data_9F1Z
# 
_entry.id   9F1Z 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9F1Z         pdb_00009f1z 10.2210/pdb9f1z/pdb 
WWPDB D_1292138026 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F1Z 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sofia.kapetanaki@aok.pte.hu 
_pdbx_contact_author.name_first         Sofia 
_pdbx_contact_author.name_last          Kapetanaki 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1286-9929 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kapetanaki, S.' 1 ? 
'Coquelle, N.'   2 ? 
'Weik, M.'       3 ? 
# 
_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            Iucrj 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                991 
_citation.page_last                 1006 
_citation.title                     
;Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallography.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2052252524010170 
_citation.pdbx_database_id_PubMed   39470573 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kapetanaki, S.M.'      1  0000-0003-1286-9929 
primary 'Coquelle, N.'          2  ?                   
primary 'von Stetten, D.'       3  0000-0001-7906-9788 
primary 'Byrdin, M.'            4  0000-0002-6389-8714 
primary 'Rios-Santacruz, R.'    5  0000-0003-2087-4779 
primary 'Bean, R.'              6  0000-0001-8151-7439 
primary 'Bielecki, J.'          7  0000-0002-3012-603X 
primary 'Boudjelida, M.'        8  ?                   
primary 'Fekete, Z.'            9  ?                   
primary 'Grime, G.W.'           10 0000-0002-4957-8175 
primary 'Han, H.'               11 0000-0002-1197-3014 
primary 'Hatton, C.'            12 0000-0002-8446-0711 
primary 'Kantamneni, S.'        13 ?                   
primary 'Kharitonov, K.'        14 ?                   
primary 'Kim, C.'               15 0000-0003-4559-7982 
primary 'Kloos, M.'             16 0000-0002-8745-9740 
primary 'Koua, F.H.M.'          17 0000-0001-8371-9587 
primary 'de Diego Martinez, I.' 18 0000-0002-6156-4032 
primary 'Melo, D.'              19 0000-0002-7417-3479 
primary 'Rane, L.'              20 0000-0003-4609-2265 
primary 'Round, A.'             21 ?                   
primary 'Round, E.'             22 ?                   
primary 'Sarma, A.'             23 0000-0002-0785-8902 
primary 'Schubert, R.'          24 0000-0002-6213-2872 
primary 'Schulz, J.'            25 0000-0002-9310-8832 
primary 'Sikorski, M.'          26 ?                   
primary 'Vakili, M.'            27 0000-0001-9776-0177 
primary 'Valerio, J.'           28 0000-0001-5931-0925 
primary 'Vitas, J.'             29 0009-0001-0375-5754 
primary 'de Wijn, R.'           30 0000-0002-8342-1008 
primary 'Wrona, A.'             31 ?                   
primary 'Zala, N.'              32 0009-0003-6162-9507 
primary 'Pearson, A.'           33 0000-0001-8499-7490 
primary 'Dorner, K.'            34 ?                   
primary 'Schiro, G.'            35 ?                   
primary 'Garman, E.F.'          36 0000-0001-8329-5665 
primary 'Lukacs, A.'            37 ?                   
primary 'Weik, M.'              38 0000-0001-9297-642X 
# 
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 'Family 3 adenylate cyclase' 39372.934 1   ? ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'      456.344   1   ? ? ? ? 
3 non-polymer syn GLYCEROL                     92.094    1   ? ? ? ? 
4 non-polymer nat 'CALCIUM ION'                40.078    2   ? ? ? ? 
5 water       nat water                        18.015    171 ? ? ? ? 
# 
_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       
;GMKRLTWISKFSRPLSGDEIEAIGRISSQKNQQANVTGVLLCLDGIFFQILEGEAEKIDRIYERILADERHTDILCLKSE
VEVQERMFPDWSMQTINLDENTDFLIRPIKVLLQTLTESHRILEKYTQPSIFKIISQGTNPLNIRPKAVEKIVFFSDIVS
FSTFAEKLPVEEVVSVVNSYFSVCTAIITRQGGEVTKFIGDCVMAYFDGDCADQAIQASLDILMELEILRNSAPEGSPLR
VLYSGIGLAKGKVIEGNIGSELKRDYTILGDAVNVAARLEALTRQLSQALVFSSEVKNSATKSWNFIWLTDSELKGKSES
IDIYSIDNEMTRKSSGGLEIARNIGHYLERV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMKRLTWISKFSRPLSGDEIEAIGRISSQKNQQANVTGVLLCLDGIFFQILEGEAEKIDRIYERILADERHTDILCLKSE
VEVQERMFPDWSMQTINLDENTDFLIRPIKVLLQTLTESHRILEKYTQPSIFKIISQGTNPLNIRPKAVEKIVFFSDIVS
FSTFAEKLPVEEVVSVVNSYFSVCTAIITRQGGEVTKFIGDCVMAYFDGDCADQAIQASLDILMELEILRNSAPEGSPLR
VLYSGIGLAKGKVIEGNIGSELKRDYTILGDAVNVAARLEALTRQLSQALVFSSEVKNSATKSWNFIWLTDSELKGKSES
IDIYSIDNEMTRKSSGGLEIARNIGHYLERV
;
_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 'FLAVIN MONONUCLEOTIDE' FMN 
3 GLYCEROL                GOL 
4 'CALCIUM ION'           CA  
5 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   MET n 
1 3   LYS n 
1 4   ARG n 
1 5   LEU n 
1 6   THR n 
1 7   TRP n 
1 8   ILE n 
1 9   SER n 
1 10  LYS n 
1 11  PHE n 
1 12  SER n 
1 13  ARG n 
1 14  PRO n 
1 15  LEU n 
1 16  SER n 
1 17  GLY n 
1 18  ASP n 
1 19  GLU n 
1 20  ILE n 
1 21  GLU n 
1 22  ALA n 
1 23  ILE n 
1 24  GLY n 
1 25  ARG n 
1 26  ILE n 
1 27  SER n 
1 28  SER n 
1 29  GLN n 
1 30  LYS n 
1 31  ASN n 
1 32  GLN n 
1 33  GLN n 
1 34  ALA n 
1 35  ASN n 
1 36  VAL n 
1 37  THR n 
1 38  GLY n 
1 39  VAL n 
1 40  LEU n 
1 41  LEU n 
1 42  CYS n 
1 43  LEU n 
1 44  ASP n 
1 45  GLY n 
1 46  ILE n 
1 47  PHE n 
1 48  PHE n 
1 49  GLN n 
1 50  ILE n 
1 51  LEU n 
1 52  GLU n 
1 53  GLY n 
1 54  GLU n 
1 55  ALA n 
1 56  GLU n 
1 57  LYS n 
1 58  ILE n 
1 59  ASP n 
1 60  ARG n 
1 61  ILE n 
1 62  TYR n 
1 63  GLU n 
1 64  ARG n 
1 65  ILE n 
1 66  LEU n 
1 67  ALA n 
1 68  ASP n 
1 69  GLU n 
1 70  ARG n 
1 71  HIS n 
1 72  THR n 
1 73  ASP n 
1 74  ILE n 
1 75  LEU n 
1 76  CYS n 
1 77  LEU n 
1 78  LYS n 
1 79  SER n 
1 80  GLU n 
1 81  VAL n 
1 82  GLU n 
1 83  VAL n 
1 84  GLN n 
1 85  GLU n 
1 86  ARG n 
1 87  MET n 
1 88  PHE n 
1 89  PRO n 
1 90  ASP n 
1 91  TRP n 
1 92  SER n 
1 93  MET n 
1 94  GLN n 
1 95  THR n 
1 96  ILE n 
1 97  ASN n 
1 98  LEU n 
1 99  ASP n 
1 100 GLU n 
1 101 ASN n 
1 102 THR n 
1 103 ASP n 
1 104 PHE n 
1 105 LEU n 
1 106 ILE n 
1 107 ARG n 
1 108 PRO n 
1 109 ILE n 
1 110 LYS n 
1 111 VAL n 
1 112 LEU n 
1 113 LEU n 
1 114 GLN n 
1 115 THR n 
1 116 LEU n 
1 117 THR n 
1 118 GLU n 
1 119 SER n 
1 120 HIS n 
1 121 ARG n 
1 122 ILE n 
1 123 LEU n 
1 124 GLU n 
1 125 LYS n 
1 126 TYR n 
1 127 THR n 
1 128 GLN n 
1 129 PRO n 
1 130 SER n 
1 131 ILE n 
1 132 PHE n 
1 133 LYS n 
1 134 ILE n 
1 135 ILE n 
1 136 SER n 
1 137 GLN n 
1 138 GLY n 
1 139 THR n 
1 140 ASN n 
1 141 PRO n 
1 142 LEU n 
1 143 ASN n 
1 144 ILE n 
1 145 ARG n 
1 146 PRO n 
1 147 LYS n 
1 148 ALA n 
1 149 VAL n 
1 150 GLU n 
1 151 LYS n 
1 152 ILE n 
1 153 VAL n 
1 154 PHE n 
1 155 PHE n 
1 156 SER n 
1 157 ASP n 
1 158 ILE n 
1 159 VAL n 
1 160 SER n 
1 161 PHE n 
1 162 SER n 
1 163 THR n 
1 164 PHE n 
1 165 ALA n 
1 166 GLU n 
1 167 LYS n 
1 168 LEU n 
1 169 PRO n 
1 170 VAL n 
1 171 GLU n 
1 172 GLU n 
1 173 VAL n 
1 174 VAL n 
1 175 SER n 
1 176 VAL n 
1 177 VAL n 
1 178 ASN n 
1 179 SER n 
1 180 TYR n 
1 181 PHE n 
1 182 SER n 
1 183 VAL n 
1 184 CYS n 
1 185 THR n 
1 186 ALA n 
1 187 ILE n 
1 188 ILE n 
1 189 THR n 
1 190 ARG n 
1 191 GLN n 
1 192 GLY n 
1 193 GLY n 
1 194 GLU n 
1 195 VAL n 
1 196 THR n 
1 197 LYS n 
1 198 PHE n 
1 199 ILE n 
1 200 GLY n 
1 201 ASP n 
1 202 CYS n 
1 203 VAL n 
1 204 MET n 
1 205 ALA n 
1 206 TYR n 
1 207 PHE n 
1 208 ASP n 
1 209 GLY n 
1 210 ASP n 
1 211 CYS n 
1 212 ALA n 
1 213 ASP n 
1 214 GLN n 
1 215 ALA n 
1 216 ILE n 
1 217 GLN n 
1 218 ALA n 
1 219 SER n 
1 220 LEU n 
1 221 ASP n 
1 222 ILE n 
1 223 LEU n 
1 224 MET n 
1 225 GLU n 
1 226 LEU n 
1 227 GLU n 
1 228 ILE n 
1 229 LEU n 
1 230 ARG n 
1 231 ASN n 
1 232 SER n 
1 233 ALA n 
1 234 PRO n 
1 235 GLU n 
1 236 GLY n 
1 237 SER n 
1 238 PRO n 
1 239 LEU n 
1 240 ARG n 
1 241 VAL n 
1 242 LEU n 
1 243 TYR n 
1 244 SER n 
1 245 GLY n 
1 246 ILE n 
1 247 GLY n 
1 248 LEU n 
1 249 ALA n 
1 250 LYS n 
1 251 GLY n 
1 252 LYS n 
1 253 VAL n 
1 254 ILE n 
1 255 GLU n 
1 256 GLY n 
1 257 ASN n 
1 258 ILE n 
1 259 GLY n 
1 260 SER n 
1 261 GLU n 
1 262 LEU n 
1 263 LYS n 
1 264 ARG n 
1 265 ASP n 
1 266 TYR n 
1 267 THR n 
1 268 ILE n 
1 269 LEU n 
1 270 GLY n 
1 271 ASP n 
1 272 ALA n 
1 273 VAL n 
1 274 ASN n 
1 275 VAL n 
1 276 ALA n 
1 277 ALA n 
1 278 ARG n 
1 279 LEU n 
1 280 GLU n 
1 281 ALA n 
1 282 LEU n 
1 283 THR n 
1 284 ARG n 
1 285 GLN n 
1 286 LEU n 
1 287 SER n 
1 288 GLN n 
1 289 ALA n 
1 290 LEU n 
1 291 VAL n 
1 292 PHE n 
1 293 SER n 
1 294 SER n 
1 295 GLU n 
1 296 VAL n 
1 297 LYS n 
1 298 ASN n 
1 299 SER n 
1 300 ALA n 
1 301 THR n 
1 302 LYS n 
1 303 SER n 
1 304 TRP n 
1 305 ASN n 
1 306 PHE n 
1 307 ILE n 
1 308 TRP n 
1 309 LEU n 
1 310 THR n 
1 311 ASP n 
1 312 SER n 
1 313 GLU n 
1 314 LEU n 
1 315 LYS n 
1 316 GLY n 
1 317 LYS n 
1 318 SER n 
1 319 GLU n 
1 320 SER n 
1 321 ILE n 
1 322 ASP n 
1 323 ILE n 
1 324 TYR n 
1 325 SER n 
1 326 ILE n 
1 327 ASP n 
1 328 ASN n 
1 329 GLU n 
1 330 MET n 
1 331 THR n 
1 332 ARG n 
1 333 LYS n 
1 334 SER n 
1 335 SER n 
1 336 GLY n 
1 337 GLY n 
1 338 LEU n 
1 339 GLU n 
1 340 ILE n 
1 341 ALA n 
1 342 ARG n 
1 343 ASN n 
1 344 ILE n 
1 345 GLY n 
1 346 HIS n 
1 347 TYR n 
1 348 LEU n 
1 349 GLU n 
1 350 ARG n 
1 351 VAL 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                   351 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Oscil6304_3613 
_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      'Oscillatoria acuminata' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     118323 
_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  
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 
CA  non-polymer         . 'CALCIUM ION'           ?                               'Ca 2'            40.078  
CYS 'L-peptide linking' y CYSTEINE                ?                               'C3 H7 N O2 S'    121.158 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE' 'RIBOFLAVIN MONOPHOSPHATE'      'C17 H21 N4 O9 P' 456.344 
GLN 'L-peptide linking' y GLUTAMINE               ?                               'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ?                               'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                 ?                               'C2 H5 N O2'      75.067  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        92.094  
HIS 'L-peptide linking' y HISTIDINE               ?                               'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                   ?                               'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ?                               'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                 ?                               'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                  ?                               'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE              ?                               'C5 H11 N O2 S'   149.211 
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 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   0   0   GLY GLY A . n 
A 1 2   MET 2   1   1   MET MET A . n 
A 1 3   LYS 3   2   2   LYS LYS A . n 
A 1 4   ARG 4   3   3   ARG ARG A . n 
A 1 5   LEU 5   4   4   LEU LEU A . n 
A 1 6   THR 6   5   5   THR THR A . n 
A 1 7   TRP 7   6   6   TRP TRP A . n 
A 1 8   ILE 8   7   7   ILE ILE A . n 
A 1 9   SER 9   8   8   SER SER A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  PHE 11  10  10  PHE PHE A . n 
A 1 12  SER 12  11  11  SER SER A . n 
A 1 13  ARG 13  12  12  ARG ARG A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  LEU 15  14  14  LEU LEU A . n 
A 1 16  SER 16  15  15  SER SER A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ASP 18  17  17  ASP ASP A . n 
A 1 19  GLU 19  18  18  GLU GLU A . n 
A 1 20  ILE 20  19  19  ILE ILE A . n 
A 1 21  GLU 21  20  20  GLU GLU A . n 
A 1 22  ALA 22  21  21  ALA ALA A . n 
A 1 23  ILE 23  22  22  ILE ILE A . n 
A 1 24  GLY 24  23  23  GLY GLY A . n 
A 1 25  ARG 25  24  24  ARG ARG A . n 
A 1 26  ILE 26  25  25  ILE ILE A . n 
A 1 27  SER 27  26  26  SER SER A . n 
A 1 28  SER 28  27  27  SER SER A . n 
A 1 29  GLN 29  28  28  GLN GLN A . n 
A 1 30  LYS 30  29  29  LYS LYS A . n 
A 1 31  ASN 31  30  30  ASN ASN A . n 
A 1 32  GLN 32  31  31  GLN GLN A . n 
A 1 33  GLN 33  32  32  GLN GLN A . n 
A 1 34  ALA 34  33  33  ALA ALA A . n 
A 1 35  ASN 35  34  34  ASN ASN A . n 
A 1 36  VAL 36  35  35  VAL VAL A . n 
A 1 37  THR 37  36  36  THR THR A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  VAL 39  38  38  VAL VAL A . n 
A 1 40  LEU 40  39  39  LEU LEU A . n 
A 1 41  LEU 41  40  40  LEU LEU A . n 
A 1 42  CYS 42  41  41  CYS CYS A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  ASP 44  43  43  ASP ASP A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  ILE 46  45  45  ILE ILE A . n 
A 1 47  PHE 47  46  46  PHE PHE A . n 
A 1 48  PHE 48  47  47  PHE PHE A . n 
A 1 49  GLN 49  48  48  GLN GLN A . n 
A 1 50  ILE 50  49  49  ILE ILE A . n 
A 1 51  LEU 51  50  50  LEU LEU A . n 
A 1 52  GLU 52  51  51  GLU GLU A . n 
A 1 53  GLY 53  52  52  GLY GLY A . n 
A 1 54  GLU 54  53  53  GLU GLU A . n 
A 1 55  ALA 55  54  54  ALA ALA A . n 
A 1 56  GLU 56  55  55  GLU GLU A . n 
A 1 57  LYS 57  56  56  LYS LYS A . n 
A 1 58  ILE 58  57  57  ILE ILE A . n 
A 1 59  ASP 59  58  58  ASP ASP A . n 
A 1 60  ARG 60  59  59  ARG ARG A . n 
A 1 61  ILE 61  60  60  ILE ILE A . n 
A 1 62  TYR 62  61  61  TYR TYR A . n 
A 1 63  GLU 63  62  62  GLU GLU A . n 
A 1 64  ARG 64  63  63  ARG ARG A . n 
A 1 65  ILE 65  64  64  ILE ILE A . n 
A 1 66  LEU 66  65  65  LEU LEU A . n 
A 1 67  ALA 67  66  66  ALA ALA A . n 
A 1 68  ASP 68  67  67  ASP ASP A . n 
A 1 69  GLU 69  68  68  GLU GLU A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  HIS 71  70  70  HIS HIS A . n 
A 1 72  THR 72  71  71  THR THR A . n 
A 1 73  ASP 73  72  72  ASP ASP A . n 
A 1 74  ILE 74  73  73  ILE ILE A . n 
A 1 75  LEU 75  74  74  LEU LEU A . n 
A 1 76  CYS 76  75  75  CYS CYS A . n 
A 1 77  LEU 77  76  76  LEU LEU A . n 
A 1 78  LYS 78  77  77  LYS LYS A . n 
A 1 79  SER 79  78  78  SER SER A . n 
A 1 80  GLU 80  79  79  GLU GLU A . n 
A 1 81  VAL 81  80  80  VAL VAL A . n 
A 1 82  GLU 82  81  81  GLU GLU A . n 
A 1 83  VAL 83  82  82  VAL VAL A . n 
A 1 84  GLN 84  83  83  GLN GLN A . n 
A 1 85  GLU 85  84  84  GLU GLU A . n 
A 1 86  ARG 86  85  85  ARG ARG A . n 
A 1 87  MET 87  86  86  MET MET A . n 
A 1 88  PHE 88  87  87  PHE PHE A . n 
A 1 89  PRO 89  88  88  PRO PRO A . n 
A 1 90  ASP 90  89  89  ASP ASP A . n 
A 1 91  TRP 91  90  90  TRP TRP A . n 
A 1 92  SER 92  91  91  SER SER A . n 
A 1 93  MET 93  92  92  MET MET A . n 
A 1 94  GLN 94  93  93  GLN GLN A . n 
A 1 95  THR 95  94  94  THR THR A . n 
A 1 96  ILE 96  95  95  ILE ILE A . n 
A 1 97  ASN 97  96  96  ASN ASN A . n 
A 1 98  LEU 98  97  97  LEU LEU A . n 
A 1 99  ASP 99  98  98  ASP ASP A . n 
A 1 100 GLU 100 99  99  GLU GLU A . n 
A 1 101 ASN 101 100 100 ASN ASN A . n 
A 1 102 THR 102 101 101 THR THR A . n 
A 1 103 ASP 103 102 102 ASP ASP A . n 
A 1 104 PHE 104 103 103 PHE PHE A . n 
A 1 105 LEU 105 104 104 LEU LEU A . n 
A 1 106 ILE 106 105 105 ILE ILE A . n 
A 1 107 ARG 107 106 106 ARG ARG A . n 
A 1 108 PRO 108 107 107 PRO PRO A . n 
A 1 109 ILE 109 108 108 ILE ILE A . n 
A 1 110 LYS 110 109 109 LYS LYS A . n 
A 1 111 VAL 111 110 110 VAL VAL A . n 
A 1 112 LEU 112 111 111 LEU LEU A . n 
A 1 113 LEU 113 112 112 LEU LEU A . n 
A 1 114 GLN 114 113 113 GLN GLN A . n 
A 1 115 THR 115 114 114 THR THR A . n 
A 1 116 LEU 116 115 115 LEU LEU A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 GLU 118 117 117 GLU GLU A . n 
A 1 119 SER 119 118 118 SER SER A . n 
A 1 120 HIS 120 119 119 HIS HIS A . n 
A 1 121 ARG 121 120 120 ARG ARG A . n 
A 1 122 ILE 122 121 121 ILE ILE A . n 
A 1 123 LEU 123 122 122 LEU LEU A . n 
A 1 124 GLU 124 123 123 GLU GLU A . n 
A 1 125 LYS 125 124 124 LYS LYS A . n 
A 1 126 TYR 126 125 125 TYR TYR A . n 
A 1 127 THR 127 126 126 THR THR A . n 
A 1 128 GLN 128 127 127 GLN GLN A . n 
A 1 129 PRO 129 128 128 PRO PRO A . n 
A 1 130 SER 130 129 129 SER SER A . n 
A 1 131 ILE 131 130 130 ILE ILE A . n 
A 1 132 PHE 132 131 131 PHE PHE A . n 
A 1 133 LYS 133 132 132 LYS LYS A . n 
A 1 134 ILE 134 133 133 ILE ILE A . n 
A 1 135 ILE 135 134 134 ILE ILE A . n 
A 1 136 SER 136 135 135 SER SER A . n 
A 1 137 GLN 137 136 136 GLN GLN A . n 
A 1 138 GLY 138 137 137 GLY GLY A . n 
A 1 139 THR 139 138 138 THR THR A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 PRO 141 140 140 PRO PRO A . n 
A 1 142 LEU 142 141 141 LEU LEU A . n 
A 1 143 ASN 143 142 142 ASN ASN A . n 
A 1 144 ILE 144 143 143 ILE ILE A . n 
A 1 145 ARG 145 144 144 ARG ARG A . n 
A 1 146 PRO 146 145 145 PRO PRO A . n 
A 1 147 LYS 147 146 146 LYS LYS A . n 
A 1 148 ALA 148 147 147 ALA ALA A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 GLU 150 149 149 GLU GLU A . n 
A 1 151 LYS 151 150 150 LYS LYS A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 VAL 153 152 152 VAL VAL A . n 
A 1 154 PHE 154 153 153 PHE PHE A . n 
A 1 155 PHE 155 154 154 PHE PHE A . n 
A 1 156 SER 156 155 155 SER SER A . n 
A 1 157 ASP 157 156 156 ASP ASP A . n 
A 1 158 ILE 158 157 157 ILE ILE A . n 
A 1 159 VAL 159 158 158 VAL VAL A . n 
A 1 160 SER 160 159 159 SER SER A . n 
A 1 161 PHE 161 160 160 PHE PHE A . n 
A 1 162 SER 162 161 161 SER SER A . n 
A 1 163 THR 163 162 162 THR THR A . n 
A 1 164 PHE 164 163 163 PHE PHE A . n 
A 1 165 ALA 165 164 164 ALA ALA A . n 
A 1 166 GLU 166 165 165 GLU GLU A . n 
A 1 167 LYS 167 166 166 LYS LYS A . n 
A 1 168 LEU 168 167 167 LEU LEU A . n 
A 1 169 PRO 169 168 168 PRO PRO A . n 
A 1 170 VAL 170 169 169 VAL VAL A . n 
A 1 171 GLU 171 170 170 GLU GLU A . n 
A 1 172 GLU 172 171 171 GLU GLU A . n 
A 1 173 VAL 173 172 172 VAL VAL A . n 
A 1 174 VAL 174 173 173 VAL VAL A . n 
A 1 175 SER 175 174 174 SER SER A . n 
A 1 176 VAL 176 175 175 VAL VAL A . n 
A 1 177 VAL 177 176 176 VAL VAL A . n 
A 1 178 ASN 178 177 177 ASN ASN A . n 
A 1 179 SER 179 178 178 SER SER A . n 
A 1 180 TYR 180 179 179 TYR TYR A . n 
A 1 181 PHE 181 180 180 PHE PHE A . n 
A 1 182 SER 182 181 181 SER SER A . n 
A 1 183 VAL 183 182 182 VAL VAL A . n 
A 1 184 CYS 184 183 183 CYS CYS A . n 
A 1 185 THR 185 184 184 THR THR A . n 
A 1 186 ALA 186 185 185 ALA ALA A . n 
A 1 187 ILE 187 186 186 ILE ILE A . n 
A 1 188 ILE 188 187 187 ILE ILE A . n 
A 1 189 THR 189 188 188 THR THR A . n 
A 1 190 ARG 190 189 189 ARG ARG A . n 
A 1 191 GLN 191 190 190 GLN GLN A . n 
A 1 192 GLY 192 191 191 GLY GLY A . n 
A 1 193 GLY 193 192 192 GLY GLY A . n 
A 1 194 GLU 194 193 193 GLU GLU A . n 
A 1 195 VAL 195 194 194 VAL VAL A . n 
A 1 196 THR 196 195 195 THR THR A . n 
A 1 197 LYS 197 196 196 LYS LYS A . n 
A 1 198 PHE 198 197 197 PHE PHE A . n 
A 1 199 ILE 199 198 198 ILE ILE A . n 
A 1 200 GLY 200 199 199 GLY GLY A . n 
A 1 201 ASP 201 200 200 ASP ASP A . n 
A 1 202 CYS 202 201 201 CYS CYS A . n 
A 1 203 VAL 203 202 202 VAL VAL A . n 
A 1 204 MET 204 203 203 MET MET A . n 
A 1 205 ALA 205 204 204 ALA ALA A . n 
A 1 206 TYR 206 205 205 TYR TYR A . n 
A 1 207 PHE 207 206 206 PHE PHE A . n 
A 1 208 ASP 208 207 207 ASP ASP A . n 
A 1 209 GLY 209 208 208 GLY GLY A . n 
A 1 210 ASP 210 209 209 ASP ASP A . n 
A 1 211 CYS 211 210 210 CYS CYS A . n 
A 1 212 ALA 212 211 211 ALA ALA A . n 
A 1 213 ASP 213 212 212 ASP ASP A . n 
A 1 214 GLN 214 213 213 GLN GLN A . n 
A 1 215 ALA 215 214 214 ALA ALA A . n 
A 1 216 ILE 216 215 215 ILE ILE A . n 
A 1 217 GLN 217 216 216 GLN GLN A . n 
A 1 218 ALA 218 217 217 ALA ALA A . n 
A 1 219 SER 219 218 218 SER SER A . n 
A 1 220 LEU 220 219 219 LEU LEU A . n 
A 1 221 ASP 221 220 220 ASP ASP A . n 
A 1 222 ILE 222 221 221 ILE ILE A . n 
A 1 223 LEU 223 222 222 LEU LEU A . n 
A 1 224 MET 224 223 223 MET MET A . n 
A 1 225 GLU 225 224 224 GLU GLU A . n 
A 1 226 LEU 226 225 225 LEU LEU A . n 
A 1 227 GLU 227 226 226 GLU GLU A . n 
A 1 228 ILE 228 227 227 ILE ILE A . n 
A 1 229 LEU 229 228 228 LEU LEU A . n 
A 1 230 ARG 230 229 229 ARG ARG A . n 
A 1 231 ASN 231 230 230 ASN ASN A . n 
A 1 232 SER 232 231 231 SER SER A . n 
A 1 233 ALA 233 232 232 ALA ALA A . n 
A 1 234 PRO 234 233 233 PRO PRO A . n 
A 1 235 GLU 235 234 234 GLU GLU A . n 
A 1 236 GLY 236 235 235 GLY GLY A . n 
A 1 237 SER 237 236 236 SER SER A . n 
A 1 238 PRO 238 237 237 PRO PRO A . n 
A 1 239 LEU 239 238 238 LEU LEU A . n 
A 1 240 ARG 240 239 239 ARG ARG A . n 
A 1 241 VAL 241 240 240 VAL VAL A . n 
A 1 242 LEU 242 241 241 LEU LEU A . n 
A 1 243 TYR 243 242 242 TYR TYR A . n 
A 1 244 SER 244 243 243 SER SER A . n 
A 1 245 GLY 245 244 244 GLY GLY A . n 
A 1 246 ILE 246 245 245 ILE ILE A . n 
A 1 247 GLY 247 246 246 GLY GLY A . n 
A 1 248 LEU 248 247 247 LEU LEU A . n 
A 1 249 ALA 249 248 248 ALA ALA A . n 
A 1 250 LYS 250 249 249 LYS LYS A . n 
A 1 251 GLY 251 250 250 GLY GLY A . n 
A 1 252 LYS 252 251 251 LYS LYS A . n 
A 1 253 VAL 253 252 252 VAL VAL A . n 
A 1 254 ILE 254 253 253 ILE ILE A . n 
A 1 255 GLU 255 254 254 GLU GLU A . n 
A 1 256 GLY 256 255 255 GLY GLY A . n 
A 1 257 ASN 257 256 256 ASN ASN A . n 
A 1 258 ILE 258 257 257 ILE ILE A . n 
A 1 259 GLY 259 258 258 GLY GLY A . n 
A 1 260 SER 260 259 259 SER SER A . n 
A 1 261 GLU 261 260 260 GLU GLU A . n 
A 1 262 LEU 262 261 261 LEU LEU A . n 
A 1 263 LYS 263 262 262 LYS LYS A . n 
A 1 264 ARG 264 263 263 ARG ARG A . n 
A 1 265 ASP 265 264 264 ASP ASP A . n 
A 1 266 TYR 266 265 265 TYR TYR A . n 
A 1 267 THR 267 266 266 THR THR A . n 
A 1 268 ILE 268 267 267 ILE ILE A . n 
A 1 269 LEU 269 268 268 LEU LEU A . n 
A 1 270 GLY 270 269 269 GLY GLY A . n 
A 1 271 ASP 271 270 270 ASP ASP A . n 
A 1 272 ALA 272 271 271 ALA ALA A . n 
A 1 273 VAL 273 272 272 VAL VAL A . n 
A 1 274 ASN 274 273 273 ASN ASN A . n 
A 1 275 VAL 275 274 274 VAL VAL A . n 
A 1 276 ALA 276 275 275 ALA ALA A . n 
A 1 277 ALA 277 276 276 ALA ALA A . n 
A 1 278 ARG 278 277 277 ARG ARG A . n 
A 1 279 LEU 279 278 278 LEU LEU A . n 
A 1 280 GLU 280 279 279 GLU GLU A . n 
A 1 281 ALA 281 280 280 ALA ALA A . n 
A 1 282 LEU 282 281 281 LEU LEU A . n 
A 1 283 THR 283 282 282 THR THR A . n 
A 1 284 ARG 284 283 283 ARG ARG A . n 
A 1 285 GLN 285 284 284 GLN GLN A . n 
A 1 286 LEU 286 285 285 LEU LEU A . n 
A 1 287 SER 287 286 286 SER SER A . n 
A 1 288 GLN 288 287 287 GLN GLN A . n 
A 1 289 ALA 289 288 288 ALA ALA A . n 
A 1 290 LEU 290 289 289 LEU LEU A . n 
A 1 291 VAL 291 290 290 VAL VAL A . n 
A 1 292 PHE 292 291 291 PHE PHE A . n 
A 1 293 SER 293 292 292 SER SER A . n 
A 1 294 SER 294 293 293 SER SER A . n 
A 1 295 GLU 295 294 294 GLU GLU A . n 
A 1 296 VAL 296 295 295 VAL VAL A . n 
A 1 297 LYS 297 296 296 LYS LYS A . n 
A 1 298 ASN 298 297 297 ASN ASN A . n 
A 1 299 SER 299 298 298 SER SER A . n 
A 1 300 ALA 300 299 299 ALA ALA A . n 
A 1 301 THR 301 300 300 THR THR A . n 
A 1 302 LYS 302 301 301 LYS LYS A . n 
A 1 303 SER 303 302 302 SER SER A . n 
A 1 304 TRP 304 303 303 TRP TRP A . n 
A 1 305 ASN 305 304 304 ASN ASN A . n 
A 1 306 PHE 306 305 305 PHE PHE A . n 
A 1 307 ILE 307 306 306 ILE ILE A . n 
A 1 308 TRP 308 307 307 TRP TRP A . n 
A 1 309 LEU 309 308 308 LEU LEU A . n 
A 1 310 THR 310 309 309 THR THR A . n 
A 1 311 ASP 311 310 310 ASP ASP A . n 
A 1 312 SER 312 311 311 SER SER A . n 
A 1 313 GLU 313 312 312 GLU GLU A . n 
A 1 314 LEU 314 313 313 LEU LEU A . n 
A 1 315 LYS 315 314 314 LYS LYS A . n 
A 1 316 GLY 316 315 315 GLY GLY A . n 
A 1 317 LYS 317 316 316 LYS LYS A . n 
A 1 318 SER 318 317 317 SER SER A . n 
A 1 319 GLU 319 318 318 GLU GLU A . n 
A 1 320 SER 320 319 319 SER SER A . n 
A 1 321 ILE 321 320 320 ILE ILE A . n 
A 1 322 ASP 322 321 321 ASP ASP A . n 
A 1 323 ILE 323 322 322 ILE ILE A . n 
A 1 324 TYR 324 323 323 TYR TYR A . n 
A 1 325 SER 325 324 324 SER SER A . n 
A 1 326 ILE 326 325 325 ILE ILE A . n 
A 1 327 ASP 327 326 326 ASP ASP A . n 
A 1 328 ASN 328 327 327 ASN ASN A . n 
A 1 329 GLU 329 328 328 GLU GLU A . n 
A 1 330 MET 330 329 329 MET MET A . n 
A 1 331 THR 331 330 330 THR THR A . n 
A 1 332 ARG 332 331 331 ARG ARG A . n 
A 1 333 LYS 333 332 332 LYS LYS A . n 
A 1 334 SER 334 333 333 SER SER A . n 
A 1 335 SER 335 334 334 SER SER A . n 
A 1 336 GLY 336 335 335 GLY GLY A . n 
A 1 337 GLY 337 336 336 GLY GLY A . n 
A 1 338 LEU 338 337 337 LEU LEU A . n 
A 1 339 GLU 339 338 338 GLU GLU A . n 
A 1 340 ILE 340 339 339 ILE ILE A . n 
A 1 341 ALA 341 340 340 ALA ALA A . n 
A 1 342 ARG 342 341 341 ARG ARG A . n 
A 1 343 ASN 343 342 342 ASN ASN A . n 
A 1 344 ILE 344 343 343 ILE ILE A . n 
A 1 345 GLY 345 344 344 GLY GLY A . n 
A 1 346 HIS 346 345 345 HIS HIS A . n 
A 1 347 TYR 347 346 346 TYR TYR A . n 
A 1 348 LEU 348 347 347 LEU LEU A . n 
A 1 349 GLU 349 348 348 GLU GLU A . n 
A 1 350 ARG 350 349 349 ARG ARG A . n 
A 1 351 VAL 351 350 350 VAL VAL A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FMN 1   401 401 FMN FMN A . 
C 3 GOL 1   402 402 GOL GOL A . 
D 4 CA  1   403 1   CA  CA  A . 
E 4 CA  1   404 2   CA  CA  A . 
F 5 HOH 1   501 157 HOH HOH A . 
F 5 HOH 2   502 248 HOH HOH A . 
F 5 HOH 3   503 116 HOH HOH A . 
F 5 HOH 4   504 142 HOH HOH A . 
F 5 HOH 5   505 225 HOH HOH A . 
F 5 HOH 6   506 128 HOH HOH A . 
F 5 HOH 7   507 145 HOH HOH A . 
F 5 HOH 8   508 41  HOH HOH A . 
F 5 HOH 9   509 29  HOH HOH A . 
F 5 HOH 10  510 147 HOH HOH A . 
F 5 HOH 11  511 112 HOH HOH A . 
F 5 HOH 12  512 215 HOH HOH A . 
F 5 HOH 13  513 204 HOH HOH A . 
F 5 HOH 14  514 27  HOH HOH A . 
F 5 HOH 15  515 146 HOH HOH A . 
F 5 HOH 16  516 173 HOH HOH A . 
F 5 HOH 17  517 196 HOH HOH A . 
F 5 HOH 18  518 159 HOH HOH A . 
F 5 HOH 19  519 102 HOH HOH A . 
F 5 HOH 20  520 123 HOH HOH A . 
F 5 HOH 21  521 107 HOH HOH A . 
F 5 HOH 22  522 224 HOH HOH A . 
F 5 HOH 23  523 6   HOH HOH A . 
F 5 HOH 24  524 42  HOH HOH A . 
F 5 HOH 25  525 221 HOH HOH A . 
F 5 HOH 26  526 109 HOH HOH A . 
F 5 HOH 27  527 217 HOH HOH A . 
F 5 HOH 28  528 60  HOH HOH A . 
F 5 HOH 29  529 127 HOH HOH A . 
F 5 HOH 30  530 140 HOH HOH A . 
F 5 HOH 31  531 216 HOH HOH A . 
F 5 HOH 32  532 154 HOH HOH A . 
F 5 HOH 33  533 207 HOH HOH A . 
F 5 HOH 34  534 4   HOH HOH A . 
F 5 HOH 35  535 172 HOH HOH A . 
F 5 HOH 36  536 194 HOH HOH A . 
F 5 HOH 37  537 190 HOH HOH A . 
F 5 HOH 38  538 247 HOH HOH A . 
F 5 HOH 39  539 180 HOH HOH A . 
F 5 HOH 40  540 114 HOH HOH A . 
F 5 HOH 41  541 183 HOH HOH A . 
F 5 HOH 42  542 5   HOH HOH A . 
F 5 HOH 43  543 125 HOH HOH A . 
F 5 HOH 44  544 8   HOH HOH A . 
F 5 HOH 45  545 124 HOH HOH A . 
F 5 HOH 46  546 155 HOH HOH A . 
F 5 HOH 47  547 40  HOH HOH A . 
F 5 HOH 48  548 208 HOH HOH A . 
F 5 HOH 49  549 93  HOH HOH A . 
F 5 HOH 50  550 26  HOH HOH A . 
F 5 HOH 51  551 87  HOH HOH A . 
F 5 HOH 52  552 234 HOH HOH A . 
F 5 HOH 53  553 56  HOH HOH A . 
F 5 HOH 54  554 25  HOH HOH A . 
F 5 HOH 55  555 95  HOH HOH A . 
F 5 HOH 56  556 2   HOH HOH A . 
F 5 HOH 57  557 120 HOH HOH A . 
F 5 HOH 58  558 209 HOH HOH A . 
F 5 HOH 59  559 211 HOH HOH A . 
F 5 HOH 60  560 191 HOH HOH A . 
F 5 HOH 61  561 3   HOH HOH A . 
F 5 HOH 62  562 20  HOH HOH A . 
F 5 HOH 63  563 251 HOH HOH A . 
F 5 HOH 64  564 94  HOH HOH A . 
F 5 HOH 65  565 11  HOH HOH A . 
F 5 HOH 66  566 181 HOH HOH A . 
F 5 HOH 67  567 78  HOH HOH A . 
F 5 HOH 68  568 49  HOH HOH A . 
F 5 HOH 69  569 104 HOH HOH A . 
F 5 HOH 70  570 164 HOH HOH A . 
F 5 HOH 71  571 58  HOH HOH A . 
F 5 HOH 72  572 168 HOH HOH A . 
F 5 HOH 73  573 98  HOH HOH A . 
F 5 HOH 74  574 249 HOH HOH A . 
F 5 HOH 75  575 210 HOH HOH A . 
F 5 HOH 76  576 38  HOH HOH A . 
F 5 HOH 77  577 182 HOH HOH A . 
F 5 HOH 78  578 233 HOH HOH A . 
F 5 HOH 79  579 77  HOH HOH A . 
F 5 HOH 80  580 156 HOH HOH A . 
F 5 HOH 81  581 126 HOH HOH A . 
F 5 HOH 82  582 206 HOH HOH A . 
F 5 HOH 83  583 171 HOH HOH A . 
F 5 HOH 84  584 85  HOH HOH A . 
F 5 HOH 85  585 69  HOH HOH A . 
F 5 HOH 86  586 200 HOH HOH A . 
F 5 HOH 87  587 166 HOH HOH A . 
F 5 HOH 88  588 195 HOH HOH A . 
F 5 HOH 89  589 96  HOH HOH A . 
F 5 HOH 90  590 110 HOH HOH A . 
F 5 HOH 91  591 243 HOH HOH A . 
F 5 HOH 92  592 178 HOH HOH A . 
F 5 HOH 93  593 141 HOH HOH A . 
F 5 HOH 94  594 118 HOH HOH A . 
F 5 HOH 95  595 185 HOH HOH A . 
F 5 HOH 96  596 151 HOH HOH A . 
F 5 HOH 97  597 184 HOH HOH A . 
F 5 HOH 98  598 7   HOH HOH A . 
F 5 HOH 99  599 214 HOH HOH A . 
F 5 HOH 100 600 223 HOH HOH A . 
F 5 HOH 101 601 32  HOH HOH A . 
F 5 HOH 102 602 21  HOH HOH A . 
F 5 HOH 103 603 1   HOH HOH A . 
F 5 HOH 104 604 16  HOH HOH A . 
F 5 HOH 105 605 97  HOH HOH A . 
F 5 HOH 106 606 28  HOH HOH A . 
F 5 HOH 107 607 66  HOH HOH A . 
F 5 HOH 108 608 227 HOH HOH A . 
F 5 HOH 109 609 113 HOH HOH A . 
F 5 HOH 110 610 59  HOH HOH A . 
F 5 HOH 111 611 119 HOH HOH A . 
F 5 HOH 112 612 61  HOH HOH A . 
F 5 HOH 113 613 106 HOH HOH A . 
F 5 HOH 114 614 162 HOH HOH A . 
F 5 HOH 115 615 158 HOH HOH A . 
F 5 HOH 116 616 51  HOH HOH A . 
F 5 HOH 117 617 101 HOH HOH A . 
F 5 HOH 118 618 22  HOH HOH A . 
F 5 HOH 119 619 131 HOH HOH A . 
F 5 HOH 120 620 117 HOH HOH A . 
F 5 HOH 121 621 235 HOH HOH A . 
F 5 HOH 122 622 163 HOH HOH A . 
F 5 HOH 123 623 19  HOH HOH A . 
F 5 HOH 124 624 175 HOH HOH A . 
F 5 HOH 125 625 148 HOH HOH A . 
F 5 HOH 126 626 152 HOH HOH A . 
F 5 HOH 127 627 149 HOH HOH A . 
F 5 HOH 128 628 192 HOH HOH A . 
F 5 HOH 129 629 35  HOH HOH A . 
F 5 HOH 130 630 150 HOH HOH A . 
F 5 HOH 131 631 9   HOH HOH A . 
F 5 HOH 132 632 121 HOH HOH A . 
F 5 HOH 133 633 198 HOH HOH A . 
F 5 HOH 134 634 136 HOH HOH A . 
F 5 HOH 135 635 10  HOH HOH A . 
F 5 HOH 136 636 132 HOH HOH A . 
F 5 HOH 137 637 135 HOH HOH A . 
F 5 HOH 138 638 45  HOH HOH A . 
F 5 HOH 139 639 100 HOH HOH A . 
F 5 HOH 140 640 232 HOH HOH A . 
F 5 HOH 141 641 177 HOH HOH A . 
F 5 HOH 142 642 73  HOH HOH A . 
F 5 HOH 143 643 220 HOH HOH A . 
F 5 HOH 144 644 212 HOH HOH A . 
F 5 HOH 145 645 89  HOH HOH A . 
F 5 HOH 146 646 165 HOH HOH A . 
F 5 HOH 147 647 213 HOH HOH A . 
F 5 HOH 148 648 99  HOH HOH A . 
F 5 HOH 149 649 188 HOH HOH A . 
F 5 HOH 150 650 245 HOH HOH A . 
F 5 HOH 151 651 47  HOH HOH A . 
F 5 HOH 152 652 167 HOH HOH A . 
F 5 HOH 153 653 189 HOH HOH A . 
F 5 HOH 154 654 18  HOH HOH A . 
F 5 HOH 155 655 105 HOH HOH A . 
F 5 HOH 156 656 231 HOH HOH A . 
F 5 HOH 157 657 92  HOH HOH A . 
F 5 HOH 158 658 88  HOH HOH A . 
F 5 HOH 159 659 57  HOH HOH A . 
F 5 HOH 160 660 80  HOH HOH A . 
F 5 HOH 161 661 250 HOH HOH A . 
F 5 HOH 162 662 170 HOH HOH A . 
F 5 HOH 163 663 160 HOH HOH A . 
F 5 HOH 164 664 134 HOH HOH A . 
F 5 HOH 165 665 201 HOH HOH A . 
F 5 HOH 166 666 186 HOH HOH A . 
F 5 HOH 167 667 187 HOH HOH A . 
F 5 HOH 168 668 197 HOH HOH A . 
F 5 HOH 169 669 33  HOH HOH A . 
F 5 HOH 170 670 179 HOH HOH A . 
F 5 HOH 171 671 228 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 0 A SER 8   ? CA  A A SER 9   CA  
2  1 Y 0 A SER 8   ? CB  A A SER 9   CB  
3  1 Y 0 A SER 8   ? OG  A A SER 9   OG  
4  1 Y 1 A GLU 338 ? CG  ? A GLU 339 CG  
5  1 Y 1 A GLU 338 ? CD  ? A GLU 339 CD  
6  1 Y 1 A GLU 338 ? OE1 ? A GLU 339 OE1 
7  1 Y 1 A GLU 338 ? OE2 ? A GLU 339 OE2 
8  1 Y 1 A ARG 341 ? CG  ? A ARG 342 CG  
9  1 Y 1 A ARG 341 ? CD  ? A ARG 342 CD  
10 1 Y 1 A ARG 341 ? NE  ? A ARG 342 NE  
11 1 Y 1 A ARG 341 ? CZ  ? A ARG 342 CZ  
12 1 Y 1 A ARG 341 ? NH1 ? A ARG 342 NH1 
13 1 Y 1 A ARG 341 ? NH2 ? A ARG 342 NH2 
# 
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 scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    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                     9F1Z 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.455 
_cell.length_a_esd                 ? 
_cell.length_b                     52.684 
_cell.length_b_esd                 ? 
_cell.length_c                     71.525 
_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                         9F1Z 
_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                   9F1Z 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.59 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.06 M divalents, 0.1 M Tris-Bicine pH 8.5, 30% v/v PEG550 MME-PEG20000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-11 
_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   0.98 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F1Z 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               46.66 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     27876 
_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                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_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                                0.063 
_reflns.pdbx_Rpim_I_all                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       106179 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.054 
_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                                    1.95 
_reflns_shell.d_res_low                                     2.00 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           7386 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1924 
_reflns_shell.percent_possible_obs                          97.8 
_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                               3.8 
_reflns_shell.pdbx_chi_squared                              0.99 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.1 
_reflns_shell.pdbx_Rrim_I_all                               1.405 
_reflns_shell.pdbx_Rpim_I_all                               0.692 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.480 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.210 
_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                                 9F1Z 
_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                            1.95 
_refine.ls_d_res_low                             46.66 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     27835 
_refine.ls_number_reflns_R_free                  1439 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.05 
_refine.ls_percent_reflns_R_free                 5.17 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1978 
_refine.ls_R_factor_R_free                       0.2335 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1958 
_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               THROUGHOUT 
_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                 28.60 
_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                            0.31 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        46.66 
_refine_hist.number_atoms_solvent             171 
_refine_hist.number_atoms_total               2965 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2755 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 2865 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.048  ? 3880 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.541 ? 395  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.064  ? 447  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 493  ? 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' 1.95 2.02  . . 146 2580 98.00  . . . . 0.3903 . . . . . . . . . . . 0.4490 
'X-RAY DIFFRACTION' 2.02 2.10  . . 135 2637 99.00  . . . . 0.2974 . . . . . . . . . . . 0.3624 
'X-RAY DIFFRACTION' 2.10 2.20  . . 141 2655 100.00 . . . . 0.2470 . . . . . . . . . . . 0.2843 
'X-RAY DIFFRACTION' 2.20 2.31  . . 145 2633 99.00  . . . . 0.2226 . . . . . . . . . . . 0.2756 
'X-RAY DIFFRACTION' 2.31 2.46  . . 135 2641 99.00  . . . . 0.2134 . . . . . . . . . . . 0.3134 
'X-RAY DIFFRACTION' 2.46 2.65  . . 136 2674 99.00  . . . . 0.2174 . . . . . . . . . . . 0.2745 
'X-RAY DIFFRACTION' 2.65 2.91  . . 141 2661 100.00 . . . . 0.2054 . . . . . . . . . . . 0.2397 
'X-RAY DIFFRACTION' 2.91 3.33  . . 156 2642 98.00  . . . . 0.1955 . . . . . . . . . . . 0.2625 
'X-RAY DIFFRACTION' 3.33 4.20  . . 151 2638 97.00  . . . . 0.1662 . . . . . . . . . . . 0.1858 
'X-RAY DIFFRACTION' 4.20 46.66 . . 153 2635 92.00  . . . . 0.1707 . . . . . . . . . . . 0.1977 
# 
_struct.entry_id                     9F1Z 
_struct.title                        'Crystal structure of adenylyate cyclase variant Y6W' 
_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        9F1Z 
_struct_keywords.text            'FAD, mutant, Y6W, adenylate cyclase, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    K9TLZ5_9CYAN 
_struct_ref.pdbx_db_accession          K9TLZ5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKRLTYISKFSRPLSGDEIEAIGRISSQKNQQANVTGVLLCLDGIFFQILEGEAEKIDRIYERILADERHTDILCLKSEV
EVQERMFPDWSMQTINLDENTDFLIRPIKVLLQTLTESHRILEKYTQPSIFKIISQGTNPLNIRPKAVEKIVFFSDIVSF
STFAEKLPVEEVVSVVNSYFSVCTAIITRQGGEVTKFIGDCVMAYFDGDCADQAIQASLDILMELEILRNSAPEGSPLRV
LYSGIGLAKGKVIEGNIGSELKRDYTILGDAVNVAARLEALTRQLSQALVFSSEVKNSATKSWNFIWLTDSELKGKSESI
DIYSIDNEMTRKSSGGLEIARNIGHYLERV
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F1Z 
_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                 351 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             K9TLZ5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  350 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       350 
# 
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 9F1Z GLY A 1 ? UNP K9TLZ5 ?   ? 'expression tag'      0 1 
1 9F1Z TRP A 7 ? UNP K9TLZ5 TYR 6 'engineered mutation' 6 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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10740 ? 
1 MORE         -131  ? 
1 'SSA (A^2)'  28880 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 16  ? ASN A 35  ? SER A 15  ASN A 34  1 ? 20 
HELX_P HELX_P2  AA2 ALA A 55  ? ALA A 67  ? ALA A 54  ALA A 66  1 ? 13 
HELX_P HELX_P3  AA3 ASP A 99  ? ASN A 101 ? ASP A 98  ASN A 100 5 ? 3  
HELX_P HELX_P4  AA4 LEU A 105 ? TYR A 126 ? LEU A 104 TYR A 125 1 ? 22 
HELX_P HELX_P5  AA5 GLN A 128 ? GLN A 137 ? GLN A 127 GLN A 136 1 ? 10 
HELX_P HELX_P6  AA6 ASN A 140 ? ILE A 144 ? ASN A 139 ILE A 143 5 ? 5  
HELX_P HELX_P7  AA7 SER A 160 ? LEU A 168 ? SER A 159 LEU A 167 1 ? 9  
HELX_P HELX_P8  AA8 PRO A 169 ? GLN A 191 ? PRO A 168 GLN A 190 1 ? 23 
HELX_P HELX_P9  AA9 CYS A 211 ? ALA A 233 ? CYS A 210 ALA A 232 1 ? 23 
HELX_P HELX_P10 AB1 SER A 237 ? LEU A 242 ? SER A 236 LEU A 241 5 ? 6  
HELX_P HELX_P11 AB2 ASP A 271 ? SER A 287 ? ASP A 270 SER A 286 1 ? 17 
HELX_P HELX_P12 AB3 SER A 294 ? ALA A 300 ? SER A 293 ALA A 299 1 ? 7  
HELX_P HELX_P13 AB4 GLY A 337 ? ARG A 350 ? GLY A 336 ARG A 349 1 ? 14 
# 
_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 ASP 90  O   ? ? ? 1_555 D CA  . CA ? ? A ASP 89  A CA  403 1_556 ? ? ? ? ? ? ? 2.383 ? ? 
metalc2  metalc ? ? A ASP 157 OD2 ? ? ? 1_555 E CA  . CA ? ? A ASP 156 A CA  404 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc3  metalc ? ? A ILE 158 O   ? ? ? 1_555 E CA  . CA ? ? A ILE 157 A CA  404 1_555 ? ? ? ? ? ? ? 2.921 ? ? 
metalc4  metalc ? ? A ASP 201 OD2 ? ? ? 1_555 E CA  . CA ? ? A ASP 200 A CA  404 1_555 ? ? ? ? ? ? ? 2.549 ? ? 
metalc5  metalc ? ? A ASP 271 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 270 A CA  404 2_555 ? ? ? ? ? ? ? 2.840 ? ? 
metalc6  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 310 A CA  403 1_555 ? ? ? ? ? ? ? 2.476 ? ? 
metalc7  metalc ? ? A ASP 311 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 310 A CA  403 1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc8  metalc ? ? A ASP 322 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 321 A CA  403 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc9  metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  403 A HOH 562 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc10 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  403 A HOH 602 1_555 ? ? ? ? ? ? ? 2.390 ? ? 
metalc11 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  403 A HOH 618 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc12 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  404 A HOH 502 2_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc13 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  404 A HOH 538 1_555 ? ? ? ? ? ? ? 2.922 ? ? 
metalc14 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  404 A HOH 550 2_555 ? ? ? ? ? ? ? 2.454 ? ? 
metalc15 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  404 A HOH 576 2_555 ? ? ? ? ? ? ? 3.041 ? ? 
# 
_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  O   ? A ASP 90  ? A ASP 89  ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 OD1 ? A ASP 311 ? A ASP 310 ? 1_555 34.8  ? 
2  O   ? A ASP 90  ? A ASP 89  ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 OD2 ? A ASP 311 ? A ASP 310 ? 1_555 33.2  ? 
3  OD1 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 OD2 ? A ASP 311 ? A ASP 310 ? 1_555 1.6   ? 
4  O   ? A ASP 90  ? A ASP 89  ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 OD1 ? A ASP 322 ? A ASP 321 ? 1_555 35.1  ? 
5  OD1 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 OD1 ? A ASP 322 ? A ASP 321 ? 1_555 1.9   ? 
6  OD2 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 OD1 ? A ASP 322 ? A ASP 321 ? 1_555 2.7   ? 
7  O   ? A ASP 90  ? A ASP 89  ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 562 ? 1_555 32.5  ? 
8  OD1 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 562 ? 1_555 3.1   ? 
9  OD2 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 562 ? 1_555 2.1   ? 
10 OD1 ? A ASP 322 ? A ASP 321 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 562 ? 1_555 2.6   ? 
11 O   ? A ASP 90  ? A ASP 89  ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 602 ? 1_555 35.3  ? 
12 OD1 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 602 ? 1_555 2.2   ? 
13 OD2 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 602 ? 1_555 2.9   ? 
14 OD1 ? A ASP 322 ? A ASP 321 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 602 ? 1_555 0.3   ? 
15 O   ? F HOH .   ? A HOH 562 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 602 ? 1_555 2.8   ? 
16 O   ? A ASP 90  ? A ASP 89  ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 618 ? 1_555 33.9  ? 
17 OD1 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 618 ? 1_555 3.7   ? 
18 OD2 ? A ASP 311 ? A ASP 310 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 618 ? 1_555 3.6   ? 
19 OD1 ? A ASP 322 ? A ASP 321 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 618 ? 1_555 2.2   ? 
20 O   ? F HOH .   ? A HOH 562 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 618 ? 1_555 2.0   ? 
21 O   ? F HOH .   ? A HOH 602 ? 1_555 CA ? D CA . ? A CA 403 ? 1_556 O   ? F HOH .   ? A HOH 618 ? 1_555 2.1   ? 
22 OD2 ? A ASP 157 ? A ASP 156 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? A ILE 158 ? A ILE 157 ? 1_555 86.9  ? 
23 OD2 ? A ASP 157 ? A ASP 156 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 OD2 ? A ASP 201 ? A ASP 200 ? 1_555 111.3 ? 
24 O   ? A ILE 158 ? A ILE 157 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 OD2 ? A ASP 201 ? A ASP 200 ? 1_555 71.0  ? 
25 OD2 ? A ASP 157 ? A ASP 156 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 OD1 ? A ASP 271 ? A ASP 270 ? 1_555 74.6  ? 
26 O   ? A ILE 158 ? A ILE 157 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 OD1 ? A ASP 271 ? A ASP 270 ? 1_555 158.4 ? 
27 OD2 ? A ASP 201 ? A ASP 200 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 OD1 ? A ASP 271 ? A ASP 270 ? 1_555 104.9 ? 
28 OD2 ? A ASP 157 ? A ASP 156 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 502 ? 2_555 97.3  ? 
29 O   ? A ILE 158 ? A ILE 157 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 502 ? 2_555 166.2 ? 
30 OD2 ? A ASP 201 ? A ASP 200 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 502 ? 2_555 118.9 ? 
31 OD1 ? A ASP 271 ? A ASP 270 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 502 ? 2_555 33.3  ? 
32 OD2 ? A ASP 157 ? A ASP 156 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 538 ? 1_555 98.2  ? 
33 O   ? A ILE 158 ? A ILE 157 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 538 ? 1_555 148.5 ? 
34 OD2 ? A ASP 201 ? A ASP 200 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 538 ? 1_555 78.3  ? 
35 OD1 ? A ASP 271 ? A ASP 270 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 538 ? 1_555 30.7  ? 
36 O   ? F HOH .   ? A HOH 502 ? 2_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 538 ? 1_555 44.0  ? 
37 OD2 ? A ASP 157 ? A ASP 156 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 550 ? 2_555 128.8 ? 
38 O   ? A ILE 158 ? A ILE 157 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 550 ? 2_555 62.4  ? 
39 OD2 ? A ASP 201 ? A ASP 200 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 550 ? 2_555 96.9  ? 
40 OD1 ? A ASP 271 ? A ASP 270 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 550 ? 2_555 138.7 ? 
41 O   ? F HOH .   ? A HOH 502 ? 2_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 550 ? 2_555 105.4 ? 
42 O   ? F HOH .   ? A HOH 538 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 550 ? 2_555 129.8 ? 
43 OD2 ? A ASP 157 ? A ASP 156 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 576 ? 2_555 92.2  ? 
44 O   ? A ILE 158 ? A ILE 157 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 576 ? 2_555 123.4 ? 
45 OD2 ? A ASP 201 ? A ASP 200 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 576 ? 2_555 153.9 ? 
46 OD1 ? A ASP 271 ? A ASP 270 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 576 ? 2_555 69.6  ? 
47 O   ? F HOH .   ? A HOH 502 ? 2_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 576 ? 2_555 43.6  ? 
48 O   ? F HOH .   ? A HOH 538 ? 1_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 576 ? 2_555 87.6  ? 
49 O   ? F HOH .   ? A HOH 550 ? 2_555 CA ? E CA . ? A CA 404 ? 1_555 O   ? F HOH .   ? A HOH 576 ? 2_555 75.4  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? 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 HIS A 71  ? VAL A 83  ? HIS A 70  VAL A 82  
AA1 2 MET A 2   ? PHE A 11  ? MET A 1   PHE A 10  
AA1 3 ILE A 46  ? GLU A 54  ? ILE A 45  GLU A 53  
AA1 4 THR A 37  ? LEU A 43  ? THR A 36  LEU A 42  
AA1 5 GLN A 94  ? ASN A 97  ? GLN A 93  ASN A 96  
AA2 1 GLU A 194 ? ILE A 199 ? GLU A 193 ILE A 198 
AA2 2 CYS A 202 ? ASP A 208 ? CYS A 201 ASP A 207 
AA2 3 LYS A 147 ? ILE A 158 ? LYS A 146 ILE A 157 
AA2 4 SER A 244 ? GLY A 259 ? SER A 243 GLY A 258 
AA2 5 ARG A 264 ? ILE A 268 ? ARG A 263 ILE A 267 
AA3 1 GLU A 194 ? ILE A 199 ? GLU A 193 ILE A 198 
AA3 2 CYS A 202 ? ASP A 208 ? CYS A 201 ASP A 207 
AA3 3 LYS A 147 ? ILE A 158 ? LYS A 146 ILE A 157 
AA3 4 SER A 244 ? GLY A 259 ? SER A 243 GLY A 258 
AA3 5 LEU A 290 ? SER A 293 ? LEU A 289 SER A 292 
AA3 6 ILE A 321 ? ILE A 326 ? ILE A 320 ILE A 325 
AA3 7 PHE A 306 ? SER A 312 ? PHE A 305 SER A 311 
# 
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 O VAL A 83  ? O VAL A 82  N MET A 2   ? N MET A 1   
AA1 2 3 N LEU A 5   ? N LEU A 4   O LEU A 51  ? O LEU A 50  
AA1 3 4 O PHE A 48  ? O PHE A 47  N LEU A 41  ? N LEU A 40  
AA1 4 5 N LEU A 40  ? N LEU A 39  O GLN A 94  ? O GLN A 93  
AA2 1 2 N ILE A 199 ? N ILE A 198 O CYS A 202 ? O CYS A 201 
AA2 2 3 O ALA A 205 ? O ALA A 204 N PHE A 154 ? N PHE A 153 
AA2 3 4 N VAL A 153 ? N VAL A 152 O ALA A 249 ? O ALA A 248 
AA2 4 5 N ILE A 254 ? N ILE A 253 O ILE A 268 ? O ILE A 267 
AA3 1 2 N ILE A 199 ? N ILE A 198 O CYS A 202 ? O CYS A 201 
AA3 2 3 O ALA A 205 ? O ALA A 204 N PHE A 154 ? N PHE A 153 
AA3 3 4 N VAL A 153 ? N VAL A 152 O ALA A 249 ? O ALA A 248 
AA3 4 5 N ILE A 246 ? N ILE A 245 O VAL A 291 ? O VAL A 290 
AA3 5 6 N PHE A 292 ? N PHE A 291 O TYR A 324 ? O TYR A 323 
AA3 6 7 O ILE A 323 ? O ILE A 322 N THR A 310 ? N THR A 309 
# 
_pdbx_entry_details.entry_id                   9F1Z 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 629 ? ? O A HOH 631 ? ? 2.04 
2  1 O   A HOH 537 ? ? O A HOH 648 ? ? 2.10 
3  1 O   A HOH 502 ? ? O A HOH 576 ? ? 2.10 
4  1 O   A HOH 589 ? ? O A HOH 651 ? ? 2.10 
5  1 O   A HOH 560 ? ? O A HOH 648 ? ? 2.11 
6  1 OD1 A ASN 273 ? ? O A HOH 502 ? ? 2.16 
7  1 O   A HOH 571 ? ? O A HOH 654 ? ? 2.17 
8  1 O   A HOH 611 ? ? O A HOH 647 ? ? 2.18 
9  1 O   A HOH 607 ? ? O A HOH 624 ? ? 2.19 
10 1 O   A HOH 606 ? ? O A HOH 642 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O  A HOH 502 ? ? 1_555 O  A HOH 538 ? ? 2_555 2.04 
2 1 OG A SER 302 ? ? 1_555 NZ A LYS 332 ? ? 3_555 2.10 
# 
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 159 ? ? 33.06   59.56  
2 1 CYS A 210 ? ? -100.97 42.91  
3 1 GLU A 260 ? ? 58.61   -47.55 
4 1 LYS A 332 ? ? -161.79 116.63 
5 1 ARG A 349 ? ? -108.54 49.54  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     671 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CA  CA     CA N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
FMN N1     N  N N 89  
FMN C2     C  N N 90  
FMN O2     O  N N 91  
FMN N3     N  N N 92  
FMN C4     C  N N 93  
FMN O4     O  N N 94  
FMN C4A    C  N N 95  
FMN N5     N  N N 96  
FMN C5A    C  Y N 97  
FMN C6     C  Y N 98  
FMN C7     C  Y N 99  
FMN C7M    C  N N 100 
FMN C8     C  Y N 101 
FMN C8M    C  N N 102 
FMN C9     C  Y N 103 
FMN C9A    C  Y N 104 
FMN N10    N  N N 105 
FMN C10    C  N N 106 
FMN "C1'"  C  N N 107 
FMN "C2'"  C  N S 108 
FMN "O2'"  O  N N 109 
FMN "C3'"  C  N S 110 
FMN "O3'"  O  N N 111 
FMN "C4'"  C  N R 112 
FMN "O4'"  O  N N 113 
FMN "C5'"  C  N N 114 
FMN "O5'"  O  N N 115 
FMN P      P  N N 116 
FMN O1P    O  N N 117 
FMN O2P    O  N N 118 
FMN O3P    O  N N 119 
FMN HN3    H  N N 120 
FMN H6     H  N N 121 
FMN HM71   H  N N 122 
FMN HM72   H  N N 123 
FMN HM73   H  N N 124 
FMN HM81   H  N N 125 
FMN HM82   H  N N 126 
FMN HM83   H  N N 127 
FMN H9     H  N N 128 
FMN "H1'1" H  N N 129 
FMN "H1'2" H  N N 130 
FMN "H2'"  H  N N 131 
FMN "HO2'" H  N N 132 
FMN "H3'"  H  N N 133 
FMN "HO3'" H  N N 134 
FMN "H4'"  H  N N 135 
FMN "HO4'" H  N N 136 
FMN "H5'1" H  N N 137 
FMN "H5'2" H  N N 138 
FMN HOP2   H  N N 139 
FMN HOP3   H  N N 140 
GLN N      N  N N 141 
GLN CA     C  N S 142 
GLN C      C  N N 143 
GLN O      O  N N 144 
GLN CB     C  N N 145 
GLN CG     C  N N 146 
GLN CD     C  N N 147 
GLN OE1    O  N N 148 
GLN NE2    N  N N 149 
GLN OXT    O  N N 150 
GLN H      H  N N 151 
GLN H2     H  N N 152 
GLN HA     H  N N 153 
GLN HB2    H  N N 154 
GLN HB3    H  N N 155 
GLN HG2    H  N N 156 
GLN HG3    H  N N 157 
GLN HE21   H  N N 158 
GLN HE22   H  N N 159 
GLN HXT    H  N N 160 
GLU N      N  N N 161 
GLU CA     C  N S 162 
GLU C      C  N N 163 
GLU O      O  N N 164 
GLU CB     C  N N 165 
GLU CG     C  N N 166 
GLU CD     C  N N 167 
GLU OE1    O  N N 168 
GLU OE2    O  N N 169 
GLU OXT    O  N N 170 
GLU H      H  N N 171 
GLU H2     H  N N 172 
GLU HA     H  N N 173 
GLU HB2    H  N N 174 
GLU HB3    H  N N 175 
GLU HG2    H  N N 176 
GLU HG3    H  N N 177 
GLU HE2    H  N N 178 
GLU HXT    H  N N 179 
GLY N      N  N N 180 
GLY CA     C  N N 181 
GLY C      C  N N 182 
GLY O      O  N N 183 
GLY OXT    O  N N 184 
GLY H      H  N N 185 
GLY H2     H  N N 186 
GLY HA2    H  N N 187 
GLY HA3    H  N N 188 
GLY HXT    H  N N 189 
GOL C1     C  N N 190 
GOL O1     O  N N 191 
GOL C2     C  N N 192 
GOL O2     O  N N 193 
GOL C3     C  N N 194 
GOL O3     O  N N 195 
GOL H11    H  N N 196 
GOL H12    H  N N 197 
GOL HO1    H  N N 198 
GOL H2     H  N N 199 
GOL HO2    H  N N 200 
GOL H31    H  N N 201 
GOL H32    H  N N 202 
GOL HO3    H  N N 203 
HIS N      N  N N 204 
HIS CA     C  N S 205 
HIS C      C  N N 206 
HIS O      O  N N 207 
HIS CB     C  N N 208 
HIS CG     C  Y N 209 
HIS ND1    N  Y N 210 
HIS CD2    C  Y N 211 
HIS CE1    C  Y N 212 
HIS NE2    N  Y N 213 
HIS OXT    O  N N 214 
HIS H      H  N N 215 
HIS H2     H  N N 216 
HIS HA     H  N N 217 
HIS HB2    H  N N 218 
HIS HB3    H  N N 219 
HIS HD1    H  N N 220 
HIS HD2    H  N N 221 
HIS HE1    H  N N 222 
HIS HE2    H  N N 223 
HIS HXT    H  N N 224 
HOH O      O  N N 225 
HOH H1     H  N N 226 
HOH H2     H  N N 227 
ILE N      N  N N 228 
ILE CA     C  N S 229 
ILE C      C  N N 230 
ILE O      O  N N 231 
ILE CB     C  N S 232 
ILE CG1    C  N N 233 
ILE CG2    C  N N 234 
ILE CD1    C  N N 235 
ILE OXT    O  N N 236 
ILE H      H  N N 237 
ILE H2     H  N N 238 
ILE HA     H  N N 239 
ILE HB     H  N N 240 
ILE HG12   H  N N 241 
ILE HG13   H  N N 242 
ILE HG21   H  N N 243 
ILE HG22   H  N N 244 
ILE HG23   H  N N 245 
ILE HD11   H  N N 246 
ILE HD12   H  N N 247 
ILE HD13   H  N N 248 
ILE HXT    H  N N 249 
LEU N      N  N N 250 
LEU CA     C  N S 251 
LEU C      C  N N 252 
LEU O      O  N N 253 
LEU CB     C  N N 254 
LEU CG     C  N N 255 
LEU CD1    C  N N 256 
LEU CD2    C  N N 257 
LEU OXT    O  N N 258 
LEU H      H  N N 259 
LEU H2     H  N N 260 
LEU HA     H  N N 261 
LEU HB2    H  N N 262 
LEU HB3    H  N N 263 
LEU HG     H  N N 264 
LEU HD11   H  N N 265 
LEU HD12   H  N N 266 
LEU HD13   H  N N 267 
LEU HD21   H  N N 268 
LEU HD22   H  N N 269 
LEU HD23   H  N N 270 
LEU HXT    H  N N 271 
LYS N      N  N N 272 
LYS CA     C  N S 273 
LYS C      C  N N 274 
LYS O      O  N N 275 
LYS CB     C  N N 276 
LYS CG     C  N N 277 
LYS CD     C  N N 278 
LYS CE     C  N N 279 
LYS NZ     N  N N 280 
LYS OXT    O  N N 281 
LYS H      H  N N 282 
LYS H2     H  N N 283 
LYS HA     H  N N 284 
LYS HB2    H  N N 285 
LYS HB3    H  N N 286 
LYS HG2    H  N N 287 
LYS HG3    H  N N 288 
LYS HD2    H  N N 289 
LYS HD3    H  N N 290 
LYS HE2    H  N N 291 
LYS HE3    H  N N 292 
LYS HZ1    H  N N 293 
LYS HZ2    H  N N 294 
LYS HZ3    H  N N 295 
LYS HXT    H  N N 296 
MET N      N  N N 297 
MET CA     C  N S 298 
MET C      C  N N 299 
MET O      O  N N 300 
MET CB     C  N N 301 
MET CG     C  N N 302 
MET SD     S  N N 303 
MET CE     C  N N 304 
MET OXT    O  N N 305 
MET H      H  N N 306 
MET H2     H  N N 307 
MET HA     H  N N 308 
MET HB2    H  N N 309 
MET HB3    H  N N 310 
MET HG2    H  N N 311 
MET HG3    H  N N 312 
MET HE1    H  N N 313 
MET HE2    H  N N 314 
MET HE3    H  N N 315 
MET HXT    H  N N 316 
PHE N      N  N N 317 
PHE CA     C  N S 318 
PHE C      C  N N 319 
PHE O      O  N N 320 
PHE CB     C  N N 321 
PHE CG     C  Y N 322 
PHE CD1    C  Y N 323 
PHE CD2    C  Y N 324 
PHE CE1    C  Y N 325 
PHE CE2    C  Y N 326 
PHE CZ     C  Y N 327 
PHE OXT    O  N N 328 
PHE H      H  N N 329 
PHE H2     H  N N 330 
PHE HA     H  N N 331 
PHE HB2    H  N N 332 
PHE HB3    H  N N 333 
PHE HD1    H  N N 334 
PHE HD2    H  N N 335 
PHE HE1    H  N N 336 
PHE HE2    H  N N 337 
PHE HZ     H  N N 338 
PHE HXT    H  N N 339 
PRO N      N  N N 340 
PRO CA     C  N S 341 
PRO C      C  N N 342 
PRO O      O  N N 343 
PRO CB     C  N N 344 
PRO CG     C  N N 345 
PRO CD     C  N N 346 
PRO OXT    O  N N 347 
PRO H      H  N N 348 
PRO HA     H  N N 349 
PRO HB2    H  N N 350 
PRO HB3    H  N N 351 
PRO HG2    H  N N 352 
PRO HG3    H  N N 353 
PRO HD2    H  N N 354 
PRO HD3    H  N N 355 
PRO HXT    H  N N 356 
SER N      N  N N 357 
SER CA     C  N S 358 
SER C      C  N N 359 
SER O      O  N N 360 
SER CB     C  N N 361 
SER OG     O  N N 362 
SER OXT    O  N N 363 
SER H      H  N N 364 
SER H2     H  N N 365 
SER HA     H  N N 366 
SER HB2    H  N N 367 
SER HB3    H  N N 368 
SER HG     H  N N 369 
SER HXT    H  N N 370 
THR N      N  N N 371 
THR CA     C  N S 372 
THR C      C  N N 373 
THR O      O  N N 374 
THR CB     C  N R 375 
THR OG1    O  N N 376 
THR CG2    C  N N 377 
THR OXT    O  N N 378 
THR H      H  N N 379 
THR H2     H  N N 380 
THR HA     H  N N 381 
THR HB     H  N N 382 
THR HG1    H  N N 383 
THR HG21   H  N N 384 
THR HG22   H  N N 385 
THR HG23   H  N N 386 
THR HXT    H  N N 387 
TRP N      N  N N 388 
TRP CA     C  N S 389 
TRP C      C  N N 390 
TRP O      O  N N 391 
TRP CB     C  N N 392 
TRP CG     C  Y N 393 
TRP CD1    C  Y N 394 
TRP CD2    C  Y N 395 
TRP NE1    N  Y N 396 
TRP CE2    C  Y N 397 
TRP CE3    C  Y N 398 
TRP CZ2    C  Y N 399 
TRP CZ3    C  Y N 400 
TRP CH2    C  Y N 401 
TRP OXT    O  N N 402 
TRP H      H  N N 403 
TRP H2     H  N N 404 
TRP HA     H  N N 405 
TRP HB2    H  N N 406 
TRP HB3    H  N N 407 
TRP HD1    H  N N 408 
TRP HE1    H  N N 409 
TRP HE3    H  N N 410 
TRP HZ2    H  N N 411 
TRP HZ3    H  N N 412 
TRP HH2    H  N N 413 
TRP HXT    H  N N 414 
TYR N      N  N N 415 
TYR CA     C  N S 416 
TYR C      C  N N 417 
TYR O      O  N N 418 
TYR CB     C  N N 419 
TYR CG     C  Y N 420 
TYR CD1    C  Y N 421 
TYR CD2    C  Y N 422 
TYR CE1    C  Y N 423 
TYR CE2    C  Y N 424 
TYR CZ     C  Y N 425 
TYR OH     O  N N 426 
TYR OXT    O  N N 427 
TYR H      H  N N 428 
TYR H2     H  N N 429 
TYR HA     H  N N 430 
TYR HB2    H  N N 431 
TYR HB3    H  N N 432 
TYR HD1    H  N N 433 
TYR HD2    H  N N 434 
TYR HE1    H  N N 435 
TYR HE2    H  N N 436 
TYR HH     H  N N 437 
TYR HXT    H  N N 438 
VAL N      N  N N 439 
VAL CA     C  N S 440 
VAL C      C  N N 441 
VAL O      O  N N 442 
VAL CB     C  N N 443 
VAL CG1    C  N N 444 
VAL CG2    C  N N 445 
VAL OXT    O  N N 446 
VAL H      H  N N 447 
VAL H2     H  N N 448 
VAL HA     H  N N 449 
VAL HB     H  N N 450 
VAL HG11   H  N N 451 
VAL HG12   H  N N 452 
VAL HG13   H  N N 453 
VAL HG21   H  N N 454 
VAL HG22   H  N N 455 
VAL HG23   H  N N 456 
VAL HXT    H  N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FMN N1    C2     sing N N 83  
FMN N1    C10    doub N N 84  
FMN C2    O2     doub N N 85  
FMN C2    N3     sing N N 86  
FMN N3    C4     sing N N 87  
FMN N3    HN3    sing N N 88  
FMN C4    O4     doub N N 89  
FMN C4    C4A    sing N N 90  
FMN C4A   N5     doub N N 91  
FMN C4A   C10    sing N N 92  
FMN N5    C5A    sing N N 93  
FMN C5A   C6     doub Y N 94  
FMN C5A   C9A    sing Y N 95  
FMN C6    C7     sing Y N 96  
FMN C6    H6     sing N N 97  
FMN C7    C7M    sing N N 98  
FMN C7    C8     doub Y N 99  
FMN C7M   HM71   sing N N 100 
FMN C7M   HM72   sing N N 101 
FMN C7M   HM73   sing N N 102 
FMN C8    C8M    sing N N 103 
FMN C8    C9     sing Y N 104 
FMN C8M   HM81   sing N N 105 
FMN C8M   HM82   sing N N 106 
FMN C8M   HM83   sing N N 107 
FMN C9    C9A    doub Y N 108 
FMN C9    H9     sing N N 109 
FMN C9A   N10    sing N N 110 
FMN N10   C10    sing N N 111 
FMN N10   "C1'"  sing N N 112 
FMN "C1'" "C2'"  sing N N 113 
FMN "C1'" "H1'1" sing N N 114 
FMN "C1'" "H1'2" sing N N 115 
FMN "C2'" "O2'"  sing N N 116 
FMN "C2'" "C3'"  sing N N 117 
FMN "C2'" "H2'"  sing N N 118 
FMN "O2'" "HO2'" sing N N 119 
FMN "C3'" "O3'"  sing N N 120 
FMN "C3'" "C4'"  sing N N 121 
FMN "C3'" "H3'"  sing N N 122 
FMN "O3'" "HO3'" sing N N 123 
FMN "C4'" "O4'"  sing N N 124 
FMN "C4'" "C5'"  sing N N 125 
FMN "C4'" "H4'"  sing N N 126 
FMN "O4'" "HO4'" sing N N 127 
FMN "C5'" "O5'"  sing N N 128 
FMN "C5'" "H5'1" sing N N 129 
FMN "C5'" "H5'2" sing N N 130 
FMN "O5'" P      sing N N 131 
FMN P     O1P    doub N N 132 
FMN P     O2P    sing N N 133 
FMN P     O3P    sing N N 134 
FMN O2P   HOP2   sing N N 135 
FMN O3P   HOP3   sing N N 136 
GLN N     CA     sing N N 137 
GLN N     H      sing N N 138 
GLN N     H2     sing N N 139 
GLN CA    C      sing N N 140 
GLN CA    CB     sing N N 141 
GLN CA    HA     sing N N 142 
GLN C     O      doub N N 143 
GLN C     OXT    sing N N 144 
GLN CB    CG     sing N N 145 
GLN CB    HB2    sing N N 146 
GLN CB    HB3    sing N N 147 
GLN CG    CD     sing N N 148 
GLN CG    HG2    sing N N 149 
GLN CG    HG3    sing N N 150 
GLN CD    OE1    doub N N 151 
GLN CD    NE2    sing N N 152 
GLN NE2   HE21   sing N N 153 
GLN NE2   HE22   sing N N 154 
GLN OXT   HXT    sing N N 155 
GLU N     CA     sing N N 156 
GLU N     H      sing N N 157 
GLU N     H2     sing N N 158 
GLU CA    C      sing N N 159 
GLU CA    CB     sing N N 160 
GLU CA    HA     sing N N 161 
GLU C     O      doub N N 162 
GLU C     OXT    sing N N 163 
GLU CB    CG     sing N N 164 
GLU CB    HB2    sing N N 165 
GLU CB    HB3    sing N N 166 
GLU CG    CD     sing N N 167 
GLU CG    HG2    sing N N 168 
GLU CG    HG3    sing N N 169 
GLU CD    OE1    doub N N 170 
GLU CD    OE2    sing N N 171 
GLU OE2   HE2    sing N N 172 
GLU OXT   HXT    sing N N 173 
GLY N     CA     sing N N 174 
GLY N     H      sing N N 175 
GLY N     H2     sing N N 176 
GLY CA    C      sing N N 177 
GLY CA    HA2    sing N N 178 
GLY CA    HA3    sing N N 179 
GLY C     O      doub N N 180 
GLY C     OXT    sing N N 181 
GLY OXT   HXT    sing N N 182 
GOL C1    O1     sing N N 183 
GOL C1    C2     sing N N 184 
GOL C1    H11    sing N N 185 
GOL C1    H12    sing N N 186 
GOL O1    HO1    sing N N 187 
GOL C2    O2     sing N N 188 
GOL C2    C3     sing N N 189 
GOL C2    H2     sing N N 190 
GOL O2    HO2    sing N N 191 
GOL C3    O3     sing N N 192 
GOL C3    H31    sing N N 193 
GOL C3    H32    sing N N 194 
GOL O3    HO3    sing N N 195 
HIS N     CA     sing N N 196 
HIS N     H      sing N N 197 
HIS N     H2     sing N N 198 
HIS CA    C      sing N N 199 
HIS CA    CB     sing N N 200 
HIS CA    HA     sing N N 201 
HIS C     O      doub N N 202 
HIS C     OXT    sing N N 203 
HIS CB    CG     sing N N 204 
HIS CB    HB2    sing N N 205 
HIS CB    HB3    sing N N 206 
HIS CG    ND1    sing Y N 207 
HIS CG    CD2    doub Y N 208 
HIS ND1   CE1    doub Y N 209 
HIS ND1   HD1    sing N N 210 
HIS CD2   NE2    sing Y N 211 
HIS CD2   HD2    sing N N 212 
HIS CE1   NE2    sing Y N 213 
HIS CE1   HE1    sing N N 214 
HIS NE2   HE2    sing N N 215 
HIS OXT   HXT    sing N N 216 
HOH O     H1     sing N N 217 
HOH O     H2     sing N N 218 
ILE N     CA     sing N N 219 
ILE N     H      sing N N 220 
ILE N     H2     sing N N 221 
ILE CA    C      sing N N 222 
ILE CA    CB     sing N N 223 
ILE CA    HA     sing N N 224 
ILE C     O      doub N N 225 
ILE C     OXT    sing N N 226 
ILE CB    CG1    sing N N 227 
ILE CB    CG2    sing N N 228 
ILE CB    HB     sing N N 229 
ILE CG1   CD1    sing N N 230 
ILE CG1   HG12   sing N N 231 
ILE CG1   HG13   sing N N 232 
ILE CG2   HG21   sing N N 233 
ILE CG2   HG22   sing N N 234 
ILE CG2   HG23   sing N N 235 
ILE CD1   HD11   sing N N 236 
ILE CD1   HD12   sing N N 237 
ILE CD1   HD13   sing N N 238 
ILE OXT   HXT    sing N N 239 
LEU N     CA     sing N N 240 
LEU N     H      sing N N 241 
LEU N     H2     sing N N 242 
LEU CA    C      sing N N 243 
LEU CA    CB     sing N N 244 
LEU CA    HA     sing N N 245 
LEU C     O      doub N N 246 
LEU C     OXT    sing N N 247 
LEU CB    CG     sing N N 248 
LEU CB    HB2    sing N N 249 
LEU CB    HB3    sing N N 250 
LEU CG    CD1    sing N N 251 
LEU CG    CD2    sing N N 252 
LEU CG    HG     sing N N 253 
LEU CD1   HD11   sing N N 254 
LEU CD1   HD12   sing N N 255 
LEU CD1   HD13   sing N N 256 
LEU CD2   HD21   sing N N 257 
LEU CD2   HD22   sing N N 258 
LEU CD2   HD23   sing N N 259 
LEU OXT   HXT    sing N N 260 
LYS N     CA     sing N N 261 
LYS N     H      sing N N 262 
LYS N     H2     sing N N 263 
LYS CA    C      sing N N 264 
LYS CA    CB     sing N N 265 
LYS CA    HA     sing N N 266 
LYS C     O      doub N N 267 
LYS C     OXT    sing N N 268 
LYS CB    CG     sing N N 269 
LYS CB    HB2    sing N N 270 
LYS CB    HB3    sing N N 271 
LYS CG    CD     sing N N 272 
LYS CG    HG2    sing N N 273 
LYS CG    HG3    sing N N 274 
LYS CD    CE     sing N N 275 
LYS CD    HD2    sing N N 276 
LYS CD    HD3    sing N N 277 
LYS CE    NZ     sing N N 278 
LYS CE    HE2    sing N N 279 
LYS CE    HE3    sing N N 280 
LYS NZ    HZ1    sing N N 281 
LYS NZ    HZ2    sing N N 282 
LYS NZ    HZ3    sing N N 283 
LYS OXT   HXT    sing N N 284 
MET N     CA     sing N N 285 
MET N     H      sing N N 286 
MET N     H2     sing N N 287 
MET CA    C      sing N N 288 
MET CA    CB     sing N N 289 
MET CA    HA     sing N N 290 
MET C     O      doub N N 291 
MET C     OXT    sing N N 292 
MET CB    CG     sing N N 293 
MET CB    HB2    sing N N 294 
MET CB    HB3    sing N N 295 
MET CG    SD     sing N N 296 
MET CG    HG2    sing N N 297 
MET CG    HG3    sing N N 298 
MET SD    CE     sing N N 299 
MET CE    HE1    sing N N 300 
MET CE    HE2    sing N N 301 
MET CE    HE3    sing N N 302 
MET OXT   HXT    sing N N 303 
PHE N     CA     sing N N 304 
PHE N     H      sing N N 305 
PHE N     H2     sing N N 306 
PHE CA    C      sing N N 307 
PHE CA    CB     sing N N 308 
PHE CA    HA     sing N N 309 
PHE C     O      doub N N 310 
PHE C     OXT    sing N N 311 
PHE CB    CG     sing N N 312 
PHE CB    HB2    sing N N 313 
PHE CB    HB3    sing N N 314 
PHE CG    CD1    doub Y N 315 
PHE CG    CD2    sing Y N 316 
PHE CD1   CE1    sing Y N 317 
PHE CD1   HD1    sing N N 318 
PHE CD2   CE2    doub Y N 319 
PHE CD2   HD2    sing N N 320 
PHE CE1   CZ     doub Y N 321 
PHE CE1   HE1    sing N N 322 
PHE CE2   CZ     sing Y N 323 
PHE CE2   HE2    sing N N 324 
PHE CZ    HZ     sing N N 325 
PHE OXT   HXT    sing N N 326 
PRO N     CA     sing N N 327 
PRO N     CD     sing N N 328 
PRO N     H      sing N N 329 
PRO CA    C      sing N N 330 
PRO CA    CB     sing N N 331 
PRO CA    HA     sing N N 332 
PRO C     O      doub N N 333 
PRO C     OXT    sing N N 334 
PRO CB    CG     sing N N 335 
PRO CB    HB2    sing N N 336 
PRO CB    HB3    sing N N 337 
PRO CG    CD     sing N N 338 
PRO CG    HG2    sing N N 339 
PRO CG    HG3    sing N N 340 
PRO CD    HD2    sing N N 341 
PRO CD    HD3    sing N N 342 
PRO OXT   HXT    sing N N 343 
SER N     CA     sing N N 344 
SER N     H      sing N N 345 
SER N     H2     sing N N 346 
SER CA    C      sing N N 347 
SER CA    CB     sing N N 348 
SER CA    HA     sing N N 349 
SER C     O      doub N N 350 
SER C     OXT    sing N N 351 
SER CB    OG     sing N N 352 
SER CB    HB2    sing N N 353 
SER CB    HB3    sing N N 354 
SER OG    HG     sing N N 355 
SER OXT   HXT    sing N N 356 
THR N     CA     sing N N 357 
THR N     H      sing N N 358 
THR N     H2     sing N N 359 
THR CA    C      sing N N 360 
THR CA    CB     sing N N 361 
THR CA    HA     sing N N 362 
THR C     O      doub N N 363 
THR C     OXT    sing N N 364 
THR CB    OG1    sing N N 365 
THR CB    CG2    sing N N 366 
THR CB    HB     sing N N 367 
THR OG1   HG1    sing N N 368 
THR CG2   HG21   sing N N 369 
THR CG2   HG22   sing N N 370 
THR CG2   HG23   sing N N 371 
THR OXT   HXT    sing N N 372 
TRP N     CA     sing N N 373 
TRP N     H      sing N N 374 
TRP N     H2     sing N N 375 
TRP CA    C      sing N N 376 
TRP CA    CB     sing N N 377 
TRP CA    HA     sing N N 378 
TRP C     O      doub N N 379 
TRP C     OXT    sing N N 380 
TRP CB    CG     sing N N 381 
TRP CB    HB2    sing N N 382 
TRP CB    HB3    sing N N 383 
TRP CG    CD1    doub Y N 384 
TRP CG    CD2    sing Y N 385 
TRP CD1   NE1    sing Y N 386 
TRP CD1   HD1    sing N N 387 
TRP CD2   CE2    doub Y N 388 
TRP CD2   CE3    sing Y N 389 
TRP NE1   CE2    sing Y N 390 
TRP NE1   HE1    sing N N 391 
TRP CE2   CZ2    sing Y N 392 
TRP CE3   CZ3    doub Y N 393 
TRP CE3   HE3    sing N N 394 
TRP CZ2   CH2    doub Y N 395 
TRP CZ2   HZ2    sing N N 396 
TRP CZ3   CH2    sing Y N 397 
TRP CZ3   HZ3    sing N N 398 
TRP CH2   HH2    sing N N 399 
TRP OXT   HXT    sing N N 400 
TYR N     CA     sing N N 401 
TYR N     H      sing N N 402 
TYR N     H2     sing N N 403 
TYR CA    C      sing N N 404 
TYR CA    CB     sing N N 405 
TYR CA    HA     sing N N 406 
TYR C     O      doub N N 407 
TYR C     OXT    sing N N 408 
TYR CB    CG     sing N N 409 
TYR CB    HB2    sing N N 410 
TYR CB    HB3    sing N N 411 
TYR CG    CD1    doub Y N 412 
TYR CG    CD2    sing Y N 413 
TYR CD1   CE1    sing Y N 414 
TYR CD1   HD1    sing N N 415 
TYR CD2   CE2    doub Y N 416 
TYR CD2   HD2    sing N N 417 
TYR CE1   CZ     doub Y N 418 
TYR CE1   HE1    sing N N 419 
TYR CE2   CZ     sing Y N 420 
TYR CE2   HE2    sing N N 421 
TYR CZ    OH     sing N N 422 
TYR OH    HH     sing N N 423 
TYR OXT   HXT    sing N N 424 
VAL N     CA     sing N N 425 
VAL N     H      sing N N 426 
VAL N     H2     sing N N 427 
VAL CA    C      sing N N 428 
VAL CA    CB     sing N N 429 
VAL CA    HA     sing N N 430 
VAL C     O      doub N N 431 
VAL C     OXT    sing N N 432 
VAL CB    CG1    sing N N 433 
VAL CB    CG2    sing N N 434 
VAL CB    HB     sing N N 435 
VAL CG1   HG11   sing N N 436 
VAL CG1   HG12   sing N N 437 
VAL CG1   HG13   sing N N 438 
VAL CG2   HG21   sing N N 439 
VAL CG2   HG22   sing N N 440 
VAL CG2   HG23   sing N N 441 
VAL OXT   HXT    sing N N 442 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4YUT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F1Z 
_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]   0.009955 
_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]   0.018981 
_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]   0.013981 
_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  
CA 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1 1   ? 10.489  27.108  42.030  1.00 76.96  ? 0   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 1   ? 9.895   25.912  41.459  1.00 78.76  ? 0   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 1   ? 10.424  24.615  42.051  1.00 75.09  ? 0   GLY A C     1 
ATOM   4    O  O     . GLY A 1 1   ? 11.607  24.283  41.908  1.00 67.58  ? 0   GLY A O     1 
ATOM   5    N  N     . MET A 1 2   ? 9.544   23.878  42.723  1.00 68.31  ? 1   MET A N     1 
ATOM   6    C  CA    . MET A 1 2   ? 9.880   22.586  43.298  1.00 60.29  ? 1   MET A CA    1 
ATOM   7    C  C     . MET A 1 2   ? 9.478   21.467  42.342  1.00 55.95  ? 1   MET A C     1 
ATOM   8    O  O     . MET A 1 2   ? 8.512   21.587  41.581  1.00 57.60  ? 1   MET A O     1 
ATOM   9    C  CB    . MET A 1 2   ? 9.190   22.394  44.649  1.00 67.21  ? 1   MET A CB    1 
ATOM   10   C  CG    . MET A 1 2   ? 10.086  22.600  45.867  1.00 70.27  ? 1   MET A CG    1 
ATOM   11   S  SD    . MET A 1 2   ? 9.352   21.947  47.387  1.00 74.96  ? 1   MET A SD    1 
ATOM   12   C  CE    . MET A 1 2   ? 8.931   23.465  48.245  1.00 66.92  ? 1   MET A CE    1 
ATOM   13   N  N     . LYS A 1 3   ? 10.233  20.376  42.391  1.00 46.28  ? 2   LYS A N     1 
ATOM   14   C  CA    . LYS A 1 3   ? 10.028  19.211  41.543  1.00 48.55  ? 2   LYS A CA    1 
ATOM   15   C  C     . LYS A 1 3   ? 9.830   17.973  42.407  1.00 54.53  ? 2   LYS A C     1 
ATOM   16   O  O     . LYS A 1 3   ? 10.485  17.816  43.447  1.00 50.03  ? 2   LYS A O     1 
ATOM   17   C  CB    . LYS A 1 3   ? 11.220  18.984  40.589  1.00 56.53  ? 2   LYS A CB    1 
ATOM   18   C  CG    . LYS A 1 3   ? 11.107  17.693  39.771  1.00 56.39  ? 2   LYS A CG    1 
ATOM   19   C  CD    . LYS A 1 3   ? 12.223  17.517  38.752  1.00 58.42  ? 2   LYS A CD    1 
ATOM   20   C  CE    . LYS A 1 3   ? 12.236  18.613  37.708  1.00 67.37  ? 2   LYS A CE    1 
ATOM   21   N  NZ    . LYS A 1 3   ? 13.206  18.296  36.613  1.00 69.52  ? 2   LYS A NZ    1 
ATOM   22   N  N     . ARG A 1 4   ? 8.938   17.089  41.960  1.00 45.42  ? 3   ARG A N     1 
ATOM   23   C  CA    . ARG A 1 4   ? 8.653   15.829  42.634  1.00 46.42  ? 3   ARG A CA    1 
ATOM   24   C  C     . ARG A 1 4   ? 8.652   14.695  41.620  1.00 44.23  ? 3   ARG A C     1 
ATOM   25   O  O     . ARG A 1 4   ? 7.913   14.741  40.630  1.00 50.07  ? 3   ARG A O     1 
ATOM   26   C  CB    . ARG A 1 4   ? 7.306   15.871  43.360  1.00 44.83  ? 3   ARG A CB    1 
ATOM   27   C  CG    . ARG A 1 4   ? 6.992   14.579  44.083  1.00 45.62  ? 3   ARG A CG    1 
ATOM   28   C  CD    . ARG A 1 4   ? 6.168   14.784  45.351  1.00 44.66  ? 3   ARG A CD    1 
ATOM   29   N  NE    . ARG A 1 4   ? 4.923   15.478  45.067  1.00 47.08  ? 3   ARG A NE    1 
ATOM   30   C  CZ    . ARG A 1 4   ? 4.557   16.626  45.621  1.00 48.35  ? 3   ARG A CZ    1 
ATOM   31   N  NH1   . ARG A 1 4   ? 5.237   17.158  46.620  1.00 44.45  ? 3   ARG A NH1   1 
ATOM   32   N  NH2   . ARG A 1 4   ? 3.470   17.244  45.172  1.00 46.18  ? 3   ARG A NH2   1 
ATOM   33   N  N     . LEU A 1 5   ? 9.451   13.668  41.886  1.00 41.88  ? 4   LEU A N     1 
ATOM   34   C  CA    . LEU A 1 5   ? 9.561   12.488  41.035  1.00 40.22  ? 4   LEU A CA    1 
ATOM   35   C  C     . LEU A 1 5   ? 9.043   11.258  41.767  1.00 41.92  ? 4   LEU A C     1 
ATOM   36   O  O     . LEU A 1 5   ? 9.341   11.057  42.948  1.00 43.98  ? 4   LEU A O     1 
ATOM   37   C  CB    . LEU A 1 5   ? 11.015  12.228  40.640  1.00 40.73  ? 4   LEU A CB    1 
ATOM   38   C  CG    . LEU A 1 5   ? 11.702  13.229  39.734  1.00 47.04  ? 4   LEU A CG    1 
ATOM   39   C  CD1   . LEU A 1 5   ? 13.065  12.687  39.361  1.00 50.29  ? 4   LEU A CD1   1 
ATOM   40   C  CD2   . LEU A 1 5   ? 10.846  13.434  38.506  1.00 45.49  ? 4   LEU A CD2   1 
ATOM   41   N  N     . THR A 1 6   ? 8.317   10.411  41.051  1.00 35.43  ? 5   THR A N     1 
ATOM   42   C  CA    . THR A 1 6   ? 7.945   9.090   41.532  1.00 36.88  ? 5   THR A CA    1 
ATOM   43   C  C     . THR A 1 6   ? 8.506   8.065   40.562  1.00 42.12  ? 5   THR A C     1 
ATOM   44   O  O     . THR A 1 6   ? 8.230   8.139   39.359  1.00 43.58  ? 5   THR A O     1 
ATOM   45   C  CB    . THR A 1 6   ? 6.424   8.949   41.632  1.00 38.90  ? 5   THR A CB    1 
ATOM   46   O  OG1   . THR A 1 6   ? 5.883   10.088  42.310  1.00 40.47  ? 5   THR A OG1   1 
ATOM   47   C  CG2   . THR A 1 6   ? 6.062   7.698   42.377  1.00 38.03  ? 5   THR A CG2   1 
ATOM   48   N  N     . TRP A 1 7   ? 9.278   7.104   41.069  1.00 38.56  ? 6   TRP A N     1 
ATOM   49   C  CA    . TRP A 1 7   ? 9.843   6.109   40.170  1.00 36.56  ? 6   TRP A CA    1 
ATOM   50   C  C     . TRP A 1 7   ? 9.881   4.745   40.831  1.00 36.58  ? 6   TRP A C     1 
ATOM   51   O  O     . TRP A 1 7   ? 9.770   4.607   42.051  1.00 38.61  ? 6   TRP A O     1 
ATOM   52   C  CB    . TRP A 1 7   ? 11.250  6.502   39.675  1.00 40.15  ? 6   TRP A CB    1 
ATOM   53   C  CG    . TRP A 1 7   ? 12.264  6.762   40.761  1.00 38.29  ? 6   TRP A CG    1 
ATOM   54   C  CD1   . TRP A 1 7   ? 12.570  7.959   41.345  1.00 36.17  ? 6   TRP A CD1   1 
ATOM   55   C  CD2   . TRP A 1 7   ? 13.058  5.776   41.418  1.00 30.59  ? 6   TRP A CD2   1 
ATOM   56   N  NE1   . TRP A 1 7   ? 13.545  7.778   42.305  1.00 37.16  ? 6   TRP A NE1   1 
ATOM   57   C  CE2   . TRP A 1 7   ? 13.855  6.445   42.374  1.00 35.86  ? 6   TRP A CE2   1 
ATOM   58   C  CE3   . TRP A 1 7   ? 13.171  4.390   41.293  1.00 34.27  ? 6   TRP A CE3   1 
ATOM   59   C  CZ2   . TRP A 1 7   ? 14.762  5.771   43.205  1.00 38.25  ? 6   TRP A CZ2   1 
ATOM   60   C  CZ3   . TRP A 1 7   ? 14.082  3.715   42.113  1.00 37.26  ? 6   TRP A CZ3   1 
ATOM   61   C  CH2   . TRP A 1 7   ? 14.863  4.410   43.058  1.00 38.30  ? 6   TRP A CH2   1 
ATOM   62   N  N     . ILE A 1 8   ? 9.992   3.725   39.986  1.00 36.39  ? 7   ILE A N     1 
ATOM   63   C  CA    . ILE A 1 8   ? 10.050  2.335   40.407  1.00 35.00  ? 7   ILE A CA    1 
ATOM   64   C  C     . ILE A 1 8   ? 11.228  1.699   39.689  1.00 42.09  ? 7   ILE A C     1 
ATOM   65   O  O     . ILE A 1 8   ? 11.609  2.134   38.598  1.00 38.44  ? 7   ILE A O     1 
ATOM   66   C  CB    . ILE A 1 8   ? 8.747   1.575   40.089  1.00 38.70  ? 7   ILE A CB    1 
ATOM   67   C  CG1   . ILE A 1 8   ? 8.407   1.718   38.602  1.00 41.71  ? 7   ILE A CG1   1 
ATOM   68   C  CG2   . ILE A 1 8   ? 7.594   2.130   40.916  1.00 41.57  ? 7   ILE A CG2   1 
ATOM   69   C  CD1   . ILE A 1 8   ? 7.449   0.664   38.089  1.00 37.75  ? 7   ILE A CD1   1 
ATOM   70   N  N     . SER A 1 9   ? 11.816  0.675   40.311  1.00 37.43  ? 8   SER A N     1 
ATOM   71   C  CA    A SER A 1 9   ? 12.957  -0.025  39.751  0.00 44.60  ? 8   SER A CA    1 
ATOM   72   C  CA    B SER A 1 9   ? 12.908  -0.056  39.673  1.00 44.96  ? 8   SER A CA    1 
ATOM   73   C  C     . SER A 1 9   ? 12.907  -1.484  40.188  1.00 47.89  ? 8   SER A C     1 
ATOM   74   O  O     . SER A 1 9   ? 12.090  -1.869  41.022  1.00 42.46  ? 8   SER A O     1 
ATOM   75   C  CB    A SER A 1 9   ? 14.269  0.634   40.183  0.00 42.33  ? 8   SER A CB    1 
ATOM   76   C  CB    B SER A 1 9   ? 14.287  0.572   39.941  1.00 41.64  ? 8   SER A CB    1 
ATOM   77   O  OG    A SER A 1 9   ? 15.332  -0.288  40.109  0.00 45.92  ? 8   SER A OG    1 
ATOM   78   O  OG    B SER A 1 9   ? 14.623  0.509   41.312  1.00 44.59  ? 8   SER A OG    1 
ATOM   79   N  N     . LYS A 1 10  ? 13.831  -2.274  39.654  1.00 45.31  ? 9   LYS A N     1 
ATOM   80   C  CA    . LYS A 1 10  ? 14.021  -3.667  40.027  1.00 46.86  ? 9   LYS A CA    1 
ATOM   81   C  C     . LYS A 1 10  ? 15.405  -3.814  40.632  1.00 46.30  ? 9   LYS A C     1 
ATOM   82   O  O     . LYS A 1 10  ? 16.366  -3.213  40.139  1.00 44.80  ? 9   LYS A O     1 
ATOM   83   C  CB    . LYS A 1 10  ? 13.889  -4.597  38.809  1.00 55.41  ? 9   LYS A CB    1 
ATOM   84   C  CG    . LYS A 1 10  ? 13.500  -6.036  39.118  1.00 66.39  ? 9   LYS A CG    1 
ATOM   85   C  CD    . LYS A 1 10  ? 12.548  -6.604  38.061  1.00 72.95  ? 9   LYS A CD    1 
ATOM   86   C  CE    . LYS A 1 10  ? 12.813  -8.100  37.820  1.00 80.25  ? 9   LYS A CE    1 
ATOM   87   N  NZ    . LYS A 1 10  ? 11.969  -9.019  38.657  1.00 75.97  ? 9   LYS A NZ    1 
ATOM   88   N  N     . PHE A 1 11  ? 15.510  -4.608  41.697  1.00 49.14  ? 10  PHE A N     1 
ATOM   89   C  CA    . PHE A 1 11  ? 16.832  -4.951  42.214  1.00 41.31  ? 10  PHE A CA    1 
ATOM   90   C  C     . PHE A 1 11  ? 17.668  -5.529  41.076  1.00 49.02  ? 10  PHE A C     1 
ATOM   91   O  O     . PHE A 1 11  ? 17.200  -6.396  40.331  1.00 51.48  ? 10  PHE A O     1 
ATOM   92   C  CB    . PHE A 1 11  ? 16.754  -5.980  43.349  1.00 43.39  ? 10  PHE A CB    1 
ATOM   93   C  CG    . PHE A 1 11  ? 16.083  -5.497  44.626  1.00 44.47  ? 10  PHE A CG    1 
ATOM   94   C  CD1   . PHE A 1 11  ? 15.406  -4.289  44.702  1.00 38.81  ? 10  PHE A CD1   1 
ATOM   95   C  CD2   . PHE A 1 11  ? 16.190  -6.269  45.780  1.00 47.70  ? 10  PHE A CD2   1 
ATOM   96   C  CE1   . PHE A 1 11  ? 14.804  -3.889  45.898  1.00 45.98  ? 10  PHE A CE1   1 
ATOM   97   C  CE2   . PHE A 1 11  ? 15.605  -5.875  46.974  1.00 47.60  ? 10  PHE A CE2   1 
ATOM   98   C  CZ    . PHE A 1 11  ? 14.906  -4.682  47.034  1.00 42.01  ? 10  PHE A CZ    1 
ATOM   99   N  N     . SER A 1 12  ? 18.896  -5.033  40.921  1.00 47.94  ? 11  SER A N     1 
ATOM   100  C  CA    . SER A 1 12  ? 19.763  -5.626  39.905  1.00 55.27  ? 11  SER A CA    1 
ATOM   101  C  C     . SER A 1 12  ? 20.320  -6.980  40.327  1.00 57.76  ? 11  SER A C     1 
ATOM   102  O  O     . SER A 1 12  ? 20.884  -7.684  39.485  1.00 64.26  ? 11  SER A O     1 
ATOM   103  C  CB    . SER A 1 12  ? 20.921  -4.689  39.571  1.00 55.16  ? 11  SER A CB    1 
ATOM   104  O  OG    . SER A 1 12  ? 21.923  -4.761  40.576  1.00 60.56  ? 11  SER A OG    1 
ATOM   105  N  N     . ARG A 1 13  ? 20.168  -7.360  41.600  1.00 54.64  ? 12  ARG A N     1 
ATOM   106  C  CA    . ARG A 1 13  ? 20.698  -8.584  42.189  1.00 55.61  ? 12  ARG A CA    1 
ATOM   107  C  C     . ARG A 1 13  ? 20.041  -8.735  43.564  1.00 65.60  ? 12  ARG A C     1 
ATOM   108  O  O     . ARG A 1 13  ? 19.361  -7.797  44.002  1.00 57.39  ? 12  ARG A O     1 
ATOM   109  C  CB    . ARG A 1 13  ? 22.226  -8.500  42.281  1.00 62.42  ? 12  ARG A CB    1 
ATOM   110  C  CG    . ARG A 1 13  ? 22.744  -7.163  42.765  1.00 65.62  ? 12  ARG A CG    1 
ATOM   111  C  CD    . ARG A 1 13  ? 23.863  -7.359  43.773  1.00 69.53  ? 12  ARG A CD    1 
ATOM   112  N  NE    . ARG A 1 13  ? 24.504  -6.100  44.133  1.00 66.92  ? 12  ARG A NE    1 
ATOM   113  C  CZ    . ARG A 1 13  ? 24.893  -5.796  45.362  1.00 64.78  ? 12  ARG A CZ    1 
ATOM   114  N  NH1   . ARG A 1 13  ? 24.680  -6.619  46.375  1.00 66.53  ? 12  ARG A NH1   1 
ATOM   115  N  NH2   . ARG A 1 13  ? 25.494  -4.629  45.584  1.00 70.35  ? 12  ARG A NH2   1 
ATOM   116  N  N     . PRO A 1 14  ? 20.191  -9.855  44.284  1.00 66.60  ? 13  PRO A N     1 
ATOM   117  C  CA    . PRO A 1 14  ? 19.555  -9.938  45.605  1.00 63.14  ? 13  PRO A CA    1 
ATOM   118  C  C     . PRO A 1 14  ? 20.223  -9.013  46.615  1.00 66.00  ? 13  PRO A C     1 
ATOM   119  O  O     . PRO A 1 14  ? 21.448  -8.851  46.635  1.00 60.45  ? 13  PRO A O     1 
ATOM   120  C  CB    . PRO A 1 14  ? 19.718  -11.410 45.984  1.00 62.33  ? 13  PRO A CB    1 
ATOM   121  C  CG    . PRO A 1 14  ? 20.967  -11.837 45.319  1.00 68.69  ? 13  PRO A CG    1 
ATOM   122  C  CD    . PRO A 1 14  ? 21.176  -10.942 44.103  1.00 66.02  ? 13  PRO A CD    1 
ATOM   123  N  N     . LEU A 1 15  ? 19.392  -8.390  47.451  1.00 56.09  ? 14  LEU A N     1 
ATOM   124  C  CA    . LEU A 1 15  ? 19.815  -7.309  48.327  1.00 51.33  ? 14  LEU A CA    1 
ATOM   125  C  C     . LEU A 1 15  ? 19.312  -7.628  49.725  1.00 56.90  ? 14  LEU A C     1 
ATOM   126  O  O     . LEU A 1 15  ? 18.122  -7.911  49.908  1.00 51.59  ? 14  LEU A O     1 
ATOM   127  C  CB    . LEU A 1 15  ? 19.244  -5.965  47.849  1.00 47.69  ? 14  LEU A CB    1 
ATOM   128  C  CG    . LEU A 1 15  ? 19.992  -5.143  46.799  1.00 53.62  ? 14  LEU A CG    1 
ATOM   129  C  CD1   . LEU A 1 15  ? 19.438  -3.733  46.739  1.00 45.80  ? 14  LEU A CD1   1 
ATOM   130  C  CD2   . LEU A 1 15  ? 21.524  -5.144  46.976  1.00 54.16  ? 14  LEU A CD2   1 
ATOM   131  N  N     . SER A 1 16  ? 20.206  -7.594  50.704  1.00 52.51  ? 15  SER A N     1 
ATOM   132  C  CA    . SER A 1 16  ? 19.810  -7.956  52.056  1.00 49.70  ? 15  SER A CA    1 
ATOM   133  C  C     . SER A 1 16  ? 19.072  -6.804  52.748  1.00 50.30  ? 15  SER A C     1 
ATOM   134  O  O     . SER A 1 16  ? 19.118  -5.643  52.318  1.00 47.59  ? 15  SER A O     1 
ATOM   135  C  CB    . SER A 1 16  ? 21.042  -8.363  52.866  1.00 57.05  ? 15  SER A CB    1 
ATOM   136  O  OG    . SER A 1 16  ? 21.831  -7.231  53.157  1.00 50.66  ? 15  SER A OG    1 
ATOM   137  N  N     . GLY A 1 17  ? 18.378  -7.145  53.838  1.00 52.01  ? 16  GLY A N     1 
ATOM   138  C  CA    . GLY A 1 17  ? 17.742  -6.118  54.647  1.00 47.63  ? 16  GLY A CA    1 
ATOM   139  C  C     . GLY A 1 17  ? 18.726  -5.059  55.112  1.00 54.51  ? 16  GLY A C     1 
ATOM   140  O  O     . GLY A 1 17  ? 18.411  -3.864  55.125  1.00 46.24  ? 16  GLY A O     1 
ATOM   141  N  N     . ASP A 1 18  ? 19.945  -5.479  55.474  1.00 50.88  ? 17  ASP A N     1 
ATOM   142  C  CA    . ASP A 1 18  ? 20.948  -4.517  55.923  1.00 48.72  ? 17  ASP A CA    1 
ATOM   143  C  C     . ASP A 1 18  ? 21.476  -3.676  54.767  1.00 43.95  ? 17  ASP A C     1 
ATOM   144  O  O     . ASP A 1 18  ? 21.842  -2.515  54.969  1.00 52.46  ? 17  ASP A O     1 
ATOM   145  C  CB    . ASP A 1 18  ? 22.098  -5.238  56.635  1.00 50.73  ? 17  ASP A CB    1 
ATOM   146  C  CG    . ASP A 1 18  ? 21.737  -5.641  58.065  1.00 66.50  ? 17  ASP A CG    1 
ATOM   147  O  OD1   . ASP A 1 18  ? 21.403  -4.752  58.884  1.00 64.77  ? 17  ASP A OD1   1 
ATOM   148  O  OD2   . ASP A 1 18  ? 21.811  -6.848  58.377  1.00 74.90  ? 17  ASP A OD2   1 
ATOM   149  N  N     . GLU A 1 19  ? 21.531  -4.233  53.554  1.00 46.73  ? 18  GLU A N     1 
ATOM   150  C  CA    . GLU A 1 19  ? 21.942  -3.437  52.399  1.00 40.21  ? 18  GLU A CA    1 
ATOM   151  C  C     . GLU A 1 19  ? 20.871  -2.419  52.015  1.00 43.83  ? 18  GLU A C     1 
ATOM   152  O  O     . GLU A 1 19  ? 21.186  -1.275  51.653  1.00 39.62  ? 18  GLU A O     1 
ATOM   153  C  CB    . GLU A 1 19  ? 22.245  -4.345  51.209  1.00 46.51  ? 18  GLU A CB    1 
ATOM   154  C  CG    . GLU A 1 19  ? 23.698  -4.786  51.094  1.00 56.59  ? 18  GLU A CG    1 
ATOM   155  C  CD    . GLU A 1 19  ? 23.848  -6.062  50.278  1.00 70.10  ? 18  GLU A CD    1 
ATOM   156  O  OE1   . GLU A 1 19  ? 23.077  -7.025  50.512  1.00 67.77  ? 18  GLU A OE1   1 
ATOM   157  O  OE2   . GLU A 1 19  ? 24.724  -6.087  49.375  1.00 79.22  ? 18  GLU A OE2   1 
ATOM   158  N  N     . ILE A 1 20  ? 19.600  -2.821  52.060  1.00 41.24  ? 19  ILE A N     1 
ATOM   159  C  CA    . ILE A 1 20  ? 18.525  -1.868  51.792  1.00 38.21  ? 19  ILE A CA    1 
ATOM   160  C  C     . ILE A 1 20  ? 18.562  -0.747  52.822  1.00 38.13  ? 19  ILE A C     1 
ATOM   161  O  O     . ILE A 1 20  ? 18.443  0.438   52.486  1.00 39.62  ? 19  ILE A O     1 
ATOM   162  C  CB    . ILE A 1 20  ? 17.176  -2.605  51.783  1.00 43.99  ? 19  ILE A CB    1 
ATOM   163  C  CG1   . ILE A 1 20  ? 17.116  -3.525  50.560  1.00 38.78  ? 19  ILE A CG1   1 
ATOM   164  C  CG2   . ILE A 1 20  ? 16.001  -1.600  51.787  1.00 38.58  ? 19  ILE A CG2   1 
ATOM   165  C  CD1   . ILE A 1 20  ? 15.907  -4.420  50.569  1.00 52.65  ? 19  ILE A CD1   1 
ATOM   166  N  N     . GLU A 1 21  ? 18.766  -1.108  54.091  1.00 41.17  ? 20  GLU A N     1 
ATOM   167  C  CA    . GLU A 1 21  ? 18.896  -0.116  55.154  1.00 39.54  ? 20  GLU A CA    1 
ATOM   168  C  C     . GLU A 1 21  ? 20.016  0.864   54.858  1.00 43.83  ? 20  GLU A C     1 
ATOM   169  O  O     . GLU A 1 21  ? 19.869  2.073   55.079  1.00 36.58  ? 20  GLU A O     1 
ATOM   170  C  CB    . GLU A 1 21  ? 19.154  -0.825  56.481  1.00 47.09  ? 20  GLU A CB    1 
ATOM   171  C  CG    . GLU A 1 21  ? 18.603  -0.126  57.712  1.00 54.31  ? 20  GLU A CG    1 
ATOM   172  C  CD    . GLU A 1 21  ? 19.231  -0.652  59.008  1.00 73.71  ? 20  GLU A CD    1 
ATOM   173  O  OE1   . GLU A 1 21  ? 19.866  -1.737  58.980  1.00 72.38  ? 20  GLU A OE1   1 
ATOM   174  O  OE2   . GLU A 1 21  ? 19.071  0.010   60.061  1.00 77.50  ? 20  GLU A OE2   1 
ATOM   175  N  N     . ALA A 1 22  ? 21.145  0.364   54.345  1.00 43.49  ? 21  ALA A N     1 
ATOM   176  C  CA    . ALA A 1 22  ? 22.267  1.242   54.041  1.00 42.27  ? 21  ALA A CA    1 
ATOM   177  C  C     . ALA A 1 22  ? 21.935  2.175   52.892  1.00 47.19  ? 21  ALA A C     1 
ATOM   178  O  O     . ALA A 1 22  ? 22.354  3.337   52.894  1.00 44.74  ? 21  ALA A O     1 
ATOM   179  C  CB    . ALA A 1 22  ? 23.525  0.427   53.710  1.00 46.18  ? 21  ALA A CB    1 
ATOM   180  N  N     . ILE A 1 23  ? 21.213  1.684   51.883  1.00 40.42  ? 22  ILE A N     1 
ATOM   181  C  CA    . ILE A 1 23  ? 20.772  2.577   50.813  1.00 39.67  ? 22  ILE A CA    1 
ATOM   182  C  C     . ILE A 1 23  ? 19.979  3.735   51.401  1.00 36.52  ? 22  ILE A C     1 
ATOM   183  O  O     . ILE A 1 23  ? 20.247  4.906   51.105  1.00 40.33  ? 22  ILE A O     1 
ATOM   184  C  CB    . ILE A 1 23  ? 19.963  1.799   49.754  1.00 43.59  ? 22  ILE A CB    1 
ATOM   185  C  CG1   . ILE A 1 23  ? 20.882  0.832   48.994  1.00 49.19  ? 22  ILE A CG1   1 
ATOM   186  C  CG2   . ILE A 1 23  ? 19.276  2.747   48.770  1.00 40.35  ? 22  ILE A CG2   1 
ATOM   187  C  CD1   . ILE A 1 23  ? 20.115  -0.187  48.147  1.00 48.23  ? 22  ILE A CD1   1 
ATOM   188  N  N     . GLY A 1 24  ? 19.008  3.427   52.270  1.00 40.67  ? 23  GLY A N     1 
ATOM   189  C  CA    . GLY A 1 24  ? 18.164  4.481   52.820  1.00 38.74  ? 23  GLY A CA    1 
ATOM   190  C  C     . GLY A 1 24  ? 18.948  5.482   53.651  1.00 41.92  ? 23  GLY A C     1 
ATOM   191  O  O     . GLY A 1 24  ? 18.616  6.673   53.688  1.00 38.84  ? 23  GLY A O     1 
ATOM   192  N  N     . ARG A 1 25  ? 19.994  5.004   54.331  1.00 35.69  ? 24  ARG A N     1 
ATOM   193  C  CA    . ARG A 1 25  ? 20.836  5.855   55.176  1.00 41.59  ? 24  ARG A CA    1 
ATOM   194  C  C     . ARG A 1 25  ? 21.623  6.879   54.370  1.00 36.52  ? 24  ARG A C     1 
ATOM   195  O  O     . ARG A 1 25  ? 21.599  8.075   54.690  1.00 37.76  ? 24  ARG A O     1 
ATOM   196  C  CB    . ARG A 1 25  ? 21.800  4.986   55.971  1.00 43.73  ? 24  ARG A CB    1 
ATOM   197  C  CG    . ARG A 1 25  ? 21.320  4.618   57.299  1.00 48.36  ? 24  ARG A CG    1 
ATOM   198  C  CD    . ARG A 1 25  ? 22.498  4.202   58.155  1.00 56.58  ? 24  ARG A CD    1 
ATOM   199  N  NE    . ARG A 1 25  ? 22.928  5.335   58.948  1.00 45.54  ? 24  ARG A NE    1 
ATOM   200  C  CZ    . ARG A 1 25  ? 22.273  5.734   60.021  1.00 40.43  ? 24  ARG A CZ    1 
ATOM   201  N  NH1   . ARG A 1 25  ? 21.128  5.167   60.370  1.00 35.32  ? 24  ARG A NH1   1 
ATOM   202  N  NH2   . ARG A 1 25  ? 22.747  6.755   60.726  1.00 34.27  ? 24  ARG A NH2   1 
ATOM   203  N  N     . ILE A 1 26  ? 22.369  6.438   53.348  1.00 41.03  ? 25  ILE A N     1 
ATOM   204  C  CA    . ILE A 1 26  ? 23.115  7.431   52.580  1.00 41.90  ? 25  ILE A CA    1 
ATOM   205  C  C     . ILE A 1 26  ? 22.158  8.328   51.816  1.00 37.73  ? 25  ILE A C     1 
ATOM   206  O  O     . ILE A 1 26  ? 22.389  9.540   51.705  1.00 42.93  ? 25  ILE A O     1 
ATOM   207  C  CB    . ILE A 1 26  ? 24.177  6.813   51.636  1.00 50.18  ? 25  ILE A CB    1 
ATOM   208  C  CG1   . ILE A 1 26  ? 25.140  5.860   52.342  1.00 60.32  ? 25  ILE A CG1   1 
ATOM   209  C  CG2   . ILE A 1 26  ? 25.056  7.896   51.011  1.00 52.10  ? 25  ILE A CG2   1 
ATOM   210  C  CD1   . ILE A 1 26  ? 24.871  4.410   52.111  1.00 55.59  ? 25  ILE A CD1   1 
ATOM   211  N  N     . SER A 1 27  ? 21.049  7.766   51.304  1.00 41.90  ? 26  SER A N     1 
ATOM   212  C  CA    . SER A 1 27  ? 20.050  8.606   50.649  1.00 39.77  ? 26  SER A CA    1 
ATOM   213  C  C     . SER A 1 27  ? 19.585  9.706   51.581  1.00 35.78  ? 26  SER A C     1 
ATOM   214  O  O     . SER A 1 27  ? 19.466  10.871  51.175  1.00 38.02  ? 26  SER A O     1 
ATOM   215  C  CB    . SER A 1 27  ? 18.853  7.774   50.184  1.00 39.48  ? 26  SER A CB    1 
ATOM   216  O  OG    . SER A 1 27  ? 19.287  6.732   49.322  1.00 44.90  ? 26  SER A OG    1 
ATOM   217  N  N     . SER A 1 28  ? 19.330  9.356   52.845  1.00 36.26  ? 27  SER A N     1 
ATOM   218  C  CA    . SER A 1 28  ? 18.852  10.358  53.791  1.00 35.51  ? 27  SER A CA    1 
ATOM   219  C  C     . SER A 1 28  ? 19.914  11.423  54.025  1.00 35.32  ? 27  SER A C     1 
ATOM   220  O  O     . SER A 1 28  ? 19.620  12.627  54.032  1.00 34.10  ? 27  SER A O     1 
ATOM   221  C  CB    . SER A 1 28  ? 18.453  9.687   55.109  1.00 33.06  ? 27  SER A CB    1 
ATOM   222  O  OG    . SER A 1 28  ? 17.941  10.660  56.016  1.00 34.70  ? 27  SER A OG    1 
ATOM   223  N  N     . GLN A 1 29  ? 21.161  10.990  54.191  1.00 38.53  ? 28  GLN A N     1 
ATOM   224  C  CA    A GLN A 1 29  ? 22.246  11.928  54.463  0.30 39.95  ? 28  GLN A CA    1 
ATOM   225  C  CA    B GLN A 1 29  ? 22.245  11.924  54.466  0.70 40.06  ? 28  GLN A CA    1 
ATOM   226  C  C     . GLN A 1 29  ? 22.460  12.879  53.292  1.00 36.82  ? 28  GLN A C     1 
ATOM   227  O  O     . GLN A 1 29  ? 22.532  14.102  53.476  1.00 35.23  ? 28  GLN A O     1 
ATOM   228  C  CB    A GLN A 1 29  ? 23.530  11.163  54.783  0.30 40.40  ? 28  GLN A CB    1 
ATOM   229  C  CB    B GLN A 1 29  ? 23.505  11.121  54.798  0.70 40.39  ? 28  GLN A CB    1 
ATOM   230  C  CG    A GLN A 1 29  ? 24.619  12.034  55.386  0.30 42.63  ? 28  GLN A CG    1 
ATOM   231  C  CG    B GLN A 1 29  ? 24.794  11.905  54.829  0.70 42.20  ? 28  GLN A CG    1 
ATOM   232  C  CD    A GLN A 1 29  ? 25.996  11.413  55.274  0.30 46.44  ? 28  GLN A CD    1 
ATOM   233  C  CD    B GLN A 1 29  ? 25.911  11.111  55.480  0.70 47.16  ? 28  GLN A CD    1 
ATOM   234  O  OE1   A GLN A 1 29  ? 26.541  11.271  54.179  0.30 45.66  ? 28  GLN A OE1   1 
ATOM   235  O  OE1   B GLN A 1 29  ? 26.074  9.908   55.231  0.70 49.84  ? 28  GLN A OE1   1 
ATOM   236  N  NE2   A GLN A 1 29  ? 26.570  11.043  56.414  0.30 44.25  ? 28  GLN A NE2   1 
ATOM   237  N  NE2   B GLN A 1 29  ? 26.666  11.771  56.349  0.70 44.54  ? 28  GLN A NE2   1 
ATOM   238  N  N     . LYS A 1 30  ? 22.547  12.334  52.071  1.00 34.30  ? 29  LYS A N     1 
ATOM   239  C  CA    . LYS A 1 30  ? 22.680  13.174  50.874  1.00 36.27  ? 29  LYS A CA    1 
ATOM   240  C  C     . LYS A 1 30  ? 21.477  14.090  50.670  1.00 37.56  ? 29  LYS A C     1 
ATOM   241  O  O     . LYS A 1 30  ? 21.630  15.269  50.331  1.00 38.27  ? 29  LYS A O     1 
ATOM   242  C  CB    . LYS A 1 30  ? 22.875  12.305  49.632  1.00 35.73  ? 29  LYS A CB    1 
ATOM   243  C  CG    . LYS A 1 30  ? 24.086  11.380  49.643  1.00 50.00  ? 29  LYS A CG    1 
ATOM   244  C  CD    . LYS A 1 30  ? 25.362  12.114  50.010  1.00 54.22  ? 29  LYS A CD    1 
ATOM   245  C  CE    . LYS A 1 30  ? 26.229  11.318  50.993  1.00 63.36  ? 29  LYS A CE    1 
ATOM   246  N  NZ    . LYS A 1 30  ? 27.031  12.151  51.959  1.00 54.32  ? 29  LYS A NZ    1 
ATOM   247  N  N     . ASN A 1 31  ? 20.260  13.566  50.834  1.00 38.39  ? 30  ASN A N     1 
ATOM   248  C  CA    . ASN A 1 31  ? 19.107  14.430  50.602  1.00 39.11  ? 30  ASN A CA    1 
ATOM   249  C  C     . ASN A 1 31  ? 19.026  15.540  51.639  1.00 37.98  ? 30  ASN A C     1 
ATOM   250  O  O     . ASN A 1 31  ? 18.594  16.657  51.319  1.00 35.87  ? 30  ASN A O     1 
ATOM   251  C  CB    . ASN A 1 31  ? 17.811  13.611  50.570  1.00 38.90  ? 30  ASN A CB    1 
ATOM   252  C  CG    . ASN A 1 31  ? 17.714  12.722  49.335  1.00 36.24  ? 30  ASN A CG    1 
ATOM   253  O  OD1   . ASN A 1 31  ? 18.521  12.839  48.408  1.00 39.49  ? 30  ASN A OD1   1 
ATOM   254  N  ND2   . ASN A 1 31  ? 16.716  11.828  49.311  1.00 32.61  ? 30  ASN A ND2   1 
ATOM   255  N  N     . GLN A 1 32  ? 19.414  15.253  52.887  1.00 35.82  ? 31  GLN A N     1 
ATOM   256  C  CA    A GLN A 1 32  ? 19.427  16.293  53.914  0.62 38.17  ? 31  GLN A CA    1 
ATOM   257  C  CA    B GLN A 1 32  ? 19.409  16.298  53.906  0.38 37.46  ? 31  GLN A CA    1 
ATOM   258  C  C     . GLN A 1 32  ? 20.317  17.455  53.505  1.00 38.51  ? 31  GLN A C     1 
ATOM   259  O  O     . GLN A 1 32  ? 19.975  18.623  53.728  1.00 37.76  ? 31  GLN A O     1 
ATOM   260  C  CB    A GLN A 1 32  ? 19.870  15.689  55.248  0.62 37.18  ? 31  GLN A CB    1 
ATOM   261  C  CB    B GLN A 1 32  ? 19.860  15.739  55.253  0.38 37.54  ? 31  GLN A CB    1 
ATOM   262  C  CG    A GLN A 1 32  ? 19.619  16.536  56.500  0.62 40.14  ? 31  GLN A CG    1 
ATOM   263  C  CG    B GLN A 1 32  ? 19.677  16.727  56.395  0.38 40.15  ? 31  GLN A CG    1 
ATOM   264  C  CD    A GLN A 1 32  ? 20.664  17.638  56.675  0.62 39.74  ? 31  GLN A CD    1 
ATOM   265  C  CD    B GLN A 1 32  ? 20.039  16.145  57.748  0.38 40.01  ? 31  GLN A CD    1 
ATOM   266  O  OE1   A GLN A 1 32  ? 21.814  17.478  56.268  0.62 40.92  ? 31  GLN A OE1   1 
ATOM   267  O  OE1   B GLN A 1 32  ? 20.410  14.982  57.855  0.38 36.93  ? 31  GLN A OE1   1 
ATOM   268  N  NE2   A GLN A 1 32  ? 20.277  18.742  57.304  0.62 44.64  ? 31  GLN A NE2   1 
ATOM   269  N  NE2   B GLN A 1 32  ? 19.857  16.935  58.798  0.38 46.07  ? 31  GLN A NE2   1 
ATOM   270  N  N     . GLN A 1 33  ? 21.481  17.146  52.923  1.00 42.23  ? 32  GLN A N     1 
ATOM   271  C  CA    . GLN A 1 33  ? 22.383  18.187  52.457  1.00 49.27  ? 32  GLN A CA    1 
ATOM   272  C  C     . GLN A 1 33  ? 21.796  18.914  51.255  1.00 47.03  ? 32  GLN A C     1 
ATOM   273  O  O     . GLN A 1 33  ? 22.080  20.097  51.046  1.00 49.30  ? 32  GLN A O     1 
ATOM   274  C  CB    . GLN A 1 33  ? 23.735  17.574  52.091  1.00 46.26  ? 32  GLN A CB    1 
ATOM   275  C  CG    . GLN A 1 33  ? 24.590  17.184  53.295  1.00 50.22  ? 32  GLN A CG    1 
ATOM   276  C  CD    . GLN A 1 33  ? 24.798  18.325  54.259  1.00 48.43  ? 32  GLN A CD    1 
ATOM   277  O  OE1   . GLN A 1 33  ? 24.189  18.366  55.333  1.00 57.33  ? 32  GLN A OE1   1 
ATOM   278  N  NE2   . GLN A 1 33  ? 25.639  19.275  53.875  1.00 56.01  ? 32  GLN A NE2   1 
ATOM   279  N  N     . ALA A 1 34  ? 20.975  18.228  50.462  1.00 43.93  ? 33  ALA A N     1 
ATOM   280  C  CA    . ALA A 1 34  ? 20.381  18.822  49.273  1.00 39.15  ? 33  ALA A CA    1 
ATOM   281  C  C     . ALA A 1 34  ? 19.056  19.496  49.562  1.00 48.94  ? 33  ALA A C     1 
ATOM   282  O  O     . ALA A 1 34  ? 18.488  20.124  48.664  1.00 49.73  ? 33  ALA A O     1 
ATOM   283  C  CB    . ALA A 1 34  ? 20.197  17.757  48.188  1.00 45.82  ? 33  ALA A CB    1 
ATOM   284  N  N     . ASN A 1 35  ? 18.559  19.389  50.796  1.00 51.06  ? 34  ASN A N     1 
ATOM   285  C  CA    . ASN A 1 35  ? 17.250  19.918  51.171  1.00 47.11  ? 34  ASN A CA    1 
ATOM   286  C  C     . ASN A 1 35  ? 16.146  19.195  50.401  1.00 44.56  ? 34  ASN A C     1 
ATOM   287  O  O     . ASN A 1 35  ? 15.139  19.790  50.004  1.00 44.27  ? 34  ASN A O     1 
ATOM   288  C  CB    . ASN A 1 35  ? 17.188  21.433  50.943  1.00 54.78  ? 34  ASN A CB    1 
ATOM   289  C  CG    . ASN A 1 35  ? 16.303  22.132  51.938  1.00 66.56  ? 34  ASN A CG    1 
ATOM   290  O  OD1   . ASN A 1 35  ? 15.196  22.574  51.615  1.00 66.32  ? 34  ASN A OD1   1 
ATOM   291  N  ND2   . ASN A 1 35  ? 16.794  22.246  53.173  1.00 63.70  ? 34  ASN A ND2   1 
ATOM   292  N  N     . VAL A 1 36  ? 16.358  17.901  50.169  1.00 44.11  ? 35  VAL A N     1 
ATOM   293  C  CA    . VAL A 1 36  ? 15.463  17.050  49.393  1.00 37.05  ? 35  VAL A CA    1 
ATOM   294  C  C     . VAL A 1 36  ? 14.779  16.105  50.377  1.00 38.99  ? 35  VAL A C     1 
ATOM   295  O  O     . VAL A 1 36  ? 15.407  15.653  51.341  1.00 35.33  ? 35  VAL A O     1 
ATOM   296  C  CB    . VAL A 1 36  ? 16.253  16.269  48.321  1.00 36.54  ? 35  VAL A CB    1 
ATOM   297  C  CG1   . VAL A 1 36  ? 15.550  14.966  47.937  1.00 41.80  ? 35  VAL A CG1   1 
ATOM   298  C  CG2   . VAL A 1 36  ? 16.577  17.155  47.097  1.00 40.70  ? 35  VAL A CG2   1 
ATOM   299  N  N     . THR A 1 37  ? 13.494  15.822  50.158  1.00 37.75  ? 36  THR A N     1 
ATOM   300  C  CA    . THR A 1 37  ? 12.756  14.920  51.039  1.00 38.10  ? 36  THR A CA    1 
ATOM   301  C  C     . THR A 1 37  ? 12.101  13.813  50.217  1.00 37.17  ? 36  THR A C     1 
ATOM   302  O  O     . THR A 1 37  ? 12.016  13.891  48.982  1.00 34.70  ? 36  THR A O     1 
ATOM   303  C  CB    . THR A 1 37  ? 11.701  15.675  51.874  1.00 37.85  ? 36  THR A CB    1 
ATOM   304  O  OG1   . THR A 1 37  ? 10.884  16.496  51.031  1.00 36.95  ? 36  THR A OG1   1 
ATOM   305  C  CG2   . THR A 1 37  ? 12.366  16.546  52.939  1.00 34.78  ? 36  THR A CG2   1 
ATOM   306  N  N     . GLY A 1 38  ? 11.663  12.762  50.897  1.00 31.89  ? 37  GLY A N     1 
ATOM   307  C  CA    . GLY A 1 38  ? 10.962  11.711  50.190  1.00 35.52  ? 37  GLY A CA    1 
ATOM   308  C  C     . GLY A 1 38  ? 10.879  10.417  50.972  1.00 34.37  ? 37  GLY A C     1 
ATOM   309  O  O     . GLY A 1 38  ? 11.133  10.369  52.174  1.00 36.17  ? 37  GLY A O     1 
ATOM   310  N  N     . VAL A 1 39  ? 10.477  9.373   50.254  1.00 33.36  ? 38  VAL A N     1 
ATOM   311  C  CA    . VAL A 1 39  ? 10.242  8.060   50.835  1.00 31.86  ? 38  VAL A CA    1 
ATOM   312  C  C     . VAL A 1 39  ? 10.700  7.002   49.849  1.00 31.80  ? 38  VAL A C     1 
ATOM   313  O  O     . VAL A 1 39  ? 10.558  7.162   48.629  1.00 37.28  ? 38  VAL A O     1 
ATOM   314  C  CB    . VAL A 1 39  ? 8.763   7.847   51.234  1.00 30.15  ? 38  VAL A CB    1 
ATOM   315  C  CG1   . VAL A 1 39  ? 7.833   7.776   50.004  1.00 31.55  ? 38  VAL A CG1   1 
ATOM   316  C  CG2   . VAL A 1 39  ? 8.637   6.548   52.025  1.00 30.39  ? 38  VAL A CG2   1 
ATOM   317  N  N     . LEU A 1 40  ? 11.269  5.922   50.378  1.00 28.10  ? 39  LEU A N     1 
ATOM   318  C  CA    . LEU A 1 40  ? 11.712  4.805   49.557  1.00 32.10  ? 39  LEU A CA    1 
ATOM   319  C  C     . LEU A 1 40  ? 11.142  3.528   50.146  1.00 36.48  ? 39  LEU A C     1 
ATOM   320  O  O     . LEU A 1 40  ? 11.313  3.267   51.341  1.00 37.65  ? 39  LEU A O     1 
ATOM   321  C  CB    . LEU A 1 40  ? 13.253  4.747   49.498  1.00 34.29  ? 39  LEU A CB    1 
ATOM   322  C  CG    . LEU A 1 40  ? 13.874  3.430   49.020  1.00 36.18  ? 39  LEU A CG    1 
ATOM   323  C  CD1   . LEU A 1 40  ? 13.643  3.278   47.530  1.00 37.68  ? 39  LEU A CD1   1 
ATOM   324  C  CD2   . LEU A 1 40  ? 15.364  3.360   49.342  1.00 36.76  ? 39  LEU A CD2   1 
ATOM   325  N  N     . LEU A 1 41  ? 10.434  2.752   49.326  1.00 37.44  ? 40  LEU A N     1 
ATOM   326  C  CA    . LEU A 1 41  ? 9.881   1.483   49.775  1.00 37.63  ? 40  LEU A CA    1 
ATOM   327  C  C     . LEU A 1 41  ? 10.443  0.368   48.917  1.00 37.28  ? 40  LEU A C     1 
ATOM   328  O  O     . LEU A 1 41  ? 10.807  0.585   47.761  1.00 36.65  ? 40  LEU A O     1 
ATOM   329  C  CB    . LEU A 1 41  ? 8.340   1.453   49.694  1.00 30.63  ? 40  LEU A CB    1 
ATOM   330  C  CG    . LEU A 1 41  ? 7.648   2.679   50.290  1.00 42.08  ? 40  LEU A CG    1 
ATOM   331  C  CD1   . LEU A 1 41  ? 7.447   3.754   49.234  1.00 35.44  ? 40  LEU A CD1   1 
ATOM   332  C  CD2   . LEU A 1 41  ? 6.348   2.329   50.995  1.00 42.42  ? 40  LEU A CD2   1 
ATOM   333  N  N     . CYS A 1 42  ? 10.498  -0.832  49.474  1.00 35.24  ? 41  CYS A N     1 
ATOM   334  C  CA    . CYS A 1 42  ? 10.851  -1.973  48.650  1.00 33.80  ? 41  CYS A CA    1 
ATOM   335  C  C     . CYS A 1 42  ? 9.934   -3.135  48.976  1.00 35.69  ? 41  CYS A C     1 
ATOM   336  O  O     . CYS A 1 42  ? 9.512   -3.313  50.125  1.00 35.84  ? 41  CYS A O     1 
ATOM   337  C  CB    . CYS A 1 42  ? 12.318  -2.385  48.833  1.00 39.02  ? 41  CYS A CB    1 
ATOM   338  S  SG    . CYS A 1 42  ? 12.657  -3.164  50.387  1.00 43.20  ? 41  CYS A SG    1 
ATOM   339  N  N     . LEU A 1 43  ? 9.630   -3.918  47.948  1.00 37.86  ? 42  LEU A N     1 
ATOM   340  C  CA    . LEU A 1 43  ? 8.780   -5.086  48.102  1.00 39.10  ? 42  LEU A CA    1 
ATOM   341  C  C     . LEU A 1 43  ? 9.159   -6.094  47.031  1.00 43.51  ? 42  LEU A C     1 
ATOM   342  O  O     . LEU A 1 43  ? 9.061   -5.788  45.836  1.00 38.34  ? 42  LEU A O     1 
ATOM   343  C  CB    . LEU A 1 43  ? 7.295   -4.708  48.002  1.00 36.56  ? 42  LEU A CB    1 
ATOM   344  C  CG    . LEU A 1 43  ? 6.335   -5.904  48.032  1.00 36.09  ? 42  LEU A CG    1 
ATOM   345  C  CD1   . LEU A 1 43  ? 6.454   -6.606  49.381  1.00 39.75  ? 42  LEU A CD1   1 
ATOM   346  C  CD2   . LEU A 1 43  ? 4.895   -5.446  47.786  1.00 38.48  ? 42  LEU A CD2   1 
ATOM   347  N  N     . ASP A 1 44  ? 9.598   -7.280  47.468  1.00 41.93  ? 43  ASP A N     1 
ATOM   348  C  CA    . ASP A 1 44  ? 9.813   -8.418  46.576  1.00 52.01  ? 43  ASP A CA    1 
ATOM   349  C  C     . ASP A 1 44  ? 10.717  -8.046  45.401  1.00 44.60  ? 43  ASP A C     1 
ATOM   350  O  O     . ASP A 1 44  ? 10.467  -8.418  44.257  1.00 55.22  ? 43  ASP A O     1 
ATOM   351  C  CB    . ASP A 1 44  ? 8.469   -8.976  46.091  1.00 53.29  ? 43  ASP A CB    1 
ATOM   352  C  CG    . ASP A 1 44  ? 8.620   -10.247 45.269  1.00 61.41  ? 43  ASP A CG    1 
ATOM   353  O  OD1   . ASP A 1 44  ? 9.000   -11.282 45.853  1.00 66.89  ? 43  ASP A OD1   1 
ATOM   354  O  OD2   . ASP A 1 44  ? 8.344   -10.210 44.045  1.00 64.22  ? 43  ASP A OD2   1 
ATOM   355  N  N     . GLY A 1 45  ? 11.769  -7.281  45.679  1.00 44.28  ? 44  GLY A N     1 
ATOM   356  C  CA    . GLY A 1 45  ? 12.738  -6.953  44.645  1.00 44.28  ? 44  GLY A CA    1 
ATOM   357  C  C     . GLY A 1 45  ? 12.363  -5.787  43.764  1.00 46.74  ? 44  GLY A C     1 
ATOM   358  O  O     . GLY A 1 45  ? 12.855  -5.685  42.633  1.00 48.87  ? 44  GLY A O     1 
ATOM   359  N  N     . ILE A 1 46  ? 11.474  -4.920  44.230  1.00 44.94  ? 45  ILE A N     1 
ATOM   360  C  CA    . ILE A 1 46  ? 11.125  -3.681  43.547  1.00 39.69  ? 45  ILE A CA    1 
ATOM   361  C  C     . ILE A 1 46  ? 11.394  -2.527  44.497  1.00 37.25  ? 45  ILE A C     1 
ATOM   362  O  O     . ILE A 1 46  ? 11.097  -2.614  45.691  1.00 36.29  ? 45  ILE A O     1 
ATOM   363  C  CB    . ILE A 1 46  ? 9.653   -3.660  43.062  1.00 42.22  ? 45  ILE A CB    1 
ATOM   364  C  CG1   . ILE A 1 46  ? 9.366   -4.741  42.000  1.00 45.70  ? 45  ILE A CG1   1 
ATOM   365  C  CG2   . ILE A 1 46  ? 9.262   -2.273  42.559  1.00 35.70  ? 45  ILE A CG2   1 
ATOM   366  C  CD1   . ILE A 1 46  ? 9.344   -6.175  42.460  1.00 48.80  ? 45  ILE A CD1   1 
ATOM   367  N  N     . PHE A 1 47  ? 11.981  -1.465  43.975  1.00 35.73  ? 46  PHE A N     1 
ATOM   368  C  CA    . PHE A 1 47  ? 12.111  -0.208  44.696  1.00 36.53  ? 46  PHE A CA    1 
ATOM   369  C  C     . PHE A 1 47  ? 11.047  0.755   44.185  1.00 43.46  ? 46  PHE A C     1 
ATOM   370  O  O     . PHE A 1 47  ? 10.779  0.805   42.979  1.00 34.85  ? 46  PHE A O     1 
ATOM   371  C  CB    . PHE A 1 47  ? 13.496  0.426   44.497  1.00 35.21  ? 46  PHE A CB    1 
ATOM   372  C  CG    . PHE A 1 47  ? 14.617  -0.220  45.298  1.00 38.54  ? 46  PHE A CG    1 
ATOM   373  C  CD1   . PHE A 1 47  ? 14.617  -0.181  46.689  1.00 36.60  ? 46  PHE A CD1   1 
ATOM   374  C  CD2   . PHE A 1 47  ? 15.708  -0.785  44.657  1.00 39.76  ? 46  PHE A CD2   1 
ATOM   375  C  CE1   . PHE A 1 47  ? 15.669  -0.748  47.429  1.00 42.89  ? 46  PHE A CE1   1 
ATOM   376  C  CE2   . PHE A 1 47  ? 16.770  -1.340  45.388  1.00 38.85  ? 46  PHE A CE2   1 
ATOM   377  C  CZ    . PHE A 1 47  ? 16.749  -1.328  46.772  1.00 35.41  ? 46  PHE A CZ    1 
ATOM   378  N  N     . PHE A 1 48  ? 10.434  1.505   45.109  1.00 35.09  ? 47  PHE A N     1 
ATOM   379  C  CA    . PHE A 1 48  ? 9.548   2.620   44.789  1.00 34.72  ? 47  PHE A CA    1 
ATOM   380  C  C     . PHE A 1 48  ? 10.076  3.834   45.531  1.00 32.61  ? 47  PHE A C     1 
ATOM   381  O  O     . PHE A 1 48  ? 10.401  3.734   46.720  1.00 32.48  ? 47  PHE A O     1 
ATOM   382  C  CB    . PHE A 1 48  ? 8.080   2.387   45.219  1.00 35.96  ? 47  PHE A CB    1 
ATOM   383  C  CG    . PHE A 1 48  ? 7.549   1.007   44.947  1.00 35.72  ? 47  PHE A CG    1 
ATOM   384  C  CD1   . PHE A 1 48  ? 7.929   -0.074  45.723  1.00 40.33  ? 47  PHE A CD1   1 
ATOM   385  C  CD2   . PHE A 1 48  ? 6.601   0.804   43.944  1.00 40.33  ? 47  PHE A CD2   1 
ATOM   386  C  CE1   . PHE A 1 48  ? 7.416   -1.340  45.492  1.00 40.84  ? 47  PHE A CE1   1 
ATOM   387  C  CE2   . PHE A 1 48  ? 6.103   -0.456  43.692  1.00 38.42  ? 47  PHE A CE2   1 
ATOM   388  C  CZ    . PHE A 1 48  ? 6.505   -1.536  44.473  1.00 42.00  ? 47  PHE A CZ    1 
ATOM   389  N  N     . GLN A 1 49  ? 10.160  4.983   44.866  1.00 31.01  ? 48  GLN A N     1 
ATOM   390  C  CA    . GLN A 1 49  ? 10.576  6.159   45.616  1.00 32.58  ? 48  GLN A CA    1 
ATOM   391  C  C     . GLN A 1 49  ? 9.843   7.395   45.128  1.00 33.46  ? 48  GLN A C     1 
ATOM   392  O  O     . GLN A 1 49  ? 9.530   7.516   43.941  1.00 37.51  ? 48  GLN A O     1 
ATOM   393  C  CB    . GLN A 1 49  ? 12.104  6.371   45.564  1.00 37.58  ? 48  GLN A CB    1 
ATOM   394  C  CG    . GLN A 1 49  ? 12.570  7.752   46.039  1.00 34.57  ? 48  GLN A CG    1 
ATOM   395  C  CD    . GLN A 1 49  ? 14.070  7.954   45.875  1.00 42.27  ? 48  GLN A CD    1 
ATOM   396  O  OE1   . GLN A 1 49  ? 14.512  8.646   44.956  1.00 48.14  ? 48  GLN A OE1   1 
ATOM   397  N  NE2   . GLN A 1 49  ? 14.856  7.413   46.811  1.00 38.90  ? 48  GLN A NE2   1 
ATOM   398  N  N     . ILE A 1 50  ? 9.528   8.277   46.076  1.00 31.15  ? 49  ILE A N     1 
ATOM   399  C  CA    . ILE A 1 50  ? 9.070   9.626   45.804  1.00 33.46  ? 49  ILE A CA    1 
ATOM   400  C  C     . ILE A 1 50  ? 10.146  10.572  46.308  1.00 41.31  ? 49  ILE A C     1 
ATOM   401  O  O     . ILE A 1 50  ? 10.621  10.442  47.445  1.00 34.78  ? 49  ILE A O     1 
ATOM   402  C  CB    . ILE A 1 50  ? 7.705   9.925   46.458  1.00 32.77  ? 49  ILE A CB    1 
ATOM   403  C  CG1   . ILE A 1 50  ? 6.593   9.087   45.827  1.00 35.77  ? 49  ILE A CG1   1 
ATOM   404  C  CG2   . ILE A 1 50  ? 7.323   11.379  46.235  1.00 35.60  ? 49  ILE A CG2   1 
ATOM   405  C  CD1   . ILE A 1 50  ? 5.490   8.672   46.823  1.00 39.24  ? 49  ILE A CD1   1 
ATOM   406  N  N     . LEU A 1 51  ? 10.544  11.502  45.450  1.00 36.45  ? 50  LEU A N     1 
ATOM   407  C  CA    . LEU A 1 51  ? 11.662  12.407  45.668  1.00 34.56  ? 50  LEU A CA    1 
ATOM   408  C  C     . LEU A 1 51  ? 11.209  13.801  45.278  1.00 47.04  ? 50  LEU A C     1 
ATOM   409  O  O     . LEU A 1 51  ? 10.662  13.992  44.184  1.00 40.14  ? 50  LEU A O     1 
ATOM   410  C  CB    . LEU A 1 51  ? 12.866  11.985  44.824  1.00 38.27  ? 50  LEU A CB    1 
ATOM   411  C  CG    . LEU A 1 51  ? 14.309  12.320  45.181  1.00 44.19  ? 50  LEU A CG    1 
ATOM   412  C  CD1   . LEU A 1 51  ? 14.760  11.677  46.471  1.00 45.08  ? 50  LEU A CD1   1 
ATOM   413  C  CD2   . LEU A 1 51  ? 15.204  11.860  44.037  1.00 45.60  ? 50  LEU A CD2   1 
ATOM   414  N  N     . GLU A 1 52  ? 11.472  14.768  46.152  1.00 41.47  ? 51  GLU A N     1 
ATOM   415  C  CA    . GLU A 1 52  ? 10.912  16.103  46.044  1.00 40.88  ? 51  GLU A CA    1 
ATOM   416  C  C     . GLU A 1 52  ? 11.897  17.152  46.549  1.00 46.35  ? 51  GLU A C     1 
ATOM   417  O  O     . GLU A 1 52  ? 12.516  17.004  47.610  1.00 41.40  ? 51  GLU A O     1 
ATOM   418  C  CB    . GLU A 1 52  ? 9.546   16.120  46.760  1.00 41.90  ? 51  GLU A CB    1 
ATOM   419  C  CG    . GLU A 1 52  ? 9.635   16.140  48.270  1.00 44.59  ? 51  GLU A CG    1 
ATOM   420  C  CD    . GLU A 1 52  ? 8.269   16.110  48.977  1.00 50.93  ? 51  GLU A CD    1 
ATOM   421  O  OE1   . GLU A 1 52  ? 7.200   16.103  48.302  1.00 41.83  ? 51  GLU A OE1   1 
ATOM   422  O  OE2   . GLU A 1 52  ? 8.271   16.002  50.227  1.00 43.42  ? 51  GLU A OE2   1 
ATOM   423  N  N     . GLY A 1 53  ? 12.078  18.187  45.740  1.00 42.99  ? 52  GLY A N     1 
ATOM   424  C  CA    . GLY A 1 53  ? 12.946  19.291  46.088  1.00 49.37  ? 52  GLY A CA    1 
ATOM   425  C  C     . GLY A 1 53  ? 13.133  20.205  44.891  1.00 61.13  ? 52  GLY A C     1 
ATOM   426  O  O     . GLY A 1 53  ? 12.519  20.015  43.838  1.00 54.10  ? 52  GLY A O     1 
ATOM   427  N  N     . GLU A 1 54  ? 13.985  21.210  45.085  1.00 62.23  ? 53  GLU A N     1 
ATOM   428  C  CA    . GLU A 1 54  ? 14.415  22.083  43.996  1.00 63.66  ? 53  GLU A CA    1 
ATOM   429  C  C     . GLU A 1 54  ? 14.858  21.286  42.769  1.00 55.53  ? 53  GLU A C     1 
ATOM   430  O  O     . GLU A 1 54  ? 15.624  20.326  42.879  1.00 52.35  ? 53  GLU A O     1 
ATOM   431  C  CB    . GLU A 1 54  ? 15.542  22.981  44.503  1.00 63.19  ? 53  GLU A CB    1 
ATOM   432  C  CG    . GLU A 1 54  ? 15.340  23.454  45.955  1.00 74.80  ? 53  GLU A CG    1 
ATOM   433  C  CD    . GLU A 1 54  ? 16.034  22.580  47.008  1.00 80.49  ? 53  GLU A CD    1 
ATOM   434  O  OE1   . GLU A 1 54  ? 15.612  21.406  47.185  1.00 64.83  ? 53  GLU A OE1   1 
ATOM   435  O  OE2   . GLU A 1 54  ? 17.009  23.065  47.636  1.00 70.71  ? 53  GLU A OE2   1 
ATOM   436  N  N     . ALA A 1 55  ? 14.371  21.704  41.593  1.00 53.42  ? 54  ALA A N     1 
ATOM   437  C  CA    . ALA A 1 55  ? 14.506  20.890  40.384  1.00 54.97  ? 54  ALA A CA    1 
ATOM   438  C  C     . ALA A 1 55  ? 15.965  20.577  40.055  1.00 52.73  ? 54  ALA A C     1 
ATOM   439  O  O     . ALA A 1 55  ? 16.294  19.442  39.686  1.00 50.53  ? 54  ALA A O     1 
ATOM   440  C  CB    . ALA A 1 55  ? 13.836  21.592  39.205  1.00 57.11  ? 54  ALA A CB    1 
ATOM   441  N  N     . GLU A 1 56  ? 16.848  21.571  40.166  1.00 61.09  ? 55  GLU A N     1 
ATOM   442  C  CA    . GLU A 1 56  ? 18.260  21.351  39.861  1.00 67.18  ? 55  GLU A CA    1 
ATOM   443  C  C     . GLU A 1 56  ? 18.839  20.216  40.702  1.00 64.03  ? 55  GLU A C     1 
ATOM   444  O  O     . GLU A 1 56  ? 19.451  19.280  40.170  1.00 63.81  ? 55  GLU A O     1 
ATOM   445  C  CB    . GLU A 1 56  ? 19.043  22.649  40.071  1.00 74.49  ? 55  GLU A CB    1 
ATOM   446  C  CG    . GLU A 1 56  ? 20.156  22.895  39.049  1.00 90.15  ? 55  GLU A CG    1 
ATOM   447  C  CD    . GLU A 1 56  ? 19.634  23.226  37.656  1.00 100.27 ? 55  GLU A CD    1 
ATOM   448  O  OE1   . GLU A 1 56  ? 19.310  24.409  37.400  1.00 107.23 ? 55  GLU A OE1   1 
ATOM   449  O  OE2   . GLU A 1 56  ? 19.573  22.301  36.813  1.00 95.82  ? 55  GLU A OE2   1 
ATOM   450  N  N     . LYS A 1 57  ? 18.637  20.269  42.019  1.00 59.08  ? 56  LYS A N     1 
ATOM   451  C  CA    . LYS A 1 57  ? 19.198  19.236  42.884  1.00 60.95  ? 56  LYS A CA    1 
ATOM   452  C  C     . LYS A 1 57  ? 18.567  17.874  42.617  1.00 53.97  ? 56  LYS A C     1 
ATOM   453  O  O     . LYS A 1 57  ? 19.264  16.855  42.619  1.00 58.62  ? 56  LYS A O     1 
ATOM   454  C  CB    . LYS A 1 57  ? 19.036  19.633  44.348  1.00 58.09  ? 56  LYS A CB    1 
ATOM   455  C  CG    . LYS A 1 57  ? 19.954  20.763  44.792  1.00 55.82  ? 56  LYS A CG    1 
ATOM   456  C  CD    . LYS A 1 57  ? 19.332  21.586  45.915  1.00 67.69  ? 56  LYS A CD    1 
ATOM   457  C  CE    . LYS A 1 57  ? 20.000  22.949  46.058  1.00 70.29  ? 56  LYS A CE    1 
ATOM   458  N  NZ    . LYS A 1 57  ? 21.467  22.825  46.300  1.00 75.34  ? 56  LYS A NZ    1 
ATOM   459  N  N     . ILE A 1 58  ? 17.261  17.839  42.357  1.00 51.97  ? 57  ILE A N     1 
ATOM   460  C  CA    . ILE A 1 58  ? 16.582  16.573  42.095  1.00 49.89  ? 57  ILE A CA    1 
ATOM   461  C  C     . ILE A 1 58  ? 17.207  15.862  40.902  1.00 50.73  ? 57  ILE A C     1 
ATOM   462  O  O     . ILE A 1 58  ? 17.477  14.654  40.953  1.00 50.87  ? 57  ILE A O     1 
ATOM   463  C  CB    . ILE A 1 58  ? 15.072  16.805  41.883  1.00 49.03  ? 57  ILE A CB    1 
ATOM   464  C  CG1   . ILE A 1 58  ? 14.394  17.113  43.221  1.00 55.41  ? 57  ILE A CG1   1 
ATOM   465  C  CG2   . ILE A 1 58  ? 14.446  15.621  41.181  1.00 46.40  ? 57  ILE A CG2   1 
ATOM   466  C  CD1   . ILE A 1 58  ? 13.957  15.869  43.988  1.00 49.34  ? 57  ILE A CD1   1 
ATOM   467  N  N     . ASP A 1 59  ? 17.430  16.596  39.803  1.00 53.50  ? 58  ASP A N     1 
ATOM   468  C  CA    . ASP A 1 59  ? 17.960  15.970  38.590  1.00 53.96  ? 58  ASP A CA    1 
ATOM   469  C  C     . ASP A 1 59  ? 19.354  15.407  38.814  1.00 50.12  ? 58  ASP A C     1 
ATOM   470  O  O     . ASP A 1 59  ? 19.663  14.302  38.353  1.00 60.03  ? 58  ASP A O     1 
ATOM   471  C  CB    . ASP A 1 59  ? 17.978  16.965  37.433  1.00 57.88  ? 58  ASP A CB    1 
ATOM   472  C  CG    . ASP A 1 59  ? 16.581  17.306  36.937  1.00 70.06  ? 58  ASP A CG    1 
ATOM   473  O  OD1   . ASP A 1 59  ? 16.292  18.513  36.773  1.00 67.04  ? 58  ASP A OD1   1 
ATOM   474  O  OD2   . ASP A 1 59  ? 15.772  16.369  36.729  1.00 73.21  ? 58  ASP A OD2   1 
ATOM   475  N  N     . ARG A 1 60  ? 20.210  16.144  39.523  1.00 52.97  ? 59  ARG A N     1 
ATOM   476  C  CA    . ARG A 1 60  ? 21.539  15.623  39.829  1.00 52.14  ? 59  ARG A CA    1 
ATOM   477  C  C     . ARG A 1 60  ? 21.443  14.351  40.660  1.00 52.27  ? 59  ARG A C     1 
ATOM   478  O  O     . ARG A 1 60  ? 22.085  13.342  40.347  1.00 48.37  ? 59  ARG A O     1 
ATOM   479  C  CB    . ARG A 1 60  ? 22.372  16.681  40.552  1.00 54.78  ? 59  ARG A CB    1 
ATOM   480  C  CG    . ARG A 1 60  ? 22.346  18.066  39.896  1.00 72.75  ? 59  ARG A CG    1 
ATOM   481  C  CD    . ARG A 1 60  ? 23.418  18.236  38.795  1.00 82.38  ? 59  ARG A CD    1 
ATOM   482  N  NE    . ARG A 1 60  ? 23.107  17.535  37.548  1.00 80.04  ? 59  ARG A NE    1 
ATOM   483  C  CZ    . ARG A 1 60  ? 22.157  17.893  36.690  1.00 76.10  ? 59  ARG A CZ    1 
ATOM   484  N  NH1   . ARG A 1 60  ? 21.423  18.979  36.879  1.00 71.22  ? 59  ARG A NH1   1 
ATOM   485  N  NH2   . ARG A 1 60  ? 21.943  17.146  35.610  1.00 75.95  ? 59  ARG A NH2   1 
ATOM   486  N  N     . ILE A 1 61  ? 20.620  14.374  41.716  1.00 51.67  ? 60  ILE A N     1 
ATOM   487  C  CA    . ILE A 1 61  ? 20.381  13.165  42.504  1.00 48.86  ? 60  ILE A CA    1 
ATOM   488  C  C     . ILE A 1 61  ? 19.828  12.056  41.620  1.00 43.80  ? 60  ILE A C     1 
ATOM   489  O  O     . ILE A 1 61  ? 20.273  10.899  41.682  1.00 41.34  ? 60  ILE A O     1 
ATOM   490  C  CB    . ILE A 1 61  ? 19.423  13.460  43.671  1.00 50.66  ? 60  ILE A CB    1 
ATOM   491  C  CG1   . ILE A 1 61  ? 19.946  14.605  44.542  1.00 46.78  ? 60  ILE A CG1   1 
ATOM   492  C  CG2   . ILE A 1 61  ? 19.200  12.186  44.464  1.00 42.48  ? 60  ILE A CG2   1 
ATOM   493  C  CD1   . ILE A 1 61  ? 19.411  14.600  45.924  1.00 54.69  ? 60  ILE A CD1   1 
ATOM   494  N  N     . TYR A 1 62  ? 18.823  12.390  40.804  1.00 46.41  ? 61  TYR A N     1 
ATOM   495  C  CA    . TYR A 1 62  ? 18.209  11.393  39.933  1.00 47.09  ? 61  TYR A CA    1 
ATOM   496  C  C     . TYR A 1 62  ? 19.211  10.811  38.943  1.00 48.39  ? 61  TYR A C     1 
ATOM   497  O  O     . TYR A 1 62  ? 19.187  9.603   38.662  1.00 48.75  ? 61  TYR A O     1 
ATOM   498  C  CB    . TYR A 1 62  ? 17.013  11.997  39.200  1.00 42.14  ? 61  TYR A CB    1 
ATOM   499  C  CG    . TYR A 1 62  ? 16.187  10.934  38.535  1.00 49.89  ? 61  TYR A CG    1 
ATOM   500  C  CD1   . TYR A 1 62  ? 15.385  10.081  39.281  1.00 55.16  ? 61  TYR A CD1   1 
ATOM   501  C  CD2   . TYR A 1 62  ? 16.223  10.767  37.153  1.00 51.67  ? 61  TYR A CD2   1 
ATOM   502  C  CE1   . TYR A 1 62  ? 14.638  9.088   38.672  1.00 54.80  ? 61  TYR A CE1   1 
ATOM   503  C  CE2   . TYR A 1 62  ? 15.474  9.783   36.532  1.00 50.56  ? 61  TYR A CE2   1 
ATOM   504  C  CZ    . TYR A 1 62  ? 14.684  8.950   37.296  1.00 54.17  ? 61  TYR A CZ    1 
ATOM   505  O  OH    . TYR A 1 62  ? 13.938  7.968   36.699  1.00 50.20  ? 61  TYR A OH    1 
ATOM   506  N  N     . GLU A 1 63  ? 20.108  11.650  38.416  1.00 52.03  ? 62  GLU A N     1 
ATOM   507  C  CA    . GLU A 1 63  ? 21.147  11.149  37.517  1.00 55.97  ? 62  GLU A CA    1 
ATOM   508  C  C     . GLU A 1 63  ? 22.028  10.130  38.231  1.00 47.54  ? 62  GLU A C     1 
ATOM   509  O  O     . GLU A 1 63  ? 22.353  9.074   37.673  1.00 51.67  ? 62  GLU A O     1 
ATOM   510  C  CB    . GLU A 1 63  ? 21.981  12.318  36.987  1.00 57.87  ? 62  GLU A CB    1 
ATOM   511  C  CG    . GLU A 1 63  ? 21.434  12.966  35.701  1.00 68.84  ? 62  GLU A CG    1 
ATOM   512  C  CD    . GLU A 1 63  ? 21.094  11.966  34.603  1.00 81.95  ? 62  GLU A CD    1 
ATOM   513  O  OE1   . GLU A 1 63  ? 19.996  12.091  34.010  1.00 84.85  ? 62  GLU A OE1   1 
ATOM   514  O  OE2   . GLU A 1 63  ? 21.928  11.073  34.319  1.00 81.79  ? 62  GLU A OE2   1 
ATOM   515  N  N     . ARG A 1 64  ? 22.394  10.418  39.485  1.00 44.45  ? 63  ARG A N     1 
ATOM   516  C  CA    . ARG A 1 64  ? 23.123  9.447   40.303  1.00 45.12  ? 63  ARG A CA    1 
ATOM   517  C  C     . ARG A 1 64  ? 22.351  8.148   40.486  1.00 49.82  ? 63  ARG A C     1 
ATOM   518  O  O     . ARG A 1 64  ? 22.934  7.058   40.411  1.00 46.06  ? 63  ARG A O     1 
ATOM   519  C  CB    . ARG A 1 64  ? 23.451  10.060  41.664  1.00 47.97  ? 63  ARG A CB    1 
ATOM   520  C  CG    . ARG A 1 64  ? 24.883  10.490  41.824  1.00 50.81  ? 63  ARG A CG    1 
ATOM   521  C  CD    . ARG A 1 64  ? 25.162  10.904  43.256  1.00 52.59  ? 63  ARG A CD    1 
ATOM   522  N  NE    . ARG A 1 64  ? 24.794  12.298  43.468  1.00 53.49  ? 63  ARG A NE    1 
ATOM   523  C  CZ    . ARG A 1 64  ? 24.119  12.771  44.506  1.00 53.86  ? 63  ARG A CZ    1 
ATOM   524  N  NH1   . ARG A 1 64  ? 23.625  11.974  45.439  1.00 50.52  ? 63  ARG A NH1   1 
ATOM   525  N  NH2   . ARG A 1 64  ? 23.936  14.084  44.610  1.00 57.98  ? 63  ARG A NH2   1 
ATOM   526  N  N     . ILE A 1 65  ? 21.042  8.239   40.767  1.00 47.83  ? 64  ILE A N     1 
ATOM   527  C  CA    . ILE A 1 65  ? 20.262  7.035   41.044  1.00 40.19  ? 64  ILE A CA    1 
ATOM   528  C  C     . ILE A 1 65  ? 20.238  6.127   39.820  1.00 38.37  ? 64  ILE A C     1 
ATOM   529  O  O     . ILE A 1 65  ? 20.301  4.896   39.935  1.00 41.88  ? 64  ILE A O     1 
ATOM   530  C  CB    . ILE A 1 65  ? 18.829  7.405   41.494  1.00 44.33  ? 64  ILE A CB    1 
ATOM   531  C  CG1   . ILE A 1 65  ? 18.811  8.065   42.880  1.00 39.24  ? 64  ILE A CG1   1 
ATOM   532  C  CG2   . ILE A 1 65  ? 17.926  6.184   41.471  1.00 40.37  ? 64  ILE A CG2   1 
ATOM   533  C  CD1   . ILE A 1 65  ? 17.522  8.901   43.147  1.00 38.88  ? 64  ILE A CD1   1 
ATOM   534  N  N     . LEU A 1 66  ? 20.131  6.717   38.631  1.00 44.28  ? 65  LEU A N     1 
ATOM   535  C  CA    . LEU A 1 66  ? 20.111  5.923   37.406  1.00 53.18  ? 65  LEU A CA    1 
ATOM   536  C  C     . LEU A 1 66  ? 21.392  5.117   37.206  1.00 47.30  ? 65  LEU A C     1 
ATOM   537  O  O     . LEU A 1 66  ? 21.358  4.083   36.530  1.00 53.25  ? 65  LEU A O     1 
ATOM   538  C  CB    . LEU A 1 66  ? 19.858  6.838   36.206  1.00 50.40  ? 65  LEU A CB    1 
ATOM   539  C  CG    . LEU A 1 66  ? 18.502  7.559   36.178  1.00 53.33  ? 65  LEU A CG    1 
ATOM   540  C  CD1   . LEU A 1 66  ? 18.555  8.763   35.256  1.00 57.86  ? 65  LEU A CD1   1 
ATOM   541  C  CD2   . LEU A 1 66  ? 17.376  6.619   35.753  1.00 47.64  ? 65  LEU A CD2   1 
ATOM   542  N  N     . ALA A 1 67  ? 22.500  5.524   37.824  1.00 51.67  ? 66  ALA A N     1 
ATOM   543  C  CA    . ALA A 1 67  ? 23.780  4.847   37.662  1.00 52.83  ? 66  ALA A CA    1 
ATOM   544  C  C     . ALA A 1 67  ? 24.094  3.843   38.765  1.00 57.64  ? 66  ALA A C     1 
ATOM   545  O  O     . ALA A 1 67  ? 25.124  3.165   38.679  1.00 52.90  ? 66  ALA A O     1 
ATOM   546  C  CB    . ALA A 1 67  ? 24.909  5.878   37.586  1.00 53.19  ? 66  ALA A CB    1 
ATOM   547  N  N     . ASP A 1 68  ? 23.252  3.727   39.794  1.00 51.32  ? 67  ASP A N     1 
ATOM   548  C  CA    . ASP A 1 68  ? 23.523  2.791   40.877  1.00 49.11  ? 67  ASP A CA    1 
ATOM   549  C  C     . ASP A 1 68  ? 23.494  1.354   40.360  1.00 53.87  ? 67  ASP A C     1 
ATOM   550  O  O     . ASP A 1 68  ? 22.544  0.938   39.686  1.00 54.46  ? 67  ASP A O     1 
ATOM   551  C  CB    . ASP A 1 68  ? 22.497  2.961   41.997  1.00 44.21  ? 67  ASP A CB    1 
ATOM   552  C  CG    . ASP A 1 68  ? 23.037  2.564   43.349  1.00 47.85  ? 67  ASP A CG    1 
ATOM   553  O  OD1   . ASP A 1 68  ? 23.143  1.345   43.608  1.00 51.15  ? 67  ASP A OD1   1 
ATOM   554  O  OD2   . ASP A 1 68  ? 23.298  3.468   44.175  1.00 45.46  ? 67  ASP A OD2   1 
ATOM   555  N  N     . GLU A 1 69  ? 24.541  0.589   40.684  1.00 57.40  ? 68  GLU A N     1 
ATOM   556  C  CA    . GLU A 1 69  ? 24.621  -0.808  40.263  1.00 59.38  ? 68  GLU A CA    1 
ATOM   557  C  C     . GLU A 1 69  ? 23.583  -1.682  40.940  1.00 56.85  ? 68  GLU A C     1 
ATOM   558  O  O     . GLU A 1 69  ? 23.289  -2.771  40.438  1.00 59.37  ? 68  GLU A O     1 
ATOM   559  C  CB    . GLU A 1 69  ? 26.013  -1.384  40.548  1.00 64.44  ? 68  GLU A CB    1 
ATOM   560  C  CG    . GLU A 1 69  ? 26.501  -2.416  39.527  1.00 81.23  ? 68  GLU A CG    1 
ATOM   561  C  CD    . GLU A 1 69  ? 27.431  -1.842  38.462  1.00 93.62  ? 68  GLU A CD    1 
ATOM   562  O  OE1   . GLU A 1 69  ? 28.628  -1.638  38.769  1.00 88.24  ? 68  GLU A OE1   1 
ATOM   563  O  OE2   . GLU A 1 69  ? 26.974  -1.626  37.313  1.00 89.55  ? 68  GLU A OE2   1 
ATOM   564  N  N     . ARG A 1 70  ? 23.019  -1.232  42.057  1.00 56.07  ? 69  ARG A N     1 
ATOM   565  C  CA    . ARG A 1 70  ? 22.149  -2.075  42.864  1.00 56.26  ? 69  ARG A CA    1 
ATOM   566  C  C     . ARG A 1 70  ? 20.720  -2.170  42.326  1.00 49.47  ? 69  ARG A C     1 
ATOM   567  O  O     . ARG A 1 70  ? 19.919  -2.951  42.860  1.00 48.42  ? 69  ARG A O     1 
ATOM   568  C  CB    . ARG A 1 70  ? 22.176  -1.565  44.307  1.00 53.71  ? 69  ARG A CB    1 
ATOM   569  C  CG    . ARG A 1 70  ? 23.568  -1.732  44.945  1.00 51.15  ? 69  ARG A CG    1 
ATOM   570  C  CD    . ARG A 1 70  ? 23.723  -0.972  46.240  1.00 49.97  ? 69  ARG A CD    1 
ATOM   571  N  NE    . ARG A 1 70  ? 23.653  0.471   46.033  1.00 47.63  ? 69  ARG A NE    1 
ATOM   572  C  CZ    . ARG A 1 70  ? 23.998  1.372   46.941  1.00 43.35  ? 69  ARG A CZ    1 
ATOM   573  N  NH1   . ARG A 1 70  ? 24.453  1.014   48.132  1.00 49.19  ? 69  ARG A NH1   1 
ATOM   574  N  NH2   . ARG A 1 70  ? 23.900  2.663   46.643  1.00 42.25  ? 69  ARG A NH2   1 
ATOM   575  N  N     . HIS A 1 71  ? 20.380  -1.441  41.269  1.00 47.02  ? 70  HIS A N     1 
ATOM   576  C  CA    . HIS A 1 71  ? 19.065  -1.620  40.668  1.00 48.85  ? 70  HIS A CA    1 
ATOM   577  C  C     . HIS A 1 71  ? 19.128  -1.298  39.180  1.00 48.38  ? 70  HIS A C     1 
ATOM   578  O  O     . HIS A 1 71  ? 20.123  -0.773  38.674  1.00 48.04  ? 70  HIS A O     1 
ATOM   579  C  CB    . HIS A 1 71  ? 17.994  -0.767  41.372  1.00 39.52  ? 70  HIS A CB    1 
ATOM   580  C  CG    . HIS A 1 71  ? 18.182  0.708   41.207  1.00 40.83  ? 70  HIS A CG    1 
ATOM   581  N  ND1   . HIS A 1 71  ? 17.180  1.617   41.463  1.00 45.37  ? 70  HIS A ND1   1 
ATOM   582  C  CD2   . HIS A 1 71  ? 19.262  1.436   40.837  1.00 47.39  ? 70  HIS A CD2   1 
ATOM   583  C  CE1   . HIS A 1 71  ? 17.627  2.840   41.239  1.00 44.99  ? 70  HIS A CE1   1 
ATOM   584  N  NE2   . HIS A 1 71  ? 18.893  2.758   40.869  1.00 40.40  ? 70  HIS A NE2   1 
ATOM   585  N  N     . THR A 1 72  ? 18.024  -1.598  38.493  1.00 51.54  ? 71  THR A N     1 
ATOM   586  C  CA    . THR A 1 72  ? 17.938  -1.536  37.041  1.00 53.22  ? 71  THR A CA    1 
ATOM   587  C  C     . THR A 1 72  ? 16.469  -1.401  36.642  1.00 56.02  ? 71  THR A C     1 
ATOM   588  O  O     . THR A 1 72  ? 15.561  -1.652  37.442  1.00 52.04  ? 71  THR A O     1 
ATOM   589  C  CB    . THR A 1 72  ? 18.560  -2.784  36.405  1.00 50.58  ? 71  THR A CB    1 
ATOM   590  O  OG1   . THR A 1 72  ? 18.840  -2.527  35.029  1.00 56.84  ? 71  THR A OG1   1 
ATOM   591  C  CG2   . THR A 1 72  ? 17.586  -3.956  36.485  1.00 47.47  ? 71  THR A CG2   1 
ATOM   592  N  N     . ASP A 1 73  ? 16.254  -1.019  35.375  1.00 51.44  ? 72  ASP A N     1 
ATOM   593  C  CA    . ASP A 1 73  ? 14.914  -0.825  34.800  1.00 53.80  ? 72  ASP A CA    1 
ATOM   594  C  C     . ASP A 1 73  ? 14.156  0.293   35.510  1.00 52.89  ? 72  ASP A C     1 
ATOM   595  O  O     . ASP A 1 73  ? 12.961  0.176   35.802  1.00 50.91  ? 72  ASP A O     1 
ATOM   596  C  CB    . ASP A 1 73  ? 14.097  -2.122  34.803  1.00 62.89  ? 72  ASP A CB    1 
ATOM   597  C  CG    . ASP A 1 73  ? 14.186  -2.868  33.484  1.00 71.35  ? 72  ASP A CG    1 
ATOM   598  O  OD1   . ASP A 1 73  ? 14.432  -4.095  33.501  1.00 73.46  ? 72  ASP A OD1   1 
ATOM   599  O  OD2   . ASP A 1 73  ? 13.992  -2.226  32.427  1.00 80.31  ? 72  ASP A OD2   1 
ATOM   600  N  N     . ILE A 1 74  ? 14.854  1.401   35.756  1.00 47.05  ? 73  ILE A N     1 
ATOM   601  C  CA    . ILE A 1 74  ? 14.263  2.531   36.455  1.00 48.88  ? 73  ILE A CA    1 
ATOM   602  C  C     . ILE A 1 74  ? 13.242  3.221   35.563  1.00 51.18  ? 73  ILE A C     1 
ATOM   603  O  O     . ILE A 1 74  ? 13.544  3.620   34.431  1.00 51.04  ? 73  ILE A O     1 
ATOM   604  C  CB    . ILE A 1 74  ? 15.355  3.501   36.918  1.00 51.77  ? 73  ILE A CB    1 
ATOM   605  C  CG1   . ILE A 1 74  ? 16.345  2.764   37.835  1.00 50.69  ? 73  ILE A CG1   1 
ATOM   606  C  CG2   . ILE A 1 74  ? 14.720  4.718   37.584  1.00 49.37  ? 73  ILE A CG2   1 
ATOM   607  C  CD1   . ILE A 1 74  ? 17.716  2.588   37.271  1.00 46.65  ? 73  ILE A CD1   1 
ATOM   608  N  N     . LEU A 1 75  ? 12.029  3.382   36.087  1.00 43.95  ? 74  LEU A N     1 
ATOM   609  C  CA    . LEU A 1 75  ? 10.891  3.924   35.347  1.00 40.51  ? 74  LEU A CA    1 
ATOM   610  C  C     . LEU A 1 75  ? 10.257  5.061   36.141  1.00 44.70  ? 74  LEU A C     1 
ATOM   611  O  O     . LEU A 1 75  ? 9.649   4.826   37.197  1.00 42.42  ? 74  LEU A O     1 
ATOM   612  C  CB    . LEU A 1 75  ? 9.858   2.832   35.073  1.00 43.16  ? 74  LEU A CB    1 
ATOM   613  C  CG    . LEU A 1 75  ? 8.674   3.313   34.238  1.00 46.84  ? 74  LEU A CG    1 
ATOM   614  C  CD1   . LEU A 1 75  ? 9.120   3.749   32.826  1.00 46.21  ? 74  LEU A CD1   1 
ATOM   615  C  CD2   . LEU A 1 75  ? 7.573   2.270   34.211  1.00 43.46  ? 74  LEU A CD2   1 
ATOM   616  N  N     . CYS A 1 76  ? 10.365  6.281   35.620  1.00 38.54  ? 75  CYS A N     1 
ATOM   617  C  CA    . CYS A 1 76  ? 9.707   7.436   36.217  1.00 44.44  ? 75  CYS A CA    1 
ATOM   618  C  C     . CYS A 1 76  ? 8.217   7.412   35.881  1.00 49.86  ? 75  CYS A C     1 
ATOM   619  O  O     . CYS A 1 76  ? 7.831   7.565   34.719  1.00 42.83  ? 75  CYS A O     1 
ATOM   620  C  CB    . CYS A 1 76  ? 10.350  8.731   35.732  1.00 39.57  ? 75  CYS A CB    1 
ATOM   621  S  SG    . CYS A 1 76  ? 9.402   10.188  36.259  1.00 56.70  ? 75  CYS A SG    1 
ATOM   622  N  N     . LEU A 1 77  ? 7.372   7.232   36.900  1.00 47.42  ? 76  LEU A N     1 
ATOM   623  C  CA    . LEU A 1 77  ? 5.928   7.179   36.696  1.00 46.51  ? 76  LEU A CA    1 
ATOM   624  C  C     . LEU A 1 77  ? 5.270   8.547   36.723  1.00 42.73  ? 76  LEU A C     1 
ATOM   625  O  O     . LEU A 1 77  ? 4.159   8.695   36.201  1.00 47.04  ? 76  LEU A O     1 
ATOM   626  C  CB    . LEU A 1 77  ? 5.254   6.306   37.756  1.00 42.98  ? 76  LEU A CB    1 
ATOM   627  C  CG    . LEU A 1 77  ? 5.730   4.860   37.856  1.00 46.17  ? 76  LEU A CG    1 
ATOM   628  C  CD1   . LEU A 1 77  ? 5.290   4.252   39.185  1.00 48.39  ? 76  LEU A CD1   1 
ATOM   629  C  CD2   . LEU A 1 77  ? 5.215   4.064   36.688  1.00 48.20  ? 76  LEU A CD2   1 
ATOM   630  N  N     . LYS A 1 78  ? 5.900   9.539   37.339  1.00 40.19  ? 77  LYS A N     1 
ATOM   631  C  CA    . LYS A 1 78  ? 5.286   10.854  37.385  1.00 40.95  ? 77  LYS A CA    1 
ATOM   632  C  C     . LYS A 1 78  ? 6.349   11.867  37.745  1.00 45.68  ? 77  LYS A C     1 
ATOM   633  O  O     . LYS A 1 78  ? 7.179   11.621  38.623  1.00 44.42  ? 77  LYS A O     1 
ATOM   634  C  CB    . LYS A 1 78  ? 4.123   10.900  38.390  1.00 46.20  ? 77  LYS A CB    1 
ATOM   635  C  CG    . LYS A 1 78  ? 3.545   12.283  38.649  1.00 47.86  ? 77  LYS A CG    1 
ATOM   636  C  CD    . LYS A 1 78  ? 2.557   12.253  39.824  1.00 49.72  ? 77  LYS A CD    1 
ATOM   637  C  CE    . LYS A 1 78  ? 1.110   12.117  39.350  1.00 62.68  ? 77  LYS A CE    1 
ATOM   638  N  NZ    . LYS A 1 78  ? 0.754   13.035  38.220  1.00 62.77  ? 77  LYS A NZ    1 
ATOM   639  N  N     . SER A 1 79  ? 6.325   12.998  37.054  1.00 46.52  ? 78  SER A N     1 
ATOM   640  C  CA    . SER A 1 79  ? 7.244   14.092  37.335  1.00 46.14  ? 78  SER A CA    1 
ATOM   641  C  C     . SER A 1 79  ? 6.416   15.357  37.454  1.00 54.12  ? 78  SER A C     1 
ATOM   642  O  O     . SER A 1 79  ? 5.812   15.804  36.474  1.00 56.34  ? 78  SER A O     1 
ATOM   643  C  CB    . SER A 1 79  ? 8.305   14.236  36.248  1.00 54.60  ? 78  SER A CB    1 
ATOM   644  O  OG    . SER A 1 79  ? 8.957   15.481  36.396  1.00 51.28  ? 78  SER A OG    1 
ATOM   645  N  N     . GLU A 1 80  ? 6.374   15.925  38.649  1.00 49.49  ? 79  GLU A N     1 
ATOM   646  C  CA    . GLU A 1 80  ? 5.610   17.132  38.891  1.00 54.81  ? 79  GLU A CA    1 
ATOM   647  C  C     . GLU A 1 80  ? 6.575   18.303  38.905  1.00 58.15  ? 79  GLU A C     1 
ATOM   648  O  O     . GLU A 1 80  ? 7.574   18.278  39.633  1.00 51.34  ? 79  GLU A O     1 
ATOM   649  C  CB    . GLU A 1 80  ? 4.859   17.044  40.216  1.00 51.71  ? 79  GLU A CB    1 
ATOM   650  C  CG    . GLU A 1 80  ? 3.937   15.855  40.321  1.00 48.11  ? 79  GLU A CG    1 
ATOM   651  C  CD    . GLU A 1 80  ? 3.415   15.660  41.728  1.00 52.61  ? 79  GLU A CD    1 
ATOM   652  O  OE1   . GLU A 1 80  ? 2.910   16.642  42.314  1.00 57.21  ? 79  GLU A OE1   1 
ATOM   653  O  OE2   . GLU A 1 80  ? 3.552   14.536  42.269  1.00 55.79  ? 79  GLU A OE2   1 
ATOM   654  N  N     . VAL A 1 81  ? 6.296   19.308  38.087  1.00 59.56  ? 80  VAL A N     1 
ATOM   655  C  CA    . VAL A 1 81  ? 7.043   20.549  38.121  1.00 61.47  ? 80  VAL A CA    1 
ATOM   656  C  C     . VAL A 1 81  ? 6.205   21.586  38.855  1.00 64.52  ? 80  VAL A C     1 
ATOM   657  O  O     . VAL A 1 81  ? 5.007   21.403  39.093  1.00 65.64  ? 80  VAL A O     1 
ATOM   658  C  CB    . VAL A 1 81  ? 7.434   21.021  36.706  1.00 67.43  ? 80  VAL A CB    1 
ATOM   659  C  CG1   . VAL A 1 81  ? 8.474   20.079  36.121  1.00 53.42  ? 80  VAL A CG1   1 
ATOM   660  C  CG2   . VAL A 1 81  ? 6.204   21.062  35.811  1.00 65.02  ? 80  VAL A CG2   1 
ATOM   661  N  N     . GLU A 1 82  ? 6.855   22.679  39.242  1.00 72.69  ? 81  GLU A N     1 
ATOM   662  C  CA    . GLU A 1 82  ? 6.242   23.745  40.038  1.00 73.86  ? 81  GLU A CA    1 
ATOM   663  C  C     . GLU A 1 82  ? 5.363   23.166  41.142  1.00 71.45  ? 81  GLU A C     1 
ATOM   664  O  O     . GLU A 1 82  ? 4.193   23.519  41.306  1.00 77.43  ? 81  GLU A O     1 
ATOM   665  C  CB    . GLU A 1 82  ? 5.454   24.717  39.162  1.00 86.05  ? 81  GLU A CB    1 
ATOM   666  C  CG    . GLU A 1 82  ? 5.338   26.109  39.784  1.00 98.53  ? 81  GLU A CG    1 
ATOM   667  C  CD    . GLU A 1 82  ? 4.630   27.111  38.891  1.00 109.91 ? 81  GLU A CD    1 
ATOM   668  O  OE1   . GLU A 1 82  ? 4.418   26.802  37.697  1.00 111.05 ? 81  GLU A OE1   1 
ATOM   669  O  OE2   . GLU A 1 82  ? 4.292   28.210  39.387  1.00 111.34 ? 81  GLU A OE2   1 
ATOM   670  N  N     . VAL A 1 83  ? 5.947   22.234  41.893  1.00 69.24  ? 82  VAL A N     1 
ATOM   671  C  CA    . VAL A 1 83  ? 5.276   21.681  43.058  1.00 64.27  ? 82  VAL A CA    1 
ATOM   672  C  C     . VAL A 1 83  ? 5.144   22.759  44.120  1.00 64.82  ? 82  VAL A C     1 
ATOM   673  O  O     . VAL A 1 83  ? 6.038   23.598  44.299  1.00 69.86  ? 82  VAL A O     1 
ATOM   674  C  CB    . VAL A 1 83  ? 6.046   20.460  43.582  1.00 63.83  ? 82  VAL A CB    1 
ATOM   675  C  CG1   . VAL A 1 83  ? 5.611   20.123  45.005  1.00 52.99  ? 82  VAL A CG1   1 
ATOM   676  C  CG2   . VAL A 1 83  ? 5.844   19.290  42.643  1.00 52.88  ? 82  VAL A CG2   1 
ATOM   677  N  N     . GLN A 1 84  ? 4.031   22.737  44.840  1.00 54.68  ? 83  GLN A N     1 
ATOM   678  C  CA    . GLN A 1 84  ? 3.719   23.820  45.753  1.00 64.28  ? 83  GLN A CA    1 
ATOM   679  C  C     . GLN A 1 84  ? 3.985   23.469  47.216  1.00 65.16  ? 83  GLN A C     1 
ATOM   680  O  O     . GLN A 1 84  ? 4.435   24.331  47.980  1.00 63.77  ? 83  GLN A O     1 
ATOM   681  C  CB    . GLN A 1 84  ? 2.256   24.217  45.559  1.00 72.99  ? 83  GLN A CB    1 
ATOM   682  C  CG    . GLN A 1 84  ? 2.020   25.017  44.279  1.00 77.01  ? 83  GLN A CG    1 
ATOM   683  C  CD    . GLN A 1 84  ? 2.765   26.329  44.265  1.00 75.49  ? 83  GLN A CD    1 
ATOM   684  O  OE1   . GLN A 1 84  ? 3.861   26.421  43.716  1.00 79.67  ? 83  GLN A OE1   1 
ATOM   685  N  NE2   . GLN A 1 84  ? 2.191   27.346  44.900  1.00 84.36  ? 83  GLN A NE2   1 
ATOM   686  N  N     . GLU A 1 85  ? 3.736   22.219  47.623  1.00 63.25  ? 84  GLU A N     1 
ATOM   687  C  CA    . GLU A 1 85  ? 3.944   21.767  48.995  1.00 59.95  ? 84  GLU A CA    1 
ATOM   688  C  C     . GLU A 1 85  ? 4.617   20.400  48.983  1.00 53.98  ? 84  GLU A C     1 
ATOM   689  O  O     . GLU A 1 85  ? 4.283   19.554  48.149  1.00 45.44  ? 84  GLU A O     1 
ATOM   690  C  CB    . GLU A 1 85  ? 2.615   21.662  49.767  1.00 64.44  ? 84  GLU A CB    1 
ATOM   691  C  CG    . GLU A 1 85  ? 2.581   22.408  51.095  1.00 73.64  ? 84  GLU A CG    1 
ATOM   692  C  CD    . GLU A 1 85  ? 1.186   22.920  51.460  1.00 87.30  ? 84  GLU A CD    1 
ATOM   693  O  OE1   . GLU A 1 85  ? 0.284   22.081  51.688  1.00 91.77  ? 84  GLU A OE1   1 
ATOM   694  O  OE2   . GLU A 1 85  ? 0.985   24.154  51.509  1.00 88.04  ? 84  GLU A OE2   1 
ATOM   695  N  N     . ARG A 1 86  ? 5.547   20.176  49.920  1.00 50.88  ? 85  ARG A N     1 
ATOM   696  C  CA    . ARG A 1 86  ? 6.158   18.855  50.064  1.00 47.42  ? 85  ARG A CA    1 
ATOM   697  C  C     . ARG A 1 86  ? 5.158   17.835  50.610  1.00 43.05  ? 85  ARG A C     1 
ATOM   698  O  O     . ARG A 1 86  ? 4.327   18.147  51.471  1.00 43.41  ? 85  ARG A O     1 
ATOM   699  C  CB    . ARG A 1 86  ? 7.389   18.916  50.974  1.00 48.17  ? 85  ARG A CB    1 
ATOM   700  C  CG    . ARG A 1 86  ? 8.487   19.897  50.519  1.00 51.28  ? 85  ARG A CG    1 
ATOM   701  C  CD    . ARG A 1 86  ? 9.634   19.976  51.523  1.00 48.35  ? 85  ARG A CD    1 
ATOM   702  N  NE    . ARG A 1 86  ? 10.769  20.762  51.039  1.00 53.51  ? 85  ARG A NE    1 
ATOM   703  C  CZ    . ARG A 1 86  ? 11.816  20.288  50.372  1.00 42.08  ? 85  ARG A CZ    1 
ATOM   704  N  NH1   . ARG A 1 86  ? 11.936  19.005  50.081  1.00 39.48  ? 85  ARG A NH1   1 
ATOM   705  N  NH2   . ARG A 1 86  ? 12.779  21.124  50.001  1.00 49.42  ? 85  ARG A NH2   1 
ATOM   706  N  N     . MET A 1 87  ? 5.237   16.608  50.081  1.00 41.59  ? 86  MET A N     1 
ATOM   707  C  CA    . MET A 1 87  ? 4.480   15.483  50.626  1.00 43.65  ? 86  MET A CA    1 
ATOM   708  C  C     . MET A 1 87  ? 5.072   15.035  51.965  1.00 47.33  ? 86  MET A C     1 
ATOM   709  O  O     . MET A 1 87  ? 4.336   14.638  52.879  1.00 42.74  ? 86  MET A O     1 
ATOM   710  C  CB    . MET A 1 87  ? 4.529   14.306  49.646  1.00 38.16  ? 86  MET A CB    1 
ATOM   711  C  CG    . MET A 1 87  ? 3.487   14.175  48.502  1.00 46.42  ? 86  MET A CG    1 
ATOM   712  S  SD    . MET A 1 87  ? 1.724   14.505  48.680  1.00 89.04  ? 86  MET A SD    1 
ATOM   713  C  CE    . MET A 1 87  ? 1.381   14.054  50.373  1.00 67.43  ? 86  MET A CE    1 
ATOM   714  N  N     . PHE A 1 88  ? 6.402   15.082  52.096  1.00 36.52  ? 87  PHE A N     1 
ATOM   715  C  CA    . PHE A 1 88  ? 7.116   14.444  53.208  1.00 35.89  ? 87  PHE A CA    1 
ATOM   716  C  C     . PHE A 1 88  ? 8.116   15.402  53.846  1.00 36.91  ? 87  PHE A C     1 
ATOM   717  O  O     . PHE A 1 88  ? 9.308   15.111  53.907  1.00 38.01  ? 87  PHE A O     1 
ATOM   718  C  CB    . PHE A 1 88  ? 7.820   13.186  52.702  1.00 33.66  ? 87  PHE A CB    1 
ATOM   719  C  CG    . PHE A 1 88  ? 6.899   12.236  51.987  1.00 38.70  ? 87  PHE A CG    1 
ATOM   720  C  CD1   . PHE A 1 88  ? 5.921   11.530  52.684  1.00 38.14  ? 87  PHE A CD1   1 
ATOM   721  C  CD2   . PHE A 1 88  ? 6.981   12.086  50.611  1.00 33.99  ? 87  PHE A CD2   1 
ATOM   722  C  CE1   . PHE A 1 88  ? 5.058   10.670  52.027  1.00 35.51  ? 87  PHE A CE1   1 
ATOM   723  C  CE2   . PHE A 1 88  ? 6.126   11.231  49.936  1.00 31.05  ? 87  PHE A CE2   1 
ATOM   724  C  CZ    . PHE A 1 88  ? 5.155   10.519  50.645  1.00 37.96  ? 87  PHE A CZ    1 
ATOM   725  N  N     . PRO A 1 89  ? 7.653   16.538  54.378  1.00 43.86  ? 88  PRO A N     1 
ATOM   726  C  CA    . PRO A 1 89  ? 8.592   17.608  54.770  1.00 44.20  ? 88  PRO A CA    1 
ATOM   727  C  C     . PRO A 1 89  ? 9.612   17.198  55.820  1.00 40.93  ? 88  PRO A C     1 
ATOM   728  O  O     . PRO A 1 89  ? 10.678  17.814  55.891  1.00 43.37  ? 88  PRO A O     1 
ATOM   729  C  CB    . PRO A 1 89  ? 7.668   18.707  55.319  1.00 42.81  ? 88  PRO A CB    1 
ATOM   730  C  CG    . PRO A 1 89  ? 6.365   18.037  55.578  1.00 42.09  ? 88  PRO A CG    1 
ATOM   731  C  CD    . PRO A 1 89  ? 6.255   16.930  54.596  1.00 41.43  ? 88  PRO A CD    1 
ATOM   732  N  N     . ASP A 1 90  ? 9.321   16.190  56.635  1.00 39.04  ? 89  ASP A N     1 
ATOM   733  C  CA    . ASP A 1 90  ? 10.190  15.786  57.733  1.00 38.21  ? 89  ASP A CA    1 
ATOM   734  C  C     . ASP A 1 90  ? 11.079  14.595  57.391  1.00 36.28  ? 89  ASP A C     1 
ATOM   735  O  O     . ASP A 1 90  ? 11.833  14.135  58.254  1.00 34.16  ? 89  ASP A O     1 
ATOM   736  C  CB    . ASP A 1 90  ? 9.332   15.446  58.952  1.00 40.92  ? 89  ASP A CB    1 
ATOM   737  C  CG    . ASP A 1 90  ? 8.426   16.595  59.365  1.00 51.29  ? 89  ASP A CG    1 
ATOM   738  O  OD1   . ASP A 1 90  ? 8.960   17.705  59.566  1.00 49.69  ? 89  ASP A OD1   1 
ATOM   739  O  OD2   . ASP A 1 90  ? 7.187   16.398  59.429  1.00 52.58  ? 89  ASP A OD2   1 
ATOM   740  N  N     . TRP A 1 91  ? 10.998  14.063  56.173  1.00 31.83  ? 90  TRP A N     1 
ATOM   741  C  CA    . TRP A 1 91  ? 11.734  12.857  55.784  1.00 31.11  ? 90  TRP A CA    1 
ATOM   742  C  C     . TRP A 1 91  ? 12.745  13.210  54.697  1.00 33.00  ? 90  TRP A C     1 
ATOM   743  O  O     . TRP A 1 91  ? 12.359  13.381  53.537  1.00 34.54  ? 90  TRP A O     1 
ATOM   744  C  CB    . TRP A 1 91  ? 10.796  11.771  55.267  1.00 29.79  ? 90  TRP A CB    1 
ATOM   745  C  CG    . TRP A 1 91  ? 9.743   11.275  56.204  1.00 34.54  ? 90  TRP A CG    1 
ATOM   746  C  CD1   . TRP A 1 91  ? 9.626   11.538  57.541  1.00 33.75  ? 90  TRP A CD1   1 
ATOM   747  C  CD2   . TRP A 1 91  ? 8.651   10.407  55.868  1.00 33.18  ? 90  TRP A CD2   1 
ATOM   748  N  NE1   . TRP A 1 91  ? 8.531   10.878  58.060  1.00 33.11  ? 90  TRP A NE1   1 
ATOM   749  C  CE2   . TRP A 1 91  ? 7.914   10.182  57.048  1.00 38.17  ? 90  TRP A CE2   1 
ATOM   750  C  CE3   . TRP A 1 91  ? 8.221   9.804   54.677  1.00 33.74  ? 90  TRP A CE3   1 
ATOM   751  C  CZ2   . TRP A 1 91  ? 6.764   9.378   57.075  1.00 38.09  ? 90  TRP A CZ2   1 
ATOM   752  C  CZ3   . TRP A 1 91  ? 7.081   8.995   54.711  1.00 32.50  ? 90  TRP A CZ3   1 
ATOM   753  C  CH2   . TRP A 1 91  ? 6.366   8.799   55.900  1.00 35.30  ? 90  TRP A CH2   1 
ATOM   754  N  N     . SER A 1 92  ? 14.030  13.289  55.046  1.00 32.15  ? 91  SER A N     1 
ATOM   755  C  CA    . SER A 1 92  ? 15.048  13.423  54.002  1.00 34.51  ? 91  SER A CA    1 
ATOM   756  C  C     . SER A 1 92  ? 15.020  12.218  53.083  1.00 35.27  ? 91  SER A C     1 
ATOM   757  O  O     . SER A 1 92  ? 15.039  12.355  51.854  1.00 33.88  ? 91  SER A O     1 
ATOM   758  C  CB    . SER A 1 92  ? 16.440  13.592  54.623  1.00 32.94  ? 91  SER A CB    1 
ATOM   759  O  OG    . SER A 1 92  ? 16.518  14.801  55.372  1.00 34.91  ? 91  SER A OG    1 
ATOM   760  N  N     . MET A 1 93  ? 14.996  11.019  53.664  1.00 31.04  ? 92  MET A N     1 
ATOM   761  C  CA    . MET A 1 93  ? 14.610  9.830   52.906  1.00 36.71  ? 92  MET A CA    1 
ATOM   762  C  C     . MET A 1 93  ? 14.160  8.825   53.956  1.00 37.34  ? 92  MET A C     1 
ATOM   763  O  O     . MET A 1 93  ? 14.990  8.322   54.720  1.00 32.28  ? 92  MET A O     1 
ATOM   764  C  CB    . MET A 1 93  ? 15.766  9.281   52.076  1.00 36.27  ? 92  MET A CB    1 
ATOM   765  C  CG    . MET A 1 93  ? 15.388  8.224   51.008  1.00 37.00  ? 92  MET A CG    1 
ATOM   766  S  SD    . MET A 1 93  ? 13.700  8.345   50.331  1.00 37.81  ? 92  MET A SD    1 
ATOM   767  C  CE    . MET A 1 93  ? 14.020  9.668   49.183  1.00 37.80  ? 92  MET A CE    1 
ATOM   768  N  N     . GLN A 1 94  ? 12.852  8.597   54.050  1.00 33.96  ? 93  GLN A N     1 
ATOM   769  C  CA    . GLN A 1 94  ? 12.318  7.572   54.930  1.00 31.44  ? 93  GLN A CA    1 
ATOM   770  C  C     . GLN A 1 94  ? 12.292  6.258   54.169  1.00 35.60  ? 93  GLN A C     1 
ATOM   771  O  O     . GLN A 1 94  ? 11.773  6.193   53.049  1.00 39.82  ? 93  GLN A O     1 
ATOM   772  C  CB    . GLN A 1 94  ? 10.911  7.932   55.406  1.00 33.38  ? 93  GLN A CB    1 
ATOM   773  C  CG    . GLN A 1 94  ? 10.244  6.831   56.201  1.00 38.73  ? 93  GLN A CG    1 
ATOM   774  C  CD    . GLN A 1 94  ? 10.674  6.792   57.658  1.00 38.94  ? 93  GLN A CD    1 
ATOM   775  O  OE1   . GLN A 1 94  ? 11.565  7.515   58.077  1.00 35.85  ? 93  GLN A OE1   1 
ATOM   776  N  NE2   . GLN A 1 94  ? 10.054  5.903   58.428  1.00 41.21  ? 93  GLN A NE2   1 
ATOM   777  N  N     . THR A 1 95  ? 12.815  5.206   54.778  1.00 31.08  ? 94  THR A N     1 
ATOM   778  C  CA    . THR A 1 95  ? 12.865  3.901   54.129  1.00 38.84  ? 94  THR A CA    1 
ATOM   779  C  C     . THR A 1 95  ? 11.867  2.953   54.784  1.00 39.84  ? 94  THR A C     1 
ATOM   780  O  O     . THR A 1 95  ? 11.799  2.864   56.018  1.00 31.33  ? 94  THR A O     1 
ATOM   781  C  CB    . THR A 1 95  ? 14.284  3.339   54.187  1.00 42.78  ? 94  THR A CB    1 
ATOM   782  O  OG1   . THR A 1 95  ? 15.159  4.282   53.558  1.00 46.24  ? 94  THR A OG1   1 
ATOM   783  C  CG2   . THR A 1 95  ? 14.374  2.005   53.438  1.00 42.70  ? 94  THR A CG2   1 
ATOM   784  N  N     . ILE A 1 96  ? 11.062  2.287   53.953  1.00 38.69  ? 95  ILE A N     1 
ATOM   785  C  CA    . ILE A 1 96  ? 10.042  1.354   54.409  1.00 36.50  ? 95  ILE A CA    1 
ATOM   786  C  C     . ILE A 1 96  ? 10.233  0.037   53.679  1.00 39.48  ? 95  ILE A C     1 
ATOM   787  O  O     . ILE A 1 96  ? 9.819   -0.109  52.525  1.00 37.41  ? 95  ILE A O     1 
ATOM   788  C  CB    . ILE A 1 96  ? 8.625   1.882   54.200  1.00 36.29  ? 95  ILE A CB    1 
ATOM   789  C  CG1   . ILE A 1 96  ? 8.505   3.322   54.716  1.00 37.92  ? 95  ILE A CG1   1 
ATOM   790  C  CG2   . ILE A 1 96  ? 7.618   0.894   54.780  1.00 33.41  ? 95  ILE A CG2   1 
ATOM   791  C  CD1   . ILE A 1 96  ? 7.069   3.931   54.564  1.00 34.74  ? 95  ILE A CD1   1 
ATOM   792  N  N     . ASN A 1 97  ? 10.796  -0.943  54.371  1.00 35.38  ? 96  ASN A N     1 
ATOM   793  C  CA    . ASN A 1 97  ? 11.036  -2.267  53.813  1.00 38.56  ? 96  ASN A CA    1 
ATOM   794  C  C     . ASN A 1 97  ? 9.760   -3.083  54.027  1.00 38.72  ? 96  ASN A C     1 
ATOM   795  O  O     . ASN A 1 97  ? 9.496   -3.565  55.129  1.00 37.30  ? 96  ASN A O     1 
ATOM   796  C  CB    . ASN A 1 97  ? 12.267  -2.881  54.478  1.00 41.12  ? 96  ASN A CB    1 
ATOM   797  C  CG    . ASN A 1 97  ? 12.651  -4.223  53.895  1.00 49.12  ? 96  ASN A CG    1 
ATOM   798  O  OD1   . ASN A 1 97  ? 11.795  -4.980  53.418  1.00 43.80  ? 96  ASN A OD1   1 
ATOM   799  N  ND2   . ASN A 1 97  ? 13.965  -4.511  53.890  1.00 41.60  ? 96  ASN A ND2   1 
ATOM   800  N  N     . LEU A 1 98  ? 8.954   -3.234  52.963  1.00 34.66  ? 97  LEU A N     1 
ATOM   801  C  CA    . LEU A 1 98  ? 7.671   -3.912  53.110  1.00 34.89  ? 97  LEU A CA    1 
ATOM   802  C  C     . LEU A 1 98  ? 7.837   -5.414  53.276  1.00 36.64  ? 97  LEU A C     1 
ATOM   803  O  O     . LEU A 1 98  ? 6.972   -6.059  53.880  1.00 39.98  ? 97  LEU A O     1 
ATOM   804  C  CB    . LEU A 1 98  ? 6.762   -3.591  51.915  1.00 34.24  ? 97  LEU A CB    1 
ATOM   805  C  CG    . LEU A 1 98  ? 6.258   -2.142  51.947  1.00 34.79  ? 97  LEU A CG    1 
ATOM   806  C  CD1   . LEU A 1 98  ? 5.512   -1.766  50.667  1.00 49.18  ? 97  LEU A CD1   1 
ATOM   807  C  CD2   . LEU A 1 98  ? 5.352   -1.881  53.164  1.00 38.09  ? 97  LEU A CD2   1 
ATOM   808  N  N     . ASP A 1 99  ? 8.940   -5.982  52.773  1.00 37.84  ? 98  ASP A N     1 
ATOM   809  C  CA    . ASP A 1 99  ? 9.214   -7.408  52.978  1.00 42.41  ? 98  ASP A CA    1 
ATOM   810  C  C     . ASP A 1 99  ? 9.270   -7.761  54.462  1.00 45.88  ? 98  ASP A C     1 
ATOM   811  O  O     . ASP A 1 99  ? 8.853   -8.854  54.863  1.00 48.06  ? 98  ASP A O     1 
ATOM   812  C  CB    . ASP A 1 99  ? 10.538  -7.805  52.328  1.00 43.20  ? 98  ASP A CB    1 
ATOM   813  C  CG    . ASP A 1 99  ? 10.493  -7.775  50.821  1.00 49.26  ? 98  ASP A CG    1 
ATOM   814  O  OD1   . ASP A 1 99  ? 9.500   -8.246  50.221  1.00 46.65  ? 98  ASP A OD1   1 
ATOM   815  O  OD2   . ASP A 1 99  ? 11.482  -7.273  50.243  1.00 61.21  ? 98  ASP A OD2   1 
ATOM   816  N  N     . GLU A 1 100 ? 9.813   -6.865  55.288  1.00 39.33  ? 99  GLU A N     1 
ATOM   817  C  CA    . GLU A 1 100 ? 9.931   -7.119  56.716  1.00 42.17  ? 99  GLU A CA    1 
ATOM   818  C  C     . GLU A 1 100 ? 8.684   -6.714  57.475  1.00 44.75  ? 99  GLU A C     1 
ATOM   819  O  O     . GLU A 1 100 ? 8.554   -7.035  58.658  1.00 44.98  ? 99  GLU A O     1 
ATOM   820  C  CB    . GLU A 1 100 ? 11.132  -6.364  57.292  1.00 39.50  ? 99  GLU A CB    1 
ATOM   821  C  CG    . GLU A 1 100 ? 12.401  -6.498  56.464  1.00 54.27  ? 99  GLU A CG    1 
ATOM   822  C  CD    . GLU A 1 100 ? 13.659  -6.098  57.233  1.00 58.03  ? 99  GLU A CD    1 
ATOM   823  O  OE1   . GLU A 1 100 ? 13.691  -4.976  57.793  1.00 56.16  ? 99  GLU A OE1   1 
ATOM   824  O  OE2   . GLU A 1 100 ? 14.631  -6.880  57.230  1.00 59.57  ? 99  GLU A OE2   1 
ATOM   825  N  N     . ASN A 1 101 ? 7.775   -5.999  56.836  1.00 36.89  ? 100 ASN A N     1 
ATOM   826  C  CA    . ASN A 1 101 ? 6.608   -5.533  57.549  1.00 38.59  ? 100 ASN A CA    1 
ATOM   827  C  C     . ASN A 1 101 ? 5.574   -6.640  57.608  1.00 43.55  ? 100 ASN A C     1 
ATOM   828  O  O     . ASN A 1 101 ? 5.246   -7.255  56.589  1.00 44.59  ? 100 ASN A O     1 
ATOM   829  C  CB    . ASN A 1 101 ? 6.041   -4.281  56.900  1.00 38.31  ? 100 ASN A CB    1 
ATOM   830  C  CG    . ASN A 1 101 ? 4.937   -3.691  57.716  1.00 43.10  ? 100 ASN A CG    1 
ATOM   831  O  OD1   . ASN A 1 101 ? 3.935   -4.352  57.966  1.00 47.90  ? 100 ASN A OD1   1 
ATOM   832  N  ND2   . ASN A 1 101 ? 5.125   -2.471  58.188  1.00 37.36  ? 100 ASN A ND2   1 
ATOM   833  N  N     . THR A 1 102 ? 5.075   -6.895  58.813  1.00 41.62  ? 101 THR A N     1 
ATOM   834  C  CA    . THR A 1 102 ? 4.083   -7.930  59.062  1.00 53.69  ? 101 THR A CA    1 
ATOM   835  C  C     . THR A 1 102 ? 2.776   -7.353  59.600  1.00 48.98  ? 101 THR A C     1 
ATOM   836  O  O     . THR A 1 102 ? 1.967   -8.096  60.157  1.00 46.12  ? 101 THR A O     1 
ATOM   837  C  CB    . THR A 1 102 ? 4.644   -8.968  60.038  1.00 53.42  ? 101 THR A CB    1 
ATOM   838  O  OG1   . THR A 1 102 ? 4.900   -8.336  61.301  1.00 59.82  ? 101 THR A OG1   1 
ATOM   839  C  CG2   . THR A 1 102 ? 5.956   -9.560  59.508  1.00 50.97  ? 101 THR A CG2   1 
ATOM   840  N  N     . ASP A 1 103 ? 2.551   -6.047  59.453  1.00 45.79  ? 102 ASP A N     1 
ATOM   841  C  CA    . ASP A 1 103 ? 1.374   -5.428  60.061  1.00 45.83  ? 102 ASP A CA    1 
ATOM   842  C  C     . ASP A 1 103 ? 0.092   -5.948  59.406  1.00 48.38  ? 102 ASP A C     1 
ATOM   843  O  O     . ASP A 1 103 ? 0.048   -6.187  58.191  1.00 45.57  ? 102 ASP A O     1 
ATOM   844  C  CB    . ASP A 1 103 ? 1.430   -3.902  59.934  1.00 44.46  ? 102 ASP A CB    1 
ATOM   845  C  CG    . ASP A 1 103 ? 2.530   -3.278  60.789  1.00 51.35  ? 102 ASP A CG    1 
ATOM   846  O  OD1   . ASP A 1 103 ? 2.898   -3.881  61.821  1.00 45.73  ? 102 ASP A OD1   1 
ATOM   847  O  OD2   . ASP A 1 103 ? 2.997   -2.165  60.436  1.00 50.45  ? 102 ASP A OD2   1 
ATOM   848  N  N     . PHE A 1 104 ? -0.960  -6.082  60.229  1.00 39.96  ? 103 PHE A N     1 
ATOM   849  C  CA    . PHE A 1 104 ? -2.247  -6.656  59.829  1.00 38.76  ? 103 PHE A CA    1 
ATOM   850  C  C     . PHE A 1 104 ? -2.807  -6.054  58.545  1.00 39.02  ? 103 PHE A C     1 
ATOM   851  O  O     . PHE A 1 104 ? -3.195  -6.779  57.623  1.00 39.94  ? 103 PHE A O     1 
ATOM   852  C  CB    . PHE A 1 104 ? -3.255  -6.458  60.959  1.00 47.13  ? 103 PHE A CB    1 
ATOM   853  C  CG    . PHE A 1 104 ? -4.606  -7.094  60.703  1.00 44.84  ? 103 PHE A CG    1 
ATOM   854  C  CD1   . PHE A 1 104 ? -4.746  -8.467  60.632  1.00 47.33  ? 103 PHE A CD1   1 
ATOM   855  C  CD2   . PHE A 1 104 ? -5.729  -6.305  60.539  1.00 43.94  ? 103 PHE A CD2   1 
ATOM   856  C  CE1   . PHE A 1 104 ? -5.973  -9.038  60.427  1.00 38.95  ? 103 PHE A CE1   1 
ATOM   857  C  CE2   . PHE A 1 104 ? -6.970  -6.869  60.326  1.00 44.26  ? 103 PHE A CE2   1 
ATOM   858  C  CZ    . PHE A 1 104 ? -7.089  -8.239  60.269  1.00 45.02  ? 103 PHE A CZ    1 
ATOM   859  N  N     . LEU A 1 105 ? -2.940  -4.730  58.504  1.00 38.62  ? 104 LEU A N     1 
ATOM   860  C  CA    . LEU A 1 105 ? -3.517  -4.067  57.347  1.00 37.23  ? 104 LEU A CA    1 
ATOM   861  C  C     . LEU A 1 105 ? -2.541  -3.987  56.177  1.00 41.25  ? 104 LEU A C     1 
ATOM   862  O  O     . LEU A 1 105 ? -2.981  -3.860  55.026  1.00 38.53  ? 104 LEU A O     1 
ATOM   863  C  CB    . LEU A 1 105 ? -3.983  -2.661  57.734  1.00 35.50  ? 104 LEU A CB    1 
ATOM   864  C  CG    . LEU A 1 105 ? -5.211  -2.608  58.674  1.00 42.84  ? 104 LEU A CG    1 
ATOM   865  C  CD1   . LEU A 1 105 ? -5.709  -1.181  58.867  1.00 49.50  ? 104 LEU A CD1   1 
ATOM   866  C  CD2   . LEU A 1 105 ? -6.373  -3.486  58.192  1.00 43.47  ? 104 LEU A CD2   1 
ATOM   867  N  N     . ILE A 1 106 ? -1.232  -4.069  56.430  1.00 34.86  ? 105 ILE A N     1 
ATOM   868  C  CA    . ILE A 1 106 ? -0.301  -3.865  55.327  1.00 31.39  ? 105 ILE A CA    1 
ATOM   869  C  C     . ILE A 1 106 ? -0.150  -5.130  54.484  1.00 39.27  ? 105 ILE A C     1 
ATOM   870  O  O     . ILE A 1 106 ? 0.155   -5.044  53.283  1.00 37.10  ? 105 ILE A O     1 
ATOM   871  C  CB    . ILE A 1 106 ? 1.040   -3.334  55.865  1.00 37.53  ? 105 ILE A CB    1 
ATOM   872  C  CG1   . ILE A 1 106 ? 0.859   -1.869  56.280  1.00 41.90  ? 105 ILE A CG1   1 
ATOM   873  C  CG2   . ILE A 1 106 ? 2.153   -3.417  54.807  1.00 35.80  ? 105 ILE A CG2   1 
ATOM   874  C  CD1   . ILE A 1 106 ? 2.118   -1.150  56.704  1.00 39.53  ? 105 ILE A CD1   1 
ATOM   875  N  N     . ARG A 1 107 ? -0.391  -6.309  55.064  1.00 36.79  ? 106 ARG A N     1 
ATOM   876  C  CA    . ARG A 1 107 ? -0.316  -7.549  54.286  1.00 40.64  ? 106 ARG A CA    1 
ATOM   877  C  C     . ARG A 1 107 ? -1.190  -7.549  53.029  1.00 37.62  ? 106 ARG A C     1 
ATOM   878  O  O     . ARG A 1 107 ? -0.654  -7.828  51.942  1.00 39.48  ? 106 ARG A O     1 
ATOM   879  C  CB    . ARG A 1 107 ? -0.617  -8.739  55.208  1.00 35.49  ? 106 ARG A CB    1 
ATOM   880  C  CG    . ARG A 1 107 ? -0.420  -10.116 54.568  1.00 47.28  ? 106 ARG A CG    1 
ATOM   881  C  CD    . ARG A 1 107 ? -0.862  -11.231 55.543  1.00 56.78  ? 106 ARG A CD    1 
ATOM   882  N  NE    . ARG A 1 107 ? -0.889  -12.589 54.993  1.00 66.36  ? 106 ARG A NE    1 
ATOM   883  C  CZ    . ARG A 1 107 ? -1.488  -12.954 53.861  1.00 62.66  ? 106 ARG A CZ    1 
ATOM   884  N  NH1   . ARG A 1 107 ? -2.213  -12.106 53.153  1.00 53.73  ? 106 ARG A NH1   1 
ATOM   885  N  NH2   . ARG A 1 107 ? -1.402  -14.219 53.457  1.00 52.06  ? 106 ARG A NH2   1 
ATOM   886  N  N     . PRO A 1 108 ? -2.490  -7.232  53.078  1.00 35.69  ? 107 PRO A N     1 
ATOM   887  C  CA    . PRO A 1 108 ? -3.253  -7.178  51.817  1.00 38.72  ? 107 PRO A CA    1 
ATOM   888  C  C     . PRO A 1 108 ? -2.793  -6.065  50.899  1.00 38.32  ? 107 PRO A C     1 
ATOM   889  O  O     . PRO A 1 108 ? -2.873  -6.221  49.678  1.00 41.65  ? 107 PRO A O     1 
ATOM   890  C  CB    . PRO A 1 108 ? -4.703  -6.961  52.274  1.00 36.21  ? 107 PRO A CB    1 
ATOM   891  C  CG    . PRO A 1 108 ? -4.572  -6.285  53.618  1.00 37.18  ? 107 PRO A CG    1 
ATOM   892  C  CD    . PRO A 1 108 ? -3.329  -6.885  54.241  1.00 38.75  ? 107 PRO A CD    1 
ATOM   893  N  N     . ILE A 1 109 ? -2.281  -4.960  51.444  1.00 37.74  ? 108 ILE A N     1 
ATOM   894  C  CA    . ILE A 1 109 ? -1.771  -3.874  50.605  1.00 31.83  ? 108 ILE A CA    1 
ATOM   895  C  C     . ILE A 1 109 ? -0.536  -4.322  49.832  1.00 38.97  ? 108 ILE A C     1 
ATOM   896  O  O     . ILE A 1 109 ? -0.329  -3.914  48.678  1.00 33.36  ? 108 ILE A O     1 
ATOM   897  C  CB    . ILE A 1 109 ? -1.485  -2.632  51.466  1.00 41.31  ? 108 ILE A CB    1 
ATOM   898  C  CG1   . ILE A 1 109 ? -2.775  -2.140  52.128  1.00 35.03  ? 108 ILE A CG1   1 
ATOM   899  C  CG2   . ILE A 1 109 ? -0.863  -1.547  50.620  1.00 40.36  ? 108 ILE A CG2   1 
ATOM   900  C  CD1   . ILE A 1 109 ? -2.549  -1.198  53.319  1.00 35.25  ? 108 ILE A CD1   1 
ATOM   901  N  N     . LYS A 1 110 ? 0.301   -5.170  50.447  1.00 34.03  ? 109 LYS A N     1 
ATOM   902  C  CA    . LYS A 1 110 ? 1.493   -5.682  49.759  1.00 35.68  ? 109 LYS A CA    1 
ATOM   903  C  C     . LYS A 1 110 ? 1.106   -6.582  48.588  1.00 37.90  ? 109 LYS A C     1 
ATOM   904  O  O     . LYS A 1 110 ? 1.734   -6.542  47.524  1.00 38.94  ? 109 LYS A O     1 
ATOM   905  C  CB    . LYS A 1 110 ? 2.381   -6.447  50.745  1.00 39.59  ? 109 LYS A CB    1 
ATOM   906  C  CG    . LYS A 1 110 ? 3.196   -5.522  51.661  1.00 35.87  ? 109 LYS A CG    1 
ATOM   907  C  CD    . LYS A 1 110 ? 3.686   -6.251  52.900  1.00 38.61  ? 109 LYS A CD    1 
ATOM   908  C  CE    . LYS A 1 110 ? 4.334   -7.577  52.520  1.00 43.04  ? 109 LYS A CE    1 
ATOM   909  N  NZ    . LYS A 1 110 ? 5.110   -8.183  53.633  1.00 39.00  ? 109 LYS A NZ    1 
ATOM   910  N  N     . VAL A 1 111 ? 0.077   -7.416  48.775  1.00 37.20  ? 110 VAL A N     1 
ATOM   911  C  CA    . VAL A 1 111 ? -0.428  -8.234  47.672  1.00 38.72  ? 110 VAL A CA    1 
ATOM   912  C  C     . VAL A 1 111 ? -0.942  -7.344  46.546  1.00 41.67  ? 110 VAL A C     1 
ATOM   913  O  O     . VAL A 1 111 ? -0.597  -7.523  45.370  1.00 42.33  ? 110 VAL A O     1 
ATOM   914  C  CB    . VAL A 1 111 ? -1.521  -9.195  48.172  1.00 44.84  ? 110 VAL A CB    1 
ATOM   915  C  CG1   . VAL A 1 111 ? -1.978  -10.106 47.027  1.00 43.99  ? 110 VAL A CG1   1 
ATOM   916  C  CG2   . VAL A 1 111 ? -1.009  -10.016 49.359  1.00 40.57  ? 110 VAL A CG2   1 
ATOM   917  N  N     . LEU A 1 112 ? -1.746  -6.346  46.898  1.00 35.72  ? 111 LEU A N     1 
ATOM   918  C  CA    . LEU A 1 112 ? -2.254  -5.411  45.902  1.00 40.98  ? 111 LEU A CA    1 
ATOM   919  C  C     . LEU A 1 112 ? -1.121  -4.675  45.193  1.00 41.56  ? 111 LEU A C     1 
ATOM   920  O  O     . LEU A 1 112 ? -1.074  -4.634  43.953  1.00 35.56  ? 111 LEU A O     1 
ATOM   921  C  CB    . LEU A 1 112 ? -3.224  -4.436  46.571  1.00 41.05  ? 111 LEU A CB    1 
ATOM   922  C  CG    . LEU A 1 112 ? -3.832  -3.384  45.659  1.00 44.44  ? 111 LEU A CG    1 
ATOM   923  C  CD1   . LEU A 1 112 ? -4.835  -4.039  44.725  1.00 48.83  ? 111 LEU A CD1   1 
ATOM   924  C  CD2   . LEU A 1 112 ? -4.483  -2.280  46.494  1.00 40.68  ? 111 LEU A CD2   1 
ATOM   925  N  N     . LEU A 1 113 ? -0.199  -4.082  45.963  1.00 41.07  ? 112 LEU A N     1 
ATOM   926  C  CA    . LEU A 1 113 ? 0.967   -3.419  45.375  1.00 41.71  ? 112 LEU A CA    1 
ATOM   927  C  C     . LEU A 1 113 ? 1.709   -4.342  44.422  1.00 39.25  ? 112 LEU A C     1 
ATOM   928  O  O     . LEU A 1 113 ? 2.149   -3.925  43.344  1.00 41.86  ? 112 LEU A O     1 
ATOM   929  C  CB    . LEU A 1 113 ? 1.949   -2.971  46.459  1.00 42.26  ? 112 LEU A CB    1 
ATOM   930  C  CG    . LEU A 1 113 ? 1.874   -1.547  46.977  1.00 53.06  ? 112 LEU A CG    1 
ATOM   931  C  CD1   . LEU A 1 113 ? 2.892   -1.407  48.108  1.00 50.55  ? 112 LEU A CD1   1 
ATOM   932  C  CD2   . LEU A 1 113 ? 2.078   -0.521  45.878  1.00 54.33  ? 112 LEU A CD2   1 
ATOM   933  N  N     . GLN A 1 114 ? 1.917   -5.586  44.843  1.00 37.22  ? 113 GLN A N     1 
ATOM   934  C  CA    . GLN A 1 114 ? 2.626   -6.544  44.009  1.00 41.50  ? 113 GLN A CA    1 
ATOM   935  C  C     . GLN A 1 114 ? 1.881   -6.749  42.690  1.00 45.76  ? 113 GLN A C     1 
ATOM   936  O  O     . GLN A 1 114 ? 2.438   -6.543  41.609  1.00 37.14  ? 113 GLN A O     1 
ATOM   937  C  CB    . GLN A 1 114 ? 2.781   -7.855  44.777  1.00 43.39  ? 113 GLN A CB    1 
ATOM   938  C  CG    . GLN A 1 114 ? 3.431   -8.985  44.018  1.00 57.74  ? 113 GLN A CG    1 
ATOM   939  C  CD    . GLN A 1 114 ? 4.891   -9.161  44.382  1.00 65.65  ? 113 GLN A CD    1 
ATOM   940  O  OE1   . GLN A 1 114 ? 5.732   -8.327  44.050  1.00 66.91  ? 113 GLN A OE1   1 
ATOM   941  N  NE2   . GLN A 1 114 ? 5.195   -10.242 45.095  1.00 68.93  ? 113 GLN A NE2   1 
ATOM   942  N  N     . THR A 1 115 ? 0.587   -7.087  42.773  1.00 45.29  ? 114 THR A N     1 
ATOM   943  C  CA    . THR A 1 115 ? -0.200  -7.376  41.576  1.00 44.81  ? 114 THR A CA    1 
ATOM   944  C  C     . THR A 1 115 ? -0.258  -6.164  40.656  1.00 44.19  ? 114 THR A C     1 
ATOM   945  O  O     . THR A 1 115 ? -0.068  -6.287  39.438  1.00 41.88  ? 114 THR A O     1 
ATOM   946  C  CB    . THR A 1 115 ? -1.606  -7.827  41.978  1.00 46.33  ? 114 THR A CB    1 
ATOM   947  O  OG1   . THR A 1 115 ? -1.511  -9.029  42.746  1.00 45.74  ? 114 THR A OG1   1 
ATOM   948  C  CG2   . THR A 1 115 ? -2.488  -8.092  40.740  1.00 38.84  ? 114 THR A CG2   1 
ATOM   949  N  N     . LEU A 1 116 ? -0.453  -4.975  41.233  1.00 40.78  ? 115 LEU A N     1 
ATOM   950  C  CA    . LEU A 1 116 ? -0.567  -3.757  40.439  1.00 37.28  ? 115 LEU A CA    1 
ATOM   951  C  C     . LEU A 1 116 ? 0.748   -3.409  39.748  1.00 45.45  ? 115 LEU A C     1 
ATOM   952  O  O     . LEU A 1 116 ? 0.753   -2.915  38.611  1.00 40.95  ? 115 LEU A O     1 
ATOM   953  C  CB    . LEU A 1 116 ? -1.034  -2.625  41.341  1.00 44.24  ? 115 LEU A CB    1 
ATOM   954  C  CG    . LEU A 1 116 ? -1.409  -1.262  40.765  1.00 58.26  ? 115 LEU A CG    1 
ATOM   955  C  CD1   . LEU A 1 116 ? -2.485  -1.375  39.670  1.00 46.44  ? 115 LEU A CD1   1 
ATOM   956  C  CD2   . LEU A 1 116 ? -1.889  -0.378  41.904  1.00 49.37  ? 115 LEU A CD2   1 
ATOM   957  N  N     . THR A 1 117 ? 1.879   -3.680  40.409  1.00 39.31  ? 116 THR A N     1 
ATOM   958  C  CA    . THR A 1 117 ? 3.181   -3.444  39.797  1.00 34.84  ? 116 THR A CA    1 
ATOM   959  C  C     . THR A 1 117 ? 3.431   -4.424  38.662  1.00 37.06  ? 116 THR A C     1 
ATOM   960  O  O     . THR A 1 117 ? 3.941   -4.038  37.605  1.00 42.30  ? 116 THR A O     1 
ATOM   961  C  CB    . THR A 1 117 ? 4.285   -3.553  40.861  1.00 37.76  ? 116 THR A CB    1 
ATOM   962  O  OG1   . THR A 1 117 ? 4.101   -2.522  41.831  1.00 39.79  ? 116 THR A OG1   1 
ATOM   963  C  CG2   . THR A 1 117 ? 5.666   -3.401  40.234  1.00 38.93  ? 116 THR A CG2   1 
ATOM   964  N  N     . GLU A 1 118 ? 3.069   -5.692  38.865  1.00 36.19  ? 117 GLU A N     1 
ATOM   965  C  CA    . GLU A 1 118 ? 3.227   -6.712  37.832  1.00 45.05  ? 117 GLU A CA    1 
ATOM   966  C  C     . GLU A 1 118 ? 2.361   -6.398  36.618  1.00 45.77  ? 117 GLU A C     1 
ATOM   967  O  O     . GLU A 1 118 ? 2.834   -6.414  35.477  1.00 41.36  ? 117 GLU A O     1 
ATOM   968  C  CB    . GLU A 1 118 ? 2.854   -8.084  38.404  1.00 48.11  ? 117 GLU A CB    1 
ATOM   969  C  CG    . GLU A 1 118 ? 3.644   -8.482  39.650  1.00 55.02  ? 117 GLU A CG    1 
ATOM   970  C  CD    . GLU A 1 118 ? 3.438   -9.933  40.054  1.00 66.80  ? 117 GLU A CD    1 
ATOM   971  O  OE1   . GLU A 1 118 ? 2.345   -10.484 39.768  1.00 69.76  ? 117 GLU A OE1   1 
ATOM   972  O  OE2   . GLU A 1 118 ? 4.359   -10.511 40.678  1.00 68.88  ? 117 GLU A OE2   1 
ATOM   973  N  N     . SER A 1 119 ? 1.074   -6.135  36.849  1.00 40.81  ? 118 SER A N     1 
ATOM   974  C  CA    . SER A 1 119 ? 0.189   -5.678  35.775  1.00 45.13  ? 118 SER A CA    1 
ATOM   975  C  C     . SER A 1 119 ? 0.815   -4.523  35.017  1.00 45.65  ? 118 SER A C     1 
ATOM   976  O  O     . SER A 1 119 ? 0.834   -4.506  33.777  1.00 46.66  ? 118 SER A O     1 
ATOM   977  C  CB    . SER A 1 119 ? -1.163  -5.255  36.362  1.00 43.31  ? 118 SER A CB    1 
ATOM   978  O  OG    . SER A 1 119 ? -1.991  -4.684  35.362  1.00 53.32  ? 118 SER A OG    1 
ATOM   979  N  N     . HIS A 1 120 ? 1.371   -3.565  35.761  1.00 42.62  ? 119 HIS A N     1 
ATOM   980  C  CA    . HIS A 1 120 ? 1.950   -2.377  35.160  1.00 42.60  ? 119 HIS A CA    1 
ATOM   981  C  C     . HIS A 1 120 ? 3.141   -2.733  34.284  1.00 47.02  ? 119 HIS A C     1 
ATOM   982  O  O     . HIS A 1 120 ? 3.347   -2.128  33.227  1.00 46.66  ? 119 HIS A O     1 
ATOM   983  C  CB    . HIS A 1 120 ? 2.347   -1.410  36.269  1.00 41.08  ? 119 HIS A CB    1 
ATOM   984  C  CG    . HIS A 1 120 ? 2.553   -0.011  35.804  1.00 42.77  ? 119 HIS A CG    1 
ATOM   985  N  ND1   . HIS A 1 120 ? 3.651   0.373   35.068  1.00 42.24  ? 119 HIS A ND1   1 
ATOM   986  C  CD2   . HIS A 1 120 ? 1.795   1.099   35.959  1.00 41.23  ? 119 HIS A CD2   1 
ATOM   987  C  CE1   . HIS A 1 120 ? 3.568   1.665   34.802  1.00 41.77  ? 119 HIS A CE1   1 
ATOM   988  N  NE2   . HIS A 1 120 ? 2.446   2.127   35.322  1.00 43.73  ? 119 HIS A NE2   1 
ATOM   989  N  N     . ARG A 1 121 ? 3.935   -3.722  34.708  1.00 52.73  ? 120 ARG A N     1 
ATOM   990  C  CA    . ARG A 1 121 ? 5.047   -4.191  33.886  1.00 47.37  ? 120 ARG A CA    1 
ATOM   991  C  C     . ARG A 1 121 ? 4.551   -4.791  32.568  1.00 48.24  ? 120 ARG A C     1 
ATOM   992  O  O     . ARG A 1 121 ? 5.157   -4.574  31.512  1.00 45.10  ? 120 ARG A O     1 
ATOM   993  C  CB    . ARG A 1 121 ? 5.889   -5.211  34.664  1.00 45.07  ? 120 ARG A CB    1 
ATOM   994  C  CG    . ARG A 1 121 ? 7.320   -4.698  35.047  1.00 64.62  ? 120 ARG A CG    1 
ATOM   995  C  CD    . ARG A 1 121 ? 7.335   -3.221  35.530  1.00 58.36  ? 120 ARG A CD    1 
ATOM   996  N  NE    . ARG A 1 121 ? 8.639   -2.553  35.456  1.00 65.12  ? 120 ARG A NE    1 
ATOM   997  C  CZ    . ARG A 1 121 ? 9.487   -2.367  36.462  1.00 67.59  ? 120 ARG A CZ    1 
ATOM   998  N  NH1   . ARG A 1 121 ? 9.265   -2.880  37.665  1.00 70.12  ? 120 ARG A NH1   1 
ATOM   999  N  NH2   . ARG A 1 121 ? 10.587  -1.638  36.255  1.00 58.16  ? 120 ARG A NH2   1 
ATOM   1000 N  N     . ILE A 1 122 ? 3.477   -5.579  32.610  1.00 42.77  ? 121 ILE A N     1 
ATOM   1001 C  CA    . ILE A 1 122 ? 2.929   -6.136  31.374  1.00 52.23  ? 121 ILE A CA    1 
ATOM   1002 C  C     . ILE A 1 122 ? 2.549   -5.023  30.413  1.00 50.72  ? 121 ILE A C     1 
ATOM   1003 O  O     . ILE A 1 122 ? 2.877   -5.070  29.223  1.00 46.75  ? 121 ILE A O     1 
ATOM   1004 C  CB    . ILE A 1 122 ? 1.723   -7.047  31.665  1.00 51.56  ? 121 ILE A CB    1 
ATOM   1005 C  CG1   . ILE A 1 122 ? 2.111   -8.157  32.629  1.00 55.15  ? 121 ILE A CG1   1 
ATOM   1006 C  CG2   . ILE A 1 122 ? 1.169   -7.630  30.366  1.00 58.21  ? 121 ILE A CG2   1 
ATOM   1007 C  CD1   . ILE A 1 122 ? 0.949   -9.053  32.977  1.00 49.34  ? 121 ILE A CD1   1 
ATOM   1008 N  N     . LEU A 1 123 ? 1.844   -4.011  30.920  1.00 47.89  ? 122 LEU A N     1 
ATOM   1009 C  CA    . LEU A 1 123 ? 1.396   -2.905  30.083  1.00 43.44  ? 122 LEU A CA    1 
ATOM   1010 C  C     . LEU A 1 123 ? 2.567   -2.128  29.500  1.00 52.13  ? 122 LEU A C     1 
ATOM   1011 O  O     . LEU A 1 123 ? 2.487   -1.648  28.363  1.00 46.63  ? 122 LEU A O     1 
ATOM   1012 C  CB    . LEU A 1 123 ? 0.494   -1.986  30.904  1.00 43.32  ? 122 LEU A CB    1 
ATOM   1013 C  CG    . LEU A 1 123 ? -1.000  -2.197  30.679  1.00 50.83  ? 122 LEU A CG    1 
ATOM   1014 C  CD1   . LEU A 1 123 ? -1.380  -3.620  31.043  1.00 54.91  ? 122 LEU A CD1   1 
ATOM   1015 C  CD2   . LEU A 1 123 ? -1.758  -1.218  31.554  1.00 51.47  ? 122 LEU A CD2   1 
ATOM   1016 N  N     . GLU A 1 124 ? 3.657   -1.982  30.271  1.00 43.56  ? 123 GLU A N     1 
ATOM   1017 C  CA    . GLU A 1 124 ? 4.845   -1.262  29.808  1.00 49.60  ? 123 GLU A CA    1 
ATOM   1018 C  C     . GLU A 1 124 ? 5.337   -1.770  28.456  1.00 52.75  ? 123 GLU A C     1 
ATOM   1019 O  O     . GLU A 1 124 ? 5.726   -0.980  27.585  1.00 56.05  ? 123 GLU A O     1 
ATOM   1020 C  CB    . GLU A 1 124 ? 5.973   -1.402  30.845  1.00 45.90  ? 123 GLU A CB    1 
ATOM   1021 C  CG    . GLU A 1 124 ? 5.987   -0.343  31.928  1.00 50.73  ? 123 GLU A CG    1 
ATOM   1022 C  CD    . GLU A 1 124 ? 6.656   -0.831  33.204  1.00 58.44  ? 123 GLU A CD    1 
ATOM   1023 O  OE1   . GLU A 1 124 ? 6.005   -0.773  34.274  1.00 57.53  ? 123 GLU A OE1   1 
ATOM   1024 O  OE2   . GLU A 1 124 ? 7.829   -1.272  33.139  1.00 64.12  ? 123 GLU A OE2   1 
ATOM   1025 N  N     . LYS A 1 125 ? 5.364   -3.089  28.280  1.00 48.57  ? 124 LYS A N     1 
ATOM   1026 C  CA    . LYS A 1 125 ? 5.907   -3.656  27.056  1.00 52.31  ? 124 LYS A CA    1 
ATOM   1027 C  C     . LYS A 1 125 ? 5.017   -3.432  25.849  1.00 60.07  ? 124 LYS A C     1 
ATOM   1028 O  O     . LYS A 1 125 ? 5.516   -3.461  24.719  1.00 50.51  ? 124 LYS A O     1 
ATOM   1029 C  CB    . LYS A 1 125 ? 6.185   -5.140  27.264  1.00 56.94  ? 124 LYS A CB    1 
ATOM   1030 C  CG    . LYS A 1 125 ? 7.054   -5.387  28.493  1.00 57.84  ? 124 LYS A CG    1 
ATOM   1031 C  CD    . LYS A 1 125 ? 7.558   -6.810  28.543  1.00 62.24  ? 124 LYS A CD    1 
ATOM   1032 C  CE    . LYS A 1 125 ? 8.758   -6.930  29.473  1.00 60.86  ? 124 LYS A CE    1 
ATOM   1033 N  NZ    . LYS A 1 125 ? 9.992   -6.411  28.806  1.00 65.63  ? 124 LYS A NZ    1 
ATOM   1034 N  N     . TYR A 1 126 ? 3.725   -3.173  26.058  1.00 56.66  ? 125 TYR A N     1 
ATOM   1035 C  CA    . TYR A 1 126 ? 2.767   -3.077  24.972  1.00 49.44  ? 125 TYR A CA    1 
ATOM   1036 C  C     . TYR A 1 126 ? 2.452   -1.646  24.572  1.00 55.06  ? 125 TYR A C     1 
ATOM   1037 O  O     . TYR A 1 126 ? 1.545   -1.438  23.765  1.00 54.80  ? 125 TYR A O     1 
ATOM   1038 C  CB    . TYR A 1 126 ? 1.480   -3.791  25.360  1.00 47.93  ? 125 TYR A CB    1 
ATOM   1039 C  CG    . TYR A 1 126 ? 1.582   -5.288  25.368  1.00 46.97  ? 125 TYR A CG    1 
ATOM   1040 C  CD1   . TYR A 1 126 ? 1.565   -6.009  24.184  1.00 51.83  ? 125 TYR A CD1   1 
ATOM   1041 C  CD2   . TYR A 1 126 ? 1.672   -5.990  26.556  1.00 51.65  ? 125 TYR A CD2   1 
ATOM   1042 C  CE1   . TYR A 1 126 ? 1.640   -7.386  24.182  1.00 46.01  ? 125 TYR A CE1   1 
ATOM   1043 C  CE2   . TYR A 1 126 ? 1.756   -7.373  26.566  1.00 54.19  ? 125 TYR A CE2   1 
ATOM   1044 C  CZ    . TYR A 1 126 ? 1.735   -8.066  25.368  1.00 51.64  ? 125 TYR A CZ    1 
ATOM   1045 O  OH    . TYR A 1 126 ? 1.813   -9.442  25.359  1.00 54.81  ? 125 TYR A OH    1 
ATOM   1046 N  N     . THR A 1 127 ? 3.148   -0.652  25.124  1.00 55.45  ? 126 THR A N     1 
ATOM   1047 C  CA    . THR A 1 127 ? 2.885   0.741   24.779  1.00 61.65  ? 126 THR A CA    1 
ATOM   1048 C  C     . THR A 1 127 ? 4.131   1.395   24.210  1.00 65.40  ? 126 THR A C     1 
ATOM   1049 O  O     . THR A 1 127 ? 5.261   1.024   24.557  1.00 68.85  ? 126 THR A O     1 
ATOM   1050 C  CB    . THR A 1 127 ? 2.391   1.582   25.985  1.00 67.70  ? 126 THR A CB    1 
ATOM   1051 O  OG1   . THR A 1 127 ? 3.503   2.128   26.702  1.00 68.91  ? 126 THR A OG1   1 
ATOM   1052 C  CG2   . THR A 1 127 ? 1.557   0.761   26.918  1.00 59.87  ? 126 THR A CG2   1 
ATOM   1053 N  N     . GLN A 1 128 ? 3.904   2.383   23.326  1.00 68.61  ? 127 GLN A N     1 
ATOM   1054 C  CA    . GLN A 1 128 ? 4.974   3.166   22.726  1.00 69.84  ? 127 GLN A CA    1 
ATOM   1055 C  C     . GLN A 1 128 ? 5.965   3.575   23.804  1.00 74.53  ? 127 GLN A C     1 
ATOM   1056 O  O     . GLN A 1 128 ? 5.560   4.102   24.850  1.00 74.12  ? 127 GLN A O     1 
ATOM   1057 C  CB    . GLN A 1 128 ? 4.458   4.426   22.025  1.00 69.16  ? 127 GLN A CB    1 
ATOM   1058 C  CG    . GLN A 1 128 ? 3.375   4.260   20.978  1.00 77.10  ? 127 GLN A CG    1 
ATOM   1059 C  CD    . GLN A 1 128 ? 2.651   5.581   20.685  1.00 78.73  ? 127 GLN A CD    1 
ATOM   1060 O  OE1   . GLN A 1 128 ? 3.251   6.531   20.157  1.00 75.33  ? 127 GLN A OE1   1 
ATOM   1061 N  NE2   . GLN A 1 128 ? 1.359   5.640   21.010  1.00 62.62  ? 127 GLN A NE2   1 
ATOM   1062 N  N     . PRO A 1 129 ? 7.262   3.341   23.598  1.00 80.76  ? 128 PRO A N     1 
ATOM   1063 C  CA    . PRO A 1 129 ? 8.254   3.879   24.541  1.00 74.93  ? 128 PRO A CA    1 
ATOM   1064 C  C     . PRO A 1 129 ? 8.221   5.397   24.639  1.00 66.70  ? 128 PRO A C     1 
ATOM   1065 O  O     . PRO A 1 129 ? 8.714   5.945   25.631  1.00 68.94  ? 128 PRO A O     1 
ATOM   1066 C  CB    . PRO A 1 129 ? 9.590   3.368   23.980  1.00 80.38  ? 128 PRO A CB    1 
ATOM   1067 C  CG    . PRO A 1 129 ? 9.322   3.100   22.524  1.00 76.06  ? 128 PRO A CG    1 
ATOM   1068 C  CD    . PRO A 1 129 ? 7.886   2.659   22.448  1.00 79.95  ? 128 PRO A CD    1 
ATOM   1069 N  N     . SER A 1 130 ? 7.634   6.092   23.655  1.00 67.89  ? 129 SER A N     1 
ATOM   1070 C  CA    . SER A 1 130 ? 7.504   7.545   23.715  1.00 60.91  ? 129 SER A CA    1 
ATOM   1071 C  C     . SER A 1 130 ? 6.519   7.987   24.785  1.00 59.82  ? 129 SER A C     1 
ATOM   1072 O  O     . SER A 1 130 ? 6.585   9.132   25.245  1.00 53.81  ? 129 SER A O     1 
ATOM   1073 C  CB    . SER A 1 130 ? 7.050   8.104   22.363  1.00 62.83  ? 129 SER A CB    1 
ATOM   1074 O  OG    . SER A 1 130 ? 7.590   7.377   21.276  1.00 67.96  ? 129 SER A OG    1 
ATOM   1075 N  N     . ILE A 1 131 ? 5.597   7.116   25.180  1.00 54.19  ? 130 ILE A N     1 
ATOM   1076 C  CA    . ILE A 1 131 ? 4.613   7.515   26.179  1.00 63.21  ? 130 ILE A CA    1 
ATOM   1077 C  C     . ILE A 1 131 ? 5.312   7.788   27.507  1.00 56.69  ? 130 ILE A C     1 
ATOM   1078 O  O     . ILE A 1 131 ? 5.100   8.826   28.148  1.00 51.51  ? 130 ILE A O     1 
ATOM   1079 C  CB    . ILE A 1 131 ? 3.523   6.433   26.290  1.00 62.06  ? 130 ILE A CB    1 
ATOM   1080 C  CG1   . ILE A 1 131 ? 2.705   6.423   24.987  1.00 63.04  ? 130 ILE A CG1   1 
ATOM   1081 C  CG2   . ILE A 1 131 ? 2.649   6.633   27.531  1.00 55.19  ? 130 ILE A CG2   1 
ATOM   1082 C  CD1   . ILE A 1 131 ? 1.719   7.550   24.860  1.00 53.14  ? 130 ILE A CD1   1 
ATOM   1083 N  N     . PHE A 1 132 ? 6.220   6.900   27.897  1.00 50.78  ? 131 PHE A N     1 
ATOM   1084 C  CA    . PHE A 1 132 ? 6.991   7.139   29.110  1.00 58.17  ? 131 PHE A CA    1 
ATOM   1085 C  C     . PHE A 1 132 ? 7.921   8.338   28.955  1.00 54.55  ? 131 PHE A C     1 
ATOM   1086 O  O     . PHE A 1 132 ? 8.190   9.044   29.938  1.00 49.87  ? 131 PHE A O     1 
ATOM   1087 C  CB    . PHE A 1 132 ? 7.736   5.860   29.472  1.00 53.23  ? 131 PHE A CB    1 
ATOM   1088 C  CG    . PHE A 1 132 ? 6.812   4.691   29.697  1.00 55.80  ? 131 PHE A CG    1 
ATOM   1089 C  CD1   . PHE A 1 132 ? 6.007   4.641   30.823  1.00 55.42  ? 131 PHE A CD1   1 
ATOM   1090 C  CD2   . PHE A 1 132 ? 6.724   3.662   28.770  1.00 64.91  ? 131 PHE A CD2   1 
ATOM   1091 C  CE1   . PHE A 1 132 ? 5.144   3.581   31.033  1.00 64.74  ? 131 PHE A CE1   1 
ATOM   1092 C  CE2   . PHE A 1 132 ? 5.863   2.593   28.973  1.00 62.03  ? 131 PHE A CE2   1 
ATOM   1093 C  CZ    . PHE A 1 132 ? 5.072   2.556   30.106  1.00 62.68  ? 131 PHE A CZ    1 
ATOM   1094 N  N     . LYS A 1 133 ? 8.371   8.613   27.726  1.00 55.12  ? 132 LYS A N     1 
ATOM   1095 C  CA    . LYS A 1 133 ? 9.130   9.832   27.459  1.00 58.24  ? 132 LYS A CA    1 
ATOM   1096 C  C     . LYS A 1 133 ? 8.335   11.071  27.853  1.00 54.22  ? 132 LYS A C     1 
ATOM   1097 O  O     . LYS A 1 133 ? 8.853   11.947  28.549  1.00 57.45  ? 132 LYS A O     1 
ATOM   1098 C  CB    . LYS A 1 133 ? 9.517   9.906   25.979  1.00 63.69  ? 132 LYS A CB    1 
ATOM   1099 C  CG    . LYS A 1 133 ? 10.839  10.607  25.681  1.00 71.31  ? 132 LYS A CG    1 
ATOM   1100 C  CD    . LYS A 1 133 ? 11.361  10.181  24.310  1.00 74.19  ? 132 LYS A CD    1 
ATOM   1101 C  CE    . LYS A 1 133 ? 11.637  8.684   24.237  1.00 76.24  ? 132 LYS A CE    1 
ATOM   1102 N  NZ    . LYS A 1 133 ? 11.500  8.179   22.838  1.00 73.49  ? 132 LYS A NZ    1 
ATOM   1103 N  N     . ILE A 1 134 ? 7.070   11.167  27.411  1.00 52.77  ? 133 ILE A N     1 
ATOM   1104 C  CA    . ILE A 1 134 ? 6.256   12.338  27.743  1.00 45.34  ? 133 ILE A CA    1 
ATOM   1105 C  C     . ILE A 1 134 ? 6.071   12.461  29.255  1.00 52.54  ? 133 ILE A C     1 
ATOM   1106 O  O     . ILE A 1 134 ? 6.084   13.568  29.808  1.00 50.28  ? 133 ILE A O     1 
ATOM   1107 C  CB    . ILE A 1 134 ? 4.888   12.300  27.021  1.00 54.10  ? 133 ILE A CB    1 
ATOM   1108 C  CG1   . ILE A 1 134 ? 5.019   12.389  25.495  1.00 57.71  ? 133 ILE A CG1   1 
ATOM   1109 C  CG2   . ILE A 1 134 ? 3.955   13.420  27.519  1.00 49.09  ? 133 ILE A CG2   1 
ATOM   1110 C  CD1   . ILE A 1 134 ? 4.476   11.191  24.756  1.00 58.26  ? 133 ILE A CD1   1 
ATOM   1111 N  N     . ILE A 1 135 ? 5.882   11.335  29.945  1.00 54.33  ? 134 ILE A N     1 
ATOM   1112 C  CA    . ILE A 1 135 ? 5.616   11.385  31.383  1.00 52.30  ? 134 ILE A CA    1 
ATOM   1113 C  C     . ILE A 1 135 ? 6.803   11.943  32.153  1.00 55.92  ? 134 ILE A C     1 
ATOM   1114 O  O     . ILE A 1 135 ? 6.632   12.777  33.052  1.00 58.79  ? 134 ILE A O     1 
ATOM   1115 C  CB    . ILE A 1 135 ? 5.209   9.998   31.898  1.00 50.93  ? 134 ILE A CB    1 
ATOM   1116 C  CG1   . ILE A 1 135 ? 4.082   9.437   31.022  1.00 49.69  ? 134 ILE A CG1   1 
ATOM   1117 C  CG2   . ILE A 1 135 ? 4.902   10.054  33.381  1.00 55.71  ? 134 ILE A CG2   1 
ATOM   1118 C  CD1   . ILE A 1 135 ? 3.465   8.156   31.518  1.00 47.74  ? 134 ILE A CD1   1 
ATOM   1119 N  N     . SER A 1 136 ? 8.021   11.498  31.827  1.00 59.18  ? 135 SER A N     1 
ATOM   1120 C  CA    . SER A 1 136 ? 9.186   11.962  32.573  1.00 57.56  ? 135 SER A CA    1 
ATOM   1121 C  C     . SER A 1 136 ? 9.429   13.453  32.383  1.00 60.28  ? 135 SER A C     1 
ATOM   1122 O  O     . SER A 1 136 ? 10.096  14.075  33.217  1.00 63.14  ? 135 SER A O     1 
ATOM   1123 C  CB    . SER A 1 136 ? 10.432  11.180  32.162  1.00 59.00  ? 135 SER A CB    1 
ATOM   1124 O  OG    . SER A 1 136 ? 10.790  11.478  30.822  1.00 62.85  ? 135 SER A OG    1 
ATOM   1125 N  N     . GLN A 1 137 ? 8.906   14.038  31.308  1.00 55.82  ? 136 GLN A N     1 
ATOM   1126 C  CA    . GLN A 1 137 ? 9.006   15.470  31.083  1.00 64.10  ? 136 GLN A CA    1 
ATOM   1127 C  C     . GLN A 1 137 ? 7.845   16.231  31.693  1.00 62.82  ? 136 GLN A C     1 
ATOM   1128 O  O     . GLN A 1 137 ? 7.628   17.399  31.349  1.00 70.10  ? 136 GLN A O     1 
ATOM   1129 C  CB    . GLN A 1 137 ? 9.138   15.757  29.583  1.00 71.50  ? 136 GLN A CB    1 
ATOM   1130 C  CG    . GLN A 1 137 ? 9.941   14.681  28.860  1.00 68.83  ? 136 GLN A CG    1 
ATOM   1131 C  CD    . GLN A 1 137 ? 10.037  14.890  27.367  1.00 74.80  ? 136 GLN A CD    1 
ATOM   1132 O  OE1   . GLN A 1 137 ? 9.139   15.469  26.752  1.00 74.33  ? 136 GLN A OE1   1 
ATOM   1133 N  NE2   . GLN A 1 137 ? 11.124  14.400  26.768  1.00 74.96  ? 136 GLN A NE2   1 
ATOM   1134 N  N     . GLY A 1 138 ? 7.096   15.595  32.588  1.00 63.33  ? 137 GLY A N     1 
ATOM   1135 C  CA    . GLY A 1 138 ? 6.153   16.293  33.425  1.00 54.39  ? 137 GLY A CA    1 
ATOM   1136 C  C     . GLY A 1 138 ? 4.779   16.473  32.842  1.00 59.76  ? 137 GLY A C     1 
ATOM   1137 O  O     . GLY A 1 138 ? 4.009   17.283  33.367  1.00 59.44  ? 137 GLY A O     1 
ATOM   1138 N  N     . THR A 1 139 ? 4.436   15.738  31.789  1.00 65.00  ? 138 THR A N     1 
ATOM   1139 C  CA    . THR A 1 139 ? 3.176   15.929  31.085  1.00 65.52  ? 138 THR A CA    1 
ATOM   1140 C  C     . THR A 1 139 ? 2.374   14.638  31.047  1.00 54.75  ? 138 THR A C     1 
ATOM   1141 O  O     . THR A 1 139 ? 2.912   13.559  30.767  1.00 54.72  ? 138 THR A O     1 
ATOM   1142 C  CB    . THR A 1 139 ? 3.412   16.430  29.657  1.00 65.11  ? 138 THR A CB    1 
ATOM   1143 O  OG1   . THR A 1 139 ? 4.553   17.295  29.644  1.00 62.20  ? 138 THR A OG1   1 
ATOM   1144 C  CG2   . THR A 1 139 ? 2.186   17.190  29.146  1.00 64.22  ? 138 THR A CG2   1 
ATOM   1145 N  N     . ASN A 1 140 ? 1.093   14.758  31.339  1.00 57.87  ? 139 ASN A N     1 
ATOM   1146 C  CA    . ASN A 1 140 ? 0.181   13.655  31.118  1.00 52.18  ? 139 ASN A CA    1 
ATOM   1147 C  C     . ASN A 1 140 ? -0.068  13.509  29.623  1.00 59.48  ? 139 ASN A C     1 
ATOM   1148 O  O     . ASN A 1 140 ? -0.570  14.453  28.993  1.00 52.92  ? 139 ASN A O     1 
ATOM   1149 C  CB    . ASN A 1 140 ? -1.110  13.894  31.889  1.00 58.96  ? 139 ASN A CB    1 
ATOM   1150 C  CG    . ASN A 1 140 ? -2.188  12.863  31.589  1.00 58.73  ? 139 ASN A CG    1 
ATOM   1151 O  OD1   . ASN A 1 140 ? -1.955  11.849  30.929  1.00 55.75  ? 139 ASN A OD1   1 
ATOM   1152 N  ND2   . ASN A 1 140 ? -3.368  13.100  32.125  1.00 57.09  ? 139 ASN A ND2   1 
ATOM   1153 N  N     . PRO A 1 141 ? 0.273   12.359  29.021  1.00 64.11  ? 140 PRO A N     1 
ATOM   1154 C  CA    . PRO A 1 141 ? 0.059   12.167  27.574  1.00 58.17  ? 140 PRO A CA    1 
ATOM   1155 C  C     . PRO A 1 141 ? -1.346  12.477  27.114  1.00 58.66  ? 140 PRO A C     1 
ATOM   1156 O  O     . PRO A 1 141 ? -1.525  12.990  26.005  1.00 64.10  ? 140 PRO A O     1 
ATOM   1157 C  CB    . PRO A 1 141 ? 0.376   10.679  27.380  1.00 59.43  ? 140 PRO A CB    1 
ATOM   1158 C  CG    . PRO A 1 141 ? 1.383   10.381  28.438  1.00 60.14  ? 140 PRO A CG    1 
ATOM   1159 C  CD    . PRO A 1 141 ? 0.968   11.210  29.632  1.00 59.17  ? 140 PRO A CD    1 
ATOM   1160 N  N     . LEU A 1 142 ? -2.356  12.181  27.931  1.00 58.05  ? 141 LEU A N     1 
ATOM   1161 C  CA    . LEU A 1 142 ? -3.738  12.433  27.553  1.00 54.67  ? 141 LEU A CA    1 
ATOM   1162 C  C     . LEU A 1 142 ? -4.085  13.911  27.554  1.00 60.19  ? 141 LEU A C     1 
ATOM   1163 O  O     . LEU A 1 142 ? -5.247  14.251  27.307  1.00 63.39  ? 141 LEU A O     1 
ATOM   1164 C  CB    . LEU A 1 142 ? -4.683  11.684  28.493  1.00 59.68  ? 141 LEU A CB    1 
ATOM   1165 C  CG    . LEU A 1 142 ? -4.430  10.180  28.614  1.00 60.14  ? 141 LEU A CG    1 
ATOM   1166 C  CD1   . LEU A 1 142 ? -5.373  9.560   29.617  1.00 60.46  ? 141 LEU A CD1   1 
ATOM   1167 C  CD2   . LEU A 1 142 ? -4.553  9.493   27.270  1.00 55.51  ? 141 LEU A CD2   1 
ATOM   1168 N  N     . ASN A 1 143 ? -3.122  14.787  27.837  1.00 61.48  ? 142 ASN A N     1 
ATOM   1169 C  CA    . ASN A 1 143 ? -3.336  16.226  27.843  1.00 59.32  ? 142 ASN A CA    1 
ATOM   1170 C  C     . ASN A 1 143 ? -2.484  16.948  26.809  1.00 61.43  ? 142 ASN A C     1 
ATOM   1171 O  O     . ASN A 1 143 ? -2.520  18.182  26.755  1.00 60.41  ? 142 ASN A O     1 
ATOM   1172 C  CB    . ASN A 1 143 ? -3.044  16.804  29.237  1.00 63.33  ? 142 ASN A CB    1 
ATOM   1173 C  CG    . ASN A 1 143 ? -4.171  16.545  30.235  1.00 69.61  ? 142 ASN A CG    1 
ATOM   1174 O  OD1   . ASN A 1 143 ? -3.975  16.653  31.451  1.00 68.80  ? 142 ASN A OD1   1 
ATOM   1175 N  ND2   . ASN A 1 143 ? -5.360  16.216  29.724  1.00 65.71  ? 142 ASN A ND2   1 
ATOM   1176 N  N     . ILE A 1 144 ? -1.699  16.216  26.011  1.00 63.22  ? 143 ILE A N     1 
ATOM   1177 C  CA    . ILE A 1 144 ? -0.887  16.822  24.961  1.00 61.37  ? 143 ILE A CA    1 
ATOM   1178 C  C     . ILE A 1 144 ? -1.772  17.697  24.085  1.00 68.30  ? 143 ILE A C     1 
ATOM   1179 O  O     . ILE A 1 144 ? -2.840  17.267  23.634  1.00 59.47  ? 143 ILE A O     1 
ATOM   1180 C  CB    . ILE A 1 144 ? -0.188  15.725  24.135  1.00 66.40  ? 143 ILE A CB    1 
ATOM   1181 C  CG1   . ILE A 1 144 ? 0.931   15.083  24.944  1.00 69.67  ? 143 ILE A CG1   1 
ATOM   1182 C  CG2   . ILE A 1 144 ? 0.393   16.297  22.833  1.00 67.45  ? 143 ILE A CG2   1 
ATOM   1183 C  CD1   . ILE A 1 144 ? 2.005   16.062  25.356  1.00 69.09  ? 143 ILE A CD1   1 
ATOM   1184 N  N     . ARG A 1 145 ? -1.352  18.939  23.877  1.00 69.68  ? 144 ARG A N     1 
ATOM   1185 C  CA    . ARG A 1 145 ? -2.008  19.775  22.888  1.00 68.09  ? 144 ARG A CA    1 
ATOM   1186 C  C     . ARG A 1 145 ? -1.594  19.320  21.491  1.00 62.50  ? 144 ARG A C     1 
ATOM   1187 O  O     . ARG A 1 145 ? -0.421  19.009  21.258  1.00 68.93  ? 144 ARG A O     1 
ATOM   1188 C  CB    . ARG A 1 145 ? -1.655  21.249  23.092  1.00 77.22  ? 144 ARG A CB    1 
ATOM   1189 C  CG    . ARG A 1 145 ? -0.173  21.572  22.896  1.00 88.69  ? 144 ARG A CG    1 
ATOM   1190 C  CD    . ARG A 1 145 ? 0.065   23.059  22.646  1.00 101.91 ? 144 ARG A CD    1 
ATOM   1191 N  NE    . ARG A 1 145 ? 1.406   23.483  23.035  1.00 114.70 ? 144 ARG A NE    1 
ATOM   1192 C  CZ    . ARG A 1 145 ? 1.703   24.093  24.176  1.00 116.22 ? 144 ARG A CZ    1 
ATOM   1193 N  NH1   . ARG A 1 145 ? 0.772   24.362  25.078  1.00 117.41 ? 144 ARG A NH1   1 
ATOM   1194 N  NH2   . ARG A 1 145 ? 2.964   24.445  24.417  1.00 106.65 ? 144 ARG A NH2   1 
ATOM   1195 N  N     . PRO A 1 146 ? -2.532  19.238  20.557  1.00 62.47  ? 145 PRO A N     1 
ATOM   1196 C  CA    . PRO A 1 146 ? -2.187  18.767  19.212  1.00 51.23  ? 145 PRO A CA    1 
ATOM   1197 C  C     . PRO A 1 146 ? -1.155  19.678  18.563  1.00 46.50  ? 145 PRO A C     1 
ATOM   1198 O  O     . PRO A 1 146 ? -1.240  20.903  18.659  1.00 52.13  ? 145 PRO A O     1 
ATOM   1199 C  CB    . PRO A 1 146 ? -3.524  18.818  18.461  1.00 56.55  ? 145 PRO A CB    1 
ATOM   1200 C  CG    . PRO A 1 146 ? -4.504  19.482  19.384  1.00 51.68  ? 145 PRO A CG    1 
ATOM   1201 C  CD    . PRO A 1 146 ? -3.984  19.359  20.762  1.00 55.02  ? 145 PRO A CD    1 
ATOM   1202 N  N     . LYS A 1 147 ? -0.176  19.074  17.888  1.00 42.03  ? 146 LYS A N     1 
ATOM   1203 C  CA    . LYS A 1 147 ? 0.781   19.867  17.122  1.00 50.58  ? 146 LYS A CA    1 
ATOM   1204 C  C     . LYS A 1 147 ? 1.245   19.078  15.899  1.00 43.44  ? 146 LYS A C     1 
ATOM   1205 O  O     . LYS A 1 147 ? 1.289   17.846  15.908  1.00 44.25  ? 146 LYS A O     1 
ATOM   1206 C  CB    . LYS A 1 147 ? 1.988   20.307  17.981  1.00 43.94  ? 146 LYS A CB    1 
ATOM   1207 C  CG    . LYS A 1 147 ? 2.966   19.210  18.361  1.00 53.86  ? 146 LYS A CG    1 
ATOM   1208 C  CD    . LYS A 1 147 ? 4.193   19.804  19.096  1.00 63.86  ? 146 LYS A CD    1 
ATOM   1209 C  CE    . LYS A 1 147 ? 5.458   18.966  18.904  1.00 65.02  ? 146 LYS A CE    1 
ATOM   1210 N  NZ    . LYS A 1 147 ? 5.737   18.019  20.026  1.00 67.05  ? 146 LYS A NZ    1 
ATOM   1211 N  N     . ALA A 1 148 ? 1.553   19.804  14.835  1.00 40.41  ? 147 ALA A N     1 
ATOM   1212 C  CA    . ALA A 1 148 ? 2.064   19.219  13.607  1.00 45.96  ? 147 ALA A CA    1 
ATOM   1213 C  C     . ALA A 1 148 ? 3.568   19.402  13.590  1.00 44.18  ? 147 ALA A C     1 
ATOM   1214 O  O     . ALA A 1 148 ? 4.058   20.520  13.790  1.00 40.91  ? 147 ALA A O     1 
ATOM   1215 C  CB    . ALA A 1 148 ? 1.440   19.879  12.376  1.00 36.46  ? 147 ALA A CB    1 
ATOM   1216 N  N     . VAL A 1 149 ? 4.301   18.312  13.374  1.00 42.25  ? 148 VAL A N     1 
ATOM   1217 C  CA    . VAL A 1 149 ? 5.761   18.369  13.374  1.00 42.13  ? 148 VAL A CA    1 
ATOM   1218 C  C     . VAL A 1 149 ? 6.292   17.532  12.221  1.00 42.78  ? 148 VAL A C     1 
ATOM   1219 O  O     . VAL A 1 149 ? 5.786   16.442  11.935  1.00 42.13  ? 148 VAL A O     1 
ATOM   1220 C  CB    . VAL A 1 149 ? 6.367   17.899  14.716  1.00 46.97  ? 148 VAL A CB    1 
ATOM   1221 C  CG1   . VAL A 1 149 ? 5.742   16.612  15.178  1.00 46.11  ? 148 VAL A CG1   1 
ATOM   1222 C  CG2   . VAL A 1 149 ? 7.883   17.762  14.609  1.00 53.91  ? 148 VAL A CG2   1 
ATOM   1223 N  N     . GLU A 1 150 ? 7.312   18.043  11.557  1.00 50.08  ? 149 GLU A N     1 
ATOM   1224 C  CA    . GLU A 1 150 ? 7.904   17.320  10.440  1.00 52.24  ? 149 GLU A CA    1 
ATOM   1225 C  C     . GLU A 1 150 ? 8.845   16.240  10.965  1.00 42.27  ? 149 GLU A C     1 
ATOM   1226 O  O     . GLU A 1 150 ? 9.654   16.495  11.864  1.00 44.20  ? 149 GLU A O     1 
ATOM   1227 C  CB    . GLU A 1 150 ? 8.652   18.278  9.524   1.00 48.79  ? 149 GLU A CB    1 
ATOM   1228 C  CG    . GLU A 1 150 ? 8.946   17.643  8.205   1.00 61.23  ? 149 GLU A CG    1 
ATOM   1229 C  CD    . GLU A 1 150 ? 8.537   18.530  7.069   1.00 66.78  ? 149 GLU A CD    1 
ATOM   1230 O  OE1   . GLU A 1 150 ? 8.992   19.691  7.037   1.00 74.91  ? 149 GLU A OE1   1 
ATOM   1231 O  OE2   . GLU A 1 150 ? 7.697   18.086  6.257   1.00 73.88  ? 149 GLU A OE2   1 
ATOM   1232 N  N     . LYS A 1 151 ? 8.718   15.026  10.434  1.00 33.39  ? 150 LYS A N     1 
ATOM   1233 C  CA    . LYS A 1 151 ? 9.578   13.939  10.851  1.00 36.32  ? 150 LYS A CA    1 
ATOM   1234 C  C     . LYS A 1 151 ? 10.148  13.202  9.643   1.00 37.09  ? 150 LYS A C     1 
ATOM   1235 O  O     . LYS A 1 151 ? 9.623   13.277  8.526   1.00 33.13  ? 150 LYS A O     1 
ATOM   1236 C  CB    . LYS A 1 151 ? 8.829   12.979  11.814  1.00 35.40  ? 150 LYS A CB    1 
ATOM   1237 C  CG    . LYS A 1 151 ? 8.654   13.643  13.212  1.00 39.73  ? 150 LYS A CG    1 
ATOM   1238 C  CD    . LYS A 1 151 ? 8.387   12.678  14.338  1.00 46.46  ? 150 LYS A CD    1 
ATOM   1239 C  CE    . LYS A 1 151 ? 8.153   13.410  15.689  1.00 44.09  ? 150 LYS A CE    1 
ATOM   1240 N  NZ    . LYS A 1 151 ? 9.360   14.107  16.216  1.00 49.17  ? 150 LYS A NZ    1 
ATOM   1241 N  N     . ILE A 1 152 ? 11.282  12.551  9.870   1.00 34.79  ? 151 ILE A N     1 
ATOM   1242 C  CA    . ILE A 1 152 ? 11.741  11.512  8.960   1.00 37.67  ? 151 ILE A CA    1 
ATOM   1243 C  C     . ILE A 1 152 ? 11.019  10.241  9.359   1.00 33.53  ? 151 ILE A C     1 
ATOM   1244 O  O     . ILE A 1 152 ? 11.140  9.784   10.499  1.00 36.37  ? 151 ILE A O     1 
ATOM   1245 C  CB    . ILE A 1 152 ? 13.262  11.321  9.020   1.00 38.22  ? 151 ILE A CB    1 
ATOM   1246 C  CG1   . ILE A 1 152 ? 13.983  12.647  8.767   1.00 42.64  ? 151 ILE A CG1   1 
ATOM   1247 C  CG2   . ILE A 1 152 ? 13.718  10.222  8.028   1.00 29.99  ? 151 ILE A CG2   1 
ATOM   1248 C  CD1   . ILE A 1 152 ? 14.037  13.026  7.332   1.00 42.56  ? 151 ILE A CD1   1 
ATOM   1249 N  N     . VAL A 1 153 ? 10.276  9.662   8.434   1.00 26.89  ? 152 VAL A N     1 
ATOM   1250 C  CA    . VAL A 1 153 ? 9.554   8.438   8.725   1.00 27.83  ? 152 VAL A CA    1 
ATOM   1251 C  C     . VAL A 1 153 ? 10.286  7.259   8.112   1.00 27.23  ? 152 VAL A C     1 
ATOM   1252 O  O     . VAL A 1 153 ? 10.699  7.297   6.948   1.00 32.89  ? 152 VAL A O     1 
ATOM   1253 C  CB    . VAL A 1 153 ? 8.093   8.465   8.250   1.00 33.62  ? 152 VAL A CB    1 
ATOM   1254 C  CG1   . VAL A 1 153 ? 7.375   7.286   8.900   1.00 28.86  ? 152 VAL A CG1   1 
ATOM   1255 C  CG2   . VAL A 1 153 ? 7.428   9.797   8.637   1.00 34.65  ? 152 VAL A CG2   1 
ATOM   1256 N  N     . PHE A 1 154 ? 10.414  6.207   8.908   1.00 31.87  ? 153 PHE A N     1 
ATOM   1257 C  CA    . PHE A 1 154 ? 11.143  4.989   8.591   1.00 32.39  ? 153 PHE A CA    1 
ATOM   1258 C  C     . PHE A 1 154 ? 10.147  3.851   8.466   1.00 32.73  ? 153 PHE A C     1 
ATOM   1259 O  O     . PHE A 1 154 ? 9.296   3.671   9.345   1.00 30.39  ? 153 PHE A O     1 
ATOM   1260 C  CB    . PHE A 1 154 ? 12.179  4.737   9.697   1.00 26.43  ? 153 PHE A CB    1 
ATOM   1261 C  CG    . PHE A 1 154 ? 12.880  3.388   9.653   1.00 31.62  ? 153 PHE A CG    1 
ATOM   1262 C  CD1   . PHE A 1 154 ? 12.212  2.205   9.945   1.00 25.35  ? 153 PHE A CD1   1 
ATOM   1263 C  CD2   . PHE A 1 154 ? 14.255  3.327   9.392   1.00 29.74  ? 153 PHE A CD2   1 
ATOM   1264 C  CE1   . PHE A 1 154 ? 12.885  0.990   9.927   1.00 37.64  ? 153 PHE A CE1   1 
ATOM   1265 C  CE2   . PHE A 1 154 ? 14.931  2.133   9.368   1.00 28.55  ? 153 PHE A CE2   1 
ATOM   1266 C  CZ    . PHE A 1 154 ? 14.281  0.957   9.644   1.00 23.88  ? 153 PHE A CZ    1 
ATOM   1267 N  N     . PHE A 1 155 ? 10.275  3.077   7.386   1.00 26.75  ? 154 PHE A N     1 
ATOM   1268 C  CA    . PHE A 1 155 ? 9.477   1.877   7.149   1.00 26.19  ? 154 PHE A CA    1 
ATOM   1269 C  C     . PHE A 1 155 ? 10.405  0.776   6.676   1.00 34.89  ? 154 PHE A C     1 
ATOM   1270 O  O     . PHE A 1 155 ? 11.030  0.925   5.621   1.00 29.66  ? 154 PHE A O     1 
ATOM   1271 C  CB    . PHE A 1 155 ? 8.412   2.098   6.069   1.00 26.54  ? 154 PHE A CB    1 
ATOM   1272 C  CG    . PHE A 1 155 ? 7.311   3.017   6.458   1.00 34.65  ? 154 PHE A CG    1 
ATOM   1273 C  CD1   . PHE A 1 155 ? 6.318   2.598   7.335   1.00 32.64  ? 154 PHE A CD1   1 
ATOM   1274 C  CD2   . PHE A 1 155 ? 7.268   4.310   5.964   1.00 38.77  ? 154 PHE A CD2   1 
ATOM   1275 C  CE1   . PHE A 1 155 ? 5.273   3.445   7.674   1.00 37.97  ? 154 PHE A CE1   1 
ATOM   1276 C  CE2   . PHE A 1 155 ? 6.213   5.175   6.318   1.00 32.20  ? 154 PHE A CE2   1 
ATOM   1277 C  CZ    . PHE A 1 155 ? 5.231   4.746   7.156   1.00 31.41  ? 154 PHE A CZ    1 
ATOM   1278 N  N     . SER A 1 156 ? 10.486  -0.323  7.431   1.00 26.91  ? 155 SER A N     1 
ATOM   1279 C  CA    . SER A 1 156 ? 11.154  -1.529  6.957   1.00 29.39  ? 155 SER A CA    1 
ATOM   1280 C  C     . SER A 1 156 ? 10.153  -2.684  6.896   1.00 35.95  ? 155 SER A C     1 
ATOM   1281 O  O     . SER A 1 156 ? 9.167   -2.705  7.640   1.00 39.15  ? 155 SER A O     1 
ATOM   1282 C  CB    . SER A 1 156 ? 12.320  -1.908  7.864   1.00 34.46  ? 155 SER A CB    1 
ATOM   1283 O  OG    . SER A 1 156 ? 11.863  -2.140  9.186   1.00 40.44  ? 155 SER A OG    1 
ATOM   1284 N  N     . ASP A 1 157 ? 10.400  -3.666  6.023   1.00 32.99  ? 156 ASP A N     1 
ATOM   1285 C  CA    . ASP A 1 157 ? 9.553   -4.854  6.004   1.00 29.05  ? 156 ASP A CA    1 
ATOM   1286 C  C     . ASP A 1 157 ? 10.402  -6.075  5.685   1.00 39.04  ? 156 ASP A C     1 
ATOM   1287 O  O     . ASP A 1 157 ? 11.556  -5.968  5.251   1.00 36.01  ? 156 ASP A O     1 
ATOM   1288 C  CB    . ASP A 1 157 ? 8.410   -4.724  4.996   1.00 32.31  ? 156 ASP A CB    1 
ATOM   1289 C  CG    . ASP A 1 157 ? 8.866   -4.929  3.553   1.00 46.57  ? 156 ASP A CG    1 
ATOM   1290 O  OD1   . ASP A 1 157 ? 9.985   -4.505  3.185   1.00 50.50  ? 156 ASP A OD1   1 
ATOM   1291 O  OD2   . ASP A 1 157 ? 8.080   -5.503  2.773   1.00 47.83  ? 156 ASP A OD2   1 
ATOM   1292 N  N     . ILE A 1 158 ? 9.817   -7.245  5.893   1.00 31.16  ? 157 ILE A N     1 
ATOM   1293 C  CA    . ILE A 1 158 ? 10.496  -8.506  5.626   1.00 34.86  ? 157 ILE A CA    1 
ATOM   1294 C  C     . ILE A 1 158 ? 10.185  -8.930  4.195   1.00 37.90  ? 157 ILE A C     1 
ATOM   1295 O  O     . ILE A 1 158 ? 9.026   -8.885  3.772   1.00 37.04  ? 157 ILE A O     1 
ATOM   1296 C  CB    . ILE A 1 158 ? 10.065  -9.582  6.638   1.00 33.40  ? 157 ILE A CB    1 
ATOM   1297 C  CG1   . ILE A 1 158 ? 10.505  -9.177  8.044   1.00 31.89  ? 157 ILE A CG1   1 
ATOM   1298 C  CG2   . ILE A 1 158 ? 10.705  -10.940 6.284   1.00 30.99  ? 157 ILE A CG2   1 
ATOM   1299 C  CD1   . ILE A 1 158 ? 10.073  -10.148 9.119   1.00 30.59  ? 157 ILE A CD1   1 
ATOM   1300 N  N     . VAL A 1 159 ? 11.222  -9.307  3.437   1.00 31.41  ? 158 VAL A N     1 
ATOM   1301 C  CA    . VAL A 1 159 ? 11.036  -9.749  2.061   1.00 29.48  ? 158 VAL A CA    1 
ATOM   1302 C  C     . VAL A 1 159 ? 10.362  -11.110 2.056   1.00 35.62  ? 158 VAL A C     1 
ATOM   1303 O  O     . VAL A 1 159 ? 10.777  -12.015 2.786   1.00 30.21  ? 158 VAL A O     1 
ATOM   1304 C  CB    . VAL A 1 159 ? 12.372  -9.818  1.306   1.00 37.99  ? 158 VAL A CB    1 
ATOM   1305 C  CG1   . VAL A 1 159 ? 12.110  -10.322 -0.091  1.00 37.82  ? 158 VAL A CG1   1 
ATOM   1306 C  CG2   . VAL A 1 159 ? 13.079  -8.440  1.295   1.00 32.92  ? 158 VAL A CG2   1 
ATOM   1307 N  N     . SER A 1 160 ? 9.326   -11.253 1.210   1.00 35.56  ? 159 SER A N     1 
ATOM   1308 C  CA    . SER A 1 160 ? 8.410   -12.389 1.117   1.00 39.60  ? 159 SER A CA    1 
ATOM   1309 C  C     . SER A 1 160 ? 8.169   -13.037 2.470   1.00 39.59  ? 159 SER A C     1 
ATOM   1310 O  O     . SER A 1 160 ? 8.403   -14.230 2.673   1.00 38.02  ? 159 SER A O     1 
ATOM   1311 C  CB    . SER A 1 160 ? 8.892   -13.422 0.089   1.00 40.75  ? 159 SER A CB    1 
ATOM   1312 O  OG    . SER A 1 160 ? 10.216  -13.826 0.333   1.00 55.75  ? 159 SER A OG    1 
ATOM   1313 N  N     . PHE A 1 161 ? 7.650   -12.242 3.393   1.00 34.93  ? 160 PHE A N     1 
ATOM   1314 C  CA    . PHE A 1 161 ? 7.278   -12.781 4.680   1.00 33.32  ? 160 PHE A CA    1 
ATOM   1315 C  C     . PHE A 1 161 ? 6.281   -13.930 4.536   1.00 35.33  ? 160 PHE A C     1 
ATOM   1316 O  O     . PHE A 1 161 ? 6.258   -14.837 5.369   1.00 35.52  ? 160 PHE A O     1 
ATOM   1317 C  CB    . PHE A 1 161 ? 6.694   -11.661 5.536   1.00 36.79  ? 160 PHE A CB    1 
ATOM   1318 C  CG    . PHE A 1 161 ? 6.056   -12.146 6.765   1.00 37.34  ? 160 PHE A CG    1 
ATOM   1319 C  CD1   . PHE A 1 161 ? 6.830   -12.434 7.869   1.00 44.17  ? 160 PHE A CD1   1 
ATOM   1320 C  CD2   . PHE A 1 161 ? 4.700   -12.390 6.813   1.00 43.87  ? 160 PHE A CD2   1 
ATOM   1321 C  CE1   . PHE A 1 161 ? 6.244   -12.912 9.020   1.00 51.66  ? 160 PHE A CE1   1 
ATOM   1322 C  CE2   . PHE A 1 161 ? 4.117   -12.879 7.957   1.00 45.94  ? 160 PHE A CE2   1 
ATOM   1323 C  CZ    . PHE A 1 161 ? 4.883   -13.133 9.059   1.00 46.14  ? 160 PHE A CZ    1 
ATOM   1324 N  N     . SER A 1 162 ? 5.441   -13.914 3.495   1.00 34.14  ? 161 SER A N     1 
ATOM   1325 C  CA    . SER A 1 162 ? 4.414   -14.950 3.404   1.00 41.11  ? 161 SER A CA    1 
ATOM   1326 C  C     . SER A 1 162 ? 5.021   -16.332 3.190   1.00 40.64  ? 161 SER A C     1 
ATOM   1327 O  O     . SER A 1 162 ? 4.425   -17.337 3.587   1.00 44.44  ? 161 SER A O     1 
ATOM   1328 C  CB    . SER A 1 162 ? 3.420   -14.613 2.296   1.00 48.05  ? 161 SER A CB    1 
ATOM   1329 O  OG    . SER A 1 162 ? 4.098   -14.475 1.060   1.00 53.33  ? 161 SER A OG    1 
ATOM   1330 N  N     . THR A 1 163 ? 6.214   -16.408 2.608   1.00 42.42  ? 162 THR A N     1 
ATOM   1331 C  CA    . THR A 1 163 ? 6.846   -17.712 2.452   1.00 39.70  ? 162 THR A CA    1 
ATOM   1332 C  C     . THR A 1 163 ? 7.192   -18.328 3.802   1.00 38.90  ? 162 THR A C     1 
ATOM   1333 O  O     . THR A 1 163 ? 7.077   -19.544 3.981   1.00 44.43  ? 162 THR A O     1 
ATOM   1334 C  CB    . THR A 1 163 ? 8.089   -17.592 1.577   1.00 44.12  ? 162 THR A CB    1 
ATOM   1335 O  OG1   . THR A 1 163 ? 7.724   -16.980 0.341   1.00 44.86  ? 162 THR A OG1   1 
ATOM   1336 C  CG2   . THR A 1 163 ? 8.678   -18.961 1.300   1.00 43.89  ? 162 THR A CG2   1 
ATOM   1337 N  N     . PHE A 1 164 ? 7.635   -17.516 4.766   1.00 40.08  ? 163 PHE A N     1 
ATOM   1338 C  CA    . PHE A 1 164 ? 7.925   -18.067 6.085   1.00 39.49  ? 163 PHE A CA    1 
ATOM   1339 C  C     . PHE A 1 164 ? 6.672   -18.701 6.680   1.00 45.25  ? 163 PHE A C     1 
ATOM   1340 O  O     . PHE A 1 164 ? 6.702   -19.834 7.174   1.00 42.87  ? 163 PHE A O     1 
ATOM   1341 C  CB    . PHE A 1 164 ? 8.450   -16.983 7.029   1.00 37.64  ? 163 PHE A CB    1 
ATOM   1342 C  CG    . PHE A 1 164 ? 9.846   -16.477 6.708   1.00 40.68  ? 163 PHE A CG    1 
ATOM   1343 C  CD1   . PHE A 1 164 ? 10.050  -15.525 5.724   1.00 33.68  ? 163 PHE A CD1   1 
ATOM   1344 C  CD2   . PHE A 1 164 ? 10.951  -16.956 7.407   1.00 34.09  ? 163 PHE A CD2   1 
ATOM   1345 C  CE1   . PHE A 1 164 ? 11.315  -15.045 5.457   1.00 37.62  ? 163 PHE A CE1   1 
ATOM   1346 C  CE2   . PHE A 1 164 ? 12.236  -16.480 7.129   1.00 29.71  ? 163 PHE A CE2   1 
ATOM   1347 C  CZ    . PHE A 1 164 ? 12.411  -15.525 6.155   1.00 32.87  ? 163 PHE A CZ    1 
ATOM   1348 N  N     . ALA A 1 165 ? 5.554   -17.973 6.637   1.00 45.67  ? 164 ALA A N     1 
ATOM   1349 C  CA    . ALA A 1 165 ? 4.302   -18.492 7.192   1.00 47.09  ? 164 ALA A CA    1 
ATOM   1350 C  C     . ALA A 1 165 ? 3.845   -19.753 6.472   1.00 36.42  ? 164 ALA A C     1 
ATOM   1351 O  O     . ALA A 1 165 ? 3.237   -20.630 7.092   1.00 48.52  ? 164 ALA A O     1 
ATOM   1352 C  CB    . ALA A 1 165 ? 3.207   -17.419 7.134   1.00 42.41  ? 164 ALA A CB    1 
ATOM   1353 N  N     . GLU A 1 166 ? 4.159   -19.885 5.184   1.00 42.12  ? 165 GLU A N     1 
ATOM   1354 C  CA    . GLU A 1 166 ? 3.751   -21.078 4.451   1.00 48.04  ? 165 GLU A CA    1 
ATOM   1355 C  C     . GLU A 1 166 ? 4.690   -22.254 4.670   1.00 51.04  ? 165 GLU A C     1 
ATOM   1356 O  O     . GLU A 1 166 ? 4.251   -23.405 4.584   1.00 52.93  ? 165 GLU A O     1 
ATOM   1357 C  CB    . GLU A 1 166 ? 3.650   -20.778 2.954   1.00 51.76  ? 165 GLU A CB    1 
ATOM   1358 C  CG    . GLU A 1 166 ? 2.440   -19.939 2.585   1.00 51.41  ? 165 GLU A CG    1 
ATOM   1359 C  CD    . GLU A 1 166 ? 2.576   -19.262 1.232   1.00 66.49  ? 165 GLU A CD    1 
ATOM   1360 O  OE1   . GLU A 1 166 ? 3.643   -19.411 0.597   1.00 62.00  ? 165 GLU A OE1   1 
ATOM   1361 O  OE2   . GLU A 1 166 ? 1.608   -18.593 0.799   1.00 75.02  ? 165 GLU A OE2   1 
ATOM   1362 N  N     . LYS A 1 167 ? 5.970   -22.002 4.951   1.00 46.35  ? 166 LYS A N     1 
ATOM   1363 C  CA    . LYS A 1 167 ? 6.938   -23.087 5.019   1.00 43.13  ? 166 LYS A CA    1 
ATOM   1364 C  C     . LYS A 1 167 ? 7.282   -23.519 6.437   1.00 46.47  ? 166 LYS A C     1 
ATOM   1365 O  O     . LYS A 1 167 ? 7.773   -24.635 6.623   1.00 51.52  ? 166 LYS A O     1 
ATOM   1366 C  CB    . LYS A 1 167 ? 8.230   -22.676 4.308   1.00 50.14  ? 166 LYS A CB    1 
ATOM   1367 C  CG    . LYS A 1 167 ? 8.054   -22.402 2.833   1.00 56.44  ? 166 LYS A CG    1 
ATOM   1368 C  CD    . LYS A 1 167 ? 8.053   -23.669 2.010   1.00 61.48  ? 166 LYS A CD    1 
ATOM   1369 C  CE    . LYS A 1 167 ? 7.124   -23.531 0.825   1.00 55.61  ? 166 LYS A CE    1 
ATOM   1370 N  NZ    . LYS A 1 167 ? 7.872   -23.051 -0.368  1.00 64.07  ? 166 LYS A NZ    1 
ATOM   1371 N  N     . LEU A 1 168 ? 7.057   -22.677 7.437   1.00 43.46  ? 167 LEU A N     1 
ATOM   1372 C  CA    . LEU A 1 168 ? 7.587   -22.989 8.754   1.00 40.70  ? 167 LEU A CA    1 
ATOM   1373 C  C     . LEU A 1 168 ? 6.489   -23.138 9.792   1.00 46.51  ? 167 LEU A C     1 
ATOM   1374 O  O     . LEU A 1 168 ? 5.422   -22.542 9.662   1.00 41.89  ? 167 LEU A O     1 
ATOM   1375 C  CB    . LEU A 1 168 ? 8.543   -21.897 9.237   1.00 46.58  ? 167 LEU A CB    1 
ATOM   1376 C  CG    . LEU A 1 168 ? 9.693   -21.503 8.337   1.00 49.10  ? 167 LEU A CG    1 
ATOM   1377 C  CD1   . LEU A 1 168 ? 10.497  -20.441 9.039   1.00 44.68  ? 167 LEU A CD1   1 
ATOM   1378 C  CD2   . LEU A 1 168 ? 10.551  -22.748 8.109   1.00 50.07  ? 167 LEU A CD2   1 
ATOM   1379 N  N     . PRO A 1 169 ? 6.741   -23.921 10.839  1.00 41.95  ? 168 PRO A N     1 
ATOM   1380 C  CA    . PRO A 1 169 ? 5.870   -23.904 12.015  1.00 47.58  ? 168 PRO A CA    1 
ATOM   1381 C  C     . PRO A 1 169 ? 5.702   -22.492 12.557  1.00 52.41  ? 168 PRO A C     1 
ATOM   1382 O  O     . PRO A 1 169 ? 6.611   -21.661 12.493  1.00 45.78  ? 168 PRO A O     1 
ATOM   1383 C  CB    . PRO A 1 169 ? 6.607   -24.791 13.023  1.00 47.35  ? 168 PRO A CB    1 
ATOM   1384 C  CG    . PRO A 1 169 ? 7.571   -25.583 12.238  1.00 47.90  ? 168 PRO A CG    1 
ATOM   1385 C  CD    . PRO A 1 169 ? 7.828   -24.907 10.938  1.00 43.42  ? 168 PRO A CD    1 
ATOM   1386 N  N     . VAL A 1 170 ? 4.531   -22.246 13.140  1.00 44.87  ? 169 VAL A N     1 
ATOM   1387 C  CA    . VAL A 1 170 ? 4.201   -20.909 13.625  1.00 44.68  ? 169 VAL A CA    1 
ATOM   1388 C  C     . VAL A 1 170 ? 5.216   -20.410 14.663  1.00 45.63  ? 169 VAL A C     1 
ATOM   1389 O  O     . VAL A 1 170 ? 5.574   -19.223 14.672  1.00 39.79  ? 169 VAL A O     1 
ATOM   1390 C  CB    . VAL A 1 170 ? 2.758   -20.894 14.160  1.00 45.93  ? 169 VAL A CB    1 
ATOM   1391 C  CG1   . VAL A 1 170 ? 2.647   -21.653 15.465  1.00 55.22  ? 169 VAL A CG1   1 
ATOM   1392 C  CG2   . VAL A 1 170 ? 2.328   -19.484 14.383  1.00 44.10  ? 169 VAL A CG2   1 
ATOM   1393 N  N     . GLU A 1 171 ? 5.708   -21.297 15.541  1.00 38.66  ? 170 GLU A N     1 
ATOM   1394 C  CA    . GLU A 1 171 ? 6.682   -20.885 16.557  1.00 45.10  ? 170 GLU A CA    1 
ATOM   1395 C  C     . GLU A 1 171 ? 7.971   -20.372 15.915  1.00 43.82  ? 170 GLU A C     1 
ATOM   1396 O  O     . GLU A 1 171 ? 8.626   -19.463 16.443  1.00 42.33  ? 170 GLU A O     1 
ATOM   1397 C  CB    . GLU A 1 171 ? 7.030   -22.051 17.492  1.00 48.72  ? 170 GLU A CB    1 
ATOM   1398 C  CG    . GLU A 1 171 ? 5.872   -22.789 18.157  1.00 58.54  ? 170 GLU A CG    1 
ATOM   1399 C  CD    . GLU A 1 171 ? 5.054   -23.645 17.181  1.00 60.23  ? 170 GLU A CD    1 
ATOM   1400 O  OE1   . GLU A 1 171 ? 5.596   -24.074 16.132  1.00 54.94  ? 170 GLU A OE1   1 
ATOM   1401 O  OE2   . GLU A 1 171 ? 3.870   -23.908 17.485  1.00 70.63  ? 170 GLU A OE2   1 
ATOM   1402 N  N     . GLU A 1 172 ? 8.374   -20.974 14.798  1.00 44.15  ? 171 GLU A N     1 
ATOM   1403 C  CA    . GLU A 1 172 ? 9.604   -20.563 14.128  1.00 42.21  ? 171 GLU A CA    1 
ATOM   1404 C  C     . GLU A 1 172 ? 9.411   -19.248 13.380  1.00 43.61  ? 171 GLU A C     1 
ATOM   1405 O  O     . GLU A 1 172 ? 10.334  -18.421 13.332  1.00 42.34  ? 171 GLU A O     1 
ATOM   1406 C  CB    . GLU A 1 172 ? 10.073  -21.662 13.167  1.00 43.71  ? 171 GLU A CB    1 
ATOM   1407 C  CG    . GLU A 1 172 ? 11.202  -22.510 13.730  1.00 58.19  ? 171 GLU A CG    1 
ATOM   1408 C  CD    . GLU A 1 172 ? 11.364  -23.857 13.027  1.00 65.01  ? 171 GLU A CD    1 
ATOM   1409 O  OE1   . GLU A 1 172 ? 11.677  -23.885 11.814  1.00 65.31  ? 171 GLU A OE1   1 
ATOM   1410 O  OE2   . GLU A 1 172 ? 11.176  -24.896 13.697  1.00 68.85  ? 171 GLU A OE2   1 
ATOM   1411 N  N     . VAL A 1 173 ? 8.231   -19.061 12.769  1.00 41.03  ? 172 VAL A N     1 
ATOM   1412 C  CA    . VAL A 1 173 ? 7.870   -17.772 12.175  1.00 37.45  ? 172 VAL A CA    1 
ATOM   1413 C  C     . VAL A 1 173 ? 7.995   -16.660 13.207  1.00 38.81  ? 172 VAL A C     1 
ATOM   1414 O  O     . VAL A 1 173 ? 8.602   -15.616 12.951  1.00 39.97  ? 172 VAL A O     1 
ATOM   1415 C  CB    . VAL A 1 173 ? 6.441   -17.818 11.602  1.00 45.74  ? 172 VAL A CB    1 
ATOM   1416 C  CG1   . VAL A 1 173 ? 6.072   -16.459 11.004  1.00 36.82  ? 172 VAL A CG1   1 
ATOM   1417 C  CG2   . VAL A 1 173 ? 6.279   -18.948 10.568  1.00 42.52  ? 172 VAL A CG2   1 
ATOM   1418 N  N     . VAL A 1 174 ? 7.393   -16.861 14.384  1.00 39.86  ? 173 VAL A N     1 
ATOM   1419 C  CA    . VAL A 1 174 ? 7.495   -15.878 15.459  1.00 37.08  ? 173 VAL A CA    1 
ATOM   1420 C  C     . VAL A 1 174 ? 8.948   -15.654 15.875  1.00 34.26  ? 173 VAL A C     1 
ATOM   1421 O  O     . VAL A 1 174 ? 9.360   -14.518 16.151  1.00 34.43  ? 173 VAL A O     1 
ATOM   1422 C  CB    . VAL A 1 174 ? 6.617   -16.308 16.649  1.00 32.66  ? 173 VAL A CB    1 
ATOM   1423 C  CG1   . VAL A 1 174 ? 6.873   -15.393 17.856  1.00 35.72  ? 173 VAL A CG1   1 
ATOM   1424 C  CG2   . VAL A 1 174 ? 5.167   -16.231 16.262  1.00 35.18  ? 173 VAL A CG2   1 
ATOM   1425 N  N     . SER A 1 175 ? 9.739   -16.726 15.972  1.00 36.40  ? 174 SER A N     1 
ATOM   1426 C  CA    . SER A 1 175 ? 11.163  -16.554 16.267  1.00 41.38  ? 174 SER A CA    1 
ATOM   1427 C  C     . SER A 1 175 ? 11.830  -15.607 15.279  1.00 37.12  ? 174 SER A C     1 
ATOM   1428 O  O     . SER A 1 175 ? 12.545  -14.676 15.674  1.00 37.77  ? 174 SER A O     1 
ATOM   1429 C  CB    . SER A 1 175 ? 11.886  -17.895 16.237  1.00 41.61  ? 174 SER A CB    1 
ATOM   1430 O  OG    . SER A 1 175 ? 13.015  -17.821 17.078  1.00 46.57  ? 174 SER A OG    1 
ATOM   1431 N  N     . VAL A 1 176 ? 11.609  -15.844 13.981  1.00 37.74  ? 175 VAL A N     1 
ATOM   1432 C  CA    . VAL A 1 176 ? 12.205  -15.010 12.946  1.00 35.24  ? 175 VAL A CA    1 
ATOM   1433 C  C     . VAL A 1 176 ? 11.743  -13.570 13.079  1.00 35.08  ? 175 VAL A C     1 
ATOM   1434 O  O     . VAL A 1 176 ? 12.555  -12.645 13.050  1.00 31.44  ? 175 VAL A O     1 
ATOM   1435 C  CB    . VAL A 1 176 ? 11.883  -15.576 11.552  1.00 39.48  ? 175 VAL A CB    1 
ATOM   1436 C  CG1   . VAL A 1 176 ? 12.357  -14.614 10.470  1.00 31.95  ? 175 VAL A CG1   1 
ATOM   1437 C  CG2   . VAL A 1 176 ? 12.548  -16.929 11.389  1.00 37.29  ? 175 VAL A CG2   1 
ATOM   1438 N  N     . VAL A 1 177 ? 10.426  -13.347 13.186  1.00 35.20  ? 176 VAL A N     1 
ATOM   1439 C  CA    . VAL A 1 177 ? 9.978   -11.956 13.225  1.00 31.67  ? 176 VAL A CA    1 
ATOM   1440 C  C     . VAL A 1 177 ? 10.440  -11.265 14.507  1.00 31.49  ? 176 VAL A C     1 
ATOM   1441 O  O     . VAL A 1 177 ? 10.731  -10.064 14.503  1.00 36.11  ? 176 VAL A O     1 
ATOM   1442 C  CB    . VAL A 1 177 ? 8.448   -11.846 13.034  1.00 32.46  ? 176 VAL A CB    1 
ATOM   1443 C  CG1   . VAL A 1 177 ? 7.996   -12.762 11.952  1.00 38.11  ? 176 VAL A CG1   1 
ATOM   1444 C  CG2   . VAL A 1 177 ? 7.689   -12.150 14.313  1.00 36.20  ? 176 VAL A CG2   1 
ATOM   1445 N  N     . ASN A 1 178 ? 10.536  -11.995 15.616  1.00 35.06  ? 177 ASN A N     1 
ATOM   1446 C  CA    . ASN A 1 178 ? 11.086  -11.394 16.832  1.00 38.48  ? 177 ASN A CA    1 
ATOM   1447 C  C     . ASN A 1 178 ? 12.554  -11.001 16.660  1.00 34.23  ? 177 ASN A C     1 
ATOM   1448 O  O     . ASN A 1 178 ? 12.975  -9.927  17.108  1.00 34.31  ? 177 ASN A O     1 
ATOM   1449 C  CB    . ASN A 1 178 ? 10.912  -12.362 17.992  1.00 39.76  ? 177 ASN A CB    1 
ATOM   1450 C  CG    . ASN A 1 178 ? 9.508   -12.333 18.539  1.00 39.58  ? 177 ASN A CG    1 
ATOM   1451 O  OD1   . ASN A 1 178 ? 8.635   -11.638 17.996  1.00 39.30  ? 177 ASN A OD1   1 
ATOM   1452 N  ND2   . ASN A 1 178 ? 9.263   -13.108 19.590  1.00 40.13  ? 177 ASN A ND2   1 
ATOM   1453 N  N     . SER A 1 179 ? 13.351  -11.846 16.005  1.00 31.44  ? 178 SER A N     1 
ATOM   1454 C  CA    . SER A 1 179 ? 14.741  -11.464 15.744  1.00 34.70  ? 178 SER A CA    1 
ATOM   1455 C  C     . SER A 1 179 ? 14.804  -10.203 14.897  1.00 31.41  ? 178 SER A C     1 
ATOM   1456 O  O     . SER A 1 179 ? 15.617  -9.310  15.160  1.00 32.25  ? 178 SER A O     1 
ATOM   1457 C  CB    . SER A 1 179 ? 15.499  -12.604 15.059  1.00 32.11  ? 178 SER A CB    1 
ATOM   1458 O  OG    . SER A 1 179 ? 15.496  -13.786 15.849  1.00 36.49  ? 178 SER A OG    1 
ATOM   1459 N  N     . TYR A 1 180 ? 13.911  -10.099 13.910  1.00 28.61  ? 179 TYR A N     1 
ATOM   1460 C  CA    . TYR A 1 180 ? 13.879  -8.942  13.021  1.00 28.09  ? 179 TYR A CA    1 
ATOM   1461 C  C     . TYR A 1 180 ? 13.467  -7.691  13.776  1.00 34.00  ? 179 TYR A C     1 
ATOM   1462 O  O     . TYR A 1 180 ? 14.130  -6.653  13.689  1.00 30.91  ? 179 TYR A O     1 
ATOM   1463 C  CB    . TYR A 1 180 ? 12.907  -9.213  11.878  1.00 29.97  ? 179 TYR A CB    1 
ATOM   1464 C  CG    . TYR A 1 180 ? 12.643  -8.028  10.991  1.00 33.80  ? 179 TYR A CG    1 
ATOM   1465 C  CD1   . TYR A 1 180 ? 13.631  -7.612  10.119  1.00 37.20  ? 179 TYR A CD1   1 
ATOM   1466 C  CD2   . TYR A 1 180 ? 11.412  -7.361  10.969  1.00 41.32  ? 179 TYR A CD2   1 
ATOM   1467 C  CE1   . TYR A 1 180 ? 13.450  -6.570  9.281   1.00 43.86  ? 179 TYR A CE1   1 
ATOM   1468 C  CE2   . TYR A 1 180 ? 11.216  -6.274  10.093  1.00 39.18  ? 179 TYR A CE2   1 
ATOM   1469 C  CZ    . TYR A 1 180 ? 12.265  -5.900  9.263   1.00 39.99  ? 179 TYR A CZ    1 
ATOM   1470 O  OH    . TYR A 1 180 ? 12.196  -4.852  8.376   1.00 46.10  ? 179 TYR A OH    1 
ATOM   1471 N  N     . PHE A 1 181 ? 12.359  -7.773  14.526  1.00 27.54  ? 180 PHE A N     1 
ATOM   1472 C  CA    . PHE A 1 181 ? 11.894  -6.616  15.277  1.00 32.18  ? 180 PHE A CA    1 
ATOM   1473 C  C     . PHE A 1 181 ? 12.920  -6.170  16.303  1.00 31.72  ? 180 PHE A C     1 
ATOM   1474 O  O     . PHE A 1 181 ? 13.057  -4.969  16.570  1.00 34.75  ? 180 PHE A O     1 
ATOM   1475 C  CB    . PHE A 1 181 ? 10.560  -6.919  15.981  1.00 34.90  ? 180 PHE A CB    1 
ATOM   1476 C  CG    . PHE A 1 181 ? 9.375   -6.934  15.065  1.00 34.41  ? 180 PHE A CG    1 
ATOM   1477 C  CD1   . PHE A 1 181 ? 9.309   -6.081  13.992  1.00 35.82  ? 180 PHE A CD1   1 
ATOM   1478 C  CD2   . PHE A 1 181 ? 8.274   -7.736  15.344  1.00 36.86  ? 180 PHE A CD2   1 
ATOM   1479 C  CE1   . PHE A 1 181 ? 8.207   -6.080  13.151  1.00 41.99  ? 180 PHE A CE1   1 
ATOM   1480 C  CE2   . PHE A 1 181 ? 7.157   -7.731  14.520  1.00 33.90  ? 180 PHE A CE2   1 
ATOM   1481 C  CZ    . PHE A 1 181 ? 7.122   -6.897  13.420  1.00 35.02  ? 180 PHE A CZ    1 
ATOM   1482 N  N     . SER A 1 182 ? 13.640  -7.122  16.908  1.00 29.48  ? 181 SER A N     1 
ATOM   1483 C  CA    . SER A 1 182 ? 14.593  -6.754  17.946  1.00 35.58  ? 181 SER A CA    1 
ATOM   1484 C  C     . SER A 1 182 ? 15.773  -5.996  17.355  1.00 36.77  ? 181 SER A C     1 
ATOM   1485 O  O     . SER A 1 182 ? 16.227  -4.997  17.928  1.00 33.58  ? 181 SER A O     1 
ATOM   1486 C  CB    . SER A 1 182 ? 15.064  -8.008  18.679  1.00 40.22  ? 181 SER A CB    1 
ATOM   1487 O  OG    . SER A 1 182 ? 13.953  -8.607  19.346  1.00 49.43  ? 181 SER A OG    1 
ATOM   1488 N  N     . VAL A 1 183 ? 16.269  -6.453  16.199  1.00 29.28  ? 182 VAL A N     1 
ATOM   1489 C  CA    . VAL A 1 183 ? 17.377  -5.774  15.528  1.00 29.45  ? 182 VAL A CA    1 
ATOM   1490 C  C     . VAL A 1 183 ? 16.962  -4.359  15.136  1.00 32.78  ? 182 VAL A C     1 
ATOM   1491 O  O     . VAL A 1 183 ? 17.639  -3.378  15.459  1.00 34.30  ? 182 VAL A O     1 
ATOM   1492 C  CB    . VAL A 1 183 ? 17.823  -6.580  14.291  1.00 27.91  ? 182 VAL A CB    1 
ATOM   1493 C  CG1   . VAL A 1 183 ? 18.750  -5.735  13.397  1.00 36.21  ? 182 VAL A CG1   1 
ATOM   1494 C  CG2   . VAL A 1 183 ? 18.491  -7.880  14.695  1.00 31.16  ? 182 VAL A CG2   1 
ATOM   1495 N  N     . CYS A 1 184 ? 15.829  -4.234  14.442  1.00 32.20  ? 183 CYS A N     1 
ATOM   1496 C  CA    . CYS A 1 184 ? 15.385  -2.914  14.011  1.00 31.23  ? 183 CYS A CA    1 
ATOM   1497 C  C     . CYS A 1 184 ? 15.208  -1.974  15.194  1.00 29.41  ? 183 CYS A C     1 
ATOM   1498 O  O     . CYS A 1 184 ? 15.694  -0.838  15.173  1.00 30.95  ? 183 CYS A O     1 
ATOM   1499 C  CB    . CYS A 1 184 ? 14.081  -3.023  13.213  1.00 32.00  ? 183 CYS A CB    1 
ATOM   1500 S  SG    . CYS A 1 184 ? 14.276  -3.892  11.652  1.00 33.31  ? 183 CYS A SG    1 
ATOM   1501 N  N     . THR A 1 185 ? 14.499  -2.423  16.232  1.00 31.48  ? 184 THR A N     1 
ATOM   1502 C  CA    . THR A 1 185 ? 14.166  -1.509  17.324  1.00 35.83  ? 184 THR A CA    1 
ATOM   1503 C  C     . THR A 1 185 ? 15.407  -1.084  18.097  1.00 35.54  ? 184 THR A C     1 
ATOM   1504 O  O     . THR A 1 185 ? 15.536  0.094   18.467  1.00 35.02  ? 184 THR A O     1 
ATOM   1505 C  CB    . THR A 1 185 ? 13.131  -2.139  18.266  1.00 36.94  ? 184 THR A CB    1 
ATOM   1506 O  OG1   . THR A 1 185 ? 12.012  -2.650  17.509  1.00 36.98  ? 184 THR A OG1   1 
ATOM   1507 C  CG2   . THR A 1 185 ? 12.647  -1.121  19.285  1.00 50.61  ? 184 THR A CG2   1 
ATOM   1508 N  N     . ALA A 1 186 ? 16.323  -2.022  18.364  1.00 31.75  ? 185 ALA A N     1 
ATOM   1509 C  CA    . ALA A 1 186 ? 17.559  -1.657  19.055  1.00 33.86  ? 185 ALA A CA    1 
ATOM   1510 C  C     . ALA A 1 186 ? 18.347  -0.607  18.275  1.00 35.53  ? 185 ALA A C     1 
ATOM   1511 O  O     . ALA A 1 186 ? 18.836  0.371   18.849  1.00 34.69  ? 185 ALA A O     1 
ATOM   1512 C  CB    . ALA A 1 186 ? 18.421  -2.904  19.286  1.00 33.23  ? 185 ALA A CB    1 
ATOM   1513 N  N     . ILE A 1 187 ? 18.470  -0.779  16.959  1.00 31.81  ? 186 ILE A N     1 
ATOM   1514 C  CA    . ILE A 1 187 ? 19.321  0.133   16.212  1.00 31.61  ? 186 ILE A CA    1 
ATOM   1515 C  C     . ILE A 1 187 ? 18.654  1.490   16.045  1.00 33.49  ? 186 ILE A C     1 
ATOM   1516 O  O     . ILE A 1 187 ? 19.317  2.532   16.149  1.00 32.57  ? 186 ILE A O     1 
ATOM   1517 C  CB    . ILE A 1 187 ? 19.737  -0.473  14.860  1.00 32.54  ? 186 ILE A CB    1 
ATOM   1518 C  CG1   . ILE A 1 187 ? 20.810  -1.535  15.079  1.00 39.41  ? 186 ILE A CG1   1 
ATOM   1519 C  CG2   . ILE A 1 187 ? 20.300  0.601   13.926  1.00 28.04  ? 186 ILE A CG2   1 
ATOM   1520 C  CD1   . ILE A 1 187 ? 20.862  -2.551  14.012  1.00 37.52  ? 186 ILE A CD1   1 
ATOM   1521 N  N     . ILE A 1 188 ? 17.346  1.508   15.758  1.00 30.03  ? 187 ILE A N     1 
ATOM   1522 C  CA    . ILE A 1 188 ? 16.629  2.772   15.648  1.00 31.69  ? 187 ILE A CA    1 
ATOM   1523 C  C     . ILE A 1 188 ? 16.755  3.564   16.952  1.00 31.92  ? 187 ILE A C     1 
ATOM   1524 O  O     . ILE A 1 188 ? 17.005  4.778   16.951  1.00 28.86  ? 187 ILE A O     1 
ATOM   1525 C  CB    . ILE A 1 188 ? 15.148  2.505   15.263  1.00 31.31  ? 187 ILE A CB    1 
ATOM   1526 C  CG1   . ILE A 1 188 ? 15.032  2.071   13.794  1.00 29.46  ? 187 ILE A CG1   1 
ATOM   1527 C  CG2   . ILE A 1 188 ? 14.283  3.737   15.470  1.00 29.88  ? 187 ILE A CG2   1 
ATOM   1528 C  CD1   . ILE A 1 188 ? 13.661  1.428   13.449  1.00 29.51  ? 187 ILE A CD1   1 
ATOM   1529 N  N     . THR A 1 189 ? 16.612  2.881   18.085  1.00 27.84  ? 188 THR A N     1 
ATOM   1530 C  CA    . THR A 1 189 ? 16.643  3.572   19.372  1.00 31.67  ? 188 THR A CA    1 
ATOM   1531 C  C     . THR A 1 189 ? 18.021  4.149   19.645  1.00 38.21  ? 188 THR A C     1 
ATOM   1532 O  O     . THR A 1 189 ? 18.148  5.295   20.089  1.00 38.52  ? 188 THR A O     1 
ATOM   1533 C  CB    . THR A 1 189 ? 16.238  2.608   20.482  1.00 36.19  ? 188 THR A CB    1 
ATOM   1534 O  OG1   . THR A 1 189 ? 14.898  2.147   20.248  1.00 41.26  ? 188 THR A OG1   1 
ATOM   1535 C  CG2   . THR A 1 189 ? 16.281  3.326   21.817  1.00 37.91  ? 188 THR A CG2   1 
ATOM   1536 N  N     A ARG A 1 190 ? 19.078  3.384   19.372  0.55 38.04  ? 189 ARG A N     1 
ATOM   1537 N  N     B ARG A 1 190 ? 19.070  3.373   19.366  0.45 37.82  ? 189 ARG A N     1 
ATOM   1538 C  CA    A ARG A 1 190 ? 20.408  3.908   19.633  0.55 40.45  ? 189 ARG A CA    1 
ATOM   1539 C  CA    B ARG A 1 190 ? 20.418  3.866   19.597  0.45 40.42  ? 189 ARG A CA    1 
ATOM   1540 C  C     A ARG A 1 190 ? 20.785  5.031   18.668  0.55 41.64  ? 189 ARG A C     1 
ATOM   1541 C  C     B ARG A 1 190 ? 20.740  5.056   18.696  0.45 41.64  ? 189 ARG A C     1 
ATOM   1542 O  O     A ARG A 1 190 ? 21.634  5.859   19.008  0.55 36.20  ? 189 ARG A O     1 
ATOM   1543 O  O     B ARG A 1 190 ? 21.501  5.945   19.096  0.45 36.06  ? 189 ARG A O     1 
ATOM   1544 C  CB    A ARG A 1 190 ? 21.416  2.749   19.638  0.55 44.28  ? 189 ARG A CB    1 
ATOM   1545 C  CB    B ARG A 1 190 ? 21.421  2.721   19.426  0.45 44.38  ? 189 ARG A CB    1 
ATOM   1546 C  CG    A ARG A 1 190 ? 22.258  2.527   18.395  0.55 43.26  ? 189 ARG A CG    1 
ATOM   1547 C  CG    B ARG A 1 190 ? 21.991  2.566   18.035  0.45 42.75  ? 189 ARG A CG    1 
ATOM   1548 C  CD    A ARG A 1 190 ? 22.912  1.137   18.519  0.55 48.75  ? 189 ARG A CD    1 
ATOM   1549 C  CD    B ARG A 1 190 ? 22.528  1.148   17.789  0.45 47.89  ? 189 ARG A CD    1 
ATOM   1550 N  NE    A ARG A 1 190 ? 23.421  0.583   17.266  0.55 48.55  ? 189 ARG A NE    1 
ATOM   1551 N  NE    B ARG A 1 190 ? 22.429  0.284   18.962  0.45 47.66  ? 189 ARG A NE    1 
ATOM   1552 C  CZ    A ARG A 1 190 ? 24.703  0.395   16.982  0.55 48.69  ? 189 ARG A CZ    1 
ATOM   1553 C  CZ    B ARG A 1 190 ? 22.851  -0.973  19.005  0.45 51.23  ? 189 ARG A CZ    1 
ATOM   1554 N  NH1   A ARG A 1 190 ? 25.657  0.713   17.842  0.55 54.87  ? 189 ARG A NH1   1 
ATOM   1555 N  NH1   B ARG A 1 190 ? 23.457  -1.534  17.971  0.45 54.87  ? 189 ARG A NH1   1 
ATOM   1556 N  NH2   A ARG A 1 190 ? 25.034  -0.157  15.819  0.55 49.01  ? 189 ARG A NH2   1 
ATOM   1557 N  NH2   B ARG A 1 190 ? 22.670  -1.682  20.115  0.45 51.42  ? 189 ARG A NH2   1 
ATOM   1558 N  N     . GLN A 1 191 ? 20.127  5.136   17.513  1.00 36.72  ? 190 GLN A N     1 
ATOM   1559 C  CA    . GLN A 1 191 ? 20.338  6.281   16.631  1.00 34.71  ? 190 GLN A CA    1 
ATOM   1560 C  C     . GLN A 1 191 ? 19.425  7.457   16.939  1.00 36.51  ? 190 GLN A C     1 
ATOM   1561 O  O     . GLN A 1 191 ? 19.423  8.433   16.178  1.00 35.73  ? 190 GLN A O     1 
ATOM   1562 C  CB    . GLN A 1 191 ? 20.191  5.880   15.167  1.00 36.79  ? 190 GLN A CB    1 
ATOM   1563 C  CG    . GLN A 1 191 ? 21.304  4.962   14.770  1.00 42.35  ? 190 GLN A CG    1 
ATOM   1564 C  CD    . GLN A 1 191 ? 22.612  5.690   14.780  1.00 40.02  ? 190 GLN A CD    1 
ATOM   1565 O  OE1   . GLN A 1 191 ? 22.674  6.887   14.484  1.00 40.05  ? 190 GLN A OE1   1 
ATOM   1566 N  NE2   . GLN A 1 191 ? 23.660  4.995   15.179  1.00 44.40  ? 190 GLN A NE2   1 
ATOM   1567 N  N     . GLY A 1 192 ? 18.666  7.394   18.028  1.00 35.73  ? 191 GLY A N     1 
ATOM   1568 C  CA    . GLY A 1 192 ? 17.831  8.504   18.451  1.00 37.24  ? 191 GLY A CA    1 
ATOM   1569 C  C     . GLY A 1 192 ? 16.426  8.536   17.888  1.00 37.11  ? 191 GLY A C     1 
ATOM   1570 O  O     . GLY A 1 192 ? 15.727  9.533   18.089  1.00 38.38  ? 191 GLY A O     1 
ATOM   1571 N  N     . GLY A 1 193 ? 15.996  7.489   17.178  1.00 34.12  ? 192 GLY A N     1 
ATOM   1572 C  CA    . GLY A 1 193 ? 14.641  7.409   16.674  1.00 37.73  ? 192 GLY A CA    1 
ATOM   1573 C  C     . GLY A 1 193 ? 13.690  6.699   17.625  1.00 37.65  ? 192 GLY A C     1 
ATOM   1574 O  O     . GLY A 1 193 ? 14.063  6.182   18.675  1.00 35.75  ? 192 GLY A O     1 
ATOM   1575 N  N     . GLU A 1 194 ? 12.416  6.671   17.240  1.00 35.48  ? 193 GLU A N     1 
ATOM   1576 C  CA    . GLU A 1 194 ? 11.399  5.990   18.031  1.00 35.01  ? 193 GLU A CA    1 
ATOM   1577 C  C     . GLU A 1 194 ? 10.568  5.085   17.138  1.00 34.15  ? 193 GLU A C     1 
ATOM   1578 O  O     . GLU A 1 194 ? 10.007  5.536   16.139  1.00 30.35  ? 193 GLU A O     1 
ATOM   1579 C  CB    . GLU A 1 194 ? 10.470  6.982   18.745  1.00 45.50  ? 193 GLU A CB    1 
ATOM   1580 C  CG    . GLU A 1 194 ? 10.291  8.312   18.015  1.00 53.26  ? 193 GLU A CG    1 
ATOM   1581 C  CD    . GLU A 1 194 ? 9.265   9.236   18.678  1.00 64.01  ? 193 GLU A CD    1 
ATOM   1582 O  OE1   . GLU A 1 194 ? 9.271   10.452  18.381  1.00 59.69  ? 193 GLU A OE1   1 
ATOM   1583 O  OE2   . GLU A 1 194 ? 8.408   8.728   19.441  1.00 57.42  ? 193 GLU A OE2   1 
ATOM   1584 N  N     . VAL A 1 195 ? 10.468  3.815   17.504  1.00 29.66  ? 194 VAL A N     1 
ATOM   1585 C  CA    . VAL A 1 195 ? 9.522   2.929   16.848  1.00 32.69  ? 194 VAL A CA    1 
ATOM   1586 C  C     . VAL A 1 195 ? 8.130   3.307   17.356  1.00 42.61  ? 194 VAL A C     1 
ATOM   1587 O  O     . VAL A 1 195 ? 7.898   3.378   18.567  1.00 36.52  ? 194 VAL A O     1 
ATOM   1588 C  CB    . VAL A 1 195 ? 9.858   1.459   17.133  1.00 36.95  ? 194 VAL A CB    1 
ATOM   1589 C  CG1   . VAL A 1 195 ? 8.813   0.537   16.533  1.00 35.14  ? 194 VAL A CG1   1 
ATOM   1590 C  CG2   . VAL A 1 195 ? 11.241  1.126   16.572  1.00 37.10  ? 194 VAL A CG2   1 
ATOM   1591 N  N     . THR A 1 196 ? 7.223   3.613   16.433  1.00 39.44  ? 195 THR A N     1 
ATOM   1592 C  CA    . THR A 1 196 ? 5.857   3.960   16.793  1.00 38.54  ? 195 THR A CA    1 
ATOM   1593 C  C     . THR A 1 196 ? 4.915   2.773   16.680  1.00 44.65  ? 195 THR A C     1 
ATOM   1594 O  O     . THR A 1 196 ? 4.025   2.619   17.518  1.00 47.52  ? 195 THR A O     1 
ATOM   1595 C  CB    . THR A 1 196 ? 5.354   5.109   15.921  1.00 43.00  ? 195 THR A CB    1 
ATOM   1596 O  OG1   . THR A 1 196 ? 5.257   4.664   14.563  1.00 42.89  ? 195 THR A OG1   1 
ATOM   1597 C  CG2   . THR A 1 196 ? 6.313   6.241   15.991  1.00 44.40  ? 195 THR A CG2   1 
ATOM   1598 N  N     . LYS A 1 197 ? 5.088   1.909   15.683  1.00 44.13  ? 196 LYS A N     1 
ATOM   1599 C  CA    . LYS A 1 197 ? 4.275   0.700   15.681  1.00 39.14  ? 196 LYS A CA    1 
ATOM   1600 C  C     . LYS A 1 197 ? 4.846   -0.348  14.743  1.00 37.55  ? 196 LYS A C     1 
ATOM   1601 O  O     . LYS A 1 197 ? 5.623   -0.051  13.830  1.00 36.16  ? 196 LYS A O     1 
ATOM   1602 C  CB    . LYS A 1 197 ? 2.820   0.968   15.280  1.00 50.20  ? 196 LYS A CB    1 
ATOM   1603 C  CG    . LYS A 1 197 ? 2.636   1.844   14.078  1.00 39.15  ? 196 LYS A CG    1 
ATOM   1604 C  CD    . LYS A 1 197 ? 1.277   2.553   14.184  1.00 50.36  ? 196 LYS A CD    1 
ATOM   1605 C  CE    . LYS A 1 197 ? 1.288   3.703   15.181  1.00 48.31  ? 196 LYS A CE    1 
ATOM   1606 N  NZ    . LYS A 1 197 ? 0.014   4.472   15.113  1.00 53.83  ? 196 LYS A NZ    1 
ATOM   1607 N  N     . PHE A 1 198 ? 4.421   -1.588  14.998  1.00 28.89  ? 197 PHE A N     1 
ATOM   1608 C  CA    . PHE A 1 198 ? 4.517   -2.690  14.057  1.00 37.46  ? 197 PHE A CA    1 
ATOM   1609 C  C     . PHE A 1 198 ? 3.211   -2.781  13.271  1.00 40.19  ? 197 PHE A C     1 
ATOM   1610 O  O     . PHE A 1 198 ? 2.125   -2.754  13.860  1.00 38.66  ? 197 PHE A O     1 
ATOM   1611 C  CB    . PHE A 1 198 ? 4.764   -3.992  14.815  1.00 31.11  ? 197 PHE A CB    1 
ATOM   1612 C  CG    . PHE A 1 198 ? 5.989   -3.962  15.674  1.00 40.46  ? 197 PHE A CG    1 
ATOM   1613 C  CD1   . PHE A 1 198 ? 7.144   -3.326  15.239  1.00 35.42  ? 197 PHE A CD1   1 
ATOM   1614 C  CD2   . PHE A 1 198 ? 5.959   -4.497  16.954  1.00 37.45  ? 197 PHE A CD2   1 
ATOM   1615 C  CE1   . PHE A 1 198 ? 8.288   -3.291  16.031  1.00 43.14  ? 197 PHE A CE1   1 
ATOM   1616 C  CE2   . PHE A 1 198 ? 7.095   -4.459  17.762  1.00 43.45  ? 197 PHE A CE2   1 
ATOM   1617 C  CZ    . PHE A 1 198 ? 8.258   -3.844  17.303  1.00 44.83  ? 197 PHE A CZ    1 
ATOM   1618 N  N     . ILE A 1 199 ? 3.321   -2.882  11.949  1.00 34.10  ? 198 ILE A N     1 
ATOM   1619 C  CA    . ILE A 1 199 ? 2.176   -3.048  11.047  1.00 34.02  ? 198 ILE A CA    1 
ATOM   1620 C  C     . ILE A 1 199 ? 2.446   -4.316  10.252  1.00 36.97  ? 198 ILE A C     1 
ATOM   1621 O  O     . ILE A 1 199 ? 3.138   -4.282  9.220   1.00 35.35  ? 198 ILE A O     1 
ATOM   1622 C  CB    . ILE A 1 199 ? 2.000   -1.858  10.104  1.00 37.98  ? 198 ILE A CB    1 
ATOM   1623 C  CG1   . ILE A 1 199 ? 2.129   -0.537  10.860  1.00 41.71  ? 198 ILE A CG1   1 
ATOM   1624 C  CG2   . ILE A 1 199 ? 0.714   -2.016  9.306   1.00 39.57  ? 198 ILE A CG2   1 
ATOM   1625 C  CD1   . ILE A 1 199 ? 2.368   0.643   9.942   1.00 49.39  ? 198 ILE A CD1   1 
ATOM   1626 N  N     . GLY A 1 200 ? 1.907   -5.429  10.711  1.00 34.38  ? 199 GLY A N     1 
ATOM   1627 C  CA    . GLY A 1 200 ? 2.305   -6.691  10.125  1.00 35.86  ? 199 GLY A CA    1 
ATOM   1628 C  C     . GLY A 1 200 ? 3.804   -6.865  10.285  1.00 33.10  ? 199 GLY A C     1 
ATOM   1629 O  O     . GLY A 1 200 ? 4.368   -6.623  11.354  1.00 30.61  ? 199 GLY A O     1 
ATOM   1630 N  N     . ASP A 1 201 ? 4.466   -7.273  9.208   1.00 34.50  ? 200 ASP A N     1 
ATOM   1631 C  CA    . ASP A 1 201 ? 5.917   -7.461  9.243   1.00 29.18  ? 200 ASP A CA    1 
ATOM   1632 C  C     . ASP A 1 201 ? 6.675   -6.169  9.085   1.00 35.25  ? 200 ASP A C     1 
ATOM   1633 O  O     . ASP A 1 201 ? 7.885   -6.199  8.869   1.00 37.57  ? 200 ASP A O     1 
ATOM   1634 C  CB    . ASP A 1 201 ? 6.336   -8.431  8.138   1.00 37.05  ? 200 ASP A CB    1 
ATOM   1635 C  CG    . ASP A 1 201 ? 6.029   -7.888  6.761   1.00 41.06  ? 200 ASP A CG    1 
ATOM   1636 O  OD1   . ASP A 1 201 ? 4.849   -7.605  6.512   1.00 35.54  ? 200 ASP A OD1   1 
ATOM   1637 O  OD2   . ASP A 1 201 ? 6.951   -7.776  5.928   1.00 39.86  ? 200 ASP A OD2   1 
ATOM   1638 N  N     . CYS A 1 202 ? 6.012   -5.029  9.174   1.00 35.65  ? 201 CYS A N     1 
ATOM   1639 C  CA    . CYS A 1 202 ? 6.660   -3.764  8.881   1.00 32.31  ? 201 CYS A CA    1 
ATOM   1640 C  C     . CYS A 1 202 ? 6.866   -2.969  10.167  1.00 33.48  ? 201 CYS A C     1 
ATOM   1641 O  O     . CYS A 1 202 ? 5.964   -2.901  11.012  1.00 32.82  ? 201 CYS A O     1 
ATOM   1642 C  CB    . CYS A 1 202 ? 5.845   -2.981  7.853   1.00 35.00  ? 201 CYS A CB    1 
ATOM   1643 S  SG    . CYS A 1 202 ? 6.135   -1.227  7.889   1.00 47.42  ? 201 CYS A SG    1 
ATOM   1644 N  N     . VAL A 1 203 ? 8.082   -2.429  10.342  1.00 28.66  ? 202 VAL A N     1 
ATOM   1645 C  CA    . VAL A 1 203 ? 8.406   -1.528  11.445  1.00 28.74  ? 202 VAL A CA    1 
ATOM   1646 C  C     . VAL A 1 203 ? 8.219   -0.097  10.963  1.00 36.67  ? 202 VAL A C     1 
ATOM   1647 O  O     . VAL A 1 203 ? 8.755   0.294   9.917   1.00 36.11  ? 202 VAL A O     1 
ATOM   1648 C  CB    . VAL A 1 203 ? 9.854   -1.741  11.938  1.00 38.79  ? 202 VAL A CB    1 
ATOM   1649 C  CG1   . VAL A 1 203 ? 10.253  -0.646  12.937  1.00 35.79  ? 202 VAL A CG1   1 
ATOM   1650 C  CG2   . VAL A 1 203 ? 10.053  -3.110  12.577  1.00 38.70  ? 202 VAL A CG2   1 
ATOM   1651 N  N     . MET A 1 204 ? 7.486   0.687   11.742  1.00 30.50  ? 203 MET A N     1 
ATOM   1652 C  CA    . MET A 1 204 ? 7.314   2.125   11.553  1.00 26.07  ? 203 MET A CA    1 
ATOM   1653 C  C     . MET A 1 204 ? 8.027   2.912   12.636  1.00 31.56  ? 203 MET A C     1 
ATOM   1654 O  O     . MET A 1 204 ? 7.818   2.648   13.827  1.00 31.29  ? 203 MET A O     1 
ATOM   1655 C  CB    . MET A 1 204 ? 5.831   2.506   11.593  1.00 32.99  ? 203 MET A CB    1 
ATOM   1656 C  CG    . MET A 1 204 ? 5.571   3.864   11.030  1.00 30.28  ? 203 MET A CG    1 
ATOM   1657 S  SD    . MET A 1 204 ? 3.811   4.260   11.030  1.00 42.21  ? 203 MET A SD    1 
ATOM   1658 C  CE    . MET A 1 204 ? 3.883   5.992   10.592  1.00 33.31  ? 203 MET A CE    1 
ATOM   1659 N  N     . ALA A 1 205 ? 8.828   3.905   12.230  1.00 30.22  ? 204 ALA A N     1 
ATOM   1660 C  CA    . ALA A 1 205 ? 9.594   4.681   13.193  1.00 34.33  ? 204 ALA A CA    1 
ATOM   1661 C  C     . ALA A 1 205 ? 9.698   6.123   12.723  1.00 32.00  ? 204 ALA A C     1 
ATOM   1662 O  O     . ALA A 1 205 ? 9.548   6.430   11.534  1.00 30.91  ? 204 ALA A O     1 
ATOM   1663 C  CB    . ALA A 1 205 ? 11.003  4.099   13.429  1.00 26.89  ? 204 ALA A CB    1 
ATOM   1664 N  N     . TYR A 1 206 ? 9.918   7.006   13.690  1.00 28.82  ? 205 TYR A N     1 
ATOM   1665 C  CA    . TYR A 1 206 ? 10.166  8.418   13.452  1.00 27.84  ? 205 TYR A CA    1 
ATOM   1666 C  C     . TYR A 1 206 ? 11.583  8.782   13.860  1.00 33.32  ? 205 TYR A C     1 
ATOM   1667 O  O     . TYR A 1 206 ? 12.098  8.279   14.858  1.00 33.00  ? 205 TYR A O     1 
ATOM   1668 C  CB    . TYR A 1 206 ? 9.215   9.303   14.254  1.00 32.56  ? 205 TYR A CB    1 
ATOM   1669 C  CG    . TYR A 1 206 ? 7.738   9.172   13.924  1.00 32.31  ? 205 TYR A CG    1 
ATOM   1670 C  CD1   . TYR A 1 206 ? 7.322   8.936   12.632  1.00 30.86  ? 205 TYR A CD1   1 
ATOM   1671 C  CD2   . TYR A 1 206 ? 6.772   9.302   14.908  1.00 39.48  ? 205 TYR A CD2   1 
ATOM   1672 C  CE1   . TYR A 1 206 ? 5.976   8.819   12.315  1.00 37.05  ? 205 TYR A CE1   1 
ATOM   1673 C  CE2   . TYR A 1 206 ? 5.402   9.179   14.598  1.00 38.29  ? 205 TYR A CE2   1 
ATOM   1674 C  CZ    . TYR A 1 206 ? 5.022   8.935   13.298  1.00 41.52  ? 205 TYR A CZ    1 
ATOM   1675 O  OH    . TYR A 1 206 ? 3.696   8.810   12.957  1.00 51.22  ? 205 TYR A OH    1 
ATOM   1676 N  N     . PHE A 1 207 ? 12.177  9.683   13.096  1.00 32.27  ? 206 PHE A N     1 
ATOM   1677 C  CA    . PHE A 1 207 ? 13.320  10.478  13.500  1.00 32.39  ? 206 PHE A CA    1 
ATOM   1678 C  C     . PHE A 1 207 ? 12.927  11.941  13.379  1.00 38.02  ? 206 PHE A C     1 
ATOM   1679 O  O     . PHE A 1 207 ? 12.098  12.295  12.537  1.00 37.79  ? 206 PHE A O     1 
ATOM   1680 C  CB    . PHE A 1 207 ? 14.563  10.188  12.609  1.00 31.50  ? 206 PHE A CB    1 
ATOM   1681 C  CG    . PHE A 1 207 ? 15.119  8.788   12.762  1.00 32.90  ? 206 PHE A CG    1 
ATOM   1682 C  CD1   . PHE A 1 207 ? 14.513  7.706   12.123  1.00 30.51  ? 206 PHE A CD1   1 
ATOM   1683 C  CD2   . PHE A 1 207 ? 16.263  8.558   13.531  1.00 29.46  ? 206 PHE A CD2   1 
ATOM   1684 C  CE1   . PHE A 1 207 ? 15.025  6.410   12.266  1.00 26.40  ? 206 PHE A CE1   1 
ATOM   1685 C  CE2   . PHE A 1 207 ? 16.776  7.270   13.681  1.00 30.75  ? 206 PHE A CE2   1 
ATOM   1686 C  CZ    . PHE A 1 207 ? 16.145  6.189   13.031  1.00 28.50  ? 206 PHE A CZ    1 
ATOM   1687 N  N     . ASP A 1 208 ? 13.509  12.781  14.231  1.00 37.68  ? 207 ASP A N     1 
ATOM   1688 C  CA    . ASP A 1 208 ? 13.325  14.222  14.107  1.00 41.87  ? 207 ASP A CA    1 
ATOM   1689 C  C     . ASP A 1 208 ? 13.546  14.665  12.669  1.00 42.19  ? 207 ASP A C     1 
ATOM   1690 O  O     . ASP A 1 208 ? 14.374  14.104  11.939  1.00 40.97  ? 207 ASP A O     1 
ATOM   1691 C  CB    . ASP A 1 208 ? 14.293  14.968  15.033  1.00 45.74  ? 207 ASP A CB    1 
ATOM   1692 C  CG    . ASP A 1 208 ? 13.805  15.020  16.471  1.00 53.40  ? 207 ASP A CG    1 
ATOM   1693 O  OD1   . ASP A 1 208 ? 12.757  14.398  16.776  1.00 58.33  ? 207 ASP A OD1   1 
ATOM   1694 O  OD2   . ASP A 1 208 ? 14.508  15.627  17.316  1.00 56.90  ? 207 ASP A OD2   1 
ATOM   1695 N  N     . GLY A 1 209 ? 12.803  15.701  12.274  1.00 43.91  ? 208 GLY A N     1 
ATOM   1696 C  CA    . GLY A 1 209 ? 12.827  16.164  10.893  1.00 45.33  ? 208 GLY A CA    1 
ATOM   1697 C  C     . GLY A 1 209 ? 14.209  16.469  10.337  1.00 43.22  ? 208 GLY A C     1 
ATOM   1698 O  O     . GLY A 1 209 ? 14.432  16.352  9.127   1.00 47.23  ? 208 GLY A O     1 
ATOM   1699 N  N     . ASP A 1 210 ? 15.148  16.892  11.180  1.00 48.56  ? 209 ASP A N     1 
ATOM   1700 C  CA    . ASP A 1 210 ? 16.467  17.228  10.659  1.00 52.80  ? 209 ASP A CA    1 
ATOM   1701 C  C     . ASP A 1 210 ? 17.528  16.203  11.044  1.00 53.26  ? 209 ASP A C     1 
ATOM   1702 O  O     . ASP A 1 210 ? 18.726  16.479  10.924  1.00 47.38  ? 209 ASP A O     1 
ATOM   1703 C  CB    . ASP A 1 210 ? 16.894  18.631  11.087  1.00 59.56  ? 209 ASP A CB    1 
ATOM   1704 C  CG    . ASP A 1 210 ? 16.631  18.909  12.539  1.00 63.69  ? 209 ASP A CG    1 
ATOM   1705 O  OD1   . ASP A 1 210 ? 16.581  17.953  13.344  1.00 62.78  ? 209 ASP A OD1   1 
ATOM   1706 O  OD2   . ASP A 1 210 ? 16.481  20.103  12.876  1.00 79.56  ? 209 ASP A OD2   1 
ATOM   1707 N  N     . CYS A 1 211 ? 17.113  15.011  11.465  1.00 45.11  ? 210 CYS A N     1 
ATOM   1708 C  CA    . CYS A 1 211 ? 18.035  13.915  11.752  1.00 37.86  ? 210 CYS A CA    1 
ATOM   1709 C  C     . CYS A 1 211 ? 18.094  12.893  10.620  1.00 36.46  ? 210 CYS A C     1 
ATOM   1710 O  O     . CYS A 1 211 ? 18.133  11.686  10.871  1.00 35.53  ? 210 CYS A O     1 
ATOM   1711 C  CB    . CYS A 1 211 ? 17.658  13.246  13.061  1.00 39.02  ? 210 CYS A CB    1 
ATOM   1712 S  SG    . CYS A 1 211 ? 17.835  14.367  14.457  1.00 52.22  ? 210 CYS A SG    1 
ATOM   1713 N  N     . ALA A 1 212 ? 18.140  13.342  9.364   1.00 36.08  ? 211 ALA A N     1 
ATOM   1714 C  CA    . ALA A 1 212 ? 18.258  12.382  8.264   1.00 39.71  ? 211 ALA A CA    1 
ATOM   1715 C  C     . ALA A 1 212 ? 19.509  11.526  8.404   1.00 31.22  ? 211 ALA A C     1 
ATOM   1716 O  O     . ALA A 1 212 ? 19.459  10.312  8.167   1.00 31.99  ? 211 ALA A O     1 
ATOM   1717 C  CB    . ALA A 1 212 ? 18.256  13.093  6.906   1.00 33.44  ? 211 ALA A CB    1 
ATOM   1718 N  N     . ASP A 1 213 ? 20.646  12.140  8.784   1.00 36.14  ? 212 ASP A N     1 
ATOM   1719 C  CA    . ASP A 1 213 ? 21.894  11.386  8.947   1.00 37.04  ? 212 ASP A CA    1 
ATOM   1720 C  C     . ASP A 1 213 ? 21.710  10.194  9.880   1.00 33.44  ? 212 ASP A C     1 
ATOM   1721 O  O     . ASP A 1 213 ? 22.247  9.105   9.628   1.00 33.78  ? 212 ASP A O     1 
ATOM   1722 C  CB    . ASP A 1 213 ? 22.999  12.301  9.488   1.00 38.75  ? 212 ASP A CB    1 
ATOM   1723 C  CG    . ASP A 1 213 ? 23.463  13.328  8.471   1.00 45.32  ? 212 ASP A CG    1 
ATOM   1724 O  OD1   . ASP A 1 213 ? 23.464  13.040  7.254   1.00 39.75  ? 212 ASP A OD1   1 
ATOM   1725 O  OD2   . ASP A 1 213 ? 23.787  14.455  8.889   1.00 58.95  ? 212 ASP A OD2   1 
ATOM   1726 N  N     . GLN A 1 214 ? 20.956  10.382  10.963  1.00 30.97  ? 213 GLN A N     1 
ATOM   1727 C  CA    . GLN A 1 214 ? 20.719  9.306   11.919  1.00 28.02  ? 213 GLN A CA    1 
ATOM   1728 C  C     . GLN A 1 214 ? 19.784  8.259   11.336  1.00 34.12  ? 213 GLN A C     1 
ATOM   1729 O  O     . GLN A 1 214 ? 19.960  7.057   11.574  1.00 31.87  ? 213 GLN A O     1 
ATOM   1730 C  CB    . GLN A 1 214 ? 20.134  9.877   13.206  1.00 31.60  ? 213 GLN A CB    1 
ATOM   1731 C  CG    . GLN A 1 214 ? 21.185  10.535  14.115  1.00 36.86  ? 213 GLN A CG    1 
ATOM   1732 C  CD    . GLN A 1 214 ? 21.801  11.772  13.474  1.00 46.25  ? 213 GLN A CD    1 
ATOM   1733 O  OE1   . GLN A 1 214 ? 21.089  12.707  13.101  1.00 46.48  ? 213 GLN A OE1   1 
ATOM   1734 N  NE2   . GLN A 1 214 ? 23.132  11.786  13.346  1.00 47.08  ? 213 GLN A NE2   1 
ATOM   1735 N  N     . ALA A 1 215 ? 18.785  8.694   10.562  1.00 31.87  ? 214 ALA A N     1 
ATOM   1736 C  CA    . ALA A 1 215 ? 17.889  7.729   9.931   1.00 30.45  ? 214 ALA A CA    1 
ATOM   1737 C  C     . ALA A 1 215 ? 18.638  6.907   8.883   1.00 31.84  ? 214 ALA A C     1 
ATOM   1738 O  O     . ALA A 1 215 ? 18.412  5.695   8.762   1.00 31.39  ? 214 ALA A O     1 
ATOM   1739 C  CB    . ALA A 1 215 ? 16.670  8.443   9.326   1.00 26.87  ? 214 ALA A CB    1 
ATOM   1740 N  N     . ILE A 1 216 ? 19.551  7.532   8.137   1.00 28.14  ? 215 ILE A N     1 
ATOM   1741 C  CA    . ILE A 1 216 ? 20.336  6.779   7.155   1.00 23.96  ? 215 ILE A CA    1 
ATOM   1742 C  C     . ILE A 1 216 ? 21.308  5.831   7.858   1.00 31.51  ? 215 ILE A C     1 
ATOM   1743 O  O     . ILE A 1 216 ? 21.415  4.648   7.496   1.00 28.69  ? 215 ILE A O     1 
ATOM   1744 C  CB    . ILE A 1 216 ? 21.046  7.752   6.195   1.00 34.48  ? 215 ILE A CB    1 
ATOM   1745 C  CG1   . ILE A 1 216 ? 19.988  8.470   5.346   1.00 31.11  ? 215 ILE A CG1   1 
ATOM   1746 C  CG2   . ILE A 1 216 ? 22.064  7.024   5.263   1.00 24.55  ? 215 ILE A CG2   1 
ATOM   1747 C  CD1   . ILE A 1 216 ? 20.505  9.744   4.668   1.00 35.17  ? 215 ILE A CD1   1 
ATOM   1748 N  N     . GLN A 1 217 ? 21.985  6.314   8.908   1.00 29.36  ? 216 GLN A N     1 
ATOM   1749 C  CA    . GLN A 1 217 ? 22.908  5.461   9.652   1.00 31.22  ? 216 GLN A CA    1 
ATOM   1750 C  C     . GLN A 1 217 ? 22.181  4.260   10.218  1.00 32.29  ? 216 GLN A C     1 
ATOM   1751 O  O     . GLN A 1 217 ? 22.671  3.123   10.133  1.00 30.01  ? 216 GLN A O     1 
ATOM   1752 C  CB    . GLN A 1 217 ? 23.562  6.231   10.796  1.00 31.08  ? 216 GLN A CB    1 
ATOM   1753 C  CG    . GLN A 1 217 ? 24.672  5.453   11.498  1.00 32.96  ? 216 GLN A CG    1 
ATOM   1754 C  CD    . GLN A 1 217 ? 25.802  5.134   10.537  1.00 42.10  ? 216 GLN A CD    1 
ATOM   1755 O  OE1   . GLN A 1 217 ? 26.524  6.041   10.133  1.00 38.11  ? 216 GLN A OE1   1 
ATOM   1756 N  NE2   . GLN A 1 217 ? 25.957  3.862   10.156  1.00 40.27  ? 216 GLN A NE2   1 
ATOM   1757 N  N     . ALA A 1 218 ? 21.015  4.500   10.839  1.00 29.51  ? 217 ALA A N     1 
ATOM   1758 C  CA    . ALA A 1 218 ? 20.223  3.403   11.385  1.00 31.19  ? 217 ALA A CA    1 
ATOM   1759 C  C     . ALA A 1 218 ? 19.884  2.392   10.303  1.00 26.91  ? 217 ALA A C     1 
ATOM   1760 O  O     . ALA A 1 218 ? 19.958  1.183   10.528  1.00 27.99  ? 217 ALA A O     1 
ATOM   1761 C  CB    . ALA A 1 218 ? 18.933  3.935   12.033  1.00 31.03  ? 217 ALA A CB    1 
ATOM   1762 N  N     . SER A 1 219 ? 19.473  2.877   9.127   1.00 23.86  ? 218 SER A N     1 
ATOM   1763 C  CA    . SER A 1 219 ? 19.097  1.978   8.035   1.00 32.29  ? 218 SER A CA    1 
ATOM   1764 C  C     . SER A 1 219 ? 20.277  1.108   7.592   1.00 35.00  ? 218 SER A C     1 
ATOM   1765 O  O     . SER A 1 219 ? 20.155  -0.119  7.446   1.00 29.08  ? 218 SER A O     1 
ATOM   1766 C  CB    . SER A 1 219 ? 18.566  2.812   6.869   1.00 26.92  ? 218 SER A CB    1 
ATOM   1767 O  OG    . SER A 1 219 ? 17.407  3.554   7.265   1.00 30.26  ? 218 SER A OG    1 
ATOM   1768 N  N     . LEU A 1 220 ? 21.430  1.729   7.366   1.00 30.98  ? 219 LEU A N     1 
ATOM   1769 C  CA    . LEU A 1 220 ? 22.624  0.966   7.004   1.00 31.35  ? 219 LEU A CA    1 
ATOM   1770 C  C     . LEU A 1 220 ? 23.040  0.016   8.126   1.00 26.41  ? 219 LEU A C     1 
ATOM   1771 O  O     . LEU A 1 220 ? 23.478  -1.112  7.866   1.00 32.04  ? 219 LEU A O     1 
ATOM   1772 C  CB    . LEU A 1 220 ? 23.767  1.933   6.676   1.00 29.47  ? 219 LEU A CB    1 
ATOM   1773 C  CG    . LEU A 1 220 ? 23.555  2.798   5.442   1.00 31.81  ? 219 LEU A CG    1 
ATOM   1774 C  CD1   . LEU A 1 220 ? 24.587  3.898   5.410   1.00 38.48  ? 219 LEU A CD1   1 
ATOM   1775 C  CD2   . LEU A 1 220 ? 23.637  1.965   4.168   1.00 34.19  ? 219 LEU A CD2   1 
ATOM   1776 N  N     . ASP A 1 221 ? 22.950  0.462   9.375   1.00 27.04  ? 220 ASP A N     1 
ATOM   1777 C  CA    . ASP A 1 221 ? 23.318  -0.418  10.481  1.00 30.43  ? 220 ASP A CA    1 
ATOM   1778 C  C     . ASP A 1 221 ? 22.405  -1.640  10.520  1.00 28.95  ? 220 ASP A C     1 
ATOM   1779 O  O     . ASP A 1 221 ? 22.861  -2.763  10.765  1.00 28.82  ? 220 ASP A O     1 
ATOM   1780 C  CB    . ASP A 1 221 ? 23.257  0.358   11.798  1.00 31.71  ? 220 ASP A CB    1 
ATOM   1781 C  CG    . ASP A 1 221 ? 24.489  1.256   12.025  1.00 45.67  ? 220 ASP A CG    1 
ATOM   1782 O  OD1   . ASP A 1 221 ? 25.384  1.360   11.137  1.00 41.84  ? 220 ASP A OD1   1 
ATOM   1783 O  OD2   . ASP A 1 221 ? 24.498  1.945   13.066  1.00 43.20  ? 220 ASP A OD2   1 
ATOM   1784 N  N     . ILE A 1 222 ? 21.118  -1.452  10.234  1.00 28.09  ? 221 ILE A N     1 
ATOM   1785 C  CA    . ILE A 1 222 ? 20.195  -2.587  10.255  1.00 28.68  ? 221 ILE A CA    1 
ATOM   1786 C  C     . ILE A 1 222 ? 20.545  -3.562  9.143   1.00 28.11  ? 221 ILE A C     1 
ATOM   1787 O  O     . ILE A 1 222 ? 20.640  -4.775  9.364   1.00 29.03  ? 221 ILE A O     1 
ATOM   1788 C  CB    . ILE A 1 222 ? 18.734  -2.104  10.141  1.00 30.14  ? 221 ILE A CB    1 
ATOM   1789 C  CG1   . ILE A 1 222 ? 18.291  -1.449  11.449  1.00 28.49  ? 221 ILE A CG1   1 
ATOM   1790 C  CG2   . ILE A 1 222 ? 17.789  -3.278  9.772   1.00 25.13  ? 221 ILE A CG2   1 
ATOM   1791 C  CD1   . ILE A 1 222 ? 17.015  -0.551  11.275  1.00 27.81  ? 221 ILE A CD1   1 
ATOM   1792 N  N     . LEU A 1 223 ? 20.746  -3.045  7.932   1.00 27.52  ? 222 LEU A N     1 
ATOM   1793 C  CA    . LEU A 1 223 ? 21.133  -3.912  6.821   1.00 35.64  ? 222 LEU A CA    1 
ATOM   1794 C  C     . LEU A 1 223 ? 22.411  -4.682  7.138   1.00 30.52  ? 222 LEU A C     1 
ATOM   1795 O  O     . LEU A 1 223 ? 22.517  -5.878  6.830   1.00 31.71  ? 222 LEU A O     1 
ATOM   1796 C  CB    . LEU A 1 223 ? 21.317  -3.099  5.543   1.00 33.38  ? 222 LEU A CB    1 
ATOM   1797 C  CG    . LEU A 1 223 ? 20.077  -2.399  5.013   1.00 38.63  ? 222 LEU A CG    1 
ATOM   1798 C  CD1   . LEU A 1 223 ? 20.442  -1.645  3.751   1.00 37.16  ? 222 LEU A CD1   1 
ATOM   1799 C  CD2   . LEU A 1 223 ? 18.947  -3.422  4.773   1.00 38.37  ? 222 LEU A CD2   1 
ATOM   1800 N  N     . MET A 1 224 ? 23.385  -4.015  7.760   1.00 27.12  ? 223 MET A N     1 
ATOM   1801 C  CA    . MET A 1 224 ? 24.656  -4.670  8.078   1.00 34.08  ? 223 MET A CA    1 
ATOM   1802 C  C     . MET A 1 224 ? 24.435  -5.757  9.120   1.00 33.08  ? 223 MET A C     1 
ATOM   1803 O  O     . MET A 1 224 ? 24.949  -6.876  8.985   1.00 29.67  ? 223 MET A O     1 
ATOM   1804 C  CB    . MET A 1 224 ? 25.663  -3.636  8.598   1.00 32.38  ? 223 MET A CB    1 
ATOM   1805 C  CG    . MET A 1 224 ? 27.007  -4.193  9.045   1.00 47.66  ? 223 MET A CG    1 
ATOM   1806 S  SD    . MET A 1 224 ? 27.551  -5.569  7.994   1.00 79.14  ? 223 MET A SD    1 
ATOM   1807 C  CE    . MET A 1 224 ? 27.881  -4.683  6.463   1.00 49.65  ? 223 MET A CE    1 
ATOM   1808 N  N     . GLU A 1 225 ? 23.659  -5.441  10.173  1.00 31.41  ? 224 GLU A N     1 
ATOM   1809 C  CA    . GLU A 1 225 ? 23.330  -6.424  11.206  1.00 32.88  ? 224 GLU A CA    1 
ATOM   1810 C  C     . GLU A 1 225 ? 22.528  -7.594  10.662  1.00 35.26  ? 224 GLU A C     1 
ATOM   1811 O  O     . GLU A 1 225 ? 22.671  -8.720  11.160  1.00 31.60  ? 224 GLU A O     1 
ATOM   1812 C  CB    . GLU A 1 225 ? 22.543  -5.781  12.357  1.00 34.29  ? 224 GLU A CB    1 
ATOM   1813 C  CG    . GLU A 1 225 ? 23.309  -4.782  13.198  1.00 46.62  ? 224 GLU A CG    1 
ATOM   1814 C  CD    . GLU A 1 225 ? 24.525  -5.383  13.885  1.00 50.04  ? 224 GLU A CD    1 
ATOM   1815 O  OE1   . GLU A 1 225 ? 24.492  -6.586  14.231  1.00 52.37  ? 224 GLU A OE1   1 
ATOM   1816 O  OE2   . GLU A 1 225 ? 25.512  -4.649  14.088  1.00 59.24  ? 224 GLU A OE2   1 
ATOM   1817 N  N     . LEU A 1 226 ? 21.651  -7.362  9.682   1.00 28.58  ? 225 LEU A N     1 
ATOM   1818 C  CA    . LEU A 1 226 ? 20.912  -8.497  9.153   1.00 29.60  ? 225 LEU A CA    1 
ATOM   1819 C  C     . LEU A 1 226 ? 21.829  -9.378  8.316   1.00 25.23  ? 225 LEU A C     1 
ATOM   1820 O  O     . LEU A 1 226 ? 21.720  -10.609 8.361   1.00 31.43  ? 225 LEU A O     1 
ATOM   1821 C  CB    . LEU A 1 226 ? 19.695  -8.053  8.321   1.00 24.85  ? 225 LEU A CB    1 
ATOM   1822 C  CG    . LEU A 1 226 ? 18.533  -7.438  9.126   1.00 29.16  ? 225 LEU A CG    1 
ATOM   1823 C  CD1   . LEU A 1 226 ? 17.342  -6.958  8.199   1.00 24.59  ? 225 LEU A CD1   1 
ATOM   1824 C  CD2   . LEU A 1 226 ? 18.076  -8.318  10.293  1.00 31.44  ? 225 LEU A CD2   1 
ATOM   1825 N  N     . GLU A 1 227 ? 22.711  -8.768  7.518   1.00 28.01  ? 226 GLU A N     1 
ATOM   1826 C  CA    . GLU A 1 227 ? 23.722  -9.557  6.803   1.00 34.19  ? 226 GLU A CA    1 
ATOM   1827 C  C     . GLU A 1 227 ? 24.559  -10.396 7.775   1.00 28.99  ? 226 GLU A C     1 
ATOM   1828 O  O     . GLU A 1 227 ? 24.786  -11.593 7.554   1.00 31.40  ? 226 GLU A O     1 
ATOM   1829 C  CB    . GLU A 1 227 ? 24.626  -8.640  5.971   1.00 32.15  ? 226 GLU A CB    1 
ATOM   1830 C  CG    . GLU A 1 227 ? 25.766  -9.364  5.207   1.00 37.10  ? 226 GLU A CG    1 
ATOM   1831 C  CD    . GLU A 1 227 ? 25.269  -10.153 3.998   1.00 43.17  ? 226 GLU A CD    1 
ATOM   1832 O  OE1   . GLU A 1 227 ? 24.236  -9.772  3.395   1.00 51.56  ? 226 GLU A OE1   1 
ATOM   1833 O  OE2   . GLU A 1 227 ? 25.896  -11.175 3.655   1.00 49.78  ? 226 GLU A OE2   1 
ATOM   1834 N  N     . ILE A 1 228 ? 25.007  -9.793  8.870   1.00 30.00  ? 227 ILE A N     1 
ATOM   1835 C  CA    . ILE A 1 228 ? 25.741  -10.563 9.875   1.00 32.96  ? 227 ILE A CA    1 
ATOM   1836 C  C     . ILE A 1 228 ? 24.865  -11.668 10.450  1.00 38.84  ? 227 ILE A C     1 
ATOM   1837 O  O     . ILE A 1 228 ? 25.322  -12.803 10.666  1.00 34.88  ? 227 ILE A O     1 
ATOM   1838 C  CB    . ILE A 1 228 ? 26.263  -9.635  10.990  1.00 38.47  ? 227 ILE A CB    1 
ATOM   1839 C  CG1   . ILE A 1 228 ? 27.455  -8.808  10.496  1.00 43.14  ? 227 ILE A CG1   1 
ATOM   1840 C  CG2   . ILE A 1 228 ? 26.616  -10.443 12.248  1.00 37.81  ? 227 ILE A CG2   1 
ATOM   1841 C  CD1   . ILE A 1 228 ? 27.595  -7.456  11.188  1.00 42.54  ? 227 ILE A CD1   1 
ATOM   1842 N  N     . LEU A 1 229 ? 23.595  -11.349 10.726  1.00 32.29  ? 228 LEU A N     1 
ATOM   1843 C  CA    . LEU A 1 229 ? 22.673  -12.342 11.258  1.00 31.70  ? 228 LEU A CA    1 
ATOM   1844 C  C     . LEU A 1 229 ? 22.532  -13.523 10.302  1.00 29.79  ? 228 LEU A C     1 
ATOM   1845 O  O     . LEU A 1 229 ? 22.646  -14.680 10.719  1.00 35.45  ? 228 LEU A O     1 
ATOM   1846 C  CB    . LEU A 1 229 ? 21.310  -11.687 11.520  1.00 34.29  ? 228 LEU A CB    1 
ATOM   1847 C  CG    . LEU A 1 229 ? 20.288  -12.543 12.236  1.00 36.10  ? 228 LEU A CG    1 
ATOM   1848 C  CD1   . LEU A 1 229 ? 20.944  -13.242 13.443  1.00 42.57  ? 228 LEU A CD1   1 
ATOM   1849 C  CD2   . LEU A 1 229 ? 19.116  -11.684 12.650  1.00 42.51  ? 228 LEU A CD2   1 
ATOM   1850 N  N     . ARG A 1 230 ? 22.275  -13.246 9.010   1.00 25.86  ? 229 ARG A N     1 
ATOM   1851 C  CA    . ARG A 1 230 ? 22.117  -14.326 8.029   1.00 31.64  ? 229 ARG A CA    1 
ATOM   1852 C  C     . ARG A 1 230 ? 23.372  -15.196 7.962   1.00 33.23  ? 229 ARG A C     1 
ATOM   1853 O  O     . ARG A 1 230 ? 23.286  -16.430 7.867   1.00 33.05  ? 229 ARG A O     1 
ATOM   1854 C  CB    . ARG A 1 230 ? 21.824  -13.756 6.634   1.00 31.64  ? 229 ARG A CB    1 
ATOM   1855 C  CG    . ARG A 1 230 ? 20.448  -13.111 6.459   1.00 32.00  ? 229 ARG A CG    1 
ATOM   1856 C  CD    . ARG A 1 230 ? 20.211  -12.751 5.009   1.00 30.05  ? 229 ARG A CD    1 
ATOM   1857 N  NE    . ARG A 1 230 ? 21.120  -11.706 4.546   1.00 29.01  ? 229 ARG A NE    1 
ATOM   1858 C  CZ    . ARG A 1 230 ? 20.791  -10.421 4.525   1.00 32.60  ? 229 ARG A CZ    1 
ATOM   1859 N  NH1   . ARG A 1 230 ? 19.664  -9.994  5.077   1.00 30.42  ? 229 ARG A NH1   1 
ATOM   1860 N  NH2   . ARG A 1 230 ? 21.622  -9.540  3.968   1.00 29.15  ? 229 ARG A NH2   1 
ATOM   1861 N  N     . ASN A 1 231 ? 24.545  -14.560 7.975   1.00 32.07  ? 230 ASN A N     1 
ATOM   1862 C  CA    . ASN A 1 231 ? 25.796  -15.306 7.833   1.00 34.41  ? 230 ASN A CA    1 
ATOM   1863 C  C     . ASN A 1 231 ? 26.141  -16.090 9.092   1.00 32.23  ? 230 ASN A C     1 
ATOM   1864 O  O     . ASN A 1 231 ? 26.747  -17.157 8.994   1.00 32.55  ? 230 ASN A O     1 
ATOM   1865 C  CB    . ASN A 1 231 ? 26.948  -14.359 7.482   1.00 29.55  ? 230 ASN A CB    1 
ATOM   1866 C  CG    . ASN A 1 231 ? 26.711  -13.588 6.194   1.00 34.71  ? 230 ASN A CG    1 
ATOM   1867 O  OD1   . ASN A 1 231 ? 25.835  -13.919 5.400   1.00 43.52  ? 230 ASN A OD1   1 
ATOM   1868 N  ND2   . ASN A 1 231 ? 27.470  -12.547 5.999   1.00 39.93  ? 230 ASN A ND2   1 
ATOM   1869 N  N     . SER A 1 232 ? 25.771  -15.591 10.275  1.00 29.34  ? 231 SER A N     1 
ATOM   1870 C  CA    . SER A 1 232 ? 26.222  -16.225 11.507  1.00 35.66  ? 231 SER A CA    1 
ATOM   1871 C  C     . SER A 1 232 ? 25.234  -17.235 12.069  1.00 36.46  ? 231 SER A C     1 
ATOM   1872 O  O     . SER A 1 232 ? 25.576  -17.945 13.023  1.00 35.79  ? 231 SER A O     1 
ATOM   1873 C  CB    . SER A 1 232 ? 26.511  -15.177 12.581  1.00 37.01  ? 231 SER A CB    1 
ATOM   1874 O  OG    . SER A 1 232 ? 25.368  -14.402 12.852  1.00 45.66  ? 231 SER A OG    1 
ATOM   1875 N  N     . ALA A 1 233 ? 24.036  -17.329 11.503  1.00 32.00  ? 232 ALA A N     1 
ATOM   1876 C  CA    . ALA A 1 233 ? 23.055  -18.286 11.973  1.00 35.88  ? 232 ALA A CA    1 
ATOM   1877 C  C     . ALA A 1 233 ? 23.534  -19.720 11.739  1.00 40.11  ? 232 ALA A C     1 
ATOM   1878 O  O     . ALA A 1 233 ? 24.331  -19.982 10.838  1.00 37.19  ? 232 ALA A O     1 
ATOM   1879 C  CB    . ALA A 1 233 ? 21.714  -18.051 11.257  1.00 33.46  ? 232 ALA A CB    1 
ATOM   1880 N  N     . PRO A 1 234 ? 23.028  -20.674 12.524  1.00 40.42  ? 233 PRO A N     1 
ATOM   1881 C  CA    . PRO A 1 234 ? 23.361  -22.087 12.285  1.00 40.13  ? 233 PRO A CA    1 
ATOM   1882 C  C     . PRO A 1 234 ? 22.963  -22.561 10.890  1.00 43.06  ? 233 PRO A C     1 
ATOM   1883 O  O     . PRO A 1 234 ? 22.104  -21.976 10.224  1.00 38.00  ? 233 PRO A O     1 
ATOM   1884 C  CB    . PRO A 1 234 ? 22.567  -22.828 13.372  1.00 45.89  ? 233 PRO A CB    1 
ATOM   1885 C  CG    . PRO A 1 234 ? 22.198  -21.792 14.386  1.00 39.62  ? 233 PRO A CG    1 
ATOM   1886 C  CD    . PRO A 1 234 ? 22.165  -20.476 13.703  1.00 37.51  ? 233 PRO A CD    1 
ATOM   1887 N  N     . GLU A 1 235 ? 23.613  -23.643 10.440  1.00 33.11  ? 234 GLU A N     1 
ATOM   1888 C  CA    . GLU A 1 235 ? 23.166  -24.335 9.233   1.00 38.46  ? 234 GLU A CA    1 
ATOM   1889 C  C     . GLU A 1 235 ? 21.677  -24.624 9.333   1.00 37.97  ? 234 GLU A C     1 
ATOM   1890 O  O     . GLU A 1 235 ? 21.185  -25.018 10.388  1.00 35.06  ? 234 GLU A O     1 
ATOM   1891 C  CB    . GLU A 1 235 ? 23.904  -25.667 9.027   1.00 40.28  ? 234 GLU A CB    1 
ATOM   1892 C  CG    . GLU A 1 235 ? 25.392  -25.581 8.773   1.00 49.45  ? 234 GLU A CG    1 
ATOM   1893 C  CD    . GLU A 1 235 ? 26.008  -26.959 8.588   1.00 62.31  ? 234 GLU A CD    1 
ATOM   1894 O  OE1   . GLU A 1 235 ? 25.259  -27.896 8.223   1.00 69.64  ? 234 GLU A OE1   1 
ATOM   1895 O  OE2   . GLU A 1 235 ? 27.234  -27.102 8.797   1.00 75.01  ? 234 GLU A OE2   1 
ATOM   1896 N  N     . GLY A 1 236 ? 20.968  -24.437 8.223   1.00 38.44  ? 235 GLY A N     1 
ATOM   1897 C  CA    . GLY A 1 236 ? 19.539  -24.668 8.186   1.00 42.38  ? 235 GLY A CA    1 
ATOM   1898 C  C     . GLY A 1 236 ? 18.690  -23.684 8.968   1.00 40.39  ? 235 GLY A C     1 
ATOM   1899 O  O     . GLY A 1 236 ? 17.483  -23.867 9.033   1.00 42.67  ? 235 GLY A O     1 
ATOM   1900 N  N     . SER A 1 237 ? 19.264  -22.656 9.570   1.00 40.05  ? 236 SER A N     1 
ATOM   1901 C  CA    . SER A 1 237 ? 18.432  -21.679 10.261  1.00 35.57  ? 236 SER A CA    1 
ATOM   1902 C  C     . SER A 1 237 ? 17.575  -20.899 9.268   1.00 35.30  ? 236 SER A C     1 
ATOM   1903 O  O     . SER A 1 237 ? 18.077  -20.443 8.232   1.00 33.74  ? 236 SER A O     1 
ATOM   1904 C  CB    . SER A 1 237 ? 19.275  -20.689 11.050  1.00 39.01  ? 236 SER A CB    1 
ATOM   1905 O  OG    . SER A 1 237 ? 18.425  -19.738 11.681  1.00 36.59  ? 236 SER A OG    1 
ATOM   1906 N  N     . PRO A 1 238 ? 16.300  -20.662 9.592   1.00 34.84  ? 237 PRO A N     1 
ATOM   1907 C  CA    . PRO A 1 238 ? 15.490  -19.764 8.754   1.00 31.92  ? 237 PRO A CA    1 
ATOM   1908 C  C     . PRO A 1 238 ? 16.013  -18.348 8.736   1.00 26.88  ? 237 PRO A C     1 
ATOM   1909 O  O     . PRO A 1 238 ? 15.710  -17.606 7.798   1.00 29.02  ? 237 PRO A O     1 
ATOM   1910 C  CB    . PRO A 1 238 ? 14.089  -19.827 9.403   1.00 34.82  ? 237 PRO A CB    1 
ATOM   1911 C  CG    . PRO A 1 238 ? 14.119  -21.028 10.331  1.00 42.13  ? 237 PRO A CG    1 
ATOM   1912 C  CD    . PRO A 1 238 ? 15.562  -21.159 10.767  1.00 33.71  ? 237 PRO A CD    1 
ATOM   1913 N  N     . LEU A 1 239 ? 16.752  -17.931 9.764   1.00 28.79  ? 238 LEU A N     1 
ATOM   1914 C  CA    . LEU A 1 239 ? 17.320  -16.583 9.776   1.00 32.47  ? 238 LEU A CA    1 
ATOM   1915 C  C     . LEU A 1 239 ? 18.225  -16.318 8.577   1.00 37.00  ? 238 LEU A C     1 
ATOM   1916 O  O     . LEU A 1 239 ? 18.406  -15.156 8.189   1.00 36.86  ? 238 LEU A O     1 
ATOM   1917 C  CB    . LEU A 1 239 ? 18.104  -16.357 11.065  1.00 29.62  ? 238 LEU A CB    1 
ATOM   1918 C  CG    . LEU A 1 239 ? 17.308  -16.323 12.370  1.00 39.25  ? 238 LEU A CG    1 
ATOM   1919 C  CD1   . LEU A 1 239 ? 18.269  -16.141 13.534  1.00 38.61  ? 238 LEU A CD1   1 
ATOM   1920 C  CD2   . LEU A 1 239 ? 16.319  -15.181 12.294  1.00 34.38  ? 238 LEU A CD2   1 
ATOM   1921 N  N     . ARG A 1 240 ? 18.788  -17.365 7.973   1.00 32.83  ? 239 ARG A N     1 
ATOM   1922 C  CA    . ARG A 1 240 ? 19.653  -17.178 6.810   1.00 33.21  ? 239 ARG A CA    1 
ATOM   1923 C  C     . ARG A 1 240 ? 18.926  -16.510 5.646   1.00 30.98  ? 239 ARG A C     1 
ATOM   1924 O  O     . ARG A 1 240 ? 19.577  -15.881 4.803   1.00 32.53  ? 239 ARG A O     1 
ATOM   1925 C  CB    . ARG A 1 240 ? 20.240  -18.532 6.372   1.00 35.57  ? 239 ARG A CB    1 
ATOM   1926 C  CG    . ARG A 1 240 ? 21.097  -18.520 5.087   1.00 29.94  ? 239 ARG A CG    1 
ATOM   1927 C  CD    . ARG A 1 240 ? 22.211  -19.552 5.161   1.00 30.99  ? 239 ARG A CD    1 
ATOM   1928 N  NE    . ARG A 1 240 ? 23.181  -19.152 6.165   1.00 28.90  ? 239 ARG A NE    1 
ATOM   1929 C  CZ    . ARG A 1 240 ? 23.289  -19.697 7.365   1.00 35.30  ? 239 ARG A CZ    1 
ATOM   1930 N  NH1   . ARG A 1 240 ? 22.671  -20.829 7.671   1.00 30.67  ? 239 ARG A NH1   1 
ATOM   1931 N  NH2   . ARG A 1 240 ? 24.019  -19.081 8.287   1.00 30.00  ? 239 ARG A NH2   1 
ATOM   1932 N  N     . VAL A 1 241 ? 17.597  -16.605 5.567   1.00 28.20  ? 240 VAL A N     1 
ATOM   1933 C  CA    . VAL A 1 241 ? 16.955  -15.958 4.431   1.00 31.20  ? 240 VAL A CA    1 
ATOM   1934 C  C     . VAL A 1 241 ? 16.052  -14.833 4.934   1.00 37.10  ? 240 VAL A C     1 
ATOM   1935 O  O     . VAL A 1 241 ? 15.024  -14.521 4.313   1.00 35.77  ? 240 VAL A O     1 
ATOM   1936 C  CB    . VAL A 1 241 ? 16.181  -16.956 3.534   1.00 34.26  ? 240 VAL A CB    1 
ATOM   1937 C  CG1   . VAL A 1 241 ? 17.171  -17.799 2.647   1.00 33.75  ? 240 VAL A CG1   1 
ATOM   1938 C  CG2   . VAL A 1 241 ? 15.233  -17.838 4.346   1.00 36.69  ? 240 VAL A CG2   1 
ATOM   1939 N  N     . LEU A 1 242 ? 16.455  -14.193 6.037   1.00 32.06  ? 241 LEU A N     1 
ATOM   1940 C  CA    . LEU A 1 242 ? 15.780  -13.001 6.545   1.00 34.89  ? 241 LEU A CA    1 
ATOM   1941 C  C     . LEU A 1 242 ? 16.395  -11.766 5.900   1.00 30.47  ? 241 LEU A C     1 
ATOM   1942 O  O     . LEU A 1 242 ? 17.516  -11.376 6.228   1.00 30.75  ? 241 LEU A O     1 
ATOM   1943 C  CB    . LEU A 1 242 ? 15.883  -12.920 8.066   1.00 34.01  ? 241 LEU A CB    1 
ATOM   1944 C  CG    . LEU A 1 242 ? 15.347  -11.617 8.665   1.00 32.65  ? 241 LEU A CG    1 
ATOM   1945 C  CD1   . LEU A 1 242 ? 13.831  -11.424 8.334   1.00 28.83  ? 241 LEU A CD1   1 
ATOM   1946 C  CD2   . LEU A 1 242 ? 15.596  -11.601 10.153  1.00 31.74  ? 241 LEU A CD2   1 
ATOM   1947 N  N     . TYR A 1 243 ? 15.657  -11.155 4.984   1.00 31.51  ? 242 TYR A N     1 
ATOM   1948 C  CA    . TYR A 1 243 ? 16.032  -9.925  4.310   1.00 29.23  ? 242 TYR A CA    1 
ATOM   1949 C  C     . TYR A 1 243 ? 15.015  -8.826  4.578   1.00 33.07  ? 242 TYR A C     1 
ATOM   1950 O  O     . TYR A 1 243 ? 13.815  -9.080  4.739   1.00 29.85  ? 242 TYR A O     1 
ATOM   1951 C  CB    . TYR A 1 243 ? 16.140  -10.109 2.785   1.00 28.24  ? 242 TYR A CB    1 
ATOM   1952 C  CG    . TYR A 1 243 ? 17.194  -11.107 2.357   1.00 36.04  ? 242 TYR A CG    1 
ATOM   1953 C  CD1   . TYR A 1 243 ? 16.916  -12.466 2.309   1.00 34.47  ? 242 TYR A CD1   1 
ATOM   1954 C  CD2   . TYR A 1 243 ? 18.492  -10.682 2.040   1.00 29.31  ? 242 TYR A CD2   1 
ATOM   1955 C  CE1   . TYR A 1 243 ? 17.885  -13.378 1.912   1.00 32.54  ? 242 TYR A CE1   1 
ATOM   1956 C  CE2   . TYR A 1 243 ? 19.472  -11.594 1.637   1.00 31.54  ? 242 TYR A CE2   1 
ATOM   1957 C  CZ    . TYR A 1 243 ? 19.154  -12.939 1.581   1.00 37.07  ? 242 TYR A CZ    1 
ATOM   1958 O  OH    . TYR A 1 243 ? 20.102  -13.857 1.202   1.00 40.15  ? 242 TYR A OH    1 
ATOM   1959 N  N     . SER A 1 244 ? 15.497  -7.597  4.560   1.00 30.92  ? 243 SER A N     1 
ATOM   1960 C  CA    . SER A 1 244 ? 14.640  -6.446  4.785   1.00 35.66  ? 243 SER A CA    1 
ATOM   1961 C  C     . SER A 1 244 ? 14.772  -5.440  3.659   1.00 37.64  ? 243 SER A C     1 
ATOM   1962 O  O     . SER A 1 244 ? 15.840  -5.295  3.063   1.00 33.50  ? 243 SER A O     1 
ATOM   1963 C  CB    . SER A 1 244 ? 14.986  -5.766  6.095   1.00 37.21  ? 243 SER A CB    1 
ATOM   1964 O  OG    . SER A 1 244 ? 14.041  -4.788  6.422   1.00 38.38  ? 243 SER A OG    1 
ATOM   1965 N  N     . GLY A 1 245 ? 13.676  -4.756  3.367   1.00 29.28  ? 244 GLY A N     1 
ATOM   1966 C  CA    . GLY A 1 245 ? 13.700  -3.535  2.584   1.00 29.93  ? 244 GLY A CA    1 
ATOM   1967 C  C     . GLY A 1 245 ? 13.391  -2.381  3.518   1.00 32.98  ? 244 GLY A C     1 
ATOM   1968 O  O     . GLY A 1 245 ? 12.617  -2.534  4.462   1.00 34.65  ? 244 GLY A O     1 
ATOM   1969 N  N     . ILE A 1 246 ? 13.997  -1.222  3.269   1.00 28.73  ? 245 ILE A N     1 
ATOM   1970 C  CA    . ILE A 1 246 ? 13.813  -0.052  4.124   1.00 29.39  ? 245 ILE A CA    1 
ATOM   1971 C  C     . ILE A 1 246 ? 13.541  1.163   3.258   1.00 31.98  ? 245 ILE A C     1 
ATOM   1972 O  O     . ILE A 1 246 ? 14.277  1.420   2.300   1.00 30.41  ? 245 ILE A O     1 
ATOM   1973 C  CB    . ILE A 1 246 ? 15.049  0.211   4.995   1.00 27.64  ? 245 ILE A CB    1 
ATOM   1974 C  CG1   . ILE A 1 246 ? 15.443  -1.029  5.791   1.00 28.22  ? 245 ILE A CG1   1 
ATOM   1975 C  CG2   . ILE A 1 246 ? 14.854  1.468   5.863   1.00 25.91  ? 245 ILE A CG2   1 
ATOM   1976 C  CD1   . ILE A 1 246 ? 16.672  -0.758  6.684   1.00 31.61  ? 245 ILE A CD1   1 
ATOM   1977 N  N     . GLY A 1 247 ? 12.507  1.918   3.597   1.00 27.50  ? 246 GLY A N     1 
ATOM   1978 C  CA    . GLY A 1 247 ? 12.212  3.167   2.912   1.00 28.16  ? 246 GLY A CA    1 
ATOM   1979 C  C     . GLY A 1 247 ? 12.185  4.306   3.910   1.00 29.75  ? 246 GLY A C     1 
ATOM   1980 O  O     . GLY A 1 247 ? 11.730  4.131   5.044   1.00 29.94  ? 246 GLY A O     1 
ATOM   1981 N  N     . LEU A 1 248 ? 12.673  5.468   3.487   1.00 29.66  ? 247 LEU A N     1 
ATOM   1982 C  CA    . LEU A 1 248 ? 12.601  6.659   4.326   1.00 30.57  ? 247 LEU A CA    1 
ATOM   1983 C  C     . LEU A 1 248 ? 11.924  7.758   3.533   1.00 30.54  ? 247 LEU A C     1 
ATOM   1984 O  O     . LEU A 1 248 ? 12.191  7.928   2.340   1.00 29.28  ? 247 LEU A O     1 
ATOM   1985 C  CB    . LEU A 1 248 ? 13.988  7.158   4.779   1.00 29.24  ? 247 LEU A CB    1 
ATOM   1986 C  CG    . LEU A 1 248 ? 15.040  6.142   5.225   1.00 33.97  ? 247 LEU A CG    1 
ATOM   1987 C  CD1   . LEU A 1 248 ? 16.393  6.876   5.464   1.00 25.69  ? 247 LEU A CD1   1 
ATOM   1988 C  CD2   . LEU A 1 248 ? 14.557  5.437   6.470   1.00 30.43  ? 247 LEU A CD2   1 
ATOM   1989 N  N     . ALA A 1 249 ? 11.040  8.494   4.197   1.00 28.27  ? 248 ALA A N     1 
ATOM   1990 C  CA    . ALA A 1 249 ? 10.447  9.681   3.612   1.00 31.97  ? 248 ALA A CA    1 
ATOM   1991 C  C     . ALA A 1 249 ? 10.313  10.724  4.705   1.00 33.42  ? 248 ALA A C     1 
ATOM   1992 O  O     . ALA A 1 249 ? 10.484  10.432  5.892   1.00 38.54  ? 248 ALA A O     1 
ATOM   1993 C  CB    . ALA A 1 249 ? 9.082   9.371   2.964   1.00 31.29  ? 248 ALA A CB    1 
ATOM   1994 N  N     . LYS A 1 250 ? 9.982   11.943  4.302   1.00 30.59  ? 249 LYS A N     1 
ATOM   1995 C  CA    . LYS A 1 250 ? 9.610   12.985  5.244   1.00 36.53  ? 249 LYS A CA    1 
ATOM   1996 C  C     . LYS A 1 250 ? 8.097   13.110  5.275   1.00 49.58  ? 249 LYS A C     1 
ATOM   1997 O  O     . LYS A 1 250 ? 7.433   13.033  4.237   1.00 41.75  ? 249 LYS A O     1 
ATOM   1998 C  CB    . LYS A 1 250 ? 10.222  14.327  4.854   1.00 45.66  ? 249 LYS A CB    1 
ATOM   1999 C  CG    . LYS A 1 250 ? 11.698  14.350  4.978   1.00 45.53  ? 249 LYS A CG    1 
ATOM   2000 C  CD    . LYS A 1 250 ? 12.253  15.758  5.053   1.00 53.52  ? 249 LYS A CD    1 
ATOM   2001 C  CE    . LYS A 1 250 ? 11.920  16.496  6.309   1.00 54.05  ? 249 LYS A CE    1 
ATOM   2002 N  NZ    . LYS A 1 250 ? 12.917  17.615  6.418   1.00 42.12  ? 249 LYS A NZ    1 
ATOM   2003 N  N     . GLY A 1 251 ? 7.552   13.300  6.471   1.00 44.97  ? 250 GLY A N     1 
ATOM   2004 C  CA    . GLY A 1 251 ? 6.131   13.519  6.615   1.00 45.98  ? 250 GLY A CA    1 
ATOM   2005 C  C     . GLY A 1 251 ? 5.889   14.539  7.708   1.00 46.40  ? 250 GLY A C     1 
ATOM   2006 O  O     . GLY A 1 251 ? 6.736   14.765  8.572   1.00 39.12  ? 250 GLY A O     1 
ATOM   2007 N  N     . LYS A 1 252 ? 4.729   15.176  7.644   1.00 43.83  ? 251 LYS A N     1 
ATOM   2008 C  CA    . LYS A 1 252 ? 4.253   15.967  8.763   1.00 43.81  ? 251 LYS A CA    1 
ATOM   2009 C  C     . LYS A 1 252 ? 3.350   15.051  9.573   1.00 38.55  ? 251 LYS A C     1 
ATOM   2010 O  O     . LYS A 1 252 ? 2.344   14.553  9.053   1.00 44.76  ? 251 LYS A O     1 
ATOM   2011 C  CB    . LYS A 1 252 ? 3.521   17.219  8.289   1.00 49.40  ? 251 LYS A CB    1 
ATOM   2012 C  CG    . LYS A 1 252 ? 4.457   18.416  8.000   1.00 55.79  ? 251 LYS A CG    1 
ATOM   2013 C  CD    . LYS A 1 252 ? 3.986   19.700  8.698   1.00 59.68  ? 251 LYS A CD    1 
ATOM   2014 C  CE    . LYS A 1 252 ? 4.224   20.928  7.823   1.00 67.50  ? 251 LYS A CE    1 
ATOM   2015 N  NZ    . LYS A 1 252 ? 3.130   21.953  7.928   1.00 63.21  ? 251 LYS A NZ    1 
ATOM   2016 N  N     . VAL A 1 253 ? 3.739   14.769  10.807  1.00 35.18  ? 252 VAL A N     1 
ATOM   2017 C  CA    . VAL A 1 253 ? 2.953   13.899  11.665  1.00 35.16  ? 252 VAL A CA    1 
ATOM   2018 C  C     . VAL A 1 253 ? 2.204   14.763  12.671  1.00 43.77  ? 252 VAL A C     1 
ATOM   2019 O  O     . VAL A 1 253 ? 2.584   15.899  12.965  1.00 42.89  ? 252 VAL A O     1 
ATOM   2020 C  CB    . VAL A 1 253 ? 3.819   12.823  12.361  1.00 39.46  ? 252 VAL A CB    1 
ATOM   2021 C  CG1   . VAL A 1 253 ? 5.066   12.528  11.523  1.00 39.61  ? 252 VAL A CG1   1 
ATOM   2022 C  CG2   . VAL A 1 253 ? 4.165   13.227  13.755  1.00 39.43  ? 252 VAL A CG2   1 
ATOM   2023 N  N     . ILE A 1 254 ? 1.093   14.238  13.177  1.00 37.64  ? 253 ILE A N     1 
ATOM   2024 C  CA    . ILE A 1 254 ? 0.295   14.940  14.176  1.00 42.39  ? 253 ILE A CA    1 
ATOM   2025 C  C     . ILE A 1 254 ? 0.546   14.286  15.519  1.00 44.20  ? 253 ILE A C     1 
ATOM   2026 O  O     . ILE A 1 254 ? 0.417   13.063  15.659  1.00 49.74  ? 253 ILE A O     1 
ATOM   2027 C  CB    . ILE A 1 254 ? -1.207  14.923  13.837  1.00 44.90  ? 253 ILE A CB    1 
ATOM   2028 C  CG1   . ILE A 1 254 ? -1.424  15.443  12.424  1.00 48.51  ? 253 ILE A CG1   1 
ATOM   2029 C  CG2   . ILE A 1 254 ? -1.965  15.770  14.829  1.00 48.79  ? 253 ILE A CG2   1 
ATOM   2030 C  CD1   . ILE A 1 254 ? -1.743  16.881  12.339  1.00 53.72  ? 253 ILE A CD1   1 
ATOM   2031 N  N     . GLU A 1 255 ? 0.929   15.095  16.497  1.00 45.75  ? 254 GLU A N     1 
ATOM   2032 C  CA    . GLU A 1 255 ? 1.121   14.646  17.862  1.00 42.83  ? 254 GLU A CA    1 
ATOM   2033 C  C     . GLU A 1 255 ? -0.070  15.135  18.680  1.00 50.89  ? 254 GLU A C     1 
ATOM   2034 O  O     . GLU A 1 255 ? -0.536  16.261  18.490  1.00 47.28  ? 254 GLU A O     1 
ATOM   2035 C  CB    . GLU A 1 255 ? 2.455   15.181  18.390  1.00 49.58  ? 254 GLU A CB    1 
ATOM   2036 C  CG    . GLU A 1 255 ? 3.664   14.524  17.687  1.00 49.33  ? 254 GLU A CG    1 
ATOM   2037 C  CD    . GLU A 1 255 ? 5.027   14.837  18.336  1.00 59.27  ? 254 GLU A CD    1 
ATOM   2038 O  OE1   . GLU A 1 255 ? 5.107   15.769  19.171  1.00 54.46  ? 254 GLU A OE1   1 
ATOM   2039 O  OE2   . GLU A 1 255 ? 6.017   14.146  18.001  1.00 53.21  ? 254 GLU A OE2   1 
ATOM   2040 N  N     . GLY A 1 256 ? -0.615  14.275  19.525  1.00 47.70  ? 255 GLY A N     1 
ATOM   2041 C  CA    . GLY A 1 256 ? -1.735  14.678  20.355  1.00 50.47  ? 255 GLY A CA    1 
ATOM   2042 C  C     . GLY A 1 256 ? -2.458  13.483  20.934  1.00 44.51  ? 255 GLY A C     1 
ATOM   2043 O  O     . GLY A 1 256 ? -2.059  12.332  20.752  1.00 47.51  ? 255 GLY A O     1 
ATOM   2044 N  N     . ASN A 1 257 ? -3.548  13.788  21.636  1.00 48.46  ? 256 ASN A N     1 
ATOM   2045 C  CA    . ASN A 1 257 ? -4.388  12.776  22.283  1.00 45.50  ? 256 ASN A CA    1 
ATOM   2046 C  C     . ASN A 1 257 ? -5.364  12.270  21.226  1.00 50.29  ? 256 ASN A C     1 
ATOM   2047 O  O     . ASN A 1 257 ? -6.387  12.904  20.949  1.00 44.48  ? 256 ASN A O     1 
ATOM   2048 C  CB    . ASN A 1 257 ? -5.084  13.376  23.506  1.00 52.78  ? 256 ASN A CB    1 
ATOM   2049 C  CG    . ASN A 1 257 ? -5.857  12.342  24.339  1.00 59.69  ? 256 ASN A CG    1 
ATOM   2050 O  OD1   . ASN A 1 257 ? -5.344  11.278  24.683  1.00 59.26  ? 256 ASN A OD1   1 
ATOM   2051 N  ND2   . ASN A 1 257 ? -7.087  12.688  24.704  1.00 55.33  ? 256 ASN A ND2   1 
ATOM   2052 N  N     . ILE A 1 258 ? -5.045  11.119  20.639  1.00 42.50  ? 257 ILE A N     1 
ATOM   2053 C  CA    . ILE A 1 258 ? -5.623  10.685  19.376  1.00 46.00  ? 257 ILE A CA    1 
ATOM   2054 C  C     . ILE A 1 258 ? -6.277  9.327   19.577  1.00 47.30  ? 257 ILE A C     1 
ATOM   2055 O  O     . ILE A 1 258 ? -5.695  8.446   20.215  1.00 42.88  ? 257 ILE A O     1 
ATOM   2056 C  CB    . ILE A 1 258 ? -4.521  10.605  18.305  1.00 50.72  ? 257 ILE A CB    1 
ATOM   2057 C  CG1   . ILE A 1 258 ? -4.219  12.002  17.785  1.00 46.32  ? 257 ILE A CG1   1 
ATOM   2058 C  CG2   . ILE A 1 258 ? -4.986  9.742   17.147  1.00 41.92  ? 257 ILE A CG2   1 
ATOM   2059 C  CD1   . ILE A 1 258 ? -3.030  12.044  16.899  1.00 51.45  ? 257 ILE A CD1   1 
ATOM   2060 N  N     . GLY A 1 259 ? -7.479  9.147   19.022  1.00 42.44  ? 258 GLY A N     1 
ATOM   2061 C  CA    . GLY A 1 259 ? -8.110  7.840   19.092  1.00 43.97  ? 258 GLY A CA    1 
ATOM   2062 C  C     . GLY A 1 259 ? -9.512  7.841   19.659  1.00 47.15  ? 258 GLY A C     1 
ATOM   2063 O  O     . GLY A 1 259 ? -10.264 8.803   19.447  1.00 44.89  ? 258 GLY A O     1 
ATOM   2064 N  N     . SER A 1 260 ? -9.882  6.795   20.414  1.00 44.22  ? 259 SER A N     1 
ATOM   2065 C  CA    . SER A 1 260 ? -11.292 6.510   20.670  1.00 51.46  ? 259 SER A CA    1 
ATOM   2066 C  C     . SER A 1 260 ? -11.616 6.227   22.132  1.00 59.09  ? 259 SER A C     1 
ATOM   2067 O  O     . SER A 1 260 ? -12.533 5.449   22.403  1.00 66.54  ? 259 SER A O     1 
ATOM   2068 C  CB    . SER A 1 260 ? -11.741 5.305   19.855  1.00 53.63  ? 259 SER A CB    1 
ATOM   2069 O  OG    . SER A 1 260 ? -11.018 4.157   20.271  1.00 52.87  ? 259 SER A OG    1 
ATOM   2070 N  N     . GLU A 1 261 ? -10.893 6.798   23.092  1.00 56.89  ? 260 GLU A N     1 
ATOM   2071 C  CA    . GLU A 1 261 ? -11.160 6.476   24.503  1.00 69.35  ? 260 GLU A CA    1 
ATOM   2072 C  C     . GLU A 1 261 ? -11.018 4.990   24.823  1.00 66.49  ? 260 GLU A C     1 
ATOM   2073 O  O     . GLU A 1 261 ? -10.407 4.626   25.836  1.00 71.87  ? 260 GLU A O     1 
ATOM   2074 C  CB    . GLU A 1 261 ? -12.555 6.918   24.949  1.00 72.91  ? 260 GLU A CB    1 
ATOM   2075 C  CG    . GLU A 1 261 ? -12.601 7.351   26.414  1.00 85.55  ? 260 GLU A CG    1 
ATOM   2076 C  CD    . GLU A 1 261 ? -13.788 8.241   26.741  1.00 97.68  ? 260 GLU A CD    1 
ATOM   2077 O  OE1   . GLU A 1 261 ? -14.841 8.104   26.076  1.00 90.54  ? 260 GLU A OE1   1 
ATOM   2078 O  OE2   . GLU A 1 261 ? -13.666 9.073   27.670  1.00 100.99 ? 260 GLU A OE2   1 
ATOM   2079 N  N     . LEU A 1 262 ? -11.616 4.125   24.001  1.00 55.41  ? 261 LEU A N     1 
ATOM   2080 C  CA    . LEU A 1 262 ? -11.245 2.714   24.016  1.00 64.75  ? 261 LEU A CA    1 
ATOM   2081 C  C     . LEU A 1 262 ? -9.755  2.540   23.733  1.00 60.98  ? 261 LEU A C     1 
ATOM   2082 O  O     . LEU A 1 262 ? -9.026  1.910   24.509  1.00 65.23  ? 261 LEU A O     1 
ATOM   2083 C  CB    . LEU A 1 262 ? -12.084 1.943   22.996  1.00 63.78  ? 261 LEU A CB    1 
ATOM   2084 C  CG    . LEU A 1 262 ? -13.581 1.886   23.312  1.00 70.70  ? 261 LEU A CG    1 
ATOM   2085 C  CD1   . LEU A 1 262 ? -14.440 2.239   22.097  1.00 62.93  ? 261 LEU A CD1   1 
ATOM   2086 C  CD2   . LEU A 1 262 ? -13.961 0.521   23.885  1.00 67.13  ? 261 LEU A CD2   1 
ATOM   2087 N  N     . LYS A 1 263 ? -9.281  3.113   22.628  1.00 53.34  ? 262 LYS A N     1 
ATOM   2088 C  CA    . LYS A 1 263 ? -7.897  2.995   22.199  1.00 44.61  ? 262 LYS A CA    1 
ATOM   2089 C  C     . LYS A 1 263 ? -7.365  4.379   21.868  1.00 46.26  ? 262 LYS A C     1 
ATOM   2090 O  O     . LYS A 1 263 ? -8.005  5.136   21.130  1.00 41.65  ? 262 LYS A O     1 
ATOM   2091 C  CB    . LYS A 1 263 ? -7.775  2.071   20.984  1.00 52.70  ? 262 LYS A CB    1 
ATOM   2092 C  CG    . LYS A 1 263 ? -6.370  1.966   20.391  1.00 55.62  ? 262 LYS A CG    1 
ATOM   2093 C  CD    . LYS A 1 263 ? -5.588  0.780   20.928  1.00 67.41  ? 262 LYS A CD    1 
ATOM   2094 C  CE    . LYS A 1 263 ? -4.105  0.801   20.506  1.00 66.32  ? 262 LYS A CE    1 
ATOM   2095 N  NZ    . LYS A 1 263 ? -3.347  2.056   20.803  1.00 59.12  ? 262 LYS A NZ    1 
ATOM   2096 N  N     . ARG A 1 264 ? -6.204  4.709   22.420  1.00 44.12  ? 263 ARG A N     1 
ATOM   2097 C  CA    . ARG A 1 264 ? -5.569  5.996   22.209  1.00 42.76  ? 263 ARG A CA    1 
ATOM   2098 C  C     . ARG A 1 264 ? -4.206  5.773   21.572  1.00 43.08  ? 263 ARG A C     1 
ATOM   2099 O  O     . ARG A 1 264 ? -3.639  4.679   21.641  1.00 41.93  ? 263 ARG A O     1 
ATOM   2100 C  CB    . ARG A 1 264 ? -5.413  6.774   23.523  1.00 45.67  ? 263 ARG A CB    1 
ATOM   2101 C  CG    . ARG A 1 264 ? -6.714  7.396   24.043  1.00 47.24  ? 263 ARG A CG    1 
ATOM   2102 C  CD    . ARG A 1 264 ? -7.157  8.584   23.215  1.00 55.26  ? 263 ARG A CD    1 
ATOM   2103 N  NE    . ARG A 1 264 ? -8.382  9.199   23.715  1.00 56.32  ? 263 ARG A NE    1 
ATOM   2104 C  CZ    . ARG A 1 264 ? -9.063  10.133  23.057  1.00 59.61  ? 263 ARG A CZ    1 
ATOM   2105 N  NH1   . ARG A 1 264 ? -8.642  10.606  21.894  1.00 55.21  ? 263 ARG A NH1   1 
ATOM   2106 N  NH2   . ARG A 1 264 ? -10.189 10.609  23.582  1.00 61.39  ? 263 ARG A NH2   1 
ATOM   2107 N  N     . ASP A 1 265 ? -3.693  6.840   20.966  1.00 43.94  ? 264 ASP A N     1 
ATOM   2108 C  CA    . ASP A 1 265 ? -2.415  6.859   20.272  1.00 45.30  ? 264 ASP A CA    1 
ATOM   2109 C  C     . ASP A 1 265 ? -1.834  8.248   20.486  1.00 41.06  ? 264 ASP A C     1 
ATOM   2110 O  O     . ASP A 1 265 ? -2.576  9.205   20.721  1.00 47.91  ? 264 ASP A O     1 
ATOM   2111 C  CB    . ASP A 1 265 ? -2.611  6.559   18.775  1.00 47.70  ? 264 ASP A CB    1 
ATOM   2112 C  CG    . ASP A 1 265 ? -1.515  5.675   18.186  1.00 66.92  ? 264 ASP A CG    1 
ATOM   2113 O  OD1   . ASP A 1 265 ? -1.835  4.887   17.252  1.00 62.03  ? 264 ASP A OD1   1 
ATOM   2114 O  OD2   . ASP A 1 265 ? -0.344  5.775   18.631  1.00 60.57  ? 264 ASP A OD2   1 
ATOM   2115 N  N     . TYR A 1 266 ? -0.513  8.363   20.420  1.00 45.55  ? 265 TYR A N     1 
ATOM   2116 C  CA    . TYR A 1 266 ? 0.131   9.663   20.597  1.00 41.84  ? 265 TYR A CA    1 
ATOM   2117 C  C     . TYR A 1 266 ? 0.396   10.391  19.274  1.00 42.74  ? 265 TYR A C     1 
ATOM   2118 O  O     . TYR A 1 266 ? 0.541   11.619  19.264  1.00 40.91  ? 265 TYR A O     1 
ATOM   2119 C  CB    . TYR A 1 266 ? 1.436   9.479   21.387  1.00 47.69  ? 265 TYR A CB    1 
ATOM   2120 C  CG    . TYR A 1 266 ? 2.301   10.720  21.430  1.00 56.72  ? 265 TYR A CG    1 
ATOM   2121 C  CD1   . TYR A 1 266 ? 1.797   11.938  21.885  1.00 57.05  ? 265 TYR A CD1   1 
ATOM   2122 C  CD2   . TYR A 1 266 ? 3.611   10.688  20.945  1.00 54.06  ? 265 TYR A CD2   1 
ATOM   2123 C  CE1   . TYR A 1 266 ? 2.591   13.083  21.891  1.00 64.37  ? 265 TYR A CE1   1 
ATOM   2124 C  CE2   . TYR A 1 266 ? 4.411   11.822  20.954  1.00 60.05  ? 265 TYR A CE2   1 
ATOM   2125 C  CZ    . TYR A 1 266 ? 3.896   13.017  21.427  1.00 58.98  ? 265 TYR A CZ    1 
ATOM   2126 O  OH    . TYR A 1 266 ? 4.680   14.149  21.433  1.00 70.60  ? 265 TYR A OH    1 
ATOM   2127 N  N     . THR A 1 267 ? 0.429   9.674   18.154  1.00 42.97  ? 266 THR A N     1 
ATOM   2128 C  CA    . THR A 1 267 ? 0.818   10.258  16.876  1.00 43.31  ? 266 THR A CA    1 
ATOM   2129 C  C     . THR A 1 267 ? 0.014   9.618   15.750  1.00 45.56  ? 266 THR A C     1 
ATOM   2130 O  O     . THR A 1 267 ? -0.361  8.443   15.833  1.00 42.91  ? 266 THR A O     1 
ATOM   2131 C  CB    . THR A 1 267 ? 2.321   10.067  16.629  1.00 40.79  ? 266 THR A CB    1 
ATOM   2132 O  OG1   . THR A 1 267 ? 2.697   10.701  15.409  1.00 49.15  ? 266 THR A OG1   1 
ATOM   2133 C  CG2   . THR A 1 267 ? 2.669   8.595   16.562  1.00 39.59  ? 266 THR A CG2   1 
ATOM   2134 N  N     . ILE A 1 268 ? -0.243  10.393  14.691  1.00 42.05  ? 267 ILE A N     1 
ATOM   2135 C  CA    . ILE A 1 268 ? -0.693  9.810   13.429  1.00 46.56  ? 267 ILE A CA    1 
ATOM   2136 C  C     . ILE A 1 268 ? 0.075   10.440  12.275  1.00 40.86  ? 267 ILE A C     1 
ATOM   2137 O  O     . ILE A 1 268 ? 0.217   11.667  12.196  1.00 37.34  ? 267 ILE A O     1 
ATOM   2138 C  CB    . ILE A 1 268 ? -2.202  9.987   13.176  1.00 41.84  ? 267 ILE A CB    1 
ATOM   2139 C  CG1   . ILE A 1 268 ? -2.661  11.373  13.617  1.00 45.62  ? 267 ILE A CG1   1 
ATOM   2140 C  CG2   . ILE A 1 268 ? -2.973  8.897   13.916  1.00 54.94  ? 267 ILE A CG2   1 
ATOM   2141 C  CD1   . ILE A 1 268 ? -4.139  11.580  13.523  1.00 64.91  ? 267 ILE A CD1   1 
ATOM   2142 N  N     . LEU A 1 269 ? 0.538   9.589   11.365  1.00 32.62  ? 268 LEU A N     1 
ATOM   2143 C  CA    . LEU A 1 269 ? 0.940   9.989   10.021  1.00 40.56  ? 268 LEU A CA    1 
ATOM   2144 C  C     . LEU A 1 269 ? -0.196  9.646   9.057   1.00 36.68  ? 268 LEU A C     1 
ATOM   2145 O  O     . LEU A 1 269 ? -0.454  8.468   8.794   1.00 36.51  ? 268 LEU A O     1 
ATOM   2146 C  CB    . LEU A 1 269 ? 2.223   9.272   9.608   1.00 37.09  ? 268 LEU A CB    1 
ATOM   2147 C  CG    . LEU A 1 269 ? 2.663   9.615   8.193   1.00 36.59  ? 268 LEU A CG    1 
ATOM   2148 C  CD1   . LEU A 1 269 ? 3.012   11.100  8.086   1.00 34.26  ? 268 LEU A CD1   1 
ATOM   2149 C  CD2   . LEU A 1 269 ? 3.859   8.748   7.805   1.00 45.20  ? 268 LEU A CD2   1 
ATOM   2150 N  N     . GLY A 1 270 ? -0.869  10.653  8.522   1.00 36.55  ? 269 GLY A N     1 
ATOM   2151 C  CA    . GLY A 1 270 ? -1.931  10.340  7.578   1.00 38.92  ? 269 GLY A CA    1 
ATOM   2152 C  C     . GLY A 1 270 ? -1.399  9.549   6.396   1.00 35.37  ? 269 GLY A C     1 
ATOM   2153 O  O     . GLY A 1 270 ? -0.284  9.810   5.940   1.00 37.04  ? 269 GLY A O     1 
ATOM   2154 N  N     . ASP A 1 271 ? -2.142  8.540   5.936   1.00 37.57  ? 270 ASP A N     1 
ATOM   2155 C  CA    . ASP A 1 271 ? -1.749  7.756   4.757   1.00 40.01  ? 270 ASP A CA    1 
ATOM   2156 C  C     . ASP A 1 271 ? -0.401  7.057   4.944   1.00 35.18  ? 270 ASP A C     1 
ATOM   2157 O  O     . ASP A 1 271 ? 0.305   6.786   3.965   1.00 38.37  ? 270 ASP A O     1 
ATOM   2158 C  CB    . ASP A 1 271 ? -1.714  8.629   3.498   1.00 42.01  ? 270 ASP A CB    1 
ATOM   2159 C  CG    . ASP A 1 271 ? -3.082  9.220   3.155   1.00 50.00  ? 270 ASP A CG    1 
ATOM   2160 O  OD1   . ASP A 1 271 ? -4.106  8.493   3.218   1.00 42.26  ? 270 ASP A OD1   1 
ATOM   2161 O  OD2   . ASP A 1 271 ? -3.126  10.425  2.829   1.00 48.00  ? 270 ASP A OD2   1 
ATOM   2162 N  N     . ALA A 1 272 ? -0.032  6.785   6.208   1.00 33.19  ? 271 ALA A N     1 
ATOM   2163 C  CA    . ALA A 1 272 ? 1.115   5.930   6.511   1.00 32.15  ? 271 ALA A CA    1 
ATOM   2164 C  C     . ALA A 1 272 ? 1.083   4.640   5.701   1.00 34.20  ? 271 ALA A C     1 
ATOM   2165 O  O     . ALA A 1 272 ? 2.122   4.167   5.211   1.00 30.10  ? 271 ALA A O     1 
ATOM   2166 C  CB    . ALA A 1 272 ? 1.127   5.594   8.006   1.00 34.84  ? 271 ALA A CB    1 
ATOM   2167 N  N     . VAL A 1 273 ? -0.106  4.041   5.580   1.00 32.72  ? 272 VAL A N     1 
ATOM   2168 C  CA    . VAL A 1 273 ? -0.251  2.756   4.897   1.00 33.32  ? 272 VAL A CA    1 
ATOM   2169 C  C     . VAL A 1 273 ? 0.198   2.866   3.439   1.00 37.35  ? 272 VAL A C     1 
ATOM   2170 O  O     . VAL A 1 273 ? 0.892   1.980   2.915   1.00 29.99  ? 272 VAL A O     1 
ATOM   2171 C  CB    . VAL A 1 273 ? -1.711  2.273   5.040   1.00 42.59  ? 272 VAL A CB    1 
ATOM   2172 C  CG1   . VAL A 1 273 ? -2.341  1.981   3.700   1.00 37.15  ? 272 VAL A CG1   1 
ATOM   2173 C  CG2   . VAL A 1 273 ? -1.772  1.060   5.953   1.00 42.35  ? 272 VAL A CG2   1 
ATOM   2174 N  N     . ASN A 1 274 ? -0.142  3.982   2.783   1.00 27.18  ? 273 ASN A N     1 
ATOM   2175 C  CA    . ASN A 1 274 ? 0.162   4.172   1.361   1.00 34.78  ? 273 ASN A CA    1 
ATOM   2176 C  C     . ASN A 1 274 ? 1.640   4.490   1.142   1.00 34.60  ? 273 ASN A C     1 
ATOM   2177 O  O     . ASN A 1 274 ? 2.247   4.025   0.167   1.00 38.28  ? 273 ASN A O     1 
ATOM   2178 C  CB    . ASN A 1 274 ? -0.704  5.310   0.833   1.00 31.91  ? 273 ASN A CB    1 
ATOM   2179 C  CG    . ASN A 1 274 ? -2.198  5.093   1.155   1.00 40.33  ? 273 ASN A CG    1 
ATOM   2180 O  OD1   . ASN A 1 274 ? -2.731  5.732   2.077   1.00 39.25  ? 273 ASN A OD1   1 
ATOM   2181 N  ND2   . ASN A 1 274 ? -2.864  4.211   0.410   1.00 40.03  ? 273 ASN A ND2   1 
ATOM   2182 N  N     . VAL A 1 275 ? 2.225   5.323   2.011   1.00 34.13  ? 274 VAL A N     1 
ATOM   2183 C  CA    . VAL A 1 275 ? 3.659   5.590   1.948   1.00 30.78  ? 274 VAL A CA    1 
ATOM   2184 C  C     . VAL A 1 275 ? 4.446   4.303   2.157   1.00 31.52  ? 274 VAL A C     1 
ATOM   2185 O  O     . VAL A 1 275 ? 5.389   4.002   1.408   1.00 29.22  ? 274 VAL A O     1 
ATOM   2186 C  CB    . VAL A 1 275 ? 4.043   6.688   2.962   1.00 39.51  ? 274 VAL A CB    1 
ATOM   2187 C  CG1   . VAL A 1 275 ? 5.549   6.906   2.995   1.00 32.84  ? 274 VAL A CG1   1 
ATOM   2188 C  CG2   . VAL A 1 275 ? 3.362   8.002   2.597   1.00 33.06  ? 274 VAL A CG2   1 
ATOM   2189 N  N     . ALA A 1 276 ? 4.045   3.500   3.148   1.00 29.13  ? 275 ALA A N     1 
ATOM   2190 C  CA    . ALA A 1 276 ? 4.748   2.250   3.422   1.00 30.85  ? 275 ALA A CA    1 
ATOM   2191 C  C     . ALA A 1 276 ? 4.642   1.307   2.233   1.00 31.58  ? 275 ALA A C     1 
ATOM   2192 O  O     . ALA A 1 276 ? 5.642   0.747   1.775   1.00 30.93  ? 275 ALA A O     1 
ATOM   2193 C  CB    . ALA A 1 276 ? 4.178   1.586   4.678   1.00 29.74  ? 275 ALA A CB    1 
ATOM   2194 N  N     . ALA A 1 277 ? 3.427   1.139   1.705   1.00 30.35  ? 276 ALA A N     1 
ATOM   2195 C  CA    . ALA A 1 277 ? 3.231   0.244   0.567   1.00 36.72  ? 276 ALA A CA    1 
ATOM   2196 C  C     . ALA A 1 277 ? 4.036   0.709   -0.644  1.00 32.13  ? 276 ALA A C     1 
ATOM   2197 O  O     . ALA A 1 277 ? 4.627   -0.112  -1.355  1.00 34.33  ? 276 ALA A O     1 
ATOM   2198 C  CB    . ALA A 1 277 ? 1.739   0.153   0.229   1.00 33.04  ? 276 ALA A CB    1 
ATOM   2199 N  N     . ARG A 1 278 ? 4.105   2.025   -0.870  1.00 30.13  ? 277 ARG A N     1 
ATOM   2200 C  CA    . ARG A 1 278 ? 4.870   2.548   -2.004  1.00 32.55  ? 277 ARG A CA    1 
ATOM   2201 C  C     . ARG A 1 278 ? 6.377   2.303   -1.834  1.00 33.93  ? 277 ARG A C     1 
ATOM   2202 O  O     . ARG A 1 278 ? 7.072   1.968   -2.807  1.00 30.61  ? 277 ARG A O     1 
ATOM   2203 C  CB    . ARG A 1 278 ? 4.585   4.040   -2.191  1.00 35.83  ? 277 ARG A CB    1 
ATOM   2204 C  CG    . ARG A 1 278 ? 3.518   4.394   -3.259  1.00 48.35  ? 277 ARG A CG    1 
ATOM   2205 C  CD    . ARG A 1 278 ? 2.540   5.508   -2.824  1.00 48.97  ? 277 ARG A CD    1 
ATOM   2206 N  NE    . ARG A 1 278 ? 1.162   5.319   -3.282  1.00 60.86  ? 277 ARG A NE    1 
ATOM   2207 C  CZ    . ARG A 1 278 ? 0.130   6.058   -2.884  1.00 62.12  ? 277 ARG A CZ    1 
ATOM   2208 N  NH1   . ARG A 1 278 ? 0.286   7.075   -2.048  1.00 58.24  ? 277 ARG A NH1   1 
ATOM   2209 N  NH2   . ARG A 1 278 ? -1.089  5.777   -3.342  1.00 65.24  ? 277 ARG A NH2   1 
ATOM   2210 N  N     . LEU A 1 279 ? 6.903   2.481   -0.617  1.00 27.99  ? 278 LEU A N     1 
ATOM   2211 C  CA    . LEU A 1 279 ? 8.322   2.225   -0.373  1.00 29.02  ? 278 LEU A CA    1 
ATOM   2212 C  C     . LEU A 1 279 ? 8.637   0.738   -0.501  1.00 34.49  ? 278 LEU A C     1 
ATOM   2213 O  O     . LEU A 1 279 ? 9.682   0.354   -1.041  1.00 35.09  ? 278 LEU A O     1 
ATOM   2214 C  CB    . LEU A 1 279 ? 8.714   2.747   1.011   1.00 28.78  ? 278 LEU A CB    1 
ATOM   2215 C  CG    . LEU A 1 279 ? 8.609   4.266   1.237   1.00 31.73  ? 278 LEU A CG    1 
ATOM   2216 C  CD1   . LEU A 1 279 ? 8.785   4.581   2.678   1.00 27.17  ? 278 LEU A CD1   1 
ATOM   2217 C  CD2   . LEU A 1 279 ? 9.705   4.983   0.424   1.00 28.22  ? 278 LEU A CD2   1 
ATOM   2218 N  N     . GLU A 1 280 ? 7.742   -0.106  0.011   1.00 35.37  ? 279 GLU A N     1 
ATOM   2219 C  CA    . GLU A 1 280 ? 7.850   -1.554  -0.141  1.00 43.28  ? 279 GLU A CA    1 
ATOM   2220 C  C     . GLU A 1 280 ? 7.990   -1.900  -1.617  1.00 36.71  ? 279 GLU A C     1 
ATOM   2221 O  O     . GLU A 1 280 ? 8.848   -2.702  -2.011  1.00 38.00  ? 279 GLU A O     1 
ATOM   2222 C  CB    . GLU A 1 280 ? 6.569   -2.187  0.419   1.00 39.43  ? 279 GLU A CB    1 
ATOM   2223 C  CG    . GLU A 1 280 ? 6.373   -2.138  1.936   1.00 50.17  ? 279 GLU A CG    1 
ATOM   2224 C  CD    . GLU A 1 280 ? 5.904   -3.443  2.600   1.00 53.98  ? 279 GLU A CD    1 
ATOM   2225 O  OE1   . GLU A 1 280 ? 5.469   -4.374  1.879   1.00 44.10  ? 279 GLU A OE1   1 
ATOM   2226 O  OE2   . GLU A 1 280 ? 5.854   -3.467  3.858   1.00 41.56  ? 279 GLU A OE2   1 
ATOM   2227 N  N     . ALA A 1 281 ? 7.146   -1.279  -2.446  1.00 31.42  ? 280 ALA A N     1 
ATOM   2228 C  CA    . ALA A 1 281 ? 7.140   -1.574  -3.871  1.00 36.25  ? 280 ALA A CA    1 
ATOM   2229 C  C     . ALA A 1 281 ? 8.425   -1.103  -4.523  1.00 36.35  ? 280 ALA A C     1 
ATOM   2230 O  O     . ALA A 1 281 ? 8.921   -1.743  -5.456  1.00 38.07  ? 280 ALA A O     1 
ATOM   2231 C  CB    . ALA A 1 281 ? 5.930   -0.918  -4.541  1.00 36.60  ? 280 ALA A CB    1 
ATOM   2232 N  N     . LEU A 1 282 ? 8.978   0.018   -4.051  1.00 31.48  ? 281 LEU A N     1 
ATOM   2233 C  CA    . LEU A 1 282 ? 10.217  0.529   -4.625  1.00 32.31  ? 281 LEU A CA    1 
ATOM   2234 C  C     . LEU A 1 282 ? 11.411  -0.357  -4.287  1.00 32.49  ? 281 LEU A C     1 
ATOM   2235 O  O     . LEU A 1 282 ? 12.270  -0.596  -5.141  1.00 34.73  ? 281 LEU A O     1 
ATOM   2236 C  CB    . LEU A 1 282 ? 10.457  1.961   -4.148  1.00 33.34  ? 281 LEU A CB    1 
ATOM   2237 C  CG    . LEU A 1 282 ? 9.665   3.020   -4.877  1.00 37.74  ? 281 LEU A CG    1 
ATOM   2238 C  CD1   . LEU A 1 282 ? 9.740   4.363   -4.150  1.00 37.47  ? 281 LEU A CD1   1 
ATOM   2239 C  CD2   . LEU A 1 282 ? 10.277  3.138   -6.266  1.00 36.97  ? 281 LEU A CD2   1 
ATOM   2240 N  N     . THR A 1 283 ? 11.520  -0.822  -3.046  1.00 35.17  ? 282 THR A N     1 
ATOM   2241 C  CA    . THR A 1 283 ? 12.626  -1.721  -2.729  1.00 34.80  ? 282 THR A CA    1 
ATOM   2242 C  C     . THR A 1 283 ? 12.570  -2.981  -3.591  1.00 43.12  ? 282 THR A C     1 
ATOM   2243 O  O     . THR A 1 283 ? 13.604  -3.438  -4.091  1.00 44.33  ? 282 THR A O     1 
ATOM   2244 C  CB    . THR A 1 283 ? 12.632  -2.069  -1.233  1.00 37.60  ? 282 THR A CB    1 
ATOM   2245 O  OG1   . THR A 1 283 ? 11.421  -2.762  -0.882  1.00 38.39  ? 282 THR A OG1   1 
ATOM   2246 C  CG2   . THR A 1 283 ? 12.806  -0.820  -0.352  1.00 34.76  ? 282 THR A CG2   1 
ATOM   2247 N  N     . ARG A 1 284 ? 11.364  -3.532  -3.799  1.00 36.52  ? 283 ARG A N     1 
ATOM   2248 C  CA    . ARG A 1 284 ? 11.181  -4.685  -4.691  1.00 43.74  ? 283 ARG A CA    1 
ATOM   2249 C  C     . ARG A 1 284 ? 11.566  -4.360  -6.129  1.00 43.19  ? 283 ARG A C     1 
ATOM   2250 O  O     . ARG A 1 284 ? 12.345  -5.081  -6.757  1.00 51.91  ? 283 ARG A O     1 
ATOM   2251 C  CB    . ARG A 1 284 ? 9.723   -5.150  -4.692  1.00 44.30  ? 283 ARG A CB    1 
ATOM   2252 C  CG    . ARG A 1 284 ? 9.279   -6.090  -3.605  1.00 56.31  ? 283 ARG A CG    1 
ATOM   2253 C  CD    . ARG A 1 284 ? 10.086  -5.986  -2.356  1.00 62.55  ? 283 ARG A CD    1 
ATOM   2254 N  NE    . ARG A 1 284 ? 9.355   -6.596  -1.253  1.00 61.41  ? 283 ARG A NE    1 
ATOM   2255 C  CZ    . ARG A 1 284 ? 9.497   -6.242  0.017   1.00 57.88  ? 283 ARG A CZ    1 
ATOM   2256 N  NH1   . ARG A 1 284 ? 10.399  -5.341  0.389   1.00 61.86  ? 283 ARG A NH1   1 
ATOM   2257 N  NH2   . ARG A 1 284 ? 8.723   -6.813  0.937   1.00 51.72  ? 283 ARG A NH2   1 
ATOM   2258 N  N     . GLN A 1 285 ? 10.973  -3.307  -6.682  1.00 39.70  ? 284 GLN A N     1 
ATOM   2259 C  CA    . GLN A 1 285 ? 11.118  -3.006  -8.101  1.00 44.92  ? 284 GLN A CA    1 
ATOM   2260 C  C     . GLN A 1 285 ? 12.555  -2.643  -8.459  1.00 50.07  ? 284 GLN A C     1 
ATOM   2261 O  O     . GLN A 1 285 ? 13.007  -2.937  -9.569  1.00 49.11  ? 284 GLN A O     1 
ATOM   2262 C  CB    . GLN A 1 285 ? 10.177  -1.861  -8.468  1.00 47.00  ? 284 GLN A CB    1 
ATOM   2263 C  CG    . GLN A 1 285 ? 10.711  -0.901  -9.523  1.00 55.41  ? 284 GLN A CG    1 
ATOM   2264 C  CD    . GLN A 1 285 ? 9.887   0.372   -9.615  1.00 59.67  ? 284 GLN A CD    1 
ATOM   2265 O  OE1   . GLN A 1 285 ? 8.678   0.364   -9.375  1.00 66.89  ? 284 GLN A OE1   1 
ATOM   2266 N  NE2   . GLN A 1 285 ? 10.538  1.474   -10.000 1.00 63.11  ? 284 GLN A NE2   1 
ATOM   2267 N  N     . LEU A 1 286 ? 13.280  -2.005  -7.532  1.00 42.65  ? 285 LEU A N     1 
ATOM   2268 C  CA    . LEU A 1 286 ? 14.635  -1.506  -7.742  1.00 40.96  ? 285 LEU A CA    1 
ATOM   2269 C  C     . LEU A 1 286 ? 15.711  -2.482  -7.283  1.00 42.50  ? 285 LEU A C     1 
ATOM   2270 O  O     . LEU A 1 286 ? 16.899  -2.207  -7.485  1.00 40.16  ? 285 LEU A O     1 
ATOM   2271 C  CB    . LEU A 1 286 ? 14.809  -0.174  -6.992  1.00 37.40  ? 285 LEU A CB    1 
ATOM   2272 C  CG    . LEU A 1 286 ? 13.913  1.001   -7.401  1.00 40.90  ? 285 LEU A CG    1 
ATOM   2273 C  CD1   . LEU A 1 286 ? 14.342  2.255   -6.682  1.00 35.17  ? 285 LEU A CD1   1 
ATOM   2274 C  CD2   . LEU A 1 286 ? 14.026  1.223   -8.894  1.00 42.36  ? 285 LEU A CD2   1 
ATOM   2275 N  N     . SER A 1 287 ? 15.333  -3.600  -6.664  1.00 41.08  ? 286 SER A N     1 
ATOM   2276 C  CA    . SER A 1 287 ? 16.308  -4.528  -6.093  1.00 54.33  ? 286 SER A CA    1 
ATOM   2277 C  C     . SER A 1 287 ? 17.302  -3.786  -5.197  1.00 55.06  ? 286 SER A C     1 
ATOM   2278 O  O     . SER A 1 287 ? 18.514  -4.020  -5.233  1.00 50.22  ? 286 SER A O     1 
ATOM   2279 C  CB    . SER A 1 287 ? 17.035  -5.301  -7.197  1.00 63.59  ? 286 SER A CB    1 
ATOM   2280 O  OG    . SER A 1 287 ? 16.158  -5.559  -8.286  1.00 69.99  ? 286 SER A OG    1 
ATOM   2281 N  N     . GLN A 1 288 ? 16.784  -2.866  -4.389  1.00 46.52  ? 287 GLN A N     1 
ATOM   2282 C  CA    . GLN A 1 288 ? 17.616  -2.010  -3.553  1.00 37.26  ? 287 GLN A CA    1 
ATOM   2283 C  C     . GLN A 1 288 ? 17.073  -2.068  -2.138  1.00 39.58  ? 287 GLN A C     1 
ATOM   2284 O  O     . GLN A 1 288 ? 15.903  -1.752  -1.918  1.00 45.71  ? 287 GLN A O     1 
ATOM   2285 C  CB    . GLN A 1 288 ? 17.593  -0.571  -4.063  1.00 41.42  ? 287 GLN A CB    1 
ATOM   2286 C  CG    . GLN A 1 288 ? 18.739  0.269   -3.567  1.00 48.25  ? 287 GLN A CG    1 
ATOM   2287 C  CD    . GLN A 1 288 ? 19.944  0.180   -4.472  1.00 44.00  ? 287 GLN A CD    1 
ATOM   2288 O  OE1   . GLN A 1 288 ? 19.826  -0.154  -5.658  1.00 51.75  ? 287 GLN A OE1   1 
ATOM   2289 N  NE2   . GLN A 1 288 ? 21.110  0.507   -3.932  1.00 48.13  ? 287 GLN A NE2   1 
ATOM   2290 N  N     . ALA A 1 289 ? 17.902  -2.471  -1.182  1.00 32.60  ? 288 ALA A N     1 
ATOM   2291 C  CA    . ALA A 1 289 ? 17.386  -2.662  0.172   1.00 34.81  ? 288 ALA A CA    1 
ATOM   2292 C  C     . ALA A 1 289 ? 17.055  -1.350  0.885   1.00 36.02  ? 288 ALA A C     1 
ATOM   2293 O  O     . ALA A 1 289 ? 16.351  -1.381  1.898   1.00 37.78  ? 288 ALA A O     1 
ATOM   2294 C  CB    . ALA A 1 289 ? 18.383  -3.474  0.999   1.00 35.16  ? 288 ALA A CB    1 
ATOM   2295 N  N     . LEU A 1 290 ? 17.522  -0.207  0.386   1.00 29.31  ? 289 LEU A N     1 
ATOM   2296 C  CA    . LEU A 1 290 ? 17.303  1.074   1.046   1.00 27.38  ? 289 LEU A CA    1 
ATOM   2297 C  C     . LEU A 1 290 ? 16.958  2.104   -0.009  1.00 28.33  ? 289 LEU A C     1 
ATOM   2298 O  O     . LEU A 1 290 ? 17.710  2.267   -0.972  1.00 29.85  ? 289 LEU A O     1 
ATOM   2299 C  CB    . LEU A 1 290 ? 18.537  1.518   1.850   1.00 32.01  ? 289 LEU A CB    1 
ATOM   2300 C  CG    . LEU A 1 290 ? 18.488  2.946   2.413   1.00 33.77  ? 289 LEU A CG    1 
ATOM   2301 C  CD1   . LEU A 1 290 ? 17.354  3.136   3.441   1.00 28.03  ? 289 LEU A CD1   1 
ATOM   2302 C  CD2   . LEU A 1 290 ? 19.857  3.332   3.031   1.00 30.01  ? 289 LEU A CD2   1 
ATOM   2303 N  N     . VAL A 1 291 ? 15.787  2.750   0.131   1.00 26.64  ? 290 VAL A N     1 
ATOM   2304 C  CA    . VAL A 1 291 ? 15.373  3.826   -0.758  1.00 23.38  ? 290 VAL A CA    1 
ATOM   2305 C  C     . VAL A 1 291 ? 14.912  4.987   0.115   1.00 29.23  ? 290 VAL A C     1 
ATOM   2306 O  O     . VAL A 1 291 ? 14.457  4.788   1.242   1.00 29.24  ? 290 VAL A O     1 
ATOM   2307 C  CB    . VAL A 1 291 ? 14.261  3.375   -1.763  1.00 27.69  ? 290 VAL A CB    1 
ATOM   2308 C  CG1   . VAL A 1 291 ? 14.726  2.135   -2.581  1.00 29.82  ? 290 VAL A CG1   1 
ATOM   2309 C  CG2   . VAL A 1 291 ? 12.954  3.066   -1.052  1.00 27.52  ? 290 VAL A CG2   1 
ATOM   2310 N  N     . PHE A 1 292 ? 15.040  6.206   -0.400  1.00 24.51  ? 291 PHE A N     1 
ATOM   2311 C  CA    . PHE A 1 292 ? 14.548  7.359   0.338   1.00 27.22  ? 291 PHE A CA    1 
ATOM   2312 C  C     . PHE A 1 292 ? 14.357  8.514   -0.629  1.00 28.28  ? 291 PHE A C     1 
ATOM   2313 O  O     . PHE A 1 292 ? 14.929  8.531   -1.716  1.00 27.52  ? 291 PHE A O     1 
ATOM   2314 C  CB    . PHE A 1 292 ? 15.450  7.718   1.539   1.00 25.65  ? 291 PHE A CB    1 
ATOM   2315 C  CG    . PHE A 1 292 ? 16.916  7.851   1.214   1.00 31.21  ? 291 PHE A CG    1 
ATOM   2316 C  CD1   . PHE A 1 292 ? 17.441  9.016   0.673   1.00 26.70  ? 291 PHE A CD1   1 
ATOM   2317 C  CD2   . PHE A 1 292 ? 17.783  6.794   1.489   1.00 25.22  ? 291 PHE A CD2   1 
ATOM   2318 C  CE1   . PHE A 1 292 ? 18.781  9.104   0.373   1.00 29.14  ? 291 PHE A CE1   1 
ATOM   2319 C  CE2   . PHE A 1 292 ? 19.140  6.882   1.173   1.00 35.15  ? 291 PHE A CE2   1 
ATOM   2320 C  CZ    . PHE A 1 292 ? 19.638  8.041   0.623   1.00 30.34  ? 291 PHE A CZ    1 
ATOM   2321 N  N     . SER A 1 293 ? 13.476  9.436   -0.246  1.00 30.35  ? 292 SER A N     1 
ATOM   2322 C  CA    . SER A 1 293 ? 13.085  10.550  -1.102  1.00 33.13  ? 292 SER A CA    1 
ATOM   2323 C  C     . SER A 1 293 ? 14.167  11.628  -1.137  1.00 31.79  ? 292 SER A C     1 
ATOM   2324 O  O     . SER A 1 293 ? 15.031  11.694  -0.262  1.00 31.69  ? 292 SER A O     1 
ATOM   2325 C  CB    . SER A 1 293 ? 11.795  11.179  -0.586  1.00 32.31  ? 292 SER A CB    1 
ATOM   2326 O  OG    . SER A 1 293 ? 12.011  11.691  0.715   1.00 33.45  ? 292 SER A OG    1 
ATOM   2327 N  N     . SER A 1 294 ? 14.062  12.532  -2.126  1.00 29.61  ? 293 SER A N     1 
ATOM   2328 C  CA    . SER A 1 294 ? 14.981  13.668  -2.193  1.00 33.99  ? 293 SER A CA    1 
ATOM   2329 C  C     . SER A 1 294 ? 14.885  14.540  -0.951  1.00 37.27  ? 293 SER A C     1 
ATOM   2330 O  O     . SER A 1 294 ? 15.878  15.156  -0.543  1.00 37.06  ? 293 SER A O     1 
ATOM   2331 C  CB    . SER A 1 294 ? 14.700  14.553  -3.413  1.00 34.37  ? 293 SER A CB    1 
ATOM   2332 O  OG    . SER A 1 294 ? 13.319  14.740  -3.553  1.00 40.02  ? 293 SER A OG    1 
ATOM   2333 N  N     . GLU A 1 295 ? 13.700  14.634  -0.358  1.00 33.12  ? 294 GLU A N     1 
ATOM   2334 C  CA    . GLU A 1 295 ? 13.551  15.435  0.859   1.00 40.70  ? 294 GLU A CA    1 
ATOM   2335 C  C     . GLU A 1 295 ? 14.419  14.887  1.986   1.00 33.36  ? 294 GLU A C     1 
ATOM   2336 O  O     . GLU A 1 295 ? 15.002  15.650  2.758   1.00 38.26  ? 294 GLU A O     1 
ATOM   2337 C  CB    . GLU A 1 295 ? 12.076  15.469  1.261   1.00 40.54  ? 294 GLU A CB    1 
ATOM   2338 C  CG    . GLU A 1 295 ? 11.276  16.555  0.554   1.00 51.31  ? 294 GLU A CG    1 
ATOM   2339 C  CD    . GLU A 1 295 ? 9.826   16.630  1.012   1.00 58.28  ? 294 GLU A CD    1 
ATOM   2340 O  OE1   . GLU A 1 295 ? 9.251   15.577  1.387   1.00 54.06  ? 294 GLU A OE1   1 
ATOM   2341 O  OE2   . GLU A 1 295 ? 9.258   17.743  0.990   1.00 73.89  ? 294 GLU A OE2   1 
ATOM   2342 N  N     . VAL A 1 296 ? 14.513  13.562  2.094   1.00 29.49  ? 295 VAL A N     1 
ATOM   2343 C  CA    . VAL A 1 296 ? 15.414  12.953  3.062   1.00 33.58  ? 295 VAL A CA    1 
ATOM   2344 C  C     . VAL A 1 296 ? 16.861  13.233  2.684   1.00 32.28  ? 295 VAL A C     1 
ATOM   2345 O  O     . VAL A 1 296 ? 17.668  13.664  3.516   1.00 34.41  ? 295 VAL A O     1 
ATOM   2346 C  CB    . VAL A 1 296 ? 15.129  11.446  3.172   1.00 27.91  ? 295 VAL A CB    1 
ATOM   2347 C  CG1   . VAL A 1 296 ? 16.225  10.757  4.033   1.00 30.18  ? 295 VAL A CG1   1 
ATOM   2348 C  CG2   . VAL A 1 296 ? 13.743  11.219  3.779   1.00 25.26  ? 295 VAL A CG2   1 
ATOM   2349 N  N     . LYS A 1 297 ? 17.183  13.041  1.406   1.00 32.00  ? 296 LYS A N     1 
ATOM   2350 C  CA    . LYS A 1 297 ? 18.536  13.220  0.890   1.00 34.65  ? 296 LYS A CA    1 
ATOM   2351 C  C     . LYS A 1 297 ? 19.065  14.625  1.167   1.00 46.04  ? 296 LYS A C     1 
ATOM   2352 O  O     . LYS A 1 297 ? 20.171  14.785  1.695   1.00 42.79  ? 296 LYS A O     1 
ATOM   2353 C  CB    . LYS A 1 297 ? 18.545  12.924  -0.614  1.00 34.74  ? 296 LYS A CB    1 
ATOM   2354 C  CG    . LYS A 1 297 ? 19.929  12.962  -1.267  1.00 39.83  ? 296 LYS A CG    1 
ATOM   2355 C  CD    . LYS A 1 297 ? 20.132  14.225  -2.050  1.00 41.92  ? 296 LYS A CD    1 
ATOM   2356 C  CE    . LYS A 1 297 ? 21.336  14.131  -2.972  1.00 44.80  ? 296 LYS A CE    1 
ATOM   2357 N  NZ    . LYS A 1 297 ? 21.454  15.370  -3.781  1.00 54.10  ? 296 LYS A NZ    1 
ATOM   2358 N  N     . ASN A 1 298 ? 18.289  15.656  0.811   1.00 47.70  ? 297 ASN A N     1 
ATOM   2359 C  CA    . ASN A 1 298 ? 18.687  17.039  1.044   1.00 42.64  ? 297 ASN A CA    1 
ATOM   2360 C  C     . ASN A 1 298 ? 18.642  17.447  2.509   1.00 46.10  ? 297 ASN A C     1 
ATOM   2361 O  O     . ASN A 1 298 ? 19.192  18.495  2.863   1.00 56.09  ? 297 ASN A O     1 
ATOM   2362 C  CB    . ASN A 1 298 ? 17.808  18.001  0.235   1.00 46.37  ? 297 ASN A CB    1 
ATOM   2363 C  CG    . ASN A 1 298 ? 17.860  17.734  -1.256  1.00 51.87  ? 297 ASN A CG    1 
ATOM   2364 O  OD1   . ASN A 1 298 ? 16.831  17.622  -1.922  1.00 58.50  ? 297 ASN A OD1   1 
ATOM   2365 N  ND2   . ASN A 1 298 ? 19.064  17.611  -1.785  1.00 55.67  ? 297 ASN A ND2   1 
ATOM   2366 N  N     . SER A 1 299 ? 18.002  16.670  3.369   1.00 42.21  ? 298 SER A N     1 
ATOM   2367 C  CA    . SER A 1 299 ? 18.068  16.957  4.792   1.00 43.35  ? 298 SER A CA    1 
ATOM   2368 C  C     . SER A 1 299 ? 19.346  16.435  5.437   1.00 48.80  ? 298 SER A C     1 
ATOM   2369 O  O     . SER A 1 299 ? 19.675  16.844  6.554   1.00 46.39  ? 298 SER A O     1 
ATOM   2370 C  CB    . SER A 1 299 ? 16.872  16.348  5.505   1.00 38.55  ? 298 SER A CB    1 
ATOM   2371 O  OG    . SER A 1 299 ? 15.769  17.215  5.459   1.00 54.18  ? 298 SER A OG    1 
ATOM   2372 N  N     . ALA A 1 300 ? 20.055  15.529  4.778   1.00 44.91  ? 299 ALA A N     1 
ATOM   2373 C  CA    . ALA A 1 300 ? 21.263  14.970  5.362   1.00 42.10  ? 299 ALA A CA    1 
ATOM   2374 C  C     . ALA A 1 300 ? 22.385  16.002  5.343   1.00 52.17  ? 299 ALA A C     1 
ATOM   2375 O  O     . ALA A 1 300 ? 22.530  16.774  4.387   1.00 53.67  ? 299 ALA A O     1 
ATOM   2376 C  CB    . ALA A 1 300 ? 21.676  13.715  4.594   1.00 40.80  ? 299 ALA A CB    1 
ATOM   2377 N  N     . THR A 1 301 ? 23.191  16.012  6.403   1.00 46.79  ? 300 THR A N     1 
ATOM   2378 C  CA    . THR A 1 301 ? 24.331  16.918  6.456   1.00 51.77  ? 300 THR A CA    1 
ATOM   2379 C  C     . THR A 1 301 ? 25.645  16.241  6.112   1.00 52.46  ? 300 THR A C     1 
ATOM   2380 O  O     . THR A 1 301 ? 26.567  16.907  5.636   1.00 54.72  ? 300 THR A O     1 
ATOM   2381 C  CB    . THR A 1 301 ? 24.446  17.558  7.840   1.00 53.47  ? 300 THR A CB    1 
ATOM   2382 O  OG1   . THR A 1 301 ? 24.969  16.591  8.754   1.00 61.17  ? 300 THR A OG1   1 
ATOM   2383 C  CG2   . THR A 1 301 ? 23.083  18.023  8.328   1.00 58.13  ? 300 THR A CG2   1 
ATOM   2384 N  N     . LYS A 1 302 ? 25.752  14.939  6.316   1.00 44.79  ? 301 LYS A N     1 
ATOM   2385 C  CA    . LYS A 1 302 ? 26.989  14.257  5.990   1.00 43.36  ? 301 LYS A CA    1 
ATOM   2386 C  C     . LYS A 1 302 ? 27.027  13.934  4.497   1.00 43.42  ? 301 LYS A C     1 
ATOM   2387 O  O     . LYS A 1 302 ? 26.014  14.004  3.786   1.00 43.25  ? 301 LYS A O     1 
ATOM   2388 C  CB    . LYS A 1 302 ? 27.125  12.998  6.852   1.00 36.97  ? 301 LYS A CB    1 
ATOM   2389 C  CG    . LYS A 1 302 ? 27.006  13.332  8.343   1.00 43.81  ? 301 LYS A CG    1 
ATOM   2390 C  CD    . LYS A 1 302 ? 27.011  12.100  9.249   1.00 48.20  ? 301 LYS A CD    1 
ATOM   2391 C  CE    . LYS A 1 302 ? 27.811  12.320  10.527  1.00 64.18  ? 301 LYS A CE    1 
ATOM   2392 N  NZ    . LYS A 1 302 ? 28.201  11.024  11.162  1.00 75.67  ? 301 LYS A NZ    1 
ATOM   2393 N  N     . SER A 1 303 ? 28.222  13.590  4.028   1.00 38.93  ? 302 SER A N     1 
ATOM   2394 C  CA    . SER A 1 303 ? 28.487  13.328  2.615   1.00 47.27  ? 302 SER A CA    1 
ATOM   2395 C  C     . SER A 1 303 ? 28.342  11.838  2.313   1.00 46.68  ? 302 SER A C     1 
ATOM   2396 O  O     . SER A 1 303 ? 29.303  11.135  1.994   1.00 37.38  ? 302 SER A O     1 
ATOM   2397 C  CB    . SER A 1 303 ? 29.883  13.804  2.241   1.00 48.93  ? 302 SER A CB    1 
ATOM   2398 O  OG    . SER A 1 303 ? 29.893  15.210  2.073   1.00 57.95  ? 302 SER A OG    1 
ATOM   2399 N  N     . TRP A 1 304 ? 27.105  11.371  2.386   1.00 39.54  ? 303 TRP A N     1 
ATOM   2400 C  CA    . TRP A 1 304 ? 26.832  9.982   2.069   1.00 35.07  ? 303 TRP A CA    1 
ATOM   2401 C  C     . TRP A 1 304 ? 27.104  9.714   0.597   1.00 29.49  ? 303 TRP A C     1 
ATOM   2402 O  O     . TRP A 1 304 ? 27.036  10.613  -0.237  1.00 32.64  ? 303 TRP A O     1 
ATOM   2403 C  CB    . TRP A 1 304 ? 25.371  9.659   2.402   1.00 31.99  ? 303 TRP A CB    1 
ATOM   2404 C  CG    . TRP A 1 304 ? 25.035  9.887   3.843   1.00 30.84  ? 303 TRP A CG    1 
ATOM   2405 C  CD1   . TRP A 1 304 ? 24.456  10.997  4.381   1.00 32.87  ? 303 TRP A CD1   1 
ATOM   2406 C  CD2   . TRP A 1 304 ? 25.263  8.987   4.936   1.00 30.83  ? 303 TRP A CD2   1 
ATOM   2407 N  NE1   . TRP A 1 304 ? 24.301  10.842  5.731   1.00 32.79  ? 303 TRP A NE1   1 
ATOM   2408 C  CE2   . TRP A 1 304 ? 24.786  9.615   6.096   1.00 29.52  ? 303 TRP A CE2   1 
ATOM   2409 C  CE3   . TRP A 1 304 ? 25.828  7.713   5.040   1.00 32.59  ? 303 TRP A CE3   1 
ATOM   2410 C  CZ2   . TRP A 1 304 ? 24.840  9.011   7.347   1.00 33.00  ? 303 TRP A CZ2   1 
ATOM   2411 C  CZ3   . TRP A 1 304 ? 25.876  7.111   6.281   1.00 36.47  ? 303 TRP A CZ3   1 
ATOM   2412 C  CH2   . TRP A 1 304 ? 25.385  7.760   7.417   1.00 37.38  ? 303 TRP A CH2   1 
ATOM   2413 N  N     . ASN A 1 305 ? 27.386  8.452   0.274   1.00 29.41  ? 304 ASN A N     1 
ATOM   2414 C  CA    . ASN A 1 305 ? 27.590  8.024   -1.106  1.00 30.33  ? 304 ASN A CA    1 
ATOM   2415 C  C     . ASN A 1 305 ? 26.242  7.821   -1.807  1.00 32.17  ? 304 ASN A C     1 
ATOM   2416 O  O     . ASN A 1 305 ? 25.857  6.719   -2.202  1.00 29.76  ? 304 ASN A O     1 
ATOM   2417 C  CB    . ASN A 1 305 ? 28.454  6.780   -1.113  1.00 31.65  ? 304 ASN A CB    1 
ATOM   2418 C  CG    . ASN A 1 305 ? 29.803  7.051   -0.490  1.00 42.74  ? 304 ASN A CG    1 
ATOM   2419 O  OD1   . ASN A 1 305 ? 30.320  8.159   -0.598  1.00 39.33  ? 304 ASN A OD1   1 
ATOM   2420 N  ND2   . ASN A 1 305 ? 30.320  6.097   0.251   1.00 38.20  ? 304 ASN A ND2   1 
ATOM   2421 N  N     . PHE A 1 306 ? 25.551  8.941   -2.009  1.00 33.52  ? 305 PHE A N     1 
ATOM   2422 C  CA    . PHE A 1 306 ? 24.212  8.945   -2.587  1.00 31.06  ? 305 PHE A CA    1 
ATOM   2423 C  C     . PHE A 1 306 ? 24.268  8.477   -4.030  1.00 35.45  ? 305 PHE A C     1 
ATOM   2424 O  O     . PHE A 1 306 ? 25.202  8.811   -4.771  1.00 29.31  ? 305 PHE A O     1 
ATOM   2425 C  CB    . PHE A 1 306 ? 23.647  10.363  -2.583  1.00 28.28  ? 305 PHE A CB    1 
ATOM   2426 C  CG    . PHE A 1 306 ? 23.296  10.885  -1.230  1.00 30.03  ? 305 PHE A CG    1 
ATOM   2427 C  CD1   . PHE A 1 306 ? 22.397  10.206  -0.391  1.00 33.92  ? 305 PHE A CD1   1 
ATOM   2428 C  CD2   . PHE A 1 306 ? 23.857  12.077  -0.788  1.00 31.35  ? 305 PHE A CD2   1 
ATOM   2429 C  CE1   . PHE A 1 306 ? 22.059  10.723  0.851   1.00 33.12  ? 305 PHE A CE1   1 
ATOM   2430 C  CE2   . PHE A 1 306 ? 23.528  12.597  0.465   1.00 32.77  ? 305 PHE A CE2   1 
ATOM   2431 C  CZ    . PHE A 1 306 ? 22.624  11.922  1.281   1.00 35.71  ? 305 PHE A CZ    1 
ATOM   2432 N  N     . ILE A 1 307 ? 23.238  7.733   -4.443  1.00 28.41  ? 306 ILE A N     1 
ATOM   2433 C  CA    . ILE A 1 307 ? 23.026  7.403   -5.847  1.00 29.62  ? 306 ILE A CA    1 
ATOM   2434 C  C     . ILE A 1 307 ? 21.559  7.656   -6.205  1.00 33.21  ? 306 ILE A C     1 
ATOM   2435 O  O     . ILE A 1 307 ? 20.650  7.285   -5.448  1.00 32.37  ? 306 ILE A O     1 
ATOM   2436 C  CB    . ILE A 1 307 ? 23.443  5.952   -6.160  1.00 31.63  ? 306 ILE A CB    1 
ATOM   2437 C  CG1   . ILE A 1 307 ? 23.269  5.657   -7.644  1.00 32.80  ? 306 ILE A CG1   1 
ATOM   2438 C  CG2   . ILE A 1 307 ? 22.725  4.962   -5.243  1.00 26.99  ? 306 ILE A CG2   1 
ATOM   2439 C  CD1   . ILE A 1 307 ? 23.746  4.257   -8.081  1.00 37.82  ? 306 ILE A CD1   1 
ATOM   2440 N  N     . TRP A 1 308 ? 21.329  8.318   -7.340  1.00 32.62  ? 307 TRP A N     1 
ATOM   2441 C  CA    . TRP A 1 308 ? 19.968  8.559   -7.801  1.00 31.61  ? 307 TRP A CA    1 
ATOM   2442 C  C     . TRP A 1 308 ? 19.481  7.323   -8.541  1.00 32.05  ? 307 TRP A C     1 
ATOM   2443 O  O     . TRP A 1 308 ? 20.221  6.742   -9.341  1.00 34.00  ? 307 TRP A O     1 
ATOM   2444 C  CB    . TRP A 1 308 ? 19.890  9.791   -8.708  1.00 31.13  ? 307 TRP A CB    1 
ATOM   2445 C  CG    . TRP A 1 308 ? 18.517  10.003  -9.321  1.00 32.46  ? 307 TRP A CG    1 
ATOM   2446 C  CD1   . TRP A 1 308 ? 17.529  10.828  -8.843  1.00 30.51  ? 307 TRP A CD1   1 
ATOM   2447 C  CD2   . TRP A 1 308 ? 18.011  9.445   -10.541 1.00 33.94  ? 307 TRP A CD2   1 
ATOM   2448 N  NE1   . TRP A 1 308 ? 16.430  10.784  -9.672  1.00 31.02  ? 307 TRP A NE1   1 
ATOM   2449 C  CE2   . TRP A 1 308 ? 16.703  9.939   -10.719 1.00 30.48  ? 307 TRP A CE2   1 
ATOM   2450 C  CE3   . TRP A 1 308 ? 18.528  8.554   -11.488 1.00 34.58  ? 307 TRP A CE3   1 
ATOM   2451 C  CZ2   . TRP A 1 308 ? 15.911  9.577   -11.805 1.00 34.59  ? 307 TRP A CZ2   1 
ATOM   2452 C  CZ3   . TRP A 1 308 ? 17.744  8.198   -12.560 1.00 34.52  ? 307 TRP A CZ3   1 
ATOM   2453 C  CH2   . TRP A 1 308 ? 16.446  8.705   -12.714 1.00 36.13  ? 307 TRP A CH2   1 
ATOM   2454 N  N     . LEU A 1 309 ? 18.248  6.900   -8.255  1.00 31.72  ? 308 LEU A N     1 
ATOM   2455 C  CA    . LEU A 1 309 ? 17.762  5.630   -8.777  1.00 31.11  ? 308 LEU A CA    1 
ATOM   2456 C  C     . LEU A 1 309 ? 16.667  5.786   -9.815  1.00 31.37  ? 308 LEU A C     1 
ATOM   2457 O  O     . LEU A 1 309 ? 16.719  5.116   -10.849 1.00 34.12  ? 308 LEU A O     1 
ATOM   2458 C  CB    . LEU A 1 309 ? 17.253  4.746   -7.627  1.00 32.81  ? 308 LEU A CB    1 
ATOM   2459 C  CG    . LEU A 1 309 ? 18.327  4.247   -6.662  1.00 30.30  ? 308 LEU A CG    1 
ATOM   2460 C  CD1   . LEU A 1 309 ? 17.736  3.284   -5.670  1.00 34.25  ? 308 LEU A CD1   1 
ATOM   2461 C  CD2   . LEU A 1 309 ? 19.483  3.567   -7.423  1.00 31.53  ? 308 LEU A CD2   1 
ATOM   2462 N  N     . THR A 1 310 ? 15.672  6.633   -9.553  1.00 31.20  ? 309 THR A N     1 
ATOM   2463 C  CA    . THR A 1 310 ? 14.431  6.697   -10.323 1.00 32.45  ? 309 THR A CA    1 
ATOM   2464 C  C     . THR A 1 310 ? 13.545  7.802   -9.749  1.00 33.57  ? 309 THR A C     1 
ATOM   2465 O  O     . THR A 1 310 ? 13.840  8.382   -8.697  1.00 35.35  ? 309 THR A O     1 
ATOM   2466 C  CB    . THR A 1 310 ? 13.663  5.369   -10.297 1.00 39.39  ? 309 THR A CB    1 
ATOM   2467 O  OG1   . THR A 1 310 ? 12.689  5.357   -11.349 1.00 32.88  ? 309 THR A OG1   1 
ATOM   2468 C  CG2   . THR A 1 310 ? 12.982  5.113   -8.913  1.00 35.46  ? 309 THR A CG2   1 
ATOM   2469 N  N     . ASP A 1 311 ? 12.441  8.075   -10.454 1.00 31.20  ? 310 ASP A N     1 
ATOM   2470 C  CA    . ASP A 1 311 ? 11.354  8.888   -9.929  1.00 34.24  ? 310 ASP A CA    1 
ATOM   2471 C  C     . ASP A 1 311 ? 10.234  7.965   -9.462  1.00 34.23  ? 310 ASP A C     1 
ATOM   2472 O  O     . ASP A 1 311 ? 10.070  6.862   -9.991  1.00 34.18  ? 310 ASP A O     1 
ATOM   2473 C  CB    . ASP A 1 311 ? 10.812  9.835   -10.997 1.00 31.33  ? 310 ASP A CB    1 
ATOM   2474 C  CG    . ASP A 1 311 ? 11.598  11.103  -11.118 1.00 34.59  ? 310 ASP A CG    1 
ATOM   2475 O  OD1   . ASP A 1 311 ? 12.705  11.041  -11.686 1.00 32.65  ? 310 ASP A OD1   1 
ATOM   2476 O  OD2   . ASP A 1 311 ? 11.081  12.170  -10.709 1.00 33.43  ? 310 ASP A OD2   1 
ATOM   2477 N  N     . SER A 1 312 ? 9.461   8.428   -8.481  1.00 34.11  ? 311 SER A N     1 
ATOM   2478 C  CA    . SER A 1 312 ? 8.283   7.712   -8.005  1.00 35.52  ? 311 SER A CA    1 
ATOM   2479 C  C     . SER A 1 312 ? 7.278   8.701   -7.406  1.00 38.90  ? 311 SER A C     1 
ATOM   2480 O  O     . SER A 1 312 ? 7.506   9.910   -7.370  1.00 41.34  ? 311 SER A O     1 
ATOM   2481 C  CB    . SER A 1 312 ? 8.661   6.633   -6.984  1.00 41.91  ? 311 SER A CB    1 
ATOM   2482 O  OG    . SER A 1 312 ? 7.666   5.606   -6.941  1.00 46.57  ? 311 SER A OG    1 
ATOM   2483 N  N     . GLU A 1 313 ? 6.124   8.188   -6.983  1.00 41.57  ? 312 GLU A N     1 
ATOM   2484 C  CA    . GLU A 1 313 ? 5.209   8.933   -6.114  1.00 48.33  ? 312 GLU A CA    1 
ATOM   2485 C  C     . GLU A 1 313 ? 5.154   8.258   -4.760  1.00 45.25  ? 312 GLU A C     1 
ATOM   2486 O  O     . GLU A 1 313 ? 4.996   7.037   -4.682  1.00 53.90  ? 312 GLU A O     1 
ATOM   2487 C  CB    . GLU A 1 313 ? 3.768   9.021   -6.640  1.00 52.10  ? 312 GLU A CB    1 
ATOM   2488 C  CG    . GLU A 1 313 ? 3.542   9.260   -8.087  1.00 59.88  ? 312 GLU A CG    1 
ATOM   2489 C  CD    . GLU A 1 313 ? 2.056   9.579   -8.417  1.00 69.93  ? 312 GLU A CD    1 
ATOM   2490 O  OE1   . GLU A 1 313 ? 1.159   9.243   -7.609  1.00 64.80  ? 312 GLU A OE1   1 
ATOM   2491 O  OE2   . GLU A 1 313 ? 1.792   10.189  -9.480  1.00 69.56  ? 312 GLU A OE2   1 
ATOM   2492 N  N     . LEU A 1 314 ? 5.243   9.046   -3.698  1.00 45.26  ? 313 LEU A N     1 
ATOM   2493 C  CA    . LEU A 1 314 ? 5.122   8.466   -2.372  1.00 48.02  ? 313 LEU A CA    1 
ATOM   2494 C  C     . LEU A 1 314 ? 3.825   8.824   -1.662  1.00 56.38  ? 313 LEU A C     1 
ATOM   2495 O  O     . LEU A 1 314 ? 3.321   8.008   -0.885  1.00 57.43  ? 313 LEU A O     1 
ATOM   2496 C  CB    . LEU A 1 314 ? 6.315   8.876   -1.501  1.00 49.28  ? 313 LEU A CB    1 
ATOM   2497 C  CG    . LEU A 1 314 ? 7.610   8.201   -1.964  1.00 43.31  ? 313 LEU A CG    1 
ATOM   2498 C  CD1   . LEU A 1 314 ? 8.771   8.495   -1.021  1.00 44.78  ? 313 LEU A CD1   1 
ATOM   2499 C  CD2   . LEU A 1 314 ? 7.403   6.695   -2.148  1.00 48.07  ? 313 LEU A CD2   1 
ATOM   2500 N  N     . LYS A 1 315 ? 3.246   9.996   -1.932  1.00 54.30  ? 314 LYS A N     1 
ATOM   2501 C  CA    . LYS A 1 315 ? 2.104   10.461  -1.150  1.00 64.35  ? 314 LYS A CA    1 
ATOM   2502 C  C     . LYS A 1 315 ? 0.757   10.279  -1.834  1.00 70.59  ? 314 LYS A C     1 
ATOM   2503 O  O     . LYS A 1 315 ? -0.273  10.313  -1.149  1.00 68.53  ? 314 LYS A O     1 
ATOM   2504 C  CB    . LYS A 1 315 ? 2.285   11.938  -0.776  1.00 65.18  ? 314 LYS A CB    1 
ATOM   2505 C  CG    . LYS A 1 315 ? 3.669   12.266  -0.218  1.00 60.99  ? 314 LYS A CG    1 
ATOM   2506 C  CD    . LYS A 1 315 ? 3.903   11.530  1.098   1.00 60.98  ? 314 LYS A CD    1 
ATOM   2507 C  CE    . LYS A 1 315 ? 5.336   11.682  1.594   1.00 56.66  ? 314 LYS A CE    1 
ATOM   2508 N  NZ    . LYS A 1 315 ? 5.717   13.119  1.686   1.00 61.30  ? 314 LYS A NZ    1 
ATOM   2509 N  N     . GLY A 1 316 ? 0.730   10.074  -3.149  1.00 74.59  ? 315 GLY A N     1 
ATOM   2510 C  CA    . GLY A 1 316 ? -0.505  9.953   -3.895  1.00 77.05  ? 315 GLY A CA    1 
ATOM   2511 C  C     . GLY A 1 316 ? -0.844  11.173  -4.722  1.00 79.96  ? 315 GLY A C     1 
ATOM   2512 O  O     . GLY A 1 316 ? -1.660  11.069  -5.649  1.00 87.72  ? 315 GLY A O     1 
ATOM   2513 N  N     . LYS A 1 317 ? -0.252  12.324  -4.413  1.00 79.23  ? 316 LYS A N     1 
ATOM   2514 C  CA    . LYS A 1 317 ? -0.386  13.482  -5.281  1.00 86.92  ? 316 LYS A CA    1 
ATOM   2515 C  C     . LYS A 1 317 ? 0.346   13.233  -6.598  1.00 86.65  ? 316 LYS A C     1 
ATOM   2516 O  O     . LYS A 1 317 ? 1.161   12.314  -6.725  1.00 89.40  ? 316 LYS A O     1 
ATOM   2517 C  CB    . LYS A 1 317 ? 0.161   14.740  -4.597  1.00 87.18  ? 316 LYS A CB    1 
ATOM   2518 C  CG    . LYS A 1 317 ? 1.470   14.530  -3.839  1.00 89.39  ? 316 LYS A CG    1 
ATOM   2519 C  CD    . LYS A 1 317 ? 1.804   15.712  -2.921  1.00 98.25  ? 316 LYS A CD    1 
ATOM   2520 C  CE    . LYS A 1 317 ? 0.721   15.978  -1.874  1.00 100.92 ? 316 LYS A CE    1 
ATOM   2521 N  NZ    . LYS A 1 317 ? 1.050   17.165  -1.018  1.00 93.94  ? 316 LYS A NZ    1 
ATOM   2522 N  N     . SER A 1 318 ? 0.041   14.065  -7.594  1.00 88.56  ? 317 SER A N     1 
ATOM   2523 C  CA    . SER A 1 318 ? 0.718   13.989  -8.889  1.00 89.53  ? 317 SER A CA    1 
ATOM   2524 C  C     . SER A 1 318 ? 2.050   14.745  -8.831  1.00 85.20  ? 317 SER A C     1 
ATOM   2525 O  O     . SER A 1 318 ? 2.303   15.702  -9.562  1.00 88.83  ? 317 SER A O     1 
ATOM   2526 C  CB    . SER A 1 318 ? -0.187  14.521  -9.993  1.00 88.64  ? 317 SER A CB    1 
ATOM   2527 O  OG    . SER A 1 318 ? -1.267  13.633  -10.233 1.00 91.61  ? 317 SER A OG    1 
ATOM   2528 N  N     . GLU A 1 319 ? 2.910   14.293  -7.920  1.00 73.05  ? 318 GLU A N     1 
ATOM   2529 C  CA    . GLU A 1 319 ? 4.223   14.891  -7.719  1.00 74.57  ? 318 GLU A CA    1 
ATOM   2530 C  C     . GLU A 1 319 ? 5.284   13.810  -7.869  1.00 57.57  ? 318 GLU A C     1 
ATOM   2531 O  O     . GLU A 1 319 ? 5.352   12.889  -7.051  1.00 56.46  ? 318 GLU A O     1 
ATOM   2532 C  CB    . GLU A 1 319 ? 4.325   15.551  -6.345  1.00 79.42  ? 318 GLU A CB    1 
ATOM   2533 C  CG    . GLU A 1 319 ? 5.123   16.838  -6.346  1.00 84.62  ? 318 GLU A CG    1 
ATOM   2534 C  CD    . GLU A 1 319 ? 4.458   17.920  -7.175  1.00 96.34  ? 318 GLU A CD    1 
ATOM   2535 O  OE1   . GLU A 1 319 ? 4.671   17.957  -8.410  1.00 95.24  ? 318 GLU A OE1   1 
ATOM   2536 O  OE2   . GLU A 1 319 ? 3.699   18.723  -6.587  1.00 97.11  ? 318 GLU A OE2   1 
ATOM   2537 N  N     . SER A 1 320 ? 6.105   13.924  -8.904  1.00 54.41  ? 319 SER A N     1 
ATOM   2538 C  CA    . SER A 1 320 ? 7.169   12.962  -9.153  1.00 46.56  ? 319 SER A CA    1 
ATOM   2539 C  C     . SER A 1 320 ? 8.409   13.357  -8.355  1.00 41.31  ? 319 SER A C     1 
ATOM   2540 O  O     . SER A 1 320 ? 8.991   14.417  -8.592  1.00 47.00  ? 319 SER A O     1 
ATOM   2541 C  CB    . SER A 1 320 ? 7.485   12.907  -10.643 1.00 40.96  ? 319 SER A CB    1 
ATOM   2542 O  OG    . SER A 1 320 ? 8.305   11.796  -10.948 1.00 39.00  ? 319 SER A OG    1 
ATOM   2543 N  N     . ILE A 1 321 ? 8.824   12.499  -7.435  1.00 36.34  ? 320 ILE A N     1 
ATOM   2544 C  CA    . ILE A 1 321 ? 9.943   12.800  -6.548  1.00 38.15  ? 320 ILE A CA    1 
ATOM   2545 C  C     . ILE A 1 321 ? 11.106  11.868  -6.847  1.00 37.28  ? 320 ILE A C     1 
ATOM   2546 O  O     . ILE A 1 321 ? 10.926  10.689  -7.183  1.00 33.76  ? 320 ILE A O     1 
ATOM   2547 C  CB    . ILE A 1 321 ? 9.533   12.695  -5.067  1.00 40.10  ? 320 ILE A CB    1 
ATOM   2548 C  CG1   . ILE A 1 321 ? 9.186   11.260  -4.724  1.00 43.14  ? 320 ILE A CG1   1 
ATOM   2549 C  CG2   . ILE A 1 321 ? 8.344   13.603  -4.753  1.00 48.11  ? 320 ILE A CG2   1 
ATOM   2550 C  CD1   . ILE A 1 321 ? 9.740   10.846  -3.416  1.00 52.20  ? 320 ILE A CD1   1 
ATOM   2551 N  N     . ASP A 1 322 ? 12.314  12.400  -6.705  1.00 30.87  ? 321 ASP A N     1 
ATOM   2552 C  CA    . ASP A 1 322 ? 13.507  11.618  -6.996  1.00 28.57  ? 321 ASP A CA    1 
ATOM   2553 C  C     . ASP A 1 322 ? 13.752  10.637  -5.868  1.00 33.29  ? 321 ASP A C     1 
ATOM   2554 O  O     . ASP A 1 322 ? 13.625  10.994  -4.695  1.00 28.75  ? 321 ASP A O     1 
ATOM   2555 C  CB    . ASP A 1 322 ? 14.720  12.522  -7.211  1.00 35.30  ? 321 ASP A CB    1 
ATOM   2556 C  CG    . ASP A 1 322 ? 14.562  13.407  -8.432  1.00 36.52  ? 321 ASP A CG    1 
ATOM   2557 O  OD1   . ASP A 1 322 ? 14.287  12.837  -9.492  1.00 34.80  ? 321 ASP A OD1   1 
ATOM   2558 O  OD2   . ASP A 1 322 ? 14.788  14.630  -8.371  1.00 40.57  ? 321 ASP A OD2   1 
ATOM   2559 N  N     . ILE A 1 323 ? 14.026  9.391   -6.227  1.00 26.03  ? 322 ILE A N     1 
ATOM   2560 C  CA    . ILE A 1 323 ? 14.323  8.348   -5.257  1.00 28.67  ? 322 ILE A CA    1 
ATOM   2561 C  C     . ILE A 1 323 ? 15.816  8.067   -5.277  1.00 31.15  ? 322 ILE A C     1 
ATOM   2562 O  O     . ILE A 1 323 ? 16.412  7.872   -6.347  1.00 29.67  ? 322 ILE A O     1 
ATOM   2563 C  CB    . ILE A 1 323 ? 13.526  7.061   -5.547  1.00 27.05  ? 322 ILE A CB    1 
ATOM   2564 C  CG1   . ILE A 1 323 ? 12.007  7.318   -5.527  1.00 26.96  ? 322 ILE A CG1   1 
ATOM   2565 C  CG2   . ILE A 1 323 ? 13.934  5.978   -4.548  1.00 28.87  ? 322 ILE A CG2   1 
ATOM   2566 C  CD1   . ILE A 1 323 ? 11.471  7.913   -4.214  1.00 29.16  ? 322 ILE A CD1   1 
ATOM   2567 N  N     . TYR A 1 324 ? 16.414  8.041   -4.096  1.00 30.44  ? 323 TYR A N     1 
ATOM   2568 C  CA    . TYR A 1 324 ? 17.842  7.817   -3.932  1.00 25.02  ? 323 TYR A CA    1 
ATOM   2569 C  C     . TYR A 1 324 ? 18.081  6.588   -3.079  1.00 29.40  ? 323 TYR A C     1 
ATOM   2570 O  O     . TYR A 1 324 ? 17.181  6.099   -2.383  1.00 28.96  ? 323 TYR A O     1 
ATOM   2571 C  CB    . TYR A 1 324 ? 18.529  9.010   -3.251  1.00 28.42  ? 323 TYR A CB    1 
ATOM   2572 C  CG    . TYR A 1 324 ? 18.525  10.276  -4.073  1.00 34.27  ? 323 TYR A CG    1 
ATOM   2573 C  CD1   . TYR A 1 324 ? 17.416  11.119  -4.078  1.00 32.14  ? 323 TYR A CD1   1 
ATOM   2574 C  CD2   . TYR A 1 324 ? 19.649  10.635  -4.845  1.00 31.93  ? 323 TYR A CD2   1 
ATOM   2575 C  CE1   . TYR A 1 324 ? 17.406  12.293  -4.828  1.00 32.59  ? 323 TYR A CE1   1 
ATOM   2576 C  CE2   . TYR A 1 324 ? 19.649  11.792  -5.606  1.00 30.98  ? 323 TYR A CE2   1 
ATOM   2577 C  CZ    . TYR A 1 324 ? 18.522  12.617  -5.588  1.00 35.81  ? 323 TYR A CZ    1 
ATOM   2578 O  OH    . TYR A 1 324 ? 18.523  13.770  -6.338  1.00 36.74  ? 323 TYR A OH    1 
ATOM   2579 N  N     . SER A 1 325 ? 19.335  6.128   -3.105  1.00 29.06  ? 324 SER A N     1 
ATOM   2580 C  CA    . SER A 1 325 ? 19.841  5.203   -2.106  1.00 29.84  ? 324 SER A CA    1 
ATOM   2581 C  C     . SER A 1 325 ? 21.282  5.591   -1.785  1.00 33.60  ? 324 SER A C     1 
ATOM   2582 O  O     . SER A 1 325 ? 21.778  6.650   -2.203  1.00 29.77  ? 324 SER A O     1 
ATOM   2583 C  CB    . SER A 1 325 ? 19.738  3.750   -2.594  1.00 31.97  ? 324 SER A CB    1 
ATOM   2584 O  OG    . SER A 1 325 ? 20.137  2.847   -1.557  1.00 34.61  ? 324 SER A OG    1 
ATOM   2585 N  N     . ILE A 1 326 ? 21.951  4.712   -1.042  1.00 35.10  ? 325 ILE A N     1 
ATOM   2586 C  CA    . ILE A 1 326 ? 23.378  4.809   -0.757  1.00 32.49  ? 325 ILE A CA    1 
ATOM   2587 C  C     . ILE A 1 326 ? 24.060  3.740   -1.587  1.00 40.34  ? 325 ILE A C     1 
ATOM   2588 O  O     . ILE A 1 326 ? 23.634  2.581   -1.559  1.00 37.16  ? 325 ILE A O     1 
ATOM   2589 C  CB    . ILE A 1 326 ? 23.680  4.591   0.732   1.00 36.01  ? 325 ILE A CB    1 
ATOM   2590 C  CG1   . ILE A 1 326 ? 22.967  5.645   1.577   1.00 36.03  ? 325 ILE A CG1   1 
ATOM   2591 C  CG2   . ILE A 1 326 ? 25.200  4.617   0.973   1.00 36.75  ? 325 ILE A CG2   1 
ATOM   2592 C  CD1   . ILE A 1 326 ? 23.301  7.038   1.196   1.00 36.46  ? 325 ILE A CD1   1 
ATOM   2593 N  N     . ASP A 1 327 ? 25.104  4.123   -2.333  1.00 33.63  ? 326 ASP A N     1 
ATOM   2594 C  CA    . ASP A 1 327 ? 25.857  3.177   -3.152  1.00 34.27  ? 326 ASP A CA    1 
ATOM   2595 C  C     . ASP A 1 327 ? 27.048  2.724   -2.331  1.00 43.76  ? 326 ASP A C     1 
ATOM   2596 O  O     . ASP A 1 327 ? 28.061  3.420   -2.255  1.00 38.07  ? 326 ASP A O     1 
ATOM   2597 C  CB    . ASP A 1 327 ? 26.369  3.793   -4.448  1.00 35.90  ? 326 ASP A CB    1 
ATOM   2598 C  CG    . ASP A 1 327 ? 27.083  2.765   -5.321  1.00 43.09  ? 326 ASP A CG    1 
ATOM   2599 O  OD1   . ASP A 1 327 ? 26.805  1.557   -5.153  1.00 42.87  ? 326 ASP A OD1   1 
ATOM   2600 O  OD2   . ASP A 1 327 ? 28.012  3.132   -6.074  1.00 37.68  ? 326 ASP A OD2   1 
ATOM   2601 N  N     . ASN A 1 328 ? 26.930  1.560   -1.718  1.00 45.04  ? 327 ASN A N     1 
ATOM   2602 C  CA    . ASN A 1 328 ? 28.025  0.970   -0.979  1.00 50.20  ? 327 ASN A CA    1 
ATOM   2603 C  C     . ASN A 1 328 ? 27.987  -0.529  -1.216  1.00 57.64  ? 327 ASN A C     1 
ATOM   2604 O  O     . ASN A 1 328 ? 27.003  -1.069  -1.732  1.00 50.80  ? 327 ASN A O     1 
ATOM   2605 C  CB    . ASN A 1 328 ? 27.998  1.420   0.505   1.00 48.76  ? 327 ASN A CB    1 
ATOM   2606 C  CG    . ASN A 1 328 ? 27.012  0.658   1.384   1.00 53.26  ? 327 ASN A CG    1 
ATOM   2607 O  OD1   . ASN A 1 328 ? 26.475  -0.387  1.031   1.00 58.62  ? 327 ASN A OD1   1 
ATOM   2608 N  ND2   . ASN A 1 328 ? 26.754  1.223   2.551   1.00 47.28  ? 327 ASN A ND2   1 
ATOM   2609 N  N     . GLU A 1 329 ? 29.115  -1.171  -0.897  1.00 59.76  ? 328 GLU A N     1 
ATOM   2610 C  CA    . GLU A 1 329 ? 29.310  -2.591  -1.179  1.00 60.40  ? 328 GLU A CA    1 
ATOM   2611 C  C     . GLU A 1 329 ? 28.091  -3.407  -0.786  1.00 53.54  ? 328 GLU A C     1 
ATOM   2612 O  O     . GLU A 1 329 ? 27.650  -4.286  -1.536  1.00 58.69  ? 328 GLU A O     1 
ATOM   2613 C  CB    . GLU A 1 329 ? 30.553  -3.075  -0.436  1.00 67.89  ? 328 GLU A CB    1 
ATOM   2614 C  CG    . GLU A 1 329 ? 31.115  -4.388  -0.906  1.00 62.08  ? 328 GLU A CG    1 
ATOM   2615 C  CD    . GLU A 1 329 ? 32.477  -4.661  -0.294  1.00 67.80  ? 328 GLU A CD    1 
ATOM   2616 O  OE1   . GLU A 1 329 ? 32.643  -4.431  0.930   1.00 61.50  ? 328 GLU A OE1   1 
ATOM   2617 O  OE2   . GLU A 1 329 ? 33.384  -5.078  -1.052  1.00 70.97  ? 328 GLU A OE2   1 
ATOM   2618 N  N     . MET A 1 330 ? 27.509  -3.089  0.369   1.00 61.19  ? 329 MET A N     1 
ATOM   2619 C  CA    . MET A 1 330 ? 26.330  -3.792  0.866   1.00 60.89  ? 329 MET A CA    1 
ATOM   2620 C  C     . MET A 1 330 ? 25.135  -3.656  -0.076  1.00 65.61  ? 329 MET A C     1 
ATOM   2621 O  O     . MET A 1 330 ? 24.571  -4.660  -0.531  1.00 69.93  ? 329 MET A O     1 
ATOM   2622 C  CB    . MET A 1 330 ? 25.988  -3.253  2.242   1.00 59.21  ? 329 MET A CB    1 
ATOM   2623 C  CG    . MET A 1 330 ? 24.904  -3.977  2.968   1.00 59.59  ? 329 MET A CG    1 
ATOM   2624 S  SD    . MET A 1 330 ? 25.106  -3.364  4.639   1.00 63.36  ? 329 MET A SD    1 
ATOM   2625 C  CE    . MET A 1 330 ? 24.654  -1.642  4.384   1.00 48.12  ? 329 MET A CE    1 
ATOM   2626 N  N     . THR A 1 331 ? 24.717  -2.416  -0.359  1.00 60.50  ? 330 THR A N     1 
ATOM   2627 C  CA    . THR A 1 331 ? 23.514  -2.188  -1.155  1.00 55.95  ? 330 THR A CA    1 
ATOM   2628 C  C     . THR A 1 331 ? 23.668  -2.596  -2.616  1.00 62.83  ? 330 THR A C     1 
ATOM   2629 O  O     . THR A 1 331 ? 22.670  -2.576  -3.343  1.00 55.40  ? 330 THR A O     1 
ATOM   2630 C  CB    . THR A 1 331 ? 23.115  -0.714  -1.100  1.00 52.89  ? 330 THR A CB    1 
ATOM   2631 O  OG1   . THR A 1 331 ? 24.168  0.074   -1.669  1.00 47.58  ? 330 THR A OG1   1 
ATOM   2632 C  CG2   . THR A 1 331 ? 22.882  -0.273  0.328   1.00 44.66  ? 330 THR A CG2   1 
ATOM   2633 N  N     . ARG A 1 332 ? 24.876  -2.936  -3.077  1.00 57.04  ? 331 ARG A N     1 
ATOM   2634 C  CA    . ARG A 1 332 ? 25.038  -3.374  -4.464  1.00 61.68  ? 331 ARG A CA    1 
ATOM   2635 C  C     . ARG A 1 332 ? 24.489  -4.787  -4.599  1.00 68.42  ? 331 ARG A C     1 
ATOM   2636 O  O     . ARG A 1 332 ? 25.004  -5.733  -3.996  1.00 74.81  ? 331 ARG A O     1 
ATOM   2637 C  CB    . ARG A 1 332 ? 26.495  -3.291  -4.899  1.00 60.39  ? 331 ARG A CB    1 
ATOM   2638 C  CG    . ARG A 1 332 ? 27.053  -1.884  -4.812  1.00 62.42  ? 331 ARG A CG    1 
ATOM   2639 C  CD    . ARG A 1 332 ? 28.472  -1.781  -5.379  1.00 62.01  ? 331 ARG A CD    1 
ATOM   2640 N  NE    . ARG A 1 332 ? 28.957  -0.412  -5.271  1.00 51.00  ? 331 ARG A NE    1 
ATOM   2641 C  CZ    . ARG A 1 332 ? 29.926  -0.033  -4.449  1.00 52.50  ? 331 ARG A CZ    1 
ATOM   2642 N  NH1   . ARG A 1 332 ? 30.590  -0.908  -3.715  1.00 54.98  ? 331 ARG A NH1   1 
ATOM   2643 N  NH2   . ARG A 1 332 ? 30.217  1.259   -4.340  1.00 49.50  ? 331 ARG A NH2   1 
ATOM   2644 N  N     . LYS A 1 333 ? 23.444  -4.921  -5.402  1.00 75.00  ? 332 LYS A N     1 
ATOM   2645 C  CA    . LYS A 1 333 ? 22.518  -6.046  -5.313  1.00 76.56  ? 332 LYS A CA    1 
ATOM   2646 C  C     . LYS A 1 333 ? 21.742  -6.134  -6.614  1.00 77.98  ? 332 LYS A C     1 
ATOM   2647 O  O     . LYS A 1 333 ? 20.985  -5.217  -6.950  1.00 80.86  ? 332 LYS A O     1 
ATOM   2648 C  CB    . LYS A 1 333 ? 21.586  -5.878  -4.110  1.00 70.71  ? 332 LYS A CB    1 
ATOM   2649 C  CG    . LYS A 1 333 ? 20.318  -6.645  -4.246  1.00 69.57  ? 332 LYS A CG    1 
ATOM   2650 C  CD    . LYS A 1 333 ? 20.089  -7.628  -3.163  1.00 75.64  ? 332 LYS A CD    1 
ATOM   2651 C  CE    . LYS A 1 333 ? 19.011  -8.524  -3.680  1.00 81.55  ? 332 LYS A CE    1 
ATOM   2652 N  NZ    . LYS A 1 333 ? 19.346  -9.935  -3.485  1.00 76.73  ? 332 LYS A NZ    1 
ATOM   2653 N  N     . SER A 1 334 ? 21.924  -7.242  -7.332  1.00 80.97  ? 333 SER A N     1 
ATOM   2654 C  CA    . SER A 1 334 ? 21.542  -7.335  -8.735  1.00 81.24  ? 333 SER A CA    1 
ATOM   2655 C  C     . SER A 1 334 ? 20.086  -7.743  -8.947  1.00 87.74  ? 333 SER A C     1 
ATOM   2656 O  O     . SER A 1 334 ? 19.437  -7.229  -9.867  1.00 93.63  ? 333 SER A O     1 
ATOM   2657 C  CB    . SER A 1 334 ? 22.492  -8.300  -9.457  1.00 74.22  ? 333 SER A CB    1 
ATOM   2658 O  OG    . SER A 1 334 ? 22.053  -9.643  -9.377  1.00 77.28  ? 333 SER A OG    1 
ATOM   2659 N  N     . SER A 1 335 ? 19.543  -8.637  -8.121  1.00 86.79  ? 334 SER A N     1 
ATOM   2660 C  CA    . SER A 1 335 ? 18.186  -9.131  -8.333  1.00 93.84  ? 334 SER A CA    1 
ATOM   2661 C  C     . SER A 1 335 ? 17.468  -9.295  -7.001  1.00 88.42  ? 334 SER A C     1 
ATOM   2662 O  O     . SER A 1 335 ? 17.932  -10.034 -6.128  1.00 89.07  ? 334 SER A O     1 
ATOM   2663 C  CB    . SER A 1 335 ? 18.194  -10.468 -9.091  1.00 97.44  ? 334 SER A CB    1 
ATOM   2664 O  OG    . SER A 1 335 ? 19.118  -10.457 -10.169 1.00 94.80  ? 334 SER A OG    1 
ATOM   2665 N  N     . GLY A 1 336 ? 16.335  -8.612  -6.859  1.00 89.53  ? 335 GLY A N     1 
ATOM   2666 C  CA    . GLY A 1 336 ? 15.493  -8.753  -5.691  1.00 81.10  ? 335 GLY A CA    1 
ATOM   2667 C  C     . GLY A 1 336 ? 14.138  -9.292  -6.085  1.00 83.34  ? 335 GLY A C     1 
ATOM   2668 O  O     . GLY A 1 336 ? 14.052  -10.176 -6.947  1.00 86.46  ? 335 GLY A O     1 
ATOM   2669 N  N     . GLY A 1 337 ? 13.078  -8.763  -5.469  1.00 78.64  ? 336 GLY A N     1 
ATOM   2670 C  CA    . GLY A 1 337 ? 11.712  -9.100  -5.826  1.00 72.25  ? 336 GLY A CA    1 
ATOM   2671 C  C     . GLY A 1 337 ? 11.432  -10.579 -6.003  1.00 74.37  ? 336 GLY A C     1 
ATOM   2672 O  O     . GLY A 1 337 ? 11.425  -11.340 -5.028  1.00 69.05  ? 336 GLY A O     1 
ATOM   2673 N  N     . LEU A 1 338 ? 11.210  -11.000 -7.253  1.00 76.69  ? 337 LEU A N     1 
ATOM   2674 C  CA    . LEU A 1 338 ? 10.873  -12.397 -7.509  1.00 80.93  ? 337 LEU A CA    1 
ATOM   2675 C  C     . LEU A 1 338 ? 12.085  -13.309 -7.346  1.00 74.76  ? 337 LEU A C     1 
ATOM   2676 O  O     . LEU A 1 338 ? 11.936  -14.476 -6.961  1.00 71.52  ? 337 LEU A O     1 
ATOM   2677 C  CB    . LEU A 1 338 ? 10.261  -12.554 -8.908  1.00 81.28  ? 337 LEU A CB    1 
ATOM   2678 C  CG    . LEU A 1 338 ? 11.130  -12.321 -10.150 1.00 83.71  ? 337 LEU A CG    1 
ATOM   2679 C  CD1   . LEU A 1 338 ? 10.860  -13.403 -11.186 1.00 80.57  ? 337 LEU A CD1   1 
ATOM   2680 C  CD2   . LEU A 1 338 ? 10.899  -10.934 -10.750 1.00 84.95  ? 337 LEU A CD2   1 
ATOM   2681 N  N     . GLU A 1 339 ? 13.286  -12.802 -7.632  1.00 75.94  ? 338 GLU A N     1 
ATOM   2682 C  CA    . GLU A 1 339 ? 14.489  -13.601 -7.438  1.00 75.47  ? 338 GLU A CA    1 
ATOM   2683 C  C     . GLU A 1 339 ? 14.631  -14.020 -5.978  1.00 65.88  ? 338 GLU A C     1 
ATOM   2684 O  O     . GLU A 1 339 ? 14.746  -15.212 -5.663  1.00 62.84  ? 338 GLU A O     1 
ATOM   2685 C  CB    . GLU A 1 339 ? 15.715  -12.817 -7.909  1.00 72.69  ? 338 GLU A CB    1 
ATOM   2686 N  N     . ILE A 1 340 ? 14.589  -13.049 -5.065  1.00 62.67  ? 339 ILE A N     1 
ATOM   2687 C  CA    . ILE A 1 340 ? 14.800  -13.362 -3.655  1.00 60.99  ? 339 ILE A CA    1 
ATOM   2688 C  C     . ILE A 1 340 ? 13.676  -14.255 -3.137  1.00 57.99  ? 339 ILE A C     1 
ATOM   2689 O  O     . ILE A 1 340 ? 13.916  -15.221 -2.403  1.00 52.36  ? 339 ILE A O     1 
ATOM   2690 C  CB    . ILE A 1 340 ? 14.918  -12.064 -2.836  1.00 63.82  ? 339 ILE A CB    1 
ATOM   2691 C  CG1   . ILE A 1 340 ? 16.323  -11.479 -2.943  1.00 65.31  ? 339 ILE A CG1   1 
ATOM   2692 C  CG2   . ILE A 1 340 ? 14.671  -12.346 -1.374  1.00 61.75  ? 339 ILE A CG2   1 
ATOM   2693 C  CD1   . ILE A 1 340 ? 16.606  -10.397 -1.912  1.00 54.39  ? 339 ILE A CD1   1 
ATOM   2694 N  N     . ALA A 1 341 ? 12.434  -13.963 -3.536  1.00 59.30  ? 340 ALA A N     1 
ATOM   2695 C  CA    . ALA A 1 341 ? 11.292  -14.725 -3.041  1.00 56.17  ? 340 ALA A CA    1 
ATOM   2696 C  C     . ALA A 1 341 ? 11.425  -16.201 -3.386  1.00 54.55  ? 340 ALA A C     1 
ATOM   2697 O  O     . ALA A 1 341 ? 11.200  -17.073 -2.537  1.00 49.30  ? 340 ALA A O     1 
ATOM   2698 C  CB    . ALA A 1 341 ? 9.993   -14.152 -3.615  1.00 59.37  ? 340 ALA A CB    1 
ATOM   2699 N  N     . ARG A 1 342 ? 11.787  -16.499 -4.635  1.00 57.42  ? 341 ARG A N     1 
ATOM   2700 C  CA    . ARG A 1 342 ? 12.005  -17.884 -5.041  1.00 56.66  ? 341 ARG A CA    1 
ATOM   2701 C  C     . ARG A 1 342 ? 13.114  -18.529 -4.215  1.00 58.26  ? 341 ARG A C     1 
ATOM   2702 O  O     . ARG A 1 342 ? 12.955  -19.652 -3.714  1.00 55.14  ? 341 ARG A O     1 
ATOM   2703 C  CB    . ARG A 1 342 ? 12.339  -17.943 -6.531  1.00 61.76  ? 341 ARG A CB    1 
ATOM   2704 N  N     . ASN A 1 343 ? 14.251  -17.833 -4.065  1.00 51.46  ? 342 ASN A N     1 
ATOM   2705 C  CA    . ASN A 1 343 ? 15.329  -18.351 -3.221  1.00 50.04  ? 342 ASN A CA    1 
ATOM   2706 C  C     . ASN A 1 343 ? 14.850  -18.648 -1.812  1.00 45.43  ? 342 ASN A C     1 
ATOM   2707 O  O     . ASN A 1 343 ? 15.180  -19.693 -1.238  1.00 45.34  ? 342 ASN A O     1 
ATOM   2708 C  CB    . ASN A 1 343 ? 16.492  -17.375 -3.153  1.00 45.33  ? 342 ASN A CB    1 
ATOM   2709 C  CG    . ASN A 1 343 ? 17.560  -17.834 -2.157  1.00 57.04  ? 342 ASN A CG    1 
ATOM   2710 O  OD1   . ASN A 1 343 ? 17.938  -19.014 -2.121  1.00 56.32  ? 342 ASN A OD1   1 
ATOM   2711 N  ND2   . ASN A 1 343 ? 18.025  -16.908 -1.329  1.00 47.17  ? 342 ASN A ND2   1 
ATOM   2712 N  N     . ILE A 1 344 ? 14.088  -17.725 -1.224  1.00 50.19  ? 343 ILE A N     1 
ATOM   2713 C  CA    . ILE A 1 344 ? 13.621  -17.922 0.144   1.00 47.81  ? 343 ILE A CA    1 
ATOM   2714 C  C     . ILE A 1 344 ? 12.792  -19.193 0.228   1.00 42.36  ? 343 ILE A C     1 
ATOM   2715 O  O     . ILE A 1 344 ? 12.986  -20.030 1.123   1.00 46.48  ? 343 ILE A O     1 
ATOM   2716 C  CB    . ILE A 1 344 ? 12.833  -16.688 0.611   1.00 46.97  ? 343 ILE A CB    1 
ATOM   2717 C  CG1   . ILE A 1 344 ? 13.803  -15.529 0.860   1.00 47.98  ? 343 ILE A CG1   1 
ATOM   2718 C  CG2   . ILE A 1 344 ? 12.104  -16.988 1.886   1.00 39.24  ? 343 ILE A CG2   1 
ATOM   2719 C  CD1   . ILE A 1 344 ? 13.122  -14.247 1.324   1.00 47.24  ? 343 ILE A CD1   1 
ATOM   2720 N  N     . GLY A 1 345 ? 11.891  -19.381 -0.737  1.00 43.47  ? 344 GLY A N     1 
ATOM   2721 C  CA    . GLY A 1 345 ? 11.037  -20.557 -0.717  1.00 47.35  ? 344 GLY A CA    1 
ATOM   2722 C  C     . GLY A 1 345 ? 11.820  -21.848 -0.865  1.00 44.49  ? 344 GLY A C     1 
ATOM   2723 O  O     . GLY A 1 345 ? 11.604  -22.809 -0.123  1.00 41.95  ? 344 GLY A O     1 
ATOM   2724 N  N     . HIS A 1 346 ? 12.750  -21.881 -1.824  1.00 45.35  ? 345 HIS A N     1 
ATOM   2725 C  CA    . HIS A 1 346 ? 13.590  -23.064 -1.984  1.00 48.48  ? 345 HIS A CA    1 
ATOM   2726 C  C     . HIS A 1 346 ? 14.318  -23.401 -0.685  1.00 47.23  ? 345 HIS A C     1 
ATOM   2727 O  O     . HIS A 1 346 ? 14.265  -24.539 -0.205  1.00 51.73  ? 345 HIS A O     1 
ATOM   2728 C  CB    . HIS A 1 346 ? 14.592  -22.858 -3.118  1.00 46.17  ? 345 HIS A CB    1 
ATOM   2729 C  CG    . HIS A 1 346 ? 15.280  -24.121 -3.530  1.00 65.28  ? 345 HIS A CG    1 
ATOM   2730 N  ND1   . HIS A 1 346 ? 16.626  -24.340 -3.320  1.00 71.92  ? 345 HIS A ND1   1 
ATOM   2731 C  CD2   . HIS A 1 346 ? 14.805  -25.243 -4.120  1.00 69.84  ? 345 HIS A CD2   1 
ATOM   2732 C  CE1   . HIS A 1 346 ? 16.952  -25.538 -3.770  1.00 69.69  ? 345 HIS A CE1   1 
ATOM   2733 N  NE2   . HIS A 1 346 ? 15.865  -26.107 -4.260  1.00 68.22  ? 345 HIS A NE2   1 
ATOM   2734 N  N     . TYR A 1 347 ? 14.996  -22.413 -0.096  1.00 45.02  ? 346 TYR A N     1 
ATOM   2735 C  CA    . TYR A 1 347 ? 15.754  -22.661 1.123   1.00 38.44  ? 346 TYR A CA    1 
ATOM   2736 C  C     . TYR A 1 347 ? 14.842  -23.134 2.244   1.00 46.59  ? 346 TYR A C     1 
ATOM   2737 O  O     . TYR A 1 347 ? 15.139  -24.106 2.952   1.00 46.85  ? 346 TYR A O     1 
ATOM   2738 C  CB    . TYR A 1 347 ? 16.492  -21.385 1.530   1.00 43.38  ? 346 TYR A CB    1 
ATOM   2739 C  CG    . TYR A 1 347 ? 17.295  -21.512 2.807   1.00 42.84  ? 346 TYR A CG    1 
ATOM   2740 C  CD1   . TYR A 1 347 ? 16.705  -21.290 4.051   1.00 38.21  ? 346 TYR A CD1   1 
ATOM   2741 C  CD2   . TYR A 1 347 ? 18.659  -21.847 2.768   1.00 40.30  ? 346 TYR A CD2   1 
ATOM   2742 C  CE1   . TYR A 1 347 ? 17.437  -21.412 5.224   1.00 37.17  ? 346 TYR A CE1   1 
ATOM   2743 C  CE2   . TYR A 1 347 ? 19.392  -21.969 3.940   1.00 37.98  ? 346 TYR A CE2   1 
ATOM   2744 C  CZ    . TYR A 1 347 ? 18.777  -21.755 5.158   1.00 36.47  ? 346 TYR A CZ    1 
ATOM   2745 O  OH    . TYR A 1 347 ? 19.517  -21.867 6.303   1.00 35.71  ? 346 TYR A OH    1 
ATOM   2746 N  N     . LEU A 1 348 ? 13.711  -22.462 2.417   1.00 45.32  ? 347 LEU A N     1 
ATOM   2747 C  CA    . LEU A 1 348 ? 12.905  -22.742 3.592   1.00 48.84  ? 347 LEU A CA    1 
ATOM   2748 C  C     . LEU A 1 348 ? 12.196  -24.083 3.448   1.00 52.48  ? 347 LEU A C     1 
ATOM   2749 O  O     . LEU A 1 348 ? 12.021  -24.804 4.438   1.00 51.08  ? 347 LEU A O     1 
ATOM   2750 C  CB    . LEU A 1 348 ? 11.911  -21.610 3.803   1.00 47.23  ? 347 LEU A CB    1 
ATOM   2751 C  CG    . LEU A 1 348 ? 12.532  -20.511 4.677   1.00 43.55  ? 347 LEU A CG    1 
ATOM   2752 C  CD1   . LEU A 1 348 ? 11.668  -19.260 4.570   1.00 44.60  ? 347 LEU A CD1   1 
ATOM   2753 C  CD2   . LEU A 1 348 ? 12.786  -20.927 6.112   1.00 45.51  ? 347 LEU A CD2   1 
ATOM   2754 N  N     . GLU A 1 349 ? 11.811  -24.433 2.216   1.00 50.07  ? 348 GLU A N     1 
ATOM   2755 C  CA    . GLU A 1 349 ? 11.269  -25.758 1.916   1.00 56.77  ? 348 GLU A CA    1 
ATOM   2756 C  C     . GLU A 1 349 ? 12.150  -26.881 2.452   1.00 62.56  ? 348 GLU A C     1 
ATOM   2757 O  O     . GLU A 1 349 ? 11.642  -27.911 2.910   1.00 64.17  ? 348 GLU A O     1 
ATOM   2758 C  CB    . GLU A 1 349 ? 11.119  -25.910 0.405   1.00 55.68  ? 348 GLU A CB    1 
ATOM   2759 C  CG    . GLU A 1 349 ? 10.181  -26.994 -0.023  1.00 62.05  ? 348 GLU A CG    1 
ATOM   2760 C  CD    . GLU A 1 349 ? 8.758   -26.502 -0.063  1.00 69.59  ? 348 GLU A CD    1 
ATOM   2761 O  OE1   . GLU A 1 349 ? 8.395   -25.833 -1.057  1.00 76.50  ? 348 GLU A OE1   1 
ATOM   2762 O  OE2   . GLU A 1 349 ? 8.008   -26.769 0.900   1.00 71.46  ? 348 GLU A OE2   1 
ATOM   2763 N  N     . ARG A 1 350 ? 13.475  -26.711 2.387   1.00 57.92  ? 349 ARG A N     1 
ATOM   2764 C  CA    . ARG A 1 350 ? 14.396  -27.789 2.734   1.00 64.56  ? 349 ARG A CA    1 
ATOM   2765 C  C     . ARG A 1 350 ? 15.115  -27.530 4.049   1.00 65.77  ? 349 ARG A C     1 
ATOM   2766 O  O     . ARG A 1 350 ? 16.339  -27.682 4.139   1.00 73.42  ? 349 ARG A O     1 
ATOM   2767 C  CB    . ARG A 1 350 ? 15.404  -27.994 1.602   1.00 62.47  ? 349 ARG A CB    1 
ATOM   2768 C  CG    . ARG A 1 350 ? 14.697  -28.261 0.298   1.00 66.49  ? 349 ARG A CG    1 
ATOM   2769 C  CD    . ARG A 1 350 ? 15.520  -27.964 -0.942  1.00 64.16  ? 349 ARG A CD    1 
ATOM   2770 N  NE    . ARG A 1 350 ? 15.060  -28.769 -2.072  1.00 83.14  ? 349 ARG A NE    1 
ATOM   2771 C  CZ    . ARG A 1 350 ? 13.799  -28.860 -2.493  1.00 86.59  ? 349 ARG A CZ    1 
ATOM   2772 N  NH1   . ARG A 1 350 ? 12.845  -28.073 -2.018  1.00 78.84  ? 349 ARG A NH1   1 
ATOM   2773 N  NH2   . ARG A 1 350 ? 13.492  -29.742 -3.440  1.00 88.72  ? 349 ARG A NH2   1 
ATOM   2774 N  N     . VAL A 1 351 ? 14.360  -27.184 5.081   1.00 62.83  ? 350 VAL A N     1 
ATOM   2775 C  CA    . VAL A 1 351 ? 14.940  -26.685 6.314   1.00 64.70  ? 350 VAL A CA    1 
ATOM   2776 C  C     . VAL A 1 351 ? 14.876  -27.734 7.435   1.00 83.39  ? 350 VAL A C     1 
ATOM   2777 O  O     . VAL A 1 351 ? 13.899  -28.481 7.598   1.00 84.97  ? 350 VAL A O     1 
ATOM   2778 C  CB    . VAL A 1 351 ? 14.229  -25.384 6.729   1.00 70.19  ? 350 VAL A CB    1 
ATOM   2779 C  CG1   . VAL A 1 351 ? 12.895  -25.671 7.438   1.00 67.40  ? 350 VAL A CG1   1 
ATOM   2780 C  CG2   . VAL A 1 351 ? 15.128  -24.534 7.550   1.00 63.22  ? 350 VAL A CG2   1 
ATOM   2781 O  OXT   . VAL A 1 351 ? 15.818  -27.866 8.218   1.00 79.12  ? 350 VAL A OXT   1 
HETATM 2782 N  N1    . FMN B 2 .   ? 21.081  8.889   46.642  1.00 39.51  ? 401 FMN A N1    1 
HETATM 2783 C  C2    . FMN B 2 .   ? 20.659  10.139  47.039  1.00 43.19  ? 401 FMN A C2    1 
HETATM 2784 O  O2    . FMN B 2 .   ? 21.473  11.043  47.207  1.00 39.12  ? 401 FMN A O2    1 
HETATM 2785 N  N3    . FMN B 2 .   ? 19.322  10.393  47.256  1.00 41.11  ? 401 FMN A N3    1 
HETATM 2786 C  C4    . FMN B 2 .   ? 18.383  9.392   47.057  1.00 39.70  ? 401 FMN A C4    1 
HETATM 2787 O  O4    . FMN B 2 .   ? 17.188  9.623   47.257  1.00 36.20  ? 401 FMN A O4    1 
HETATM 2788 C  C4A   . FMN B 2 .   ? 18.798  8.132   46.649  1.00 38.67  ? 401 FMN A C4A   1 
HETATM 2789 N  N5    . FMN B 2 .   ? 17.876  7.126   46.452  1.00 34.76  ? 401 FMN A N5    1 
HETATM 2790 C  C5A   . FMN B 2 .   ? 18.298  5.875   46.042  1.00 39.09  ? 401 FMN A C5A   1 
HETATM 2791 C  C6    . FMN B 2 .   ? 17.384  4.854   45.836  1.00 37.73  ? 401 FMN A C6    1 
HETATM 2792 C  C7    . FMN B 2 .   ? 17.810  3.590   45.432  1.00 38.70  ? 401 FMN A C7    1 
HETATM 2793 C  C7M   . FMN B 2 .   ? 16.809  2.491   45.216  1.00 37.73  ? 401 FMN A C7M   1 
HETATM 2794 C  C8    . FMN B 2 .   ? 19.161  3.351   45.214  1.00 41.00  ? 401 FMN A C8    1 
HETATM 2795 C  C8M   . FMN B 2 .   ? 19.623  1.989   44.775  1.00 42.06  ? 401 FMN A C8M   1 
HETATM 2796 C  C9    . FMN B 2 .   ? 20.080  4.374   45.416  1.00 40.46  ? 401 FMN A C9    1 
HETATM 2797 C  C9A   . FMN B 2 .   ? 19.656  5.631   45.831  1.00 38.28  ? 401 FMN A C9A   1 
HETATM 2798 N  N10   . FMN B 2 .   ? 20.572  6.640   46.020  1.00 41.28  ? 401 FMN A N10   1 
HETATM 2799 C  C10   . FMN B 2 .   ? 20.156  7.887   46.435  1.00 43.58  ? 401 FMN A C10   1 
HETATM 2800 C  "C1'" . FMN B 2 .   ? 22.035  6.334   45.845  1.00 46.87  ? 401 FMN A "C1'" 1 
HETATM 2801 C  "C2'" . FMN B 2 .   ? 22.804  7.013   44.739  1.00 50.85  ? 401 FMN A "C2'" 1 
HETATM 2802 O  "O2'" . FMN B 2 .   ? 22.661  6.120   43.654  1.00 44.10  ? 401 FMN A "O2'" 1 
HETATM 2803 C  "C3'" . FMN B 2 .   ? 24.275  7.182   45.189  1.00 49.03  ? 401 FMN A "C3'" 1 
HETATM 2804 O  "O3'" . FMN B 2 .   ? 24.810  5.928   45.565  1.00 47.52  ? 401 FMN A "O3'" 1 
HETATM 2805 C  "C4'" . FMN B 2 .   ? 24.439  8.129   46.389  1.00 52.56  ? 401 FMN A "C4'" 1 
HETATM 2806 O  "O4'" . FMN B 2 .   ? 23.720  9.326   46.182  1.00 54.13  ? 401 FMN A "O4'" 1 
HETATM 2807 C  "C5'" . FMN B 2 .   ? 25.895  8.484   46.735  1.00 65.85  ? 401 FMN A "C5'" 1 
HETATM 2808 O  "O5'" . FMN B 2 .   ? 26.399  9.560   45.953  1.00 75.48  ? 401 FMN A "O5'" 1 
HETATM 2809 P  P     . FMN B 2 .   ? 27.491  10.651  46.494  1.00 119.81 ? 401 FMN A P     1 
HETATM 2810 O  O1P   . FMN B 2 .   ? 26.771  11.639  47.391  1.00 92.94  ? 401 FMN A O1P   1 
HETATM 2811 O  O2P   . FMN B 2 .   ? 28.626  10.006  47.273  1.00 95.16  ? 401 FMN A O2P   1 
HETATM 2812 O  O3P   . FMN B 2 .   ? 28.099  11.419  45.335  1.00 89.44  ? 401 FMN A O3P   1 
HETATM 2813 C  C1    . GOL C 3 .   ? 1.600   14.467  35.371  1.00 60.46  ? 402 GOL A C1    1 
HETATM 2814 O  O1    . GOL C 3 .   ? 2.367   15.291  36.219  1.00 66.37  ? 402 GOL A O1    1 
HETATM 2815 C  C2    . GOL C 3 .   ? 2.534   13.362  34.752  1.00 64.58  ? 402 GOL A C2    1 
HETATM 2816 O  O2    . GOL C 3 .   ? 3.891   13.467  35.126  1.00 61.85  ? 402 GOL A O2    1 
HETATM 2817 C  C3    . GOL C 3 .   ? 1.893   12.007  35.160  1.00 56.66  ? 402 GOL A C3    1 
HETATM 2818 O  O3    . GOL C 3 .   ? 0.559   12.069  34.786  1.00 66.85  ? 402 GOL A O3    1 
HETATM 2819 CA CA    . CA  D 4 .   ? 12.986  13.470  -11.294 1.00 37.71  ? 403 CA  A CA    1 
HETATM 2820 CA CA    . CA  E 4 .   ? 6.639   -7.232  3.457   1.00 56.11  ? 404 CA  A CA    1 
HETATM 2821 O  O     . HOH F 5 .   ? 21.466  13.130  57.995  0.65 39.03  ? 501 HOH A O     1 
HETATM 2822 O  O     . HOH F 5 .   ? -4.701  6.274   2.782   1.00 36.88  ? 502 HOH A O     1 
HETATM 2823 O  O     . HOH F 5 .   ? 6.878   5.370   20.712  1.00 61.73  ? 503 HOH A O     1 
HETATM 2824 O  O     . HOH F 5 .   ? 5.247   15.721  60.309  1.00 65.51  ? 504 HOH A O     1 
HETATM 2825 O  O     . HOH F 5 .   ? 6.563   14.887  22.412  1.00 64.16  ? 505 HOH A O     1 
HETATM 2826 O  O     . HOH F 5 .   ? 20.065  -0.387  -7.881  1.00 64.03  ? 506 HOH A O     1 
HETATM 2827 O  O     . HOH F 5 .   ? 16.955  24.917  48.915  1.00 72.24  ? 507 HOH A O     1 
HETATM 2828 O  O     . HOH F 5 .   ? 19.852  -3.383  -7.652  1.00 54.23  ? 508 HOH A O     1 
HETATM 2829 O  O     . HOH F 5 .   ? 27.556  14.330  52.377  1.00 70.26  ? 509 HOH A O     1 
HETATM 2830 O  O     . HOH F 5 .   ? 10.818  -30.008 3.277   1.00 66.13  ? 510 HOH A O     1 
HETATM 2831 O  O     . HOH F 5 .   ? 6.937   15.449  1.199   1.00 70.21  ? 511 HOH A O     1 
HETATM 2832 O  O     . HOH F 5 .   ? -3.434  -10.023 43.698  1.00 43.97  ? 512 HOH A O     1 
HETATM 2833 O  O     . HOH F 5 .   ? 2.631   21.731  41.474  1.00 64.01  ? 513 HOH A O     1 
HETATM 2834 O  O     . HOH F 5 .   ? -4.879  11.669  1.798   1.00 43.80  ? 514 HOH A O     1 
HETATM 2835 O  O     . HOH F 5 .   ? 27.632  13.180  49.006  1.00 72.43  ? 515 HOH A O     1 
HETATM 2836 O  O     . HOH F 5 .   ? 23.085  15.942  45.857  1.00 51.61  ? 516 HOH A O     1 
HETATM 2837 O  O     . HOH F 5 .   ? 17.938  -20.101 14.010  1.00 43.03  ? 517 HOH A O     1 
HETATM 2838 O  O     . HOH F 5 .   ? 10.737  16.128  16.066  1.00 53.50  ? 518 HOH A O     1 
HETATM 2839 O  O     . HOH F 5 .   ? 1.996   3.817   18.318  1.00 55.30  ? 519 HOH A O     1 
HETATM 2840 O  O     . HOH F 5 .   ? 25.234  -2.169  14.124  1.00 54.27  ? 520 HOH A O     1 
HETATM 2841 O  O     . HOH F 5 .   ? 24.630  -4.836  -7.604  1.00 68.50  ? 521 HOH A O     1 
HETATM 2842 O  O     . HOH F 5 .   ? 7.886   16.968  19.263  1.00 66.49  ? 522 HOH A O     1 
HETATM 2843 O  O     . HOH F 5 .   ? 20.529  -16.094 2.307   1.00 39.44  ? 523 HOH A O     1 
HETATM 2844 O  O     . HOH F 5 .   ? 27.777  -29.393 7.837   1.00 64.02  ? 524 HOH A O     1 
HETATM 2845 O  O     . HOH F 5 .   ? 22.579  16.422  1.863   1.00 58.75  ? 525 HOH A O     1 
HETATM 2846 O  O     . HOH F 5 .   ? 22.896  -5.220  60.923  1.00 74.29  ? 526 HOH A O     1 
HETATM 2847 O  O     . HOH F 5 .   ? 5.757   12.483  41.370  1.00 40.50  ? 527 HOH A O     1 
HETATM 2848 O  O     . HOH F 5 .   ? 12.415  15.015  -5.953  1.00 34.73  ? 528 HOH A O     1 
HETATM 2849 O  O     . HOH F 5 .   ? 28.200  -25.048 10.038  1.00 63.07  ? 529 HOH A O     1 
HETATM 2850 O  O     . HOH F 5 .   ? 12.172  -3.177  58.875  1.00 57.35  ? 530 HOH A O     1 
HETATM 2851 O  O     . HOH F 5 .   ? 2.653   12.855  44.031  1.00 55.55  ? 531 HOH A O     1 
HETATM 2852 O  O     . HOH F 5 .   ? 25.056  15.616  1.984   1.00 53.26  ? 532 HOH A O     1 
HETATM 2853 O  O     . HOH F 5 .   ? 23.636  -8.997  13.754  1.00 41.53  ? 533 HOH A O     1 
HETATM 2854 O  O     . HOH F 5 .   ? 27.577  13.149  -0.461  1.00 35.74  ? 534 HOH A O     1 
HETATM 2855 O  O     . HOH F 5 .   ? 23.575  16.139  48.831  1.00 41.53  ? 535 HOH A O     1 
HETATM 2856 O  O     . HOH F 5 .   ? 25.248  -19.015 15.378  1.00 45.02  ? 536 HOH A O     1 
HETATM 2857 O  O     . HOH F 5 .   ? -3.185  -9.380  57.808  1.00 46.46  ? 537 HOH A O     1 
HETATM 2858 O  O     . HOH F 5 .   ? 4.568   -5.583  4.695   1.00 35.50  ? 538 HOH A O     1 
HETATM 2859 O  O     . HOH F 5 .   ? 20.136  -7.914  56.425  1.00 54.96  ? 539 HOH A O     1 
HETATM 2860 O  O     . HOH F 5 .   ? 2.987   19.710  38.992  1.00 66.61  ? 540 HOH A O     1 
HETATM 2861 O  O     . HOH F 5 .   ? 6.601   -10.221 52.850  1.00 54.60  ? 541 HOH A O     1 
HETATM 2862 O  O     . HOH F 5 .   ? 13.157  9.629   -13.881 1.00 30.59  ? 542 HOH A O     1 
HETATM 2863 O  O     . HOH F 5 .   ? 8.898   8.007   32.318  1.00 57.75  ? 543 HOH A O     1 
HETATM 2864 O  O     . HOH F 5 .   ? 21.144  -6.773  4.727   1.00 30.80  ? 544 HOH A O     1 
HETATM 2865 O  O     . HOH F 5 .   ? 7.655   -10.091 50.817  1.00 61.86  ? 545 HOH A O     1 
HETATM 2866 O  O     . HOH F 5 .   ? 24.388  -7.842  53.659  1.00 54.34  ? 546 HOH A O     1 
HETATM 2867 O  O     . HOH F 5 .   ? 9.611   12.750  1.277   1.00 31.92  ? 547 HOH A O     1 
HETATM 2868 O  O     . HOH F 5 .   ? 23.203  14.920  55.957  1.00 40.31  ? 548 HOH A O     1 
HETATM 2869 O  O     . HOH F 5 .   ? 1.588   -11.485 23.611  1.00 57.63  ? 549 HOH A O     1 
HETATM 2870 O  O     . HOH F 5 .   ? -6.531  9.550   2.658   1.00 44.78  ? 550 HOH A O     1 
HETATM 2871 O  O     . HOH F 5 .   ? 11.196  11.608  16.860  1.00 47.78  ? 551 HOH A O     1 
HETATM 2872 O  O     . HOH F 5 .   ? 32.449  1.292   -2.789  1.00 47.82  ? 552 HOH A O     1 
HETATM 2873 O  O     . HOH F 5 .   ? 21.832  15.227  12.395  1.00 64.90  ? 553 HOH A O     1 
HETATM 2874 O  O     . HOH F 5 .   ? 2.602   -5.282  6.739   1.00 36.62  ? 554 HOH A O     1 
HETATM 2875 O  O     . HOH F 5 .   ? 10.438  -2.218  1.745   1.00 44.95  ? 555 HOH A O     1 
HETATM 2876 O  O     . HOH F 5 .   ? 16.148  5.914   55.533  1.00 43.17  ? 556 HOH A O     1 
HETATM 2877 O  O     . HOH F 5 .   ? 26.903  3.313   13.076  1.00 54.31  ? 557 HOH A O     1 
HETATM 2878 O  O     . HOH F 5 .   ? 20.186  11.153  57.571  1.00 45.18  ? 558 HOH A O     1 
HETATM 2879 O  O     . HOH F 5 .   ? 17.624  -9.651  54.765  1.00 55.82  ? 559 HOH A O     1 
HETATM 2880 O  O     . HOH F 5 .   ? -3.958  -12.493 55.278  1.00 60.43  ? 560 HOH A O     1 
HETATM 2881 O  O     . HOH F 5 .   ? -0.025  13.182  9.527   1.00 47.22  ? 561 HOH A O     1 
HETATM 2882 O  O     . HOH F 5 .   ? 11.706  14.745  -9.874  1.00 35.92  ? 562 HOH A O     1 
HETATM 2883 O  O     . HOH F 5 .   ? 1.229   -0.035  60.191  1.00 52.73  ? 563 HOH A O     1 
HETATM 2884 O  O     . HOH F 5 .   ? 13.180  -12.441 4.189   1.00 35.44  ? 564 HOH A O     1 
HETATM 2885 O  O     . HOH F 5 .   ? 23.594  -12.718 3.372   1.00 36.91  ? 565 HOH A O     1 
HETATM 2886 O  O     . HOH F 5 .   ? 15.678  -3.010  55.496  1.00 46.70  ? 566 HOH A O     1 
HETATM 2887 O  O     . HOH F 5 .   ? 15.849  16.982  53.757  1.00 43.32  ? 567 HOH A O     1 
HETATM 2888 O  O     . HOH F 5 .   ? 28.856  -29.033 10.053  1.00 73.74  ? 568 HOH A O     1 
HETATM 2889 O  O     . HOH F 5 .   ? 6.679   -5.673  43.954  1.00 48.28  ? 569 HOH A O     1 
HETATM 2890 O  O     . HOH F 5 .   ? 15.215  11.035  56.671  1.00 33.70  ? 570 HOH A O     1 
HETATM 2891 O  O     . HOH F 5 .   ? 27.137  21.659  54.245  1.00 66.38  ? 571 HOH A O     1 
HETATM 2892 O  O     . HOH F 5 .   ? 16.430  14.793  58.217  1.00 50.74  ? 572 HOH A O     1 
HETATM 2893 O  O     . HOH F 5 .   ? 15.237  -4.964  20.604  1.00 50.88  ? 573 HOH A O     1 
HETATM 2894 O  O     . HOH F 5 .   ? 15.539  11.676  15.948  1.00 39.72  ? 574 HOH A O     1 
HETATM 2895 O  O     . HOH F 5 .   ? 15.360  -8.677  50.183  1.00 58.46  ? 575 HOH A O     1 
HETATM 2896 O  O     . HOH F 5 .   ? -5.039  7.080   0.876   1.00 42.59  ? 576 HOH A O     1 
HETATM 2897 O  O     . HOH F 5 .   ? 2.401   -6.769  56.402  1.00 44.40  ? 577 HOH A O     1 
HETATM 2898 O  O     . HOH F 5 .   ? 16.766  -9.627  47.435  1.00 53.67  ? 578 HOH A O     1 
HETATM 2899 O  O     . HOH F 5 .   ? 27.594  -0.616  14.528  1.00 64.20  ? 579 HOH A O     1 
HETATM 2900 O  O     . HOH F 5 .   ? -12.070 10.945  21.392  1.00 54.87  ? 580 HOH A O     1 
HETATM 2901 O  O     . HOH F 5 .   ? 5.888   -5.180  61.025  1.00 54.34  ? 581 HOH A O     1 
HETATM 2902 O  O     . HOH F 5 .   ? 2.544   -1.855  17.234  1.00 39.50  ? 582 HOH A O     1 
HETATM 2903 O  O     . HOH F 5 .   ? 3.636   -2.787  -2.045  1.00 46.87  ? 583 HOH A O     1 
HETATM 2904 O  O     . HOH F 5 .   ? 27.820  6.576   2.497   1.00 38.60  ? 584 HOH A O     1 
HETATM 2905 O  O     . HOH F 5 .   ? 7.684   12.810  -0.481  1.00 58.57  ? 585 HOH A O     1 
HETATM 2906 O  O     . HOH F 5 .   ? 25.813  -24.780 12.033  1.00 51.42  ? 586 HOH A O     1 
HETATM 2907 O  O     . HOH F 5 .   ? 20.942  15.033  9.434   1.00 48.98  ? 587 HOH A O     1 
HETATM 2908 O  O     . HOH F 5 .   ? 28.877  9.203   56.270  1.00 42.28  ? 588 HOH A O     1 
HETATM 2909 O  O     . HOH F 5 .   ? 13.238  -5.539  -0.439  1.00 61.25  ? 589 HOH A O     1 
HETATM 2910 O  O     . HOH F 5 .   ? 11.085  20.442  54.575  1.00 55.82  ? 590 HOH A O     1 
HETATM 2911 O  O     . HOH F 5 .   ? 14.346  14.034  35.522  1.00 62.24  ? 591 HOH A O     1 
HETATM 2912 O  O     . HOH F 5 .   ? -11.770 8.686   29.950  1.00 74.58  ? 592 HOH A O     1 
HETATM 2913 O  O     . HOH F 5 .   ? 27.130  10.927  -3.893  1.00 44.27  ? 593 HOH A O     1 
HETATM 2914 O  O     . HOH F 5 .   ? 8.030   -9.395  -0.756  1.00 53.42  ? 594 HOH A O     1 
HETATM 2915 O  O     . HOH F 5 .   ? 11.049  14.107  -1.676  1.00 44.08  ? 595 HOH A O     1 
HETATM 2916 O  O     . HOH F 5 .   ? 24.032  0.410   -4.915  1.00 52.06  ? 596 HOH A O     1 
HETATM 2917 O  O     . HOH F 5 .   ? -2.194  -2.955  60.825  1.00 40.63  ? 597 HOH A O     1 
HETATM 2918 O  O     . HOH F 5 .   ? -0.351  -6.573  12.354  1.00 30.05  ? 598 HOH A O     1 
HETATM 2919 O  O     . HOH F 5 .   ? 11.355  7.006   32.860  1.00 48.41  ? 599 HOH A O     1 
HETATM 2920 O  O     . HOH F 5 .   ? 21.448  8.727   57.636  1.00 39.67  ? 600 HOH A O     1 
HETATM 2921 O  O     . HOH F 5 .   ? 24.637  15.189  11.699  1.00 63.72  ? 601 HOH A O     1 
HETATM 2922 O  O     . HOH F 5 .   ? 14.668  12.987  -12.922 1.00 35.81  ? 602 HOH A O     1 
HETATM 2923 O  O     . HOH F 5 .   ? 18.504  -7.239  4.381   1.00 32.98  ? 603 HOH A O     1 
HETATM 2924 O  O     . HOH F 5 .   ? 18.300  11.235  15.826  1.00 50.02  ? 604 HOH A O     1 
HETATM 2925 O  O     . HOH F 5 .   ? 14.236  5.313   -13.971 1.00 45.04  ? 605 HOH A O     1 
HETATM 2926 O  O     . HOH F 5 .   ? 27.260  14.309  45.807  1.00 65.02  ? 606 HOH A O     1 
HETATM 2927 O  O     . HOH F 5 .   ? 12.053  12.724  19.239  1.00 73.24  ? 607 HOH A O     1 
HETATM 2928 O  O     . HOH F 5 .   ? -0.752  2.909   -2.316  1.00 50.80  ? 608 HOH A O     1 
HETATM 2929 O  O     . HOH F 5 .   ? 17.296  -5.579  58.023  1.00 64.57  ? 609 HOH A O     1 
HETATM 2930 O  O     . HOH F 5 .   ? 7.131   14.022  56.481  1.00 47.29  ? 610 HOH A O     1 
HETATM 2931 O  O     . HOH F 5 .   ? 14.640  -7.325  52.790  1.00 58.96  ? 611 HOH A O     1 
HETATM 2932 O  O     . HOH F 5 .   ? 9.483   -0.394  3.279   1.00 43.49  ? 612 HOH A O     1 
HETATM 2933 O  O     . HOH F 5 .   ? -3.198  9.739   -7.994  1.00 66.20  ? 613 HOH A O     1 
HETATM 2934 O  O     . HOH F 5 .   ? 18.308  13.506  59.603  1.00 54.59  ? 614 HOH A O     1 
HETATM 2935 O  O     . HOH F 5 .   ? 28.371  3.878   2.609   1.00 53.54  ? 615 HOH A O     1 
HETATM 2936 O  O     . HOH F 5 .   ? 11.378  -0.578  57.426  1.00 51.53  ? 616 HOH A O     1 
HETATM 2937 O  O     . HOH F 5 .   ? 17.286  19.598  55.015  1.00 58.59  ? 617 HOH A O     1 
HETATM 2938 O  O     . HOH F 5 .   ? 14.031  15.537  -11.298 1.00 45.22  ? 618 HOH A O     1 
HETATM 2939 O  O     . HOH F 5 .   ? 11.288  17.784  14.261  1.00 59.38  ? 619 HOH A O     1 
HETATM 2940 O  O     . HOH F 5 .   ? 25.714  14.796  56.716  1.00 52.33  ? 620 HOH A O     1 
HETATM 2941 O  O     . HOH F 5 .   ? 31.274  -4.056  -3.973  1.00 70.31  ? 621 HOH A O     1 
HETATM 2942 O  O     . HOH F 5 .   ? 18.502  17.382  61.707  1.00 52.72  ? 622 HOH A O     1 
HETATM 2943 O  O     . HOH F 5 .   ? 24.103  7.935   18.683  1.00 66.15  ? 623 HOH A O     1 
HETATM 2944 O  O     . HOH F 5 .   ? 12.770  10.866  18.333  1.00 59.70  ? 624 HOH A O     1 
HETATM 2945 O  O     . HOH F 5 .   ? 13.826  17.332  56.586  1.00 53.61  ? 625 HOH A O     1 
HETATM 2946 O  O     . HOH F 5 .   ? 1.161   23.047  14.889  1.00 50.81  ? 626 HOH A O     1 
HETATM 2947 O  O     . HOH F 5 .   ? 3.664   -13.141 45.154  1.00 72.08  ? 627 HOH A O     1 
HETATM 2948 O  O     . HOH F 5 .   ? 5.113   14.516  57.702  1.00 61.82  ? 628 HOH A O     1 
HETATM 2949 O  O     . HOH F 5 .   ? 19.596  15.791  14.047  1.00 57.59  ? 629 HOH A O     1 
HETATM 2950 O  O     . HOH F 5 .   ? 26.485  1.178   43.497  1.00 66.87  ? 630 HOH A O     1 
HETATM 2951 O  O     . HOH F 5 .   ? 19.995  14.589  15.648  1.00 60.58  ? 631 HOH A O     1 
HETATM 2952 O  O     . HOH F 5 .   ? 31.134  -0.572  1.722   1.00 61.77  ? 632 HOH A O     1 
HETATM 2953 O  O     . HOH F 5 .   ? 17.939  21.069  56.536  1.00 63.08  ? 633 HOH A O     1 
HETATM 2954 O  O     . HOH F 5 .   ? 0.786   -10.703 44.592  1.00 58.37  ? 634 HOH A O     1 
HETATM 2955 O  O     . HOH F 5 .   ? 20.178  17.616  -6.001  1.00 72.30  ? 635 HOH A O     1 
HETATM 2956 O  O     . HOH F 5 .   ? 13.663  -14.840 18.891  1.00 49.70  ? 636 HOH A O     1 
HETATM 2957 O  O     . HOH F 5 .   ? 7.711   -6.869  62.568  1.00 74.07  ? 637 HOH A O     1 
HETATM 2958 O  O     . HOH F 5 .   ? 12.658  -5.430  30.885  1.00 77.73  ? 638 HOH A O     1 
HETATM 2959 O  O     . HOH F 5 .   ? 24.752  4.332   55.139  1.00 53.82  ? 639 HOH A O     1 
HETATM 2960 O  O     . HOH F 5 .   ? 0.912   19.230  8.436   1.00 67.38  ? 640 HOH A O     1 
HETATM 2961 O  O     . HOH F 5 .   ? 12.500  -3.920  29.193  1.00 69.02  ? 641 HOH A O     1 
HETATM 2962 O  O     . HOH F 5 .   ? 27.018  15.166  47.812  1.00 71.43  ? 642 HOH A O     1 
HETATM 2963 O  O     . HOH F 5 .   ? -0.191  23.890  16.991  1.00 57.64  ? 643 HOH A O     1 
HETATM 2964 O  O     . HOH F 5 .   ? 31.758  1.186   0.077   1.00 50.69  ? 644 HOH A O     1 
HETATM 2965 O  O     . HOH F 5 .   ? 27.212  -2.332  11.780  1.00 63.85  ? 645 HOH A O     1 
HETATM 2966 O  O     . HOH F 5 .   ? 21.715  -5.481  1.733   1.00 56.26  ? 646 HOH A O     1 
HETATM 2967 O  O     . HOH F 5 .   ? 14.299  -8.990  54.149  1.00 62.71  ? 647 HOH A O     1 
HETATM 2968 O  O     . HOH F 5 .   ? -3.830  -10.624 56.250  1.00 57.66  ? 648 HOH A O     1 
HETATM 2969 O  O     . HOH F 5 .   ? 5.402   -27.568 6.119   1.00 67.90  ? 649 HOH A O     1 
HETATM 2970 O  O     . HOH F 5 .   ? 22.865  -0.147  36.024  1.00 65.56  ? 650 HOH A O     1 
HETATM 2971 O  O     . HOH F 5 .   ? 15.108  -5.718  -1.375  1.00 60.69  ? 651 HOH A O     1 
HETATM 2972 O  O     . HOH F 5 .   ? 22.590  9.564   18.351  1.00 58.64  ? 652 HOH A O     1 
HETATM 2973 O  O     . HOH F 5 .   ? 2.764   -25.016 8.290   1.00 70.47  ? 653 HOH A O     1 
HETATM 2974 O  O     . HOH F 5 .   ? 29.182  20.938  54.351  1.00 60.57  ? 654 HOH A O     1 
HETATM 2975 O  O     . HOH F 5 .   ? 24.405  2.102   57.172  1.00 57.66  ? 655 HOH A O     1 
HETATM 2976 O  O     . HOH F 5 .   ? 2.251   -10.529 51.696  1.00 57.86  ? 656 HOH A O     1 
HETATM 2977 O  O     . HOH F 5 .   ? 4.736   12.091  57.841  1.00 53.51  ? 657 HOH A O     1 
HETATM 2978 O  O     . HOH F 5 .   ? 19.870  -6.264  19.001  1.00 63.35  ? 658 HOH A O     1 
HETATM 2979 O  O     . HOH F 5 .   ? 26.010  6.685   18.034  1.00 70.33  ? 659 HOH A O     1 
HETATM 2980 O  O     . HOH F 5 .   ? 4.268   26.012  7.963   1.00 68.04  ? 660 HOH A O     1 
HETATM 2981 O  O     . HOH F 5 .   ? 3.375   -9.983  49.495  1.00 57.70  ? 661 HOH A O     1 
HETATM 2982 O  O     . HOH F 5 .   ? -4.179  8.663   -1.053  1.00 62.93  ? 662 HOH A O     1 
HETATM 2983 O  O     . HOH F 5 .   ? 9.941   17.943  18.082  1.00 63.71  ? 663 HOH A O     1 
HETATM 2984 O  O     . HOH F 5 .   ? 25.130  20.677  10.236  1.00 66.28  ? 664 HOH A O     1 
HETATM 2985 O  O     . HOH F 5 .   ? -4.628  6.746   -5.883  1.00 61.37  ? 665 HOH A O     1 
HETATM 2986 O  O     . HOH F 5 .   ? 9.901   16.091  20.208  1.00 67.82  ? 666 HOH A O     1 
HETATM 2987 O  O     . HOH F 5 .   ? 29.219  -3.377  16.466  1.00 66.61  ? 667 HOH A O     1 
HETATM 2988 O  O     . HOH F 5 .   ? 19.589  -18.679 16.079  1.00 46.53  ? 668 HOH A O     1 
HETATM 2989 O  O     . HOH F 5 .   ? 19.811  13.261  17.692  1.00 61.05  ? 669 HOH A O     1 
HETATM 2990 O  O     . HOH F 5 .   ? 19.589  -6.872  0.223   1.00 62.98  ? 670 HOH A O     1 
HETATM 2991 O  O     . HOH F 5 .   ? -0.000  0.000   -3.767  0.50 52.69  ? 671 HOH A O     1 
# 
