C  C   . LEU B 1 248 ? -29.934 41.024  1.565   1.00 10.82 ? 353  LEU B C   1 
ATOM   5342 O  O   . LEU B 1 248 ? -30.836 41.669  1.056   1.00 11.06 ? 353  LEU B O   1 
ATOM   5343 C  CB  . LEU B 1 248 ? -27.568 41.762  1.691   1.00 10.40 ? 353  LEU B CB  1 
ATOM   5344 C  CG  . LEU B 1 248 ? -27.658 42.486  0.328   1.00 10.65 ? 353  LEU B CG  1 
ATOM   5345 C  CD1 . LEU B 1 248 ? -27.920 44.003  0.519   1.00 12.47 ? 353  LEU B CD1 1 
ATOM   5346 C  CD2 . LEU B 1 248 ? -26.365 42.326  -0.434  1.00 13.28 ? 353  LEU B CD2 1 
ATOM   5347 N  N   . THR B 1 249 ? -29.851 39.686  1.414   1.00 11.32 ? 354  THR B N   1 
ATOM   5348 C  CA  . THR B 1 249 ? -30.773 38.965  0.492   1.00 12.32 ? 354  THR B CA  1 
ATOM   5349 C  C   . THR B 1 249 ? -32.176 39.149  0.974   1.00 12.24 ? 354  THR B C   1 
ATOM   5350 O  O   . THR B 1 249 ? -33.119 39.452  0.213   1.00 13.13 ? 354  THR B O   1 
ATOM   5351 C  CB  . THR B 1 249 ? -30.356 37.453  0.443   1.00 13.24 ? 354  THR B CB  1 
ATOM   5352 O  OG1 . THR B 1 249 ? -29.056 37.391  -0.056  1.00 14.89 ? 354  THR B OG1 1 
ATOM   5353 C  CG2 . THR B 1 249 ? -31.281 36.731  -0.616  1.00 13.95 ? 354  THR B CG2 1 
ATOM   5354 N  N   . ARG B 1 250 ? -32.433 39.037  2.319   1.00 12.57 ? 355  ARG B N   1 
ATOM   5355 C  CA  . ARG B 1 250 ? -33.768 39.211  2.803   1.00 12.82 ? 355  ARG B CA  1 
ATOM   5356 C  C   . ARG B 1 250 ? -34.295 40.688  2.644   1.00 12.11 ? 355  ARG B C   1 
ATOM   5357 O  O   . ARG B 1 250 ? -35.506 40.959  2.291   1.00 15.24 ? 355  ARG B O   1 
ATOM   5358 C  CB  . ARG B 1 250 ? -33.773 38.787  4.312   1.00 14.58 ? 355  ARG B CB  1 
ATOM   5359 C  CG  . ARG B 1 250 ? -33.595 37.246  4.489   1.00 24.33 ? 355  ARG B CG  1 
ATOM   5360 C  CD  . ARG B 1 250 ? -33.536 36.685  5.947   1.00 34.51 ? 355  ARG B CD  1 
ATOM   5361 N  NE  . ARG B 1 250 ? -33.126 35.266  5.758   1.00 40.62 ? 355  ARG B NE  1 
ATOM   5362 C  CZ  . ARG B 1 250 ? -33.133 34.257  6.644   1.00 52.29 ? 355  ARG B CZ  1 
ATOM   5363 N  NH1 . ARG B 1 250 ? -33.520 34.443  7.909   1.00 48.80 ? 355  ARG B NH1 1 
ATOM   5364 N  NH2 . ARG B 1 250 ? -32.742 33.025  6.236   1.00 46.21 ? 355  ARG B NH2 1 
ATOM   5365 N  N   . TYR B 1 251 ? -33.405 41.652  2.957   1.00 11.37 ? 356  TYR B N   1 
ATOM   5366 C  CA  . TYR B 1 251 ? -33.762 43.016  2.827   1.00 11.28 ? 356  TYR B CA  1 
ATOM   5367 C  C   . TYR B 1 251 ? -34.149 43.503  1.439   1.00 11.12 ? 356  TYR B C   1 
ATOM   5368 O  O   . TYR B 1 251 ? -35.086 44.317  1.270   1.00 11.78 ? 356  TYR B O   1 
ATOM   5369 C  CB  . TYR B 1 251 ? -32.590 43.866  3.398   1.00 11.67 ? 356  TYR B CB  1 
ATOM   5370 C  CG  . TYR B 1 251 ? -32.880 45.361  3.436   1.00 12.77 ? 356  TYR B CG  1 
ATOM   5371 C  CD1 . TYR B 1 251 ? -33.740 45.943  4.415   1.00 13.58 ? 356  TYR B CD1 1 
ATOM   5372 C  CD2 . TYR B 1 251 ? -32.379 46.223  2.423   1.00 11.07 ? 356  TYR B CD2 1 
ATOM   5373 C  CE1 . TYR B 1 251 ? -33.998 47.303  4.374   1.00 13.90 ? 356  TYR B CE1 1 
ATOM   5374 C  CE2 . TYR B 1 251 ? -32.719 47.604  2.417   1.00 12.32 ? 356  TYR B CE2 1 
ATOM   5375 C  CZ  . TYR B 1 251 ? -33.503 48.109  3.406   1.00 12.74 ? 356  TYR B CZ  1 
ATOM   5376 O  OH  . TYR B 1 251 ? -33.801 49.479  3.318   1.00 15.95 ? 356  TYR B OH  1 
ATOM   5377 N  N   . LEU B 1 252 ? -33.450 42.961  0.453   1.00 10.38 ? 357  LEU B N   1 
ATOM   5378 C  CA  . LEU B 1 252 ? -33.674 43.440  -0.918  1.00 10.91 ? 357  LEU B CA  1 
ATOM   5379 C  C   . LEU B 1 252 ? -34.955 42.957  -1.516  1.00 11.41 ? 357  LEU B C   1 
ATOM   5380 O  O   . LEU B 1 252 ? -35.407 43.490  -2.541  1.00 12.11 ? 357  LEU B O   1 
ATOM   5381 C  CB  . LEU B 1 252 ? -32.432 43.063  -1.789  1.00 11.94 ? 357  LEU B CB  1 
ATOM   5382 C  CG  . LEU B 1 252 ? -31.134 43.840  -1.522  1.00 10.31 ? 357  LEU B CG  1 
ATOM   5383 C  CD1 . LEU B 1 252 ? -30.040 43.191  -2.409  1.00 12.31 ? 357  LEU B CD1 1 
ATOM   5384 C  CD2 . LEU B 1 252 ? -31.263 45.341  -1.740  1.00 11.25 ? 357  LEU B CD2 1 
ATOM   5385 N  N   . LYS B 1 253 ? -35.614 41.961  -0.906  1.00 12.83 ? 358  LYS B N   1 
ATOM   5386 C  CA  . LYS B 1 253 ? -36.878 41.410  -1.507  1.00 15.13 ? 358  LYS B CA  1 
ATOM   5387 C  C   . LYS B 1 253 ? -37.919 42.489  -1.596  1.00 14.23 ? 358  LYS B C   1 
ATOM   5388 O  O   . LYS B 1 253 ? -38.749 42.333  -2.550  1.00 16.84 ? 358  LYS B O   1 
ATOM   5389 C  CB  . LYS B 1 253 ? -37.391 40.227  -0.667  1.00 17.97 ? 358  LYS B CB  1 
ATOM   5390 C  CG  . LYS B 1 253 ? -36.445 39.059  -0.799  1.00 21.86 ? 358  LYS B CG  1 
ATOM   5391 C  CD  . LYS B 1 253 ? -36.959 37.848  -0.026  1.00 30.52 ? 358  LYS B CD  1 
ATOM   5392 C  CE  . LYS B 1 253 ? -36.587 36.570  -0.808  1.00 40.66 ? 358  LYS B CE  1 
ATOM   5393 N  NZ  . LYS B 1 253 ? -35.267 35.806  -0.667  1.00 39.92 ? 358  LYS B NZ  1 
ATOM   5394 N  N   . GLN B 1 254 ? -37.915 43.539  -0.814  1.00 14.76 ? 359  GLN B N   1 
ATOM   5395 C  CA  . GLN B 1 254 ? -38.971 44.528  -0.830  1.00 13.64 ? 359  GLN B CA  1 
ATOM   5396 C  C   . GLN B 1 254 ? -38.902 45.471  -2.069  1.00 16.70 ? 359  GLN B C   1 
ATOM   5397 O  O   . GLN B 1 254 ? -39.808 46.264  -2.278  1.00 17.08 ? 359  GLN B O   1 
ATOM   5398 C  CB  . GLN B 1 254 ? -39.031 45.344  0.460   1.00 15.55 ? 359  GLN B CB  1 
ATOM   5399 C  CG  . GLN B 1 254 ? -37.749 46.193  0.570   1.00 15.12 ? 359  GLN B CG  1 
ATOM   5400 C  CD  . GLN B 1 254 ? -37.645 46.768  1.970   1.00 18.49 ? 359  GLN B CD  1 
ATOM   5401 O  OE1 . GLN B 1 254 ? -38.465 47.650  2.359   1.00 20.34 ? 359  GLN B OE1 1 
ATOM   5402 N  NE2 . GLN B 1 254 ? -36.705 46.281  2.761   1.00 14.79 ? 359  GLN B NE2 1 
ATOM   5403 N  N   . PHE B 1 255 ? -37.750 45.471  -2.791  1.00 13.04 ? 360  PHE B N   1 
ATOM   5404 C  CA  . PHE B 1 255 ? -37.630 46.375  -3.911  1.00 13.06 ? 360  PHE B CA  1 
ATOM   5405 C  C   . PHE B 1 255 ? -37.915 45.668  -5.219  1.00 12.04 ? 360  PHE B C   1 
ATOM   5406 O  O   . PHE B 1 255 ? -37.988 44.422  -5.244  1.00 14.78 ? 360  PHE B O   1 
ATOM   5407 C  CB  . PHE B 1 255 ? -36.202 46.986  -3.914  1.00 10.82 ? 360  PHE B CB  1 
ATOM   5408 C  CG  . PHE B 1 255 ? -35.870 47.613  -2.566  1.00 11.28 ? 360  PHE B CG  1 
ATOM   5409 C  CD1 . PHE B 1 255 ? -36.581 48.717  -2.045  1.00 10.21 ? 360  PHE B CD1 1 
ATOM   5410 C  CD2 . PHE B 1 255 ? -34.877 47.020  -1.768  1.00 10.66 ? 360  PHE B CD2 1 
ATOM   5411 C  CE1 . PHE B 1 255 ? -36.298 49.220  -0.783  1.00 10.31 ? 360  PHE B CE1 1 
ATOM   5412 C  CE2 . PHE B 1 255 ? -34.638 47.508  -0.447  1.00 10.56 ? 360  PHE B CE2 1 
ATOM   5413 C  CZ  . PHE B 1 255 ? -35.299 48.613  -0.006  1.00 10.47 ? 360  PHE B CZ  1 
ATOM   5414 N  N   . HIS B 1 256 ? -37.984 46.447  -6.348  1.00 11.02 ? 361  HIS B N   1 
ATOM   5415 C  CA  . HIS B 1 256 ? -38.291 45.829  -7.652  1.00 11.77 ? 361  HIS B CA  1 
ATOM   5416 C  C   . HIS B 1 256 ? -37.111 45.660  -8.614  1.00 11.20 ? 361  HIS B C   1 
ATOM   5417 O  O   . HIS B 1 256 ? -37.295 44.997  -9.624  1.00 11.95 ? 361  HIS B O   1 
ATOM   5418 C  CB  . HIS B 1 256 ? -39.437 46.588  -8.402  1.00 13.39 ? 361  HIS B CB  1 
ATOM   5419 C  CG  . HIS B 1 256 ? -40.761 46.554  -7.669  1.00 18.71 ? 361  HIS B CG  1 
ATOM   5420 N  ND1 . HIS B 1 256 ? -41.248 45.402  -7.113  1.00 20.82 ? 361  HIS B ND1 1 
ATOM   5421 C  CD2 . HIS B 1 256 ? -41.726 47.506  -7.533  1.00 21.37 ? 361  HIS B CD2 1 
ATOM   5422 C  CE1 . HIS B 1 256 ? -42.474 45.660  -6.607  1.00 24.89 ? 361  HIS B CE1 1 
ATOM   5423 N  NE2 . HIS B 1 256 ? -42.770 46.917  -6.853  1.00 24.21 ? 361  HIS B NE2 1 
ATOM   5424 N  N   . LEU B 1 257 ? -35.965 46.332  -8.367  1.00 9.79  ? 362  LEU B N   1 
ATOM   5425 C  CA  . LEU B 1 257 ? -34.783 46.090  -9.202  1.00 9.73  ? 362  LEU B CA  1 
ATOM   5426 C  C   . LEU B 1 257 ? -33.635 45.936  -8.225  1.00 8.51  ? 362  LEU B C   1 
ATOM   5427 O  O   . LEU B 1 257 ? -33.300 46.920  -7.505  1.00 9.58  ? 362  LEU B O   1 
ATOM   5428 C  CB  . LEU B 1 257 ? -34.545 47.316  -10.098 1.00 10.89 ? 362  LEU B CB  1 
ATOM   5429 C  CG  . LEU B 1 257 ? -33.193 47.331  -10.842 1.00 9.96  ? 362  LEU B CG  1 
ATOM   5430 C  CD1 . LEU B 1 257 ? -33.045 46.076  -11.735 1.00 10.96 ? 362  LEU B CD1 1 
ATOM   5431 C  CD2 . LEU B 1 257 ? -33.080 48.647  -11.675 1.00 11.92 ? 362  LEU B CD2 1 
ATOM   5432 N  N   . THR B 1 258 ? -33.015 44.763  -8.140  1.00 8.88  ? 363  THR B N   1 
ATOM   5433 C  CA  . THR B 1 258 ? -31.973 44.509  -7.096  1.00 10.16 ? 363  THR B CA  1 
ATOM   5434 C  C   . THR B 1 258 ? -30.993 43.510  -7.699  1.00 9.73  ? 363  THR B C   1 
ATOM   5435 O  O   . THR B 1 258 ? -31.301 42.723  -8.622  1.00 9.72  ? 363  THR B O   1 
ATOM   5436 C  CB  . THR B 1 258 ? -32.515 43.931  -5.788  1.00 11.54 ? 363  THR B CB  1 
ATOM   5437 O  OG1 . THR B 1 258 ? -32.818 42.576  -5.974  1.00 15.60 ? 363  THR B OG1 1 
ATOM   5438 C  CG2 . THR B 1 258 ? -33.755 44.652  -5.264  1.00 12.50 ? 363  THR B CG2 1 
ATOM   5439 N  N   . PRO B 1 259 ? -29.764 43.492  -7.143  1.00 9.45  ? 364  PRO B N   1 
ATOM   5440 C  CA  . PRO B 1 259 ? -28.892 42.324  -7.398  1.00 9.79  ? 364  PRO B CA  1 
ATOM   5441 C  C   . PRO B 1 259 ? -29.272 41.134  -6.593  1.00 9.27  ? 364  PRO B C   1 
ATOM   5442 O  O   . PRO B 1 259 ? -29.941 41.285  -5.551  1.00 11.26 ? 364  PRO B O   1 
ATOM   5443 C  CB  . PRO B 1 259 ? -27.493 42.885  -6.932  1.00 10.52 ? 364  PRO B CB  1 
ATOM   5444 C  CG  . PRO B 1 259 ? -27.851 43.752  -5.714  1.00 9.47  ? 364  PRO B CG  1 
ATOM   5445 C  CD  . PRO B 1 259 ? -29.208 44.440  -6.151  1.00 10.68 ? 364  PRO B CD  1 
ATOM   5446 N  N   . VAL B 1 260 ? -28.818 39.945  -7.025  1.00 10.03 ? 365  VAL B N   1 
ATOM   5447 C  CA  . VAL B 1 260 ? -28.893 38.762  -6.217  1.00 10.82 ? 365  VAL B CA  1 
ATOM   5448 C  C   . VAL B 1 260 ? -27.475 38.279  -6.117  1.00 10.07 ? 365  VAL B C   1 
ATOM   5449 O  O   . VAL B 1 260 ? -26.856 37.906  -7.132  1.00 12.12 ? 365  VAL B O   1 
ATOM   5450 C  CB  . VAL B 1 260 ? -29.745 37.676  -6.903  1.00 13.00 ? 365  VAL B CB  1 
ATOM   5451 C  CG1 . VAL B 1 260 ? -29.795 36.411  -6.075  1.00 15.10 ? 365  VAL B CG1 1 
ATOM   5452 C  CG2 . VAL B 1 260 ? -31.206 38.238  -7.140  1.00 16.35 ? 365  VAL B CG2 1 
ATOM   5453 N  N   . MET B 1 261 ? -26.876 38.358  -4.957  1.00 10.51 ? 366  MET B N   1 
ATOM   5454 C  CA  . MET B 1 261 ? -25.405 38.103  -4.780  1.00 10.95 ? 366  MET B CA  1 
ATOM   5455 C  C   . MET B 1 261 ? -25.220 36.734  -4.182  1.00 10.08 ? 366  MET B C   1 
ATOM   5456 O  O   . MET B 1 261 ? -25.809 36.370  -3.175  1.00 12.80 ? 366  MET B O   1 
ATOM   5457 C  CB  . MET B 1 261 ? -24.796 39.174  -3.862  1.00 10.48 ? 366  MET B CB  1 
ATOM   5458 C  CG  . MET B 1 261 ? -24.812 40.567  -4.443  1.00 11.92 ? 366  MET B CG  1 
ATOM   5459 S  SD  . MET B 1 261 ? -23.804 41.645  -3.412  1.00 12.30 ? 366  MET B SD  1 
ATOM   5460 C  CE  . MET B 1 261 ? -24.088 43.189  -4.237  1.00 15.08 ? 366  MET B CE  1 
ATOM   5461 N  N   . SER B 1 262 ? -24.198 36.003  -4.688  1.00 9.58  ? 367  SER B N   1 
ATOM   5462 C  CA  . SER B 1 262 ? -23.714 34.814  -3.986  1.00 9.68  ? 367  SER B CA  1 
ATOM   5463 C  C   . SER B 1 262 ? -22.893 35.238  -2.742  1.00 10.64 ? 367  SER B C   1 
ATOM   5464 O  O   . SER B 1 262 ? -22.557 36.423  -2.544  1.00 10.35 ? 367  SER B O   1 
ATOM   5465 C  CB  . SER B 1 262 ? -22.709 34.079  -4.915  1.00 9.84  ? 367  SER B CB  1 
ATOM   5466 O  OG  . SER B 1 262 ? -21.563 34.819  -5.092  1.00 10.72 ? 367  SER B OG  1 
ATOM   5467 N  N   . GLN B 1 263 ? -22.571 34.242  -1.910  1.00 9.57  ? 368  GLN B N   1 
ATOM   5468 C  CA  . GLN B 1 263 ? -21.697 34.582  -0.730  1.00 9.47  ? 368  GLN B CA  1 
ATOM   5469 C  C   . GLN B 1 263 ? -20.385 35.074  -1.172  1.00 9.71  ? 368  GLN B C   1 
ATOM   5470 O  O   . GLN B 1 263 ? -19.787 35.964  -0.529  1.00 11.24 ? 368  GLN B O   1 
ATOM   5471 C  CB  . GLN B 1 263 ? -21.603 33.330  0.164   1.00 10.62 ? 368  GLN B CB  1 
ATOM   5472 C  CG  . GLN B 1 263 ? -21.126 33.656  1.543   1.00 11.02 ? 368  GLN B CG  1 
ATOM   5473 C  CD  . GLN B 1 263 ? -21.588 32.646  2.576   1.00 11.27 ? 368  GLN B CD  1 
ATOM   5474 O  OE1 . GLN B 1 263 ? -22.765 32.475  2.872   1.00 11.99 ? 368  GLN B OE1 1 
ATOM   5475 N  NE2 . GLN B 1 263 ? -20.580 31.899  3.117   1.00 10.36 ? 368  GLN B NE2 1 
ATOM   5476 N  N   . GLU B 1 264 ? -19.792 34.543  -2.281  1.00 10.16 ? 369  GLU B N   1 
ATOM   5477 C  CA  . GLU B 1 264 ? -18.528 35.064  -2.776  1.00 10.50 ? 369  GLU B CA  1 
ATOM   5478 C  C   . GLU B 1 264 ? -18.672 36.521  -3.227  1.00 8.97  ? 369  GLU B C   1 
ATOM   5479 O  O   . GLU B 1 264 ? -17.750 37.309  -3.053  1.00 10.02 ? 369  GLU B O   1 
ATOM   5480 C  CB  . GLU B 1 264 ? -18.043 34.169  -4.000  1.00 13.53 ? 369  GLU B CB  1 
ATOM   5481 C  CG  . GLU B 1 264 ? -17.497 32.763  -3.540  1.00 17.52 ? 369  GLU B CG  1 
ATOM   5482 C  CD  . GLU B 1 264 ? -16.319 32.852  -2.569  1.00 22.97 ? 369  GLU B CD  1 
ATOM   5483 O  OE1 . GLU B 1 264 ? -15.428 33.730  -2.754  1.00 26.91 ? 369  GLU B OE1 1 
ATOM   5484 O  OE2 . GLU B 1 264 ? -16.281 32.037  -1.574  1.00 25.32 ? 369  GLU B OE2 1 
ATOM   5485 N  N   . GLU B 1 265 ? -19.805 36.825  -3.899  1.00 8.99  ? 370  GLU B N   1 
ATOM   5486 C  CA  . GLU B 1 265 ? -19.987 38.251  -4.334  1.00 9.63  ? 370  GLU B CA  1 
ATOM   5487 C  C   . GLU B 1 265 ? -20.150 39.160  -3.076  1.00 9.07  ? 370  GLU B C   1 
ATOM   5488 O  O   . GLU B 1 265 ? -19.657 40.254  -3.126  1.00 8.84  ? 370  GLU B O   1 
ATOM   5489 C  CB  . GLU B 1 265 ? -21.206 38.348  -5.222  1.00 8.90  ? 370  GLU B CB  1 
ATOM   5490 C  CG  . GLU B 1 265 ? -20.924 37.824  -6.652  1.00 9.66  ? 370  GLU B CG  1 
ATOM   5491 C  CD  . GLU B 1 265 ? -22.233 37.711  -7.431  1.00 9.55  ? 370  GLU B CD  1 
ATOM   5492 O  OE1 . GLU B 1 265 ? -23.190 37.062  -7.078  1.00 11.47 ? 370  GLU B OE1 1 
ATOM   5493 O  OE2 . GLU B 1 265 ? -22.209 38.290  -8.607  1.00 13.50 ? 370  GLU B OE2 1 
ATOM   5494 N  N   . VAL B 1 266 ? -20.863 38.685  -2.050  1.00 8.85  ? 371  VAL B N   1 
ATOM   5495 C  CA  . VAL B 1 266 ? -20.986 39.519  -0.797  1.00 8.53  ? 371  VAL B CA  1 
ATOM   5496 C  C   . VAL B 1 266 ? -19.588 39.777  -0.255  1.00 8.49  ? 371  VAL B C   1 
ATOM   5497 O  O   . VAL B 1 266 ? -19.281 40.902  0.174   1.00 8.95  ? 371  VAL B O   1 
ATOM   5498 C  CB  . VAL B 1 266 ? -21.874 38.812  0.185   1.00 9.52  ? 371  VAL B CB  1 
ATOM   5499 C  CG1 . VAL B 1 266 ? -21.736 39.441  1.614   1.00 10.71 ? 371  VAL B CG1 1 
ATOM   5500 C  CG2 . VAL B 1 266 ? -23.307 38.943  -0.352  1.00 11.49 ? 371  VAL B CG2 1 
ATOM   5501 N  N   . GLU B 1 267 ? -18.701 38.744  -0.182  1.00 8.24  ? 372  GLU B N   1 
ATOM   5502 C  CA  . GLU B 1 267 ? -17.377 38.999  0.292   1.00 8.52  ? 372  GLU B CA  1 
ATOM   5503 C  C   . GLU B 1 267 ? -16.671 40.050  -0.556  1.00 9.19  ? 372  GLU B C   1 
ATOM   5504 O  O   . GLU B 1 267 ? -16.069 41.041  -0.020  1.00 9.67  ? 372  GLU B O   1 
ATOM   5505 C  CB  . GLU B 1 267 ? -16.619 37.646  0.300   1.00 9.98  ? 372  GLU B CB  1 
ATOM   5506 C  CG  . GLU B 1 267 ? -15.186 37.854  0.711   1.00 11.24 ? 372  GLU B CG  1 
ATOM   5507 C  CD  . GLU B 1 267 ? -14.391 36.558  0.679   1.00 18.50 ? 372  GLU B CD  1 
ATOM   5508 O  OE1 . GLU B 1 267 ? -14.905 35.439  0.531   1.00 18.47 ? 372  GLU B OE1 1 
ATOM   5509 O  OE2 . GLU B 1 267 ? -13.112 36.677  0.714   1.00 25.00 ? 372  GLU B OE2 1 
ATOM   5510 N  N   . HIS B 1 268 ? -16.724 39.945  -1.902  1.00 8.29  ? 373  HIS B N   1 
ATOM   5511 C  CA  . HIS B 1 268 ? -16.092 40.928  -2.718  1.00 8.21  ? 373  HIS B CA  1 
ATOM   5512 C  C   . HIS B 1 268 ? -16.611 42.376  -2.488  1.00 7.80  ? 373  HIS B C   1 
ATOM   5513 O  O   . HIS B 1 268 ? -15.818 43.321  -2.388  1.00 8.82  ? 373  HIS B O   1 
ATOM   5514 C  CB  . HIS B 1 268 ? -16.258 40.533  -4.219  1.00 8.08  ? 373  HIS B CB  1 
ATOM   5515 C  CG  . HIS B 1 268 ? -15.516 41.479  -5.104  1.00 9.52  ? 373  HIS B CG  1 
ATOM   5516 N  ND1 . HIS B 1 268 ? -14.137 41.401  -5.311  1.00 10.59 ? 373  HIS B ND1 1 
ATOM   5517 C  CD2 . HIS B 1 268 ? -15.952 42.582  -5.799  1.00 8.84  ? 373  HIS B CD2 1 
ATOM   5518 C  CE1 . HIS B 1 268 ? -13.763 42.393  -6.131  1.00 10.86 ? 373  HIS B CE1 1 
ATOM   5519 N  NE2 . HIS B 1 268 ? -14.834 43.140  -6.410  1.00 9.33  ? 373  HIS B NE2 1 
ATOM   5520 N  N   . TRP B 1 269 ? -17.909 42.484  -2.486  1.00 8.46  ? 374  TRP B N   1 
ATOM   5521 C  CA  . TRP B 1 269 ? -18.496 43.854  -2.523  1.00 8.53  ? 374  TRP B CA  1 
ATOM   5522 C  C   . TRP B 1 269 ? -18.492 44.502  -1.143  1.00 8.69  ? 374  TRP B C   1 
ATOM   5523 O  O   . TRP B 1 269 ? -18.556 45.747  -1.096  1.00 8.87  ? 374  TRP B O   1 
ATOM   5524 C  CB  . TRP B 1 269 ? -19.886 43.828  -3.063  1.00 9.30  ? 374  TRP B CB  1 
ATOM   5525 C  CG  . TRP B 1 269 ? -19.945 43.545  -4.604  1.00 8.21  ? 374  TRP B CG  1 
ATOM   5526 C  CD1 . TRP B 1 269 ? -20.604 42.492  -5.162  1.00 9.93  ? 374  TRP B CD1 1 
ATOM   5527 C  CD2 . TRP B 1 269 ? -19.285 44.272  -5.614  1.00 9.16  ? 374  TRP B CD2 1 
ATOM   5528 N  NE1 . TRP B 1 269 ? -20.396 42.556  -6.549  1.00 10.29 ? 374  TRP B NE1 1 
ATOM   5529 C  CE2 . TRP B 1 269 ? -19.555 43.594  -6.852  1.00 8.95  ? 374  TRP B CE2 1 
ATOM   5530 C  CE3 . TRP B 1 269 ? -18.465 45.416  -5.629  1.00 10.16 ? 374  TRP B CE3 1 
ATOM   5531 C  CZ2 . TRP B 1 269 ? -19.081 44.085  -8.118  1.00 9.56  ? 374  TRP B CZ2 1 
ATOM   5532 C  CZ3 . TRP B 1 269 ? -17.920 45.859  -6.894  1.00 12.00 ? 374  TRP B CZ3 1 
ATOM   5533 C  CH2 . TRP B 1 269 ? -18.294 45.177  -8.125  1.00 10.53 ? 374  TRP B CH2 1 
ATOM   5534 N  N   . PHE B 1 270 ? -18.423 43.737  -0.021  1.00 8.16  ? 375  PHE B N   1 
ATOM   5535 C  CA  . PHE B 1 270 ? -18.563 44.326  1.334   1.00 7.96  ? 375  PHE B CA  1 
ATOM   5536 C  C   . PHE B 1 270 ? -17.336 44.158  2.211   1.00 8.57  ? 375  PHE B C   1 
ATOM   5537 O  O   . PHE B 1 270 ? -17.186 44.980  3.124   1.00 9.88  ? 375  PHE B O   1 
ATOM   5538 C  CB  . PHE B 1 270 ? -19.802 43.776  2.050   1.00 9.43  ? 375  PHE B CB  1 
ATOM   5539 C  CG  . PHE B 1 270 ? -21.055 44.174  1.346   1.00 8.33  ? 375  PHE B CG  1 
ATOM   5540 C  CD1 . PHE B 1 270 ? -21.566 45.460  1.491   1.00 9.85  ? 375  PHE B CD1 1 
ATOM   5541 C  CD2 . PHE B 1 270 ? -21.689 43.264  0.471   1.00 9.40  ? 375  PHE B CD2 1 
ATOM   5542 C  CE1 . PHE B 1 270 ? -22.749 45.814  0.808   1.00 10.73 ? 375  PHE B CE1 1 
ATOM   5543 C  CE2 . PHE B 1 270 ? -22.843 43.648  -0.243  1.00 9.87  ? 375  PHE B CE2 1 
ATOM   5544 C  CZ  . PHE B 1 270 ? -23.391 44.920  -0.049  1.00 10.09 ? 375  PHE B CZ  1 
ATOM   5545 N  N   . TYR B 1 271 ? -16.474 43.156  2.015   1.00 9.38  ? 376  TYR B N   1 
ATOM   5546 C  CA  . TYR B 1 271 ? -15.384 42.988  2.976   1.00 9.30  ? 376  TYR B CA  1 
ATOM   5547 C  C   . TYR B 1 271 ? -14.519 44.220  2.933   1.00 10.27 ? 376  TYR B C   1 
ATOM   5548 O  O   . TYR B 1 271 ? -14.073 44.690  1.863   1.00 10.53 ? 376  TYR B O   1 
ATOM   5549 C  CB  . TYR B 1 271 ? -14.570 41.711  2.599   1.00 10.26 ? 376  TYR B CB  1 
ATOM   5550 C  CG  . TYR B 1 271 ? -13.499 41.393  3.658   1.00 10.48 ? 376  TYR B CG  1 
ATOM   5551 C  CD1 . TYR B 1 271 ? -13.860 40.824  4.833   1.00 12.77 ? 376  TYR B CD1 1 
ATOM   5552 C  CD2 . TYR B 1 271 ? -12.223 41.749  3.424   1.00 12.42 ? 376  TYR B CD2 1 
ATOM   5553 C  CE1 . TYR B 1 271 ? -12.888 40.521  5.826   1.00 13.72 ? 376  TYR B CE1 1 
ATOM   5554 C  CE2 . TYR B 1 271 ? -11.186 41.433  4.384   1.00 13.17 ? 376  TYR B CE2 1 
ATOM   5555 C  CZ  . TYR B 1 271 ? -11.571 40.858  5.546   1.00 13.74 ? 376  TYR B CZ  1 
ATOM   5556 O  OH  . TYR B 1 271 ? -10.636 40.524  6.560   1.00 16.76 ? 376  TYR B OH  1 
ATOM   5557 N  N   . PRO B 1 272 ? -14.162 44.811  4.093   1.00 9.17  ? 377  PRO B N   1 
ATOM   5558 C  CA  . PRO B 1 272 ? -13.564 46.174  4.026   1.00 10.28 ? 377  PRO B CA  1 
ATOM   5559 C  C   . PRO B 1 272 ? -12.198 46.162  3.359   1.00 10.35 ? 377  PRO B C   1 
ATOM   5560 O  O   . PRO B 1 272 ? -11.326 45.272  3.619   1.00 11.92 ? 377  PRO B O   1 
ATOM   5561 C  CB  . PRO B 1 272 ? -13.478 46.588  5.521   1.00 10.52 ? 377  PRO B CB  1 
ATOM   5562 C  CG  . PRO B 1 272 ? -14.663 45.878  6.159   1.00 10.79 ? 377  PRO B CG  1 
ATOM   5563 C  CD  . PRO B 1 272 ? -14.703 44.504  5.490   1.00 9.84  ? 377  PRO B CD  1 
ATOM   5564 N  N   . GLN B 1 273 ? -11.982 47.181  2.551   1.00 10.82 ? 378  GLN B N   1 
ATOM   5565 C  CA  . GLN B 1 273 ? -10.666 47.477  2.005   1.00 10.73 ? 378  GLN B CA  1 
ATOM   5566 C  C   . GLN B 1 273 ? -10.417 48.957  2.156   1.00 11.23 ? 378  GLN B C   1 
ATOM   5567 O  O   . GLN B 1 273 ? -11.196 49.790  1.675   1.00 11.25 ? 378  GLN B O   1 
ATOM   5568 C  CB  . GLN B 1 273 ? -10.596 47.121  0.497   1.00 11.72 ? 378  GLN B CB  1 
ATOM   5569 C  CG  . GLN B 1 273 ? -10.739 45.634  0.120   1.00 12.94 ? 378  GLN B CG  1 
ATOM   5570 C  CD  . GLN B 1 273 ? -10.605 45.411  -1.398  1.00 15.62 ? 378  GLN B CD  1 
ATOM   5571 O  OE1 . GLN B 1 273 ? -11.545 44.834  -2.019  1.00 17.15 ? 378  GLN B OE1 1 
ATOM   5572 N  NE2 . GLN B 1 273 ? -9.609  46.020  -2.056  1.00 14.98 ? 378  GLN B NE2 1 
ATOM   5573 N  N   . GLU B 1 274 ? -9.357  49.319  2.882   1.00 13.91 ? 379  GLU B N   1 
ATOM   5574 C  CA  . GLU B 1 274 ? -9.155  50.736  3.227   1.00 13.80 ? 379  GLU B CA  1 
ATOM   5575 C  C   . GLU B 1 274 ? -9.086  51.592  1.966   1.00 13.31 ? 379  GLU B C   1 
ATOM   5576 O  O   . GLU B 1 274 ? -8.500  51.230  0.933   1.00 14.63 ? 379  GLU B O   1 
ATOM   5577 C  CB  . GLU B 1 274 ? -7.793  50.837  3.999   1.00 18.02 ? 379  GLU B CB  1 
ATOM   5578 C  CG  . GLU B 1 274 ? -7.528  52.229  4.482   1.00 21.13 ? 379  GLU B CG  1 
ATOM   5579 C  CD  . GLU B 1 274 ? -6.314  52.296  5.451   1.00 29.82 ? 379  GLU B CD  1 
ATOM   5580 O  OE1 . GLU B 1 274 ? -5.480  51.329  5.442   1.00 34.99 ? 379  GLU B OE1 1 
ATOM   5581 O  OE2 . GLU B 1 274 ? -6.182  53.289  6.208   1.00 37.55 ? 379  GLU B OE2 1 
ATOM   5582 N  N   . ASN B 1 275 ? -9.762  52.721  2.027   1.00 13.65 ? 380  ASN B N   1 
ATOM   5583 C  CA  . ASN B 1 275 ? -9.799  53.672  0.887   1.00 14.32 ? 380  ASN B CA  1 
ATOM   5584 C  C   . ASN B 1 275 ? -10.556 53.200  -0.353  1.00 13.20 ? 380  ASN B C   1 
ATOM   5585 O  O   . ASN B 1 275 ? -10.479 53.817  -1.446  1.00 13.17 ? 380  ASN B O   1 
ATOM   5586 C  CB  . ASN B 1 275 ? -8.340  54.178  0.480   1.00 17.57 ? 380  ASN B CB  1 
ATOM   5587 C  CG  . ASN B 1 275 ? -7.629  54.881  1.621   1.00 24.09 ? 380  ASN B CG  1 
ATOM   5588 O  OD1 . ASN B 1 275 ? -8.217  55.698  2.337   1.00 26.07 ? 380  ASN B OD1 1 
ATOM   5589 N  ND2 . ASN B 1 275 ? -6.420  54.479  1.855   1.00 28.55 ? 380  ASN B ND2 1 
ATOM   5590 N  N   . ILE B 1 276 ? -11.384 52.148  -0.148  1.00 11.15 ? 381  ILE B N   1 
ATOM   5591 C  CA  . ILE B 1 276 ? -12.203 51.611  -1.255  1.00 10.70 ? 381  ILE B CA  1 
ATOM   5592 C  C   . ILE B 1 276 ? -13.655 51.382  -0.714  1.00 9.39  ? 381  ILE B C   1 
ATOM   5593 O  O   . ILE B 1 276 ? -14.596 52.003  -1.261  1.00 10.17 ? 381  ILE B O   1 
ATOM   5594 C  CB  . ILE B 1 276 ? -11.615 50.312  -1.858  1.00 11.13 ? 381  ILE B CB  1 
ATOM   5595 C  CG1 . ILE B 1 276 ? -10.205 50.507  -2.444  1.00 13.25 ? 381  ILE B CG1 1 
ATOM   5596 C  CG2 . ILE B 1 276 ? -12.624 49.748  -2.914  1.00 11.91 ? 381  ILE B CG2 1 
ATOM   5597 C  CD1 . ILE B 1 276 ? -9.517  49.226  -2.868  1.00 13.04 ? 381  ILE B CD1 1 
ATOM   5598 N  N   . ILE B 1 277 ? -13.781 50.451  0.236   1.00 9.00  ? 382  ILE B N   1 
ATOM   5599 C  CA  . ILE B 1 277 ? -15.137 50.058  0.710   1.00 9.82  ? 382  ILE B CA  1 
ATOM   5600 C  C   . ILE B 1 277 ? -15.033 49.905  2.238   1.00 9.01  ? 382  ILE B C   1 
ATOM   5601 O  O   . ILE B 1 277 ? -14.167 49.209  2.769   1.00 9.24  ? 382  ILE B O   1 
ATOM   5602 C  CB  . ILE B 1 277 ? -15.658 48.778  -0.006  1.00 9.44  ? 382  ILE B CB  1 
ATOM   5603 C  CG1 . ILE B 1 277 ? -16.964 48.227  0.542   1.00 10.64 ? 382  ILE B CG1 1 
ATOM   5604 C  CG2 . ILE B 1 277 ? -14.612 47.630  0.002   1.00 11.19 ? 382  ILE B CG2 1 
ATOM   5605 C  CD1 . ILE B 1 277 ? -18.151 49.159  0.300   1.00 11.57 ? 382  ILE B CD1 1 
ATOM   5606 N  N   . ASP B 1 278 ? -16.032 50.460  2.906   1.00 9.03  ? 383  ASP B N   1 
ATOM   5607 C  CA  . ASP B 1 278 ? -16.195 50.292  4.376   1.00 9.32  ? 383  ASP B CA  1 
ATOM   5608 C  C   . ASP B 1 278 ? -17.524 49.679  4.655   1.00 9.68  ? 383  ASP B C   1 
ATOM   5609 O  O   . ASP B 1 278 ? -18.564 50.097  4.083   1.00 9.60  ? 383  ASP B O   1 
ATOM   5610 C  CB  . ASP B 1 278 ? -16.121 51.686  5.041   1.00 11.85 ? 383  ASP B CB  1 
ATOM   5611 C  CG  . ASP B 1 278 ? -14.711 52.131  5.194   1.00 12.02 ? 383  ASP B CG  1 
ATOM   5612 O  OD1 . ASP B 1 278 ? -14.021 51.622  6.115   1.00 12.81 ? 383  ASP B OD1 1 
ATOM   5613 O  OD2 . ASP B 1 278 ? -14.239 52.995  4.430   1.00 12.64 ? 383  ASP B OD2 1 
ATOM   5614 N  N   . THR B 1 279 ? -17.529 48.652  5.538   1.00 9.29  ? 384  THR B N   1 
ATOM   5615 C  CA  . THR B 1 279 ? -18.823 48.056  5.970   1.00 9.41  ? 384  THR B CA  1 
ATOM   5616 C  C   . THR B 1 279 ? -18.723 47.871  7.473   1.00 8.88  ? 384  THR B C   1 
ATOM   5617 O  O   . THR B 1 279 ? -17.677 47.324  7.964   1.00 9.94  ? 384  THR B O   1 
ATOM   5618 C  CB  . THR B 1 279 ? -18.990 46.660  5.349   1.00 8.22  ? 384  THR B CB  1 
ATOM   5619 O  OG1 . THR B 1 279 ? -19.012 46.849  3.906   1.00 10.35 ? 384  THR B OG1 1 
ATOM   5620 C  CG2 . THR B 1 279 ? -20.310 46.018  5.680   1.00 9.67  ? 384  THR B CG2 1 
ATOM   5621 N  N   . PHE B 1 280 ? -19.731 48.331  8.193   1.00 8.97  ? 385  PHE B N   1 
ATOM   5622 C  CA  . PHE B 1 280 ? -19.758 48.135  9.701   1.00 8.62  ? 385  PHE B CA  1 
ATOM   5623 C  C   . PHE B 1 280 ? -21.012 47.388  9.967   1.00 8.57  ? 385  PHE B C   1 
ATOM   5624 O  O   . PHE B 1 280 ? -22.105 47.674  9.432   1.00 9.95  ? 385  PHE B O   1 
ATOM   5625 C  CB  . PHE B 1 280 ? -19.778 49.475  10.436  1.00 10.58 ? 385  PHE B CB  1 
ATOM   5626 C  CG  . PHE B 1 280 ? -18.447 50.183  10.412  1.00 10.87 ? 385  PHE B CG  1 
ATOM   5627 C  CD1 . PHE B 1 280 ? -17.739 50.307  11.638  1.00 13.10 ? 385  PHE B CD1 1 
ATOM   5628 C  CD2 . PHE B 1 280 ? -17.912 50.748  9.300   1.00 13.57 ? 385  PHE B CD2 1 
ATOM   5629 C  CE1 . PHE B 1 280 ? -16.472 50.940  11.656  1.00 15.14 ? 385  PHE B CE1 1 
ATOM   5630 C  CE2 . PHE B 1 280 ? -16.615 51.399  9.361   1.00 15.71 ? 385  PHE B CE2 1 
ATOM   5631 C  CZ  . PHE B 1 280 ? -15.936 51.448  10.568  1.00 15.74 ? 385  PHE B CZ  1 
ATOM   5632 N  N   . VAL B 1 281 ? -20.949 46.418  10.871  1.00 8.65  ? 386  VAL B N   1 
ATOM   5633 C  CA  . VAL B 1 281 ? -22.063 45.618  11.337  1.00 8.96  ? 386  VAL B CA  1 
ATOM   5634 C  C   . VAL B 1 281 ? -22.413 45.998  12.797  1.00 9.34  ? 386  VAL B C   1 
ATOM   5635 O  O   . VAL B 1 281 ? -21.547 46.497  13.525  1.00 10.32 ? 386  VAL B O   1 
ATOM   5636 C  CB  . VAL B 1 281 ? -21.736 44.101  11.277  1.00 9.72  ? 386  VAL B CB  1 
ATOM   5637 C  CG1 . VAL B 1 281 ? -21.377 43.751  9.820   1.00 10.40 ? 386  VAL B CG1 1 
ATOM   5638 C  CG2 . VAL B 1 281 ? -20.626 43.649  12.226  1.00 10.78 ? 386  VAL B CG2 1 
ATOM   5639 N  N   . VAL B 1 282 ? -23.678 45.744  13.129  1.00 9.25  ? 387  VAL B N   1 
ATOM   5640 C  CA  . VAL B 1 282 ? -24.124 45.918  14.559  1.00 9.39  ? 387  VAL B CA  1 
ATOM   5641 C  C   . VAL B 1 282 ? -24.207 44.529  15.110  1.00 9.98  ? 387  VAL B C   1 
ATOM   5642 O  O   . VAL B 1 282 ? -25.000 43.681  14.672  1.00 10.63 ? 387  VAL B O   1 
ATOM   5643 C  CB  . VAL B 1 282 ? -25.518 46.572  14.578  1.00 9.97  ? 387  VAL B CB  1 
ATOM   5644 C  CG1 . VAL B 1 282 ? -25.948 46.695  16.086  1.00 11.05 ? 387  VAL B CG1 1 
ATOM   5645 C  CG2 . VAL B 1 282 ? -25.458 47.995  14.015  1.00 11.79 ? 387  VAL B CG2 1 
ATOM   5646 N  N   . GLU B 1 283 ? -23.381 44.277  16.120  1.00 9.57  ? 388  GLU B N   1 
ATOM   5647 C  CA  . GLU B 1 283 ? -23.415 42.980  16.858  1.00 9.95  ? 388  GLU B CA  1 
ATOM   5648 C  C   . GLU B 1 283 ? -23.938 43.255  18.265  1.00 9.69  ? 388  GLU B C   1 
ATOM   5649 O  O   . GLU B 1 283 ? -23.304 44.006  19.029  1.00 10.99 ? 388  GLU B O   1 
ATOM   5650 C  CB  . GLU B 1 283 ? -22.020 42.374  16.963  1.00 10.63 ? 388  GLU B CB  1 
ATOM   5651 C  CG  . GLU B 1 283 ? -21.974 41.053  17.789  1.00 10.00 ? 388  GLU B CG  1 
ATOM   5652 C  CD  . GLU B 1 283 ? -20.616 40.603  18.079  1.00 11.30 ? 388  GLU B CD  1 
ATOM   5653 O  OE1 . GLU B 1 283 ? -20.535 39.610  18.964  1.00 10.99 ? 388  GLU B OE1 1 
ATOM   5654 O  OE2 . GLU B 1 283 ? -19.570 41.006  17.642  1.00 13.15 ? 388  GLU B OE2 1 
ATOM   5655 N  N   . ASN B 1 284 ? -25.075 42.672  18.548  1.00 9.82  ? 389  ASN B N   1 
ATOM   5656 C  CA  . ASN B 1 284 ? -25.833 42.974  19.804  1.00 10.61 ? 389  ASN B CA  1 
ATOM   5657 C  C   . ASN B 1 284 ? -25.266 42.257  21.056  1.00 10.10 ? 389  ASN B C   1 
ATOM   5658 O  O   . ASN B 1 284 ? -24.217 41.590  21.011  1.00 9.90  ? 389  ASN B O   1 
ATOM   5659 C  CB  . ASN B 1 284 ? -27.304 42.772  19.597  1.00 10.77 ? 389  ASN B CB  1 
ATOM   5660 C  CG  . ASN B 1 284 ? -27.716 41.352  19.467  1.00 12.68 ? 389  ASN B CG  1 
ATOM   5661 O  OD1 . ASN B 1 284 ? -26.952 40.435  19.816  1.00 11.95 ? 389  ASN B OD1 1 
ATOM   5662 N  ND2 . ASN B 1 284 ? -28.963 41.066  19.020  1.00 15.61 ? 389  ASN B ND2 1 
ATOM   5663 N  N   . ALA B 1 285 ? -25.997 42.432  22.156  1.00 10.17 ? 390  ALA B N   1 
ATOM   5664 C  CA  . ALA B 1 285 ? -25.517 41.908  23.461  1.00 9.83  ? 390  ALA B CA  1 
ATOM   5665 C  C   . ALA B 1 285 ? -25.512 40.387  23.483  1.00 9.87  ? 390  ALA B C   1 
ATOM   5666 O  O   . ALA B 1 285 ? -24.948 39.785  24.421  1.00 9.59  ? 390  ALA B O   1 
ATOM   5667 C  CB  . ALA B 1 285 ? -26.443 42.483  24.565  1.00 10.04 ? 390  ALA B CB  1 
ATOM   5668 N  N   . ASN B 1 286 ? -26.194 39.764  22.500  1.00 10.25 ? 391  ASN B N   1 
ATOM   5669 C  CA  . ASN B 1 286 ? -26.256 38.291  22.378  1.00 10.37 ? 391  ASN B CA  1 
ATOM   5670 C  C   . ASN B 1 286 ? -25.218 37.786  21.448  1.00 10.95 ? 391  ASN B C   1 
ATOM   5671 O  O   . ASN B 1 286 ? -25.140 36.557  21.226  1.00 12.84 ? 391  ASN B O   1 
ATOM   5672 C  CB  . ASN B 1 286 ? -27.650 37.831  21.927  1.00 12.31 ? 391  ASN B CB  1 
ATOM   5673 C  CG  . ASN B 1 286 ? -28.721 37.951  23.000  1.00 18.74 ? 391  ASN B CG  1 
ATOM   5674 O  OD1 . ASN B 1 286 ? -28.809 38.863  23.666  1.00 18.19 ? 391  ASN B OD1 1 
ATOM   5675 N  ND2 . ASN B 1 286 ? -29.431 36.860  23.261  1.00 22.18 ? 391  ASN B ND2 1 
ATOM   5676 N  N   . GLY B 1 287 ? -24.437 38.660  20.823  1.00 9.61  ? 392  GLY B N   1 
ATOM   5677 C  CA  . GLY B 1 287 ? -23.499 38.258  19.776  1.00 10.94 ? 392  GLY B CA  1 
ATOM   5678 C  C   . GLY B 1 287 ? -24.106 38.169  18.391  1.00 11.43 ? 392  GLY B C   1 
ATOM   5679 O  O   . GLY B 1 287 ? -23.353 37.664  17.517  1.00 12.84 ? 392  GLY B O   1 
ATOM   5680 N  N   . GLU B 1 288 ? -25.334 38.551  18.176  1.00 11.24 ? 393  GLU B N   1 
ATOM   5681 C  CA  A GLU B 1 288 ? -25.972 38.379  16.831  0.50 11.12 ? 393  GLU B CA  1 
ATOM   5682 C  CA  B GLU B 1 288 ? -26.018 38.381  16.856  0.50 11.42 ? 393  GLU B CA  1 
ATOM   5683 C  C   . GLU B 1 288 ? -25.796 39.667  16.044  1.00 11.12 ? 393  GLU B C   1 
ATOM   5684 O  O   . GLU B 1 288 ? -25.966 40.806  16.573  1.00 10.83 ? 393  GLU B O   1 
ATOM   5685 C  CB  A GLU B 1 288 ? -27.474 38.082  17.031  0.50 14.09 ? 393  GLU B CB  1 
ATOM   5686 C  CB  B GLU B 1 288 ? -27.542 38.171  17.132  0.50 14.88 ? 393  GLU B CB  1 
ATOM   5687 C  CG  A GLU B 1 288 ? -28.296 37.858  15.764  0.50 15.39 ? 393  GLU B CG  1 
ATOM   5688 C  CG  B GLU B 1 288 ? -27.943 36.805  17.762  0.50 17.49 ? 393  GLU B CG  1 
ATOM   5689 C  CD  A GLU B 1 288 ? -29.803 37.677  15.935  0.50 23.87 ? 393  GLU B CD  1 
ATOM   5690 C  CD  B GLU B 1 288 ? -29.132 36.819  18.775  0.50 22.66 ? 393  GLU B CD  1 
ATOM   5691 O  OE1 A GLU B 1 288 ? -30.328 37.679  17.053  0.50 30.53 ? 393  GLU B OE1 1 
ATOM   5692 O  OE1 B GLU B 1 288 ? -29.345 35.696  19.373  0.50 23.95 ? 393  GLU B OE1 1 
ATOM   5693 O  OE2 A GLU B 1 288 ? -30.474 37.531  14.894  0.50 21.79 ? 393  GLU B OE2 1 
ATOM   5694 O  OE2 B GLU B 1 288 ? -29.801 37.889  19.021  0.50 22.38 ? 393  GLU B OE2 1 
ATOM   5695 N  N   . VAL B 1 289 ? -25.451 39.506  14.761  1.00 10.93 ? 394  VAL B N   1 
ATOM   5696 C  CA  . VAL B 1 289 ? -25.388 40.665  13.821  1.00 10.99 ? 394  VAL B CA  1 
ATOM   5697 C  C   . VAL B 1 289 ? -26.732 40.897  13.265  1.00 10.85 ? 394  VAL B C   1 
ATOM   5698 O  O   . VAL B 1 289 ? -27.345 40.026  12.621  1.00 12.19 ? 394  VAL B O   1 
ATOM   5699 C  CB  . VAL B 1 289 ? -24.362 40.384  12.708  1.00 10.50 ? 394  VAL B CB  1 
ATOM   5700 C  CG1 . VAL B 1 289 ? -24.449 41.488  11.641  1.00 11.61 ? 394  VAL B CG1 1 
ATOM   5701 C  CG2 . VAL B 1 289 ? -22.903 40.307  13.306  1.00 13.74 ? 394  VAL B CG2 1 
ATOM   5702 N  N   . THR B 1 290 ? -27.247 42.113  13.491  1.00 9.84  ? 395  THR B N   1 
ATOM   5703 C  CA  . THR B 1 290 ? -28.650 42.412  13.110  1.00 12.17 ? 395  THR B CA  1 
ATOM   5704 C  C   . THR B 1 290 ? -28.765 43.532  12.024  1.00 10.21 ? 395  THR B C   1 
ATOM   5705 O  O   . THR B 1 290 ? -29.849 43.770  11.518  1.00 11.26 ? 395  THR B O   1 
ATOM   5706 C  CB  . THR B 1 290 ? -29.469 42.906  14.350  1.00 11.43 ? 395  THR B CB  1 
ATOM   5707 O  OG1 . THR B 1 290 ? -28.747 43.907  14.961  1.00 12.18 ? 395  THR B OG1 1 
ATOM   5708 C  CG2 . THR B 1 290 ? -29.565 41.716  15.396  1.00 15.20 ? 395  THR B CG2 1 
ATOM   5709 N  N   . ASP B 1 291 ? -27.672 44.277  11.773  1.00 9.51  ? 396  ASP B N   1 
ATOM   5710 C  CA  . ASP B 1 291 ? -27.791 45.405  10.837  1.00 9.67  ? 396  ASP B CA  1 
ATOM   5711 C  C   . ASP B 1 291 ? -26.420 45.631  10.256  1.00 9.28  ? 396  ASP B C   1 
ATOM   5712 O  O   . ASP B 1 291 ? -25.368 45.212  10.822  1.00 9.58  ? 396  ASP B O   1 
ATOM   5713 C  CB  . ASP B 1 291 ? -28.195 46.733  11.554  1.00 10.85 ? 396  ASP B CB  1 
ATOM   5714 C  CG  . ASP B 1 291 ? -29.378 46.584  12.460  1.00 10.87 ? 396  ASP B CG  1 
ATOM   5715 O  OD1 . ASP B 1 291 ? -29.123 46.266  13.705  1.00 12.86 ? 396  ASP B OD1 1 
ATOM   5716 O  OD2 . ASP B 1 291 ? -30.543 46.785  12.067  1.00 11.86 ? 396  ASP B OD2 1 
ATOM   5717 N  N   . PHE B 1 292 ? -26.379 46.301  9.066   1.00 9.00  ? 397  PHE B N   1 
ATOM   5718 C  CA  . PHE B 1 292 ? -25.042 46.766  8.642   1.00 8.54  ? 397  PHE B CA  1 
ATOM   5719 C  C   . PHE B 1 292 ? -25.202 48.021  7.752   1.00 8.25  ? 397  PHE B C   1 
ATOM   5720 O  O   . PHE B 1 292 ? -26.251 48.225  7.140   1.00 9.18  ? 397  PHE B O   1 
ATOM   5721 C  CB  . PHE B 1 292 ? -24.194 45.638  7.854   1.00 9.09  ? 397  PHE B CB  1 
ATOM   5722 C  CG  . PHE B 1 292 ? -24.719 45.262  6.476   1.00 8.84  ? 397  PHE B CG  1 
ATOM   5723 C  CD1 . PHE B 1 292 ? -24.331 46.029  5.362   1.00 8.93  ? 397  PHE B CD1 1 
ATOM   5724 C  CD2 . PHE B 1 292 ? -25.612 44.172  6.325   1.00 9.87  ? 397  PHE B CD2 1 
ATOM   5725 C  CE1 . PHE B 1 292 ? -24.792 45.632  4.073   1.00 10.38 ? 397  PHE B CE1 1 
ATOM   5726 C  CE2 . PHE B 1 292 ? -26.018 43.803  5.042   1.00 10.65 ? 397  PHE B CE2 1 
ATOM   5727 C  CZ  . PHE B 1 292 ? -25.632 44.539  3.912   1.00 10.41 ? 397  PHE B CZ  1 
ATOM   5728 N  N   . LEU B 1 293 ? -24.114 48.802  7.686   1.00 7.91  ? 398  LEU B N   1 
ATOM   5729 C  CA  . LEU B 1 293 ? -24.051 49.984  6.824   1.00 8.60  ? 398  LEU B CA  1 
ATOM   5730 C  C   . LEU B 1 293 ? -22.817 49.894  5.959   1.00 9.58  ? 398  LEU B C   1 
ATOM   5731 O  O   . LEU B 1 293 ? -21.821 49.221  6.363   1.00 8.88  ? 398  LEU B O   1 
ATOM   5732 C  CB  . LEU B 1 293 ? -24.034 51.309  7.662   1.00 10.17 ? 398  LEU B CB  1 
ATOM   5733 C  CG  . LEU B 1 293 ? -22.805 51.482  8.550   1.00 10.14 ? 398  LEU B CG  1 
ATOM   5734 C  CD1 . LEU B 1 293 ? -21.684 52.248  7.861   1.00 11.06 ? 398  LEU B CD1 1 
ATOM   5735 C  CD2 . LEU B 1 293 ? -23.144 52.285  9.845   1.00 9.94  ? 398  LEU B CD2 1 
ATOM   5736 N  N   . SER B 1 294 ? -22.810 50.488  4.761   1.00 8.71  ? 399  SER B N   1 
ATOM   5737 C  CA  . SER B 1 294 ? -21.611 50.470  3.940   1.00 8.68  ? 399  SER B CA  1 
ATOM   5738 C  C   . SER B 1 294 ? -21.538 51.726  3.038   1.00 7.90  ? 399  SER B C   1 
ATOM   5739 O  O   . SER B 1 294 ? -22.595 52.266  2.660   1.00 8.94  ? 399  SER B O   1 
ATOM   5740 C  CB  . SER B 1 294 ? -21.577 49.185  3.043   1.00 9.05  ? 399  SER B CB  1 
ATOM   5741 O  OG  . SER B 1 294 ? -22.664 49.064  2.155   1.00 8.94  ? 399  SER B OG  1 
ATOM   5742 N  N   . PHE B 1 295 ? -20.326 52.102  2.717   1.00 8.04  ? 400  PHE B N   1 
ATOM   5743 C  CA  . PHE B 1 295 ? -20.140 53.249  1.799   1.00 7.87  ? 400  PHE B CA  1 
ATOM   5744 C  C   . PHE B 1 295 ? -18.767 53.088  1.142   1.00 8.92  ? 400  PHE B C   1 
ATOM   5745 O  O   . PHE B 1 295 ? -17.845 52.490  1.699   1.00 9.31  ? 400  PHE B O   1 
ATOM   5746 C  CB  . PHE B 1 295 ? -20.235 54.616  2.576   1.00 8.99  ? 400  PHE B CB  1 
ATOM   5747 C  CG  . PHE B 1 295 ? -19.317 54.747  3.806   1.00 9.32  ? 400  PHE B CG  1 
ATOM   5748 C  CD1 . PHE B 1 295 ? -17.977 55.125  3.737   1.00 10.78 ? 400  PHE B CD1 1 
ATOM   5749 C  CD2 . PHE B 1 295 ? -19.853 54.493  5.094   1.00 10.17 ? 400  PHE B CD2 1 
ATOM   5750 C  CE1 . PHE B 1 295 ? -17.163 55.300  4.903   1.00 11.37 ? 400  PHE B CE1 1 
ATOM   5751 C  CE2 . PHE B 1 295 ? -19.049 54.610  6.250   1.00 11.70 ? 400  PHE B CE2 1 
ATOM   5752 C  CZ  . PHE B 1 295 ? -17.692 54.962  6.158   1.00 11.39 ? 400  PHE B CZ  1 
ATOM   5753 N  N   . TYR B 1 296 ? -18.718 53.551  -0.125  1.00 9.14  ? 401  TYR B N   1 
ATOM   5754 C  CA  . TYR B 1 296 ? -17.449 53.426  -0.893  1.00 9.57  ? 401  TYR B CA  1 
ATOM   5755 C  C   . TYR B 1 296 ? -16.727 54.816  -1.025  1.00 9.70  ? 401  TYR B C   1 
ATOM   5756 O  O   . TYR B 1 296 ? -17.376 55.884  -0.829  1.00 10.58 ? 401  TYR B O   1 
ATOM   5757 C  CB  . TYR B 1 296 ? -17.654 52.715  -2.267  1.00 9.41  ? 401  TYR B CB  1 
ATOM   5758 C  CG  . TYR B 1 296 ? -18.615 53.407  -3.262  1.00 9.75  ? 401  TYR B CG  1 
ATOM   5759 C  CD1 . TYR B 1 296 ? -18.182 54.449  -4.105  1.00 9.61  ? 401  TYR B CD1 1 
ATOM   5760 C  CD2 . TYR B 1 296 ? -19.959 52.966  -3.375  1.00 10.98 ? 401  TYR B CD2 1 
ATOM   5761 C  CE1 . TYR B 1 296 ? -19.057 55.019  -5.053  1.00 10.14 ? 401  TYR B CE1 1 
ATOM   5762 C  CE2 . TYR B 1 296 ? -20.825 53.509  -4.268  1.00 11.79 ? 401  TYR B CE2 1 
ATOM   5763 C  CZ  . TYR B 1 296 ? -20.357 54.537  -5.099  1.00 11.53 ? 401  TYR B CZ  1 
ATOM   5764 O  OH  . TYR B 1 296 ? -21.207 55.180  -5.987  1.00 15.03 ? 401  TYR B OH  1 
ATOM   5765 N  N   . THR B 1 297 ? -15.430 54.735  -1.273  1.00 9.41  ? 402  THR B N   1 
ATOM   5766 C  CA  . THR B 1 297 ? -14.566 55.909  -1.308  1.00 10.49 ? 402  THR B CA  1 
ATOM   5767 C  C   . THR B 1 297 ? -14.312 56.356  -2.758  1.00 10.69 ? 402  THR B C   1 
ATOM   5768 O  O   . THR B 1 297 ? -13.782 55.541  -3.541  1.00 10.80 ? 402  THR B O   1 
ATOM   5769 C  CB  . THR B 1 297 ? -13.188 55.531  -0.718  1.00 10.61 ? 402  THR B CB  1 
ATOM   5770 O  OG1 . THR B 1 297 ? -13.359 55.229  0.690   1.00 12.24 ? 402  THR B OG1 1 
ATOM   5771 C  CG2 . THR B 1 297 ? -12.186 56.663  -0.829  1.00 12.85 ? 402  THR B CG2 1 
ATOM   5772 N  N   . LEU B 1 298 ? -14.680 57.582  -3.099  1.00 9.72  ? 403  LEU B N   1 
ATOM   5773 C  CA  . LEU B 1 298 ? -14.554 58.074  -4.488  1.00 10.27 ? 403  LEU B CA  1 
ATOM   5774 C  C   . LEU B 1 298 ? -14.268 59.584  -4.446  1.00 10.82 ? 403  LEU B C   1 
ATOM   5775 O  O   . LEU B 1 298 ? -15.225 60.375  -4.354  1.00 10.74 ? 403  LEU B O   1 
ATOM   5776 C  CB  . LEU B 1 298 ? -15.758 57.651  -5.328  1.00 11.34 ? 403  LEU B CB  1 
ATOM   5777 C  CG  . LEU B 1 298 ? -15.811 58.246  -6.756  1.00 11.52 ? 403  LEU B CG  1 
ATOM   5778 C  CD1 . LEU B 1 298 ? -14.540 57.870  -7.485  1.00 12.60 ? 403  LEU B CD1 1 
ATOM   5779 C  CD2 . LEU B 1 298 ? -17.052 57.717  -7.500  1.00 11.98 ? 403  LEU B CD2 1 
ATOM   5780 N  N   . PRO B 1 299 ? -13.014 59.969  -4.508  1.00 10.76 ? 404  PRO B N   1 
ATOM   5781 C  CA  . PRO B 1 299 ? -12.703 61.398  -4.472  1.00 10.60 ? 404  PRO B CA  1 
ATOM   5782 C  C   . PRO B 1 299 ? -13.065 62.009  -5.809  1.00 10.74 ? 404  PRO B C   1 
ATOM   5783 O  O   . PRO B 1 299 ? -13.182 61.333  -6.870  1.00 11.18 ? 404  PRO B O   1 
ATOM   5784 C  CB  . PRO B 1 299 ? -11.226 61.483  -4.235  1.00 13.23 ? 404  PRO B CB  1 
ATOM   5785 C  CG  . PRO B 1 299 ? -10.644 60.152  -4.442  1.00 19.06 ? 404  PRO B CG  1 
ATOM   5786 C  CD  . PRO B 1 299 ? -11.807 59.134  -4.443  1.00 12.95 ? 404  PRO B CD  1 
ATOM   5787 N  N   . SER B 1 300 ? -13.210 63.373  -5.817  1.00 12.09 ? 405  SER B N   1 
ATOM   5788 C  CA  . SER B 1 300 ? -13.289 64.125  -7.096  1.00 12.34 ? 405  SER B CA  1 
ATOM   5789 C  C   . SER B 1 300 ? -12.148 65.129  -7.176  1.00 13.90 ? 405  SER B C   1 
ATOM   5790 O  O   . SER B 1 300 ? -11.833 65.843  -6.174  1.00 15.08 ? 405  SER B O   1 
ATOM   5791 C  CB  . SER B 1 300 ? -14.611 64.836  -7.254  1.00 15.72 ? 405  SER B CB  1 
ATOM   5792 O  OG  . SER B 1 300 ? -15.718 63.890  -7.572  1.00 15.96 ? 405  SER B OG  1 
ATOM   5793 N  N   . THR B 1 301 ? -11.530 65.168  -8.335  1.00 13.05 ? 406  THR B N   1 
ATOM   5794 C  CA  . THR B 1 301 ? -10.530 66.248  -8.641  1.00 13.05 ? 406  THR B CA  1 
ATOM   5795 C  C   . THR B 1 301 ? -11.251 67.557  -8.658  1.00 14.09 ? 406  THR B C   1 
ATOM   5796 O  O   . THR B 1 301 ? -12.376 67.719  -9.171  1.00 14.28 ? 406  THR B O   1 
ATOM   5797 C  CB  . THR B 1 301 ? -10.037 65.902  -10.042 1.00 13.91 ? 406  THR B CB  1 
ATOM   5798 O  OG1 . THR B 1 301 ? -9.310  64.674  -9.987  1.00 16.32 ? 406  THR B OG1 1 
ATOM   5799 C  CG2 . THR B 1 301 ? -9.063  67.071  -10.489 1.00 16.06 ? 406  THR B CG2 1 
ATOM   5800 N  N   . ILE B 1 302 ? -10.547 68.578  -8.071  1.00 15.10 ? 407  ILE B N   1 
ATOM   5801 C  CA  A ILE B 1 302 ? -11.019 69.963  -8.114  0.50 18.17 ? 407  ILE B CA  1 
ATOM   5802 C  CA  B ILE B 1 302 ? -11.047 69.952  -8.119  0.50 18.29 ? 407  ILE B CA  1 
ATOM   5803 C  C   . ILE B 1 302 ? -10.529 70.522  -9.467  1.00 18.22 ? 407  ILE B C   1 
ATOM   5804 O  O   . ILE B 1 302 ? -9.335  70.743  -9.658  1.00 19.89 ? 407  ILE B O   1 
ATOM   5805 C  CB  A ILE B 1 302 ? -10.342 70.807  -6.986  0.50 18.68 ? 407  ILE B CB  1 
ATOM   5806 C  CB  B ILE B 1 302 ? -10.495 70.785  -6.916  0.50 19.43 ? 407  ILE B CB  1 
ATOM   5807 C  CG1 A ILE B 1 302 ? -10.533 70.141  -5.611  0.50 20.59 ? 407  ILE B CG1 1 
ATOM   5808 C  CG1 B ILE B 1 302 ? -10.868 70.115  -5.574  0.50 22.19 ? 407  ILE B CG1 1 
ATOM   5809 C  CG2 A ILE B 1 302 ? -10.851 72.245  -7.003  0.50 21.23 ? 407  ILE B CG2 1 
ATOM   5810 C  CG2 B ILE B 1 302 ? -10.974 72.230  -6.988  0.50 21.84 ? 407  ILE B CG2 1 
ATOM   5811 C  CD1 A ILE B 1 302 ? -11.998 69.845  -5.325  0.50 20.08 ? 407  ILE B CD1 1 
ATOM   5812 C  CD1 B ILE B 1 302 ? -10.214 70.735  -4.361  0.50 21.90 ? 407  ILE B CD1 1 
ATOM   5813 N  N   . MET B 1 303 ? -11.435 70.639  -10.368 1.00 16.68 ? 408  MET B N   1 
ATOM   5814 C  CA  . MET B 1 303 ? -11.097 70.911  -11.780 1.00 18.58 ? 408  MET B CA  1 
ATOM   5815 C  C   . MET B 1 303 ? -10.341 72.223  -11.893 1.00 25.09 ? 408  MET B C   1 
ATOM   5816 O  O   . MET B 1 303 ? -9.372  72.292  -12.675 1.00 25.91 ? 408  MET B O   1 
ATOM   5817 C  CB  . MET B 1 303 ? -12.327 70.850  -12.603 1.00 18.68 ? 408  MET B CB  1 
ATOM   5818 C  CG  . MET B 1 303 ? -12.851 69.409  -12.941 1.00 17.45 ? 408  MET B CG  1 
ATOM   5819 S  SD  . MET B 1 303 ? -14.379 69.353  -13.798 1.00 16.51 ? 408  MET B SD  1 
ATOM   5820 C  CE  . MET B 1 303 ? -13.928 70.314  -15.302 1.00 14.42 ? 408  MET B CE  1 
ATOM   5821 N  N   . ASN B 1 304 ? -10.777 73.233  -11.157 1.00 21.58 ? 409  ASN B N   1 
ATOM   5822 C  CA  . ASN B 1 304 ? -10.016 74.542  -11.321 1.00 27.30 ? 409  ASN B CA  1 
ATOM   5823 C  C   . ASN B 1 304 ? -8.615  74.531  -10.686 1.00 29.39 ? 409  ASN B C   1 
ATOM   5824 O  O   . ASN B 1 304 ? -7.761  75.396  -11.048 1.00 33.16 ? 409  ASN B O   1 
ATOM   5825 C  CB  . ASN B 1 304 ? -10.885 75.672  -10.805 1.00 30.86 ? 409  ASN B CB  1 
ATOM   5826 C  CG  . ASN B 1 304 ? -12.142 75.816  -11.630 1.00 40.82 ? 409  ASN B CG  1 
ATOM   5827 O  OD1 . ASN B 1 304 ? -13.240 75.946  -11.082 1.00 49.49 ? 409  ASN B OD1 1 
ATOM   5828 N  ND2 . ASN B 1 304 ? -11.995 75.768  -12.969 1.00 46.78 ? 409  ASN B ND2 1 
ATOM   5829 N  N   . HIS B 1 305 ? -8.348  73.600  -9.765  1.00 31.18 ? 410  HIS B N   1 
ATOM   5830 C  CA  . HIS B 1 305 ? -7.074  73.498  -9.074  1.00 33.51 ? 410  HIS B CA  1 
ATOM   5831 C  C   . HIS B 1 305 ? -6.665  72.025  -8.957  1.00 36.61 ? 410  HIS B C   1 
ATOM   5832 O  O   . HIS B 1 305 ? -6.731  71.472  -7.833  1.00 32.81 ? 410  HIS B O   1 
ATOM   5833 C  CB  . HIS B 1 305 ? -7.187  74.167  -7.690  1.00 38.67 ? 410  HIS B CB  1 
ATOM   5834 C  CG  . HIS B 1 305 ? -7.531  75.626  -7.773  1.00 47.69 ? 410  HIS B CG  1 
ATOM   5835 N  ND1 . HIS B 1 305 ? -6.568  76.611  -7.936  1.00 50.81 ? 410  HIS B ND1 1 
ATOM   5836 C  CD2 . HIS B 1 305 ? -8.731  76.262  -7.818  1.00 46.44 ? 410  HIS B CD2 1 
ATOM   5837 C  CE1 . HIS B 1 305 ? -7.163  77.790  -8.029  1.00 49.63 ? 410  HIS B CE1 1 
ATOM   5838 N  NE2 . HIS B 1 305 ? -8.474  77.605  -7.954  1.00 51.14 ? 410  HIS B NE2 1 
ATOM   5839 N  N   . PRO B 1 306 ? -6.294  71.362  -10.101 1.00 33.12 ? 411  PRO B N   1 
ATOM   5840 C  CA  . PRO B 1 306 ? -6.053  69.879  -10.140 1.00 35.88 ? 411  PRO B CA  1 
ATOM   5841 C  C   . PRO B 1 306 ? -4.840  69.380  -9.310  1.00 37.73 ? 411  PRO B C   1 
ATOM   5842 O  O   . PRO B 1 306 ? -4.733  68.187  -9.005  1.00 38.42 ? 411  PRO B O   1 
ATOM   5843 C  CB  . PRO B 1 306 ? -5.791  69.600  -11.647 1.00 35.68 ? 411  PRO B CB  1 
ATOM   5844 C  CG  . PRO B 1 306 ? -5.287  70.924  -12.166 1.00 37.11 ? 411  PRO B CG  1 
ATOM   5845 C  CD  . PRO B 1 306 ? -6.174  71.945  -11.465 1.00 34.07 ? 411  PRO B CD  1 
ATOM   5846 N  N   . THR B 1 307 ? -3.925  70.316  -9.016  1.00 37.55 ? 412  THR B N   1 
ATOM   5847 C  CA  . THR B 1 307 ? -2.807  70.185  -8.093  1.00 41.16 ? 412  THR B CA  1 
ATOM   5848 C  C   . THR B 1 307 ? -3.302  70.078  -6.636  1.00 43.09 ? 412  THR B C   1 
ATOM   5849 O  O   . THR B 1 307 ? -2.717  69.316  -5.842  1.00 49.43 ? 412  THR B O   1 
ATOM   5850 C  CB  . THR B 1 307 ? -1.828  71.383  -8.321  0.50 39.23 ? 412  THR B CB  1 
ATOM   5851 O  OG1 . THR B 1 307 ? -0.796  70.985  -9.235  0.50 40.09 ? 412  THR B OG1 1 
ATOM   5852 C  CG2 . THR B 1 307 ? -1.235  71.957  -7.037  0.50 40.14 ? 412  THR B CG2 1 
ATOM   5853 N  N   . HIS B 1 308 ? -4.360  70.811  -6.265  1.00 36.40 ? 413  HIS B N   1 
ATOM   5854 C  CA  . HIS B 1 308 ? -4.837  70.748  -4.856  1.00 35.40 ? 413  HIS B CA  1 
ATOM   5855 C  C   . HIS B 1 308 ? -5.355  69.348  -4.483  1.00 39.41 ? 413  HIS B C   1 
ATOM   5856 O  O   . HIS B 1 308 ? -5.665  68.509  -5.365  1.00 34.61 ? 413  HIS B O   1 
ATOM   5857 C  CB  . HIS B 1 308 ? -5.885  71.825  -4.533  1.00 36.58 ? 413  HIS B CB  1 
ATOM   5858 C  CG  . HIS B 1 308 ? -5.400  73.232  -4.723  1.00 40.80 ? 413  HIS B CG  1 
ATOM   5859 N  ND1 . HIS B 1 308 ? -6.228  74.327  -4.571  1.00 41.92 ? 413  HIS B ND1 1 
ATOM   5860 C  CD2 . HIS B 1 308 ? -4.183  73.725  -5.087  1.00 41.88 ? 413  HIS B CD2 1 
ATOM   5861 C  CE1 . HIS B 1 308 ? -5.541  75.435  -4.808  1.00 45.10 ? 413  HIS B CE1 1 
ATOM   5862 N  NE2 . HIS B 1 308 ? -4.301  75.096  -5.137  1.00 42.17 ? 413  HIS B NE2 1 
ATOM   5863 N  N   . LYS B 1 309 ? -5.403  69.067  -3.179  1.00 40.67 ? 414  LYS B N   1 
ATOM   5864 C  CA  . LYS B 1 309 ? -5.911  67.776  -2.728  1.00 37.19 ? 414  LYS B CA  1 
ATOM   5865 C  C   . LYS B 1 309 ? -7.442  67.663  -3.179  1.00 25.93 ? 414  LYS B C   1 
ATOM   5866 O  O   . LYS B 1 309 ? -8.210  68.644  -3.133  1.00 28.14 ? 414  LYS B O   1 
ATOM   5867 C  CB  . LYS B 1 309 ? -5.644  67.629  -1.227  1.00 39.12 ? 414  LYS B CB  1 
ATOM   5868 C  CG  . LYS B 1 309 ? -5.003  66.304  -0.844  0.50 42.40 ? 414  LYS B CG  1 
ATOM   5869 C  CD  . LYS B 1 309 ? -3.944  66.431  0.253   0.50 43.23 ? 414  LYS B CD  1 
ATOM   5870 C  CE  . LYS B 1 309 ? -4.516  66.270  1.652   0.50 43.60 ? 414  LYS B CE  1 
ATOM   5871 N  NZ  . LYS B 1 309 ? -5.082  67.555  2.159   0.50 46.68 ? 414  LYS B NZ  1 
ATOM   5872 N  N   . SER B 1 310 ? -7.799  66.478  -3.654  1.00 29.56 ? 415  SER B N   1 
ATOM   5873 C  CA  . SER B 1 310 ? -9.144  66.194  -4.145  1.00 26.44 ? 415  SER B CA  1 
ATOM   5874 C  C   . SER B 1 310 ? -10.241 66.349  -3.039  1.00 23.70 ? 415  SER B C   1 
ATOM   5875 O  O   . SER B 1 310 ? -9.915  66.250  -1.801  1.00 25.41 ? 415  SER B O   1 
ATOM   5876 C  CB  . SER B 1 310 ? -9.113  64.744  -4.599  1.00 26.38 ? 415  SER B CB  1 
ATOM   5877 O  OG  . SER B 1 310 ? -8.736  63.906  -3.527  1.00 32.73 ? 415  SER B OG  1 
ATOM   5878 N  N   . LEU B 1 311 ? -11.485 66.595  -3.427  1.00 18.13 ? 416  LEU B N   1 
ATOM   5879 C  CA  . LEU B 1 311 ? -12.631 66.527  -2.536  1.00 18.05 ? 416  LEU B CA  1 
ATOM   5880 C  C   . LEU B 1 311 ? -12.768 65.069  -2.074  1.00 16.12 ? 416  LEU B C   1 
ATOM   5881 O  O   . LEU B 1 311 ? -12.842 64.137  -2.942  1.00 16.03 ? 416  LEU B O   1 
ATOM   5882 C  CB  . LEU B 1 311 ? -13.856 66.942  -3.342  1.00 18.89 ? 416  LEU B CB  1 
ATOM   5883 C  CG  . LEU B 1 311 ? -15.347 66.723  -2.864  1.00 19.40 ? 416  LEU B CG  1 
ATOM   5884 C  CD1 . LEU B 1 311 ? -15.589 67.817  -1.818  1.00 24.12 ? 416  LEU B CD1 1 
ATOM   5885 C  CD2 . LEU B 1 311 ? -16.456 66.686  -3.916  1.00 21.70 ? 416  LEU B CD2 1 
ATOM   5886 N  N   . LYS B 1 312 ? -12.808 64.826  -0.778  1.00 14.30 ? 417  LYS B N   1 
ATOM   5887 C  CA  A LYS B 1 312 ? -12.895 63.442  -0.269  0.50 15.38 ? 417  LYS B CA  1 
ATOM   5888 C  CA  B LYS B 1 312 ? -12.894 63.441  -0.276  0.50 14.98 ? 417  LYS B CA  1 
ATOM   5889 C  C   . LYS B 1 312 ? -14.353 63.143  -0.030  1.00 13.98 ? 417  LYS B C   1 
ATOM   5890 O  O   . LYS B 1 312 ? -14.985 63.769  0.864   1.00 15.10 ? 417  LYS B O   1 
ATOM   5891 C  CB  A LYS B 1 312 ? -12.082 63.257  1.015   0.50 17.48 ? 417  LYS B CB  1 
ATOM   5892 C  CB  B LYS B 1 312 ? -12.068 63.267  0.996   0.50 16.34 ? 417  LYS B CB  1 
ATOM   5893 C  CG  A LYS B 1 312 ? -10.575 63.339  0.774   0.50 20.71 ? 417  LYS B CG  1 
ATOM   5894 C  CG  B LYS B 1 312 ? -10.615 63.722  0.813   0.50 18.18 ? 417  LYS B CG  1 
ATOM   5895 C  CD  A LYS B 1 312 ? -10.261 62.981  -0.681  0.50 24.66 ? 417  LYS B CD  1 
ATOM   5896 C  CD  B LYS B 1 312 ? -9.831  62.776  -0.094  0.50 22.86 ? 417  LYS B CD  1 
ATOM   5897 C  CE  A LYS B 1 312 ? -8.973  62.168  -0.811  0.50 29.24 ? 417  LYS B CE  1 
ATOM   5898 C  CE  B LYS B 1 312 ? -8.311  63.064  -0.092  0.50 22.77 ? 417  LYS B CE  1 
ATOM   5899 N  NZ  A LYS B 1 312 ? -9.138  60.752  -0.416  0.50 32.42 ? 417  LYS B NZ  1 
ATOM   5900 N  NZ  B LYS B 1 312 ? -7.977  64.317  -0.787  0.50 19.91 ? 417  LYS B NZ  1 
ATOM   5901 N  N   . ALA B 1 313 ? -14.905 62.228  -0.842  1.00 11.20 ? 418  ALA B N   1 
ATOM   5902 C  CA  . ALA B 1 313 ? -16.360 61.958  -0.837  1.00 12.46 ? 418  ALA B CA  1 
ATOM   5903 C  C   . ALA B 1 313 ? -16.606 60.484  -0.571  1.00 11.28 ? 418  ALA B C   1 
ATOM   5904 O  O   . ALA B 1 313 ? -15.888 59.604  -1.150  1.00 11.66 ? 418  ALA B O   1 
ATOM   5905 C  CB  . ALA B 1 313 ? -16.978 62.373  -2.179  1.00 13.92 ? 418  ALA B CB  1 
ATOM   5906 N  N   . ALA B 1 314 ? -17.572 60.222  0.292   1.00 10.80 ? 419  ALA B N   1 
ATOM   5907 C  CA  . ALA B 1 314 ? -18.076 58.874  0.602   1.00 10.22 ? 419  ALA B CA  1 
ATOM   5908 C  C   . ALA B 1 314 ? -19.394 58.714  -0.047  1.00 11.23 ? 419  ALA B C   1 
ATOM   5909 O  O   . ALA B 1 314 ? -20.225 59.685  -0.101  1.00 12.14 ? 419  ALA B O   1 
ATOM   5910 C  CB  . ALA B 1 314 ? -18.206 58.675  2.134   1.00 11.74 ? 419  ALA B CB  1 
ATOM   5911 N  N   . TYR B 1 315 ? -19.714 57.528  -0.603  1.00 9.34  ? 420  TYR B N   1 
ATOM   5912 C  CA  . TYR B 1 315 ? -20.991 57.258  -1.255  1.00 9.52  ? 420  TYR B CA  1 
ATOM   5913 C  C   . TYR B 1 315 ? -21.702 56.126  -0.560  1.00 8.59  ? 420  TYR B C   1 
ATOM   5914 O  O   . TYR B 1 315 ? -21.174 54.986  -0.457  1.00 9.18  ? 420  TYR B O   1 
ATOM   5915 C  CB  . TYR B 1 315 ? -20.770 56.874  -2.774  1.00 8.95  ? 420  TYR B CB  1 
ATOM   5916 C  CG  . TYR B 1 315 ? -20.267 58.061  -3.545  1.00 9.59  ? 420  TYR B CG  1 
ATOM   5917 C  CD1 . TYR B 1 315 ? -21.177 58.728  -4.340  1.00 11.39 ? 420  TYR B CD1 1 
ATOM   5918 C  CD2 . TYR B 1 315 ? -18.945 58.551  -3.424  1.00 10.26 ? 420  TYR B CD2 1 
ATOM   5919 C  CE1 . TYR B 1 315 ? -20.848 59.905  -5.036  1.00 12.30 ? 420  TYR B CE1 1 
ATOM   5920 C  CE2 . TYR B 1 315 ? -18.589 59.722  -4.140  1.00 10.76 ? 420  TYR B CE2 1 
ATOM   5921 C  CZ  . TYR B 1 315 ? -19.587 60.408  -4.904  1.00 10.95 ? 420  TYR B CZ  1 
ATOM   5922 O  OH  . TYR B 1 315 ? -19.191 61.607  -5.550  1.00 13.47 ? 420  TYR B OH  1 
ATOM   5923 N  N   . SER B 1 316 ? -22.945 56.353  -0.129  1.00 8.88  ? 421  SER B N   1 
ATOM   5924 C  CA  . SER B 1 316 ? -23.759 55.300  0.455   1.00 8.88  ? 421  SER B CA  1 
ATOM   5925 C  C   . SER B 1 316 ? -23.915 54.129  -0.527  1.00 8.88  ? 421  SER B C   1 
ATOM   5926 O  O   . SER B 1 316 ? -24.130 54.327  -1.713  1.00 9.78  ? 421  SER B O   1 
ATOM   5927 C  CB  . SER B 1 316 ? -25.174 55.931  0.742   1.00 9.69  ? 421  SER B CB  1 
ATOM   5928 O  OG  . SER B 1 316 ? -26.044 54.965  1.329   1.00 9.90  ? 421  SER B OG  1 
ATOM   5929 N  N   . PHE B 1 317 ? -23.826 52.910  0.019   1.00 7.94  ? 422  PHE B N   1 
ATOM   5930 C  CA  . PHE B 1 317 ? -23.831 51.715  -0.831  1.00 8.44  ? 422  PHE B CA  1 
ATOM   5931 C  C   . PHE B 1 317 ? -25.063 50.920  -0.522  1.00 8.59  ? 422  PHE B C   1 
ATOM   5932 O  O   . PHE B 1 317 ? -26.171 51.293  -0.928  1.00 9.38  ? 422  PHE B O   1 
ATOM   5933 C  CB  . PHE B 1 317 ? -22.423 51.061  -0.669  1.00 9.11  ? 422  PHE B CB  1 
ATOM   5934 C  CG  . PHE B 1 317 ? -22.162 49.906  -1.673  1.00 8.54  ? 422  PHE B CG  1 
ATOM   5935 C  CD1 . PHE B 1 317 ? -22.417 50.034  -3.013  1.00 9.07  ? 422  PHE B CD1 1 
ATOM   5936 C  CD2 . PHE B 1 317 ? -21.569 48.709  -1.225  1.00 10.11 ? 422  PHE B CD2 1 
ATOM   5937 C  CE1 . PHE B 1 317 ? -22.169 49.010  -3.940  1.00 9.74  ? 422  PHE B CE1 1 
ATOM   5938 C  CE2 . PHE B 1 317 ? -21.215 47.652  -2.115  1.00 9.52  ? 422  PHE B CE2 1 
ATOM   5939 C  CZ  . PHE B 1 317 ? -21.489 47.805  -3.479  1.00 9.71  ? 422  PHE B CZ  1 
ATOM   5940 N  N   . TYR B 1 318 ? -24.967 49.864  0.310   1.00 8.33  ? 423  TYR B N   1 
ATOM   5941 C  CA  . TYR B 1 318 ? -26.167 49.162  0.846   1.00 8.47  ? 423  TYR B CA  1 
ATOM   5942 C  C   . TYR B 1 318 ? -26.210 49.243  2.357   1.00 8.74  ? 423  TYR B C   1 
ATOM   5943 O  O   . TYR B 1 318 ? -25.199 48.983  3.055   1.00 9.74  ? 423  TYR B O   1 
ATOM   5944 C  CB  . TYR B 1 318 ? -26.218 47.694  0.357   1.00 8.98  ? 423  TYR B CB  1 
ATOM   5945 C  CG  . TYR B 1 318 ? -26.272 47.536  -1.145  1.00 9.77  ? 423  TYR B CG  1 
ATOM   5946 C  CD1 . TYR B 1 318 ? -27.569 47.423  -1.776  1.00 10.44 ? 423  TYR B CD1 1 
ATOM   5947 C  CD2 . TYR B 1 318 ? -25.139 47.465  -1.917  1.00 9.48  ? 423  TYR B CD2 1 
ATOM   5948 C  CE1 . TYR B 1 318 ? -27.703 47.215  -3.173  1.00 9.80  ? 423  TYR B CE1 1 
ATOM   5949 C  CE2 . TYR B 1 318 ? -25.231 47.300  -3.331  1.00 9.61  ? 423  TYR B CE2 1 
ATOM   5950 C  CZ  . TYR B 1 318 ? -26.511 47.186  -3.895  1.00 8.64  ? 423  TYR B CZ  1 
ATOM   5951 O  OH  . TYR B 1 318 ? -26.651 46.995  -5.280  1.00 10.20 ? 423  TYR B OH  1 
ATOM   5952 N  N   . ASN B 1 319 ? -27.387 49.627  2.876   1.00 8.59  ? 424  ASN B N   1 
ATOM   5953 C  CA  . ASN B 1 319 ? -27.626 49.754  4.316   1.00 8.53  ? 424  ASN B CA  1 
ATOM   5954 C  C   . ASN B 1 319 ? -28.826 48.895  4.669   1.00 9.53  ? 424  ASN B C   1 
ATOM   5955 O  O   . ASN B 1 319 ? -29.903 49.067  4.105   1.00 12.12 ? 424  ASN B O   1 
ATOM   5956 C  CB  . ASN B 1 319 ? -27.854 51.213  4.608   1.00 9.51  ? 424  ASN B CB  1 
ATOM   5957 C  CG  . ASN B 1 319 ? -26.621 52.059  4.234   1.00 8.54  ? 424  ASN B CG  1 
ATOM   5958 O  OD1 . ASN B 1 319 ? -25.564 51.911  4.812   1.00 9.75  ? 424  ASN B OD1 1 
ATOM   5959 N  ND2 . ASN B 1 319 ? -26.798 52.937  3.213   1.00 9.58  ? 424  ASN B ND2 1 
ATOM   5960 N  N   . VAL B 1 320 ? -28.604 47.950  5.601   1.00 9.04  ? 425  VAL B N   1 
ATOM   5961 C  CA  . VAL B 1 320 ? -29.661 46.978  5.920   1.00 9.58  ? 425  VAL B CA  1 
ATOM   5962 C  C   . VAL B 1 320 ? -29.925 47.100  7.443   1.00 10.19 ? 425  VAL B C   1 
ATOM   5963 O  O   . VAL B 1 320 ? -29.044 47.060  8.278   1.00 10.46 ? 425  VAL B O   1 
ATOM   5964 C  CB  . VAL B 1 320 ? -29.193 45.564  5.634   1.00 9.71  ? 425  VAL B CB  1 
ATOM   5965 C  CG1 . VAL B 1 320 ? -30.237 44.568  6.138   1.00 12.25 ? 425  VAL B CG1 1 
ATOM   5966 C  CG2 . VAL B 1 320 ? -29.069 45.404  4.101   1.00 12.44 ? 425  VAL B CG2 1 
ATOM   5967 N  N   . HIS B 1 321 ? -31.226 47.312  7.765   1.00 11.63 ? 426  HIS B N   1 
ATOM   5968 C  CA  . HIS B 1 321 ? -31.634 47.426  9.174   1.00 11.84 ? 426  HIS B CA  1 
ATOM   5969 C  C   . HIS B 1 321 ? -32.708 46.356  9.409   1.00 12.33 ? 426  HIS B C   1 
ATOM   5970 O  O   . HIS B 1 321 ? -33.631 46.208  8.623   1.00 13.88 ? 426  HIS B O   1 
ATOM   5971 C  CB  . HIS B 1 321 ? -32.227 48.836  9.479   1.00 12.71 ? 426  HIS B CB  1 
ATOM   5972 C  CG  . HIS B 1 321 ? -33.471 49.157  8.734   1.00 13.14 ? 426  HIS B CG  1 
ATOM   5973 N  ND1 . HIS B 1 321 ? -34.740 48.966  9.287   1.00 14.60 ? 426  HIS B ND1 1 
ATOM   5974 C  CD2 . HIS B 1 321 ? -33.699 49.566  7.435   1.00 12.11 ? 426  HIS B CD2 1 
ATOM   5975 C  CE1 . HIS B 1 321 ? -35.669 49.227  8.390   1.00 15.24 ? 426  HIS B CE1 1 
ATOM   5976 N  NE2 . HIS B 1 321 ? -35.075 49.597  7.260   1.00 14.83 ? 426  HIS B NE2 1 
ATOM   5977 N  N   . THR B 1 322 ? -32.602 45.720  10.622  1.00 12.34 ? 427  THR B N   1 
ATOM   5978 C  CA  . THR B 1 322 ? -33.662 44.836  11.121  1.00 12.61 ? 427  THR B CA  1 
ATOM   5979 C  C   . THR B 1 322 ? -33.952 45.197  12.616  1.00 13.28 ? 427  THR B C   1 
ATOM   5980 O  O   . THR B 1 322 ? -35.058 44.767  13.089  1.00 15.73 ? 427  THR B O   1 
ATOM   5981 C  CB  . THR B 1 322 ? -33.385 43.306  11.009  1.00 13.64 ? 427  THR B CB  1 
ATOM   5982 O  OG1 . THR B 1 322 ? -32.353 42.918  11.946  1.00 13.81 ? 427  THR B OG1 1 
ATOM   5983 C  CG2 . THR B 1 322 ? -33.005 42.941  9.543   1.00 14.68 ? 427  THR B CG2 1 
ATOM   5984 N  N   . GLN B 1 323 ? -33.019 45.757  13.345  1.00 12.61 ? 428  GLN B N   1 
ATOM   5985 C  CA  . GLN B 1 323 ? -33.271 46.040  14.802  1.00 12.87 ? 428  GLN B CA  1 
ATOM   5986 C  C   . GLN B 1 323 ? -32.819 47.363  15.164  1.00 15.54 ? 428  GLN B C   1 
ATOM   5987 O  O   . GLN B 1 323 ? -33.297 47.912  16.172  1.00 21.49 ? 428  GLN B O   1 
ATOM   5988 C  CB  . GLN B 1 323 ? -32.634 44.944  15.678  1.00 15.35 ? 428  GLN B CB  1 
ATOM   5989 C  CG  . GLN B 1 323 ? -33.462 43.568  15.521  1.00 18.93 ? 428  GLN B CG  1 
ATOM   5990 C  CD  . GLN B 1 323 ? -35.011 43.428  15.983  1.00 19.80 ? 428  GLN B CD  1 
ATOM   5991 O  OE1 . GLN B 1 323 ? -35.474 44.248  16.809  1.00 26.90 ? 428  GLN B OE1 1 
ATOM   5992 N  NE2 . GLN B 1 323 ? -35.789 42.442  15.433  1.00 19.24 ? 428  GLN B NE2 1 
ATOM   5993 N  N   . THR B 1 324 ? -31.860 48.004  14.477  1.00 15.15 ? 429  THR B N   1 
ATOM   5994 C  CA  . THR B 1 324 ? -31.504 49.411  14.681  1.00 13.08 ? 429  THR B CA  1 
ATOM   5995 C  C   . THR B 1 324 ? -32.299 50.245  13.716  1.00 13.10 ? 429  THR B C   1 
ATOM   5996 O  O   . THR B 1 324 ? -32.389 49.932  12.513  1.00 13.77 ? 429  THR B O   1 
ATOM   5997 C  CB  . THR B 1 324 ? -30.020 49.562  14.339  1.00 13.14 ? 429  THR B CB  1 
ATOM   5998 O  OG1 . THR B 1 324 ? -29.222 48.634  15.127  1.00 13.64 ? 429  THR B OG1 1 
ATOM   5999 C  CG2 . THR B 1 324 ? -29.505 50.963  14.567  1.00 13.72 ? 429  THR B CG2 1 
ATOM   6000 N  N   . PRO B 1 325 ? -32.911 51.386  14.158  1.00 13.72 ? 430  PRO B N   1 
ATOM   6001 C  CA  . PRO B 1 325 ? -33.565 52.244  13.214  1.00 13.32 ? 430  PRO B CA  1 
ATOM   6002 C  C   . PRO B 1 325 ? -32.617 52.722  12.076  1.00 12.72 ? 430  PRO B C   1 
ATOM   6003 O  O   . PRO B 1 325 ? -31.436 53.067  12.336  1.00 13.50 ? 430  PRO B O   1 
ATOM   6004 C  CB  . PRO B 1 325 ? -34.049 53.437  14.056  1.00 14.06 ? 430  PRO B CB  1 
ATOM   6005 C  CG  . PRO B 1 325 ? -34.012 52.953  15.427  1.00 15.79 ? 430  PRO B CG  1 
ATOM   6006 C  CD  . PRO B 1 325 ? -32.967 51.885  15.545  1.00 15.04 ? 430  PRO B CD  1 
ATOM   6007 N  N   . LEU B 1 326 ? -33.172 52.747  10.851  1.00 13.45 ? 431  LEU B N   1 
ATOM   6008 C  CA  . LEU B 1 326 ? -32.367 53.207  9.693   1.00 13.20 ? 431  LEU B CA  1 
ATOM   6009 C  C   . LEU B 1 326 ? -31.787 54.599  9.937   1.00 14.00 ? 431  LEU B C   1 
ATOM   6010 O  O   . LEU B 1 326 ? -30.602 54.881  9.622   1.00 12.59 ? 431  LEU B O   1 
ATOM   6011 C  CB  . LEU B 1 326 ? -33.179 53.121  8.394   1.00 13.27 ? 431  LEU B CB  1 
ATOM   6012 C  CG  . LEU B 1 326 ? -32.436 53.651  7.157   1.00 13.82 ? 431  LEU B CG  1 
ATOM   6013 C  CD1 . LEU B 1 326 ? -31.152 52.808  6.844   1.00 13.68 ? 431  LEU B CD1 1 
ATOM   6014 C  CD2 . LEU B 1 326 ? -33.418 53.596  5.983   1.00 15.27 ? 431  LEU B CD2 1 
ATOM   6015 N  N   . LEU B 1 327 ? -32.589 55.474  10.540  1.00 13.54 ? 432  LEU B N   1 
ATOM   6016 C  CA  . LEU B 1 327 ? -32.151 56.801  10.886  1.00 14.29 ? 432  LEU B CA  1 
ATOM   6017 C  C   . LEU B 1 327 ? -30.899 56.829  11.711  1.00 13.71 ? 432  LEU B C   1 
ATOM   6018 O  O   . LEU B 1 327 ? -29.935 57.569  11.423  1.00 13.96 ? 432  LEU B O   1 
ATOM   6019 C  CB  . LEU B 1 327 ? -33.303 57.643  11.560  1.00 15.42 ? 432  LEU B CB  1 
ATOM   6020 C  CG  . LEU B 1 327 ? -32.896 59.110  11.860  1.00 17.26 ? 432  LEU B CG  1 
ATOM   6021 C  CD1 . LEU B 1 327 ? -32.840 59.886  10.570  1.00 16.97 ? 432  LEU B CD1 1 
ATOM   6022 C  CD2 . LEU B 1 327 ? -33.939 59.760  12.814  1.00 19.50 ? 432  LEU B CD2 1 
ATOM   6023 N  N   . ASP B 1 328 ? -30.837 55.976  12.717  1.00 14.30 ? 433  ASP B N   1 
ATOM   6024 C  CA  . ASP B 1 328 ? -29.638 55.885  13.580  1.00 13.71 ? 433  ASP B CA  1 
ATOM   6025 C  C   . ASP B 1 328 ? -28.448 55.256  12.849  1.00 12.61 ? 433  ASP B C   1 
ATOM   6026 O  O   . ASP B 1 328 ? -27.318 55.681  13.014  1.00 13.25 ? 433  ASP B O   1 
ATOM   6027 C  CB  . ASP B 1 328 ? -29.911 54.978  14.817  1.00 16.86 ? 433  ASP B CB  1 
ATOM   6028 C  CG  . ASP B 1 328 ? -30.917 55.562  15.785  1.00 22.27 ? 433  ASP B CG  1 
ATOM   6029 O  OD1 . ASP B 1 328 ? -31.101 54.853  16.782  1.00 23.81 ? 433  ASP B OD1 1 
ATOM   6030 O  OD2 . ASP B 1 328 ? -31.384 56.676  15.627  1.00 23.62 ? 433  ASP B OD2 1 
ATOM   6031 N  N   . LEU B 1 329 ? -28.728 54.243  12.019  1.00 14.11 ? 434  LEU B N   1 
ATOM   6032 C  CA  . LEU B 1 329 ? -27.632 53.630  11.329  1.00 14.10 ? 434  LEU B CA  1 
ATOM   6033 C  C   . LEU B 1 329 ? -26.975 54.599  10.352  1.00 12.40 ? 434  LEU B C   1 
ATOM   6034 O  O   . LEU B 1 329 ? -25.734 54.693  10.220  1.00 13.31 ? 434  LEU B O   1 
ATOM   6035 C  CB  . LEU B 1 329 ? -28.178 52.481  10.438  1.00 17.12 ? 434  LEU B CB  1 
ATOM   6036 C  CG  . LEU B 1 329 ? -27.275 51.421  9.949   1.00 20.58 ? 434  LEU B CG  1 
ATOM   6037 C  CD1 . LEU B 1 329 ? -26.761 50.558  11.138  1.00 19.60 ? 434  LEU B CD1 1 
ATOM   6038 C  CD2 . LEU B 1 329 ? -28.143 50.470  9.051   1.00 19.98 ? 434  LEU B CD2 1 
ATOM   6039 N  N   . MET B 1 330 ? -27.766 55.486  9.698   1.00 12.30 ? 435  MET B N   1 
ATOM   6040 C  CA  . MET B 1 330 ? -27.214 56.481  8.788   1.00 12.75 ? 435  MET B CA  1 
ATOM   6041 C  C   . MET B 1 330 ? -26.510 57.650  9.517   1.00 11.62 ? 435  MET B C   1 
ATOM   6042 O  O   . MET B 1 330 ? -25.477 58.135  9.043   1.00 10.81 ? 435  MET B O   1 
ATOM   6043 C  CB  . MET B 1 330 ? -28.315 57.018  7.844   1.00 12.06 ? 435  MET B CB  1 
ATOM   6044 C  CG  . MET B 1 330 ? -28.829 55.888  6.923   1.00 11.94 ? 435  MET B CG  1 
ATOM   6045 S  SD  . MET B 1 330 ? -27.544 54.875  6.067   1.00 13.71 ? 435  MET B SD  1 
ATOM   6046 C  CE  . MET B 1 330 ? -26.790 56.117  5.066   1.00 14.20 ? 435  MET B CE  1 
ATOM   6047 N  N   . SER B 1 331 ? -26.983 58.003  10.748  1.00 11.45 ? 436  SER B N   1 
ATOM   6048 C  CA  A SER B 1 331 ? -26.262 58.950  11.524  0.50 12.32 ? 436  SER B CA  1 
ATOM   6049 C  CA  B SER B 1 331 ? -26.267 58.899  11.636  0.50 12.47 ? 436  SER B CA  1 
ATOM   6050 C  C   . SER B 1 331 ? -24.901 58.380  11.887  1.00 11.89 ? 436  SER B C   1 
ATOM   6051 O  O   . SER B 1 331 ? -23.886 59.096  11.833  1.00 12.83 ? 436  SER B O   1 
ATOM   6052 C  CB  A SER B 1 331 ? -27.075 59.303  12.759  0.50 12.69 ? 436  SER B CB  1 
ATOM   6053 C  CB  B SER B 1 331 ? -27.030 59.006  12.970  0.50 13.51 ? 436  SER B CB  1 
ATOM   6054 O  OG  A SER B 1 331 ? -26.296 60.138  13.581  0.50 14.36 ? 436  SER B OG  1 
ATOM   6055 O  OG  B SER B 1 331 ? -28.120 59.852  12.737  0.50 15.55 ? 436  SER B OG  1 
ATOM   6056 N  N   . ASP B 1 332 ? -24.861 57.093  12.179  1.00 11.87 ? 437  ASP B N   1 
ATOM   6057 C  CA  A ASP B 1 332 ? -23.604 56.315  12.427  0.50 11.81 ? 437  ASP B CA  1 
ATOM   6058 C  CA  B ASP B 1 332 ? -23.536 56.512  12.456  0.50 11.95 ? 437  ASP B CA  1 
ATOM   6059 C  C   . ASP B 1 332 ? -22.654 56.402  11.229  1.00 10.87 ? 437  ASP B C   1 
ATOM   6060 O  O   . ASP B 1 332 ? -21.454 56.646  11.357  1.00 11.35 ? 437  ASP B O   1 
ATOM   6061 C  CB  A ASP B 1 332 ? -23.916 54.794  12.644  0.50 11.42 ? 437  ASP B CB  1 
ATOM   6062 C  CB  B ASP B 1 332 ? -23.658 55.202  13.207  0.50 13.07 ? 437  ASP B CB  1 
ATOM   6063 C  CG  A ASP B 1 332 ? -24.726 54.484  13.885  0.50 11.67 ? 437  ASP B CG  1 
ATOM   6064 C  CG  B ASP B 1 332 ? -23.998 55.428  14.680  0.50 13.32 ? 437  ASP B CG  1 
ATOM   6065 O  OD1 A ASP B 1 332 ? -24.766 55.259  14.911  0.50 13.66 ? 437  ASP B OD1 1 
ATOM   6066 O  OD1 B ASP B 1 332 ? -23.985 56.561  15.209  0.50 15.18 ? 437  ASP B OD1 1 
ATOM   6067 O  OD2 A ASP B 1 332 ? -25.393 53.441  13.859  0.50 11.30 ? 437  ASP B OD2 1 
ATOM   6068 O  OD2 B ASP B 1 332 ? -24.268 54.393  15.319  0.50 13.90 ? 437  ASP B OD2 1 
ATOM   6069 N  N   . ALA B 1 333 ? -23.244 56.174  10.030  1.00 10.52 ? 438  ALA B N   1 
ATOM   6070 C  CA  . ALA B 1 333 ? -22.418 56.273  8.798   1.00 11.25 ? 438  ALA B CA  1 
ATOM   6071 C  C   . ALA B 1 333 ? -21.787 57.626  8.626   1.00 11.52 ? 438  ALA B C   1 
ATOM   6072 O  O   . ALA B 1 333 ? -20.643 57.726  8.260   1.00 10.99 ? 438  ALA B O   1 
ATOM   6073 C  CB  . ALA B 1 333 ? -23.251 55.903  7.545   1.00 11.06 ? 438  ALA B CB  1 
ATOM   6074 N  N   . LEU B 1 334 ? -22.581 58.712  8.895   1.00 11.16 ? 439  LEU B N   1 
ATOM   6075 C  CA  . LEU B 1 334 ? -21.997 60.047  8.763   1.00 10.29 ? 439  LEU B CA  1 
ATOM   6076 C  C   . LEU B 1 334 ? -20.849 60.304  9.741   1.00 11.14 ? 439  LEU B C   1 
ATOM   6077 O  O   . LEU B 1 334 ? -19.820 60.835  9.396   1.00 11.68 ? 439  LEU B O   1 
ATOM   6078 C  CB  . LEU B 1 334 ? -23.130 61.112  9.053   1.00 10.99 ? 439  LEU B CB  1 
ATOM   6079 C  CG  . LEU B 1 334 ? -24.256 61.162  8.063   1.00 10.68 ? 439  LEU B CG  1 
ATOM   6080 C  CD1 . LEU B 1 334 ? -25.366 62.178  8.560   1.00 12.40 ? 439  LEU B CD1 1 
ATOM   6081 C  CD2 . LEU B 1 334 ? -23.782 61.474  6.607   1.00 11.87 ? 439  LEU B CD2 1 
ATOM   6082 N  N   . VAL B 1 335 ? -21.056 59.812  10.985  1.00 11.17 ? 440  VAL B N   1 
ATOM   6083 C  CA  . VAL B 1 335 ? -19.993 60.001  12.028  1.00 11.52 ? 440  VAL B CA  1 
ATOM   6084 C  C   . VAL B 1 335 ? -18.728 59.245  11.623  1.00 11.94 ? 440  VAL B C   1 
ATOM   6085 O  O   . VAL B 1 335 ? -17.603 59.749  11.730  1.00 12.34 ? 440  VAL B O   1 
ATOM   6086 C  CB  . VAL B 1 335 ? -20.497 59.481  13.388  1.00 11.38 ? 440  VAL B CB  1 
ATOM   6087 C  CG1 . VAL B 1 335 ? -19.366 59.405  14.427  1.00 14.22 ? 440  VAL B CG1 1 
ATOM   6088 C  CG2 . VAL B 1 335 ? -21.570 60.435  13.976  1.00 14.31 ? 440  VAL B CG2 1 
ATOM   6089 N  N   . LEU B 1 336 ? -18.916 57.993  11.155  1.00 11.62 ? 441  LEU B N   1 
ATOM   6090 C  CA  . LEU B 1 336 ? -17.721 57.192  10.746  1.00 11.86 ? 441  LEU B CA  1 
ATOM   6091 C  C   . LEU B 1 336 ? -16.985 57.811  9.560   1.00 11.45 ? 441  LEU B C   1 
ATOM   6092 O  O   . LEU B 1 336 ? -15.751 57.855  9.483   1.00 13.24 ? 441  LEU B O   1 
ATOM   6093 C  CB  . LEU B 1 336 ? -18.162 55.751  10.391  1.00 13.45 ? 441  LEU B CB  1 
ATOM   6094 C  CG  . LEU B 1 336 ? -18.548 54.950  11.609  1.00 11.97 ? 441  LEU B CG  1 
ATOM   6095 C  CD1 . LEU B 1 336 ? -19.313 53.692  11.065  1.00 15.02 ? 441  LEU B CD1 1 
ATOM   6096 C  CD2 . LEU B 1 336 ? -17.316 54.567  12.465  1.00 14.73 ? 441  LEU B CD2 1 
ATOM   6097 N  N   . ALA B 1 337 ? -17.770 58.318  8.581   1.00 10.88 ? 442  ALA B N   1 
ATOM   6098 C  CA  . ALA B 1 337 ? -17.148 58.956  7.410   1.00 12.89 ? 442  ALA B CA  1 
ATOM   6099 C  C   . ALA B 1 337 ? -16.364 60.208  7.840   1.00 13.84 ? 442  ALA B C   1 
ATOM   6100 O  O   . ALA B 1 337 ? -15.254 60.503  7.377   1.00 13.85 ? 442  ALA B O   1 
ATOM   6101 C  CB  . ALA B 1 337 ? -18.247 59.283  6.347   1.00 13.84 ? 442  ALA B CB  1 
ATOM   6102 N  N   . LYS B 1 338 ? -16.984 61.001  8.758   1.00 12.84 ? 443  LYS B N   1 
ATOM   6103 C  CA  . LYS B 1 338 ? -16.287 62.238  9.246   1.00 14.21 ? 443  LYS B CA  1 
ATOM   6104 C  C   . LYS B 1 338 ? -15.022 61.765  9.976   1.00 13.63 ? 443  LYS B C   1 
ATOM   6105 O  O   . LYS B 1 338 ? -13.924 62.340  9.712   1.00 15.27 ? 443  LYS B O   1 
ATOM   6106 C  CB  . LYS B 1 338 ? -17.238 63.045  10.158  1.00 15.06 ? 443  LYS B CB  1 
ATOM   6107 C  CG  . LYS B 1 338 ? -16.533 64.257  10.849  1.00 19.82 ? 443  LYS B CG  1 
ATOM   6108 C  CD  . LYS B 1 338 ? -16.315 65.431  9.953   1.00 24.79 ? 443  LYS B CD  1 
ATOM   6109 C  CE  . LYS B 1 338 ? -15.573 66.552  10.722  1.00 25.73 ? 443  LYS B CE  1 
ATOM   6110 N  NZ  . LYS B 1 338 ? -14.644 67.201  9.777   1.00 35.66 ? 443  LYS B NZ  1 
ATOM   6111 N  N   . MET B 1 339 ? -15.110 60.747  10.840  1.00 13.57 ? 444  MET B N   1 
ATOM   6112 C  CA  . MET B 1 339 ? -13.875 60.236  11.523  1.00 16.91 ? 444  MET B CA  1 
ATOM   6113 C  C   . MET B 1 339 ? -12.783 59.835  10.510  1.00 17.30 ? 444  MET B C   1 
ATOM   6114 O  O   . MET B 1 339 ? -11.577 60.052  10.798  1.00 19.28 ? 444  MET B O   1 
ATOM   6115 C  CB  . MET B 1 339 ? -14.212 59.026  12.338  1.00 19.17 ? 444  MET B CB  1 
ATOM   6116 C  CG  . MET B 1 339 ? -15.030 59.345  13.627  1.00 20.87 ? 444  MET B CG  1 
ATOM   6117 S  SD  . MET B 1 339 ? -15.819 57.792  14.295  1.00 24.92 ? 444  MET B SD  1 
ATOM   6118 C  CE  . MET B 1 339 ? -14.243 56.724  14.256  1.00 22.60 ? 444  MET B CE  1 
ATOM   6119 N  N   . LYS B 1 340 ? -13.174 59.264  9.359   1.00 13.27 ? 445  LYS B N   1 
ATOM   6120 C  CA  . LYS B 1 340 ? -12.217 58.799  8.399   1.00 16.27 ? 445  LYS B CA  1 
ATOM   6121 C  C   . LYS B 1 340 ? -11.701 59.929  7.514   1.00 15.48 ? 445  LYS B C   1 
ATOM   6122 O  O   . LYS B 1 340 ? -10.911 59.616  6.558   1.00 19.91 ? 445  LYS B O   1 
ATOM   6123 C  CB  . LYS B 1 340 ? -12.893 57.658  7.579   1.00 14.36 ? 445  LYS B CB  1 
ATOM   6124 C  CG  . LYS B 1 340 ? -13.000 56.431  8.405   1.00 15.32 ? 445  LYS B CG  1 
ATOM   6125 C  CD  . LYS B 1 340 ? -13.783 55.388  7.642   1.00 16.82 ? 445  LYS B CD  1 
ATOM   6126 C  CE  . LYS B 1 340 ? -13.991 54.083  8.444   1.00 19.49 ? 445  LYS B CE  1 
ATOM   6127 N  NZ  . LYS B 1 340 ? -12.787 53.242  8.290   1.00 23.74 ? 445  LYS B NZ  1 
ATOM   6128 N  N   . GLY B 1 341 ? -12.094 61.199  7.749   1.00 15.48 ? 446  GLY B N   1 
ATOM   6129 C  CA  . GLY B 1 341 ? -11.524 62.313  6.978   1.00 15.84 ? 446  GLY B CA  1 
ATOM   6130 C  C   . GLY B 1 341 ? -12.289 62.674  5.731   1.00 15.94 ? 446  GLY B C   1 
ATOM   6131 O  O   . GLY B 1 341 ? -11.834 63.515  4.952   1.00 17.87 ? 446  GLY B O   1 
ATOM   6132 N  N   . PHE B 1 342 ? -13.495 62.109  5.522   1.00 13.44 ? 447  PHE B N   1 
ATOM   6133 C  CA  . PHE B 1 342 ? -14.295 62.558  4.355   1.00 13.52 ? 447  PHE B CA  1 
ATOM   6134 C  C   . PHE B 1 342 ? -14.862 63.961  4.505   1.00 12.36 ? 447  PHE B C   1 
ATOM   6135 O  O   . PHE B 1 342 ? -15.163 64.392  5.647   1.00 14.47 ? 447  PHE B O   1 
ATOM   6136 C  CB  . PHE B 1 342 ? -15.481 61.624  4.089   1.00 12.24 ? 447  PHE B CB  1 
ATOM   6137 C  CG  . PHE B 1 342 ? -15.079 60.257  3.601   1.00 12.68 ? 447  PHE B CG  1 
ATOM   6138 C  CD1 . PHE B 1 342 ? -14.892 60.037  2.191   1.00 13.65 ? 447  PHE B CD1 1 
ATOM   6139 C  CD2 . PHE B 1 342 ? -14.848 59.164  4.506   1.00 12.30 ? 447  PHE B CD2 1 
ATOM   6140 C  CE1 . PHE B 1 342 ? -14.522 58.780  1.755   1.00 13.79 ? 447  PHE B CE1 1 
ATOM   6141 C  CE2 . PHE B 1 342 ? -14.470 57.939  4.018   1.00 13.33 ? 447  PHE B CE2 1 
ATOM   6142 C  CZ  . PHE B 1 342 ? -14.333 57.748  2.621   1.00 13.49 ? 447  PHE B CZ  1 
ATOM   6143 N  N   . ASP B 1 343 ? -14.993 64.731  3.430   1.00 12.92 ? 448  ASP B N   1 
ATOM   6144 C  CA  . ASP B 1 343 ? -15.519 66.088  3.428   1.00 11.86 ? 448  ASP B CA  1 
ATOM   6145 C  C   . ASP B 1 343 ? -17.034 66.087  3.268   1.00 12.14 ? 448  ASP B C   1 
ATOM   6146 O  O   . ASP B 1 343 ? -17.715 67.049  3.715   1.00 12.96 ? 448  ASP B O   1 
ATOM   6147 C  CB  . ASP B 1 343 ? -14.880 66.909  2.284   1.00 14.77 ? 448  ASP B CB  1 
ATOM   6148 C  CG  . ASP B 1 343 ? -13.401 66.971  2.359   1.00 19.44 ? 448  ASP B CG  1 
ATOM   6149 O  OD1 . ASP B 1 343 ? -12.698 66.824  1.296   1.00 18.06 ? 448  ASP B OD1 1 
ATOM   6150 O  OD2 . ASP B 1 343 ? -12.888 67.231  3.459   1.00 17.37 ? 448  ASP B OD2 1 
ATOM   6151 N  N   . VAL B 1 344 ? -17.600 65.118  2.537   1.00 11.84 ? 449  VAL B N   1 
ATOM   6152 C  CA  . VAL B 1 344 ? -19.032 65.073  2.177   1.00 11.68 ? 449  VAL B CA  1 
ATOM   6153 C  C   . VAL B 1 344 ? -19.468 63.608  2.080   1.00 9.67  ? 449  VAL B C   1 
ATOM   6154 O  O   . VAL B 1 344 ? -18.617 62.761  1.675   1.00 11.34 ? 449  VAL B O   1 
ATOM   6155 C  CB  . VAL B 1 344 ? -19.292 65.870  0.856   1.00 11.25 ? 449  VAL B CB  1 
ATOM   6156 C  CG1 . VAL B 1 344 ? -18.474 65.259  -0.360  1.00 12.97 ? 449  VAL B CG1 1 
ATOM   6157 C  CG2 . VAL B 1 344 ? -20.751 66.041  0.529   1.00 12.54 ? 449  VAL B CG2 1 
ATOM   6158 N  N   . PHE B 1 345 ? -20.736 63.363  2.371   1.00 10.59 ? 450  PHE B N   1 
ATOM   6159 C  CA  . PHE B 1 345 ? -21.303 62.017  2.249   1.00 9.66  ? 450  PHE B CA  1 
ATOM   6160 C  C   . PHE B 1 345 ? -22.392 62.115  1.240   1.00 11.23 ? 450  PHE B C   1 
ATOM   6161 O  O   . PHE B 1 345 ? -23.293 63.016  1.345   1.00 13.59 ? 450  PHE B O   1 
ATOM   6162 C  CB  . PHE B 1 345 ? -21.877 61.587  3.633   1.00 10.44 ? 450  PHE B CB  1 
ATOM   6163 C  CG  . PHE B 1 345 ? -22.290 60.128  3.675   1.00 9.68  ? 450  PHE B CG  1 
ATOM   6164 C  CD1 . PHE B 1 345 ? -21.394 59.148  4.189   1.00 11.31 ? 450  PHE B CD1 1 
ATOM   6165 C  CD2 . PHE B 1 345 ? -23.552 59.735  3.272   1.00 10.70 ? 450  PHE B CD2 1 
ATOM   6166 C  CE1 . PHE B 1 345 ? -21.812 57.805  4.270   1.00 11.59 ? 450  PHE B CE1 1 
ATOM   6167 C  CE2 . PHE B 1 345 ? -23.980 58.436  3.405   1.00 11.45 ? 450  PHE B CE2 1 
ATOM   6168 C  CZ  . PHE B 1 345 ? -23.101 57.493  3.881   1.00 11.03 ? 450  PHE B CZ  1 
ATOM   6169 N  N   . ASN B 1 346 ? -22.468 61.270  0.213   1.00 9.79  ? 451  ASN B N   1 
ATOM   6170 C  CA  . ASN B 1 346 ? -23.437 61.348  -0.898  1.00 10.23 ? 451  ASN B CA  1 
ATOM   6171 C  C   . ASN B 1 346 ? -24.362 60.192  -0.876  1.00 9.76  ? 451  ASN B C   1 
ATOM   6172 O  O   . ASN B 1 346 ? -23.894 59.032  -0.605  1.00 10.60 ? 451  ASN B O   1 
ATOM   6173 C  CB  . ASN B 1 346 ? -22.682 61.379  -2.241  1.00 12.16 ? 451  ASN B CB  1 
ATOM   6174 C  CG  . ASN B 1 346 ? -21.744 62.576  -2.375  1.00 14.77 ? 451  ASN B CG  1 
ATOM   6175 O  OD1 . ASN B 1 346 ? -22.180 63.646  -2.456  1.00 19.45 ? 451  ASN B OD1 1 
ATOM   6176 N  ND2 . ASN B 1 346 ? -20.481 62.362  -2.169  1.00 21.27 ? 451  ASN B ND2 1 
ATOM   6177 N  N   . ALA B 1 347 ? -25.622 60.355  -1.196  1.00 9.49  ? 452  ALA B N   1 
ATOM   6178 C  CA  . ALA B 1 347 ? -26.587 59.243  -1.256  1.00 9.17  ? 452  ALA B CA  1 
ATOM   6179 C  C   . ALA B 1 347 ? -27.621 59.532  -2.273  1.00 10.00 ? 452  ALA B C   1 
ATOM   6180 O  O   . ALA B 1 347 ? -27.997 60.742  -2.503  1.00 10.52 ? 452  ALA B O   1 
ATOM   6181 C  CB  . ALA B 1 347 ? -27.248 58.988  0.119   1.00 10.59 ? 452  ALA B CB  1 
ATOM   6182 N  N   . LEU B 1 348 ? -28.181 58.540  -2.926  1.00 9.95  ? 453  LEU B N   1 
ATOM   6183 C  CA  . LEU B 1 348 ? -29.324 58.700  -3.794  1.00 10.59 ? 453  LEU B CA  1 
ATOM   6184 C  C   . LEU B 1 348 ? -30.628 58.595  -3.019  1.00 11.42 ? 453  LEU B C   1 
ATOM   6185 O  O   . LEU B 1 348 ? -30.616 58.176  -1.819  1.00 11.38 ? 453  LEU B O   1 
ATOM   6186 C  CB  . LEU B 1 348 ? -29.280 57.549  -4.857  1.00 10.45 ? 453  LEU B CB  1 
ATOM   6187 C  CG  . LEU B 1 348 ? -28.036 57.643  -5.794  1.00 10.28 ? 453  LEU B CG  1 
ATOM   6188 C  CD1 . LEU B 1 348 ? -27.765 56.290  -6.409  1.00 11.06 ? 453  LEU B CD1 1 
ATOM   6189 C  CD2 . LEU B 1 348 ? -28.263 58.689  -6.889  1.00 11.20 ? 453  LEU B CD2 1 
ATOM   6190 N  N   . ASP B 1 349 ? -31.758 58.905  -3.650  1.00 9.88  ? 454  ASP B N   1 
ATOM   6191 C  CA  . ASP B 1 349 ? -33.065 58.785  -2.970  1.00 10.12 ? 454  ASP B CA  1 
ATOM   6192 C  C   . ASP B 1 349 ? -33.804 57.477  -3.168  1.00 10.66 ? 454  ASP B C   1 
ATOM   6193 O  O   . ASP B 1 349 ? -35.030 57.390  -2.985  1.00 12.17 ? 454  ASP B O   1 
ATOM   6194 C  CB  . ASP B 1 349 ? -33.933 59.962  -3.411  1.00 10.96 ? 454  ASP B CB  1 
ATOM   6195 C  CG  . ASP B 1 349 ? -34.254 59.915  -4.897  1.00 12.36 ? 454  ASP B CG  1 
ATOM   6196 O  OD1 . ASP B 1 349 ? -33.731 59.086  -5.691  1.00 11.80 ? 454  ASP B OD1 1 
ATOM   6197 O  OD2 . ASP B 1 349 ? -35.056 60.780  -5.379  1.00 13.40 ? 454  ASP B OD2 1 
ATOM   6198 N  N   . LEU B 1 350 ? -33.029 56.408  -3.505  1.00 9.38  ? 455  LEU B N   1 
ATOM   6199 C  CA  . LEU B 1 350 ? -33.564 55.056  -3.728  1.00 10.26 ? 455  LEU B CA  1 
ATOM   6200 C  C   . LEU B 1 350 ? -33.704 54.307  -2.424  1.00 9.70  ? 455  LEU B C   1 
ATOM   6201 O  O   . LEU B 1 350 ? -33.455 54.829  -1.307  1.00 10.47 ? 455  LEU B O   1 
ATOM   6202 C  CB  . LEU B 1 350 ? -32.684 54.264  -4.793  1.00 10.80 ? 455  LEU B CB  1 
ATOM   6203 C  CG  . LEU B 1 350 ? -31.176 54.381  -4.651  1.00 10.29 ? 455  LEU B CG  1 
ATOM   6204 C  CD1 . LEU B 1 350 ? -30.689 53.935  -3.271  1.00 11.29 ? 455  LEU B CD1 1 
ATOM   6205 C  CD2 . LEU B 1 350 ? -30.554 53.416  -5.698  1.00 10.94 ? 455  LEU B CD2 1 
ATOM   6206 N  N   . MET B 1 351 ? -34.192 53.087  -2.523  1.00 10.29 ? 456  MET B N   1 
ATOM   6207 C  CA  . MET B 1 351 ? -34.512 52.218  -1.336  1.00 10.68 ? 456  MET B CA  1 
ATOM   6208 C  C   . MET B 1 351 ? -35.360 53.009  -0.311  1.00 10.81 ? 456  MET B C   1 
ATOM   6209 O  O   . MET B 1 351 ? -36.277 53.740  -0.747  1.00 10.40 ? 456  MET B O   1 
ATOM   6210 C  CB  . MET B 1 351 ? -33.259 51.531  -0.753  1.00 10.69 ? 456  MET B CB  1 
ATOM   6211 C  CG  . MET B 1 351 ? -32.756 50.467  -1.765  1.00 10.20 ? 456  MET B CG  1 
ATOM   6212 S  SD  . MET B 1 351 ? -31.275 49.518  -1.239  1.00 10.73 ? 456  MET B SD  1 
ATOM   6213 C  CE  . MET B 1 351 ? -29.907 50.564  -1.684  1.00 12.47 ? 456  MET B CE  1 
ATOM   6214 N  N   . GLU B 1 352 ? -34.985 52.960  0.955   1.00 10.95 ? 457  GLU B N   1 
ATOM   6215 C  CA  . GLU B 1 352 ? -35.757 53.781  1.976   1.00 10.96 ? 457  GLU B CA  1 
ATOM   6216 C  C   . GLU B 1 352 ? -35.048 55.073  2.238   1.00 11.06 ? 457  GLU B C   1 
ATOM   6217 O  O   . GLU B 1 352 ? -35.260 55.679  3.322   1.00 11.91 ? 457  GLU B O   1 
ATOM   6218 C  CB  . GLU B 1 352 ? -35.977 52.945  3.252   1.00 11.19 ? 457  GLU B CB  1 
ATOM   6219 C  CG  . GLU B 1 352 ? -36.700 51.644  3.015   1.00 12.43 ? 457  GLU B CG  1 
ATOM   6220 C  CD  . GLU B 1 352 ? -36.813 50.940  4.321   1.00 15.06 ? 457  GLU B CD  1 
ATOM   6221 O  OE1 . GLU B 1 352 ? -35.908 50.159  4.740   1.00 14.52 ? 457  GLU B OE1 1 
ATOM   6222 O  OE2 . GLU B 1 352 ? -37.810 51.228  5.056   1.00 17.51 ? 457  GLU B OE2 1 
ATOM   6223 N  N   . ASN B 1 353 ? -34.163 55.591  1.386   1.00 10.62 ? 458  ASN B N   1 
ATOM   6224 C  CA  . ASN B 1 353 ? -33.321 56.701  1.740   1.00 10.31 ? 458  ASN B CA  1 
ATOM   6225 C  C   . ASN B 1 353 ? -34.138 57.999  2.009   1.00 10.07 ? 458  ASN B C   1 
ATOM   6226 O  O   . ASN B 1 353 ? -33.653 58.823  2.804   1.00 11.31 ? 458  ASN B O   1 
ATOM   6227 C  CB  . ASN B 1 353 ? -32.208 56.927  0.709   1.00 10.02 ? 458  ASN B CB  1 
ATOM   6228 C  CG  . ASN B 1 353 ? -31.176 55.839  0.727   1.00 9.89  ? 458  ASN B CG  1 
ATOM   6229 O  OD1 . ASN B 1 353 ? -31.261 54.852  1.470   1.00 10.99 ? 458  ASN B OD1 1 
ATOM   6230 N  ND2 . ASN B 1 353 ? -30.178 56.022  -0.105  1.00 10.23 ? 458  ASN B ND2 1 
ATOM   6231 N  N   . LYS B 1 354 ? -35.281 58.184  1.322   1.00 11.57 ? 459  LYS B N   1 
ATOM   6232 C  CA  . LYS B 1 354 ? -36.070 59.412  1.637   1.00 12.01 ? 459  LYS B CA  1 
ATOM   6233 C  C   . LYS B 1 354 ? -36.504 59.454  3.084   1.00 14.35 ? 459  LYS B C   1 
ATOM   6234 O  O   . LYS B 1 354 ? -36.766 60.603  3.579   1.00 15.08 ? 459  LYS B O   1 
ATOM   6235 C  CB  . LYS B 1 354 ? -37.244 59.503  0.669   1.00 12.56 ? 459  LYS B CB  1 
ATOM   6236 C  CG  . LYS B 1 354 ? -36.810 59.817  -0.768  1.00 13.81 ? 459  LYS B CG  1 
ATOM   6237 C  CD  . LYS B 1 354 ? -38.049 59.795  -1.658  1.00 15.64 ? 459  LYS B CD  1 
ATOM   6238 C  CE  . LYS B 1 354 ? -37.690 60.009  -3.108  1.00 16.67 ? 459  LYS B CE  1 
ATOM   6239 N  NZ  . LYS B 1 354 ? -38.999 60.137  -3.852  1.00 19.72 ? 459  LYS B NZ  1 
ATOM   6240 N  N   . THR B 1 355 ? -36.545 58.348  3.787   1.00 13.09 ? 460  THR B N   1 
ATOM   6241 C  CA  . THR B 1 355 ? -36.875 58.375  5.199   1.00 12.45 ? 460  THR B CA  1 
ATOM   6242 C  C   . THR B 1 355 ? -35.864 59.079  6.006   1.00 14.25 ? 460  THR B C   1 
ATOM   6243 O  O   . THR B 1 355 ? -36.240 59.539  7.173   1.00 18.59 ? 460  THR B O   1 
ATOM   6244 C  CB  . THR B 1 355 ? -37.245 57.019  5.769   1.00 13.85 ? 460  THR B CB  1 
ATOM   6245 O  OG1 . THR B 1 355 ? -36.060 56.227  5.901   1.00 14.40 ? 460  THR B OG1 1 
ATOM   6246 C  CG2 . THR B 1 355 ? -38.264 56.273  4.940   1.00 14.42 ? 460  THR B CG2 1 
ATOM   6247 N  N   . PHE B 1 356 ? -34.599 59.223  5.640   1.00 11.59 ? 461  PHE B N   1 
ATOM   6248 C  CA  . PHE B 1 356 ? -33.591 59.910  6.464   1.00 12.51 ? 461  PHE B CA  1 
ATOM   6249 C  C   . PHE B 1 356 ? -32.944 61.127  5.873   1.00 10.44 ? 461  PHE B C   1 
ATOM   6250 O  O   . PHE B 1 356 ? -32.223 61.862  6.612   1.00 11.53 ? 461  PHE B O   1 
ATOM   6251 C  CB  . PHE B 1 356 ? -32.456 58.911  6.932   1.00 12.39 ? 461  PHE B CB  1 
ATOM   6252 C  CG  . PHE B 1 356 ? -31.656 58.346  5.798   1.00 11.68 ? 461  PHE B CG  1 
ATOM   6253 C  CD1 . PHE B 1 356 ? -30.654 59.086  5.235   1.00 11.38 ? 461  PHE B CD1 1 
ATOM   6254 C  CD2 . PHE B 1 356 ? -31.925 57.022  5.361   1.00 11.73 ? 461  PHE B CD2 1 
ATOM   6255 C  CE1 . PHE B 1 356 ? -29.887 58.569  4.146   1.00 11.99 ? 461  PHE B CE1 1 
ATOM   6256 C  CE2 . PHE B 1 356 ? -31.147 56.487  4.323   1.00 11.98 ? 461  PHE B CE2 1 
ATOM   6257 C  CZ  . PHE B 1 356 ? -30.135 57.229  3.740   1.00 12.40 ? 461  PHE B CZ  1 
ATOM   6258 N  N   . LEU B 1 357 ? -33.077 61.372  4.531   1.00 10.74 ? 462  LEU B N   1 
ATOM   6259 C  CA  . LEU B 1 357 ? -32.213 62.380  3.926   1.00 10.48 ? 462  LEU B CA  1 
ATOM   6260 C  C   . LEU B 1 357 ? -32.406 63.790  4.587   1.00 10.85 ? 462  LEU B C   1 
ATOM   6261 O  O   . LEU B 1 357 ? -31.437 64.438  4.995   1.00 11.68 ? 462  LEU B O   1 
ATOM   6262 C  CB  . LEU B 1 357 ? -32.523 62.451  2.382   1.00 11.99 ? 462  LEU B CB  1 
ATOM   6263 C  CG  . LEU B 1 357 ? -31.909 61.238  1.610   1.00 11.63 ? 462  LEU B CG  1 
ATOM   6264 C  CD1 . LEU B 1 357 ? -32.495 61.167  0.200   1.00 12.05 ? 462  LEU B CD1 1 
ATOM   6265 C  CD2 . LEU B 1 357 ? -30.375 61.305  1.522   1.00 12.45 ? 462  LEU B CD2 1 
ATOM   6266 N  N   . GLU B 1 358 ? -33.685 64.273  4.541   1.00 12.05 ? 463  GLU B N   1 
ATOM   6267 C  CA  . GLU B 1 358 ? -33.875 65.596  5.167   1.00 13.53 ? 463  GLU B CA  1 
ATOM   6268 C  C   . GLU B 1 358 ? -33.668 65.574  6.675   1.00 10.97 ? 463  GLU B C   1 
ATOM   6269 O  O   . GLU B 1 358 ? -33.125 66.528  7.214   1.00 12.17 ? 463  GLU B O   1 
ATOM   6270 C  CB  . GLU B 1 358 ? -35.329 66.057  4.905   1.00 14.23 ? 463  GLU B CB  1 
ATOM   6271 C  CG  . GLU B 1 358 ? -35.474 66.370  3.409   1.00 18.20 ? 463  GLU B CG  1 
ATOM   6272 C  CD  . GLU B 1 358 ? -36.687 67.213  3.115   1.00 29.12 ? 463  GLU B CD  1 
ATOM   6273 O  OE1 . GLU B 1 358 ? -37.738 66.871  3.747   1.00 24.08 ? 463  GLU B OE1 1 
ATOM   6274 O  OE2 . GLU B 1 358 ? -36.479 68.217  2.303   1.00 37.06 ? 463  GLU B OE2 1 
ATOM   6275 N  N   . LYS B 1 359 ? -34.035 64.523  7.390   1.00 11.21 ? 464  LYS B N   1 
ATOM   6276 C  CA  . LYS B 1 359 ? -33.854 64.479  8.831   1.00 11.45 ? 464  LYS B CA  1 
ATOM   6277 C  C   . LYS B 1 359 ? -32.390 64.628  9.229   1.00 13.15 ? 464  LYS B C   1 
ATOM   6278 O  O   . LYS B 1 359 ? -32.083 65.172  10.291  1.00 14.84 ? 464  LYS B O   1 
ATOM   6279 C  CB  . LYS B 1 359 ? -34.457 63.232  9.434   1.00 13.37 ? 464  LYS B CB  1 
ATOM   6280 C  CG  . LYS B 1 359 ? -36.003 63.238  9.496   1.00 13.84 ? 464  LYS B CG  1 
ATOM   6281 C  CD  . LYS B 1 359 ? -36.480 61.950  10.157  1.00 16.28 ? 464  LYS B CD  1 
ATOM   6282 C  CE  . LYS B 1 359 ? -37.914 62.170  10.778  1.00 19.08 ? 464  LYS B CE  1 
ATOM   6283 N  NZ  . LYS B 1 359 ? -38.971 62.461  9.827   1.00 20.03 ? 464  LYS B NZ  1 
ATOM   6284 N  N   . LEU B 1 360 ? -31.464 64.090  8.397   1.00 10.81 ? 465  LEU B N   1 
ATOM   6285 C  CA  . LEU B 1 360 ? -30.043 64.143  8.683   1.00 10.61 ? 465  LEU B CA  1 
ATOM   6286 C  C   . LEU B 1 360 ? -29.340 65.261  8.002   1.00 11.35 ? 465  LEU B C   1 
ATOM   6287 O  O   . LEU B 1 360 ? -28.085 65.243  7.910   1.00 12.54 ? 465  LEU B O   1 
ATOM   6288 C  CB  . LEU B 1 360 ? -29.405 62.736  8.324   1.00 10.68 ? 465  LEU B CB  1 
ATOM   6289 C  CG  . LEU B 1 360 ? -29.911 61.599  9.216   1.00 10.83 ? 465  LEU B CG  1 
ATOM   6290 C  CD1 . LEU B 1 360 ? -29.195 60.266  8.845   1.00 12.53 ? 465  LEU B CD1 1 
ATOM   6291 C  CD2 . LEU B 1 360 ? -29.663 61.888  10.717  1.00 13.86 ? 465  LEU B CD2 1 
ATOM   6292 N  N   . LYS B 1 361 ? -30.110 66.299  7.532   1.00 11.05 ? 466  LYS B N   1 
ATOM   6293 C  CA  . LYS B 1 361 ? -29.559 67.532  6.974   1.00 11.36 ? 466  LYS B CA  1 
ATOM   6294 C  C   . LYS B 1 361 ? -28.768 67.361  5.687   1.00 12.39 ? 466  LYS B C   1 
ATOM   6295 O  O   . LYS B 1 361 ? -27.909 68.185  5.318   1.00 12.83 ? 466  LYS B O   1 
ATOM   6296 C  CB  . LYS B 1 361 ? -28.642 68.234  8.055   1.00 13.38 ? 466  LYS B CB  1 
ATOM   6297 C  CG  . LYS B 1 361 ? -29.321 68.469  9.390   1.00 15.15 ? 466  LYS B CG  1 
ATOM   6298 C  CD  . LYS B 1 361 ? -28.441 69.343  10.264  1.00 17.45 ? 466  LYS B CD  1 
ATOM   6299 C  CE  . LYS B 1 361 ? -28.987 69.654  11.713  1.00 19.94 ? 466  LYS B CE  1 
ATOM   6300 N  NZ  . LYS B 1 361 ? -29.111 68.404  12.462  1.00 27.01 ? 466  LYS B NZ  1 
ATOM   6301 N  N   . PHE B 1 362 ? -29.206 66.350  4.909   1.00 11.91 ? 467  PHE B N   1 
ATOM   6302 C  CA  . PHE B 1 362 ? -28.725 66.332  3.478   1.00 11.71 ? 467  PHE B CA  1 
ATOM   6303 C  C   . PHE B 1 362 ? -29.424 67.442  2.706   1.00 13.07 ? 467  PHE B C   1 
ATOM   6304 O  O   . PHE B 1 362 ? -30.568 67.817  3.068   1.00 15.32 ? 467  PHE B O   1 
ATOM   6305 C  CB  . PHE B 1 362 ? -29.143 64.967  2.826   1.00 11.59 ? 467  PHE B CB  1 
ATOM   6306 C  CG  . PHE B 1 362 ? -28.281 63.729  3.212   1.00 10.72 ? 467  PHE B CG  1 
ATOM   6307 C  CD1 . PHE B 1 362 ? -27.444 63.123  2.273   1.00 10.18 ? 467  PHE B CD1 1 
ATOM   6308 C  CD2 . PHE B 1 362 ? -28.412 63.142  4.477   1.00 10.95 ? 467  PHE B CD2 1 
ATOM   6309 C  CE1 . PHE B 1 362 ? -26.714 61.983  2.600   1.00 10.79 ? 467  PHE B CE1 1 
ATOM   6310 C  CE2 . PHE B 1 362 ? -27.690 62.000  4.817   1.00 11.17 ? 467  PHE B CE2 1 
ATOM   6311 C  CZ  . PHE B 1 362 ? -26.847 61.380  3.837   1.00 11.58 ? 467  PHE B CZ  1 
ATOM   6312 N  N   . GLY B 1 363 ? -28.762 67.891  1.700   1.00 11.99 ? 468  GLY B N   1 
ATOM   6313 C  CA  . GLY B 1 363 ? -29.276 68.883  0.706   1.00 12.43 ? 468  GLY B CA  1 
ATOM   6314 C  C   . GLY B 1 363 ? -29.390 68.208  -0.663  1.00 13.17 ? 468  GLY B C   1 
ATOM   6315 O  O   . GLY B 1 363 ? -28.470 67.439  -1.042  1.00 13.32 ? 468  GLY B O   1 
ATOM   6316 N  N   . ILE B 1 364 ? -30.416 68.546  -1.420  1.00 13.52 ? 469  ILE B N   1 
ATOM   6317 C  CA  . ILE B 1 364 ? -30.519 67.917  -2.775  1.00 14.83 ? 469  ILE B CA  1 
ATOM   6318 C  C   . ILE B 1 364 ? -29.508 68.480  -3.724  1.00 15.19 ? 469  ILE B C   1 
ATOM   6319 O  O   . ILE B 1 364 ? -29.152 69.655  -3.709  1.00 15.40 ? 469  ILE B O   1 
ATOM   6320 C  CB  . ILE B 1 364 ? -31.958 67.976  -3.273  1.00 15.00 ? 469  ILE B CB  1 
ATOM   6321 C  CG1 . ILE B 1 364 ? -32.239 66.987  -4.410  1.00 15.03 ? 469  ILE B CG1 1 
ATOM   6322 C  CG2 . ILE B 1 364 ? -32.357 69.393  -3.848  1.00 16.87 ? 469  ILE B CG2 1 
ATOM   6323 C  CD1 . ILE B 1 364 ? -33.721 66.714  -4.608  1.00 18.54 ? 469  ILE B CD1 1 
ATOM   6324 N  N   . GLY B 1 365 ? -29.074 67.647  -4.671  1.00 15.37 ? 470  GLY B N   1 
ATOM   6325 C  CA  . GLY B 1 365 ? -28.061 68.041  -5.697  1.00 17.35 ? 470  GLY B CA  1 
ATOM   6326 C  C   . GLY B 1 365 ? -28.856 68.594  -6.887  1.00 16.90 ? 470  GLY B C   1 
ATOM   6327 O  O   . GLY B 1 365 ? -30.084 68.884  -6.774  1.00 19.09 ? 470  GLY B O   1 
ATOM   6328 N  N   . ASP B 1 366 ? -28.178 68.701  -7.996  1.00 17.21 ? 471  ASP B N   1 
ATOM   6329 C  CA  A ASP B 1 366 ? -28.834 69.341  -9.148  0.50 17.32 ? 471  ASP B CA  1 
ATOM   6330 C  CA  B ASP B 1 366 ? -28.656 69.375  -9.223  0.50 18.48 ? 471  ASP B CA  1 
ATOM   6331 C  C   . ASP B 1 366 ? -29.227 68.411  -10.285 1.00 20.65 ? 471  ASP B C   1 
ATOM   6332 O  O   . ASP B 1 366 ? -29.946 68.771  -11.174 1.00 27.41 ? 471  ASP B O   1 
ATOM   6333 C  CB  A ASP B 1 366 ? -27.956 70.452  -9.720  0.50 17.78 ? 471  ASP B CB  1 
ATOM   6334 C  CB  B ASP B 1 366 ? -27.490 70.196  -9.872  0.50 19.67 ? 471  ASP B CB  1 
ATOM   6335 C  CG  A ASP B 1 366 ? -26.589 69.986  -9.992  0.50 16.33 ? 471  ASP B CG  1 
ATOM   6336 C  CG  B ASP B 1 366 ? -27.140 71.465  -9.083  0.50 23.78 ? 471  ASP B CG  1 
ATOM   6337 O  OD1 A ASP B 1 366 ? -26.389 68.770  -9.884  0.50 17.71 ? 471  ASP B OD1 1 
ATOM   6338 O  OD1 B ASP B 1 366 ? -28.086 71.964  -8.417  0.50 25.51 ? 471  ASP B OD1 1 
ATOM   6339 O  OD2 A ASP B 1 366 ? -25.709 70.809  -10.234 0.50 24.25 ? 471  ASP B OD2 1 
ATOM   6340 O  OD2 B ASP B 1 366 ? -25.962 71.959  -9.155  0.50 23.32 ? 471  ASP B OD2 1 
ATOM   6341 N  N   . GLY B 1 367 ? -28.790 67.198  -10.280 1.00 18.85 ? 472  GLY B N   1 
ATOM   6342 C  CA  . GLY B 1 367 ? -29.115 66.342  -11.444 1.00 18.20 ? 472  GLY B CA  1 
ATOM   6343 C  C   . GLY B 1 367 ? -29.663 64.977  -10.966 1.00 15.24 ? 472  GLY B C   1 
ATOM   6344 O  O   . GLY B 1 367 ? -29.864 64.675  -9.796  1.00 15.45 ? 472  GLY B O   1 
ATOM   6345 N  N   . ASN B 1 368 ? -29.899 64.100  -11.998 1.00 14.71 ? 473  ASN B N   1 
ATOM   6346 C  CA  A ASN B 1 368 ? -30.442 62.756  -11.677 0.50 14.40 ? 473  ASN B CA  1 
ATOM   6347 C  CA  B ASN B 1 368 ? -30.514 62.773  -11.869 0.50 14.38 ? 473  ASN B CA  1 
ATOM   6348 C  C   . ASN B 1 368 ? -29.488 61.665  -12.118 1.00 12.36 ? 473  ASN B C   1 
ATOM   6349 O  O   . ASN B 1 368 ? -28.603 61.898  -12.919 1.00 13.65 ? 473  ASN B O   1 
ATOM   6350 C  CB  A ASN B 1 368 ? -31.794 62.524  -12.375 0.50 14.96 ? 473  ASN B CB  1 
ATOM   6351 C  CB  B ASN B 1 368 ? -31.553 62.654  -12.991 0.50 13.90 ? 473  ASN B CB  1 
ATOM   6352 C  CG  A ASN B 1 368 ? -32.951 63.283  -11.724 0.50 19.56 ? 473  ASN B CG  1 
ATOM   6353 C  CG  B ASN B 1 368 ? -32.471 63.815  -13.032 0.50 17.48 ? 473  ASN B CG  1 
ATOM   6354 O  OD1 A ASN B 1 368 ? -33.473 62.915  -10.673 0.50 19.58 ? 473  ASN B OD1 1 
ATOM   6355 O  OD1 B ASN B 1 368 ? -32.722 64.403  -14.090 0.50 21.77 ? 473  ASN B OD1 1 
ATOM   6356 N  ND2 A ASN B 1 368 ? -33.420 64.243  -12.438 0.50 21.10 ? 473  ASN B ND2 1 
ATOM   6357 N  ND2 B ASN B 1 368 ? -32.949 64.184  -11.863 0.50 17.42 ? 473  ASN B ND2 1 
ATOM   6358 N  N   . LEU B 1 369 ? -29.697 60.507  -11.540 1.00 11.67 ? 474  LEU B N   1 
ATOM   6359 C  CA  . LEU B 1 369 ? -29.036 59.244  -12.041 1.00 10.76 ? 474  LEU B CA  1 
ATOM   6360 C  C   . LEU B 1 369 ? -30.178 58.418  -12.502 1.00 10.36 ? 474  LEU B C   1 
ATOM   6361 O  O   . LEU B 1 369 ? -31.088 58.005  -11.690 1.00 10.35 ? 474  LEU B O   1 
ATOM   6362 C  CB  . LEU B 1 369 ? -28.224 58.590  -10.918 1.00 12.21 ? 474  LEU B CB  1 
ATOM   6363 C  CG  . LEU B 1 369 ? -27.405 57.383  -11.443 1.00 10.83 ? 474  LEU B CG  1 
ATOM   6364 C  CD1 . LEU B 1 369 ? -26.294 57.803  -12.419 1.00 11.20 ? 474  LEU B CD1 1 
ATOM   6365 C  CD2 . LEU B 1 369 ? -26.831 56.605  -10.257 1.00 12.63 ? 474  LEU B CD2 1 
ATOM   6366 N  N   . GLN B 1 370 ? -30.228 58.165  -13.845 1.00 10.01 ? 475  GLN B N   1 
ATOM   6367 C  CA  A GLN B 1 370 ? -31.228 57.372  -14.477 0.50 9.13  ? 475  GLN B CA  1 
ATOM   6368 C  CA  B GLN B 1 370 ? -31.290 57.309  -14.383 0.50 10.56 ? 475  GLN B CA  1 
ATOM   6369 C  C   . GLN B 1 370 ? -30.841 55.866  -14.445 1.00 9.29  ? 475  GLN B C   1 
ATOM   6370 O  O   . GLN B 1 370 ? -29.652 55.566  -14.681 1.00 10.88 ? 475  GLN B O   1 
ATOM   6371 C  CB  A GLN B 1 370 ? -31.307 57.857  -15.960 0.50 8.19  ? 475  GLN B CB  1 
ATOM   6372 C  CB  B GLN B 1 370 ? -31.802 57.699  -15.811 0.50 12.33 ? 475  GLN B CB  1 
ATOM   6373 C  CG  A GLN B 1 370 ? -31.738 59.328  -16.150 0.50 8.28  ? 475  GLN B CG  1 
ATOM   6374 C  CG  B GLN B 1 370 ? -32.729 58.943  -15.766 0.50 15.84 ? 475  GLN B CG  1 
ATOM   6375 C  CD  A GLN B 1 370 ? -33.121 59.704  -15.707 0.50 9.74  ? 475  GLN B CD  1 
ATOM   6376 C  CD  B GLN B 1 370 ? -31.973 60.249  -15.803 0.50 19.25 ? 475  GLN B CD  1 
ATOM   6377 O  OE1 A GLN B 1 370 ? -33.415 60.914  -15.748 0.50 13.63 ? 475  GLN B OE1 1 
ATOM   6378 O  OE1 B GLN B 1 370 ? -30.733 60.317  -15.902 0.50 21.36 ? 475  GLN B OE1 1 
ATOM   6379 N  NE2 A GLN B 1 370 ? -33.923 58.792  -15.357 0.50 7.38  ? 475  GLN B NE2 1 
ATOM   6380 N  NE2 B GLN B 1 370 ? -32.729 61.342  -15.697 0.50 17.79 ? 475  GLN B NE2 1 
ATOM   6381 N  N   . TYR B 1 371 ? -31.771 54.957  -14.246 1.00 9.02  ? 476  TYR B N   1 
ATOM   6382 C  CA  . TYR B 1 371 ? -31.506 53.474  -14.357 1.00 8.61  ? 476  TYR B CA  1 
ATOM   6383 C  C   . TYR B 1 371 ? -32.161 52.980  -15.592 1.00 9.64  ? 476  TYR B C   1 
ATOM   6384 O  O   . TYR B 1 371 ? -33.303 53.362  -15.912 1.00 11.12 ? 476  TYR B O   1 
ATOM   6385 C  CB  . TYR B 1 371 ? -32.153 52.826  -13.129 1.00 9.09  ? 476  TYR B CB  1 
ATOM   6386 C  CG  . TYR B 1 371 ? -31.289 52.959  -11.891 1.00 9.31  ? 476  TYR B CG  1 
ATOM   6387 C  CD1 . TYR B 1 371 ? -30.631 51.819  -11.371 1.00 9.45  ? 476  TYR B CD1 1 
ATOM   6388 C  CD2 . TYR B 1 371 ? -31.132 54.176  -11.228 1.00 10.30 ? 476  TYR B CD2 1 
ATOM   6389 C  CE1 . TYR B 1 371 ? -29.776 51.896  -10.271 1.00 9.46  ? 476  TYR B CE1 1 
ATOM   6390 C  CE2 . TYR B 1 371 ? -30.287 54.292  -10.076 1.00 9.86  ? 476  TYR B CE2 1 
ATOM   6391 C  CZ  . TYR B 1 371 ? -29.609 53.135  -9.643  1.00 9.24  ? 476  TYR B CZ  1 
ATOM   6392 O  OH  . TYR B 1 371 ? -28.816 53.275  -8.527  1.00 9.17  ? 476  TYR B OH  1 
ATOM   6393 N  N   . TYR B 1 372 ? -31.490 51.999  -16.249 1.00 9.83  ? 477  TYR B N   1 
ATOM   6394 C  CA  . TYR B 1 372 ? -31.937 51.466  -17.568 1.00 9.41  ? 477  TYR B CA  1 
ATOM   6395 C  C   . TYR B 1 372 ? -31.761 49.976  -17.573 1.00 9.50  ? 477  TYR B C   1 
ATOM   6396 O  O   . TYR B 1 372 ? -30.791 49.410  -16.958 1.00 9.74  ? 477  TYR B O   1 
ATOM   6397 C  CB  . TYR B 1 372 ? -31.072 52.019  -18.690 1.00 9.87  ? 477  TYR B CB  1 
ATOM   6398 C  CG  . TYR B 1 372 ? -31.179 53.523  -18.852 1.00 9.62  ? 477  TYR B CG  1 
ATOM   6399 C  CD1 . TYR B 1 372 ? -32.276 54.079  -19.586 1.00 11.29 ? 477  TYR B CD1 1 
ATOM   6400 C  CD2 . TYR B 1 372 ? -30.226 54.344  -18.277 1.00 10.32 ? 477  TYR B CD2 1 
ATOM   6401 C  CE1 . TYR B 1 372 ? -32.388 55.440  -19.715 1.00 10.91 ? 477  TYR B CE1 1 
ATOM   6402 C  CE2 . TYR B 1 372 ? -30.313 55.752  -18.384 1.00 10.56 ? 477  TYR B CE2 1 
ATOM   6403 C  CZ  . TYR B 1 372 ? -31.428 56.258  -19.133 1.00 10.44 ? 477  TYR B CZ  1 
ATOM   6404 O  OH  . TYR B 1 372 ? -31.570 57.651  -19.261 1.00 12.42 ? 477  TYR B OH  1 
ATOM   6405 N  N   . LEU B 1 373 ? -32.617 49.292  -18.340 1.00 9.35  ? 478  LEU B N   1 
ATOM   6406 C  CA  . LEU B 1 373 ? -32.342 47.903  -18.770 1.00 9.18  ? 478  LEU B CA  1 
ATOM   6407 C  C   . LEU B 1 373 ? -32.222 47.896  -20.299 1.00 9.60  ? 478  LEU B C   1 
ATOM   6408 O  O   . LEU B 1 373 ? -32.945 48.638  -21.018 1.00 10.06 ? 478  LEU B O   1 
ATOM   6409 C  CB  . LEU B 1 373 ? -33.458 46.925  -18.321 1.00 11.02 ? 478  LEU B CB  1 
ATOM   6410 C  CG  . LEU B 1 373 ? -33.563 46.922  -16.828 1.00 11.67 ? 478  LEU B CG  1 
ATOM   6411 C  CD1 . LEU B 1 373 ? -34.946 46.464  -16.402 1.00 17.54 ? 478  LEU B CD1 1 
ATOM   6412 C  CD2 . LEU B 1 373 ? -32.504 46.122  -16.192 1.00 18.88 ? 478  LEU B CD2 1 
ATOM   6413 N  N   . TYR B 1 374 ? -31.335 47.017  -20.821 1.00 8.47  ? 479  TYR B N   1 
ATOM   6414 C  CA  . TYR B 1 374 ? -31.236 46.740  -22.253 1.00 8.71  ? 479  TYR B CA  1 
ATOM   6415 C  C   . TYR B 1 374 ? -31.915 45.447  -22.566 1.00 8.12  ? 479  TYR B C   1 
ATOM   6416 O  O   . TYR B 1 374 ? -31.694 44.420  -21.909 1.00 8.63  ? 479  TYR B O   1 
ATOM   6417 C  CB  . TYR B 1 374 ? -29.719 46.668  -22.599 1.00 8.96  ? 479  TYR B CB  1 
ATOM   6418 C  CG  . TYR B 1 374 ? -29.425 46.473  -24.087 1.00 8.80  ? 479  TYR B CG  1 
ATOM   6419 C  CD1 . TYR B 1 374 ? -29.194 47.590  -24.881 1.00 8.49  ? 479  TYR B CD1 1 
ATOM   6420 C  CD2 . TYR B 1 374 ? -29.370 45.221  -24.683 1.00 8.41  ? 479  TYR B CD2 1 
ATOM   6421 C  CE1 . TYR B 1 374 ? -28.898 47.490  -26.220 1.00 9.02  ? 479  TYR B CE1 1 
ATOM   6422 C  CE2 . TYR B 1 374 ? -29.069 45.061  -26.036 1.00 8.62  ? 479  TYR B CE2 1 
ATOM   6423 C  CZ  . TYR B 1 374 ? -28.822 46.192  -26.783 1.00 7.78  ? 479  TYR B CZ  1 
ATOM   6424 O  OH  . TYR B 1 374 ? -28.529 46.053  -28.118 1.00 10.10 ? 479  TYR B OH  1 
ATOM   6425 N  N   . ASN B 1 375 ? -32.801 45.506  -23.590 1.00 9.14  ? 480  ASN B N   1 
ATOM   6426 C  CA  . ASN B 1 375 ? -33.561 44.325  -24.048 1.00 8.06  ? 480  ASN B CA  1 
ATOM   6427 C  C   . ASN B 1 375 ? -34.427 43.672  -22.974 1.00 7.98  ? 480  ASN B C   1 
ATOM   6428 O  O   . ASN B 1 375 ? -34.584 42.469  -22.882 1.00 9.33  ? 480  ASN B O   1 
ATOM   6429 C  CB  . ASN B 1 375 ? -32.613 43.286  -24.695 1.00 9.70  ? 480  ASN B CB  1 
ATOM   6430 C  CG  . ASN B 1 375 ? -33.350 42.175  -25.402 1.00 9.23  ? 480  ASN B CG  1 
ATOM   6431 O  OD1 . ASN B 1 375 ? -34.368 42.456  -26.057 1.00 10.75 ? 480  ASN B OD1 1 
ATOM   6432 N  ND2 . ASN B 1 375 ? -32.784 40.965  -25.367 1.00 9.85  ? 480  ASN B ND2 1 
ATOM   6433 N  N   . TRP B 1 376 ? -35.008 44.557  -22.137 1.00 10.04 ? 481  TRP B N   1 
ATOM   6434 C  CA  . TRP B 1 376 ? -36.019 44.118  -21.145 1.00 10.41 ? 481  TRP B CA  1 
ATOM   6435 C  C   . TRP B 1 376 ? -37.032 45.211  -20.972 1.00 11.56 ? 481  TRP B C   1 
ATOM   6436 O  O   . TRP B 1 376 ? -36.715 46.277  -20.388 1.00 13.47 ? 481  TRP B O   1 
ATOM   6437 C  CB  . TRP B 1 376 ? -35.378 43.725  -19.792 1.00 10.62 ? 481  TRP B CB  1 
ATOM   6438 C  CG  . TRP B 1 376 ? -36.364 42.927  -18.974 1.00 10.23 ? 481  TRP B CG  1 
ATOM   6439 C  CD1 . TRP B 1 376 ? -37.199 43.359  -17.923 1.00 10.60 ? 481  TRP B CD1 1 
ATOM   6440 C  CD2 . TRP B 1 376 ? -36.584 41.521  -19.106 1.00 10.68 ? 481  TRP B CD2 1 
ATOM   6441 N  NE1 . TRP B 1 376 ? -37.900 42.315  -17.441 1.00 11.18 ? 481  TRP B NE1 1 
ATOM   6442 C  CE2 . TRP B 1 376 ? -37.544 41.157  -18.101 1.00 10.78 ? 481  TRP B CE2 1 
ATOM   6443 C  CE3 . TRP B 1 376 ? -36.064 40.544  -19.941 1.00 10.27 ? 481  TRP B CE3 1 
ATOM   6444 C  CZ2 . TRP B 1 376 ? -38.039 39.845  -17.941 1.00 13.09 ? 481  TRP B CZ2 1 
ATOM   6445 C  CZ3 . TRP B 1 376 ? -36.545 39.207  -19.756 1.00 11.51 ? 481  TRP B CZ3 1 
ATOM   6446 C  CH2 . TRP B 1 376 ? -37.516 38.874  -18.747 1.00 12.51 ? 481  TRP B CH2 1 
ATOM   6447 N  N   . LYS B 1 377 ? -38.227 44.991  -21.505 1.00 12.20 ? 482  LYS B N   1 
ATOM   6448 C  CA  . LYS B 1 377 ? -39.296 45.987  -21.356 1.00 14.17 ? 482  LYS B CA  1 
ATOM   6449 C  C   . LYS B 1 377 ? -40.042 45.644  -20.133 1.00 15.95 ? 482  LYS B C   1 
ATOM   6450 O  O   . LYS B 1 377 ? -40.466 44.474  -19.969 1.00 22.34 ? 482  LYS B O   1 
ATOM   6451 C  CB  . LYS B 1 377 ? -40.166 45.812  -22.625 1.00 19.11 ? 482  LYS B CB  1 
ATOM   6452 C  CG  . LYS B 1 377 ? -40.981 47.017  -22.958 1.00 23.13 ? 482  LYS B CG  1 
ATOM   6453 C  CD  . LYS B 1 377 ? -41.807 46.834  -24.247 1.00 22.87 ? 482  LYS B CD  1 
ATOM   6454 C  CE  . LYS B 1 377 ? -41.038 47.492  -25.337 1.00 24.32 ? 482  LYS B CE  1 
ATOM   6455 N  NZ  . LYS B 1 377 ? -41.921 47.618  -26.606 1.00 26.84 ? 482  LYS B NZ  1 
ATOM   6456 N  N   . CYS B 1 378 ? -40.213 46.612  -19.194 1.00 13.46 ? 483  CYS B N   1 
ATOM   6457 C  CA  . CYS B 1 378 ? -41.005 46.418  -18.004 1.00 14.71 ? 483  CYS B CA  1 
ATOM   6458 C  C   . CYS B 1 378 ? -41.536 47.790  -17.574 1.00 13.29 ? 483  CYS B C   1 
ATOM   6459 O  O   . CYS B 1 378 ? -41.045 48.783  -18.006 1.00 13.54 ? 483  CYS B O   1 
ATOM   6460 C  CB  . CYS B 1 378 ? -40.155 45.775  -16.890 1.00 17.96 ? 483  CYS B CB  1 
ATOM   6461 S  SG  . CYS B 1 378 ? -38.746 46.745  -16.414 1.00 14.57 ? 483  CYS B SG  1 
ATOM   6462 N  N   . PRO B 1 379 ? -42.530 47.782  -16.627 1.00 13.63 ? 484  PRO B N   1 
ATOM   6463 C  CA  . PRO B 1 379 ? -43.015 49.109  -16.193 1.00 13.46 ? 484  PRO B CA  1 
ATOM   6464 C  C   . PRO B 1 379 ? -41.930 49.923  -15.445 1.00 12.92 ? 484  PRO B C   1 
ATOM   6465 O  O   . PRO B 1 379 ? -41.045 49.250  -14.766 1.00 14.38 ? 484  PRO B O   1 
ATOM   6466 C  CB  . PRO B 1 379 ? -44.177 48.761  -15.208 1.00 14.17 ? 484  PRO B CB  1 
ATOM   6467 C  CG  . PRO B 1 379 ? -44.643 47.414  -15.674 1.00 15.47 ? 484  PRO B CG  1 
ATOM   6468 C  CD  . PRO B 1 379 ? -43.328 46.657  -16.118 1.00 13.76 ? 484  PRO B CD  1 
ATOM   6469 N  N   . SER B 1 380 ? -41.940 51.183  -15.545 1.00 13.15 ? 485  SER B N   1 
ATOM   6470 C  CA  . SER B 1 380 ? -41.023 52.015  -14.714 1.00 12.55 ? 485  SER B CA  1 
ATOM   6471 C  C   . SER B 1 380 ? -41.475 51.957  -13.225 1.00 12.92 ? 485  SER B C   1 
ATOM   6472 O  O   . SER B 1 380 ? -42.565 51.453  -12.894 1.00 14.53 ? 485  SER B O   1 
ATOM   6473 C  CB  . SER B 1 380 ? -40.917 53.446  -15.182 1.00 14.61 ? 485  SER B CB  1 
ATOM   6474 O  OG  . SER B 1 380 ? -42.253 53.994  -15.116 1.00 19.34 ? 485  SER B OG  1 
ATOM   6475 N  N   . MET B 1 381 ? -40.534 52.323  -12.356 1.00 11.67 ? 486  MET B N   1 
ATOM   6476 C  CA  . MET B 1 381 ? -40.845 52.287  -10.881 1.00 12.08 ? 486  MET B CA  1 
ATOM   6477 C  C   . MET B 1 381 ? -40.386 53.534  -10.247 1.00 11.08 ? 486  MET B C   1 
ATOM   6478 O  O   . MET B 1 381 ? -39.544 54.277  -10.749 1.00 12.92 ? 486  MET B O   1 
ATOM   6479 C  CB  . MET B 1 381 ? -40.193 51.072  -10.268 1.00 13.28 ? 486  MET B CB  1 
ATOM   6480 C  CG  . MET B 1 381 ? -38.643 51.191  -10.241 1.00 13.51 ? 486  MET B CG  1 
ATOM   6481 S  SD  . MET B 1 381 ? -37.790 49.634  -9.789  1.00 13.07 ? 486  MET B SD  1 
ATOM   6482 C  CE  . MET B 1 381 ? -38.068 48.635  -11.244 1.00 13.58 ? 486  MET B CE  1 
ATOM   6483 N  N   . GLY B 1 382 ? -40.963 53.805  -9.054  1.00 12.66 ? 487  GLY B N   1 
ATOM   6484 C  CA  . GLY B 1 382 ? -40.451 54.974  -8.280  1.00 12.59 ? 487  GLY B CA  1 
ATOM   6485 C  C   . GLY B 1 382 ? -39.089 54.713  -7.666  1.00 11.87 ? 487  GLY B C   1 
ATOM   6486 O  O   . GLY B 1 382 ? -38.684 53.540  -7.565  1.00 11.75 ? 487  GLY B O   1 
ATOM   6487 N  N   . ALA B 1 383 ? -38.402 55.806  -7.321  1.00 12.42 ? 488  ALA B N   1 
ATOM   6488 C  CA  . ALA B 1 383 ? -36.982 55.688  -6.799  1.00 11.71 ? 488  ALA B CA  1 
ATOM   6489 C  C   . ALA B 1 383 ? -36.979 54.806  -5.573  1.00 12.48 ? 488  ALA B C   1 
ATOM   6490 O  O   . ALA B 1 383 ? -36.048 54.031  -5.381  1.00 11.76 ? 488  ALA B O   1 
ATOM   6491 C  CB  . ALA B 1 383 ? -36.534 57.076  -6.473  1.00 15.22 ? 488  ALA B CB  1 
ATOM   6492 N  N   . GLU B 1 384 ? -38.067 54.788  -4.760  1.00 11.75 ? 489  GLU B N   1 
ATOM   6493 C  CA  A GLU B 1 384 ? -38.116 53.961  -3.517  0.50 12.84 ? 489  GLU B CA  1 
ATOM   6494 C  CA  B GLU B 1 384 ? -38.031 53.968  -3.521  0.50 12.36 ? 489  GLU B CA  1 
ATOM   6495 C  C   . GLU B 1 384 ? -38.126 52.461  -3.772  1.00 11.82 ? 489  GLU B C   1 
ATOM   6496 O  O   . GLU B 1 384 ? -37.978 51.649  -2.860  1.00 12.35 ? 489  GLU B O   1 
ATOM   6497 C  CB  A GLU B 1 384 ? -39.394 54.355  -2.676  0.50 15.85 ? 489  GLU B CB  1 
ATOM   6498 C  CB  B GLU B 1 384 ? -39.152 54.481  -2.564  0.50 14.45 ? 489  GLU B CB  1 
ATOM   6499 C  CG  A GLU B 1 384 ? -39.567 55.837  -2.272  0.50 17.68 ? 489  GLU B CG  1 
ATOM   6500 C  CG  B GLU B 1 384 ? -40.583 54.011  -2.932  0.50 15.75 ? 489  GLU B CG  1 
ATOM   6501 C  CD  A GLU B 1 384 ? -40.173 56.752  -3.370  0.50 18.25 ? 489  GLU B CD  1 
ATOM   6502 C  CD  B GLU B 1 384 ? -41.222 54.571  -4.215  0.50 18.08 ? 489  GLU B CD  1 
ATOM   6503 O  OE1 A GLU B 1 384 ? -40.402 56.365  -4.531  0.50 16.32 ? 489  GLU B OE1 1 
ATOM   6504 O  OE1 B GLU B 1 384 ? -40.817 55.647  -4.672  0.50 19.55 ? 489  GLU B OE1 1 
ATOM   6505 O  OE2 A GLU B 1 384 ? -40.414 57.898  -3.102  0.50 15.83 ? 489  GLU B OE2 1 
ATOM   6506 O  OE2 B GLU B 1 384 ? -42.135 53.910  -4.784  0.50 22.70 ? 489  GLU B OE2 1 
ATOM   6507 N  N   . LYS B 1 385 ? -38.408 52.081  -5.027  1.00 11.86 ? 490  LYS B N   1 
ATOM   6508 C  CA  . LYS B 1 385 ? -38.424 50.676  -5.395  1.00 11.81 ? 490  LYS B CA  1 
ATOM   6509 C  C   . LYS B 1 385 ? -37.119 50.233  -6.112  1.00 10.40 ? 490  LYS B C   1 
ATOM   6510 O  O   . LYS B 1 385 ? -36.966 49.050  -6.412  1.00 11.30 ? 490  LYS B O   1 
ATOM   6511 C  CB  . LYS B 1 385 ? -39.647 50.320  -6.304  1.00 13.82 ? 490  LYS B CB  1 
ATOM   6512 C  CG  . LYS B 1 385 ? -41.020 50.468  -5.515  1.00 19.81 ? 490  LYS B CG  1 
ATOM   6513 C  CD  . LYS B 1 385 ? -41.051 49.537  -4.291  1.00 22.81 ? 490  LYS B CD  1 
ATOM   6514 C  CE  . LYS B 1 385 ? -42.359 49.260  -3.488  1.00 30.89 ? 490  LYS B CE  1 
ATOM   6515 N  NZ  . LYS B 1 385 ? -43.076 50.550  -3.640  1.00 34.61 ? 490  LYS B NZ  1 
ATOM   6516 N  N   . VAL B 1 386 ? -36.260 51.196  -6.378  1.00 9.85  ? 491  VAL B N   1 
ATOM   6517 C  CA  . VAL B 1 386 ? -34.908 50.858  -6.988  1.00 10.03 ? 491  VAL B CA  1 
ATOM   6518 C  C   . VAL B 1 386 ? -34.024 50.390  -5.807  1.00 9.27  ? 491  VAL B C   1 
ATOM   6519 O  O   . VAL B 1 386 ? -33.844 51.119  -4.779  1.00 10.05 ? 491  VAL B O   1 
ATOM   6520 C  CB  . VAL B 1 386 ? -34.291 52.047  -7.673  1.00 10.28 ? 491  VAL B CB  1 
ATOM   6521 C  CG1 . VAL B 1 386 ? -32.906 51.702  -8.273  1.00 11.88 ? 491  VAL B CG1 1 
ATOM   6522 C  CG2 . VAL B 1 386 ? -35.175 52.492  -8.868  1.00 12.41 ? 491  VAL B CG2 1 
ATOM   6523 N  N   . GLY B 1 387 ? -33.439 49.184  -5.924  1.00 9.25  ? 492  GLY B N   1 
ATOM   6524 C  CA  . GLY B 1 387 ? -32.575 48.577  -4.872  1.00 10.07 ? 492  GLY B CA  1 
ATOM   6525 C  C   . GLY B 1 387 ? -31.241 48.091  -5.403  1.00 9.10  ? 492  GLY B C   1 
ATOM   6526 O  O   . GLY B 1 387 ? -30.759 47.008  -5.014  1.00 9.32  ? 492  GLY B O   1 
ATOM   6527 N  N   . LEU B 1 388 ? -30.645 48.896  -6.252  1.00 10.07 ? 493  LEU B N   1 
ATOM   6528 C  CA  . LEU B 1 388 ? -29.372 48.568  -6.918  1.00 8.95  ? 493  LEU B CA  1 
ATOM   6529 C  C   . LEU B 1 388 ? -28.502 49.778  -6.962  1.00 8.80  ? 493  LEU B C   1 
ATOM   6530 O  O   . LEU B 1 388 ? -28.979 50.861  -7.347  1.00 9.53  ? 493  LEU B O   1 
ATOM   6531 C  CB  . LEU B 1 388 ? -29.681 48.103  -8.364  1.00 9.14  ? 493  LEU B CB  1 
ATOM   6532 C  CG  . LEU B 1 388 ? -28.500 47.810  -9.293  1.00 10.48 ? 493  LEU B CG  1 
ATOM   6533 C  CD1 . LEU B 1 388 ? -27.702 46.605  -8.812  1.00 12.27 ? 493  LEU B CD1 1 
ATOM   6534 C  CD2 . LEU B 1 388 ? -28.992 47.644  -10.738 1.00 11.86 ? 493  LEU B CD2 1 
ATOM   6535 N  N   . VAL B 1 389 ? -27.249 49.642  -6.572  1.00 8.81  ? 494  VAL B N   1 
ATOM   6536 C  CA  . VAL B 1 389 ? -26.266 50.745  -6.555  1.00 9.25  ? 494  VAL B CA  1 
ATOM   6537 C  C   . VAL B 1 389 ? -25.067 50.337  -7.414  1.00 9.96  ? 494  VAL B C   1 
ATOM   6538 O  O   . VAL B 1 389 ? -24.442 49.241  -7.116  1.00 11.98 ? 494  VAL B O   1 
ATOM   6539 C  CB  . VAL B 1 389 ? -25.824 51.086  -5.113  1.00 9.88  ? 494  VAL B CB  1 
ATOM   6540 C  CG1 . VAL B 1 389 ? -24.783 52.226  -5.142  1.00 11.36 ? 494  VAL B CG1 1 
ATOM   6541 C  CG2 . VAL B 1 389 ? -27.029 51.532  -4.278  1.00 12.80 ? 494  VAL B CG2 1 
ATOM   6542 N  N   . LEU B 1 390 ? -24.694 51.116  -8.399  1.00 10.25 ? 495  LEU B N   1 
ATOM   6543 C  CA  . LEU B 1 390 ? -23.433 50.862  -9.196  1.00 10.99 ? 495  LEU B CA  1 
ATOM   6544 C  C   . LEU B 1 390 ? -22.364 51.900  -8.828  1.00 11.12 ? 495  LEU B C   1 
ATOM   6545 O  O   . LEU B 1 390 ? -22.732 53.064  -8.517  1.00 14.81 ? 495  LEU B O   1 
ATOM   6546 C  CB  . LEU B 1 390 ? -23.718 50.963  -10.720 1.00 12.31 ? 495  LEU B CB  1 
ATOM   6547 C  CG  . LEU B 1 390 ? -24.621 49.880  -11.290 1.00 15.00 ? 495  LEU B CG  1 
ATOM   6548 C  CD1 . LEU B 1 390 ? -24.593 49.993  -12.814 1.00 15.35 ? 495  LEU B CD1 1 
ATOM   6549 C  CD2 . LEU B 1 390 ? -24.500 48.475  -10.810 1.00 21.99 ? 495  LEU B CD2 1 
ATOM   6550 N  N   . GLN B 1 391 ? -21.103 51.562  -8.904  1.00 12.25 ? 496  GLN B N   1 
ATOM   6551 C  CA  . GLN B 1 391 ? -20.046 52.503  -8.585  1.00 13.05 ? 496  GLN B CA  1 
ATOM   6552 C  C   . GLN B 1 391 ? -19.859 53.533  -9.643  1.00 13.32 ? 496  GLN B C   1 
ATOM   6553 O  O   . GLN B 1 391 ? -19.249 54.573  -9.265  1.00 14.61 ? 496  GLN B O   1 
ATOM   6554 C  CB  . GLN B 1 391 ? -18.697 51.734  -8.458  1.00 15.82 ? 496  GLN B CB  1 
ATOM   6555 C  CG  . GLN B 1 391 ? -18.612 50.735  -7.284  1.00 16.11 ? 496  GLN B CG  1 
ATOM   6556 C  CD  . GLN B 1 391 ? -19.353 49.442  -7.529  1.00 16.48 ? 496  GLN B CD  1 
ATOM   6557 O  OE1 . GLN B 1 391 ? -19.736 49.081  -8.655  1.00 17.52 ? 496  GLN B OE1 1 
ATOM   6558 N  NE2 . GLN B 1 391 ? -19.666 48.718  -6.466  1.00 16.43 ? 496  GLN B NE2 1 
ATOM   6559 O  OXT . GLN B 1 391 ? -20.328 53.409  -10.784 1.00 11.57 ? 496  GLN B OXT 1 
HETATM 6560 S  S1  . MYA C 2 .   ? -19.371 9.246   -12.215 1.00 12.62 ? 2001 MYA A S1  1 
HETATM 6561 C  C2  . MYA C 2 .   ? -17.747 8.491   -12.200 1.00 11.69 ? 2001 MYA A C2  1 
HETATM 6562 C  C3  . MYA C 2 .   ? -17.426 7.965   -10.766 1.00 11.20 ? 2001 MYA A C3  1 
HETATM 6563 N  N4  . MYA C 2 .   ? -16.082 7.455   -10.667 1.00 11.20 ? 2001 MYA A N4  1 
HETATM 6564 C  C5  . MYA C 2 .   ? -15.718 6.149   -10.716 1.00 11.34 ? 2001 MYA A C5  1 
HETATM 6565 O  O5  . MYA C 2 .   ? -16.564 5.255   -10.913 1.00 12.44 ? 2001 MYA A O5  1 
HETATM 6566 C  C6  . MYA C 2 .   ? -14.298 5.853   -10.630 1.00 10.93 ? 2001 MYA A C6  1 
HETATM 6567 C  C7  . MYA C 2 .   ? -13.943 4.508   -9.943  1.00 10.44 ? 2001 MYA A C7  1 
HETATM 6568 N  N8  . MYA C 2 .   ? -14.541 4.483   -8.579  1.00 11.98 ? 2001 MYA A N8  1 
HETATM 6569 C  C9  . MYA C 2 .   ? -14.178 5.267   -7.560  1.00 10.49 ? 2001 MYA A C9  1 
HETATM 6570 O  O9  . MYA C 2 .   ? -13.230 6.081   -7.705  1.00 10.53 ? 2001 MYA A O9  1 
HETATM 6571 C  C10 . MYA C 2 .   ? -14.888 5.123   -6.234  1.00 10.64 ? 2001 MYA A C10 1 
HETATM 6572 O  O10 . MYA C 2 .   ? -15.500 3.775   -6.247  1.00 12.91 ? 2001 MYA A O10 1 
HETATM 6573 C  C11 . MYA C 2 .   ? -15.998 6.199   -6.038  1.00 11.24 ? 2001 MYA A C11 1 
HETATM 6574 C  C12 . MYA C 2 .   ? -16.836 5.855   -4.771  1.00 12.99 ? 2001 MYA A C12 1 
HETATM 6575 C  C13 . MYA C 2 .   ? -16.977 6.345   -7.224  1.00 13.47 ? 2001 MYA A C13 1 
HETATM 6576 C  C14 . MYA C 2 .   ? -15.255 7.548   -5.777  1.00 11.60 ? 2001 MYA A C14 1 
HETATM 6577 N  N1A . MYA C 2 .   ? -21.670 8.925   -7.503  1.00 14.27 ? 2001 MYA A N1A 1 
HETATM 6578 O  O1A . MYA C 2 .   ? -16.211 6.445   -0.350  1.00 12.85 ? 2001 MYA A O1A 1 
HETATM 6579 P  P1A . MYA C 2 .   ? -17.210 5.365   -0.363  1.00 12.72 ? 2001 MYA A P1A 1 
HETATM 6580 C  C1X . MYA C 2 .   ? -21.859 6.416   -3.018  1.00 15.41 ? 2001 MYA A C1X 1 
HETATM 6581 C  C2A . MYA C 2 .   ? -22.245 9.266   -6.351  1.00 15.16 ? 2001 MYA A C2A 1 
HETATM 6582 O  O2A . MYA C 2 .   ? -17.163 4.286   0.737   1.00 14.13 ? 2001 MYA A O2A 1 
HETATM 6583 P  P2A . MYA C 2 .   ? -15.917 4.365   -2.731  1.00 13.09 ? 2001 MYA A P2A 1 
HETATM 6584 C  C2M . MYA C 2 .   ? -19.045 10.866  -11.636 1.00 10.63 ? 2001 MYA A C2M 1 
HETATM 6585 O  O2M . MYA C 2 .   ? -17.901 11.247  -11.585 1.00 11.30 ? 2001 MYA A O2M 1 
HETATM 6586 C  C2X . MYA C 2 .   ? -22.459 5.095   -2.535  1.00 16.02 ? 2001 MYA A C2X 1 
HETATM 6587 O  O2X . MYA C 2 .   ? -23.781 4.849   -3.055  1.00 18.13 ? 2001 MYA A O2X 1 
HETATM 6588 N  N3A . MYA C 2 .   ? -22.251 8.496   -5.220  1.00 13.89 ? 2001 MYA A N3A 1 
HETATM 6589 O  O3A . MYA C 2 .   ? -17.186 4.569   -1.784  1.00 12.96 ? 2001 MYA A O3A 1 
HETATM 6590 C  C3M . MYA C 2 .   ? -20.231 11.705  -11.190 1.00 9.49  ? 2001 MYA A C3M 1 
HETATM 6591 C  C3X . MYA C 2 .   ? -22.322 5.354   -1.031  1.00 15.11 ? 2001 MYA A C3X 1 
HETATM 6592 O  O3X . MYA C 2 .   ? -23.371 6.283   -0.658  1.00 15.85 ? 2001 MYA A O3X 1 
HETATM 6593 P  P3X . MYA C 2 .   ? -24.575 5.697   0.227   1.00 17.22 ? 2001 MYA A P3X 1 
HETATM 6594 C  C4A . MYA C 2 .   ? -21.560 7.365   -5.320  1.00 16.26 ? 2001 MYA A C4A 1 
HETATM 6595 O  O4A . MYA C 2 .   ? -16.282 3.203   -3.651  1.00 13.29 ? 2001 MYA A O4A 1 
HETATM 6596 C  C4M . MYA C 2 .   ? -20.143 11.813  -9.661  1.00 10.42 ? 2001 MYA A C4M 1 
HETATM 6597 C  C4X . MYA C 2 .   ? -20.981 6.072   -0.898  1.00 13.82 ? 2001 MYA A C4X 1 
HETATM 6598 O  O4X . MYA C 2 .   ? -20.732 6.704   -2.203  1.00 14.95 ? 2001 MYA A O4X 1 
HETATM 6599 C  C5A . MYA C 2 .   ? -20.946 6.937   -6.482  1.00 14.85 ? 2001 MYA A C5A 1 
HETATM 6600 O  O5A . MYA C 2 .   ? -14.648 4.287   -2.036  1.00 13.46 ? 2001 MYA A O5A 1 
HETATM 6601 C  C5M . MYA C 2 .   ? -21.397 12.506  -9.096  1.00 9.61  ? 2001 MYA A C5M 1 
HETATM 6602 C  C5X . MYA C 2 .   ? -19.802 5.167   -0.550  1.00 14.45 ? 2001 MYA A C5X 1 
HETATM 6603 O  O5X . MYA C 2 .   ? -18.670 5.991   -0.415  1.00 13.98 ? 2001 MYA A O5X 1 
HETATM 6604 C  C6A . MYA C 2 .   ? -20.993 7.769   -7.634  1.00 14.24 ? 2001 MYA A C6A 1 
HETATM 6605 N  N6A . MYA C 2 .   ? -20.410 7.460   -8.861  1.00 14.23 ? 2001 MYA A N6A 1 
HETATM 6606 O  O6A . MYA C 2 .   ? -15.935 5.685   -3.639  1.00 12.27 ? 2001 MYA A O6A 1 
HETATM 6607 C  C6M . MYA C 2 .   ? -21.305 12.694  -7.544  1.00 10.22 ? 2001 MYA A C6M 1 
HETATM 6608 N  N7A . MYA C 2 .   ? -20.372 5.743   -6.245  1.00 16.91 ? 2001 MYA A N7A 1 
HETATM 6609 O  O7A . MYA C 2 .   ? -25.029 4.512   -0.671  1.00 21.27 ? 2001 MYA A O7A 1 
HETATM 6610 C  C7M . MYA C 2 .   ? -22.541 13.339  -6.918  1.00 10.71 ? 2001 MYA A C7M 1 
HETATM 6611 C  C8A . MYA C 2 .   ? -20.642 5.439   -4.961  1.00 14.68 ? 2001 MYA A C8A 1 
HETATM 6612 O  O8A . MYA C 2 .   ? -23.971 5.294   1.585   1.00 23.34 ? 2001 MYA A O8A 1 
HETATM 6613 C  C8M . MYA C 2 .   ? -22.701 14.837  -7.232  1.00 10.55 ? 2001 MYA A C8M 1 
HETATM 6614 N  N9A . MYA C 2 .   ? -21.403 6.384   -4.386  1.00 15.72 ? 2001 MYA A N9A 1 
HETATM 6615 O  O9A . MYA C 2 .   ? -25.578 6.771   0.389   1.00 16.05 ? 2001 MYA A O9A 1 
HETATM 6616 C  C9M . MYA C 2 .   ? -23.938 15.452  -6.593  1.00 9.98  ? 2001 MYA A C9M 1 
HETATM 6617 C  CAM . MYA C 2 .   ? -23.993 17.003  -6.825  1.00 10.03 ? 2001 MYA A CAM 1 
HETATM 6618 C  CBM . MYA C 2 .   ? -22.925 17.830  -6.110  1.00 9.17  ? 2001 MYA A CBM 1 
HETATM 6619 C  CCM . MYA C 2 .   ? -23.054 19.299  -6.476  1.00 8.81  ? 2001 MYA A CCM 1 
HETATM 6620 C  CDM . MYA C 2 .   ? -24.338 20.021  -5.985  1.00 10.19 ? 2001 MYA A CDM 1 
HETATM 6621 C  CEM . MYA C 2 .   ? -24.267 21.528  -6.209  1.00 9.46  ? 2001 MYA A CEM 1 
HETATM 6622 C  CFM . MYA C 2 .   ? -25.607 22.234  -5.900  1.00 10.15 ? 2001 MYA A CFM 1 
HETATM 6623 P  P   . PO4 D 3 .   ? -28.815 20.320  3.323   1.00 17.28 ? 2002 PO4 A P   1 
HETATM 6624 O  O1  . PO4 D 3 .   ? -28.526 20.812  1.857   1.00 18.37 ? 2002 PO4 A O1  1 
HETATM 6625 O  O2  . PO4 D 3 .   ? -30.173 19.546  3.143   1.00 21.14 ? 2002 PO4 A O2  1 
HETATM 6626 O  O3  . PO4 D 3 .   ? -27.756 19.384  3.829   1.00 18.75 ? 2002 PO4 A O3  1 
HETATM 6627 O  O4  . PO4 D 3 .   ? -29.100 21.550  4.098   1.00 20.50 ? 2002 PO4 A O4  1 
HETATM 6628 P  P   . PO4 E 3 .   ? -17.050 15.758  7.646   1.00 16.66 ? 2003 PO4 A P   1 
HETATM 6629 O  O1  . PO4 E 3 .   ? -16.158 14.902  6.738   1.00 19.77 ? 2003 PO4 A O1  1 
HETATM 6630 O  O2  . PO4 E 3 .   ? -18.426 15.567  7.155   1.00 16.08 ? 2003 PO4 A O2  1 
HETATM 6631 O  O3  . PO4 E 3 .   ? -16.463 17.047  7.804   1.00 17.04 ? 2003 PO4 A O3  1 
HETATM 6632 O  O4  . PO4 E 3 .   ? -17.017 15.166  9.141   1.00 19.80 ? 2003 PO4 A O4  1 
HETATM 6633 P  P   . PO4 F 3 .   ? -21.357 9.584   5.327   1.00 62.45 ? 2004 PO4 A P   1 
HETATM 6634 O  O1  . PO4 F 3 .   ? -20.990 8.403   4.441   1.00 54.37 ? 2004 PO4 A O1  1 
HETATM 6635 O  O2  . PO4 F 3 .   ? -22.500 10.473  4.848   1.00 46.24 ? 2004 PO4 A O2  1 
HETATM 6636 O  O3  . PO4 F 3 .   ? -20.145 10.514  5.488   1.00 59.47 ? 2004 PO4 A O3  1 
HETATM 6637 O  O4  . PO4 F 3 .   ? -21.852 8.878   6.600   1.00 64.71 ? 2004 PO4 A O4  1 
HETATM 6638 C  C12 . 9M2 G 4 .   ? -21.156 6.139   -23.234 1.00 13.36 ? 2005 9M2 A C12 1 
HETATM 6639 C  C8  . 9M2 G 4 .   ? -19.282 6.322   -19.347 1.00 13.72 ? 2005 9M2 A C8  1 
HETATM 6640 C  C9  . 9M2 G 4 .   ? -19.129 6.433   -17.938 1.00 13.67 ? 2005 9M2 A C9  1 
HETATM 6641 C  C10 . 9M2 G 4 .   ? -20.149 5.087   -21.239 1.00 14.09 ? 2005 9M2 A C10 1 
HETATM 6642 C  C11 . 9M2 G 4 .   ? -20.809 6.173   -21.893 1.00 14.62 ? 2005 9M2 A C11 1 
HETATM 6643 C  C7  . 9M2 G 4 .   ? -19.878 5.126   -19.814 1.00 12.81 ? 2005 9M2 A C7  1 
HETATM 6644 C  C6  . 9M2 G 4 .   ? -20.266 4.135   -18.867 1.00 13.50 ? 2005 9M2 A C6  1 
HETATM 6645 N  N1  . 9M2 G 4 .   ? -18.629 7.136   -15.845 1.00 12.88 ? 2005 9M2 A N1  1 
HETATM 6646 C  C5  . 9M2 G 4 .   ? -20.133 4.264   -17.466 1.00 14.97 ? 2005 9M2 A C5  1 
HETATM 6647 C  C4  . 9M2 G 4 .   ? -19.537 5.447   -17.020 1.00 12.90 ? 2005 9M2 A C4  1 
HETATM 6648 F  F   . 9M2 G 4 .   ? -21.239 4.895   -25.259 1.00 15.04 ? 2005 9M2 A F   1 
HETATM 6649 C  C13 . 9M2 G 4 .   ? -20.892 4.969   -23.920 1.00 14.48 ? 2005 9M2 A C13 1 
HETATM 6650 C  C14 . 9M2 G 4 .   ? -20.210 3.851   -23.386 1.00 14.54 ? 2005 9M2 A C14 1 
HETATM 6651 C  C15 . 9M2 G 4 .   ? -19.852 3.904   -22.053 1.00 14.49 ? 2005 9M2 A C15 1 
HETATM 6652 N  N2  . 9M2 G 4 .   ? -19.219 5.885   -15.761 1.00 14.60 ? 2005 9M2 A N2  1 
HETATM 6653 C  C3  . 9M2 G 4 .   ? -18.558 7.536   -17.077 1.00 13.77 ? 2005 9M2 A C3  1 
HETATM 6654 C  C2  . 9M2 G 4 .   ? -17.819 8.799   -17.430 1.00 13.26 ? 2005 9M2 A C2  1 
HETATM 6655 N  N   . 9M2 G 4 .   ? -18.721 9.988   -17.564 1.00 12.07 ? 2005 9M2 A N   1 
HETATM 6656 C  C1  . 9M2 G 4 .   ? -19.250 10.313  -16.167 1.00 14.83 ? 2005 9M2 A C1  1 
HETATM 6657 C  C   . 9M2 G 4 .   ? -19.834 9.833   -18.510 1.00 13.02 ? 2005 9M2 A C   1 
HETATM 6658 O  O   . 9M2 G 4 .   ? -19.205 2.900   -21.415 1.00 15.33 ? 2005 9M2 A O   1 
HETATM 6659 C  C16 . 9M2 G 4 .   ? -18.772 1.793   -22.314 1.00 19.10 ? 2005 9M2 A C16 1 
HETATM 6660 C  C17 . 9M2 G 4 .   ? -18.056 0.668   -21.500 1.00 20.52 ? 2005 9M2 A C17 1 
HETATM 6661 C  C18 . 9M2 G 4 .   ? -16.668 0.982   -21.126 1.00 20.92 ? 2005 9M2 A C18 1 
HETATM 6662 C  C22 . 9M2 G 4 .   ? -15.370 0.945   -21.863 1.00 19.44 ? 2005 9M2 A C22 1 
HETATM 6663 C  C23 . 9M2 G 4 .   ? -15.162 0.543   -23.289 1.00 24.82 ? 2005 9M2 A C23 1 
HETATM 6664 N  N4  . 9M2 G 4 .   ? -14.317 1.323   -21.173 1.00 20.08 ? 2005 9M2 A N4  1 
HETATM 6665 N  N3  . 9M2 G 4 .   ? -14.957 1.529   -19.946 1.00 15.52 ? 2005 9M2 A N3  1 
HETATM 6666 C  C21 . 9M2 G 4 .   ? -13.999 1.951   -18.931 1.00 18.01 ? 2005 9M2 A C21 1 
HETATM 6667 C  C19 . 9M2 G 4 .   ? -16.279 1.380   -19.775 1.00 14.82 ? 2005 9M2 A C19 1 
HETATM 6668 C  C20 . 9M2 G 4 .   ? -17.044 1.837   -18.573 1.00 15.67 ? 2005 9M2 A C20 1 
HETATM 6669 MG MG  . MG  H 5 .   ? -13.534 5.674   0.396   1.00 21.63 ? 2006 MG  A MG  1 
HETATM 6670 C  C1  . GOL I 6 .   ? -35.754 12.367  -10.719 1.00 20.49 ? 2007 GOL A C1  1 
HETATM 6671 O  O1  . GOL I 6 .   ? -36.793 12.394  -11.773 1.00 20.84 ? 2007 GOL A O1  1 
HETATM 6672 C  C2  . GOL I 6 .   ? -35.121 13.786  -10.661 1.00 17.53 ? 2007 GOL A C2  1 
HETATM 6673 O  O2  . GOL I 6 .   ? -36.022 14.623  -9.915  1.00 18.10 ? 2007 GOL A O2  1 
HETATM 6674 C  C3  . GOL I 6 .   ? -33.842 13.747  -9.861  1.00 18.77 ? 2007 GOL A C3  1 
HETATM 6675 O  O3  . GOL I 6 .   ? -32.723 13.126  -10.616 1.00 18.33 ? 2007 GOL A O3  1 
HETATM 6676 S  S   . DMS J 7 .   ? -14.566 13.859  12.924  1.00 39.48 ? 2008 DMS A S   1 
HETATM 6677 O  O   . DMS J 7 .   ? -13.502 12.724  13.076  1.00 40.29 ? 2008 DMS A O   1 
HETATM 6678 C  C1  . DMS J 7 .   ? -13.770 15.400  13.131  1.00 36.39 ? 2008 DMS A C1  1 
HETATM 6679 C  C2  . DMS J 7 .   ? -15.229 13.842  11.331  1.00 37.67 ? 2008 DMS A C2  1 
HETATM 6680 S  S1  . MYA K 2 .   ? -22.458 56.132  -17.467 1.00 11.61 ? 2001 MYA B S1  1 
HETATM 6681 C  C2  . MYA K 2 .   ? -20.934 57.085  -17.475 1.00 11.34 ? 2001 MYA B C2  1 
HETATM 6682 C  C3  . MYA K 2 .   ? -20.710 57.691  -18.859 1.00 10.73 ? 2001 MYA B C3  1 
HETATM 6683 N  N4  . MYA K 2 .   ? -19.437 58.362  -18.996 1.00 10.82 ? 2001 MYA B N4  1 
HETATM 6684 C  C5  . MYA K 2 .   ? -19.229 59.663  -18.935 1.00 11.08 ? 2001 MYA B C5  1 
HETATM 6685 O  O5  . MYA K 2 .   ? -20.215 60.474  -18.737 1.00 12.06 ? 2001 MYA B O5  1 
HETATM 6686 C  C6  . MYA K 2 .   ? -17.844 60.197  -19.024 1.00 10.45 ? 2001 MYA B C6  1 
HETATM 6687 C  C7  . MYA K 2 .   ? -17.733 61.566  -19.745 1.00 10.91 ? 2001 MYA B C7  1 
HETATM 6688 N  N8  . MYA K 2 .   ? -18.289 61.508  -21.107 1.00 9.96  ? 2001 MYA B N8  1 
HETATM 6689 C  C9  . MYA K 2 .   ? -17.822 60.773  -22.104 1.00 11.32 ? 2001 MYA B C9  1 
HETATM 6690 O  O9  . MYA K 2 .   ? -16.807 60.100  -21.943 1.00 10.43 ? 2001 MYA B O9  1 
HETATM 6691 C  C10 . MYA K 2 .   ? -18.530 60.809  -23.416 1.00 10.78 ? 2001 MYA B C10 1 
HETATM 6692 O  O10 . MYA K 2 .   ? -19.332 62.039  -23.387 1.00 10.87 ? 2001 MYA B O10 1 
HETATM 6693 C  C11 . MYA K 2 .   ? -19.475 59.610  -23.643 1.00 10.82 ? 2001 MYA B C11 1 
HETATM 6694 C  C12 . MYA K 2 .   ? -20.315 59.762  -24.902 1.00 11.78 ? 2001 MYA B C12 1 
HETATM 6695 C  C13 . MYA K 2 .   ? -20.472 59.333  -22.493 1.00 11.45 ? 2001 MYA B C13 1 
HETATM 6696 C  C14 . MYA K 2 .   ? -18.517 58.379  -23.841 1.00 10.65 ? 2001 MYA B C14 1 
HETATM 6697 N  N1A . MYA K 2 .   ? -24.716 56.183  -22.140 1.00 12.61 ? 2001 MYA B N1A 1 
HETATM 6698 O  O1A . MYA K 2 .   ? -19.607 59.299  -29.323 1.00 11.43 ? 2001 MYA B O1A 1 
HETATM 6699 P  P1A . MYA K 2 .   ? -20.746 60.258  -29.301 1.00 11.60 ? 2001 MYA B P1A 1 
HETATM 6700 C  C1X . MYA K 2 .   ? -25.252 58.563  -26.692 1.00 13.08 ? 2001 MYA B C1X 1 
HETATM 6701 C  C2A . MYA K 2 .   ? -25.301 55.738  -23.255 1.00 12.48 ? 2001 MYA B C2A 1 
HETATM 6702 O  O2A . MYA K 2 .   ? -20.759 61.260  -30.414 1.00 12.64 ? 2001 MYA B O2A 1 
HETATM 6703 P  P2A . MYA K 2 .   ? -19.602 61.418  -26.902 1.00 11.74 ? 2001 MYA B P2A 1 
HETATM 6704 C  C2M . MYA K 2 .   ? -21.900 54.549  -18.043 1.00 9.80  ? 2001 MYA B C2M 1 
HETATM 6705 O  O2M . MYA K 2 .   ? -20.706 54.269  -18.093 1.00 10.80 ? 2001 MYA B O2M 1 
HETATM 6706 C  C2X . MYA K 2 .   ? -25.955 59.820  -27.195 1.00 14.42 ? 2001 MYA B C2X 1 
HETATM 6707 O  O2X . MYA K 2 .   ? -27.306 59.857  -26.707 1.00 15.50 ? 2001 MYA B O2X 1 
HETATM 6708 N  N3A . MYA K 2 .   ? -25.409 56.448  -24.425 1.00 10.85 ? 2001 MYA B N3A 1 
HETATM 6709 O  O3A . MYA K 2 .   ? -20.815 61.048  -27.871 1.00 11.45 ? 2001 MYA B O3A 1 
HETATM 6710 C  C3M . MYA K 2 .   ? -22.953 53.534  -18.487 1.00 9.33  ? 2001 MYA B C3M 1 
HETATM 6711 C  C3X . MYA K 2 .   ? -25.837 59.551  -28.689 1.00 13.33 ? 2001 MYA B C3X 1 
HETATM 6712 O  O3X . MYA K 2 .   ? -26.762 58.527  -29.080 1.00 13.47 ? 2001 MYA B O3X 1 
HETATM 6713 P  P3X . MYA K 2 .   ? -28.034 58.993  -29.943 1.00 14.14 ? 2001 MYA B P3X 1 
HETATM 6714 C  C4A . MYA K 2 .   ? -24.874 57.702  -24.335 1.00 12.27 ? 2001 MYA B C4A 1 
HETATM 6715 O  O4A . MYA K 2 .   ? -20.150 62.514  -25.996 1.00 12.80 ? 2001 MYA B O4A 1 
HETATM 6716 C  C4M . MYA K 2 .   ? -22.912 53.449  -20.020 1.00 9.49  ? 2001 MYA B C4M 1 
HETATM 6717 C  C4X . MYA K 2 .   ? -24.421 59.027  -28.802 1.00 12.23 ? 2001 MYA B C4X 1 
HETATM 6718 O  O4X . MYA K 2 .   ? -24.109 58.435  -27.502 1.00 13.54 ? 2001 MYA B O4X 1 
HETATM 6719 C  C5A . MYA K 2 .   ? -24.295 58.227  -23.198 1.00 12.18 ? 2001 MYA B C5A 1 
HETATM 6720 O  O5A . MYA K 2 .   ? -18.369 61.650  -27.618 1.00 11.97 ? 2001 MYA B O5A 1 
HETATM 6721 C  C5M . MYA K 2 .   ? -24.013 52.610  -20.611 1.00 8.17  ? 2001 MYA B C5M 1 
HETATM 6722 C  C5X . MYA K 2 .   ? -23.395 60.072  -29.089 1.00 12.95 ? 2001 MYA B C5X 1 
HETATM 6723 O  O5X . MYA K 2 .   ? -22.104 59.439  -29.236 1.00 12.04 ? 2001 MYA B O5X 1 
HETATM 6724 C  C6A . MYA K 2 .   ? -24.239 57.414  -22.064 1.00 11.65 ? 2001 MYA B C6A 1 
HETATM 6725 N  N6A . MYA K 2 .   ? -23.713 57.787  -20.890 1.00 12.61 ? 2001 MYA B N6A 1 
HETATM 6726 O  O6A . MYA K 2 .   ? -19.408 60.085  -26.018 1.00 11.27 ? 2001 MYA B O6A 1 
HETATM 6727 C  C6M . MYA K 2 .   ? -23.912 52.426  -22.107 1.00 8.03  ? 2001 MYA B C6M 1 
HETATM 6728 N  N7A . MYA K 2 .   ? -23.827 59.489  -23.477 1.00 13.83 ? 2001 MYA B N7A 1 
HETATM 6729 O  O7A . MYA K 2 .   ? -28.643 60.128  -29.059 1.00 15.21 ? 2001 MYA B O7A 1 
HETATM 6730 C  C7M . MYA K 2 .   ? -25.055 51.629  -22.743 1.00 8.66  ? 2001 MYA B C7M 1 
HETATM 6731 C  C8A . MYA K 2 .   ? -24.121 59.727  -24.747 1.00 13.15 ? 2001 MYA B C8A 1 
HETATM 6732 O  O8A . MYA K 2 .   ? -27.624 59.553  -31.254 1.00 17.98 ? 2001 MYA B O8A 1 
HETATM 6733 C  C8M . MYA K 2 .   ? -24.993 50.130  -22.422 1.00 8.47  ? 2001 MYA B C8M 1 
HETATM 6734 N  N9A . MYA K 2 .   ? -24.768 58.672  -25.264 1.00 13.60 ? 2001 MYA B N9A 1 
HETATM 6735 O  O9A . MYA K 2 .   ? -28.896 57.801  -30.070 1.00 14.95 ? 2001 MYA B O9A 1 
HETATM 6736 C  C9M . MYA K 2 .   ? -26.143 49.340  -23.069 1.00 9.00  ? 2001 MYA B C9M 1 
HETATM 6737 C  CAM . MYA K 2 .   ? -26.027 47.808  -22.830 1.00 9.28  ? 2001 MYA B CAM 1 
HETATM 6738 C  CBM . MYA K 2 .   ? -24.826 47.135  -23.586 1.00 9.01  ? 2001 MYA B CBM 1 
HETATM 6739 C  CCM . MYA K 2 .   ? -24.723 45.661  -23.261 1.00 9.02  ? 2001 MYA B CCM 1 
HETATM 6740 C  CDM . MYA K 2 .   ? -25.939 44.809  -23.695 1.00 8.60  ? 2001 MYA B CDM 1 
HETATM 6741 C  CEM . MYA K 2 .   ? -25.653 43.256  -23.498 1.00 8.44  ? 2001 MYA B CEM 1 
HETATM 6742 C  CFM . MYA K 2 .   ? -26.908 42.413  -23.790 1.00 8.91  ? 2001 MYA B CFM 1 
HETATM 6743 P  P   . PO4 L 3 .   ? -30.188 43.991  -33.057 1.00 16.66 ? 2002 PO4 B P   1 
HETATM 6744 O  O1  . PO4 L 3 .   ? -30.377 42.778  -33.839 1.00 19.16 ? 2002 PO4 B O1  1 
HETATM 6745 O  O2  . PO4 L 3 .   ? -31.570 44.634  -32.820 1.00 23.14 ? 2002 PO4 B O2  1 
HETATM 6746 O  O3  . PO4 L 3 .   ? -29.269 45.014  -33.582 1.00 18.64 ? 2002 PO4 B O3  1 
HETATM 6747 O  O4  . PO4 L 3 .   ? -29.806 43.418  -31.655 1.00 23.05 ? 2002 PO4 B O4  1 
HETATM 6748 P  P   . PO4 M 3 .   ? -19.513 50.003  -37.393 1.00 16.82 ? 2003 PO4 B P   1 
HETATM 6749 O  O1  . PO4 M 3 .   ? -19.539 50.677  -38.856 1.00 20.26 ? 2003 PO4 B O1  1 
HETATM 6750 O  O2  . PO4 M 3 .   ? -20.906 49.944  -36.876 1.00 17.67 ? 2003 PO4 B O2  1 
HETATM 6751 O  O3  . PO4 M 3 .   ? -18.729 48.770  -37.525 1.00 16.60 ? 2003 PO4 B O3  1 
HETATM 6752 O  O4  . PO4 M 3 .   ? -18.814 50.942  -36.372 1.00 18.99 ? 2003 PO4 B O4  1 
HETATM 6753 P  P   . PO4 N 3 .   ? -24.302 55.451  -34.935 1.00 48.83 ? 2004 PO4 B P   1 
HETATM 6754 O  O1  . PO4 N 3 .   ? -24.999 56.041  -36.171 1.00 64.13 ? 2004 PO4 B O1  1 
HETATM 6755 O  O2  . PO4 N 3 .   ? -22.974 54.714  -35.198 1.00 48.54 ? 2004 PO4 B O2  1 
HETATM 6756 O  O3  . PO4 N 3 .   ? -25.196 54.381  -34.321 1.00 64.03 ? 2004 PO4 B O3  1 
HETATM 6757 O  O4  . PO4 N 3 .   ? -24.200 56.720  -34.059 1.00 52.19 ? 2004 PO4 B O4  1 
HETATM 6758 P  P   . PO4 O 3 .   ? 3.105   53.109  -10.412 1.00 55.54 ? 2005 PO4 B P   1 
HETATM 6759 O  O1  . PO4 O 3 .   ? 3.408   54.125  -11.532 1.00 61.38 ? 2005 PO4 B O1  1 
HETATM 6760 O  O2  . PO4 O 3 .   ? 4.278   53.194  -9.421  1.00 61.15 ? 2005 PO4 B O2  1 
HETATM 6761 O  O3  . PO4 O 3 .   ? 3.076   51.637  -10.876 1.00 42.96 ? 2005 PO4 B O3  1 
HETATM 6762 O  O4  . PO4 O 3 .   ? 1.852   53.518  -9.626  1.00 44.62 ? 2005 PO4 B O4  1 
HETATM 6763 P  P   . PO4 P 3 .   ? -12.329 39.095  -3.420  1.00 56.75 ? 2006 PO4 B P   1 
HETATM 6764 O  O1  . PO4 P 3 .   ? -12.840 39.015  -4.807  1.00 44.15 ? 2006 PO4 B O1  1 
HETATM 6765 O  O2  . PO4 P 3 .   ? -11.723 40.485  -3.198  1.00 56.43 ? 2006 PO4 B O2  1 
HETATM 6766 O  O3  . PO4 P 3 .   ? -11.248 38.028  -3.357  1.00 62.43 ? 2006 PO4 B O3  1 
HETATM 6767 O  O4  . PO4 P 3 .   ? -13.387 38.740  -2.351  1.00 58.65 ? 2006 PO4 B O4  1 
HETATM 6768 C  C12 . 9M2 Q 4 .   ? -24.595 58.847  -6.284  1.00 12.64 ? 2007 9M2 B C12 1 
HETATM 6769 C  C8  . 9M2 Q 4 .   ? -22.683 58.911  -10.143 1.00 14.45 ? 2007 9M2 B C8  1 
HETATM 6770 C  C9  . 9M2 Q 4 .   ? -22.513 58.891  -11.556 1.00 13.31 ? 2007 9M2 B C9  1 
HETATM 6771 C  C10 . 9M2 Q 4 .   ? -23.689 60.049  -8.207  1.00 12.54 ? 2007 9M2 B C10 1 
HETATM 6772 C  C11 . 9M2 Q 4 .   ? -24.254 58.870  -7.624  1.00 11.88 ? 2007 9M2 B C11 1 
HETATM 6773 C  C7  . 9M2 Q 4 .   ? -23.455 60.036  -9.656  1.00 13.05 ? 2007 9M2 B C7  1 
HETATM 6774 C  C6  . 9M2 Q 4 .   ? -23.997 61.063  -10.490 1.00 13.39 ? 2007 9M2 B C6  1 
HETATM 6775 N  N1  . 9M2 Q 4 .   ? -21.942 58.299  -13.660 1.00 13.64 ? 2007 9M2 B N1  1 
HETATM 6776 C  C5  . 9M2 Q 4 .   ? -23.785 60.955  -11.901 1.00 14.16 ? 2007 9M2 B C5  1 
HETATM 6777 C  C4  . 9M2 Q 4 .   ? -23.041 59.856  -12.453 1.00 13.03 ? 2007 9M2 B C4  1 
HETATM 6778 F  F   . 9M2 Q 4 .   ? -24.825 60.024  -4.255  1.00 13.17 ? 2007 9M2 B F   1 
HETATM 6779 C  C13 . 9M2 Q 4 .   ? -24.461 60.010  -5.583  1.00 11.76 ? 2007 9M2 B C13 1 
HETATM 6780 C  C14 . 9M2 Q 4 .   ? -23.936 61.220  -6.080  1.00 12.30 ? 2007 9M2 B C14 1 
HETATM 6781 C  C15 . 9M2 Q 4 .   ? -23.604 61.253  -7.431  1.00 12.57 ? 2007 9M2 B C15 1 
HETATM 6782 N  N2  . 9M2 Q 4 .   ? -22.700 59.437  -13.758 1.00 13.00 ? 2007 9M2 B N2  1 
HETATM 6783 C  C3  . 9M2 Q 4 .   ? -21.809 57.880  -12.404 1.00 12.62 ? 2007 9M2 B C3  1 
HETATM 6784 C  C2  . 9M2 Q 4 .   ? -20.921 56.700  -12.063 1.00 13.10 ? 2007 9M2 B C2  1 
HETATM 6785 N  N   . 9M2 Q 4 .   ? -21.668 55.412  -12.086 1.00 13.16 ? 2007 9M2 B N   1 
HETATM 6786 C  C1  . 9M2 Q 4 .   ? -22.877 55.430  -11.130 1.00 14.26 ? 2007 9M2 B C1  1 
HETATM 6787 C  C   . 9M2 Q 4 .   ? -22.144 54.989  -13.459 1.00 14.10 ? 2007 9M2 B C   1 
HETATM 6788 O  O   . 9M2 Q 4 .   ? -23.060 62.343  -8.040  1.00 13.75 ? 2007 9M2 B O   1 
HETATM 6789 C  C16 . 9M2 Q 4 .   ? -22.843 63.544  -7.171  1.00 14.56 ? 2007 9M2 B C16 1 
HETATM 6790 C  C17 . 9M2 Q 4 .   ? -22.293 64.660  -8.112  1.00 17.04 ? 2007 9M2 B C17 1 
HETATM 6791 C  C18 . 9M2 Q 4 .   ? -20.813 64.569  -8.364  1.00 16.97 ? 2007 9M2 B C18 1 
HETATM 6792 C  C22 . 9M2 Q 4 .   ? -19.549 64.919  -7.689  1.00 16.53 ? 2007 9M2 B C22 1 
HETATM 6793 C  C23 . 9M2 Q 4 .   ? -19.415 65.363  -6.261  1.00 18.98 ? 2007 9M2 B C23 1 
HETATM 6794 N  N4  . 9M2 Q 4 .   ? -18.394 64.625  -8.365  1.00 17.75 ? 2007 9M2 B N4  1 
HETATM 6795 N  N3  . 9M2 Q 4 .   ? -18.972 64.278  -9.572  1.00 13.23 ? 2007 9M2 B N3  1 
HETATM 6796 C  C21 . 9M2 Q 4 .   ? -17.973 63.917  -10.540 1.00 17.32 ? 2007 9M2 B C21 1 
HETATM 6797 C  C19 . 9M2 Q 4 .   ? -20.308 64.167  -9.660  1.00 12.69 ? 2007 9M2 B C19 1 
HETATM 6798 C  C20 . 9M2 Q 4 .   ? -20.998 63.563  -10.826 1.00 13.06 ? 2007 9M2 B C20 1 
HETATM 6799 MG MG  . MG  R 5 .   ? -17.042 60.361  -30.045 1.00 20.31 ? 2008 MG  B MG  1 
HETATM 6800 C  C1  . GOL S 6 .   ? -38.067 50.917  -18.905 1.00 17.55 ? 2009 GOL B C1  1 
HETATM 6801 O  O1  . GOL S 6 .   ? -39.155 50.672  -17.878 1.00 20.78 ? 2009 GOL B O1  1 
HETATM 6802 C  C2  . GOL S 6 .   ? -37.286 49.583  -18.983 1.00 16.35 ? 2009 GOL B C2  1 
HETATM 6803 O  O2  . GOL S 6 .   ? -38.034 48.612  -19.792 1.00 17.54 ? 2009 GOL B O2  1 
HETATM 6804 C  C3  . GOL S 6 .   ? -36.045 49.767  -19.840 1.00 18.55 ? 2009 GOL B C3  1 
HETATM 6805 O  O3  . GOL S 6 .   ? -35.033 50.635  -19.174 1.00 16.26 ? 2009 GOL B O3  1 
HETATM 6806 C  C1  . GOL T 6 .   ? -17.718 51.741  17.309  1.00 35.52 ? 2010 GOL B C1  1 
HETATM 6807 O  O1  . GOL T 6 .   ? -17.639 52.924  18.132  1.00 49.50 ? 2010 GOL B O1  1 
HETATM 6808 C  C2  . GOL T 6 .   ? -17.212 52.080  15.869  1.00 23.26 ? 2010 GOL B C2  1 
HETATM 6809 O  O2  . GOL T 6 .   ? -16.354 53.271  15.795  1.00 33.98 ? 2010 GOL B O2  1 
HETATM 6810 C  C3  . GOL T 6 .   ? -16.502 50.745  15.530  1.00 33.99 ? 2010 GOL B C3  1 
HETATM 6811 O  O3  . GOL T 6 .   ? -15.193 50.726  14.897  1.00 38.20 ? 2010 GOL B O3  1 
HETATM 6812 O  O   . HOH U 8 .   ? -2.191  15.161  -23.730 0.50 15.19 ? 2101 HOH A O   1 
HETATM 6813 O  O   . HOH U 8 .   ? -34.057 27.178  -22.295 0.50 30.61 ? 2102 HOH A O   1 
HETATM 6814 O  O   . HOH U 8 .   ? -29.408 25.590  -48.899 0.50 20.55 ? 2103 HOH A O   1 
HETATM 6815 O  O   . HOH U 8 .   ? -30.034 30.020  6.640   0.50 25.57 ? 2104 HOH A O   1 
HETATM 6816 O  O   . HOH U 8 .   ? -33.000 25.835  -4.955  0.50 15.34 ? 2105 HOH A O   1 
HETATM 6817 O  O   . HOH U 8 .   ? -20.916 6.575   -44.994 1.00 23.72 ? 2106 HOH A O   1 
HETATM 6818 O  O   . HOH U 8 .   ? -15.716 20.922  9.634   1.00 23.96 ? 2107 HOH A O   1 
HETATM 6819 O  O   . HOH U 8 .   ? -30.684 32.401  -4.763  1.00 33.69 ? 2108 HOH A O   1 
HETATM 6820 O  O   . HOH U 8 .   ? -32.099 25.064  -2.820  1.00 27.67 ? 2109 HOH A O   1 
HETATM 6821 O  O   . HOH U 8 .   ? -39.192 14.600  -28.747 1.00 35.15 ? 2110 HOH A O   1 
HETATM 6822 O  O   . HOH U 8 .   ? -33.026 8.214   -0.391  1.00 39.30 ? 2111 HOH A O   1 
HETATM 6823 O  O   . HOH U 8 .   ? -32.313 33.163  -0.881  1.00 42.15 ? 2112 HOH A O   1 
HETATM 6824 O  O   . HOH U 8 .   ? -16.011 25.978  -46.765 1.00 27.56 ? 2113 HOH A O   1 
HETATM 6825 O  O   . HOH U 8 .   ? -18.364 -5.294  -19.652 1.00 32.86 ? 2114 HOH A O   1 
HETATM 6826 O  O   . HOH U 8 .   ? -29.478 13.298  -34.212 1.00 28.99 ? 2115 HOH A O   1 
HETATM 6827 O  O   . HOH U 8 .   ? -16.166 18.395  9.891   1.00 25.63 ? 2116 HOH A O   1 
HETATM 6828 O  O   . HOH U 8 .   ? -25.030 -21.562 -32.758 1.00 30.29 ? 2117 HOH A O   1 
HETATM 6829 O  O   . HOH U 8 .   ? -35.125 29.593  -14.108 1.00 32.33 ? 2118 HOH A O   1 
HETATM 6830 O  O   . HOH U 8 .   ? -17.670 10.028  5.598   1.00 31.79 ? 2119 HOH A O   1 
HETATM 6831 O  O   . HOH U 8 .   ? -14.758 34.782  -29.922 1.00 31.27 ? 2120 HOH A O   1 
HETATM 6832 O  O   . HOH U 8 .   ? -2.632  14.934  -29.730 1.00 29.95 ? 2121 HOH A O   1 
HETATM 6833 O  O   . HOH U 8 .   ? -26.011 1.855   -5.745  1.00 30.53 ? 2122 HOH A O   1 
HETATM 6834 O  O   . HOH U 8 .   ? -23.226 20.567  -21.180 1.00 15.88 ? 2123 HOH A O   1 
HETATM 6835 O  O   . HOH U 8 .   ? -6.735  8.241   8.134   1.00 32.20 ? 2124 HOH A O   1 
HETATM 6836 O  O   . HOH U 8 .   ? -38.233 4.935   -23.533 1.00 34.37 ? 2125 HOH A O   1 
HETATM 6837 O  O   . HOH U 8 .   ? -40.343 22.807  -5.220  1.00 38.82 ? 2126 HOH A O   1 
HETATM 6838 O  O   . HOH U 8 .   ? -31.412 23.354  -42.667 1.00 34.00 ? 2127 HOH A O   1 
HETATM 6839 O  O   . HOH U 8 .   ? -12.302 28.133  -45.281 1.00 36.13 ? 2128 HOH A O   1 
HETATM 6840 O  O   . HOH U 8 .   ? 3.664   26.070  -13.473 1.00 32.77 ? 2129 HOH A O   1 
HETATM 6841 O  O   . HOH U 8 .   ? -18.667 2.368   1.625   1.00 29.03 ? 2130 HOH A O   1 
HETATM 6842 O  O   . HOH U 8 .   ? -10.108 -6.361  -37.697 1.00 27.05 ? 2131 HOH A O   1 
HETATM 6843 O  O   . HOH U 8 .   ? 5.654   23.301  -12.278 1.00 29.37 ? 2132 HOH A O   1 
HETATM 6844 O  O   . HOH U 8 .   ? -28.366 26.035  -42.020 1.00 29.78 ? 2133 HOH A O   1 
HETATM 6845 O  O   . HOH U 8 .   ? -1.569  13.010  -24.897 1.00 27.63 ? 2134 HOH A O   1 
HETATM 6846 O  O   . HOH U 8 .   ? -14.526 29.212  -26.496 1.00 25.42 ? 2135 HOH A O   1 
HETATM 6847 O  O   . HOH U 8 .   ? 0.534   14.866  -22.870 1.00 41.29 ? 2136 HOH A O   1 
HETATM 6848 O  O   . HOH U 8 .   ? -14.319 29.974  9.901   1.00 40.26 ? 2137 HOH A O   1 
HETATM 6849 O  O   . HOH U 8 .   ? -15.893 10.880  -16.588 1.00 10.23 ? 2138 HOH A O   1 
HETATM 6850 O  O   . HOH U 8 .   ? -25.587 -1.476  -22.197 1.00 21.58 ? 2139 HOH A O   1 
HETATM 6851 O  O   . HOH U 8 .   ? -37.927 14.941  -34.151 1.00 37.07 ? 2140 HOH A O   1 
HETATM 6852 O  O   . HOH U 8 .   ? -33.257 22.781  -25.216 1.00 19.82 ? 2141 HOH A O   1 
HETATM 6853 O  O   . HOH U 8 .   ? -6.679  7.747   -28.331 1.00 32.20 ? 2142 HOH A O   1 
HETATM 6854 O  O   . HOH U 8 .   ? -11.010 25.126  -29.194 1.00 17.65 ? 2143 HOH A O   1 
HETATM 6855 O  O   . HOH U 8 .   ? -35.438 19.818  -41.820 1.00 33.10 ? 2144 HOH A O   1 
HETATM 6856 O  O   . HOH U 8 .   ? -38.801 10.796  -10.989 1.00 30.24 ? 2145 HOH A O   1 
HETATM 6857 O  O   . HOH U 8 .   ? -22.564 18.446  -23.174 1.00 16.16 ? 2146 HOH A O   1 
HETATM 6858 O  O   . HOH U 8 .   ? -19.992 34.202  -7.204  1.00 15.60 ? 2147 HOH A O   1 
HETATM 6859 O  O   . HOH U 8 .   ? -12.912 3.952   -23.906 1.00 14.35 ? 2148 HOH A O   1 
HETATM 6860 O  O   . HOH U 8 .   ? -31.806 0.537   -32.806 1.00 24.98 ? 2149 HOH A O   1 
HETATM 6861 O  O   . HOH U 8 .   ? -37.551 13.622  -30.615 1.00 26.76 ? 2150 HOH A O   1 
HETATM 6862 O  O   . HOH U 8 .   ? -28.855 26.390  -9.521  1.00 22.93 ? 2151 HOH A O   1 
HETATM 6863 O  O   . HOH U 8 .   ? -18.129 12.820  -48.649 1.00 31.16 ? 2152 HOH A O   1 
HETATM 6864 O  O   . HOH U 8 .   ? -21.073 -23.351 -34.119 1.00 17.28 ? 2153 HOH A O   1 
HETATM 6865 O  O   . HOH U 8 .   ? -27.149 1.102   -13.240 1.00 36.95 ? 2154 HOH A O   1 
HETATM 6866 O  O   . HOH U 8 .   ? -31.258 0.564   -25.595 1.00 16.59 ? 2155 HOH A O   1 
HETATM 6867 O  O   . HOH U 8 .   ? -26.508 20.589  0.140   1.00 15.17 ? 2156 HOH A O   1 
HETATM 6868 O  O   . HOH U 8 .   ? -4.843  18.030  -29.757 1.00 21.94 ? 2157 HOH A O   1 
HETATM 6869 O  O   . HOH U 8 .   ? -17.438 8.879   -21.702 1.00 17.27 ? 2158 HOH A O   1 
HETATM 6870 O  O   . HOH U 8 .   ? -25.663 -1.210  -41.633 1.00 31.35 ? 2159 HOH A O   1 
HETATM 6871 O  O   . HOH U 8 .   ? -0.465  27.606  -14.054 1.00 30.23 ? 2160 HOH A O   1 
HETATM 6872 O  O   . HOH U 8 .   ? -5.180  3.392   -23.035 1.00 16.82 ? 2161 HOH A O   1 
HETATM 6873 O  O   . HOH U 8 .   ? -13.684 24.913  -46.255 1.00 21.19 ? 2162 HOH A O   1 
HETATM 6874 O  O   . HOH U 8 .   ? -24.712 10.308  6.332   1.00 34.79 ? 2163 HOH A O   1 
HETATM 6875 O  O   . HOH U 8 .   ? 3.220   18.313  -9.418  1.00 16.82 ? 2164 HOH A O   1 
HETATM 6876 O  O   . HOH U 8 .   ? -17.972 6.262   -50.092 1.00 35.59 ? 2165 HOH A O   1 
HETATM 6877 O  O   . HOH U 8 .   ? -19.801 31.267  -22.638 1.00 13.57 ? 2166 HOH A O   1 
HETATM 6878 O  O   . HOH U 8 .   ? -27.408 19.596  -47.276 1.00 22.22 ? 2167 HOH A O   1 
HETATM 6879 O  O   . HOH U 8 .   ? -27.814 10.741  -6.389  1.00 16.40 ? 2168 HOH A O   1 
HETATM 6880 O  O   . HOH U 8 .   ? -18.293 30.476  -13.730 1.00 16.92 ? 2169 HOH A O   1 
HETATM 6881 O  O   . HOH U 8 .   ? -12.644 -13.283 -27.597 1.00 31.67 ? 2170 HOH A O   1 
HETATM 6882 O  O   . HOH U 8 .   ? -32.402 2.955   -21.820 1.00 17.20 ? 2171 HOH A O   1 
HETATM 6883 O  O   . HOH U 8 .   ? -6.597  3.618   -17.682 1.00 12.41 ? 2172 HOH A O   1 
HETATM 6884 O  O   . HOH U 8 .   ? -6.737  -8.463  -15.715 1.00 41.97 ? 2173 HOH A O   1 
HETATM 6885 O  O   . HOH U 8 .   ? -25.601 18.121  2.854   1.00 17.71 ? 2174 HOH A O   1 
HETATM 6886 O  O   . HOH U 8 .   ? -4.224  0.707   -10.561 1.00 18.06 ? 2175 HOH A O   1 
HETATM 6887 O  O   . HOH U 8 .   ? -16.017 -7.170  -32.874 1.00 20.84 ? 2176 HOH A O   1 
HETATM 6888 O  O   . HOH U 8 .   ? -34.008 18.536  -37.331 1.00 19.89 ? 2177 HOH A O   1 
HETATM 6889 O  O   . HOH U 8 .   ? -12.748 21.957  -43.254 1.00 12.62 ? 2178 HOH A O   1 
HETATM 6890 O  O   . HOH U 8 .   ? -35.258 6.468   -18.607 1.00 23.06 ? 2179 HOH A O   1 
HETATM 6891 O  O   . HOH U 8 .   ? -14.268 27.892  -2.136  1.00 24.95 ? 2180 HOH A O   1 
HETATM 6892 O  O   . HOH U 8 .   ? -24.261 -7.172  -27.691 1.00 30.28 ? 2181 HOH A O   1 
HETATM 6893 O  O   . HOH U 8 .   ? -10.820 22.667  -38.143 1.00 14.52 ? 2182 HOH A O   1 
HETATM 6894 O  O   . HOH U 8 .   ? -12.517 12.666  -31.536 1.00 12.29 ? 2183 HOH A O   1 
HETATM 6895 O  O   . HOH U 8 .   ? -12.391 22.852  8.121   1.00 19.61 ? 2184 HOH A O   1 
HETATM 6896 O  O   . HOH U 8 .   ? -1.129  20.966  -6.587  1.00 12.81 ? 2185 HOH A O   1 
HETATM 6897 O  O   . HOH U 8 .   ? -22.639 1.040   -16.308 1.00 26.07 ? 2186 HOH A O   1 
HETATM 6898 O  O   . HOH U 8 .   ? -11.430 12.858  14.804  1.00 35.80 ? 2187 HOH A O   1 
HETATM 6899 O  O   . HOH U 8 .   ? -31.512 21.843  5.284   1.00 34.01 ? 2188 HOH A O   1 
HETATM 6900 O  O   . HOH U 8 .   ? -5.961  -0.108  -33.783 1.00 39.00 ? 2189 HOH A O   1 
HETATM 6901 O  O   . HOH U 8 .   ? -27.497 -5.621  -32.371 1.00 40.86 ? 2190 HOH A O   1 
HETATM 6902 O  O   . HOH U 8 .   ? -2.654  -5.748  -11.766 1.00 25.71 ? 2191 HOH A O   1 
HETATM 6903 O  O   . HOH U 8 .   ? -38.629 20.125  -22.606 1.00 26.50 ? 2192 HOH A O   1 
HETATM 6904 O  O   . HOH U 8 .   ? -34.884 6.288   -15.379 1.00 29.11 ? 2193 HOH A O   1 
HETATM 6905 O  O   . HOH U 8 .   ? 2.853   10.184  -13.392 1.00 21.87 ? 2194 HOH A O   1 
HETATM 6906 O  O   . HOH U 8 .   ? -12.393 22.732  -29.099 1.00 10.70 ? 2195 HOH A O   1 
HETATM 6907 O  O   . HOH U 8 .   ? -20.418 -2.947  -42.134 1.00 18.36 ? 2196 HOH A O   1 
HETATM 6908 O  O   . HOH U 8 .   ? -7.418  24.943  -9.347  1.00 14.41 ? 2197 HOH A O   1 
HETATM 6909 O  O   . HOH U 8 .   ? -17.102 -19.296 -35.443 1.00 32.09 ? 2198 HOH A O   1 
HETATM 6910 O  O   . HOH U 8 .   ? -15.740 0.599   -3.106  1.00 20.71 ? 2199 HOH A O   1 
HETATM 6911 O  O   . HOH U 8 .   ? -19.359 -11.286 -17.506 1.00 38.22 ? 2200 HOH A O   1 
HETATM 6912 O  O   . HOH U 8 .   ? -28.343 22.653  -3.316  1.00 12.26 ? 2201 HOH A O   1 
HETATM 6913 O  O   . HOH U 8 .   ? -28.092 -5.236  -36.243 1.00 38.92 ? 2202 HOH A O   1 
HETATM 6914 O  O   . HOH U 8 .   ? -17.104 2.696   -11.664 1.00 23.19 ? 2203 HOH A O   1 
HETATM 6915 O  O   . HOH U 8 .   ? -23.687 29.704  -20.838 1.00 27.52 ? 2204 HOH A O   1 
HETATM 6916 O  O   . HOH U 8 .   ? -22.506 30.111  -50.790 1.00 26.23 ? 2205 HOH A O   1 
HETATM 6917 O  O   . HOH U 8 .   ? 1.542   7.988   -0.133  1.00 25.32 ? 2206 HOH A O   1 
HETATM 6918 O  O   . HOH U 8 .   ? -33.193 13.982  2.120   1.00 28.98 ? 2207 HOH A O   1 
HETATM 6919 O  O   . HOH U 8 .   ? -39.412 19.329  -1.357  1.00 30.97 ? 2208 HOH A O   1 
HETATM 6920 O  O   . HOH U 8 .   ? 1.617   -3.409  -27.368 1.00 39.74 ? 2209 HOH A O   1 
HETATM 6921 O  O   . HOH U 8 .   ? -14.294 -15.157 -29.264 1.00 35.02 ? 2210 HOH A O   1 
HETATM 6922 O  O   . HOH U 8 .   ? 3.324   15.004  -5.834  1.00 20.41 ? 2211 HOH A O   1 
HETATM 6923 O  O   . HOH U 8 .   ? -9.455  30.456  -37.182 1.00 33.96 ? 2212 HOH A O   1 
HETATM 6924 O  O   . HOH U 8 .   ? 0.472   12.319  -7.200  1.00 13.43 ? 2213 HOH A O   1 
HETATM 6925 O  O   . HOH U 8 .   ? -23.768 -22.140 -37.096 1.00 17.99 ? 2214 HOH A O   1 
HETATM 6926 O  O   . HOH U 8 .   ? -29.207 26.941  -39.538 1.00 37.92 ? 2215 HOH A O   1 
HETATM 6927 O  O   . HOH U 8 .   ? -32.201 24.527  -27.247 1.00 20.00 ? 2216 HOH A O   1 
HETATM 6928 O  O   . HOH U 8 .   ? -18.611 25.139  -18.750 1.00 16.96 ? 2217 HOH A O   1 
HETATM 6929 O  O   . HOH U 8 .   ? -22.598 19.780  7.138   1.00 21.11 ? 2218 HOH A O   1 
HETATM 6930 O  O   . HOH U 8 .   ? -13.868 -1.208  -42.686 1.00 25.83 ? 2219 HOH A O   1 
HETATM 6931 O  O   . HOH U 8 .   ? -21.809 8.753   -26.154 1.00 30.15 ? 2220 HOH A O   1 
HETATM 6932 O  O   . HOH U 8 .   ? -33.255 7.069   -28.865 1.00 15.62 ? 2221 HOH A O   1 
HETATM 6933 O  O   . HOH U 8 .   ? -20.834 -1.551  -24.978 1.00 19.47 ? 2222 HOH A O   1 
HETATM 6934 O  O   . HOH U 8 .   ? -26.555 11.435  -31.227 1.00 12.82 ? 2223 HOH A O   1 
HETATM 6935 O  O   . HOH U 8 .   ? 3.964   20.935  -10.233 1.00 15.60 ? 2224 HOH A O   1 
HETATM 6936 O  O   . HOH U 8 .   ? -29.771 23.967  -1.351  1.00 18.07 ? 2225 HOH A O   1 
HETATM 6937 O  O   . HOH U 8 .   ? 3.672   15.028  -12.419 1.00 18.54 ? 2226 HOH A O   1 
HETATM 6938 O  O   . HOH U 8 .   ? -12.656 28.793  5.284   1.00 39.28 ? 2227 HOH A O   1 
HETATM 6939 O  O   . HOH U 8 .   ? -24.335 -19.194 -39.690 1.00 18.29 ? 2228 HOH A O   1 
HETATM 6940 O  O   . HOH U 8 .   ? -5.487  13.664  -26.650 1.00 17.80 ? 2229 HOH A O   1 
HETATM 6941 O  O   . HOH U 8 .   ? -29.714 24.331  -26.363 1.00 21.72 ? 2230 HOH A O   1 
HETATM 6942 O  O   . HOH U 8 .   ? -20.219 28.340  -19.165 1.00 27.53 ? 2231 HOH A O   1 
HETATM 6943 O  O   . HOH U 8 .   ? -20.117 24.541  -21.060 1.00 16.81 ? 2232 HOH A O   1 
HETATM 6944 O  O   . HOH U 8 .   ? -21.120 9.795   -22.029 1.00 32.15 ? 2233 HOH A O   1 
HETATM 6945 O  O   . HOH U 8 .   ? -28.452 32.231  -6.337  1.00 26.85 ? 2234 HOH A O   1 
HETATM 6946 O  O   . HOH U 8 .   ? -9.973  16.454  -34.389 1.00 12.44 ? 2235 HOH A O   1 
HETATM 6947 O  O   . HOH U 8 .   ? -32.509 15.324  -41.675 1.00 20.70 ? 2236 HOH A O   1 
HETATM 6948 O  O   . HOH U 8 .   ? -28.499 16.969  4.950   1.00 25.66 ? 2237 HOH A O   1 
HETATM 6949 O  O   . HOH U 8 .   ? -2.610  3.047   -19.859 1.00 16.31 ? 2238 HOH A O   1 
HETATM 6950 O  O   . HOH U 8 .   ? -14.214 -1.331  -47.664 1.00 36.04 ? 2239 HOH A O   1 
HETATM 6951 O  O   . HOH U 8 .   ? -20.153 28.119  -43.029 1.00 13.59 ? 2240 HOH A O   1 
HETATM 6952 O  O   . HOH U 8 .   ? -39.249 11.530  -28.672 1.00 35.96 ? 2241 HOH A O   1 
HETATM 6953 O  O   . HOH U 8 .   ? -26.695 20.016  6.297   1.00 18.50 ? 2242 HOH A O   1 
HETATM 6954 O  O   . HOH U 8 .   ? -23.680 31.933  -11.564 1.00 27.20 ? 2243 HOH A O   1 
HETATM 6955 O  O   . HOH U 8 .   ? -19.244 32.861  -40.328 1.00 30.31 ? 2244 HOH A O   1 
HETATM 6956 O  O   . HOH U 8 .   ? -18.839 0.125   -15.389 1.00 24.94 ? 2245 HOH A O   1 
HETATM 6957 O  O   . HOH U 8 .   ? 1.116   9.268   5.576   1.00 35.49 ? 2246 HOH A O   1 
HETATM 6958 O  O   . HOH U 8 .   ? -12.430 18.534  12.072  1.00 25.83 ? 2247 HOH A O   1 
HETATM 6959 O  O   . HOH U 8 .   ? -12.906 30.629  -16.464 1.00 22.43 ? 2248 HOH A O   1 
HETATM 6960 O  O   . HOH U 8 .   ? -30.210 5.979   5.713   1.00 26.79 ? 2249 HOH A O   1 
HETATM 6961 O  O   . HOH U 8 .   ? -34.569 11.132  -37.358 1.00 30.76 ? 2250 HOH A O   1 
HETATM 6962 O  O   . HOH U 8 .   ? -8.884  13.184  -33.915 1.00 17.03 ? 2251 HOH A O   1 
HETATM 6963 O  O   . HOH U 8 .   ? -12.158 31.836  -8.379  1.00 32.37 ? 2252 HOH A O   1 
HETATM 6964 O  O   . HOH U 8 .   ? -36.211 6.761   -12.401 1.00 29.39 ? 2253 HOH A O   1 
HETATM 6965 O  O   . HOH U 8 .   ? -19.558 -2.232  -18.566 1.00 22.16 ? 2254 HOH A O   1 
HETATM 6966 O  O   . HOH U 8 .   ? -18.573 -12.752 -34.771 1.00 27.47 ? 2255 HOH A O   1 
HETATM 6967 O  O   . HOH U 8 .   ? -44.542 15.030  -6.796  1.00 45.97 ? 2256 HOH A O   1 
HETATM 6968 O  O   . HOH U 8 .   ? -5.712  22.274  2.360   1.00 27.37 ? 2257 HOH A O   1 
HETATM 6969 O  O   . HOH U 8 .   ? -7.807  23.114  -32.408 1.00 16.27 ? 2258 HOH A O   1 
HETATM 6970 O  O   . HOH U 8 .   ? -17.223 31.571  -30.284 1.00 16.92 ? 2259 HOH A O   1 
HETATM 6971 O  O   . HOH U 8 .   ? -4.045  2.114   -8.083  1.00 17.79 ? 2260 HOH A O   1 
HETATM 6972 O  O   . HOH U 8 .   ? -37.106 10.402  -33.692 1.00 22.46 ? 2261 HOH A O   1 
HETATM 6973 O  O   . HOH U 8 .   ? -12.503 27.804  -21.831 1.00 28.08 ? 2262 HOH A O   1 
HETATM 6974 O  O   . HOH U 8 .   ? -33.533 26.513  -6.430  0.50 16.65 ? 2263 HOH A O   1 
HETATM 6975 O  O   . HOH U 8 .   ? -1.748  9.018   -7.705  1.00 17.25 ? 2264 HOH A O   1 
HETATM 6976 O  O   . HOH U 8 .   ? -30.005 11.329  -32.223 1.00 16.48 ? 2265 HOH A O   1 
HETATM 6977 O  O   . HOH U 8 .   ? 1.004   6.227   -9.066  1.00 26.55 ? 2266 HOH A O   1 
HETATM 6978 O  O   . HOH U 8 .   ? -36.478 23.967  -33.106 1.00 32.43 ? 2267 HOH A O   1 
HETATM 6979 O  O   . HOH U 8 .   ? -28.006 29.109  -26.766 1.00 28.85 ? 2268 HOH A O   1 
HETATM 6980 O  O   . HOH U 8 .   ? -33.058 16.098  -7.240  1.00 14.10 ? 2269 HOH A O   1 
HETATM 6981 O  O   . HOH U 8 .   ? -34.946 2.869   -22.863 1.00 25.43 ? 2270 HOH A O   1 
HETATM 6982 O  O   . HOH U 8 .   ? -27.217 31.822  -16.504 1.00 21.73 ? 2271 HOH A O   1 
HETATM 6983 O  O   . HOH U 8 .   ? -24.735 14.005  4.863   1.00 25.92 ? 2272 HOH A O   1 
HETATM 6984 O  O   . HOH U 8 .   ? -36.271 11.477  -29.468 1.00 18.69 ? 2273 HOH A O   1 
HETATM 6985 O  O   . HOH U 8 .   ? -23.375 2.857   -4.961  1.00 31.34 ? 2274 HOH A O   1 
HETATM 6986 O  O   . HOH U 8 .   ? -23.289 11.226  -21.017 1.00 16.50 ? 2275 HOH A O   1 
HETATM 6987 O  O   . HOH U 8 .   ? -40.365 10.226  -21.697 1.00 29.85 ? 2276 HOH A O   1 
HETATM 6988 O  O   . HOH U 8 .   ? -3.203  1.905   -15.730 1.00 21.66 ? 2277 HOH A O   1 
HETATM 6989 O  O   . HOH U 8 .   ? -36.267 14.459  -1.105  1.00 35.59 ? 2278 HOH A O   1 
HETATM 6990 O  O   . HOH U 8 .   ? -10.281 -3.916  -10.741 1.00 24.57 ? 2279 HOH A O   1 
HETATM 6991 O  O   . HOH U 8 .   ? -22.985 2.003   -42.704 1.00 32.63 ? 2280 HOH A O   1 
HETATM 6992 O  O   . HOH U 8 .   ? -14.238 24.457  -12.941 1.00 9.94  ? 2281 HOH A O   1 
HETATM 6993 O  O   . HOH U 8 .   ? -7.488  15.597  7.542   1.00 35.43 ? 2282 HOH A O   1 
HETATM 6994 O  O   . HOH U 8 .   ? -10.823 27.033  -38.668 1.00 14.89 ? 2283 HOH A O   1 
HETATM 6995 O  O   . HOH U 8 .   ? -5.536  20.579  -28.939 1.00 20.12 ? 2284 HOH A O   1 
HETATM 6996 O  O   . HOH U 8 .   ? -18.433 28.735  11.617  1.00 27.05 ? 2285 HOH A O   1 
HETATM 6997 O  O   . HOH U 8 .   ? -23.597 17.431  -0.606  1.00 11.62 ? 2286 HOH A O   1 
HETATM 6998 O  O   . HOH U 8 .   ? -8.130  -6.840  -19.716 1.00 16.28 ? 2287 HOH A O   1 
HETATM 6999 O  O   . HOH U 8 .   ? -27.698 13.939  -31.384 1.00 13.86 ? 2288 HOH A O   1 
HETATM 7000 O  O   . HOH U 8 .   ? 4.653   10.888  -15.282 1.00 27.64 ? 2289 HOH A O   1 
HETATM 7001 O  O   . HOH U 8 .   ? -8.676  10.755  -32.472 1.00 24.89 ? 2290 HOH A O   1 
HETATM 7002 O  O   . HOH U 8 .   ? -30.142 29.369  -17.012 1.00 31.49 ? 2291 HOH A O   1 
HETATM 7003 O  O   . HOH U 8 .   ? -21.686 30.073  -39.539 1.00 13.32 ? 2292 HOH A O   1 
HETATM 7004 O  O   . HOH U 8 .   ? -8.622  17.865  -36.189 1.00 14.47 ? 2293 HOH A O   1 
HETATM 7005 O  O   . HOH U 8 .   ? -19.965 18.374  -20.511 1.00 27.22 ? 2294 HOH A O   1 
HETATM 7006 O  O   . HOH U 8 .   ? -2.494  -3.268  -16.470 1.00 27.04 ? 2295 HOH A O   1 
HETATM 7007 O  O   . HOH U 8 .   ? -24.805 10.921  -29.112 1.00 11.32 ? 2296 HOH A O   1 
HETATM 7008 O  O   . HOH U 8 .   ? -5.100  -10.579 -20.647 1.00 35.76 ? 2297 HOH A O   1 
HETATM 7009 O  O   . HOH U 8 .   ? -26.013 11.054  -47.271 1.00 22.10 ? 2298 HOH A O   1 
HETATM 7010 O  O   . HOH U 8 .   ? -35.045 29.042  -3.349  1.00 40.71 ? 2299 HOH A O   1 
HETATM 7011 O  O   . HOH U 8 .   ? -20.956 10.957  -34.117 1.00 12.02 ? 2300 HOH A O   1 
HETATM 7012 O  O   . HOH U 8 .   ? 3.780   -5.779  -25.259 1.00 36.24 ? 2301 HOH A O   1 
HETATM 7013 O  O   . HOH U 8 .   ? -0.676  4.251   -6.768  1.00 31.88 ? 2302 HOH A O   1 
HETATM 7014 O  O   . HOH U 8 .   ? -6.262  9.534   -17.236 1.00 11.83 ? 2303 HOH A O   1 
HETATM 7015 O  O   . HOH U 8 .   ? -35.433 21.412  -24.639 1.00 33.45 ? 2304 HOH A O   1 
HETATM 7016 O  O   . HOH U 8 .   ? -27.791 26.131  -27.159 1.00 26.66 ? 2305 HOH A O   1 
HETATM 7017 O  O   . HOH U 8 .   ? -0.700  10.957  -9.369  1.00 13.70 ? 2306 HOH A O   1 
HETATM 7018 O  O   . HOH U 8 .   ? -7.236  24.338  -13.208 1.00 13.77 ? 2307 HOH A O   1 
HETATM 7019 O  O   . HOH U 8 .   ? -23.231 24.151  1.700   1.00 12.23 ? 2308 HOH A O   1 
HETATM 7020 O  O   . HOH U 8 .   ? -20.436 1.139   -25.545 1.00 14.58 ? 2309 HOH A O   1 
HETATM 7021 O  O   . HOH U 8 .   ? -8.570  8.108   -17.139 1.00 9.89  ? 2310 HOH A O   1 
HETATM 7022 O  O   . HOH U 8 .   ? -26.508 5.012   -44.178 1.00 34.59 ? 2311 HOH A O   1 
HETATM 7023 O  O   . HOH U 8 .   ? -2.330  -2.220  -20.567 1.00 25.41 ? 2312 HOH A O   1 
HETATM 7024 O  O   . HOH U 8 .   ? -38.155 22.920  -25.495 1.00 33.28 ? 2313 HOH A O   1 
HETATM 7025 O  O   . HOH U 8 .   ? -14.676 -1.784  -40.170 1.00 24.11 ? 2314 HOH A O   1 
HETATM 7026 O  O   . HOH U 8 .   ? -3.643  20.555  -26.880 1.00 42.32 ? 2315 HOH A O   1 
HETATM 7027 O  O   . HOH U 8 .   ? -4.562  8.938   -23.090 1.00 13.95 ? 2316 HOH A O   1 
HETATM 7028 O  O   . HOH U 8 .   ? -19.953 4.675   -13.015 1.00 25.11 ? 2317 HOH A O   1 
HETATM 7029 O  O   . HOH U 8 .   ? -13.194 -18.297 -37.917 1.00 27.29 ? 2318 HOH A O   1 
HETATM 7030 O  O   . HOH U 8 .   ? -28.927 8.327   6.423   1.00 25.98 ? 2319 HOH A O   1 
HETATM 7031 O  O   . HOH U 8 .   ? -19.243 4.999   -10.035 1.00 17.61 ? 2320 HOH A O   1 
HETATM 7032 O  O   . HOH U 8 .   ? -24.117 25.738  -20.821 1.00 15.76 ? 2321 HOH A O   1 
HETATM 7033 O  O   . HOH U 8 .   ? -25.130 16.581  -49.054 1.00 22.79 ? 2322 HOH A O   1 
HETATM 7034 O  O   . HOH U 8 .   ? -12.841 17.017  -36.922 1.00 11.21 ? 2323 HOH A O   1 
HETATM 7035 O  O   . HOH U 8 .   ? -24.118 31.856  -2.143  1.00 12.74 ? 2324 HOH A O   1 
HETATM 7036 O  O   . HOH U 8 .   ? -16.956 18.689  -14.053 1.00 11.01 ? 2325 HOH A O   1 
HETATM 7037 O  O   . HOH U 8 .   ? -9.238  22.469  -35.849 1.00 13.98 ? 2326 HOH A O   1 
HETATM 7038 O  O   . HOH U 8 .   ? -36.179 20.468  -32.021 1.00 20.07 ? 2327 HOH A O   1 
HETATM 7039 O  O   . HOH U 8 .   ? 0.050   4.700   -15.139 1.00 38.21 ? 2328 HOH A O   1 
HETATM 7040 O  O   . HOH U 8 .   ? -2.570  6.461   -8.567  1.00 15.46 ? 2329 HOH A O   1 
HETATM 7041 O  O   . HOH U 8 .   ? -8.183  -8.438  -22.115 1.00 22.56 ? 2330 HOH A O   1 
HETATM 7042 O  O   . HOH U 8 .   ? -9.490  1.766   -37.641 1.00 27.00 ? 2331 HOH A O   1 
HETATM 7043 O  O   . HOH U 8 .   ? -12.036 29.178  -33.762 1.00 33.87 ? 2332 HOH A O   1 
HETATM 7044 O  O   . HOH U 8 .   ? -10.988 1.721   -10.564 1.00 17.87 ? 2333 HOH A O   1 
HETATM 7045 O  O   . HOH U 8 .   ? -32.301 8.540   -40.441 1.00 23.72 ? 2334 HOH A O   1 
HETATM 7046 O  O   . HOH U 8 .   ? -27.008 15.680  -47.672 1.00 26.24 ? 2335 HOH A O   1 
HETATM 7047 O  O   . HOH U 8 .   ? -1.257  22.260  -18.456 1.00 22.37 ? 2336 HOH A O   1 
HETATM 7048 O  O   . HOH U 8 .   ? -28.443 29.126  -10.685 1.00 23.54 ? 2337 HOH A O   1 
HETATM 7049 O  O   . HOH U 8 .   ? -19.602 29.087  8.321   1.00 19.47 ? 2338 HOH A O   1 
HETATM 7050 O  O   . HOH U 8 .   ? -16.175 28.254  -4.153  1.00 18.37 ? 2339 HOH A O   1 
HETATM 7051 O  O   . HOH U 8 .   ? -5.361  -9.378  -18.699 1.00 37.54 ? 2340 HOH A O   1 
HETATM 7052 O  O   . HOH U 8 .   ? -7.335  20.700  -24.831 1.00 15.43 ? 2341 HOH A O   1 
HETATM 7053 O  O   . HOH U 8 .   ? -12.287 11.422  10.845  1.00 35.62 ? 2342 HOH A O   1 
HETATM 7054 O  O   . HOH U 8 .   ? -23.204 -0.220  -41.034 1.00 24.43 ? 2343 HOH A O   1 
HETATM 7055 O  O   . HOH U 8 .   ? -42.437 10.107  -15.691 1.00 34.61 ? 2344 HOH A O   1 
HETATM 7056 O  O   . HOH U 8 .   ? 3.969   12.753  -4.297  1.00 24.01 ? 2345 HOH A O   1 
HETATM 7057 O  O   . HOH U 8 .   ? -0.229  -7.056  -15.405 1.00 21.92 ? 2346 HOH A O   1 
HETATM 7058 O  O   . HOH U 8 .   ? -21.129 12.728  -14.440 1.00 10.98 ? 2347 HOH A O   1 
HETATM 7059 O  O   . HOH U 8 .   ? -24.258 8.793   -27.226 1.00 13.61 ? 2348 HOH A O   1 
HETATM 7060 O  O   . HOH U 8 .   ? -26.086 29.637  -22.223 1.00 25.62 ? 2349 HOH A O   1 
HETATM 7061 O  O   . HOH U 8 .   ? -28.160 22.816  6.491   1.00 22.38 ? 2350 HOH A O   1 
HETATM 7062 O  O   . HOH U 8 .   ? -22.364 21.540  2.109   1.00 13.92 ? 2351 HOH A O   1 
HETATM 7063 O  O   . HOH U 8 .   ? -9.567  23.909  -22.259 1.00 20.84 ? 2352 HOH A O   1 
HETATM 7064 O  O   . HOH U 8 .   ? -20.856 -3.897  -33.362 1.00 19.46 ? 2353 HOH A O   1 
HETATM 7065 O  O   . HOH U 8 .   ? -39.427 19.497  -25.609 1.00 27.74 ? 2354 HOH A O   1 
HETATM 7066 O  O   . HOH U 8 .   ? -9.308  26.388  -21.593 1.00 38.40 ? 2355 HOH A O   1 
HETATM 7067 O  O   . HOH U 8 .   ? -1.006  26.541  -18.812 1.00 32.24 ? 2356 HOH A O   1 
HETATM 7068 O  O   . HOH U 8 .   ? -15.227 1.005   -12.106 1.00 16.61 ? 2357 HOH A O   1 
HETATM 7069 O  O   . HOH U 8 .   ? -36.189 4.758   -21.960 1.00 31.14 ? 2358 HOH A O   1 
HETATM 7070 O  O   . HOH U 8 .   ? -18.966 -6.642  -26.859 1.00 36.21 ? 2359 HOH A O   1 
HETATM 7071 O  O   . HOH U 8 .   ? -21.734 -7.295  -29.797 1.00 38.84 ? 2360 HOH A O   1 
HETATM 7072 O  O   . HOH U 8 .   ? -0.735  -4.363  -19.884 1.00 29.84 ? 2361 HOH A O   1 
HETATM 7073 O  O   . HOH U 8 .   ? -33.972 6.182   -1.851  1.00 25.41 ? 2362 HOH A O   1 
HETATM 7074 O  O   . HOH U 8 .   ? -33.672 3.120   -1.086  1.00 41.25 ? 2363 HOH A O   1 
HETATM 7075 O  O   . HOH U 8 .   ? -31.438 22.434  -36.315 1.00 14.87 ? 2364 HOH A O   1 
HETATM 7076 O  O   . HOH U 8 .   ? -4.247  15.176  9.012   1.00 37.89 ? 2365 HOH A O   1 
HETATM 7077 O  O   . HOH U 8 .   ? -11.827 25.429  0.409   1.00 28.09 ? 2366 HOH A O   1 
HETATM 7078 O  O   . HOH U 8 .   ? 0.708   17.332  -18.232 1.00 24.87 ? 2367 HOH A O   1 
HETATM 7079 O  O   . HOH U 8 .   ? -32.364 29.915  -23.972 1.00 32.52 ? 2368 HOH A O   1 
HETATM 7080 O  O   . HOH U 8 .   ? -41.242 20.429  -21.251 1.00 26.47 ? 2369 HOH A O   1 
HETATM 7081 O  O   . HOH U 8 .   ? -10.503 20.136  6.118   1.00 33.45 ? 2370 HOH A O   1 
HETATM 7082 O  O   . HOH U 8 .   ? -5.819  19.873  -33.606 1.00 17.35 ? 2371 HOH A O   1 
HETATM 7083 O  O   . HOH U 8 .   ? -8.509  27.729  -5.634  1.00 28.84 ? 2372 HOH A O   1 
HETATM 7084 O  O   . HOH U 8 .   ? -9.276  6.323   -28.325 1.00 15.71 ? 2373 HOH A O   1 
HETATM 7085 O  O   . HOH U 8 .   ? 5.149   17.136  -16.422 1.00 42.93 ? 2374 HOH A O   1 
HETATM 7086 O  O   . HOH U 8 .   ? -17.286 33.424  -9.902  1.00 24.35 ? 2375 HOH A O   1 
HETATM 7087 O  O   . HOH U 8 .   ? -3.070  28.178  -17.371 1.00 42.31 ? 2376 HOH A O   1 
HETATM 7088 O  O   . HOH U 8 .   ? -5.914  -5.354  -12.208 1.00 29.16 ? 2377 HOH A O   1 
HETATM 7089 O  O   . HOH U 8 .   ? -3.091  25.352  -6.926  1.00 31.46 ? 2378 HOH A O   1 
HETATM 7090 O  O   . HOH U 8 .   ? -30.898 12.466  -7.997  1.00 16.15 ? 2379 HOH A O   1 
HETATM 7091 O  O   . HOH U 8 .   ? -41.581 12.706  -18.817 1.00 28.44 ? 2380 HOH A O   1 
HETATM 7092 O  O   . HOH U 8 .   ? -15.331 -2.699  -10.018 1.00 37.68 ? 2381 HOH A O   1 
HETATM 7093 O  O   . HOH U 8 .   ? -17.803 33.220  -32.450 1.00 13.23 ? 2382 HOH A O   1 
HETATM 7094 O  O   . HOH U 8 .   ? -13.251 31.685  -32.710 1.00 34.40 ? 2383 HOH A O   1 
HETATM 7095 O  O   . HOH U 8 .   ? -7.417  24.496  -36.370 1.00 34.71 ? 2384 HOH A O   1 
HETATM 7096 O  O   . HOH U 8 .   ? -3.346  28.248  -15.008 1.00 33.88 ? 2385 HOH A O   1 
HETATM 7097 O  O   . HOH U 8 .   ? -0.276  5.999   -18.135 1.00 23.21 ? 2386 HOH A O   1 
HETATM 7098 O  O   . HOH U 8 .   ? -19.884 -6.153  -31.844 1.00 32.60 ? 2387 HOH A O   1 
HETATM 7099 O  O   . HOH U 8 .   ? -19.164 2.757   -3.748  1.00 22.56 ? 2388 HOH A O   1 
HETATM 7100 O  O   . HOH U 8 .   ? -14.508 32.856  4.302   1.00 30.88 ? 2389 HOH A O   1 
HETATM 7101 O  O   . HOH U 8 .   ? -9.959  25.127  -44.657 1.00 32.48 ? 2390 HOH A O   1 
HETATM 7102 O  O   . HOH U 8 .   ? -19.319 3.499   -7.804  1.00 23.89 ? 2391 HOH A O   1 
HETATM 7103 O  O   . HOH U 8 .   ? -2.658  21.130  0.450   1.00 28.59 ? 2392 HOH A O   1 
HETATM 7104 O  O   . HOH U 8 .   ? -10.834 30.607  -13.744 1.00 23.90 ? 2393 HOH A O   1 
HETATM 7105 O  O   . HOH U 8 .   ? -31.776 6.939   -38.282 1.00 32.25 ? 2394 HOH A O   1 
HETATM 7106 O  O   . HOH U 8 .   ? -14.989 32.135  -19.210 1.00 39.40 ? 2395 HOH A O   1 
HETATM 7107 O  O   . HOH U 8 .   ? -31.703 24.959  1.863   1.00 23.42 ? 2396 HOH A O   1 
HETATM 7108 O  O   . HOH U 8 .   ? -5.951  24.477  -2.201  1.00 22.07 ? 2397 HOH A O   1 
HETATM 7109 O  O   . HOH U 8 .   ? 4.772   17.005  3.262   1.00 37.23 ? 2398 HOH A O   1 
HETATM 7110 O  O   . HOH U 8 .   ? -18.543 17.098  -17.737 1.00 26.14 ? 2399 HOH A O   1 
HETATM 7111 O  O   . HOH U 8 .   ? -32.383 -1.610  -21.165 1.00 28.23 ? 2400 HOH A O   1 
HETATM 7112 O  O   . HOH U 8 .   ? -24.803 12.912  -50.813 1.00 23.85 ? 2401 HOH A O   1 
HETATM 7113 O  O   . HOH U 8 .   ? -13.923 -5.237  -40.497 1.00 28.88 ? 2402 HOH A O   1 
HETATM 7114 O  O   . HOH U 8 .   ? 3.670   24.102  -16.311 1.00 26.28 ? 2403 HOH A O   1 
HETATM 7115 O  O   . HOH U 8 .   ? -38.384 20.994  -14.594 1.00 16.33 ? 2404 HOH A O   1 
HETATM 7116 O  O   . HOH U 8 .   ? -20.551 30.013  -12.255 1.00 20.92 ? 2405 HOH A O   1 
HETATM 7117 O  O   . HOH U 8 .   ? -24.643 28.034  -43.507 1.00 15.80 ? 2406 HOH A O   1 
HETATM 7118 O  O   . HOH U 8 .   ? -9.139  29.737  -19.536 1.00 31.09 ? 2407 HOH A O   1 
HETATM 7119 O  O   . HOH U 8 .   ? -14.127 -0.118  -5.333  1.00 18.66 ? 2408 HOH A O   1 
HETATM 7120 O  O   . HOH U 8 .   ? -16.161 18.067  -16.758 1.00 13.51 ? 2409 HOH A O   1 
HETATM 7121 O  O   . HOH U 8 .   ? -1.790  23.144  -8.121  1.00 13.27 ? 2410 HOH A O   1 
HETATM 7122 O  O   . HOH U 8 .   ? -41.358 10.079  -12.516 1.00 31.53 ? 2411 HOH A O   1 
HETATM 7123 O  O   . HOH U 8 .   ? -33.296 11.450  -40.106 1.00 24.14 ? 2412 HOH A O   1 
HETATM 7124 O  O   . HOH U 8 .   ? -32.835 11.334  -0.502  1.00 22.56 ? 2413 HOH A O   1 
HETATM 7125 O  O   . HOH U 8 .   ? -9.266  17.778  6.249   1.00 29.34 ? 2414 HOH A O   1 
HETATM 7126 O  O   . HOH U 8 .   ? -16.323 -1.666  -12.654 1.00 20.20 ? 2415 HOH A O   1 
HETATM 7127 O  O   . HOH U 8 .   ? -5.639  26.037  -19.942 1.00 25.31 ? 2416 HOH A O   1 
HETATM 7128 O  O   . HOH U 8 .   ? -13.336 3.811   -43.161 1.00 29.01 ? 2417 HOH A O   1 
HETATM 7129 O  O   . HOH U 8 .   ? -13.861 12.191  6.980   1.00 33.07 ? 2418 HOH A O   1 
HETATM 7130 O  O   . HOH U 8 .   ? -24.963 -0.543  -15.027 1.00 35.70 ? 2419 HOH A O   1 
HETATM 7131 O  O   . HOH U 8 .   ? -35.692 0.348   -26.598 1.00 30.33 ? 2420 HOH A O   1 
HETATM 7132 O  O   . HOH U 8 .   ? -3.734  8.325   6.536   1.00 43.18 ? 2421 HOH A O   1 
HETATM 7133 O  O   . HOH U 8 .   ? -7.063  10.823  -26.413 1.00 29.01 ? 2422 HOH A O   1 
HETATM 7134 O  O   . HOH U 8 .   ? 0.126   11.807  5.644   1.00 27.22 ? 2423 HOH A O   1 
HETATM 7135 O  O   . HOH U 8 .   ? -36.187 14.331  -36.302 1.00 34.02 ? 2424 HOH A O   1 
HETATM 7136 O  O   . HOH U 8 .   ? -23.882 -6.193  -34.141 1.00 37.64 ? 2425 HOH A O   1 
HETATM 7137 O  O   . HOH U 8 .   ? -29.441 21.012  -48.387 1.00 27.62 ? 2426 HOH A O   1 
HETATM 7138 O  O   . HOH U 8 .   ? -13.215 -10.856 -44.733 1.00 31.74 ? 2427 HOH A O   1 
HETATM 7139 O  O   . HOH U 8 .   ? -19.348 -9.770  -28.894 1.00 34.65 ? 2428 HOH A O   1 
HETATM 7140 O  O   . HOH U 8 .   ? -15.411 4.907   -50.691 1.00 35.68 ? 2429 HOH A O   1 
HETATM 7141 O  O   . HOH U 8 .   ? -12.385 -17.236 -41.222 1.00 30.30 ? 2430 HOH A O   1 
HETATM 7142 O  O   . HOH U 8 .   ? -9.787  10.450  10.845  1.00 27.50 ? 2431 HOH A O   1 
HETATM 7143 O  O   . HOH U 8 .   ? -2.545  11.945  -29.095 1.00 38.84 ? 2432 HOH A O   1 
HETATM 7144 O  O   . HOH U 8 .   ? -31.267 27.130  -54.519 1.00 27.03 ? 2433 HOH A O   1 
HETATM 7145 O  O   . HOH U 8 .   ? -18.907 8.326   7.145   1.00 37.66 ? 2434 HOH A O   1 
HETATM 7146 O  O   . HOH U 8 .   ? -8.630  11.060  -24.112 1.00 11.51 ? 2435 HOH A O   1 
HETATM 7147 O  O   . HOH U 8 .   ? -0.769  19.559  4.119   1.00 33.52 ? 2436 HOH A O   1 
HETATM 7148 O  O   . HOH U 8 .   ? -20.110 26.974  -45.572 1.00 15.20 ? 2437 HOH A O   1 
HETATM 7149 O  O   . HOH U 8 .   ? -9.343  21.040  -3.076  1.00 20.44 ? 2438 HOH A O   1 
HETATM 7150 O  O   . HOH U 8 .   ? -34.764 20.507  -22.379 1.00 29.61 ? 2439 HOH A O   1 
HETATM 7151 O  O   . HOH U 8 .   ? -35.213 16.956  -35.458 1.00 18.57 ? 2440 HOH A O   1 
HETATM 7152 O  O   . HOH U 8 .   ? -26.021 0.068   -8.958  1.00 29.20 ? 2441 HOH A O   1 
HETATM 7153 O  O   . HOH U 8 .   ? -31.959 1.019   -35.888 1.00 23.18 ? 2442 HOH A O   1 
HETATM 7154 O  O   . HOH U 8 .   ? -27.646 -6.051  -29.480 1.00 24.49 ? 2443 HOH A O   1 
HETATM 7155 O  O   . HOH U 8 .   ? -9.471  22.586  -24.777 1.00 16.92 ? 2444 HOH A O   1 
HETATM 7156 O  O   . HOH U 8 .   ? -12.913 29.589  -41.043 1.00 17.91 ? 2445 HOH A O   1 
HETATM 7157 O  O   . HOH U 8 .   ? -34.243 31.173  -0.010  1.00 41.48 ? 2446 HOH A O   1 
HETATM 7158 O  O   . HOH U 8 .   ? -13.962 9.975   5.009   1.00 29.73 ? 2447 HOH A O   1 
HETATM 7159 O  O   . HOH U 8 .   ? -14.259 27.897  1.266   1.00 24.99 ? 2448 HOH A O   1 
HETATM 7160 O  O   . HOH U 8 .   ? -7.535  19.620  4.369   1.00 23.38 ? 2449 HOH A O   1 
HETATM 7161 O  O   . HOH U 8 .   ? -10.022 15.683  -39.781 1.00 20.42 ? 2450 HOH A O   1 
HETATM 7162 O  O   . HOH U 8 .   ? -3.703  -2.136  -14.397 1.00 31.33 ? 2451 HOH A O   1 
HETATM 7163 O  O   . HOH U 8 .   ? -36.929 29.173  -17.033 1.00 23.80 ? 2452 HOH A O   1 
HETATM 7164 O  O   . HOH U 8 .   ? -11.792 27.240  -25.831 1.00 32.58 ? 2453 HOH A O   1 
HETATM 7165 O  O   . HOH U 8 .   ? -17.801 1.421   4.244   1.00 34.75 ? 2454 HOH A O   1 
HETATM 7166 O  O   . HOH U 8 .   ? -36.977 4.409   -8.774  1.00 39.71 ? 2455 HOH A O   1 
HETATM 7167 O  O   . HOH U 8 .   ? -34.697 11.266  1.733   0.50 28.08 ? 2456 HOH A O   1 
HETATM 7168 O  O   . HOH U 8 .   ? -14.827 32.726  9.309   1.00 35.79 ? 2457 HOH A O   1 
HETATM 7169 O  O   . HOH U 8 .   ? -20.652 4.332   8.981   1.00 34.79 ? 2458 HOH A O   1 
HETATM 7170 O  O   . HOH U 8 .   ? -29.127 28.605  -7.966  1.00 21.60 ? 2459 HOH A O   1 
HETATM 7171 O  O   . HOH U 8 .   ? -16.833 11.857  7.193   1.00 34.34 ? 2460 HOH A O   1 
HETATM 7172 O  O   . HOH U 8 .   ? -31.034 18.663  6.045   1.00 38.59 ? 2461 HOH A O   1 
HETATM 7173 O  O   . HOH U 8 .   ? 5.463   21.536  -14.012 1.00 31.73 ? 2462 HOH A O   1 
HETATM 7174 O  O   . HOH U 8 .   ? -23.677 30.932  -16.781 1.00 29.21 ? 2463 HOH A O   1 
HETATM 7175 O  O   . HOH U 8 .   ? -17.054 2.440   -8.655  1.00 28.38 ? 2464 HOH A O   1 
HETATM 7176 O  O   . HOH U 8 .   ? -32.369 0.838   -20.000 1.00 28.01 ? 2465 HOH A O   1 
HETATM 7177 O  O   . HOH U 8 .   ? -19.953 19.102  -23.037 1.00 19.01 ? 2466 HOH A O   1 
HETATM 7178 O  O   . HOH U 8 .   ? -20.626 -3.075  -22.815 1.00 25.94 ? 2467 HOH A O   1 
HETATM 7179 O  O   . HOH U 8 .   ? -40.463 22.628  -15.554 1.00 34.27 ? 2468 HOH A O   1 
HETATM 7180 O  O   . HOH U 8 .   ? -21.061 31.770  -10.196 1.00 29.68 ? 2469 HOH A O   1 
HETATM 7181 O  O   . HOH U 8 .   ? -5.247  -2.914  -12.785 1.00 36.58 ? 2470 HOH A O   1 
HETATM 7182 O  O   . HOH U 8 .   ? -13.022 30.569  -18.951 1.00 32.67 ? 2471 HOH A O   1 
HETATM 7183 O  O   . HOH U 8 .   ? -43.099 17.131  -17.107 1.00 33.79 ? 2472 HOH A O   1 
HETATM 7184 O  O   . HOH U 8 .   ? -24.365 29.741  -45.796 1.00 39.55 ? 2473 HOH A O   1 
HETATM 7185 O  O   . HOH U 8 .   ? -10.511 6.029   -51.168 1.00 34.66 ? 2474 HOH A O   1 
HETATM 7186 O  O   . HOH U 8 .   ? -15.655 30.647  2.706   1.00 21.81 ? 2475 HOH A O   1 
HETATM 7187 O  O   . HOH U 8 .   ? -6.510  26.452  -11.647 1.00 17.21 ? 2476 HOH A O   1 
HETATM 7188 O  O   . HOH U 8 .   ? -26.604 31.969  -27.017 1.00 24.45 ? 2477 HOH A O   1 
HETATM 7189 O  O   . HOH U 8 .   ? -14.860 33.079  -7.927  1.00 36.85 ? 2478 HOH A O   1 
HETATM 7190 O  O   . HOH U 8 .   ? -36.847 19.003  -34.310 1.00 27.67 ? 2479 HOH A O   1 
HETATM 7191 O  O   . HOH U 8 .   ? -35.927 27.501  -9.096  1.00 33.80 ? 2480 HOH A O   1 
HETATM 7192 O  O   . HOH U 8 .   ? -8.453  23.372  -1.638  1.00 22.43 ? 2481 HOH A O   1 
HETATM 7193 O  O   . HOH U 8 .   ? -13.415 0.623   -10.140 1.00 24.96 ? 2482 HOH A O   1 
HETATM 7194 O  O   . HOH U 8 .   ? -9.658  23.872  0.941   1.00 28.86 ? 2483 HOH A O   1 
HETATM 7195 O  O   . HOH U 8 .   ? -26.852 30.465  -24.455 1.00 24.33 ? 2484 HOH A O   1 
HETATM 7196 O  O   . HOH U 8 .   ? -28.516 4.092   6.494   1.00 41.94 ? 2485 HOH A O   1 
HETATM 7197 O  O   . HOH U 8 .   ? -22.763 -2.112  -43.490 1.00 37.47 ? 2486 HOH A O   1 
HETATM 7198 O  O   . HOH U 8 .   ? -38.676 21.066  -31.264 1.00 31.38 ? 2487 HOH A O   1 
HETATM 7199 O  O   . HOH U 8 .   ? -30.648 23.248  -50.869 1.00 37.97 ? 2488 HOH A O   1 
HETATM 7200 O  O   . HOH U 8 .   ? -26.949 31.506  -10.454 1.00 27.96 ? 2489 HOH A O   1 
HETATM 7201 O  O   . HOH U 8 .   ? -18.235 -21.516 -37.227 1.00 37.09 ? 2490 HOH A O   1 
HETATM 7202 O  O   . HOH U 8 .   ? -13.106 32.351  -40.212 1.00 28.50 ? 2491 HOH A O   1 
HETATM 7203 O  O   . HOH U 8 .   ? -7.468  20.341  -35.871 1.00 18.57 ? 2492 HOH A O   1 
HETATM 7204 O  O   . HOH U 8 .   ? -16.291 31.582  -46.338 1.00 32.81 ? 2493 HOH A O   1 
HETATM 7205 O  O   . HOH U 8 .   ? -33.668 20.828  -35.802 1.00 18.73 ? 2494 HOH A O   1 
HETATM 7206 O  O   . HOH U 8 .   ? 4.476   -9.490  -25.701 1.00 21.93 ? 2495 HOH A O   1 
HETATM 7207 O  O   . HOH U 8 .   ? -31.243 10.042  6.449   1.00 34.99 ? 2496 HOH A O   1 
HETATM 7208 O  O   . HOH U 8 .   ? -20.345 34.523  -9.679  1.00 36.18 ? 2497 HOH A O   1 
HETATM 7209 O  O   . HOH U 8 .   ? -35.365 28.001  -6.298  1.00 35.37 ? 2498 HOH A O   1 
HETATM 7210 O  O   . HOH U 8 .   ? -5.541  26.391  -7.982  1.00 22.32 ? 2499 HOH A O   1 
HETATM 7211 O  O   . HOH U 8 .   ? -10.169 31.770  -16.401 1.00 24.25 ? 2500 HOH A O   1 
HETATM 7212 O  O   . HOH U 8 .   ? -9.661  24.697  -39.616 1.00 19.99 ? 2501 HOH A O   1 
HETATM 7213 O  O   . HOH U 8 .   ? 2.706   12.344  -11.791 1.00 25.95 ? 2502 HOH A O   1 
HETATM 7214 O  O   . HOH U 8 .   ? -3.451  -8.351  -11.435 1.00 28.45 ? 2503 HOH A O   1 
HETATM 7215 O  O   . HOH U 8 .   ? -8.561  -8.814  -17.790 1.00 29.63 ? 2504 HOH A O   1 
HETATM 7216 O  O   . HOH U 8 .   ? -33.330 23.664  3.545   1.00 34.57 ? 2505 HOH A O   1 
HETATM 7217 O  O   . HOH U 8 .   ? -22.640 23.206  -21.609 1.00 18.26 ? 2506 HOH A O   1 
HETATM 7218 O  O   . HOH U 8 .   ? -21.490 29.629  -17.107 1.00 28.06 ? 2507 HOH A O   1 
HETATM 7219 O  O   . HOH U 8 .   ? -30.225 -5.935  -28.430 1.00 36.21 ? 2508 HOH A O   1 
HETATM 7220 O  O   . HOH U 8 .   ? -24.422 16.681  4.865   1.00 25.05 ? 2509 HOH A O   1 
HETATM 7221 O  O   . HOH U 8 .   ? 3.533   19.335  -6.766  1.00 20.80 ? 2510 HOH A O   1 
HETATM 7222 O  O   . HOH U 8 .   ? -0.715  1.112   -14.043 1.00 32.04 ? 2511 HOH A O   1 
HETATM 7223 O  O   . HOH U 8 .   ? -10.846 3.426   -43.649 1.00 35.74 ? 2512 HOH A O   1 
HETATM 7224 O  O   . HOH U 8 .   ? -35.377 7.123   -30.951 1.00 22.50 ? 2513 HOH A O   1 
HETATM 7225 O  O   . HOH U 8 .   ? -17.656 32.990  -17.291 1.00 27.75 ? 2514 HOH A O   1 
HETATM 7226 O  O   . HOH U 8 .   ? -36.646 9.384   -31.103 1.00 20.07 ? 2515 HOH A O   1 
HETATM 7227 O  O   . HOH U 8 .   ? -26.789 33.023  -19.032 1.00 22.12 ? 2516 HOH A O   1 
HETATM 7228 O  O   . HOH U 8 .   ? -43.383 14.692  -17.978 1.00 33.35 ? 2517 HOH A O   1 
HETATM 7229 O  O   . HOH U 8 .   ? -10.502 28.989  -40.326 1.00 27.26 ? 2518 HOH A O   1 
HETATM 7230 O  O   . HOH U 8 .   ? 5.060   14.517  -8.021  1.00 29.27 ? 2519 HOH A O   1 
HETATM 7231 O  O   . HOH U 8 .   ? -24.062 19.594  1.158   1.00 12.74 ? 2520 HOH A O   1 
HETATM 7232 O  O   . HOH U 8 .   ? -8.154  -11.002 -21.886 1.00 37.27 ? 2521 HOH A O   1 
HETATM 7233 O  O   . HOH U 8 .   ? -3.450  11.846  -26.673 1.00 22.54 ? 2522 HOH A O   1 
HETATM 7234 O  O   . HOH U 8 .   ? 3.537   17.540  -4.734  1.00 21.49 ? 2523 HOH A O   1 
HETATM 7235 O  O   . HOH U 8 .   ? -12.105 21.189  -45.850 1.00 16.67 ? 2524 HOH A O   1 
HETATM 7236 O  O   . HOH U 8 .   ? -14.262 32.747  -16.378 1.00 38.93 ? 2525 HOH A O   1 
HETATM 7237 O  O   . HOH U 8 .   ? -36.785 5.052   -31.872 1.00 37.34 ? 2526 HOH A O   1 
HETATM 7238 O  O   . HOH U 8 .   ? -43.242 18.721  -21.605 1.00 42.34 ? 2527 HOH A O   1 
HETATM 7239 O  O   . HOH U 8 .   ? -32.544 -1.526  -24.071 1.00 29.71 ? 2528 HOH A O   1 
HETATM 7240 O  O   . HOH U 8 .   ? 5.018   16.257  -10.233 1.00 24.04 ? 2529 HOH A O   1 
HETATM 7241 O  O   . HOH U 8 .   ? -9.107  30.162  -5.796  1.00 40.76 ? 2530 HOH A O   1 
HETATM 7242 O  O   . HOH U 8 .   ? -4.978  -1.960  -10.335 1.00 33.57 ? 2531 HOH A O   1 
HETATM 7243 O  O   . HOH U 8 .   ? -5.982  29.118  -11.799 1.00 23.03 ? 2532 HOH A O   1 
HETATM 7244 O  O   . HOH U 8 .   ? -19.363 30.708  -43.856 1.00 27.53 ? 2533 HOH A O   1 
HETATM 7245 O  O   . HOH U 8 .   ? -9.015  23.894  -42.147 1.00 34.97 ? 2534 HOH A O   1 
HETATM 7246 O  O   . HOH U 8 .   ? -19.780 31.137  -15.989 1.00 22.56 ? 2535 HOH A O   1 
HETATM 7247 O  O   . HOH U 8 .   ? 0.741   13.457  7.980   1.00 37.07 ? 2536 HOH A O   1 
HETATM 7248 O  O   . HOH U 8 .   ? -27.651 2.662   -43.883 1.00 33.79 ? 2537 HOH A O   1 
HETATM 7249 O  O   . HOH U 8 .   ? -35.869 22.632  -35.868 1.00 40.82 ? 2538 HOH A O   1 
HETATM 7250 O  O   . HOH U 8 .   ? -31.209 34.360  -3.191  1.00 37.46 ? 2539 HOH A O   1 
HETATM 7251 O  O   . HOH U 8 .   ? -24.889 18.272  -51.325 1.00 22.96 ? 2540 HOH A O   1 
HETATM 7252 O  O   . HOH U 8 .   ? -13.929 36.958  -29.473 1.00 34.24 ? 2541 HOH A O   1 
HETATM 7253 O  O   . HOH U 8 .   ? -1.631  0.777   -11.351 1.00 37.26 ? 2542 HOH A O   1 
HETATM 7254 O  O   . HOH U 8 .   ? -27.125 28.932  -42.609 1.00 28.65 ? 2543 HOH A O   1 
HETATM 7255 O  O   . HOH U 8 .   ? -17.791 -1.053  -3.850  1.00 36.18 ? 2544 HOH A O   1 
HETATM 7256 O  O   . HOH U 8 .   ? -28.983 19.567  7.834   1.00 35.72 ? 2545 HOH A O   1 
HETATM 7257 O  O   . HOH U 8 .   ? -9.116  7.026   -49.014 1.00 41.67 ? 2546 HOH A O   1 
HETATM 7258 O  O   . HOH U 8 .   ? 1.841   10.665  -10.256 1.00 34.24 ? 2547 HOH A O   1 
HETATM 7259 O  O   . HOH U 8 .   ? -35.689 18.829  -39.416 1.00 39.06 ? 2548 HOH A O   1 
HETATM 7260 O  O   . HOH U 8 .   ? -22.043 33.008  -39.873 1.00 36.74 ? 2549 HOH A O   1 
HETATM 7261 O  O   . HOH U 8 .   ? -24.139 -7.544  -31.839 1.00 39.84 ? 2550 HOH A O   1 
HETATM 7262 O  O   . HOH U 8 .   ? -2.766  18.660  -31.433 1.00 33.26 ? 2551 HOH A O   1 
HETATM 7263 O  O   . HOH U 8 .   ? -39.049 12.214  -32.722 1.00 35.66 ? 2552 HOH A O   1 
HETATM 7264 O  O   . HOH U 8 .   ? -2.588  24.742  -20.035 1.00 30.00 ? 2553 HOH A O   1 
HETATM 7265 O  O   . HOH U 8 .   ? -1.270  1.377   -18.251 1.00 30.38 ? 2554 HOH A O   1 
HETATM 7266 O  O   . HOH U 8 .   ? -13.528 22.491  10.714  1.00 19.10 ? 2555 HOH A O   1 
HETATM 7267 O  O   . HOH U 8 .   ? -10.433 18.087  -38.276 1.00 14.54 ? 2556 HOH A O   1 
HETATM 7268 O  O   . HOH U 8 .   ? 2.546   10.679  -7.261  1.00 29.16 ? 2557 HOH A O   1 
HETATM 7269 O  O   . HOH U 8 .   ? -33.036 -0.044  -27.544 1.00 24.98 ? 2558 HOH A O   1 
HETATM 7270 O  O   . HOH U 8 .   ? -7.828  31.599  -17.705 1.00 39.87 ? 2559 HOH A O   1 
HETATM 7271 O  O   . HOH U 8 .   ? -7.094  24.793  -21.651 1.00 34.60 ? 2560 HOH A O   1 
HETATM 7272 O  O   . HOH U 8 .   ? -22.436 29.230  -42.205 1.00 21.17 ? 2561 HOH A O   1 
HETATM 7273 O  O   . HOH U 8 .   ? -14.522 -19.882 -36.476 1.00 32.98 ? 2562 HOH A O   1 
HETATM 7274 O  O   . HOH U 8 .   ? -3.449  0.335   -6.106  1.00 28.07 ? 2563 HOH A O   1 
HETATM 7275 O  O   . HOH U 8 .   ? -11.667 26.551  -47.571 1.00 31.64 ? 2564 HOH A O   1 
HETATM 7276 O  O   . HOH U 8 .   ? -10.250 21.286  -42.293 1.00 18.85 ? 2565 HOH A O   1 
HETATM 7277 O  O   . HOH U 8 .   ? -33.867 26.671  -26.669 1.00 34.50 ? 2566 HOH A O   1 
HETATM 7278 O  O   . HOH U 8 .   ? -8.466  24.913  -30.362 1.00 20.57 ? 2567 HOH A O   1 
HETATM 7279 O  O   . HOH U 8 .   ? -1.602  -1.531  -18.234 1.00 33.46 ? 2568 HOH A O   1 
HETATM 7280 O  O   . HOH U 8 .   ? -26.816 12.921  -48.727 1.00 32.09 ? 2569 HOH A O   1 
HETATM 7281 O  O   . HOH U 8 .   ? -8.099  -5.203  -11.150 1.00 39.45 ? 2570 HOH A O   1 
HETATM 7282 O  O   . HOH U 8 .   ? -32.252 24.310  -37.933 1.00 27.90 ? 2571 HOH A O   1 
HETATM 7283 O  O   . HOH U 8 .   ? -8.938  12.252  13.182  1.00 31.39 ? 2572 HOH A O   1 
HETATM 7284 O  O   . HOH U 8 .   ? -19.425 2.138   -13.080 1.00 30.78 ? 2573 HOH A O   1 
HETATM 7285 O  O   . HOH U 8 .   ? -13.068 31.528  6.481   1.00 27.43 ? 2574 HOH A O   1 
HETATM 7286 O  O   . HOH U 8 .   ? -5.623  21.665  -31.467 1.00 24.52 ? 2575 HOH A O   1 
HETATM 7287 O  O   . HOH U 8 .   ? 4.164   12.057  -9.256  1.00 28.96 ? 2576 HOH A O   1 
HETATM 7288 O  O   . HOH U 8 .   ? -25.659 -6.790  -36.684 1.00 43.10 ? 2577 HOH A O   1 
HETATM 7289 O  O   . HOH U 8 .   ? -4.636  21.679  -24.600 1.00 31.59 ? 2578 HOH A O   1 
HETATM 7290 O  O   . HOH U 8 .   ? -9.775  20.476  -39.526 1.00 16.09 ? 2579 HOH A O   1 
HETATM 7291 O  O   . HOH U 8 .   ? -9.710  22.427  -46.481 1.00 32.00 ? 2580 HOH A O   1 
HETATM 7292 O  O   . HOH U 8 .   ? -8.644  22.087  5.399   1.00 33.03 ? 2581 HOH A O   1 
HETATM 7293 O  O   . HOH U 8 .   ? -38.216 8.694   -35.498 1.00 34.33 ? 2582 HOH A O   1 
HETATM 7294 O  O   . HOH U 8 .   ? -10.792 15.501  15.582  1.00 37.19 ? 2583 HOH A O   1 
HETATM 7295 O  O   . HOH U 8 .   ? 5.484   14.974  -14.361 1.00 36.21 ? 2584 HOH A O   1 
HETATM 7296 O  O   . HOH U 8 .   ? -35.536 4.647   -11.025 1.00 36.11 ? 2585 HOH A O   1 
HETATM 7297 O  O   . HOH U 8 .   ? -33.437 3.166   -11.071 1.00 39.72 ? 2586 HOH A O   1 
HETATM 7298 O  O   . HOH U 8 .   ? -10.830 33.103  -39.229 1.00 33.97 ? 2587 HOH A O   1 
HETATM 7299 O  O   . HOH U 8 .   ? -12.187 32.846  -10.729 1.00 33.21 ? 2588 HOH A O   1 
HETATM 7300 O  O   . HOH U 8 .   ? -8.353  23.147  3.210   1.00 34.36 ? 2589 HOH A O   1 
HETATM 7301 O  O   . HOH U 8 .   ? -0.118  20.145  -19.812 1.00 32.90 ? 2590 HOH A O   1 
HETATM 7302 O  O   . HOH U 8 .   ? -5.127  28.855  -9.273  1.00 36.14 ? 2591 HOH A O   1 
HETATM 7303 O  O   . HOH U 8 .   ? -5.401  20.586  -37.641 1.00 35.54 ? 2592 HOH A O   1 
HETATM 7304 O  O   . HOH U 8 .   ? -10.466 17.312  13.469  1.00 34.80 ? 2593 HOH A O   1 
HETATM 7305 O  O   . HOH U 8 .   ? -7.966  31.129  -12.375 1.00 29.89 ? 2594 HOH A O   1 
HETATM 7306 O  O   . HOH U 8 .   ? -14.703 33.078  -44.121 1.00 32.18 ? 2595 HOH A O   1 
HETATM 7307 O  O   . HOH U 8 .   ? -9.202  32.694  -10.105 1.00 42.28 ? 2596 HOH A O   1 
HETATM 7308 O  O   . HOH U 8 .   ? -9.012  19.215  -43.812 1.00 28.42 ? 2597 HOH A O   1 
HETATM 7309 O  O   . HOH V 8 .   ? -13.400 37.012  -22.079 0.50 16.24 ? 2101 HOH B O   1 
HETATM 7310 O  O   . HOH V 8 .   ? -24.596 58.683  15.351  1.00 25.48 ? 2102 HOH B O   1 
HETATM 7311 O  O   . HOH V 8 .   ? -23.514 70.418  -9.874  1.00 28.24 ? 2103 HOH B O   1 
HETATM 7312 O  O   . HOH V 8 .   ? -20.817 55.361  -34.995 1.00 29.00 ? 2104 HOH B O   1 
HETATM 7313 O  O   . HOH V 8 .   ? -36.205 55.496  -29.350 1.00 36.09 ? 2105 HOH B O   1 
HETATM 7314 O  O   . HOH V 8 .   ? -32.043 50.679  4.484   1.00 23.05 ? 2106 HOH B O   1 
HETATM 7315 O  O   . HOH V 8 .   ? -1.962  52.891  -6.770  1.00 38.39 ? 2107 HOH B O   1 
HETATM 7316 O  O   . HOH V 8 .   ? -28.192 43.853  -29.864 1.00 18.17 ? 2108 HOH B O   1 
HETATM 7317 O  O   . HOH V 8 .   ? -40.821 39.247  -15.556 1.00 26.28 ? 2109 HOH B O   1 
HETATM 7318 O  O   . HOH V 8 .   ? -23.507 72.003  0.145   1.00 31.30 ? 2110 HOH B O   1 
HETATM 7319 O  O   . HOH V 8 .   ? -14.587 31.462  0.146   1.00 33.24 ? 2111 HOH B O   1 
HETATM 7320 O  O   . HOH V 8 .   ? -29.735 88.182  3.963   1.00 34.94 ? 2112 HOH B O   1 
HETATM 7321 O  O   . HOH V 8 .   ? -13.150 40.226  -27.610 0.50 15.06 ? 2113 HOH B O   1 
HETATM 7322 O  O   . HOH V 8 .   ? -4.735  43.413  -25.042 1.00 21.50 ? 2114 HOH B O   1 
HETATM 7323 O  O   . HOH V 8 .   ? -18.153 47.460  -39.576 1.00 21.33 ? 2115 HOH B O   1 
HETATM 7324 O  O   . HOH V 8 .   ? -31.138 63.111  -16.485 1.00 28.00 ? 2116 HOH B O   1 
HETATM 7325 O  O   . HOH V 8 .   ? -38.956 64.752  4.316   1.00 36.04 ? 2117 HOH B O   1 
HETATM 7326 O  O   . HOH V 8 .   ? -28.135 70.137  -13.253 1.00 39.96 ? 2118 HOH B O   1 
HETATM 7327 O  O   . HOH V 8 .   ? -49.162 52.332  -21.058 1.00 36.97 ? 2119 HOH B O   1 
HETATM 7328 O  O   . HOH V 8 .   ? -27.374 67.138  13.764  1.00 35.58 ? 2120 HOH B O   1 
HETATM 7329 O  O   . HOH V 8 .   ? -35.770 64.207  -11.548 1.00 39.00 ? 2121 HOH B O   1 
HETATM 7330 O  O   . HOH V 8 .   ? -5.368  60.439  -7.696  1.00 30.87 ? 2122 HOH B O   1 
HETATM 7331 O  O   . HOH V 8 .   ? -9.131  58.422  -1.391  1.00 34.85 ? 2123 HOH B O   1 
HETATM 7332 O  O   . HOH V 8 .   ? -41.090 49.655  -28.311 1.00 33.22 ? 2124 HOH B O   1 
HETATM 7333 O  O   . HOH V 8 .   ? -34.964 40.169  14.643  1.00 27.88 ? 2125 HOH B O   1 
HETATM 7334 O  O   . HOH V 8 .   ? -20.952 52.629  -39.679 1.00 31.28 ? 2126 HOH B O   1 
HETATM 7335 O  O   . HOH V 8 .   ? -24.068 78.457  5.537   1.00 37.31 ? 2127 HOH B O   1 
HETATM 7336 O  O   . HOH V 8 .   ? -10.408 67.446  4.072   1.00 34.42 ? 2128 HOH B O   1 
HETATM 7337 O  O   . HOH V 8 .   ? -14.911 36.847  -3.170  1.00 23.10 ? 2129 HOH B O   1 
HETATM 7338 O  O   . HOH V 8 .   ? -16.688 62.219  -5.655  1.00 15.01 ? 2130 HOH B O   1 
HETATM 7339 O  O   . HOH V 8 .   ? -18.733 54.944  -13.057 1.00 11.76 ? 2131 HOH B O   1 
HETATM 7340 O  O   . HOH V 8 .   ? -30.015 65.782  -7.453  1.00 17.45 ? 2132 HOH B O   1 
HETATM 7341 O  O   . HOH V 8 .   ? -21.157 72.678  3.384   1.00 19.05 ? 2133 HOH B O   1 
HETATM 7342 O  O   . HOH V 8 .   ? -28.216 88.414  8.212   1.00 26.07 ? 2134 HOH B O   1 
HETATM 7343 O  O   . HOH V 8 .   ? -40.935 58.400  -28.233 1.00 38.20 ? 2135 HOH B O   1 
HETATM 7344 O  O   . HOH V 8 .   ? -21.746 35.594  -12.683 1.00 27.88 ? 2136 HOH B O   1 
HETATM 7345 O  O   . HOH V 8 .   ? -26.678 79.039  16.405  1.00 32.16 ? 2137 HOH B O   1 
HETATM 7346 O  O   . HOH V 8 .   ? -31.679 34.445  -22.295 1.00 19.34 ? 2138 HOH B O   1 
HETATM 7347 O  O   . HOH V 8 .   ? -0.998  41.109  -20.352 1.00 30.82 ? 2139 HOH B O   1 
HETATM 7348 O  O   . HOH V 8 .   ? -24.747 44.284  -8.468  1.00 17.08 ? 2140 HOH B O   1 
HETATM 7349 O  O   . HOH V 8 .   ? -29.629 62.573  -23.758 1.00 27.21 ? 2141 HOH B O   1 
HETATM 7350 O  O   . HOH V 8 .   ? -8.517  54.193  -3.153  1.00 23.74 ? 2142 HOH B O   1 
HETATM 7351 O  O   . HOH V 8 .   ? -41.485 58.157  -0.703  1.00 34.53 ? 2143 HOH B O   1 
HETATM 7352 O  O   . HOH V 8 .   ? 4.935   49.850  -10.302 1.00 29.64 ? 2144 HOH B O   1 
HETATM 7353 O  O   . HOH V 8 .   ? -22.520 62.994  -31.349 1.00 25.19 ? 2145 HOH B O   1 
HETATM 7354 O  O   . HOH V 8 .   ? -35.968 63.063  3.034   1.00 19.19 ? 2146 HOH B O   1 
HETATM 7355 O  O   . HOH V 8 .   ? -38.549 56.686  -11.188 1.00 21.59 ? 2147 HOH B O   1 
HETATM 7356 O  O   . HOH V 8 .   ? -10.421 63.294  -11.950 1.00 14.24 ? 2148 HOH B O   1 
HETATM 7357 O  O   . HOH V 8 .   ? -13.298 74.728  -7.025  1.00 27.64 ? 2149 HOH B O   1 
HETATM 7358 O  O   . HOH V 8 .   ? -14.328 44.305  13.556  1.00 13.50 ? 2150 HOH B O   1 
HETATM 7359 O  O   . HOH V 8 .   ? -20.423 56.714  -8.000  1.00 16.25 ? 2151 HOH B O   1 
HETATM 7360 O  O   . HOH V 8 .   ? -9.491  64.745  4.807   1.00 41.85 ? 2152 HOH B O   1 
HETATM 7361 O  O   . HOH V 8 .   ? -17.153 60.223  -36.707 1.00 28.68 ? 2153 HOH B O   1 
HETATM 7362 O  O   . HOH V 8 .   ? -32.420 39.041  -32.015 1.00 17.13 ? 2154 HOH B O   1 
HETATM 7363 O  O   . HOH V 8 .   ? -13.185 38.194  15.641  1.00 41.04 ? 2155 HOH B O   1 
HETATM 7364 O  O   . HOH V 8 .   ? -39.906 49.340  0.879   1.00 24.67 ? 2156 HOH B O   1 
HETATM 7365 O  O   . HOH V 8 .   ? -24.193 35.277  -8.798  1.00 27.54 ? 2157 HOH B O   1 
HETATM 7366 O  O   . HOH V 8 .   ? -37.040 41.932  -4.991  1.00 27.48 ? 2158 HOH B O   1 
HETATM 7367 O  O   . HOH V 8 .   ? -33.345 69.109  6.539   1.00 24.13 ? 2159 HOH B O   1 
HETATM 7368 O  O   . HOH V 8 .   ? -21.193 62.681  -17.580 1.00 19.12 ? 2160 HOH B O   1 
HETATM 7369 O  O   . HOH V 8 .   ? -8.538  42.178  -20.375 1.00 13.57 ? 2161 HOH B O   1 
HETATM 7370 O  O   . HOH V 8 .   ? -21.322 59.476  20.506  1.00 32.66 ? 2162 HOH B O   1 
HETATM 7371 O  O   . HOH V 8 .   ? -13.784 65.759  -31.255 1.00 33.14 ? 2163 HOH B O   1 
HETATM 7372 O  O   . HOH V 8 .   ? -34.776 48.246  11.870  1.00 21.82 ? 2164 HOH B O   1 
HETATM 7373 O  O   . HOH V 8 .   ? -30.711 53.545  -23.323 1.00 14.82 ? 2165 HOH B O   1 
HETATM 7374 O  O   . HOH V 8 .   ? -32.738 34.116  -5.431  1.00 37.63 ? 2166 HOH B O   1 
HETATM 7375 O  O   . HOH V 8 .   ? -29.087 38.063  12.058  1.00 28.09 ? 2167 HOH B O   1 
HETATM 7376 O  O   . HOH V 8 .   ? -24.364 46.485  -6.593  1.00 15.98 ? 2168 HOH B O   1 
HETATM 7377 O  O   . HOH V 8 .   ? -32.873 40.358  12.588  1.00 23.48 ? 2169 HOH B O   1 
HETATM 7378 O  O   . HOH V 8 .   ? -41.528 37.940  -18.309 1.00 27.61 ? 2170 HOH B O   1 
HETATM 7379 O  O   . HOH V 8 .   ? -32.877 69.093  3.596   1.00 29.81 ? 2171 HOH B O   1 
HETATM 7380 O  O   . HOH V 8 .   ? -2.383  55.643  -22.861 1.00 13.77 ? 2172 HOH B O   1 
HETATM 7381 O  O   . HOH V 8 .   ? -36.187 60.627  -7.817  1.00 14.83 ? 2173 HOH B O   1 
HETATM 7382 O  O   . HOH V 8 .   ? -33.459 29.594  -30.515 1.00 35.57 ? 2174 HOH B O   1 
HETATM 7383 O  O   . HOH V 8 .   ? -12.251 43.915  8.480   1.00 14.95 ? 2175 HOH B O   1 
HETATM 7384 O  O   . HOH V 8 .   ? -1.640  46.235  -26.546 1.00 24.47 ? 2176 HOH B O   1 
HETATM 7385 O  O   . HOH V 8 .   ? -36.742 54.685  8.005   1.00 32.04 ? 2177 HOH B O   1 
HETATM 7386 O  O   . HOH V 8 .   ? -14.922 41.151  16.531  1.00 24.21 ? 2178 HOH B O   1 
HETATM 7387 O  O   . HOH V 8 .   ? -32.895 38.599  -26.777 1.00 15.00 ? 2179 HOH B O   1 
HETATM 7388 O  O   . HOH V 8 .   ? -30.027 65.908  11.998  1.00 22.05 ? 2180 HOH B O   1 
HETATM 7389 O  O   . HOH V 8 .   ? -29.511 41.703  -26.325 1.00 9.81  ? 2181 HOH B O   1 
HETATM 7390 O  O   . HOH V 8 .   ? -35.763 44.912  7.589   1.00 20.34 ? 2182 HOH B O   1 
HETATM 7391 O  O   . HOH V 8 .   ? -7.455  45.216  -32.277 1.00 27.15 ? 2183 HOH B O   1 
HETATM 7392 O  O   . HOH V 8 .   ? -30.315 33.702  -12.316 1.00 37.31 ? 2184 HOH B O   1 
HETATM 7393 O  O   . HOH V 8 .   ? -21.784 32.796  -14.795 1.00 34.66 ? 2185 HOH B O   1 
HETATM 7394 O  O   . HOH V 8 .   ? -23.738 72.018  -2.608  1.00 31.52 ? 2186 HOH B O   1 
HETATM 7395 O  O   . HOH V 8 .   ? -37.626 45.464  13.568  1.00 26.84 ? 2187 HOH B O   1 
HETATM 7396 O  O   . HOH V 8 .   ? -28.967 32.245  -28.081 1.00 32.58 ? 2188 HOH B O   1 
HETATM 7397 O  O   . HOH V 8 .   ? -13.348 37.674  -35.278 1.00 32.78 ? 2189 HOH B O   1 
HETATM 7398 O  O   . HOH V 8 .   ? -32.793 42.337  -34.982 1.00 31.56 ? 2190 HOH B O   1 
HETATM 7399 O  O   . HOH V 8 .   ? -9.680  47.389  -34.261 1.00 20.09 ? 2191 HOH B O   1 
HETATM 7400 O  O   . HOH V 8 .   ? -11.591 53.551  4.269   1.00 19.67 ? 2192 HOH B O   1 
HETATM 7401 O  O   . HOH V 8 .   ? -33.125 55.596  18.425  1.00 40.69 ? 2193 HOH B O   1 
HETATM 7402 O  O   . HOH V 8 .   ? -19.477 40.471  -11.052 1.00 17.78 ? 2194 HOH B O   1 
HETATM 7403 O  O   . HOH V 8 .   ? -15.492 74.306  -15.711 1.00 38.52 ? 2195 HOH B O   1 
HETATM 7404 O  O   . HOH V 8 .   ? -7.304  46.766  -0.839  1.00 24.73 ? 2196 HOH B O   1 
HETATM 7405 O  O   . HOH V 8 .   ? -46.483 47.514  -22.749 1.00 38.46 ? 2197 HOH B O   1 
HETATM 7406 O  O   . HOH V 8 .   ? -8.505  66.553  -19.049 1.00 19.70 ? 2198 HOH B O   1 
HETATM 7407 O  O   . HOH V 8 .   ? -29.400 38.215  -19.920 1.00 14.44 ? 2199 HOH B O   1 
HETATM 7408 O  O   . HOH V 8 .   ? -30.103 37.506  9.393   1.00 34.95 ? 2200 HOH B O   1 
HETATM 7409 O  O   . HOH V 8 .   ? -13.763 64.670  7.957   1.00 26.25 ? 2201 HOH B O   1 
HETATM 7410 O  O   . HOH V 8 .   ? -34.002 32.781  -31.234 1.00 34.10 ? 2202 HOH B O   1 
HETATM 7411 O  O   . HOH V 8 .   ? -37.532 70.630  2.972   1.00 24.40 ? 2203 HOH B O   1 
HETATM 7412 O  O   . HOH V 8 .   ? -26.634 63.838  -13.323 1.00 23.39 ? 2204 HOH B O   1 
HETATM 7413 O  O   . HOH V 8 .   ? -27.324 46.643  -32.600 1.00 18.03 ? 2205 HOH B O   1 
HETATM 7414 O  O   . HOH V 8 .   ? -11.922 38.892  1.756   1.00 32.12 ? 2206 HOH B O   1 
HETATM 7415 O  O   . HOH V 8 .   ? -42.134 43.589  -22.567 1.00 22.47 ? 2207 HOH B O   1 
HETATM 7416 O  O   . HOH V 8 .   ? -1.939  59.912  -29.864 1.00 22.75 ? 2208 HOH B O   1 
HETATM 7417 O  O   . HOH V 8 .   ? -29.257 53.003  1.489   1.00 10.92 ? 2209 HOH B O   1 
HETATM 7418 O  O   . HOH V 8 .   ? -39.868 52.668  3.989   1.00 19.22 ? 2210 HOH B O   1 
HETATM 7419 O  O   . HOH V 8 .   ? -20.635 71.900  -7.987  1.00 33.93 ? 2211 HOH B O   1 
HETATM 7420 O  O   . HOH V 8 .   ? -19.778 65.141  -26.636 1.00 16.47 ? 2212 HOH B O   1 
HETATM 7421 O  O   . HOH V 8 .   ? -5.974  53.218  -3.227  1.00 38.87 ? 2213 HOH B O   1 
HETATM 7422 O  O   . HOH V 8 .   ? -10.555 60.705  13.245  1.00 33.62 ? 2214 HOH B O   1 
HETATM 7423 O  O   . HOH V 8 .   ? -36.430 56.467  -0.798  1.00 12.35 ? 2215 HOH B O   1 
HETATM 7424 O  O   . HOH V 8 .   ? -13.897 43.678  -37.926 1.00 22.35 ? 2216 HOH B O   1 
HETATM 7425 O  O   . HOH V 8 .   ? -28.413 32.066  -23.228 1.00 21.58 ? 2217 HOH B O   1 
HETATM 7426 O  O   . HOH V 8 .   ? -33.928 36.977  -23.235 1.00 15.73 ? 2218 HOH B O   1 
HETATM 7427 O  O   . HOH V 8 .   ? -3.094  46.924  -23.311 1.00 14.47 ? 2219 HOH B O   1 
HETATM 7428 O  O   . HOH V 8 .   ? -23.045 65.166  -14.087 1.00 26.36 ? 2220 HOH B O   1 
HETATM 7429 O  O   . HOH V 8 .   ? -25.214 66.518  -4.599  1.00 19.17 ? 2221 HOH B O   1 
HETATM 7430 O  O   . HOH V 8 .   ? -0.273  44.420  -11.338 1.00 34.38 ? 2222 HOH B O   1 
HETATM 7431 O  O   . HOH V 8 .   ? -15.173 53.573  1.893   1.00 12.73 ? 2223 HOH B O   1 
HETATM 7432 O  O   . HOH V 8 .   ? -13.707 43.610  -0.623  1.00 11.70 ? 2224 HOH B O   1 
HETATM 7433 O  O   . HOH V 8 .   ? -25.193 68.226  12.554  1.00 17.74 ? 2225 HOH B O   1 
HETATM 7434 O  O   . HOH V 8 .   ? -27.262 48.023  19.255  1.00 24.86 ? 2226 HOH B O   1 
HETATM 7435 O  O   . HOH V 8 .   ? -41.225 39.607  -24.784 1.00 11.91 ? 2227 HOH B O   1 
HETATM 7436 O  O   . HOH V 8 .   ? -24.421 63.933  -4.009  1.00 13.70 ? 2228 HOH B O   1 
HETATM 7437 O  O   . HOH V 8 .   ? -25.288 45.938  -35.798 1.00 31.62 ? 2229 HOH B O   1 
HETATM 7438 O  O   . HOH V 8 .   ? -15.528 72.546  8.494   1.00 26.36 ? 2230 HOH B O   1 
HETATM 7439 O  O   . HOH V 8 .   ? -2.688  61.705  -20.746 1.00 27.68 ? 2231 HOH B O   1 
HETATM 7440 O  O   . HOH V 8 .   ? -30.293 59.309  14.528  1.00 32.02 ? 2232 HOH B O   1 
HETATM 7441 O  O   . HOH V 8 .   ? -39.536 68.588  2.579   1.00 24.71 ? 2233 HOH B O   1 
HETATM 7442 O  O   . HOH V 8 .   ? -12.175 50.187  4.672   1.00 13.41 ? 2234 HOH B O   1 
HETATM 7443 O  O   . HOH V 8 .   ? -18.715 76.709  15.182  1.00 28.20 ? 2235 HOH B O   1 
HETATM 7444 O  O   . HOH V 8 .   ? -4.689  43.584  -28.783 1.00 32.96 ? 2236 HOH B O   1 
HETATM 7445 O  O   . HOH V 8 .   ? -23.939 71.619  16.961  1.00 34.42 ? 2237 HOH B O   1 
HETATM 7446 O  O   . HOH V 8 .   ? -34.342 40.878  -4.439  1.00 18.54 ? 2238 HOH B O   1 
HETATM 7447 O  O   . HOH V 8 .   ? -33.453 58.172  -35.282 1.00 31.30 ? 2239 HOH B O   1 
HETATM 7448 O  O   . HOH V 8 .   ? -34.980 56.781  8.371   1.00 30.82 ? 2240 HOH B O   1 
HETATM 7449 O  O   . HOH V 8 .   ? -4.743  46.311  -30.179 1.00 23.32 ? 2241 HOH B O   1 
HETATM 7450 O  O   . HOH V 8 .   ? -38.237 41.939  -7.508  1.00 29.58 ? 2242 HOH B O   1 
HETATM 7451 O  O   . HOH V 8 .   ? -30.054 50.323  1.659   1.00 12.61 ? 2243 HOH B O   1 
HETATM 7452 O  O   . HOH V 8 .   ? -19.375 67.996  10.742  1.00 24.70 ? 2244 HOH B O   1 
HETATM 7453 O  O   . HOH V 8 .   ? -18.577 35.147  -15.979 1.00 17.50 ? 2245 HOH B O   1 
HETATM 7454 O  O   . HOH V 8 .   ? -18.299 78.894  -1.701  1.00 37.38 ? 2246 HOH B O   1 
HETATM 7455 O  O   . HOH V 8 .   ? -17.378 34.225  0.530   1.00 17.53 ? 2247 HOH B O   1 
HETATM 7456 O  O   . HOH V 8 .   ? -35.257 63.164  -4.013  1.00 13.50 ? 2248 HOH B O   1 
HETATM 7457 O  O   . HOH V 8 .   ? -27.563 53.644  -0.568  1.00 10.33 ? 2249 HOH B O   1 
HETATM 7458 O  O   . HOH V 8 .   ? -5.491  64.468  -21.293 1.00 26.48 ? 2250 HOH B O   1 
HETATM 7459 O  O   . HOH V 8 .   ? -4.946  58.541  -22.191 1.00 16.99 ? 2251 HOH B O   1 
HETATM 7460 O  O   . HOH V 8 .   ? -24.409 40.820  -31.369 1.00 10.41 ? 2252 HOH B O   1 
HETATM 7461 O  O   . HOH V 8 .   ? -13.185 35.735  -13.349 1.00 22.57 ? 2253 HOH B O   1 
HETATM 7462 O  O   . HOH V 8 .   ? -25.584 32.381  -14.332 1.00 28.08 ? 2254 HOH B O   1 
HETATM 7463 O  O   . HOH V 8 .   ? -38.883 51.649  -0.249  1.00 16.60 ? 2255 HOH B O   1 
HETATM 7464 O  O   . HOH V 8 .   ? -20.737 37.183  13.282  1.00 13.47 ? 2256 HOH B O   1 
HETATM 7465 O  O   . HOH V 8 .   ? -33.217 39.224  -2.541  1.00 17.55 ? 2257 HOH B O   1 
HETATM 7466 O  O   . HOH V 8 .   ? -22.964 61.364  -15.725 1.00 24.14 ? 2258 HOH B O   1 
HETATM 7467 O  O   . HOH V 8 .   ? -21.091 40.819  -8.689  1.00 16.62 ? 2259 HOH B O   1 
HETATM 7468 O  O   . HOH V 8 .   ? -28.345 35.367  -2.709  1.00 27.83 ? 2260 HOH B O   1 
HETATM 7469 O  O   . HOH V 8 .   ? -45.165 51.991  -13.675 1.00 25.35 ? 2261 HOH B O   1 
HETATM 7470 O  O   . HOH V 8 .   ? -10.778 42.867  -7.531  1.00 21.03 ? 2262 HOH B O   1 
HETATM 7471 O  O   . HOH V 8 .   ? -6.704  49.204  0.347   1.00 26.92 ? 2263 HOH B O   1 
HETATM 7472 O  O   . HOH V 8 .   ? -25.655 47.459  -29.043 1.00 10.64 ? 2264 HOH B O   1 
HETATM 7473 O  O   . HOH V 8 .   ? -12.489 70.030  -20.281 1.00 34.39 ? 2265 HOH B O   1 
HETATM 7474 O  O   . HOH V 8 .   ? -40.319 44.398  -29.544 1.00 21.79 ? 2266 HOH B O   1 
HETATM 7475 O  O   . HOH V 8 .   ? -44.917 45.098  -12.553 1.00 24.62 ? 2267 HOH B O   1 
HETATM 7476 O  O   . HOH V 8 .   ? -28.924 53.337  17.602  1.00 19.28 ? 2268 HOH B O   1 
HETATM 7477 O  O   . HOH V 8 .   ? -19.214 32.606  10.559  1.00 32.74 ? 2269 HOH B O   1 
HETATM 7478 O  O   . HOH V 8 .   ? -13.261 73.332  -9.539  1.00 20.13 ? 2270 HOH B O   1 
HETATM 7479 O  O   . HOH V 8 .   ? -34.462 32.690  -23.833 1.00 32.86 ? 2271 HOH B O   1 
HETATM 7480 O  O   . HOH V 8 .   ? -9.094  43.855  2.773   1.00 19.43 ? 2272 HOH B O   1 
HETATM 7481 O  O   . HOH V 8 .   ? -16.878 37.536  -25.517 1.00 17.53 ? 2273 HOH B O   1 
HETATM 7482 O  O   . HOH V 8 .   ? -8.466  42.803  -16.550 1.00 14.54 ? 2274 HOH B O   1 
HETATM 7483 O  O   . HOH V 8 .   ? -30.169 47.488  -34.528 1.00 25.35 ? 2275 HOH B O   1 
HETATM 7484 O  O   . HOH V 8 .   ? -24.097 67.429  -10.705 1.00 23.42 ? 2276 HOH B O   1 
HETATM 7485 O  O   . HOH V 8 .   ? -3.889  62.765  -14.686 1.00 27.86 ? 2277 HOH B O   1 
HETATM 7486 O  O   . HOH V 8 .   ? -19.766 81.039  0.007   1.00 34.24 ? 2278 HOH B O   1 
HETATM 7487 O  O   . HOH V 8 .   ? -23.704 59.720  -17.372 1.00 27.37 ? 2279 HOH B O   1 
HETATM 7488 O  O   . HOH V 8 .   ? -10.908 59.194  -37.551 1.00 30.49 ? 2280 HOH B O   1 
HETATM 7489 O  O   . HOH V 8 .   ? -32.704 52.538  2.506   1.00 15.11 ? 2281 HOH B O   1 
HETATM 7490 O  O   . HOH V 8 .   ? 1.245   53.409  -17.561 1.00 20.74 ? 2282 HOH B O   1 
HETATM 7491 O  O   . HOH V 8 .   ? 1.064   50.097  -20.313 1.00 24.44 ? 2283 HOH B O   1 
HETATM 7492 O  O   . HOH V 8 .   ? -28.091 44.600  -36.080 1.00 19.21 ? 2284 HOH B O   1 
HETATM 7493 O  O   . HOH V 8 .   ? -17.325 64.995  14.530  1.00 37.24 ? 2285 HOH B O   1 
HETATM 7494 O  O   . HOH V 8 .   ? -38.610 48.977  6.505   1.00 29.28 ? 2286 HOH B O   1 
HETATM 7495 O  O   . HOH V 8 .   ? -27.328 61.877  -24.776 1.00 27.68 ? 2287 HOH B O   1 
HETATM 7496 O  O   . HOH V 8 .   ? -22.007 35.112  9.791   1.00 13.09 ? 2288 HOH B O   1 
HETATM 7497 O  O   . HOH V 8 .   ? -24.860 55.837  -3.956  1.00 22.47 ? 2289 HOH B O   1 
HETATM 7498 O  O   . HOH V 8 .   ? -29.192 44.796  17.582  1.00 24.32 ? 2290 HOH B O   1 
HETATM 7499 O  O   . HOH V 8 .   ? -29.253 35.485  -21.654 1.00 15.22 ? 2291 HOH B O   1 
HETATM 7500 O  O   . HOH V 8 .   ? -13.197 38.808  -7.645  1.00 23.54 ? 2292 HOH B O   1 
HETATM 7501 O  O   . HOH V 8 .   ? -29.709 71.760  -1.941  1.00 25.78 ? 2293 HOH B O   1 
HETATM 7502 O  O   . HOH V 8 .   ? -18.820 47.054  -15.626 1.00 10.61 ? 2294 HOH B O   1 
HETATM 7503 O  O   . HOH V 8 .   ? -35.452 34.384  -27.013 1.00 19.28 ? 2295 HOH B O   1 
HETATM 7504 O  O   . HOH V 8 .   ? -39.985 37.583  -7.632  1.00 39.51 ? 2296 HOH B O   1 
HETATM 7505 O  O   . HOH V 8 .   ? -37.945 68.162  6.235   1.00 15.22 ? 2297 HOH B O   1 
HETATM 7506 O  O   . HOH V 8 .   ? -19.073 71.028  11.063  1.00 26.74 ? 2298 HOH B O   1 
HETATM 7507 O  O   . HOH V 8 .   ? 2.599   47.922  -19.051 1.00 28.21 ? 2299 HOH B O   1 
HETATM 7508 O  O   . HOH V 8 .   ? -40.410 42.718  -7.113  1.00 27.82 ? 2300 HOH B O   1 
HETATM 7509 O  O   . HOH V 8 .   ? -41.004 43.452  -25.210 1.00 20.10 ? 2301 HOH B O   1 
HETATM 7510 O  O   . HOH V 8 .   ? -21.410 63.939  -33.996 1.00 30.13 ? 2302 HOH B O   1 
HETATM 7511 O  O   . HOH V 8 .   ? -30.724 39.835  -3.270  1.00 18.70 ? 2303 HOH B O   1 
HETATM 7512 O  O   . HOH V 8 .   ? -30.757 40.074  -28.208 1.00 13.45 ? 2304 HOH B O   1 
HETATM 7513 O  O   . HOH V 8 .   ? -38.846 65.036  8.698   1.00 16.38 ? 2305 HOH B O   1 
HETATM 7514 O  O   . HOH V 8 .   ? -46.666 41.452  -18.204 1.00 34.31 ? 2306 HOH B O   1 
HETATM 7515 O  O   . HOH V 8 .   ? -33.518 46.564  -32.182 1.00 36.47 ? 2307 HOH B O   1 
HETATM 7516 O  O   . HOH V 8 .   ? -30.563 31.749  -24.840 1.00 25.15 ? 2308 HOH B O   1 
HETATM 7517 O  O   . HOH V 8 .   ? -15.344 41.714  -16.815 1.00 9.14  ? 2309 HOH B O   1 
HETATM 7518 O  O   . HOH V 8 .   ? -10.539 51.524  -37.342 1.00 24.35 ? 2310 HOH B O   1 
HETATM 7519 O  O   . HOH V 8 .   ? -22.807 60.443  -19.840 1.00 15.90 ? 2311 HOH B O   1 
HETATM 7520 O  O   . HOH V 8 .   ? -37.330 57.327  -27.879 1.00 29.01 ? 2312 HOH B O   1 
HETATM 7521 O  O   . HOH V 8 .   ? -14.472 47.870  -41.871 1.00 22.66 ? 2313 HOH B O   1 
HETATM 7522 O  O   . HOH V 8 .   ? -38.339 57.143  -14.320 1.00 25.61 ? 2314 HOH B O   1 
HETATM 7523 O  O   . HOH V 8 .   ? -29.295 41.611  -36.166 1.00 21.69 ? 2315 HOH B O   1 
HETATM 7524 O  O   . HOH V 8 .   ? -6.243  60.818  -21.135 1.00 17.66 ? 2316 HOH B O   1 
HETATM 7525 O  O   . HOH V 8 .   ? -2.671  45.511  -11.363 1.00 23.46 ? 2317 HOH B O   1 
HETATM 7526 O  O   . HOH V 8 .   ? -7.344  65.490  -14.062 1.00 21.14 ? 2318 HOH B O   1 
HETATM 7527 O  O   . HOH V 8 .   ? -29.369 48.501  17.943  1.00 25.11 ? 2319 HOH B O   1 
HETATM 7528 O  O   . HOH V 8 .   ? -35.087 47.526  -22.483 1.00 10.93 ? 2320 HOH B O   1 
HETATM 7529 O  O   . HOH V 8 .   ? -42.455 41.647  -8.444  1.00 28.37 ? 2321 HOH B O   1 
HETATM 7530 O  O   . HOH V 8 .   ? -37.680 42.761  2.209   1.00 21.25 ? 2322 HOH B O   1 
HETATM 7531 O  O   . HOH V 8 .   ? -8.282  58.351  -5.913  1.00 19.08 ? 2323 HOH B O   1 
HETATM 7532 O  O   . HOH V 8 .   ? -19.663 53.593  -36.861 1.00 36.57 ? 2324 HOH B O   1 
HETATM 7533 O  O   . HOH V 8 .   ? -24.211 33.043  -27.511 1.00 10.89 ? 2325 HOH B O   1 
HETATM 7534 O  O   . HOH V 8 .   ? -41.935 56.377  -16.603 1.00 28.24 ? 2326 HOH B O   1 
HETATM 7535 O  O   . HOH V 8 .   ? -41.925 44.888  -27.340 1.00 24.79 ? 2327 HOH B O   1 
HETATM 7536 O  O   . HOH V 8 .   ? -10.687 44.232  6.169   1.00 15.92 ? 2328 HOH B O   1 
HETATM 7537 O  O   . HOH V 8 .   ? -31.907 36.894  24.626  1.00 21.13 ? 2329 HOH B O   1 
HETATM 7538 O  O   . HOH V 8 .   ? -30.895 43.114  18.749  1.00 31.28 ? 2330 HOH B O   1 
HETATM 7539 O  O   . HOH V 8 .   ? -25.994 53.616  -8.676  1.00 13.95 ? 2331 HOH B O   1 
HETATM 7540 O  O   . HOH V 8 .   ? -8.147  52.388  -38.618 1.00 30.23 ? 2332 HOH B O   1 
HETATM 7541 O  O   . HOH V 8 .   ? -8.862  46.369  -4.887  1.00 18.43 ? 2333 HOH B O   1 
HETATM 7542 O  O   . HOH V 8 .   ? -23.678 52.423  -15.236 1.00 10.84 ? 2334 HOH B O   1 
HETATM 7543 O  O   . HOH V 8 .   ? -43.922 49.855  -10.984 1.00 25.15 ? 2335 HOH B O   1 
HETATM 7544 O  O   . HOH V 8 .   ? -9.270  57.527  -12.475 1.00 14.43 ? 2336 HOH B O   1 
HETATM 7545 O  O   . HOH V 8 .   ? -3.730  56.715  -20.580 1.00 13.77 ? 2337 HOH B O   1 
HETATM 7546 O  O   . HOH V 8 .   ? -26.856 70.974  14.591  1.00 33.55 ? 2338 HOH B O   1 
HETATM 7547 O  O   . HOH V 8 .   ? 1.592   55.573  -13.905 1.00 39.65 ? 2339 HOH B O   1 
HETATM 7548 O  O   . HOH V 8 .   ? -3.857  39.574  -15.028 1.00 37.56 ? 2340 HOH B O   1 
HETATM 7549 O  O   . HOH V 8 .   ? -0.198  48.960  -27.039 1.00 21.86 ? 2341 HOH B O   1 
HETATM 7550 O  O   . HOH V 8 .   ? -43.184 52.403  -7.958  1.00 30.88 ? 2342 HOH B O   1 
HETATM 7551 O  O   . HOH V 8 .   ? -20.187 36.422  -38.066 1.00 16.05 ? 2343 HOH B O   1 
HETATM 7552 O  O   . HOH V 8 .   ? -14.980 49.203  7.270   1.00 12.67 ? 2344 HOH B O   1 
HETATM 7553 O  O   . HOH V 8 .   ? -34.422 36.752  -3.217  1.00 33.05 ? 2345 HOH B O   1 
HETATM 7554 O  O   . HOH V 8 .   ? -7.897  68.130  -7.128  1.00 25.41 ? 2346 HOH B O   1 
HETATM 7555 O  O   . HOH V 8 .   ? -4.290  63.263  -23.177 1.00 30.03 ? 2347 HOH B O   1 
HETATM 7556 O  O   . HOH V 8 .   ? -27.290 55.874  -2.465  1.00 11.36 ? 2348 HOH B O   1 
HETATM 7557 O  O   . HOH V 8 .   ? -6.434  64.368  -10.078 1.00 32.01 ? 2349 HOH B O   1 
HETATM 7558 O  O   . HOH V 8 .   ? -23.757 54.134  4.472   1.00 10.95 ? 2350 HOH B O   1 
HETATM 7559 O  O   . HOH V 8 .   ? -24.910 39.172  -8.833  1.00 13.29 ? 2351 HOH B O   1 
HETATM 7560 O  O   . HOH V 8 .   ? -40.945 43.238  -4.126  1.00 27.55 ? 2352 HOH B O   1 
HETATM 7561 O  O   . HOH V 8 .   ? -47.877 45.679  -15.688 1.00 34.94 ? 2353 HOH B O   1 
HETATM 7562 O  O   . HOH V 8 .   ? -29.041 64.726  -14.858 1.00 34.04 ? 2354 HOH B O   1 
HETATM 7563 O  O   . HOH V 8 .   ? -27.090 50.754  -34.544 1.00 22.94 ? 2355 HOH B O   1 
HETATM 7564 O  O   . HOH V 8 .   ? -38.711 60.483  -6.671  1.00 21.06 ? 2356 HOH B O   1 
HETATM 7565 O  O   . HOH V 8 .   ? -25.521 68.988  3.975   1.00 18.18 ? 2357 HOH B O   1 
HETATM 7566 O  O   . HOH V 8 .   ? -17.682 68.020  -19.503 1.00 22.55 ? 2358 HOH B O   1 
HETATM 7567 O  O   . HOH V 8 .   ? -8.077  65.242  -21.507 1.00 17.32 ? 2359 HOH B O   1 
HETATM 7568 O  O   . HOH V 8 .   ? -7.607  47.296  3.889   1.00 19.87 ? 2360 HOH B O   1 
HETATM 7569 O  O   . HOH V 8 .   ? 3.558   54.270  -35.286 1.00 20.09 ? 2361 HOH B O   1 
HETATM 7570 O  O   . HOH V 8 .   ? -1.019  40.429  -15.994 1.00 37.47 ? 2362 HOH B O   1 
HETATM 7571 O  O   . HOH V 8 .   ? -39.275 56.575  -16.890 1.00 24.15 ? 2363 HOH B O   1 
HETATM 7572 O  O   . HOH V 8 .   ? -11.658 39.537  9.045   1.00 17.38 ? 2364 HOH B O   1 
HETATM 7573 O  O   . HOH V 8 .   ? -24.264 75.284  -0.197  1.00 32.75 ? 2365 HOH B O   1 
HETATM 7574 O  O   . HOH V 8 .   ? -18.345 67.140  13.096  1.00 25.94 ? 2366 HOH B O   1 
HETATM 7575 O  O   . HOH V 8 .   ? -29.781 34.192  -36.489 1.00 27.89 ? 2367 HOH B O   1 
HETATM 7576 O  O   . HOH V 8 .   ? -35.597 49.514  -31.954 1.00 30.66 ? 2368 HOH B O   1 
HETATM 7577 O  O   . HOH V 8 .   ? -28.829 70.885  5.009   1.00 31.28 ? 2369 HOH B O   1 
HETATM 7578 O  O   . HOH V 8 .   ? -3.454  44.641  -21.815 1.00 15.02 ? 2370 HOH B O   1 
HETATM 7579 O  O   . HOH V 8 .   ? -23.019 62.590  -26.002 1.00 19.50 ? 2371 HOH B O   1 
HETATM 7580 O  O   . HOH V 8 .   ? -11.743 58.642  -12.493 1.00 11.22 ? 2372 HOH B O   1 
HETATM 7581 O  O   . HOH V 8 .   ? -28.739 35.001  -18.978 1.00 16.95 ? 2373 HOH B O   1 
HETATM 7582 O  O   . HOH V 8 .   ? -20.375 68.710  -19.161 1.00 23.93 ? 2374 HOH B O   1 
HETATM 7583 O  O   . HOH V 8 .   ? -32.537 70.123  -0.292  1.00 24.63 ? 2375 HOH B O   1 
HETATM 7584 O  O   . HOH V 8 .   ? -26.825 76.973  20.824  1.00 36.56 ? 2376 HOH B O   1 
HETATM 7585 O  O   . HOH V 8 .   ? -11.001 35.565  -23.216 1.00 43.12 ? 2377 HOH B O   1 
HETATM 7586 O  O   . HOH V 8 .   ? -23.913 55.176  -6.964  1.00 24.06 ? 2378 HOH B O   1 
HETATM 7587 O  O   . HOH V 8 .   ? -32.196 55.790  -36.056 1.00 25.45 ? 2379 HOH B O   1 
HETATM 7588 O  O   . HOH V 8 .   ? -8.634  42.590  6.540   1.00 33.16 ? 2380 HOH B O   1 
HETATM 7589 O  O   . HOH V 8 .   ? -17.364 32.349  -19.864 1.00 25.31 ? 2381 HOH B O   1 
HETATM 7590 O  O   . HOH V 8 .   ? -11.421 56.115  2.629   1.00 27.81 ? 2382 HOH B O   1 
HETATM 7591 O  O   . HOH V 8 .   ? -24.240 67.095  16.665  1.00 39.72 ? 2383 HOH B O   1 
HETATM 7592 O  O   . HOH V 8 .   ? -11.396 63.100  10.873  1.00 36.12 ? 2384 HOH B O   1 
HETATM 7593 O  O   . HOH V 8 .   ? -15.318 64.635  -19.135 1.00 14.63 ? 2385 HOH B O   1 
HETATM 7594 O  O   . HOH V 8 .   ? -39.033 35.363  -16.718 1.00 37.78 ? 2386 HOH B O   1 
HETATM 7595 O  O   . HOH V 8 .   ? -4.627  46.869  -33.088 1.00 26.39 ? 2387 HOH B O   1 
HETATM 7596 O  O   . HOH V 8 .   ? -26.520 35.057  -7.453  1.00 22.56 ? 2388 HOH B O   1 
HETATM 7597 O  O   . HOH V 8 .   ? -28.159 39.284  -2.541  1.00 27.73 ? 2389 HOH B O   1 
HETATM 7598 O  O   . HOH V 8 .   ? -36.104 35.698  -20.471 1.00 31.59 ? 2390 HOH B O   1 
HETATM 7599 O  O   . HOH V 8 .   ? 0.709   53.089  -24.346 1.00 23.66 ? 2391 HOH B O   1 
HETATM 7600 O  O   . HOH V 8 .   ? -39.619 62.836  -3.026  1.00 29.61 ? 2392 HOH B O   1 
HETATM 7601 O  O   . HOH V 8 .   ? -26.893 62.941  13.186  1.00 26.89 ? 2393 HOH B O   1 
HETATM 7602 O  O   . HOH V 8 .   ? -27.447 51.688  21.075  1.00 24.56 ? 2394 HOH B O   1 
HETATM 7603 O  O   . HOH V 8 .   ? -13.356 56.374  -40.629 1.00 27.94 ? 2395 HOH B O   1 
HETATM 7604 O  O   . HOH V 8 .   ? -27.579 64.984  11.418  1.00 22.62 ? 2396 HOH B O   1 
HETATM 7605 O  O   . HOH V 8 .   ? -32.044 34.005  -33.409 1.00 26.14 ? 2397 HOH B O   1 
HETATM 7606 O  O   . HOH V 8 .   ? -13.467 36.719  11.256  1.00 19.80 ? 2398 HOH B O   1 
HETATM 7607 O  O   . HOH V 8 .   ? -27.702 54.570  -36.265 1.00 29.51 ? 2399 HOH B O   1 
HETATM 7608 O  O   . HOH V 8 .   ? -39.614 41.865  -15.105 1.00 13.17 ? 2400 HOH B O   1 
HETATM 7609 O  O   . HOH V 8 .   ? -19.565 64.834  -17.288 1.00 15.47 ? 2401 HOH B O   1 
HETATM 7610 O  O   . HOH V 8 .   ? -32.712 41.399  6.569   1.00 14.58 ? 2402 HOH B O   1 
HETATM 7611 O  O   . HOH V 8 .   ? -33.476 51.373  -21.834 1.00 13.41 ? 2403 HOH B O   1 
HETATM 7612 O  O   . HOH V 8 .   ? -6.407  41.485  -9.914  1.00 26.79 ? 2404 HOH B O   1 
HETATM 7613 O  O   . HOH V 8 .   ? -11.181 36.047  -16.012 1.00 26.45 ? 2405 HOH B O   1 
HETATM 7614 O  O   . HOH V 8 .   ? -18.783 84.002  8.091   1.00 30.35 ? 2406 HOH B O   1 
HETATM 7615 O  O   . HOH V 8 .   ? -11.725 49.135  -35.943 1.00 25.43 ? 2407 HOH B O   1 
HETATM 7616 O  O   . HOH V 8 .   ? -21.727 46.752  -9.205  1.00 25.54 ? 2408 HOH B O   1 
HETATM 7617 O  O   . HOH V 8 .   ? -12.605 37.362  3.974   1.00 29.05 ? 2409 HOH B O   1 
HETATM 7618 O  O   . HOH V 8 .   ? -22.730 34.935  21.003  1.00 22.08 ? 2410 HOH B O   1 
HETATM 7619 O  O   . HOH V 8 .   ? -23.072 61.989  -22.179 1.00 27.31 ? 2411 HOH B O   1 
HETATM 7620 O  O   . HOH V 8 .   ? -19.031 37.026  -41.394 1.00 26.53 ? 2412 HOH B O   1 
HETATM 7621 O  O   . HOH V 8 .   ? -2.197  60.437  -14.551 1.00 28.60 ? 2413 HOH B O   1 
HETATM 7622 O  O   . HOH V 8 .   ? -1.530  41.187  -11.294 1.00 36.22 ? 2414 HOH B O   1 
HETATM 7623 O  O   . HOH V 8 .   ? -27.481 72.019  -0.190  1.00 33.14 ? 2415 HOH B O   1 
HETATM 7624 O  O   . HOH V 8 .   ? -0.902  43.680  -21.100 1.00 24.46 ? 2416 HOH B O   1 
HETATM 7625 O  O   . HOH V 8 .   ? -32.903 67.090  -11.544 1.00 33.39 ? 2417 HOH B O   1 
HETATM 7626 O  O   . HOH V 8 .   ? -20.260 48.529  -11.542 1.00 26.17 ? 2418 HOH B O   1 
HETATM 7627 O  O   . HOH V 8 .   ? -30.246 64.310  -20.586 1.00 28.53 ? 2419 HOH B O   1 
HETATM 7628 O  O   . HOH V 8 .   ? -26.173 35.077  18.922  1.00 29.59 ? 2420 HOH B O   1 
HETATM 7629 O  O   . HOH V 8 .   ? 3.355   51.458  -13.786 1.00 30.46 ? 2421 HOH B O   1 
HETATM 7630 O  O   . HOH V 8 .   ? -12.130 41.326  -0.421  1.00 19.24 ? 2422 HOH B O   1 
HETATM 7631 O  O   . HOH V 8 .   ? -37.129 52.143  7.756   1.00 32.74 ? 2423 HOH B O   1 
HETATM 7632 O  O   . HOH V 8 .   ? -16.711 53.896  -37.353 1.00 29.47 ? 2424 HOH B O   1 
HETATM 7633 O  O   . HOH V 8 .   ? 1.077   55.130  -25.901 1.00 21.57 ? 2425 HOH B O   1 
HETATM 7634 O  O   . HOH V 8 .   ? -17.282 62.150  13.553  1.00 33.12 ? 2426 HOH B O   1 
HETATM 7635 O  O   . HOH V 8 .   ? -12.766 60.259  -1.265  1.00 19.29 ? 2427 HOH B O   1 
HETATM 7636 O  O   . HOH V 8 .   ? -17.741 32.505  2.660   1.00 14.59 ? 2428 HOH B O   1 
HETATM 7637 O  O   . HOH V 8 .   ? -3.452  56.350  -35.738 1.00 17.21 ? 2429 HOH B O   1 
HETATM 7638 O  O   . HOH V 8 .   ? -35.486 55.027  10.792  1.00 18.33 ? 2430 HOH B O   1 
HETATM 7639 O  O   . HOH V 8 .   ? -24.019 33.116  -18.227 1.00 27.71 ? 2431 HOH B O   1 
HETATM 7640 O  O   . HOH V 8 .   ? -15.020 33.554  -38.913 1.00 30.79 ? 2432 HOH B O   1 
HETATM 7641 O  O   . HOH V 8 .   ? -17.228 45.010  -39.388 1.00 20.21 ? 2433 HOH B O   1 
HETATM 7642 O  O   . HOH V 8 .   ? -35.531 52.110  -29.338 1.00 23.78 ? 2434 HOH B O   1 
HETATM 7643 O  O   . HOH V 8 .   ? -23.906 43.492  -31.744 1.00 13.53 ? 2435 HOH B O   1 
HETATM 7644 O  O   . HOH V 8 .   ? -12.362 46.381  -35.966 1.00 32.70 ? 2436 HOH B O   1 
HETATM 7645 O  O   . HOH V 8 .   ? -13.380 34.648  2.942   1.00 30.21 ? 2437 HOH B O   1 
HETATM 7646 O  O   . HOH V 8 .   ? -25.273 36.699  13.837  1.00 16.03 ? 2438 HOH B O   1 
HETATM 7647 O  O   . HOH V 8 .   ? -20.949 67.319  -16.671 1.00 18.03 ? 2439 HOH B O   1 
HETATM 7648 O  O   . HOH V 8 .   ? -36.043 52.238  10.325  1.00 22.88 ? 2440 HOH B O   1 
HETATM 7649 O  O   . HOH V 8 .   ? -44.117 52.372  -17.167 1.00 25.85 ? 2441 HOH B O   1 
HETATM 7650 O  O   . HOH V 8 .   ? -10.442 69.959  -16.764 1.00 31.41 ? 2442 HOH B O   1 
HETATM 7651 O  O   . HOH V 8 .   ? -2.894  59.030  -35.356 1.00 32.05 ? 2443 HOH B O   1 
HETATM 7652 O  O   . HOH V 8 .   ? -7.221  42.854  -27.636 1.00 20.18 ? 2444 HOH B O   1 
HETATM 7653 O  O   . HOH V 8 .   ? -2.148  47.118  -9.309  1.00 24.67 ? 2445 HOH B O   1 
HETATM 7654 O  O   . HOH V 8 .   ? -18.106 47.786  -12.954 1.00 13.51 ? 2446 HOH B O   1 
HETATM 7655 O  O   . HOH V 8 .   ? -35.866 62.528  6.162   1.00 16.24 ? 2447 HOH B O   1 
HETATM 7656 O  O   . HOH V 8 .   ? -12.478 34.509  -21.423 1.00 37.73 ? 2448 HOH B O   1 
HETATM 7657 O  O   . HOH V 8 .   ? -32.228 60.335  -35.973 1.00 38.14 ? 2449 HOH B O   1 
HETATM 7658 O  O   . HOH V 8 .   ? -9.499  58.291  1.224   1.00 44.31 ? 2450 HOH B O   1 
HETATM 7659 O  O   . HOH V 8 .   ? -15.073 38.285  -30.965 1.00 27.65 ? 2451 HOH B O   1 
HETATM 7660 O  O   . HOH V 8 .   ? 3.256   57.021  -28.265 1.00 29.16 ? 2452 HOH B O   1 
HETATM 7661 O  O   . HOH V 8 .   ? -12.416 52.694  -40.331 1.00 34.16 ? 2453 HOH B O   1 
HETATM 7662 O  O   . HOH V 8 .   ? -34.155 46.158  18.695  1.00 42.56 ? 2454 HOH B O   1 
HETATM 7663 O  O   . HOH V 8 .   ? -35.944 62.492  -16.017 1.00 35.69 ? 2455 HOH B O   1 
HETATM 7664 O  O   . HOH V 8 .   ? -45.339 48.403  -24.420 1.00 37.41 ? 2456 HOH B O   1 
HETATM 7665 O  O   . HOH V 8 .   ? -38.975 39.810  -4.148  1.00 38.21 ? 2457 HOH B O   1 
HETATM 7666 O  O   . HOH V 8 .   ? -39.926 58.352  -7.740  1.00 23.45 ? 2458 HOH B O   1 
HETATM 7667 O  O   . HOH V 8 .   ? -43.037 54.961  -12.387 1.00 37.66 ? 2459 HOH B O   1 
HETATM 7668 O  O   . HOH V 8 .   ? -9.323  37.392  -10.212 1.00 29.15 ? 2460 HOH B O   1 
HETATM 7669 O  O   . HOH V 8 .   ? -37.150 34.069  -12.725 1.00 24.79 ? 2461 HOH B O   1 
HETATM 7670 O  O   . HOH V 8 .   ? -21.943 71.298  -5.760  1.00 39.94 ? 2462 HOH B O   1 
HETATM 7671 O  O   . HOH V 8 .   ? -25.422 68.080  -6.981  1.00 28.41 ? 2463 HOH B O   1 
HETATM 7672 O  O   . HOH V 8 .   ? -27.436 34.012  10.735  1.00 35.63 ? 2464 HOH B O   1 
HETATM 7673 O  O   . HOH V 8 .   ? -12.663 49.183  15.452  1.00 33.05 ? 2465 HOH B O   1 
HETATM 7674 O  O   . HOH V 8 .   ? -3.666  39.646  -11.999 1.00 35.85 ? 2466 HOH B O   1 
HETATM 7675 O  O   . HOH V 8 .   ? -11.396 55.679  -5.559  1.00 14.90 ? 2467 HOH B O   1 
HETATM 7676 O  O   . HOH V 8 .   ? -37.193 46.387  5.743   1.00 19.70 ? 2468 HOH B O   1 
HETATM 7677 O  O   . HOH V 8 .   ? -5.800  58.426  -34.745 1.00 35.33 ? 2469 HOH B O   1 
HETATM 7678 O  O   . HOH V 8 .   ? -20.946 38.415  15.843  1.00 16.19 ? 2470 HOH B O   1 
HETATM 7679 O  O   . HOH V 8 .   ? -20.757 63.260  -20.934 1.00 30.49 ? 2471 HOH B O   1 
HETATM 7680 O  O   . HOH V 8 .   ? -14.971 34.068  -10.230 1.00 37.14 ? 2472 HOH B O   1 
HETATM 7681 O  O   . HOH V 8 .   ? -19.273 60.995  20.927  1.00 39.25 ? 2473 HOH B O   1 
HETATM 7682 O  O   . HOH V 8 .   ? -7.528  61.260  -4.669  1.00 30.11 ? 2474 HOH B O   1 
HETATM 7683 O  O   . HOH V 8 .   ? -12.440 50.776  10.026  1.00 21.52 ? 2475 HOH B O   1 
HETATM 7684 O  O   . HOH V 8 .   ? -36.853 65.116  -8.394  1.00 23.14 ? 2476 HOH B O   1 
HETATM 7685 O  O   . HOH V 8 .   ? -12.950 50.989  12.855  1.00 35.66 ? 2477 HOH B O   1 
HETATM 7686 O  O   . HOH V 8 .   ? -32.530 32.256  -11.554 1.00 42.92 ? 2478 HOH B O   1 
HETATM 7687 O  O   . HOH V 8 .   ? -11.112 45.985  -26.676 1.00 17.49 ? 2479 HOH B O   1 
HETATM 7688 O  O   . HOH V 8 .   ? -20.783 35.371  -17.588 1.00 27.34 ? 2480 HOH B O   1 
HETATM 7689 O  O   . HOH V 8 .   ? -9.395  56.969  6.624   1.00 39.24 ? 2481 HOH B O   1 
HETATM 7690 O  O   . HOH V 8 .   ? -25.074 71.109  2.385   1.00 38.00 ? 2482 HOH B O   1 
HETATM 7691 O  O   . HOH V 8 .   ? -4.407  42.215  -23.015 1.00 24.68 ? 2483 HOH B O   1 
HETATM 7692 O  O   . HOH V 8 .   ? -10.834 44.110  -4.915  1.00 19.06 ? 2484 HOH B O   1 
HETATM 7693 O  O   . HOH V 8 .   ? -3.604  73.286  -9.719  1.00 31.89 ? 2485 HOH B O   1 
HETATM 7694 O  O   . HOH V 8 .   ? -34.437 56.951  15.461  1.00 31.95 ? 2486 HOH B O   1 
HETATM 7695 O  O   . HOH V 8 .   ? -29.563 33.063  -15.450 1.00 26.39 ? 2487 HOH B O   1 
HETATM 7696 O  O   . HOH V 8 .   ? -44.684 45.164  -25.437 1.00 41.53 ? 2488 HOH B O   1 
HETATM 7697 O  O   . HOH V 8 .   ? -45.098 40.519  -21.315 1.00 19.82 ? 2489 HOH B O   1 
HETATM 7698 O  O   . HOH V 8 .   ? -13.435 35.728  -10.799 1.00 27.92 ? 2490 HOH B O   1 
HETATM 7699 O  O   . HOH V 8 .   ? -36.132 42.933  -7.269  1.00 31.12 ? 2491 HOH B O   1 
HETATM 7700 O  O   . HOH V 8 .   ? -5.378  48.235  5.135   1.00 38.19 ? 2492 HOH B O   1 
HETATM 7701 O  O   . HOH V 8 .   ? -36.424 62.696  -9.701  1.00 27.10 ? 2493 HOH B O   1 
HETATM 7702 O  O   . HOH V 8 .   ? -8.728  69.953  -14.647 1.00 35.97 ? 2494 HOH B O   1 
HETATM 7703 O  O   . HOH V 8 .   ? -32.842 68.225  10.173  1.00 31.97 ? 2495 HOH B O   1 
HETATM 7704 O  O   . HOH V 8 .   ? -21.646 46.255  -6.734  1.00 20.97 ? 2496 HOH B O   1 
HETATM 7705 O  O   . HOH V 8 .   ? -24.547 60.723  -38.779 1.00 39.77 ? 2497 HOH B O   1 
HETATM 7706 O  O   . HOH V 8 .   ? -9.982  43.668  -28.009 1.00 22.07 ? 2498 HOH B O   1 
HETATM 7707 O  O   . HOH V 8 .   ? -8.075  49.062  -36.477 1.00 25.27 ? 2499 HOH B O   1 
HETATM 7708 O  O   . HOH V 8 .   ? -14.631 60.705  21.415  1.00 31.80 ? 2500 HOH B O   1 
HETATM 7709 O  O   . HOH V 8 .   ? -26.640 32.482  -2.487  1.00 21.53 ? 2501 HOH B O   1 
HETATM 7710 O  O   . HOH V 8 .   ? -15.266 32.947  -22.007 1.00 33.82 ? 2502 HOH B O   1 
HETATM 7711 O  O   . HOH V 8 .   ? -40.027 60.433  3.361   1.00 32.49 ? 2503 HOH B O   1 
HETATM 7712 O  O   . HOH V 8 .   ? -14.289 33.626  -34.041 1.00 27.46 ? 2504 HOH B O   1 
HETATM 7713 O  O   . HOH V 8 .   ? -13.112 58.584  17.146  1.00 40.12 ? 2505 HOH B O   1 
HETATM 7714 O  O   . HOH V 8 .   ? -27.107 33.919  -5.039  1.00 26.74 ? 2506 HOH B O   1 
HETATM 7715 O  O   . HOH V 8 .   ? -42.659 47.662  -29.867 1.00 39.09 ? 2507 HOH B O   1 
HETATM 7716 O  O   . HOH V 8 .   ? -15.970 35.377  -32.417 1.00 24.16 ? 2508 HOH B O   1 
HETATM 7717 O  O   . HOH V 8 .   ? -12.805 40.964  -30.218 1.00 31.99 ? 2509 HOH B O   1 
HETATM 7718 O  O   . HOH V 8 .   ? -43.311 49.870  -8.381  1.00 29.55 ? 2510 HOH B O   1 
HETATM 7719 O  O   . HOH V 8 .   ? -44.581 42.655  -10.696 1.00 41.39 ? 2511 HOH B O   1 
HETATM 7720 O  O   . HOH V 8 .   ? -7.511  40.792  -18.211 1.00 18.36 ? 2512 HOH B O   1 
HETATM 7721 O  O   . HOH V 8 .   ? -38.300 43.994  4.712   1.00 30.83 ? 2513 HOH B O   1 
HETATM 7722 O  O   . HOH V 8 .   ? -24.876 34.911  16.140  1.00 32.07 ? 2514 HOH B O   1 
HETATM 7723 O  O   . HOH V 8 .   ? -10.823 42.945  -30.866 1.00 30.70 ? 2515 HOH B O   1 
HETATM 7724 O  O   . HOH V 8 .   ? -45.395 38.503  -19.401 1.00 26.84 ? 2516 HOH B O   1 
HETATM 7725 O  O   . HOH V 8 .   ? -52.226 49.424  -17.935 1.00 26.95 ? 2517 HOH B O   1 
HETATM 7726 O  O   . HOH V 8 .   ? -36.733 66.675  8.314   1.00 15.25 ? 2518 HOH B O   1 
HETATM 7727 O  O   . HOH V 8 .   ? -35.864 49.361  14.107  1.00 38.35 ? 2519 HOH B O   1 
HETATM 7728 O  O   . HOH V 8 .   ? -18.151 65.323  -19.484 1.00 18.48 ? 2520 HOH B O   1 
HETATM 7729 O  O   . HOH V 8 .   ? -9.135  46.640  6.135   1.00 19.18 ? 2521 HOH B O   1 
HETATM 7730 O  O   . HOH V 8 .   ? -31.790 41.632  21.214  1.00 37.43 ? 2522 HOH B O   1 
HETATM 7731 O  O   . HOH V 8 .   ? -43.093 40.992  -23.179 1.00 16.58 ? 2523 HOH B O   1 
HETATM 7732 O  O   . HOH V 8 .   ? -10.862 41.991  9.873   1.00 24.82 ? 2524 HOH B O   1 
HETATM 7733 O  O   . HOH V 8 .   ? -38.491 63.480  6.372   1.00 23.72 ? 2525 HOH B O   1 
HETATM 7734 O  O   . HOH V 8 .   ? -38.917 58.832  -18.359 1.00 29.80 ? 2526 HOH B O   1 
HETATM 7735 O  O   . HOH V 8 .   ? 0.019   55.740  -17.656 1.00 35.00 ? 2527 HOH B O   1 
HETATM 7736 O  O   . HOH V 8 .   ? -35.101 42.711  6.062   1.00 19.49 ? 2528 HOH B O   1 
HETATM 7737 O  O   . HOH V 8 .   ? 0.550   50.329  -24.889 1.00 28.06 ? 2529 HOH B O   1 
HETATM 7738 O  O   . HOH V 8 .   ? -38.455 56.261  1.170   1.00 20.04 ? 2530 HOH B O   1 
HETATM 7739 O  O   . HOH V 8 .   ? -45.680 46.296  -9.092  1.00 34.05 ? 2531 HOH B O   1 
HETATM 7740 O  O   . HOH V 8 .   ? -39.952 41.700  1.723   1.00 37.88 ? 2532 HOH B O   1 
HETATM 7741 O  O   . HOH V 8 .   ? -45.918 53.614  -15.798 1.00 35.33 ? 2533 HOH B O   1 
HETATM 7742 O  O   . HOH V 8 .   ? -26.511 48.059  -34.430 1.00 30.29 ? 2534 HOH B O   1 
HETATM 7743 O  O   . HOH V 8 .   ? -28.594 55.254  19.832  1.00 34.31 ? 2535 HOH B O   1 
HETATM 7744 O  O   . HOH V 8 .   ? -34.243 54.096  -36.146 1.00 36.54 ? 2536 HOH B O   1 
HETATM 7745 O  O   . HOH V 8 .   ? 2.838   53.670  -15.241 1.00 31.27 ? 2537 HOH B O   1 
HETATM 7746 O  O   . HOH V 8 .   ? -37.362 47.301  15.602  1.00 35.99 ? 2538 HOH B O   1 
HETATM 7747 O  O   . HOH V 8 .   ? 3.414   48.426  -8.679  1.00 30.88 ? 2539 HOH B O   1 
HETATM 7748 O  O   . HOH V 8 .   ? -25.174 63.049  -23.867 1.00 31.18 ? 2540 HOH B O   1 
HETATM 7749 O  O   . HOH V 8 .   ? -13.052 33.964  10.745  1.00 36.31 ? 2541 HOH B O   1 
HETATM 7750 O  O   . HOH V 8 .   ? -10.559 42.828  12.617  1.00 35.84 ? 2542 HOH B O   1 
HETATM 7751 O  O   . HOH V 8 .   ? -27.762 35.763  12.817  1.00 27.07 ? 2543 HOH B O   1 
HETATM 7752 O  O   . HOH V 8 .   ? -23.848 41.738  -8.080  1.00 18.48 ? 2544 HOH B O   1 
HETATM 7753 O  O   . HOH V 8 .   ? -0.412  47.195  -23.633 1.00 25.00 ? 2545 HOH B O   1 
HETATM 7754 O  O   . HOH V 8 .   ? -19.768 34.748  13.888  1.00 31.16 ? 2546 HOH B O   1 
HETATM 7755 O  O   . HOH V 8 .   ? -14.279 33.627  -13.261 1.00 39.92 ? 2547 HOH B O   1 
HETATM 7756 O  O   . HOH V 8 .   ? -10.665 48.864  6.538   1.00 15.43 ? 2548 HOH B O   1 
HETATM 7757 O  O   . HOH V 8 .   ? -16.573 34.215  16.545  1.00 32.37 ? 2549 HOH B O   1 
HETATM 7758 O  O   . HOH V 8 .   ? 6.478   50.231  -8.108  1.00 24.55 ? 2550 HOH B O   1 
HETATM 7759 O  O   . HOH V 8 .   ? -39.525 53.736  1.449   1.00 15.87 ? 2551 HOH B O   1 
HETATM 7760 O  O   . HOH V 8 .   ? -34.268 40.380  -33.594 1.00 22.53 ? 2552 HOH B O   1 
HETATM 7761 O  O   . HOH V 8 .   ? -45.368 47.472  -11.564 1.00 28.40 ? 2553 HOH B O   1 
HETATM 7762 O  O   . HOH V 8 .   ? -5.729  57.655  -6.937  1.00 26.79 ? 2554 HOH B O   1 
HETATM 7763 O  O   . HOH V 8 .   ? -10.154 34.869  -13.515 1.00 24.14 ? 2555 HOH B O   1 
HETATM 7764 O  O   . HOH V 8 .   ? -6.605  40.969  -21.878 1.00 21.94 ? 2556 HOH B O   1 
HETATM 7765 O  O   . HOH V 8 .   ? -17.558 32.788  -12.505 1.00 26.14 ? 2557 HOH B O   1 
HETATM 7766 O  O   . HOH V 8 .   ? -24.459 63.361  -14.781 1.00 30.04 ? 2558 HOH B O   1 
HETATM 7767 O  O   . HOH V 8 .   ? -20.465 30.868  -20.069 1.00 27.93 ? 2559 HOH B O   1 
HETATM 7768 O  O   . HOH V 8 .   ? -25.752 45.326  -30.884 1.00 14.76 ? 2560 HOH B O   1 
HETATM 7769 O  O   . HOH V 8 .   ? -13.801 45.157  16.193  1.00 17.25 ? 2561 HOH B O   1 
HETATM 7770 O  O   . HOH V 8 .   ? -1.160  57.339  -19.632 1.00 22.80 ? 2562 HOH B O   1 
HETATM 7771 O  O   . HOH V 8 .   ? -36.837 65.026  -5.599  1.00 24.46 ? 2563 HOH B O   1 
HETATM 7772 O  O   . HOH V 8 .   ? -40.245 57.949  2.134   1.00 25.77 ? 2564 HOH B O   1 
HETATM 7773 O  O   . HOH V 8 .   ? -47.239 49.988  -13.649 1.00 40.39 ? 2565 HOH B O   1 
HETATM 7774 O  O   . HOH V 8 .   ? -12.934 59.861  19.338  1.00 33.19 ? 2566 HOH B O   1 
HETATM 7775 O  O   . HOH V 8 .   ? -19.842 34.308  -13.677 1.00 22.80 ? 2567 HOH B O   1 
HETATM 7776 O  O   . HOH V 8 .   ? 2.676   52.383  -19.750 1.00 33.33 ? 2568 HOH B O   1 
HETATM 7777 O  O   . HOH V 8 .   ? -9.277  57.076  -3.666  1.00 23.34 ? 2569 HOH B O   1 
HETATM 7778 O  O   . HOH V 8 .   ? -32.927 30.157  -28.090 1.00 38.27 ? 2570 HOH B O   1 
HETATM 7779 O  O   . HOH V 8 .   ? -2.779  55.409  -38.257 1.00 31.24 ? 2571 HOH B O   1 
HETATM 7780 O  O   . HOH V 8 .   ? -8.268  42.358  -8.349  1.00 32.56 ? 2572 HOH B O   1 
HETATM 7781 O  O   . HOH V 8 .   ? -37.293 63.673  -13.876 1.00 36.68 ? 2573 HOH B O   1 
HETATM 7782 O  O   . HOH V 8 .   ? -41.446 50.727  3.075   1.00 28.95 ? 2574 HOH B O   1 
HETATM 7783 O  O   . HOH V 8 .   ? 0.925   53.598  -37.608 1.00 39.00 ? 2575 HOH B O   1 
HETATM 7784 O  O   . HOH V 8 .   ? -9.575  69.096  -19.131 1.00 30.08 ? 2576 HOH B O   1 
HETATM 7785 O  O   . HOH V 8 .   ? -37.090 63.400  -1.999  1.00 20.22 ? 2577 HOH B O   1 
HETATM 7786 O  O   . HOH V 8 .   ? -0.118  56.912  -23.728 1.00 32.53 ? 2578 HOH B O   1 
HETATM 7787 O  O   . HOH V 8 .   ? -9.611  68.957  -24.138 1.00 35.20 ? 2579 HOH B O   1 
HETATM 7788 O  O   . HOH V 8 .   ? -15.012 43.554  -40.346 1.00 20.40 ? 2580 HOH B O   1 
HETATM 7789 O  O   . HOH V 8 .   ? -6.715  38.034  -18.059 1.00 20.93 ? 2581 HOH B O   1 
HETATM 7790 O  O   . HOH V 8 .   ? 1.091   56.283  -21.162 1.00 35.01 ? 2582 HOH B O   1 
HETATM 7791 O  O   . HOH V 8 .   ? -37.261 43.826  9.527   1.00 32.31 ? 2583 HOH B O   1 
HETATM 7792 O  O   . HOH V 8 .   ? -12.485 48.455  8.579   1.00 14.32 ? 2584 HOH B O   1 
HETATM 7793 O  O   . HOH V 8 .   ? -37.199 63.799  0.713   1.00 28.14 ? 2585 HOH B O   1 
HETATM 7794 O  O   . HOH V 8 .   ? -10.776 44.864  -35.214 1.00 32.42 ? 2586 HOH B O   1 
HETATM 7795 O  O   . HOH V 8 .   ? -7.731  67.046  -23.690 1.00 25.98 ? 2587 HOH B O   1 
HETATM 7796 O  O   . HOH V 8 .   ? -22.831 35.848  12.507  1.00 19.00 ? 2588 HOH B O   1 
HETATM 7797 O  O   . HOH V 8 .   ? -13.502 34.850  -36.390 1.00 24.91 ? 2589 HOH B O   1 
HETATM 7798 O  O   . HOH V 8 .   ? -23.141 63.680  -19.178 1.00 41.00 ? 2590 HOH B O   1 
HETATM 7799 O  O   . HOH V 8 .   ? -49.250 46.919  -22.949 1.00 37.66 ? 2591 HOH B O   1 
HETATM 7800 O  O   . HOH V 8 .   ? -40.257 62.743  -7.130  1.00 37.05 ? 2592 HOH B O   1 
HETATM 7801 O  O   . HOH V 8 .   ? -11.868 45.321  12.617  1.00 19.19 ? 2593 HOH B O   1 
HETATM 7802 O  O   . HOH V 8 .   ? -22.346 66.472  -25.746 1.00 30.21 ? 2594 HOH B O   1 
HETATM 7803 O  O   . HOH V 8 .   ? -9.552  42.022  0.697   1.00 22.06 ? 2595 HOH B O   1 
HETATM 7804 O  O   . HOH V 8 .   ? -2.527  40.320  -22.713 1.00 36.46 ? 2596 HOH B O   1 
HETATM 7805 O  O   . HOH V 8 .   ? -3.659  42.768  -9.840  1.00 31.48 ? 2597 HOH B O   1 
HETATM 7806 O  O   . HOH V 8 .   ? -22.160 31.983  10.180  1.00 36.75 ? 2598 HOH B O   1 
HETATM 7807 O  O   . HOH V 8 .   ? -7.206  45.520  1.690   1.00 29.60 ? 2599 HOH B O   1 
HETATM 7808 O  O   . HOH V 8 .   ? -11.496 46.142  9.905   1.00 17.04 ? 2600 HOH B O   1 
HETATM 7809 O  O   . HOH V 8 .   ? -36.318 56.353  13.000  1.00 33.86 ? 2601 HOH B O   1 
HETATM 7810 O  O   . HOH V 8 .   ? -5.798  38.621  -20.692 1.00 28.89 ? 2602 HOH B O   1 
HETATM 7811 O  O   . HOH V 8 .   ? -14.949 38.476  -27.676 1.00 31.02 ? 2603 HOH B O   1 
HETATM 7812 O  O   . HOH V 8 .   ? 3.833   55.830  -25.224 1.00 31.83 ? 2604 HOH B O   1 
HETATM 7813 O  O   . HOH V 8 .   ? 4.346   57.706  -30.980 1.00 41.27 ? 2605 HOH B O   1 
HETATM 7814 O  O   . HOH V 8 .   ? -39.000 61.614  -10.933 1.00 39.84 ? 2606 HOH B O   1 
HETATM 7815 O  O   . HOH V 8 .   ? -9.444  37.913  12.573  1.00 41.53 ? 2607 HOH B O   1 
HETATM 7816 O  O   . HOH V 8 .   ? -0.596  60.236  -19.869 1.00 36.29 ? 2608 HOH B O   1 
HETATM 7817 O  O   . HOH V 8 .   ? 0.070   45.069  -25.062 1.00 36.88 ? 2609 HOH B O   1 
HETATM 7818 O  O   . HOH V 8 .   ? -37.081 61.215  13.971  1.00 39.25 ? 2610 HOH B O   1 
HETATM 7819 O  O   . HOH V 8 .   ? -12.627 60.224  22.924  1.00 32.04 ? 2611 HOH B O   1 
HETATM 7820 O  O   . HOH V 8 .   ? -9.701  44.050  -33.221 1.00 26.55 ? 2612 HOH B O   1 
HETATM 7821 O  O   . HOH V 8 .   ? -41.360 54.341  5.584   1.00 30.67 ? 2613 HOH B O   1 
HETATM 7822 O  O   . HOH V 8 .   ? -37.169 60.469  -18.639 1.00 34.97 ? 2614 HOH B O   1 
HETATM 7823 O  O   . HOH V 8 .   ? -4.973  47.099  -2.576  1.00 30.35 ? 2615 HOH B O   1 
HETATM 7824 O  O   . HOH V 8 .   ? -11.201 62.442  -34.535 1.00 36.38 ? 2616 HOH B O   1 
HETATM 7825 O  O   . HOH V 8 .   ? -6.992  36.312  -21.938 1.00 36.84 ? 2617 HOH B O   1 
HETATM 7826 O  O   . HOH V 8 .   ? -50.491 54.838  -21.470 1.00 32.03 ? 2618 HOH B O   1 
HETATM 7827 O  O   . HOH V 8 .   ? -8.235  35.939  -17.368 1.00 34.21 ? 2619 HOH B O   1 
HETATM 7828 O  O   . HOH V 8 .   ? -11.069 47.584  13.990  1.00 33.73 ? 2620 HOH B O   1 
HETATM 7829 O  O   . HOH V 8 .   ? -42.125 56.522  3.481   1.00 39.65 ? 2621 HOH B O   1 
# 
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   GLY 1   106 ?   ?   ?   A . n 
A 1 2   PRO 2   107 ?   ?   ?   A . n 
A 1 3   HIS 3   108 ?   ?   ?   A . n 
A 1 4   MET 4   109 ?   ?   ?   A . n 
A 1 5   GLU 5   110 ?   ?   ?   A . n 
A 1 6   GLU 6   111 ?   ?   ?   A . n 
A 1 7   ALA 7   112 ?   ?   ?   A . n 
A 1 8   SER 8   113 ?   ?   ?   A . n 
A 1 9   LYS 9   114 ?   ?   ?   A . n 
A 1 10  ARG 10  115 115 ARG ARG A . n 
A 1 11  SER 11  116 116 SER SER A . n 
A 1 12  TYR 12  117 117 TYR TYR A . n 
A 1 13  GLN 13  118 118 GLN GLN A . n 
A 1 14  PHE 14  119 119 PHE PHE A . n 
A 1 15  TRP 15  120 120 TRP TRP A . n 
A 1 16  ASP 16  121 121 ASP ASP A . n 
A 1 17  THR 17  122 122 THR THR A . n 
A 1 18  GLN 18  123 123 GLN GLN A . n 
A 1 19  PRO 19  124 124 PRO PRO A . n 
A 1 20  VAL 20  125 125 VAL VAL A . n 
A 1 21  PRO 21  126 126 PRO PRO A . n 
A 1 22  LYS 22  127 127 LYS LYS A . n 
A 1 23  LEU 23  128 128 LEU LEU A . n 
A 1 24  GLY 24  129 129 GLY GLY A . n 
A 1 25  GLU 25  130 130 GLU GLU A . n 
A 1 26  VAL 26  131 131 VAL VAL A . n 
A 1 27  VAL 27  132 132 VAL VAL A . n 
A 1 28  ASN 28  133 133 ASN ASN A . n 
A 1 29  THR 29  134 134 THR THR A . n 
A 1 30  HIS 30  135 135 HIS HIS A . n 
A 1 31  GLY 31  136 136 GLY GLY A . n 
A 1 32  PRO 32  137 137 PRO PRO A . n 
A 1 33  VAL 33  138 138 VAL VAL A . n 
A 1 34  GLU 34  139 139 GLU GLU A . n 
A 1 35  PRO 35  140 140 PRO PRO A . n 
A 1 36  ASP 36  141 141 ASP ASP A . n 
A 1 37  LYS 37  142 142 LYS LYS A . n 
A 1 38  ASP 38  143 143 ASP ASP A . n 
A 1 39  ASN 39  144 144 ASN ASN A . n 
A 1 40  ILE 40  145 145 ILE ILE A . n 
A 1 41  ARG 41  146 146 ARG ARG A . n 
A 1 42  GLN 42  147 147 GLN GLN A . n 
A 1 43  GLU 43  148 148 GLU GLU A . n 
A 1 44  PRO 44  149 149 PRO PRO A . n 
A 1 45  TYR 45  150 150 TYR TYR A . n 
A 1 46  THR 46  151 151 THR THR A . n 
A 1 47  LEU 47  152 152 LEU LEU A . n 
A 1 48  PRO 48  153 153 PRO PRO A . n 
A 1 49  GLN 49  154 154 GLN GLN A . n 
A 1 50  GLY 50  155 155 GLY GLY A . n 
A 1 51  PHE 51  156 156 PHE PHE A . n 
A 1 52  THR 52  157 157 THR THR A . n 
A 1 53  TRP 53  158 158 TRP TRP A . n 
A 1 54  ASP 54  159 159 ASP ASP A . n 
A 1 55  ALA 55  160 160 ALA ALA A . n 
A 1 56  LEU 56  161 161 LEU LEU A . n 
A 1 57  ASP 57  162 162 ASP ASP A . n 
A 1 58  LEU 58  163 163 LEU LEU A . n 
A 1 59  GLY 59  164 164 GLY GLY A . n 
A 1 60  ASP 60  165 165 ASP ASP A . n 
A 1 61  ARG 61  166 166 ARG ARG A . n 
A 1 62  GLY 62  167 167 GLY GLY A . n 
A 1 63  VAL 63  168 168 VAL VAL A . n 
A 1 64  LEU 64  169 169 LEU LEU A . n 
A 1 65  LYS 65  170 170 LYS LYS A . n 
A 1 66  GLU 66  171 171 GLU GLU A . n 
A 1 67  LEU 67  172 172 LEU LEU A . n 
A 1 68  TYR 68  173 173 TYR TYR A . n 
A 1 69  THR 69  174 174 THR THR A . n 
A 1 70  LEU 70  175 175 LEU LEU A . n 
A 1 71  LEU 71  176 176 LEU LEU A . n 
A 1 72  ASN 72  177 177 ASN ASN A . n 
A 1 73  GLU 73  178 178 GLU GLU A . n 
A 1 74  ASN 74  179 179 ASN ASN A . n 
A 1 75  TYR 75  180 180 TYR TYR A . n 
A 1 76  VAL 76  181 181 VAL VAL A . n 
A 1 77  GLU 77  182 182 GLU GLU A . n 
A 1 78  ASP 78  183 183 ASP ASP A . n 
A 1 79  ASP 79  184 184 ASP ASP A . n 
A 1 80  ASP 80  185 185 ASP ASP A . n 
A 1 81  ASN 81  186 186 ASN ASN A . n 
A 1 82  MET 82  187 187 MET MET A . n 
A 1 83  PHE 83  188 188 PHE PHE A . n 
A 1 84  ARG 84  189 189 ARG ARG A . n 
A 1 85  PHE 85  190 190 PHE PHE A . n 
A 1 86  ASP 86  191 191 ASP ASP A . n 
A 1 87  TYR 87  192 192 TYR TYR A . n 
A 1 88  SER 88  193 193 SER SER A . n 
A 1 89  PRO 89  194 194 PRO PRO A . n 
A 1 90  GLU 90  195 195 GLU GLU A . n 
A 1 91  PHE 91  196 196 PHE PHE A . n 
A 1 92  LEU 92  197 197 LEU LEU A . n 
A 1 93  LEU 93  198 198 LEU LEU A . n 
A 1 94  TRP 94  199 199 TRP TRP A . n 
A 1 95  ALA 95  200 200 ALA ALA A . n 
A 1 96  LEU 96  201 201 LEU LEU A . n 
A 1 97  ARG 97  202 202 ARG ARG A . n 
A 1 98  PRO 98  203 203 PRO PRO A . n 
A 1 99  PRO 99  204 204 PRO PRO A . n 
A 1 100 GLY 100 205 205 GLY GLY A . n 
A 1 101 TRP 101 206 206 TRP TRP A . n 
A 1 102 LEU 102 207 207 LEU LEU A . n 
A 1 103 PRO 103 208 208 PRO PRO A . n 
A 1 104 GLN 104 209 209 GLN GLN A . n 
A 1 105 TRP 105 210 210 TRP TRP A . n 
A 1 106 HIS 106 211 211 HIS HIS A . n 
A 1 107 CYS 107 212 212 CYS CYS A . n 
A 1 108 GLY 108 213 213 GLY GLY A . n 
A 1 109 VAL 109 214 214 VAL VAL A . n 
A 1 110 ARG 110 215 215 ARG ARG A . n 
A 1 111 VAL 111 216 216 VAL VAL A . n 
A 1 112 VAL 112 217 217 VAL VAL A . n 
A 1 113 SER 113 218 218 SER SER A . n 
A 1 114 SER 114 219 219 SER SER A . n 
A 1 115 ARG 115 220 220 ARG ARG A . n 
A 1 116 LYS 116 221 221 LYS LYS A . n 
A 1 117 LEU 117 222 222 LEU LEU A . n 
A 1 118 VAL 118 223 223 VAL VAL A . n 
A 1 119 GLY 119 224 224 GLY GLY A . n 
A 1 120 PHE 120 225 225 PHE PHE A . n 
A 1 121 ILE 121 226 226 ILE ILE A . n 
A 1 122 SER 122 227 227 SER SER A . n 
A 1 123 ALA 123 228 228 ALA ALA A . n 
A 1 124 ILE 124 229 229 ILE ILE A . n 
A 1 125 PRO 125 230 230 PRO PRO A . n 
A 1 126 ALA 126 231 231 ALA ALA A . n 
A 1 127 ASN 127 232 232 ASN ASN A . n 
A 1 128 ILE 128 233 233 ILE ILE A . n 
A 1 129 HIS 129 234 234 HIS HIS A . n 
A 1 130 ILE 130 235 235 ILE ILE A . n 
A 1 131 TYR 131 236 236 TYR TYR A . n 
A 1 132 ASP 132 237 237 ASP ASP A . n 
A 1 133 THR 133 238 238 THR THR A . n 
A 1 134 GLU 134 239 239 GLU GLU A . n 
A 1 135 LYS 135 240 240 LYS LYS A . n 
A 1 136 LYS 136 241 241 LYS LYS A . n 
A 1 137 MET 137 242 242 MET MET A . n 
A 1 138 VAL 138 243 243 VAL VAL A . n 
A 1 139 GLU 139 244 244 GLU GLU A . n 
A 1 140 ILE 140 245 245 ILE ILE A . n 
A 1 141 ASN 141 246 246 ASN ASN A . n 
A 1 142 PHE 142 247 247 PHE PHE A . n 
A 1 143 LEU 143 248 248 LEU LEU A . n 
A 1 144 CYS 144 249 249 CYS CYS A . n 
A 1 145 VAL 145 250 250 VAL VAL A . n 
A 1 146 HIS 146 251 251 HIS HIS A . n 
A 1 147 LYS 147 252 252 LYS LYS A . n 
A 1 148 LYS 148 253 253 LYS LYS A . n 
A 1 149 LEU 149 254 254 LEU LEU A . n 
A 1 150 ARG 150 255 255 ARG ARG A . n 
A 1 151 SER 151 256 256 SER SER A . n 
A 1 152 LYS 152 257 257 LYS LYS A . n 
A 1 153 ARG 153 258 258 ARG ARG A . n 
A 1 154 VAL 154 259 259 VAL VAL A . n 
A 1 155 ALA 155 260 260 ALA ALA A . n 
A 1 156 PRO 156 261 261 PRO PRO A . n 
A 1 157 VAL 157 262 262 VAL VAL A . n 
A 1 158 LEU 158 263 263 LEU LEU A . n 
A 1 159 ILE 159 264 264 ILE ILE A . n 
A 1 160 ARG 160 265 265 ARG ARG A . n 
A 1 161 GLU 161 266 266 GLU GLU A . n 
A 1 162 ILE 162 267 267 ILE ILE A . n 
A 1 163 THR 163 268 268 THR THR A . n 
A 1 164 ARG 164 269 269 ARG ARG A . n 
A 1 165 ARG 165 270 270 ARG ARG A . n 
A 1 166 VAL 166 271 271 VAL VAL A . n 
A 1 167 HIS 167 272 272 HIS HIS A . n 
A 1 168 LEU 168 273 273 LEU LEU A . n 
A 1 169 GLU 169 274 274 GLU GLU A . n 
A 1 170 GLY 170 275 275 GLY GLY A . n 
A 1 171 ILE 171 276 276 ILE ILE A . n 
A 1 172 PHE 172 277 277 PHE PHE A . n 
A 1 173 GLN 173 278 278 GLN GLN A . n 
A 1 174 ALA 174 279 279 ALA ALA A . n 
A 1 175 VAL 175 280 280 VAL VAL A . n 
A 1 176 TYR 176 281 281 TYR TYR A . n 
A 1 177 THR 177 282 282 THR THR A . n 
A 1 178 ALA 178 283 283 ALA ALA A . n 
A 1 179 GLY 179 284 284 GLY GLY A . n 
A 1 180 VAL 180 285 285 VAL VAL A . n 
A 1 181 VAL 181 286 286 VAL VAL A . n 
A 1 182 LEU 182 287 287 LEU LEU A . n 
A 1 183 PRO 183 288 288 PRO PRO A . n 
A 1 184 LYS 184 289 289 LYS LYS A . n 
A 1 185 PRO 185 290 290 PRO PRO A . n 
A 1 186 VAL 186 291 291 VAL VAL A . n 
A 1 187 GLY 187 292 292 GLY GLY A . n 
A 1 188 THR 188 293 293 THR THR A . n 
A 1 189 CYS 189 294 294 CYS CYS A . n 
A 1 190 ARG 190 295 295 ARG ARG A . n 
A 1 191 TYR 191 296 296 TYR TYR A . n 
A 1 192 TRP 192 297 297 TRP TRP A . n 
A 1 193 HIS 193 298 298 HIS HIS A . n 
A 1 194 ARG 194 299 299 ARG ARG A . n 
A 1 195 SER 195 300 300 SER SER A . n 
A 1 196 LEU 196 301 301 LEU LEU A . n 
A 1 197 ASN 197 302 302 ASN ASN A . n 
A 1 198 PRO 198 303 303 PRO PRO A . n 
A 1 199 ARG 199 304 304 ARG ARG A . n 
A 1 200 LYS 200 305 305 LYS LYS A . n 
A 1 201 LEU 201 306 306 LEU LEU A . n 
A 1 202 ILE 202 307 307 ILE ILE A . n 
A 1 203 GLU 203 308 308 GLU GLU A . n 
A 1 204 VAL 204 309 309 VAL VAL A . n 
A 1 205 LYS 205 310 310 LYS LYS A . n 
A 1 206 PHE 206 311 311 PHE PHE A . n 
A 1 207 SER 207 312 312 SER SER A . n 
A 1 208 HIS 208 313 313 HIS HIS A . n 
A 1 209 LEU 209 314 314 LEU LEU A . n 
A 1 210 SER 210 315 315 SER SER A . n 
A 1 211 ARG 211 316 316 ARG ARG A . n 
A 1 212 ASN 212 317 317 ASN ASN A . n 
A 1 213 MET 213 318 318 MET MET A . n 
A 1 214 THR 214 319 319 THR THR A . n 
A 1 215 MET 215 320 320 MET MET A . n 
A 1 216 GLN 216 321 321 GLN GLN A . n 
A 1 217 ARG 217 322 322 ARG ARG A . n 
A 1 218 THR 218 323 323 THR THR A . n 
A 1 219 MET 219 324 324 MET MET A . n 
A 1 220 LYS 220 325 325 LYS LYS A . n 
A 1 221 LEU 221 326 326 LEU LEU A . n 
A 1 222 TYR 222 327 327 TYR TYR A . n 
A 1 223 ARG 223 328 328 ARG ARG A . n 
A 1 224 LEU 224 329 329 LEU LEU A . n 
A 1 225 PRO 225 330 330 PRO PRO A . n 
A 1 226 GLU 226 331 331 GLU GLU A . n 
A 1 227 THR 227 332 332 THR THR A . n 
A 1 228 PRO 228 333 333 PRO PRO A . n 
A 1 229 LYS 229 334 334 LYS LYS A . n 
A 1 230 THR 230 335 335 THR THR A . n 
A 1 231 ALA 231 336 336 ALA ALA A . n 
A 1 232 GLY 232 337 337 GLY GLY A . n 
A 1 233 LEU 233 338 338 LEU LEU A . n 
A 1 234 ARG 234 339 339 ARG ARG A . n 
A 1 235 PRO 235 340 340 PRO PRO A . n 
A 1 236 MET 236 341 341 MET MET A . n 
A 1 237 GLU 237 342 342 GLU GLU A . n 
A 1 238 THR 238 343 343 THR THR A . n 
A 1 239 LYS 239 344 344 LYS LYS A . n 
A 1 240 ASP 240 345 345 ASP ASP A . n 
A 1 241 ILE 241 346 346 ILE ILE A . n 
A 1 242 PRO 242 347 347 PRO PRO A . n 
A 1 243 VAL 243 348 348 VAL VAL A . n 
A 1 244 VAL 244 349 349 VAL VAL A . n 
A 1 245 HIS 245 350 350 HIS HIS A . n 
A 1 246 GLN 246 351 351 GLN GLN A . n 
A 1 247 LEU 247 352 352 LEU LEU A . n 
A 1 248 LEU 248 353 353 LEU LEU A . n 
A 1 249 THR 249 354 354 THR THR A . n 
A 1 250 ARG 250 355 355 ARG ARG A . n 
A 1 251 TYR 251 356 356 TYR TYR A . n 
A 1 252 LEU 252 357 357 LEU LEU A . n 
A 1 253 LYS 253 358 358 LYS LYS A . n 
A 1 254 GLN 254 359 359 GLN GLN A . n 
A 1 255 PHE 255 360 360 PHE PHE A . n 
A 1 256 HIS 256 361 361 HIS HIS A . n 
A 1 257 LEU 257 362 362 LEU LEU A . n 
A 1 258 THR 258 363 363 THR THR A . n 
A 1 259 PRO 259 364 364 PRO PRO A . n 
A 1 260 VAL 260 365 365 VAL VAL A . n 
A 1 261 MET 261 366 366 MET MET A . n 
A 1 262 SER 262 367 367 SER SER A . n 
A 1 263 GLN 263 368 368 GLN GLN A . n 
A 1 264 GLU 264 369 369 GLU GLU A . n 
A 1 265 GLU 265 370 370 GLU GLU A . n 
A 1 266 VAL 266 371 371 VAL VAL A . n 
A 1 267 GLU 267 372 372 GLU GLU A . n 
A 1 268 HIS 268 373 373 HIS HIS A . n 
A 1 269 TRP 269 374 374 TRP TRP A . n 
A 1 270 PHE 270 375 375 PHE PHE A . n 
A 1 271 TYR 271 376 376 TYR TYR A . n 
A 1 272 PRO 272 377 377 PRO PRO A . n 
A 1 273 GLN 273 378 378 GLN GLN A . n 
A 1 274 GLU 274 379 379 GLU GLU A . n 
A 1 275 ASN 275 380 380 ASN ASN A . n 
A 1 276 ILE 276 381 381 ILE ILE A . n 
A 1 277 ILE 277 382 382 ILE ILE A . n 
A 1 278 ASP 278 383 383 ASP ASP A . n 
A 1 279 THR 279 384 384 THR THR A . n 
A 1 280 PHE 280 385 385 PHE PHE A . n 
A 1 281 VAL 281 386 386 VAL VAL A . n 
A 1 282 VAL 282 387 387 VAL VAL A . n 
A 1 283 GLU 283 388 388 GLU GLU A . n 
A 1 284 ASN 284 389 389 ASN ASN A . n 
A 1 285 ALA 285 390 390 ALA ALA A . n 
A 1 286 ASN 286 391 391 ASN ASN A . n 
A 1 287 GLY 287 392 392 GLY GLY A . n 
A 1 288 GLU 288 393 393 GLU GLU A . n 
A 1 289 VAL 289 394 394 VAL VAL A . n 
A 1 290 THR 290 395 395 THR THR A . n 
A 1 291 ASP 291 396 396 ASP ASP A . n 
A 1 292 PHE 292 397 397 PHE PHE A . n 
A 1 293 LEU 293 398 398 LEU LEU A . n 
A 1 294 SER 294 399 399 SER SER A . n 
A 1 295 PHE 295 400 400 PHE PHE A . n 
A 1 296 TYR 296 401 401 TYR TYR A . n 
A 1 297 THR 297 402 402 THR THR A . n 
A 1 298 LEU 298 403 403 LEU LEU A . n 
A 1 299 PRO 299 404 404 PRO PRO A . n 
A 1 300 SER 300 405 405 SER SER A . n 
A 1 301 THR 301 406 406 THR THR A . n 
A 1 302 ILE 302 407 407 ILE ILE A . n 
A 1 303 MET 303 408 408 MET MET A . n 
A 1 304 ASN 304 409 409 ASN ASN A . n 
A 1 305 HIS 305 410 410 HIS HIS A . n 
A 1 306 PRO 306 411 411 PRO PRO A . n 
A 1 307 THR 307 412 412 THR THR A . n 
A 1 308 HIS 308 413 413 HIS HIS A . n 
A 1 309 LYS 309 414 414 LYS LYS A . n 
A 1 310 SER 310 415 415 SER SER A . n 
A 1 311 LEU 311 416 416 LEU LEU A . n 
A 1 312 LYS 312 417 417 LYS LYS A . n 
A 1 313 ALA 313 418 418 ALA ALA A . n 
A 1 314 ALA 314 419 419 ALA ALA A . n 
A 1 315 TYR 315 420 420 TYR TYR A . n 
A 1 316 SER 316 421 421 SER SER A . n 
A 1 317 PHE 317 422 422 PHE PHE A . n 
A 1 318 TYR 318 423 423 TYR TYR A . n 
A 1 319 ASN 319 424 424 ASN ASN A . n 
A 1 320 VAL 320 425 425 VAL VAL A . n 
A 1 321 HIS 321 426 426 HIS HIS A . n 
A 1 322 THR 322 427 427 THR THR A . n 
A 1 323 GLN 323 428 428 GLN GLN A . n 
A 1 324 THR 324 429 429 THR THR A . n 
A 1 325 PRO 325 430 430 PRO PRO A . n 
A 1 326 LEU 326 431 431 LEU LEU A . n 
A 1 327 LEU 327 432 432 LEU LEU A . n 
A 1 328 ASP 328 433 433 ASP ASP A . n 
A 1 329 LEU 329 434 434 LEU LEU A . n 
A 1 330 MET 330 435 435 MET MET A . n 
A 1 331 SER 331 436 436 SER SER A . n 
A 1 332 ASP 332 437 437 ASP ASP A . n 
A 1 333 ALA 333 438 438 ALA ALA A . n 
A 1 334 LEU 334 439 439 LEU LEU A . n 
A 1 335 VAL 335 440 440 VAL VAL A . n 
A 1 336 LEU 336 441 441 LEU LEU A . n 
A 1 337 ALA 337 442 442 ALA ALA A . n 
A 1 338 LYS 338 443 443 LYS LYS A . n 
A 1 339 MET 339 444 444 MET MET A . n 
A 1 340 LYS 340 445 445 LYS LYS A . n 
A 1 341 GLY 341 446 446 GLY GLY A . n 
A 1 342 PHE 342 447 447 PHE PHE A . n 
A 1 343 ASP 343 448 448 ASP ASP A . n 
A 1 344 VAL 344 449 449 VAL VAL A . n 
A 1 345 PHE 345 450 450 PHE PHE A . n 
A 1 346 ASN 346 451 451 ASN ASN A . n 
A 1 347 ALA 347 452 452 ALA ALA A . n 
A 1 348 LEU 348 453 453 LEU LEU A . n 
A 1 349 ASP 349 454 454 ASP ASP A . n 
A 1 350 LEU 350 455 455 LEU LEU A . n 
A 1 351 MET 351 456 456 MET MET A . n 
A 1 352 GLU 352 457 457 GLU GLU A . n 
A 1 353 ASN 353 458 458 ASN ASN A . n 
A 1 354 LYS 354 459 459 LYS LYS A . n 
A 1 355 THR 355 460 460 THR THR A . n 
A 1 356 PHE 356 461 461 PHE PHE A . n 
A 1 357 LEU 357 462 462 LEU LEU A . n 
A 1 358 GLU 358 463 463 GLU GLU A . n 
A 1 359 LYS 359 464 464 LYS LYS A . n 
A 1 360 LEU 360 465 465 LEU LEU A . n 
A 1 361 LYS 361 466 466 LYS LYS A . n 
A 1 362 PHE 362 467 467 PHE PHE A . n 
A 1 363 GLY 363 468 468 GLY GLY A . n 
A 1 364 ILE 364 469 469 ILE ILE A . n 
A 1 365 GLY 365 470 470 GLY GLY A . n 
A 1 366 ASP 366 471 471 ASP ASP A . n 
A 1 367 GLY 367 472 472 GLY GLY A . n 
A 1 368 ASN 368 473 473 ASN ASN A . n 
A 1 369 LEU 369 474 474 LEU LEU A . n 
A 1 370 GLN 370 475 475 GLN GLN A . n 
A 1 371 TYR 371 476 476 TYR TYR A . n 
A 1 372 TYR 372 477 477 TYR TYR A . n 
A 1 373 LEU 373 478 478 LEU LEU A . n 
A 1 374 TYR 374 479 479 TYR TYR A . n 
A 1 375 ASN 375 480 480 ASN ASN A . n 
A 1 376 TRP 376 481 481 TRP TRP A . n 
A 1 377 LYS 377 482 482 LYS LYS A . n 
A 1 378 CYS 378 483 483 CYS CYS A . n 
A 1 379 PRO 379 484 484 PRO PRO A . n 
A 1 380 SER 380 485 485 SER SER A . n 
A 1 381 MET 381 486 486 MET MET A . n 
A 1 382 GLY 382 487 487 GLY GLY A . n 
A 1 383 ALA 383 488 488 ALA ALA A . n 
A 1 384 GLU 384 489 489 GLU GLU A . n 
A 1 385 LYS 385 490 490 LYS LYS A . n 
A 1 386 VAL 386 491 491 VAL VAL A . n 
A 1 387 GLY 387 492 492 GLY GLY A . n 
A 1 388 LEU 388 493 493 LEU LEU A . n 
A 1 389 VAL 389 494 494 VAL VAL A . n 
A 1 390 LEU 390 495 495 LEU LEU A . n 
A 1 391 GLN 391 496 496 GLN GLN A . n 
B 1 1   GLY 1   106 ?   ?   ?   B . n 
B 1 2   PRO 2   107 ?   ?   ?   B . n 
B 1 3   HIS 3   108 ?   ?   ?   B . n 
B 1 4   MET 4   109 ?   ?   ?   B . n 
B 1 5   GLU 5   110 ?   ?   ?   B . n 
B 1 6   GLU 6   111 ?   ?   ?   B . n 
B 1 7   ALA 7   112 ?   ?   ?   B . n 
B 1 8   SER 8   113 ?   ?   ?   B . n 
B 1 9   LYS 9   114 ?   ?   ?   B . n 
B 1 10  ARG 10  115 115 ARG ARG B . n 
B 1 11  SER 11  116 116 SER SER B . n 
B 1 12  TYR 12  117 117 TYR TYR B . n 
B 1 13  GLN 13  118 118 GLN GLN B . n 
B 1 14  PHE 14  119 119 PHE PHE B . n 
B 1 15  TRP 15  120 120 TRP TRP B . n 
B 1 16  ASP 16  121 121 ASP ASP B . n 
B 1 17  THR 17  122 122 THR THR B . n 
B 1 18  GLN 18  123 123 GLN GLN B . n 
B 1 19  PRO 19  124 124 PRO PRO B . n 
B 1 20  VAL 20  125 125 VAL VAL B . n 
B 1 21  PRO 21  126 126 PRO PRO B . n 
B 1 22  LYS 22  127 127 LYS LYS B . n 
B 1 23  LEU 23  128 128 LEU LEU B . n 
B 1 24  GLY 24  129 129 GLY GLY B . n 
B 1 25  GLU 25  130 130 GLU GLU B . n 
B 1 26  VAL 26  131 131 VAL VAL B . n 
B 1 27  VAL 27  132 132 VAL VAL B . n 
B 1 28  ASN 28  133 133 ASN ASN B . n 
B 1 29  THR 29  134 134 THR THR B . n 
B 1 30  HIS 30  135 135 HIS HIS B . n 
B 1 31  GLY 31  136 136 GLY GLY B . n 
B 1 32  PRO 32  137 137 PRO PRO B . n 
B 1 33  VAL 33  138 138 VAL VAL B . n 
B 1 34  GLU 34  139 139 GLU GLU B . n 
B 1 35  PRO 35  140 140 PRO PRO B . n 
B 1 36  ASP 36  141 141 ASP ASP B . n 
B 1 37  LYS 37  142 142 LYS LYS B . n 
B 1 38  ASP 38  143 143 ASP ASP B . n 
B 1 39  ASN 39  144 144 ASN ASN B . n 
B 1 40  ILE 40  145 145 ILE ILE B . n 
B 1 41  ARG 41  146 146 ARG ARG B . n 
B 1 42  GLN 42  147 147 GLN GLN B . n 
B 1 43  GLU 43  148 148 GLU GLU B . n 
B 1 44  PRO 44  149 149 PRO PRO B . n 
B 1 45  TYR 45  150 150 TYR TYR B . n 
B 1 46  THR 46  151 151 THR THR B . n 
B 1 47  LEU 47  152 152 LEU LEU B . n 
B 1 48  PRO 48  153 153 PRO PRO B . n 
B 1 49  GLN 49  154 154 GLN GLN B . n 
B 1 50  GLY 50  155 155 GLY GLY B . n 
B 1 51  PHE 51  156 156 PHE PHE B . n 
B 1 52  THR 52  157 157 THR THR B . n 
B 1 53  TRP 53  158 158 TRP TRP B . n 
B 1 54  ASP 54  159 159 ASP ASP B . n 
B 1 55  ALA 55  160 160 ALA ALA B . n 
B 1 56  LEU 56  161 161 LEU LEU B . n 
B 1 57  ASP 57  162 162 ASP ASP B . n 
B 1 58  LEU 58  163 163 LEU LEU B . n 
B 1 59  GLY 59  164 164 GLY GLY B . n 
B 1 60  ASP 60  165 165 ASP ASP B . n 
B 1 61  ARG 61  166 166 ARG ARG B . n 
B 1 62  GLY 62  167 167 GLY GLY B . n 
B 1 63  VAL 63  168 168 VAL VAL B . n 
B 1 64  LEU 64  169 169 LEU LEU B . n 
B 1 65  LYS 65  170 170 LYS LYS B . n 
B 1 66  GLU 66  171 171 GLU GLU B . n 
B 1 67  LEU 67  172 172 LEU LEU B . n 
B 1 68  TYR 68  173 173 TYR TYR B . n 
B 1 69  THR 69  174 174 THR THR B . n 
B 1 70  LEU 70  175 175 LEU LEU B . n 
B 1 71  LEU 71  176 176 LEU LEU B . n 
B 1 72  ASN 72  177 177 ASN ASN B . n 
B 1 73  GLU 73  178 178 GLU GLU B . n 
B 1 74  ASN 74  179 179 ASN ASN B . n 
B 1 75  TYR 75  180 180 TYR TYR B . n 
B 1 76  VAL 76  181 181 VAL VAL B . n 
B 1 77  GLU 77  182 182 GLU GLU B . n 
B 1 78  ASP 78  183 183 ASP ASP B . n 
B 1 79  ASP 79  184 184 ASP ASP B . n 
B 1 80  ASP 80  185 185 ASP ASP B . n 
B 1 81  ASN 81  186 186 ASN ASN B . n 
B 1 82  MET 82  187 187 MET MET B . n 
B 1 83  PHE 83  188 188 PHE PHE B . n 
B 1 84  ARG 84  189 189 ARG ARG B . n 
B 1 85  PHE 85  190 190 PHE PHE B . n 
B 1 86  ASP 86  191 191 ASP ASP B . n 
B 1 87  TYR 87  192 192 TYR TYR B . n 
B 1 88  SER 88  193 193 SER SER B . n 
B 1 89  PRO 89  194 194 PRO PRO B . n 
B 1 90  GLU 90  195 195 GLU GLU B . n 
B 1 91  PHE 91  196 196 PHE PHE B . n 
B 1 92  LEU 92  197 197 LEU LEU B . n 
B 1 93  LEU 93  198 198 LEU LEU B . n 
B 1 94  TRP 94  199 199 TRP TRP B . n 
B 1 95  ALA 95  200 200 ALA ALA B . n 
B 1 96  LEU 96  201 201 LEU LEU B . n 
B 1 97  ARG 97  202 202 ARG ARG B . n 
B 1 98  PRO 98  203 203 PRO PRO B . n 
B 1 99  PRO 99  204 204 PRO PRO B . n 
B 1 100 GLY 100 205 205 GLY GLY B . n 
B 1 101 TRP 101 206 206 TRP TRP B . n 
B 1 102 LEU 102 207 207 LEU LEU B . n 
B 1 103 PRO 103 208 208 PRO PRO B . n 
B 1 104 GLN 104 209 209 GLN GLN B . n 
B 1 105 TRP 105 210 210 TRP TRP B . n 
B 1 106 HIS 106 211 211 HIS HIS B . n 
B 1 107 CYS 107 212 212 CYS CYS B . n 
B 1 108 GLY 108 213 213 GLY GLY B . n 
B 1 109 VAL 109 214 214 VAL VAL B . n 
B 1 110 ARG 110 215 215 ARG ARG B . n 
B 1 111 VAL 111 216 216 VAL VAL B . n 
B 1 112 VAL 112 217 217 VAL VAL B . n 
B 1 113 SER 113 218 218 SER SER B . n 
B 1 114 SER 114 219 219 SER SER B . n 
B 1 115 ARG 115 220 220 ARG ARG B . n 
B 1 116 LYS 116 221 221 LYS LYS B . n 
B 1 117 LEU 117 222 222 LEU LEU B . n 
B 1 118 VAL 118 223 223 VAL VAL B . n 
B 1 119 GLY 119 224 224 GLY GLY B . n 
B 1 120 PHE 120 225 225 PHE PHE B . n 
B 1 121 ILE 121 226 226 ILE ILE B . n 
B 1 122 SER 122 227 227 SER SER B . n 
B 1 123 ALA 123 228 228 ALA ALA B . n 
B 1 124 ILE 124 229 229 ILE ILE B . n 
B 1 125 PRO 125 230 230 PRO PRO B . n 
B 1 126 ALA 126 231 231 ALA ALA B . n 
B 1 127 ASN 127 232 232 ASN ASN B . n 
B 1 128 ILE 128 233 233 ILE ILE B . n 
B 1 129 HIS 129 234 234 HIS HIS B . n 
B 1 130 ILE 130 235 235 ILE ILE B . n 
B 1 131 TYR 131 236 236 TYR TYR B . n 
B 1 132 ASP 132 237 237 ASP ASP B . n 
B 1 133 THR 133 238 238 THR THR B . n 
B 1 134 GLU 134 239 239 GLU GLU B . n 
B 1 135 LYS 135 240 240 LYS LYS B . n 
B 1 136 LYS 136 241 241 LYS LYS B . n 
B 1 137 MET 137 242 242 MET MET B . n 
B 1 138 VAL 138 243 243 VAL VAL B . n 
B 1 139 GLU 139 244 244 GLU GLU B . n 
B 1 140 ILE 140 245 245 ILE ILE B . n 
B 1 141 ASN 141 246 246 ASN ASN B . n 
B 1 142 PHE 142 247 247 PHE PHE B . n 
B 1 143 LEU 143 248 248 LEU LEU B . n 
B 1 144 CYS 144 249 249 CYS CYS B . n 
B 1 145 VAL 145 250 250 VAL VAL B . n 
B 1 146 HIS 146 251 251 HIS HIS B . n 
B 1 147 LYS 147 252 252 LYS LYS B . n 
B 1 148 LYS 148 253 253 LYS LYS B . n 
B 1 149 LEU 149 254 254 LEU LEU B . n 
B 1 150 ARG 150 255 255 ARG ARG B . n 
B 1 151 SER 151 256 256 SER SER B . n 
B 1 152 LYS 152 257 257 LYS LYS B . n 
B 1 153 ARG 153 258 258 ARG ARG B . n 
B 1 154 VAL 154 259 259 VAL VAL B . n 
B 1 155 ALA 155 260 260 ALA ALA B . n 
B 1 156 PRO 156 261 261 PRO PRO B . n 
B 1 157 VAL 157 262 262 VAL VAL B . n 
B 1 158 LEU 158 263 263 LEU LEU B . n 
B 1 159 ILE 159 264 264 ILE ILE B . n 
B 1 160 ARG 160 265 265 ARG ARG B . n 
B 1 161 GLU 161 266 266 GLU GLU B . n 
B 1 162 ILE 162 267 267 ILE ILE B . n 
B 1 163 THR 163 268 268 THR THR B . n 
B 1 164 ARG 164 269 269 ARG ARG B . n 
B 1 165 ARG 165 270 270 ARG ARG B . n 
B 1 166 VAL 166 271 271 VAL VAL B . n 
B 1 167 HIS 167 272 272 HIS HIS B . n 
B 1 168 LEU 168 273 273 LEU LEU B . n 
B 1 169 GLU 169 274 274 GLU GLU B . n 
B 1 170 GLY 170 275 275 GLY GLY B . n 
B 1 171 ILE 171 276 276 ILE ILE B . n 
B 1 172 PHE 172 277 277 PHE PHE B . n 
B 1 173 GLN 173 278 278 GLN GLN B . n 
B 1 174 ALA 174 279 279 ALA ALA B . n 
B 1 175 VAL 175 280 280 VAL VAL B . n 
B 1 176 TYR 176 281 281 TYR TYR B . n 
B 1 177 THR 177 282 282 THR THR B . n 
B 1 178 ALA 178 283 283 ALA ALA B . n 
B 1 179 GLY 179 284 284 GLY GLY B . n 
B 1 180 VAL 180 285 285 VAL VAL B . n 
B 1 181 VAL 181 286 286 VAL VAL B . n 
B 1 182 LEU 182 287 287 LEU LEU B . n 
B 1 183 PRO 183 288 288 PRO PRO B . n 
B 1 184 LYS 184 289 289 LYS LYS B . n 
B 1 185 PRO 185 290 290 PRO PRO B . n 
B 1 186 VAL 186 291 291 VAL VAL B . n 
B 1 187 GLY 187 292 292 GLY GLY B . n 
B 1 188 THR 188 293 293 THR THR B . n 
B 1 189 CYS 189 294 294 CYS CYS B . n 
B 1 190 ARG 190 295 295 ARG ARG B . n 
B 1 191 TYR 191 296 296 TYR TYR B . n 
B 1 192 TRP 192 297 297 TRP TRP B . n 
B 1 193 HIS 193 298 298 HIS HIS B . n 
B 1 194 ARG 194 299 299 ARG ARG B . n 
B 1 195 SER 195 300 300 SER SER B . n 
B 1 196 LEU 196 301 301 LEU LEU B . n 
B 1 197 ASN 197 302 302 ASN ASN B . n 
B 1 198 PRO 198 303 303 PRO PRO B . n 
B 1 199 ARG 199 304 304 ARG ARG B . n 
B 1 200 LYS 200 305 305 LYS LYS B . n 
B 1 201 LEU 201 306 306 LEU LEU B . n 
B 1 202 ILE 202 307 307 ILE ILE B . n 
B 1 203 GLU 203 308 308 GLU GLU B . n 
B 1 204 VAL 204 309 309 VAL VAL B . n 
B 1 205 LYS 205 310 310 LYS LYS B . n 
B 1 206 PHE 206 311 311 PHE PHE B . n 
B 1 207 SER 207 312 312 SER SER B . n 
B 1 208 HIS 208 313 313 HIS HIS B . n 
B 1 209 LEU 209 314 314 LEU LEU B . n 
B 1 210 SER 210 315 315 SER SER B . n 
B 1 211 ARG 211 316 316 ARG ARG B . n 
B 1 212 ASN 212 317 317 ASN ASN B . n 
B 1 213 MET 213 318 318 MET MET B . n 
B 1 214 THR 214 319 319 THR THR B . n 
B 1 215 MET 215 320 320 MET MET B . n 
B 1 216 GLN 216 321 321 GLN GLN B . n 
B 1 217 ARG 217 322 322 ARG ARG B . n 
B 1 218 THR 218 323 323 THR THR B . n 
B 1 219 MET 219 324 324 MET MET B . n 
B 1 220 LYS 220 325 325 LYS LYS B . n 
B 1 221 LEU 221 326 326 LEU LEU B . n 
B 1 222 TYR 222 327 327 TYR TYR B . n 
B 1 223 ARG 223 328 328 ARG ARG B . n 
B 1 224 LEU 224 329 329 LEU LEU B . n 
B 1 225 PRO 225 330 330 PRO PRO B . n 
B 1 226 GLU 226 331 331 GLU GLU B . n 
B 1 227 THR 227 332 332 THR THR B . n 
B 1 228 PRO 228 333 333 PRO PRO B . n 
B 1 229 LYS 229 334 334 LYS LYS B . n 
B 1 230 THR 230 335 335 THR THR B . n 
B 1 231 ALA 231 336 336 ALA ALA B . n 
B 1 232 GLY 232 337 337 GLY GLY B . n 
B 1 233 LEU 233 338 338 LEU LEU B . n 
B 1 234 ARG 234 339 339 ARG ARG B . n 
B 1 235 PRO 235 340 340 PRO PRO B . n 
B 1 236 MET 236 341 341 MET MET B . n 
B 1 237 GLU 237 342 342 GLU GLU B . n 
B 1 238 THR 238 343 343 THR THR B . n 
B 1 239 LYS 239 344 344 LYS LYS B . n 
B 1 240 ASP 240 345 345 ASP ASP B . n 
B 1 241 ILE 241 346 346 ILE ILE B . n 
B 1 242 PRO 242 347 347 PRO PRO B . n 
B 1 243 VAL 243 348 348 VAL VAL B . n 
B 1 244 VAL 244 349 349 VAL VAL B . n 
B 1 245 HIS 245 350 350 HIS HIS B . n 
B 1 246 GLN 246 351 351 GLN GLN B . n 
B 1 247 LEU 247 352 352 LEU LEU B . n 
B 1 248 LEU 248 353 353 LEU LEU B . n 
B 1 249 THR 249 354 354 THR THR B . n 
B 1 250 ARG 250 355 355 ARG ARG B . n 
B 1 251 TYR 251 356 356 TYR TYR B . n 
B 1 252 LEU 252 357 357 LEU LEU B . n 
B 1 253 LYS 253 358 358 LYS LYS B . n 
B 1 254 GLN 254 359 359 GLN GLN B . n 
B 1 255 PHE 255 360 360 PHE PHE B . n 
B 1 256 HIS 256 361 361 HIS HIS B . n 
B 1 257 LEU 257 362 362 LEU LEU B . n 
B 1 258 THR 258 363 363 THR THR B . n 
B 1 259 PRO 259 364 364 PRO PRO B . n 
B 1 260 VAL 260 365 365 VAL VAL B . n 
B 1 261 MET 261 366 366 MET MET B . n 
B 1 262 SER 262 367 367 SER SER B . n 
B 1 263 GLN 263 368 368 GLN GLN B . n 
B 1 264 GLU 264 369 369 GLU GLU B . n 
B 1 265 GLU 265 370 370 GLU GLU B . n 
B 1 266 VAL 266 371 371 VAL VAL B . n 
B 1 267 GLU 267 372 372 GLU GLU B . n 
B 1 268 HIS 268 373 373 HIS HIS B . n 
B 1 269 TRP 269 374 374 TRP TRP B . n 
B 1 270 PHE 270 375 375 PHE PHE B . n 
B 1 271 TYR 271 376 376 TYR TYR B . n 
B 1 272 PRO 272 377 377 PRO PRO B . n 
B 1 273 GLN 273 378 378 GLN GLN B . n 
B 1 274 GLU 274 379 379 GLU GLU B . n 
B 1 275 ASN 275 380 380 ASN ASN B . n 
B 1 276 ILE 276 381 381 ILE ILE B . n 
B 1 277 ILE 277 382 382 ILE ILE B . n 
B 1 278 ASP 278 383 383 ASP ASP B . n 
B 1 279 THR 279 384 384 THR THR B . n 
B 1 280 PHE 280 385 385 PHE PHE B . n 
B 1 281 VAL 281 386 386 VAL VAL B . n 
B 1 282 VAL 282 387 387 VAL VAL B . n 
B 1 283 GLU 283 388 388 GLU GLU B . n 
B 1 284 ASN 284 389 389 ASN ASN B . n 
B 1 285 ALA 285 390 390 ALA ALA B . n 
B 1 286 ASN 286 391 391 ASN ASN B . n 
B 1 287 GLY 287 392 392 GLY GLY B . n 
B 1 288 GLU 288 393 393 GLU GLU B . n 
B 1 289 VAL 289 394 394 VAL VAL B . n 
B 1 290 THR 290 395 395 THR THR B . n 
B 1 291 ASP 291 396 396 ASP ASP B . n 
B 1 292 PHE 292 397 397 PHE PHE B . n 
B 1 293 LEU 293 398 398 LEU LEU B . n 
B 1 294 SER 294 399 399 SER SER B . n 
B 1 295 PHE 295 400 400 PHE PHE B . n 
B 1 296 TYR 296 401 401 TYR TYR B . n 
B 1 297 THR 297 402 402 THR THR B . n 
B 1 298 LEU 298 403 403 LEU LEU B . n 
B 1 299 PRO 299 404 404 PRO PRO B . n 
B 1 300 SER 300 405 405 SER SER B . n 
B 1 301 THR 301 406 406 THR THR B . n 
B 1 302 ILE 302 407 407 ILE ILE B . n 
B 1 303 MET 303 408 408 MET MET B . n 
B 1 304 ASN 304 409 409 ASN ASN B . n 
B 1 305 HIS 305 410 410 HIS HIS B . n 
B 1 306 PRO 306 411 411 PRO PRO B . n 
B 1 307 THR 307 412 412 THR THR B . n 
B 1 308 HIS 308 413 413 HIS HIS B . n 
B 1 309 LYS 309 414 414 LYS LYS B . n 
B 1 310 SER 310 415 415 SER SER B . n 
B 1 311 LEU 311 416 416 LEU LEU B . n 
B 1 312 LYS 312 417 417 LYS LYS B . n 
B 1 313 ALA 313 418 418 ALA ALA B . n 
B 1 314 ALA 314 419 419 ALA ALA B . n 
B 1 315 TYR 315 420 420 TYR TYR B . n 
B 1 316 SER 316 421 421 SER SER B . n 
B 1 317 PHE 317 422 422 PHE PHE B . n 
B 1 318 TYR 318 423 423 TYR TYR B . n 
B 1 319 ASN 319 424 424 ASN ASN B . n 
B 1 320 VAL 320 425 425 VAL VAL B . n 
B 1 321 HIS 321 426 426 HIS HIS B . n 
B 1 322 THR 322 427 427 THR THR B . n 
B 1 323 GLN 323 428 428 GLN GLN B . n 
B 1 324 THR 324 429 429 THR THR B . n 
B 1 325 PRO 325 430 430 PRO PRO B . n 
B 1 326 LEU 326 431 431 LEU LEU B . n 
B 1 327 LEU 327 432 432 LEU LEU B . n 
B 1 328 ASP 328 433 433 ASP ASP B . n 
B 1 329 LEU 329 434 434 LEU LEU B . n 
B 1 330 MET 330 435 435 MET MET B . n 
B 1 331 SER 331 436 436 SER SER B . n 
B 1 332 ASP 332 437 437 ASP ASP B . n 
B 1 333 ALA 333 438 438 ALA ALA B . n 
B 1 334 LEU 334 439 439 LEU LEU B . n 
B 1 335 VAL 335 440 440 VAL VAL B . n 
B 1 336 LEU 336 441 441 LEU LEU B . n 
B 1 337 ALA 337 442 442 ALA ALA B . n 
B 1 338 LYS 338 443 443 LYS LYS B . n 
B 1 339 MET 339 444 444 MET MET B . n 
B 1 340 LYS 340 445 445 LYS LYS B . n 
B 1 341 GLY 341 446 446 GLY GLY B . n 
B 1 342 PHE 342 447 447 PHE PHE B . n 
B 1 343 ASP 343 448 448 ASP ASP B . n 
B 1 344 VAL 344 449 449 VAL VAL B . n 
B 1 345 PHE 345 450 450 PHE PHE B . n 
B 1 346 ASN 346 451 451 ASN ASN B . n 
B 1 347 ALA 347 452 452 ALA ALA B . n 
B 1 348 LEU 348 453 453 LEU LEU B . n 
B 1 349 ASP 349 454 454 ASP ASP B . n 
B 1 350 LEU 350 455 455 LEU LEU B . n 
B 1 351 MET 351 456 456 MET MET B . n 
B 1 352 GLU 352 457 457 GLU GLU B . n 
B 1 353 ASN 353 458 458 ASN ASN B . n 
B 1 354 LYS 354 459 459 LYS LYS B . n 
B 1 355 THR 355 460 460 THR THR B . n 
B 1 356 PHE 356 461 461 PHE PHE B . n 
B 1 357 LEU 357 462 462 LEU LEU B . n 
B 1 358 GLU 358 463 463 GLU GLU B . n 
B 1 359 LYS 359 464 464 LYS LYS B . n 
B 1 360 LEU 360 465 465 LEU LEU B . n 
B 1 361 LYS 361 466 466 LYS LYS B . n 
B 1 362 PHE 362 467 467 PHE PHE B . n 
B 1 363 GLY 363 468 468 GLY GLY B . n 
B 1 364 ILE 364 469 469 ILE ILE B . n 
B 1 365 GLY 365 470 470 GLY GLY B . n 
B 1 366 ASP 366 471 471 ASP ASP B . n 
B 1 367 GLY 367 472 472 GLY GLY B . n 
B 1 368 ASN 368 473 473 ASN ASN B . n 
B 1 369 LEU 369 474 474 LEU LEU B . n 
B 1 370 GLN 370 475 475 GLN GLN B . n 
B 1 371 TYR 371 476 476 TYR TYR B . n 
B 1 372 TYR 372 477 477 TYR TYR B . n 
B 1 373 LEU 373 478 478 LEU LEU B . n 
B 1 374 TYR 374 479 479 TYR TYR B . n 
B 1 375 ASN 375 480 480 ASN ASN B . n 
B 1 376 TRP 376 481 481 TRP TRP B . n 
B 1 377 LYS 377 482 482 LYS LYS B . n 
B 1 378 CYS 378 483 483 CYS CYS B . n 
B 1 379 PRO 379 484 484 PRO PRO B . n 
B 1 380 SER 380 485 485 SER SER B . n 
B 1 381 MET 381 486 486 MET MET B . n 
B 1 382 GLY 382 487 487 GLY GLY B . n 
B 1 383 ALA 383 488 488 ALA ALA B . n 
B 1 384 GLU 384 489 489 GLU GLU B . n 
B 1 385 LYS 385 490 490 LYS LYS B . n 
B 1 386 VAL 386 491 491 VAL VAL B . n 
B 1 387 GLY 387 492 492 GLY GLY B . n 
B 1 388 LEU 388 493 493 LEU LEU B . n 
B 1 389 VAL 389 494 494 VAL VAL B . n 
B 1 390 LEU 390 495 495 LEU LEU B . n 
B 1 391 GLN 391 496 496 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 MYA 1   2001 2001 MYA MYA A . 
D 3 PO4 1   2002 1    PO4 PO4 A . 
E 3 PO4 1   2003 2    PO4 PO4 A . 
F 3 PO4 1   2004 6    PO4 PO4 A . 
G 4 9M2 1   2005 1    9M2 159 A . 
H 5 MG  1   2006 1    MG  MG  A . 
I 6 GOL 1   2007 1    GOL GOL A . 
J 7 DMS 1   2008 1    DMS DMS A . 
K 2 MYA 1   2001 2001 MYA MYA B . 
L 3 PO4 1   2002 3    PO4 PO4 B . 
M 3 PO4 1   2003 4    PO4 PO4 B . 
N 3 PO4 1   2004 5    PO4 PO4 B . 
O 3 PO4 1   2005 8    PO4 PO4 B . 
P 3 PO4 1   2006 9    PO4 PO4 B . 
Q 4 9M2 1   2007 2    9M2 159 B . 
R 5 MG  1   2008 1    MG  MG  B . 
S 6 GOL 1   2009 2    GOL GOL B . 
T 6 GOL 1   2010 4    GOL GOL B . 
U 8 HOH 1   2101 857  HOH HOH A . 
U 8 HOH 2   2102 862  HOH HOH A . 
U 8 HOH 3   2103 881  HOH HOH A . 
U 8 HOH 4   2104 917  HOH HOH A . 
U 8 HOH 5   2105 1014 HOH HOH A . 
U 8 HOH 6   2106 284  HOH HOH A . 
U 8 HOH 7   2107 141  HOH HOH A . 
U 8 HOH 8   2108 433  HOH HOH A . 
U 8 HOH 9   2109 62   HOH HOH A . 
U 8 HOH 10  2110 732  HOH HOH A . 
U 8 HOH 11  2111 689  HOH HOH A . 
U 8 HOH 12  2112 436  HOH HOH A . 
U 8 HOH 13  2113 380  HOH HOH A . 
U 8 HOH 14  2114 924  HOH HOH A . 
U 8 HOH 15  2115 692  HOH HOH A . 
U 8 HOH 16  2116 336  HOH HOH A . 
U 8 HOH 17  2117 868  HOH HOH A . 
U 8 HOH 18  2118 735  HOH HOH A . 
U 8 HOH 19  2119 913  HOH HOH A . 
U 8 HOH 20  2120 668  HOH HOH A . 
U 8 HOH 21  2121 662  HOH HOH A . 
U 8 HOH 22  2122 339  HOH HOH A . 
U 8 HOH 23  2123 128  HOH HOH A . 
U 8 HOH 24  2124 634  HOH HOH A . 
U 8 HOH 25  2125 723  HOH HOH A . 
U 8 HOH 26  2126 9    HOH HOH A . 
U 8 HOH 27  2127 407  HOH HOH A . 
U 8 HOH 28  2128 774  HOH HOH A . 
U 8 HOH 29  2129 853  HOH HOH A . 
U 8 HOH 30  2130 244  HOH HOH A . 
U 8 HOH 31  2131 331  HOH HOH A . 
U 8 HOH 32  2132 585  HOH HOH A . 
U 8 HOH 33  2133 350  HOH HOH A . 
U 8 HOH 34  2134 656  HOH HOH A . 
U 8 HOH 35  2135 297  HOH HOH A . 
U 8 HOH 36  2136 787  HOH HOH A . 
U 8 HOH 37  2137 763  HOH HOH A . 
U 8 HOH 38  2138 29   HOH HOH A . 
U 8 HOH 39  2139 346  HOH HOH A . 
U 8 HOH 40  2140 964  HOH HOH A . 
U 8 HOH 41  2141 246  HOH HOH A . 
U 8 HOH 42  2142 942  HOH HOH A . 
U 8 HOH 43  2143 80   HOH HOH A . 
U 8 HOH 44  2144 729  HOH HOH A . 
U 8 HOH 45  2145 843  HOH HOH A . 
U 8 HOH 46  2146 30   HOH HOH A . 
U 8 HOH 47  2147 51   HOH HOH A . 
U 8 HOH 48  2148 210  HOH HOH A . 
U 8 HOH 49  2149 363  HOH HOH A . 
U 8 HOH 50  2150 282  HOH HOH A . 
U 8 HOH 51  2151 87   HOH HOH A . 
U 8 HOH 52  2152 619  HOH HOH A . 
U 8 HOH 53  2153 327  HOH HOH A . 
U 8 HOH 54  2154 275  HOH HOH A . 
U 8 HOH 55  2155 13   HOH HOH A . 
U 8 HOH 56  2156 101  HOH HOH A . 
U 8 HOH 57  2157 468  HOH HOH A . 
U 8 HOH 58  2158 291  HOH HOH A . 
U 8 HOH 59  2159 243  HOH HOH A . 
U 8 HOH 60  2160 758  HOH HOH A . 
U 8 HOH 61  2161 527  HOH HOH A . 
U 8 HOH 62  2162 189  HOH HOH A . 
U 8 HOH 63  2163 744  HOH HOH A . 
U 8 HOH 64  2164 164  HOH HOH A . 
U 8 HOH 65  2165 438  HOH HOH A . 
U 8 HOH 66  2166 107  HOH HOH A . 
U 8 HOH 67  2167 374  HOH HOH A . 
U 8 HOH 68  2168 132  HOH HOH A . 
U 8 HOH 69  2169 103  HOH HOH A . 
U 8 HOH 70  2170 665  HOH HOH A . 
U 8 HOH 71  2171 49   HOH HOH A . 
U 8 HOH 72  2172 322  HOH HOH A . 
U 8 HOH 73  2173 778  HOH HOH A . 
U 8 HOH 74  2174 396  HOH HOH A . 
U 8 HOH 75  2175 285  HOH HOH A . 
U 8 HOH 76  2176 33   HOH HOH A . 
U 8 HOH 77  2177 100  HOH HOH A . 
U 8 HOH 78  2178 6    HOH HOH A . 
U 8 HOH 79  2179 155  HOH HOH A . 
U 8 HOH 80  2180 848  HOH HOH A . 
U 8 HOH 81  2181 592  HOH HOH A . 
U 8 HOH 82  2182 121  HOH HOH A . 
U 8 HOH 83  2183 97   HOH HOH A . 
U 8 HOH 84  2184 534  HOH HOH A . 
U 8 HOH 85  2185 96   HOH HOH A . 
U 8 HOH 86  2186 591  HOH HOH A . 
U 8 HOH 87  2187 877  HOH HOH A . 
U 8 HOH 88  2188 510  HOH HOH A . 
U 8 HOH 89  2189 779  HOH HOH A . 
U 8 HOH 90  2190 370  HOH HOH A . 
U 8 HOH 91  2191 597  HOH HOH A . 
U 8 HOH 92  2192 348  HOH HOH A . 
U 8 HOH 93  2193 329  HOH HOH A . 
U 8 HOH 94  2194 562  HOH HOH A . 
U 8 HOH 95  2195 17   HOH HOH A . 
U 8 HOH 96  2196 48   HOH HOH A . 
U 8 HOH 97  2197 28   HOH HOH A . 
U 8 HOH 98  2198 951  HOH HOH A . 
U 8 HOH 99  2199 75   HOH HOH A . 
U 8 HOH 100 2200 792  HOH HOH A . 
U 8 HOH 101 2201 8    HOH HOH A . 
U 8 HOH 102 2202 439  HOH HOH A . 
U 8 HOH 103 2203 265  HOH HOH A . 
U 8 HOH 104 2204 413  HOH HOH A . 
U 8 HOH 105 2205 590  HOH HOH A . 
U 8 HOH 106 2206 362  HOH HOH A . 
U 8 HOH 107 2207 632  HOH HOH A . 
U 8 HOH 108 2208 279  HOH HOH A . 
U 8 HOH 109 2209 776  HOH HOH A . 
U 8 HOH 110 2210 622  HOH HOH A . 
U 8 HOH 111 2211 334  HOH HOH A . 
U 8 HOH 112 2212 737  HOH HOH A . 
U 8 HOH 113 2213 56   HOH HOH A . 
U 8 HOH 114 2214 905  HOH HOH A . 
U 8 HOH 115 2215 430  HOH HOH A . 
U 8 HOH 116 2216 190  HOH HOH A . 
U 8 HOH 117 2217 290  HOH HOH A . 
U 8 HOH 118 2218 561  HOH HOH A . 
U 8 HOH 119 2219 402  HOH HOH A . 
U 8 HOH 120 2220 2    HOH HOH A . 
U 8 HOH 121 2221 19   HOH HOH A . 
U 8 HOH 122 2222 511  HOH HOH A . 
U 8 HOH 123 2223 70   HOH HOH A . 
U 8 HOH 124 2224 851  HOH HOH A . 
U 8 HOH 125 2225 86   HOH HOH A . 
U 8 HOH 126 2226 181  HOH HOH A . 
U 8 HOH 127 2227 354  HOH HOH A . 
U 8 HOH 128 2228 539  HOH HOH A . 
U 8 HOH 129 2229 393  HOH HOH A . 
U 8 HOH 130 2230 222  HOH HOH A . 
U 8 HOH 131 2231 440  HOH HOH A . 
U 8 HOH 132 2232 245  HOH HOH A . 
U 8 HOH 133 2233 319  HOH HOH A . 
U 8 HOH 134 2234 390  HOH HOH A . 
U 8 HOH 135 2235 59   HOH HOH A . 
U 8 HOH 136 2236 213  HOH HOH A . 
U 8 HOH 137 2237 531  HOH HOH A . 
U 8 HOH 138 2238 522  HOH HOH A . 
U 8 HOH 139 2239 757  HOH HOH A . 
U 8 HOH 140 2240 154  HOH HOH A . 
U 8 HOH 141 2241 697  HOH HOH A . 
U 8 HOH 142 2242 360  HOH HOH A . 
U 8 HOH 143 2243 312  HOH HOH A . 
U 8 HOH 144 2244 726  HOH HOH A . 
U 8 HOH 145 2245 459  HOH HOH A . 
U 8 HOH 146 2246 768  HOH HOH A . 
U 8 HOH 147 2247 876  HOH HOH A . 
U 8 HOH 148 2248 175  HOH HOH A . 
U 8 HOH 149 2249 442  HOH HOH A . 
U 8 HOH 150 2250 478  HOH HOH A . 
U 8 HOH 151 2251 23   HOH HOH A . 
U 8 HOH 152 2252 766  HOH HOH A . 
U 8 HOH 153 2253 239  HOH HOH A . 
U 8 HOH 154 2254 257  HOH HOH A . 
U 8 HOH 155 2255 487  HOH HOH A . 
U 8 HOH 156 2256 387  HOH HOH A . 
U 8 HOH 157 2257 454  HOH HOH A . 
U 8 HOH 158 2258 208  HOH HOH A . 
U 8 HOH 159 2259 270  HOH HOH A . 
U 8 HOH 160 2260 124  HOH HOH A . 
U 8 HOH 161 2261 136  HOH HOH A . 
U 8 HOH 162 2262 259  HOH HOH A . 
U 8 HOH 163 2263 114  HOH HOH A . 
U 8 HOH 164 2264 165  HOH HOH A . 
U 8 HOH 165 2265 55   HOH HOH A . 
U 8 HOH 166 2266 556  HOH HOH A . 
U 8 HOH 167 2267 650  HOH HOH A . 
U 8 HOH 168 2268 274  HOH HOH A . 
U 8 HOH 169 2269 43   HOH HOH A . 
U 8 HOH 170 2270 173  HOH HOH A . 
U 8 HOH 171 2271 156  HOH HOH A . 
U 8 HOH 172 2272 509  HOH HOH A . 
U 8 HOH 173 2273 60   HOH HOH A . 
U 8 HOH 174 2274 411  HOH HOH A . 
U 8 HOH 175 2275 26   HOH HOH A . 
U 8 HOH 176 2276 232  HOH HOH A . 
U 8 HOH 177 2277 475  HOH HOH A . 
U 8 HOH 178 2278 756  HOH HOH A . 
U 8 HOH 179 2279 593  HOH HOH A . 
U 8 HOH 180 2280 93   HOH HOH A . 
U 8 HOH 181 2281 16   HOH HOH A . 
U 8 HOH 182 2282 324  HOH HOH A . 
U 8 HOH 183 2283 171  HOH HOH A . 
U 8 HOH 184 2284 445  HOH HOH A . 
U 8 HOH 185 2285 421  HOH HOH A . 
U 8 HOH 186 2286 41   HOH HOH A . 
U 8 HOH 187 2287 420  HOH HOH A . 
U 8 HOH 188 2288 27   HOH HOH A . 
U 8 HOH 189 2289 808  HOH HOH A . 
U 8 HOH 190 2290 422  HOH HOH A . 
U 8 HOH 191 2291 727  HOH HOH A . 
U 8 HOH 192 2292 162  HOH HOH A . 
U 8 HOH 193 2293 185  HOH HOH A . 
U 8 HOH 194 2294 183  HOH HOH A . 
U 8 HOH 195 2295 595  HOH HOH A . 
U 8 HOH 196 2296 36   HOH HOH A . 
U 8 HOH 197 2297 655  HOH HOH A . 
U 8 HOH 198 2298 347  HOH HOH A . 
U 8 HOH 199 2299 400  HOH HOH A . 
U 8 HOH 200 2300 157  HOH HOH A . 
U 8 HOH 201 2301 941  HOH HOH A . 
U 8 HOH 202 2302 711  HOH HOH A . 
U 8 HOH 203 2303 206  HOH HOH A . 
U 8 HOH 204 2304 717  HOH HOH A . 
U 8 HOH 205 2305 332  HOH HOH A . 
U 8 HOH 206 2306 47   HOH HOH A . 
U 8 HOH 207 2307 37   HOH HOH A . 
U 8 HOH 208 2308 514  HOH HOH A . 
U 8 HOH 209 2309 483  HOH HOH A . 
U 8 HOH 210 2310 225  HOH HOH A . 
U 8 HOH 211 2311 696  HOH HOH A . 
U 8 HOH 212 2312 548  HOH HOH A . 
U 8 HOH 213 2313 780  HOH HOH A . 
U 8 HOH 214 2314 276  HOH HOH A . 
U 8 HOH 215 2315 501  HOH HOH A . 
U 8 HOH 216 2316 361  HOH HOH A . 
U 8 HOH 217 2317 489  HOH HOH A . 
U 8 HOH 218 2318 446  HOH HOH A . 
U 8 HOH 219 2319 384  HOH HOH A . 
U 8 HOH 220 2320 180  HOH HOH A . 
U 8 HOH 221 2321 73   HOH HOH A . 
U 8 HOH 222 2322 379  HOH HOH A . 
U 8 HOH 223 2323 135  HOH HOH A . 
U 8 HOH 224 2324 25   HOH HOH A . 
U 8 HOH 225 2325 1    HOH HOH A . 
U 8 HOH 226 2326 24   HOH HOH A . 
U 8 HOH 227 2327 145  HOH HOH A . 
U 8 HOH 228 2328 472  HOH HOH A . 
U 8 HOH 229 2329 205  HOH HOH A . 
U 8 HOH 230 2330 552  HOH HOH A . 
U 8 HOH 231 2331 368  HOH HOH A . 
U 8 HOH 232 2332 389  HOH HOH A . 
U 8 HOH 233 2333 315  HOH HOH A . 
U 8 HOH 234 2334 130  HOH HOH A . 
U 8 HOH 235 2335 218  HOH HOH A . 
U 8 HOH 236 2336 227  HOH HOH A . 
U 8 HOH 237 2337 376  HOH HOH A . 
U 8 HOH 238 2338 204  HOH HOH A . 
U 8 HOH 239 2339 278  HOH HOH A . 
U 8 HOH 240 2340 724  HOH HOH A . 
U 8 HOH 241 2341 139  HOH HOH A . 
U 8 HOH 242 2342 626  HOH HOH A . 
U 8 HOH 243 2343 266  HOH HOH A . 
U 8 HOH 244 2344 652  HOH HOH A . 
U 8 HOH 245 2345 176  HOH HOH A . 
U 8 HOH 246 2346 541  HOH HOH A . 
U 8 HOH 247 2347 120  HOH HOH A . 
U 8 HOH 248 2348 10   HOH HOH A . 
U 8 HOH 249 2349 174  HOH HOH A . 
U 8 HOH 250 2350 399  HOH HOH A . 
U 8 HOH 251 2351 83   HOH HOH A . 
U 8 HOH 252 2352 375  HOH HOH A . 
U 8 HOH 253 2353 192  HOH HOH A . 
U 8 HOH 254 2354 601  HOH HOH A . 
U 8 HOH 255 2355 794  HOH HOH A . 
U 8 HOH 256 2356 473  HOH HOH A . 
U 8 HOH 257 2357 81   HOH HOH A . 
U 8 HOH 258 2358 133  HOH HOH A . 
U 8 HOH 259 2359 736  HOH HOH A . 
U 8 HOH 260 2360 700  HOH HOH A . 
U 8 HOH 261 2361 719  HOH HOH A . 
U 8 HOH 262 2362 309  HOH HOH A . 
U 8 HOH 263 2363 912  HOH HOH A . 
U 8 HOH 264 2364 68   HOH HOH A . 
U 8 HOH 265 2365 412  HOH HOH A . 
U 8 HOH 266 2366 847  HOH HOH A . 
U 8 HOH 267 2367 466  HOH HOH A . 
U 8 HOH 268 2368 616  HOH HOH A . 
U 8 HOH 269 2369 406  HOH HOH A . 
U 8 HOH 270 2370 722  HOH HOH A . 
U 8 HOH 271 2371 137  HOH HOH A . 
U 8 HOH 272 2372 269  HOH HOH A . 
U 8 HOH 273 2373 526  HOH HOH A . 
U 8 HOH 274 2374 461  HOH HOH A . 
U 8 HOH 275 2375 549  HOH HOH A . 
U 8 HOH 276 2376 802  HOH HOH A . 
U 8 HOH 277 2377 885  HOH HOH A . 
U 8 HOH 278 2378 441  HOH HOH A . 
U 8 HOH 279 2379 518  HOH HOH A . 
U 8 HOH 280 2380 378  HOH HOH A . 
U 8 HOH 281 2381 508  HOH HOH A . 
U 8 HOH 282 2382 125  HOH HOH A . 
U 8 HOH 283 2383 418  HOH HOH A . 
U 8 HOH 284 2384 432  HOH HOH A . 
U 8 HOH 285 2385 364  HOH HOH A . 
U 8 HOH 286 2386 694  HOH HOH A . 
U 8 HOH 287 2387 867  HOH HOH A . 
U 8 HOH 288 2388 283  HOH HOH A . 
U 8 HOH 289 2389 654  HOH HOH A . 
U 8 HOH 290 2390 793  HOH HOH A . 
U 8 HOH 291 2391 313  HOH HOH A . 
U 8 HOH 292 2392 241  HOH HOH A . 
U 8 HOH 293 2393 449  HOH HOH A . 
U 8 HOH 294 2394 752  HOH HOH A . 
U 8 HOH 295 2395 715  HOH HOH A . 
U 8 HOH 296 2396 140  HOH HOH A . 
U 8 HOH 297 2397 182  HOH HOH A . 
U 8 HOH 298 2398 714  HOH HOH A . 
U 8 HOH 299 2399 341  HOH HOH A . 
U 8 HOH 300 2400 414  HOH HOH A . 
U 8 HOH 301 2401 572  HOH HOH A . 
U 8 HOH 302 2402 160  HOH HOH A . 
U 8 HOH 303 2403 640  HOH HOH A . 
U 8 HOH 304 2404 32   HOH HOH A . 
U 8 HOH 305 2405 196  HOH HOH A . 
U 8 HOH 306 2406 223  HOH HOH A . 
U 8 HOH 307 2407 611  HOH HOH A . 
U 8 HOH 308 2408 262  HOH HOH A . 
U 8 HOH 309 2409 258  HOH HOH A . 
U 8 HOH 310 2410 71   HOH HOH A . 
U 8 HOH 311 2411 108  HOH HOH A . 
U 8 HOH 312 2412 202  HOH HOH A . 
U 8 HOH 313 2413 143  HOH HOH A . 
U 8 HOH 314 2414 292  HOH HOH A . 
U 8 HOH 315 2415 856  HOH HOH A . 
U 8 HOH 316 2416 581  HOH HOH A . 
U 8 HOH 317 2417 397  HOH HOH A . 
U 8 HOH 318 2418 371  HOH HOH A . 
U 8 HOH 319 2419 250  HOH HOH A . 
U 8 HOH 320 2420 707  HOH HOH A . 
U 8 HOH 321 2421 777  HOH HOH A . 
U 8 HOH 322 2422 109  HOH HOH A . 
U 8 HOH 323 2423 323  HOH HOH A . 
U 8 HOH 324 2424 410  HOH HOH A . 
U 8 HOH 325 2425 429  HOH HOH A . 
U 8 HOH 326 2426 642  HOH HOH A . 
U 8 HOH 327 2427 467  HOH HOH A . 
U 8 HOH 328 2428 637  HOH HOH A . 
U 8 HOH 329 2429 799  HOH HOH A . 
U 8 HOH 330 2430 437  HOH HOH A . 
U 8 HOH 331 2431 623  HOH HOH A . 
U 8 HOH 332 2432 943  HOH HOH A . 
U 8 HOH 333 2433 289  HOH HOH A . 
U 8 HOH 334 2434 914  HOH HOH A . 
U 8 HOH 335 2435 356  HOH HOH A . 
U 8 HOH 336 2436 765  HOH HOH A . 
U 8 HOH 337 2437 219  HOH HOH A . 
U 8 HOH 338 2438 146  HOH HOH A . 
U 8 HOH 339 2439 629  HOH HOH A . 
U 8 HOH 340 2440 72   HOH HOH A . 
U 8 HOH 341 2441 394  HOH HOH A . 
U 8 HOH 342 2442 99   HOH HOH A . 
U 8 HOH 343 2443 392  HOH HOH A . 
U 8 HOH 344 2444 301  HOH HOH A . 
U 8 HOH 345 2445 149  HOH HOH A . 
U 8 HOH 346 2446 415  HOH HOH A . 
U 8 HOH 347 2447 659  HOH HOH A . 
U 8 HOH 348 2448 355  HOH HOH A . 
U 8 HOH 349 2449 307  HOH HOH A . 
U 8 HOH 350 2450 263  HOH HOH A . 
U 8 HOH 351 2451 740  HOH HOH A . 
U 8 HOH 352 2452 179  HOH HOH A . 
U 8 HOH 353 2453 525  HOH HOH A . 
U 8 HOH 354 2454 769  HOH HOH A . 
U 8 HOH 355 2455 388  HOH HOH A . 
U 8 HOH 356 2456 915  HOH HOH A . 
U 8 HOH 357 2457 747  HOH HOH A . 
U 8 HOH 358 2458 1017 HOH HOH A . 
U 8 HOH 359 2459 203  HOH HOH A . 
U 8 HOH 360 2460 803  HOH HOH A . 
U 8 HOH 361 2461 926  HOH HOH A . 
U 8 HOH 362 2462 667  HOH HOH A . 
U 8 HOH 363 2463 158  HOH HOH A . 
U 8 HOH 364 2464 599  HOH HOH A . 
U 8 HOH 365 2465 866  HOH HOH A . 
U 8 HOH 366 2466 343  HOH HOH A . 
U 8 HOH 367 2467 566  HOH HOH A . 
U 8 HOH 368 2468 198  HOH HOH A . 
U 8 HOH 369 2469 1010 HOH HOH A . 
U 8 HOH 370 2470 651  HOH HOH A . 
U 8 HOH 371 2471 353  HOH HOH A . 
U 8 HOH 372 2472 728  HOH HOH A . 
U 8 HOH 373 2473 960  HOH HOH A . 
U 8 HOH 374 2474 939  HOH HOH A . 
U 8 HOH 375 2475 252  HOH HOH A . 
U 8 HOH 376 2476 504  HOH HOH A . 
U 8 HOH 377 2477 678  HOH HOH A . 
U 8 HOH 378 2478 443  HOH HOH A . 
U 8 HOH 379 2479 294  HOH HOH A . 
U 8 HOH 380 2480 693  HOH HOH A . 
U 8 HOH 381 2481 233  HOH HOH A . 
U 8 HOH 382 2482 922  HOH HOH A . 
U 8 HOH 383 2483 846  HOH HOH A . 
U 8 HOH 384 2484 220  HOH HOH A . 
U 8 HOH 385 2485 499  HOH HOH A . 
U 8 HOH 386 2486 956  HOH HOH A . 
U 8 HOH 387 2487 963  HOH HOH A . 
U 8 HOH 388 2488 928  HOH HOH A . 
U 8 HOH 389 2489 303  HOH HOH A . 
U 8 HOH 390 2490 934  HOH HOH A . 
U 8 HOH 391 2491 236  HOH HOH A . 
U 8 HOH 392 2492 872  HOH HOH A . 
U 8 HOH 393 2493 829  HOH HOH A . 
U 8 HOH 394 2494 123  HOH HOH A . 
U 8 HOH 395 2495 683  HOH HOH A . 
U 8 HOH 396 2496 842  HOH HOH A . 
U 8 HOH 397 2497 1011 HOH HOH A . 
U 8 HOH 398 2498 695  HOH HOH A . 
U 8 HOH 399 2499 52   HOH HOH A . 
U 8 HOH 400 2500 860  HOH HOH A . 
U 8 HOH 401 2501 300  HOH HOH A . 
U 8 HOH 402 2502 588  HOH HOH A . 
U 8 HOH 403 2503 621  HOH HOH A . 
U 8 HOH 404 2504 817  HOH HOH A . 
U 8 HOH 405 2505 916  HOH HOH A . 
U 8 HOH 406 2506 151  HOH HOH A . 
U 8 HOH 407 2507 815  HOH HOH A . 
U 8 HOH 408 2508 948  HOH HOH A . 
U 8 HOH 409 2509 864  HOH HOH A . 
U 8 HOH 410 2510 854  HOH HOH A . 
U 8 HOH 411 2511 883  HOH HOH A . 
U 8 HOH 412 2512 968  HOH HOH A . 
U 8 HOH 413 2513 148  HOH HOH A . 
U 8 HOH 414 2514 816  HOH HOH A . 
U 8 HOH 415 2515 298  HOH HOH A . 
U 8 HOH 416 2516 538  HOH HOH A . 
U 8 HOH 417 2517 819  HOH HOH A . 
U 8 HOH 418 2518 880  HOH HOH A . 
U 8 HOH 419 2519 620  HOH HOH A . 
U 8 HOH 420 2520 494  HOH HOH A . 
U 8 HOH 421 2521 887  HOH HOH A . 
U 8 HOH 422 2522 681  HOH HOH A . 
U 8 HOH 423 2523 855  HOH HOH A . 
U 8 HOH 424 2524 178  HOH HOH A . 
U 8 HOH 425 2525 447  HOH HOH A . 
U 8 HOH 426 2526 280  HOH HOH A . 
U 8 HOH 427 2527 944  HOH HOH A . 
U 8 HOH 428 2528 947  HOH HOH A . 
U 8 HOH 429 2529 682  HOH HOH A . 
U 8 HOH 430 2530 1008 HOH HOH A . 
U 8 HOH 431 2531 886  HOH HOH A . 
U 8 HOH 432 2532 503  HOH HOH A . 
U 8 HOH 433 2533 224  HOH HOH A . 
U 8 HOH 434 2534 820  HOH HOH A . 
U 8 HOH 435 2535 163  HOH HOH A . 
U 8 HOH 436 2536 330  HOH HOH A . 
U 8 HOH 437 2537 731  HOH HOH A . 
U 8 HOH 438 2538 962  HOH HOH A . 
U 8 HOH 439 2539 1004 HOH HOH A . 
U 8 HOH 440 2540 865  HOH HOH A . 
U 8 HOH 441 2541 983  HOH HOH A . 
U 8 HOH 442 2542 884  HOH HOH A . 
U 8 HOH 443 2543 260  HOH HOH A . 
U 8 HOH 444 2544 945  HOH HOH A . 
U 8 HOH 445 2545 927  HOH HOH A . 
U 8 HOH 446 2546 940  HOH HOH A . 
U 8 HOH 447 2547 672  HOH HOH A . 
U 8 HOH 448 2548 965  HOH HOH A . 
U 8 HOH 449 2549 961  HOH HOH A . 
U 8 HOH 450 2550 775  HOH HOH A . 
U 8 HOH 451 2551 966  HOH HOH A . 
U 8 HOH 452 2552 869  HOH HOH A . 
U 8 HOH 453 2553 859  HOH HOH A . 
U 8 HOH 454 2554 882  HOH HOH A . 
U 8 HOH 455 2555 844  HOH HOH A . 
U 8 HOH 456 2556 299  HOH HOH A . 
U 8 HOH 457 2557 607  HOH HOH A . 
U 8 HOH 458 2558 264  HOH HOH A . 
U 8 HOH 459 2559 1006 HOH HOH A . 
U 8 HOH 460 2560 821  HOH HOH A . 
U 8 HOH 461 2561 959  HOH HOH A . 
U 8 HOH 462 2562 950  HOH HOH A . 
U 8 HOH 463 2563 863  HOH HOH A . 
U 8 HOH 464 2564 845  HOH HOH A . 
U 8 HOH 465 2565 197  HOH HOH A . 
U 8 HOH 466 2566 643  HOH HOH A . 
U 8 HOH 467 2567 871  HOH HOH A . 
U 8 HOH 468 2568 967  HOH HOH A . 
U 8 HOH 469 2569 477  HOH HOH A . 
U 8 HOH 470 2570 423  HOH HOH A . 
U 8 HOH 471 2571 215  HOH HOH A . 
U 8 HOH 472 2572 879  HOH HOH A . 
U 8 HOH 473 2573 495  HOH HOH A . 
U 8 HOH 474 2574 491  HOH HOH A . 
U 8 HOH 475 2575 497  HOH HOH A . 
U 8 HOH 476 2576 602  HOH HOH A . 
U 8 HOH 477 2577 805  HOH HOH A . 
U 8 HOH 478 2578 858  HOH HOH A . 
U 8 HOH 479 2579 229  HOH HOH A . 
U 8 HOH 480 2580 824  HOH HOH A . 
U 8 HOH 481 2581 807  HOH HOH A . 
U 8 HOH 482 2582 870  HOH HOH A . 
U 8 HOH 483 2583 878  HOH HOH A . 
U 8 HOH 484 2584 500  HOH HOH A . 
U 8 HOH 485 2585 493  HOH HOH A . 
U 8 HOH 486 2586 946  HOH HOH A . 
U 8 HOH 487 2587 957  HOH HOH A . 
U 8 HOH 488 2588 818  HOH HOH A . 
U 8 HOH 489 2589 919  HOH HOH A . 
U 8 HOH 490 2590 920  HOH HOH A . 
U 8 HOH 491 2591 505  HOH HOH A . 
U 8 HOH 492 2592 873  HOH HOH A . 
U 8 HOH 493 2593 875  HOH HOH A . 
U 8 HOH 494 2594 498  HOH HOH A . 
U 8 HOH 495 2595 827  HOH HOH A . 
U 8 HOH 496 2596 1007 HOH HOH A . 
U 8 HOH 497 2597 874  HOH HOH A . 
V 8 HOH 1   2101 902  HOH HOH B . 
V 8 HOH 2   2102 907  HOH HOH B . 
V 8 HOH 3   2103 830  HOH HOH B . 
V 8 HOH 4   2104 929  HOH HOH B . 
V 8 HOH 5   2105 484  HOH HOH B . 
V 8 HOH 6   2106 627  HOH HOH B . 
V 8 HOH 7   2107 718  HOH HOH B . 
V 8 HOH 8   2108 328  HOH HOH B . 
V 8 HOH 9   2109 791  HOH HOH B . 
V 8 HOH 10  2110 832  HOH HOH B . 
V 8 HOH 11  2111 704  HOH HOH B . 
V 8 HOH 12  2112 488  HOH HOH B . 
V 8 HOH 13  2113 337  HOH HOH B . 
V 8 HOH 14  2114 691  HOH HOH B . 
V 8 HOH 15  2115 492  HOH HOH B . 
V 8 HOH 16  2116 624  HOH HOH B . 
V 8 HOH 17  2117 783  HOH HOH B . 
V 8 HOH 18  2118 801  HOH HOH B . 
V 8 HOH 19  2119 975  HOH HOH B . 
V 8 HOH 20  2120 790  HOH HOH B . 
V 8 HOH 21  2121 936  HOH HOH B . 
V 8 HOH 22  2122 638  HOH HOH B . 
V 8 HOH 23  2123 788  HOH HOH B . 
V 8 HOH 24  2124 457  HOH HOH B . 
V 8 HOH 25  2125 613  HOH HOH B . 
V 8 HOH 26  2126 594  HOH HOH B . 
V 8 HOH 27  2127 699  HOH HOH B . 
V 8 HOH 28  2128 710  HOH HOH B . 
V 8 HOH 29  2129 242  HOH HOH B . 
V 8 HOH 30  2130 169  HOH HOH B . 
V 8 HOH 31  2131 22   HOH HOH B . 
V 8 HOH 32  2132 515  HOH HOH B . 
V 8 HOH 33  2133 529  HOH HOH B . 
V 8 HOH 34  2134 923  HOH HOH B . 
V 8 HOH 35  2135 969  HOH HOH B . 
V 8 HOH 36  2136 470  HOH HOH B . 
V 8 HOH 37  2137 463  HOH HOH B . 
V 8 HOH 38  2138 540  HOH HOH B . 
V 8 HOH 39  2139 721  HOH HOH B . 
V 8 HOH 40  2140 317  HOH HOH B . 
V 8 HOH 41  2141 333  HOH HOH B . 
V 8 HOH 42  2142 564  HOH HOH B . 
V 8 HOH 43  2143 834  HOH HOH B . 
V 8 HOH 44  2144 989  HOH HOH B . 
V 8 HOH 45  2145 537  HOH HOH B . 
V 8 HOH 46  2146 352  HOH HOH B . 
V 8 HOH 47  2147 152  HOH HOH B . 
V 8 HOH 48  2148 186  HOH HOH B . 
V 8 HOH 49  2149 587  HOH HOH B . 
V 8 HOH 50  2150 306  HOH HOH B . 
V 8 HOH 51  2151 35   HOH HOH B . 
V 8 HOH 52  2152 703  HOH HOH B . 
V 8 HOH 53  2153 568  HOH HOH B . 
V 8 HOH 54  2154 453  HOH HOH B . 
V 8 HOH 55  2155 742  HOH HOH B . 
V 8 HOH 56  2156 554  HOH HOH B . 
V 8 HOH 57  2157 474  HOH HOH B . 
V 8 HOH 58  2158 630  HOH HOH B . 
V 8 HOH 59  2159 550  HOH HOH B . 
V 8 HOH 60  2160 308  HOH HOH B . 
V 8 HOH 61  2161 111  HOH HOH B . 
V 8 HOH 62  2162 569  HOH HOH B . 
V 8 HOH 63  2163 786  HOH HOH B . 
V 8 HOH 64  2164 172  HOH HOH B . 
V 8 HOH 65  2165 90   HOH HOH B . 
V 8 HOH 66  2166 460  HOH HOH B . 
V 8 HOH 67  2167 268  HOH HOH B . 
V 8 HOH 68  2168 214  HOH HOH B . 
V 8 HOH 69  2169 563  HOH HOH B . 
V 8 HOH 70  2170 485  HOH HOH B . 
V 8 HOH 71  2171 664  HOH HOH B . 
V 8 HOH 72  2172 61   HOH HOH B . 
V 8 HOH 73  2173 110  HOH HOH B . 
V 8 HOH 74  2174 733  HOH HOH B . 
V 8 HOH 75  2175 76   HOH HOH B . 
V 8 HOH 76  2176 405  HOH HOH B . 
V 8 HOH 77  2177 458  HOH HOH B . 
V 8 HOH 78  2178 193  HOH HOH B . 
V 8 HOH 79  2179 512  HOH HOH B . 
V 8 HOH 80  2180 373  HOH HOH B . 
V 8 HOH 81  2181 234  HOH HOH B . 
V 8 HOH 82  2182 106  HOH HOH B . 
V 8 HOH 83  2183 583  HOH HOH B . 
V 8 HOH 84  2184 404  HOH HOH B . 
V 8 HOH 85  2185 1005 HOH HOH B . 
V 8 HOH 86  2186 612  HOH HOH B . 
V 8 HOH 87  2187 614  HOH HOH B . 
V 8 HOH 88  2188 646  HOH HOH B . 
V 8 HOH 89  2189 565  HOH HOH B . 
V 8 HOH 90  2190 749  HOH HOH B . 
V 8 HOH 91  2191 126  HOH HOH B . 
V 8 HOH 92  2192 102  HOH HOH B . 
V 8 HOH 93  2193 800  HOH HOH B . 
V 8 HOH 94  2194 385  HOH HOH B . 
V 8 HOH 95  2195 751  HOH HOH B . 
V 8 HOH 96  2196 142  HOH HOH B . 
V 8 HOH 97  2197 972  HOH HOH B . 
V 8 HOH 98  2198 240  HOH HOH B . 
V 8 HOH 99  2199 207  HOH HOH B . 
V 8 HOH 100 2200 452  HOH HOH B . 
V 8 HOH 101 2201 519  HOH HOH B . 
V 8 HOH 102 2202 734  HOH HOH B . 
V 8 HOH 103 2203 235  HOH HOH B . 
V 8 HOH 104 2204 533  HOH HOH B . 
V 8 HOH 105 2205 184  HOH HOH B . 
V 8 HOH 106 2206 464  HOH HOH B . 
V 8 HOH 107 2207 745  HOH HOH B . 
V 8 HOH 108 2208 351  HOH HOH B . 
V 8 HOH 109 2209 21   HOH HOH B . 
V 8 HOH 110 2210 231  HOH HOH B . 
V 8 HOH 111 2211 796  HOH HOH B . 
V 8 HOH 112 2212 195  HOH HOH B . 
V 8 HOH 113 2213 383  HOH HOH B . 
V 8 HOH 114 2214 720  HOH HOH B . 
V 8 HOH 115 2215 31   HOH HOH B . 
V 8 HOH 116 2216 230  HOH HOH B . 
V 8 HOH 117 2217 476  HOH HOH B . 
V 8 HOH 118 2218 658  HOH HOH B . 
V 8 HOH 119 2219 85   HOH HOH B . 
V 8 HOH 120 2220 598  HOH HOH B . 
V 8 HOH 121 2221 517  HOH HOH B . 
V 8 HOH 122 2222 988  HOH HOH B . 
V 8 HOH 123 2223 7    HOH HOH B . 
V 8 HOH 124 2224 12   HOH HOH B . 
V 8 HOH 125 2225 523  HOH HOH B . 
V 8 HOH 126 2226 910  HOH HOH B . 
V 8 HOH 127 2227 486  HOH HOH B . 
V 8 HOH 128 2228 516  HOH HOH B . 
V 8 HOH 129 2229 1013 HOH HOH B . 
V 8 HOH 130 2230 596  HOH HOH B . 
V 8 HOH 131 2231 377  HOH HOH B . 
V 8 HOH 132 2232 631  HOH HOH B . 
V 8 HOH 133 2233 617  HOH HOH B . 
V 8 HOH 134 2234 46   HOH HOH B . 
V 8 HOH 135 2235 570  HOH HOH B . 
V 8 HOH 136 2236 600  HOH HOH B . 
V 8 HOH 137 2237 730  HOH HOH B . 
V 8 HOH 138 2238 559  HOH HOH B . 
V 8 HOH 139 2239 419  HOH HOH B . 
V 8 HOH 140 2240 781  HOH HOH B . 
V 8 HOH 141 2241 398  HOH HOH B . 
V 8 HOH 142 2242 606  HOH HOH B . 
V 8 HOH 143 2243 63   HOH HOH B . 
V 8 HOH 144 2244 584  HOH HOH B . 
V 8 HOH 145 2245 167  HOH HOH B . 
V 8 HOH 146 2246 789  HOH HOH B . 
V 8 HOH 147 2247 118  HOH HOH B . 
V 8 HOH 148 2248 314  HOH HOH B . 
V 8 HOH 149 2249 38   HOH HOH B . 
V 8 HOH 150 2250 625  HOH HOH B . 
V 8 HOH 151 2251 74   HOH HOH B . 
V 8 HOH 152 2252 134  HOH HOH B . 
V 8 HOH 153 2253 82   HOH HOH B . 
V 8 HOH 154 2254 701  HOH HOH B . 
V 8 HOH 155 2255 153  HOH HOH B . 
V 8 HOH 156 2256 14   HOH HOH B . 
V 8 HOH 157 2257 147  HOH HOH B . 
V 8 HOH 158 2258 434  HOH HOH B . 
V 8 HOH 159 2259 311  HOH HOH B . 
V 8 HOH 160 2260 316  HOH HOH B . 
V 8 HOH 161 2261 482  HOH HOH B . 
V 8 HOH 162 2262 131  HOH HOH B . 
V 8 HOH 163 2263 261  HOH HOH B . 
V 8 HOH 164 2264 65   HOH HOH B . 
V 8 HOH 165 2265 716  HOH HOH B . 
V 8 HOH 166 2266 520  HOH HOH B . 
V 8 HOH 167 2267 889  HOH HOH B . 
V 8 HOH 168 2268 479  HOH HOH B . 
V 8 HOH 169 2269 746  HOH HOH B . 
V 8 HOH 170 2270 528  HOH HOH B . 
V 8 HOH 171 2271 636  HOH HOH B . 
V 8 HOH 172 2272 253  HOH HOH B . 
V 8 HOH 173 2273 105  HOH HOH B . 
V 8 HOH 174 2274 98   HOH HOH B . 
V 8 HOH 175 2275 644  HOH HOH B . 
V 8 HOH 176 2276 555  HOH HOH B . 
V 8 HOH 177 2277 450  HOH HOH B . 
V 8 HOH 178 2278 657  HOH HOH B . 
V 8 HOH 179 2279 365  HOH HOH B . 
V 8 HOH 180 2280 610  HOH HOH B . 
V 8 HOH 181 2281 58   HOH HOH B . 
V 8 HOH 182 2282 113  HOH HOH B . 
V 8 HOH 183 2283 92   HOH HOH B . 
V 8 HOH 184 2284 1012 HOH HOH B . 
V 8 HOH 185 2285 998  HOH HOH B . 
V 8 HOH 186 2286 663  HOH HOH B . 
V 8 HOH 187 2287 228  HOH HOH B . 
V 8 HOH 188 2288 20   HOH HOH B . 
V 8 HOH 189 2289 34   HOH HOH B . 
V 8 HOH 190 2290 115  HOH HOH B . 
V 8 HOH 191 2291 428  HOH HOH B . 
V 8 HOH 192 2292 426  HOH HOH B . 
V 8 HOH 193 2293 641  HOH HOH B . 
V 8 HOH 194 2294 5    HOH HOH B . 
V 8 HOH 195 2295 427  HOH HOH B . 
V 8 HOH 196 2296 903  HOH HOH B . 
V 8 HOH 197 2297 506  HOH HOH B . 
V 8 HOH 198 2298 542  HOH HOH B . 
V 8 HOH 199 2299 177  HOH HOH B . 
V 8 HOH 200 2300 481  HOH HOH B . 
V 8 HOH 201 2301 545  HOH HOH B . 
V 8 HOH 202 2302 669  HOH HOH B . 
V 8 HOH 203 2303 547  HOH HOH B . 
V 8 HOH 204 2304 335  HOH HOH B . 
V 8 HOH 205 2305 507  HOH HOH B . 
V 8 HOH 206 2306 888  HOH HOH B . 
V 8 HOH 207 2307 741  HOH HOH B . 
V 8 HOH 208 2308 574  HOH HOH B . 
V 8 HOH 209 2309 91   HOH HOH B . 
V 8 HOH 210 2310 536  HOH HOH B . 
V 8 HOH 211 2311 340  HOH HOH B . 
V 8 HOH 212 2312 391  HOH HOH B . 
V 8 HOH 213 2313 894  HOH HOH B . 
V 8 HOH 214 2314 579  HOH HOH B . 
V 8 HOH 215 2315 557  HOH HOH B . 
V 8 HOH 216 2316 166  HOH HOH B . 
V 8 HOH 217 2317 281  HOH HOH B . 
V 8 HOH 218 2318 573  HOH HOH B . 
V 8 HOH 219 2319 359  HOH HOH B . 
V 8 HOH 220 2320 64   HOH HOH B . 
V 8 HOH 221 2321 455  HOH HOH B . 
V 8 HOH 222 2322 209  HOH HOH B . 
V 8 HOH 223 2323 524  HOH HOH B . 
V 8 HOH 224 2324 795  HOH HOH B . 
V 8 HOH 225 2325 39   HOH HOH B . 
V 8 HOH 226 2326 935  HOH HOH B . 
V 8 HOH 227 2327 690  HOH HOH B . 
V 8 HOH 228 2328 119  HOH HOH B . 
V 8 HOH 229 2329 435  HOH HOH B . 
V 8 HOH 230 2330 372  HOH HOH B . 
V 8 HOH 231 2331 95   HOH HOH B . 
V 8 HOH 232 2332 576  HOH HOH B . 
V 8 HOH 233 2333 191  HOH HOH B . 
V 8 HOH 234 2334 4    HOH HOH B . 
V 8 HOH 235 2335 381  HOH HOH B . 
V 8 HOH 236 2336 187  HOH HOH B . 
V 8 HOH 237 2337 42   HOH HOH B . 
V 8 HOH 238 2338 725  HOH HOH B . 
V 8 HOH 239 2339 702  HOH HOH B . 
V 8 HOH 240 2340 358  HOH HOH B . 
V 8 HOH 241 2341 296  HOH HOH B . 
V 8 HOH 242 2342 409  HOH HOH B . 
V 8 HOH 243 2343 78   HOH HOH B . 
V 8 HOH 244 2344 88   HOH HOH B . 
V 8 HOH 245 2345 706  HOH HOH B . 
V 8 HOH 246 2346 954  HOH HOH B . 
V 8 HOH 247 2347 698  HOH HOH B . 
V 8 HOH 248 2348 3    HOH HOH B . 
V 8 HOH 249 2349 116  HOH HOH B . 
V 8 HOH 250 2350 221  HOH HOH B . 
V 8 HOH 251 2351 159  HOH HOH B . 
V 8 HOH 252 2352 633  HOH HOH B . 
V 8 HOH 253 2353 979  HOH HOH B . 
V 8 HOH 254 2354 471  HOH HOH B . 
V 8 HOH 255 2355 469  HOH HOH B . 
V 8 HOH 256 2356 271  HOH HOH B . 
V 8 HOH 257 2357 129  HOH HOH B . 
V 8 HOH 258 2358 589  HOH HOH B . 
V 8 HOH 259 2359 79   HOH HOH B . 
V 8 HOH 260 2360 66   HOH HOH B . 
V 8 HOH 261 2361 530  HOH HOH B . 
V 8 HOH 262 2362 201  HOH HOH B . 
V 8 HOH 263 2363 571  HOH HOH B . 
V 8 HOH 264 2364 50   HOH HOH B . 
V 8 HOH 265 2365 639  HOH HOH B . 
V 8 HOH 266 2366 608  HOH HOH B . 
V 8 HOH 267 2367 670  HOH HOH B . 
V 8 HOH 268 2368 603  HOH HOH B . 
V 8 HOH 269 2369 666  HOH HOH B . 
V 8 HOH 270 2370 54   HOH HOH B . 
V 8 HOH 271 2371 320  HOH HOH B . 
V 8 HOH 272 2372 53   HOH HOH B . 
V 8 HOH 273 2373 535  HOH HOH B . 
V 8 HOH 274 2374 544  HOH HOH B . 
V 8 HOH 275 2375 560  HOH HOH B . 
V 8 HOH 276 2376 925  HOH HOH B . 
V 8 HOH 277 2377 754  HOH HOH B . 
V 8 HOH 278 2378 104  HOH HOH B . 
V 8 HOH 279 2379 604  HOH HOH B . 
V 8 HOH 280 2380 345  HOH HOH B . 
V 8 HOH 281 2381 712  HOH HOH B . 
V 8 HOH 282 2382 249  HOH HOH B . 
V 8 HOH 283 2383 709  HOH HOH B . 
V 8 HOH 284 2384 762  HOH HOH B . 
V 8 HOH 285 2385 112  HOH HOH B . 
V 8 HOH 286 2386 773  HOH HOH B . 
V 8 HOH 287 2387 673  HOH HOH B . 
V 8 HOH 288 2388 238  HOH HOH B . 
V 8 HOH 289 2389 567  HOH HOH B . 
V 8 HOH 290 2390 784  HOH HOH B . 
V 8 HOH 291 2391 57   HOH HOH B . 
V 8 HOH 292 2392 660  HOH HOH B . 
V 8 HOH 293 2393 546  HOH HOH B . 
V 8 HOH 294 2394 502  HOH HOH B . 
V 8 HOH 295 2395 366  HOH HOH B . 
V 8 HOH 296 2396 251  HOH HOH B . 
V 8 HOH 297 2397 575  HOH HOH B . 
V 8 HOH 298 2398 45   HOH HOH B . 
V 8 HOH 299 2399 217  HOH HOH B . 
V 8 HOH 300 2400 67   HOH HOH B . 
V 8 HOH 301 2401 11   HOH HOH B . 
V 8 HOH 302 2402 40   HOH HOH B . 
V 8 HOH 303 2403 84   HOH HOH B . 
V 8 HOH 304 2404 226  HOH HOH B . 
V 8 HOH 305 2405 325  HOH HOH B . 
V 8 HOH 306 2406 582  HOH HOH B . 
V 8 HOH 307 2407 586  HOH HOH B . 
V 8 HOH 308 2408 382  HOH HOH B . 
V 8 HOH 309 2409 417  HOH HOH B . 
V 8 HOH 310 2410 806  HOH HOH B . 
V 8 HOH 311 2411 338  HOH HOH B . 
V 8 HOH 312 2412 401  HOH HOH B . 
V 8 HOH 313 2413 349  HOH HOH B . 
V 8 HOH 314 2414 992  HOH HOH B . 
V 8 HOH 315 2415 628  HOH HOH B . 
V 8 HOH 316 2416 577  HOH HOH B . 
V 8 HOH 317 2417 649  HOH HOH B . 
V 8 HOH 318 2418 558  HOH HOH B . 
V 8 HOH 319 2419 444  HOH HOH B . 
V 8 HOH 320 2420 708  HOH HOH B . 
V 8 HOH 321 2421 814  HOH HOH B . 
V 8 HOH 322 2422 89   HOH HOH B . 
V 8 HOH 323 2423 671  HOH HOH B . 
V 8 HOH 324 2424 456  HOH HOH B . 
V 8 HOH 325 2425 247  HOH HOH B . 
V 8 HOH 326 2426 713  HOH HOH B . 
V 8 HOH 327 2427 342  HOH HOH B . 
V 8 HOH 328 2428 18   HOH HOH B . 
V 8 HOH 329 2429 344  HOH HOH B . 
V 8 HOH 330 2430 200  HOH HOH B . 
V 8 HOH 331 2431 408  HOH HOH B . 
V 8 HOH 332 2432 367  HOH HOH B . 
V 8 HOH 333 2433 480  HOH HOH B . 
V 8 HOH 334 2434 150  HOH HOH B . 
V 8 HOH 335 2435 69   HOH HOH B . 
V 8 HOH 336 2436 645  HOH HOH B . 
V 8 HOH 337 2437 386  HOH HOH B . 
V 8 HOH 338 2438 254  HOH HOH B . 
V 8 HOH 339 2439 532  HOH HOH B . 
V 8 HOH 340 2440 216  HOH HOH B . 
V 8 HOH 341 2441 1016 HOH HOH B . 
V 8 HOH 342 2442 609  HOH HOH B . 
V 8 HOH 343 2443 738  HOH HOH B . 
V 8 HOH 344 2444 273  HOH HOH B . 
V 8 HOH 345 2445 513  HOH HOH B . 
V 8 HOH 346 2446 465  HOH HOH B . 
V 8 HOH 347 2447 293  HOH HOH B . 
V 8 HOH 348 2448 930  HOH HOH B . 
V 8 HOH 349 2449 705  HOH HOH B . 
V 8 HOH 350 2450 462  HOH HOH B . 
V 8 HOH 351 2451 431  HOH HOH B . 
V 8 HOH 352 2452 764  HOH HOH B . 
V 8 HOH 353 2453 767  HOH HOH B . 
V 8 HOH 354 2454 772  HOH HOH B . 
V 8 HOH 355 2455 782  HOH HOH B . 
V 8 HOH 356 2456 973  HOH HOH B . 
V 8 HOH 357 2457 785  HOH HOH B . 
V 8 HOH 358 2458 551  HOH HOH B . 
V 8 HOH 359 2459 891  HOH HOH B . 
V 8 HOH 360 2460 403  HOH HOH B . 
V 8 HOH 361 2461 369  HOH HOH B . 
V 8 HOH 362 2462 615  HOH HOH B . 
V 8 HOH 363 2463 996  HOH HOH B . 
V 8 HOH 364 2464 750  HOH HOH B . 
V 8 HOH 365 2465 895  HOH HOH B . 
V 8 HOH 366 2466 759  HOH HOH B . 
V 8 HOH 367 2467 15   HOH HOH B . 
V 8 HOH 368 2468 168  HOH HOH B . 
V 8 HOH 369 2469 986  HOH HOH B . 
V 8 HOH 370 2470 94   HOH HOH B . 
V 8 HOH 371 2471 318  HOH HOH B . 
V 8 HOH 372 2472 997  HOH HOH B . 
V 8 HOH 373 2473 743  HOH HOH B . 
V 8 HOH 374 2474 578  HOH HOH B . 
V 8 HOH 375 2475 267  HOH HOH B . 
V 8 HOH 376 2476 521  HOH HOH B . 
V 8 HOH 377 2477 981  HOH HOH B . 
V 8 HOH 378 2478 804  HOH HOH B . 
V 8 HOH 379 2479 287  HOH HOH B . 
V 8 HOH 380 2480 395  HOH HOH B . 
V 8 HOH 381 2481 760  HOH HOH B . 
V 8 HOH 382 2482 831  HOH HOH B . 
V 8 HOH 383 2483 635  HOH HOH B . 
V 8 HOH 384 2484 272  HOH HOH B . 
V 8 HOH 385 2485 955  HOH HOH B . 
V 8 HOH 386 2486 770  HOH HOH B . 
V 8 HOH 387 2487 425  HOH HOH B . 
V 8 HOH 388 2488 971  HOH HOH B . 
V 8 HOH 389 2489 553  HOH HOH B . 
V 8 HOH 390 2490 424  HOH HOH B . 
V 8 HOH 391 2491 755  HOH HOH B . 
V 8 HOH 392 2492 771  HOH HOH B . 
V 8 HOH 393 2493 618  HOH HOH B . 
V 8 HOH 394 2494 953  HOH HOH B . 
V 8 HOH 395 2495 852  HOH HOH B . 
V 8 HOH 396 2496 248  HOH HOH B . 
V 8 HOH 397 2497 797  HOH HOH B . 
V 8 HOH 398 2498 161  HOH HOH B . 
V 8 HOH 399 2499 893  HOH HOH B . 
V 8 HOH 400 2500 987  HOH HOH B . 
V 8 HOH 401 2501 144  HOH HOH B . 
V 8 HOH 402 2502 605  HOH HOH B . 
V 8 HOH 403 2503 1003 HOH HOH B . 
V 8 HOH 404 2504 451  HOH HOH B . 
V 8 HOH 405 2505 798  HOH HOH B . 
V 8 HOH 406 2506 211  HOH HOH B . 
V 8 HOH 407 2507 974  HOH HOH B . 
V 8 HOH 408 2508 194  HOH HOH B . 
V 8 HOH 409 2509 647  HOH HOH B . 
V 8 HOH 410 2510 904  HOH HOH B . 
V 8 HOH 411 2511 1009 HOH HOH B . 
V 8 HOH 412 2512 897  HOH HOH B . 
V 8 HOH 413 2513 840  HOH HOH B . 
V 8 HOH 414 2514 909  HOH HOH B . 
V 8 HOH 415 2515 685  HOH HOH B . 
V 8 HOH 416 2516 680  HOH HOH B . 
V 8 HOH 417 2517 813  HOH HOH B . 
V 8 HOH 418 2518 850  HOH HOH B . 
V 8 HOH 419 2519 993  HOH HOH B . 
V 8 HOH 420 2520 321  HOH HOH B . 
V 8 HOH 421 2521 188  HOH HOH B . 
V 8 HOH 422 2522 1002 HOH HOH B . 
V 8 HOH 423 2523 675  HOH HOH B . 
V 8 HOH 424 2524 256  HOH HOH B . 
V 8 HOH 425 2525 849  HOH HOH B . 
V 8 HOH 426 2526 648  HOH HOH B . 
V 8 HOH 427 2527 828  HOH HOH B . 
V 8 HOH 428 2528 295  HOH HOH B . 
V 8 HOH 429 2529 255  HOH HOH B . 
V 8 HOH 430 2530 122  HOH HOH B . 
V 8 HOH 431 2531 1018 HOH HOH B . 
V 8 HOH 432 2532 999  HOH HOH B . 
V 8 HOH 433 2533 976  HOH HOH B . 
V 8 HOH 434 2534 906  HOH HOH B . 
V 8 HOH 435 2535 739  HOH HOH B . 
V 8 HOH 436 2536 970  HOH HOH B . 
V 8 HOH 437 2537 811  HOH HOH B . 
V 8 HOH 438 2538 357  HOH HOH B . 
V 8 HOH 439 2539 990  HOH HOH B . 
V 8 HOH 440 2540 933  HOH HOH B . 
V 8 HOH 441 2541 753  HOH HOH B . 
V 8 HOH 442 2542 496  HOH HOH B . 
V 8 HOH 443 2543 277  HOH HOH B . 
V 8 HOH 444 2544 326  HOH HOH B . 
V 8 HOH 445 2545 896  HOH HOH B . 
V 8 HOH 446 2546 170  HOH HOH B . 
V 8 HOH 447 2547 448  HOH HOH B . 
V 8 HOH 448 2548 44   HOH HOH B . 
V 8 HOH 449 2549 810  HOH HOH B . 
V 8 HOH 450 2550 841  HOH HOH B . 
V 8 HOH 451 2551 288  HOH HOH B . 
V 8 HOH 452 2552 809  HOH HOH B . 
V 8 HOH 453 2553 890  HOH HOH B . 
V 8 HOH 454 2554 117  HOH HOH B . 
V 8 HOH 455 2555 861  HOH HOH B . 
V 8 HOH 456 2556 674  HOH HOH B . 
V 8 HOH 457 2557 237  HOH HOH B . 
V 8 HOH 458 2558 931  HOH HOH B . 
V 8 HOH 459 2559 812  HOH HOH B . 
V 8 HOH 460 2560 138  HOH HOH B . 
V 8 HOH 461 2561 310  HOH HOH B . 
V 8 HOH 462 2562 826  HOH HOH B . 
V 8 HOH 463 2563 543  HOH HOH B . 
V 8 HOH 464 2564 835  HOH HOH B . 
V 8 HOH 465 2565 978  HOH HOH B . 
V 8 HOH 466 2566 985  HOH HOH B . 
V 8 HOH 467 2567 302  HOH HOH B . 
V 8 HOH 468 2568 212  HOH HOH B . 
V 8 HOH 469 2569 580  HOH HOH B . 
V 8 HOH 470 2570 1015 HOH HOH B . 
V 8 HOH 471 2571 982  HOH HOH B . 
V 8 HOH 472 2572 900  HOH HOH B . 
V 8 HOH 473 2573 825  HOH HOH B . 
V 8 HOH 474 2574 838  HOH HOH B . 
V 8 HOH 475 2575 892  HOH HOH B . 
V 8 HOH 476 2576 661  HOH HOH B . 
V 8 HOH 477 2577 676  HOH HOH B . 
V 8 HOH 478 2578 994  HOH HOH B . 
V 8 HOH 479 2579 952  HOH HOH B . 
V 8 HOH 480 2580 305  HOH HOH B . 
V 8 HOH 481 2581 688  HOH HOH B . 
V 8 HOH 482 2582 995  HOH HOH B . 
V 8 HOH 483 2583 839  HOH HOH B . 
V 8 HOH 484 2584 77   HOH HOH B . 
V 8 HOH 485 2585 687  HOH HOH B . 
V 8 HOH 486 2586 984  HOH HOH B . 
V 8 HOH 487 2587 286  HOH HOH B . 
V 8 HOH 488 2588 908  HOH HOH B . 
V 8 HOH 489 2589 490  HOH HOH B . 
V 8 HOH 490 2590 932  HOH HOH B . 
V 8 HOH 491 2591 686  HOH HOH B . 
V 8 HOH 492 2592 833  HOH HOH B . 
V 8 HOH 493 2593 304  HOH HOH B . 
V 8 HOH 494 2594 949  HOH HOH B . 
V 8 HOH 495 2595 127  HOH HOH B . 
V 8 HOH 496 2596 653  HOH HOH B . 
V 8 HOH 497 2597 901  HOH HOH B . 
V 8 HOH 498 2598 918  HOH HOH B . 
V 8 HOH 499 2599 1000 HOH HOH B . 
V 8 HOH 500 2600 199  HOH HOH B . 
V 8 HOH 501 2601 911  HOH HOH B . 
V 8 HOH 502 2602 679  HOH HOH B . 
V 8 HOH 503 2603 416  HOH HOH B . 
V 8 HOH 504 2604 761  HOH HOH B . 
V 8 HOH 505 2605 823  HOH HOH B . 
V 8 HOH 506 2606 937  HOH HOH B . 
V 8 HOH 507 2607 977  HOH HOH B . 
V 8 HOH 508 2608 822  HOH HOH B . 
V 8 HOH 509 2609 991  HOH HOH B . 
V 8 HOH 510 2610 921  HOH HOH B . 
V 8 HOH 511 2611 684  HOH HOH B . 
V 8 HOH 512 2612 677  HOH HOH B . 
V 8 HOH 513 2613 837  HOH HOH B . 
V 8 HOH 514 2614 938  HOH HOH B . 
V 8 HOH 515 2615 1001 HOH HOH B . 
V 8 HOH 516 2616 748  HOH HOH B . 
V 8 HOH 517 2617 899  HOH HOH B . 
V 8 HOH 518 2618 958  HOH HOH B . 
V 8 HOH 519 2619 898  HOH HOH B . 
V 8 HOH 520 2620 980  HOH HOH B . 
V 8 HOH 521 2621 836  HOH HOH B . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,U     
2 1 B,K,L,M,N,O,P,Q,R,S,T,V 
# 
_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_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 O ? A LEU 149 ? A LEU 254 ? 1_555 MG ? H MG . ? A MG 2006 ? 1_555 O1A ? C MYA . ? A MYA 2001 ? 1_555 160.7 ? 
2 O ? B LEU 149 ? B LEU 254 ? 1_555 MG ? R MG . ? B MG 2008 ? 1_555 O1A ? K MYA . ? B MYA 2001 ? 1_555 159.5 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2018-05-16 
2 'Structure model' 1 1 2018-05-23 
3 'Structure model' 1 2 2018-07-04 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
3 3 'Structure model' 'Data collection'     
4 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.pdbx_database_id_DOI'    
6  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
7  2 'Structure model' '_citation.title'                   
8  2 'Structure model' '_citation.year'                    
9  3 'Structure model' '_citation.journal_volume'          
10 3 'Structure model' '_citation.page_first'              
11 3 'Structure model' '_citation.page_last'               
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? .        4 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    437 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    2106 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.09 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 CG A TRP 199 ? ? CD1 A TRP 199 ? ? 1.463 1.363 0.100  0.014 N 
2  1 CD A GLU 244 ? ? OE2 A GLU 244 ? ? 1.322 1.252 0.070  0.011 N 
3  1 CD A GLU 388 ? ? OE1 A GLU 388 ? ? 1.349 1.252 0.097  0.011 N 
4  1 CB A SER 415 ? ? OG  A SER 415 ? ? 1.509 1.418 0.091  0.013 N 
5  1 CD B ARG 189 ? ? NE  B ARG 189 ? ? 1.324 1.460 -0.136 0.017 N 
6  1 CZ B ARG 189 ? ? NH2 B ARG 189 ? ? 1.237 1.326 -0.089 0.013 N 
7  1 CD B GLU 195 ? ? OE1 B GLU 195 ? ? 1.322 1.252 0.070  0.011 N 
8  1 CD B GLU 244 ? ? OE1 B GLU 244 ? ? 1.185 1.252 -0.067 0.011 N 
9  1 NE B ARG 270 ? ? CZ  B ARG 270 ? ? 1.245 1.326 -0.081 0.013 N 
10 1 CD B GLU 388 ? ? OE1 B GLU 388 ? ? 1.333 1.252 0.081  0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB  A ASP 141 ? A CG A ASP 141 ? A OD1 A ASP 141 ? A 124.91 118.30 6.61   0.90 N 
2  1 CB  A ASP 141 ? B CG A ASP 141 ? B OD1 A ASP 141 ? B 112.28 118.30 -6.02  0.90 N 
3  1 NE  A ARG 146 ? B CZ A ARG 146 ? B NH2 A ARG 146 ? B 117.03 120.30 -3.27  0.50 N 
4  1 CB  A ASP 162 ? ? CG A ASP 162 ? ? OD1 A ASP 162 ? ? 124.37 118.30 6.07   0.90 N 
5  1 CB  A ASP 165 ? ? CG A ASP 165 ? ? OD2 A ASP 165 ? ? 124.44 118.30 6.14   0.90 N 
6  1 NE  A ARG 189 ? ? CZ A ARG 189 ? ? NH1 A ARG 189 ? ? 114.19 120.30 -6.11  0.50 N 
7  1 CB  A ASP 191 ? ? CG A ASP 191 ? ? OD1 A ASP 191 ? ? 123.90 118.30 5.60   0.90 N 
8  1 OE1 A GLU 244 ? ? CD A GLU 244 ? ? OE2 A GLU 244 ? ? 130.61 123.30 7.31   1.20 N 
9  1 OE1 A GLU 274 ? ? CD A GLU 274 ? ? OE2 A GLU 274 ? ? 132.42 123.30 9.12   1.20 N 
10 1 NE  A ARG 299 ? ? CZ A ARG 299 ? ? NH1 A ARG 299 ? ? 124.32 120.30 4.02   0.50 N 
11 1 NE  A ARG 299 ? ? CZ A ARG 299 ? ? NH2 A ARG 299 ? ? 113.86 120.30 -6.44  0.50 N 
12 1 CG  A MET 324 ? B SD A MET 324 ? B CE  A MET 324 ? B 89.45  100.20 -10.75 1.60 N 
13 1 NE  A ARG 339 ? ? CZ A ARG 339 ? ? NH2 A ARG 339 ? ? 116.90 120.30 -3.40  0.50 N 
14 1 OE1 A GLU 388 ? ? CD A GLU 388 ? ? OE2 A GLU 388 ? ? 113.63 123.30 -9.67  1.20 N 
15 1 CG  A GLU 388 ? ? CD A GLU 388 ? ? OE2 A GLU 388 ? ? 131.07 118.30 12.77  2.00 N 
16 1 CB  A ASP 396 ? ? CG A ASP 396 ? ? OD1 A ASP 396 ? ? 112.57 118.30 -5.73  0.90 N 
17 1 CB  A ASP 448 ? ? CG A ASP 448 ? ? OD1 A ASP 448 ? ? 124.37 118.30 6.07   0.90 N 
18 1 CD  B ARG 189 ? ? NE B ARG 189 ? ? CZ  B ARG 189 ? ? 143.39 123.60 19.79  1.40 N 
19 1 NE  B ARG 189 ? ? CZ B ARG 189 ? ? NH1 B ARG 189 ? ? 141.23 120.30 20.93  0.50 N 
20 1 NE  B ARG 189 ? ? CZ B ARG 189 ? ? NH2 B ARG 189 ? ? 99.47  120.30 -20.83 0.50 N 
21 1 CB  B ASP 237 ? B CG B ASP 237 ? B OD1 B ASP 237 ? B 123.79 118.30 5.49   0.90 N 
22 1 CB  B ASP 237 ? B CG B ASP 237 ? B OD2 B ASP 237 ? B 112.45 118.30 -5.85  0.90 N 
23 1 NE  B ARG 270 ? ? CZ B ARG 270 ? ? NH1 B ARG 270 ? ? 123.74 120.30 3.44   0.50 N 
24 1 NE  B ARG 270 ? ? CZ B ARG 270 ? ? NH2 B ARG 270 ? ? 117.24 120.30 -3.06  0.50 N 
25 1 OE1 B GLU 274 ? ? CD B GLU 274 ? ? OE2 B GLU 274 ? ? 133.12 123.30 9.82   1.20 N 
26 1 NE  B ARG 299 ? ? CZ B ARG 299 ? ? NH2 B ARG 299 ? ? 117.29 120.30 -3.01  0.50 N 
27 1 OE1 B GLU 388 ? ? CD B GLU 388 ? ? OE2 B GLU 388 ? ? 115.97 123.30 -7.33  1.20 N 
28 1 CB  B TYR 420 ? ? CG B TYR 420 ? ? CD1 B TYR 420 ? ? 117.18 121.00 -3.82  0.60 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 202 ? ? -119.03 54.13   
2  1 TYR A 236 ? ? 50.08   -117.47 
3  1 ILE A 381 ? ? -134.94 -63.54  
4  1 THR A 412 ? ? -100.67 -87.32  
5  1 PHE A 422 ? ? -113.38 -101.41 
6  1 MET A 456 ? ? 46.31   -135.03 
7  1 TYR B 180 ? ? -90.40  -156.29 
8  1 TYR B 236 ? ? 48.75   -119.73 
9  1 ILE B 381 ? ? -134.66 -65.07  
10 1 PHE B 422 ? ? -115.54 -98.84  
11 1 MET B 456 ? ? 49.25   -132.05 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       2621 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.88 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 106 ? A GLY 1 
2  1 Y 1 A PRO 107 ? A PRO 2 
3  1 Y 1 A HIS 108 ? A HIS 3 
4  1 Y 1 A MET 109 ? A MET 4 
5  1 Y 1 A GLU 110 ? A GLU 5 
6  1 Y 1 A GLU 111 ? A GLU 6 
7  1 Y 1 A ALA 112 ? A ALA 7 
8  1 Y 1 A SER 113 ? A SER 8 
9  1 Y 1 A LYS 114 ? A LYS 9 
10 1 Y 1 B GLY 106 ? B GLY 1 
11 1 Y 1 B PRO 107 ? B PRO 2 
12 1 Y 1 B HIS 108 ? B HIS 3 
13 1 Y 1 B MET 109 ? B MET 4 
14 1 Y 1 B GLU 110 ? B GLU 5 
15 1 Y 1 B GLU 111 ? B GLU 6 
16 1 Y 1 B ALA 112 ? B ALA 7 
17 1 Y 1 B SER 113 ? B SER 8 
18 1 Y 1 B LYS 114 ? B LYS 9 
# 
_pdbx_audit_support.funding_organization   'Wellcome Trust' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           087792 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 TETRADECANOYL-COA                                                                                                       MYA 
3 'PHOSPHATE ION'                                                                                                         PO4 
4 '1-[5-[4-fluoranyl-2-[2-(1,3,5-trimethylpyrazol-4-yl)ethoxy]phenyl]-2~{H}-indazol-3-yl]-~{N},~{N}-dimethyl-methanamine' 9M2 
5 'MAGNESIUM ION'                                                                                                         MG  
6 GLYCEROL                                                                                                                GOL 
7 'DIMETHYL SULFOXIDE'                                                                                                    DMS 
8 water                                                                                                                   HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
