data_9C8T
# 
_entry.id   9C8T 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9C8T         pdb_00009c8t 10.2210/pdb9c8t/pdb 
WWPDB D_1000284995 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C8T 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9C8N 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              li.wang-5@hotmail.com 
_pdbx_contact_author.name_first         Li 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8686-6627 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, L.'     1 0000-0002-8686-6627 
'Sietsema, D.' 2 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3669 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                88 
_citation.page_last                 88 
_citation.title                     
'Structural insight into the cGAS active site explains differences between therapeutically relevant species.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42004-025-01481-7 
_citation.pdbx_database_id_PubMed   40121343 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Skeldon, A.M.'    1  ?                   
primary 'Wang, L.'         2  ?                   
primary 'Sgarioto, N.'     3  ?                   
primary 'Beveridge, R.E.'  4  ?                   
primary 'Chan, S.'         5  0009-0004-8326-4227 
primary 'Dorich, S.'       6  ?                   
primary 'Dumais, V.'       7  ?                   
primary 'Fradet, N.'       8  ?                   
primary 'Gaudreault, S.'   9  ?                   
primary 'LeGros, P.'       10 ?                   
primary 'McKay, D.'        11 ?                   
primary 'Seliniotakis, R.' 12 ?                   
primary 'Sietsema, D.V.'   13 ?                   
primary 'Zhang, L.'        14 ?                   
primary 'Boily, M.O.'      15 ?                   
primary 'Burch, J.D.'      16 ?                   
primary 'Caron, A.'        17 ?                   
primary 'Fader, L.D.'      18 ?                   
primary 'Lama, L.'         19 ?                   
primary 'Xie, W.'          20 0000-0002-4550-6211 
primary 'Patel, D.J.'      21 0000-0002-9779-7778 
primary 'Tuschl, T.'       22 0000-0002-6483-5678 
primary 'Crackower, M.A.'  23 ?                   
primary 'Pike, K.A.'       24 0000-0003-3829-9661 
# 
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 'Cyclic GMP-AMP synthase'                                                                                     
42846.277 1   2.7.7.86 K427E ? ? 
2 non-polymer syn 'MAGNESIUM ION'                                                                                               
24.305    2   ?        ?     ? ? 
3 non-polymer syn 'ZINC ION'                                                                                                    
65.409    1   ?        ?     ? ? 
4 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                                                                 
506.196   1   ?        ?     ? ? 
5 non-polymer syn GLYCEROL                                                                                                      
92.094    1   ?        ?     ? ? 
6 non-polymer syn '1-[9-(6-aminopyridin-3-yl)-6,7-dichloro-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indol-2-yl]-2-hydroxyethan-1-one' 
391.251   1   ?        ?     ? ? 
7 water       nat water                                                                                                         
18.015    300 ?        ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;cGAMP synthase,cGAS,h-cGAS,2'3'-cGAMP synthase,Mab-21 domain-containing protein 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       
;SDAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVP
RIQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEK
ISVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKT
CCENKEEKCCRKDCLKLMKYLLEQLKERFKDEKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCL
RTEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SDAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVP
RIQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEK
ISVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKT
CCENKEEKCCRKDCLKLMKYLLEQLKERFKDEKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCL
RTEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MAGNESIUM ION'                                                                                               MG  
3 'ZINC ION'                                                                                                    ZN  
4 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                                                                 ANP 
5 GLYCEROL                                                                                                      GOL 
6 '1-[9-(6-aminopyridin-3-yl)-6,7-dichloro-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indol-2-yl]-2-hydroxyethan-1-one' JUJ 
7 water                                                                                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASP n 
1 3   ALA n 
1 4   ALA n 
1 5   PRO n 
1 6   GLY n 
1 7   ALA n 
1 8   SER n 
1 9   LYS n 
1 10  LEU n 
1 11  ARG n 
1 12  ALA n 
1 13  VAL n 
1 14  LEU n 
1 15  GLU n 
1 16  LYS n 
1 17  LEU n 
1 18  LYS n 
1 19  LEU n 
1 20  SER n 
1 21  ARG n 
1 22  ASP n 
1 23  ASP n 
1 24  ILE n 
1 25  SER n 
1 26  THR n 
1 27  ALA n 
1 28  ALA n 
1 29  GLY n 
1 30  MET n 
1 31  VAL n 
1 32  LYS n 
1 33  GLY n 
1 34  VAL n 
1 35  VAL n 
1 36  ASP n 
1 37  HIS n 
1 38  LEU n 
1 39  LEU n 
1 40  LEU n 
1 41  ARG n 
1 42  LEU n 
1 43  LYS n 
1 44  CYS n 
1 45  ASP n 
1 46  SER n 
1 47  ALA n 
1 48  PHE n 
1 49  ARG n 
1 50  GLY n 
1 51  VAL n 
1 52  GLY n 
1 53  LEU n 
1 54  LEU n 
1 55  ASN n 
1 56  THR n 
1 57  GLY n 
1 58  SER n 
1 59  TYR n 
1 60  TYR n 
1 61  GLU n 
1 62  HIS n 
1 63  VAL n 
1 64  LYS n 
1 65  ILE n 
1 66  SER n 
1 67  ALA n 
1 68  PRO n 
1 69  ASN n 
1 70  GLU n 
1 71  PHE n 
1 72  ASP n 
1 73  VAL n 
1 74  MET n 
1 75  PHE n 
1 76  LYS n 
1 77  LEU n 
1 78  GLU n 
1 79  VAL n 
1 80  PRO n 
1 81  ARG n 
1 82  ILE n 
1 83  GLN n 
1 84  LEU n 
1 85  GLU n 
1 86  GLU n 
1 87  TYR n 
1 88  SER n 
1 89  ASN n 
1 90  THR n 
1 91  ARG n 
1 92  ALA n 
1 93  TYR n 
1 94  TYR n 
1 95  PHE n 
1 96  VAL n 
1 97  LYS n 
1 98  PHE n 
1 99  LYS n 
1 100 ARG n 
1 101 ASN n 
1 102 PRO n 
1 103 LYS n 
1 104 GLU n 
1 105 ASN n 
1 106 PRO n 
1 107 LEU n 
1 108 SER n 
1 109 GLN n 
1 110 PHE n 
1 111 LEU n 
1 112 GLU n 
1 113 GLY n 
1 114 GLU n 
1 115 ILE n 
1 116 LEU n 
1 117 SER n 
1 118 ALA n 
1 119 SER n 
1 120 LYS n 
1 121 MET n 
1 122 LEU n 
1 123 SER n 
1 124 LYS n 
1 125 PHE n 
1 126 ARG n 
1 127 LYS n 
1 128 ILE n 
1 129 ILE n 
1 130 LYS n 
1 131 GLU n 
1 132 GLU n 
1 133 ILE n 
1 134 ASN n 
1 135 ASP n 
1 136 ILE n 
1 137 LYS n 
1 138 ASP n 
1 139 THR n 
1 140 ASP n 
1 141 VAL n 
1 142 ILE n 
1 143 MET n 
1 144 LYS n 
1 145 ARG n 
1 146 LYS n 
1 147 ARG n 
1 148 GLY n 
1 149 GLY n 
1 150 SER n 
1 151 PRO n 
1 152 ALA n 
1 153 VAL n 
1 154 THR n 
1 155 LEU n 
1 156 LEU n 
1 157 ILE n 
1 158 SER n 
1 159 GLU n 
1 160 LYS n 
1 161 ILE n 
1 162 SER n 
1 163 VAL n 
1 164 ASP n 
1 165 ILE n 
1 166 THR n 
1 167 LEU n 
1 168 ALA n 
1 169 LEU n 
1 170 GLU n 
1 171 SER n 
1 172 LYS n 
1 173 SER n 
1 174 SER n 
1 175 TRP n 
1 176 PRO n 
1 177 ALA n 
1 178 SER n 
1 179 THR n 
1 180 GLN n 
1 181 GLU n 
1 182 GLY n 
1 183 LEU n 
1 184 ARG n 
1 185 ILE n 
1 186 GLN n 
1 187 ASN n 
1 188 TRP n 
1 189 LEU n 
1 190 SER n 
1 191 ALA n 
1 192 LYS n 
1 193 VAL n 
1 194 ARG n 
1 195 LYS n 
1 196 GLN n 
1 197 LEU n 
1 198 ARG n 
1 199 LEU n 
1 200 LYS n 
1 201 PRO n 
1 202 PHE n 
1 203 TYR n 
1 204 LEU n 
1 205 VAL n 
1 206 PRO n 
1 207 LYS n 
1 208 HIS n 
1 209 ALA n 
1 210 LYS n 
1 211 GLU n 
1 212 GLY n 
1 213 ASN n 
1 214 GLY n 
1 215 PHE n 
1 216 GLN n 
1 217 GLU n 
1 218 GLU n 
1 219 THR n 
1 220 TRP n 
1 221 ARG n 
1 222 LEU n 
1 223 SER n 
1 224 PHE n 
1 225 SER n 
1 226 HIS n 
1 227 ILE n 
1 228 GLU n 
1 229 LYS n 
1 230 GLU n 
1 231 ILE n 
1 232 LEU n 
1 233 ASN n 
1 234 ASN n 
1 235 HIS n 
1 236 GLY n 
1 237 LYS n 
1 238 SER n 
1 239 LYS n 
1 240 THR n 
1 241 CYS n 
1 242 CYS n 
1 243 GLU n 
1 244 ASN n 
1 245 LYS n 
1 246 GLU n 
1 247 GLU n 
1 248 LYS n 
1 249 CYS n 
1 250 CYS n 
1 251 ARG n 
1 252 LYS n 
1 253 ASP n 
1 254 CYS n 
1 255 LEU n 
1 256 LYS n 
1 257 LEU n 
1 258 MET n 
1 259 LYS n 
1 260 TYR n 
1 261 LEU n 
1 262 LEU n 
1 263 GLU n 
1 264 GLN n 
1 265 LEU n 
1 266 LYS n 
1 267 GLU n 
1 268 ARG n 
1 269 PHE n 
1 270 LYS n 
1 271 ASP n 
1 272 GLU n 
1 273 LYS n 
1 274 HIS n 
1 275 LEU n 
1 276 ASP n 
1 277 LYS n 
1 278 PHE n 
1 279 SER n 
1 280 SER n 
1 281 TYR n 
1 282 HIS n 
1 283 VAL n 
1 284 LYS n 
1 285 THR n 
1 286 ALA n 
1 287 PHE n 
1 288 PHE n 
1 289 HIS n 
1 290 VAL n 
1 291 CYS n 
1 292 THR n 
1 293 GLN n 
1 294 ASN n 
1 295 PRO n 
1 296 GLN n 
1 297 ASP n 
1 298 SER n 
1 299 GLN n 
1 300 TRP n 
1 301 ASP n 
1 302 ARG n 
1 303 LYS n 
1 304 ASP n 
1 305 LEU n 
1 306 GLY n 
1 307 LEU n 
1 308 CYS n 
1 309 PHE n 
1 310 ASP n 
1 311 ASN n 
1 312 CYS n 
1 313 VAL n 
1 314 THR n 
1 315 TYR n 
1 316 PHE n 
1 317 LEU n 
1 318 GLN n 
1 319 CYS n 
1 320 LEU n 
1 321 ARG n 
1 322 THR n 
1 323 GLU n 
1 324 LYS n 
1 325 LEU n 
1 326 GLU n 
1 327 ASN n 
1 328 TYR n 
1 329 PHE n 
1 330 ILE n 
1 331 PRO n 
1 332 GLU n 
1 333 PHE n 
1 334 ASN n 
1 335 LEU n 
1 336 PHE n 
1 337 SER n 
1 338 SER n 
1 339 ASN n 
1 340 LEU n 
1 341 ILE n 
1 342 ASP n 
1 343 LYS n 
1 344 ARG n 
1 345 SER n 
1 346 LYS n 
1 347 GLU n 
1 348 PHE n 
1 349 LEU n 
1 350 THR n 
1 351 LYS n 
1 352 GLN n 
1 353 ILE n 
1 354 GLU n 
1 355 TYR n 
1 356 GLU n 
1 357 ARG n 
1 358 ASN n 
1 359 ASN n 
1 360 GLU n 
1 361 PHE n 
1 362 PRO n 
1 363 VAL n 
1 364 PHE n 
1 365 ASP n 
1 366 GLU n 
1 367 PHE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   367 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CGAS, C6orf150, MB21D1' 
_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              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ?                               'C10 H17 N6 O12 P3' 
506.196 
ARG 'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'        75.067  
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 
JUJ non-polymer         . 
'1-[9-(6-aminopyridin-3-yl)-6,7-dichloro-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indol-2-yl]-2-hydroxyethan-1-one' ? 
'C18 H16 Cl2 N4 O2' 391.251 
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  
PHE 'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?                               'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                               'C5 H11 N O2'       117.146 
ZN  non-polymer         . 'ZINC ION' ?                               'Zn 2'              65.409  
# 
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   SER 1   156 ?   ?   ?   A . n 
A 1 2   ASP 2   157 ?   ?   ?   A . n 
A 1 3   ALA 3   158 ?   ?   ?   A . n 
A 1 4   ALA 4   159 ?   ?   ?   A . n 
A 1 5   PRO 5   160 ?   ?   ?   A . n 
A 1 6   GLY 6   161 ?   ?   ?   A . n 
A 1 7   ALA 7   162 ?   ?   ?   A . n 
A 1 8   SER 8   163 163 SER SER A . n 
A 1 9   LYS 9   164 164 LYS LYS A . n 
A 1 10  LEU 10  165 165 LEU LEU A . n 
A 1 11  ARG 11  166 166 ARG ARG A . n 
A 1 12  ALA 12  167 167 ALA ALA A . n 
A 1 13  VAL 13  168 168 VAL VAL A . n 
A 1 14  LEU 14  169 169 LEU LEU A . n 
A 1 15  GLU 15  170 170 GLU GLU A . n 
A 1 16  LYS 16  171 171 LYS LYS A . n 
A 1 17  LEU 17  172 172 LEU LEU A . n 
A 1 18  LYS 18  173 173 LYS LYS A . n 
A 1 19  LEU 19  174 174 LEU LEU A . n 
A 1 20  SER 20  175 175 SER SER A . n 
A 1 21  ARG 21  176 176 ARG ARG A . n 
A 1 22  ASP 22  177 177 ASP ASP A . n 
A 1 23  ASP 23  178 178 ASP ASP A . n 
A 1 24  ILE 24  179 179 ILE ILE A . n 
A 1 25  SER 25  180 180 SER SER A . n 
A 1 26  THR 26  181 181 THR THR A . n 
A 1 27  ALA 27  182 182 ALA ALA A . n 
A 1 28  ALA 28  183 183 ALA ALA A . n 
A 1 29  GLY 29  184 184 GLY GLY A . n 
A 1 30  MET 30  185 185 MET MET A . n 
A 1 31  VAL 31  186 186 VAL VAL A . n 
A 1 32  LYS 32  187 187 LYS LYS A . n 
A 1 33  GLY 33  188 188 GLY GLY A . n 
A 1 34  VAL 34  189 189 VAL VAL A . n 
A 1 35  VAL 35  190 190 VAL VAL A . n 
A 1 36  ASP 36  191 191 ASP ASP A . n 
A 1 37  HIS 37  192 192 HIS HIS A . n 
A 1 38  LEU 38  193 193 LEU LEU A . n 
A 1 39  LEU 39  194 194 LEU LEU A . n 
A 1 40  LEU 40  195 195 LEU LEU A . n 
A 1 41  ARG 41  196 196 ARG ARG A . n 
A 1 42  LEU 42  197 197 LEU LEU A . n 
A 1 43  LYS 43  198 198 LYS LYS A . n 
A 1 44  CYS 44  199 199 CYS CYS A . n 
A 1 45  ASP 45  200 200 ASP ASP A . n 
A 1 46  SER 46  201 201 SER SER A . n 
A 1 47  ALA 47  202 202 ALA ALA A . n 
A 1 48  PHE 48  203 203 PHE PHE A . n 
A 1 49  ARG 49  204 204 ARG ARG A . n 
A 1 50  GLY 50  205 205 GLY GLY A . n 
A 1 51  VAL 51  206 206 VAL VAL A . n 
A 1 52  GLY 52  207 207 GLY GLY A . n 
A 1 53  LEU 53  208 208 LEU LEU A . n 
A 1 54  LEU 54  209 209 LEU LEU A . n 
A 1 55  ASN 55  210 210 ASN ASN A . n 
A 1 56  THR 56  211 211 THR THR A . n 
A 1 57  GLY 57  212 212 GLY GLY A . n 
A 1 58  SER 58  213 213 SER SER A . n 
A 1 59  TYR 59  214 214 TYR TYR A . n 
A 1 60  TYR 60  215 215 TYR TYR A . n 
A 1 61  GLU 61  216 216 GLU GLU A . n 
A 1 62  HIS 62  217 217 HIS HIS A . n 
A 1 63  VAL 63  218 218 VAL VAL A . n 
A 1 64  LYS 64  219 219 LYS LYS A . n 
A 1 65  ILE 65  220 220 ILE ILE A . n 
A 1 66  SER 66  221 221 SER SER A . n 
A 1 67  ALA 67  222 222 ALA ALA A . n 
A 1 68  PRO 68  223 223 PRO PRO A . n 
A 1 69  ASN 69  224 224 ASN ASN A . n 
A 1 70  GLU 70  225 225 GLU GLU A . n 
A 1 71  PHE 71  226 226 PHE PHE A . n 
A 1 72  ASP 72  227 227 ASP ASP A . n 
A 1 73  VAL 73  228 228 VAL VAL A . n 
A 1 74  MET 74  229 229 MET MET A . n 
A 1 75  PHE 75  230 230 PHE PHE A . n 
A 1 76  LYS 76  231 231 LYS LYS A . n 
A 1 77  LEU 77  232 232 LEU LEU A . n 
A 1 78  GLU 78  233 233 GLU GLU A . n 
A 1 79  VAL 79  234 234 VAL VAL A . n 
A 1 80  PRO 80  235 235 PRO PRO A . n 
A 1 81  ARG 81  236 236 ARG ARG A . n 
A 1 82  ILE 82  237 237 ILE ILE A . n 
A 1 83  GLN 83  238 238 GLN GLN A . n 
A 1 84  LEU 84  239 239 LEU LEU A . n 
A 1 85  GLU 85  240 240 GLU GLU A . n 
A 1 86  GLU 86  241 241 GLU GLU A . n 
A 1 87  TYR 87  242 242 TYR TYR A . n 
A 1 88  SER 88  243 243 SER SER A . n 
A 1 89  ASN 89  244 244 ASN ASN A . n 
A 1 90  THR 90  245 245 THR THR A . n 
A 1 91  ARG 91  246 246 ARG ARG A . n 
A 1 92  ALA 92  247 247 ALA ALA A . n 
A 1 93  TYR 93  248 248 TYR TYR A . n 
A 1 94  TYR 94  249 249 TYR TYR A . n 
A 1 95  PHE 95  250 250 PHE PHE A . n 
A 1 96  VAL 96  251 251 VAL VAL A . n 
A 1 97  LYS 97  252 252 LYS LYS A . n 
A 1 98  PHE 98  253 253 PHE PHE A . n 
A 1 99  LYS 99  254 ?   ?   ?   A . n 
A 1 100 ARG 100 255 ?   ?   ?   A . n 
A 1 101 ASN 101 256 ?   ?   ?   A . n 
A 1 102 PRO 102 257 ?   ?   ?   A . n 
A 1 103 LYS 103 258 ?   ?   ?   A . n 
A 1 104 GLU 104 259 ?   ?   ?   A . n 
A 1 105 ASN 105 260 ?   ?   ?   A . n 
A 1 106 PRO 106 261 261 PRO PRO A . n 
A 1 107 LEU 107 262 262 LEU LEU A . n 
A 1 108 SER 108 263 263 SER SER A . n 
A 1 109 GLN 109 264 264 GLN GLN A . n 
A 1 110 PHE 110 265 265 PHE PHE A . n 
A 1 111 LEU 111 266 266 LEU LEU A . n 
A 1 112 GLU 112 267 267 GLU GLU A . n 
A 1 113 GLY 113 268 268 GLY GLY A . n 
A 1 114 GLU 114 269 269 GLU GLU A . n 
A 1 115 ILE 115 270 270 ILE ILE A . n 
A 1 116 LEU 116 271 271 LEU LEU A . n 
A 1 117 SER 117 272 272 SER SER A . n 
A 1 118 ALA 118 273 273 ALA ALA A . n 
A 1 119 SER 119 274 274 SER SER A . n 
A 1 120 LYS 120 275 275 LYS LYS A . n 
A 1 121 MET 121 276 276 MET MET A . n 
A 1 122 LEU 122 277 277 LEU LEU A . n 
A 1 123 SER 123 278 278 SER SER A . n 
A 1 124 LYS 124 279 279 LYS LYS A . n 
A 1 125 PHE 125 280 280 PHE PHE A . n 
A 1 126 ARG 126 281 281 ARG ARG A . n 
A 1 127 LYS 127 282 282 LYS LYS A . n 
A 1 128 ILE 128 283 283 ILE ILE A . n 
A 1 129 ILE 129 284 284 ILE ILE A . n 
A 1 130 LYS 130 285 285 LYS LYS A . n 
A 1 131 GLU 131 286 286 GLU GLU A . n 
A 1 132 GLU 132 287 287 GLU GLU A . n 
A 1 133 ILE 133 288 288 ILE ILE A . n 
A 1 134 ASN 134 289 ?   ?   ?   A . n 
A 1 135 ASP 135 290 ?   ?   ?   A . n 
A 1 136 ILE 136 291 ?   ?   ?   A . n 
A 1 137 LYS 137 292 ?   ?   ?   A . n 
A 1 138 ASP 138 293 293 ASP ASP A . n 
A 1 139 THR 139 294 294 THR THR A . n 
A 1 140 ASP 140 295 295 ASP ASP A . n 
A 1 141 VAL 141 296 296 VAL VAL A . n 
A 1 142 ILE 142 297 297 ILE ILE A . n 
A 1 143 MET 143 298 298 MET MET A . n 
A 1 144 LYS 144 299 299 LYS LYS A . n 
A 1 145 ARG 145 300 300 ARG ARG A . n 
A 1 146 LYS 146 301 301 LYS LYS A . n 
A 1 147 ARG 147 302 ?   ?   ?   A . n 
A 1 148 GLY 148 303 ?   ?   ?   A . n 
A 1 149 GLY 149 304 ?   ?   ?   A . n 
A 1 150 SER 150 305 305 SER SER A . n 
A 1 151 PRO 151 306 306 PRO PRO A . n 
A 1 152 ALA 152 307 307 ALA ALA A . n 
A 1 153 VAL 153 308 308 VAL VAL A . n 
A 1 154 THR 154 309 309 THR THR A . n 
A 1 155 LEU 155 310 310 LEU LEU A . n 
A 1 156 LEU 156 311 311 LEU LEU A . n 
A 1 157 ILE 157 312 312 ILE ILE A . n 
A 1 158 SER 158 313 313 SER SER A . n 
A 1 159 GLU 159 314 314 GLU GLU A . n 
A 1 160 LYS 160 315 315 LYS LYS A . n 
A 1 161 ILE 161 316 316 ILE ILE A . n 
A 1 162 SER 162 317 317 SER SER A . n 
A 1 163 VAL 163 318 318 VAL VAL A . n 
A 1 164 ASP 164 319 319 ASP ASP A . n 
A 1 165 ILE 165 320 320 ILE ILE A . n 
A 1 166 THR 166 321 321 THR THR A . n 
A 1 167 LEU 167 322 322 LEU LEU A . n 
A 1 168 ALA 168 323 323 ALA ALA A . n 
A 1 169 LEU 169 324 324 LEU LEU A . n 
A 1 170 GLU 170 325 325 GLU GLU A . n 
A 1 171 SER 171 326 326 SER SER A . n 
A 1 172 LYS 172 327 327 LYS LYS A . n 
A 1 173 SER 173 328 328 SER SER A . n 
A 1 174 SER 174 329 329 SER SER A . n 
A 1 175 TRP 175 330 330 TRP TRP A . n 
A 1 176 PRO 176 331 331 PRO PRO A . n 
A 1 177 ALA 177 332 332 ALA ALA A . n 
A 1 178 SER 178 333 333 SER SER A . n 
A 1 179 THR 179 334 334 THR THR A . n 
A 1 180 GLN 180 335 335 GLN GLN A . n 
A 1 181 GLU 181 336 336 GLU GLU A . n 
A 1 182 GLY 182 337 337 GLY GLY A . n 
A 1 183 LEU 183 338 338 LEU LEU A . n 
A 1 184 ARG 184 339 339 ARG ARG A . n 
A 1 185 ILE 185 340 340 ILE ILE A . n 
A 1 186 GLN 186 341 341 GLN GLN A . n 
A 1 187 ASN 187 342 342 ASN ASN A . n 
A 1 188 TRP 188 343 343 TRP TRP A . n 
A 1 189 LEU 189 344 344 LEU LEU A . n 
A 1 190 SER 190 345 345 SER SER A . n 
A 1 191 ALA 191 346 346 ALA ALA A . n 
A 1 192 LYS 192 347 347 LYS LYS A . n 
A 1 193 VAL 193 348 348 VAL VAL A . n 
A 1 194 ARG 194 349 349 ARG ARG A . n 
A 1 195 LYS 195 350 350 LYS LYS A . n 
A 1 196 GLN 196 351 351 GLN GLN A . n 
A 1 197 LEU 197 352 352 LEU LEU A . n 
A 1 198 ARG 198 353 353 ARG ARG A . n 
A 1 199 LEU 199 354 354 LEU LEU A . n 
A 1 200 LYS 200 355 355 LYS LYS A . n 
A 1 201 PRO 201 356 356 PRO PRO A . n 
A 1 202 PHE 202 357 357 PHE PHE A . n 
A 1 203 TYR 203 358 358 TYR TYR A . n 
A 1 204 LEU 204 359 359 LEU LEU A . n 
A 1 205 VAL 205 360 360 VAL VAL A . n 
A 1 206 PRO 206 361 361 PRO PRO A . n 
A 1 207 LYS 207 362 362 LYS LYS A . n 
A 1 208 HIS 208 363 363 HIS HIS A . n 
A 1 209 ALA 209 364 364 ALA ALA A . n 
A 1 210 LYS 210 365 365 LYS LYS A . n 
A 1 211 GLU 211 366 366 GLU GLU A . n 
A 1 212 GLY 212 367 ?   ?   ?   A . n 
A 1 213 ASN 213 368 ?   ?   ?   A . n 
A 1 214 GLY 214 369 369 GLY GLY A . n 
A 1 215 PHE 215 370 370 PHE PHE A . n 
A 1 216 GLN 216 371 371 GLN GLN A . n 
A 1 217 GLU 217 372 372 GLU GLU A . n 
A 1 218 GLU 218 373 373 GLU GLU A . n 
A 1 219 THR 219 374 374 THR THR A . n 
A 1 220 TRP 220 375 375 TRP TRP A . n 
A 1 221 ARG 221 376 376 ARG ARG A . n 
A 1 222 LEU 222 377 377 LEU LEU A . n 
A 1 223 SER 223 378 378 SER SER A . n 
A 1 224 PHE 224 379 379 PHE PHE A . n 
A 1 225 SER 225 380 380 SER SER A . n 
A 1 226 HIS 226 381 381 HIS HIS A . n 
A 1 227 ILE 227 382 382 ILE ILE A . n 
A 1 228 GLU 228 383 383 GLU GLU A . n 
A 1 229 LYS 229 384 384 LYS LYS A . n 
A 1 230 GLU 230 385 385 GLU GLU A . n 
A 1 231 ILE 231 386 386 ILE ILE A . n 
A 1 232 LEU 232 387 387 LEU LEU A . n 
A 1 233 ASN 233 388 388 ASN ASN A . n 
A 1 234 ASN 234 389 389 ASN ASN A . n 
A 1 235 HIS 235 390 390 HIS HIS A . n 
A 1 236 GLY 236 391 391 GLY GLY A . n 
A 1 237 LYS 237 392 392 LYS LYS A . n 
A 1 238 SER 238 393 393 SER SER A . n 
A 1 239 LYS 239 394 394 LYS LYS A . n 
A 1 240 THR 240 395 395 THR THR A . n 
A 1 241 CYS 241 396 396 CYS CYS A . n 
A 1 242 CYS 242 397 397 CYS CYS A . n 
A 1 243 GLU 243 398 398 GLU GLU A . n 
A 1 244 ASN 244 399 399 ASN ASN A . n 
A 1 245 LYS 245 400 400 LYS LYS A . n 
A 1 246 GLU 246 401 401 GLU GLU A . n 
A 1 247 GLU 247 402 402 GLU GLU A . n 
A 1 248 LYS 248 403 403 LYS LYS A . n 
A 1 249 CYS 249 404 404 CYS CYS A . n 
A 1 250 CYS 250 405 405 CYS CYS A . n 
A 1 251 ARG 251 406 406 ARG ARG A . n 
A 1 252 LYS 252 407 407 LYS LYS A . n 
A 1 253 ASP 253 408 408 ASP ASP A . n 
A 1 254 CYS 254 409 409 CYS CYS A . n 
A 1 255 LEU 255 410 410 LEU LEU A . n 
A 1 256 LYS 256 411 411 LYS LYS A . n 
A 1 257 LEU 257 412 412 LEU LEU A . n 
A 1 258 MET 258 413 413 MET MET A . n 
A 1 259 LYS 259 414 414 LYS LYS A . n 
A 1 260 TYR 260 415 415 TYR TYR A . n 
A 1 261 LEU 261 416 416 LEU LEU A . n 
A 1 262 LEU 262 417 417 LEU LEU A . n 
A 1 263 GLU 263 418 418 GLU GLU A . n 
A 1 264 GLN 264 419 419 GLN GLN A . n 
A 1 265 LEU 265 420 420 LEU LEU A . n 
A 1 266 LYS 266 421 421 LYS LYS A . n 
A 1 267 GLU 267 422 422 GLU GLU A . n 
A 1 268 ARG 268 423 423 ARG ARG A . n 
A 1 269 PHE 269 424 424 PHE PHE A . n 
A 1 270 LYS 270 425 425 LYS LYS A . n 
A 1 271 ASP 271 426 426 ASP ASP A . n 
A 1 272 GLU 272 427 427 GLU GLU A . n 
A 1 273 LYS 273 428 428 LYS LYS A . n 
A 1 274 HIS 274 429 429 HIS HIS A . n 
A 1 275 LEU 275 430 430 LEU LEU A . n 
A 1 276 ASP 276 431 431 ASP ASP A . n 
A 1 277 LYS 277 432 432 LYS LYS A . n 
A 1 278 PHE 278 433 433 PHE PHE A . n 
A 1 279 SER 279 434 434 SER SER A . n 
A 1 280 SER 280 435 435 SER SER A . n 
A 1 281 TYR 281 436 436 TYR TYR A . n 
A 1 282 HIS 282 437 437 HIS HIS A . n 
A 1 283 VAL 283 438 438 VAL VAL A . n 
A 1 284 LYS 284 439 439 LYS LYS A . n 
A 1 285 THR 285 440 440 THR THR A . n 
A 1 286 ALA 286 441 441 ALA ALA A . n 
A 1 287 PHE 287 442 442 PHE PHE A . n 
A 1 288 PHE 288 443 443 PHE PHE A . n 
A 1 289 HIS 289 444 444 HIS HIS A . n 
A 1 290 VAL 290 445 445 VAL VAL A . n 
A 1 291 CYS 291 446 446 CYS CYS A . n 
A 1 292 THR 292 447 447 THR THR A . n 
A 1 293 GLN 293 448 448 GLN GLN A . n 
A 1 294 ASN 294 449 449 ASN ASN A . n 
A 1 295 PRO 295 450 450 PRO PRO A . n 
A 1 296 GLN 296 451 451 GLN GLN A . n 
A 1 297 ASP 297 452 452 ASP ASP A . n 
A 1 298 SER 298 453 453 SER SER A . n 
A 1 299 GLN 299 454 454 GLN GLN A . n 
A 1 300 TRP 300 455 455 TRP TRP A . n 
A 1 301 ASP 301 456 456 ASP ASP A . n 
A 1 302 ARG 302 457 457 ARG ARG A . n 
A 1 303 LYS 303 458 458 LYS LYS A . n 
A 1 304 ASP 304 459 459 ASP ASP A . n 
A 1 305 LEU 305 460 460 LEU LEU A . n 
A 1 306 GLY 306 461 461 GLY GLY A . n 
A 1 307 LEU 307 462 462 LEU LEU A . n 
A 1 308 CYS 308 463 463 CYS CYS A . n 
A 1 309 PHE 309 464 464 PHE PHE A . n 
A 1 310 ASP 310 465 465 ASP ASP A . n 
A 1 311 ASN 311 466 466 ASN ASN A . n 
A 1 312 CYS 312 467 467 CYS CYS A . n 
A 1 313 VAL 313 468 468 VAL VAL A . n 
A 1 314 THR 314 469 469 THR THR A . n 
A 1 315 TYR 315 470 470 TYR TYR A . n 
A 1 316 PHE 316 471 471 PHE PHE A . n 
A 1 317 LEU 317 472 472 LEU LEU A . n 
A 1 318 GLN 318 473 473 GLN GLN A . n 
A 1 319 CYS 319 474 474 CYS CYS A . n 
A 1 320 LEU 320 475 475 LEU LEU A . n 
A 1 321 ARG 321 476 476 ARG ARG A . n 
A 1 322 THR 322 477 477 THR THR A . n 
A 1 323 GLU 323 478 478 GLU GLU A . n 
A 1 324 LYS 324 479 479 LYS LYS A . n 
A 1 325 LEU 325 480 480 LEU LEU A . n 
A 1 326 GLU 326 481 481 GLU GLU A . n 
A 1 327 ASN 327 482 482 ASN ASN A . n 
A 1 328 TYR 328 483 483 TYR TYR A . n 
A 1 329 PHE 329 484 484 PHE PHE A . n 
A 1 330 ILE 330 485 485 ILE ILE A . n 
A 1 331 PRO 331 486 486 PRO PRO A . n 
A 1 332 GLU 332 487 487 GLU GLU A . n 
A 1 333 PHE 333 488 488 PHE PHE A . n 
A 1 334 ASN 334 489 489 ASN ASN A . n 
A 1 335 LEU 335 490 490 LEU LEU A . n 
A 1 336 PHE 336 491 491 PHE PHE A . n 
A 1 337 SER 337 492 492 SER SER A . n 
A 1 338 SER 338 493 493 SER SER A . n 
A 1 339 ASN 339 494 494 ASN ASN A . n 
A 1 340 LEU 340 495 495 LEU LEU A . n 
A 1 341 ILE 341 496 496 ILE ILE A . n 
A 1 342 ASP 342 497 497 ASP ASP A . n 
A 1 343 LYS 343 498 498 LYS LYS A . n 
A 1 344 ARG 344 499 499 ARG ARG A . n 
A 1 345 SER 345 500 500 SER SER A . n 
A 1 346 LYS 346 501 501 LYS LYS A . n 
A 1 347 GLU 347 502 502 GLU GLU A . n 
A 1 348 PHE 348 503 503 PHE PHE A . n 
A 1 349 LEU 349 504 504 LEU LEU A . n 
A 1 350 THR 350 505 505 THR THR A . n 
A 1 351 LYS 351 506 506 LYS LYS A . n 
A 1 352 GLN 352 507 507 GLN GLN A . n 
A 1 353 ILE 353 508 508 ILE ILE A . n 
A 1 354 GLU 354 509 509 GLU GLU A . n 
A 1 355 TYR 355 510 510 TYR TYR A . n 
A 1 356 GLU 356 511 511 GLU GLU A . n 
A 1 357 ARG 357 512 512 ARG ARG A . n 
A 1 358 ASN 358 513 513 ASN ASN A . n 
A 1 359 ASN 359 514 514 ASN ASN A . n 
A 1 360 GLU 360 515 515 GLU GLU A . n 
A 1 361 PHE 361 516 516 PHE PHE A . n 
A 1 362 PRO 362 517 517 PRO PRO A . n 
A 1 363 VAL 363 518 518 VAL VAL A . n 
A 1 364 PHE 364 519 519 PHE PHE A . n 
A 1 365 ASP 365 520 520 ASP ASP A . n 
A 1 366 GLU 366 521 ?   ?   ?   A . n 
A 1 367 PHE 367 522 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        JUJ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   JUJ 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 MG  1   601  1   MG  MG  A . 
C 2 MG  1   602  2   MG  MG  A . 
D 3 ZN  1   603  603 ZN  ZN  A . 
E 4 ANP 1   604  604 ANP ANP A . 
F 5 GOL 1   605  605 GOL GOL A . 
G 6 JUJ 1   606  606 JUJ LIG A . 
H 7 HOH 1   701  340 HOH HOH A . 
H 7 HOH 2   702  277 HOH HOH A . 
H 7 HOH 3   703  307 HOH HOH A . 
H 7 HOH 4   704  262 HOH HOH A . 
H 7 HOH 5   705  145 HOH HOH A . 
H 7 HOH 6   706  132 HOH HOH A . 
H 7 HOH 7   707  70  HOH HOH A . 
H 7 HOH 8   708  249 HOH HOH A . 
H 7 HOH 9   709  268 HOH HOH A . 
H 7 HOH 10  710  161 HOH HOH A . 
H 7 HOH 11  711  209 HOH HOH A . 
H 7 HOH 12  712  306 HOH HOH A . 
H 7 HOH 13  713  199 HOH HOH A . 
H 7 HOH 14  714  309 HOH HOH A . 
H 7 HOH 15  715  225 HOH HOH A . 
H 7 HOH 16  716  220 HOH HOH A . 
H 7 HOH 17  717  200 HOH HOH A . 
H 7 HOH 18  718  76  HOH HOH A . 
H 7 HOH 19  719  125 HOH HOH A . 
H 7 HOH 20  720  95  HOH HOH A . 
H 7 HOH 21  721  27  HOH HOH A . 
H 7 HOH 22  722  115 HOH HOH A . 
H 7 HOH 23  723  15  HOH HOH A . 
H 7 HOH 24  724  55  HOH HOH A . 
H 7 HOH 25  725  281 HOH HOH A . 
H 7 HOH 26  726  336 HOH HOH A . 
H 7 HOH 27  727  169 HOH HOH A . 
H 7 HOH 28  728  75  HOH HOH A . 
H 7 HOH 29  729  165 HOH HOH A . 
H 7 HOH 30  730  73  HOH HOH A . 
H 7 HOH 31  731  190 HOH HOH A . 
H 7 HOH 32  732  60  HOH HOH A . 
H 7 HOH 33  733  194 HOH HOH A . 
H 7 HOH 34  734  19  HOH HOH A . 
H 7 HOH 35  735  214 HOH HOH A . 
H 7 HOH 36  736  149 HOH HOH A . 
H 7 HOH 37  737  157 HOH HOH A . 
H 7 HOH 38  738  81  HOH HOH A . 
H 7 HOH 39  739  77  HOH HOH A . 
H 7 HOH 40  740  201 HOH HOH A . 
H 7 HOH 41  741  228 HOH HOH A . 
H 7 HOH 42  742  246 HOH HOH A . 
H 7 HOH 43  743  85  HOH HOH A . 
H 7 HOH 44  744  109 HOH HOH A . 
H 7 HOH 45  745  124 HOH HOH A . 
H 7 HOH 46  746  242 HOH HOH A . 
H 7 HOH 47  747  135 HOH HOH A . 
H 7 HOH 48  748  97  HOH HOH A . 
H 7 HOH 49  749  134 HOH HOH A . 
H 7 HOH 50  750  105 HOH HOH A . 
H 7 HOH 51  751  338 HOH HOH A . 
H 7 HOH 52  752  53  HOH HOH A . 
H 7 HOH 53  753  146 HOH HOH A . 
H 7 HOH 54  754  168 HOH HOH A . 
H 7 HOH 55  755  99  HOH HOH A . 
H 7 HOH 56  756  151 HOH HOH A . 
H 7 HOH 57  757  1   HOH HOH A . 
H 7 HOH 58  758  317 HOH HOH A . 
H 7 HOH 59  759  52  HOH HOH A . 
H 7 HOH 60  760  304 HOH HOH A . 
H 7 HOH 61  761  341 HOH HOH A . 
H 7 HOH 62  762  108 HOH HOH A . 
H 7 HOH 63  763  23  HOH HOH A . 
H 7 HOH 64  764  164 HOH HOH A . 
H 7 HOH 65  765  284 HOH HOH A . 
H 7 HOH 66  766  11  HOH HOH A . 
H 7 HOH 67  767  158 HOH HOH A . 
H 7 HOH 68  768  230 HOH HOH A . 
H 7 HOH 69  769  285 HOH HOH A . 
H 7 HOH 70  770  39  HOH HOH A . 
H 7 HOH 71  771  88  HOH HOH A . 
H 7 HOH 72  772  65  HOH HOH A . 
H 7 HOH 73  773  66  HOH HOH A . 
H 7 HOH 74  774  245 HOH HOH A . 
H 7 HOH 75  775  50  HOH HOH A . 
H 7 HOH 76  776  82  HOH HOH A . 
H 7 HOH 77  777  86  HOH HOH A . 
H 7 HOH 78  778  324 HOH HOH A . 
H 7 HOH 79  779  79  HOH HOH A . 
H 7 HOH 80  780  46  HOH HOH A . 
H 7 HOH 81  781  17  HOH HOH A . 
H 7 HOH 82  782  110 HOH HOH A . 
H 7 HOH 83  783  51  HOH HOH A . 
H 7 HOH 84  784  107 HOH HOH A . 
H 7 HOH 85  785  5   HOH HOH A . 
H 7 HOH 86  786  183 HOH HOH A . 
H 7 HOH 87  787  78  HOH HOH A . 
H 7 HOH 88  788  312 HOH HOH A . 
H 7 HOH 89  789  172 HOH HOH A . 
H 7 HOH 90  790  104 HOH HOH A . 
H 7 HOH 91  791  280 HOH HOH A . 
H 7 HOH 92  792  103 HOH HOH A . 
H 7 HOH 93  793  94  HOH HOH A . 
H 7 HOH 94  794  49  HOH HOH A . 
H 7 HOH 95  795  271 HOH HOH A . 
H 7 HOH 96  796  133 HOH HOH A . 
H 7 HOH 97  797  3   HOH HOH A . 
H 7 HOH 98  798  42  HOH HOH A . 
H 7 HOH 99  799  113 HOH HOH A . 
H 7 HOH 100 800  236 HOH HOH A . 
H 7 HOH 101 801  167 HOH HOH A . 
H 7 HOH 102 802  247 HOH HOH A . 
H 7 HOH 103 803  13  HOH HOH A . 
H 7 HOH 104 804  37  HOH HOH A . 
H 7 HOH 105 805  16  HOH HOH A . 
H 7 HOH 106 806  48  HOH HOH A . 
H 7 HOH 107 807  180 HOH HOH A . 
H 7 HOH 108 808  6   HOH HOH A . 
H 7 HOH 109 809  114 HOH HOH A . 
H 7 HOH 110 810  206 HOH HOH A . 
H 7 HOH 111 811  106 HOH HOH A . 
H 7 HOH 112 812  120 HOH HOH A . 
H 7 HOH 113 813  62  HOH HOH A . 
H 7 HOH 114 814  10  HOH HOH A . 
H 7 HOH 115 815  14  HOH HOH A . 
H 7 HOH 116 816  252 HOH HOH A . 
H 7 HOH 117 817  330 HOH HOH A . 
H 7 HOH 118 818  176 HOH HOH A . 
H 7 HOH 119 819  98  HOH HOH A . 
H 7 HOH 120 820  20  HOH HOH A . 
H 7 HOH 121 821  219 HOH HOH A . 
H 7 HOH 122 822  154 HOH HOH A . 
H 7 HOH 123 823  226 HOH HOH A . 
H 7 HOH 124 824  9   HOH HOH A . 
H 7 HOH 125 825  21  HOH HOH A . 
H 7 HOH 126 826  26  HOH HOH A . 
H 7 HOH 127 827  18  HOH HOH A . 
H 7 HOH 128 828  238 HOH HOH A . 
H 7 HOH 129 829  181 HOH HOH A . 
H 7 HOH 130 830  43  HOH HOH A . 
H 7 HOH 131 831  224 HOH HOH A . 
H 7 HOH 132 832  213 HOH HOH A . 
H 7 HOH 133 833  80  HOH HOH A . 
H 7 HOH 134 834  175 HOH HOH A . 
H 7 HOH 135 835  139 HOH HOH A . 
H 7 HOH 136 836  89  HOH HOH A . 
H 7 HOH 137 837  118 HOH HOH A . 
H 7 HOH 138 838  58  HOH HOH A . 
H 7 HOH 139 839  56  HOH HOH A . 
H 7 HOH 140 840  153 HOH HOH A . 
H 7 HOH 141 841  96  HOH HOH A . 
H 7 HOH 142 842  91  HOH HOH A . 
H 7 HOH 143 843  163 HOH HOH A . 
H 7 HOH 144 844  38  HOH HOH A . 
H 7 HOH 145 845  129 HOH HOH A . 
H 7 HOH 146 846  162 HOH HOH A . 
H 7 HOH 147 847  126 HOH HOH A . 
H 7 HOH 148 848  69  HOH HOH A . 
H 7 HOH 149 849  64  HOH HOH A . 
H 7 HOH 150 850  297 HOH HOH A . 
H 7 HOH 151 851  318 HOH HOH A . 
H 7 HOH 152 852  7   HOH HOH A . 
H 7 HOH 153 853  87  HOH HOH A . 
H 7 HOH 154 854  74  HOH HOH A . 
H 7 HOH 155 855  195 HOH HOH A . 
H 7 HOH 156 856  83  HOH HOH A . 
H 7 HOH 157 857  2   HOH HOH A . 
H 7 HOH 158 858  217 HOH HOH A . 
H 7 HOH 159 859  223 HOH HOH A . 
H 7 HOH 160 860  142 HOH HOH A . 
H 7 HOH 161 861  188 HOH HOH A . 
H 7 HOH 162 862  101 HOH HOH A . 
H 7 HOH 163 863  47  HOH HOH A . 
H 7 HOH 164 864  40  HOH HOH A . 
H 7 HOH 165 865  63  HOH HOH A . 
H 7 HOH 166 866  155 HOH HOH A . 
H 7 HOH 167 867  269 HOH HOH A . 
H 7 HOH 168 868  90  HOH HOH A . 
H 7 HOH 169 869  36  HOH HOH A . 
H 7 HOH 170 870  22  HOH HOH A . 
H 7 HOH 171 871  202 HOH HOH A . 
H 7 HOH 172 872  68  HOH HOH A . 
H 7 HOH 173 873  191 HOH HOH A . 
H 7 HOH 174 874  218 HOH HOH A . 
H 7 HOH 175 875  25  HOH HOH A . 
H 7 HOH 176 876  35  HOH HOH A . 
H 7 HOH 177 877  182 HOH HOH A . 
H 7 HOH 178 878  117 HOH HOH A . 
H 7 HOH 179 879  334 HOH HOH A . 
H 7 HOH 180 880  263 HOH HOH A . 
H 7 HOH 181 881  171 HOH HOH A . 
H 7 HOH 182 882  211 HOH HOH A . 
H 7 HOH 183 883  100 HOH HOH A . 
H 7 HOH 184 884  170 HOH HOH A . 
H 7 HOH 185 885  12  HOH HOH A . 
H 7 HOH 186 886  4   HOH HOH A . 
H 7 HOH 187 887  184 HOH HOH A . 
H 7 HOH 188 888  160 HOH HOH A . 
H 7 HOH 189 889  28  HOH HOH A . 
H 7 HOH 190 890  259 HOH HOH A . 
H 7 HOH 191 891  54  HOH HOH A . 
H 7 HOH 192 892  44  HOH HOH A . 
H 7 HOH 193 893  127 HOH HOH A . 
H 7 HOH 194 894  173 HOH HOH A . 
H 7 HOH 195 895  335 HOH HOH A . 
H 7 HOH 196 896  45  HOH HOH A . 
H 7 HOH 197 897  232 HOH HOH A . 
H 7 HOH 198 898  152 HOH HOH A . 
H 7 HOH 199 899  294 HOH HOH A . 
H 7 HOH 200 900  8   HOH HOH A . 
H 7 HOH 201 901  266 HOH HOH A . 
H 7 HOH 202 902  41  HOH HOH A . 
H 7 HOH 203 903  196 HOH HOH A . 
H 7 HOH 204 904  137 HOH HOH A . 
H 7 HOH 205 905  178 HOH HOH A . 
H 7 HOH 206 906  189 HOH HOH A . 
H 7 HOH 207 907  293 HOH HOH A . 
H 7 HOH 208 908  121 HOH HOH A . 
H 7 HOH 209 909  116 HOH HOH A . 
H 7 HOH 210 910  61  HOH HOH A . 
H 7 HOH 211 911  141 HOH HOH A . 
H 7 HOH 212 912  339 HOH HOH A . 
H 7 HOH 213 913  235 HOH HOH A . 
H 7 HOH 214 914  111 HOH HOH A . 
H 7 HOH 215 915  210 HOH HOH A . 
H 7 HOH 216 916  67  HOH HOH A . 
H 7 HOH 217 917  29  HOH HOH A . 
H 7 HOH 218 918  185 HOH HOH A . 
H 7 HOH 219 919  93  HOH HOH A . 
H 7 HOH 220 920  140 HOH HOH A . 
H 7 HOH 221 921  186 HOH HOH A . 
H 7 HOH 222 922  240 HOH HOH A . 
H 7 HOH 223 923  207 HOH HOH A . 
H 7 HOH 224 924  208 HOH HOH A . 
H 7 HOH 225 925  144 HOH HOH A . 
H 7 HOH 226 926  237 HOH HOH A . 
H 7 HOH 227 927  329 HOH HOH A . 
H 7 HOH 228 928  59  HOH HOH A . 
H 7 HOH 229 929  279 HOH HOH A . 
H 7 HOH 230 930  241 HOH HOH A . 
H 7 HOH 231 931  24  HOH HOH A . 
H 7 HOH 232 932  128 HOH HOH A . 
H 7 HOH 233 933  102 HOH HOH A . 
H 7 HOH 234 934  222 HOH HOH A . 
H 7 HOH 235 935  323 HOH HOH A . 
H 7 HOH 236 936  159 HOH HOH A . 
H 7 HOH 237 937  302 HOH HOH A . 
H 7 HOH 238 938  204 HOH HOH A . 
H 7 HOH 239 939  303 HOH HOH A . 
H 7 HOH 240 940  33  HOH HOH A . 
H 7 HOH 241 941  275 HOH HOH A . 
H 7 HOH 242 942  136 HOH HOH A . 
H 7 HOH 243 943  342 HOH HOH A . 
H 7 HOH 244 944  314 HOH HOH A . 
H 7 HOH 245 945  265 HOH HOH A . 
H 7 HOH 246 946  261 HOH HOH A . 
H 7 HOH 247 947  251 HOH HOH A . 
H 7 HOH 248 948  32  HOH HOH A . 
H 7 HOH 249 949  248 HOH HOH A . 
H 7 HOH 250 950  254 HOH HOH A . 
H 7 HOH 251 951  112 HOH HOH A . 
H 7 HOH 252 952  138 HOH HOH A . 
H 7 HOH 253 953  288 HOH HOH A . 
H 7 HOH 254 954  30  HOH HOH A . 
H 7 HOH 255 955  290 HOH HOH A . 
H 7 HOH 256 956  31  HOH HOH A . 
H 7 HOH 257 957  130 HOH HOH A . 
H 7 HOH 258 958  233 HOH HOH A . 
H 7 HOH 259 959  260 HOH HOH A . 
H 7 HOH 260 960  325 HOH HOH A . 
H 7 HOH 261 961  234 HOH HOH A . 
H 7 HOH 262 962  72  HOH HOH A . 
H 7 HOH 263 963  278 HOH HOH A . 
H 7 HOH 264 964  205 HOH HOH A . 
H 7 HOH 265 965  84  HOH HOH A . 
H 7 HOH 266 966  315 HOH HOH A . 
H 7 HOH 267 967  316 HOH HOH A . 
H 7 HOH 268 968  156 HOH HOH A . 
H 7 HOH 269 969  57  HOH HOH A . 
H 7 HOH 270 970  227 HOH HOH A . 
H 7 HOH 271 971  258 HOH HOH A . 
H 7 HOH 272 972  119 HOH HOH A . 
H 7 HOH 273 973  229 HOH HOH A . 
H 7 HOH 274 974  216 HOH HOH A . 
H 7 HOH 275 975  322 HOH HOH A . 
H 7 HOH 276 976  92  HOH HOH A . 
H 7 HOH 277 977  203 HOH HOH A . 
H 7 HOH 278 978  300 HOH HOH A . 
H 7 HOH 279 979  179 HOH HOH A . 
H 7 HOH 280 980  212 HOH HOH A . 
H 7 HOH 281 981  243 HOH HOH A . 
H 7 HOH 282 982  123 HOH HOH A . 
H 7 HOH 283 983  273 HOH HOH A . 
H 7 HOH 284 984  253 HOH HOH A . 
H 7 HOH 285 985  231 HOH HOH A . 
H 7 HOH 286 986  143 HOH HOH A . 
H 7 HOH 287 987  267 HOH HOH A . 
H 7 HOH 288 988  34  HOH HOH A . 
H 7 HOH 289 989  250 HOH HOH A . 
H 7 HOH 290 990  292 HOH HOH A . 
H 7 HOH 291 991  147 HOH HOH A . 
H 7 HOH 292 992  276 HOH HOH A . 
H 7 HOH 293 993  255 HOH HOH A . 
H 7 HOH 294 994  274 HOH HOH A . 
H 7 HOH 295 995  71  HOH HOH A . 
H 7 HOH 296 996  192 HOH HOH A . 
H 7 HOH 297 997  308 HOH HOH A . 
H 7 HOH 298 998  150 HOH HOH A . 
H 7 HOH 299 999  221 HOH HOH A . 
H 7 HOH 300 1000 264 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 236 ? CG  ? A ARG 81  CG  
2  1 Y 1 A ARG 236 ? CD  ? A ARG 81  CD  
3  1 Y 1 A ARG 236 ? NE  ? A ARG 81  NE  
4  1 Y 1 A ARG 236 ? CZ  ? A ARG 81  CZ  
5  1 Y 1 A ARG 236 ? NH1 ? A ARG 81  NH1 
6  1 Y 1 A ARG 236 ? NH2 ? A ARG 81  NH2 
7  1 Y 1 A GLU 267 ? CG  ? A GLU 112 CG  
8  1 Y 1 A GLU 267 ? CD  ? A GLU 112 CD  
9  1 Y 1 A GLU 267 ? OE1 ? A GLU 112 OE1 
10 1 Y 1 A GLU 267 ? OE2 ? A GLU 112 OE2 
11 1 Y 1 A GLU 269 ? CG  ? A GLU 114 CG  
12 1 Y 1 A GLU 269 ? CD  ? A GLU 114 CD  
13 1 Y 1 A GLU 269 ? OE1 ? A GLU 114 OE1 
14 1 Y 1 A GLU 269 ? OE2 ? A GLU 114 OE2 
15 1 Y 1 A ASP 293 ? CG  ? A ASP 138 CG  
16 1 Y 1 A ASP 293 ? OD1 ? A ASP 138 OD1 
17 1 Y 1 A ASP 293 ? OD2 ? A ASP 138 OD2 
18 1 Y 1 A GLU 314 ? CG  ? A GLU 159 CG  
19 1 Y 1 A GLU 314 ? CD  ? A GLU 159 CD  
20 1 Y 1 A GLU 314 ? OE1 ? A GLU 159 OE1 
21 1 Y 1 A GLU 314 ? OE2 ? A GLU 159 OE2 
22 1 Y 1 A LYS 365 ? CG  ? A LYS 210 CG  
23 1 Y 1 A LYS 365 ? CD  ? A LYS 210 CD  
24 1 Y 1 A LYS 365 ? CE  ? A LYS 210 CE  
25 1 Y 1 A LYS 365 ? NZ  ? A LYS 210 NZ  
26 1 Y 1 A LYS 400 ? CG  ? A LYS 245 CG  
27 1 Y 1 A LYS 400 ? CD  ? A LYS 245 CD  
28 1 Y 1 A LYS 400 ? CE  ? A LYS 245 CE  
29 1 Y 1 A LYS 400 ? NZ  ? A LYS 245 NZ  
30 1 Y 1 A LYS 428 ? CG  ? A LYS 273 CG  
31 1 Y 1 A LYS 428 ? CD  ? A LYS 273 CD  
32 1 Y 1 A LYS 428 ? CE  ? A LYS 273 CE  
33 1 Y 1 A LYS 428 ? NZ  ? A LYS 273 NZ  
34 1 Y 1 A GLN 473 ? CG  ? A GLN 318 CG  
35 1 Y 1 A GLN 473 ? CD  ? A GLN 318 CD  
36 1 Y 1 A GLN 473 ? OE1 ? A GLN 318 OE1 
37 1 Y 1 A GLN 473 ? NE2 ? A GLN 318 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           4 
# 
_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                     9C8T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     126.426 
_cell.length_a_esd                 ? 
_cell.length_b                     51.972 
_cell.length_b_esd                 ? 
_cell.length_c                     59.777 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9C8T 
_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   ? 
# 
_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                   9C8T 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.28 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Tris pH 8.0, 0.1 M Lithium Sulfate, 20% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-08-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9C8T 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.47 
_reflns.d_resolution_low                               63.21 
_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                                     67719 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.471 
_reflns_shell.d_res_low                                     1.496 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3349 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.537 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9C8T 
_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                            1.47 
_refine.ls_d_res_low                             63.21 
_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                     67708 
_refine.ls_number_reflns_R_free                  3304 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1877 
_refine.ls_R_factor_R_free                       0.2121 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1864 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 20.38 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2788 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         66 
_refine_hist.number_atoms_solvent             300 
_refine_hist.number_atoms_total               3154 
_refine_hist.d_res_high                       1.47 
_refine_hist.d_res_low                        63.21 
# 
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' ? 0.014  ? 2948 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.339  ? 3972 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.975 ? 1114 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.105  ? 433  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 491  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.47 1.49  . . 142 2642 100.00 . . . . 0.2546 . . . . . . . . . . . 0.2725 
'X-RAY DIFFRACTION' 1.49 1.51  . . 124 2643 100.00 . . . . 0.2464 . . . . . . . . . . . 0.2854 
'X-RAY DIFFRACTION' 1.51 1.54  . . 148 2664 100.00 . . . . 0.2381 . . . . . . . . . . . 0.2871 
'X-RAY DIFFRACTION' 1.54 1.56  . . 139 2609 100.00 . . . . 0.2177 . . . . . . . . . . . 0.2423 
'X-RAY DIFFRACTION' 1.56 1.59  . . 130 2667 100.00 . . . . 0.2076 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 1.59 1.62  . . 133 2675 100.00 . . . . 0.2077 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 1.62 1.65  . . 130 2652 100.00 . . . . 0.1983 . . . . . . . . . . . 0.2309 
'X-RAY DIFFRACTION' 1.65 1.68  . . 125 2658 100.00 . . . . 0.1999 . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 1.68 1.72  . . 136 2653 100.00 . . . . 0.1988 . . . . . . . . . . . 0.2064 
'X-RAY DIFFRACTION' 1.72 1.76  . . 148 2676 100.00 . . . . 0.1917 . . . . . . . . . . . 0.2057 
'X-RAY DIFFRACTION' 1.76 1.80  . . 135 2630 100.00 . . . . 0.1880 . . . . . . . . . . . 0.2314 
'X-RAY DIFFRACTION' 1.80 1.85  . . 143 2664 100.00 . . . . 0.1881 . . . . . . . . . . . 0.2218 
'X-RAY DIFFRACTION' 1.85 1.91  . . 123 2657 100.00 . . . . 0.1896 . . . . . . . . . . . 0.2119 
'X-RAY DIFFRACTION' 1.91 1.97  . . 132 2680 100.00 . . . . 0.1902 . . . . . . . . . . . 0.2109 
'X-RAY DIFFRACTION' 1.97 2.04  . . 144 2683 100.00 . . . . 0.1843 . . . . . . . . . . . 0.2515 
'X-RAY DIFFRACTION' 2.04 2.12  . . 126 2672 100.00 . . . . 0.1826 . . . . . . . . . . . 0.1924 
'X-RAY DIFFRACTION' 2.12 2.22  . . 148 2690 100.00 . . . . 0.1820 . . . . . . . . . . . 0.2020 
'X-RAY DIFFRACTION' 2.22 2.33  . . 135 2688 100.00 . . . . 0.1842 . . . . . . . . . . . 0.2081 
'X-RAY DIFFRACTION' 2.33 2.48  . . 139 2709 100.00 . . . . 0.1844 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 2.48 2.67  . . 143 2673 100.00 . . . . 0.1952 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 2.67 2.94  . . 142 2710 100.00 . . . . 0.1871 . . . . . . . . . . . 0.2367 
'X-RAY DIFFRACTION' 2.94 3.37  . . 148 2733 100.00 . . . . 0.1837 . . . . . . . . . . . 0.1836 
'X-RAY DIFFRACTION' 3.37 4.24  . . 142 2777 100.00 . . . . 0.1648 . . . . . . . . . . . 0.1755 
'X-RAY DIFFRACTION' 4.24 63.21 . . 149 2899 100.00 . . . . 0.1832 . . . . . . . . . . . 0.2091 
# 
_struct.entry_id                     9C8T 
_struct.title                        'Crystal Structure of human cyclic GMP-AMP synthase in complex with AMPPNP and compound 2' 
_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        9C8T 
_struct_keywords.text            'DNA sensor, Nucleotidyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CGAS_HUMAN 
_struct_ref.pdbx_db_accession          Q8N884 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPR
IQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKI
SVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTC
CENKEEKCCRKDCLKLMKYLLEQLKERFKDKKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLR
TEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
;
_struct_ref.pdbx_align_begin           157 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9C8T 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 367 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8N884 
_struct_ref_seq.db_align_beg                  157 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  522 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       157 
_struct_ref_seq.pdbx_auth_seq_align_end       522 
# 
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 9C8T SER A 1   ? UNP Q8N884 ?   ?   'expression tag'      156 1 
1 9C8T GLU A 272 ? UNP Q8N884 LYS 427 'engineered mutation' 427 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 8   ? LYS A 18  ? SER A 163 LYS A 173 1 ? 11 
HELX_P HELX_P2  AA2 SER A 20  ? CYS A 44  ? SER A 175 CYS A 199 1 ? 25 
HELX_P HELX_P3  AA3 GLY A 57  ? GLU A 61  ? GLY A 212 GLU A 216 1 ? 5  
HELX_P HELX_P4  AA4 LEU A 107 ? GLN A 109 ? LEU A 262 GLN A 264 5 ? 3  
HELX_P HELX_P5  AA5 SER A 117 ? ILE A 133 ? SER A 272 ILE A 288 1 ? 17 
HELX_P HELX_P6  AA6 PRO A 176 ? GLN A 180 ? PRO A 331 GLN A 335 5 ? 5  
HELX_P HELX_P7  AA7 SER A 190 ? LEU A 199 ? SER A 345 LEU A 354 1 ? 10 
HELX_P HELX_P8  AA8 PHE A 224 ? ASN A 233 ? PHE A 379 ASN A 388 1 ? 10 
HELX_P HELX_P9  AA9 ASN A 244 ? LYS A 248 ? ASN A 399 LYS A 403 5 ? 5  
HELX_P HELX_P10 AB1 CYS A 250 ? PHE A 269 ? CYS A 405 PHE A 424 1 ? 20 
HELX_P HELX_P11 AB2 GLU A 272 ? ASP A 276 ? GLU A 427 ASP A 431 5 ? 5  
HELX_P HELX_P12 AB3 SER A 279 ? ASN A 294 ? SER A 434 ASN A 449 1 ? 16 
HELX_P HELX_P13 AB4 GLN A 296 ? LYS A 303 ? GLN A 451 LYS A 458 5 ? 8  
HELX_P HELX_P14 AB5 ASP A 304 ? GLU A 323 ? ASP A 459 GLU A 478 1 ? 20 
HELX_P HELX_P15 AB6 ASP A 342 ? ASN A 359 ? ASP A 497 ASN A 514 1 ? 18 
HELX_P HELX_P16 AB7 GLU A 360 ? ASP A 365 ? GLU A 515 ASP A 520 5 ? 6  
# 
_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 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A GLU 70  OE2 ? ? ? 1_555 B MG  . MG  ? ? A GLU 225 A MG  601 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc2  metalc ? ? A GLU 70  OE1 ? ? ? 1_555 C MG  . MG  ? ? A GLU 225 A MG  602 1_555 ? ? ? ? ? ? ? 2.071 ? ? 
metalc3  metalc ? ? A ASP 72  OD1 ? ? ? 1_555 B MG  . MG  ? ? A ASP 227 A MG  601 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc4  metalc ? ? A ASP 72  OD2 ? ? ? 1_555 C MG  . MG  ? ? A ASP 227 A MG  602 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc5  metalc ? ? A ASP 164 OD2 ? ? ? 1_555 B MG  . MG  ? ? A ASP 319 A MG  601 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc6  metalc ? ? A HIS 235 NE2 ? ? ? 1_555 D ZN  . ZN  ? ? A HIS 390 A ZN  603 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc7  metalc ? ? A CYS 241 SG  ? ? ? 1_555 D ZN  . ZN  ? ? A CYS 396 A ZN  603 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc8  metalc ? ? A CYS 242 SG  ? ? ? 1_555 D ZN  . ZN  ? ? A CYS 397 A ZN  603 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc9  metalc ? ? A CYS 249 SG  ? ? ? 1_555 D ZN  . ZN  ? ? A CYS 404 A ZN  603 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc10 metalc ? ? B MG  .   MG  ? ? ? 1_555 E ANP . O2A ? ? A MG  601 A ANP 604 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc11 metalc ? ? B MG  .   MG  ? ? ? 1_555 G JUJ . O04 ? ? A MG  601 A JUJ 606 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc12 metalc ? ? B MG  .   MG  ? ? ? 1_555 G JUJ . O01 ? ? A MG  601 A JUJ 606 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc13 metalc ? ? C MG  .   MG  ? ? ? 1_555 E ANP . O3G ? ? A MG  602 A ANP 604 1_555 ? ? ? ? ? ? ? 2.114 ? ? 
metalc14 metalc ? ? C MG  .   MG  ? ? ? 1_555 E ANP . O2B ? ? A MG  602 A ANP 604 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc15 metalc ? ? C MG  .   MG  ? ? ? 1_555 E ANP . O2A ? ? A MG  602 A ANP 604 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc16 metalc ? ? C MG  .   MG  ? ? ? 1_555 H HOH . O   ? ? A MG  602 A HOH 757 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  OE2 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 OD1 ? A ASP 72  ? A ASP 227 ? 1_555 105.1 ? 
2  OE2 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 OD2 ? A ASP 164 ? A ASP 319 ? 1_555 83.9  ? 
3  OD1 ? A ASP 72  ? A ASP 227 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 OD2 ? A ASP 164 ? A ASP 319 ? 1_555 92.5  ? 
4  OE2 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O2A ? E ANP .   ? A ANP 604 ? 1_555 94.5  ? 
5  OD1 ? A ASP 72  ? A ASP 227 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O2A ? E ANP .   ? A ANP 604 ? 1_555 88.0  ? 
6  OD2 ? A ASP 164 ? A ASP 319 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O2A ? E ANP .   ? A ANP 604 ? 1_555 178.5 ? 
7  OE2 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O04 ? G JUJ .   ? A JUJ 606 ? 1_555 159.7 ? 
8  OD1 ? A ASP 72  ? A ASP 227 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O04 ? G JUJ .   ? A JUJ 606 ? 1_555 93.6  ? 
9  OD2 ? A ASP 164 ? A ASP 319 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O04 ? G JUJ .   ? A JUJ 606 ? 1_555 87.3  ? 
10 O2A ? E ANP .   ? A ANP 604 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O04 ? G JUJ .   ? A JUJ 606 ? 1_555 94.1  ? 
11 OE2 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O01 ? G JUJ .   ? A JUJ 606 ? 1_555 84.8  ? 
12 OD1 ? A ASP 72  ? A ASP 227 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O01 ? G JUJ .   ? A JUJ 606 ? 1_555 169.9 ? 
13 OD2 ? A ASP 164 ? A ASP 319 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O01 ? G JUJ .   ? A JUJ 606 ? 1_555 86.4  ? 
14 O2A ? E ANP .   ? A ANP 604 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O01 ? G JUJ .   ? A JUJ 606 ? 1_555 93.4  ? 
15 O04 ? G JUJ .   ? A JUJ 606 ? 1_555 MG ? B MG . ? A MG 601 ? 1_555 O01 ? G JUJ .   ? A JUJ 606 ? 1_555 76.4  ? 
16 OE1 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 OD2 ? A ASP 72  ? A ASP 227 ? 1_555 97.1  ? 
17 OE1 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O3G ? E ANP .   ? A ANP 604 ? 1_555 89.5  ? 
18 OD2 ? A ASP 72  ? A ASP 227 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O3G ? E ANP .   ? A ANP 604 ? 1_555 172.8 ? 
19 OE1 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O2B ? E ANP .   ? A ANP 604 ? 1_555 173.9 ? 
20 OD2 ? A ASP 72  ? A ASP 227 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O2B ? E ANP .   ? A ANP 604 ? 1_555 86.7  ? 
21 O3G ? E ANP .   ? A ANP 604 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O2B ? E ANP .   ? A ANP 604 ? 1_555 86.8  ? 
22 OE1 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O2A ? E ANP .   ? A ANP 604 ? 1_555 95.0  ? 
23 OD2 ? A ASP 72  ? A ASP 227 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O2A ? E ANP .   ? A ANP 604 ? 1_555 84.9  ? 
24 O3G ? E ANP .   ? A ANP 604 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O2A ? E ANP .   ? A ANP 604 ? 1_555 91.8  ? 
25 O2B ? E ANP .   ? A ANP 604 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O2A ? E ANP .   ? A ANP 604 ? 1_555 90.0  ? 
26 OE1 ? A GLU 70  ? A GLU 225 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? H HOH .   ? A HOH 757 ? 1_555 85.3  ? 
27 OD2 ? A ASP 72  ? A ASP 227 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? H HOH .   ? A HOH 757 ? 1_555 87.6  ? 
28 O3G ? E ANP .   ? A ANP 604 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? H HOH .   ? A HOH 757 ? 1_555 95.7  ? 
29 O2B ? E ANP .   ? A ANP 604 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? H HOH .   ? A HOH 757 ? 1_555 90.2  ? 
30 O2A ? E ANP .   ? A ANP 604 ? 1_555 MG ? C MG . ? A MG 602 ? 1_555 O   ? H HOH .   ? A HOH 757 ? 1_555 172.5 ? 
31 NE2 ? A HIS 235 ? A HIS 390 ? 1_555 ZN ? D ZN . ? A ZN 603 ? 1_555 SG  ? A CYS 241 ? A CYS 396 ? 1_555 112.0 ? 
32 NE2 ? A HIS 235 ? A HIS 390 ? 1_555 ZN ? D ZN . ? A ZN 603 ? 1_555 SG  ? A CYS 242 ? A CYS 397 ? 1_555 106.6 ? 
33 SG  ? A CYS 241 ? A CYS 396 ? 1_555 ZN ? D ZN . ? A ZN 603 ? 1_555 SG  ? A CYS 242 ? A CYS 397 ? 1_555 129.3 ? 
34 NE2 ? A HIS 235 ? A HIS 390 ? 1_555 ZN ? D ZN . ? A ZN 603 ? 1_555 SG  ? A CYS 249 ? A CYS 404 ? 1_555 95.2  ? 
35 SG  ? A CYS 241 ? A CYS 396 ? 1_555 ZN ? D ZN . ? A ZN 603 ? 1_555 SG  ? A CYS 249 ? A CYS 404 ? 1_555 100.1 ? 
36 SG  ? A CYS 242 ? A CYS 397 ? 1_555 ZN ? D ZN . ? A ZN 603 ? 1_555 SG  ? A CYS 249 ? A CYS 404 ? 1_555 107.9 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY A 52  ? THR A 56  ? GLY A 207 THR A 211 
AA1 2 GLU A 70  ? GLU A 78  ? GLU A 225 GLU A 233 
AA1 3 ILE A 161 ? SER A 171 ? ILE A 316 SER A 326 
AA1 4 PHE A 202 ? VAL A 205 ? PHE A 357 VAL A 360 
AA1 5 TRP A 220 ? SER A 223 ? TRP A 375 SER A 378 
AA1 6 TYR A 93  ? LYS A 97  ? TYR A 248 LYS A 252 
AA1 7 GLN A 83  ? GLU A 86  ? GLN A 238 GLU A 241 
AA2 1 GLY A 52  ? THR A 56  ? GLY A 207 THR A 211 
AA2 2 GLU A 70  ? GLU A 78  ? GLU A 225 GLU A 233 
AA2 3 ILE A 161 ? SER A 171 ? ILE A 316 SER A 326 
AA2 4 ALA A 152 ? ILE A 157 ? ALA A 307 ILE A 312 
AA2 5 VAL A 141 ? MET A 143 ? VAL A 296 MET A 298 
AA3 1 LEU A 111 ? GLU A 112 ? LEU A 266 GLU A 267 
AA3 2 ILE A 115 ? LEU A 116 ? ILE A 270 LEU A 271 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 54  ? N LEU A 209 O MET A 74  ? O MET A 229 
AA1 2 3 N VAL A 73  ? N VAL A 228 O ASP A 164 ? O ASP A 319 
AA1 3 4 N SER A 171 ? N SER A 326 O PHE A 202 ? O PHE A 357 
AA1 4 5 N VAL A 205 ? N VAL A 360 O ARG A 221 ? O ARG A 376 
AA1 5 6 O TRP A 220 ? O TRP A 375 N TYR A 94  ? N TYR A 249 
AA1 6 7 O LYS A 97  ? O LYS A 252 N GLN A 83  ? N GLN A 238 
AA2 1 2 N LEU A 54  ? N LEU A 209 O MET A 74  ? O MET A 229 
AA2 2 3 N VAL A 73  ? N VAL A 228 O ASP A 164 ? O ASP A 319 
AA2 3 4 O ILE A 161 ? O ILE A 316 N ILE A 157 ? N ILE A 312 
AA2 4 5 O LEU A 156 ? O LEU A 311 N ILE A 142 ? N ILE A 297 
AA3 1 2 N GLU A 112 ? N GLU A 267 O ILE A 115 ? O ILE A 270 
# 
_pdbx_entry_details.entry_id                   9C8T 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 SER A 221 ? ? 75.98   -59.72 
2 1 ARG A 246 ? ? 73.99   -29.09 
3 1 TRP A 343 ? ? -108.98 -65.50 
4 1 SER A 345 ? ? 102.16  149.34 
5 1 ASN A 389 ? ? -151.44 70.42  
6 1 PHE A 424 ? ? -99.61  30.38  
7 1 PHE A 516 ? ? 63.04   61.30  
# 
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 SER 156 ? A SER 1   
2  1 Y 1 A ASP 157 ? A ASP 2   
3  1 Y 1 A ALA 158 ? A ALA 3   
4  1 Y 1 A ALA 159 ? A ALA 4   
5  1 Y 1 A PRO 160 ? A PRO 5   
6  1 Y 1 A GLY 161 ? A GLY 6   
7  1 Y 1 A ALA 162 ? A ALA 7   
8  1 Y 1 A LYS 254 ? A LYS 99  
9  1 Y 1 A ARG 255 ? A ARG 100 
10 1 Y 1 A ASN 256 ? A ASN 101 
11 1 Y 1 A PRO 257 ? A PRO 102 
12 1 Y 1 A LYS 258 ? A LYS 103 
13 1 Y 1 A GLU 259 ? A GLU 104 
14 1 Y 1 A ASN 260 ? A ASN 105 
15 1 Y 1 A ASN 289 ? A ASN 134 
16 1 Y 1 A ASP 290 ? A ASP 135 
17 1 Y 1 A ILE 291 ? A ILE 136 
18 1 Y 1 A LYS 292 ? A LYS 137 
19 1 Y 1 A ARG 302 ? A ARG 147 
20 1 Y 1 A GLY 303 ? A GLY 148 
21 1 Y 1 A GLY 304 ? A GLY 149 
22 1 Y 1 A GLY 367 ? A GLY 212 
23 1 Y 1 A ASN 368 ? A ASN 213 
24 1 Y 1 A GLU 521 ? A GLU 366 
25 1 Y 1 A PHE 522 ? A PHE 367 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ANP PG     P  N N 14  
ANP O1G    O  N N 15  
ANP O2G    O  N N 16  
ANP O3G    O  N N 17  
ANP PB     P  N N 18  
ANP O1B    O  N N 19  
ANP O2B    O  N N 20  
ANP N3B    N  N N 21  
ANP PA     P  N N 22  
ANP O1A    O  N N 23  
ANP O2A    O  N N 24  
ANP O3A    O  N N 25  
ANP "O5'"  O  N N 26  
ANP "C5'"  C  N N 27  
ANP "C4'"  C  N R 28  
ANP "O4'"  O  N N 29  
ANP "C3'"  C  N S 30  
ANP "O3'"  O  N N 31  
ANP "C2'"  C  N R 32  
ANP "O2'"  O  N N 33  
ANP "C1'"  C  N R 34  
ANP N9     N  Y N 35  
ANP C8     C  Y N 36  
ANP N7     N  Y N 37  
ANP C5     C  Y N 38  
ANP C6     C  Y N 39  
ANP N6     N  N N 40  
ANP N1     N  Y N 41  
ANP C2     C  Y N 42  
ANP N3     N  Y N 43  
ANP C4     C  Y N 44  
ANP HOG2   H  N N 45  
ANP HOG3   H  N N 46  
ANP HOB2   H  N N 47  
ANP HNB1   H  N N 48  
ANP HOA2   H  N N 49  
ANP "H5'1" H  N N 50  
ANP "H5'2" H  N N 51  
ANP "H4'"  H  N N 52  
ANP "H3'"  H  N N 53  
ANP "HO3'" H  N N 54  
ANP "H2'"  H  N N 55  
ANP "HO2'" H  N N 56  
ANP "H1'"  H  N N 57  
ANP H8     H  N N 58  
ANP HN61   H  N N 59  
ANP HN62   H  N N 60  
ANP H2     H  N N 61  
ARG N      N  N N 62  
ARG CA     C  N S 63  
ARG C      C  N N 64  
ARG O      O  N N 65  
ARG CB     C  N N 66  
ARG CG     C  N N 67  
ARG CD     C  N N 68  
ARG NE     N  N N 69  
ARG CZ     C  N N 70  
ARG NH1    N  N N 71  
ARG NH2    N  N N 72  
ARG OXT    O  N N 73  
ARG H      H  N N 74  
ARG H2     H  N N 75  
ARG HA     H  N N 76  
ARG HB2    H  N N 77  
ARG HB3    H  N N 78  
ARG HG2    H  N N 79  
ARG HG3    H  N N 80  
ARG HD2    H  N N 81  
ARG HD3    H  N N 82  
ARG HE     H  N N 83  
ARG HH11   H  N N 84  
ARG HH12   H  N N 85  
ARG HH21   H  N N 86  
ARG HH22   H  N N 87  
ARG HXT    H  N N 88  
ASN N      N  N N 89  
ASN CA     C  N S 90  
ASN C      C  N N 91  
ASN O      O  N N 92  
ASN CB     C  N N 93  
ASN CG     C  N N 94  
ASN OD1    O  N N 95  
ASN ND2    N  N N 96  
ASN OXT    O  N N 97  
ASN H      H  N N 98  
ASN H2     H  N N 99  
ASN HA     H  N N 100 
ASN HB2    H  N N 101 
ASN HB3    H  N N 102 
ASN HD21   H  N N 103 
ASN HD22   H  N N 104 
ASN HXT    H  N N 105 
ASP N      N  N N 106 
ASP CA     C  N S 107 
ASP C      C  N N 108 
ASP O      O  N N 109 
ASP CB     C  N N 110 
ASP CG     C  N N 111 
ASP OD1    O  N N 112 
ASP OD2    O  N N 113 
ASP OXT    O  N N 114 
ASP H      H  N N 115 
ASP H2     H  N N 116 
ASP HA     H  N N 117 
ASP HB2    H  N N 118 
ASP HB3    H  N N 119 
ASP HD2    H  N N 120 
ASP HXT    H  N N 121 
CYS N      N  N N 122 
CYS CA     C  N R 123 
CYS C      C  N N 124 
CYS O      O  N N 125 
CYS CB     C  N N 126 
CYS SG     S  N N 127 
CYS OXT    O  N N 128 
CYS H      H  N N 129 
CYS H2     H  N N 130 
CYS HA     H  N N 131 
CYS HB2    H  N N 132 
CYS HB3    H  N N 133 
CYS HG     H  N N 134 
CYS HXT    H  N N 135 
GLN N      N  N N 136 
GLN CA     C  N S 137 
GLN C      C  N N 138 
GLN O      O  N N 139 
GLN CB     C  N N 140 
GLN CG     C  N N 141 
GLN CD     C  N N 142 
GLN OE1    O  N N 143 
GLN NE2    N  N N 144 
GLN OXT    O  N N 145 
GLN H      H  N N 146 
GLN H2     H  N N 147 
GLN HA     H  N N 148 
GLN HB2    H  N N 149 
GLN HB3    H  N N 150 
GLN HG2    H  N N 151 
GLN HG3    H  N N 152 
GLN HE21   H  N N 153 
GLN HE22   H  N N 154 
GLN HXT    H  N N 155 
GLU N      N  N N 156 
GLU CA     C  N S 157 
GLU C      C  N N 158 
GLU O      O  N N 159 
GLU CB     C  N N 160 
GLU CG     C  N N 161 
GLU CD     C  N N 162 
GLU OE1    O  N N 163 
GLU OE2    O  N N 164 
GLU OXT    O  N N 165 
GLU H      H  N N 166 
GLU H2     H  N N 167 
GLU HA     H  N N 168 
GLU HB2    H  N N 169 
GLU HB3    H  N N 170 
GLU HG2    H  N N 171 
GLU HG3    H  N N 172 
GLU HE2    H  N N 173 
GLU HXT    H  N N 174 
GLY N      N  N N 175 
GLY CA     C  N N 176 
GLY C      C  N N 177 
GLY O      O  N N 178 
GLY OXT    O  N N 179 
GLY H      H  N N 180 
GLY H2     H  N N 181 
GLY HA2    H  N N 182 
GLY HA3    H  N N 183 
GLY HXT    H  N N 184 
GOL C1     C  N N 185 
GOL O1     O  N N 186 
GOL C2     C  N N 187 
GOL O2     O  N N 188 
GOL C3     C  N N 189 
GOL O3     O  N N 190 
GOL H11    H  N N 191 
GOL H12    H  N N 192 
GOL HO1    H  N N 193 
GOL H2     H  N N 194 
GOL HO2    H  N N 195 
GOL H31    H  N N 196 
GOL H32    H  N N 197 
GOL HO3    H  N N 198 
HIS N      N  N N 199 
HIS CA     C  N S 200 
HIS C      C  N N 201 
HIS O      O  N N 202 
HIS CB     C  N N 203 
HIS CG     C  Y N 204 
HIS ND1    N  Y N 205 
HIS CD2    C  Y N 206 
HIS CE1    C  Y N 207 
HIS NE2    N  Y N 208 
HIS OXT    O  N N 209 
HIS H      H  N N 210 
HIS H2     H  N N 211 
HIS HA     H  N N 212 
HIS HB2    H  N N 213 
HIS HB3    H  N N 214 
HIS HD1    H  N N 215 
HIS HD2    H  N N 216 
HIS HE1    H  N N 217 
HIS HE2    H  N N 218 
HIS HXT    H  N N 219 
HOH O      O  N N 220 
HOH H1     H  N N 221 
HOH H2     H  N N 222 
ILE N      N  N N 223 
ILE CA     C  N S 224 
ILE C      C  N N 225 
ILE O      O  N N 226 
ILE CB     C  N S 227 
ILE CG1    C  N N 228 
ILE CG2    C  N N 229 
ILE CD1    C  N N 230 
ILE OXT    O  N N 231 
ILE H      H  N N 232 
ILE H2     H  N N 233 
ILE HA     H  N N 234 
ILE HB     H  N N 235 
ILE HG12   H  N N 236 
ILE HG13   H  N N 237 
ILE HG21   H  N N 238 
ILE HG22   H  N N 239 
ILE HG23   H  N N 240 
ILE HD11   H  N N 241 
ILE HD12   H  N N 242 
ILE HD13   H  N N 243 
ILE HXT    H  N N 244 
JUJ C13    C  N N 245 
JUJ C20    C  Y N 246 
JUJ C21    C  Y N 247 
JUJ C26    C  Y N 248 
JUJ O01    O  N N 249 
JUJ C02    C  N N 250 
JUJ C03    C  N N 251 
JUJ O04    O  N N 252 
JUJ N05    N  N N 253 
JUJ C06    C  N N 254 
JUJ C07    C  Y N 255 
JUJ C08    C  Y N 256 
JUJ C09    C  Y N 257 
JUJ N10    N  Y N 258 
JUJ C11    C  Y N 259 
JUJ C12    C  N N 260 
JUJ C14    C  Y N 261 
JUJ CL2    CL N N 262 
JUJ C16    C  Y N 263 
JUJ CL1    CL N N 264 
JUJ C18    C  Y N 265 
JUJ C19    C  Y N 266 
JUJ N22    N  Y N 267 
JUJ C23    C  Y N 268 
JUJ N24    N  N N 269 
JUJ C25    C  Y N 270 
JUJ H1     H  N N 271 
JUJ H2     H  N N 272 
JUJ H3     H  N N 273 
JUJ H4     H  N N 274 
JUJ H5     H  N N 275 
JUJ H6     H  N N 276 
JUJ H7     H  N N 277 
JUJ H8     H  N N 278 
JUJ H9     H  N N 279 
JUJ H10    H  N N 280 
JUJ H11    H  N N 281 
JUJ H12    H  N N 282 
JUJ H13    H  N N 283 
JUJ H14    H  N N 284 
JUJ H15    H  N N 285 
JUJ H16    H  N N 286 
LEU N      N  N N 287 
LEU CA     C  N S 288 
LEU C      C  N N 289 
LEU O      O  N N 290 
LEU CB     C  N N 291 
LEU CG     C  N N 292 
LEU CD1    C  N N 293 
LEU CD2    C  N N 294 
LEU OXT    O  N N 295 
LEU H      H  N N 296 
LEU H2     H  N N 297 
LEU HA     H  N N 298 
LEU HB2    H  N N 299 
LEU HB3    H  N N 300 
LEU HG     H  N N 301 
LEU HD11   H  N N 302 
LEU HD12   H  N N 303 
LEU HD13   H  N N 304 
LEU HD21   H  N N 305 
LEU HD22   H  N N 306 
LEU HD23   H  N N 307 
LEU HXT    H  N N 308 
LYS N      N  N N 309 
LYS CA     C  N S 310 
LYS C      C  N N 311 
LYS O      O  N N 312 
LYS CB     C  N N 313 
LYS CG     C  N N 314 
LYS CD     C  N N 315 
LYS CE     C  N N 316 
LYS NZ     N  N N 317 
LYS OXT    O  N N 318 
LYS H      H  N N 319 
LYS H2     H  N N 320 
LYS HA     H  N N 321 
LYS HB2    H  N N 322 
LYS HB3    H  N N 323 
LYS HG2    H  N N 324 
LYS HG3    H  N N 325 
LYS HD2    H  N N 326 
LYS HD3    H  N N 327 
LYS HE2    H  N N 328 
LYS HE3    H  N N 329 
LYS HZ1    H  N N 330 
LYS HZ2    H  N N 331 
LYS HZ3    H  N N 332 
LYS HXT    H  N N 333 
MET N      N  N N 334 
MET CA     C  N S 335 
MET C      C  N N 336 
MET O      O  N N 337 
MET CB     C  N N 338 
MET CG     C  N N 339 
MET SD     S  N N 340 
MET CE     C  N N 341 
MET OXT    O  N N 342 
MET H      H  N N 343 
MET H2     H  N N 344 
MET HA     H  N N 345 
MET HB2    H  N N 346 
MET HB3    H  N N 347 
MET HG2    H  N N 348 
MET HG3    H  N N 349 
MET HE1    H  N N 350 
MET HE2    H  N N 351 
MET HE3    H  N N 352 
MET HXT    H  N N 353 
MG  MG     MG N N 354 
PHE N      N  N N 355 
PHE CA     C  N S 356 
PHE C      C  N N 357 
PHE O      O  N N 358 
PHE CB     C  N N 359 
PHE CG     C  Y N 360 
PHE CD1    C  Y N 361 
PHE CD2    C  Y N 362 
PHE CE1    C  Y N 363 
PHE CE2    C  Y N 364 
PHE CZ     C  Y N 365 
PHE OXT    O  N N 366 
PHE H      H  N N 367 
PHE H2     H  N N 368 
PHE HA     H  N N 369 
PHE HB2    H  N N 370 
PHE HB3    H  N N 371 
PHE HD1    H  N N 372 
PHE HD2    H  N N 373 
PHE HE1    H  N N 374 
PHE HE2    H  N N 375 
PHE HZ     H  N N 376 
PHE HXT    H  N N 377 
PRO N      N  N N 378 
PRO CA     C  N S 379 
PRO C      C  N N 380 
PRO O      O  N N 381 
PRO CB     C  N N 382 
PRO CG     C  N N 383 
PRO CD     C  N N 384 
PRO OXT    O  N N 385 
PRO H      H  N N 386 
PRO HA     H  N N 387 
PRO HB2    H  N N 388 
PRO HB3    H  N N 389 
PRO HG2    H  N N 390 
PRO HG3    H  N N 391 
PRO HD2    H  N N 392 
PRO HD3    H  N N 393 
PRO HXT    H  N N 394 
SER N      N  N N 395 
SER CA     C  N S 396 
SER C      C  N N 397 
SER O      O  N N 398 
SER CB     C  N N 399 
SER OG     O  N N 400 
SER OXT    O  N N 401 
SER H      H  N N 402 
SER H2     H  N N 403 
SER HA     H  N N 404 
SER HB2    H  N N 405 
SER HB3    H  N N 406 
SER HG     H  N N 407 
SER HXT    H  N N 408 
THR N      N  N N 409 
THR CA     C  N S 410 
THR C      C  N N 411 
THR O      O  N N 412 
THR CB     C  N R 413 
THR OG1    O  N N 414 
THR CG2    C  N N 415 
THR OXT    O  N N 416 
THR H      H  N N 417 
THR H2     H  N N 418 
THR HA     H  N N 419 
THR HB     H  N N 420 
THR HG1    H  N N 421 
THR HG21   H  N N 422 
THR HG22   H  N N 423 
THR HG23   H  N N 424 
THR HXT    H  N N 425 
TRP N      N  N N 426 
TRP CA     C  N S 427 
TRP C      C  N N 428 
TRP O      O  N N 429 
TRP CB     C  N N 430 
TRP CG     C  Y N 431 
TRP CD1    C  Y N 432 
TRP CD2    C  Y N 433 
TRP NE1    N  Y N 434 
TRP CE2    C  Y N 435 
TRP CE3    C  Y N 436 
TRP CZ2    C  Y N 437 
TRP CZ3    C  Y N 438 
TRP CH2    C  Y N 439 
TRP OXT    O  N N 440 
TRP H      H  N N 441 
TRP H2     H  N N 442 
TRP HA     H  N N 443 
TRP HB2    H  N N 444 
TRP HB3    H  N N 445 
TRP HD1    H  N N 446 
TRP HE1    H  N N 447 
TRP HE3    H  N N 448 
TRP HZ2    H  N N 449 
TRP HZ3    H  N N 450 
TRP HH2    H  N N 451 
TRP HXT    H  N N 452 
TYR N      N  N N 453 
TYR CA     C  N S 454 
TYR C      C  N N 455 
TYR O      O  N N 456 
TYR CB     C  N N 457 
TYR CG     C  Y N 458 
TYR CD1    C  Y N 459 
TYR CD2    C  Y N 460 
TYR CE1    C  Y N 461 
TYR CE2    C  Y N 462 
TYR CZ     C  Y N 463 
TYR OH     O  N N 464 
TYR OXT    O  N N 465 
TYR H      H  N N 466 
TYR H2     H  N N 467 
TYR HA     H  N N 468 
TYR HB2    H  N N 469 
TYR HB3    H  N N 470 
TYR HD1    H  N N 471 
TYR HD2    H  N N 472 
TYR HE1    H  N N 473 
TYR HE2    H  N N 474 
TYR HH     H  N N 475 
TYR HXT    H  N N 476 
VAL N      N  N N 477 
VAL CA     C  N S 478 
VAL C      C  N N 479 
VAL O      O  N N 480 
VAL CB     C  N N 481 
VAL CG1    C  N N 482 
VAL CG2    C  N N 483 
VAL OXT    O  N N 484 
VAL H      H  N N 485 
VAL H2     H  N N 486 
VAL HA     H  N N 487 
VAL HB     H  N N 488 
VAL HG11   H  N N 489 
VAL HG12   H  N N 490 
VAL HG13   H  N N 491 
VAL HG21   H  N N 492 
VAL HG22   H  N N 493 
VAL HG23   H  N N 494 
VAL HXT    H  N N 495 
ZN  ZN     ZN N N 496 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
GOL C1    O1     sing N N 179 
GOL C1    C2     sing N N 180 
GOL C1    H11    sing N N 181 
GOL C1    H12    sing N N 182 
GOL O1    HO1    sing N N 183 
GOL C2    O2     sing N N 184 
GOL C2    C3     sing N N 185 
GOL C2    H2     sing N N 186 
GOL O2    HO2    sing N N 187 
GOL C3    O3     sing N N 188 
GOL C3    H31    sing N N 189 
GOL C3    H32    sing N N 190 
GOL O3    HO3    sing N N 191 
HIS N     CA     sing N N 192 
HIS N     H      sing N N 193 
HIS N     H2     sing N N 194 
HIS CA    C      sing N N 195 
HIS CA    CB     sing N N 196 
HIS CA    HA     sing N N 197 
HIS C     O      doub N N 198 
HIS C     OXT    sing N N 199 
HIS CB    CG     sing N N 200 
HIS CB    HB2    sing N N 201 
HIS CB    HB3    sing N N 202 
HIS CG    ND1    sing Y N 203 
HIS CG    CD2    doub Y N 204 
HIS ND1   CE1    doub Y N 205 
HIS ND1   HD1    sing N N 206 
HIS CD2   NE2    sing Y N 207 
HIS CD2   HD2    sing N N 208 
HIS CE1   NE2    sing Y N 209 
HIS CE1   HE1    sing N N 210 
HIS NE2   HE2    sing N N 211 
HIS OXT   HXT    sing N N 212 
HOH O     H1     sing N N 213 
HOH O     H2     sing N N 214 
ILE N     CA     sing N N 215 
ILE N     H      sing N N 216 
ILE N     H2     sing N N 217 
ILE CA    C      sing N N 218 
ILE CA    CB     sing N N 219 
ILE CA    HA     sing N N 220 
ILE C     O      doub N N 221 
ILE C     OXT    sing N N 222 
ILE CB    CG1    sing N N 223 
ILE CB    CG2    sing N N 224 
ILE CB    HB     sing N N 225 
ILE CG1   CD1    sing N N 226 
ILE CG1   HG12   sing N N 227 
ILE CG1   HG13   sing N N 228 
ILE CG2   HG21   sing N N 229 
ILE CG2   HG22   sing N N 230 
ILE CG2   HG23   sing N N 231 
ILE CD1   HD11   sing N N 232 
ILE CD1   HD12   sing N N 233 
ILE CD1   HD13   sing N N 234 
ILE OXT   HXT    sing N N 235 
JUJ O04   C03    doub N N 236 
JUJ C25   C26    doub Y N 237 
JUJ C25   C23    sing Y N 238 
JUJ C26   C20    sing Y N 239 
JUJ C03   C02    sing N N 240 
JUJ C03   N05    sing N N 241 
JUJ C02   O01    sing N N 242 
JUJ C06   N05    sing N N 243 
JUJ C06   C07    sing N N 244 
JUJ C23   N24    sing N N 245 
JUJ C23   N22    doub Y N 246 
JUJ N05   C13    sing N N 247 
JUJ C20   C19    sing N N 248 
JUJ C20   C21    doub Y N 249 
JUJ C07   C11    doub Y N 250 
JUJ C07   C08    sing Y N 251 
JUJ C12   C11    sing N N 252 
JUJ C12   C13    sing N N 253 
JUJ C19   C08    doub Y N 254 
JUJ C19   C18    sing Y N 255 
JUJ C11   N10    sing Y N 256 
JUJ C08   C09    sing Y N 257 
JUJ C18   C16    doub Y N 258 
JUJ C09   N10    sing Y N 259 
JUJ C09   C14    doub Y N 260 
JUJ C16   C14    sing Y N 261 
JUJ C16   CL1    sing N N 262 
JUJ C14   CL2    sing N N 263 
JUJ N22   C21    sing Y N 264 
JUJ C13   H1     sing N N 265 
JUJ C13   H2     sing N N 266 
JUJ C21   H3     sing N N 267 
JUJ C26   H4     sing N N 268 
JUJ O01   H5     sing N N 269 
JUJ C02   H6     sing N N 270 
JUJ C02   H7     sing N N 271 
JUJ C06   H8     sing N N 272 
JUJ C06   H9     sing N N 273 
JUJ N10   H10    sing N N 274 
JUJ C12   H11    sing N N 275 
JUJ C12   H12    sing N N 276 
JUJ C18   H13    sing N N 277 
JUJ N24   H14    sing N N 278 
JUJ N24   H15    sing N N 279 
JUJ C25   H16    sing N N 280 
LEU N     CA     sing N N 281 
LEU N     H      sing N N 282 
LEU N     H2     sing N N 283 
LEU CA    C      sing N N 284 
LEU CA    CB     sing N N 285 
LEU CA    HA     sing N N 286 
LEU C     O      doub N N 287 
LEU C     OXT    sing N N 288 
LEU CB    CG     sing N N 289 
LEU CB    HB2    sing N N 290 
LEU CB    HB3    sing N N 291 
LEU CG    CD1    sing N N 292 
LEU CG    CD2    sing N N 293 
LEU CG    HG     sing N N 294 
LEU CD1   HD11   sing N N 295 
LEU CD1   HD12   sing N N 296 
LEU CD1   HD13   sing N N 297 
LEU CD2   HD21   sing N N 298 
LEU CD2   HD22   sing N N 299 
LEU CD2   HD23   sing N N 300 
LEU OXT   HXT    sing N N 301 
LYS N     CA     sing N N 302 
LYS N     H      sing N N 303 
LYS N     H2     sing N N 304 
LYS CA    C      sing N N 305 
LYS CA    CB     sing N N 306 
LYS CA    HA     sing N N 307 
LYS C     O      doub N N 308 
LYS C     OXT    sing N N 309 
LYS CB    CG     sing N N 310 
LYS CB    HB2    sing N N 311 
LYS CB    HB3    sing N N 312 
LYS CG    CD     sing N N 313 
LYS CG    HG2    sing N N 314 
LYS CG    HG3    sing N N 315 
LYS CD    CE     sing N N 316 
LYS CD    HD2    sing N N 317 
LYS CD    HD3    sing N N 318 
LYS CE    NZ     sing N N 319 
LYS CE    HE2    sing N N 320 
LYS CE    HE3    sing N N 321 
LYS NZ    HZ1    sing N N 322 
LYS NZ    HZ2    sing N N 323 
LYS NZ    HZ3    sing N N 324 
LYS OXT   HXT    sing N N 325 
MET N     CA     sing N N 326 
MET N     H      sing N N 327 
MET N     H2     sing N N 328 
MET CA    C      sing N N 329 
MET CA    CB     sing N N 330 
MET CA    HA     sing N N 331 
MET C     O      doub N N 332 
MET C     OXT    sing N N 333 
MET CB    CG     sing N N 334 
MET CB    HB2    sing N N 335 
MET CB    HB3    sing N N 336 
MET CG    SD     sing N N 337 
MET CG    HG2    sing N N 338 
MET CG    HG3    sing N N 339 
MET SD    CE     sing N N 340 
MET CE    HE1    sing N N 341 
MET CE    HE2    sing N N 342 
MET CE    HE3    sing N N 343 
MET OXT   HXT    sing N N 344 
PHE N     CA     sing N N 345 
PHE N     H      sing N N 346 
PHE N     H2     sing N N 347 
PHE CA    C      sing N N 348 
PHE CA    CB     sing N N 349 
PHE CA    HA     sing N N 350 
PHE C     O      doub N N 351 
PHE C     OXT    sing N N 352 
PHE CB    CG     sing N N 353 
PHE CB    HB2    sing N N 354 
PHE CB    HB3    sing N N 355 
PHE CG    CD1    doub Y N 356 
PHE CG    CD2    sing Y N 357 
PHE CD1   CE1    sing Y N 358 
PHE CD1   HD1    sing N N 359 
PHE CD2   CE2    doub Y N 360 
PHE CD2   HD2    sing N N 361 
PHE CE1   CZ     doub Y N 362 
PHE CE1   HE1    sing N N 363 
PHE CE2   CZ     sing Y N 364 
PHE CE2   HE2    sing N N 365 
PHE CZ    HZ     sing N N 366 
PHE OXT   HXT    sing N N 367 
PRO N     CA     sing N N 368 
PRO N     CD     sing N N 369 
PRO N     H      sing N N 370 
PRO CA    C      sing N N 371 
PRO CA    CB     sing N N 372 
PRO CA    HA     sing N N 373 
PRO C     O      doub N N 374 
PRO C     OXT    sing N N 375 
PRO CB    CG     sing N N 376 
PRO CB    HB2    sing N N 377 
PRO CB    HB3    sing N N 378 
PRO CG    CD     sing N N 379 
PRO CG    HG2    sing N N 380 
PRO CG    HG3    sing N N 381 
PRO CD    HD2    sing N N 382 
PRO CD    HD3    sing N N 383 
PRO OXT   HXT    sing N N 384 
SER N     CA     sing N N 385 
SER N     H      sing N N 386 
SER N     H2     sing N N 387 
SER CA    C      sing N N 388 
SER CA    CB     sing N N 389 
SER CA    HA     sing N N 390 
SER C     O      doub N N 391 
SER C     OXT    sing N N 392 
SER CB    OG     sing N N 393 
SER CB    HB2    sing N N 394 
SER CB    HB3    sing N N 395 
SER OG    HG     sing N N 396 
SER OXT   HXT    sing N N 397 
THR N     CA     sing N N 398 
THR N     H      sing N N 399 
THR N     H2     sing N N 400 
THR CA    C      sing N N 401 
THR CA    CB     sing N N 402 
THR CA    HA     sing N N 403 
THR C     O      doub N N 404 
THR C     OXT    sing N N 405 
THR CB    OG1    sing N N 406 
THR CB    CG2    sing N N 407 
THR CB    HB     sing N N 408 
THR OG1   HG1    sing N N 409 
THR CG2   HG21   sing N N 410 
THR CG2   HG22   sing N N 411 
THR CG2   HG23   sing N N 412 
THR OXT   HXT    sing N N 413 
TRP N     CA     sing N N 414 
TRP N     H      sing N N 415 
TRP N     H2     sing N N 416 
TRP CA    C      sing N N 417 
TRP CA    CB     sing N N 418 
TRP CA    HA     sing N N 419 
TRP C     O      doub N N 420 
TRP C     OXT    sing N N 421 
TRP CB    CG     sing N N 422 
TRP CB    HB2    sing N N 423 
TRP CB    HB3    sing N N 424 
TRP CG    CD1    doub Y N 425 
TRP CG    CD2    sing Y N 426 
TRP CD1   NE1    sing Y N 427 
TRP CD1   HD1    sing N N 428 
TRP CD2   CE2    doub Y N 429 
TRP CD2   CE3    sing Y N 430 
TRP NE1   CE2    sing Y N 431 
TRP NE1   HE1    sing N N 432 
TRP CE2   CZ2    sing Y N 433 
TRP CE3   CZ3    doub Y N 434 
TRP CE3   HE3    sing N N 435 
TRP CZ2   CH2    doub Y N 436 
TRP CZ2   HZ2    sing N N 437 
TRP CZ3   CH2    sing Y N 438 
TRP CZ3   HZ3    sing N N 439 
TRP CH2   HH2    sing N N 440 
TRP OXT   HXT    sing N N 441 
TYR N     CA     sing N N 442 
TYR N     H      sing N N 443 
TYR N     H2     sing N N 444 
TYR CA    C      sing N N 445 
TYR CA    CB     sing N N 446 
TYR CA    HA     sing N N 447 
TYR C     O      doub N N 448 
TYR C     OXT    sing N N 449 
TYR CB    CG     sing N N 450 
TYR CB    HB2    sing N N 451 
TYR CB    HB3    sing N N 452 
TYR CG    CD1    doub Y N 453 
TYR CG    CD2    sing Y N 454 
TYR CD1   CE1    sing Y N 455 
TYR CD1   HD1    sing N N 456 
TYR CD2   CE2    doub Y N 457 
TYR CD2   HD2    sing N N 458 
TYR CE1   CZ     doub Y N 459 
TYR CE1   HE1    sing N N 460 
TYR CE2   CZ     sing Y N 461 
TYR CE2   HE2    sing N N 462 
TYR CZ    OH     sing N N 463 
TYR OH    HH     sing N N 464 
TYR OXT   HXT    sing N N 465 
VAL N     CA     sing N N 466 
VAL N     H      sing N N 467 
VAL N     H2     sing N N 468 
VAL CA    C      sing N N 469 
VAL CA    CB     sing N N 470 
VAL CA    HA     sing N N 471 
VAL C     O      doub N N 472 
VAL C     OXT    sing N N 473 
VAL CB    CG1    sing N N 474 
VAL CB    CG2    sing N N 475 
VAL CB    HB     sing N N 476 
VAL CG1   HG11   sing N N 477 
VAL CG1   HG12   sing N N 478 
VAL CG1   HG13   sing N N 479 
VAL CG2   HG21   sing N N 480 
VAL CG2   HG22   sing N N 481 
VAL CG2   HG23   sing N N 482 
VAL OXT   HXT    sing N N 483 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'Ventus therapeutics' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4LEW 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9C8T 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.007910 
_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]   0.019241 
_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]   0.016729 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
MG 
N  
O  
P  
S  
ZN 
# 
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     . SER A 1 8   ? 10.419 -3.489  11.471  1.00 43.34 ? 163  SER A N     1 
ATOM   2    C  CA    . SER A 1 8   ? 9.716  -2.313  10.980  1.00 34.26 ? 163  SER A CA    1 
ATOM   3    C  C     . SER A 1 8   ? 10.595 -1.501  10.062  1.00 30.42 ? 163  SER A C     1 
ATOM   4    O  O     . SER A 1 8   ? 10.101 -0.907  9.102   1.00 23.99 ? 163  SER A O     1 
ATOM   5    C  CB    . SER A 1 8   ? 9.193  -1.435  12.119  1.00 47.54 ? 163  SER A CB    1 
ATOM   6    O  OG    . SER A 1 8   ? 8.139  -0.597  11.665  1.00 48.18 ? 163  SER A OG    1 
ATOM   7    N  N     . LYS A 1 9   ? 11.895 -1.448  10.357  1.00 26.25 ? 164  LYS A N     1 
ATOM   8    C  CA    . LYS A 1 9   ? 12.821 -0.797  9.439   1.00 22.52 ? 164  LYS A CA    1 
ATOM   9    C  C     . LYS A 1 9   ? 12.737 -1.430  8.047   1.00 21.97 ? 164  LYS A C     1 
ATOM   10   O  O     . LYS A 1 9   ? 12.671 -0.732  7.030   1.00 22.42 ? 164  LYS A O     1 
ATOM   11   C  CB    . LYS A 1 9   ? 14.242 -0.862  9.983   1.00 32.81 ? 164  LYS A CB    1 
ATOM   12   C  CG    . LYS A 1 9   ? 15.296 -0.283  9.048   1.00 35.71 ? 164  LYS A CG    1 
ATOM   13   C  CD    . LYS A 1 9   ? 16.495 0.299   9.830   1.00 42.71 ? 164  LYS A CD    1 
ATOM   14   C  CE    . LYS A 1 9   ? 17.711 0.489   8.906   1.00 45.77 ? 164  LYS A CE    1 
ATOM   15   N  NZ    . LYS A 1 9   ? 19.049 0.765   9.579   1.00 41.62 ? 164  LYS A NZ    1 
ATOM   16   N  N     . LEU A 1 10  ? 12.771 -2.755  7.984   1.00 22.57 ? 165  LEU A N     1 
ATOM   17   C  CA    . LEU A 1 10  ? 12.710 -3.403  6.673   1.00 19.72 ? 165  LEU A CA    1 
ATOM   18   C  C     . LEU A 1 10  ? 11.370 -3.162  5.995   1.00 18.27 ? 165  LEU A C     1 
ATOM   19   O  O     . LEU A 1 10  ? 11.317 -2.984  4.767   1.00 17.45 ? 165  LEU A O     1 
ATOM   20   C  CB    . LEU A 1 10  ? 12.988 -4.893  6.834   1.00 17.50 ? 165  LEU A CB    1 
ATOM   21   C  CG    . LEU A 1 10  ? 14.416 -5.174  7.262   1.00 19.88 ? 165  LEU A CG    1 
ATOM   22   C  CD1   . LEU A 1 10  ? 14.480 -6.699  7.450   1.00 21.10 ? 165  LEU A CD1   1 
ATOM   23   C  CD2   . LEU A 1 10  ? 15.483 -4.710  6.268   1.00 21.17 ? 165  LEU A CD2   1 
ATOM   24   N  N     . ARG A 1 11  ? 10.282 -3.158  6.753   1.00 20.01 ? 166  ARG A N     1 
ATOM   25   C  CA    . ARG A 1 11  ? 8.994  -2.875  6.137   1.00 18.73 ? 166  ARG A CA    1 
ATOM   26   C  C     . ARG A 1 11  ? 9.005  -1.482  5.535   1.00 19.85 ? 166  ARG A C     1 
ATOM   27   O  O     . ARG A 1 11  ? 8.485  -1.257  4.438   1.00 18.96 ? 166  ARG A O     1 
ATOM   28   C  CB    . ARG A 1 11  ? 7.838  -3.049  7.130   1.00 22.28 ? 166  ARG A CB    1 
ATOM   29   C  CG    . ARG A 1 11  ? 6.441  -2.809  6.528   1.00 26.61 ? 166  ARG A CG    1 
ATOM   30   C  CD    . ARG A 1 11  ? 6.065  -3.842  5.451   1.00 26.17 ? 166  ARG A CD    1 
ATOM   31   N  NE    . ARG A 1 11  ? 6.126  -5.214  5.948   1.00 24.96 ? 166  ARG A NE    1 
ATOM   32   C  CZ    . ARG A 1 11  ? 6.255  -6.284  5.173   1.00 28.03 ? 166  ARG A CZ    1 
ATOM   33   N  NH1   . ARG A 1 11  ? 6.270  -6.182  3.850   1.00 22.54 ? 166  ARG A NH1   1 
ATOM   34   N  NH2   . ARG A 1 11  ? 6.373  -7.481  5.735   1.00 24.78 ? 166  ARG A NH2   1 
ATOM   35   N  N     . ALA A 1 12  ? 9.610  -0.526  6.239   1.00 18.52 ? 167  ALA A N     1 
ATOM   36   C  CA    . ALA A 1 12  ? 9.680  0.827   5.693   1.00 20.28 ? 167  ALA A CA    1 
ATOM   37   C  C     . ALA A 1 12  ? 10.541 0.880   4.436   1.00 19.62 ? 167  ALA A C     1 
ATOM   38   O  O     . ALA A 1 12  ? 10.258 1.658   3.509   1.00 19.36 ? 167  ALA A O     1 
ATOM   39   C  CB    . ALA A 1 12  ? 10.173 1.809   6.768   1.00 19.33 ? 167  ALA A CB    1 
ATOM   40   N  N     . VAL A 1 13  ? 11.615 0.091   4.385   1.00 17.65 ? 168  VAL A N     1 
ATOM   41   C  CA    . VAL A 1 13  ? 12.385 -0.010  3.145   1.00 17.55 ? 168  VAL A CA    1 
ATOM   42   C  C     . VAL A 1 13  ? 11.498 -0.527  2.024   1.00 16.75 ? 168  VAL A C     1 
ATOM   43   O  O     . VAL A 1 13  ? 11.488 0.017   0.916   1.00 16.25 ? 168  VAL A O     1 
ATOM   44   C  CB    . VAL A 1 13  ? 13.643 -0.886  3.321   1.00 18.80 ? 168  VAL A CB    1 
ATOM   45   C  CG1   . VAL A 1 13  ? 14.364 -1.046  2.001   1.00 19.43 ? 168  VAL A CG1   1 
ATOM   46   C  CG2   . VAL A 1 13  ? 14.563 -0.244  4.403   1.00 23.32 ? 168  VAL A CG2   1 
ATOM   47   N  N     . LEU A 1 14  ? 10.757 -1.596  2.287   1.00 15.57 ? 169  LEU A N     1 
ATOM   48   C  CA    . LEU A 1 14  ? 9.912  -2.157  1.229   1.00 16.00 ? 169  LEU A CA    1 
ATOM   49   C  C     . LEU A 1 14  ? 8.879  -1.155  0.734   1.00 17.41 ? 169  LEU A C     1 
ATOM   50   O  O     . LEU A 1 14  ? 8.565  -1.119  -0.456  1.00 16.84 ? 169  LEU A O     1 
ATOM   51   C  CB    . LEU A 1 14  ? 9.234  -3.408  1.738   1.00 15.89 ? 169  LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 14  ? 10.182 -4.595  1.825   1.00 16.99 ? 169  LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 14  ? 9.618  -5.612  2.764   1.00 17.58 ? 169  LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 14  ? 10.446 -5.215  0.409   1.00 17.83 ? 169  LEU A CD2   1 
ATOM   55   N  N     . GLU A 1 15  ? 8.348  -0.319  1.623   1.00 16.24 ? 170  GLU A N     1 
ATOM   56   C  CA    . GLU A 1 15  ? 7.412  0.721   1.183   1.00 16.38 ? 170  GLU A CA    1 
ATOM   57   C  C     . GLU A 1 15  ? 8.045  1.669   0.177   1.00 16.71 ? 170  GLU A C     1 
ATOM   58   O  O     . GLU A 1 15  ? 7.420  2.035   -0.828  1.00 21.06 ? 170  GLU A O     1 
ATOM   59   C  CB    . GLU A 1 15  ? 6.919  1.510   2.396   1.00 23.70 ? 170  GLU A CB    1 
ATOM   60   C  CG    . GLU A 1 15  ? 6.299  0.665   3.455   1.00 37.23 ? 170  GLU A CG    1 
ATOM   61   C  CD    . GLU A 1 15  ? 5.374  -0.389  2.880   1.00 49.68 ? 170  GLU A CD    1 
ATOM   62   O  OE1   . GLU A 1 15  ? 4.322  0.002   2.296   1.00 43.16 ? 170  GLU A OE1   1 
ATOM   63   O  OE2   . GLU A 1 15  ? 5.730  -1.605  3.000   1.00 37.30 ? 170  GLU A OE2   1 
ATOM   64   N  N     . LYS A 1 16  ? 9.283  2.083   0.421   1.00 17.09 ? 171  LYS A N     1 
ATOM   65   C  CA    . LYS A 1 16  ? 10.002 2.949   -0.489  1.00 20.20 ? 171  LYS A CA    1 
ATOM   66   C  C     . LYS A 1 16  ? 10.296 2.253   -1.806  1.00 19.04 ? 171  LYS A C     1 
ATOM   67   O  O     . LYS A 1 16  ? 10.442 2.918   -2.832  1.00 24.16 ? 171  LYS A O     1 
ATOM   68   C  CB    . LYS A 1 16  ? 11.316 3.370   0.173   1.00 29.59 ? 171  LYS A CB    1 
ATOM   69   C  CG    . LYS A 1 16  ? 12.273 4.225   -0.671  1.00 32.86 ? 171  LYS A CG    1 
ATOM   70   C  CD    . LYS A 1 16  ? 13.768 3.905   -0.368  1.00 38.33 ? 171  LYS A CD    1 
ATOM   71   C  CE    . LYS A 1 16  ? 14.136 4.208   1.097   1.00 44.82 ? 171  LYS A CE    1 
ATOM   72   N  NZ    . LYS A 1 16  ? 15.412 3.571   1.588   1.00 42.56 ? 171  LYS A NZ    1 
ATOM   73   N  N     . LEU A 1 17  ? 10.429 0.922   -1.806  1.00 16.11 ? 172  LEU A N     1 
ATOM   74   C  CA    . LEU A 1 17  ? 10.740 0.188   -3.034  1.00 15.89 ? 172  LEU A CA    1 
ATOM   75   C  C     . LEU A 1 17  ? 9.515  -0.058  -3.902  1.00 17.20 ? 172  LEU A C     1 
ATOM   76   O  O     . LEU A 1 17  ? 9.677  -0.487  -5.054  1.00 16.13 ? 172  LEU A O     1 
ATOM   77   C  CB    . LEU A 1 17  ? 11.359 -1.171  -2.692  1.00 16.05 ? 172  LEU A CB    1 
ATOM   78   C  CG    . LEU A 1 17  ? 12.686 -0.997  -1.955  1.00 20.37 ? 172  LEU A CG    1 
ATOM   79   C  CD1   . LEU A 1 17  ? 13.279 -2.373  -1.789  1.00 16.90 ? 172  LEU A CD1   1 
ATOM   80   C  CD2   . LEU A 1 17  ? 13.608 -0.092  -2.703  1.00 20.66 ? 172  LEU A CD2   1 
ATOM   81   N  N     . LYS A 1 18  ? 8.317  0.191   -3.392  1.00 15.17 ? 173  LYS A N     1 
ATOM   82   C  CA    . LYS A 1 18  ? 7.116  -0.071  -4.175  1.00 14.52 ? 173  LYS A CA    1 
ATOM   83   C  C     . LYS A 1 18  ? 7.050  0.807   -5.412  1.00 16.66 ? 173  LYS A C     1 
ATOM   84   O  O     . LYS A 1 18  ? 7.471  1.966   -5.426  1.00 18.72 ? 173  LYS A O     1 
ATOM   85   C  CB    . LYS A 1 18  ? 5.856  0.209   -3.338  1.00 15.43 ? 173  LYS A CB    1 
ATOM   86   C  CG    . LYS A 1 18  ? 5.594  -0.857  -2.311  1.00 17.34 ? 173  LYS A CG    1 
ATOM   87   C  CD    . LYS A 1 18  ? 4.349  -0.494  -1.509  1.00 19.34 ? 173  LYS A CD    1 
ATOM   88   C  CE    . LYS A 1 18  ? 4.097  -1.624  -0.519  1.00 22.39 ? 173  LYS A CE    1 
ATOM   89   N  NZ    . LYS A 1 18  ? 2.912  -1.322  0.345   1.00 24.85 ? 173  LYS A NZ    1 
ATOM   90   N  N     . LEU A 1 19  ? 6.503  0.233   -6.465  1.00 15.14 ? 174  LEU A N     1 
ATOM   91   C  CA    . LEU A 1 19  ? 6.348  0.961   -7.713  1.00 15.75 ? 174  LEU A CA    1 
ATOM   92   C  C     . LEU A 1 19  ? 5.062  1.785   -7.676  1.00 15.09 ? 174  LEU A C     1 
ATOM   93   O  O     . LEU A 1 19  ? 4.013  1.327   -7.207  1.00 16.19 ? 174  LEU A O     1 
ATOM   94   C  CB    . LEU A 1 19  ? 6.247  -0.021  -8.871  1.00 14.12 ? 174  LEU A CB    1 
ATOM   95   C  CG    . LEU A 1 19  ? 7.393  -1.021  -9.049  1.00 18.29 ? 174  LEU A CG    1 
ATOM   96   C  CD1   . LEU A 1 19  ? 7.089  -1.836  -10.324 1.00 17.46 ? 174  LEU A CD1   1 
ATOM   97   C  CD2   . LEU A 1 19  ? 8.734  -0.253  -9.136  1.00 18.54 ? 174  LEU A CD2   1 
ATOM   98   N  N     . SER A 1 20  ? 5.163  3.013   -8.167  1.00 16.00 ? 175  SER A N     1 
ATOM   99   C  CA    . SER A 1 20  ? 3.995  3.891   -8.244  1.00 15.60 ? 175  SER A CA    1 
ATOM   100  C  C     . SER A 1 20  ? 3.011  3.367   -9.293  1.00 15.67 ? 175  SER A C     1 
ATOM   101  O  O     . SER A 1 20  ? 3.405  2.978   -10.397 1.00 16.94 ? 175  SER A O     1 
ATOM   102  C  CB    . SER A 1 20  ? 4.500  5.269   -8.657  1.00 20.22 ? 175  SER A CB    1 
ATOM   103  O  OG    . SER A 1 20  ? 3.586  5.985   -9.470  1.00 24.69 ? 175  SER A OG    1 
ATOM   104  N  N     . ARG A 1 21  ? 1.718  3.426   -8.970  1.00 15.12 ? 176  ARG A N     1 
ATOM   105  C  CA    . ARG A 1 21  ? 0.710  2.975   -9.910  1.00 16.80 ? 176  ARG A CA    1 
ATOM   106  C  C     . ARG A 1 21  ? 0.701  3.848   -11.153 1.00 17.35 ? 176  ARG A C     1 
ATOM   107  O  O     . ARG A 1 21  ? 0.543  3.340   -12.267 1.00 15.48 ? 176  ARG A O     1 
ATOM   108  C  CB    . ARG A 1 21  ? -0.635 2.987   -9.229  1.00 16.17 ? 176  ARG A CB    1 
ATOM   109  C  CG    . ARG A 1 21  ? -0.821 1.840   -8.243  1.00 15.92 ? 176  ARG A CG    1 
ATOM   110  C  CD    . ARG A 1 21  ? -2.152 2.007   -7.494  1.00 15.77 ? 176  ARG A CD    1 
ATOM   111  N  NE    . ARG A 1 21  ? -2.417 0.843   -6.652  1.00 16.40 ? 176  ARG A NE    1 
ATOM   112  C  CZ    . ARG A 1 21  ? -1.937 0.664   -5.437  1.00 17.62 ? 176  ARG A CZ    1 
ATOM   113  N  NH1   . ARG A 1 21  ? -1.140 1.556   -4.885  1.00 18.68 ? 176  ARG A NH1   1 
ATOM   114  N  NH2   . ARG A 1 21  ? -2.263 -0.437  -4.767  1.00 19.06 ? 176  ARG A NH2   1 
ATOM   115  N  N     . ASP A 1 22  ? 0.952  5.147   -10.985 1.00 16.66 ? 177  ASP A N     1 
ATOM   116  C  CA    . ASP A 1 22  ? 0.966  6.041   -12.124 1.00 16.57 ? 177  ASP A CA    1 
ATOM   117  C  C     . ASP A 1 22  ? 2.155  5.756   -13.033 1.00 18.77 ? 177  ASP A C     1 
ATOM   118  O  O     . ASP A 1 22  ? 1.987  5.664   -14.253 1.00 16.29 ? 177  ASP A O     1 
ATOM   119  C  CB    . ASP A 1 22  ? 0.959  7.497   -11.656 1.00 19.34 ? 177  ASP A CB    1 
ATOM   120  C  CG    . ASP A 1 22  ? 0.945  8.456   -12.829 1.00 37.93 ? 177  ASP A CG    1 
ATOM   121  O  OD1   . ASP A 1 22  ? -0.104 8.523   -13.503 1.00 39.86 ? 177  ASP A OD1   1 
ATOM   122  O  OD2   . ASP A 1 22  ? 1.969  9.131   -13.080 1.00 42.54 ? 177  ASP A OD2   1 
ATOM   123  N  N     . ASP A 1 23  ? 3.339  5.528   -12.451 1.00 17.83 ? 178  ASP A N     1 
ATOM   124  C  CA    . ASP A 1 23  ? 4.498  5.139   -13.250 1.00 16.87 ? 178  ASP A CA    1 
ATOM   125  C  C     . ASP A 1 23  ? 4.265  3.813   -13.969 1.00 14.86 ? 178  ASP A C     1 
ATOM   126  O  O     . ASP A 1 23  ? 4.646  3.675   -15.132 1.00 15.80 ? 178  ASP A O     1 
ATOM   127  C  CB    . ASP A 1 23  ? 5.689  4.960   -12.320 1.00 17.53 ? 178  ASP A CB    1 
ATOM   128  C  CG    . ASP A 1 23  ? 6.257  6.263   -11.828 1.00 39.40 ? 178  ASP A CG    1 
ATOM   129  O  OD1   . ASP A 1 23  ? 5.835  7.338   -12.319 1.00 35.58 ? 178  ASP A OD1   1 
ATOM   130  O  OD2   . ASP A 1 23  ? 7.126  6.186   -10.921 1.00 36.13 ? 178  ASP A OD2   1 
ATOM   131  N  N     . ILE A 1 24  ? 3.616  2.838   -13.316 1.00 15.14 ? 179  ILE A N     1 
ATOM   132  C  CA    . ILE A 1 24  ? 3.284  1.579   -13.989 1.00 15.62 ? 179  ILE A CA    1 
ATOM   133  C  C     . ILE A 1 24  ? 2.410  1.824   -15.210 1.00 16.37 ? 179  ILE A C     1 
ATOM   134  O  O     . ILE A 1 24  ? 2.654  1.301   -16.296 1.00 15.36 ? 179  ILE A O     1 
ATOM   135  C  CB    . ILE A 1 24  ? 2.620  0.606   -12.997 1.00 15.79 ? 179  ILE A CB    1 
ATOM   136  C  CG1   . ILE A 1 24  ? 3.680  0.048   -12.036 1.00 15.75 ? 179  ILE A CG1   1 
ATOM   137  C  CG2   . ILE A 1 24  ? 1.923  -0.540  -13.698 1.00 16.40 ? 179  ILE A CG2   1 
ATOM   138  C  CD1   . ILE A 1 24  ? 3.069  -0.558  -10.866 1.00 18.47 ? 179  ILE A CD1   1 
ATOM   139  N  N     . SER A 1 25  ? 1.347  2.604   -15.048 1.00 14.87 ? 180  SER A N     1 
ATOM   140  C  CA    . SER A 1 25  ? 0.422  2.791   -16.150 1.00 15.71 ? 180  SER A CA    1 
ATOM   141  C  C     . SER A 1 25  ? 1.115  3.462   -17.336 1.00 18.18 ? 180  SER A C     1 
ATOM   142  O  O     . SER A 1 25  ? 0.986  3.005   -18.479 1.00 20.09 ? 180  SER A O     1 
ATOM   143  C  CB    . SER A 1 25  ? -0.679 3.673   -15.604 1.00 15.97 ? 180  SER A CB    1 
ATOM   144  O  OG    . SER A 1 25  ? -1.697 3.765   -16.607 1.00 20.34 ? 180  SER A OG    1 
ATOM   145  N  N     . THR A 1 26  ? 1.892  4.512   -17.072 1.00 16.83 ? 181  THR A N     1 
ATOM   146  C  CA    . THR A 1 26  ? 2.626  5.201   -18.123 1.00 18.12 ? 181  THR A CA    1 
ATOM   147  C  C     . THR A 1 26  ? 3.660  4.294   -18.771 1.00 19.58 ? 181  THR A C     1 
ATOM   148  O  O     . THR A 1 26  ? 3.750  4.227   -19.995 1.00 18.80 ? 181  THR A O     1 
ATOM   149  C  CB    . THR A 1 26  ? 3.280  6.436   -17.531 1.00 21.70 ? 181  THR A CB    1 
ATOM   150  O  OG1   . THR A 1 26  ? 2.241  7.370   -17.181 1.00 24.80 ? 181  THR A OG1   1 
ATOM   151  C  CG2   . THR A 1 26  ? 4.262  7.084   -18.525 1.00 24.96 ? 181  THR A CG2   1 
ATOM   152  N  N     . ALA A 1 27  ? 4.417  3.547   -17.968 1.00 17.77 ? 182  ALA A N     1 
ATOM   153  C  CA    . ALA A 1 27  ? 5.501  2.742   -18.546 1.00 17.80 ? 182  ALA A CA    1 
ATOM   154  C  C     . ALA A 1 27  ? 4.953  1.577   -19.338 1.00 17.83 ? 182  ALA A C     1 
ATOM   155  O  O     . ALA A 1 27  ? 5.467  1.256   -20.415 1.00 18.68 ? 182  ALA A O     1 
ATOM   156  C  CB    . ALA A 1 27  ? 6.425  2.200   -17.465 1.00 17.36 ? 182  ALA A CB    1 
ATOM   157  N  N     . ALA A 1 28  ? 3.909  0.930   -18.835 1.00 18.85 ? 183  ALA A N     1 
ATOM   158  C  CA    . ALA A 1 28  ? 3.319  -0.191  -19.558 1.00 18.84 ? 183  ALA A CA    1 
ATOM   159  C  C     . ALA A 1 28  ? 2.881  0.216   -20.957 1.00 24.44 ? 183  ALA A C     1 
ATOM   160  O  O     . ALA A 1 28  ? 3.117  -0.519  -21.925 1.00 21.69 ? 183  ALA A O     1 
ATOM   161  C  CB    . ALA A 1 28  ? 2.161  -0.767  -18.761 1.00 24.98 ? 183  ALA A CB    1 
ATOM   162  N  N     . GLY A 1 29  ? 2.326  1.423   -21.104 1.00 21.54 ? 184  GLY A N     1 
ATOM   163  C  CA    . GLY A 1 29  ? 1.910  1.867   -22.423 1.00 22.72 ? 184  GLY A CA    1 
ATOM   164  C  C     . GLY A 1 29  ? 3.086  2.227   -23.312 1.00 21.25 ? 184  GLY A C     1 
ATOM   165  O  O     . GLY A 1 29  ? 3.082  1.928   -24.507 1.00 24.78 ? 184  GLY A O     1 
ATOM   166  N  N     . MET A 1 30  ? 4.110  2.866   -22.752 1.00 18.85 ? 185  MET A N     1 
ATOM   167  C  CA    . MET A 1 30  ? 5.265  3.224   -23.563 1.00 20.56 ? 185  MET A CA    1 
ATOM   168  C  C     . MET A 1 30  ? 5.932  1.968   -24.098 1.00 20.72 ? 185  MET A C     1 
ATOM   169  O  O     . MET A 1 30  ? 6.242  1.873   -25.287 1.00 25.39 ? 185  MET A O     1 
ATOM   170  C  CB    . MET A 1 30  ? 6.259  4.029   -22.738 1.00 21.60 ? 185  MET A CB    1 
ATOM   171  C  CG    . MET A 1 30  ? 5.695  5.378   -22.273 1.00 29.74 ? 185  MET A CG    1 
ATOM   172  S  SD    . MET A 1 30  ? 6.712  6.200   -21.015 1.00 61.46 ? 185  MET A SD    1 
ATOM   173  C  CE    . MET A 1 30  ? 8.032  6.863   -22.006 1.00 45.44 ? 185  MET A CE    1 
ATOM   174  N  N     . VAL A 1 31  ? 6.125  0.971   -23.234 1.00 19.24 ? 186  VAL A N     1 
ATOM   175  C  CA    . VAL A 1 31  ? 6.741  -0.276  -23.673 1.00 20.48 ? 186  VAL A CA    1 
ATOM   176  C  C     . VAL A 1 31  ? 5.890  -0.965  -24.733 1.00 21.99 ? 186  VAL A C     1 
ATOM   177  O  O     . VAL A 1 31  ? 6.410  -1.478  -25.737 1.00 21.68 ? 186  VAL A O     1 
ATOM   178  C  CB    . VAL A 1 31  ? 6.989  -1.171  -22.441 1.00 16.88 ? 186  VAL A CB    1 
ATOM   179  C  CG1   . VAL A 1 31  ? 7.381  -2.621  -22.866 1.00 19.26 ? 186  VAL A CG1   1 
ATOM   180  C  CG2   . VAL A 1 31  ? 8.074  -0.563  -21.587 1.00 18.23 ? 186  VAL A CG2   1 
ATOM   181  N  N     . LYS A 1 32  ? 4.584  -1.041  -24.510 1.00 19.79 ? 187  LYS A N     1 
ATOM   182  C  CA    . LYS A 1 32  ? 3.710  -1.715  -25.459 1.00 25.00 ? 187  LYS A CA    1 
ATOM   183  C  C     . LYS A 1 32  ? 3.793  -1.079  -26.832 1.00 23.06 ? 187  LYS A C     1 
ATOM   184  O  O     . LYS A 1 32  ? 3.885  -1.786  -27.839 1.00 23.39 ? 187  LYS A O     1 
ATOM   185  C  CB    . LYS A 1 32  ? 2.270  -1.686  -24.959 1.00 23.23 ? 187  LYS A CB    1 
ATOM   186  C  CG    . LYS A 1 32  ? 1.317  -2.398  -25.940 1.00 26.27 ? 187  LYS A CG    1 
ATOM   187  C  CD    . LYS A 1 32  ? -0.117 -2.109  -25.613 1.00 33.19 ? 187  LYS A CD    1 
ATOM   188  C  CE    . LYS A 1 32  ? -1.055 -2.881  -26.542 1.00 34.83 ? 187  LYS A CE    1 
ATOM   189  N  NZ    . LYS A 1 32  ? -0.552 -4.235  -26.905 1.00 39.96 ? 187  LYS A NZ    1 
ATOM   190  N  N     . GLY A 1 33  ? 3.792  0.247   -26.899 1.00 20.97 ? 188  GLY A N     1 
ATOM   191  C  CA    . GLY A 1 33  ? 3.865  0.891   -28.204 1.00 26.09 ? 188  GLY A CA    1 
ATOM   192  C  C     . GLY A 1 33  ? 5.123  0.520   -28.961 1.00 28.95 ? 188  GLY A C     1 
ATOM   193  O  O     . GLY A 1 33  ? 5.088  0.271   -30.165 1.00 25.50 ? 188  GLY A O     1 
ATOM   194  N  N     . VAL A 1 34  ? 6.245  0.440   -28.261 1.00 22.27 ? 189  VAL A N     1 
ATOM   195  C  CA    . VAL A 1 34  ? 7.512  0.100   -28.908 1.00 22.78 ? 189  VAL A CA    1 
ATOM   196  C  C     . VAL A 1 34  ? 7.551  -1.373  -29.276 1.00 24.31 ? 189  VAL A C     1 
ATOM   197  O  O     . VAL A 1 34  ? 7.888  -1.731  -30.416 1.00 21.26 ? 189  VAL A O     1 
ATOM   198  C  CB    . VAL A 1 34  ? 8.680  0.506   -28.013 1.00 22.34 ? 189  VAL A CB    1 
ATOM   199  C  CG1   . VAL A 1 34  ? 9.975  0.048   -28.624 1.00 24.66 ? 189  VAL A CG1   1 
ATOM   200  C  CG2   . VAL A 1 34  ? 8.685  2.006   -27.841 1.00 28.41 ? 189  VAL A CG2   1 
ATOM   201  N  N     . VAL A 1 35  ? 7.153  -2.248  -28.341 1.00 20.20 ? 190  VAL A N     1 
ATOM   202  C  CA    . VAL A 1 35  ? 7.230  -3.688  -28.580 1.00 19.74 ? 190  VAL A CA    1 
ATOM   203  C  C     . VAL A 1 35  ? 6.318  -4.101  -29.715 1.00 25.31 ? 190  VAL A C     1 
ATOM   204  O  O     . VAL A 1 35  ? 6.708  -4.890  -30.588 1.00 24.38 ? 190  VAL A O     1 
ATOM   205  C  CB    . VAL A 1 35  ? 6.968  -4.458  -27.275 1.00 23.67 ? 190  VAL A CB    1 
ATOM   206  C  CG1   . VAL A 1 35  ? 6.717  -5.946  -27.542 1.00 26.53 ? 190  VAL A CG1   1 
ATOM   207  C  CG2   . VAL A 1 35  ? 8.148  -4.250  -26.384 1.00 25.47 ? 190  VAL A CG2   1 
ATOM   208  N  N     . ASP A 1 36  ? 5.103  -3.567  -29.728 1.00 25.84 ? 191  ASP A N     1 
ATOM   209  C  CA    . ASP A 1 36  ? 4.147  -3.911  -30.769 1.00 26.92 ? 191  ASP A CA    1 
ATOM   210  C  C     . ASP A 1 36  ? 4.638  -3.452  -32.127 1.00 24.46 ? 191  ASP A C     1 
ATOM   211  O  O     . ASP A 1 36  ? 4.520  -4.191  -33.109 1.00 26.75 ? 191  ASP A O     1 
ATOM   212  C  CB    . ASP A 1 36  ? 2.798  -3.267  -30.444 1.00 25.95 ? 191  ASP A CB    1 
ATOM   213  C  CG    . ASP A 1 36  ? 2.062  -4.000  -29.341 1.00 37.39 ? 191  ASP A CG    1 
ATOM   214  O  OD1   . ASP A 1 36  ? 2.637  -4.961  -28.774 1.00 33.12 ? 191  ASP A OD1   1 
ATOM   215  O  OD2   . ASP A 1 36  ? 0.906  -3.612  -29.044 1.00 40.64 ? 191  ASP A OD2   1 
ATOM   216  N  N     . HIS A 1 37  ? 5.197  -2.239  -32.203 1.00 22.31 ? 192  HIS A N     1 
ATOM   217  C  CA    . HIS A 1 37  ? 5.704  -1.750  -33.480 1.00 26.28 ? 192  HIS A CA    1 
ATOM   218  C  C     . HIS A 1 37  ? 6.827  -2.643  -34.002 1.00 29.43 ? 192  HIS A C     1 
ATOM   219  O  O     . HIS A 1 37  ? 6.836  -3.029  -35.179 1.00 25.84 ? 192  HIS A O     1 
ATOM   220  C  CB    . HIS A 1 37  ? 6.162  -0.299  -33.322 1.00 30.87 ? 192  HIS A CB    1 
ATOM   221  C  CG    . HIS A 1 37  ? 6.651  0.337   -34.587 1.00 34.22 ? 192  HIS A CG    1 
ATOM   222  N  ND1   . HIS A 1 37  ? 7.983  0.364   -34.939 1.00 36.27 ? 192  HIS A ND1   1 
ATOM   223  C  CD2   . HIS A 1 37  ? 5.996  1.047   -35.534 1.00 39.66 ? 192  HIS A CD2   1 
ATOM   224  C  CE1   . HIS A 1 37  ? 8.123  1.024   -36.076 1.00 40.52 ? 192  HIS A CE1   1 
ATOM   225  N  NE2   . HIS A 1 37  ? 6.931  1.448   -36.459 1.00 42.58 ? 192  HIS A NE2   1 
ATOM   226  N  N     . LEU A 1 38  ? 7.762  -3.019  -33.130 1.00 21.59 ? 193  LEU A N     1 
ATOM   227  C  CA    . LEU A 1 38  ? 8.879  -3.848  -33.560 1.00 24.17 ? 193  LEU A CA    1 
ATOM   228  C  C     . LEU A 1 38  ? 8.428  -5.248  -33.946 1.00 24.94 ? 193  LEU A C     1 
ATOM   229  O  O     . LEU A 1 38  ? 8.950  -5.836  -34.909 1.00 24.76 ? 193  LEU A O     1 
ATOM   230  C  CB    . LEU A 1 38  ? 9.931  -3.892  -32.460 1.00 20.60 ? 193  LEU A CB    1 
ATOM   231  C  CG    . LEU A 1 38  ? 10.551 -2.521  -32.225 1.00 23.83 ? 193  LEU A CG    1 
ATOM   232  C  CD1   . LEU A 1 38  ? 11.521 -2.572  -31.057 1.00 23.15 ? 193  LEU A CD1   1 
ATOM   233  C  CD2   . LEU A 1 38  ? 11.195 -1.984  -33.527 1.00 26.38 ? 193  LEU A CD2   1 
ATOM   234  N  N     . LEU A 1 39  ? 7.478  -5.814  -33.215 1.00 22.88 ? 194  LEU A N     1 
ATOM   235  C  CA    . LEU A 1 39  ? 6.998  -7.142  -33.583 1.00 26.12 ? 194  LEU A CA    1 
ATOM   236  C  C     . LEU A 1 39  ? 6.390  -7.118  -34.973 1.00 29.75 ? 194  LEU A C     1 
ATOM   237  O  O     . LEU A 1 39  ? 6.616  -8.029  -35.777 1.00 29.66 ? 194  LEU A O     1 
ATOM   238  C  CB    . LEU A 1 39  ? 5.947  -7.626  -32.589 1.00 26.72 ? 194  LEU A CB    1 
ATOM   239  C  CG    . LEU A 1 39  ? 6.480  -8.116  -31.258 1.00 26.88 ? 194  LEU A CG    1 
ATOM   240  C  CD1   . LEU A 1 39  ? 5.261  -8.275  -30.354 1.00 26.92 ? 194  LEU A CD1   1 
ATOM   241  C  CD2   . LEU A 1 39  ? 7.205  -9.457  -31.501 1.00 26.50 ? 194  LEU A CD2   1 
ATOM   242  N  N     . LEU A 1 40  ? 5.600  -6.087  -35.260 1.00 26.51 ? 195  LEU A N     1 
ATOM   243  C  CA    . LEU A 1 40  ? 4.948  -5.984  -36.564 1.00 32.93 ? 195  LEU A CA    1 
ATOM   244  C  C     . LEU A 1 40  ? 5.978  -5.891  -37.674 1.00 33.23 ? 195  LEU A C     1 
ATOM   245  O  O     . LEU A 1 40  ? 5.853  -6.550  -38.713 1.00 31.36 ? 195  LEU A O     1 
ATOM   246  C  CB    . LEU A 1 40  ? 4.048  -4.753  -36.584 1.00 28.97 ? 195  LEU A CB    1 
ATOM   247  C  CG    . LEU A 1 40  ? 2.570  -4.870  -36.254 1.00 41.45 ? 195  LEU A CG    1 
ATOM   248  C  CD1   . LEU A 1 40  ? 1.829  -3.668  -36.837 1.00 40.11 ? 195  LEU A CD1   1 
ATOM   249  C  CD2   . LEU A 1 40  ? 2.029  -6.173  -36.827 1.00 43.89 ? 195  LEU A CD2   1 
ATOM   250  N  N     . ARG A 1 41  ? 7.006  -5.069  -37.478 1.00 24.37 ? 196  ARG A N     1 
ATOM   251  C  CA    . ARG A 1 41  ? 8.049  -4.937  -38.481 1.00 27.83 ? 196  ARG A CA    1 
ATOM   252  C  C     . ARG A 1 41  ? 8.802  -6.249  -38.661 1.00 32.22 ? 196  ARG A C     1 
ATOM   253  O  O     . ARG A 1 41  ? 9.071  -6.661  -39.795 1.00 26.71 ? 196  ARG A O     1 
ATOM   254  C  CB    . ARG A 1 41  ? 9.020  -3.823  -38.078 1.00 34.46 ? 196  ARG A CB    1 
ATOM   255  C  CG    . ARG A 1 41  ? 10.324 -3.787  -38.908 1.00 39.59 ? 196  ARG A CG    1 
ATOM   256  C  CD    . ARG A 1 41  ? 10.067 -3.549  -40.420 1.00 46.82 ? 196  ARG A CD    1 
ATOM   257  N  NE    . ARG A 1 41  ? 11.306 -3.495  -41.192 1.00 41.45 ? 196  ARG A NE    1 
ATOM   258  C  CZ    . ARG A 1 41  ? 11.886 -4.549  -41.753 1.00 41.32 ? 196  ARG A CZ    1 
ATOM   259  N  NH1   . ARG A 1 41  ? 11.342 -5.762  -41.674 1.00 34.05 ? 196  ARG A NH1   1 
ATOM   260  N  NH2   . ARG A 1 41  ? 13.036 -4.382  -42.412 1.00 38.19 ? 196  ARG A NH2   1 
ATOM   261  N  N     . LEU A 1 42  ? 9.174  -6.911  -37.558 1.00 28.53 ? 197  LEU A N     1 
ATOM   262  C  CA    . LEU A 1 42  ? 9.976  -8.126  -37.680 1.00 25.29 ? 197  LEU A CA    1 
ATOM   263  C  C     . LEU A 1 42  ? 9.227  -9.218  -38.425 1.00 28.97 ? 197  LEU A C     1 
ATOM   264  O  O     . LEU A 1 42  ? 9.843  -9.999  -39.155 1.00 26.27 ? 197  LEU A O     1 
ATOM   265  C  CB    . LEU A 1 42  ? 10.450 -8.611  -36.298 1.00 22.38 ? 197  LEU A CB    1 
ATOM   266  C  CG    . LEU A 1 42  ? 11.628 -7.821  -35.740 1.00 21.24 ? 197  LEU A CG    1 
ATOM   267  C  CD1   . LEU A 1 42  ? 11.556 -7.994  -34.230 1.00 26.01 ? 197  LEU A CD1   1 
ATOM   268  C  CD2   . LEU A 1 42  ? 13.053 -8.230  -36.251 1.00 22.54 ? 197  LEU A CD2   1 
ATOM   269  N  N     . LYS A 1 43  ? 7.921  -9.324  -38.207 1.00 28.06 ? 198  LYS A N     1 
ATOM   270  C  CA    . LYS A 1 43  ? 7.144  -10.367 -38.856 1.00 31.25 ? 198  LYS A CA    1 
ATOM   271  C  C     . LYS A 1 43  ? 7.158  -10.237 -40.375 1.00 31.62 ? 198  LYS A C     1 
ATOM   272  O  O     . LYS A 1 43  ? 6.901  -11.230 -41.065 1.00 31.72 ? 198  LYS A O     1 
ATOM   273  C  CB    . LYS A 1 43  ? 5.715  -10.352 -38.324 1.00 35.38 ? 198  LYS A CB    1 
ATOM   274  C  CG    . LYS A 1 43  ? 5.594  -10.864 -36.882 1.00 35.35 ? 198  LYS A CG    1 
ATOM   275  C  CD    . LYS A 1 43  ? 4.200  -11.435 -36.622 1.00 40.37 ? 198  LYS A CD    1 
ATOM   276  C  CE    . LYS A 1 43  ? 4.168  -12.300 -35.373 1.00 41.38 ? 198  LYS A CE    1 
ATOM   277  N  NZ    . LYS A 1 43  ? 4.538  -13.742 -35.610 1.00 38.25 ? 198  LYS A NZ    1 
ATOM   278  N  N     . CYS A 1 44  ? 7.459  -9.046  -40.906 1.00 30.14 ? 199  CYS A N     1 
ATOM   279  C  CA    . CYS A 1 44  ? 7.579  -8.870  -42.359 1.00 30.92 ? 199  CYS A CA    1 
ATOM   280  C  C     . CYS A 1 44  ? 8.825  -9.513  -42.929 1.00 32.84 ? 199  CYS A C     1 
ATOM   281  O  O     . CYS A 1 44  ? 8.877  -9.769  -44.138 1.00 29.63 ? 199  CYS A O     1 
ATOM   282  C  CB    . CYS A 1 44  ? 7.615  -7.399  -42.736 1.00 33.21 ? 199  CYS A CB    1 
ATOM   283  S  SG    . CYS A 1 44  ? 6.121  -6.536  -42.270 1.00 42.12 ? 199  CYS A SG    1 
ATOM   284  N  N     . ASP A 1 45  ? 9.844  -9.739  -42.116 1.00 29.27 ? 200  ASP A N     1 
ATOM   285  C  CA    . ASP A 1 45  ? 11.059 -10.357 -42.607 1.00 25.11 ? 200  ASP A CA    1 
ATOM   286  C  C     . ASP A 1 45  ? 10.916 -11.870 -42.650 1.00 27.38 ? 200  ASP A C     1 
ATOM   287  O  O     . ASP A 1 45  ? 10.420 -12.494 -41.713 1.00 23.71 ? 200  ASP A O     1 
ATOM   288  C  CB    . ASP A 1 45  ? 12.236 -9.956  -41.726 1.00 25.53 ? 200  ASP A CB    1 
ATOM   289  C  CG    . ASP A 1 45  ? 13.538 -10.376 -42.327 1.00 35.49 ? 200  ASP A CG    1 
ATOM   290  O  OD1   . ASP A 1 45  ? 13.918 -11.542 -42.107 1.00 32.57 ? 200  ASP A OD1   1 
ATOM   291  O  OD2   . ASP A 1 45  ? 14.136 -9.569  -43.075 1.00 34.28 ? 200  ASP A OD2   1 
ATOM   292  N  N     . SER A 1 46  ? 11.361 -12.473 -43.750 1.00 24.20 ? 201  SER A N     1 
ATOM   293  C  CA    . SER A 1 46  ? 11.210 -13.916 -43.889 1.00 23.87 ? 201  SER A CA    1 
ATOM   294  C  C     . SER A 1 46  ? 11.827 -14.674 -42.723 1.00 25.33 ? 201  SER A C     1 
ATOM   295  O  O     . SER A 1 46  ? 11.329 -15.743 -42.359 1.00 27.47 ? 201  SER A O     1 
ATOM   296  C  CB    . SER A 1 46  ? 11.844 -14.373 -45.204 1.00 23.82 ? 201  SER A CB    1 
ATOM   297  O  OG    . SER A 1 46  ? 11.247 -13.634 -46.250 1.00 22.72 ? 201  SER A OG    1 
ATOM   298  N  N     . ALA A 1 47  ? 12.907 -14.151 -42.133 1.00 22.49 ? 202  ALA A N     1 
ATOM   299  C  CA    . ALA A 1 47  ? 13.592 -14.912 -41.091 1.00 25.57 ? 202  ALA A CA    1 
ATOM   300  C  C     . ALA A 1 47  ? 12.856 -14.843 -39.762 1.00 27.63 ? 202  ALA A C     1 
ATOM   301  O  O     . ALA A 1 47  ? 12.907 -15.800 -38.988 1.00 25.66 ? 202  ALA A O     1 
ATOM   302  C  CB    . ALA A 1 47  ? 15.015 -14.406 -40.897 1.00 27.98 ? 202  ALA A CB    1 
ATOM   303  N  N     . PHE A 1 48  ? 12.185 -13.725 -39.486 1.00 24.69 ? 203  PHE A N     1 
ATOM   304  C  CA    . PHE A 1 48  ? 11.551 -13.475 -38.193 1.00 22.33 ? 203  PHE A CA    1 
ATOM   305  C  C     . PHE A 1 48  ? 10.038 -13.531 -38.254 1.00 27.82 ? 203  PHE A C     1 
ATOM   306  O  O     . PHE A 1 48  ? 9.361  -13.041 -37.340 1.00 24.90 ? 203  PHE A O     1 
ATOM   307  C  CB    . PHE A 1 48  ? 12.067 -12.157 -37.636 1.00 22.09 ? 203  PHE A CB    1 
ATOM   308  C  CG    . PHE A 1 48  ? 13.547 -12.145 -37.491 1.00 21.73 ? 203  PHE A CG    1 
ATOM   309  C  CD1   . PHE A 1 48  ? 14.143 -13.032 -36.599 1.00 23.46 ? 203  PHE A CD1   1 
ATOM   310  C  CD2   . PHE A 1 48  ? 14.348 -11.272 -38.222 1.00 24.30 ? 203  PHE A CD2   1 
ATOM   311  C  CE1   . PHE A 1 48  ? 15.494 -13.070 -36.434 1.00 22.61 ? 203  PHE A CE1   1 
ATOM   312  C  CE2   . PHE A 1 48  ? 15.725 -11.295 -38.060 1.00 22.43 ? 203  PHE A CE2   1 
ATOM   313  C  CZ    . PHE A 1 48  ? 16.299 -12.197 -37.163 1.00 23.77 ? 203  PHE A CZ    1 
ATOM   314  N  N     . ARG A 1 49  ? 9.487  -14.159 -39.299 1.00 25.65 ? 204  ARG A N     1 
ATOM   315  C  CA    . ARG A 1 49  ? 8.044  -14.105 -39.502 1.00 28.76 ? 204  ARG A CA    1 
ATOM   316  C  C     . ARG A 1 49  ? 7.269  -14.684 -38.321 1.00 28.60 ? 204  ARG A C     1 
ATOM   317  O  O     . ARG A 1 49  ? 6.187  -14.184 -37.993 1.00 28.86 ? 204  ARG A O     1 
ATOM   318  C  CB    . ARG A 1 49  ? 7.651  -14.820 -40.804 1.00 31.99 ? 204  ARG A CB    1 
ATOM   319  C  CG    . ARG A 1 49  ? 6.171  -14.656 -41.113 1.00 35.88 ? 204  ARG A CG    1 
ATOM   320  C  CD    . ARG A 1 49  ? 5.947  -14.733 -42.580 1.00 39.48 ? 204  ARG A CD    1 
ATOM   321  N  NE    . ARG A 1 49  ? 6.610  -13.627 -43.243 1.00 38.10 ? 204  ARG A NE    1 
ATOM   322  C  CZ    . ARG A 1 49  ? 7.259  -13.783 -44.385 1.00 31.96 ? 204  ARG A CZ    1 
ATOM   323  N  NH1   . ARG A 1 49  ? 7.385  -14.977 -44.937 1.00 28.65 ? 204  ARG A NH1   1 
ATOM   324  N  NH2   . ARG A 1 49  ? 7.857  -12.740 -44.941 1.00 28.46 ? 204  ARG A NH2   1 
ATOM   325  N  N     . GLY A 1 50  ? 7.809  -15.712 -37.665 1.00 26.11 ? 205  GLY A N     1 
ATOM   326  C  CA    . GLY A 1 50  ? 7.097  -16.369 -36.581 1.00 30.23 ? 205  GLY A CA    1 
ATOM   327  C  C     . GLY A 1 50  ? 7.401  -15.866 -35.177 1.00 30.88 ? 205  GLY A C     1 
ATOM   328  O  O     . GLY A 1 50  ? 7.050  -16.532 -34.203 1.00 33.71 ? 205  GLY A O     1 
ATOM   329  N  N     . VAL A 1 51  ? 8.022  -14.691 -35.061 1.00 24.23 ? 206  VAL A N     1 
ATOM   330  C  CA    . VAL A 1 51  ? 8.370  -14.153 -33.747 1.00 23.32 ? 206  VAL A CA    1 
ATOM   331  C  C     . VAL A 1 51  ? 7.131  -13.926 -32.879 1.00 28.11 ? 206  VAL A C     1 
ATOM   332  O  O     . VAL A 1 51  ? 6.057  -13.551 -33.363 1.00 25.62 ? 206  VAL A O     1 
ATOM   333  C  CB    . VAL A 1 51  ? 9.197  -12.869 -33.937 1.00 26.79 ? 206  VAL A CB    1 
ATOM   334  C  CG1   . VAL A 1 51  ? 8.303  -11.665 -34.222 1.00 31.22 ? 206  VAL A CG1   1 
ATOM   335  C  CG2   . VAL A 1 51  ? 10.066 -12.641 -32.771 1.00 37.38 ? 206  VAL A CG2   1 
ATOM   336  N  N     . GLY A 1 52  ? 7.280  -14.178 -31.576 1.00 21.66 ? 207  GLY A N     1 
ATOM   337  C  CA    . GLY A 1 52  ? 6.206  -13.938 -30.626 1.00 25.78 ? 207  GLY A CA    1 
ATOM   338  C  C     . GLY A 1 52  ? 6.801  -13.362 -29.355 1.00 22.99 ? 207  GLY A C     1 
ATOM   339  O  O     . GLY A 1 52  ? 7.995  -13.440 -29.140 1.00 23.24 ? 207  GLY A O     1 
ATOM   340  N  N     . LEU A 1 53  ? 5.958  -12.760 -28.536 1.00 21.18 ? 208  LEU A N     1 
ATOM   341  C  CA    . LEU A 1 53  ? 6.429  -12.042 -27.352 1.00 20.27 ? 208  LEU A CA    1 
ATOM   342  C  C     . LEU A 1 53  ? 6.431  -12.974 -26.151 1.00 19.72 ? 208  LEU A C     1 
ATOM   343  O  O     . LEU A 1 53  ? 5.464  -13.701 -25.913 1.00 22.92 ? 208  LEU A O     1 
ATOM   344  C  CB    . LEU A 1 53  ? 5.455  -10.912 -27.038 1.00 19.85 ? 208  LEU A CB    1 
ATOM   345  C  CG    . LEU A 1 53  ? 5.787  -10.028 -25.834 1.00 22.41 ? 208  LEU A CG    1 
ATOM   346  C  CD1   . LEU A 1 53  ? 7.209  -9.465  -25.888 1.00 23.63 ? 208  LEU A CD1   1 
ATOM   347  C  CD2   . LEU A 1 53  ? 4.720  -8.921  -25.612 1.00 23.36 ? 208  LEU A CD2   1 
ATOM   348  N  N     . LEU A 1 54  ? 7.490  -12.901 -25.362 1.00 17.74 ? 209  LEU A N     1 
ATOM   349  C  CA    . LEU A 1 54  ? 7.534  -13.565 -24.058 1.00 18.57 ? 209  LEU A CA    1 
ATOM   350  C  C     . LEU A 1 54  ? 8.074  -12.556 -23.068 1.00 15.78 ? 209  LEU A C     1 
ATOM   351  O  O     . LEU A 1 54  ? 9.246  -12.159 -23.159 1.00 17.54 ? 209  LEU A O     1 
ATOM   352  C  CB    . LEU A 1 54  ? 8.432  -14.804 -24.135 1.00 19.34 ? 209  LEU A CB    1 
ATOM   353  C  CG    . LEU A 1 54  ? 8.807  -15.572 -22.857 1.00 27.99 ? 209  LEU A CG    1 
ATOM   354  C  CD1   . LEU A 1 54  ? 7.603  -15.905 -22.023 1.00 24.25 ? 209  LEU A CD1   1 
ATOM   355  C  CD2   . LEU A 1 54  ? 9.613  -16.854 -23.261 1.00 26.64 ? 209  LEU A CD2   1 
ATOM   356  N  N     . ASN A 1 55  ? 7.252  -12.166 -22.108 1.00 14.90 ? 210  ASN A N     1 
ATOM   357  C  CA    . ASN A 1 55  ? 7.667  -11.196 -21.100 1.00 14.69 ? 210  ASN A CA    1 
ATOM   358  C  C     . ASN A 1 55  ? 8.415  -11.908 -19.987 1.00 14.65 ? 210  ASN A C     1 
ATOM   359  O  O     . ASN A 1 55  ? 7.996  -12.968 -19.527 1.00 18.68 ? 210  ASN A O     1 
ATOM   360  C  CB    . ASN A 1 55  ? 6.431  -10.500 -20.554 1.00 15.17 ? 210  ASN A CB    1 
ATOM   361  C  CG    . ASN A 1 55  ? 5.776  -9.623  -21.604 1.00 17.14 ? 210  ASN A CG    1 
ATOM   362  O  OD1   . ASN A 1 55  ? 6.446  -9.045  -22.478 1.00 18.00 ? 210  ASN A OD1   1 
ATOM   363  N  ND2   . ASN A 1 55  ? 4.452  -9.509  -21.508 1.00 20.52 ? 210  ASN A ND2   1 
ATOM   364  N  N     . THR A 1 56  ? 9.538  -11.322 -19.567 1.00 12.58 ? 211  THR A N     1 
ATOM   365  C  CA    . THR A 1 56  ? 10.448 -11.980 -18.621 1.00 12.54 ? 211  THR A CA    1 
ATOM   366  C  C     . THR A 1 56  ? 11.023 -10.933 -17.674 1.00 13.23 ? 211  THR A C     1 
ATOM   367  O  O     . THR A 1 56  ? 10.742 -9.725  -17.790 1.00 13.20 ? 211  THR A O     1 
ATOM   368  C  CB    . THR A 1 56  ? 11.612 -12.654 -19.352 1.00 17.95 ? 211  THR A CB    1 
ATOM   369  O  OG1   . THR A 1 56  ? 12.341 -11.658 -20.074 1.00 20.81 ? 211  THR A OG1   1 
ATOM   370  C  CG2   . THR A 1 56  ? 11.119 -13.737 -20.343 1.00 22.07 ? 211  THR A CG2   1 
ATOM   371  N  N     . GLY A 1 57  ? 11.847 -11.411 -16.712 1.00 14.12 ? 212  GLY A N     1 
ATOM   372  C  CA    . GLY A 1 57  ? 12.565 -10.517 -15.835 1.00 12.81 ? 212  GLY A CA    1 
ATOM   373  C  C     . GLY A 1 57  ? 11.640 -9.904  -14.775 1.00 10.62 ? 212  GLY A C     1 
ATOM   374  O  O     . GLY A 1 57  ? 10.495 -10.276 -14.575 1.00 11.20 ? 212  GLY A O     1 
ATOM   375  N  N     . SER A 1 58  ? 12.258 -8.970  -14.004 1.00 10.98 ? 213  SER A N     1 
ATOM   376  C  CA    . SER A 1 58  ? 11.710 -8.614  -12.710 1.00 11.53 ? 213  SER A CA    1 
ATOM   377  C  C     . SER A 1 58  ? 10.367 -7.912  -12.804 1.00 12.42 ? 213  SER A C     1 
ATOM   378  O  O     . SER A 1 58  ? 9.560  -8.040  -11.890 1.00 12.74 ? 213  SER A O     1 
ATOM   379  C  CB    . SER A 1 58  ? 12.660 -7.779  -11.882 1.00 11.77 ? 213  SER A CB    1 
ATOM   380  O  OG    . SER A 1 58  ? 12.911 -6.536  -12.541 1.00 12.39 ? 213  SER A OG    1 
ATOM   381  N  N     . TYR A 1 59  ? 10.124 -7.116  -13.833 1.00 11.97 ? 214  TYR A N     1 
ATOM   382  C  CA    . TYR A 1 59  ? 8.823  -6.469  -13.909 1.00 11.93 ? 214  TYR A CA    1 
ATOM   383  C  C     . TYR A 1 59  ? 7.710  -7.511  -13.991 1.00 13.22 ? 214  TYR A C     1 
ATOM   384  O  O     . TYR A 1 59  ? 6.721  -7.408  -13.299 1.00 14.98 ? 214  TYR A O     1 
ATOM   385  C  CB    . TYR A 1 59  ? 8.802  -5.551  -15.136 1.00 12.94 ? 214  TYR A CB    1 
ATOM   386  C  CG    . TYR A 1 59  ? 7.481  -4.807  -15.242 1.00 12.62 ? 214  TYR A CG    1 
ATOM   387  C  CD1   . TYR A 1 59  ? 7.278  -3.599  -14.563 1.00 13.84 ? 214  TYR A CD1   1 
ATOM   388  C  CD2   . TYR A 1 59  ? 6.442  -5.325  -16.023 1.00 13.02 ? 214  TYR A CD2   1 
ATOM   389  C  CE1   . TYR A 1 59  ? 6.058  -2.930  -14.627 1.00 14.57 ? 214  TYR A CE1   1 
ATOM   390  C  CE2   . TYR A 1 59  ? 5.202  -4.630  -16.099 1.00 16.84 ? 214  TYR A CE2   1 
ATOM   391  C  CZ    . TYR A 1 59  ? 5.056  -3.440  -15.415 1.00 16.20 ? 214  TYR A CZ    1 
ATOM   392  O  OH    . TYR A 1 59  ? 3.838  -2.769  -15.532 1.00 19.33 ? 214  TYR A OH    1 
ATOM   393  N  N     . TYR A 1 60  ? 7.886  -8.547  -14.810 1.00 12.10 ? 215  TYR A N     1 
ATOM   394  C  CA    . TYR A 1 60  ? 6.837  -9.525  -15.022 1.00 14.06 ? 215  TYR A CA    1 
ATOM   395  C  C     . TYR A 1 60  ? 6.823  -10.592 -13.954 1.00 14.31 ? 215  TYR A C     1 
ATOM   396  O  O     . TYR A 1 60  ? 5.857  -11.353 -13.878 1.00 14.75 ? 215  TYR A O     1 
ATOM   397  C  CB    . TYR A 1 60  ? 6.955  -10.098 -16.455 1.00 13.90 ? 215  TYR A CB    1 
ATOM   398  C  CG    . TYR A 1 60  ? 6.785  -9.004  -17.464 1.00 14.92 ? 215  TYR A CG    1 
ATOM   399  C  CD1   . TYR A 1 60  ? 5.500  -8.510  -17.746 1.00 15.63 ? 215  TYR A CD1   1 
ATOM   400  C  CD2   . TYR A 1 60  ? 7.869  -8.438  -18.114 1.00 12.88 ? 215  TYR A CD2   1 
ATOM   401  C  CE1   . TYR A 1 60  ? 5.321  -7.493  -18.621 1.00 13.78 ? 215  TYR A CE1   1 
ATOM   402  C  CE2   . TYR A 1 60  ? 7.696  -7.411  -19.018 1.00 15.19 ? 215  TYR A CE2   1 
ATOM   403  C  CZ    . TYR A 1 60  ? 6.404  -6.949  -19.251 1.00 15.00 ? 215  TYR A CZ    1 
ATOM   404  O  OH    . TYR A 1 60  ? 6.236  -5.880  -20.151 1.00 18.81 ? 215  TYR A OH    1 
ATOM   405  N  N     . GLU A 1 61  ? 7.831  -10.594 -13.102 1.00 12.15 ? 216  GLU A N     1 
ATOM   406  C  CA    . GLU A 1 61  ? 7.847  -11.382 -11.872 1.00 14.39 ? 216  GLU A CA    1 
ATOM   407  C  C     . GLU A 1 61  ? 7.381  -10.586 -10.669 1.00 13.15 ? 216  GLU A C     1 
ATOM   408  O  O     . GLU A 1 61  ? 7.349  -11.137 -9.559  1.00 12.80 ? 216  GLU A O     1 
ATOM   409  C  CB    . GLU A 1 61  ? 9.273  -11.890 -11.572 1.00 14.75 ? 216  GLU A CB    1 
ATOM   410  C  CG    . GLU A 1 61  ? 9.847  -12.781 -12.701 1.00 16.46 ? 216  GLU A CG    1 
ATOM   411  C  CD    . GLU A 1 61  ? 11.365 -12.873 -12.631 1.00 26.91 ? 216  GLU A CD    1 
ATOM   412  O  OE1   . GLU A 1 61  ? 12.003 -11.996 -11.974 1.00 19.70 ? 216  GLU A OE1   1 
ATOM   413  O  OE2   . GLU A 1 61  ? 11.904 -13.799 -13.285 1.00 21.86 ? 216  GLU A OE2   1 
ATOM   414  N  N     . HIS A 1 62  ? 7.055  -9.299  -10.849 1.00 12.72 ? 217  HIS A N     1 
ATOM   415  C  CA    . HIS A 1 62  ? 6.618  -8.421  -9.752  1.00 14.37 ? 217  HIS A CA    1 
ATOM   416  C  C     . HIS A 1 62  ? 7.662  -8.312  -8.651  1.00 14.87 ? 217  HIS A C     1 
ATOM   417  O  O     . HIS A 1 62  ? 7.334  -8.210  -7.464  1.00 16.45 ? 217  HIS A O     1 
ATOM   418  C  CB    . HIS A 1 62  ? 5.263  -8.826  -9.172  1.00 15.64 ? 217  HIS A CB    1 
ATOM   419  C  CG    . HIS A 1 62  ? 4.263  -9.216  -10.206 1.00 15.52 ? 217  HIS A CG    1 
ATOM   420  N  ND1   . HIS A 1 62  ? 3.488  -8.290  -10.874 1.00 21.58 ? 217  HIS A ND1   1 
ATOM   421  C  CD2   . HIS A 1 62  ? 3.983  -10.419 -10.752 1.00 17.77 ? 217  HIS A CD2   1 
ATOM   422  C  CE1   . HIS A 1 62  ? 2.705  -8.928  -11.727 1.00 22.73 ? 217  HIS A CE1   1 
ATOM   423  N  NE2   . HIS A 1 62  ? 3.002  -10.213 -11.696 1.00 19.07 ? 217  HIS A NE2   1 
ATOM   424  N  N     . VAL A 1 63  ? 8.951  -8.314  -9.011  1.00 12.97 ? 218  VAL A N     1 
ATOM   425  C  CA    . VAL A 1 63  ? 10.001 -8.018  -8.046  1.00 13.32 ? 218  VAL A CA    1 
ATOM   426  C  C     . VAL A 1 63  ? 10.867 -6.869  -8.524  1.00 13.41 ? 218  VAL A C     1 
ATOM   427  O  O     . VAL A 1 63  ? 11.930 -6.633  -7.971  1.00 16.46 ? 218  VAL A O     1 
ATOM   428  C  CB    . VAL A 1 63  ? 10.845 -9.257  -7.673  1.00 13.16 ? 218  VAL A CB    1 
ATOM   429  C  CG1   . VAL A 1 63  ? 9.981  -10.310 -6.958  1.00 16.01 ? 218  VAL A CG1   1 
ATOM   430  C  CG2   . VAL A 1 63  ? 11.524 -9.877  -8.915  1.00 14.42 ? 218  VAL A CG2   1 
ATOM   431  N  N     . LYS A 1 64  ? 10.425 -6.131  -9.548  1.00 12.76 ? 219  LYS A N     1 
ATOM   432  C  CA    . LYS A 1 64  ? 11.103 -4.903  -9.917  1.00 13.36 ? 219  LYS A CA    1 
ATOM   433  C  C     . LYS A 1 64  ? 10.960 -3.919  -8.758  1.00 13.53 ? 219  LYS A C     1 
ATOM   434  O  O     . LYS A 1 64  ? 9.872  -3.781  -8.186  1.00 14.91 ? 219  LYS A O     1 
ATOM   435  C  CB    . LYS A 1 64  ? 10.446 -4.343  -11.199 1.00 13.43 ? 219  LYS A CB    1 
ATOM   436  C  CG    . LYS A 1 64  ? 11.071 -3.016  -11.656 1.00 13.79 ? 219  LYS A CG    1 
ATOM   437  C  CD    . LYS A 1 64  ? 12.363 -3.327  -12.458 1.00 13.42 ? 219  LYS A CD    1 
ATOM   438  C  CE    . LYS A 1 64  ? 13.183 -2.082  -12.811 1.00 15.77 ? 219  LYS A CE    1 
ATOM   439  N  NZ    . LYS A 1 64  ? 13.703 -1.300  -11.622 1.00 18.26 ? 219  LYS A NZ    1 
ATOM   440  N  N     . ILE A 1 65  ? 12.058 -3.217  -8.424  1.00 13.50 ? 220  ILE A N     1 
ATOM   441  C  CA    . ILE A 1 65  ? 12.049 -2.274  -7.296  1.00 14.23 ? 220  ILE A CA    1 
ATOM   442  C  C     . ILE A 1 65  ? 12.222 -0.847  -7.785  1.00 17.05 ? 220  ILE A C     1 
ATOM   443  O  O     . ILE A 1 65  ? 12.763 -0.591  -8.855  1.00 15.39 ? 220  ILE A O     1 
ATOM   444  C  CB    . ILE A 1 65  ? 13.054 -2.617  -6.190  1.00 14.62 ? 220  ILE A CB    1 
ATOM   445  C  CG1   . ILE A 1 65  ? 14.453 -2.676  -6.772  1.00 15.34 ? 220  ILE A CG1   1 
ATOM   446  C  CG2   . ILE A 1 65  ? 12.637 -3.940  -5.565  1.00 17.90 ? 220  ILE A CG2   1 
ATOM   447  C  CD1   . ILE A 1 65  ? 15.589 -2.821  -5.671  1.00 18.47 ? 220  ILE A CD1   1 
ATOM   448  N  N     . SER A 1 66  ? 11.708 0.087   -6.976  1.00 15.52 ? 221  SER A N     1 
ATOM   449  C  CA    . SER A 1 66  ? 11.935 1.538   -7.067  1.00 18.72 ? 221  SER A CA    1 
ATOM   450  C  C     . SER A 1 66  ? 11.161 2.225   -8.187  1.00 19.57 ? 221  SER A C     1 
ATOM   451  O  O     . SER A 1 66  ? 10.368 3.142   -7.937  1.00 22.71 ? 221  SER A O     1 
ATOM   452  C  CB    . SER A 1 66  ? 13.412 1.888   -7.141  1.00 19.87 ? 221  SER A CB    1 
ATOM   453  O  OG    . SER A 1 66  ? 14.083 1.369   -5.995  1.00 23.84 ? 221  SER A OG    1 
ATOM   454  N  N     . ALA A 1 67  ? 11.394 1.815   -9.422  1.00 18.05 ? 222  ALA A N     1 
ATOM   455  C  CA    . ALA A 1 67  ? 10.691 2.420   -10.546 1.00 17.73 ? 222  ALA A CA    1 
ATOM   456  C  C     . ALA A 1 67  ? 10.549 1.393   -11.642 1.00 17.57 ? 222  ALA A C     1 
ATOM   457  O  O     . ALA A 1 67  ? 11.405 0.515   -11.777 1.00 16.82 ? 222  ALA A O     1 
ATOM   458  C  CB    . ALA A 1 67  ? 11.446 3.616   -11.121 1.00 20.51 ? 222  ALA A CB    1 
ATOM   459  N  N     . PRO A 1 68  ? 9.498  1.476   -12.446 1.00 14.97 ? 223  PRO A N     1 
ATOM   460  C  CA    . PRO A 1 68  ? 9.340  0.534   -13.580 1.00 16.11 ? 223  PRO A CA    1 
ATOM   461  C  C     . PRO A 1 68  ? 10.088 1.066   -14.794 1.00 17.05 ? 223  PRO A C     1 
ATOM   462  O  O     . PRO A 1 68  ? 9.515  1.486   -15.810 1.00 17.99 ? 223  PRO A O     1 
ATOM   463  C  CB    . PRO A 1 68  ? 7.822  0.499   -13.786 1.00 17.23 ? 223  PRO A CB    1 
ATOM   464  C  CG    . PRO A 1 68  ? 7.384  1.939   -13.436 1.00 19.16 ? 223  PRO A CG    1 
ATOM   465  C  CD    . PRO A 1 68  ? 8.306  2.344   -12.283 1.00 15.92 ? 223  PRO A CD    1 
ATOM   466  N  N     . ASN A 1 69  ? 11.406 1.093   -14.679 1.00 16.29 ? 224  ASN A N     1 
ATOM   467  C  CA    . ASN A 1 69  ? 12.238 1.688   -15.721 1.00 17.85 ? 224  ASN A CA    1 
ATOM   468  C  C     . ASN A 1 69  ? 13.127 0.677   -16.430 1.00 17.62 ? 224  ASN A C     1 
ATOM   469  O  O     . ASN A 1 69  ? 14.074 1.078   -17.103 1.00 16.75 ? 224  ASN A O     1 
ATOM   470  C  CB    . ASN A 1 69  ? 13.079 2.837   -15.148 1.00 20.15 ? 224  ASN A CB    1 
ATOM   471  C  CG    . ASN A 1 69  ? 14.041 2.381   -14.106 1.00 23.88 ? 224  ASN A CG    1 
ATOM   472  O  OD1   . ASN A 1 69  ? 14.067 1.214   -13.665 1.00 20.56 ? 224  ASN A OD1   1 
ATOM   473  N  ND2   . ASN A 1 69  ? 14.900 3.320   -13.687 1.00 34.93 ? 224  ASN A ND2   1 
ATOM   474  N  N     . GLU A 1 70  ? 12.870 -0.615  -16.272 1.00 13.84 ? 225  GLU A N     1 
ATOM   475  C  CA    . GLU A 1 70  ? 13.691 -1.612  -16.972 1.00 13.84 ? 225  GLU A CA    1 
ATOM   476  C  C     . GLU A 1 70  ? 12.872 -2.868  -17.205 1.00 12.80 ? 225  GLU A C     1 
ATOM   477  O  O     . GLU A 1 70  ? 12.385 -3.505  -16.250 1.00 13.06 ? 225  GLU A O     1 
ATOM   478  C  CB    . GLU A 1 70  ? 14.963 -1.926  -16.213 1.00 14.44 ? 225  GLU A CB    1 
ATOM   479  C  CG    . GLU A 1 70  ? 16.049 -2.482  -17.159 1.00 16.62 ? 225  GLU A CG    1 
ATOM   480  C  CD    . GLU A 1 70  ? 16.127 -4.005  -17.197 1.00 16.01 ? 225  GLU A CD    1 
ATOM   481  O  OE1   . GLU A 1 70  ? 15.351 -4.644  -16.510 1.00 13.79 ? 225  GLU A OE1   1 
ATOM   482  O  OE2   . GLU A 1 70  ? 17.029 -4.521  -17.895 1.00 15.69 ? 225  GLU A OE2   1 
ATOM   483  N  N     . PHE A 1 71  ? 12.684 -3.198  -18.471 1.00 13.30 ? 226  PHE A N     1 
ATOM   484  C  CA    . PHE A 1 71  ? 11.817 -4.293  -18.873 1.00 12.56 ? 226  PHE A CA    1 
ATOM   485  C  C     . PHE A 1 71  ? 12.581 -5.246  -19.770 1.00 13.98 ? 226  PHE A C     1 
ATOM   486  O  O     . PHE A 1 71  ? 13.440 -4.818  -20.541 1.00 15.53 ? 226  PHE A O     1 
ATOM   487  C  CB    . PHE A 1 71  ? 10.688 -3.741  -19.727 1.00 14.03 ? 226  PHE A CB    1 
ATOM   488  C  CG    . PHE A 1 71  ? 9.700  -2.907  -18.998 1.00 15.00 ? 226  PHE A CG    1 
ATOM   489  C  CD1   . PHE A 1 71  ? 9.999  -1.604  -18.626 1.00 14.25 ? 226  PHE A CD1   1 
ATOM   490  C  CD2   . PHE A 1 71  ? 8.434  -3.426  -18.717 1.00 18.05 ? 226  PHE A CD2   1 
ATOM   491  C  CE1   . PHE A 1 71  ? 9.023  -0.795  -17.961 1.00 14.29 ? 226  PHE A CE1   1 
ATOM   492  C  CE2   . PHE A 1 71  ? 7.458  -2.618  -18.055 1.00 17.86 ? 226  PHE A CE2   1 
ATOM   493  C  CZ    . PHE A 1 71  ? 7.812  -1.307  -17.657 1.00 14.78 ? 226  PHE A CZ    1 
ATOM   494  N  N     . ASP A 1 72  ? 12.284 -6.537  -19.651 1.00 13.31 ? 227  ASP A N     1 
ATOM   495  C  CA    . ASP A 1 72  ? 13.009 -7.597  -20.358 1.00 12.19 ? 227  ASP A CA    1 
ATOM   496  C  C     . ASP A 1 72  ? 12.028 -8.420  -21.133 1.00 13.99 ? 227  ASP A C     1 
ATOM   497  O  O     . ASP A 1 72  ? 11.077 -8.960  -20.567 1.00 14.33 ? 227  ASP A O     1 
ATOM   498  C  CB    . ASP A 1 72  ? 13.737 -8.465  -19.359 1.00 13.00 ? 227  ASP A CB    1 
ATOM   499  C  CG    . ASP A 1 72  ? 14.657 -7.673  -18.535 1.00 13.19 ? 227  ASP A CG    1 
ATOM   500  O  OD1   . ASP A 1 72  ? 15.722 -7.228  -19.053 1.00 13.80 ? 227  ASP A OD1   1 
ATOM   501  O  OD2   . ASP A 1 72  ? 14.348 -7.474  -17.348 1.00 13.50 ? 227  ASP A OD2   1 
ATOM   502  N  N     . VAL A 1 73  ? 12.203 -8.474  -22.445 1.00 14.52 ? 228  VAL A N     1 
ATOM   503  C  CA    . VAL A 1 73  ? 11.271 -9.190  -23.296 1.00 14.85 ? 228  VAL A CA    1 
ATOM   504  C  C     . VAL A 1 73  ? 12.033 -10.099 -24.225 1.00 13.36 ? 228  VAL A C     1 
ATOM   505  O  O     . VAL A 1 73  ? 13.125 -9.749  -24.676 1.00 15.78 ? 228  VAL A O     1 
ATOM   506  C  CB    . VAL A 1 73  ? 10.314 -8.289  -24.103 1.00 16.77 ? 228  VAL A CB    1 
ATOM   507  C  CG1   . VAL A 1 73  ? 9.543  -7.314  -23.173 1.00 19.28 ? 228  VAL A CG1   1 
ATOM   508  C  CG2   . VAL A 1 73  ? 11.065 -7.563  -25.196 1.00 21.20 ? 228  VAL A CG2   1 
ATOM   509  N  N     . MET A 1 74  ? 11.478 -11.254 -24.494 1.00 13.92 ? 229  MET A N     1 
ATOM   510  C  CA    . MET A 1 74  ? 12.066 -12.187 -25.446 1.00 15.21 ? 229  MET A CA    1 
ATOM   511  C  C     . MET A 1 74  ? 11.177 -12.147 -26.669 1.00 17.11 ? 229  MET A C     1 
ATOM   512  O  O     . MET A 1 74  ? 9.941  -12.131 -26.554 1.00 18.98 ? 229  MET A O     1 
ATOM   513  C  CB    . MET A 1 74  ? 12.070 -13.581 -24.852 1.00 18.62 ? 229  MET A CB    1 
ATOM   514  C  CG    . MET A 1 74  ? 13.313 -13.853 -24.020 1.00 23.53 ? 229  MET A CG    1 
ATOM   515  S  SD    . MET A 1 74  ? 13.290 -15.607 -23.514 1.00 31.28 ? 229  MET A SD    1 
ATOM   516  C  CE    . MET A 1 74  ? 14.954 -15.800 -22.793 1.00 23.22 ? 229  MET A CE    1 
ATOM   517  N  N     . PHE A 1 75  ? 11.798 -12.055 -27.833 1.00 17.88 ? 230  PHE A N     1 
ATOM   518  C  CA    . PHE A 1 75  ? 11.093 -12.246 -29.093 1.00 18.63 ? 230  PHE A CA    1 
ATOM   519  C  C     . PHE A 1 75  ? 11.451 -13.658 -29.522 1.00 17.98 ? 230  PHE A C     1 
ATOM   520  O  O     . PHE A 1 75  ? 12.539 -13.913 -30.054 1.00 20.08 ? 230  PHE A O     1 
ATOM   521  C  CB    . PHE A 1 75  ? 11.542 -11.219 -30.115 1.00 20.64 ? 230  PHE A CB    1 
ATOM   522  C  CG    . PHE A 1 75  ? 10.945 -9.853  -29.943 1.00 19.40 ? 230  PHE A CG    1 
ATOM   523  C  CD1   . PHE A 1 75  ? 10.167 -9.511  -28.830 1.00 22.01 ? 230  PHE A CD1   1 
ATOM   524  C  CD2   . PHE A 1 75  ? 11.169 -8.896  -30.899 1.00 20.75 ? 230  PHE A CD2   1 
ATOM   525  C  CE1   . PHE A 1 75  ? 9.628  -8.238  -28.696 1.00 20.59 ? 230  PHE A CE1   1 
ATOM   526  C  CE2   . PHE A 1 75  ? 10.634 -7.635  -30.788 1.00 21.73 ? 230  PHE A CE2   1 
ATOM   527  C  CZ    . PHE A 1 75  ? 9.874  -7.287  -29.667 1.00 24.26 ? 230  PHE A CZ    1 
ATOM   528  N  N     . LYS A 1 76  ? 10.542 -14.587 -29.249 1.00 17.54 ? 231  LYS A N     1 
ATOM   529  C  CA    . LYS A 1 76  ? 10.831 -16.001 -29.355 1.00 24.96 ? 231  LYS A CA    1 
ATOM   530  C  C     . LYS A 1 76  ? 10.485 -16.477 -30.758 1.00 25.26 ? 231  LYS A C     1 
ATOM   531  O  O     . LYS A 1 76  ? 9.579  -15.947 -31.410 1.00 23.41 ? 231  LYS A O     1 
ATOM   532  C  CB    . LYS A 1 76  ? 10.040 -16.776 -28.292 1.00 28.05 ? 231  LYS A CB    1 
ATOM   533  C  CG    . LYS A 1 76  ? 8.531  -16.852 -28.550 1.00 30.65 ? 231  LYS A CG    1 
ATOM   534  C  CD    . LYS A 1 76  ? 7.816  -17.741 -27.534 1.00 33.53 ? 231  LYS A CD    1 
ATOM   535  C  CE    . LYS A 1 76  ? 6.651  -16.999 -26.893 1.00 39.19 ? 231  LYS A CE    1 
ATOM   536  N  NZ    . LYS A 1 76  ? 5.605  -16.627 -27.882 1.00 45.18 ? 231  LYS A NZ    1 
ATOM   537  N  N     . LEU A 1 77  ? 11.239 -17.458 -31.231 1.00 22.15 ? 232  LEU A N     1 
ATOM   538  C  CA    . LEU A 1 77  ? 11.076 -17.944 -32.596 1.00 23.14 ? 232  LEU A CA    1 
ATOM   539  C  C     . LEU A 1 77  ? 11.099 -19.460 -32.535 1.00 23.11 ? 232  LEU A C     1 
ATOM   540  O  O     . LEU A 1 77  ? 12.121 -20.047 -32.176 1.00 24.84 ? 232  LEU A O     1 
ATOM   541  C  CB    . LEU A 1 77  ? 12.236 -17.442 -33.449 1.00 29.33 ? 232  LEU A CB    1 
ATOM   542  C  CG    . LEU A 1 77  ? 12.125 -17.535 -34.957 1.00 33.94 ? 232  LEU A CG    1 
ATOM   543  C  CD1   . LEU A 1 77  ? 10.996 -16.624 -35.434 1.00 33.02 ? 232  LEU A CD1   1 
ATOM   544  C  CD2   . LEU A 1 77  ? 13.463 -17.070 -35.483 1.00 31.21 ? 232  LEU A CD2   1 
ATOM   545  N  N     . GLU A 1 78  ? 9.988  -20.092 -32.872 1.00 25.68 ? 233  GLU A N     1 
ATOM   546  C  CA    . GLU A 1 78  ? 9.980  -21.545 -32.903 1.00 31.13 ? 233  GLU A CA    1 
ATOM   547  C  C     . GLU A 1 78  ? 10.880 -22.040 -34.026 1.00 38.64 ? 233  GLU A C     1 
ATOM   548  O  O     . GLU A 1 78  ? 10.750 -21.616 -35.178 1.00 36.40 ? 233  GLU A O     1 
ATOM   549  C  CB    . GLU A 1 78  ? 8.564  -22.083 -33.061 1.00 37.12 ? 233  GLU A CB    1 
ATOM   550  C  CG    . GLU A 1 78  ? 8.465  -23.606 -33.298 1.00 50.31 ? 233  GLU A CG    1 
ATOM   551  C  CD    . GLU A 1 78  ? 9.012  -24.483 -32.177 1.00 54.89 ? 233  GLU A CD    1 
ATOM   552  O  OE1   . GLU A 1 78  ? 10.145 -24.257 -31.723 1.00 54.70 ? 233  GLU A OE1   1 
ATOM   553  O  OE2   . GLU A 1 78  ? 8.325  -25.452 -31.790 1.00 56.97 ? 233  GLU A OE2   1 
ATOM   554  N  N     . VAL A 1 79  ? 11.815 -22.912 -33.680 1.00 37.50 ? 234  VAL A N     1 
ATOM   555  C  CA    . VAL A 1 79  ? 12.694 -23.516 -34.669 1.00 41.32 ? 234  VAL A CA    1 
ATOM   556  C  C     . VAL A 1 79  ? 12.569 -25.024 -34.522 1.00 46.46 ? 234  VAL A C     1 
ATOM   557  O  O     . VAL A 1 79  ? 13.033 -25.600 -33.523 1.00 46.80 ? 234  VAL A O     1 
ATOM   558  C  CB    . VAL A 1 79  ? 14.140 -23.041 -34.505 1.00 37.79 ? 234  VAL A CB    1 
ATOM   559  C  CG1   . VAL A 1 79  ? 15.041 -23.872 -35.371 1.00 44.56 ? 234  VAL A CG1   1 
ATOM   560  C  CG2   . VAL A 1 79  ? 14.258 -21.582 -34.887 1.00 36.08 ? 234  VAL A CG2   1 
ATOM   561  N  N     . PRO A 1 80  ? 11.939 -25.696 -35.473 1.00 44.40 ? 235  PRO A N     1 
ATOM   562  C  CA    . PRO A 1 80  ? 11.748 -27.141 -35.347 1.00 46.38 ? 235  PRO A CA    1 
ATOM   563  C  C     . PRO A 1 80  ? 13.055 -27.883 -35.562 1.00 40.01 ? 235  PRO A C     1 
ATOM   564  O  O     . PRO A 1 80  ? 13.997 -27.377 -36.173 1.00 46.59 ? 235  PRO A O     1 
ATOM   565  C  CB    . PRO A 1 80  ? 10.748 -27.462 -36.462 1.00 53.43 ? 235  PRO A CB    1 
ATOM   566  C  CG    . PRO A 1 80  ? 10.074 -26.129 -36.773 1.00 50.98 ? 235  PRO A CG    1 
ATOM   567  C  CD    . PRO A 1 80  ? 11.183 -25.131 -36.601 1.00 45.26 ? 235  PRO A CD    1 
ATOM   568  N  N     . ARG A 1 81  ? 13.106 -29.086 -34.995 1.00 39.43 ? 236  ARG A N     1 
ATOM   569  C  CA    . ARG A 1 81  ? 14.157 -30.056 -35.261 1.00 43.76 ? 236  ARG A CA    1 
ATOM   570  C  C     . ARG A 1 81  ? 15.546 -29.444 -35.092 1.00 42.66 ? 236  ARG A C     1 
ATOM   571  O  O     . ARG A 1 81  ? 16.337 -29.375 -36.032 1.00 48.35 ? 236  ARG A O     1 
ATOM   572  C  CB    . ARG A 1 81  ? 13.991 -30.672 -36.656 1.00 46.25 ? 236  ARG A CB    1 
ATOM   573  N  N     . ILE A 1 82  ? 15.841 -28.992 -33.871 1.00 37.82 ? 237  ILE A N     1 
ATOM   574  C  CA    . ILE A 1 82  ? 17.193 -28.535 -33.571 1.00 39.06 ? 237  ILE A CA    1 
ATOM   575  C  C     . ILE A 1 82  ? 17.983 -29.675 -32.940 1.00 36.01 ? 237  ILE A C     1 
ATOM   576  O  O     . ILE A 1 82  ? 17.458 -30.497 -32.185 1.00 38.15 ? 237  ILE A O     1 
ATOM   577  C  CB    . ILE A 1 82  ? 17.271 -27.242 -32.724 1.00 38.77 ? 237  ILE A CB    1 
ATOM   578  C  CG1   . ILE A 1 82  ? 17.087 -27.528 -31.253 1.00 47.29 ? 237  ILE A CG1   1 
ATOM   579  C  CG2   . ILE A 1 82  ? 16.183 -26.269 -33.121 1.00 44.32 ? 237  ILE A CG2   1 
ATOM   580  C  CD1   . ILE A 1 82  ? 17.024 -26.274 -30.472 1.00 43.10 ? 237  ILE A CD1   1 
ATOM   581  N  N     . GLN A 1 83  ? 19.261 -29.724 -33.260 1.00 33.28 ? 238  GLN A N     1 
ATOM   582  C  CA    . GLN A 1 83  ? 20.201 -30.616 -32.618 1.00 34.73 ? 238  GLN A CA    1 
ATOM   583  C  C     . GLN A 1 83  ? 21.253 -29.733 -31.967 1.00 30.54 ? 238  GLN A C     1 
ATOM   584  O  O     . GLN A 1 83  ? 21.787 -28.826 -32.617 1.00 31.78 ? 238  GLN A O     1 
ATOM   585  C  CB    . GLN A 1 83  ? 20.841 -31.501 -33.683 1.00 39.28 ? 238  GLN A CB    1 
ATOM   586  C  CG    . GLN A 1 83  ? 19.836 -31.996 -34.708 1.00 53.38 ? 238  GLN A CG    1 
ATOM   587  C  CD    . GLN A 1 83  ? 20.127 -33.401 -35.181 1.00 69.32 ? 238  GLN A CD    1 
ATOM   588  O  OE1   . GLN A 1 83  ? 21.099 -34.024 -34.743 1.00 64.45 ? 238  GLN A OE1   1 
ATOM   589  N  NE2   . GLN A 1 83  ? 19.287 -33.911 -36.087 1.00 71.79 ? 238  GLN A NE2   1 
ATOM   590  N  N     . LEU A 1 84  ? 21.528 -29.970 -30.685 1.00 25.56 ? 239  LEU A N     1 
ATOM   591  C  CA    . LEU A 1 84  ? 22.459 -29.146 -29.932 1.00 28.38 ? 239  LEU A CA    1 
ATOM   592  C  C     . LEU A 1 84  ? 23.782 -29.859 -29.760 1.00 26.53 ? 239  LEU A C     1 
ATOM   593  O  O     . LEU A 1 84  ? 23.818 -31.071 -29.561 1.00 32.93 ? 239  LEU A O     1 
ATOM   594  C  CB    . LEU A 1 84  ? 21.922 -28.869 -28.530 1.00 26.61 ? 239  LEU A CB    1 
ATOM   595  C  CG    . LEU A 1 84  ? 20.649 -28.035 -28.554 1.00 30.35 ? 239  LEU A CG    1 
ATOM   596  C  CD1   . LEU A 1 84  ? 20.258 -27.850 -27.133 1.00 31.27 ? 239  LEU A CD1   1 
ATOM   597  C  CD2   . LEU A 1 84  ? 20.918 -26.699 -29.201 1.00 30.24 ? 239  LEU A CD2   1 
ATOM   598  N  N     . GLU A 1 85  ? 24.851 -29.086 -29.758 1.00 24.97 ? 240  GLU A N     1 
ATOM   599  C  CA    . GLU A 1 85  ? 26.186 -29.589 -29.486 1.00 27.44 ? 240  GLU A CA    1 
ATOM   600  C  C     . GLU A 1 85  ? 26.791 -28.661 -28.446 1.00 26.20 ? 240  GLU A C     1 
ATOM   601  O  O     . GLU A 1 85  ? 26.997 -27.472 -28.718 1.00 24.27 ? 240  GLU A O     1 
ATOM   602  C  CB    . GLU A 1 85  ? 27.025 -29.574 -30.766 1.00 34.91 ? 240  GLU A CB    1 
ATOM   603  C  CG    . GLU A 1 85  ? 27.037 -30.888 -31.530 1.00 53.25 ? 240  GLU A CG    1 
ATOM   604  C  CD    . GLU A 1 85  ? 28.024 -30.881 -32.693 1.00 73.46 ? 240  GLU A CD    1 
ATOM   605  O  OE1   . GLU A 1 85  ? 29.148 -30.344 -32.533 1.00 73.31 ? 240  GLU A OE1   1 
ATOM   606  O  OE2   . GLU A 1 85  ? 27.668 -31.423 -33.767 1.00 70.20 ? 240  GLU A OE2   1 
ATOM   607  N  N     . GLU A 1 86  ? 27.087 -29.202 -27.267 1.00 24.59 ? 241  GLU A N     1 
ATOM   608  C  CA    . GLU A 1 86  ? 27.664 -28.398 -26.211 1.00 25.09 ? 241  GLU A CA    1 
ATOM   609  C  C     . GLU A 1 86  ? 29.038 -27.901 -26.623 1.00 30.43 ? 241  GLU A C     1 
ATOM   610  O  O     . GLU A 1 86  ? 29.831 -28.628 -27.240 1.00 29.93 ? 241  GLU A O     1 
ATOM   611  C  CB    . GLU A 1 86  ? 27.756 -29.215 -24.917 1.00 28.31 ? 241  GLU A CB    1 
ATOM   612  C  CG    . GLU A 1 86  ? 28.341 -28.467 -23.761 1.00 27.17 ? 241  GLU A CG    1 
ATOM   613  C  CD    . GLU A 1 86  ? 28.484 -29.345 -22.518 1.00 28.23 ? 241  GLU A CD    1 
ATOM   614  O  OE1   . GLU A 1 86  ? 28.136 -30.547 -22.566 1.00 40.70 ? 241  GLU A OE1   1 
ATOM   615  O  OE2   . GLU A 1 86  ? 28.988 -28.850 -21.504 1.00 24.40 ? 241  GLU A OE2   1 
ATOM   616  N  N     . TYR A 1 87  ? 29.311 -26.640 -26.337 1.00 24.15 ? 242  TYR A N     1 
ATOM   617  C  CA    . TYR A 1 87  ? 30.594 -26.048 -26.653 1.00 26.07 ? 242  TYR A CA    1 
ATOM   618  C  C     . TYR A 1 87  ? 31.534 -26.201 -25.466 1.00 30.64 ? 242  TYR A C     1 
ATOM   619  O  O     . TYR A 1 87  ? 31.260 -25.686 -24.382 1.00 24.91 ? 242  TYR A O     1 
ATOM   620  C  CB    . TYR A 1 87  ? 30.424 -24.574 -27.004 1.00 26.03 ? 242  TYR A CB    1 
ATOM   621  C  CG    . TYR A 1 87  ? 31.755 -23.901 -27.161 1.00 28.08 ? 242  TYR A CG    1 
ATOM   622  C  CD1   . TYR A 1 87  ? 32.588 -24.213 -28.246 1.00 33.50 ? 242  TYR A CD1   1 
ATOM   623  C  CD2   . TYR A 1 87  ? 32.197 -22.976 -26.235 1.00 28.77 ? 242  TYR A CD2   1 
ATOM   624  C  CE1   . TYR A 1 87  ? 33.820 -23.617 -28.385 1.00 32.00 ? 242  TYR A CE1   1 
ATOM   625  C  CE2   . TYR A 1 87  ? 33.446 -22.364 -26.379 1.00 32.63 ? 242  TYR A CE2   1 
ATOM   626  C  CZ    . TYR A 1 87  ? 34.245 -22.695 -27.459 1.00 33.36 ? 242  TYR A CZ    1 
ATOM   627  O  OH    . TYR A 1 87  ? 35.480 -22.096 -27.628 1.00 37.45 ? 242  TYR A OH    1 
ATOM   628  N  N     . SER A 1 88  ? 32.629 -26.933 -25.662 1.00 25.83 ? 243  SER A N     1 
ATOM   629  C  CA    . SER A 1 88  ? 33.774 -26.920 -24.737 1.00 32.29 ? 243  SER A CA    1 
ATOM   630  C  C     . SER A 1 88  ? 33.380 -27.202 -23.283 1.00 31.51 ? 243  SER A C     1 
ATOM   631  O  O     . SER A 1 88  ? 33.844 -26.534 -22.358 1.00 33.59 ? 243  SER A O     1 
ATOM   632  C  CB    . SER A 1 88  ? 34.530 -25.598 -24.830 1.00 33.24 ? 243  SER A CB    1 
ATOM   633  O  OG    . SER A 1 88  ? 35.564 -25.543 -23.859 1.00 40.82 ? 243  SER A OG    1 
ATOM   634  N  N     . ASN A 1 89  ? 32.542 -28.213 -23.076 1.00 29.03 ? 244  ASN A N     1 
ATOM   635  C  CA    . ASN A 1 89  ? 32.016 -28.521 -21.740 1.00 32.97 ? 244  ASN A CA    1 
ATOM   636  C  C     . ASN A 1 89  ? 31.624 -27.304 -20.881 1.00 34.33 ? 244  ASN A C     1 
ATOM   637  O  O     . ASN A 1 89  ? 31.837 -27.297 -19.659 1.00 28.06 ? 244  ASN A O     1 
ATOM   638  C  CB    . ASN A 1 89  ? 32.952 -29.472 -20.980 1.00 39.77 ? 244  ASN A CB    1 
ATOM   639  C  CG    . ASN A 1 89  ? 33.129 -30.802 -21.692 1.00 42.43 ? 244  ASN A CG    1 
ATOM   640  O  OD1   . ASN A 1 89  ? 32.202 -31.612 -21.752 1.00 46.14 ? 244  ASN A OD1   1 
ATOM   641  N  ND2   . ASN A 1 89  ? 34.332 -31.040 -22.232 1.00 42.99 ? 244  ASN A ND2   1 
ATOM   642  N  N     . THR A 1 90  ? 31.037 -26.271 -21.496 1.00 29.57 ? 245  THR A N     1 
ATOM   643  C  CA    . THR A 1 90  ? 30.641 -25.081 -20.741 1.00 23.56 ? 245  THR A CA    1 
ATOM   644  C  C     . THR A 1 90  ? 29.295 -25.244 -20.047 1.00 21.92 ? 245  THR A C     1 
ATOM   645  O  O     . THR A 1 90  ? 28.939 -24.373 -19.238 1.00 23.54 ? 245  THR A O     1 
ATOM   646  C  CB    . THR A 1 90  ? 30.505 -23.872 -21.660 1.00 19.93 ? 245  THR A CB    1 
ATOM   647  O  OG1   . THR A 1 90  ? 29.557 -24.186 -22.692 1.00 22.67 ? 245  THR A OG1   1 
ATOM   648  C  CG2   . THR A 1 90  ? 31.849 -23.476 -22.253 1.00 26.48 ? 245  THR A CG2   1 
ATOM   649  N  N     . ARG A 1 91  ? 28.555 -26.291 -20.393 1.00 20.05 ? 246  ARG A N     1 
ATOM   650  C  CA    . ARG A 1 91  ? 27.273 -26.705 -19.829 1.00 18.49 ? 246  ARG A CA    1 
ATOM   651  C  C     . ARG A 1 91  ? 26.123 -25.807 -20.275 1.00 18.32 ? 246  ARG A C     1 
ATOM   652  O  O     . ARG A 1 91  ? 24.993 -26.293 -20.396 1.00 19.87 ? 246  ARG A O     1 
ATOM   653  C  CB    . ARG A 1 91  ? 27.328 -26.795 -18.296 1.00 19.09 ? 246  ARG A CB    1 
ATOM   654  C  CG    . ARG A 1 91  ? 28.361 -27.805 -17.775 1.00 23.30 ? 246  ARG A CG    1 
ATOM   655  C  CD    . ARG A 1 91  ? 27.997 -29.194 -18.219 1.00 28.40 ? 246  ARG A CD    1 
ATOM   656  N  NE    . ARG A 1 91  ? 28.862 -30.219 -17.642 1.00 35.77 ? 246  ARG A NE    1 
ATOM   657  C  CZ    . ARG A 1 91  ? 29.870 -30.809 -18.277 1.00 39.97 ? 246  ARG A CZ    1 
ATOM   658  N  NH1   . ARG A 1 91  ? 30.128 -30.561 -19.552 1.00 39.27 ? 246  ARG A NH1   1 
ATOM   659  N  NH2   . ARG A 1 91  ? 30.619 -31.692 -17.623 1.00 35.87 ? 246  ARG A NH2   1 
ATOM   660  N  N     . ALA A 1 92  ? 26.409 -24.529 -20.559 1.00 17.42 ? 247  ALA A N     1 
ATOM   661  C  CA    . ALA A 1 92  ? 25.340 -23.595 -20.917 1.00 16.64 ? 247  ALA A CA    1 
ATOM   662  C  C     . ALA A 1 92  ? 25.398 -23.077 -22.349 1.00 18.91 ? 247  ALA A C     1 
ATOM   663  O  O     . ALA A 1 92  ? 24.421 -22.467 -22.803 1.00 18.35 ? 247  ALA A O     1 
ATOM   664  C  CB    . ALA A 1 92  ? 25.320 -22.391 -19.956 1.00 19.89 ? 247  ALA A CB    1 
ATOM   665  N  N     . TYR A 1 93  ? 26.511 -23.261 -23.074 1.00 17.84 ? 248  TYR A N     1 
ATOM   666  C  CA    . TYR A 1 93  ? 26.660 -22.707 -24.418 1.00 16.89 ? 248  TYR A CA    1 
ATOM   667  C  C     . TYR A 1 93  ? 26.691 -23.827 -25.445 1.00 18.59 ? 248  TYR A C     1 
ATOM   668  O  O     . TYR A 1 93  ? 27.303 -24.867 -25.207 1.00 20.13 ? 248  TYR A O     1 
ATOM   669  C  CB    . TYR A 1 93  ? 27.906 -21.850 -24.547 1.00 18.00 ? 248  TYR A CB    1 
ATOM   670  C  CG    . TYR A 1 93  ? 27.888 -20.616 -23.652 1.00 19.71 ? 248  TYR A CG    1 
ATOM   671  C  CD1   . TYR A 1 93  ? 28.336 -20.689 -22.337 1.00 20.81 ? 248  TYR A CD1   1 
ATOM   672  C  CD2   . TYR A 1 93  ? 27.336 -19.393 -24.126 1.00 19.47 ? 248  TYR A CD2   1 
ATOM   673  C  CE1   . TYR A 1 93  ? 28.296 -19.581 -21.520 1.00 22.26 ? 248  TYR A CE1   1 
ATOM   674  C  CE2   . TYR A 1 93  ? 27.303 -18.296 -23.319 1.00 20.47 ? 248  TYR A CE2   1 
ATOM   675  C  CZ    . TYR A 1 93  ? 27.777 -18.405 -22.011 1.00 24.97 ? 248  TYR A CZ    1 
ATOM   676  O  OH    . TYR A 1 93  ? 27.745 -17.326 -21.173 1.00 26.46 ? 248  TYR A OH    1 
ATOM   677  N  N     . TYR A 1 94  ? 25.999 -23.613 -26.574 1.00 18.03 ? 249  TYR A N     1 
ATOM   678  C  CA    . TYR A 1 94  ? 25.792 -24.667 -27.551 1.00 18.66 ? 249  TYR A CA    1 
ATOM   679  C  C     . TYR A 1 94  ? 25.895 -24.128 -28.964 1.00 22.01 ? 249  TYR A C     1 
ATOM   680  O  O     . TYR A 1 94  ? 25.602 -22.958 -29.247 1.00 21.24 ? 249  TYR A O     1 
ATOM   681  C  CB    . TYR A 1 94  ? 24.389 -25.263 -27.414 1.00 20.36 ? 249  TYR A CB    1 
ATOM   682  C  CG    . TYR A 1 94  ? 24.212 -25.971 -26.123 1.00 21.14 ? 249  TYR A CG    1 
ATOM   683  C  CD1   . TYR A 1 94  ? 23.917 -25.261 -24.956 1.00 19.46 ? 249  TYR A CD1   1 
ATOM   684  C  CD2   . TYR A 1 94  ? 24.341 -27.331 -26.049 1.00 23.27 ? 249  TYR A CD2   1 
ATOM   685  C  CE1   . TYR A 1 94  ? 23.769 -25.909 -23.769 1.00 20.92 ? 249  TYR A CE1   1 
ATOM   686  C  CE2   . TYR A 1 94  ? 24.195 -28.016 -24.845 1.00 23.03 ? 249  TYR A CE2   1 
ATOM   687  C  CZ    . TYR A 1 94  ? 23.915 -27.264 -23.704 1.00 23.44 ? 249  TYR A CZ    1 
ATOM   688  O  OH    . TYR A 1 94  ? 23.762 -27.900 -22.509 1.00 25.41 ? 249  TYR A OH    1 
ATOM   689  N  N     . PHE A 1 95  ? 26.308 -25.022 -29.849 1.00 23.55 ? 250  PHE A N     1 
ATOM   690  C  CA    . PHE A 1 95  ? 26.035 -24.874 -31.265 1.00 20.52 ? 250  PHE A CA    1 
ATOM   691  C  C     . PHE A 1 95  ? 24.681 -25.482 -31.577 1.00 21.35 ? 250  PHE A C     1 
ATOM   692  O  O     . PHE A 1 95  ? 24.294 -26.506 -31.008 1.00 23.40 ? 250  PHE A O     1 
ATOM   693  C  CB    . PHE A 1 95  ? 27.060 -25.639 -32.110 1.00 22.71 ? 250  PHE A CB    1 
ATOM   694  C  CG    . PHE A 1 95  ? 28.446 -25.107 -31.966 1.00 23.18 ? 250  PHE A CG    1 
ATOM   695  C  CD1   . PHE A 1 95  ? 28.810 -23.915 -32.573 1.00 26.08 ? 250  PHE A CD1   1 
ATOM   696  C  CD2   . PHE A 1 95  ? 29.390 -25.784 -31.182 1.00 30.20 ? 250  PHE A CD2   1 
ATOM   697  C  CE1   . PHE A 1 95  ? 30.088 -23.404 -32.407 1.00 29.33 ? 250  PHE A CE1   1 
ATOM   698  C  CE2   . PHE A 1 95  ? 30.655 -25.280 -31.017 1.00 30.96 ? 250  PHE A CE2   1 
ATOM   699  C  CZ    . PHE A 1 95  ? 31.014 -24.091 -31.642 1.00 30.75 ? 250  PHE A CZ    1 
ATOM   700  N  N     . VAL A 1 96  ? 23.952 -24.825 -32.478 1.00 21.66 ? 251  VAL A N     1 
ATOM   701  C  CA    . VAL A 1 96  ? 22.666 -25.276 -32.978 1.00 24.18 ? 251  VAL A CA    1 
ATOM   702  C  C     . VAL A 1 96  ? 22.874 -25.701 -34.425 1.00 24.75 ? 251  VAL A C     1 
ATOM   703  O  O     . VAL A 1 96  ? 23.422 -24.935 -35.234 1.00 25.96 ? 251  VAL A O     1 
ATOM   704  C  CB    . VAL A 1 96  ? 21.638 -24.129 -32.900 1.00 27.43 ? 251  VAL A CB    1 
ATOM   705  C  CG1   . VAL A 1 96  ? 20.352 -24.454 -33.639 1.00 26.66 ? 251  VAL A CG1   1 
ATOM   706  C  CG2   . VAL A 1 96  ? 21.414 -23.756 -31.432 1.00 24.57 ? 251  VAL A CG2   1 
ATOM   707  N  N     . LYS A 1 97  ? 22.436 -26.912 -34.735 1.00 26.27 ? 252  LYS A N     1 
ATOM   708  C  CA    . LYS A 1 97  ? 22.298 -27.413 -36.097 1.00 31.07 ? 252  LYS A CA    1 
ATOM   709  C  C     . LYS A 1 97  ? 20.864 -27.886 -36.285 1.00 34.54 ? 252  LYS A C     1 
ATOM   710  O  O     . LYS A 1 97  ? 20.134 -28.102 -35.318 1.00 39.70 ? 252  LYS A O     1 
ATOM   711  C  CB    . LYS A 1 97  ? 23.218 -28.597 -36.294 1.00 33.85 ? 252  LYS A CB    1 
ATOM   712  C  CG    . LYS A 1 97  ? 24.641 -28.333 -35.889 1.00 35.26 ? 252  LYS A CG    1 
ATOM   713  C  CD    . LYS A 1 97  ? 25.429 -29.629 -35.883 1.00 43.27 ? 252  LYS A CD    1 
ATOM   714  C  CE    . LYS A 1 97  ? 26.918 -29.346 -35.868 1.00 44.29 ? 252  LYS A CE    1 
ATOM   715  N  NZ    . LYS A 1 97  ? 27.676 -30.460 -36.513 1.00 48.38 ? 252  LYS A NZ    1 
ATOM   716  N  N     . PHE A 1 98  ? 20.460 -28.041 -37.543 1.00 38.72 ? 253  PHE A N     1 
ATOM   717  C  CA    . PHE A 1 98  ? 19.112 -28.541 -37.857 1.00 42.77 ? 253  PHE A CA    1 
ATOM   718  C  C     . PHE A 1 98  ? 19.045 -30.061 -38.020 1.00 46.70 ? 253  PHE A C     1 
ATOM   719  O  O     . PHE A 1 98  ? 19.818 -30.641 -38.784 1.00 54.40 ? 253  PHE A O     1 
ATOM   720  C  CB    . PHE A 1 98  ? 18.590 -27.872 -39.123 1.00 44.70 ? 253  PHE A CB    1 
ATOM   721  C  CG    . PHE A 1 98  ? 18.306 -26.415 -38.953 1.00 41.62 ? 253  PHE A CG    1 
ATOM   722  C  CD1   . PHE A 1 98  ? 17.613 -25.964 -37.847 1.00 43.30 ? 253  PHE A CD1   1 
ATOM   723  C  CD2   . PHE A 1 98  ? 18.768 -25.493 -39.880 1.00 43.56 ? 253  PHE A CD2   1 
ATOM   724  C  CE1   . PHE A 1 98  ? 17.364 -24.617 -37.681 1.00 45.07 ? 253  PHE A CE1   1 
ATOM   725  C  CE2   . PHE A 1 98  ? 18.515 -24.140 -39.720 1.00 41.07 ? 253  PHE A CE2   1 
ATOM   726  C  CZ    . PHE A 1 98  ? 17.813 -23.705 -38.617 1.00 46.20 ? 253  PHE A CZ    1 
ATOM   727  N  N     . PRO A 1 106 ? 13.654 -20.305 -43.602 1.00 54.16 ? 261  PRO A N     1 
ATOM   728  C  CA    . PRO A 1 106 ? 14.288 -19.066 -44.061 1.00 38.52 ? 261  PRO A CA    1 
ATOM   729  C  C     . PRO A 1 106 ? 15.490 -18.755 -43.193 1.00 37.89 ? 261  PRO A C     1 
ATOM   730  O  O     . PRO A 1 106 ? 15.949 -17.618 -43.156 1.00 34.07 ? 261  PRO A O     1 
ATOM   731  C  CB    . PRO A 1 106 ? 13.208 -18.018 -43.819 1.00 35.53 ? 261  PRO A CB    1 
ATOM   732  C  CG    . PRO A 1 106 ? 11.925 -18.793 -43.927 1.00 47.72 ? 261  PRO A CG    1 
ATOM   733  C  CD    . PRO A 1 106 ? 12.243 -20.090 -43.238 1.00 48.63 ? 261  PRO A CD    1 
ATOM   734  N  N     . LEU A 1 107 ? 15.995 -19.770 -42.503 1.00 40.31 ? 262  LEU A N     1 
ATOM   735  C  CA    . LEU A 1 107 ? 17.152 -19.611 -41.632 1.00 37.14 ? 262  LEU A CA    1 
ATOM   736  C  C     . LEU A 1 107 ? 18.457 -19.965 -42.317 1.00 38.85 ? 262  LEU A C     1 
ATOM   737  O  O     . LEU A 1 107 ? 19.517 -19.811 -41.703 1.00 33.99 ? 262  LEU A O     1 
ATOM   738  C  CB    . LEU A 1 107 ? 16.990 -20.433 -40.355 1.00 39.53 ? 262  LEU A CB    1 
ATOM   739  C  CG    . LEU A 1 107 ? 15.795 -20.127 -39.458 1.00 38.06 ? 262  LEU A CG    1 
ATOM   740  C  CD1   . LEU A 1 107 ? 15.663 -18.633 -39.245 1.00 35.90 ? 262  LEU A CD1   1 
ATOM   741  C  CD2   . LEU A 1 107 ? 14.505 -20.726 -39.993 1.00 54.17 ? 262  LEU A CD2   1 
ATOM   742  N  N     . SER A 1 108 ? 18.397 -20.413 -43.576 1.00 40.40 ? 263  SER A N     1 
ATOM   743  C  CA    . SER A 1 108 ? 19.595 -20.805 -44.315 1.00 35.70 ? 263  SER A CA    1 
ATOM   744  C  C     . SER A 1 108 ? 20.574 -19.645 -44.466 1.00 34.57 ? 263  SER A C     1 
ATOM   745  O  O     . SER A 1 108 ? 21.792 -19.848 -44.468 1.00 35.55 ? 263  SER A O     1 
ATOM   746  C  CB    . SER A 1 108 ? 19.195 -21.355 -45.690 1.00 43.15 ? 263  SER A CB    1 
ATOM   747  O  OG    . SER A 1 108 ? 18.331 -22.487 -45.570 1.00 41.20 ? 263  SER A OG    1 
ATOM   748  N  N     . GLN A 1 109 ? 20.067 -18.420 -44.565 1.00 35.99 ? 264  GLN A N     1 
ATOM   749  C  CA    . GLN A 1 109 ? 20.934 -17.254 -44.620 1.00 31.42 ? 264  GLN A CA    1 
ATOM   750  C  C     . GLN A 1 109 ? 21.837 -17.146 -43.404 1.00 34.22 ? 264  GLN A C     1 
ATOM   751  O  O     . GLN A 1 109 ? 22.856 -16.447 -43.454 1.00 35.68 ? 264  GLN A O     1 
ATOM   752  C  CB    . GLN A 1 109 ? 20.056 -15.994 -44.740 1.00 36.46 ? 264  GLN A CB    1 
ATOM   753  C  CG    . GLN A 1 109 ? 18.975 -15.900 -43.637 1.00 29.69 ? 264  GLN A CG    1 
ATOM   754  C  CD    . GLN A 1 109 ? 17.999 -14.735 -43.827 1.00 32.50 ? 264  GLN A CD    1 
ATOM   755  O  OE1   . GLN A 1 109 ? 18.374 -13.562 -43.742 1.00 29.75 ? 264  GLN A OE1   1 
ATOM   756  N  NE2   . GLN A 1 109 ? 16.725 -15.068 -44.044 1.00 27.99 ? 264  GLN A NE2   1 
ATOM   757  N  N     . PHE A 1 110 ? 21.487 -17.800 -42.300 1.00 33.82 ? 265  PHE A N     1 
ATOM   758  C  CA    . PHE A 1 110 ? 22.311 -17.721 -41.102 1.00 29.32 ? 265  PHE A CA    1 
ATOM   759  C  C     . PHE A 1 110 ? 23.176 -18.941 -40.884 1.00 32.39 ? 265  PHE A C     1 
ATOM   760  O  O     . PHE A 1 110 ? 23.839 -19.015 -39.850 1.00 30.23 ? 265  PHE A O     1 
ATOM   761  C  CB    . PHE A 1 110 ? 21.457 -17.475 -39.849 1.00 26.77 ? 265  PHE A CB    1 
ATOM   762  C  CG    . PHE A 1 110 ? 20.461 -16.359 -39.987 1.00 27.18 ? 265  PHE A CG    1 
ATOM   763  C  CD1   . PHE A 1 110 ? 20.881 -15.056 -40.126 1.00 27.76 ? 265  PHE A CD1   1 
ATOM   764  C  CD2   . PHE A 1 110 ? 19.095 -16.623 -39.961 1.00 26.91 ? 265  PHE A CD2   1 
ATOM   765  C  CE1   . PHE A 1 110 ? 19.950 -14.022 -40.236 1.00 25.31 ? 265  PHE A CE1   1 
ATOM   766  C  CE2   . PHE A 1 110 ? 18.161 -15.588 -40.082 1.00 27.01 ? 265  PHE A CE2   1 
ATOM   767  C  CZ    . PHE A 1 110 ? 18.597 -14.293 -40.220 1.00 24.18 ? 265  PHE A CZ    1 
ATOM   768  N  N     . LEU A 1 111 ? 23.183 -19.894 -41.819 1.00 30.94 ? 266  LEU A N     1 
ATOM   769  C  CA    . LEU A 1 111 ? 23.959 -21.116 -41.641 1.00 32.05 ? 266  LEU A CA    1 
ATOM   770  C  C     . LEU A 1 111 ? 25.409 -20.919 -42.073 1.00 38.24 ? 266  LEU A C     1 
ATOM   771  O  O     . LEU A 1 111 ? 25.682 -20.331 -43.124 1.00 44.48 ? 266  LEU A O     1 
ATOM   772  C  CB    . LEU A 1 111 ? 23.344 -22.274 -42.427 1.00 35.42 ? 266  LEU A CB    1 
ATOM   773  C  CG    . LEU A 1 111 ? 21.960 -22.731 -41.987 1.00 33.14 ? 266  LEU A CG    1 
ATOM   774  C  CD1   . LEU A 1 111 ? 21.411 -23.771 -42.955 1.00 37.94 ? 266  LEU A CD1   1 
ATOM   775  C  CD2   . LEU A 1 111 ? 22.028 -23.266 -40.531 1.00 33.94 ? 266  LEU A CD2   1 
ATOM   776  N  N     . GLU A 1 112 ? 26.330 -21.384 -41.241 1.00 35.84 ? 267  GLU A N     1 
ATOM   777  C  CA    . GLU A 1 112 ? 27.732 -21.595 -41.599 1.00 39.27 ? 267  GLU A CA    1 
ATOM   778  C  C     . GLU A 1 112 ? 27.885 -23.112 -41.646 1.00 39.11 ? 267  GLU A C     1 
ATOM   779  O  O     . GLU A 1 112 ? 28.045 -23.768 -40.611 1.00 36.09 ? 267  GLU A O     1 
ATOM   780  C  CB    . GLU A 1 112 ? 28.658 -20.949 -40.567 1.00 35.99 ? 267  GLU A CB    1 
ATOM   781  N  N     . GLY A 1 113 ? 27.798 -23.669 -42.840 1.00 39.03 ? 268  GLY A N     1 
ATOM   782  C  CA    . GLY A 1 113 ? 27.723 -25.112 -42.952 1.00 38.65 ? 268  GLY A CA    1 
ATOM   783  C  C     . GLY A 1 113 ? 26.386 -25.586 -42.427 1.00 40.02 ? 268  GLY A C     1 
ATOM   784  O  O     . GLY A 1 113 ? 25.320 -25.168 -42.898 1.00 45.46 ? 268  GLY A O     1 
ATOM   785  N  N     . GLU A 1 114 ? 26.423 -26.474 -41.440 1.00 40.60 ? 269  GLU A N     1 
ATOM   786  C  CA    . GLU A 1 114 ? 25.213 -26.935 -40.781 1.00 38.59 ? 269  GLU A CA    1 
ATOM   787  C  C     . GLU A 1 114 ? 24.921 -26.160 -39.501 1.00 32.37 ? 269  GLU A C     1 
ATOM   788  O  O     . GLU A 1 114 ? 23.906 -26.421 -38.853 1.00 33.94 ? 269  GLU A O     1 
ATOM   789  C  CB    . GLU A 1 114 ? 25.301 -28.438 -40.492 1.00 38.45 ? 269  GLU A CB    1 
ATOM   790  N  N     . ILE A 1 115 ? 25.772 -25.207 -39.147 1.00 30.80 ? 270  ILE A N     1 
ATOM   791  C  CA    . ILE A 1 115 ? 25.674 -24.487 -37.875 1.00 30.50 ? 270  ILE A CA    1 
ATOM   792  C  C     . ILE A 1 115 ? 24.881 -23.193 -38.027 1.00 28.48 ? 270  ILE A C     1 
ATOM   793  O  O     . ILE A 1 115 ? 25.190 -22.339 -38.863 1.00 26.35 ? 270  ILE A O     1 
ATOM   794  C  CB    . ILE A 1 115 ? 27.071 -24.224 -37.295 1.00 28.06 ? 270  ILE A CB    1 
ATOM   795  C  CG1   . ILE A 1 115 ? 27.740 -25.562 -36.934 1.00 35.64 ? 270  ILE A CG1   1 
ATOM   796  C  CG2   . ILE A 1 115 ? 27.032 -23.238 -36.111 1.00 32.06 ? 270  ILE A CG2   1 
ATOM   797  C  CD1   . ILE A 1 115 ? 29.130 -25.399 -36.433 1.00 38.14 ? 270  ILE A CD1   1 
ATOM   798  N  N     . LEU A 1 116 ? 23.883 -23.019 -37.173 1.00 24.08 ? 271  LEU A N     1 
ATOM   799  C  CA    . LEU A 1 116 ? 23.082 -21.802 -37.198 1.00 24.01 ? 271  LEU A CA    1 
ATOM   800  C  C     . LEU A 1 116 ? 23.802 -20.734 -36.397 1.00 25.21 ? 271  LEU A C     1 
ATOM   801  O  O     . LEU A 1 116 ? 23.880 -20.826 -35.167 1.00 25.76 ? 271  LEU A O     1 
ATOM   802  C  CB    . LEU A 1 116 ? 21.712 -22.089 -36.601 1.00 20.77 ? 271  LEU A CB    1 
ATOM   803  C  CG    . LEU A 1 116 ? 20.740 -20.923 -36.745 1.00 25.75 ? 271  LEU A CG    1 
ATOM   804  C  CD1   . LEU A 1 116 ? 20.268 -20.706 -38.206 1.00 26.23 ? 271  LEU A CD1   1 
ATOM   805  C  CD2   . LEU A 1 116 ? 19.553 -21.129 -35.789 1.00 33.75 ? 271  LEU A CD2   1 
ATOM   806  N  N     . SER A 1 117 ? 24.327 -19.714 -37.072 1.00 23.02 ? 272  SER A N     1 
ATOM   807  C  CA    . SER A 1 117 ? 25.163 -18.716 -36.416 1.00 23.73 ? 272  SER A CA    1 
ATOM   808  C  C     . SER A 1 117 ? 24.328 -17.794 -35.539 1.00 20.56 ? 272  SER A C     1 
ATOM   809  O  O     . SER A 1 117 ? 23.508 -17.015 -36.048 1.00 22.22 ? 272  SER A O     1 
ATOM   810  C  CB    . SER A 1 117 ? 25.884 -17.838 -37.423 1.00 25.60 ? 272  SER A CB    1 
ATOM   811  O  OG    . SER A 1 117 ? 26.562 -16.819 -36.733 1.00 26.92 ? 272  SER A OG    1 
ATOM   812  N  N     . ALA A 1 118 ? 24.633 -17.802 -34.236 1.00 19.96 ? 273  ALA A N     1 
ATOM   813  C  CA    . ALA A 1 118 ? 24.002 -16.850 -33.330 1.00 23.06 ? 273  ALA A CA    1 
ATOM   814  C  C     . ALA A 1 118 ? 24.329 -15.422 -33.707 1.00 22.03 ? 273  ALA A C     1 
ATOM   815  O  O     . ALA A 1 118 ? 23.438 -14.560 -33.684 1.00 19.87 ? 273  ALA A O     1 
ATOM   816  C  CB    . ALA A 1 118 ? 24.447 -17.123 -31.896 1.00 22.46 ? 273  ALA A CB    1 
ATOM   817  N  N     . SER A 1 119 ? 25.612 -15.129 -34.019 1.00 22.71 ? 274  SER A N     1 
ATOM   818  C  CA    . SER A 1 119 ? 25.968 -13.748 -34.353 1.00 20.19 ? 274  SER A CA    1 
ATOM   819  C  C     . SER A 1 119 ? 25.273 -13.261 -35.623 1.00 20.45 ? 274  SER A C     1 
ATOM   820  O  O     . SER A 1 119 ? 24.853 -12.102 -35.693 1.00 23.19 ? 274  SER A O     1 
ATOM   821  C  CB    . SER A 1 119 ? 27.491 -13.560 -34.423 1.00 25.07 ? 274  SER A CB    1 
ATOM   822  O  OG    . SER A 1 119 ? 27.992 -14.428 -35.415 1.00 29.93 ? 274  SER A OG    1 
ATOM   823  N  N     . LYS A 1 120 ? 25.138 -14.112 -36.643 1.00 21.05 ? 275  LYS A N     1 
ATOM   824  C  CA    . LYS A 1 120 ? 24.509 -13.627 -37.872 1.00 24.37 ? 275  LYS A CA    1 
ATOM   825  C  C     . LYS A 1 120 ? 23.021 -13.342 -37.671 1.00 21.81 ? 275  LYS A C     1 
ATOM   826  O  O     . LYS A 1 120 ? 22.477 -12.372 -38.223 1.00 23.96 ? 275  LYS A O     1 
ATOM   827  C  CB    . LYS A 1 120 ? 24.745 -14.601 -39.025 1.00 28.77 ? 275  LYS A CB    1 
ATOM   828  C  CG    . LYS A 1 120 ? 26.204 -14.570 -39.506 1.00 31.44 ? 275  LYS A CG    1 
ATOM   829  C  CD    . LYS A 1 120 ? 26.596 -15.834 -40.243 1.00 45.05 ? 275  LYS A CD    1 
ATOM   830  C  CE    . LYS A 1 120 ? 25.570 -16.286 -41.281 1.00 48.69 ? 275  LYS A CE    1 
ATOM   831  N  NZ    . LYS A 1 120 ? 24.814 -15.189 -41.976 1.00 54.37 ? 275  LYS A NZ    1 
ATOM   832  N  N     . MET A 1 121 ? 22.346 -14.176 -36.881 1.00 22.26 ? 276  MET A N     1 
ATOM   833  C  CA    . MET A 1 121 ? 20.926 -13.978 -36.643 1.00 24.38 ? 276  MET A CA    1 
ATOM   834  C  C     . MET A 1 121 ? 20.720 -12.749 -35.777 1.00 17.53 ? 276  MET A C     1 
ATOM   835  O  O     . MET A 1 121 ? 19.842 -11.929 -36.050 1.00 19.70 ? 276  MET A O     1 
ATOM   836  C  CB    . MET A 1 121 ? 20.444 -15.199 -35.884 1.00 23.82 ? 276  MET A CB    1 
ATOM   837  C  CG    . MET A 1 121 ? 19.906 -16.262 -36.767 1.00 29.61 ? 276  MET A CG    1 
ATOM   838  S  SD    . MET A 1 121 ? 18.692 -17.356 -36.025 1.00 28.88 ? 276  MET A SD    1 
ATOM   839  C  CE    . MET A 1 121 ? 17.127 -16.570 -36.224 1.00 33.93 ? 276  MET A CE    1 
ATOM   840  N  N     . LEU A 1 122 ? 21.554 -12.598 -34.745 1.00 18.24 ? 277  LEU A N     1 
ATOM   841  C  CA    . LEU A 1 122 ? 21.487 -11.399 -33.924 1.00 19.73 ? 277  LEU A CA    1 
ATOM   842  C  C     . LEU A 1 122 ? 21.776 -10.137 -34.727 1.00 20.23 ? 277  LEU A C     1 
ATOM   843  O  O     . LEU A 1 122 ? 21.107 -9.117  -34.545 1.00 22.41 ? 277  LEU A O     1 
ATOM   844  C  CB    . LEU A 1 122 ? 22.431 -11.504 -32.735 1.00 17.47 ? 277  LEU A CB    1 
ATOM   845  C  CG    . LEU A 1 122 ? 22.542 -10.311 -31.801 1.00 19.47 ? 277  LEU A CG    1 
ATOM   846  C  CD1   . LEU A 1 122 ? 21.147 -9.927  -31.222 1.00 18.53 ? 277  LEU A CD1   1 
ATOM   847  C  CD2   . LEU A 1 122 ? 23.538 -10.606 -30.655 1.00 21.80 ? 277  LEU A CD2   1 
ATOM   848  N  N     . SER A 1 123 ? 22.781 -10.176 -35.627 1.00 20.99 ? 278  SER A N     1 
ATOM   849  C  CA    . SER A 1 123 ? 23.098 -8.981  -36.410 1.00 23.34 ? 278  SER A CA    1 
ATOM   850  C  C     . SER A 1 123 ? 21.912 -8.533  -37.252 1.00 20.19 ? 278  SER A C     1 
ATOM   851  O  O     . SER A 1 123 ? 21.617 -7.333  -37.337 1.00 21.84 ? 278  SER A O     1 
ATOM   852  C  CB    . SER A 1 123 ? 24.319 -9.216  -37.325 1.00 23.65 ? 278  SER A CB    1 
ATOM   853  O  OG    . SER A 1 123 ? 25.511 -9.309  -36.572 1.00 41.31 ? 278  SER A OG    1 
ATOM   854  N  N     . LYS A 1 124 ? 21.223 -9.477  -37.891 1.00 18.77 ? 279  LYS A N     1 
ATOM   855  C  CA    . LYS A 1 124 ? 20.067 -9.081  -38.692 1.00 20.74 ? 279  LYS A CA    1 
ATOM   856  C  C     . LYS A 1 124 ? 18.928 -8.572  -37.810 1.00 20.93 ? 279  LYS A C     1 
ATOM   857  O  O     . LYS A 1 124 ? 18.288 -7.572  -38.132 1.00 23.17 ? 279  LYS A O     1 
ATOM   858  C  CB    . LYS A 1 124 ? 19.581 -10.244 -39.561 1.00 21.55 ? 279  LYS A CB    1 
ATOM   859  C  CG    . LYS A 1 124 ? 18.662 -9.758  -40.702 1.00 25.93 ? 279  LYS A CG    1 
ATOM   860  C  CD    . LYS A 1 124 ? 18.139 -10.898 -41.554 1.00 28.92 ? 279  LYS A CD    1 
ATOM   861  C  CE    . LYS A 1 124 ? 17.333 -10.344 -42.750 1.00 33.69 ? 279  LYS A CE    1 
ATOM   862  N  NZ    . LYS A 1 124 ? 16.586 -11.405 -43.527 1.00 37.00 ? 279  LYS A NZ    1 
ATOM   863  N  N     . PHE A 1 125 ? 18.667 -9.258  -36.693 1.00 21.70 ? 280  PHE A N     1 
ATOM   864  C  CA    . PHE A 1 125 ? 17.635 -8.819  -35.760 1.00 19.42 ? 280  PHE A CA    1 
ATOM   865  C  C     . PHE A 1 125 ? 17.903 -7.395  -35.278 1.00 19.08 ? 280  PHE A C     1 
ATOM   866  O  O     . PHE A 1 125 ? 17.014 -6.542  -35.289 1.00 19.62 ? 280  PHE A O     1 
ATOM   867  C  CB    . PHE A 1 125 ? 17.671 -9.820  -34.603 1.00 17.44 ? 280  PHE A CB    1 
ATOM   868  C  CG    . PHE A 1 125 ? 16.598 -9.633  -33.535 1.00 15.19 ? 280  PHE A CG    1 
ATOM   869  C  CD1   . PHE A 1 125 ? 15.306 -10.089 -33.750 1.00 19.93 ? 280  PHE A CD1   1 
ATOM   870  C  CD2   . PHE A 1 125 ? 16.930 -9.079  -32.302 1.00 17.93 ? 280  PHE A CD2   1 
ATOM   871  C  CE1   . PHE A 1 125 ? 14.361 -9.973  -32.763 1.00 20.04 ? 280  PHE A CE1   1 
ATOM   872  C  CE2   . PHE A 1 125 ? 15.977 -8.967  -31.302 1.00 17.82 ? 280  PHE A CE2   1 
ATOM   873  C  CZ    . PHE A 1 125 ? 14.695 -9.385  -31.551 1.00 18.85 ? 280  PHE A CZ    1 
ATOM   874  N  N     . ARG A 1 126 ? 19.138 -7.119  -34.862 1.00 18.45 ? 281  ARG A N     1 
ATOM   875  C  CA    . ARG A 1 126 ? 19.497 -5.770  -34.436 1.00 18.71 ? 281  ARG A CA    1 
ATOM   876  C  C     . ARG A 1 126 ? 19.362 -4.763  -35.574 1.00 20.36 ? 281  ARG A C     1 
ATOM   877  O  O     . ARG A 1 126 ? 18.904 -3.642  -35.355 1.00 22.82 ? 281  ARG A O     1 
ATOM   878  C  CB    . ARG A 1 126 ? 20.920 -5.766  -33.900 1.00 19.53 ? 281  ARG A CB    1 
ATOM   879  C  CG    . ARG A 1 126 ? 21.357 -4.467  -33.337 1.00 21.84 ? 281  ARG A CG    1 
ATOM   880  C  CD    . ARG A 1 126 ? 22.792 -4.592  -32.835 1.00 22.93 ? 281  ARG A CD    1 
ATOM   881  N  NE    . ARG A 1 126 ? 23.192 -3.323  -32.262 1.00 27.07 ? 281  ARG A NE    1 
ATOM   882  C  CZ    . ARG A 1 126 ? 23.056 -3.016  -30.981 1.00 26.79 ? 281  ARG A CZ    1 
ATOM   883  N  NH1   . ARG A 1 126 ? 22.570 -3.893  -30.108 1.00 23.36 ? 281  ARG A NH1   1 
ATOM   884  N  NH2   . ARG A 1 126 ? 23.434 -1.812  -30.558 1.00 26.99 ? 281  ARG A NH2   1 
ATOM   885  N  N     . LYS A 1 127 ? 19.800 -5.138  -36.782 1.00 21.52 ? 282  LYS A N     1 
ATOM   886  C  CA    . LYS A 1 127 ? 19.713 -4.229  -37.922 1.00 24.33 ? 282  LYS A CA    1 
ATOM   887  C  C     . LYS A 1 127 ? 18.275 -3.837  -38.215 1.00 22.31 ? 282  LYS A C     1 
ATOM   888  O  O     . LYS A 1 127 ? 17.976 -2.663  -38.480 1.00 25.18 ? 282  LYS A O     1 
ATOM   889  C  CB    . LYS A 1 127 ? 20.358 -4.887  -39.149 1.00 27.88 ? 282  LYS A CB    1 
ATOM   890  C  CG    . LYS A 1 127 ? 20.265 -4.105  -40.457 1.00 38.60 ? 282  LYS A CG    1 
ATOM   891  C  CD    . LYS A 1 127 ? 19.930 -5.091  -41.608 1.00 48.89 ? 282  LYS A CD    1 
ATOM   892  C  CE    . LYS A 1 127 ? 19.410 -4.441  -42.897 1.00 49.22 ? 282  LYS A CE    1 
ATOM   893  N  NZ    . LYS A 1 127 ? 17.978 -4.030  -42.793 1.00 51.35 ? 282  LYS A NZ    1 
ATOM   894  N  N     . ILE A 1 128 ? 17.368 -4.799  -38.159 1.00 23.08 ? 283  ILE A N     1 
ATOM   895  C  CA    . ILE A 1 128 ? 15.975 -4.492  -38.435 1.00 23.76 ? 283  ILE A CA    1 
ATOM   896  C  C     . ILE A 1 128 ? 15.410 -3.561  -37.373 1.00 22.39 ? 283  ILE A C     1 
ATOM   897  O  O     . ILE A 1 128 ? 14.691 -2.605  -37.675 1.00 27.05 ? 283  ILE A O     1 
ATOM   898  C  CB    . ILE A 1 128 ? 15.158 -5.784  -38.535 1.00 24.21 ? 283  ILE A CB    1 
ATOM   899  C  CG1   . ILE A 1 128 ? 15.554 -6.548  -39.791 1.00 23.89 ? 283  ILE A CG1   1 
ATOM   900  C  CG2   . ILE A 1 128 ? 13.684 -5.459  -38.496 1.00 25.83 ? 283  ILE A CG2   1 
ATOM   901  C  CD1   . ILE A 1 128 ? 14.945 -7.928  -39.854 1.00 24.25 ? 283  ILE A CD1   1 
ATOM   902  N  N     . ILE A 1 129 ? 15.698 -3.852  -36.098 1.00 23.09 ? 284  ILE A N     1 
ATOM   903  C  CA    . ILE A 1 129 ? 15.216 -2.989  -35.021 1.00 23.05 ? 284  ILE A CA    1 
ATOM   904  C  C     . ILE A 1 129 ? 15.754 -1.573  -35.164 1.00 26.19 ? 284  ILE A C     1 
ATOM   905  O  O     . ILE A 1 129 ? 15.000 -0.598  -35.098 1.00 25.29 ? 284  ILE A O     1 
ATOM   906  C  CB    . ILE A 1 129 ? 15.546 -3.606  -33.654 1.00 20.80 ? 284  ILE A CB    1 
ATOM   907  C  CG1   . ILE A 1 129 ? 14.696 -4.865  -33.450 1.00 23.17 ? 284  ILE A CG1   1 
ATOM   908  C  CG2   . ILE A 1 129 ? 15.362 -2.557  -32.550 1.00 21.61 ? 284  ILE A CG2   1 
ATOM   909  C  CD1   . ILE A 1 129 ? 15.057 -5.651  -32.197 1.00 22.66 ? 284  ILE A CD1   1 
ATOM   910  N  N     . LYS A 1 130 ? 17.061 -1.448  -35.410 1.00 21.57 ? 285  LYS A N     1 
ATOM   911  C  CA    . LYS A 1 130 ? 17.705 -0.145  -35.570 1.00 27.65 ? 285  LYS A CA    1 
ATOM   912  C  C     . LYS A 1 130 ? 17.034 0.683   -36.663 1.00 28.52 ? 285  LYS A C     1 
ATOM   913  O  O     . LYS A 1 130 ? 16.829 1.891   -36.502 1.00 30.52 ? 285  LYS A O     1 
ATOM   914  C  CB    . LYS A 1 130 ? 19.180 -0.387  -35.912 1.00 27.09 ? 285  LYS A CB    1 
ATOM   915  C  CG    . LYS A 1 130 ? 20.092 0.791   -35.555 1.00 33.87 ? 285  LYS A CG    1 
ATOM   916  C  CD    . LYS A 1 130 ? 21.490 0.578   -36.156 1.00 34.77 ? 285  LYS A CD    1 
ATOM   917  C  CE    . LYS A 1 130 ? 22.407 1.789   -36.020 1.00 46.75 ? 285  LYS A CE    1 
ATOM   918  N  NZ    . LYS A 1 130 ? 22.102 2.865   -37.009 1.00 48.15 ? 285  LYS A NZ    1 
ATOM   919  N  N     . GLU A 1 131 ? 16.699 0.059   -37.787 1.00 25.72 ? 286  GLU A N     1 
ATOM   920  C  CA    . GLU A 1 131 ? 16.057 0.816   -38.852 1.00 30.50 ? 286  GLU A CA    1 
ATOM   921  C  C     . GLU A 1 131 ? 14.637 1.208   -38.508 1.00 34.50 ? 286  GLU A C     1 
ATOM   922  O  O     . GLU A 1 131 ? 14.119 2.179   -39.065 1.00 44.79 ? 286  GLU A O     1 
ATOM   923  C  CB    . GLU A 1 131 ? 16.095 0.040   -40.169 1.00 38.16 ? 286  GLU A CB    1 
ATOM   924  C  CG    . GLU A 1 131 ? 17.493 -0.086  -40.741 1.00 44.08 ? 286  GLU A CG    1 
ATOM   925  C  CD    . GLU A 1 131 ? 17.622 -1.239  -41.707 1.00 58.60 ? 286  GLU A CD    1 
ATOM   926  O  OE1   . GLU A 1 131 ? 16.627 -1.977  -41.885 1.00 55.37 ? 286  GLU A OE1   1 
ATOM   927  O  OE2   . GLU A 1 131 ? 18.719 -1.414  -42.285 1.00 71.62 ? 286  GLU A OE2   1 
ATOM   928  N  N     . GLU A 1 132 ? 14.001 0.496   -37.597 1.00 30.15 ? 287  GLU A N     1 
ATOM   929  C  CA    . GLU A 1 132 ? 12.605 0.763   -37.328 1.00 31.73 ? 287  GLU A CA    1 
ATOM   930  C  C     . GLU A 1 132 ? 12.369 1.807   -36.252 1.00 36.36 ? 287  GLU A C     1 
ATOM   931  O  O     . GLU A 1 132 ? 11.288 2.396   -36.223 1.00 38.32 ? 287  GLU A O     1 
ATOM   932  C  CB    . GLU A 1 132 ? 11.901 -0.532  -36.946 1.00 30.91 ? 287  GLU A CB    1 
ATOM   933  C  CG    . GLU A 1 132 ? 10.507 -0.644  -37.470 1.00 52.42 ? 287  GLU A CG    1 
ATOM   934  C  CD    . GLU A 1 132 ? 10.333 -0.001  -38.829 1.00 52.83 ? 287  GLU A CD    1 
ATOM   935  O  OE1   . GLU A 1 132 ? 10.870 -0.551  -39.817 1.00 56.27 ? 287  GLU A OE1   1 
ATOM   936  O  OE2   . GLU A 1 132 ? 9.666  1.058   -38.900 1.00 50.00 ? 287  GLU A OE2   1 
ATOM   937  N  N     . ILE A 1 133 ? 13.335 2.066   -35.382 1.00 37.47 ? 288  ILE A N     1 
ATOM   938  C  CA    . ILE A 1 133 ? 13.035 2.876   -34.218 1.00 34.97 ? 288  ILE A CA    1 
ATOM   939  C  C     . ILE A 1 133 ? 12.958 4.362   -34.561 1.00 41.54 ? 288  ILE A C     1 
ATOM   940  O  O     . ILE A 1 133 ? 12.080 5.059   -34.054 1.00 58.44 ? 288  ILE A O     1 
ATOM   941  C  CB    . ILE A 1 133 ? 14.000 2.604   -33.067 1.00 33.74 ? 288  ILE A CB    1 
ATOM   942  C  CG1   . ILE A 1 133 ? 15.424 2.893   -33.514 1.00 32.25 ? 288  ILE A CG1   1 
ATOM   943  C  CG2   . ILE A 1 133 ? 13.811 1.159   -32.544 1.00 30.03 ? 288  ILE A CG2   1 
ATOM   944  C  CD1   . ILE A 1 133 ? 16.415 2.851   -32.381 1.00 35.02 ? 288  ILE A CD1   1 
ATOM   945  N  N     . ASP A 1 138 ? 5.194  8.612   -31.817 1.00 43.38 ? 293  ASP A N     1 
ATOM   946  C  CA    . ASP A 1 138 ? 5.119  9.508   -30.665 1.00 47.26 ? 293  ASP A CA    1 
ATOM   947  C  C     . ASP A 1 138 ? 6.054  9.053   -29.549 1.00 49.89 ? 293  ASP A C     1 
ATOM   948  O  O     . ASP A 1 138 ? 5.733  9.159   -28.365 1.00 50.98 ? 293  ASP A O     1 
ATOM   949  C  CB    . ASP A 1 138 ? 3.684  9.569   -30.135 1.00 48.71 ? 293  ASP A CB    1 
ATOM   950  N  N     . THR A 1 139 ? 7.221  8.544   -29.919 1.00 42.83 ? 294  THR A N     1 
ATOM   951  C  CA    . THR A 1 139 ? 8.127  7.983   -28.932 1.00 39.06 ? 294  THR A CA    1 
ATOM   952  C  C     . THR A 1 139 ? 9.553  8.350   -29.289 1.00 39.29 ? 294  THR A C     1 
ATOM   953  O  O     . THR A 1 139 ? 9.952  8.228   -30.450 1.00 38.73 ? 294  THR A O     1 
ATOM   954  C  CB    . THR A 1 139 ? 7.997  6.458   -28.887 1.00 41.90 ? 294  THR A CB    1 
ATOM   955  O  OG1   . THR A 1 139 ? 6.634  6.071   -29.131 1.00 49.43 ? 294  THR A OG1   1 
ATOM   956  C  CG2   . THR A 1 139 ? 8.454  5.939   -27.554 1.00 35.06 ? 294  THR A CG2   1 
ATOM   957  N  N     . ASP A 1 140 ? 10.322 8.790   -28.298 1.00 29.88 ? 295  ASP A N     1 
ATOM   958  C  CA    . ASP A 1 140 ? 11.755 8.993   -28.490 1.00 40.33 ? 295  ASP A CA    1 
ATOM   959  C  C     . ASP A 1 140 ? 12.448 7.705   -28.073 1.00 35.85 ? 295  ASP A C     1 
ATOM   960  O  O     . ASP A 1 140 ? 12.403 7.334   -26.897 1.00 30.87 ? 295  ASP A O     1 
ATOM   961  C  CB    . ASP A 1 140 ? 12.268 10.167  -27.659 1.00 50.64 ? 295  ASP A CB    1 
ATOM   962  C  CG    . ASP A 1 140 ? 12.250 11.491  -28.426 1.00 65.84 ? 295  ASP A CG    1 
ATOM   963  O  OD1   . ASP A 1 140 ? 11.324 11.705  -29.240 1.00 66.05 ? 295  ASP A OD1   1 
ATOM   964  O  OD2   . ASP A 1 140 ? 13.163 12.323  -28.209 1.00 71.15 ? 295  ASP A OD2   1 
ATOM   965  N  N     . VAL A 1 141 ? 13.070 7.023   -29.032 1.00 29.48 ? 296  VAL A N     1 
ATOM   966  C  CA    . VAL A 1 141 ? 13.681 5.717   -28.806 1.00 26.81 ? 296  VAL A CA    1 
ATOM   967  C  C     . VAL A 1 141 ? 15.099 5.759   -29.354 1.00 32.18 ? 296  VAL A C     1 
ATOM   968  O  O     . VAL A 1 141 ? 15.321 6.183   -30.493 1.00 31.40 ? 296  VAL A O     1 
ATOM   969  C  CB    . VAL A 1 141 ? 12.894 4.592   -29.500 1.00 28.90 ? 296  VAL A CB    1 
ATOM   970  C  CG1   . VAL A 1 141 ? 13.496 3.231   -29.094 1.00 30.84 ? 296  VAL A CG1   1 
ATOM   971  C  CG2   . VAL A 1 141 ? 11.400 4.684   -29.193 1.00 36.48 ? 296  VAL A CG2   1 
ATOM   972  N  N     . ILE A 1 142 ? 16.063 5.342   -28.546 1.00 25.30 ? 297  ILE A N     1 
ATOM   973  C  CA    . ILE A 1 142 ? 17.413 5.186   -29.042 1.00 30.01 ? 297  ILE A CA    1 
ATOM   974  C  C     . ILE A 1 142 ? 17.879 3.781   -28.695 1.00 31.12 ? 297  ILE A C     1 
ATOM   975  O  O     . ILE A 1 142 ? 17.317 3.111   -27.826 1.00 24.62 ? 297  ILE A O     1 
ATOM   976  C  CB    . ILE A 1 142 ? 18.365 6.255   -28.488 1.00 31.53 ? 297  ILE A CB    1 
ATOM   977  C  CG1   . ILE A 1 142 ? 18.579 6.021   -26.999 1.00 34.87 ? 297  ILE A CG1   1 
ATOM   978  C  CG2   . ILE A 1 142 ? 17.811 7.681   -28.780 1.00 33.98 ? 297  ILE A CG2   1 
ATOM   979  C  CD1   . ILE A 1 142 ? 19.864 6.599   -26.463 1.00 35.47 ? 297  ILE A CD1   1 
ATOM   980  N  N     . MET A 1 143 ? 18.893 3.326   -29.419 1.00 26.21 ? 298  MET A N     1 
ATOM   981  C  CA    . MET A 1 143 ? 19.494 2.018   -29.205 1.00 24.94 ? 298  MET A CA    1 
ATOM   982  C  C     . MET A 1 143 ? 20.852 2.147   -28.531 1.00 32.90 ? 298  MET A C     1 
ATOM   983  O  O     . MET A 1 143 ? 21.718 2.906   -28.993 1.00 27.12 ? 298  MET A O     1 
ATOM   984  C  CB    . MET A 1 143 ? 19.538 1.207   -30.502 1.00 26.18 ? 298  MET A CB    1 
ATOM   985  C  CG    . MET A 1 143 ? 20.022 -0.232  -30.305 1.00 22.63 ? 298  MET A CG    1 
ATOM   986  S  SD    . MET A 1 143 ? 20.311 -1.123  -31.875 1.00 27.43 ? 298  MET A SD    1 
ATOM   987  C  CE    . MET A 1 143 ? 18.617 -1.144  -32.477 1.00 26.02 ? 298  MET A CE    1 
ATOM   988  N  N     . LYS A 1 144 ? 21.020 1.420   -27.427 1.00 23.60 ? 299  LYS A N     1 
ATOM   989  C  CA    . LYS A 1 144 ? 22.269 1.409   -26.693 1.00 24.83 ? 299  LYS A CA    1 
ATOM   990  C  C     . LYS A 1 144 ? 23.261 0.502   -27.401 1.00 26.66 ? 299  LYS A C     1 
ATOM   991  O  O     . LYS A 1 144 ? 22.878 -0.445  -28.091 1.00 25.55 ? 299  LYS A O     1 
ATOM   992  C  CB    . LYS A 1 144 ? 22.047 0.936   -25.252 1.00 25.64 ? 299  LYS A CB    1 
ATOM   993  C  CG    . LYS A 1 144 ? 21.031 1.784   -24.451 1.00 29.67 ? 299  LYS A CG    1 
ATOM   994  C  CD    . LYS A 1 144 ? 21.338 1.699   -22.944 1.00 43.90 ? 299  LYS A CD    1 
ATOM   995  C  CE    . LYS A 1 144 ? 20.089 1.450   -22.095 1.00 41.49 ? 299  LYS A CE    1 
ATOM   996  N  NZ    . LYS A 1 144 ? 20.310 1.665   -20.643 1.00 39.47 ? 299  LYS A NZ    1 
ATOM   997  N  N     . ARG A 1 145 ? 24.549 0.819   -27.246 1.00 24.96 ? 300  ARG A N     1 
ATOM   998  C  CA    . ARG A 1 145 ? 25.578 0.088   -27.980 1.00 33.05 ? 300  ARG A CA    1 
ATOM   999  C  C     . ARG A 1 145 ? 25.551 -1.394  -27.633 1.00 33.07 ? 300  ARG A C     1 
ATOM   1000 O  O     . ARG A 1 145 ? 25.213 -1.794  -26.509 1.00 26.54 ? 300  ARG A O     1 
ATOM   1001 C  CB    . ARG A 1 145 ? 26.968 0.670   -27.693 1.00 33.60 ? 300  ARG A CB    1 
ATOM   1002 C  CG    . ARG A 1 145 ? 27.336 0.694   -26.228 1.00 30.46 ? 300  ARG A CG    1 
ATOM   1003 C  CD    . ARG A 1 145 ? 28.752 1.224   -26.030 1.00 42.53 ? 300  ARG A CD    1 
ATOM   1004 N  NE    . ARG A 1 145 ? 29.751 0.272   -26.487 1.00 45.66 ? 300  ARG A NE    1 
ATOM   1005 C  CZ    . ARG A 1 145 ? 30.428 -0.536  -25.683 1.00 52.02 ? 300  ARG A CZ    1 
ATOM   1006 N  NH1   . ARG A 1 145 ? 30.312 -0.457  -24.365 1.00 51.25 ? 300  ARG A NH1   1 
ATOM   1007 N  NH2   . ARG A 1 145 ? 31.252 -1.437  -26.213 1.00 48.06 ? 300  ARG A NH2   1 
ATOM   1008 N  N     . LYS A 1 146 ? 25.923 -2.198  -28.633 1.00 34.04 ? 301  LYS A N     1 
ATOM   1009 C  CA    . LYS A 1 146 ? 25.973 -3.654  -28.565 1.00 30.03 ? 301  LYS A CA    1 
ATOM   1010 C  C     . LYS A 1 146 ? 26.932 -4.078  -27.455 1.00 35.49 ? 301  LYS A C     1 
ATOM   1011 O  O     . LYS A 1 146 ? 28.029 -3.511  -27.322 1.00 35.31 ? 301  LYS A O     1 
ATOM   1012 C  CB    . LYS A 1 146 ? 26.470 -4.204  -29.916 1.00 32.65 ? 301  LYS A CB    1 
ATOM   1013 C  CG    . LYS A 1 146 ? 26.078 -5.656  -30.171 1.00 40.19 ? 301  LYS A CG    1 
ATOM   1014 C  CD    . LYS A 1 146 ? 27.215 -6.624  -29.899 1.00 48.31 ? 301  LYS A CD    1 
ATOM   1015 C  CE    . LYS A 1 146 ? 27.020 -7.948  -30.649 1.00 49.38 ? 301  LYS A CE    1 
ATOM   1016 N  NZ    . LYS A 1 146 ? 28.093 -8.948  -30.342 1.00 50.03 ? 301  LYS A NZ    1 
ATOM   1017 N  N     . SER A 1 150 ? 25.819 -9.362  -23.445 1.00 27.08 ? 305  SER A N     1 
ATOM   1018 C  CA    . SER A 1 150 ? 24.376 -9.487  -23.423 1.00 21.68 ? 305  SER A CA    1 
ATOM   1019 C  C     . SER A 1 150 ? 23.879 -10.004 -24.750 1.00 20.45 ? 305  SER A C     1 
ATOM   1020 O  O     . SER A 1 150 ? 24.364 -9.607  -25.813 1.00 23.30 ? 305  SER A O     1 
ATOM   1021 C  CB    . SER A 1 150 ? 23.739 -8.118  -23.241 1.00 21.98 ? 305  SER A CB    1 
ATOM   1022 O  OG    . SER A 1 150 ? 22.331 -8.239  -23.296 1.00 22.80 ? 305  SER A OG    1 
ATOM   1023 N  N     . PRO A 1 151 ? 22.859 -10.861 -24.722 1.00 19.40 ? 306  PRO A N     1 
ATOM   1024 C  CA    . PRO A 1 151 ? 22.200 -11.248 -25.974 1.00 17.38 ? 306  PRO A CA    1 
ATOM   1025 C  C     . PRO A 1 151 ? 21.164 -10.222 -26.464 1.00 16.46 ? 306  PRO A C     1 
ATOM   1026 O  O     . PRO A 1 151 ? 20.553 -10.424 -27.542 1.00 19.60 ? 306  PRO A O     1 
ATOM   1027 C  CB    . PRO A 1 151 ? 21.486 -12.543 -25.581 1.00 17.80 ? 306  PRO A CB    1 
ATOM   1028 C  CG    . PRO A 1 151 ? 21.120 -12.285 -24.090 1.00 19.82 ? 306  PRO A CG    1 
ATOM   1029 C  CD    . PRO A 1 151 ? 22.255 -11.513 -23.540 1.00 18.03 ? 306  PRO A CD    1 
ATOM   1030 N  N     . ALA A 1 152 ? 20.889 -9.176  -25.677 1.00 16.06 ? 307  ALA A N     1 
ATOM   1031 C  CA    . ALA A 1 152 ? 19.746 -8.305  -25.911 1.00 16.92 ? 307  ALA A CA    1 
ATOM   1032 C  C     . ALA A 1 152 ? 20.111 -7.184  -26.877 1.00 17.28 ? 307  ALA A C     1 
ATOM   1033 O  O     . ALA A 1 152 ? 21.273 -6.763  -26.976 1.00 20.50 ? 307  ALA A O     1 
ATOM   1034 C  CB    . ALA A 1 152 ? 19.347 -7.658  -24.597 1.00 17.94 ? 307  ALA A CB    1 
ATOM   1035 N  N     . VAL A 1 153 ? 19.102 -6.697  -27.584 1.00 17.53 ? 308  VAL A N     1 
ATOM   1036 C  CA    . VAL A 1 153 ? 19.138 -5.381  -28.207 1.00 17.85 ? 308  VAL A CA    1 
ATOM   1037 C  C     . VAL A 1 153 ? 18.448 -4.451  -27.229 1.00 18.93 ? 308  VAL A C     1 
ATOM   1038 O  O     . VAL A 1 153 ? 17.286 -4.675  -26.895 1.00 20.41 ? 308  VAL A O     1 
ATOM   1039 C  CB    . VAL A 1 153 ? 18.389 -5.404  -29.545 1.00 18.65 ? 308  VAL A CB    1 
ATOM   1040 C  CG1   . VAL A 1 153 ? 18.301 -3.976  -30.118 1.00 20.61 ? 308  VAL A CG1   1 
ATOM   1041 C  CG2   . VAL A 1 153 ? 19.068 -6.402  -30.549 1.00 20.23 ? 308  VAL A CG2   1 
ATOM   1042 N  N     . THR A 1 154 ? 19.157 -3.456  -26.727 1.00 18.28 ? 309  THR A N     1 
ATOM   1043 C  CA    . THR A 1 154 ? 18.669 -2.652  -25.606 1.00 17.01 ? 309  THR A CA    1 
ATOM   1044 C  C     . THR A 1 154 ? 18.266 -1.275  -26.114 1.00 23.91 ? 309  THR A C     1 
ATOM   1045 O  O     . THR A 1 154 ? 19.086 -0.566  -26.718 1.00 20.46 ? 309  THR A O     1 
ATOM   1046 C  CB    . THR A 1 154 ? 19.708 -2.533  -24.493 1.00 19.37 ? 309  THR A CB    1 
ATOM   1047 O  OG1   . THR A 1 154 ? 20.085 -3.849  -24.050 1.00 23.78 ? 309  THR A OG1   1 
ATOM   1048 C  CG2   . THR A 1 154 ? 19.158 -1.723  -23.297 1.00 21.03 ? 309  THR A CG2   1 
ATOM   1049 N  N     . LEU A 1 155 ? 17.015 -0.899  -25.850 1.00 18.30 ? 310  LEU A N     1 
ATOM   1050 C  CA    . LEU A 1 155 ? 16.450 0.388   -26.232 1.00 17.85 ? 310  LEU A CA    1 
ATOM   1051 C  C     . LEU A 1 155 ? 16.231 1.237   -24.998 1.00 24.58 ? 310  LEU A C     1 
ATOM   1052 O  O     . LEU A 1 155 ? 16.007 0.715   -23.905 1.00 22.81 ? 310  LEU A O     1 
ATOM   1053 C  CB    . LEU A 1 155 ? 15.106 0.205   -26.925 1.00 21.74 ? 310  LEU A CB    1 
ATOM   1054 C  CG    . LEU A 1 155 ? 15.208 -0.690  -28.166 1.00 20.63 ? 310  LEU A CG    1 
ATOM   1055 C  CD1   . LEU A 1 155 ? 13.867 -0.749  -28.844 1.00 23.61 ? 310  LEU A CD1   1 
ATOM   1056 C  CD2   . LEU A 1 155 ? 16.331 -0.223  -29.127 1.00 24.19 ? 310  LEU A CD2   1 
ATOM   1057 N  N     . LEU A 1 156 ? 16.305 2.552   -25.182 1.00 20.97 ? 311  LEU A N     1 
ATOM   1058 C  CA    . LEU A 1 156 ? 15.999 3.535   -24.148 1.00 20.84 ? 311  LEU A CA    1 
ATOM   1059 C  C     . LEU A 1 156 ? 14.863 4.401   -24.664 1.00 27.65 ? 311  LEU A C     1 
ATOM   1060 O  O     . LEU A 1 156 ? 15.019 5.085   -25.682 1.00 26.39 ? 311  LEU A O     1 
ATOM   1061 C  CB    . LEU A 1 156 ? 17.218 4.419   -23.853 1.00 25.10 ? 311  LEU A CB    1 
ATOM   1062 C  CG    . LEU A 1 156 ? 17.091 5.346   -22.641 1.00 30.66 ? 311  LEU A CG    1 
ATOM   1063 C  CD1   . LEU A 1 156 ? 16.629 4.638   -21.347 1.00 25.90 ? 311  LEU A CD1   1 
ATOM   1064 C  CD2   . LEU A 1 156 ? 18.378 6.175   -22.424 1.00 26.13 ? 311  LEU A CD2   1 
ATOM   1065 N  N     . ILE A 1 157 ? 13.724 4.361   -23.977 1.00 22.11 ? 312  ILE A N     1 
ATOM   1066 C  CA    . ILE A 1 157 ? 12.507 5.067   -24.399 1.00 20.19 ? 312  ILE A CA    1 
ATOM   1067 C  C     . ILE A 1 157 ? 12.416 6.339   -23.560 1.00 28.33 ? 312  ILE A C     1 
ATOM   1068 O  O     . ILE A 1 157 ? 12.464 6.281   -22.328 1.00 25.23 ? 312  ILE A O     1 
ATOM   1069 C  CB    . ILE A 1 157 ? 11.260 4.195   -24.167 1.00 24.58 ? 312  ILE A CB    1 
ATOM   1070 C  CG1   . ILE A 1 157 ? 11.352 2.855   -24.904 1.00 23.22 ? 312  ILE A CG1   1 
ATOM   1071 C  CG2   . ILE A 1 157 ? 9.962  4.979   -24.530 1.00 28.46 ? 312  ILE A CG2   1 
ATOM   1072 C  CD1   . ILE A 1 157 ? 10.192 1.883   -24.571 1.00 24.02 ? 312  ILE A CD1   1 
ATOM   1073 N  N     . SER A 1 158 ? 12.306 7.495   -24.217 1.00 28.11 ? 313  SER A N     1 
ATOM   1074 C  CA    . SER A 1 158 ? 12.096 8.778   -23.535 1.00 30.86 ? 313  SER A CA    1 
ATOM   1075 C  C     . SER A 1 158 ? 13.203 9.112   -22.540 1.00 32.94 ? 313  SER A C     1 
ATOM   1076 O  O     . SER A 1 158 ? 12.982 9.835   -21.569 1.00 38.80 ? 313  SER A O     1 
ATOM   1077 C  CB    . SER A 1 158 ? 10.716 8.849   -22.875 1.00 36.36 ? 313  SER A CB    1 
ATOM   1078 O  OG    . SER A 1 158 ? 9.711  8.565   -23.836 1.00 41.94 ? 313  SER A OG    1 
ATOM   1079 N  N     . GLU A 1 159 ? 14.410 8.614   -22.778 1.00 29.11 ? 314  GLU A N     1 
ATOM   1080 C  CA    . GLU A 1 159 ? 15.554 8.775   -21.889 1.00 28.38 ? 314  GLU A CA    1 
ATOM   1081 C  C     . GLU A 1 159 ? 15.355 8.157   -20.510 1.00 31.32 ? 314  GLU A C     1 
ATOM   1082 O  O     . GLU A 1 159 ? 16.185 8.386   -19.618 1.00 37.11 ? 314  GLU A O     1 
ATOM   1083 C  CB    . GLU A 1 159 ? 16.005 10.237  -21.750 1.00 31.45 ? 314  GLU A CB    1 
ATOM   1084 N  N     . LYS A 1 160 ? 14.286 7.368   -20.304 1.00 28.93 ? 315  LYS A N     1 
ATOM   1085 C  CA    . LYS A 1 160 ? 13.937 6.870   -18.974 1.00 29.38 ? 315  LYS A CA    1 
ATOM   1086 C  C     . LYS A 1 160 ? 13.801 5.365   -18.886 1.00 24.80 ? 315  LYS A C     1 
ATOM   1087 O  O     . LYS A 1 160 ? 14.225 4.787   -17.888 1.00 27.28 ? 315  LYS A O     1 
ATOM   1088 C  CB    . LYS A 1 160 ? 12.627 7.482   -18.446 1.00 35.62 ? 315  LYS A CB    1 
ATOM   1089 C  CG    . LYS A 1 160 ? 12.341 8.865   -18.969 1.00 52.34 ? 315  LYS A CG    1 
ATOM   1090 C  CD    . LYS A 1 160 ? 11.678 9.805   -17.956 1.00 60.91 ? 315  LYS A CD    1 
ATOM   1091 C  CE    . LYS A 1 160 ? 11.547 11.227  -18.541 1.00 57.03 ? 315  LYS A CE    1 
ATOM   1092 N  NZ    . LYS A 1 160 ? 11.027 11.236  -19.945 1.00 51.88 ? 315  LYS A NZ    1 
ATOM   1093 N  N     . ILE A 1 161 ? 13.158 4.719   -19.854 1.00 21.39 ? 316  ILE A N     1 
ATOM   1094 C  CA    . ILE A 1 161 ? 12.776 3.317   -19.701 1.00 19.79 ? 316  ILE A CA    1 
ATOM   1095 C  C     . ILE A 1 161 ? 13.680 2.473   -20.578 1.00 18.63 ? 316  ILE A C     1 
ATOM   1096 O  O     . ILE A 1 161 ? 13.690 2.641   -21.799 1.00 20.55 ? 316  ILE A O     1 
ATOM   1097 C  CB    . ILE A 1 161 ? 11.315 3.083   -20.093 1.00 19.86 ? 316  ILE A CB    1 
ATOM   1098 C  CG1   . ILE A 1 161 ? 10.410 4.017   -19.294 1.00 25.80 ? 316  ILE A CG1   1 
ATOM   1099 C  CG2   . ILE A 1 161 ? 10.994 1.559   -19.925 1.00 20.04 ? 316  ILE A CG2   1 
ATOM   1100 C  CD1   . ILE A 1 161 ? 8.971  3.892   -19.669 1.00 30.70 ? 316  ILE A CD1   1 
ATOM   1101 N  N     . SER A 1 162 ? 14.416 1.550   -19.975 1.00 17.40 ? 317  SER A N     1 
ATOM   1102 C  CA    . SER A 1 162 ? 15.236 0.647   -20.776 1.00 18.22 ? 317  SER A CA    1 
ATOM   1103 C  C     . SER A 1 162 ? 14.466 -0.626  -21.062 1.00 19.55 ? 317  SER A C     1 
ATOM   1104 O  O     . SER A 1 162 ? 13.791 -1.151  -20.180 1.00 18.68 ? 317  SER A O     1 
ATOM   1105 C  CB    . SER A 1 162 ? 16.505 0.274   -20.039 1.00 21.76 ? 317  SER A CB    1 
ATOM   1106 O  OG    . SER A 1 162 ? 17.334 1.405   -19.891 1.00 36.06 ? 317  SER A OG    1 
ATOM   1107 N  N     . VAL A 1 163 ? 14.620 -1.146  -22.267 1.00 17.69 ? 318  VAL A N     1 
ATOM   1108 C  CA    . VAL A 1 163 ? 13.948 -2.375  -22.690 1.00 16.16 ? 318  VAL A CA    1 
ATOM   1109 C  C     . VAL A 1 163 ? 14.986 -3.264  -23.335 1.00 17.98 ? 318  VAL A C     1 
ATOM   1110 O  O     . VAL A 1 163 ? 15.582 -2.888  -24.356 1.00 19.91 ? 318  VAL A O     1 
ATOM   1111 C  CB    . VAL A 1 163 ? 12.784 -2.137  -23.665 1.00 15.95 ? 318  VAL A CB    1 
ATOM   1112 C  CG1   . VAL A 1 163 ? 12.054 -3.417  -23.925 1.00 18.95 ? 318  VAL A CG1   1 
ATOM   1113 C  CG2   . VAL A 1 163 ? 11.804 -1.117  -23.095 1.00 18.33 ? 318  VAL A CG2   1 
ATOM   1114 N  N     . ASP A 1 164 ? 15.209 -4.448  -22.750 1.00 15.97 ? 319  ASP A N     1 
ATOM   1115 C  CA    . ASP A 1 164 ? 16.092 -5.451  -23.341 1.00 19.07 ? 319  ASP A CA    1 
ATOM   1116 C  C     . ASP A 1 164 ? 15.233 -6.370  -24.189 1.00 17.77 ? 319  ASP A C     1 
ATOM   1117 O  O     . ASP A 1 164 ? 14.301 -7.035  -23.679 1.00 18.13 ? 319  ASP A O     1 
ATOM   1118 C  CB    . ASP A 1 164 ? 16.744 -6.279  -22.242 1.00 16.43 ? 319  ASP A CB    1 
ATOM   1119 C  CG    . ASP A 1 164 ? 17.815 -5.517  -21.485 1.00 21.42 ? 319  ASP A CG    1 
ATOM   1120 O  OD1   . ASP A 1 164 ? 18.631 -4.815  -22.131 1.00 24.33 ? 319  ASP A OD1   1 
ATOM   1121 O  OD2   . ASP A 1 164 ? 17.868 -5.615  -20.246 1.00 16.69 ? 319  ASP A OD2   1 
ATOM   1122 N  N     . ILE A 1 165 ? 15.486 -6.375  -25.501 1.00 15.75 ? 320  ILE A N     1 
ATOM   1123 C  CA    . ILE A 1 165 ? 14.751 -7.179  -26.452 1.00 14.83 ? 320  ILE A CA    1 
ATOM   1124 C  C     . ILE A 1 165 ? 15.678 -8.282  -26.905 1.00 17.92 ? 320  ILE A C     1 
ATOM   1125 O  O     . ILE A 1 165 ? 16.675 -8.020  -27.601 1.00 18.78 ? 320  ILE A O     1 
ATOM   1126 C  CB    . ILE A 1 165 ? 14.284 -6.363  -27.648 1.00 18.31 ? 320  ILE A CB    1 
ATOM   1127 C  CG1   . ILE A 1 165 ? 13.447 -5.192  -27.151 1.00 21.05 ? 320  ILE A CG1   1 
ATOM   1128 C  CG2   . ILE A 1 165 ? 13.475 -7.240  -28.559 1.00 21.33 ? 320  ILE A CG2   1 
ATOM   1129 C  CD1   . ILE A 1 165 ? 12.978 -4.393  -28.323 1.00 23.15 ? 320  ILE A CD1   1 
ATOM   1130 N  N     . THR A 1 166 ? 15.332 -9.517  -26.592 1.00 15.09 ? 321  THR A N     1 
ATOM   1131 C  CA    . THR A 1 166 ? 16.258 -10.626 -26.824 1.00 15.18 ? 321  THR A CA    1 
ATOM   1132 C  C     . THR A 1 166 ? 15.643 -11.634 -27.777 1.00 15.63 ? 321  THR A C     1 
ATOM   1133 O  O     . THR A 1 166 ? 14.609 -12.230 -27.478 1.00 17.57 ? 321  THR A O     1 
ATOM   1134 C  CB    . THR A 1 166 ? 16.645 -11.275 -25.494 1.00 15.66 ? 321  THR A CB    1 
ATOM   1135 O  OG1   . THR A 1 166 ? 17.258 -10.257 -24.706 1.00 18.51 ? 321  THR A OG1   1 
ATOM   1136 C  CG2   . THR A 1 166 ? 17.643 -12.387 -25.708 1.00 16.03 ? 321  THR A CG2   1 
ATOM   1137 N  N     . LEU A 1 167 ? 16.299 -11.822 -28.920 1.00 15.79 ? 322  LEU A N     1 
ATOM   1138 C  CA    . LEU A 1 167 ? 15.948 -12.900 -29.811 1.00 17.85 ? 322  LEU A CA    1 
ATOM   1139 C  C     . LEU A 1 167 ? 16.155 -14.227 -29.082 1.00 16.92 ? 322  LEU A C     1 
ATOM   1140 O  O     . LEU A 1 167 ? 17.170 -14.441 -28.401 1.00 18.45 ? 322  LEU A O     1 
ATOM   1141 C  CB    . LEU A 1 167 ? 16.865 -12.804 -31.038 1.00 19.79 ? 322  LEU A CB    1 
ATOM   1142 C  CG    . LEU A 1 167 ? 16.723 -13.982 -31.996 1.00 20.08 ? 322  LEU A CG    1 
ATOM   1143 C  CD1   . LEU A 1 167 ? 15.340 -14.020 -32.726 1.00 20.28 ? 322  LEU A CD1   1 
ATOM   1144 C  CD2   . LEU A 1 167 ? 17.863 -13.886 -33.038 1.00 22.04 ? 322  LEU A CD2   1 
ATOM   1145 N  N     . ALA A 1 168 ? 15.192 -15.123 -29.196 1.00 17.84 ? 323  ALA A N     1 
ATOM   1146 C  CA    . ALA A 1 168 ? 15.289 -16.397 -28.502 1.00 19.61 ? 323  ALA A CA    1 
ATOM   1147 C  C     . ALA A 1 168 ? 14.737 -17.499 -29.386 1.00 22.15 ? 323  ALA A C     1 
ATOM   1148 O  O     . ALA A 1 168 ? 13.602 -17.405 -29.862 1.00 28.13 ? 323  ALA A O     1 
ATOM   1149 C  CB    . ALA A 1 168 ? 14.582 -16.355 -27.142 1.00 21.09 ? 323  ALA A CB    1 
ATOM   1150 N  N     . LEU A 1 169 ? 15.541 -18.535 -29.618 1.00 18.44 ? 324  LEU A N     1 
ATOM   1151 C  CA    . LEU A 1 169 ? 15.044 -19.705 -30.315 1.00 20.29 ? 324  LEU A CA    1 
ATOM   1152 C  C     . LEU A 1 169 ? 14.289 -20.556 -29.316 1.00 18.69 ? 324  LEU A C     1 
ATOM   1153 O  O     . LEU A 1 169 ? 14.788 -20.817 -28.218 1.00 20.64 ? 324  LEU A O     1 
ATOM   1154 C  CB    . LEU A 1 169 ? 16.192 -20.547 -30.853 1.00 19.06 ? 324  LEU A CB    1 
ATOM   1155 C  CG    . LEU A 1 169 ? 17.166 -19.778 -31.728 1.00 25.67 ? 324  LEU A CG    1 
ATOM   1156 C  CD1   . LEU A 1 169 ? 18.223 -20.785 -32.247 1.00 21.67 ? 324  LEU A CD1   1 
ATOM   1157 C  CD2   . LEU A 1 169 ? 16.474 -19.081 -32.880 1.00 24.39 ? 324  LEU A CD2   1 
ATOM   1158 N  N     . GLU A 1 170 ? 13.110 -21.013 -29.692 1.00 19.45 ? 325  GLU A N     1 
ATOM   1159 C  CA    . GLU A 1 170 ? 12.295 -21.849 -28.833 1.00 19.67 ? 325  GLU A CA    1 
ATOM   1160 C  C     . GLU A 1 170 ? 12.415 -23.279 -29.318 1.00 25.81 ? 325  GLU A C     1 
ATOM   1161 O  O     . GLU A 1 170 ? 12.164 -23.559 -30.497 1.00 26.86 ? 325  GLU A O     1 
ATOM   1162 C  CB    . GLU A 1 170 ? 10.851 -21.410 -28.953 1.00 22.23 ? 325  GLU A CB    1 
ATOM   1163 C  CG    . GLU A 1 170 ? 9.909  -22.201 -28.084 1.00 21.36 ? 325  GLU A CG    1 
ATOM   1164 C  CD    . GLU A 1 170 ? 8.490  -21.652 -28.152 1.00 36.66 ? 325  GLU A CD    1 
ATOM   1165 O  OE1   . GLU A 1 170 ? 7.846  -21.846 -29.202 1.00 44.85 ? 325  GLU A OE1   1 
ATOM   1166 O  OE2   . GLU A 1 170 ? 8.044  -21.012 -27.172 1.00 27.15 ? 325  GLU A OE2   1 
ATOM   1167 N  N     . SER A 1 171 ? 12.752 -24.187 -28.426 1.00 20.19 ? 326  SER A N     1 
ATOM   1168 C  CA    . SER A 1 171 ? 12.826 -25.590 -28.788 1.00 19.59 ? 326  SER A CA    1 
ATOM   1169 C  C     . SER A 1 171 ? 11.856 -26.352 -27.911 1.00 23.02 ? 326  SER A C     1 
ATOM   1170 O  O     . SER A 1 171 ? 11.930 -26.270 -26.679 1.00 22.43 ? 326  SER A O     1 
ATOM   1171 C  CB    . SER A 1 171 ? 14.235 -26.116 -28.615 1.00 26.10 ? 326  SER A CB    1 
ATOM   1172 O  OG    . SER A 1 171 ? 14.268 -27.525 -28.803 1.00 31.39 ? 326  SER A OG    1 
ATOM   1173 N  N     . LYS A 1 172 ? 10.959 -27.104 -28.529 1.00 25.28 ? 327  LYS A N     1 
ATOM   1174 C  CA    . LYS A 1 172 ? 9.997  -27.893 -27.772 1.00 26.21 ? 327  LYS A CA    1 
ATOM   1175 C  C     . LYS A 1 172 ? 10.498 -29.283 -27.435 1.00 29.57 ? 327  LYS A C     1 
ATOM   1176 O  O     . LYS A 1 172 ? 9.704  -30.122 -26.996 1.00 40.00 ? 327  LYS A O     1 
ATOM   1177 C  CB    . LYS A 1 172 ? 8.657  -27.953 -28.502 1.00 29.47 ? 327  LYS A CB    1 
ATOM   1178 C  CG    . LYS A 1 172 ? 8.043  -26.591 -28.650 1.00 33.39 ? 327  LYS A CG    1 
ATOM   1179 C  CD    . LYS A 1 172 ? 6.682  -26.662 -29.326 1.00 42.77 ? 327  LYS A CD    1 
ATOM   1180 C  CE    . LYS A 1 172 ? 5.948  -25.324 -29.284 1.00 55.17 ? 327  LYS A CE    1 
ATOM   1181 N  NZ    . LYS A 1 172 ? 4.616  -25.386 -29.958 1.00 66.80 ? 327  LYS A NZ    1 
ATOM   1182 N  N     . SER A 1 173 ? 11.783 -29.540 -27.607 1.00 27.33 ? 328  SER A N     1 
ATOM   1183 C  CA    . SER A 1 173 ? 12.328 -30.842 -27.285 1.00 26.07 ? 328  SER A CA    1 
ATOM   1184 C  C     . SER A 1 173 ? 12.684 -30.907 -25.795 1.00 26.23 ? 328  SER A C     1 
ATOM   1185 O  O     . SER A 1 173 ? 12.638 -29.909 -25.064 1.00 24.86 ? 328  SER A O     1 
ATOM   1186 C  CB    . SER A 1 173 ? 13.580 -31.112 -28.116 1.00 34.46 ? 328  SER A CB    1 
ATOM   1187 O  OG    . SER A 1 173 ? 13.401 -30.712 -29.464 1.00 46.97 ? 328  SER A OG    1 
ATOM   1188 N  N     . SER A 1 174 ? 13.071 -32.101 -25.358 1.00 26.66 ? 329  SER A N     1 
ATOM   1189 C  CA    . SER A 1 174 ? 13.518 -32.292 -23.991 1.00 24.38 ? 329  SER A CA    1 
ATOM   1190 C  C     . SER A 1 174 ? 14.709 -31.390 -23.671 1.00 20.52 ? 329  SER A C     1 
ATOM   1191 O  O     . SER A 1 174 ? 15.572 -31.114 -24.513 1.00 21.99 ? 329  SER A O     1 
ATOM   1192 C  CB    . SER A 1 174 ? 13.903 -33.749 -23.763 1.00 30.13 ? 329  SER A CB    1 
ATOM   1193 O  OG    . SER A 1 174 ? 12.865 -34.583 -24.215 1.00 42.93 ? 329  SER A OG    1 
ATOM   1194 N  N     . TRP A 1 175 ? 14.764 -30.953 -22.419 1.00 21.40 ? 330  TRP A N     1 
ATOM   1195 C  CA    . TRP A 1 175 ? 15.836 -30.055 -22.033 1.00 20.51 ? 330  TRP A CA    1 
ATOM   1196 C  C     . TRP A 1 175 ? 17.202 -30.743 -22.141 1.00 21.30 ? 330  TRP A C     1 
ATOM   1197 O  O     . TRP A 1 175 ? 17.321 -31.980 -22.000 1.00 20.63 ? 330  TRP A O     1 
ATOM   1198 C  CB    . TRP A 1 175 ? 15.598 -29.611 -20.590 1.00 20.41 ? 330  TRP A CB    1 
ATOM   1199 C  CG    . TRP A 1 175 ? 14.382 -28.736 -20.386 1.00 19.93 ? 330  TRP A CG    1 
ATOM   1200 C  CD1   . TRP A 1 175 ? 13.359 -28.439 -21.280 1.00 19.16 ? 330  TRP A CD1   1 
ATOM   1201 C  CD2   . TRP A 1 175 ? 14.094 -28.035 -19.200 1.00 20.51 ? 330  TRP A CD2   1 
ATOM   1202 N  NE1   . TRP A 1 175 ? 12.437 -27.593 -20.671 1.00 18.19 ? 330  TRP A NE1   1 
ATOM   1203 C  CE2   . TRP A 1 175 ? 12.882 -27.328 -19.404 1.00 17.51 ? 330  TRP A CE2   1 
ATOM   1204 C  CE3   . TRP A 1 175 ? 14.734 -27.945 -17.966 1.00 16.57 ? 330  TRP A CE3   1 
ATOM   1205 C  CZ2   . TRP A 1 175 ? 12.298 -26.541 -18.414 1.00 18.13 ? 330  TRP A CZ2   1 
ATOM   1206 C  CZ3   . TRP A 1 175 ? 14.170 -27.138 -16.993 1.00 17.48 ? 330  TRP A CZ3   1 
ATOM   1207 C  CH2   . TRP A 1 175 ? 12.947 -26.466 -17.220 1.00 16.19 ? 330  TRP A CH2   1 
ATOM   1208 N  N     . PRO A 1 176 ? 18.251 -29.972 -22.380 1.00 19.29 ? 331  PRO A N     1 
ATOM   1209 C  CA    . PRO A 1 176 ? 19.581 -30.577 -22.545 1.00 18.91 ? 331  PRO A CA    1 
ATOM   1210 C  C     . PRO A 1 176 ? 20.040 -31.296 -21.295 1.00 21.37 ? 331  PRO A C     1 
ATOM   1211 O  O     . PRO A 1 176 ? 19.619 -31.000 -20.169 1.00 21.36 ? 331  PRO A O     1 
ATOM   1212 C  CB    . PRO A 1 176 ? 20.486 -29.377 -22.861 1.00 22.52 ? 331  PRO A CB    1 
ATOM   1213 C  CG    . PRO A 1 176 ? 19.563 -28.382 -23.508 1.00 22.82 ? 331  PRO A CG    1 
ATOM   1214 C  CD    . PRO A 1 176 ? 18.250 -28.553 -22.775 1.00 20.29 ? 331  PRO A CD    1 
ATOM   1215 N  N     . ALA A 1 177 ? 20.988 -32.233 -21.484 1.00 21.12 ? 332  ALA A N     1 
ATOM   1216 C  CA    . ALA A 1 177 ? 21.441 -33.076 -20.380 1.00 23.45 ? 332  ALA A CA    1 
ATOM   1217 C  C     . ALA A 1 177 ? 22.049 -32.297 -19.220 1.00 19.84 ? 332  ALA A C     1 
ATOM   1218 O  O     . ALA A 1 177 ? 21.998 -32.771 -18.069 1.00 20.86 ? 332  ALA A O     1 
ATOM   1219 C  CB    . ALA A 1 177 ? 22.485 -34.069 -20.876 1.00 26.76 ? 332  ALA A CB    1 
ATOM   1220 N  N     . SER A 1 178 ? 22.657 -31.137 -19.498 1.00 21.75 ? 333  SER A N     1 
ATOM   1221 C  CA    . SER A 1 178 ? 23.222 -30.321 -18.433 1.00 18.37 ? 333  SER A CA    1 
ATOM   1222 C  C     . SER A 1 178 ? 22.173 -29.897 -17.397 1.00 17.63 ? 333  SER A C     1 
ATOM   1223 O  O     . SER A 1 178 ? 22.548 -29.445 -16.321 1.00 17.87 ? 333  SER A O     1 
ATOM   1224 C  CB    . SER A 1 178 ? 23.939 -29.092 -18.999 1.00 20.30 ? 333  SER A CB    1 
ATOM   1225 O  OG    . SER A 1 178 ? 22.975 -28.236 -19.591 1.00 20.11 ? 333  SER A OG    1 
ATOM   1226 N  N     . THR A 1 179 ? 20.895 -30.007 -17.709 1.00 16.65 ? 334  THR A N     1 
ATOM   1227 C  CA    . THR A 1 179 ? 19.835 -29.643 -16.772 1.00 17.26 ? 334  THR A CA    1 
ATOM   1228 C  C     . THR A 1 179 ? 19.259 -30.812 -15.985 1.00 18.15 ? 334  THR A C     1 
ATOM   1229 O  O     . THR A 1 179 ? 18.377 -30.595 -15.150 1.00 19.96 ? 334  THR A O     1 
ATOM   1230 C  CB    . THR A 1 179 ? 18.665 -28.953 -17.474 1.00 17.48 ? 334  THR A CB    1 
ATOM   1231 O  OG1   . THR A 1 179 ? 17.943 -29.934 -18.253 1.00 19.11 ? 334  THR A OG1   1 
ATOM   1232 C  CG2   . THR A 1 179 ? 19.078 -27.843 -18.308 1.00 16.42 ? 334  THR A CG2   1 
ATOM   1233 N  N     . GLN A 1 180 ? 19.755 -32.037 -16.197 1.00 19.77 ? 335  GLN A N     1 
ATOM   1234 C  CA    . GLN A 1 180 ? 19.114 -33.218 -15.616 1.00 23.99 ? 335  GLN A CA    1 
ATOM   1235 C  C     . GLN A 1 180 ? 18.946 -33.129 -14.101 1.00 24.23 ? 335  GLN A C     1 
ATOM   1236 O  O     . GLN A 1 180 ? 17.909 -33.546 -13.568 1.00 25.96 ? 335  GLN A O     1 
ATOM   1237 C  CB    . GLN A 1 180 ? 19.927 -34.460 -15.985 1.00 29.21 ? 335  GLN A CB    1 
ATOM   1238 C  CG    . GLN A 1 180 ? 19.414 -35.736 -15.352 1.00 39.71 ? 335  GLN A CG    1 
ATOM   1239 C  CD    . GLN A 1 180 ? 18.100 -36.215 -15.940 1.00 54.83 ? 335  GLN A CD    1 
ATOM   1240 O  OE1   . GLN A 1 180 ? 17.675 -35.771 -17.012 1.00 55.81 ? 335  GLN A OE1   1 
ATOM   1241 N  NE2   . GLN A 1 180 ? 17.454 -37.149 -15.245 1.00 60.53 ? 335  GLN A NE2   1 
ATOM   1242 N  N     A GLU A 1 181 ? 19.949 -32.601 -13.392 0.44 21.89 ? 336  GLU A N     1 
ATOM   1243 N  N     B GLU A 1 181 ? 19.951 -32.606 -13.391 0.56 21.86 ? 336  GLU A N     1 
ATOM   1244 C  CA    A GLU A 1 181 ? 19.895 -32.479 -11.939 0.44 22.00 ? 336  GLU A CA    1 
ATOM   1245 C  CA    B GLU A 1 181 ? 19.900 -32.477 -11.939 0.56 21.96 ? 336  GLU A CA    1 
ATOM   1246 C  C     A GLU A 1 181 ? 19.565 -31.070 -11.467 0.44 22.76 ? 336  GLU A C     1 
ATOM   1247 C  C     B GLU A 1 181 ? 19.567 -31.069 -11.466 0.56 22.75 ? 336  GLU A C     1 
ATOM   1248 O  O     A GLU A 1 181 ? 19.701 -30.785 -10.275 0.44 24.18 ? 336  GLU A O     1 
ATOM   1249 O  O     B GLU A 1 181 ? 19.698 -30.786 -10.275 0.56 24.15 ? 336  GLU A O     1 
ATOM   1250 C  CB    A GLU A 1 181 ? 21.210 -32.934 -11.302 0.44 25.59 ? 336  GLU A CB    1 
ATOM   1251 C  CB    B GLU A 1 181 ? 21.222 -32.931 -11.310 0.56 25.56 ? 336  GLU A CB    1 
ATOM   1252 C  CG    A GLU A 1 181 ? 21.617 -34.342 -11.677 0.44 31.29 ? 336  GLU A CG    1 
ATOM   1253 C  CG    B GLU A 1 181 ? 21.646 -34.329 -11.714 0.56 31.29 ? 336  GLU A CG    1 
ATOM   1254 C  CD    A GLU A 1 181 ? 22.779 -34.845 -10.852 0.44 35.86 ? 336  GLU A CD    1 
ATOM   1255 C  CD    B GLU A 1 181 ? 20.603 -35.382 -11.367 0.56 33.47 ? 336  GLU A CD    1 
ATOM   1256 O  OE1   A GLU A 1 181 ? 22.670 -34.842 -9.604  0.44 40.83 ? 336  GLU A OE1   1 
ATOM   1257 O  OE1   B GLU A 1 181 ? 19.938 -35.266 -10.306 0.56 37.98 ? 336  GLU A OE1   1 
ATOM   1258 O  OE2   A GLU A 1 181 ? 23.807 -35.224 -11.449 0.44 39.44 ? 336  GLU A OE2   1 
ATOM   1259 O  OE2   B GLU A 1 181 ? 20.451 -36.336 -12.157 0.56 38.20 ? 336  GLU A OE2   1 
ATOM   1260 N  N     . GLY A 1 182 ? 19.149 -30.185 -12.371 1.00 19.09 ? 337  GLY A N     1 
ATOM   1261 C  CA    . GLY A 1 182 ? 18.761 -28.840 -11.999 1.00 18.09 ? 337  GLY A CA    1 
ATOM   1262 C  C     . GLY A 1 182 ? 17.316 -28.772 -11.560 1.00 18.82 ? 337  GLY A C     1 
ATOM   1263 O  O     . GLY A 1 182 ? 16.589 -29.765 -11.490 1.00 18.55 ? 337  GLY A O     1 
ATOM   1264 N  N     . LEU A 1 183 ? 16.878 -27.552 -11.279 1.00 14.99 ? 338  LEU A N     1 
ATOM   1265 C  CA    . LEU A 1 183 ? 15.456 -27.334 -10.954 1.00 16.75 ? 338  LEU A CA    1 
ATOM   1266 C  C     . LEU A 1 183 ? 15.002 -28.231 -9.802  1.00 15.26 ? 338  LEU A C     1 
ATOM   1267 O  O     . LEU A 1 183 ? 14.016 -28.962 -9.899  1.00 17.05 ? 338  LEU A O     1 
ATOM   1268 C  CB    . LEU A 1 183 ? 14.543 -27.485 -12.199 1.00 15.38 ? 338  LEU A CB    1 
ATOM   1269 C  CG    . LEU A 1 183 ? 13.134 -26.872 -12.063 1.00 16.39 ? 338  LEU A CG    1 
ATOM   1270 C  CD1   . LEU A 1 183 ? 13.117 -25.373 -11.810 1.00 17.59 ? 338  LEU A CD1   1 
ATOM   1271 C  CD2   . LEU A 1 183 ? 12.382 -27.212 -13.353 1.00 19.43 ? 338  LEU A CD2   1 
ATOM   1272 N  N     . ARG A 1 184 ? 15.744 -28.180 -8.695  1.00 17.91 ? 339  ARG A N     1 
ATOM   1273 C  CA    . ARG A 1 184 ? 15.512 -29.095 -7.575  1.00 17.09 ? 339  ARG A CA    1 
ATOM   1274 C  C     . ARG A 1 184 ? 14.402 -28.592 -6.670  1.00 15.68 ? 339  ARG A C     1 
ATOM   1275 O  O     . ARG A 1 184 ? 14.593 -28.306 -5.492  1.00 19.69 ? 339  ARG A O     1 
ATOM   1276 C  CB    . ARG A 1 184 ? 16.797 -29.342 -6.786  1.00 21.39 ? 339  ARG A CB    1 
ATOM   1277 C  CG    . ARG A 1 184 ? 17.867 -30.006 -7.582  1.00 34.47 ? 339  ARG A CG    1 
ATOM   1278 C  CD    . ARG A 1 184 ? 18.969 -30.514 -6.658  1.00 51.10 ? 339  ARG A CD    1 
ATOM   1279 N  NE    . ARG A 1 184 ? 19.671 -31.635 -7.266  1.00 57.77 ? 339  ARG A NE    1 
ATOM   1280 C  CZ    . ARG A 1 184 ? 19.214 -32.879 -7.290  1.00 59.50 ? 339  ARG A CZ    1 
ATOM   1281 N  NH1   . ARG A 1 184 ? 18.056 -33.204 -6.726  1.00 54.77 ? 339  ARG A NH1   1 
ATOM   1282 N  NH2   . ARG A 1 184 ? 19.924 -33.818 -7.913  1.00 53.76 ? 339  ARG A NH2   1 
ATOM   1283 N  N     . ILE A 1 185 ? 13.200 -28.522 -7.248  1.00 15.23 ? 340  ILE A N     1 
ATOM   1284 C  CA    . ILE A 1 185 ? 12.053 -27.924 -6.573  1.00 14.49 ? 340  ILE A CA    1 
ATOM   1285 C  C     . ILE A 1 185 ? 11.117 -28.948 -5.948  1.00 16.19 ? 340  ILE A C     1 
ATOM   1286 O  O     . ILE A 1 185 ? 10.059 -28.567 -5.421  1.00 16.02 ? 340  ILE A O     1 
ATOM   1287 C  CB    . ILE A 1 185 ? 11.264 -27.036 -7.554  1.00 15.95 ? 340  ILE A CB    1 
ATOM   1288 C  CG1   . ILE A 1 185 ? 10.646 -27.920 -8.668  1.00 14.48 ? 340  ILE A CG1   1 
ATOM   1289 C  CG2   . ILE A 1 185 ? 12.156 -25.940 -8.111  1.00 17.12 ? 340  ILE A CG2   1 
ATOM   1290 C  CD1   . ILE A 1 185 ? 9.841  -27.188 -9.655  1.00 16.98 ? 340  ILE A CD1   1 
ATOM   1291 N  N     . GLN A 1 186 ? 11.437 -30.231 -6.037  1.00 15.37 ? 341  GLN A N     1 
ATOM   1292 C  CA    . GLN A 1 186 ? 10.471 -31.273 -5.660  1.00 16.80 ? 341  GLN A CA    1 
ATOM   1293 C  C     . GLN A 1 186 ? 9.963  -31.158 -4.223  1.00 17.50 ? 341  GLN A C     1 
ATOM   1294 O  O     . GLN A 1 186 ? 8.795  -31.500 -3.959  1.00 21.19 ? 341  GLN A O     1 
ATOM   1295 C  CB    . GLN A 1 186 ? 11.075 -32.658 -5.901  1.00 20.51 ? 341  GLN A CB    1 
ATOM   1296 C  CG    . GLN A 1 186 ? 11.503 -32.884 -7.313  1.00 31.10 ? 341  GLN A CG    1 
ATOM   1297 C  CD    . GLN A 1 186 ? 12.983 -32.679 -7.540  1.00 38.12 ? 341  GLN A CD    1 
ATOM   1298 O  OE1   . GLN A 1 186 ? 13.569 -31.742 -7.007  1.00 21.60 ? 341  GLN A OE1   1 
ATOM   1299 N  NE2   . GLN A 1 186 ? 13.595 -33.559 -8.335  1.00 32.78 ? 341  GLN A NE2   1 
ATOM   1300 N  N     . ASN A 1 187 ? 10.805 -30.778 -3.264  1.00 16.50 ? 342  ASN A N     1 
ATOM   1301 C  CA    . ASN A 1 187 ? 10.350 -30.666 -1.879  1.00 16.57 ? 342  ASN A CA    1 
ATOM   1302 C  C     . ASN A 1 187 ? 9.622  -29.359 -1.591  1.00 16.88 ? 342  ASN A C     1 
ATOM   1303 O  O     . ASN A 1 187 ? 9.026  -29.202 -0.525  1.00 18.11 ? 342  ASN A O     1 
ATOM   1304 C  CB    . ASN A 1 187 ? 11.512 -30.837 -0.892  1.00 24.22 ? 342  ASN A CB    1 
ATOM   1305 C  CG    . ASN A 1 187 ? 12.138 -32.207 -0.956  1.00 32.48 ? 342  ASN A CG    1 
ATOM   1306 O  OD1   . ASN A 1 187 ? 11.470 -33.188 -1.279  1.00 35.98 ? 342  ASN A OD1   1 
ATOM   1307 N  ND2   . ASN A 1 187 ? 13.433 -32.286 -0.656  1.00 41.21 ? 342  ASN A ND2   1 
ATOM   1308 N  N     . TRP A 1 188 ? 9.640  -28.409 -2.531  1.00 16.26 ? 343  TRP A N     1 
ATOM   1309 C  CA    . TRP A 1 188 ? 9.058  -27.104 -2.358  1.00 14.07 ? 343  TRP A CA    1 
ATOM   1310 C  C     . TRP A 1 188 ? 7.804  -26.963 -3.208  1.00 15.55 ? 343  TRP A C     1 
ATOM   1311 O  O     . TRP A 1 188 ? 6.691  -26.903 -2.666  1.00 15.72 ? 343  TRP A O     1 
ATOM   1312 C  CB    . TRP A 1 188 ? 10.122 -26.059 -2.706  1.00 15.35 ? 343  TRP A CB    1 
ATOM   1313 C  CG    . TRP A 1 188 ? 9.660  -24.647 -2.969  1.00 13.63 ? 343  TRP A CG    1 
ATOM   1314 C  CD1   . TRP A 1 188 ? 8.591  -24.003 -2.437  1.00 14.20 ? 343  TRP A CD1   1 
ATOM   1315 C  CD2   . TRP A 1 188 ? 10.331 -23.721 -3.819  1.00 13.36 ? 343  TRP A CD2   1 
ATOM   1316 N  NE1   . TRP A 1 188 ? 8.538  -22.700 -2.915  1.00 14.50 ? 343  TRP A NE1   1 
ATOM   1317 C  CE2   . TRP A 1 188 ? 9.574  -22.525 -3.804  1.00 15.11 ? 343  TRP A CE2   1 
ATOM   1318 C  CE3   . TRP A 1 188 ? 11.464 -23.811 -4.652  1.00 15.27 ? 343  TRP A CE3   1 
ATOM   1319 C  CZ2   . TRP A 1 188 ? 9.923  -21.408 -4.557  1.00 15.12 ? 343  TRP A CZ2   1 
ATOM   1320 C  CZ3   . TRP A 1 188 ? 11.823 -22.673 -5.407  1.00 17.63 ? 343  TRP A CZ3   1 
ATOM   1321 C  CH2   . TRP A 1 188 ? 11.037 -21.501 -5.357  1.00 14.45 ? 343  TRP A CH2   1 
ATOM   1322 N  N     . LEU A 1 189 ? 7.949  -26.990 -4.529  1.00 15.39 ? 344  LEU A N     1 
ATOM   1323 C  CA    . LEU A 1 189 ? 6.826  -26.836 -5.462  1.00 13.97 ? 344  LEU A CA    1 
ATOM   1324 C  C     . LEU A 1 189 ? 6.232  -28.149 -5.935  1.00 15.51 ? 344  LEU A C     1 
ATOM   1325 O  O     . LEU A 1 189 ? 5.182  -28.101 -6.594  1.00 14.27 ? 344  LEU A O     1 
ATOM   1326 C  CB    . LEU A 1 189 ? 7.246  -26.025 -6.667  1.00 13.83 ? 344  LEU A CB    1 
ATOM   1327 C  CG    . LEU A 1 189 ? 7.785  -24.629 -6.314  1.00 13.48 ? 344  LEU A CG    1 
ATOM   1328 C  CD1   . LEU A 1 189 ? 8.341  -23.957 -7.589  1.00 15.83 ? 344  LEU A CD1   1 
ATOM   1329 C  CD2   . LEU A 1 189 ? 6.681  -23.754 -5.682  1.00 14.34 ? 344  LEU A CD2   1 
ATOM   1330 N  N     . SER A 1 190 ? 6.889  -29.261 -5.650  1.00 15.12 ? 345  SER A N     1 
ATOM   1331 C  CA    . SER A 1 190 ? 6.465  -30.629 -6.041  1.00 15.42 ? 345  SER A CA    1 
ATOM   1332 C  C     . SER A 1 190 ? 7.149  -31.290 -7.210  1.00 15.07 ? 345  SER A C     1 
ATOM   1333 O  O     . SER A 1 190 ? 7.613  -30.633 -8.098  1.00 15.38 ? 345  SER A O     1 
ATOM   1334 C  CB    . SER A 1 190 ? 4.931  -30.834 -6.165  1.00 15.57 ? 345  SER A CB    1 
ATOM   1335 O  OG    . SER A 1 190 ? 4.467  -30.443 -7.424  1.00 15.29 ? 345  SER A OG    1 
ATOM   1336 N  N     . ALA A 1 191 ? 7.235  -32.602 -7.150  1.00 17.10 ? 346  ALA A N     1 
ATOM   1337 C  CA    . ALA A 1 191 ? 7.739  -33.378 -8.265  1.00 17.35 ? 346  ALA A CA    1 
ATOM   1338 C  C     . ALA A 1 191 ? 6.821  -33.274 -9.488  1.00 15.23 ? 346  ALA A C     1 
ATOM   1339 O  O     . ALA A 1 191 ? 7.270  -33.259 -10.601 1.00 17.77 ? 346  ALA A O     1 
ATOM   1340 C  CB    . ALA A 1 191 ? 7.880  -34.824 -7.840  1.00 22.61 ? 346  ALA A CB    1 
ATOM   1341 N  N     . LYS A 1 192 ? 5.516  -33.221 -9.244  1.00 16.18 ? 347  LYS A N     1 
ATOM   1342 C  CA    . LYS A 1 192 ? 4.588  -33.052 -10.361 1.00 17.39 ? 347  LYS A CA    1 
ATOM   1343 C  C     . LYS A 1 192 ? 4.789  -31.738 -11.101 1.00 16.34 ? 347  LYS A C     1 
ATOM   1344 O  O     . LYS A 1 192 ? 4.706  -31.694 -12.290 1.00 18.96 ? 347  LYS A O     1 
ATOM   1345 C  CB    . LYS A 1 192 ? 3.119  -33.344 -9.966  1.00 25.31 ? 347  LYS A CB    1 
ATOM   1346 C  CG    . LYS A 1 192 ? 2.465  -32.467 -8.934  1.00 27.01 ? 347  LYS A CG    1 
ATOM   1347 C  CD    . LYS A 1 192 ? 1.061  -32.985 -8.633  1.00 26.01 ? 347  LYS A CD    1 
ATOM   1348 C  CE    . LYS A 1 192 ? 1.100  -34.391 -8.064  1.00 25.13 ? 347  LYS A CE    1 
ATOM   1349 N  NZ    . LYS A 1 192 ? -0.214 -34.827 -7.516  1.00 31.08 ? 347  LYS A NZ    1 
ATOM   1350 N  N     . VAL A 1 193 ? 5.061  -30.676 -10.355 1.00 16.98 ? 348  VAL A N     1 
ATOM   1351 C  CA    . VAL A 1 193 ? 5.355  -29.404 -10.977 1.00 16.63 ? 348  VAL A CA    1 
ATOM   1352 C  C     . VAL A 1 193 ? 6.685  -29.449 -11.723 1.00 14.38 ? 348  VAL A C     1 
ATOM   1353 O  O     . VAL A 1 193 ? 6.783  -28.970 -12.810 1.00 15.20 ? 348  VAL A O     1 
ATOM   1354 C  CB    . VAL A 1 193 ? 5.354  -28.269 -9.941  1.00 16.13 ? 348  VAL A CB    1 
ATOM   1355 C  CG1   . VAL A 1 193 ? 5.927  -26.984 -10.506 1.00 14.90 ? 348  VAL A CG1   1 
ATOM   1356 C  CG2   . VAL A 1 193 ? 3.925  -28.012 -9.492  1.00 15.63 ? 348  VAL A CG2   1 
ATOM   1357 N  N     . ARG A 1 194 ? 7.679  -30.055 -11.108 1.00 14.61 ? 349  ARG A N     1 
ATOM   1358 C  CA    . ARG A 1 194 ? 8.956  -30.180 -11.829 1.00 16.06 ? 349  ARG A CA    1 
ATOM   1359 C  C     . ARG A 1 194 ? 8.765  -30.887 -13.164 1.00 17.37 ? 349  ARG A C     1 
ATOM   1360 O  O     . ARG A 1 194 ? 9.281  -30.431 -14.187 1.00 15.90 ? 349  ARG A O     1 
ATOM   1361 C  CB    . ARG A 1 194 ? 9.991  -30.915 -11.002 1.00 15.36 ? 349  ARG A CB    1 
ATOM   1362 C  CG    . ARG A 1 194 ? 11.404 -30.749 -11.592 1.00 16.14 ? 349  ARG A CG    1 
ATOM   1363 C  CD    . ARG A 1 194 ? 12.438 -31.557 -10.816 1.00 18.48 ? 349  ARG A CD    1 
ATOM   1364 N  NE    . ARG A 1 194 ? 13.796 -31.472 -11.395 1.00 20.61 ? 349  ARG A NE    1 
ATOM   1365 C  CZ    . ARG A 1 194 ? 14.383 -32.312 -12.254 1.00 25.47 ? 349  ARG A CZ    1 
ATOM   1366 N  NH1   . ARG A 1 194 ? 13.773 -33.406 -12.718 1.00 24.29 ? 349  ARG A NH1   1 
ATOM   1367 N  NH2   . ARG A 1 194 ? 15.638 -32.057 -12.649 1.00 22.86 ? 349  ARG A NH2   1 
ATOM   1368 N  N     . LYS A 1 195 ? 8.001  -31.981 -13.172 1.00 15.84 ? 350  LYS A N     1 
ATOM   1369 C  CA    . LYS A 1 195 ? 7.740  -32.677 -14.436 1.00 17.36 ? 350  LYS A CA    1 
ATOM   1370 C  C     . LYS A 1 195 ? 6.970  -31.800 -15.425 1.00 18.31 ? 350  LYS A C     1 
ATOM   1371 O  O     . LYS A 1 195 ? 7.310  -31.751 -16.620 1.00 19.60 ? 350  LYS A O     1 
ATOM   1372 C  CB    . LYS A 1 195 ? 7.020  -33.984 -14.095 1.00 25.12 ? 350  LYS A CB    1 
ATOM   1373 C  CG    . LYS A 1 195 ? 6.586  -34.793 -15.291 1.00 34.99 ? 350  LYS A CG    1 
ATOM   1374 C  CD    . LYS A 1 195 ? 6.186  -36.216 -14.879 1.00 38.28 ? 350  LYS A CD    1 
ATOM   1375 C  CE    . LYS A 1 195 ? 5.358  -36.896 -15.985 1.00 51.16 ? 350  LYS A CE    1 
ATOM   1376 N  NZ    . LYS A 1 195 ? 5.182  -36.070 -17.221 1.00 43.66 ? 350  LYS A NZ    1 
ATOM   1377 N  N     . GLN A 1 196 ? 5.976  -31.038 -14.951 1.00 16.60 ? 351  GLN A N     1 
ATOM   1378 C  CA    . GLN A 1 196 ? 5.252  -30.138 -15.843 1.00 18.80 ? 351  GLN A CA    1 
ATOM   1379 C  C     . GLN A 1 196 ? 6.165  -29.067 -16.425 1.00 17.75 ? 351  GLN A C     1 
ATOM   1380 O  O     . GLN A 1 196 ? 6.075  -28.727 -17.615 1.00 18.69 ? 351  GLN A O     1 
ATOM   1381 C  CB    . GLN A 1 196 ? 4.117  -29.467 -15.061 1.00 20.06 ? 351  GLN A CB    1 
ATOM   1382 C  CG    . GLN A 1 196 ? 2.859  -30.314 -14.959 1.00 42.24 ? 351  GLN A CG    1 
ATOM   1383 C  CD    . GLN A 1 196 ? 1.870  -29.748 -13.942 1.00 62.50 ? 351  GLN A CD    1 
ATOM   1384 O  OE1   . GLN A 1 196 ? 1.931  -28.558 -13.601 1.00 59.83 ? 351  GLN A OE1   1 
ATOM   1385 N  NE2   . GLN A 1 196 ? 0.954  -30.592 -13.458 1.00 58.22 ? 351  GLN A NE2   1 
ATOM   1386 N  N     . LEU A 1 197 ? 7.030  -28.495 -15.588 1.00 15.75 ? 352  LEU A N     1 
ATOM   1387 C  CA    . LEU A 1 197 ? 7.889  -27.429 -16.070 1.00 18.40 ? 352  LEU A CA    1 
ATOM   1388 C  C     . LEU A 1 197 ? 8.891  -27.935 -17.098 1.00 16.14 ? 352  LEU A C     1 
ATOM   1389 O  O     . LEU A 1 197 ? 9.184  -27.229 -18.076 1.00 17.08 ? 352  LEU A O     1 
ATOM   1390 C  CB    . LEU A 1 197 ? 8.569  -26.760 -14.894 1.00 16.23 ? 352  LEU A CB    1 
ATOM   1391 C  CG    . LEU A 1 197 ? 7.673  -25.945 -13.960 1.00 16.64 ? 352  LEU A CG    1 
ATOM   1392 C  CD1   . LEU A 1 197 ? 8.466  -25.463 -12.800 1.00 18.44 ? 352  LEU A CD1   1 
ATOM   1393 C  CD2   . LEU A 1 197 ? 6.998  -24.792 -14.662 1.00 21.92 ? 352  LEU A CD2   1 
ATOM   1394 N  N     . ARG A 1 198 ? 9.382  -29.161 -16.912 1.00 16.28 ? 353  ARG A N     1 
ATOM   1395 C  CA    . ARG A 1 198 ? 10.364 -29.761 -17.816 1.00 16.95 ? 353  ARG A CA    1 
ATOM   1396 C  C     . ARG A 1 198 ? 9.748  -30.171 -19.146 1.00 20.67 ? 353  ARG A C     1 
ATOM   1397 O  O     . ARG A 1 198 ? 10.494 -30.415 -20.104 1.00 21.45 ? 353  ARG A O     1 
ATOM   1398 C  CB    . ARG A 1 198 ? 11.086 -30.901 -17.109 1.00 16.30 ? 353  ARG A CB    1 
ATOM   1399 C  CG    . ARG A 1 198 ? 12.068 -30.396 -16.035 1.00 22.14 ? 353  ARG A CG    1 
ATOM   1400 C  CD    . ARG A 1 198 ? 12.872 -31.541 -15.448 1.00 26.88 ? 353  ARG A CD    1 
ATOM   1401 N  NE    . ARG A 1 198 ? 13.804 -32.082 -16.428 1.00 31.86 ? 353  ARG A NE    1 
ATOM   1402 C  CZ    . ARG A 1 198 ? 15.007 -31.550 -16.618 1.00 31.25 ? 353  ARG A CZ    1 
ATOM   1403 N  NH1   . ARG A 1 198 ? 15.428 -30.529 -15.886 1.00 36.73 ? 353  ARG A NH1   1 
ATOM   1404 N  NH2   . ARG A 1 198 ? 15.806 -32.056 -17.553 1.00 34.82 ? 353  ARG A NH2   1 
ATOM   1405 N  N     . LEU A 1 199 ? 8.423  -30.222 -19.231 1.00 19.38 ? 354  LEU A N     1 
ATOM   1406 C  CA    . LEU A 1 199 ? 7.739  -30.377 -20.504 1.00 19.50 ? 354  LEU A CA    1 
ATOM   1407 C  C     . LEU A 1 199 ? 7.613  -29.078 -21.272 1.00 20.41 ? 354  LEU A C     1 
ATOM   1408 O  O     . LEU A 1 199 ? 7.195  -29.096 -22.434 1.00 22.93 ? 354  LEU A O     1 
ATOM   1409 C  CB    . LEU A 1 199 ? 6.365  -31.031 -20.293 1.00 22.04 ? 354  LEU A CB    1 
ATOM   1410 C  CG    . LEU A 1 199 ? 6.492  -32.479 -19.873 1.00 26.19 ? 354  LEU A CG    1 
ATOM   1411 C  CD1   . LEU A 1 199 ? 5.141  -33.034 -19.374 1.00 29.75 ? 354  LEU A CD1   1 
ATOM   1412 C  CD2   . LEU A 1 199 ? 7.083  -33.322 -21.025 1.00 30.95 ? 354  LEU A CD2   1 
ATOM   1413 N  N     . LYS A 1 200 ? 7.879  -27.939 -20.649 1.00 18.77 ? 355  LYS A N     1 
ATOM   1414 C  CA    . LYS A 1 200 ? 7.824  -26.679 -21.366 1.00 18.15 ? 355  LYS A CA    1 
ATOM   1415 C  C     . LYS A 1 200 ? 9.034  -26.535 -22.282 1.00 19.64 ? 355  LYS A C     1 
ATOM   1416 O  O     . LYS A 1 200 ? 10.027 -27.249 -22.144 1.00 18.62 ? 355  LYS A O     1 
ATOM   1417 C  CB    . LYS A 1 200 ? 7.754  -25.523 -20.367 1.00 20.93 ? 355  LYS A CB    1 
ATOM   1418 C  CG    . LYS A 1 200 ? 6.422  -25.526 -19.613 1.00 26.13 ? 355  LYS A CG    1 
ATOM   1419 C  CD    . LYS A 1 200 ? 6.369  -24.412 -18.590 1.00 26.55 ? 355  LYS A CD    1 
ATOM   1420 C  CE    . LYS A 1 200 ? 4.962  -24.317 -17.961 1.00 33.32 ? 355  LYS A CE    1 
ATOM   1421 N  NZ    . LYS A 1 200 ? 3.921  -25.120 -18.657 1.00 42.28 ? 355  LYS A NZ    1 
ATOM   1422 N  N     . PRO A 1 201 ? 8.958  -25.655 -23.266 1.00 19.12 ? 356  PRO A N     1 
ATOM   1423 C  CA    . PRO A 1 201 ? 10.116 -25.438 -24.134 1.00 20.05 ? 356  PRO A CA    1 
ATOM   1424 C  C     . PRO A 1 201 ? 11.303 -24.888 -23.364 1.00 17.52 ? 356  PRO A C     1 
ATOM   1425 O  O     . PRO A 1 201 ? 11.208 -24.428 -22.231 1.00 17.89 ? 356  PRO A O     1 
ATOM   1426 C  CB    . PRO A 1 201 ? 9.617  -24.419 -25.166 1.00 22.17 ? 356  PRO A CB    1 
ATOM   1427 C  CG    . PRO A 1 201 ? 8.356  -23.892 -24.640 1.00 28.43 ? 356  PRO A CG    1 
ATOM   1428 C  CD    . PRO A 1 201 ? 7.789  -24.855 -23.663 1.00 25.89 ? 356  PRO A CD    1 
ATOM   1429 N  N     . PHE A 1 202 ? 12.443 -24.938 -24.003 1.00 18.40 ? 357  PHE A N     1 
ATOM   1430 C  CA    . PHE A 1 202 ? 13.595 -24.187 -23.537 1.00 16.30 ? 357  PHE A CA    1 
ATOM   1431 C  C     . PHE A 1 202 ? 14.009 -23.217 -24.626 1.00 16.51 ? 357  PHE A C     1 
ATOM   1432 O  O     . PHE A 1 202 ? 13.540 -23.316 -25.767 1.00 17.59 ? 357  PHE A O     1 
ATOM   1433 C  CB    . PHE A 1 202 ? 14.766 -25.085 -23.109 1.00 20.32 ? 357  PHE A CB    1 
ATOM   1434 C  CG    . PHE A 1 202 ? 15.389 -25.874 -24.211 1.00 21.02 ? 357  PHE A CG    1 
ATOM   1435 C  CD1   . PHE A 1 202 ? 14.897 -27.128 -24.570 1.00 23.18 ? 357  PHE A CD1   1 
ATOM   1436 C  CD2   . PHE A 1 202 ? 16.497 -25.392 -24.886 1.00 21.77 ? 357  PHE A CD2   1 
ATOM   1437 C  CE1   . PHE A 1 202 ? 15.500 -27.863 -25.583 1.00 22.40 ? 357  PHE A CE1   1 
ATOM   1438 C  CE2   . PHE A 1 202 ? 17.121 -26.104 -25.907 1.00 26.51 ? 357  PHE A CE2   1 
ATOM   1439 C  CZ    . PHE A 1 202 ? 16.627 -27.358 -26.264 1.00 23.87 ? 357  PHE A CZ    1 
ATOM   1440 N  N     . TYR A 1 203 ? 14.823 -22.225 -24.257 1.00 14.39 ? 358  TYR A N     1 
ATOM   1441 C  CA    . TYR A 1 203 ? 15.196 -21.136 -25.148 1.00 14.70 ? 358  TYR A CA    1 
ATOM   1442 C  C     . TYR A 1 203 ? 16.710 -21.060 -25.288 1.00 15.80 ? 358  TYR A C     1 
ATOM   1443 O  O     . TYR A 1 203 ? 17.474 -21.455 -24.385 1.00 16.46 ? 358  TYR A O     1 
ATOM   1444 C  CB    . TYR A 1 203 ? 14.619 -19.791 -24.673 1.00 15.93 ? 358  TYR A CB    1 
ATOM   1445 C  CG    . TYR A 1 203 ? 13.133 -19.819 -24.730 1.00 16.96 ? 358  TYR A CG    1 
ATOM   1446 C  CD1   . TYR A 1 203 ? 12.447 -19.501 -25.902 1.00 15.22 ? 358  TYR A CD1   1 
ATOM   1447 C  CD2   . TYR A 1 203 ? 12.398 -20.213 -23.631 1.00 17.82 ? 358  TYR A CD2   1 
ATOM   1448 C  CE1   . TYR A 1 203 ? 11.060 -19.606 -25.971 1.00 17.82 ? 358  TYR A CE1   1 
ATOM   1449 C  CE2   . TYR A 1 203 ? 11.026 -20.315 -23.685 1.00 17.88 ? 358  TYR A CE2   1 
ATOM   1450 C  CZ    . TYR A 1 203 ? 10.371 -20.000 -24.852 1.00 18.15 ? 358  TYR A CZ    1 
ATOM   1451 O  OH    . TYR A 1 203 ? 8.994  -20.133 -24.893 1.00 22.86 ? 358  TYR A OH    1 
ATOM   1452 N  N     . LEU A 1 204 ? 17.136 -20.552 -26.433 1.00 16.00 ? 359  LEU A N     1 
ATOM   1453 C  CA    . LEU A 1 204 ? 18.541 -20.277 -26.683 1.00 15.98 ? 359  LEU A CA    1 
ATOM   1454 C  C     . LEU A 1 204 ? 18.639 -18.828 -27.109 1.00 15.10 ? 359  LEU A C     1 
ATOM   1455 O  O     . LEU A 1 204 ? 17.893 -18.395 -27.988 1.00 16.01 ? 359  LEU A O     1 
ATOM   1456 C  CB    . LEU A 1 204 ? 19.036 -21.163 -27.833 1.00 17.36 ? 359  LEU A CB    1 
ATOM   1457 C  CG    . LEU A 1 204 ? 19.034 -22.641 -27.489 1.00 20.48 ? 359  LEU A CG    1 
ATOM   1458 C  CD1   . LEU A 1 204 ? 19.055 -23.443 -28.748 1.00 25.61 ? 359  LEU A CD1   1 
ATOM   1459 C  CD2   . LEU A 1 204 ? 20.223 -22.963 -26.649 1.00 25.97 ? 359  LEU A CD2   1 
ATOM   1460 N  N     . VAL A 1 205 ? 19.554 -18.084 -26.506 1.00 16.11 ? 360  VAL A N     1 
ATOM   1461 C  CA    . VAL A 1 205 ? 19.694 -16.659 -26.737 1.00 14.97 ? 360  VAL A CA    1 
ATOM   1462 C  C     . VAL A 1 205 ? 21.087 -16.441 -27.304 1.00 15.24 ? 360  VAL A C     1 
ATOM   1463 O  O     . VAL A 1 205 ? 22.005 -17.205 -26.966 1.00 16.08 ? 360  VAL A O     1 
ATOM   1464 C  CB    . VAL A 1 205 ? 19.421 -15.834 -25.449 1.00 16.19 ? 360  VAL A CB    1 
ATOM   1465 C  CG1   . VAL A 1 205 ? 17.975 -16.127 -24.944 1.00 16.17 ? 360  VAL A CG1   1 
ATOM   1466 C  CG2   . VAL A 1 205 ? 20.501 -16.115 -24.330 1.00 15.43 ? 360  VAL A CG2   1 
ATOM   1467 N  N     . PRO A 1 206 ? 21.279 -15.433 -28.122 1.00 16.72 ? 361  PRO A N     1 
ATOM   1468 C  CA    . PRO A 1 206 ? 22.576 -15.230 -28.814 1.00 17.86 ? 361  PRO A CA    1 
ATOM   1469 C  C     . PRO A 1 206 ? 23.583 -14.506 -27.936 1.00 17.49 ? 361  PRO A C     1 
ATOM   1470 O  O     . PRO A 1 206 ? 23.955 -13.374 -28.196 1.00 20.82 ? 361  PRO A O     1 
ATOM   1471 C  CB    . PRO A 1 206 ? 22.154 -14.391 -30.029 1.00 17.75 ? 361  PRO A CB    1 
ATOM   1472 C  CG    . PRO A 1 206 ? 21.001 -13.532 -29.475 1.00 19.17 ? 361  PRO A CG    1 
ATOM   1473 C  CD    . PRO A 1 206 ? 20.238 -14.505 -28.608 1.00 15.69 ? 361  PRO A CD    1 
ATOM   1474 N  N     . LYS A 1 207 ? 23.928 -15.138 -26.816 1.00 17.02 ? 362  LYS A N     1 
ATOM   1475 C  CA    . LYS A 1 207 ? 25.050 -14.767 -25.967 1.00 18.47 ? 362  LYS A CA    1 
ATOM   1476 C  C     . LYS A 1 207 ? 26.134 -15.813 -26.187 1.00 19.14 ? 362  LYS A C     1 
ATOM   1477 O  O     . LYS A 1 207 ? 25.891 -17.014 -26.033 1.00 19.38 ? 362  LYS A O     1 
ATOM   1478 C  CB    . LYS A 1 207 ? 24.642 -14.779 -24.480 1.00 17.50 ? 362  LYS A CB    1 
ATOM   1479 C  CG    . LYS A 1 207 ? 25.799 -14.431 -23.595 1.00 20.91 ? 362  LYS A CG    1 
ATOM   1480 C  CD    . LYS A 1 207 ? 25.382 -14.496 -22.154 1.00 19.71 ? 362  LYS A CD    1 
ATOM   1481 C  CE    . LYS A 1 207 ? 26.520 -13.952 -21.309 1.00 28.98 ? 362  LYS A CE    1 
ATOM   1482 N  NZ    . LYS A 1 207 ? 27.758 -14.716 -21.553 1.00 33.60 ? 362  LYS A NZ    1 
ATOM   1483 N  N     . HIS A 1 208 ? 27.322 -15.353 -26.587 1.00 17.72 ? 363  HIS A N     1 
ATOM   1484 C  CA    . HIS A 1 208 ? 28.390 -16.265 -27.000 1.00 21.52 ? 363  HIS A CA    1 
ATOM   1485 C  C     . HIS A 1 208 ? 29.294 -16.678 -25.866 1.00 20.65 ? 363  HIS A C     1 
ATOM   1486 O  O     . HIS A 1 208 ? 29.555 -15.905 -24.955 1.00 21.76 ? 363  HIS A O     1 
ATOM   1487 C  CB    . HIS A 1 208 ? 29.231 -15.625 -28.100 1.00 23.97 ? 363  HIS A CB    1 
ATOM   1488 C  CG    . HIS A 1 208 ? 28.415 -14.998 -29.178 1.00 22.93 ? 363  HIS A CG    1 
ATOM   1489 N  ND1   . HIS A 1 208 ? 27.424 -15.692 -29.834 1.00 21.30 ? 363  HIS A ND1   1 
ATOM   1490 C  CD2   . HIS A 1 208 ? 28.446 -13.762 -29.733 1.00 25.09 ? 363  HIS A CD2   1 
ATOM   1491 C  CE1   . HIS A 1 208 ? 26.859 -14.903 -30.734 1.00 24.34 ? 363  HIS A CE1   1 
ATOM   1492 N  NE2   . HIS A 1 208 ? 27.471 -13.730 -30.699 1.00 25.53 ? 363  HIS A NE2   1 
ATOM   1493 N  N     . ALA A 1 209 ? 29.808 -17.900 -25.967 1.00 22.12 ? 364  ALA A N     1 
ATOM   1494 C  CA    . ALA A 1 209 ? 30.838 -18.366 -25.053 1.00 23.72 ? 364  ALA A CA    1 
ATOM   1495 C  C     . ALA A 1 209 ? 32.157 -17.630 -25.304 1.00 29.15 ? 364  ALA A C     1 
ATOM   1496 O  O     . ALA A 1 209 ? 32.445 -17.190 -26.422 1.00 27.28 ? 364  ALA A O     1 
ATOM   1497 C  CB    . ALA A 1 209 ? 31.041 -19.862 -25.275 1.00 24.62 ? 364  ALA A CB    1 
ATOM   1498 N  N     . LYS A 1 210 ? 32.943 -17.482 -24.250 1.00 26.34 ? 365  LYS A N     1 
ATOM   1499 C  CA    . LYS A 1 210 ? 34.305 -16.964 -24.418 1.00 34.82 ? 365  LYS A CA    1 
ATOM   1500 C  C     . LYS A 1 210 ? 35.189 -17.945 -25.200 1.00 37.36 ? 365  LYS A C     1 
ATOM   1501 O  O     . LYS A 1 210 ? 35.109 -19.164 -25.021 1.00 35.69 ? 365  LYS A O     1 
ATOM   1502 C  CB    . LYS A 1 210 ? 34.920 -16.645 -23.050 1.00 37.28 ? 365  LYS A CB    1 
ATOM   1503 N  N     . GLU A 1 211 ? 36.014 -17.407 -26.107 1.00 34.02 ? 366  GLU A N     1 
ATOM   1504 C  CA    . GLU A 1 211 ? 36.967 -18.217 -26.895 1.00 37.33 ? 366  GLU A CA    1 
ATOM   1505 C  C     . GLU A 1 211 ? 38.200 -17.396 -27.294 1.00 33.56 ? 366  GLU A C     1 
ATOM   1506 O  O     . GLU A 1 211 ? 39.171 -17.321 -26.540 1.00 49.63 ? 366  GLU A O     1 
ATOM   1507 C  CB    . GLU A 1 211 ? 36.323 -18.807 -28.164 1.00 39.07 ? 366  GLU A CB    1 
ATOM   1508 C  CG    . GLU A 1 211 ? 37.288 -19.658 -29.025 1.00 41.77 ? 366  GLU A CG    1 
ATOM   1509 C  CD    . GLU A 1 211 ? 36.694 -20.082 -30.368 1.00 49.71 ? 366  GLU A CD    1 
ATOM   1510 O  OE1   . GLU A 1 211 ? 36.337 -19.175 -31.156 1.00 50.82 ? 366  GLU A OE1   1 
ATOM   1511 O  OE2   . GLU A 1 211 ? 36.597 -21.309 -30.648 1.00 44.54 ? 366  GLU A OE2   1 
ATOM   1512 N  N     . GLY A 1 214 ? 38.008 -12.749 -27.050 1.00 42.56 ? 369  GLY A N     1 
ATOM   1513 C  CA    . GLY A 1 214 ? 37.490 -13.656 -28.054 1.00 40.36 ? 369  GLY A CA    1 
ATOM   1514 C  C     . GLY A 1 214 ? 36.210 -14.382 -27.664 1.00 41.80 ? 369  GLY A C     1 
ATOM   1515 O  O     . GLY A 1 214 ? 36.037 -14.808 -26.518 1.00 37.28 ? 369  GLY A O     1 
ATOM   1516 N  N     . PHE A 1 215 ? 35.310 -14.517 -28.634 1.00 37.75 ? 370  PHE A N     1 
ATOM   1517 C  CA    . PHE A 1 215 ? 34.040 -15.198 -28.447 1.00 35.52 ? 370  PHE A CA    1 
ATOM   1518 C  C     . PHE A 1 215 ? 33.848 -16.184 -29.582 1.00 32.14 ? 370  PHE A C     1 
ATOM   1519 O  O     . PHE A 1 215 ? 34.225 -15.913 -30.727 1.00 28.15 ? 370  PHE A O     1 
ATOM   1520 C  CB    . PHE A 1 215 ? 32.856 -14.209 -28.488 1.00 31.52 ? 370  PHE A CB    1 
ATOM   1521 C  CG    . PHE A 1 215 ? 32.797 -13.292 -27.314 1.00 37.10 ? 370  PHE A CG    1 
ATOM   1522 C  CD1   . PHE A 1 215 ? 32.168 -13.688 -26.146 1.00 37.24 ? 370  PHE A CD1   1 
ATOM   1523 C  CD2   . PHE A 1 215 ? 33.337 -12.025 -27.377 1.00 42.31 ? 370  PHE A CD2   1 
ATOM   1524 C  CE1   . PHE A 1 215 ? 32.103 -12.847 -25.056 1.00 40.16 ? 370  PHE A CE1   1 
ATOM   1525 C  CE2   . PHE A 1 215 ? 33.268 -11.174 -26.281 1.00 49.05 ? 370  PHE A CE2   1 
ATOM   1526 C  CZ    . PHE A 1 215 ? 32.649 -11.592 -25.124 1.00 43.04 ? 370  PHE A CZ    1 
ATOM   1527 N  N     . GLN A 1 216 ? 33.266 -17.329 -29.256 1.00 25.65 ? 371  GLN A N     1 
ATOM   1528 C  CA    . GLN A 1 216 ? 32.810 -18.268 -30.260 1.00 24.38 ? 371  GLN A CA    1 
ATOM   1529 C  C     . GLN A 1 216 ? 31.477 -17.716 -30.742 1.00 29.82 ? 371  GLN A C     1 
ATOM   1530 O  O     . GLN A 1 216 ? 30.439 -17.894 -30.096 1.00 23.50 ? 371  GLN A O     1 
ATOM   1531 C  CB    . GLN A 1 216 ? 32.701 -19.662 -29.653 1.00 29.29 ? 371  GLN A CB    1 
ATOM   1532 C  CG    . GLN A 1 216 ? 33.027 -20.798 -30.625 1.00 32.81 ? 371  GLN A CG    1 
ATOM   1533 C  CD    . GLN A 1 216 ? 32.292 -20.678 -31.949 1.00 36.42 ? 371  GLN A CD    1 
ATOM   1534 O  OE1   . GLN A 1 216 ? 31.120 -20.302 -31.986 1.00 28.40 ? 371  GLN A OE1   1 
ATOM   1535 N  NE2   . GLN A 1 216 ? 32.944 -21.083 -33.038 1.00 36.54 ? 371  GLN A NE2   1 
ATOM   1536 N  N     . GLU A 1 217 ? 31.505 -17.025 -31.871 1.00 25.60 ? 372  GLU A N     1 
ATOM   1537 C  CA    . GLU A 1 217 ? 30.387 -16.190 -32.290 1.00 26.54 ? 372  GLU A CA    1 
ATOM   1538 C  C     . GLU A 1 217 ? 29.248 -16.976 -32.908 1.00 23.80 ? 372  GLU A C     1 
ATOM   1539 O  O     . GLU A 1 217 ? 28.236 -16.375 -33.268 1.00 25.84 ? 372  GLU A O     1 
ATOM   1540 C  CB    . GLU A 1 217 ? 30.849 -15.107 -33.264 1.00 32.98 ? 372  GLU A CB    1 
ATOM   1541 C  CG    . GLU A 1 217 ? 31.751 -14.071 -32.626 1.00 41.27 ? 372  GLU A CG    1 
ATOM   1542 C  CD    . GLU A 1 217 ? 32.223 -13.028 -33.618 1.00 65.43 ? 372  GLU A CD    1 
ATOM   1543 O  OE1   . GLU A 1 217 ? 32.267 -13.337 -34.831 1.00 79.93 ? 372  GLU A OE1   1 
ATOM   1544 O  OE2   . GLU A 1 217 ? 32.563 -11.908 -33.182 1.00 74.77 ? 372  GLU A OE2   1 
ATOM   1545 N  N     . GLU A 1 218 ? 29.374 -18.287 -33.060 1.00 22.20 ? 373  GLU A N     1 
ATOM   1546 C  CA    . GLU A 1 218 ? 28.233 -19.058 -33.494 1.00 25.18 ? 373  GLU A CA    1 
ATOM   1547 C  C     . GLU A 1 218 ? 27.411 -19.563 -32.330 1.00 19.97 ? 373  GLU A C     1 
ATOM   1548 O  O     . GLU A 1 218 ? 26.316 -20.073 -32.569 1.00 21.69 ? 373  GLU A O     1 
ATOM   1549 C  CB    . GLU A 1 218 ? 28.640 -20.268 -34.342 1.00 26.53 ? 373  GLU A CB    1 
ATOM   1550 C  CG    . GLU A 1 218 ? 29.025 -19.899 -35.771 1.00 31.06 ? 373  GLU A CG    1 
ATOM   1551 C  CD    . GLU A 1 218 ? 30.502 -19.561 -35.886 1.00 50.63 ? 373  GLU A CD    1 
ATOM   1552 O  OE1   . GLU A 1 218 ? 31.351 -20.446 -35.611 1.00 46.18 ? 373  GLU A OE1   1 
ATOM   1553 O  OE2   . GLU A 1 218 ? 30.803 -18.396 -36.231 1.00 53.63 ? 373  GLU A OE2   1 
ATOM   1554 N  N     . THR A 1 219 ? 27.942 -19.476 -31.114 1.00 19.94 ? 374  THR A N     1 
ATOM   1555 C  CA    . THR A 1 219 ? 27.338 -20.152 -29.976 1.00 20.45 ? 374  THR A CA    1 
ATOM   1556 C  C     . THR A 1 219 ? 26.154 -19.377 -29.398 1.00 18.55 ? 374  THR A C     1 
ATOM   1557 O  O     . THR A 1 219 ? 26.087 -18.136 -29.417 1.00 19.24 ? 374  THR A O     1 
ATOM   1558 C  CB    . THR A 1 219 ? 28.333 -20.455 -28.856 1.00 17.00 ? 374  THR A CB    1 
ATOM   1559 O  OG1   . THR A 1 219 ? 28.967 -19.275 -28.385 1.00 19.62 ? 374  THR A OG1   1 
ATOM   1560 C  CG2   . THR A 1 219 ? 29.349 -21.561 -29.285 1.00 22.83 ? 374  THR A CG2   1 
ATOM   1561 N  N     . TRP A 1 220 ? 25.230 -20.167 -28.883 1.00 18.39 ? 375  TRP A N     1 
ATOM   1562 C  CA    . TRP A 1 220 ? 24.004 -19.729 -28.224 1.00 17.55 ? 375  TRP A CA    1 
ATOM   1563 C  C     . TRP A 1 220 ? 24.089 -20.140 -26.765 1.00 17.28 ? 375  TRP A C     1 
ATOM   1564 O  O     . TRP A 1 220 ? 24.814 -21.056 -26.393 1.00 17.80 ? 375  TRP A O     1 
ATOM   1565 C  CB    . TRP A 1 220 ? 22.801 -20.432 -28.859 1.00 17.83 ? 375  TRP A CB    1 
ATOM   1566 C  CG    . TRP A 1 220 ? 22.570 -20.091 -30.314 1.00 18.89 ? 375  TRP A CG    1 
ATOM   1567 C  CD1   . TRP A 1 220 ? 23.225 -20.634 -31.413 1.00 20.96 ? 375  TRP A CD1   1 
ATOM   1568 C  CD2   . TRP A 1 220 ? 21.609 -19.174 -30.852 1.00 18.94 ? 375  TRP A CD2   1 
ATOM   1569 N  NE1   . TRP A 1 220 ? 22.724 -20.096 -32.571 1.00 19.63 ? 375  TRP A NE1   1 
ATOM   1570 C  CE2   . TRP A 1 220 ? 21.727 -19.208 -32.269 1.00 19.70 ? 375  TRP A CE2   1 
ATOM   1571 C  CE3   . TRP A 1 220 ? 20.660 -18.328 -30.275 1.00 18.71 ? 375  TRP A CE3   1 
ATOM   1572 C  CZ2   . TRP A 1 220 ? 20.937 -18.426 -33.103 1.00 19.93 ? 375  TRP A CZ2   1 
ATOM   1573 C  CZ3   . TRP A 1 220 ? 19.896 -17.547 -31.089 1.00 20.07 ? 375  TRP A CZ3   1 
ATOM   1574 C  CH2   . TRP A 1 220 ? 20.027 -17.587 -32.494 1.00 22.10 ? 375  TRP A CH2   1 
ATOM   1575 N  N     . ARG A 1 221 ? 23.235 -19.534 -25.922 1.00 15.89 ? 376  ARG A N     1 
ATOM   1576 C  CA    . ARG A 1 221 ? 23.229 -19.818 -24.501 1.00 15.72 ? 376  ARG A CA    1 
ATOM   1577 C  C     . ARG A 1 221 ? 21.832 -20.268 -24.094 1.00 16.80 ? 376  ARG A C     1 
ATOM   1578 O  O     . ARG A 1 221 ? 20.840 -19.651 -24.485 1.00 15.85 ? 376  ARG A O     1 
ATOM   1579 C  CB    . ARG A 1 221 ? 23.611 -18.609 -23.706 1.00 22.76 ? 376  ARG A CB    1 
ATOM   1580 C  CG    . ARG A 1 221 ? 23.421 -18.910 -22.265 1.00 25.54 ? 376  ARG A CG    1 
ATOM   1581 C  CD    . ARG A 1 221 ? 24.245 -18.231 -21.338 1.00 26.90 ? 376  ARG A CD    1 
ATOM   1582 N  NE    . ARG A 1 221 ? 23.963 -18.847 -20.046 1.00 27.55 ? 376  ARG A NE    1 
ATOM   1583 C  CZ    . ARG A 1 221 ? 24.642 -18.552 -18.956 1.00 24.14 ? 376  ARG A CZ    1 
ATOM   1584 N  NH1   . ARG A 1 221 ? 25.673 -17.719 -18.989 1.00 35.59 ? 376  ARG A NH1   1 
ATOM   1585 N  NH2   . ARG A 1 221 ? 24.236 -19.052 -17.793 1.00 31.28 ? 376  ARG A NH2   1 
ATOM   1586 N  N     A LEU A 1 222 ? 21.769 -21.330 -23.302 0.55 16.33 ? 377  LEU A N     1 
ATOM   1587 N  N     B LEU A 1 222 ? 21.773 -21.325 -23.285 0.45 16.35 ? 377  LEU A N     1 
ATOM   1588 C  CA    A LEU A 1 222 ? 20.512 -21.827 -22.764 0.55 16.52 ? 377  LEU A CA    1 
ATOM   1589 C  CA    B LEU A 1 222 ? 20.513 -21.842 -22.766 0.45 16.54 ? 377  LEU A CA    1 
ATOM   1590 C  C     A LEU A 1 222 ? 19.912 -20.826 -21.789 0.55 16.29 ? 377  LEU A C     1 
ATOM   1591 C  C     B LEU A 1 222 ? 19.909 -20.842 -21.791 0.45 16.31 ? 377  LEU A C     1 
ATOM   1592 O  O     A LEU A 1 222 ? 20.607 -20.299 -20.919 0.55 17.01 ? 377  LEU A O     1 
ATOM   1593 O  O     B LEU A 1 222 ? 20.605 -20.341 -20.906 0.45 17.04 ? 377  LEU A O     1 
ATOM   1594 C  CB    A LEU A 1 222 ? 20.841 -23.089 -21.978 0.55 19.25 ? 377  LEU A CB    1 
ATOM   1595 C  CB    B LEU A 1 222 ? 20.812 -23.096 -21.948 0.45 19.27 ? 377  LEU A CB    1 
ATOM   1596 C  CG    A LEU A 1 222 ? 20.491 -24.445 -22.525 0.55 25.36 ? 377  LEU A CG    1 
ATOM   1597 C  CG    B LEU A 1 222 ? 19.790 -24.208 -21.806 0.45 16.16 ? 377  LEU A CG    1 
ATOM   1598 C  CD1   A LEU A 1 222 ? 20.935 -25.447 -21.479 0.55 20.25 ? 377  LEU A CD1   1 
ATOM   1599 C  CD1   B LEU A 1 222 ? 19.279 -24.592 -23.191 0.45 22.15 ? 377  LEU A CD1   1 
ATOM   1600 C  CD2   A LEU A 1 222 ? 18.938 -24.456 -22.644 0.55 19.51 ? 377  LEU A CD2   1 
ATOM   1601 C  CD2   B LEU A 1 222 ? 20.447 -25.381 -21.123 0.45 20.85 ? 377  LEU A CD2   1 
ATOM   1602 N  N     . SER A 1 223 ? 18.602 -20.611 -21.904 1.00 15.16 ? 378  SER A N     1 
ATOM   1603 C  CA    . SER A 1 223 ? 17.887 -19.734 -20.978 1.00 15.41 ? 378  SER A CA    1 
ATOM   1604 C  C     . SER A 1 223 ? 16.590 -20.391 -20.518 1.00 14.37 ? 378  SER A C     1 
ATOM   1605 O  O     . SER A 1 223 ? 15.840 -20.977 -21.316 1.00 15.76 ? 378  SER A O     1 
ATOM   1606 C  CB    . SER A 1 223 ? 17.546 -18.431 -21.667 1.00 16.22 ? 378  SER A CB    1 
ATOM   1607 O  OG    . SER A 1 223 ? 16.848 -17.599 -20.744 1.00 16.90 ? 378  SER A OG    1 
ATOM   1608 N  N     . PHE A 1 224 ? 16.315 -20.252 -19.222 1.00 15.60 ? 379  PHE A N     1 
ATOM   1609 C  CA    . PHE A 1 224 ? 15.049 -20.660 -18.624 1.00 15.40 ? 379  PHE A CA    1 
ATOM   1610 C  C     . PHE A 1 224 ? 14.350 -19.484 -17.965 1.00 16.66 ? 379  PHE A C     1 
ATOM   1611 O  O     . PHE A 1 224 ? 13.680 -19.657 -16.934 1.00 14.62 ? 379  PHE A O     1 
ATOM   1612 C  CB    . PHE A 1 224 ? 15.268 -21.812 -17.637 1.00 16.73 ? 379  PHE A CB    1 
ATOM   1613 C  CG    . PHE A 1 224 ? 15.852 -23.024 -18.306 1.00 15.17 ? 379  PHE A CG    1 
ATOM   1614 C  CD1   . PHE A 1 224 ? 15.022 -23.839 -19.026 1.00 17.68 ? 379  PHE A CD1   1 
ATOM   1615 C  CD2   . PHE A 1 224 ? 17.229 -23.246 -18.297 1.00 17.77 ? 379  PHE A CD2   1 
ATOM   1616 C  CE1   . PHE A 1 224 ? 15.503 -24.930 -19.689 1.00 20.11 ? 379  PHE A CE1   1 
ATOM   1617 C  CE2   . PHE A 1 224 ? 17.737 -24.373 -18.990 1.00 19.89 ? 379  PHE A CE2   1 
ATOM   1618 C  CZ    . PHE A 1 224 ? 16.816 -25.209 -19.674 1.00 19.64 ? 379  PHE A CZ    1 
ATOM   1619 N  N     . SER A 1 225 ? 14.460 -18.296 -18.569 1.00 14.85 ? 380  SER A N     1 
ATOM   1620 C  CA    . SER A 1 225 ? 13.881 -17.112 -17.933 1.00 14.95 ? 380  SER A CA    1 
ATOM   1621 C  C     . SER A 1 225 ? 12.370 -17.268 -17.765 1.00 14.97 ? 380  SER A C     1 
ATOM   1622 O  O     . SER A 1 225 ? 11.773 -16.702 -16.834 1.00 16.07 ? 380  SER A O     1 
ATOM   1623 C  CB    . SER A 1 225 ? 14.197 -15.909 -18.841 1.00 19.32 ? 380  SER A CB    1 
ATOM   1624 O  OG    . SER A 1 225 ? 13.971 -14.692 -18.170 1.00 24.97 ? 380  SER A OG    1 
ATOM   1625 N  N     . HIS A 1 226 ? 11.726 -18.016 -18.657 1.00 14.51 ? 381  HIS A N     1 
ATOM   1626 C  CA    . HIS A 1 226 ? 10.286 -18.225 -18.535 1.00 15.25 ? 381  HIS A CA    1 
ATOM   1627 C  C     . HIS A 1 226 ? 9.946  -19.067 -17.313 1.00 15.25 ? 381  HIS A C     1 
ATOM   1628 O  O     . HIS A 1 226 ? 8.880  -18.873 -16.718 1.00 15.52 ? 381  HIS A O     1 
ATOM   1629 C  CB    . HIS A 1 226 ? 9.743  -18.843 -19.829 1.00 16.10 ? 381  HIS A CB    1 
ATOM   1630 C  CG    . HIS A 1 226 ? 10.351 -20.170 -20.156 1.00 15.94 ? 381  HIS A CG    1 
ATOM   1631 N  ND1   . HIS A 1 226 ? 11.707 -20.388 -20.211 1.00 16.73 ? 381  HIS A ND1   1 
ATOM   1632 C  CD2   . HIS A 1 226 ? 9.756  -21.338 -20.496 1.00 17.09 ? 381  HIS A CD2   1 
ATOM   1633 C  CE1   . HIS A 1 226 ? 11.923 -21.646 -20.565 1.00 18.42 ? 381  HIS A CE1   1 
ATOM   1634 N  NE2   . HIS A 1 226 ? 10.757 -22.252 -20.700 1.00 17.76 ? 381  HIS A NE2   1 
ATOM   1635 N  N     . ILE A 1 227 ? 10.822 -19.999 -16.940 1.00 13.56 ? 382  ILE A N     1 
ATOM   1636 C  CA    . ILE A 1 227 ? 10.576 -20.847 -15.790 1.00 15.02 ? 382  ILE A CA    1 
ATOM   1637 C  C     . ILE A 1 227 ? 10.845 -20.062 -14.523 1.00 15.13 ? 382  ILE A C     1 
ATOM   1638 O  O     . ILE A 1 227 ? 10.122 -20.204 -13.541 1.00 13.40 ? 382  ILE A O     1 
ATOM   1639 C  CB    . ILE A 1 227 ? 11.422 -22.128 -15.853 1.00 14.29 ? 382  ILE A CB    1 
ATOM   1640 C  CG1   . ILE A 1 227 ? 11.284 -22.839 -17.224 1.00 14.47 ? 382  ILE A CG1   1 
ATOM   1641 C  CG2   . ILE A 1 227 ? 11.042 -23.078 -14.664 1.00 14.31 ? 382  ILE A CG2   1 
ATOM   1642 C  CD1   . ILE A 1 227 ? 9.918  -23.506 -17.462 1.00 18.08 ? 382  ILE A CD1   1 
ATOM   1643 N  N     . GLU A 1 228 ? 11.824 -19.164 -14.558 1.00 13.84 ? 383  GLU A N     1 
ATOM   1644 C  CA    . GLU A 1 228 ? 12.033 -18.283 -13.403 1.00 13.35 ? 383  GLU A CA    1 
ATOM   1645 C  C     . GLU A 1 228 ? 10.787 -17.465 -13.124 1.00 13.75 ? 383  GLU A C     1 
ATOM   1646 O  O     . GLU A 1 228 ? 10.381 -17.307 -11.968 1.00 13.49 ? 383  GLU A O     1 
ATOM   1647 C  CB    . GLU A 1 228 ? 13.214 -17.343 -13.690 1.00 14.21 ? 383  GLU A CB    1 
ATOM   1648 C  CG    . GLU A 1 228 ? 14.502 -18.167 -13.855 1.00 14.78 ? 383  GLU A CG    1 
ATOM   1649 C  CD    . GLU A 1 228 ? 15.700 -17.375 -14.367 1.00 24.07 ? 383  GLU A CD    1 
ATOM   1650 O  OE1   . GLU A 1 228 ? 15.627 -16.130 -14.459 1.00 21.45 ? 383  GLU A OE1   1 
ATOM   1651 O  OE2   . GLU A 1 228 ? 16.722 -18.031 -14.698 1.00 19.86 ? 383  GLU A OE2   1 
ATOM   1652 N  N     . LYS A 1 229 ? 10.133 -16.975 -14.175 1.00 12.94 ? 384  LYS A N     1 
ATOM   1653 C  CA    . LYS A 1 229 ? 8.906  -16.222 -13.980 1.00 12.86 ? 384  LYS A CA    1 
ATOM   1654 C  C     . LYS A 1 229 ? 7.804  -17.108 -13.406 1.00 13.27 ? 384  LYS A C     1 
ATOM   1655 O  O     . LYS A 1 229 ? 7.077  -16.678 -12.500 1.00 14.28 ? 384  LYS A O     1 
ATOM   1656 C  CB    . LYS A 1 229 ? 8.468  -15.648 -15.331 1.00 14.31 ? 384  LYS A CB    1 
ATOM   1657 C  CG    . LYS A 1 229 ? 7.149  -14.783 -15.198 1.00 16.77 ? 384  LYS A CG    1 
ATOM   1658 C  CD    . LYS A 1 229 ? 6.749  -14.037 -16.488 1.00 17.53 ? 384  LYS A CD    1 
ATOM   1659 C  CE    . LYS A 1 229 ? 6.306  -15.005 -17.551 1.00 18.88 ? 384  LYS A CE    1 
ATOM   1660 N  NZ    . LYS A 1 229 ? 5.760  -14.251 -18.742 1.00 20.42 ? 384  LYS A NZ    1 
ATOM   1661 N  N     . GLU A 1 230 ? 7.664  -18.343 -13.937 1.00 13.46 ? 385  GLU A N     1 
ATOM   1662 C  CA    . GLU A 1 230 ? 6.635  -19.276 -13.472 1.00 14.65 ? 385  GLU A CA    1 
ATOM   1663 C  C     . GLU A 1 230 ? 6.794  -19.569 -11.989 1.00 15.79 ? 385  GLU A C     1 
ATOM   1664 O  O     . GLU A 1 230 ? 5.812  -19.529 -11.227 1.00 16.84 ? 385  GLU A O     1 
ATOM   1665 C  CB    . GLU A 1 230 ? 6.691  -20.607 -14.220 1.00 19.56 ? 385  GLU A CB    1 
ATOM   1666 C  CG    . GLU A 1 230 ? 6.341  -20.472 -15.676 1.00 32.36 ? 385  GLU A CG    1 
ATOM   1667 C  CD    . GLU A 1 230 ? 4.903  -20.870 -15.956 1.00 45.73 ? 385  GLU A CD    1 
ATOM   1668 O  OE1   . GLU A 1 230 ? 4.022  -20.560 -15.125 1.00 53.92 ? 385  GLU A OE1   1 
ATOM   1669 O  OE2   . GLU A 1 230 ? 4.655  -21.459 -17.024 1.00 51.12 ? 385  GLU A OE2   1 
ATOM   1670 N  N     . ILE A 1 231 ? 8.016  -19.823 -11.554 1.00 14.49 ? 386  ILE A N     1 
ATOM   1671 C  CA    . ILE A 1 231 ? 8.291  -20.082 -10.143 1.00 14.53 ? 386  ILE A CA    1 
ATOM   1672 C  C     . ILE A 1 231 ? 7.957  -18.849 -9.304  1.00 15.09 ? 386  ILE A C     1 
ATOM   1673 O  O     . ILE A 1 231 ? 7.223  -18.938 -8.316  1.00 15.12 ? 386  ILE A O     1 
ATOM   1674 C  CB    . ILE A 1 231 ? 9.752  -20.558 -9.976  1.00 15.53 ? 386  ILE A CB    1 
ATOM   1675 C  CG1   . ILE A 1 231 ? 9.895  -21.973 -10.571 1.00 19.46 ? 386  ILE A CG1   1 
ATOM   1676 C  CG2   . ILE A 1 231 ? 10.222 -20.388 -8.514  1.00 19.00 ? 386  ILE A CG2   1 
ATOM   1677 C  CD1   . ILE A 1 231 ? 11.322 -22.333 -10.740 1.00 28.55 ? 386  ILE A CD1   1 
ATOM   1678 N  N     . LEU A 1 232 ? 8.439  -17.674 -9.692  1.00 13.79 ? 387  LEU A N     1 
ATOM   1679 C  CA    . LEU A 1 232 ? 8.242  -16.504 -8.831  1.00 13.74 ? 387  LEU A CA    1 
ATOM   1680 C  C     . LEU A 1 232 ? 6.778  -16.125 -8.749  1.00 13.58 ? 387  LEU A C     1 
ATOM   1681 O  O     . LEU A 1 232 ? 6.328  -15.673 -7.692  1.00 14.91 ? 387  LEU A O     1 
ATOM   1682 C  CB    . LEU A 1 232 ? 9.059  -15.303 -9.317  1.00 13.03 ? 387  LEU A CB    1 
ATOM   1683 C  CG    . LEU A 1 232 ? 10.488 -15.461 -8.837  1.00 13.72 ? 387  LEU A CG    1 
ATOM   1684 C  CD1   . LEU A 1 232 ? 11.402 -14.536 -9.623  1.00 16.46 ? 387  LEU A CD1   1 
ATOM   1685 C  CD2   . LEU A 1 232 ? 10.554 -15.043 -7.339  1.00 17.46 ? 387  LEU A CD2   1 
ATOM   1686 N  N     . ASN A 1 233 ? 5.993  -16.377 -9.780  1.00 11.90 ? 388  ASN A N     1 
ATOM   1687 C  CA    . ASN A 1 233 ? 4.585  -16.001 -9.703  1.00 14.15 ? 388  ASN A CA    1 
ATOM   1688 C  C     . ASN A 1 233 ? 3.700  -17.119 -9.216  1.00 16.82 ? 388  ASN A C     1 
ATOM   1689 O  O     . ASN A 1 233 ? 2.468  -16.952 -9.187  1.00 18.47 ? 388  ASN A O     1 
ATOM   1690 C  CB    . ASN A 1 233 ? 4.101  -15.549 -11.067 1.00 14.61 ? 388  ASN A CB    1 
ATOM   1691 C  CG    . ASN A 1 233 ? 4.706  -14.223 -11.449 1.00 16.88 ? 388  ASN A CG    1 
ATOM   1692 O  OD1   . ASN A 1 233 ? 5.165  -13.456 -10.597 1.00 17.78 ? 388  ASN A OD1   1 
ATOM   1693 N  ND2   . ASN A 1 233 ? 4.730  -13.940 -12.725 1.00 16.33 ? 388  ASN A ND2   1 
ATOM   1694 N  N     . ASN A 1 234 ? 4.283  -18.229 -8.831  1.00 12.60 ? 389  ASN A N     1 
ATOM   1695 C  CA    . ASN A 1 234 ? 3.524  -19.349 -8.295  1.00 13.58 ? 389  ASN A CA    1 
ATOM   1696 C  C     . ASN A 1 234 ? 4.485  -20.057 -7.352  1.00 13.33 ? 389  ASN A C     1 
ATOM   1697 O  O     . ASN A 1 234 ? 4.997  -21.128 -7.625  1.00 15.76 ? 389  ASN A O     1 
ATOM   1698 C  CB    . ASN A 1 234 ? 3.021  -20.262 -9.417  1.00 14.47 ? 389  ASN A CB    1 
ATOM   1699 C  CG    . ASN A 1 234 ? 1.958  -21.191 -8.946  1.00 17.60 ? 389  ASN A CG    1 
ATOM   1700 O  OD1   . ASN A 1 234 ? 1.565  -21.207 -7.779  1.00 16.75 ? 389  ASN A OD1   1 
ATOM   1701 N  ND2   . ASN A 1 234 ? 1.440  -21.967 -9.882  1.00 22.32 ? 389  ASN A ND2   1 
ATOM   1702 N  N     . HIS A 1 235 ? 4.774  -19.402 -6.230  1.00 13.50 ? 390  HIS A N     1 
ATOM   1703 C  CA    . HIS A 1 235 ? 6.014  -19.621 -5.491  1.00 12.53 ? 390  HIS A CA    1 
ATOM   1704 C  C     . HIS A 1 235 ? 5.836  -20.327 -4.175  1.00 13.10 ? 390  HIS A C     1 
ATOM   1705 O  O     . HIS A 1 235 ? 6.832  -20.521 -3.476  1.00 14.25 ? 390  HIS A O     1 
ATOM   1706 C  CB    . HIS A 1 235 ? 6.701  -18.259 -5.191  1.00 13.25 ? 390  HIS A CB    1 
ATOM   1707 C  CG    . HIS A 1 235 ? 5.862  -17.348 -4.392  1.00 14.73 ? 390  HIS A CG    1 
ATOM   1708 N  ND1   . HIS A 1 235 ? 5.374  -16.164 -4.885  1.00 18.16 ? 390  HIS A ND1   1 
ATOM   1709 C  CD2   . HIS A 1 235 ? 5.324  -17.501 -3.154  1.00 11.94 ? 390  HIS A CD2   1 
ATOM   1710 C  CE1   . HIS A 1 235 ? 4.593  -15.599 -3.967  1.00 18.06 ? 390  HIS A CE1   1 
ATOM   1711 N  NE2   . HIS A 1 235 ? 4.564  -16.384 -2.902  1.00 13.13 ? 390  HIS A NE2   1 
ATOM   1712 N  N     . GLY A 1 236 ? 4.623  -20.672 -3.799  1.00 13.32 ? 391  GLY A N     1 
ATOM   1713 C  CA    . GLY A 1 236 ? 4.446  -21.245 -2.480  1.00 14.12 ? 391  GLY A CA    1 
ATOM   1714 C  C     . GLY A 1 236 ? 4.289  -22.743 -2.523  1.00 12.13 ? 391  GLY A C     1 
ATOM   1715 O  O     . GLY A 1 236 ? 4.010  -23.331 -3.562  1.00 14.06 ? 391  GLY A O     1 
ATOM   1716 N  N     . LYS A 1 237 ? 4.471  -23.380 -1.383  1.00 11.67 ? 392  LYS A N     1 
ATOM   1717 C  CA    . LYS A 1 237 ? 4.045  -24.769 -1.290  1.00 13.70 ? 392  LYS A CA    1 
ATOM   1718 C  C     . LYS A 1 237 ? 2.514  -24.860 -1.354  1.00 14.35 ? 392  LYS A C     1 
ATOM   1719 O  O     . LYS A 1 237 ? 1.945  -25.711 -2.065  1.00 14.99 ? 392  LYS A O     1 
ATOM   1720 C  CB    . LYS A 1 237 ? 4.534  -25.361 0.011   1.00 13.75 ? 392  LYS A CB    1 
ATOM   1721 C  CG    . LYS A 1 237 ? 4.052  -26.820 0.111   1.00 16.33 ? 392  LYS A CG    1 
ATOM   1722 C  CD    . LYS A 1 237 ? 4.697  -27.599 1.277   1.00 21.17 ? 392  LYS A CD    1 
ATOM   1723 C  CE    . LYS A 1 237 ? 6.165  -27.854 0.966   1.00 20.07 ? 392  LYS A CE    1 
ATOM   1724 N  NZ    . LYS A 1 237 ? 6.262  -28.609 -0.334  1.00 21.08 ? 392  LYS A NZ    1 
ATOM   1725 N  N     . SER A 1 238 ? 1.819  -23.967 -0.661  1.00 11.81 ? 393  SER A N     1 
ATOM   1726 C  CA    . SER A 1 238 ? 0.377  -23.828 -0.823  1.00 12.42 ? 393  SER A CA    1 
ATOM   1727 C  C     . SER A 1 238 ? 0.040  -23.203 -2.158  1.00 12.86 ? 393  SER A C     1 
ATOM   1728 O  O     . SER A 1 238 ? 0.580  -22.146 -2.535  1.00 13.12 ? 393  SER A O     1 
ATOM   1729 C  CB    . SER A 1 238 ? -0.159 -22.941 0.273   1.00 12.81 ? 393  SER A CB    1 
ATOM   1730 O  OG    . SER A 1 238 ? -1.544 -22.728 -0.006  1.00 16.48 ? 393  SER A OG    1 
ATOM   1731 N  N     . LYS A 1 239 ? -0.922 -23.801 -2.843  1.00 13.16 ? 394  LYS A N     1 
ATOM   1732 C  CA    . LYS A 1 239 ? -1.403 -23.209 -4.083  1.00 12.73 ? 394  LYS A CA    1 
ATOM   1733 C  C     . LYS A 1 239 ? -2.027 -21.841 -3.864  1.00 13.17 ? 394  LYS A C     1 
ATOM   1734 O  O     . LYS A 1 239 ? -2.042 -21.029 -4.790  1.00 14.73 ? 394  LYS A O     1 
ATOM   1735 C  CB    . LYS A 1 239 ? -2.410 -24.157 -4.756  1.00 12.91 ? 394  LYS A CB    1 
ATOM   1736 C  CG    . LYS A 1 239 ? -1.726 -25.392 -5.248  1.00 11.48 ? 394  LYS A CG    1 
ATOM   1737 C  CD    . LYS A 1 239 ? -2.767 -26.432 -5.634  1.00 13.28 ? 394  LYS A CD    1 
ATOM   1738 C  CE    . LYS A 1 239 ? -2.075 -27.775 -5.885  1.00 12.63 ? 394  LYS A CE    1 
ATOM   1739 N  NZ    . LYS A 1 239 ? -3.103 -28.818 -6.211  1.00 12.67 ? 394  LYS A NZ    1 
ATOM   1740 N  N     . THR A 1 240 ? -2.508 -21.558 -2.657  1.00 12.67 ? 395  THR A N     1 
ATOM   1741 C  CA    . THR A 1 240 ? -3.085 -20.248 -2.356  1.00 14.34 ? 395  THR A CA    1 
ATOM   1742 C  C     . THR A 1 240 ? -2.125 -19.282 -1.679  1.00 15.09 ? 395  THR A C     1 
ATOM   1743 O  O     . THR A 1 240 ? -2.578 -18.222 -1.216  1.00 16.84 ? 395  THR A O     1 
ATOM   1744 C  CB    . THR A 1 240 ? -4.418 -20.406 -1.599  1.00 16.68 ? 395  THR A CB    1 
ATOM   1745 O  OG1   . THR A 1 240 ? -4.246 -21.319 -0.484  1.00 16.40 ? 395  THR A OG1   1 
ATOM   1746 C  CG2   . THR A 1 240 ? -5.453 -20.979 -2.535  1.00 15.76 ? 395  THR A CG2   1 
ATOM   1747 N  N     . CYS A 1 241 ? -0.806 -19.563 -1.718  1.00 12.01 ? 396  CYS A N     1 
ATOM   1748 C  CA    . CYS A 1 241 ? 0.181  -18.631 -1.168  1.00 14.02 ? 396  CYS A CA    1 
ATOM   1749 C  C     . CYS A 1 241 ? -0.017 -17.263 -1.768  1.00 13.32 ? 396  CYS A C     1 
ATOM   1750 O  O     . CYS A 1 241 ? -0.143 -17.116 -2.985  1.00 16.32 ? 396  CYS A O     1 
ATOM   1751 C  CB    . CYS A 1 241 ? 1.581  -19.185 -1.411  1.00 13.29 ? 396  CYS A CB    1 
ATOM   1752 S  SG    . CYS A 1 241 ? 2.835  -18.285 -0.362  1.00 15.12 ? 396  CYS A SG    1 
ATOM   1753 N  N     . CYS A 1 242 ? -0.090 -16.256 -0.902  1.00 17.21 ? 397  CYS A N     1 
ATOM   1754 C  CA    . CYS A 1 242 ? -0.239 -14.865 -1.347  1.00 18.59 ? 397  CYS A CA    1 
ATOM   1755 C  C     . CYS A 1 242 ? -1.578 -14.556 -2.018  1.00 20.95 ? 397  CYS A C     1 
ATOM   1756 O  O     . CYS A 1 242 ? -1.718 -13.489 -2.622  1.00 23.62 ? 397  CYS A O     1 
ATOM   1757 C  CB    . CYS A 1 242 ? 0.924  -14.300 -2.173  1.00 18.05 ? 397  CYS A CB    1 
ATOM   1758 S  SG    . CYS A 1 242 ? 2.447  -14.275 -1.125  1.00 17.69 ? 397  CYS A SG    1 
ATOM   1759 N  N     . GLU A 1 243 ? -2.577 -15.446 -1.931  1.00 18.14 ? 398  GLU A N     1 
ATOM   1760 C  CA    . GLU A 1 243 ? -3.904 -15.171 -2.489  1.00 18.68 ? 398  GLU A CA    1 
ATOM   1761 C  C     . GLU A 1 243 ? -4.899 -14.738 -1.436  1.00 20.11 ? 398  GLU A C     1 
ATOM   1762 O  O     . GLU A 1 243 ? -6.060 -14.453 -1.763  1.00 24.42 ? 398  GLU A O     1 
ATOM   1763 C  CB    . GLU A 1 243 ? -4.468 -16.404 -3.213  1.00 17.60 ? 398  GLU A CB    1 
ATOM   1764 C  CG    . GLU A 1 243 ? -3.828 -16.619 -4.557  1.00 19.09 ? 398  GLU A CG    1 
ATOM   1765 C  CD    . GLU A 1 243 ? -4.642 -17.543 -5.471  1.00 27.85 ? 398  GLU A CD    1 
ATOM   1766 O  OE1   . GLU A 1 243 ? -5.658 -18.118 -4.998  1.00 22.63 ? 398  GLU A OE1   1 
ATOM   1767 O  OE2   . GLU A 1 243 ? -4.273 -17.653 -6.658  1.00 21.54 ? 398  GLU A OE2   1 
ATOM   1768 N  N     . ASN A 1 244 ? -4.506 -14.740 -0.177  1.00 18.59 ? 399  ASN A N     1 
ATOM   1769 C  CA    . ASN A 1 244 ? -5.386 -14.290 0.878   1.00 22.99 ? 399  ASN A CA    1 
ATOM   1770 C  C     . ASN A 1 244 ? -4.528 -13.741 1.998   1.00 27.82 ? 399  ASN A C     1 
ATOM   1771 O  O     . ASN A 1 244 ? -3.317 -13.977 2.057   1.00 21.75 ? 399  ASN A O     1 
ATOM   1772 C  CB    . ASN A 1 244 ? -6.295 -15.405 1.400   1.00 20.38 ? 399  ASN A CB    1 
ATOM   1773 C  CG    . ASN A 1 244 ? -5.516 -16.571 1.963   1.00 30.43 ? 399  ASN A CG    1 
ATOM   1774 O  OD1   . ASN A 1 244 ? -4.967 -16.489 3.056   1.00 27.69 ? 399  ASN A OD1   1 
ATOM   1775 N  ND2   . ASN A 1 244 ? -5.513 -17.701 1.236   1.00 22.23 ? 399  ASN A ND2   1 
ATOM   1776 N  N     . LYS A 1 245 ? -5.193 -13.038 2.917   1.00 26.27 ? 400  LYS A N     1 
ATOM   1777 C  CA    . LYS A 1 245 ? -4.487 -12.357 3.994   1.00 28.39 ? 400  LYS A CA    1 
ATOM   1778 C  C     . LYS A 1 245 ? -3.803 -13.299 4.977   1.00 30.68 ? 400  LYS A C     1 
ATOM   1779 O  O     . LYS A 1 245 ? -2.864 -12.874 5.657   1.00 36.38 ? 400  LYS A O     1 
ATOM   1780 C  CB    . LYS A 1 245 ? -5.409 -11.395 4.756   1.00 31.76 ? 400  LYS A CB    1 
ATOM   1781 N  N     . GLU A 1 246 ? -4.240 -14.550 5.087   1.00 24.85 ? 401  GLU A N     1 
ATOM   1782 C  CA    . GLU A 1 246 ? -3.581 -15.477 5.987   1.00 28.42 ? 401  GLU A CA    1 
ATOM   1783 C  C     . GLU A 1 246 ? -2.368 -16.150 5.367   1.00 22.18 ? 401  GLU A C     1 
ATOM   1784 O  O     . GLU A 1 246 ? -1.651 -16.860 6.080   1.00 25.20 ? 401  GLU A O     1 
ATOM   1785 C  CB    . GLU A 1 246 ? -4.566 -16.542 6.459   1.00 34.00 ? 401  GLU A CB    1 
ATOM   1786 C  CG    . GLU A 1 246 ? -5.701 -15.987 7.301   1.00 47.18 ? 401  GLU A CG    1 
ATOM   1787 C  CD    . GLU A 1 246 ? -6.981 -15.816 6.518   1.00 50.84 ? 401  GLU A CD    1 
ATOM   1788 O  OE1   . GLU A 1 246 ? -6.947 -15.171 5.441   1.00 51.41 ? 401  GLU A OE1   1 
ATOM   1789 O  OE2   . GLU A 1 246 ? -8.026 -16.331 6.974   1.00 68.78 ? 401  GLU A OE2   1 
ATOM   1790 N  N     . GLU A 1 247 ? -2.118 -15.955 4.073   1.00 20.54 ? 402  GLU A N     1 
ATOM   1791 C  CA    . GLU A 1 247 ? -1.000 -16.641 3.433   1.00 19.59 ? 402  GLU A CA    1 
ATOM   1792 C  C     . GLU A 1 247 ? -0.097 -15.652 2.683   1.00 21.26 ? 402  GLU A C     1 
ATOM   1793 O  O     . GLU A 1 247 ? 0.430  -15.954 1.592   1.00 21.65 ? 402  GLU A O     1 
ATOM   1794 C  CB    . GLU A 1 247 ? -1.505 -17.741 2.500   1.00 20.41 ? 402  GLU A CB    1 
ATOM   1795 C  CG    . GLU A 1 247 ? -2.313 -18.867 3.163   1.00 20.52 ? 402  GLU A CG    1 
ATOM   1796 C  CD    . GLU A 1 247 ? -2.634 -19.978 2.170   1.00 20.69 ? 402  GLU A CD    1 
ATOM   1797 O  OE1   . GLU A 1 247 ? -1.720 -20.720 1.740   1.00 22.62 ? 402  GLU A OE1   1 
ATOM   1798 O  OE2   . GLU A 1 247 ? -3.805 -20.082 1.786   1.00 22.24 ? 402  GLU A OE2   1 
ATOM   1799 N  N     . LYS A 1 248 ? 0.155  -14.465 3.268   1.00 22.46 ? 403  LYS A N     1 
ATOM   1800 C  CA    . LYS A 1 248 ? 0.991  -13.441 2.623   1.00 21.65 ? 403  LYS A CA    1 
ATOM   1801 C  C     . LYS A 1 248 ? 2.434  -13.659 3.044   1.00 18.93 ? 403  LYS A C     1 
ATOM   1802 O  O     . LYS A 1 248 ? 2.907  -13.087 4.027   1.00 22.91 ? 403  LYS A O     1 
ATOM   1803 C  CB    . LYS A 1 248 ? 0.510  -12.037 2.976   1.00 22.85 ? 403  LYS A CB    1 
ATOM   1804 C  CG    . LYS A 1 248 ? -0.823 -11.694 2.338   1.00 27.71 ? 403  LYS A CG    1 
ATOM   1805 C  CD    . LYS A 1 248 ? -0.694 -11.471 0.831   1.00 29.16 ? 403  LYS A CD    1 
ATOM   1806 C  CE    . LYS A 1 248 ? -2.052 -11.149 0.183   1.00 35.01 ? 403  LYS A CE    1 
ATOM   1807 N  NZ    . LYS A 1 248 ? -1.850 -10.798 -1.260  1.00 37.59 ? 403  LYS A NZ    1 
ATOM   1808 N  N     . CYS A 1 249 ? 3.149  -14.497 2.288   1.00 14.34 ? 404  CYS A N     1 
ATOM   1809 C  CA    . CYS A 1 249 ? 4.491  -14.854 2.684   1.00 14.76 ? 404  CYS A CA    1 
ATOM   1810 C  C     . CYS A 1 249 ? 5.443  -13.704 2.348   1.00 15.55 ? 404  CYS A C     1 
ATOM   1811 O  O     . CYS A 1 249 ? 5.094  -12.743 1.674   1.00 16.39 ? 404  CYS A O     1 
ATOM   1812 C  CB    . CYS A 1 249 ? 4.922  -16.171 2.013   1.00 13.98 ? 404  CYS A CB    1 
ATOM   1813 S  SG    . CYS A 1 249 ? 5.494  -15.983 0.232   1.00 13.55 ? 404  CYS A SG    1 
ATOM   1814 N  N     . CYS A 1 250 ? 6.687  -13.846 2.787   1.00 14.07 ? 405  CYS A N     1 
ATOM   1815 C  CA    . CYS A 1 250 ? 7.675  -12.798 2.587   1.00 14.42 ? 405  CYS A CA    1 
ATOM   1816 C  C     . CYS A 1 250 ? 8.729  -13.143 1.542   1.00 12.56 ? 405  CYS A C     1 
ATOM   1817 O  O     . CYS A 1 250 ? 9.753  -12.478 1.477   1.00 13.94 ? 405  CYS A O     1 
ATOM   1818 C  CB    . CYS A 1 250 ? 8.232  -12.361 3.954   1.00 17.47 ? 405  CYS A CB    1 
ATOM   1819 S  SG    . CYS A 1 250 ? 9.408  -13.485 4.695   1.00 17.74 ? 405  CYS A SG    1 
ATOM   1820 N  N     . ARG A 1 251 ? 8.479  -14.130 0.705   1.00 13.98 ? 406  ARG A N     1 
ATOM   1821 C  CA    . ARG A 1 251 ? 9.482  -14.515 -0.285  1.00 13.00 ? 406  ARG A CA    1 
ATOM   1822 C  C     . ARG A 1 251 ? 9.849  -13.367 -1.237  1.00 12.64 ? 406  ARG A C     1 
ATOM   1823 O  O     . ARG A 1 251 ? 11.036 -13.065 -1.399  1.00 12.80 ? 406  ARG A O     1 
ATOM   1824 C  CB    . ARG A 1 251 ? 8.979  -15.714 -1.098  1.00 12.06 ? 406  ARG A CB    1 
ATOM   1825 C  CG    . ARG A 1 251 ? 9.074  -17.050 -0.338  1.00 12.39 ? 406  ARG A CG    1 
ATOM   1826 C  CD    . ARG A 1 251 ? 8.690  -18.191 -1.298  1.00 13.27 ? 406  ARG A CD    1 
ATOM   1827 N  NE    . ARG A 1 251 ? 8.651  -19.496 -0.624  1.00 12.52 ? 406  ARG A NE    1 
ATOM   1828 C  CZ    . ARG A 1 251 ? 7.543  -20.009 -0.067  1.00 12.28 ? 406  ARG A CZ    1 
ATOM   1829 N  NH1   . ARG A 1 251 ? 6.407  -19.304 0.014   1.00 13.36 ? 406  ARG A NH1   1 
ATOM   1830 N  NH2   . ARG A 1 251 ? 7.572  -21.293 0.343   1.00 13.77 ? 406  ARG A NH2   1 
ATOM   1831 N  N     . LYS A 1 252 ? 8.861  -12.732 -1.878  1.00 12.14 ? 407  LYS A N     1 
ATOM   1832 C  CA    . LYS A 1 252 ? 9.180  -11.649 -2.826  1.00 11.98 ? 407  LYS A CA    1 
ATOM   1833 C  C     . LYS A 1 252 ? 9.796  -10.454 -2.118  1.00 13.04 ? 407  LYS A C     1 
ATOM   1834 O  O     . LYS A 1 252 ? 10.727 -9.843  -2.672  1.00 12.77 ? 407  LYS A O     1 
ATOM   1835 C  CB    . LYS A 1 252 ? 7.943  -11.238 -3.649  1.00 14.44 ? 407  LYS A CB    1 
ATOM   1836 C  CG    . LYS A 1 252 ? 7.584  -12.276 -4.668  1.00 14.88 ? 407  LYS A CG    1 
ATOM   1837 C  CD    . LYS A 1 252 ? 6.605  -11.734 -5.742  1.00 18.44 ? 407  LYS A CD    1 
ATOM   1838 C  CE    . LYS A 1 252 ? 6.399  -12.832 -6.743  1.00 20.10 ? 407  LYS A CE    1 
ATOM   1839 N  NZ    . LYS A 1 252 ? 5.461  -12.446 -7.876  1.00 17.94 ? 407  LYS A NZ    1 
ATOM   1840 N  N     . ASP A 1 253 ? 9.315  -10.147 -0.884  1.00 13.03 ? 408  ASP A N     1 
ATOM   1841 C  CA    . ASP A 1 253 ? 9.920  -9.063  -0.105  1.00 12.56 ? 408  ASP A CA    1 
ATOM   1842 C  C     . ASP A 1 253 ? 11.407 -9.343  0.127   1.00 12.09 ? 408  ASP A C     1 
ATOM   1843 O  O     . ASP A 1 253 ? 12.254 -8.452  -0.036  1.00 13.36 ? 408  ASP A O     1 
ATOM   1844 C  CB    . ASP A 1 253 ? 9.203  -8.897  1.224   1.00 14.43 ? 408  ASP A CB    1 
ATOM   1845 C  CG    . ASP A 1 253 ? 7.830  -8.198  1.079   1.00 21.64 ? 408  ASP A CG    1 
ATOM   1846 O  OD1   . ASP A 1 253 ? 7.585  -7.540  0.032   1.00 22.44 ? 408  ASP A OD1   1 
ATOM   1847 O  OD2   . ASP A 1 253 ? 6.997  -8.297  2.020   1.00 23.00 ? 408  ASP A OD2   1 
ATOM   1848 N  N     . CYS A 1 254 ? 11.758 -10.584 0.432   1.00 11.82 ? 409  CYS A N     1 
ATOM   1849 C  CA    . CYS A 1 254 ? 13.142 -10.898 0.696   1.00 13.01 ? 409  CYS A CA    1 
ATOM   1850 C  C     . CYS A 1 254 ? 13.989 -10.749 -0.567  1.00 12.03 ? 409  CYS A C     1 
ATOM   1851 O  O     . CYS A 1 254 ? 15.115 -10.216 -0.497  1.00 13.58 ? 409  CYS A O     1 
ATOM   1852 C  CB    . CYS A 1 254 ? 13.291 -12.300 1.242   1.00 13.05 ? 409  CYS A CB    1 
ATOM   1853 S  SG    . CYS A 1 254 ? 12.841 -12.384 2.991   1.00 17.41 ? 409  CYS A SG    1 
ATOM   1854 N  N     . LEU A 1 255 ? 13.473 -11.210 -1.746  1.00 12.59 ? 410  LEU A N     1 
ATOM   1855 C  CA    . LEU A 1 255 ? 14.197 -11.000 -2.992  1.00 12.59 ? 410  LEU A CA    1 
ATOM   1856 C  C     . LEU A 1 255 ? 14.337 -9.513  -3.293  1.00 11.61 ? 410  LEU A C     1 
ATOM   1857 O  O     . LEU A 1 255 ? 15.425 -9.068  -3.688  1.00 12.21 ? 410  LEU A O     1 
ATOM   1858 C  CB    . LEU A 1 255 ? 13.507 -11.791 -4.093  1.00 12.46 ? 410  LEU A CB    1 
ATOM   1859 C  CG    . LEU A 1 255 ? 14.141 -11.585 -5.470  1.00 11.85 ? 410  LEU A CG    1 
ATOM   1860 C  CD1   . LEU A 1 255 ? 15.691 -11.934 -5.495  1.00 13.22 ? 410  LEU A CD1   1 
ATOM   1861 C  CD2   . LEU A 1 255 ? 13.451 -12.473 -6.501  1.00 13.89 ? 410  LEU A CD2   1 
ATOM   1862 N  N     . LYS A 1 256 ? 13.277 -8.729  -3.027  1.00 11.93 ? 411  LYS A N     1 
ATOM   1863 C  CA    . LYS A 1 256 ? 13.383 -7.287  -3.276  1.00 12.08 ? 411  LYS A CA    1 
ATOM   1864 C  C     . LYS A 1 256 ? 14.444 -6.646  -2.405  1.00 11.52 ? 411  LYS A C     1 
ATOM   1865 O  O     . LYS A 1 256 ? 15.247 -5.851  -2.911  1.00 11.97 ? 411  LYS A O     1 
ATOM   1866 C  CB    . LYS A 1 256 ? 12.068 -6.602  -3.036  1.00 11.21 ? 411  LYS A CB    1 
ATOM   1867 C  CG    . LYS A 1 256 ? 10.982 -6.900  -4.091  1.00 12.82 ? 411  LYS A CG    1 
ATOM   1868 C  CD    . LYS A 1 256 ? 9.684  -6.194  -3.653  1.00 14.86 ? 411  LYS A CD    1 
ATOM   1869 C  CE    . LYS A 1 256 ? 8.634  -6.405  -4.716  1.00 17.76 ? 411  LYS A CE    1 
ATOM   1870 N  NZ    . LYS A 1 256 ? 7.371  -5.769  -4.255  1.00 26.86 ? 411  LYS A NZ    1 
ATOM   1871 N  N     . LEU A 1 257 ? 14.507 -7.038  -1.119  1.00 11.87 ? 412  LEU A N     1 
ATOM   1872 C  CA    . LEU A 1 257 ? 15.528 -6.476  -0.234  1.00 12.16 ? 412  LEU A CA    1 
ATOM   1873 C  C     . LEU A 1 257 ? 16.928 -6.892  -0.650  1.00 11.96 ? 412  LEU A C     1 
ATOM   1874 O  O     . LEU A 1 257 ? 17.864 -6.085  -0.563  1.00 13.60 ? 412  LEU A O     1 
ATOM   1875 C  CB    . LEU A 1 257 ? 15.255 -6.858  1.198   1.00 13.06 ? 412  LEU A CB    1 
ATOM   1876 C  CG    . LEU A 1 257 ? 14.023 -6.210  1.825   1.00 13.85 ? 412  LEU A CG    1 
ATOM   1877 C  CD1   . LEU A 1 257 ? 13.662 -6.930  3.106   1.00 15.37 ? 412  LEU A CD1   1 
ATOM   1878 C  CD2   . LEU A 1 257 ? 14.225 -4.702  2.107   1.00 15.65 ? 412  LEU A CD2   1 
ATOM   1879 N  N     . MET A 1 258 ? 17.122 -8.148  -1.046  1.00 12.46 ? 413  MET A N     1 
ATOM   1880 C  CA    . MET A 1 258 ? 18.436 -8.573  -1.516  1.00 12.23 ? 413  MET A CA    1 
ATOM   1881 C  C     . MET A 1 258 ? 18.835 -7.808  -2.776  1.00 13.44 ? 413  MET A C     1 
ATOM   1882 O  O     . MET A 1 258 ? 20.003 -7.415  -2.940  1.00 13.21 ? 413  MET A O     1 
ATOM   1883 C  CB    . MET A 1 258 ? 18.396 -10.061 -1.885  1.00 14.57 ? 413  MET A CB    1 
ATOM   1884 C  CG    . MET A 1 258 ? 18.377 -10.913 -0.672  1.00 14.15 ? 413  MET A CG    1 
ATOM   1885 S  SD    . MET A 1 258 ? 19.894 -10.850 0.386   1.00 19.48 ? 413  MET A SD    1 
ATOM   1886 C  CE    . MET A 1 258 ? 21.235 -11.265 -0.805  1.00 22.27 ? 413  MET A CE    1 
ATOM   1887 N  N     . LYS A 1 259 ? 17.879 -7.624  -3.715  1.00 12.25 ? 414  LYS A N     1 
ATOM   1888 C  CA    . LYS A 1 259 ? 18.136 -6.829  -4.915  1.00 13.05 ? 414  LYS A CA    1 
ATOM   1889 C  C     . LYS A 1 259 ? 18.538 -5.410  -4.538  1.00 13.59 ? 414  LYS A C     1 
ATOM   1890 O  O     . LYS A 1 259 ? 19.451 -4.861  -5.140  1.00 13.77 ? 414  LYS A O     1 
ATOM   1891 C  CB    . LYS A 1 259 ? 16.884 -6.800  -5.791  1.00 12.99 ? 414  LYS A CB    1 
ATOM   1892 C  CG    . LYS A 1 259 ? 16.695 -8.154  -6.526  1.00 13.60 ? 414  LYS A CG    1 
ATOM   1893 C  CD    . LYS A 1 259 ? 15.279 -8.167  -7.185  1.00 15.85 ? 414  LYS A CD    1 
ATOM   1894 C  CE    . LYS A 1 259 ? 15.097 -6.974  -8.131  1.00 20.96 ? 414  LYS A CE    1 
ATOM   1895 N  NZ    . LYS A 1 259 ? 16.052 -7.215  -9.202  1.00 24.47 ? 414  LYS A NZ    1 
ATOM   1896 N  N     . TYR A 1 260 ? 17.831 -4.816  -3.593  1.00 12.57 ? 415  TYR A N     1 
ATOM   1897 C  CA    . TYR A 1 260 ? 18.164 -3.432  -3.221  1.00 12.68 ? 415  TYR A CA    1 
ATOM   1898 C  C     . TYR A 1 260 ? 19.508 -3.357  -2.513  1.00 14.72 ? 415  TYR A C     1 
ATOM   1899 O  O     . TYR A 1 260 ? 20.271 -2.414  -2.725  1.00 13.88 ? 415  TYR A O     1 
ATOM   1900 C  CB    . TYR A 1 260 ? 17.076 -2.887  -2.320  1.00 12.96 ? 415  TYR A CB    1 
ATOM   1901 C  CG    . TYR A 1 260 ? 17.121 -1.384  -2.028  1.00 14.10 ? 415  TYR A CG    1 
ATOM   1902 C  CD1   . TYR A 1 260 ? 17.275 -0.481  -3.039  1.00 16.29 ? 415  TYR A CD1   1 
ATOM   1903 C  CD2   . TYR A 1 260 ? 17.011 -0.926  -0.740  1.00 17.17 ? 415  TYR A CD2   1 
ATOM   1904 C  CE1   . TYR A 1 260 ? 17.287 0.906   -2.782  1.00 18.38 ? 415  TYR A CE1   1 
ATOM   1905 C  CE2   . TYR A 1 260 ? 17.046 0.450   -0.472  1.00 19.41 ? 415  TYR A CE2   1 
ATOM   1906 C  CZ    . TYR A 1 260 ? 17.168 1.332   -1.513  1.00 22.66 ? 415  TYR A CZ    1 
ATOM   1907 O  OH    . TYR A 1 260 ? 17.203 2.701   -1.303  1.00 22.77 ? 415  TYR A OH    1 
ATOM   1908 N  N     . LEU A 1 261 ? 19.819 -4.334  -1.676  1.00 12.85 ? 416  LEU A N     1 
ATOM   1909 C  CA    . LEU A 1 261 ? 21.126 -4.375  -1.042  1.00 12.57 ? 416  LEU A CA    1 
ATOM   1910 C  C     . LEU A 1 261 ? 22.226 -4.345  -2.083  1.00 13.38 ? 416  LEU A C     1 
ATOM   1911 O  O     . LEU A 1 261 ? 23.171 -3.535  -2.008  1.00 13.93 ? 416  LEU A O     1 
ATOM   1912 C  CB    . LEU A 1 261 ? 21.224 -5.626  -0.174  1.00 12.95 ? 416  LEU A CB    1 
ATOM   1913 C  CG    . LEU A 1 261 ? 22.576 -5.860  0.471   1.00 17.77 ? 416  LEU A CG    1 
ATOM   1914 C  CD1   . LEU A 1 261 ? 22.970 -4.689  1.358   1.00 17.36 ? 416  LEU A CD1   1 
ATOM   1915 C  CD2   . LEU A 1 261 ? 22.500 -7.200  1.261   1.00 17.33 ? 416  LEU A CD2   1 
ATOM   1916 N  N     . LEU A 1 262 ? 22.146 -5.199  -3.073  1.00 12.76 ? 417  LEU A N     1 
ATOM   1917 C  CA    . LEU A 1 262 ? 23.148 -5.225  -4.111  1.00 14.20 ? 417  LEU A CA    1 
ATOM   1918 C  C     . LEU A 1 262 ? 23.160 -3.979  -4.987  1.00 15.49 ? 417  LEU A C     1 
ATOM   1919 O  O     . LEU A 1 262 ? 24.209 -3.427  -5.214  1.00 16.60 ? 417  LEU A O     1 
ATOM   1920 C  CB    . LEU A 1 262 ? 22.999 -6.457  -4.973  1.00 14.84 ? 417  LEU A CB    1 
ATOM   1921 C  CG    . LEU A 1 262 ? 24.126 -6.619  -5.997  1.00 16.52 ? 417  LEU A CG    1 
ATOM   1922 C  CD1   . LEU A 1 262 ? 25.484 -6.815  -5.342  1.00 18.72 ? 417  LEU A CD1   1 
ATOM   1923 C  CD2   . LEU A 1 262 ? 23.829 -7.767  -6.932  1.00 17.57 ? 417  LEU A CD2   1 
ATOM   1924 N  N     A GLU A 1 263 ? 21.988 -3.474  -5.330  0.66 14.49 ? 418  GLU A N     1 
ATOM   1925 N  N     B GLU A 1 263 ? 22.000 -3.476  -5.316  0.34 14.49 ? 418  GLU A N     1 
ATOM   1926 C  CA    A GLU A 1 263 ? 21.917 -2.243  -6.111  0.66 19.31 ? 418  GLU A CA    1 
ATOM   1927 C  CA    B GLU A 1 263 ? 21.929 -2.256  -6.105  0.34 19.34 ? 418  GLU A CA    1 
ATOM   1928 C  C     A GLU A 1 263 ? 22.591 -1.095  -5.372  0.66 17.29 ? 418  GLU A C     1 
ATOM   1929 C  C     B GLU A 1 263 ? 22.590 -1.094  -5.372  0.34 17.31 ? 418  GLU A C     1 
ATOM   1930 O  O     A GLU A 1 263 ? 23.342 -0.345  -5.967  0.66 17.87 ? 418  GLU A O     1 
ATOM   1931 O  O     B GLU A 1 263 ? 23.353 -0.351  -5.963  0.34 17.90 ? 418  GLU A O     1 
ATOM   1932 C  CB    A GLU A 1 263 ? 20.472 -1.865  -6.439  0.66 21.77 ? 418  GLU A CB    1 
ATOM   1933 C  CB    B GLU A 1 263 ? 20.482 -1.914  -6.433  0.34 21.91 ? 418  GLU A CB    1 
ATOM   1934 C  CG    A GLU A 1 263 ? 19.864 -2.596  -7.631  0.66 35.83 ? 418  GLU A CG    1 
ATOM   1935 C  CG    B GLU A 1 263 ? 20.321 -0.747  -7.386  0.34 35.83 ? 418  GLU A CG    1 
ATOM   1936 C  CD    A GLU A 1 263 ? 18.564 -1.967  -8.116  0.66 56.99 ? 418  GLU A CD    1 
ATOM   1937 C  CD    B GLU A 1 263 ? 18.950 -0.700  -8.028  0.34 56.99 ? 418  GLU A CD    1 
ATOM   1938 O  OE1   A GLU A 1 263 ? 18.368 -0.763  -7.871  0.66 52.95 ? 418  GLU A OE1   1 
ATOM   1939 O  OE1   B GLU A 1 263 ? 18.113 -1.566  -7.712  0.34 48.82 ? 418  GLU A OE1   1 
ATOM   1940 O  OE2   A GLU A 1 263 ? 17.737 -2.670  -8.747  0.66 48.80 ? 418  GLU A OE2   1 
ATOM   1941 O  OE2   B GLU A 1 263 ? 18.706 0.206   -8.848  0.34 45.55 ? 418  GLU A OE2   1 
ATOM   1942 N  N     . GLN A 1 264 ? 22.294 -0.957  -4.085  1.00 14.91 ? 419  GLN A N     1 
ATOM   1943 C  CA    . GLN A 1 264 ? 22.853 0.158   -3.321  1.00 16.02 ? 419  GLN A CA    1 
ATOM   1944 C  C     . GLN A 1 264 ? 24.346 0.018   -3.186  1.00 18.13 ? 419  GLN A C     1 
ATOM   1945 O  O     . GLN A 1 264 ? 25.092 1.000   -3.298  1.00 16.89 ? 419  GLN A O     1 
ATOM   1946 C  CB    . GLN A 1 264 ? 22.223 0.175   -1.936  1.00 16.93 ? 419  GLN A CB    1 
ATOM   1947 C  CG    . GLN A 1 264 ? 20.789 0.615   -1.912  1.00 20.66 ? 419  GLN A CG    1 
ATOM   1948 C  CD    . GLN A 1 264 ? 20.642 2.062   -2.146  1.00 24.84 ? 419  GLN A CD    1 
ATOM   1949 O  OE1   . GLN A 1 264 ? 20.573 2.506   -3.280  1.00 28.71 ? 419  GLN A OE1   1 
ATOM   1950 N  NE2   . GLN A 1 264 ? 20.603 2.829   -1.055  1.00 29.27 ? 419  GLN A NE2   1 
ATOM   1951 N  N     . LEU A 1 265 ? 24.816 -1.190  -2.921  1.00 15.57 ? 420  LEU A N     1 
ATOM   1952 C  CA    . LEU A 1 265 ? 26.257 -1.378  -2.845  1.00 15.96 ? 420  LEU A CA    1 
ATOM   1953 C  C     . LEU A 1 265 ? 26.944 -1.092  -4.173  1.00 17.89 ? 420  LEU A C     1 
ATOM   1954 O  O     . LEU A 1 265 ? 28.013 -0.458  -4.193  1.00 20.06 ? 420  LEU A O     1 
ATOM   1955 C  CB    . LEU A 1 265 ? 26.614 -2.767  -2.343  1.00 14.93 ? 420  LEU A CB    1 
ATOM   1956 C  CG    . LEU A 1 265 ? 26.288 -2.976  -0.875  1.00 15.09 ? 420  LEU A CG    1 
ATOM   1957 C  CD1   . LEU A 1 265 ? 26.549 -4.441  -0.501  1.00 18.49 ? 420  LEU A CD1   1 
ATOM   1958 C  CD2   . LEU A 1 265 ? 27.074 -2.131  0.063   1.00 20.33 ? 420  LEU A CD2   1 
ATOM   1959 N  N     . LYS A 1 266 ? 26.353 -1.533  -5.290  1.00 17.21 ? 421  LYS A N     1 
ATOM   1960 C  CA    . LYS A 1 266 ? 26.981 -1.283  -6.584  1.00 22.18 ? 421  LYS A CA    1 
ATOM   1961 C  C     . LYS A 1 266 ? 27.001 0.194   -6.902  1.00 21.00 ? 421  LYS A C     1 
ATOM   1962 O  O     . LYS A 1 266 ? 27.958 0.669   -7.520  1.00 26.84 ? 421  LYS A O     1 
ATOM   1963 C  CB    . LYS A 1 266 ? 26.241 -2.040  -7.678  1.00 21.59 ? 421  LYS A CB    1 
ATOM   1964 C  CG    . LYS A 1 266 ? 26.581 -3.540  -7.675  1.00 20.36 ? 421  LYS A CG    1 
ATOM   1965 C  CD    . LYS A 1 266 ? 25.717 -4.344  -8.598  1.00 22.55 ? 421  LYS A CD    1 
ATOM   1966 C  CE    . LYS A 1 266 ? 25.979 -3.993  -10.087 1.00 23.51 ? 421  LYS A CE    1 
ATOM   1967 N  NZ    . LYS A 1 266 ? 27.341 -4.300  -10.482 1.00 23.29 ? 421  LYS A NZ    1 
ATOM   1968 N  N     . GLU A 1 267 ? 25.970 0.926   -6.476  1.00 19.34 ? 422  GLU A N     1 
ATOM   1969 C  CA    . GLU A 1 267 ? 25.929 2.362   -6.720  1.00 21.40 ? 422  GLU A CA    1 
ATOM   1970 C  C     . GLU A 1 267 ? 26.944 3.088   -5.837  1.00 21.76 ? 422  GLU A C     1 
ATOM   1971 O  O     . GLU A 1 267 ? 27.686 3.952   -6.323  1.00 24.24 ? 422  GLU A O     1 
ATOM   1972 C  CB    . GLU A 1 267 ? 24.521 2.897   -6.501  1.00 25.62 ? 422  GLU A CB    1 
ATOM   1973 C  CG    . GLU A 1 267 ? 24.450 4.413   -6.645  1.00 37.60 ? 422  GLU A CG    1 
ATOM   1974 C  CD    . GLU A 1 267 ? 23.023 4.953   -6.630  1.00 66.76 ? 422  GLU A CD    1 
ATOM   1975 O  OE1   . GLU A 1 267 ? 22.073 4.139   -6.598  1.00 66.69 ? 422  GLU A OE1   1 
ATOM   1976 O  OE2   . GLU A 1 267 ? 22.850 6.193   -6.682  1.00 74.89 ? 422  GLU A OE2   1 
ATOM   1977 N  N     . ARG A 1 268 ? 27.002 2.746   -4.547  1.00 20.63 ? 423  ARG A N     1 
ATOM   1978 C  CA    . ARG A 1 268 ? 27.967 3.405   -3.657  1.00 22.41 ? 423  ARG A CA    1 
ATOM   1979 C  C     . ARG A 1 268 ? 29.394 3.158   -4.124  1.00 20.98 ? 423  ARG A C     1 
ATOM   1980 O  O     . ARG A 1 268 ? 30.240 4.074   -4.085  1.00 22.85 ? 423  ARG A O     1 
ATOM   1981 C  CB    . ARG A 1 268 ? 27.827 2.889   -2.221  1.00 21.74 ? 423  ARG A CB    1 
ATOM   1982 C  CG    . ARG A 1 268 ? 26.517 3.168   -1.524  1.00 26.50 ? 423  ARG A CG    1 
ATOM   1983 C  CD    . ARG A 1 268 ? 26.349 4.610   -1.150  1.00 29.32 ? 423  ARG A CD    1 
ATOM   1984 N  NE    . ARG A 1 268 ? 25.052 4.845   -0.526  1.00 33.72 ? 423  ARG A NE    1 
ATOM   1985 C  CZ    . ARG A 1 268 ? 24.799 4.716   0.772   1.00 39.24 ? 423  ARG A CZ    1 
ATOM   1986 N  NH1   . ARG A 1 268 ? 25.744 4.367   1.633   1.00 35.53 ? 423  ARG A NH1   1 
ATOM   1987 N  NH2   . ARG A 1 268 ? 23.570 4.954   1.221   1.00 36.95 ? 423  ARG A NH2   1 
ATOM   1988 N  N     . PHE A 1 269 ? 29.691 1.920   -4.535  1.00 21.02 ? 424  PHE A N     1 
ATOM   1989 C  CA    . PHE A 1 269 ? 31.011 1.474   -4.959  1.00 24.26 ? 424  PHE A CA    1 
ATOM   1990 C  C     . PHE A 1 269 ? 31.130 1.452   -6.481  1.00 25.56 ? 424  PHE A C     1 
ATOM   1991 O  O     . PHE A 1 269 ? 31.865 0.638   -7.037  1.00 33.79 ? 424  PHE A O     1 
ATOM   1992 C  CB    . PHE A 1 269 ? 31.311 0.087   -4.369  1.00 23.05 ? 424  PHE A CB    1 
ATOM   1993 C  CG    . PHE A 1 269 ? 31.514 0.081   -2.877  1.00 23.72 ? 424  PHE A CG    1 
ATOM   1994 C  CD1   . PHE A 1 269 ? 32.760 0.369   -2.331  1.00 24.55 ? 424  PHE A CD1   1 
ATOM   1995 C  CD2   . PHE A 1 269 ? 30.485 -0.256  -2.000  1.00 19.73 ? 424  PHE A CD2   1 
ATOM   1996 C  CE1   . PHE A 1 269 ? 32.938 0.353   -0.975  1.00 18.20 ? 424  PHE A CE1   1 
ATOM   1997 C  CE2   . PHE A 1 269 ? 30.661 -0.277  -0.639  1.00 22.79 ? 424  PHE A CE2   1 
ATOM   1998 C  CZ    . PHE A 1 269 ? 31.914 0.043   -0.124  1.00 21.57 ? 424  PHE A CZ    1 
ATOM   1999 N  N     . LYS A 1 270 ? 30.427 2.318   -7.163  1.00 26.06 ? 425  LYS A N     1 
ATOM   2000 C  CA    . LYS A 1 270 ? 30.447 2.325   -8.622  1.00 28.85 ? 425  LYS A CA    1 
ATOM   2001 C  C     . LYS A 1 270 ? 31.826 2.531   -9.239  1.00 42.64 ? 425  LYS A C     1 
ATOM   2002 O  O     . LYS A 1 270 ? 32.051 2.144   -10.367 1.00 45.56 ? 425  LYS A O     1 
ATOM   2003 C  CB    . LYS A 1 270 ? 29.477 3.366   -9.152  1.00 34.65 ? 425  LYS A CB    1 
ATOM   2004 C  CG    . LYS A 1 270 ? 29.891 4.804   -8.923  1.00 41.71 ? 425  LYS A CG    1 
ATOM   2005 C  CD    . LYS A 1 270 ? 29.044 5.750   -9.758  1.00 50.11 ? 425  LYS A CD    1 
ATOM   2006 C  CE    . LYS A 1 270 ? 27.567 5.506   -9.518  1.00 53.93 ? 425  LYS A CE    1 
ATOM   2007 N  NZ    . LYS A 1 270 ? 26.710 6.524   -10.182 1.00 58.79 ? 425  LYS A NZ    1 
ATOM   2008 N  N     . ASP A 1 271 ? 32.738 3.120   -8.503  1.00 34.48 ? 426  ASP A N     1 
ATOM   2009 C  CA    . ASP A 1 271 ? 34.078 3.298   -9.002  1.00 40.09 ? 426  ASP A CA    1 
ATOM   2010 C  C     . ASP A 1 271 ? 35.037 2.208   -8.534  1.00 39.70 ? 426  ASP A C     1 
ATOM   2011 O  O     . ASP A 1 271 ? 36.225 2.287   -8.767  1.00 38.23 ? 426  ASP A O     1 
ATOM   2012 C  CB    . ASP A 1 271 ? 34.563 4.689   -8.707  1.00 36.59 ? 426  ASP A CB    1 
ATOM   2013 C  CG    . ASP A 1 271 ? 33.690 5.749   -9.339  1.00 54.53 ? 426  ASP A CG    1 
ATOM   2014 O  OD1   . ASP A 1 271 ? 33.219 5.542   -10.477 1.00 52.86 ? 426  ASP A OD1   1 
ATOM   2015 O  OD2   . ASP A 1 271 ? 33.477 6.798   -8.704  1.00 58.64 ? 426  ASP A OD2   1 
ATOM   2016 N  N     . GLU A 1 272 ? 34.504 1.193   -7.882  1.00 35.55 ? 427  GLU A N     1 
ATOM   2017 C  CA    . GLU A 1 272 ? 35.297 0.072   -7.457  1.00 34.86 ? 427  GLU A CA    1 
ATOM   2018 C  C     . GLU A 1 272 ? 35.027 -1.047  -8.432  1.00 33.62 ? 427  GLU A C     1 
ATOM   2019 O  O     . GLU A 1 272 ? 33.927 -1.556  -8.521  1.00 34.94 ? 427  GLU A O     1 
ATOM   2020 C  CB    . GLU A 1 272 ? 34.854 -0.378  -6.077  1.00 30.00 ? 427  GLU A CB    1 
ATOM   2021 C  CG    . GLU A 1 272 ? 35.452 -1.670  -5.583  1.00 30.00 ? 427  GLU A CG    1 
ATOM   2022 C  CD    . GLU A 1 272 ? 36.950 -1.607  -5.474  1.00 30.00 ? 427  GLU A CD    1 
ATOM   2023 O  OE1   . GLU A 1 272 ? 37.452 -0.776  -4.690  1.00 30.00 ? 427  GLU A OE1   1 
ATOM   2024 O  OE2   . GLU A 1 272 ? 37.621 -2.393  -6.172  1.00 30.00 ? 427  GLU A OE2   1 
ATOM   2025 N  N     . LYS A 1 273 ? 36.057 -1.510  -9.088  1.00 34.48 ? 428  LYS A N     1 
ATOM   2026 C  CA    . LYS A 1 273 ? 35.913 -2.567  -10.063 1.00 36.15 ? 428  LYS A CA    1 
ATOM   2027 C  C     . LYS A 1 273 ? 35.439 -3.850  -9.455  1.00 31.56 ? 428  LYS A C     1 
ATOM   2028 O  O     . LYS A 1 273 ? 34.897 -4.674  -10.137 1.00 31.58 ? 428  LYS A O     1 
ATOM   2029 C  CB    . LYS A 1 273 ? 37.263 -2.828  -10.716 1.00 38.30 ? 428  LYS A CB    1 
ATOM   2030 N  N     . HIS A 1 274 ? 35.649 -4.016  -8.162  1.00 25.87 ? 429  HIS A N     1 
ATOM   2031 C  CA    . HIS A 1 274 ? 35.344 -5.264  -7.532  1.00 26.15 ? 429  HIS A CA    1 
ATOM   2032 C  C     . HIS A 1 274 ? 33.870 -5.623  -7.637  1.00 26.45 ? 429  HIS A C     1 
ATOM   2033 O  O     . HIS A 1 274 ? 33.553 -6.774  -7.575  1.00 25.69 ? 429  HIS A O     1 
ATOM   2034 C  CB    . HIS A 1 274 ? 35.827 -5.315  -6.089  1.00 29.40 ? 429  HIS A CB    1 
ATOM   2035 C  CG    . HIS A 1 274 ? 37.268 -5.679  -5.948  1.00 36.41 ? 429  HIS A CG    1 
ATOM   2036 N  ND1   . HIS A 1 274 ? 38.114 -5.045  -5.066  1.00 40.55 ? 429  HIS A ND1   1 
ATOM   2037 C  CD2   . HIS A 1 274 ? 38.013 -6.614  -6.580  1.00 36.75 ? 429  HIS A CD2   1 
ATOM   2038 C  CE1   . HIS A 1 274 ? 39.318 -5.578  -5.158  1.00 48.73 ? 429  HIS A CE1   1 
ATOM   2039 N  NE2   . HIS A 1 274 ? 39.284 -6.533  -6.070  1.00 48.53 ? 429  HIS A NE2   1 
ATOM   2040 N  N     . LEU A 1 275 ? 32.981 -4.647  -7.737  1.00 24.11 ? 430  LEU A N     1 
ATOM   2041 C  CA    . LEU A 1 275 ? 31.583 -4.966  -7.815  1.00 22.33 ? 430  LEU A CA    1 
ATOM   2042 C  C     . LEU A 1 275 ? 30.991 -5.000  -9.217  1.00 25.13 ? 430  LEU A C     1 
ATOM   2043 O  O     . LEU A 1 275 ? 29.828 -5.265  -9.363  1.00 23.01 ? 430  LEU A O     1 
ATOM   2044 C  CB    . LEU A 1 275 ? 30.761 -4.073  -6.888  1.00 27.21 ? 430  LEU A CB    1 
ATOM   2045 C  CG    . LEU A 1 275 ? 31.077 -4.169  -5.392  1.00 22.08 ? 430  LEU A CG    1 
ATOM   2046 C  CD1   . LEU A 1 275 ? 29.950 -3.557  -4.591  1.00 26.76 ? 430  LEU A CD1   1 
ATOM   2047 C  CD2   . LEU A 1 275 ? 31.292 -5.605  -4.946  1.00 23.27 ? 430  LEU A CD2   1 
ATOM   2048 N  N     . ASP A 1 276 ? 31.829 -4.826  -10.243 1.00 25.82 ? 431  ASP A N     1 
ATOM   2049 C  CA    . ASP A 1 276 ? 31.302 -4.703  -11.607 1.00 25.50 ? 431  ASP A CA    1 
ATOM   2050 C  C     . ASP A 1 276 ? 30.627 -5.983  -12.087 1.00 24.99 ? 431  ASP A C     1 
ATOM   2051 O  O     . ASP A 1 276 ? 29.636 -5.927  -12.823 1.00 23.23 ? 431  ASP A O     1 
ATOM   2052 C  CB    . ASP A 1 276 ? 32.432 -4.366  -12.589 1.00 31.73 ? 431  ASP A CB    1 
ATOM   2053 C  CG    . ASP A 1 276 ? 33.100 -3.030  -12.294 1.00 53.60 ? 431  ASP A CG    1 
ATOM   2054 O  OD1   . ASP A 1 276 ? 32.675 -2.325  -11.352 1.00 55.20 ? 431  ASP A OD1   1 
ATOM   2055 O  OD2   . ASP A 1 276 ? 34.073 -2.696  -13.009 1.00 60.42 ? 431  ASP A OD2   1 
ATOM   2056 N  N     . LYS A 1 277 ? 31.137 -7.137  -11.690 1.00 23.01 ? 432  LYS A N     1 
ATOM   2057 C  CA    . LYS A 1 277 ? 30.606 -8.359  -12.275 1.00 21.72 ? 432  LYS A CA    1 
ATOM   2058 C  C     . LYS A 1 277 ? 29.402 -8.939  -11.525 1.00 21.20 ? 432  LYS A C     1 
ATOM   2059 O  O     . LYS A 1 277 ? 28.796 -9.884  -12.041 1.00 23.05 ? 432  LYS A O     1 
ATOM   2060 C  CB    . LYS A 1 277 ? 31.697 -9.418  -12.406 1.00 27.80 ? 432  LYS A CB    1 
ATOM   2061 C  CG    . LYS A 1 277 ? 32.804 -9.014  -13.384 1.00 31.67 ? 432  LYS A CG    1 
ATOM   2062 C  CD    . LYS A 1 277 ? 34.013 -9.921  -13.251 1.00 39.46 ? 432  LYS A CD    1 
ATOM   2063 C  CE    . LYS A 1 277 ? 35.096 -9.466  -14.220 1.00 51.98 ? 432  LYS A CE    1 
ATOM   2064 N  NZ    . LYS A 1 277 ? 34.684 -9.667  -15.646 1.00 56.93 ? 432  LYS A NZ    1 
ATOM   2065 N  N     . PHE A 1 278 ? 29.039 -8.414  -10.353 1.00 17.09 ? 433  PHE A N     1 
ATOM   2066 C  CA    . PHE A 1 278 ? 27.852 -8.911  -9.642  1.00 15.45 ? 433  PHE A CA    1 
ATOM   2067 C  C     . PHE A 1 278 ? 26.595 -8.311  -10.252 1.00 18.67 ? 433  PHE A C     1 
ATOM   2068 O  O     . PHE A 1 278 ? 26.585 -7.157  -10.682 1.00 20.01 ? 433  PHE A O     1 
ATOM   2069 C  CB    . PHE A 1 278 ? 27.964 -8.582  -8.148  1.00 17.05 ? 433  PHE A CB    1 
ATOM   2070 C  CG    . PHE A 1 278 ? 29.110 -9.270  -7.501  1.00 16.06 ? 433  PHE A CG    1 
ATOM   2071 C  CD1   . PHE A 1 278 ? 29.052 -10.642 -7.222  1.00 16.61 ? 433  PHE A CD1   1 
ATOM   2072 C  CD2   . PHE A 1 278 ? 30.267 -8.575  -7.197  1.00 16.61 ? 433  PHE A CD2   1 
ATOM   2073 C  CE1   . PHE A 1 278 ? 30.101 -11.314 -6.671  1.00 17.53 ? 433  PHE A CE1   1 
ATOM   2074 C  CE2   . PHE A 1 278 ? 31.368 -9.274  -6.618  1.00 17.28 ? 433  PHE A CE2   1 
ATOM   2075 C  CZ    . PHE A 1 278 ? 31.269 -10.626 -6.357  1.00 19.20 ? 433  PHE A CZ    1 
ATOM   2076 N  N     . SER A 1 279 ? 25.529 -9.107  -10.298 1.00 15.80 ? 434  SER A N     1 
ATOM   2077 C  CA    . SER A 1 279 ? 24.289 -8.580  -10.863 1.00 15.90 ? 434  SER A CA    1 
ATOM   2078 C  C     . SER A 1 279 ? 23.125 -9.118  -10.057 1.00 14.83 ? 434  SER A C     1 
ATOM   2079 O  O     . SER A 1 279 ? 23.260 -10.008 -9.215  1.00 14.28 ? 434  SER A O     1 
ATOM   2080 C  CB    . SER A 1 279 ? 24.101 -8.973  -12.317 1.00 18.04 ? 434  SER A CB    1 
ATOM   2081 O  OG    . SER A 1 279 ? 23.711 -10.328 -12.420 1.00 21.77 ? 434  SER A OG    1 
ATOM   2082 N  N     . SER A 1 280 ? 21.940 -8.566  -10.325 1.00 15.04 ? 435  SER A N     1 
ATOM   2083 C  CA    . SER A 1 280 ? 20.789 -9.071  -9.609  1.00 14.99 ? 435  SER A CA    1 
ATOM   2084 C  C     . SER A 1 280 ? 20.541 -10.547 -9.884  1.00 15.32 ? 435  SER A C     1 
ATOM   2085 O  O     . SER A 1 280 ? 19.884 -11.190 -9.074  1.00 14.94 ? 435  SER A O     1 
ATOM   2086 C  CB    . SER A 1 280 ? 19.563 -8.220  -9.964  1.00 18.13 ? 435  SER A CB    1 
ATOM   2087 O  OG    . SER A 1 280 ? 19.266 -8.333  -11.341 1.00 18.16 ? 435  SER A OG    1 
ATOM   2088 N  N     . TYR A 1 281 ? 21.045 -11.113 -10.985 1.00 13.35 ? 436  TYR A N     1 
ATOM   2089 C  CA    . TYR A 1 281 ? 20.860 -12.540 -11.210 1.00 13.81 ? 436  TYR A CA    1 
ATOM   2090 C  C     . TYR A 1 281 ? 21.605 -13.367 -10.187 1.00 12.24 ? 436  TYR A C     1 
ATOM   2091 O  O     . TYR A 1 281 ? 21.162 -14.473 -9.897  1.00 11.79 ? 436  TYR A O     1 
ATOM   2092 C  CB    . TYR A 1 281 ? 21.291 -12.921 -12.625 1.00 12.72 ? 436  TYR A CB    1 
ATOM   2093 C  CG    . TYR A 1 281 ? 20.809 -14.280 -13.015 1.00 13.64 ? 436  TYR A CG    1 
ATOM   2094 C  CD1   . TYR A 1 281 ? 19.432 -14.511 -13.218 1.00 15.29 ? 436  TYR A CD1   1 
ATOM   2095 C  CD2   . TYR A 1 281 ? 21.676 -15.345 -13.137 1.00 14.48 ? 436  TYR A CD2   1 
ATOM   2096 C  CE1   . TYR A 1 281 ? 18.962 -15.763 -13.596 1.00 15.80 ? 436  TYR A CE1   1 
ATOM   2097 C  CE2   . TYR A 1 281 ? 21.192 -16.639 -13.528 1.00 14.13 ? 436  TYR A CE2   1 
ATOM   2098 C  CZ    . TYR A 1 281 ? 19.837 -16.811 -13.728 1.00 16.82 ? 436  TYR A CZ    1 
ATOM   2099 O  OH    . TYR A 1 281 ? 19.342 -18.051 -14.094 1.00 17.58 ? 436  TYR A OH    1 
ATOM   2100 N  N     . HIS A 1 282 ? 22.697 -12.840 -9.626  1.00 12.30 ? 437  HIS A N     1 
ATOM   2101 C  CA    . HIS A 1 282 ? 23.342 -13.573 -8.542  1.00 12.06 ? 437  HIS A CA    1 
ATOM   2102 C  C     . HIS A 1 282 ? 22.446 -13.661 -7.334  1.00 13.42 ? 437  HIS A C     1 
ATOM   2103 O  O     . HIS A 1 282 ? 22.348 -14.726 -6.706  1.00 14.22 ? 437  HIS A O     1 
ATOM   2104 C  CB    . HIS A 1 282 ? 24.682 -12.930 -8.200  1.00 13.42 ? 437  HIS A CB    1 
ATOM   2105 C  CG    . HIS A 1 282 ? 25.631 -13.023 -9.305  1.00 14.25 ? 437  HIS A CG    1 
ATOM   2106 N  ND1   . HIS A 1 282 ? 26.128 -11.904 -9.933  1.00 17.02 ? 437  HIS A ND1   1 
ATOM   2107 C  CD2   . HIS A 1 282 ? 26.156 -14.090 -9.947  1.00 16.87 ? 437  HIS A CD2   1 
ATOM   2108 C  CE1   . HIS A 1 282 ? 26.945 -12.283 -10.910 1.00 18.32 ? 437  HIS A CE1   1 
ATOM   2109 N  NE2   . HIS A 1 282 ? 26.975 -13.603 -10.940 1.00 17.81 ? 437  HIS A NE2   1 
ATOM   2110 N  N     . VAL A 1 283 ? 21.815 -12.550 -6.952  1.00 12.58 ? 438  VAL A N     1 
ATOM   2111 C  CA    . VAL A 1 283 ? 20.911 -12.659 -5.801  1.00 14.97 ? 438  VAL A CA    1 
ATOM   2112 C  C     . VAL A 1 283 ? 19.661 -13.469 -6.140  1.00 13.12 ? 438  VAL A C     1 
ATOM   2113 O  O     . VAL A 1 283 ? 19.134 -14.181 -5.271  1.00 13.55 ? 438  VAL A O     1 
ATOM   2114 C  CB    . VAL A 1 283 ? 20.608 -11.318 -5.085  1.00 16.76 ? 438  VAL A CB    1 
ATOM   2115 C  CG1   . VAL A 1 283 ? 21.880 -10.653 -4.559  1.00 16.93 ? 438  VAL A CG1   1 
ATOM   2116 C  CG2   . VAL A 1 283 ? 19.931 -10.393 -5.974  1.00 19.75 ? 438  VAL A CG2   1 
ATOM   2117 N  N     . LYS A 1 284 ? 19.147 -13.368 -7.374  1.00 12.76 ? 439  LYS A N     1 
ATOM   2118 C  CA    . LYS A 1 284 ? 17.986 -14.169 -7.732  1.00 12.43 ? 439  LYS A CA    1 
ATOM   2119 C  C     . LYS A 1 284 ? 18.302 -15.658 -7.626  1.00 14.51 ? 439  LYS A C     1 
ATOM   2120 O  O     . LYS A 1 284 ? 17.476 -16.435 -7.131  1.00 12.18 ? 439  LYS A O     1 
ATOM   2121 C  CB    . LYS A 1 284 ? 17.563 -13.786 -9.145  1.00 13.49 ? 439  LYS A CB    1 
ATOM   2122 C  CG    . LYS A 1 284 ? 16.271 -14.379 -9.575  1.00 14.43 ? 439  LYS A CG    1 
ATOM   2123 C  CD    . LYS A 1 284 ? 16.048 -13.914 -11.028 1.00 17.17 ? 439  LYS A CD    1 
ATOM   2124 C  CE    . LYS A 1 284 ? 14.645 -14.282 -11.480 1.00 17.16 ? 439  LYS A CE    1 
ATOM   2125 N  NZ    . LYS A 1 284 ? 14.463 -13.940 -12.992 1.00 18.51 ? 439  LYS A NZ    1 
ATOM   2126 N  N     . THR A 1 285 ? 19.480 -16.064 -8.100  1.00 12.62 ? 440  THR A N     1 
ATOM   2127 C  CA    . THR A 1 285 ? 19.851 -17.485 -8.079  1.00 12.88 ? 440  THR A CA    1 
ATOM   2128 C  C     . THR A 1 285 ? 20.033 -17.963 -6.644  1.00 13.15 ? 440  THR A C     1 
ATOM   2129 O  O     . THR A 1 285 ? 19.523 -19.028 -6.258  1.00 13.29 ? 440  THR A O     1 
ATOM   2130 C  CB    . THR A 1 285 ? 21.131 -17.670 -8.891  1.00 11.45 ? 440  THR A CB    1 
ATOM   2131 O  OG1   . THR A 1 285 ? 20.912 -17.358 -10.263 1.00 13.64 ? 440  THR A OG1   1 
ATOM   2132 C  CG2   . THR A 1 285 ? 21.682 -19.123 -8.806  1.00 12.99 ? 440  THR A CG2   1 
ATOM   2133 N  N     . ALA A 1 286 ? 20.739 -17.169 -5.829  1.00 12.64 ? 441  ALA A N     1 
ATOM   2134 C  CA    . ALA A 1 286 ? 20.866 -17.510 -4.415  1.00 13.15 ? 441  ALA A CA    1 
ATOM   2135 C  C     . ALA A 1 286 ? 19.501 -17.591 -3.748  1.00 14.02 ? 441  ALA A C     1 
ATOM   2136 O  O     . ALA A 1 286 ? 19.237 -18.485 -2.956  1.00 12.95 ? 441  ALA A O     1 
ATOM   2137 C  CB    . ALA A 1 286 ? 21.742 -16.468 -3.702  1.00 14.51 ? 441  ALA A CB    1 
ATOM   2138 N  N     . PHE A 1 287 ? 18.601 -16.720 -4.118  1.00 12.72 ? 442  PHE A N     1 
ATOM   2139 C  CA    . PHE A 1 287 ? 17.279 -16.730 -3.534  1.00 12.78 ? 442  PHE A CA    1 
ATOM   2140 C  C     . PHE A 1 287 ? 16.513 -18.021 -3.875  1.00 12.70 ? 442  PHE A C     1 
ATOM   2141 O  O     . PHE A 1 287 ? 15.886 -18.632 -2.993  1.00 11.80 ? 442  PHE A O     1 
ATOM   2142 C  CB    . PHE A 1 287 ? 16.510 -15.486 -4.023  1.00 13.79 ? 442  PHE A CB    1 
ATOM   2143 C  CG    . PHE A 1 287 ? 15.095 -15.524 -3.628  1.00 15.59 ? 442  PHE A CG    1 
ATOM   2144 C  CD1   . PHE A 1 287 ? 14.781 -15.233 -2.291  1.00 17.16 ? 442  PHE A CD1   1 
ATOM   2145 C  CD2   . PHE A 1 287 ? 14.084 -15.914 -4.525  1.00 17.16 ? 442  PHE A CD2   1 
ATOM   2146 C  CE1   . PHE A 1 287 ? 13.466 -15.265 -1.856  1.00 21.10 ? 442  PHE A CE1   1 
ATOM   2147 C  CE2   . PHE A 1 287 ? 12.753 -15.961 -4.045  1.00 20.57 ? 442  PHE A CE2   1 
ATOM   2148 C  CZ    . PHE A 1 287 ? 12.504 -15.636 -2.747  1.00 17.27 ? 442  PHE A CZ    1 
ATOM   2149 N  N     . PHE A 1 288 ? 16.591 -18.484 -5.123  1.00 12.15 ? 443  PHE A N     1 
ATOM   2150 C  CA    . PHE A 1 288 ? 15.949 -19.755 -5.452  1.00 13.18 ? 443  PHE A CA    1 
ATOM   2151 C  C     . PHE A 1 288 ? 16.535 -20.887 -4.634  1.00 13.22 ? 443  PHE A C     1 
ATOM   2152 O  O     . PHE A 1 288 ? 15.802 -21.789 -4.221  1.00 11.83 ? 443  PHE A O     1 
ATOM   2153 C  CB    . PHE A 1 288 ? 16.066 -20.093 -6.943  1.00 12.62 ? 443  PHE A CB    1 
ATOM   2154 C  CG    . PHE A 1 288 ? 15.158 -19.274 -7.848  1.00 15.37 ? 443  PHE A CG    1 
ATOM   2155 C  CD1   . PHE A 1 288 ? 13.897 -18.872 -7.455  1.00 18.26 ? 443  PHE A CD1   1 
ATOM   2156 C  CD2   . PHE A 1 288 ? 15.628 -18.866 -9.084  1.00 22.25 ? 443  PHE A CD2   1 
ATOM   2157 C  CE1   . PHE A 1 288 ? 13.068 -18.114 -8.343  1.00 23.19 ? 443  PHE A CE1   1 
ATOM   2158 C  CE2   . PHE A 1 288 ? 14.817 -18.120 -9.953  1.00 24.09 ? 443  PHE A CE2   1 
ATOM   2159 C  CZ    . PHE A 1 288 ? 13.551 -17.765 -9.565  1.00 20.62 ? 443  PHE A CZ    1 
ATOM   2160 N  N     . HIS A 1 289 ? 17.848 -20.893 -4.442  1.00 12.60 ? 444  HIS A N     1 
ATOM   2161 C  CA    . HIS A 1 289 ? 18.433 -21.942 -3.613  1.00 12.69 ? 444  HIS A CA    1 
ATOM   2162 C  C     . HIS A 1 289 ? 17.938 -21.865 -2.173  1.00 13.40 ? 444  HIS A C     1 
ATOM   2163 O  O     . HIS A 1 289 ? 17.689 -22.918 -1.557  1.00 13.71 ? 444  HIS A O     1 
ATOM   2164 C  CB    . HIS A 1 289 ? 19.947 -21.864 -3.645  1.00 12.85 ? 444  HIS A CB    1 
ATOM   2165 C  CG    . HIS A 1 289 ? 20.536 -22.296 -4.936  1.00 13.04 ? 444  HIS A CG    1 
ATOM   2166 N  ND1   . HIS A 1 289 ? 20.365 -23.568 -5.438  1.00 15.50 ? 444  HIS A ND1   1 
ATOM   2167 C  CD2   . HIS A 1 289 ? 21.354 -21.640 -5.795  1.00 15.26 ? 444  HIS A CD2   1 
ATOM   2168 C  CE1   . HIS A 1 289 ? 21.037 -23.655 -6.570  1.00 14.43 ? 444  HIS A CE1   1 
ATOM   2169 N  NE2   . HIS A 1 289 ? 21.620 -22.491 -6.825  1.00 16.10 ? 444  HIS A NE2   1 
ATOM   2170 N  N     . VAL A 1 290 ? 17.764 -20.654 -1.599  1.00 13.43 ? 445  VAL A N     1 
ATOM   2171 C  CA    . VAL A 1 290 ? 17.210 -20.551 -0.244  1.00 12.92 ? 445  VAL A CA    1 
ATOM   2172 C  C     . VAL A 1 290 ? 15.781 -21.071 -0.202  1.00 13.40 ? 445  VAL A C     1 
ATOM   2173 O  O     . VAL A 1 290 ? 15.340 -21.640 0.806   1.00 15.09 ? 445  VAL A O     1 
ATOM   2174 C  CB    . VAL A 1 290 ? 17.318 -19.109 0.283   1.00 14.85 ? 445  VAL A CB    1 
ATOM   2175 C  CG1   . VAL A 1 290 ? 16.758 -18.992 1.728   1.00 18.93 ? 445  VAL A CG1   1 
ATOM   2176 C  CG2   . VAL A 1 290 ? 18.712 -18.702 0.277   1.00 17.32 ? 445  VAL A CG2   1 
ATOM   2177 N  N     . CYS A 1 291 ? 14.997 -20.822 -1.269  1.00 13.29 ? 446  CYS A N     1 
ATOM   2178 C  CA    . CYS A 1 291 ? 13.650 -21.346 -1.299  1.00 14.96 ? 446  CYS A CA    1 
ATOM   2179 C  C     . CYS A 1 291 ? 13.665 -22.875 -1.297  1.00 16.04 ? 446  CYS A C     1 
ATOM   2180 O  O     . CYS A 1 291 ? 12.778 -23.510 -0.708  1.00 16.52 ? 446  CYS A O     1 
ATOM   2181 C  CB    . CYS A 1 291 ? 12.964 -20.863 -2.584  1.00 13.75 ? 446  CYS A CB    1 
ATOM   2182 S  SG    . CYS A 1 291 ? 12.439 -19.130 -2.455  1.00 17.31 ? 446  CYS A SG    1 
ATOM   2183 N  N     . THR A 1 292 ? 14.625 -23.484 -1.984  1.00 15.19 ? 447  THR A N     1 
ATOM   2184 C  CA    . THR A 1 292 ? 14.748 -24.941 -1.963  1.00 16.45 ? 447  THR A CA    1 
ATOM   2185 C  C     . THR A 1 292 ? 15.118 -25.410 -0.562  1.00 17.55 ? 447  THR A C     1 
ATOM   2186 O  O     . THR A 1 292 ? 14.563 -26.398 -0.063  1.00 19.72 ? 447  THR A O     1 
ATOM   2187 C  CB    . THR A 1 292 ? 15.787 -25.391 -2.995  1.00 16.38 ? 447  THR A CB    1 
ATOM   2188 O  OG1   . THR A 1 292 ? 15.340 -25.106 -4.330  1.00 24.19 ? 447  THR A OG1   1 
ATOM   2189 C  CG2   . THR A 1 292 ? 16.112 -26.905 -2.860  1.00 19.76 ? 447  THR A CG2   1 
ATOM   2190 N  N     . GLN A 1 293 ? 16.034 -24.699 0.087   1.00 15.26 ? 448  GLN A N     1 
ATOM   2191 C  CA    . GLN A 1 293 ? 16.474 -25.086 1.419   1.00 16.72 ? 448  GLN A CA    1 
ATOM   2192 C  C     . GLN A 1 293 ? 15.346 -24.939 2.432   1.00 17.87 ? 448  GLN A C     1 
ATOM   2193 O  O     . GLN A 1 293 ? 15.276 -25.716 3.397   1.00 19.08 ? 448  GLN A O     1 
ATOM   2194 C  CB    . GLN A 1 293 ? 17.672 -24.215 1.798   1.00 17.99 ? 448  GLN A CB    1 
ATOM   2195 C  CG    . GLN A 1 293 ? 18.145 -24.323 3.235   1.00 26.81 ? 448  GLN A CG    1 
ATOM   2196 C  CD    . GLN A 1 293 ? 19.104 -23.197 3.607   1.00 39.44 ? 448  GLN A CD    1 
ATOM   2197 O  OE1   . GLN A 1 293 ? 18.703 -22.185 4.219   1.00 31.51 ? 448  GLN A OE1   1 
ATOM   2198 N  NE2   . GLN A 1 293 ? 20.378 -23.375 3.267   1.00 34.04 ? 448  GLN A NE2   1 
ATOM   2199 N  N     . ASN A 1 294 ? 14.428 -23.983 2.214   1.00 16.24 ? 449  ASN A N     1 
ATOM   2200 C  CA    . ASN A 1 294 ? 13.394 -23.588 3.168   1.00 16.29 ? 449  ASN A CA    1 
ATOM   2201 C  C     . ASN A 1 294 ? 12.071 -23.706 2.410   1.00 16.49 ? 449  ASN A C     1 
ATOM   2202 O  O     . ASN A 1 294 ? 11.435 -22.698 2.049   1.00 15.56 ? 449  ASN A O     1 
ATOM   2203 C  CB    . ASN A 1 294 ? 13.624 -22.156 3.694   1.00 16.72 ? 449  ASN A CB    1 
ATOM   2204 C  CG    . ASN A 1 294 ? 14.860 -22.041 4.581   1.00 22.91 ? 449  ASN A CG    1 
ATOM   2205 O  OD1   . ASN A 1 294 ? 15.612 -23.018 4.783   1.00 25.87 ? 449  ASN A OD1   1 
ATOM   2206 N  ND2   . ASN A 1 294 ? 15.102 -20.827 5.099   1.00 27.83 ? 449  ASN A ND2   1 
ATOM   2207 N  N     . PRO A 1 295 ? 11.603 -24.928 2.176   1.00 13.55 ? 450  PRO A N     1 
ATOM   2208 C  CA    . PRO A 1 295 ? 10.472 -25.136 1.253   1.00 15.92 ? 450  PRO A CA    1 
ATOM   2209 C  C     . PRO A 1 295 ? 9.103  -24.819 1.821   1.00 16.41 ? 450  PRO A C     1 
ATOM   2210 O  O     . PRO A 1 295 ? 8.152  -24.695 1.048   1.00 18.37 ? 450  PRO A O     1 
ATOM   2211 C  CB    . PRO A 1 295 ? 10.556 -26.642 0.927   1.00 15.91 ? 450  PRO A CB    1 
ATOM   2212 C  CG    . PRO A 1 295 ? 11.216 -27.225 2.173   1.00 17.29 ? 450  PRO A CG    1 
ATOM   2213 C  CD    . PRO A 1 295 ? 12.244 -26.186 2.602   1.00 16.68 ? 450  PRO A CD    1 
ATOM   2214 N  N     . GLN A 1 296 ? 8.939  -24.721 3.133   1.00 15.08 ? 451  GLN A N     1 
ATOM   2215 C  CA    . GLN A 1 296 ? 7.610  -24.557 3.697   1.00 16.07 ? 451  GLN A CA    1 
ATOM   2216 C  C     . GLN A 1 296 ? 7.214  -23.088 3.767   1.00 15.42 ? 451  GLN A C     1 
ATOM   2217 O  O     . GLN A 1 296 ? 8.062  -22.219 4.008   1.00 15.08 ? 451  GLN A O     1 
ATOM   2218 C  CB    . GLN A 1 296 ? 7.591  -25.115 5.128   1.00 18.69 ? 451  GLN A CB    1 
ATOM   2219 C  CG    . GLN A 1 296 ? 8.000  -26.596 5.251   1.00 23.20 ? 451  GLN A CG    1 
ATOM   2220 C  CD    . GLN A 1 296 ? 6.976  -27.539 4.672   1.00 26.79 ? 451  GLN A CD    1 
ATOM   2221 O  OE1   . GLN A 1 296 ? 5.817  -27.179 4.493   1.00 26.31 ? 451  GLN A OE1   1 
ATOM   2222 N  NE2   . GLN A 1 296 ? 7.409  -28.748 4.332   1.00 30.61 ? 451  GLN A NE2   1 
ATOM   2223 N  N     . ASP A 1 297 ? 5.941  -22.804 3.502   1.00 16.43 ? 452  ASP A N     1 
ATOM   2224 C  CA    . ASP A 1 297 ? 5.469  -21.424 3.590   1.00 16.05 ? 452  ASP A CA    1 
ATOM   2225 C  C     . ASP A 1 297 ? 5.654  -20.844 4.992   1.00 16.69 ? 452  ASP A C     1 
ATOM   2226 O  O     . ASP A 1 297 ? 5.825  -19.627 5.138   1.00 16.30 ? 452  ASP A O     1 
ATOM   2227 C  CB    . ASP A 1 297 ? 3.999  -21.344 3.152   1.00 15.49 ? 452  ASP A CB    1 
ATOM   2228 C  CG    . ASP A 1 297 ? 3.810  -21.727 1.681   1.00 15.79 ? 452  ASP A CG    1 
ATOM   2229 O  OD1   . ASP A 1 297 ? 4.806  -21.676 0.900   1.00 14.16 ? 452  ASP A OD1   1 
ATOM   2230 O  OD2   . ASP A 1 297 ? 2.660  -22.102 1.327   1.00 17.30 ? 452  ASP A OD2   1 
ATOM   2231 N  N     . SER A 1 298 ? 5.593  -21.691 6.034   1.00 17.63 ? 453  SER A N     1 
ATOM   2232 C  CA    . SER A 1 298 ? 5.797  -21.201 7.389   1.00 18.89 ? 453  SER A CA    1 
ATOM   2233 C  C     . SER A 1 298 ? 7.228  -20.772 7.661   1.00 18.65 ? 453  SER A C     1 
ATOM   2234 O  O     . SER A 1 298 ? 7.465  -20.133 8.699   1.00 20.49 ? 453  SER A O     1 
ATOM   2235 C  CB    . SER A 1 298 ? 5.406  -22.297 8.369   1.00 21.07 ? 453  SER A CB    1 
ATOM   2236 O  OG    . SER A 1 298 ? 6.296  -23.375 8.192   1.00 24.46 ? 453  SER A OG    1 
ATOM   2237 N  N     . GLN A 1 299 ? 8.170  -21.074 6.765   1.00 15.23 ? 454  GLN A N     1 
ATOM   2238 C  CA    . GLN A 1 299 ? 9.529  -20.559 6.866   1.00 16.13 ? 454  GLN A CA    1 
ATOM   2239 C  C     . GLN A 1 299 ? 9.669  -19.183 6.216   1.00 15.08 ? 454  GLN A C     1 
ATOM   2240 O  O     . GLN A 1 299 ? 10.788 -18.660 6.138   1.00 14.84 ? 454  GLN A O     1 
ATOM   2241 C  CB    . GLN A 1 299 ? 10.489 -21.516 6.194   1.00 16.58 ? 454  GLN A CB    1 
ATOM   2242 C  CG    . GLN A 1 299 ? 10.529 -22.850 6.920   1.00 16.45 ? 454  GLN A CG    1 
ATOM   2243 C  CD    . GLN A 1 299 ? 11.429 -23.851 6.276   1.00 20.08 ? 454  GLN A CD    1 
ATOM   2244 O  OE1   . GLN A 1 299 ? 11.063 -24.490 5.289   1.00 17.97 ? 454  GLN A OE1   1 
ATOM   2245 N  NE2   . GLN A 1 299 ? 12.622 -24.010 6.829   1.00 23.72 ? 454  GLN A NE2   1 
ATOM   2246 N  N     . TRP A 1 300 ? 8.567  -18.616 5.710   1.00 14.33 ? 455  TRP A N     1 
ATOM   2247 C  CA    . TRP A 1 300 ? 8.553  -17.313 5.054   1.00 14.24 ? 455  TRP A CA    1 
ATOM   2248 C  C     . TRP A 1 300 ? 7.369  -16.509 5.567   1.00 15.20 ? 455  TRP A C     1 
ATOM   2249 O  O     . TRP A 1 300 ? 6.676  -15.805 4.836   1.00 15.46 ? 455  TRP A O     1 
ATOM   2250 C  CB    . TRP A 1 300 ? 8.471  -17.500 3.543   1.00 14.07 ? 455  TRP A CB    1 
ATOM   2251 C  CG    . TRP A 1 300 ? 9.626  -18.244 2.986   1.00 13.07 ? 455  TRP A CG    1 
ATOM   2252 C  CD1   . TRP A 1 300 ? 9.713  -19.587 2.738   1.00 12.05 ? 455  TRP A CD1   1 
ATOM   2253 C  CD2   . TRP A 1 300 ? 10.872 -17.677 2.601   1.00 13.28 ? 455  TRP A CD2   1 
ATOM   2254 N  NE1   . TRP A 1 300 ? 10.937 -19.878 2.230   1.00 15.37 ? 455  TRP A NE1   1 
ATOM   2255 C  CE2   . TRP A 1 300 ? 11.682 -18.729 2.122   1.00 16.05 ? 455  TRP A CE2   1 
ATOM   2256 C  CE3   . TRP A 1 300 ? 11.374 -16.357 2.602   1.00 15.11 ? 455  TRP A CE3   1 
ATOM   2257 C  CZ2   . TRP A 1 300 ? 12.942 -18.521 1.597   1.00 17.33 ? 455  TRP A CZ2   1 
ATOM   2258 C  CZ3   . TRP A 1 300 ? 12.648 -16.134 2.120   1.00 16.42 ? 455  TRP A CZ3   1 
ATOM   2259 C  CH2   . TRP A 1 300 ? 13.435 -17.231 1.635   1.00 16.46 ? 455  TRP A CH2   1 
ATOM   2260 N  N     . ASP A 1 301 ? 7.072  -16.631 6.850   1.00 17.31 ? 456  ASP A N     1 
ATOM   2261 C  CA    . ASP A 1 301 ? 5.955  -15.889 7.394   1.00 16.43 ? 456  ASP A CA    1 
ATOM   2262 C  C     . ASP A 1 301 ? 6.268  -14.399 7.422   1.00 18.19 ? 456  ASP A C     1 
ATOM   2263 O  O     . ASP A 1 301 ? 7.383  -13.994 7.731   1.00 16.87 ? 456  ASP A O     1 
ATOM   2264 C  CB    . ASP A 1 301 ? 5.722  -16.397 8.821   1.00 18.52 ? 456  ASP A CB    1 
ATOM   2265 C  CG    . ASP A 1 301 ? 4.375  -15.993 9.381   1.00 26.69 ? 456  ASP A CG    1 
ATOM   2266 O  OD1   . ASP A 1 301 ? 4.104  -14.777 9.478   1.00 25.58 ? 456  ASP A OD1   1 
ATOM   2267 O  OD2   . ASP A 1 301 ? 3.577  -16.906 9.706   1.00 34.97 ? 456  ASP A OD2   1 
ATOM   2268 N  N     . ARG A 1 302 ? 5.251  -13.589 7.106   1.00 17.67 ? 457  ARG A N     1 
ATOM   2269 C  CA    . ARG A 1 302 ? 5.399  -12.141 7.121   1.00 18.96 ? 457  ARG A CA    1 
ATOM   2270 C  C     . ARG A 1 302 ? 5.918  -11.633 8.454   1.00 20.88 ? 457  ARG A C     1 
ATOM   2271 O  O     . ARG A 1 302 ? 6.725  -10.692 8.488   1.00 20.38 ? 457  ARG A O     1 
ATOM   2272 C  CB    . ARG A 1 302 ? 4.040  -11.509 6.836   1.00 23.73 ? 457  ARG A CB    1 
ATOM   2273 C  CG    . ARG A 1 302 ? 4.038  -9.999  6.798   1.00 25.47 ? 457  ARG A CG    1 
ATOM   2274 C  CD    . ARG A 1 302 ? 2.580  -9.511  6.555   1.00 27.54 ? 457  ARG A CD    1 
ATOM   2275 N  NE    . ARG A 1 302 ? 2.487  -8.054  6.645   1.00 32.00 ? 457  ARG A NE    1 
ATOM   2276 C  CZ    . ARG A 1 302 ? 2.709  -7.247  5.615   1.00 35.47 ? 457  ARG A CZ    1 
ATOM   2277 N  NH1   . ARG A 1 302 ? 3.003  -7.726  4.408   1.00 29.03 ? 457  ARG A NH1   1 
ATOM   2278 N  NH2   . ARG A 1 302 ? 2.685  -5.930  5.805   1.00 33.01 ? 457  ARG A NH2   1 
ATOM   2279 N  N     . LYS A 1 303 ? 5.481  -12.246 9.559   1.00 19.94 ? 458  LYS A N     1 
ATOM   2280 C  CA    . LYS A 1 303 ? 5.972  -11.726 10.833  1.00 22.82 ? 458  LYS A CA    1 
ATOM   2281 C  C     . LYS A 1 303 ? 7.436  -12.055 11.097  1.00 19.43 ? 458  LYS A C     1 
ATOM   2282 O  O     . LYS A 1 303 ? 7.995  -11.571 12.090  1.00 21.71 ? 458  LYS A O     1 
ATOM   2283 C  CB    . LYS A 1 303 ? 5.102  -12.235 11.989  1.00 25.73 ? 458  LYS A CB    1 
ATOM   2284 C  CG    . LYS A 1 303 ? 5.131  -13.706 12.215  1.00 33.33 ? 458  LYS A CG    1 
ATOM   2285 C  CD    . LYS A 1 303 ? 3.714  -14.219 12.500  1.00 47.46 ? 458  LYS A CD    1 
ATOM   2286 C  CE    . LYS A 1 303 ? 3.056  -13.435 13.631  1.00 49.59 ? 458  LYS A CE    1 
ATOM   2287 N  NZ    . LYS A 1 303 ? 1.557  -13.425 13.519  1.00 59.94 ? 458  LYS A NZ    1 
ATOM   2288 N  N     . ASP A 1 304 ? 8.079  -12.853 10.251  1.00 17.51 ? 459  ASP A N     1 
ATOM   2289 C  CA    . ASP A 1 304 ? 9.482  -13.215 10.386  1.00 17.17 ? 459  ASP A CA    1 
ATOM   2290 C  C     . ASP A 1 304 ? 10.351 -12.585 9.299   1.00 16.47 ? 459  ASP A C     1 
ATOM   2291 O  O     . ASP A 1 304 ? 11.443 -13.056 9.045   1.00 17.15 ? 459  ASP A O     1 
ATOM   2292 C  CB    . ASP A 1 304 ? 9.649  -14.727 10.378  1.00 18.04 ? 459  ASP A CB    1 
ATOM   2293 C  CG    . ASP A 1 304 ? 8.986  -15.379 11.558  1.00 26.32 ? 459  ASP A CG    1 
ATOM   2294 O  OD1   . ASP A 1 304 ? 9.107  -14.837 12.698  1.00 22.64 ? 459  ASP A OD1   1 
ATOM   2295 O  OD2   . ASP A 1 304 ? 8.363  -16.437 11.357  1.00 23.05 ? 459  ASP A OD2   1 
ATOM   2296 N  N     . LEU A 1 305 ? 9.906  -11.453 8.754   1.00 15.53 ? 460  LEU A N     1 
ATOM   2297 C  CA    . LEU A 1 305 ? 10.619 -10.815 7.635   1.00 15.83 ? 460  LEU A CA    1 
ATOM   2298 C  C     . LEU A 1 305 ? 12.118 -10.612 7.906   1.00 16.07 ? 460  LEU A C     1 
ATOM   2299 O  O     . LEU A 1 305 ? 12.976 -10.919 7.062   1.00 16.44 ? 460  LEU A O     1 
ATOM   2300 C  CB    . LEU A 1 305 ? 9.968  -9.476  7.336   1.00 17.20 ? 460  LEU A CB    1 
ATOM   2301 C  CG    . LEU A 1 305 ? 10.674 -8.585  6.309   1.00 16.73 ? 460  LEU A CG    1 
ATOM   2302 C  CD1   . LEU A 1 305 ? 10.640 -9.295  4.923   1.00 18.92 ? 460  LEU A CD1   1 
ATOM   2303 C  CD2   . LEU A 1 305 ? 10.026 -7.229  6.261   1.00 16.70 ? 460  LEU A CD2   1 
ATOM   2304 N  N     . GLY A 1 306 ? 12.455 -10.062 9.071   1.00 17.06 ? 461  GLY A N     1 
ATOM   2305 C  CA    . GLY A 1 306 ? 13.866 -9.809  9.359   1.00 16.64 ? 461  GLY A CA    1 
ATOM   2306 C  C     . GLY A 1 306 ? 14.702 -11.073 9.421   1.00 14.25 ? 461  GLY A C     1 
ATOM   2307 O  O     . GLY A 1 306 ? 15.802 -11.126 8.893   1.00 17.44 ? 461  GLY A O     1 
ATOM   2308 N  N     . LEU A 1 307 ? 14.137 -12.141 9.986   1.00 16.10 ? 462  LEU A N     1 
ATOM   2309 C  CA    . LEU A 1 307 ? 14.854 -13.393 10.046  1.00 16.35 ? 462  LEU A CA    1 
ATOM   2310 C  C     . LEU A 1 307 ? 14.953 -14.021 8.670   1.00 16.49 ? 462  LEU A C     1 
ATOM   2311 O  O     . LEU A 1 307 ? 15.993 -14.558 8.297   1.00 16.68 ? 462  LEU A O     1 
ATOM   2312 C  CB    . LEU A 1 307 ? 14.113 -14.318 11.022  1.00 22.30 ? 462  LEU A CB    1 
ATOM   2313 C  CG    . LEU A 1 307 ? 14.685 -15.731 11.116  1.00 21.85 ? 462  LEU A CG    1 
ATOM   2314 C  CD1   . LEU A 1 307 ? 16.099 -15.732 11.575  1.00 25.56 ? 462  LEU A CD1   1 
ATOM   2315 C  CD2   . LEU A 1 307 ? 13.790 -16.560 12.051  1.00 26.94 ? 462  LEU A CD2   1 
ATOM   2316 N  N     . CYS A 1 308 ? 13.866 -13.939 7.899   1.00 15.47 ? 463  CYS A N     1 
ATOM   2317 C  CA    . CYS A 1 308 ? 13.906 -14.507 6.549   1.00 17.06 ? 463  CYS A CA    1 
ATOM   2318 C  C     . CYS A 1 308 ? 14.908 -13.763 5.677   1.00 16.06 ? 463  CYS A C     1 
ATOM   2319 O  O     . CYS A 1 308 ? 15.654 -14.387 4.922   1.00 16.19 ? 463  CYS A O     1 
ATOM   2320 C  CB    . CYS A 1 308 ? 12.518 -14.408 5.944   1.00 16.96 ? 463  CYS A CB    1 
ATOM   2321 S  SG    . CYS A 1 308 ? 11.343 -15.481 6.828   1.00 18.92 ? 463  CYS A SG    1 
ATOM   2322 N  N     . PHE A 1 309 ? 14.948 -12.427 5.782   1.00 14.16 ? 464  PHE A N     1 
ATOM   2323 C  CA    . PHE A 1 309 ? 15.949 -11.669 5.044   1.00 15.76 ? 464  PHE A CA    1 
ATOM   2324 C  C     . PHE A 1 309 ? 17.348 -12.045 5.512   1.00 15.09 ? 464  PHE A C     1 
ATOM   2325 O  O     . PHE A 1 309 ? 18.235 -12.284 4.690   1.00 15.10 ? 464  PHE A O     1 
ATOM   2326 C  CB    . PHE A 1 309 ? 15.686 -10.176 5.192   1.00 15.67 ? 464  PHE A CB    1 
ATOM   2327 C  CG    . PHE A 1 309 ? 16.706 -9.304  4.486   1.00 16.33 ? 464  PHE A CG    1 
ATOM   2328 C  CD1   . PHE A 1 309 ? 16.988 -9.437  3.099   1.00 15.31 ? 464  PHE A CD1   1 
ATOM   2329 C  CD2   . PHE A 1 309 ? 17.413 -8.344  5.213   1.00 16.74 ? 464  PHE A CD2   1 
ATOM   2330 C  CE1   . PHE A 1 309 ? 17.941 -8.609  2.478   1.00 15.47 ? 464  PHE A CE1   1 
ATOM   2331 C  CE2   . PHE A 1 309 ? 18.354 -7.554  4.588   1.00 17.61 ? 464  PHE A CE2   1 
ATOM   2332 C  CZ    . PHE A 1 309 ? 18.639 -7.688  3.245   1.00 16.07 ? 464  PHE A CZ    1 
ATOM   2333 N  N     . ASP A 1 310 ? 17.531 -12.187 6.825   1.00 16.18 ? 465  ASP A N     1 
ATOM   2334 C  CA    . ASP A 1 310 ? 18.823 -12.637 7.303   1.00 18.15 ? 465  ASP A CA    1 
ATOM   2335 C  C     . ASP A 1 310 ? 19.231 -13.990 6.723   1.00 17.24 ? 465  ASP A C     1 
ATOM   2336 O  O     . ASP A 1 310 ? 20.394 -14.176 6.386   1.00 18.13 ? 465  ASP A O     1 
ATOM   2337 C  CB    . ASP A 1 310 ? 18.863 -12.660 8.827   1.00 18.11 ? 465  ASP A CB    1 
ATOM   2338 C  CG    . ASP A 1 310 ? 20.284 -12.802 9.340   1.00 31.34 ? 465  ASP A CG    1 
ATOM   2339 O  OD1   . ASP A 1 310 ? 21.100 -11.871 9.109   1.00 30.47 ? 465  ASP A OD1   1 
ATOM   2340 O  OD2   . ASP A 1 310 ? 20.604 -13.895 9.858   1.00 26.46 ? 465  ASP A OD2   1 
ATOM   2341 N  N     . ASN A 1 311 ? 18.295 -14.961 6.637   1.00 19.94 ? 466  ASN A N     1 
ATOM   2342 C  CA    . ASN A 1 311 ? 18.582 -16.259 6.000   1.00 20.29 ? 466  ASN A CA    1 
ATOM   2343 C  C     . ASN A 1 311 ? 19.073 -16.081 4.574   1.00 18.20 ? 466  ASN A C     1 
ATOM   2344 O  O     . ASN A 1 311 ? 19.937 -16.825 4.099   1.00 19.11 ? 466  ASN A O     1 
ATOM   2345 C  CB    . ASN A 1 311 ? 17.305 -17.096 5.898   1.00 22.85 ? 466  ASN A CB    1 
ATOM   2346 C  CG    . ASN A 1 311 ? 16.731 -17.543 7.252   1.00 26.55 ? 466  ASN A CG    1 
ATOM   2347 O  OD1   . ASN A 1 311 ? 17.402 -17.529 8.288   1.00 29.35 ? 466  ASN A OD1   1 
ATOM   2348 N  ND2   . ASN A 1 311 ? 15.448 -17.936 7.232   1.00 23.04 ? 466  ASN A ND2   1 
ATOM   2349 N  N     . CYS A 1 312 ? 18.540 -15.084 3.865   1.00 17.38 ? 467  CYS A N     1 
ATOM   2350 C  CA    . CYS A 1 312 ? 18.952 -14.887 2.478   1.00 15.77 ? 467  CYS A CA    1 
ATOM   2351 C  C     . CYS A 1 312 ? 20.351 -14.281 2.428   1.00 15.00 ? 467  CYS A C     1 
ATOM   2352 O  O     . CYS A 1 312 ? 21.202 -14.712 1.654   1.00 14.95 ? 467  CYS A O     1 
ATOM   2353 C  CB    . CYS A 1 312 ? 17.989 -13.897 1.835   1.00 14.22 ? 467  CYS A CB    1 
ATOM   2354 S  SG    . CYS A 1 312 ? 16.351 -14.691 1.470   1.00 18.31 ? 467  CYS A SG    1 
ATOM   2355 N  N     . VAL A 1 313 ? 20.603 -13.311 3.300   1.00 13.92 ? 468  VAL A N     1 
ATOM   2356 C  CA    . VAL A 1 313 ? 21.917 -12.661 3.343   1.00 15.29 ? 468  VAL A CA    1 
ATOM   2357 C  C     . VAL A 1 313 ? 22.994 -13.658 3.746   1.00 13.70 ? 468  VAL A C     1 
ATOM   2358 O  O     . VAL A 1 313 ? 24.036 -13.716 3.131   1.00 14.10 ? 468  VAL A O     1 
ATOM   2359 C  CB    . VAL A 1 313 ? 21.877 -11.472 4.313   1.00 17.25 ? 468  VAL A CB    1 
ATOM   2360 C  CG1   . VAL A 1 313 ? 23.283 -10.900 4.508   1.00 16.42 ? 468  VAL A CG1   1 
ATOM   2361 C  CG2   . VAL A 1 313 ? 20.896 -10.386 3.810   1.00 17.38 ? 468  VAL A CG2   1 
ATOM   2362 N  N     . THR A 1 314 ? 22.736 -14.454 4.792   1.00 15.28 ? 469  THR A N     1 
ATOM   2363 C  CA    . THR A 1 314 ? 23.756 -15.408 5.213   1.00 17.13 ? 469  THR A CA    1 
ATOM   2364 C  C     . THR A 1 314 ? 23.986 -16.485 4.172   1.00 15.09 ? 469  THR A C     1 
ATOM   2365 O  O     . THR A 1 314 ? 25.143 -16.888 3.970   1.00 16.10 ? 469  THR A O     1 
ATOM   2366 C  CB    . THR A 1 314 ? 23.425 -16.023 6.573   1.00 20.94 ? 469  THR A CB    1 
ATOM   2367 O  OG1   . THR A 1 314 ? 22.186 -16.717 6.529   1.00 29.52 ? 469  THR A OG1   1 
ATOM   2368 C  CG2   . THR A 1 314 ? 23.368 -14.975 7.656   1.00 23.74 ? 469  THR A CG2   1 
ATOM   2369 N  N     . TYR A 1 315 ? 22.918 -16.932 3.471   1.00 16.56 ? 470  TYR A N     1 
ATOM   2370 C  CA    . TYR A 1 315 ? 23.121 -17.879 2.390   1.00 17.69 ? 470  TYR A CA    1 
ATOM   2371 C  C     . TYR A 1 315 ? 24.014 -17.278 1.306   1.00 15.87 ? 470  TYR A C     1 
ATOM   2372 O  O     . TYR A 1 315 ? 24.953 -17.899 0.832   1.00 15.43 ? 470  TYR A O     1 
ATOM   2373 C  CB    . TYR A 1 315 ? 21.766 -18.318 1.801   1.00 15.96 ? 470  TYR A CB    1 
ATOM   2374 C  CG    . TYR A 1 315 ? 21.935 -19.468 0.864   1.00 18.66 ? 470  TYR A CG    1 
ATOM   2375 C  CD1   . TYR A 1 315 ? 22.136 -19.242 -0.487  1.00 17.40 ? 470  TYR A CD1   1 
ATOM   2376 C  CD2   . TYR A 1 315 ? 21.866 -20.777 1.326   1.00 29.66 ? 470  TYR A CD2   1 
ATOM   2377 C  CE1   . TYR A 1 315 ? 22.339 -20.262 -1.389  1.00 19.69 ? 470  TYR A CE1   1 
ATOM   2378 C  CE2   . TYR A 1 315 ? 22.018 -21.815 0.448   1.00 28.29 ? 470  TYR A CE2   1 
ATOM   2379 C  CZ    . TYR A 1 315 ? 22.276 -21.564 -0.877  1.00 24.46 ? 470  TYR A CZ    1 
ATOM   2380 O  OH    . TYR A 1 315 ? 22.397 -22.677 -1.658  1.00 29.09 ? 470  TYR A OH    1 
ATOM   2381 N  N     . PHE A 1 316 ? 23.746 -16.028 0.919   1.00 14.63 ? 471  PHE A N     1 
ATOM   2382 C  CA    . PHE A 1 316 ? 24.557 -15.403 -0.112  1.00 15.35 ? 471  PHE A CA    1 
ATOM   2383 C  C     . PHE A 1 316 ? 26.014 -15.215 0.345   1.00 14.00 ? 471  PHE A C     1 
ATOM   2384 O  O     . PHE A 1 316 ? 26.956 -15.415 -0.452  1.00 15.64 ? 471  PHE A O     1 
ATOM   2385 C  CB    . PHE A 1 316 ? 23.891 -14.065 -0.468  1.00 13.58 ? 471  PHE A CB    1 
ATOM   2386 C  CG    . PHE A 1 316 ? 24.453 -13.429 -1.682  1.00 14.15 ? 471  PHE A CG    1 
ATOM   2387 C  CD1   . PHE A 1 316 ? 24.231 -13.946 -2.936  1.00 17.75 ? 471  PHE A CD1   1 
ATOM   2388 C  CD2   . PHE A 1 316 ? 25.306 -12.321 -1.589  1.00 16.80 ? 471  PHE A CD2   1 
ATOM   2389 C  CE1   . PHE A 1 316 ? 24.771 -13.340 -4.083  1.00 16.75 ? 471  PHE A CE1   1 
ATOM   2390 C  CE2   . PHE A 1 316 ? 25.851 -11.744 -2.713  1.00 17.15 ? 471  PHE A CE2   1 
ATOM   2391 C  CZ    . PHE A 1 316 ? 25.585 -12.258 -3.958  1.00 18.31 ? 471  PHE A CZ    1 
ATOM   2392 N  N     . LEU A 1 317 ? 26.216 -14.870 1.626   1.00 14.97 ? 472  LEU A N     1 
ATOM   2393 C  CA    . LEU A 1 317 ? 27.573 -14.787 2.162   1.00 14.73 ? 472  LEU A CA    1 
ATOM   2394 C  C     . LEU A 1 317 ? 28.272 -16.133 2.079   1.00 16.24 ? 472  LEU A C     1 
ATOM   2395 O  O     . LEU A 1 317 ? 29.456 -16.193 1.718   1.00 16.76 ? 472  LEU A O     1 
ATOM   2396 C  CB    . LEU A 1 317 ? 27.546 -14.271 3.590   1.00 14.76 ? 472  LEU A CB    1 
ATOM   2397 C  CG    . LEU A 1 317 ? 27.343 -12.769 3.749   1.00 15.89 ? 472  LEU A CG    1 
ATOM   2398 C  CD1   . LEU A 1 317 ? 27.036 -12.458 5.216   1.00 18.21 ? 472  LEU A CD1   1 
ATOM   2399 C  CD2   . LEU A 1 317 ? 28.499 -11.956 3.301   1.00 16.00 ? 472  LEU A CD2   1 
ATOM   2400 N  N     . GLN A 1 318 ? 27.546 -17.210 2.388   1.00 16.67 ? 473  GLN A N     1 
ATOM   2401 C  CA    . GLN A 1 318 ? 28.124 -18.548 2.283   1.00 17.53 ? 473  GLN A CA    1 
ATOM   2402 C  C     . GLN A 1 318 ? 28.537 -18.867 0.858   1.00 17.16 ? 473  GLN A C     1 
ATOM   2403 O  O     . GLN A 1 318 ? 29.622 -19.414 0.613   1.00 18.27 ? 473  GLN A O     1 
ATOM   2404 C  CB    . GLN A 1 318 ? 27.149 -19.568 2.824   1.00 19.57 ? 473  GLN A CB    1 
ATOM   2405 N  N     . CYS A 1 319 ? 27.701 -18.490 -0.125  1.00 15.55 ? 474  CYS A N     1 
ATOM   2406 C  CA    . CYS A 1 319 ? 28.060 -18.657 -1.540  1.00 15.81 ? 474  CYS A CA    1 
ATOM   2407 C  C     . CYS A 1 319 ? 29.337 -17.905 -1.921  1.00 14.63 ? 474  CYS A C     1 
ATOM   2408 O  O     . CYS A 1 319 ? 30.194 -18.416 -2.637  1.00 14.85 ? 474  CYS A O     1 
ATOM   2409 C  CB    . CYS A 1 319 ? 26.914 -18.144 -2.426  1.00 14.80 ? 474  CYS A CB    1 
ATOM   2410 S  SG    . CYS A 1 319 ? 25.403 -19.156 -2.320  1.00 18.92 ? 474  CYS A SG    1 
ATOM   2411 N  N     . LEU A 1 320 ? 29.476 -16.649 -1.452  1.00 15.31 ? 475  LEU A N     1 
ATOM   2412 C  CA    . LEU A 1 320 ? 30.664 -15.866 -1.734  1.00 15.66 ? 475  LEU A CA    1 
ATOM   2413 C  C     . LEU A 1 320 ? 31.909 -16.499 -1.113  1.00 14.52 ? 475  LEU A C     1 
ATOM   2414 O  O     . LEU A 1 320 ? 32.943 -16.626 -1.783  1.00 18.65 ? 475  LEU A O     1 
ATOM   2415 C  CB    . LEU A 1 320 ? 30.452 -14.448 -1.172  1.00 15.56 ? 475  LEU A CB    1 
ATOM   2416 C  CG    . LEU A 1 320 ? 29.484 -13.535 -1.946  1.00 14.21 ? 475  LEU A CG    1 
ATOM   2417 C  CD1   . LEU A 1 320 ? 29.202 -12.364 -1.079  1.00 15.63 ? 475  LEU A CD1   1 
ATOM   2418 C  CD2   . LEU A 1 320 ? 30.088 -13.124 -3.255  1.00 15.99 ? 475  LEU A CD2   1 
ATOM   2419 N  N     . ARG A 1 321 ? 31.773 -16.990 0.122   1.00 15.78 ? 476  ARG A N     1 
ATOM   2420 C  CA    . ARG A 1 321 ? 32.924 -17.536 0.840   1.00 15.01 ? 476  ARG A CA    1 
ATOM   2421 C  C     . ARG A 1 321 ? 33.375 -18.836 0.198   1.00 20.14 ? 476  ARG A C     1 
ATOM   2422 O  O     . ARG A 1 321 ? 34.587 -19.084 0.038   1.00 20.77 ? 476  ARG A O     1 
ATOM   2423 C  CB    . ARG A 1 321 ? 32.516 -17.781 2.293   1.00 15.92 ? 476  ARG A CB    1 
ATOM   2424 C  CG    . ARG A 1 321 ? 33.629 -18.400 3.181   1.00 29.53 ? 476  ARG A CG    1 
ATOM   2425 C  CD    . ARG A 1 321 ? 33.118 -18.741 4.573   1.00 27.66 ? 476  ARG A CD    1 
ATOM   2426 N  NE    . ARG A 1 321 ? 34.188 -19.331 5.388   1.00 33.38 ? 476  ARG A NE    1 
ATOM   2427 C  CZ    . ARG A 1 321 ? 35.040 -18.637 6.134   1.00 40.42 ? 476  ARG A CZ    1 
ATOM   2428 N  NH1   . ARG A 1 321 ? 35.013 -17.315 6.171   1.00 39.04 ? 476  ARG A NH1   1 
ATOM   2429 N  NH2   . ARG A 1 321 ? 35.950 -19.286 6.858   1.00 41.79 ? 476  ARG A NH2   1 
ATOM   2430 N  N     . THR A 1 322 ? 32.408 -19.703 -0.125  1.00 18.01 ? 477  THR A N     1 
ATOM   2431 C  CA    . THR A 1 322 ? 32.734 -20.986 -0.739  1.00 18.55 ? 477  THR A CA    1 
ATOM   2432 C  C     . THR A 1 322 ? 32.996 -20.887 -2.232  1.00 18.95 ? 477  THR A C     1 
ATOM   2433 O  O     . THR A 1 322 ? 33.431 -21.863 -2.860  1.00 19.68 ? 477  THR A O     1 
ATOM   2434 C  CB    . THR A 1 322 ? 31.632 -22.002 -0.499  1.00 18.88 ? 477  THR A CB    1 
ATOM   2435 O  OG1   . THR A 1 322 ? 30.437 -21.536 -1.182  1.00 18.61 ? 477  THR A OG1   1 
ATOM   2436 C  CG2   . THR A 1 322 ? 31.347 -22.187 0.965   1.00 18.83 ? 477  THR A CG2   1 
ATOM   2437 N  N     . GLU A 1 323 ? 32.750 -19.723 -2.828  1.00 18.23 ? 478  GLU A N     1 
ATOM   2438 C  CA    . GLU A 1 323 ? 32.915 -19.521 -4.262  1.00 17.30 ? 478  GLU A CA    1 
ATOM   2439 C  C     . GLU A 1 323 ? 32.028 -20.493 -5.041  1.00 16.61 ? 478  GLU A C     1 
ATOM   2440 O  O     . GLU A 1 323 ? 32.428 -21.008 -6.085  1.00 18.60 ? 478  GLU A O     1 
ATOM   2441 C  CB    . GLU A 1 323 ? 34.362 -19.615 -4.720  1.00 19.89 ? 478  GLU A CB    1 
ATOM   2442 C  CG    . GLU A 1 323 ? 35.207 -18.573 -4.012  1.00 25.20 ? 478  GLU A CG    1 
ATOM   2443 C  CD    . GLU A 1 323 ? 36.642 -18.598 -4.510  1.00 44.56 ? 478  GLU A CD    1 
ATOM   2444 O  OE1   . GLU A 1 323 ? 36.898 -17.972 -5.572  1.00 37.05 ? 478  GLU A OE1   1 
ATOM   2445 O  OE2   . GLU A 1 323 ? 37.502 -19.228 -3.849  1.00 51.30 ? 478  GLU A OE2   1 
ATOM   2446 N  N     . LYS A 1 324 ? 30.815 -20.724 -4.534  1.00 16.09 ? 479  LYS A N     1 
ATOM   2447 C  CA    . LYS A 1 324 ? 29.874 -21.657 -5.153  1.00 16.09 ? 479  LYS A CA    1 
ATOM   2448 C  C     . LYS A 1 324 ? 28.504 -20.989 -5.240  1.00 14.48 ? 479  LYS A C     1 
ATOM   2449 O  O     . LYS A 1 324 ? 27.906 -20.667 -4.217  1.00 16.47 ? 479  LYS A O     1 
ATOM   2450 C  CB    . LYS A 1 324 ? 29.705 -22.914 -4.286  1.00 19.77 ? 479  LYS A CB    1 
ATOM   2451 C  CG    . LYS A 1 324 ? 30.958 -23.799 -4.102  1.00 24.26 ? 479  LYS A CG    1 
ATOM   2452 C  CD    . LYS A 1 324 ? 31.647 -24.146 -5.390  1.00 25.13 ? 479  LYS A CD    1 
ATOM   2453 C  CE    . LYS A 1 324 ? 30.720 -24.956 -6.297  1.00 34.39 ? 479  LYS A CE    1 
ATOM   2454 N  NZ    . LYS A 1 324 ? 30.222 -26.211 -5.647  1.00 37.21 ? 479  LYS A NZ    1 
ATOM   2455 N  N     . LEU A 1 325 ? 27.992 -20.855 -6.465  1.00 15.33 ? 480  LEU A N     1 
ATOM   2456 C  CA    . LEU A 1 325 ? 26.604 -20.406 -6.685  1.00 13.20 ? 480  LEU A CA    1 
ATOM   2457 C  C     . LEU A 1 325 ? 26.183 -21.099 -7.983  1.00 13.77 ? 480  LEU A C     1 
ATOM   2458 O  O     . LEU A 1 325 ? 26.379 -20.572 -9.075  1.00 15.34 ? 480  LEU A O     1 
ATOM   2459 C  CB    . LEU A 1 325 ? 26.568 -18.884 -6.823  1.00 14.08 ? 480  LEU A CB    1 
ATOM   2460 C  CG    . LEU A 1 325 ? 25.121 -18.397 -7.050  1.00 13.15 ? 480  LEU A CG    1 
ATOM   2461 C  CD1   . LEU A 1 325 ? 24.227 -18.829 -5.898  1.00 13.86 ? 480  LEU A CD1   1 
ATOM   2462 C  CD2   . LEU A 1 325 ? 25.158 -16.862 -7.097  1.00 15.02 ? 480  LEU A CD2   1 
ATOM   2463 N  N     . GLU A 1 326 ? 25.623 -22.292 -7.849  1.00 14.07 ? 481  GLU A N     1 
ATOM   2464 C  CA    . GLU A 1 326 ? 25.229 -23.046 -9.035  1.00 14.07 ? 481  GLU A CA    1 
ATOM   2465 C  C     . GLU A 1 326 ? 24.061 -22.384 -9.714  1.00 14.07 ? 481  GLU A C     1 
ATOM   2466 O  O     . GLU A 1 326 ? 23.110 -21.962 -9.056  1.00 14.26 ? 481  GLU A O     1 
ATOM   2467 C  CB    . GLU A 1 326 ? 24.771 -24.457 -8.634  1.00 16.43 ? 481  GLU A CB    1 
ATOM   2468 C  CG    . GLU A 1 326 ? 25.862 -25.327 -8.038  1.00 21.46 ? 481  GLU A CG    1 
ATOM   2469 C  CD    . GLU A 1 326 ? 25.301 -26.693 -7.667  1.00 36.24 ? 481  GLU A CD    1 
ATOM   2470 O  OE1   . GLU A 1 326 ? 24.066 -26.908 -7.820  1.00 24.09 ? 481  GLU A OE1   1 
ATOM   2471 O  OE2   . GLU A 1 326 ? 26.089 -27.543 -7.213  1.00 30.41 ? 481  GLU A OE2   1 
ATOM   2472 N  N     . ASN A 1 327 ? 24.122 -22.329 -11.031 1.00 12.42 ? 482  ASN A N     1 
ATOM   2473 C  CA    . ASN A 1 327 ? 22.914 -21.950 -11.774 1.00 13.09 ? 482  ASN A CA    1 
ATOM   2474 C  C     . ASN A 1 327 ? 21.776 -22.888 -11.381 1.00 13.23 ? 482  ASN A C     1 
ATOM   2475 O  O     . ASN A 1 327 ? 21.970 -24.092 -11.233 1.00 14.09 ? 482  ASN A O     1 
ATOM   2476 C  CB    . ASN A 1 327 ? 23.225 -22.026 -13.282 1.00 13.97 ? 482  ASN A CB    1 
ATOM   2477 C  CG    . ASN A 1 327 ? 22.083 -21.612 -14.151 1.00 16.69 ? 482  ASN A CG    1 
ATOM   2478 O  OD1   . ASN A 1 327 ? 21.104 -22.345 -14.244 1.00 15.18 ? 482  ASN A OD1   1 
ATOM   2479 N  ND2   . ASN A 1 327 ? 22.183 -20.432 -14.813 1.00 17.53 ? 482  ASN A ND2   1 
ATOM   2480 N  N     . TYR A 1 328 ? 20.582 -22.319 -11.157 1.00 12.51 ? 483  TYR A N     1 
ATOM   2481 C  CA    . TYR A 1 328 ? 19.483 -23.106 -10.611 1.00 11.11 ? 483  TYR A CA    1 
ATOM   2482 C  C     . TYR A 1 328 ? 19.029 -24.196 -11.554 1.00 13.82 ? 483  TYR A C     1 
ATOM   2483 O  O     . TYR A 1 328 ? 18.483 -25.201 -11.085 1.00 15.25 ? 483  TYR A O     1 
ATOM   2484 C  CB    . TYR A 1 328 ? 18.302 -22.191 -10.273 1.00 13.81 ? 483  TYR A CB    1 
ATOM   2485 C  CG    . TYR A 1 328 ? 17.336 -22.797 -9.273  1.00 13.50 ? 483  TYR A CG    1 
ATOM   2486 C  CD1   . TYR A 1 328 ? 17.723 -23.057 -7.965  1.00 13.15 ? 483  TYR A CD1   1 
ATOM   2487 C  CD2   . TYR A 1 328 ? 16.002 -23.102 -9.636  1.00 17.17 ? 483  TYR A CD2   1 
ATOM   2488 C  CE1   . TYR A 1 328 ? 16.858 -23.595 -7.031  1.00 16.56 ? 483  TYR A CE1   1 
ATOM   2489 C  CE2   . TYR A 1 328 ? 15.116 -23.618 -8.721  1.00 17.28 ? 483  TYR A CE2   1 
ATOM   2490 C  CZ    . TYR A 1 328 ? 15.545 -23.888 -7.441  1.00 17.83 ? 483  TYR A CZ    1 
ATOM   2491 O  OH    . TYR A 1 328 ? 14.622 -24.409 -6.548  1.00 21.03 ? 483  TYR A OH    1 
ATOM   2492 N  N     . PHE A 1 329 ? 19.255 -24.028 -12.856 1.00 12.29 ? 484  PHE A N     1 
ATOM   2493 C  CA    . PHE A 1 329 ? 18.820 -24.975 -13.868 1.00 13.61 ? 484  PHE A CA    1 
ATOM   2494 C  C     . PHE A 1 329 ? 19.947 -25.829 -14.402 1.00 14.95 ? 484  PHE A C     1 
ATOM   2495 O  O     . PHE A 1 329 ? 19.681 -26.924 -14.915 1.00 16.38 ? 484  PHE A O     1 
ATOM   2496 C  CB    . PHE A 1 329 ? 18.194 -24.216 -15.043 1.00 13.11 ? 484  PHE A CB    1 
ATOM   2497 C  CG    . PHE A 1 329 ? 17.035 -23.369 -14.630 1.00 14.45 ? 484  PHE A CG    1 
ATOM   2498 C  CD1   . PHE A 1 329 ? 17.203 -22.073 -14.195 1.00 16.85 ? 484  PHE A CD1   1 
ATOM   2499 C  CD2   . PHE A 1 329 ? 15.747 -23.913 -14.622 1.00 19.56 ? 484  PHE A CD2   1 
ATOM   2500 C  CE1   . PHE A 1 329 ? 16.076 -21.308 -13.803 1.00 18.14 ? 484  PHE A CE1   1 
ATOM   2501 C  CE2   . PHE A 1 329 ? 14.657 -23.140 -14.221 1.00 21.35 ? 484  PHE A CE2   1 
ATOM   2502 C  CZ    . PHE A 1 329 ? 14.844 -21.870 -13.795 1.00 17.88 ? 484  PHE A CZ    1 
ATOM   2503 N  N     . ILE A 1 330 ? 21.178 -25.360 -14.270 1.00 13.11 ? 485  ILE A N     1 
ATOM   2504 C  CA    . ILE A 1 330 ? 22.368 -25.974 -14.878 1.00 15.71 ? 485  ILE A CA    1 
ATOM   2505 C  C     . ILE A 1 330 ? 23.397 -26.096 -13.757 1.00 14.90 ? 485  ILE A C     1 
ATOM   2506 O  O     . ILE A 1 330 ? 24.266 -25.212 -13.616 1.00 15.39 ? 485  ILE A O     1 
ATOM   2507 C  CB    . ILE A 1 330 ? 22.917 -25.131 -16.043 1.00 15.30 ? 485  ILE A CB    1 
ATOM   2508 C  CG1   . ILE A 1 330 ? 21.805 -24.798 -17.033 1.00 16.72 ? 485  ILE A CG1   1 
ATOM   2509 C  CG2   . ILE A 1 330 ? 24.015 -25.927 -16.765 1.00 15.56 ? 485  ILE A CG2   1 
ATOM   2510 C  CD1   . ILE A 1 330 ? 22.172 -23.774 -18.083 1.00 18.47 ? 485  ILE A CD1   1 
ATOM   2511 N  N     . PRO A 1 331 ? 23.341 -27.161 -12.952 1.00 14.87 ? 486  PRO A N     1 
ATOM   2512 C  CA    . PRO A 1 331 ? 24.104 -27.170 -11.694 1.00 17.81 ? 486  PRO A CA    1 
ATOM   2513 C  C     . PRO A 1 331 ? 25.599 -27.133 -11.894 1.00 17.19 ? 486  PRO A C     1 
ATOM   2514 O  O     . PRO A 1 331 ? 26.284 -26.564 -11.038 1.00 19.66 ? 486  PRO A O     1 
ATOM   2515 C  CB    . PRO A 1 331 ? 23.681 -28.472 -11.005 1.00 22.23 ? 486  PRO A CB    1 
ATOM   2516 C  CG    . PRO A 1 331 ? 22.379 -28.842 -11.602 1.00 22.43 ? 486  PRO A CG    1 
ATOM   2517 C  CD    . PRO A 1 331 ? 22.359 -28.254 -13.011 1.00 16.83 ? 486  PRO A CD    1 
ATOM   2518 N  N     . GLU A 1 332 ? 26.115 -27.678 -12.989 1.00 16.05 ? 487  GLU A N     1 
ATOM   2519 C  CA    . GLU A 1 332 ? 27.563 -27.599 -13.181 1.00 17.67 ? 487  GLU A CA    1 
ATOM   2520 C  C     . GLU A 1 332 ? 28.035 -26.253 -13.724 1.00 17.80 ? 487  GLU A C     1 
ATOM   2521 O  O     . GLU A 1 332 ? 29.248 -26.084 -13.957 1.00 20.89 ? 487  GLU A O     1 
ATOM   2522 C  CB    . GLU A 1 332 ? 28.069 -28.758 -14.056 1.00 19.46 ? 487  GLU A CB    1 
ATOM   2523 C  CG    . GLU A 1 332 ? 27.941 -30.083 -13.324 1.00 23.34 ? 487  GLU A CG    1 
ATOM   2524 C  CD    . GLU A 1 332 ? 28.826 -31.172 -13.913 1.00 40.03 ? 487  GLU A CD    1 
ATOM   2525 O  OE1   . GLU A 1 332 ? 28.635 -31.520 -15.093 1.00 34.06 ? 487  GLU A OE1   1 
ATOM   2526 O  OE2   . GLU A 1 332 ? 29.697 -31.700 -13.176 1.00 48.27 ? 487  GLU A OE2   1 
ATOM   2527 N  N     . PHE A 1 333 ? 27.139 -25.274 -13.936 1.00 15.60 ? 488  PHE A N     1 
ATOM   2528 C  CA    . PHE A 1 333 ? 27.547 -23.923 -14.275 1.00 14.89 ? 488  PHE A CA    1 
ATOM   2529 C  C     . PHE A 1 333 ? 27.597 -23.134 -12.966 1.00 16.80 ? 488  PHE A C     1 
ATOM   2530 O  O     . PHE A 1 333 ? 26.555 -22.827 -12.357 1.00 17.18 ? 488  PHE A O     1 
ATOM   2531 C  CB    . PHE A 1 333 ? 26.566 -23.293 -15.261 1.00 15.96 ? 488  PHE A CB    1 
ATOM   2532 C  CG    . PHE A 1 333 ? 27.070 -22.043 -15.867 1.00 16.88 ? 488  PHE A CG    1 
ATOM   2533 C  CD1   . PHE A 1 333 ? 26.908 -20.831 -15.196 1.00 18.21 ? 488  PHE A CD1   1 
ATOM   2534 C  CD2   . PHE A 1 333 ? 27.770 -22.030 -17.080 1.00 17.59 ? 488  PHE A CD2   1 
ATOM   2535 C  CE1   . PHE A 1 333 ? 27.379 -19.638 -15.733 1.00 20.02 ? 488  PHE A CE1   1 
ATOM   2536 C  CE2   . PHE A 1 333 ? 28.228 -20.836 -17.610 1.00 22.62 ? 488  PHE A CE2   1 
ATOM   2537 C  CZ    . PHE A 1 333 ? 28.013 -19.635 -16.927 1.00 22.48 ? 488  PHE A CZ    1 
ATOM   2538 N  N     . ASN A 1 334 ? 28.803 -22.803 -12.510 1.00 15.94 ? 489  ASN A N     1 
ATOM   2539 C  CA    . ASN A 1 334 ? 28.977 -22.124 -11.244 1.00 16.33 ? 489  ASN A CA    1 
ATOM   2540 C  C     . ASN A 1 334 ? 29.149 -20.647 -11.509 1.00 15.79 ? 489  ASN A C     1 
ATOM   2541 O  O     . ASN A 1 334 ? 30.186 -20.216 -12.024 1.00 16.97 ? 489  ASN A O     1 
ATOM   2542 C  CB    . ASN A 1 334 ? 30.218 -22.697 -10.567 1.00 16.41 ? 489  ASN A CB    1 
ATOM   2543 C  CG    . ASN A 1 334 ? 30.498 -22.033 -9.230  1.00 19.26 ? 489  ASN A CG    1 
ATOM   2544 O  OD1   . ASN A 1 334 ? 29.719 -21.204 -8.767  1.00 16.54 ? 489  ASN A OD1   1 
ATOM   2545 N  ND2   . ASN A 1 334 ? 31.629 -22.375 -8.602  1.00 17.92 ? 489  ASN A ND2   1 
ATOM   2546 N  N     . LEU A 1 335 ? 28.151 -19.863 -11.118 1.00 13.05 ? 490  LEU A N     1 
ATOM   2547 C  CA    . LEU A 1 335 ? 28.184 -18.436 -11.392 1.00 15.06 ? 490  LEU A CA    1 
ATOM   2548 C  C     . LEU A 1 335 ? 29.343 -17.761 -10.647 1.00 17.05 ? 490  LEU A C     1 
ATOM   2549 O  O     . LEU A 1 335 ? 29.777 -16.671 -11.031 1.00 16.38 ? 490  LEU A O     1 
ATOM   2550 C  CB    . LEU A 1 335 ? 26.889 -17.759 -10.918 1.00 16.47 ? 490  LEU A CB    1 
ATOM   2551 C  CG    . LEU A 1 335 ? 25.607 -17.893 -11.764 1.00 18.70 ? 490  LEU A CG    1 
ATOM   2552 C  CD1   . LEU A 1 335 ? 25.113 -19.281 -11.902 1.00 20.40 ? 490  LEU A CD1   1 
ATOM   2553 C  CD2   . LEU A 1 335 ? 24.537 -17.057 -11.166 1.00 22.04 ? 490  LEU A CD2   1 
ATOM   2554 N  N     . PHE A 1 336 ? 29.808 -18.362 -9.550  1.00 14.38 ? 491  PHE A N     1 
ATOM   2555 C  CA    . PHE A 1 336 ? 30.895 -17.800 -8.734  1.00 15.99 ? 491  PHE A CA    1 
ATOM   2556 C  C     . PHE A 1 336 ? 32.243 -18.467 -8.998  1.00 21.02 ? 491  PHE A C     1 
ATOM   2557 O  O     . PHE A 1 336 ? 33.167 -18.298 -8.198  1.00 22.80 ? 491  PHE A O     1 
ATOM   2558 C  CB    . PHE A 1 336 ? 30.578 -17.833 -7.233  1.00 17.50 ? 491  PHE A CB    1 
ATOM   2559 C  CG    . PHE A 1 336 ? 29.665 -16.712 -6.754  1.00 15.44 ? 491  PHE A CG    1 
ATOM   2560 C  CD1   . PHE A 1 336 ? 29.239 -15.709 -7.619  1.00 16.23 ? 491  PHE A CD1   1 
ATOM   2561 C  CD2   . PHE A 1 336 ? 29.237 -16.691 -5.446  1.00 15.48 ? 491  PHE A CD2   1 
ATOM   2562 C  CE1   . PHE A 1 336 ? 28.389 -14.662 -7.137  1.00 15.52 ? 491  PHE A CE1   1 
ATOM   2563 C  CE2   . PHE A 1 336 ? 28.415 -15.675 -4.972  1.00 17.77 ? 491  PHE A CE2   1 
ATOM   2564 C  CZ    . PHE A 1 336 ? 27.983 -14.683 -5.814  1.00 16.38 ? 491  PHE A CZ    1 
ATOM   2565 N  N     . SER A 1 337 ? 32.369 -19.209 -10.079 1.00 17.23 ? 492  SER A N     1 
ATOM   2566 C  CA    . SER A 1 337 ? 33.673 -19.757 -10.449 1.00 20.11 ? 492  SER A CA    1 
ATOM   2567 C  C     . SER A 1 337 ? 34.672 -18.617 -10.603 1.00 22.67 ? 492  SER A C     1 
ATOM   2568 O  O     . SER A 1 337 ? 34.335 -17.543 -11.100 1.00 22.42 ? 492  SER A O     1 
ATOM   2569 C  CB    . SER A 1 337 ? 33.502 -20.438 -11.792 1.00 25.56 ? 492  SER A CB    1 
ATOM   2570 O  OG    . SER A 1 337 ? 34.760 -20.919 -12.256 1.00 33.20 ? 492  SER A OG    1 
ATOM   2571 N  N     . SER A 1 338 ? 35.926 -18.857 -10.184 1.00 27.96 ? 493  SER A N     1 
ATOM   2572 C  CA    . SER A 1 338 ? 36.978 -17.882 -10.438 1.00 26.93 ? 493  SER A CA    1 
ATOM   2573 C  C     . SER A 1 338 ? 37.171 -17.604 -11.921 1.00 27.47 ? 493  SER A C     1 
ATOM   2574 O  O     . SER A 1 338 ? 37.698 -16.549 -12.268 1.00 31.67 ? 493  SER A O     1 
ATOM   2575 C  CB    . SER A 1 338 ? 38.290 -18.372 -9.840  1.00 30.17 ? 493  SER A CB    1 
ATOM   2576 O  OG    . SER A 1 338 ? 38.580 -19.654 -10.372 1.00 40.31 ? 493  SER A OG    1 
ATOM   2577 N  N     . ASN A 1 339 ? 36.715 -18.490 -12.811 1.00 26.15 ? 494  ASN A N     1 
ATOM   2578 C  CA    . ASN A 1 339 ? 36.746 -18.168 -14.232 1.00 30.16 ? 494  ASN A CA    1 
ATOM   2579 C  C     . ASN A 1 339 ? 35.834 -17.008 -14.588 1.00 27.79 ? 494  ASN A C     1 
ATOM   2580 O  O     . ASN A 1 339 ? 36.045 -16.366 -15.621 1.00 33.91 ? 494  ASN A O     1 
ATOM   2581 C  CB    . ASN A 1 339 ? 36.354 -19.389 -15.059 1.00 35.54 ? 494  ASN A CB    1 
ATOM   2582 C  CG    . ASN A 1 339 ? 37.150 -20.618 -14.689 1.00 54.64 ? 494  ASN A CG    1 
ATOM   2583 O  OD1   . ASN A 1 339 ? 38.364 -20.540 -14.451 1.00 58.99 ? 494  ASN A OD1   1 
ATOM   2584 N  ND2   . ASN A 1 339 ? 36.471 -21.766 -14.623 1.00 58.76 ? 494  ASN A ND2   1 
ATOM   2585 N  N     . LEU A 1 340 ? 34.799 -16.744 -13.775 1.00 23.54 ? 495  LEU A N     1 
ATOM   2586 C  CA    . LEU A 1 340 ? 33.857 -15.668 -14.031 1.00 22.27 ? 495  LEU A CA    1 
ATOM   2587 C  C     . LEU A 1 340 ? 34.061 -14.452 -13.142 1.00 22.17 ? 495  LEU A C     1 
ATOM   2588 O  O     . LEU A 1 340 ? 33.828 -13.327 -13.596 1.00 28.12 ? 495  LEU A O     1 
ATOM   2589 C  CB    . LEU A 1 340 ? 32.404 -16.155 -13.869 1.00 24.92 ? 495  LEU A CB    1 
ATOM   2590 C  CG    . LEU A 1 340 ? 31.970 -17.257 -14.814 1.00 25.12 ? 495  LEU A CG    1 
ATOM   2591 C  CD1   . LEU A 1 340 ? 30.506 -17.701 -14.543 1.00 22.30 ? 495  LEU A CD1   1 
ATOM   2592 C  CD2   . LEU A 1 340 ? 32.099 -16.702 -16.228 1.00 30.21 ? 495  LEU A CD2   1 
ATOM   2593 N  N     . ILE A 1 341 ? 34.414 -14.660 -11.880 1.00 22.51 ? 496  ILE A N     1 
ATOM   2594 C  CA    . ILE A 1 341 ? 34.540 -13.569 -10.913 1.00 21.45 ? 496  ILE A CA    1 
ATOM   2595 C  C     . ILE A 1 341 ? 35.749 -13.882 -10.053 1.00 20.57 ? 496  ILE A C     1 
ATOM   2596 O  O     . ILE A 1 341 ? 35.804 -14.934 -9.411  1.00 23.68 ? 496  ILE A O     1 
ATOM   2597 C  CB    . ILE A 1 341 ? 33.288 -13.428 -10.013 1.00 22.40 ? 496  ILE A CB    1 
ATOM   2598 C  CG1   . ILE A 1 341 ? 32.029 -13.251 -10.850 1.00 26.76 ? 496  ILE A CG1   1 
ATOM   2599 C  CG2   . ILE A 1 341 ? 33.411 -12.230 -9.012  1.00 25.87 ? 496  ILE A CG2   1 
ATOM   2600 C  CD1   . ILE A 1 341 ? 30.778 -13.148 -10.003 1.00 25.28 ? 496  ILE A CD1   1 
ATOM   2601 N  N     . ASP A 1 342 ? 36.694 -12.951 -10.004 1.00 23.77 ? 497  ASP A N     1 
ATOM   2602 C  CA    . ASP A 1 342 ? 37.897 -13.107 -9.199  1.00 28.05 ? 497  ASP A CA    1 
ATOM   2603 C  C     . ASP A 1 342 ? 37.592 -13.300 -7.713  1.00 24.65 ? 497  ASP A C     1 
ATOM   2604 O  O     . ASP A 1 342 ? 36.653 -12.725 -7.150  1.00 20.71 ? 497  ASP A O     1 
ATOM   2605 C  CB    . ASP A 1 342 ? 38.721 -11.822 -9.312  1.00 34.46 ? 497  ASP A CB    1 
ATOM   2606 C  CG    . ASP A 1 342 ? 39.580 -11.783 -10.554 1.00 61.80 ? 497  ASP A CG    1 
ATOM   2607 O  OD1   . ASP A 1 342 ? 39.341 -12.603 -11.470 1.00 67.20 ? 497  ASP A OD1   1 
ATOM   2608 O  OD2   . ASP A 1 342 ? 40.474 -10.911 -10.627 1.00 73.40 ? 497  ASP A OD2   1 
ATOM   2609 N  N     . LYS A 1 343 ? 38.454 -14.060 -7.050  1.00 21.41 ? 498  LYS A N     1 
ATOM   2610 C  CA    . LYS A 1 343 ? 38.344 -14.271 -5.618  1.00 21.65 ? 498  LYS A CA    1 
ATOM   2611 C  C     . LYS A 1 343 ? 38.367 -12.943 -4.853  1.00 24.66 ? 498  LYS A C     1 
ATOM   2612 O  O     . LYS A 1 343 ? 37.614 -12.770 -3.891  1.00 24.30 ? 498  LYS A O     1 
ATOM   2613 C  CB    . LYS A 1 343 ? 39.519 -15.158 -5.175  1.00 26.95 ? 498  LYS A CB    1 
ATOM   2614 C  CG    . LYS A 1 343 ? 39.705 -15.260 -3.699  1.00 33.92 ? 498  LYS A CG    1 
ATOM   2615 C  CD    . LYS A 1 343 ? 38.502 -15.899 -3.026  1.00 51.70 ? 498  LYS A CD    1 
ATOM   2616 C  CE    . LYS A 1 343 ? 38.875 -16.779 -1.829  1.00 58.56 ? 498  LYS A CE    1 
ATOM   2617 N  NZ    . LYS A 1 343 ? 37.705 -17.645 -1.398  1.00 46.11 ? 498  LYS A NZ    1 
ATOM   2618 N  N     . ARG A 1 344 ? 39.250 -12.011 -5.252  1.00 23.06 ? 499  ARG A N     1 
ATOM   2619 C  CA    . ARG A 1 344 ? 39.345 -10.712 -4.591  1.00 26.13 ? 499  ARG A CA    1 
ATOM   2620 C  C     . ARG A 1 344 ? 38.020 -9.956  -4.654  1.00 21.48 ? 499  ARG A C     1 
ATOM   2621 O  O     . ARG A 1 344 ? 37.673 -9.238  -3.705  1.00 22.94 ? 499  ARG A O     1 
ATOM   2622 C  CB    . ARG A 1 344 ? 40.456 -9.889  -5.241  1.00 35.34 ? 499  ARG A CB    1 
ATOM   2623 C  CG    . ARG A 1 344 ? 41.105 -8.883  -4.315  1.00 49.19 ? 499  ARG A CG    1 
ATOM   2624 C  CD    . ARG A 1 344 ? 42.557 -9.324  -4.043  1.00 65.79 ? 499  ARG A CD    1 
ATOM   2625 N  NE    . ARG A 1 344 ? 43.374 -9.320  -5.253  1.00 88.58 ? 499  ARG A NE    1 
ATOM   2626 C  CZ    . ARG A 1 344 ? 44.591 -9.848  -5.353  1.00 84.98 ? 499  ARG A CZ    1 
ATOM   2627 N  NH1   . ARG A 1 344 ? 45.177 -10.441 -4.322  1.00 73.28 ? 499  ARG A NH1   1 
ATOM   2628 N  NH2   . ARG A 1 344 ? 45.229 -9.791  -6.521  1.00 74.30 ? 499  ARG A NH2   1 
ATOM   2629 N  N     . SER A 1 345 ? 37.287 -10.104 -5.756  1.00 21.99 ? 500  SER A N     1 
ATOM   2630 C  CA    . SER A 1 345 ? 35.991 -9.427  -5.901  1.00 20.94 ? 500  SER A CA    1 
ATOM   2631 C  C     . SER A 1 345 ? 34.947 -10.023 -4.962  1.00 23.55 ? 500  SER A C     1 
ATOM   2632 O  O     . SER A 1 345 ? 34.180 -9.283  -4.336  1.00 19.51 ? 500  SER A O     1 
ATOM   2633 C  CB    . SER A 1 345 ? 35.526 -9.461  -7.360  1.00 23.09 ? 500  SER A CB    1 
ATOM   2634 O  OG    . SER A 1 345 ? 36.435 -8.745  -8.212  1.00 29.62 ? 500  SER A OG    1 
ATOM   2635 N  N     . LYS A 1 346 ? 34.918 -11.355 -4.834  1.00 20.13 ? 501  LYS A N     1 
ATOM   2636 C  CA    . LYS A 1 346 ? 33.995 -11.978 -3.904  1.00 17.04 ? 501  LYS A CA    1 
ATOM   2637 C  C     . LYS A 1 346 ? 34.335 -11.594 -2.466  1.00 17.76 ? 501  LYS A C     1 
ATOM   2638 O  O     . LYS A 1 346 ? 33.445 -11.314 -1.649  1.00 17.07 ? 501  LYS A O     1 
ATOM   2639 C  CB    . LYS A 1 346 ? 34.004 -13.502 -4.116  1.00 19.21 ? 501  LYS A CB    1 
ATOM   2640 C  CG    . LYS A 1 346 ? 33.366 -13.840 -5.490  1.00 20.98 ? 501  LYS A CG    1 
ATOM   2641 C  CD    . LYS A 1 346 ? 33.526 -15.284 -5.985  1.00 25.46 ? 501  LYS A CD    1 
ATOM   2642 C  CE    . LYS A 1 346 ? 34.941 -15.527 -6.383  1.00 27.75 ? 501  LYS A CE    1 
ATOM   2643 N  NZ    . LYS A 1 346 ? 35.101 -16.690 -7.284  1.00 23.88 ? 501  LYS A NZ    1 
ATOM   2644 N  N     . GLU A 1 347 ? 35.641 -11.512 -2.133  1.00 18.53 ? 502  GLU A N     1 
ATOM   2645 C  CA    . GLU A 1 347 ? 35.984 -11.128 -0.774  1.00 20.57 ? 502  GLU A CA    1 
ATOM   2646 C  C     . GLU A 1 347 ? 35.607 -9.676  -0.494  1.00 15.53 ? 502  GLU A C     1 
ATOM   2647 O  O     . GLU A 1 347 ? 35.186 -9.353  0.620   1.00 17.54 ? 502  GLU A O     1 
ATOM   2648 C  CB    . GLU A 1 347 ? 37.478 -11.354 -0.542  1.00 21.71 ? 502  GLU A CB    1 
ATOM   2649 C  CG    . GLU A 1 347 ? 37.830 -12.847 -0.661  1.00 25.01 ? 502  GLU A CG    1 
ATOM   2650 C  CD    . GLU A 1 347 ? 39.325 -13.124 -0.568  1.00 47.17 ? 502  GLU A CD    1 
ATOM   2651 O  OE1   . GLU A 1 347 ? 40.115 -12.286 -1.054  1.00 45.50 ? 502  GLU A OE1   1 
ATOM   2652 O  OE2   . GLU A 1 347 ? 39.700 -14.186 -0.018  1.00 48.45 ? 502  GLU A OE2   1 
ATOM   2653 N  N     . PHE A 1 348 ? 35.732 -8.827  -1.507  1.00 16.10 ? 503  PHE A N     1 
ATOM   2654 C  CA    . PHE A 1 348 ? 35.356 -7.432  -1.352  1.00 17.64 ? 503  PHE A CA    1 
ATOM   2655 C  C     . PHE A 1 348 ? 33.863 -7.309  -1.060  1.00 17.52 ? 503  PHE A C     1 
ATOM   2656 O  O     . PHE A 1 348 ? 33.455 -6.605  -0.147  1.00 17.99 ? 503  PHE A O     1 
ATOM   2657 C  CB    . PHE A 1 348 ? 35.741 -6.605  -2.566  1.00 18.38 ? 503  PHE A CB    1 
ATOM   2658 C  CG    . PHE A 1 348 ? 35.521 -5.121  -2.355  1.00 20.56 ? 503  PHE A CG    1 
ATOM   2659 C  CD1   . PHE A 1 348 ? 36.521 -4.338  -1.789  1.00 26.38 ? 503  PHE A CD1   1 
ATOM   2660 C  CD2   . PHE A 1 348 ? 34.325 -4.511  -2.711  1.00 22.43 ? 503  PHE A CD2   1 
ATOM   2661 C  CE1   . PHE A 1 348 ? 36.328 -2.985  -1.569  1.00 28.34 ? 503  PHE A CE1   1 
ATOM   2662 C  CE2   . PHE A 1 348 ? 34.113 -3.141  -2.502  1.00 23.34 ? 503  PHE A CE2   1 
ATOM   2663 C  CZ    . PHE A 1 348 ? 35.149 -2.374  -1.948  1.00 26.37 ? 503  PHE A CZ    1 
ATOM   2664 N  N     . LEU A 1 349 ? 33.027 -8.004  -1.841  1.00 15.71 ? 504  LEU A N     1 
ATOM   2665 C  CA    . LEU A 1 349 ? 31.590 -7.967  -1.585  1.00 15.73 ? 504  LEU A CA    1 
ATOM   2666 C  C     . LEU A 1 349 ? 31.229 -8.579  -0.232  1.00 16.04 ? 504  LEU A C     1 
ATOM   2667 O  O     . LEU A 1 349 ? 30.372 -8.056  0.480   1.00 17.69 ? 504  LEU A O     1 
ATOM   2668 C  CB    . LEU A 1 349 ? 30.855 -8.655  -2.718  1.00 14.65 ? 504  LEU A CB    1 
ATOM   2669 C  CG    . LEU A 1 349 ? 29.305 -8.624  -2.644  1.00 14.69 ? 504  LEU A CG    1 
ATOM   2670 C  CD1   . LEU A 1 349 ? 28.791 -7.164  -2.513  1.00 15.30 ? 504  LEU A CD1   1 
ATOM   2671 C  CD2   . LEU A 1 349 ? 28.704 -9.225  -3.893  1.00 15.64 ? 504  LEU A CD2   1 
ATOM   2672 N  N     . THR A 1 350 ? 31.924 -9.661  0.175   1.00 14.43 ? 505  THR A N     1 
ATOM   2673 C  CA    . THR A 1 350 ? 31.704 -10.231 1.492   1.00 16.29 ? 505  THR A CA    1 
ATOM   2674 C  C     . THR A 1 350 ? 31.920 -9.181  2.577   1.00 17.40 ? 505  THR A C     1 
ATOM   2675 O  O     . THR A 1 350 ? 31.104 -9.035  3.485   1.00 17.67 ? 505  THR A O     1 
ATOM   2676 C  CB    . THR A 1 350 ? 32.663 -11.410 1.693   1.00 20.13 ? 505  THR A CB    1 
ATOM   2677 O  OG1   . THR A 1 350 ? 32.226 -12.508 0.880   1.00 20.85 ? 505  THR A OG1   1 
ATOM   2678 C  CG2   . THR A 1 350 ? 32.688 -11.849 3.150   1.00 23.21 ? 505  THR A CG2   1 
ATOM   2679 N  N     . LYS A 1 351 ? 33.044 -8.454  2.486   1.00 16.88 ? 506  LYS A N     1 
ATOM   2680 C  CA    . LYS A 1 351 ? 33.341 -7.419  3.474   1.00 17.24 ? 506  LYS A CA    1 
ATOM   2681 C  C     . LYS A 1 351 ? 32.207 -6.390  3.570   1.00 16.44 ? 506  LYS A C     1 
ATOM   2682 O  O     . LYS A 1 351 ? 31.777 -6.009  4.657   1.00 18.70 ? 506  LYS A O     1 
ATOM   2683 C  CB    . LYS A 1 351 ? 34.654 -6.733  3.098   1.00 18.82 ? 506  LYS A CB    1 
ATOM   2684 C  CG    . LYS A 1 351 ? 35.022 -5.559  4.009   1.00 29.26 ? 506  LYS A CG    1 
ATOM   2685 C  CD    . LYS A 1 351 ? 36.366 -4.934  3.583   1.00 28.74 ? 506  LYS A CD    1 
ATOM   2686 C  CE    . LYS A 1 351 ? 36.705 -3.691  4.421   1.00 37.28 ? 506  LYS A CE    1 
ATOM   2687 N  NZ    . LYS A 1 351 ? 36.773 -4.030  5.859   1.00 37.04 ? 506  LYS A NZ    1 
ATOM   2688 N  N     . GLN A 1 352 ? 31.708 -5.919  2.415   1.00 16.08 ? 507  GLN A N     1 
ATOM   2689 C  CA    . GLN A 1 352 ? 30.681 -4.880  2.474   1.00 18.76 ? 507  GLN A CA    1 
ATOM   2690 C  C     . GLN A 1 352 ? 29.359 -5.422  3.020   1.00 17.69 ? 507  GLN A C     1 
ATOM   2691 O  O     . GLN A 1 352 ? 28.681 -4.747  3.801   1.00 17.82 ? 507  GLN A O     1 
ATOM   2692 C  CB    . GLN A 1 352 ? 30.495 -4.229  1.094   1.00 16.73 ? 507  GLN A CB    1 
ATOM   2693 C  CG    . GLN A 1 352 ? 31.819 -3.789  0.419   1.00 18.42 ? 507  GLN A CG    1 
ATOM   2694 C  CD    . GLN A 1 352 ? 32.767 -3.043  1.314   1.00 26.81 ? 507  GLN A CD    1 
ATOM   2695 O  OE1   . GLN A 1 352 ? 32.333 -2.252  2.139   1.00 24.37 ? 507  GLN A OE1   1 
ATOM   2696 N  NE2   . GLN A 1 352 ? 34.065 -3.315  1.169   1.00 31.58 ? 507  GLN A NE2   1 
ATOM   2697 N  N     . ILE A 1 353 ? 28.950 -6.624  2.589   1.00 15.20 ? 508  ILE A N     1 
ATOM   2698 C  CA    . ILE A 1 353 ? 27.712 -7.179  3.114   1.00 15.92 ? 508  ILE A CA    1 
ATOM   2699 C  C     . ILE A 1 353 ? 27.824 -7.493  4.605   1.00 16.19 ? 508  ILE A C     1 
ATOM   2700 O  O     . ILE A 1 353 ? 26.868 -7.282  5.355   1.00 18.75 ? 508  ILE A O     1 
ATOM   2701 C  CB    . ILE A 1 353 ? 27.304 -8.391  2.269   1.00 15.65 ? 508  ILE A CB    1 
ATOM   2702 C  CG1   . ILE A 1 353 ? 26.925 -7.959  0.837   1.00 15.20 ? 508  ILE A CG1   1 
ATOM   2703 C  CG2   . ILE A 1 353 ? 26.112 -9.091  2.928   1.00 16.13 ? 508  ILE A CG2   1 
ATOM   2704 C  CD1   . ILE A 1 353 ? 26.630 -9.192  -0.090  1.00 16.38 ? 508  ILE A CD1   1 
ATOM   2705 N  N     . GLU A 1 354 ? 29.001 -7.957  5.066   1.00 17.45 ? 509  GLU A N     1 
ATOM   2706 C  CA    . GLU A 1 354 ? 29.168 -8.211  6.484   1.00 20.12 ? 509  GLU A CA    1 
ATOM   2707 C  C     . GLU A 1 354 ? 29.049 -6.922  7.266   1.00 18.44 ? 509  GLU A C     1 
ATOM   2708 O  O     . GLU A 1 354 ? 28.360 -6.885  8.284   1.00 18.49 ? 509  GLU A O     1 
ATOM   2709 C  CB    . GLU A 1 354 ? 30.496 -8.892  6.760   1.00 20.72 ? 509  GLU A CB    1 
ATOM   2710 C  CG    . GLU A 1 354 ? 30.493 -10.354 6.347   1.00 22.23 ? 509  GLU A CG    1 
ATOM   2711 C  CD    . GLU A 1 354 ? 31.814 -11.054 6.640   1.00 48.75 ? 509  GLU A CD    1 
ATOM   2712 O  OE1   . GLU A 1 354 ? 32.806 -10.340 6.887   1.00 46.38 ? 509  GLU A OE1   1 
ATOM   2713 O  OE2   . GLU A 1 354 ? 31.852 -12.308 6.636   1.00 48.36 ? 509  GLU A OE2   1 
ATOM   2714 N  N     . TYR A 1 355 ? 29.649 -5.844  6.758   1.00 19.33 ? 510  TYR A N     1 
ATOM   2715 C  CA    . TYR A 1 355 ? 29.481 -4.563  7.440   1.00 22.94 ? 510  TYR A CA    1 
ATOM   2716 C  C     . TYR A 1 355 ? 28.009 -4.177  7.513   1.00 20.28 ? 510  TYR A C     1 
ATOM   2717 O  O     . TYR A 1 355 ? 27.511 -3.714  8.543   1.00 20.43 ? 510  TYR A O     1 
ATOM   2718 C  CB    . TYR A 1 355 ? 30.276 -3.481  6.714   1.00 19.06 ? 510  TYR A CB    1 
ATOM   2719 C  CG    . TYR A 1 355 ? 30.079 -2.110  7.321   1.00 19.78 ? 510  TYR A CG    1 
ATOM   2720 C  CD1   . TYR A 1 355 ? 29.055 -1.262  6.892   1.00 21.42 ? 510  TYR A CD1   1 
ATOM   2721 C  CD2   . TYR A 1 355 ? 30.907 -1.637  8.328   1.00 20.53 ? 510  TYR A CD2   1 
ATOM   2722 C  CE1   . TYR A 1 355 ? 28.855 -0.015  7.471   1.00 20.41 ? 510  TYR A CE1   1 
ATOM   2723 C  CE2   . TYR A 1 355 ? 30.685 -0.377  8.910   1.00 21.34 ? 510  TYR A CE2   1 
ATOM   2724 C  CZ    . TYR A 1 355 ? 29.667 0.421   8.469   1.00 23.97 ? 510  TYR A CZ    1 
ATOM   2725 O  OH    . TYR A 1 355 ? 29.472 1.672   9.033   1.00 26.20 ? 510  TYR A OH    1 
ATOM   2726 N  N     . GLU A 1 356 ? 27.282 -4.348  6.414   1.00 16.21 ? 511  GLU A N     1 
ATOM   2727 C  CA    . GLU A 1 356 ? 25.881 -4.012  6.456   1.00 18.16 ? 511  GLU A CA    1 
ATOM   2728 C  C     . GLU A 1 356 ? 25.113 -4.874  7.456   1.00 18.43 ? 511  GLU A C     1 
ATOM   2729 O  O     . GLU A 1 356 ? 24.302 -4.356  8.230   1.00 19.57 ? 511  GLU A O     1 
ATOM   2730 C  CB    . GLU A 1 356 ? 25.272 -4.152  5.064   1.00 18.73 ? 511  GLU A CB    1 
ATOM   2731 C  CG    . GLU A 1 356 ? 25.790 -3.139  4.058   1.00 19.53 ? 511  GLU A CG    1 
ATOM   2732 C  CD    . GLU A 1 356 ? 25.508 -1.713  4.490   1.00 30.34 ? 511  GLU A CD    1 
ATOM   2733 O  OE1   . GLU A 1 356 ? 24.371 -1.458  4.951   1.00 31.03 ? 511  GLU A OE1   1 
ATOM   2734 O  OE2   . GLU A 1 356 ? 26.408 -0.849  4.368   1.00 29.67 ? 511  GLU A OE2   1 
ATOM   2735 N  N     . ARG A 1 357 ? 25.329 -6.193  7.426   1.00 17.27 ? 512  ARG A N     1 
ATOM   2736 C  CA    . ARG A 1 357 ? 24.614 -7.082  8.349   1.00 19.55 ? 512  ARG A CA    1 
ATOM   2737 C  C     . ARG A 1 357 ? 24.932 -6.738  9.800   1.00 20.99 ? 512  ARG A C     1 
ATOM   2738 O  O     . ARG A 1 357 ? 24.030 -6.713  10.643  1.00 22.92 ? 512  ARG A O     1 
ATOM   2739 C  CB    . ARG A 1 357 ? 24.966 -8.537  8.049   1.00 21.81 ? 512  ARG A CB    1 
ATOM   2740 C  CG    . ARG A 1 357 ? 24.192 -9.520  8.820   1.00 24.76 ? 512  ARG A CG    1 
ATOM   2741 C  CD    . ARG A 1 357 ? 24.568 -10.897 8.347   1.00 26.12 ? 512  ARG A CD    1 
ATOM   2742 N  NE    . ARG A 1 357 ? 23.909 -11.909 9.149   1.00 33.32 ? 512  ARG A NE    1 
ATOM   2743 C  CZ    . ARG A 1 357 ? 24.481 -12.530 10.166  1.00 38.25 ? 512  ARG A CZ    1 
ATOM   2744 N  NH1   . ARG A 1 357 ? 25.740 -12.285 10.500  1.00 33.68 ? 512  ARG A NH1   1 
ATOM   2745 N  NH2   . ARG A 1 357 ? 23.781 -13.429 10.850  1.00 35.09 ? 512  ARG A NH2   1 
ATOM   2746 N  N     . ASN A 1 358 ? 26.205 -6.420  10.088  1.00 21.57 ? 513  ASN A N     1 
ATOM   2747 C  CA    . ASN A 1 358 ? 26.674 -6.105  11.436  1.00 22.97 ? 513  ASN A CA    1 
ATOM   2748 C  C     . ASN A 1 358 ? 26.162 -4.768  11.955  1.00 24.97 ? 513  ASN A C     1 
ATOM   2749 O  O     . ASN A 1 358 ? 26.251 -4.528  13.167  1.00 32.16 ? 513  ASN A O     1 
ATOM   2750 C  CB    . ASN A 1 358 ? 28.213 -6.113  11.516  1.00 23.10 ? 513  ASN A CB    1 
ATOM   2751 C  CG    . ASN A 1 358 ? 28.823 -7.480  11.284  1.00 26.60 ? 513  ASN A CG    1 
ATOM   2752 O  OD1   . ASN A 1 358 ? 28.145 -8.510  11.396  1.00 30.79 ? 513  ASN A OD1   1 
ATOM   2753 N  ND2   . ASN A 1 358 ? 30.105 -7.502  10.934  1.00 29.11 ? 513  ASN A ND2   1 
ATOM   2754 N  N     . ASN A 1 359 ? 25.640 -3.894  11.095  1.00 21.17 ? 514  ASN A N     1 
ATOM   2755 C  CA    . ASN A 1 359 ? 25.230 -2.553  11.464  1.00 24.08 ? 514  ASN A CA    1 
ATOM   2756 C  C     . ASN A 1 359 ? 23.773 -2.285  11.118  1.00 24.00 ? 514  ASN A C     1 
ATOM   2757 O  O     . ASN A 1 359 ? 23.368 -1.134  10.983  1.00 26.99 ? 514  ASN A O     1 
ATOM   2758 C  CB    . ASN A 1 359 ? 26.159 -1.503  10.873  1.00 27.79 ? 514  ASN A CB    1 
ATOM   2759 C  CG    . ASN A 1 359 ? 27.560 -1.613  11.448  1.00 26.12 ? 514  ASN A CG    1 
ATOM   2760 O  OD1   . ASN A 1 359 ? 28.456 -2.226  10.865  1.00 23.42 ? 514  ASN A OD1   1 
ATOM   2761 N  ND2   . ASN A 1 359 ? 27.744 -1.048  12.641  1.00 29.42 ? 514  ASN A ND2   1 
ATOM   2762 N  N     A GLU A 1 360 ? 22.980 -3.353  11.023  0.45 26.70 ? 515  GLU A N     1 
ATOM   2763 N  N     B GLU A 1 360 ? 22.975 -3.339  10.951  0.55 26.68 ? 515  GLU A N     1 
ATOM   2764 C  CA    A GLU A 1 360 ? 21.560 -3.295  10.646  0.45 27.81 ? 515  GLU A CA    1 
ATOM   2765 C  CA    B GLU A 1 360 ? 21.540 -3.187  10.708  0.55 27.84 ? 515  GLU A CA    1 
ATOM   2766 C  C     A GLU A 1 360 ? 21.317 -2.477  9.378   0.45 25.23 ? 515  GLU A C     1 
ATOM   2767 C  C     B GLU A 1 360 ? 21.230 -2.580  9.340   0.55 25.16 ? 515  GLU A C     1 
ATOM   2768 O  O     A GLU A 1 360 ? 20.439 -1.612  9.325   0.45 24.69 ? 515  GLU A O     1 
ATOM   2769 O  O     B GLU A 1 360 ? 20.201 -1.925  9.178   0.55 25.22 ? 515  GLU A O     1 
ATOM   2770 C  CB    A GLU A 1 360 ? 20.627 -2.892  11.805  0.45 33.74 ? 515  GLU A CB    1 
ATOM   2771 C  CB    B GLU A 1 360 ? 20.865 -2.357  11.813  0.55 33.08 ? 515  GLU A CB    1 
ATOM   2772 C  CG    A GLU A 1 360 ? 21.013 -1.644  12.621  0.45 34.04 ? 515  GLU A CG    1 
ATOM   2773 C  CG    B GLU A 1 360 ? 20.927 -2.940  13.220  0.55 36.11 ? 515  GLU A CG    1 
ATOM   2774 C  CD    A GLU A 1 360 ? 21.978 -1.978  13.749  0.45 35.41 ? 515  GLU A CD    1 
ATOM   2775 C  CD    B GLU A 1 360 ? 20.035 -4.148  13.383  0.55 41.75 ? 515  GLU A CD    1 
ATOM   2776 O  OE1   A GLU A 1 360 ? 21.986 -3.147  14.179  0.45 39.84 ? 515  GLU A OE1   1 
ATOM   2777 O  OE1   B GLU A 1 360 ? 18.841 -3.962  13.727  0.55 44.79 ? 515  GLU A OE1   1 
ATOM   2778 O  OE2   A GLU A 1 360 ? 22.767 -1.105  14.171  0.45 33.78 ? 515  GLU A OE2   1 
ATOM   2779 O  OE2   B GLU A 1 360 ? 20.521 -5.277  13.157  0.55 41.32 ? 515  GLU A OE2   1 
ATOM   2780 N  N     . PHE A 1 361 ? 22.117 -2.757  8.350   1.00 22.69 ? 516  PHE A N     1 
ATOM   2781 C  CA    . PHE A 1 361 ? 21.883 -2.254  6.992   1.00 22.05 ? 516  PHE A CA    1 
ATOM   2782 C  C     . PHE A 1 361 ? 21.769 -0.740  6.842   1.00 20.72 ? 516  PHE A C     1 
ATOM   2783 O  O     . PHE A 1 361 ? 20.759 -0.216  6.341   1.00 20.43 ? 516  PHE A O     1 
ATOM   2784 C  CB    . PHE A 1 361 ? 20.728 -3.016  6.308   1.00 18.54 ? 516  PHE A CB    1 
ATOM   2785 C  CG    . PHE A 1 361 ? 20.942 -4.490  6.332   1.00 18.25 ? 516  PHE A CG    1 
ATOM   2786 C  CD1   . PHE A 1 361 ? 21.673 -5.117  5.352   1.00 22.55 ? 516  PHE A CD1   1 
ATOM   2787 C  CD2   . PHE A 1 361 ? 20.409 -5.245  7.369   1.00 25.00 ? 516  PHE A CD2   1 
ATOM   2788 C  CE1   . PHE A 1 361 ? 21.923 -6.480  5.426   1.00 20.42 ? 516  PHE A CE1   1 
ATOM   2789 C  CE2   . PHE A 1 361 ? 20.632 -6.610  7.420   1.00 22.60 ? 516  PHE A CE2   1 
ATOM   2790 C  CZ    . PHE A 1 361 ? 21.384 -7.211  6.445   1.00 19.91 ? 516  PHE A CZ    1 
ATOM   2791 N  N     . PRO A 1 362 ? 22.836 -0.018  7.191   1.00 21.37 ? 517  PRO A N     1 
ATOM   2792 C  CA    . PRO A 1 362 ? 22.813 1.435   7.022   1.00 20.98 ? 517  PRO A CA    1 
ATOM   2793 C  C     . PRO A 1 362 ? 22.660 1.879   5.579   1.00 22.58 ? 517  PRO A C     1 
ATOM   2794 O  O     . PRO A 1 362 ? 22.137 2.971   5.328   1.00 23.51 ? 517  PRO A O     1 
ATOM   2795 C  CB    . PRO A 1 362 ? 24.148 1.871   7.655   1.00 25.24 ? 517  PRO A CB    1 
ATOM   2796 C  CG    . PRO A 1 362 ? 24.991 0.655   7.627   1.00 26.45 ? 517  PRO A CG    1 
ATOM   2797 C  CD    . PRO A 1 362 ? 24.036 -0.460  7.912   1.00 25.30 ? 517  PRO A CD    1 
ATOM   2798 N  N     . VAL A 1 363 ? 22.989 1.022   4.614   1.00 19.45 ? 518  VAL A N     1 
ATOM   2799 C  CA    . VAL A 1 363 ? 22.813 1.367   3.225   1.00 20.67 ? 518  VAL A CA    1 
ATOM   2800 C  C     . VAL A 1 363 ? 21.344 1.466   2.861   1.00 21.72 ? 518  VAL A C     1 
ATOM   2801 O  O     . VAL A 1 363 ? 21.023 2.048   1.838   1.00 26.68 ? 518  VAL A O     1 
ATOM   2802 C  CB    . VAL A 1 363 ? 23.605 0.399   2.318   1.00 26.49 ? 518  VAL A CB    1 
ATOM   2803 C  CG1   . VAL A 1 363 ? 22.773 -0.878  2.004   1.00 23.44 ? 518  VAL A CG1   1 
ATOM   2804 C  CG2   . VAL A 1 363 ? 24.028 1.098   1.090   1.00 30.56 ? 518  VAL A CG2   1 
ATOM   2805 N  N     . PHE A 1 364 ? 20.453 1.006   3.743   1.00 21.97 ? 519  PHE A N     1 
ATOM   2806 C  CA    . PHE A 1 364 ? 19.027 1.148   3.502   1.00 25.79 ? 519  PHE A CA    1 
ATOM   2807 C  C     . PHE A 1 364 ? 18.468 2.489   3.964   1.00 35.54 ? 519  PHE A C     1 
ATOM   2808 O  O     . PHE A 1 364 ? 17.382 2.877   3.515   1.00 39.91 ? 519  PHE A O     1 
ATOM   2809 C  CB    . PHE A 1 364 ? 18.242 0.026   4.175   1.00 20.93 ? 519  PHE A CB    1 
ATOM   2810 C  CG    . PHE A 1 364 ? 18.360 -1.326  3.491   1.00 19.33 ? 519  PHE A CG    1 
ATOM   2811 C  CD1   . PHE A 1 364 ? 18.897 -1.504  2.195   1.00 21.71 ? 519  PHE A CD1   1 
ATOM   2812 C  CD2   . PHE A 1 364 ? 17.905 -2.434  4.185   1.00 18.17 ? 519  PHE A CD2   1 
ATOM   2813 C  CE1   . PHE A 1 364 ? 18.938 -2.810  1.636   1.00 18.90 ? 519  PHE A CE1   1 
ATOM   2814 C  CE2   . PHE A 1 364 ? 17.975 -3.706  3.608   1.00 18.68 ? 519  PHE A CE2   1 
ATOM   2815 C  CZ    . PHE A 1 364 ? 18.472 -3.875  2.355   1.00 15.98 ? 519  PHE A CZ    1 
ATOM   2816 N  N     . ASP A 1 365 ? 19.166 3.195   4.834   1.00 24.45 ? 520  ASP A N     1 
ATOM   2817 C  CA    . ASP A 1 365 ? 18.657 4.471   5.362   1.00 30.94 ? 520  ASP A CA    1 
ATOM   2818 C  C     . ASP A 1 365 ? 18.609 5.583   4.308   1.00 37.00 ? 520  ASP A C     1 
ATOM   2819 O  O     . ASP A 1 365 ? 19.477 5.684   3.437   1.00 37.35 ? 520  ASP A O     1 
ATOM   2820 C  CB    . ASP A 1 365 ? 19.504 4.890   6.557   1.00 36.19 ? 520  ASP A CB    1 
ATOM   2821 C  CG    . ASP A 1 365 ? 19.466 3.870   7.669   1.00 47.81 ? 520  ASP A CG    1 
ATOM   2822 O  OD1   . ASP A 1 365 ? 18.407 3.230   7.826   1.00 57.51 ? 520  ASP A OD1   1 
ATOM   2823 O  OD2   . ASP A 1 365 ? 20.480 3.700   8.378   1.00 48.05 ? 520  ASP A OD2   1 
HETATM 2824 MG MG    . MG  B 2 .   ? 17.473 -6.435  -18.418 1.00 13.94 ? 601  MG  A MG    1 
HETATM 2825 MG MG    . MG  C 2 .   ? 15.213 -6.543  -15.694 1.00 12.98 ? 602  MG  A MG    1 
HETATM 2826 ZN ZN    . ZN  D 3 .   ? 3.544  -16.249 -1.098  1.00 15.85 ? 603  ZN  A ZN    1 
HETATM 2827 P  PG    . ANP E 4 .   ? 16.308 -6.288  -12.512 1.00 14.58 ? 604  ANP A PG    1 
HETATM 2828 O  O1G   . ANP E 4 .   ? 15.209 -5.742  -11.627 1.00 14.07 ? 604  ANP A O1G   1 
HETATM 2829 O  O2G   . ANP E 4 .   ? 17.721 -5.867  -11.920 1.00 15.73 ? 604  ANP A O2G   1 
HETATM 2830 O  O3G   . ANP E 4 .   ? 16.172 -5.843  -13.945 1.00 13.61 ? 604  ANP A O3G   1 
HETATM 2831 P  PB    . ANP E 4 .   ? 16.017 -8.900  -13.726 1.00 13.13 ? 604  ANP A PB    1 
HETATM 2832 O  O1B   . ANP E 4 .   ? 15.801 -10.330 -13.359 1.00 15.48 ? 604  ANP A O1B   1 
HETATM 2833 O  O2B   . ANP E 4 .   ? 14.978 -8.349  -14.704 1.00 12.03 ? 604  ANP A O2B   1 
HETATM 2834 N  N3B   . ANP E 4 .   ? 16.095 -7.956  -12.406 1.00 13.16 ? 604  ANP A N3B   1 
HETATM 2835 P  PA    . ANP E 4 .   ? 17.909 -8.296  -15.851 1.00 13.91 ? 604  ANP A PA    1 
HETATM 2836 O  O1A   . ANP E 4 .   ? 19.362 -7.993  -15.664 1.00 17.33 ? 604  ANP A O1A   1 
HETATM 2837 O  O2A   . ANP E 4 .   ? 17.056 -7.230  -16.511 1.00 13.15 ? 604  ANP A O2A   1 
HETATM 2838 O  O3A   . ANP E 4 .   ? 17.462 -8.836  -14.428 1.00 12.99 ? 604  ANP A O3A   1 
HETATM 2839 O  "O5'" . ANP E 4 .   ? 17.915 -9.656  -16.707 1.00 14.03 ? 604  ANP A "O5'" 1 
HETATM 2840 C  "C5'" . ANP E 4 .   ? 16.704 -10.146 -17.273 1.00 13.33 ? 604  ANP A "C5'" 1 
HETATM 2841 C  "C4'" . ANP E 4 .   ? 16.724 -11.672 -17.261 1.00 14.43 ? 604  ANP A "C4'" 1 
HETATM 2842 O  "O4'" . ANP E 4 .   ? 17.890 -12.159 -17.951 1.00 16.34 ? 604  ANP A "O4'" 1 
HETATM 2843 C  "C3'" . ANP E 4 .   ? 16.851 -12.299 -15.874 1.00 16.00 ? 604  ANP A "C3'" 1 
HETATM 2844 O  "O3'" . ANP E 4 .   ? 15.627 -12.321 -15.154 1.00 17.83 ? 604  ANP A "O3'" 1 
HETATM 2845 C  "C2'" . ANP E 4 .   ? 17.371 -13.694 -16.208 1.00 17.12 ? 604  ANP A "C2'" 1 
HETATM 2846 O  "O2'" . ANP E 4 .   ? 16.315 -14.557 -16.598 1.00 19.19 ? 604  ANP A "O2'" 1 
HETATM 2847 C  "C1'" . ANP E 4 .   ? 18.284 -13.408 -17.407 1.00 16.20 ? 604  ANP A "C1'" 1 
HETATM 2848 N  N9    . ANP E 4 .   ? 19.674 -13.318 -17.017 1.00 15.26 ? 604  ANP A N9    1 
HETATM 2849 C  C8    . ANP E 4 .   ? 20.377 -12.210 -16.613 1.00 15.20 ? 604  ANP A C8    1 
HETATM 2850 N  N7    . ANP E 4 .   ? 21.616 -12.455 -16.272 1.00 16.04 ? 604  ANP A N7    1 
HETATM 2851 C  C5    . ANP E 4 .   ? 21.723 -13.825 -16.423 1.00 14.97 ? 604  ANP A C5    1 
HETATM 2852 C  C6    . ANP E 4 .   ? 22.795 -14.708 -16.214 1.00 18.12 ? 604  ANP A C6    1 
HETATM 2853 N  N6    . ANP E 4 .   ? 23.976 -14.322 -15.735 1.00 21.47 ? 604  ANP A N6    1 
HETATM 2854 N  N1    . ANP E 4 .   ? 22.571 -16.014 -16.445 1.00 18.18 ? 604  ANP A N1    1 
HETATM 2855 C  C2    . ANP E 4 .   ? 21.378 -16.398 -16.911 1.00 17.59 ? 604  ANP A C2    1 
HETATM 2856 N  N3    . ANP E 4 .   ? 20.299 -15.657 -17.176 1.00 16.60 ? 604  ANP A N3    1 
HETATM 2857 C  C4    . ANP E 4 .   ? 20.545 -14.372 -16.882 1.00 16.05 ? 604  ANP A C4    1 
HETATM 2858 C  C1    . GOL F 5 .   ? 2.690  -4.327  -12.481 1.00 24.10 ? 605  GOL A C1    1 
HETATM 2859 O  O1    . GOL F 5 .   ? 2.936  -5.346  -13.329 1.00 38.65 ? 605  GOL A O1    1 
HETATM 2860 C  C2    . GOL F 5 .   ? 4.022  -3.954  -11.675 1.00 6.74  ? 605  GOL A C2    1 
HETATM 2861 O  O2    . GOL F 5 .   ? 3.719  -3.953  -10.356 1.00 24.42 ? 605  GOL A O2    1 
HETATM 2862 C  C3    . GOL F 5 .   ? 4.975  -5.208  -11.967 1.00 22.99 ? 605  GOL A C3    1 
HETATM 2863 O  O3    . GOL F 5 .   ? 6.187  -4.955  -11.388 1.00 35.63 ? 605  GOL A O3    1 
HETATM 2864 C  C13   . JUJ G 6 .   ? 21.993 -8.789  -19.618 1.00 17.88 ? 606  JUJ A C13   1 
HETATM 2865 C  C20   . JUJ G 6 .   ? 18.076 -12.887 -21.084 1.00 14.13 ? 606  JUJ A C20   1 
HETATM 2866 C  C21   . JUJ G 6 .   ? 17.978 -11.777 -21.914 1.00 14.58 ? 606  JUJ A C21   1 
HETATM 2867 C  C26   . JUJ G 6 .   ? 16.844 -13.316 -20.516 1.00 15.18 ? 606  JUJ A C26   1 
HETATM 2868 O  O01   . JUJ G 6 .   ? 19.520 -5.894  -17.887 1.00 16.32 ? 606  JUJ A O01   1 
HETATM 2869 C  C02   . JUJ G 6 .   ? 20.480 -6.792  -18.380 1.00 15.97 ? 606  JUJ A C02   1 
HETATM 2870 C  C03   . JUJ G 6 .   ? 19.777 -7.989  -18.995 1.00 16.01 ? 606  JUJ A C03   1 
HETATM 2871 O  O04   . JUJ G 6 .   ? 18.593 -8.088  -19.027 1.00 14.59 ? 606  JUJ A O04   1 
HETATM 2872 N  N05   . JUJ G 6 .   ? 20.519 -8.906  -19.504 1.00 16.07 ? 606  JUJ A N05   1 
HETATM 2873 C  C06   . JUJ G 6 .   ? 19.936 -10.055 -20.203 1.00 15.17 ? 606  JUJ A C06   1 
HETATM 2874 C  C07   . JUJ G 6 .   ? 20.806 -11.329 -20.057 1.00 15.40 ? 606  JUJ A C07   1 
HETATM 2875 C  C08   . JUJ G 6 .   ? 20.479 -12.724 -20.332 1.00 14.54 ? 606  JUJ A C08   1 
HETATM 2876 C  C09   . JUJ G 6 .   ? 21.695 -13.429 -19.983 1.00 15.31 ? 606  JUJ A C09   1 
HETATM 2877 N  N10   . JUJ G 6 .   ? 22.639 -12.487 -19.581 1.00 15.86 ? 606  JUJ A N10   1 
HETATM 2878 C  C11   . JUJ G 6 .   ? 22.075 -11.236 -19.631 1.00 15.96 ? 606  JUJ A C11   1 
HETATM 2879 C  C12   . JUJ G 6 .   ? 22.788 -10.009 -19.235 1.00 15.24 ? 606  JUJ A C12   1 
HETATM 2880 C  C14   . JUJ G 6 .   ? 21.763 -14.774 -20.062 1.00 14.65 ? 606  JUJ A C14   1 
HETATM 2881 CL CL2   . JUJ G 6 .   ? 23.267 -15.570 -19.601 1.00 99.84 ? 606  JUJ A CL2   1 
HETATM 2882 C  C16   . JUJ G 6 .   ? 20.679 -15.474 -20.466 1.00 15.74 ? 606  JUJ A C16   1 
HETATM 2883 CL CL1   . JUJ G 6 .   ? 20.704 -17.205 -20.511 1.00 18.09 ? 606  JUJ A CL1   1 
HETATM 2884 C  C18   . JUJ G 6 .   ? 19.475 -14.845 -20.800 1.00 14.05 ? 606  JUJ A C18   1 
HETATM 2885 C  C19   . JUJ G 6 .   ? 19.370 -13.509 -20.738 1.00 13.90 ? 606  JUJ A C19   1 
HETATM 2886 N  N22   . JUJ G 6 .   ? 16.839 -11.150 -22.275 1.00 17.18 ? 606  JUJ A N22   1 
HETATM 2887 C  C23   . JUJ G 6 .   ? 15.643 -11.565 -21.718 1.00 16.36 ? 606  JUJ A C23   1 
HETATM 2888 N  N24   . JUJ G 6 .   ? 14.512 -10.894 -22.077 1.00 17.89 ? 606  JUJ A N24   1 
HETATM 2889 C  C25   . JUJ G 6 .   ? 15.642 -12.668 -20.833 1.00 14.61 ? 606  JUJ A C25   1 
HETATM 2890 O  O     . HOH H 7 .   ? 19.447 -6.308  11.499  1.00 44.03 ? 701  HOH A O     1 
HETATM 2891 O  O     . HOH H 7 .   ? 3.407  -19.196 9.580   1.00 37.04 ? 702  HOH A O     1 
HETATM 2892 O  O     . HOH H 7 .   ? 31.000 -1.322  3.771   1.00 33.43 ? 703  HOH A O     1 
HETATM 2893 O  O     . HOH H 7 .   ? 35.702 -8.525  -10.426 1.00 36.59 ? 704  HOH A O     1 
HETATM 2894 O  O     . HOH H 7 .   ? 20.342 -9.587  8.871   1.00 30.05 ? 705  HOH A O     1 
HETATM 2895 O  O     . HOH H 7 .   ? 8.195  -23.482 9.778   1.00 32.21 ? 706  HOH A O     1 
HETATM 2896 O  O     . HOH H 7 .   ? -7.740 -18.075 -3.618  1.00 24.41 ? 707  HOH A O     1 
HETATM 2897 O  O     . HOH H 7 .   ? 3.963  -13.674 -39.019 1.00 42.04 ? 708  HOH A O     1 
HETATM 2898 O  O     . HOH H 7 .   ? 3.638  -18.077 -15.340 1.00 41.23 ? 709  HOH A O     1 
HETATM 2899 O  O     . HOH H 7 .   ? 20.244 -4.409  -15.969 1.00 30.45 ? 710  HOH A O     1 
HETATM 2900 O  O     . HOH H 7 .   ? 26.215 -31.381 -15.879 1.00 31.17 ? 711  HOH A O     1 
HETATM 2901 O  O     . HOH H 7 .   ? -0.455 -13.702 5.919   1.00 30.98 ? 712  HOH A O     1 
HETATM 2902 O  O     . HOH H 7 .   ? -1.948 5.769   -18.186 1.00 30.23 ? 713  HOH A O     1 
HETATM 2903 O  O     . HOH H 7 .   ? 31.420 -1.586  -9.125  1.00 38.14 ? 714  HOH A O     1 
HETATM 2904 O  O     . HOH H 7 .   ? 27.498 -10.622 9.587   1.00 36.38 ? 715  HOH A O     1 
HETATM 2905 O  O     . HOH H 7 .   ? 29.006 -16.797 -37.605 1.00 35.25 ? 716  HOH A O     1 
HETATM 2906 O  O     . HOH H 7 .   ? -5.975 -20.754 3.075   1.00 33.87 ? 717  HOH A O     1 
HETATM 2907 O  O     . HOH H 7 .   ? 33.124 -7.976  -9.858  1.00 29.71 ? 718  HOH A O     1 
HETATM 2908 O  O     . HOH H 7 .   ? 4.633  -8.939  1.099   1.00 29.03 ? 719  HOH A O     1 
HETATM 2909 O  O     . HOH H 7 .   ? 9.422  3.715   -5.315  1.00 29.65 ? 720  HOH A O     1 
HETATM 2910 O  O     . HOH H 7 .   ? 0.679  -20.743 2.800   1.00 19.06 ? 721  HOH A O     1 
HETATM 2911 O  O     . HOH H 7 .   ? 6.140  -17.331 12.428  1.00 34.81 ? 722  HOH A O     1 
HETATM 2912 O  O     . HOH H 7 .   ? 14.224 -10.847 -11.163 1.00 19.94 ? 723  HOH A O     1 
HETATM 2913 O  O     . HOH H 7 .   ? 5.172  -4.239  -8.179  1.00 22.70 ? 724  HOH A O     1 
HETATM 2914 O  O     . HOH H 7 .   ? 28.888 -34.010 -15.911 1.00 46.25 ? 725  HOH A O     1 
HETATM 2915 O  O     . HOH H 7 .   ? 6.426  -9.656  4.203   1.00 23.96 ? 726  HOH A O     1 
HETATM 2916 O  O     . HOH H 7 .   ? 15.494 7.657   -25.356 1.00 30.73 ? 727  HOH A O     1 
HETATM 2917 O  O     . HOH H 7 .   ? 17.970 -5.290  -8.924  1.00 25.67 ? 728  HOH A O     1 
HETATM 2918 O  O     . HOH H 7 .   ? 2.433  -5.796  -33.265 1.00 34.41 ? 729  HOH A O     1 
HETATM 2919 O  O     . HOH H 7 .   ? 14.491 -26.084 5.888   1.00 27.32 ? 730  HOH A O     1 
HETATM 2920 O  O     . HOH H 7 .   ? 11.704 -14.097 -15.899 1.00 19.19 ? 731  HOH A O     1 
HETATM 2921 O  O     . HOH H 7 .   ? 6.445  -5.171  -0.251  1.00 21.47 ? 732  HOH A O     1 
HETATM 2922 O  O     . HOH H 7 .   ? 3.178  -3.165  -21.866 1.00 26.34 ? 733  HOH A O     1 
HETATM 2923 O  O     . HOH H 7 .   ? 18.511 -9.862  -29.132 1.00 20.24 ? 734  HOH A O     1 
HETATM 2924 O  O     . HOH H 7 .   ? 35.753 -13.148 -30.860 1.00 42.02 ? 735  HOH A O     1 
HETATM 2925 O  O     . HOH H 7 .   ? 39.159 -7.958  -1.921  1.00 29.36 ? 736  HOH A O     1 
HETATM 2926 O  O     . HOH H 7 .   ? 20.830 -12.563 -43.712 1.00 36.05 ? 737  HOH A O     1 
HETATM 2927 O  O     . HOH H 7 .   ? 13.335 -29.569 -3.525  1.00 26.20 ? 738  HOH A O     1 
HETATM 2928 O  O     . HOH H 7 .   ? 4.147  -4.318  -19.653 1.00 23.29 ? 739  HOH A O     1 
HETATM 2929 O  O     . HOH H 7 .   ? 6.910  -20.453 -23.276 1.00 33.84 ? 740  HOH A O     1 
HETATM 2930 O  O     . HOH H 7 .   ? 21.557 -7.665  10.845  1.00 32.57 ? 741  HOH A O     1 
HETATM 2931 O  O     . HOH H 7 .   ? 29.695 -1.481  -28.487 1.00 38.24 ? 742  HOH A O     1 
HETATM 2932 O  O     . HOH H 7 .   ? 22.304 5.065   3.558   1.00 35.05 ? 743  HOH A O     1 
HETATM 2933 O  O     . HOH H 7 .   ? 28.746 -1.757  3.465   1.00 28.12 ? 744  HOH A O     1 
HETATM 2934 O  O     . HOH H 7 .   ? 18.916 -25.776 -5.054  1.00 30.10 ? 745  HOH A O     1 
HETATM 2935 O  O     . HOH H 7 .   ? 27.346 2.664   10.319  1.00 37.53 ? 746  HOH A O     1 
HETATM 2936 O  O     . HOH H 7 .   ? -4.181 -15.352 -8.020  1.00 28.16 ? 747  HOH A O     1 
HETATM 2937 O  O     . HOH H 7 .   ? 3.725  -28.606 -18.891 1.00 31.08 ? 748  HOH A O     1 
HETATM 2938 O  O     . HOH H 7 .   ? 21.636 -25.056 -0.684  1.00 34.14 ? 749  HOH A O     1 
HETATM 2939 O  O     . HOH H 7 .   ? 6.780  -8.014  -2.483  1.00 23.12 ? 750  HOH A O     1 
HETATM 2940 O  O     . HOH H 7 .   ? 28.727 -27.411 -7.689  1.00 35.91 ? 751  HOH A O     1 
HETATM 2941 O  O     . HOH H 7 .   ? 12.799 -31.738 -20.482 1.00 24.82 ? 752  HOH A O     1 
HETATM 2942 O  O     . HOH H 7 .   ? 16.835 0.900   -6.421  1.00 36.37 ? 753  HOH A O     1 
HETATM 2943 O  O     . HOH H 7 .   ? 9.199  4.096   3.902   1.00 29.73 ? 754  HOH A O     1 
HETATM 2944 O  O     . HOH H 7 .   ? 9.422  -34.799 -11.067 1.00 25.54 ? 755  HOH A O     1 
HETATM 2945 O  O     . HOH H 7 .   ? 20.130 -31.795 -29.290 1.00 40.74 ? 756  HOH A O     1 
HETATM 2946 O  O     . HOH H 7 .   ? 13.351 -5.988  -15.138 1.00 12.94 ? 757  HOH A O     1 
HETATM 2947 O  O     . HOH H 7 .   ? 36.521 -10.853 -11.685 1.00 40.44 ? 758  HOH A O     1 
HETATM 2948 O  O     . HOH H 7 .   ? 21.209 -6.307  -21.790 1.00 24.87 ? 759  HOH A O     1 
HETATM 2949 O  O     . HOH H 7 .   ? 5.526  -6.551  -6.350  1.00 26.95 ? 760  HOH A O     1 
HETATM 2950 O  O     . HOH H 7 .   ? 24.023 -18.202 -15.244 1.00 21.19 ? 761  HOH A O     1 
HETATM 2951 O  O     . HOH H 7 .   ? 7.100  -9.521  -46.151 1.00 32.70 ? 762  HOH A O     1 
HETATM 2952 O  O     . HOH H 7 .   ? 30.955 -26.243 -11.875 1.00 24.04 ? 763  HOH A O     1 
HETATM 2953 O  O     . HOH H 7 .   ? 26.667 1.836   4.389   1.00 30.60 ? 764  HOH A O     1 
HETATM 2954 O  O     . HOH H 7 .   ? 11.264 -7.245  -16.850 1.00 13.19 ? 765  HOH A O     1 
HETATM 2955 O  O     . HOH H 7 .   ? 7.587  -5.235  -9.083  1.00 17.96 ? 766  HOH A O     1 
HETATM 2956 O  O     . HOH H 7 .   ? 30.650 -14.596 5.815   1.00 37.63 ? 767  HOH A O     1 
HETATM 2957 O  O     . HOH H 7 .   ? 3.412  9.047   -15.377 1.00 35.12 ? 768  HOH A O     1 
HETATM 2958 O  O     . HOH H 7 .   ? 27.311 -11.185 -31.670 1.00 28.64 ? 769  HOH A O     1 
HETATM 2959 O  O     . HOH H 7 .   ? 19.829 -6.075  -13.623 1.00 22.50 ? 770  HOH A O     1 
HETATM 2960 O  O     . HOH H 7 .   ? 29.513 -17.277 -19.109 1.00 26.06 ? 771  HOH A O     1 
HETATM 2961 O  O     . HOH H 7 .   ? 35.423 -15.517 -1.665  1.00 25.43 ? 772  HOH A O     1 
HETATM 2962 O  O     . HOH H 7 .   ? 23.499 -5.426  -36.872 1.00 25.91 ? 773  HOH A O     1 
HETATM 2963 O  O     . HOH H 7 .   ? 7.620  -19.188 -34.038 1.00 41.77 ? 774  HOH A O     1 
HETATM 2964 O  O     . HOH H 7 .   ? 5.410  -4.108  1.979   1.00 25.53 ? 775  HOH A O     1 
HETATM 2965 O  O     . HOH H 7 .   ? 23.101 -10.440 -15.193 1.00 24.16 ? 776  HOH A O     1 
HETATM 2966 O  O     . HOH H 7 .   ? 2.966  -11.517 0.491   1.00 26.00 ? 777  HOH A O     1 
HETATM 2967 O  O     . HOH H 7 .   ? 13.380 8.043   -31.544 1.00 44.03 ? 778  HOH A O     1 
HETATM 2968 O  O     . HOH H 7 .   ? 3.616  -11.001 -15.395 1.00 24.38 ? 779  HOH A O     1 
HETATM 2969 O  O     . HOH H 7 .   ? 17.673 -19.289 -16.927 1.00 21.28 ? 780  HOH A O     1 
HETATM 2970 O  O     . HOH H 7 .   ? 25.037 -29.091 -15.254 1.00 20.80 ? 781  HOH A O     1 
HETATM 2971 O  O     . HOH H 7 .   ? 21.548 -20.064 -18.355 1.00 27.77 ? 782  HOH A O     1 
HETATM 2972 O  O     . HOH H 7 .   ? 34.435 -14.051 0.411   1.00 24.03 ? 783  HOH A O     1 
HETATM 2973 O  O     . HOH H 7 .   ? 17.533 -3.499  -14.352 1.00 25.54 ? 784  HOH A O     1 
HETATM 2974 O  O     . HOH H 7 .   ? 14.729 -3.578  -10.013 1.00 17.45 ? 785  HOH A O     1 
HETATM 2975 O  O     . HOH H 7 .   ? 31.252 -14.430 2.813   1.00 25.27 ? 786  HOH A O     1 
HETATM 2976 O  O     . HOH H 7 .   ? 6.522  -18.399 -18.041 1.00 30.21 ? 787  HOH A O     1 
HETATM 2977 O  O     . HOH H 7 .   ? 22.366 -4.965  -25.095 1.00 30.49 ? 788  HOH A O     1 
HETATM 2978 O  O     . HOH H 7 .   ? 16.364 4.368   -3.330  1.00 40.73 ? 789  HOH A O     1 
HETATM 2979 O  O     . HOH H 7 .   ? 23.786 -30.637 -22.146 1.00 25.45 ? 790  HOH A O     1 
HETATM 2980 O  O     . HOH H 7 .   ? 1.077  -16.710 10.862  1.00 48.27 ? 791  HOH A O     1 
HETATM 2981 O  O     . HOH H 7 .   ? 29.149 -13.377 -23.920 1.00 27.89 ? 792  HOH A O     1 
HETATM 2982 O  O     . HOH H 7 .   ? -3.079 -3.060  -4.447  1.00 27.69 ? 793  HOH A O     1 
HETATM 2983 O  O     . HOH H 7 .   ? 8.872  -17.750 8.976   1.00 21.30 ? 794  HOH A O     1 
HETATM 2984 O  O     . HOH H 7 .   ? 15.120 -12.841 -45.382 1.00 35.07 ? 795  HOH A O     1 
HETATM 2985 O  O     . HOH H 7 .   ? 15.574 -34.789 -14.382 1.00 34.38 ? 796  HOH A O     1 
HETATM 2986 O  O     . HOH H 7 .   ? 10.282 -2.086  -15.141 1.00 13.94 ? 797  HOH A O     1 
HETATM 2987 O  O     . HOH H 7 .   ? 8.542  -3.122  -5.847  1.00 19.48 ? 798  HOH A O     1 
HETATM 2988 O  O     . HOH H 7 .   ? 36.301 -10.319 2.965   1.00 30.34 ? 799  HOH A O     1 
HETATM 2989 O  O     . HOH H 7 .   ? 3.997  -7.627  -14.495 1.00 29.04 ? 800  HOH A O     1 
HETATM 2990 O  O     . HOH H 7 .   ? 23.553 -11.273 -40.537 1.00 30.61 ? 801  HOH A O     1 
HETATM 2991 O  O     . HOH H 7 .   ? 34.483 -8.179  7.378   1.00 39.39 ? 802  HOH A O     1 
HETATM 2992 O  O     . HOH H 7 .   ? 28.502 -14.990 -12.840 1.00 19.94 ? 803  HOH A O     1 
HETATM 2993 O  O     . HOH H 7 .   ? -0.143 -18.922 -5.098  1.00 19.52 ? 804  HOH A O     1 
HETATM 2994 O  O     . HOH H 7 .   ? 25.210 -22.497 -33.366 1.00 22.59 ? 805  HOH A O     1 
HETATM 2995 O  O     . HOH H 7 .   ? 21.743 -25.972 -9.031  1.00 21.63 ? 806  HOH A O     1 
HETATM 2996 O  O     . HOH H 7 .   ? 40.354 -15.377 -8.598  1.00 34.73 ? 807  HOH A O     1 
HETATM 2997 O  O     . HOH H 7 .   ? -4.151 -27.670 -8.519  1.00 16.85 ? 808  HOH A O     1 
HETATM 2998 O  O     . HOH H 7 .   ? 3.408  -10.853 -6.878  1.00 25.15 ? 809  HOH A O     1 
HETATM 2999 O  O     . HOH H 7 .   ? 13.748 3.455   -4.181  1.00 33.66 ? 810  HOH A O     1 
HETATM 3000 O  O     . HOH H 7 .   ? 38.035 -21.890 -4.496  1.00 35.23 ? 811  HOH A O     1 
HETATM 3001 O  O     . HOH H 7 .   ? 39.981 -15.297 -11.113 1.00 37.55 ? 812  HOH A O     1 
HETATM 3002 O  O     . HOH H 7 .   ? 2.056  5.783   -21.579 1.00 28.88 ? 813  HOH A O     1 
HETATM 3003 O  O     . HOH H 7 .   ? 18.197 -11.221 -12.234 1.00 18.42 ? 814  HOH A O     1 
HETATM 3004 O  O     . HOH H 7 .   ? 17.959 -16.843 -18.140 1.00 21.25 ? 815  HOH A O     1 
HETATM 3005 O  O     . HOH H 7 .   ? 27.184 -7.516  -37.921 1.00 48.45 ? 816  HOH A O     1 
HETATM 3006 O  O     . HOH H 7 .   ? -0.113 -5.301  -24.353 1.00 41.64 ? 817  HOH A O     1 
HETATM 3007 O  O     . HOH H 7 .   ? 14.817 5.994   -15.431 1.00 34.52 ? 818  HOH A O     1 
HETATM 3008 O  O     . HOH H 7 .   ? 25.704 -11.234 -27.738 1.00 26.61 ? 819  HOH A O     1 
HETATM 3009 O  O     . HOH H 7 .   ? 12.064 -11.381 -47.703 1.00 23.34 ? 820  HOH A O     1 
HETATM 3010 O  O     . HOH H 7 .   ? 31.044 -30.548 -11.004 1.00 36.65 ? 821  HOH A O     1 
HETATM 3011 O  O     . HOH H 7 .   ? 26.000 -10.124 -33.933 1.00 27.32 ? 822  HOH A O     1 
HETATM 3012 O  O     . HOH H 7 .   ? 4.583  -16.345 -20.191 1.00 37.53 ? 823  HOH A O     1 
HETATM 3013 O  O     . HOH H 7 .   ? 20.253 -19.576 -11.852 1.00 16.10 ? 824  HOH A O     1 
HETATM 3014 O  O     . HOH H 7 .   ? 6.155  -6.231  -22.938 1.00 22.18 ? 825  HOH A O     1 
HETATM 3015 O  O     . HOH H 7 .   ? 28.862 -25.992 -10.076 1.00 22.29 ? 826  HOH A O     1 
HETATM 3016 O  O     . HOH H 7 .   ? -1.046 -22.128 -7.295  1.00 19.41 ? 827  HOH A O     1 
HETATM 3017 O  O     . HOH H 7 .   ? 28.060 -3.640  -13.258 1.00 37.31 ? 828  HOH A O     1 
HETATM 3018 O  O     . HOH H 7 .   ? 6.338  -19.976 11.271  1.00 34.78 ? 829  HOH A O     1 
HETATM 3019 O  O     . HOH H 7 .   ? 3.203  -33.641 -13.657 1.00 28.49 ? 830  HOH A O     1 
HETATM 3020 O  O     . HOH H 7 .   ? 17.525 -33.298 -19.406 1.00 33.47 ? 831  HOH A O     1 
HETATM 3021 O  O     . HOH H 7 .   ? 5.683  3.994   -4.637  1.00 30.21 ? 832  HOH A O     1 
HETATM 3022 O  O     . HOH H 7 .   ? 9.003  -33.776 -17.603 1.00 24.01 ? 833  HOH A O     1 
HETATM 3023 O  O     . HOH H 7 .   ? 2.545  -5.850  -26.102 1.00 38.51 ? 834  HOH A O     1 
HETATM 3024 O  O     . HOH H 7 .   ? 21.646 -32.949 -24.131 1.00 34.16 ? 835  HOH A O     1 
HETATM 3025 O  O     . HOH H 7 .   ? 16.469 -9.924  -9.879  1.00 22.66 ? 836  HOH A O     1 
HETATM 3026 O  O     . HOH H 7 .   ? 20.230 -19.454 5.092   1.00 27.07 ? 837  HOH A O     1 
HETATM 3027 O  O     . HOH H 7 .   ? 22.461 -31.682 -14.314 1.00 24.31 ? 838  HOH A O     1 
HETATM 3028 O  O     . HOH H 7 .   ? 13.357 -18.291 5.009   1.00 21.03 ? 839  HOH A O     1 
HETATM 3029 O  O     . HOH H 7 .   ? 19.302 -25.245 -1.501  1.00 28.25 ? 840  HOH A O     1 
HETATM 3030 O  O     . HOH H 7 .   ? 2.468  -6.142  -9.066  1.00 25.99 ? 841  HOH A O     1 
HETATM 3031 O  O     . HOH H 7 .   ? 32.978 -6.195  7.216   1.00 29.51 ? 842  HOH A O     1 
HETATM 3032 O  O     . HOH H 7 .   ? 12.676 -34.224 -27.192 1.00 38.04 ? 843  HOH A O     1 
HETATM 3033 O  O     . HOH H 7 .   ? 11.009 -33.885 -13.118 1.00 23.86 ? 844  HOH A O     1 
HETATM 3034 O  O     . HOH H 7 .   ? 8.079  -28.503 -25.062 1.00 29.04 ? 845  HOH A O     1 
HETATM 3035 O  O     . HOH H 7 .   ? 31.632 -29.864 -25.194 1.00 35.87 ? 846  HOH A O     1 
HETATM 3036 O  O     . HOH H 7 .   ? 11.409 -27.225 5.958   1.00 29.14 ? 847  HOH A O     1 
HETATM 3037 O  O     . HOH H 7 .   ? 6.710  -7.859  8.637   1.00 28.78 ? 848  HOH A O     1 
HETATM 3038 O  O     . HOH H 7 .   ? 34.744 -22.384 -6.976  1.00 29.20 ? 849  HOH A O     1 
HETATM 3039 O  O     . HOH H 7 .   ? 36.044 -6.541  -11.941 1.00 42.69 ? 850  HOH A O     1 
HETATM 3040 O  O     . HOH H 7 .   ? 6.827  -31.298 -24.190 1.00 38.65 ? 851  HOH A O     1 
HETATM 3041 O  O     . HOH H 7 .   ? 6.646  -10.845 -0.206  1.00 17.90 ? 852  HOH A O     1 
HETATM 3042 O  O     . HOH H 7 .   ? 18.298 -2.822  -19.790 1.00 28.03 ? 853  HOH A O     1 
HETATM 3043 O  O     . HOH H 7 .   ? 27.091 -17.084 6.033   1.00 32.31 ? 854  HOH A O     1 
HETATM 3044 O  O     . HOH H 7 .   ? -0.333 3.904   -20.835 1.00 27.41 ? 855  HOH A O     1 
HETATM 3045 O  O     . HOH H 7 .   ? 0.308  -36.677 -5.417  1.00 28.96 ? 856  HOH A O     1 
HETATM 3046 O  O     . HOH H 7 .   ? 10.302 -21.915 -0.443  1.00 14.44 ? 857  HOH A O     1 
HETATM 3047 O  O     . HOH H 7 .   ? 17.642 -20.670 6.385   1.00 33.12 ? 858  HOH A O     1 
HETATM 3048 O  O     . HOH H 7 .   ? 26.773 -31.987 -26.757 1.00 36.39 ? 859  HOH A O     1 
HETATM 3049 O  O     . HOH H 7 .   ? 2.641  -13.589 -26.283 1.00 41.08 ? 860  HOH A O     1 
HETATM 3050 O  O     . HOH H 7 .   ? 35.252 -23.812 -1.853  1.00 33.83 ? 861  HOH A O     1 
HETATM 3051 O  O     . HOH H 7 .   ? 23.296 -0.003  -8.798  1.00 25.59 ? 862  HOH A O     1 
HETATM 3052 O  O     . HOH H 7 .   ? 17.440 -8.789  8.887   1.00 21.73 ? 863  HOH A O     1 
HETATM 3053 O  O     . HOH H 7 .   ? 20.567 -9.589  -13.551 1.00 21.44 ? 864  HOH A O     1 
HETATM 3054 O  O     . HOH H 7 .   ? 4.090  -25.067 3.634   1.00 24.49 ? 865  HOH A O     1 
HETATM 3055 O  O     . HOH H 7 .   ? 1.519  -11.902 -13.465 1.00 29.73 ? 866  HOH A O     1 
HETATM 3056 O  O     . HOH H 7 .   ? 6.148  7.826   -15.120 1.00 38.77 ? 867  HOH A O     1 
HETATM 3057 O  O     . HOH H 7 .   ? 10.390 -30.029 -23.295 1.00 29.86 ? 868  HOH A O     1 
HETATM 3058 O  O     . HOH H 7 .   ? 22.013 -3.074  -27.357 1.00 21.73 ? 869  HOH A O     1 
HETATM 3059 O  O     . HOH H 7 .   ? 22.020 -6.157  -11.872 1.00 20.68 ? 870  HOH A O     1 
HETATM 3060 O  O     . HOH H 7 .   ? 1.823  -21.240 -12.628 1.00 37.36 ? 871  HOH A O     1 
HETATM 3061 O  O     . HOH H 7 .   ? 2.745  -14.791 6.328   1.00 26.74 ? 872  HOH A O     1 
HETATM 3062 O  O     . HOH H 7 .   ? 3.786  -10.404 3.506   1.00 26.20 ? 873  HOH A O     1 
HETATM 3063 O  O     . HOH H 7 .   ? 11.423 -35.250 -9.156  1.00 35.13 ? 874  HOH A O     1 
HETATM 3064 O  O     . HOH H 7 .   ? 7.702  3.909   -9.170  1.00 18.62 ? 875  HOH A O     1 
HETATM 3065 O  O     . HOH H 7 .   ? 4.658  -13.377 -21.808 1.00 25.35 ? 876  HOH A O     1 
HETATM 3066 O  O     . HOH H 7 .   ? 17.279 -18.184 -45.650 1.00 40.03 ? 877  HOH A O     1 
HETATM 3067 O  O     . HOH H 7 .   ? 7.754  -31.405 0.832   1.00 29.45 ? 878  HOH A O     1 
HETATM 3068 O  O     . HOH H 7 .   ? 8.076  -3.473  -2.049  1.00 19.53 ? 879  HOH A O     1 
HETATM 3069 O  O     . HOH H 7 .   ? 10.159 -29.429 4.878   1.00 35.63 ? 880  HOH A O     1 
HETATM 3070 O  O     . HOH H 7 .   ? 33.669 -27.526 -28.291 1.00 32.66 ? 881  HOH A O     1 
HETATM 3071 O  O     . HOH H 7 .   ? 20.171 -15.849 -0.794  1.00 23.34 ? 882  HOH A O     1 
HETATM 3072 O  O     . HOH H 7 .   ? 13.525 -28.031 -31.550 1.00 36.34 ? 883  HOH A O     1 
HETATM 3073 O  O     . HOH H 7 .   ? -7.559 -18.040 -0.778  1.00 26.42 ? 884  HOH A O     1 
HETATM 3074 O  O     . HOH H 7 .   ? 18.014 -26.404 -8.458  1.00 19.19 ? 885  HOH A O     1 
HETATM 3075 O  O     . HOH H 7 .   ? 1.900  -20.817 -4.768  1.00 14.66 ? 886  HOH A O     1 
HETATM 3076 O  O     . HOH H 7 .   ? 26.297 -31.672 -20.635 1.00 36.47 ? 887  HOH A O     1 
HETATM 3077 O  O     . HOH H 7 .   ? 10.957 -8.656  11.114  1.00 30.93 ? 888  HOH A O     1 
HETATM 3078 O  O     . HOH H 7 .   ? 31.157 -23.126 -14.172 1.00 22.99 ? 889  HOH A O     1 
HETATM 3079 O  O     . HOH H 7 .   ? -9.041 -14.451 3.564   1.00 41.72 ? 890  HOH A O     1 
HETATM 3080 O  O     . HOH H 7 .   ? 3.306  -18.753 -12.491 1.00 25.59 ? 891  HOH A O     1 
HETATM 3081 O  O     . HOH H 7 .   ? 20.284 -5.891  -7.735  1.00 21.97 ? 892  HOH A O     1 
HETATM 3082 O  O     . HOH H 7 .   ? 5.314  3.901   -27.164 1.00 31.43 ? 893  HOH A O     1 
HETATM 3083 O  O     . HOH H 7 .   ? 41.466 -12.559 -7.079  1.00 35.45 ? 894  HOH A O     1 
HETATM 3084 O  O     . HOH H 7 .   ? 0.842  3.862   -6.211  1.00 22.75 ? 895  HOH A O     1 
HETATM 3085 O  O     . HOH H 7 .   ? 5.622  -2.541  -6.145  1.00 19.26 ? 896  HOH A O     1 
HETATM 3086 O  O     . HOH H 7 .   ? 33.944 -20.614 -22.759 1.00 39.77 ? 897  HOH A O     1 
HETATM 3087 O  O     . HOH H 7 .   ? 28.136 -23.309 -0.808  1.00 32.60 ? 898  HOH A O     1 
HETATM 3088 O  O     . HOH H 7 .   ? 5.133  -26.055 7.948   1.00 38.29 ? 899  HOH A O     1 
HETATM 3089 O  O     . HOH H 7 .   ? 6.007  -13.277 -1.486  1.00 16.78 ? 900  HOH A O     1 
HETATM 3090 O  O     . HOH H 7 .   ? -8.808 -14.054 -0.803  1.00 38.61 ? 901  HOH A O     1 
HETATM 3091 O  O     . HOH H 7 .   ? 3.585  -17.726 5.089   1.00 23.96 ? 902  HOH A O     1 
HETATM 3092 O  O     . HOH H 7 .   ? 19.993 5.158   -31.439 1.00 32.93 ? 903  HOH A O     1 
HETATM 3093 O  O     . HOH H 7 .   ? 25.294 3.163   -25.610 1.00 37.59 ? 904  HOH A O     1 
HETATM 3094 O  O     . HOH H 7 .   ? 15.817 0.463   -9.415  1.00 39.81 ? 905  HOH A O     1 
HETATM 3095 O  O     . HOH H 7 .   ? 33.863 -17.072 -33.657 1.00 32.70 ? 906  HOH A O     1 
HETATM 3096 O  O     . HOH H 7 .   ? 13.980 -19.273 9.431   1.00 38.70 ? 907  HOH A O     1 
HETATM 3097 O  O     . HOH H 7 .   ? 3.794  -24.044 5.857   1.00 27.07 ? 908  HOH A O     1 
HETATM 3098 O  O     . HOH H 7 .   ? 3.316  -12.048 -29.685 1.00 31.41 ? 909  HOH A O     1 
HETATM 3099 O  O     . HOH H 7 .   ? 5.607  -22.691 -10.079 1.00 19.29 ? 910  HOH A O     1 
HETATM 3100 O  O     . HOH H 7 .   ? 13.083 -10.785 -45.579 1.00 29.34 ? 911  HOH A O     1 
HETATM 3101 O  O     . HOH H 7 .   ? 32.201 -18.485 -21.547 1.00 40.13 ? 912  HOH A O     1 
HETATM 3102 O  O     . HOH H 7 .   ? 6.809  5.524   -16.007 1.00 33.18 ? 913  HOH A O     1 
HETATM 3103 O  O     . HOH H 7 .   ? 33.730 -15.198 4.516   1.00 33.01 ? 914  HOH A O     1 
HETATM 3104 O  O     . HOH H 7 .   ? 19.368 -13.656 -2.348  1.00 26.38 ? 915  HOH A O     1 
HETATM 3105 O  O     . HOH H 7 .   ? 2.797  -11.000 -19.514 1.00 30.58 ? 916  HOH A O     1 
HETATM 3106 O  O     . HOH H 7 .   ? -2.589 -34.600 -5.714  1.00 19.33 ? 917  HOH A O     1 
HETATM 3107 O  O     . HOH H 7 .   ? 3.433  2.008   -31.954 1.00 40.62 ? 918  HOH A O     1 
HETATM 3108 O  O     . HOH H 7 .   ? 0.322  6.522   -8.400  1.00 22.69 ? 919  HOH A O     1 
HETATM 3109 O  O     . HOH H 7 .   ? 31.128 -2.853  12.075  1.00 29.17 ? 920  HOH A O     1 
HETATM 3110 O  O     . HOH H 7 .   ? 25.341 -12.648 -18.279 1.00 21.99 ? 921  HOH A O     1 
HETATM 3111 O  O     . HOH H 7 .   ? 9.037  4.452   -15.585 1.00 33.71 ? 922  HOH A O     1 
HETATM 3112 O  O     . HOH H 7 .   ? 3.573  -15.993 -14.606 1.00 28.80 ? 923  HOH A O     1 
HETATM 3113 O  O     . HOH H 7 .   ? 30.172 1.415   11.960  1.00 30.73 ? 924  HOH A O     1 
HETATM 3114 O  O     . HOH H 7 .   ? 5.247  -5.719  8.799   1.00 39.68 ? 925  HOH A O     1 
HETATM 3115 O  O     . HOH H 7 .   ? 2.386  0.050   -31.512 1.00 36.65 ? 926  HOH A O     1 
HETATM 3116 O  O     . HOH H 7 .   ? 16.351 -32.075 -9.542  1.00 35.57 ? 927  HOH A O     1 
HETATM 3117 O  O     . HOH H 7 .   ? 27.869 -12.370 -26.599 1.00 23.81 ? 928  HOH A O     1 
HETATM 3118 O  O     . HOH H 7 .   ? 20.488 -3.361  -20.224 1.00 37.43 ? 929  HOH A O     1 
HETATM 3119 O  O     . HOH H 7 .   ? 30.956 -22.750 -17.645 1.00 39.71 ? 930  HOH A O     1 
HETATM 3120 O  O     . HOH H 7 .   ? -0.599 -24.100 -9.126  1.00 20.61 ? 931  HOH A O     1 
HETATM 3121 O  O     . HOH H 7 .   ? 36.616 -21.192 -8.350  1.00 31.84 ? 932  HOH A O     1 
HETATM 3122 O  O     . HOH H 7 .   ? 3.589  -12.288 -17.890 1.00 30.22 ? 933  HOH A O     1 
HETATM 3123 O  O     . HOH H 7 .   ? 2.677  -7.330  -22.752 1.00 33.02 ? 934  HOH A O     1 
HETATM 3124 O  O     . HOH H 7 .   ? 9.257  5.756   -2.867  1.00 36.37 ? 935  HOH A O     1 
HETATM 3125 O  O     . HOH H 7 .   ? 19.730 -21.000 -16.648 1.00 27.48 ? 936  HOH A O     1 
HETATM 3126 O  O     . HOH H 7 .   ? 29.144 -1.938  -9.640  1.00 34.16 ? 937  HOH A O     1 
HETATM 3127 O  O     . HOH H 7 .   ? 26.667 -6.380  -13.693 1.00 34.86 ? 938  HOH A O     1 
HETATM 3128 O  O     . HOH H 7 .   ? 26.879 -0.860  -31.283 1.00 33.24 ? 939  HOH A O     1 
HETATM 3129 O  O     . HOH H 7 .   ? 2.012  -18.300 2.910   1.00 19.14 ? 940  HOH A O     1 
HETATM 3130 O  O     . HOH H 7 .   ? 30.626 -24.793 -16.461 1.00 33.36 ? 941  HOH A O     1 
HETATM 3131 O  O     . HOH H 7 .   ? 25.990 -22.707 -2.742  1.00 32.40 ? 942  HOH A O     1 
HETATM 3132 O  O     . HOH H 7 .   ? 20.179 -27.950 -8.780  1.00 25.42 ? 943  HOH A O     1 
HETATM 3133 O  O     . HOH H 7 .   ? 0.699  -17.831 -11.760 1.00 32.65 ? 944  HOH A O     1 
HETATM 3134 O  O     . HOH H 7 .   ? 1.225  -13.927 -9.334  1.00 34.13 ? 945  HOH A O     1 
HETATM 3135 O  O     . HOH H 7 .   ? 27.186 -25.760 -4.494  1.00 31.57 ? 946  HOH A O     1 
HETATM 3136 O  O     . HOH H 7 .   ? 13.078 6.093   -13.616 1.00 39.78 ? 947  HOH A O     1 
HETATM 3137 O  O     . HOH H 7 .   ? 26.594 -16.170 -14.844 1.00 22.86 ? 948  HOH A O     1 
HETATM 3138 O  O     . HOH H 7 .   ? 17.062 3.104   -8.876  1.00 45.16 ? 949  HOH A O     1 
HETATM 3139 O  O     . HOH H 7 .   ? 3.463  -33.263 -16.593 1.00 36.84 ? 950  HOH A O     1 
HETATM 3140 O  O     . HOH H 7 .   ? 4.584  -5.522  -2.351  1.00 33.13 ? 951  HOH A O     1 
HETATM 3141 O  O     . HOH H 7 .   ? 3.831  -22.598 -12.402 1.00 32.59 ? 952  HOH A O     1 
HETATM 3142 O  O     . HOH H 7 .   ? -3.749 3.708   -4.293  1.00 29.33 ? 953  HOH A O     1 
HETATM 3143 O  O     . HOH H 7 .   ? 2.943  -14.508 -6.727  1.00 24.33 ? 954  HOH A O     1 
HETATM 3144 O  O     . HOH H 7 .   ? 24.668 -7.881  -33.540 1.00 33.02 ? 955  HOH A O     1 
HETATM 3145 O  O     . HOH H 7 .   ? 1.740  -25.412 -9.484  1.00 19.48 ? 956  HOH A O     1 
HETATM 3146 O  O     . HOH H 7 .   ? 26.207 -32.360 -18.481 1.00 36.94 ? 957  HOH A O     1 
HETATM 3147 O  O     . HOH H 7 .   ? 2.258  -1.165  -33.867 1.00 39.04 ? 958  HOH A O     1 
HETATM 3148 O  O     . HOH H 7 .   ? 24.540 -23.024 -4.502  1.00 23.55 ? 959  HOH A O     1 
HETATM 3149 O  O     . HOH H 7 .   ? 25.235 -31.983 -10.823 1.00 39.98 ? 960  HOH A O     1 
HETATM 3150 O  O     . HOH H 7 .   ? 5.092  -36.459 -10.788 1.00 32.86 ? 961  HOH A O     1 
HETATM 3151 O  O     . HOH H 7 .   ? 25.522 -5.990  -35.137 1.00 30.24 ? 962  HOH A O     1 
HETATM 3152 O  O     . HOH H 7 .   ? 35.100 0.191   2.077   1.00 39.76 ? 963  HOH A O     1 
HETATM 3153 O  O     . HOH H 7 .   ? 38.132 -6.935  0.576   1.00 30.38 ? 964  HOH A O     1 
HETATM 3154 O  O     . HOH H 7 .   ? 22.646 -2.763  -36.619 1.00 30.58 ? 965  HOH A O     1 
HETATM 3155 O  O     . HOH H 7 .   ? -2.168 -2.906  -1.954  1.00 40.45 ? 966  HOH A O     1 
HETATM 3156 O  O     . HOH H 7 .   ? 18.439 -27.542 -0.474  1.00 37.63 ? 967  HOH A O     1 
HETATM 3157 O  O     . HOH H 7 .   ? 1.078  -14.621 -13.350 1.00 37.30 ? 968  HOH A O     1 
HETATM 3158 O  O     . HOH H 7 .   ? 22.280 -4.966  -9.212  1.00 24.54 ? 969  HOH A O     1 
HETATM 3159 O  O     . HOH H 7 .   ? 2.318  -25.061 -12.145 1.00 36.44 ? 970  HOH A O     1 
HETATM 3160 O  O     . HOH H 7 .   ? 15.824 9.944   -26.839 1.00 44.82 ? 971  HOH A O     1 
HETATM 3161 O  O     . HOH H 7 .   ? 10.880 -34.569 -15.907 1.00 31.08 ? 972  HOH A O     1 
HETATM 3162 O  O     . HOH H 7 .   ? 38.403 -8.710  2.705   1.00 40.85 ? 973  HOH A O     1 
HETATM 3163 O  O     . HOH H 7 .   ? 4.424  3.277   -34.087 1.00 39.95 ? 974  HOH A O     1 
HETATM 3164 O  O     . HOH H 7 .   ? 4.227  -23.376 -22.178 1.00 39.15 ? 975  HOH A O     1 
HETATM 3165 O  O     . HOH H 7 .   ? 9.108  -6.909  9.967   1.00 31.62 ? 976  HOH A O     1 
HETATM 3166 O  O     . HOH H 7 .   ? 24.121 -5.364  -13.262 1.00 31.70 ? 977  HOH A O     1 
HETATM 3167 O  O     . HOH H 7 .   ? 11.189 -36.354 -6.695  1.00 46.88 ? 978  HOH A O     1 
HETATM 3168 O  O     . HOH H 7 .   ? 23.977 -32.075 -24.206 1.00 38.58 ? 979  HOH A O     1 
HETATM 3169 O  O     . HOH H 7 .   ? 4.009  -5.027  -23.955 1.00 30.55 ? 980  HOH A O     1 
HETATM 3170 O  O     . HOH H 7 .   ? 16.484 -4.130  10.336  1.00 39.84 ? 981  HOH A O     1 
HETATM 3171 O  O     . HOH H 7 .   ? 2.346  -12.602 -5.146  1.00 29.96 ? 982  HOH A O     1 
HETATM 3172 O  O     . HOH H 7 .   ? -1.735 8.071   -18.377 1.00 38.45 ? 983  HOH A O     1 
HETATM 3173 O  O     . HOH H 7 .   ? 35.561 -14.910 2.685   1.00 34.64 ? 984  HOH A O     1 
HETATM 3174 O  O     . HOH H 7 .   ? 24.022 -2.573  -12.555 1.00 39.76 ? 985  HOH A O     1 
HETATM 3175 O  O     . HOH H 7 .   ? -9.320 -16.062 -4.130  1.00 34.67 ? 986  HOH A O     1 
HETATM 3176 O  O     . HOH H 7 .   ? 27.872 -14.832 7.783   1.00 42.86 ? 987  HOH A O     1 
HETATM 3177 O  O     . HOH H 7 .   ? 4.052  -12.127 -3.123  1.00 24.25 ? 988  HOH A O     1 
HETATM 3178 O  O     . HOH H 7 .   ? 17.336 -6.513  10.402  1.00 42.05 ? 989  HOH A O     1 
HETATM 3179 O  O     . HOH H 7 .   ? -2.625 5.543   -6.038  1.00 36.90 ? 990  HOH A O     1 
HETATM 3180 O  O     . HOH H 7 .   ? 6.422  -21.899 -21.461 1.00 30.65 ? 991  HOH A O     1 
HETATM 3181 O  O     . HOH H 7 .   ? 31.168 -19.048 -18.954 1.00 39.76 ? 992  HOH A O     1 
HETATM 3182 O  O     . HOH H 7 .   ? 36.647 -12.956 2.988   1.00 39.55 ? 993  HOH A O     1 
HETATM 3183 O  O     . HOH H 7 .   ? 2.369  -31.217 -18.086 1.00 39.67 ? 994  HOH A O     1 
HETATM 3184 O  O     . HOH H 7 .   ? 22.663 -2.297  -10.064 1.00 27.94 ? 995  HOH A O     1 
HETATM 3185 O  O     . HOH H 7 .   ? 4.497  -9.548  -3.001  1.00 29.10 ? 996  HOH A O     1 
HETATM 3186 O  O     . HOH H 7 .   ? 2.811  -9.421  -0.905  1.00 42.02 ? 997  HOH A O     1 
HETATM 3187 O  O     . HOH H 7 .   ? 2.891  -36.216 -12.442 1.00 36.00 ? 998  HOH A O     1 
HETATM 3188 O  O     . HOH H 7 .   ? 38.829 -4.352  1.150   1.00 42.62 ? 999  HOH A O     1 
HETATM 3189 O  O     . HOH H 7 .   ? 40.076 -3.233  -0.851  1.00 44.35 ? 1000 HOH A O     1 
# 
