data_8XWW
# 
_entry.id   8XWW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8XWW         pdb_00008xww 10.2210/pdb8xww/pdb 
WWPDB D_1300044304 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XWW 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 wyinuo3@mail.sysu.edu.cn Yinuo   Wu    ? 'principal investigator/group leader' 0000-0003-3071-5333 
6 hbluo@hainanu.edu.cn     Hai-Bin Luo   ? 'principal investigator/group leader' 0000-0002-2163-0509 
7 742646380@qq.com         Yi-You  Huang ? 'principal investigator/group leader' 0000-0002-0712-1310 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, F.C.' 1 0009-0007-0307-5584 
'Huang, Y.Y.' 2 0000-0002-0712-1310 
'Luo, H.B.'   3 0000-0002-2163-0509 
'Wu, Y.Y.'    4 0000-0003-3071-5333 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Discovery of Highly Potent and Selective PDE5 Inhibitors for the Treatment of Idiopathic Pulmonary Fibrosis' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhang, F.C.' 1 0009-0007-0307-5584 
primary 'Huang, Y.Y.' 2 0000-0002-0712-1310 
primary 'Luo, H.B.'   3 0000-0002-2163-0509 
primary 'Wu, Y.Y.'    4 0000-0003-3071-5333 
# 
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 
;Isoform PDE5A1 of cGMP-specific 3',5'-cyclic phosphodiesterase
;
40266.242 1  3.1.4.35 ? ? ? 
2 non-polymer syn '2-[(3-chlorophenyl)methyl]-4-oxidanylidene-3~{H}-quinazoline-7-carboxylic acid' 314.723   1  ?        ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                       65.409    1  ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                  24.305    1  ?        ? ? ? 
5 water       nat water                                                                            18.015    67 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'cGMP-binding cGMP-specific phosphodiesterase,CGB-PDE' 
# 
_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       
;SYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNY
RKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHF
DQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLS
AITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGC
RKNRQKWQALAEQQEKMLINGESGQAKRN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNY
RKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHF
DQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLS
AITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGC
RKNRQKWQALAEQQEKMLINGESGQAKRN
;
_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 '2-[(3-chlorophenyl)methyl]-4-oxidanylidene-3~{H}-quinazoline-7-carboxylic acid' A1D5K 
3 'ZINC ION'                                                                       ZN    
4 'MAGNESIUM ION'                                                                  MG    
5 water                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   TYR n 
1 3   HIS n 
1 4   ALA n 
1 5   SER n 
1 6   ALA n 
1 7   ALA n 
1 8   GLU n 
1 9   GLU n 
1 10  GLU n 
1 11  THR n 
1 12  ARG n 
1 13  GLU n 
1 14  LEU n 
1 15  GLN n 
1 16  SER n 
1 17  LEU n 
1 18  ALA n 
1 19  ALA n 
1 20  ALA n 
1 21  VAL n 
1 22  VAL n 
1 23  PRO n 
1 24  SER n 
1 25  ALA n 
1 26  GLN n 
1 27  THR n 
1 28  LEU n 
1 29  LYS n 
1 30  ILE n 
1 31  THR n 
1 32  ASP n 
1 33  PHE n 
1 34  SER n 
1 35  PHE n 
1 36  SER n 
1 37  ASP n 
1 38  PHE n 
1 39  GLU n 
1 40  LEU n 
1 41  SER n 
1 42  ASP n 
1 43  LEU n 
1 44  GLU n 
1 45  THR n 
1 46  ALA n 
1 47  LEU n 
1 48  CYS n 
1 49  THR n 
1 50  ILE n 
1 51  ARG n 
1 52  MET n 
1 53  PHE n 
1 54  THR n 
1 55  ASP n 
1 56  LEU n 
1 57  ASN n 
1 58  LEU n 
1 59  VAL n 
1 60  GLN n 
1 61  ASN n 
1 62  PHE n 
1 63  GLN n 
1 64  MET n 
1 65  LYS n 
1 66  HIS n 
1 67  GLU n 
1 68  VAL n 
1 69  LEU n 
1 70  CYS n 
1 71  ARG n 
1 72  TRP n 
1 73  ILE n 
1 74  LEU n 
1 75  SER n 
1 76  VAL n 
1 77  LYS n 
1 78  LYS n 
1 79  ASN n 
1 80  TYR n 
1 81  ARG n 
1 82  LYS n 
1 83  ASN n 
1 84  VAL n 
1 85  ALA n 
1 86  TYR n 
1 87  HIS n 
1 88  ASN n 
1 89  TRP n 
1 90  ARG n 
1 91  HIS n 
1 92  ALA n 
1 93  PHE n 
1 94  ASN n 
1 95  THR n 
1 96  ALA n 
1 97  GLN n 
1 98  CYS n 
1 99  MET n 
1 100 PHE n 
1 101 ALA n 
1 102 ALA n 
1 103 LEU n 
1 104 LYS n 
1 105 ALA n 
1 106 GLY n 
1 107 LYS n 
1 108 ILE n 
1 109 GLN n 
1 110 ASN n 
1 111 LYS n 
1 112 LEU n 
1 113 THR n 
1 114 ASP n 
1 115 LEU n 
1 116 GLU n 
1 117 ILE n 
1 118 LEU n 
1 119 ALA n 
1 120 LEU n 
1 121 LEU n 
1 122 ILE n 
1 123 ALA n 
1 124 ALA n 
1 125 LEU n 
1 126 SER n 
1 127 HIS n 
1 128 ASP n 
1 129 LEU n 
1 130 ASP n 
1 131 HIS n 
1 132 ARG n 
1 133 GLY n 
1 134 VAL n 
1 135 ASN n 
1 136 ASN n 
1 137 SER n 
1 138 TYR n 
1 139 ILE n 
1 140 GLN n 
1 141 ARG n 
1 142 SER n 
1 143 GLU n 
1 144 HIS n 
1 145 PRO n 
1 146 LEU n 
1 147 ALA n 
1 148 GLN n 
1 149 LEU n 
1 150 TYR n 
1 151 CYS n 
1 152 HIS n 
1 153 SER n 
1 154 ILE n 
1 155 MET n 
1 156 GLU n 
1 157 HIS n 
1 158 HIS n 
1 159 HIS n 
1 160 PHE n 
1 161 ASP n 
1 162 GLN n 
1 163 CYS n 
1 164 LEU n 
1 165 MET n 
1 166 ILE n 
1 167 LEU n 
1 168 ASN n 
1 169 SER n 
1 170 PRO n 
1 171 GLY n 
1 172 ASN n 
1 173 GLN n 
1 174 ILE n 
1 175 LEU n 
1 176 SER n 
1 177 GLY n 
1 178 LEU n 
1 179 SER n 
1 180 ILE n 
1 181 GLU n 
1 182 GLU n 
1 183 TYR n 
1 184 LYS n 
1 185 THR n 
1 186 THR n 
1 187 LEU n 
1 188 LYS n 
1 189 ILE n 
1 190 ILE n 
1 191 LYS n 
1 192 GLN n 
1 193 ALA n 
1 194 ILE n 
1 195 LEU n 
1 196 ALA n 
1 197 THR n 
1 198 ASP n 
1 199 LEU n 
1 200 ALA n 
1 201 LEU n 
1 202 TYR n 
1 203 ILE n 
1 204 LYS n 
1 205 ARG n 
1 206 ARG n 
1 207 GLY n 
1 208 GLU n 
1 209 PHE n 
1 210 PHE n 
1 211 GLU n 
1 212 LEU n 
1 213 ILE n 
1 214 ARG n 
1 215 LYS n 
1 216 ASN n 
1 217 GLN n 
1 218 PHE n 
1 219 ASN n 
1 220 LEU n 
1 221 GLU n 
1 222 ASP n 
1 223 PRO n 
1 224 HIS n 
1 225 GLN n 
1 226 LYS n 
1 227 GLU n 
1 228 LEU n 
1 229 PHE n 
1 230 LEU n 
1 231 ALA n 
1 232 MET n 
1 233 LEU n 
1 234 MET n 
1 235 THR n 
1 236 ALA n 
1 237 CYS n 
1 238 ASP n 
1 239 LEU n 
1 240 SER n 
1 241 ALA n 
1 242 ILE n 
1 243 THR n 
1 244 LYS n 
1 245 PRO n 
1 246 TRP n 
1 247 PRO n 
1 248 ILE n 
1 249 GLN n 
1 250 GLN n 
1 251 ARG n 
1 252 ILE n 
1 253 ALA n 
1 254 GLU n 
1 255 LEU n 
1 256 VAL n 
1 257 ALA n 
1 258 THR n 
1 259 GLU n 
1 260 PHE n 
1 261 PHE n 
1 262 ASP n 
1 263 GLN n 
1 264 GLY n 
1 265 ASP n 
1 266 ARG n 
1 267 GLU n 
1 268 ARG n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 ASN n 
1 273 ILE n 
1 274 GLU n 
1 275 PRO n 
1 276 THR n 
1 277 ASP n 
1 278 LEU n 
1 279 MET n 
1 280 ASN n 
1 281 ARG n 
1 282 GLU n 
1 283 LYS n 
1 284 LYS n 
1 285 ASN n 
1 286 LYS n 
1 287 ILE n 
1 288 PRO n 
1 289 SER n 
1 290 MET n 
1 291 GLN n 
1 292 VAL n 
1 293 GLY n 
1 294 PHE n 
1 295 ILE n 
1 296 ASP n 
1 297 ALA n 
1 298 ILE n 
1 299 CYS n 
1 300 LEU n 
1 301 GLN n 
1 302 LEU n 
1 303 TYR n 
1 304 GLU n 
1 305 ALA n 
1 306 LEU n 
1 307 THR n 
1 308 HIS n 
1 309 VAL n 
1 310 SER n 
1 311 GLU n 
1 312 ASP n 
1 313 CYS n 
1 314 PHE n 
1 315 PRO n 
1 316 LEU n 
1 317 LEU n 
1 318 ASP n 
1 319 GLY n 
1 320 CYS n 
1 321 ARG n 
1 322 LYS n 
1 323 ASN n 
1 324 ARG n 
1 325 GLN n 
1 326 LYS n 
1 327 TRP n 
1 328 GLN n 
1 329 ALA n 
1 330 LEU n 
1 331 ALA n 
1 332 GLU n 
1 333 GLN n 
1 334 GLN n 
1 335 GLU n 
1 336 LYS n 
1 337 MET n 
1 338 LEU n 
1 339 ILE n 
1 340 ASN n 
1 341 GLY n 
1 342 GLU n 
1 343 SER n 
1 344 GLY n 
1 345 GLN n 
1 346 ALA n 
1 347 LYS n 
1 348 ARG n 
1 349 ASN 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                   349 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PDE5A, PDE5' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1D5K non-polymer         . '2-[(3-chlorophenyl)methyl]-4-oxidanylidene-3~{H}-quinazoline-7-carboxylic acid' ? 'C16 H11 Cl N2 O3' 
314.723 
ALA   'L-peptide linking' y ALANINE                                                                          ? 'C3 H7 N O2'       
89.093  
ARG   'L-peptide linking' y ARGININE                                                                         ? 'C6 H15 N4 O2 1'   
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                       ? 'C4 H8 N2 O3'      
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                  ? 'C4 H7 N O4'       
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                         ? 'C3 H7 N O2 S'     
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'     
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'       
147.129 
GLY   'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'       
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1'   
156.162 
HOH   non-polymer         . WATER                                                                            ? 'H2 O'             
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                       ? 'C6 H13 N O2'      
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                          ? 'C6 H13 N O2'      
131.173 
LYS   'L-peptide linking' y LYSINE                                                                           ? 'C6 H15 N2 O2 1'   
147.195 
MET   'L-peptide linking' y METHIONINE                                                                       ? 'C5 H11 N O2 S'    
149.211 
MG    non-polymer         . 'MAGNESIUM ION'                                                                  ? 'Mg 2'             
24.305  
PHE   'L-peptide linking' y PHENYLALANINE                                                                    ? 'C9 H11 N O2'      
165.189 
PRO   'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'       
115.130 
SER   'L-peptide linking' y SERINE                                                                           ? 'C3 H7 N O3'       
105.093 
THR   'L-peptide linking' y THREONINE                                                                        ? 'C4 H9 N O3'       
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                       ? 'C11 H12 N2 O2'    
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                         ? 'C9 H11 N O3'      
181.189 
VAL   'L-peptide linking' y VALINE                                                                           ? 'C5 H11 N O2'      
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                       ? 'Zn 2'             
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   527 ?   ?   ?   A . n 
A 1 2   TYR 2   528 ?   ?   ?   A . n 
A 1 3   HIS 3   529 ?   ?   ?   A . n 
A 1 4   ALA 4   530 ?   ?   ?   A . n 
A 1 5   SER 5   531 ?   ?   ?   A . n 
A 1 6   ALA 6   532 ?   ?   ?   A . n 
A 1 7   ALA 7   533 ?   ?   ?   A . n 
A 1 8   GLU 8   534 ?   ?   ?   A . n 
A 1 9   GLU 9   535 ?   ?   ?   A . n 
A 1 10  GLU 10  536 ?   ?   ?   A . n 
A 1 11  THR 11  537 537 THR THR A . n 
A 1 12  ARG 12  538 538 ARG ARG A . n 
A 1 13  GLU 13  539 539 GLU GLU A . n 
A 1 14  LEU 14  540 540 LEU LEU A . n 
A 1 15  GLN 15  541 541 GLN GLN A . n 
A 1 16  SER 16  542 542 SER SER A . n 
A 1 17  LEU 17  543 543 LEU LEU A . n 
A 1 18  ALA 18  544 544 ALA ALA A . n 
A 1 19  ALA 19  545 545 ALA ALA A . n 
A 1 20  ALA 20  546 546 ALA ALA A . n 
A 1 21  VAL 21  547 547 VAL VAL A . n 
A 1 22  VAL 22  548 548 VAL VAL A . n 
A 1 23  PRO 23  549 549 PRO PRO A . n 
A 1 24  SER 24  550 550 SER SER A . n 
A 1 25  ALA 25  551 551 ALA ALA A . n 
A 1 26  GLN 26  552 552 GLN GLN A . n 
A 1 27  THR 27  553 553 THR THR A . n 
A 1 28  LEU 28  554 554 LEU LEU A . n 
A 1 29  LYS 29  555 555 LYS LYS A . n 
A 1 30  ILE 30  556 556 ILE ILE A . n 
A 1 31  THR 31  557 557 THR THR A . n 
A 1 32  ASP 32  558 558 ASP ASP A . n 
A 1 33  PHE 33  559 559 PHE PHE A . n 
A 1 34  SER 34  560 560 SER SER A . n 
A 1 35  PHE 35  561 561 PHE PHE A . n 
A 1 36  SER 36  562 562 SER SER A . n 
A 1 37  ASP 37  563 563 ASP ASP A . n 
A 1 38  PHE 38  564 564 PHE PHE A . n 
A 1 39  GLU 39  565 565 GLU GLU A . n 
A 1 40  LEU 40  566 566 LEU LEU A . n 
A 1 41  SER 41  567 567 SER SER A . n 
A 1 42  ASP 42  568 568 ASP ASP A . n 
A 1 43  LEU 43  569 569 LEU LEU A . n 
A 1 44  GLU 44  570 570 GLU GLU A . n 
A 1 45  THR 45  571 571 THR THR A . n 
A 1 46  ALA 46  572 572 ALA ALA A . n 
A 1 47  LEU 47  573 573 LEU LEU A . n 
A 1 48  CYS 48  574 574 CYS CYS A . n 
A 1 49  THR 49  575 575 THR THR A . n 
A 1 50  ILE 50  576 576 ILE ILE A . n 
A 1 51  ARG 51  577 577 ARG ARG A . n 
A 1 52  MET 52  578 578 MET MET A . n 
A 1 53  PHE 53  579 579 PHE PHE A . n 
A 1 54  THR 54  580 580 THR THR A . n 
A 1 55  ASP 55  581 581 ASP ASP A . n 
A 1 56  LEU 56  582 582 LEU LEU A . n 
A 1 57  ASN 57  583 583 ASN ASN A . n 
A 1 58  LEU 58  584 584 LEU LEU A . n 
A 1 59  VAL 59  585 585 VAL VAL A . n 
A 1 60  GLN 60  586 586 GLN GLN A . n 
A 1 61  ASN 61  587 587 ASN ASN A . n 
A 1 62  PHE 62  588 588 PHE PHE A . n 
A 1 63  GLN 63  589 589 GLN GLN A . n 
A 1 64  MET 64  590 590 MET MET A . n 
A 1 65  LYS 65  591 591 LYS LYS A . n 
A 1 66  HIS 66  592 592 HIS HIS A . n 
A 1 67  GLU 67  593 593 GLU GLU A . n 
A 1 68  VAL 68  594 594 VAL VAL A . n 
A 1 69  LEU 69  595 595 LEU LEU A . n 
A 1 70  CYS 70  596 596 CYS CYS A . n 
A 1 71  ARG 71  597 597 ARG ARG A . n 
A 1 72  TRP 72  598 598 TRP TRP A . n 
A 1 73  ILE 73  599 599 ILE ILE A . n 
A 1 74  LEU 74  600 600 LEU LEU A . n 
A 1 75  SER 75  601 601 SER SER A . n 
A 1 76  VAL 76  602 602 VAL VAL A . n 
A 1 77  LYS 77  603 603 LYS LYS A . n 
A 1 78  LYS 78  604 604 LYS LYS A . n 
A 1 79  ASN 79  605 605 ASN ASN A . n 
A 1 80  TYR 80  606 606 TYR TYR A . n 
A 1 81  ARG 81  607 607 ARG ARG A . n 
A 1 82  LYS 82  608 608 LYS LYS A . n 
A 1 83  ASN 83  609 609 ASN ASN A . n 
A 1 84  VAL 84  610 610 VAL VAL A . n 
A 1 85  ALA 85  611 611 ALA ALA A . n 
A 1 86  TYR 86  612 612 TYR TYR A . n 
A 1 87  HIS 87  613 613 HIS HIS A . n 
A 1 88  ASN 88  614 614 ASN ASN A . n 
A 1 89  TRP 89  615 615 TRP TRP A . n 
A 1 90  ARG 90  616 616 ARG ARG A . n 
A 1 91  HIS 91  617 617 HIS HIS A . n 
A 1 92  ALA 92  618 618 ALA ALA A . n 
A 1 93  PHE 93  619 619 PHE PHE A . n 
A 1 94  ASN 94  620 620 ASN ASN A . n 
A 1 95  THR 95  621 621 THR THR A . n 
A 1 96  ALA 96  622 622 ALA ALA A . n 
A 1 97  GLN 97  623 623 GLN GLN A . n 
A 1 98  CYS 98  624 624 CYS CYS A . n 
A 1 99  MET 99  625 625 MET MET A . n 
A 1 100 PHE 100 626 626 PHE PHE A . n 
A 1 101 ALA 101 627 627 ALA ALA A . n 
A 1 102 ALA 102 628 628 ALA ALA A . n 
A 1 103 LEU 103 629 629 LEU LEU A . n 
A 1 104 LYS 104 630 630 LYS LYS A . n 
A 1 105 ALA 105 631 631 ALA ALA A . n 
A 1 106 GLY 106 632 632 GLY GLY A . n 
A 1 107 LYS 107 633 633 LYS LYS A . n 
A 1 108 ILE 108 634 634 ILE ILE A . n 
A 1 109 GLN 109 635 635 GLN GLN A . n 
A 1 110 ASN 110 636 636 ASN ASN A . n 
A 1 111 LYS 111 637 637 LYS LYS A . n 
A 1 112 LEU 112 638 638 LEU LEU A . n 
A 1 113 THR 113 639 639 THR THR A . n 
A 1 114 ASP 114 640 640 ASP ASP A . n 
A 1 115 LEU 115 641 641 LEU LEU A . n 
A 1 116 GLU 116 642 642 GLU GLU A . n 
A 1 117 ILE 117 643 643 ILE ILE A . n 
A 1 118 LEU 118 644 644 LEU LEU A . n 
A 1 119 ALA 119 645 645 ALA ALA A . n 
A 1 120 LEU 120 646 646 LEU LEU A . n 
A 1 121 LEU 121 647 647 LEU LEU A . n 
A 1 122 ILE 122 648 648 ILE ILE A . n 
A 1 123 ALA 123 649 649 ALA ALA A . n 
A 1 124 ALA 124 650 650 ALA ALA A . n 
A 1 125 LEU 125 651 651 LEU LEU A . n 
A 1 126 SER 126 652 652 SER SER A . n 
A 1 127 HIS 127 653 653 HIS HIS A . n 
A 1 128 ASP 128 654 654 ASP ASP A . n 
A 1 129 LEU 129 655 655 LEU LEU A . n 
A 1 130 ASP 130 656 656 ASP ASP A . n 
A 1 131 HIS 131 657 657 HIS HIS A . n 
A 1 132 ARG 132 658 658 ARG ARG A . n 
A 1 133 GLY 133 659 659 GLY GLY A . n 
A 1 134 VAL 134 660 660 VAL VAL A . n 
A 1 135 ASN 135 661 661 ASN ASN A . n 
A 1 136 ASN 136 662 662 ASN ASN A . n 
A 1 137 SER 137 663 663 SER SER A . n 
A 1 138 TYR 138 664 664 TYR TYR A . n 
A 1 139 ILE 139 665 665 ILE ILE A . n 
A 1 140 GLN 140 666 666 GLN GLN A . n 
A 1 141 ARG 141 667 ?   ?   ?   A . n 
A 1 142 SER 142 668 ?   ?   ?   A . n 
A 1 143 GLU 143 669 ?   ?   ?   A . n 
A 1 144 HIS 144 670 ?   ?   ?   A . n 
A 1 145 PRO 145 671 ?   ?   ?   A . n 
A 1 146 LEU 146 672 ?   ?   ?   A . n 
A 1 147 ALA 147 673 ?   ?   ?   A . n 
A 1 148 GLN 148 674 ?   ?   ?   A . n 
A 1 149 LEU 149 675 ?   ?   ?   A . n 
A 1 150 TYR 150 676 ?   ?   ?   A . n 
A 1 151 CYS 151 677 ?   ?   ?   A . n 
A 1 152 HIS 152 678 678 HIS HIS A . n 
A 1 153 SER 153 679 679 SER SER A . n 
A 1 154 ILE 154 680 680 ILE ILE A . n 
A 1 155 MET 155 681 681 MET MET A . n 
A 1 156 GLU 156 682 682 GLU GLU A . n 
A 1 157 HIS 157 683 683 HIS HIS A . n 
A 1 158 HIS 158 684 684 HIS HIS A . n 
A 1 159 HIS 159 685 685 HIS HIS A . n 
A 1 160 PHE 160 686 686 PHE PHE A . n 
A 1 161 ASP 161 687 687 ASP ASP A . n 
A 1 162 GLN 162 688 688 GLN GLN A . n 
A 1 163 CYS 163 689 689 CYS CYS A . n 
A 1 164 LEU 164 690 690 LEU LEU A . n 
A 1 165 MET 165 691 691 MET MET A . n 
A 1 166 ILE 166 692 692 ILE ILE A . n 
A 1 167 LEU 167 693 693 LEU LEU A . n 
A 1 168 ASN 168 694 694 ASN ASN A . n 
A 1 169 SER 169 695 695 SER SER A . n 
A 1 170 PRO 170 696 696 PRO PRO A . n 
A 1 171 GLY 171 697 697 GLY GLY A . n 
A 1 172 ASN 172 698 698 ASN ASN A . n 
A 1 173 GLN 173 699 699 GLN GLN A . n 
A 1 174 ILE 174 700 700 ILE ILE A . n 
A 1 175 LEU 175 701 701 LEU LEU A . n 
A 1 176 SER 176 702 702 SER SER A . n 
A 1 177 GLY 177 703 703 GLY GLY A . n 
A 1 178 LEU 178 704 704 LEU LEU A . n 
A 1 179 SER 179 705 705 SER SER A . n 
A 1 180 ILE 180 706 706 ILE ILE A . n 
A 1 181 GLU 181 707 707 GLU GLU A . n 
A 1 182 GLU 182 708 708 GLU GLU A . n 
A 1 183 TYR 183 709 709 TYR TYR A . n 
A 1 184 LYS 184 710 710 LYS LYS A . n 
A 1 185 THR 185 711 711 THR THR A . n 
A 1 186 THR 186 712 712 THR THR A . n 
A 1 187 LEU 187 713 713 LEU LEU A . n 
A 1 188 LYS 188 714 714 LYS LYS A . n 
A 1 189 ILE 189 715 715 ILE ILE A . n 
A 1 190 ILE 190 716 716 ILE ILE A . n 
A 1 191 LYS 191 717 717 LYS LYS A . n 
A 1 192 GLN 192 718 718 GLN GLN A . n 
A 1 193 ALA 193 719 719 ALA ALA A . n 
A 1 194 ILE 194 720 720 ILE ILE A . n 
A 1 195 LEU 195 721 721 LEU LEU A . n 
A 1 196 ALA 196 722 722 ALA ALA A . n 
A 1 197 THR 197 723 723 THR THR A . n 
A 1 198 ASP 198 724 724 ASP ASP A . n 
A 1 199 LEU 199 725 725 LEU LEU A . n 
A 1 200 ALA 200 726 726 ALA ALA A . n 
A 1 201 LEU 201 727 727 LEU LEU A . n 
A 1 202 TYR 202 728 728 TYR TYR A . n 
A 1 203 ILE 203 729 729 ILE ILE A . n 
A 1 204 LYS 204 730 730 LYS LYS A . n 
A 1 205 ARG 205 731 731 ARG ARG A . n 
A 1 206 ARG 206 732 732 ARG ARG A . n 
A 1 207 GLY 207 733 733 GLY GLY A . n 
A 1 208 GLU 208 734 734 GLU GLU A . n 
A 1 209 PHE 209 735 735 PHE PHE A . n 
A 1 210 PHE 210 736 736 PHE PHE A . n 
A 1 211 GLU 211 737 737 GLU GLU A . n 
A 1 212 LEU 212 738 738 LEU LEU A . n 
A 1 213 ILE 213 739 739 ILE ILE A . n 
A 1 214 ARG 214 740 740 ARG ARG A . n 
A 1 215 LYS 215 741 741 LYS LYS A . n 
A 1 216 ASN 216 742 742 ASN ASN A . n 
A 1 217 GLN 217 743 743 GLN GLN A . n 
A 1 218 PHE 218 744 744 PHE PHE A . n 
A 1 219 ASN 219 745 745 ASN ASN A . n 
A 1 220 LEU 220 746 746 LEU LEU A . n 
A 1 221 GLU 221 747 747 GLU GLU A . n 
A 1 222 ASP 222 748 748 ASP ASP A . n 
A 1 223 PRO 223 749 749 PRO PRO A . n 
A 1 224 HIS 224 750 750 HIS HIS A . n 
A 1 225 GLN 225 751 751 GLN GLN A . n 
A 1 226 LYS 226 752 752 LYS LYS A . n 
A 1 227 GLU 227 753 753 GLU GLU A . n 
A 1 228 LEU 228 754 754 LEU LEU A . n 
A 1 229 PHE 229 755 755 PHE PHE A . n 
A 1 230 LEU 230 756 756 LEU LEU A . n 
A 1 231 ALA 231 757 757 ALA ALA A . n 
A 1 232 MET 232 758 758 MET MET A . n 
A 1 233 LEU 233 759 759 LEU LEU A . n 
A 1 234 MET 234 760 760 MET MET A . n 
A 1 235 THR 235 761 761 THR THR A . n 
A 1 236 ALA 236 762 762 ALA ALA A . n 
A 1 237 CYS 237 763 763 CYS CYS A . n 
A 1 238 ASP 238 764 764 ASP ASP A . n 
A 1 239 LEU 239 765 765 LEU LEU A . n 
A 1 240 SER 240 766 766 SER SER A . n 
A 1 241 ALA 241 767 767 ALA ALA A . n 
A 1 242 ILE 242 768 768 ILE ILE A . n 
A 1 243 THR 243 769 769 THR THR A . n 
A 1 244 LYS 244 770 770 LYS LYS A . n 
A 1 245 PRO 245 771 771 PRO PRO A . n 
A 1 246 TRP 246 772 772 TRP TRP A . n 
A 1 247 PRO 247 773 773 PRO PRO A . n 
A 1 248 ILE 248 774 774 ILE ILE A . n 
A 1 249 GLN 249 775 775 GLN GLN A . n 
A 1 250 GLN 250 776 776 GLN GLN A . n 
A 1 251 ARG 251 777 777 ARG ARG A . n 
A 1 252 ILE 252 778 778 ILE ILE A . n 
A 1 253 ALA 253 779 779 ALA ALA A . n 
A 1 254 GLU 254 780 780 GLU GLU A . n 
A 1 255 LEU 255 781 781 LEU LEU A . n 
A 1 256 VAL 256 782 782 VAL VAL A . n 
A 1 257 ALA 257 783 783 ALA ALA A . n 
A 1 258 THR 258 784 784 THR THR A . n 
A 1 259 GLU 259 785 785 GLU GLU A . n 
A 1 260 PHE 260 786 786 PHE PHE A . n 
A 1 261 PHE 261 787 787 PHE PHE A . n 
A 1 262 ASP 262 788 788 ASP ASP A . n 
A 1 263 GLN 263 789 789 GLN GLN A . n 
A 1 264 GLY 264 790 790 GLY GLY A . n 
A 1 265 ASP 265 791 ?   ?   ?   A . n 
A 1 266 ARG 266 792 ?   ?   ?   A . n 
A 1 267 GLU 267 793 ?   ?   ?   A . n 
A 1 268 ARG 268 794 ?   ?   ?   A . n 
A 1 269 LYS 269 795 ?   ?   ?   A . n 
A 1 270 GLU 270 796 ?   ?   ?   A . n 
A 1 271 LEU 271 797 ?   ?   ?   A . n 
A 1 272 ASN 272 798 ?   ?   ?   A . n 
A 1 273 ILE 273 799 ?   ?   ?   A . n 
A 1 274 GLU 274 800 ?   ?   ?   A . n 
A 1 275 PRO 275 801 ?   ?   ?   A . n 
A 1 276 THR 276 802 ?   ?   ?   A . n 
A 1 277 ASP 277 803 ?   ?   ?   A . n 
A 1 278 LEU 278 804 ?   ?   ?   A . n 
A 1 279 MET 279 805 ?   ?   ?   A . n 
A 1 280 ASN 280 806 ?   ?   ?   A . n 
A 1 281 ARG 281 807 ?   ?   ?   A . n 
A 1 282 GLU 282 808 ?   ?   ?   A . n 
A 1 283 LYS 283 809 ?   ?   ?   A . n 
A 1 284 LYS 284 810 ?   ?   ?   A . n 
A 1 285 ASN 285 811 811 ASN ASN A . n 
A 1 286 LYS 286 812 812 LYS LYS A . n 
A 1 287 ILE 287 813 813 ILE ILE A . n 
A 1 288 PRO 288 814 814 PRO PRO A . n 
A 1 289 SER 289 815 815 SER SER A . n 
A 1 290 MET 290 816 816 MET MET A . n 
A 1 291 GLN 291 817 817 GLN GLN A . n 
A 1 292 VAL 292 818 818 VAL VAL A . n 
A 1 293 GLY 293 819 819 GLY GLY A . n 
A 1 294 PHE 294 820 820 PHE PHE A . n 
A 1 295 ILE 295 821 821 ILE ILE A . n 
A 1 296 ASP 296 822 822 ASP ASP A . n 
A 1 297 ALA 297 823 823 ALA ALA A . n 
A 1 298 ILE 298 824 824 ILE ILE A . n 
A 1 299 CYS 299 825 825 CYS CYS A . n 
A 1 300 LEU 300 826 826 LEU LEU A . n 
A 1 301 GLN 301 827 827 GLN GLN A . n 
A 1 302 LEU 302 828 828 LEU LEU A . n 
A 1 303 TYR 303 829 829 TYR TYR A . n 
A 1 304 GLU 304 830 830 GLU GLU A . n 
A 1 305 ALA 305 831 831 ALA ALA A . n 
A 1 306 LEU 306 832 832 LEU LEU A . n 
A 1 307 THR 307 833 833 THR THR A . n 
A 1 308 HIS 308 834 834 HIS HIS A . n 
A 1 309 VAL 309 835 835 VAL VAL A . n 
A 1 310 SER 310 836 836 SER SER A . n 
A 1 311 GLU 311 837 837 GLU GLU A . n 
A 1 312 ASP 312 838 838 ASP ASP A . n 
A 1 313 CYS 313 839 839 CYS CYS A . n 
A 1 314 PHE 314 840 840 PHE PHE A . n 
A 1 315 PRO 315 841 841 PRO PRO A . n 
A 1 316 LEU 316 842 842 LEU LEU A . n 
A 1 317 LEU 317 843 843 LEU LEU A . n 
A 1 318 ASP 318 844 844 ASP ASP A . n 
A 1 319 GLY 319 845 845 GLY GLY A . n 
A 1 320 CYS 320 846 846 CYS CYS A . n 
A 1 321 ARG 321 847 847 ARG ARG A . n 
A 1 322 LYS 322 848 848 LYS LYS A . n 
A 1 323 ASN 323 849 849 ASN ASN A . n 
A 1 324 ARG 324 850 850 ARG ARG A . n 
A 1 325 GLN 325 851 851 GLN GLN A . n 
A 1 326 LYS 326 852 852 LYS LYS A . n 
A 1 327 TRP 327 853 853 TRP TRP A . n 
A 1 328 GLN 328 854 854 GLN GLN A . n 
A 1 329 ALA 329 855 855 ALA ALA A . n 
A 1 330 LEU 330 856 856 LEU LEU A . n 
A 1 331 ALA 331 857 857 ALA ALA A . n 
A 1 332 GLU 332 858 858 GLU GLU A . n 
A 1 333 GLN 333 859 859 GLN GLN A . n 
A 1 334 GLN 334 860 ?   ?   ?   A . n 
A 1 335 GLU 335 861 ?   ?   ?   A . n 
A 1 336 LYS 336 862 ?   ?   ?   A . n 
A 1 337 MET 337 863 ?   ?   ?   A . n 
A 1 338 LEU 338 864 ?   ?   ?   A . n 
A 1 339 ILE 339 865 ?   ?   ?   A . n 
A 1 340 ASN 340 866 ?   ?   ?   A . n 
A 1 341 GLY 341 867 ?   ?   ?   A . n 
A 1 342 GLU 342 868 ?   ?   ?   A . n 
A 1 343 SER 343 869 ?   ?   ?   A . n 
A 1 344 GLY 344 870 ?   ?   ?   A . n 
A 1 345 GLN 345 871 ?   ?   ?   A . n 
A 1 346 ALA 346 872 ?   ?   ?   A . n 
A 1 347 LYS 347 873 ?   ?   ?   A . n 
A 1 348 ARG 348 874 ?   ?   ?   A . n 
A 1 349 ASN 349 875 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D5K 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D5K 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1D5K 1  901  901 A1D5K HC0 A . 
C 3 ZN    1  902  1   ZN    ZN  A . 
D 4 MG    1  903  1   MG    MG  A . 
E 5 HOH   1  1001 22  HOH   HOH A . 
E 5 HOH   2  1002 33  HOH   HOH A . 
E 5 HOH   3  1003 65  HOH   HOH A . 
E 5 HOH   4  1004 28  HOH   HOH A . 
E 5 HOH   5  1005 5   HOH   HOH A . 
E 5 HOH   6  1006 61  HOH   HOH A . 
E 5 HOH   7  1007 25  HOH   HOH A . 
E 5 HOH   8  1008 31  HOH   HOH A . 
E 5 HOH   9  1009 60  HOH   HOH A . 
E 5 HOH   10 1010 53  HOH   HOH A . 
E 5 HOH   11 1011 9   HOH   HOH A . 
E 5 HOH   12 1012 8   HOH   HOH A . 
E 5 HOH   13 1013 19  HOH   HOH A . 
E 5 HOH   14 1014 24  HOH   HOH A . 
E 5 HOH   15 1015 11  HOH   HOH A . 
E 5 HOH   16 1016 20  HOH   HOH A . 
E 5 HOH   17 1017 39  HOH   HOH A . 
E 5 HOH   18 1018 34  HOH   HOH A . 
E 5 HOH   19 1019 64  HOH   HOH A . 
E 5 HOH   20 1020 3   HOH   HOH A . 
E 5 HOH   21 1021 67  HOH   HOH A . 
E 5 HOH   22 1022 16  HOH   HOH A . 
E 5 HOH   23 1023 15  HOH   HOH A . 
E 5 HOH   24 1024 41  HOH   HOH A . 
E 5 HOH   25 1025 68  HOH   HOH A . 
E 5 HOH   26 1026 4   HOH   HOH A . 
E 5 HOH   27 1027 49  HOH   HOH A . 
E 5 HOH   28 1028 37  HOH   HOH A . 
E 5 HOH   29 1029 1   HOH   HOH A . 
E 5 HOH   30 1030 58  HOH   HOH A . 
E 5 HOH   31 1031 21  HOH   HOH A . 
E 5 HOH   32 1032 43  HOH   HOH A . 
E 5 HOH   33 1033 54  HOH   HOH A . 
E 5 HOH   34 1034 12  HOH   HOH A . 
E 5 HOH   35 1035 30  HOH   HOH A . 
E 5 HOH   36 1036 14  HOH   HOH A . 
E 5 HOH   37 1037 17  HOH   HOH A . 
E 5 HOH   38 1038 26  HOH   HOH A . 
E 5 HOH   39 1039 2   HOH   HOH A . 
E 5 HOH   40 1040 6   HOH   HOH A . 
E 5 HOH   41 1041 63  HOH   HOH A . 
E 5 HOH   42 1042 40  HOH   HOH A . 
E 5 HOH   43 1043 45  HOH   HOH A . 
E 5 HOH   44 1044 59  HOH   HOH A . 
E 5 HOH   45 1045 13  HOH   HOH A . 
E 5 HOH   46 1046 18  HOH   HOH A . 
E 5 HOH   47 1047 62  HOH   HOH A . 
E 5 HOH   48 1048 29  HOH   HOH A . 
E 5 HOH   49 1049 27  HOH   HOH A . 
E 5 HOH   50 1050 32  HOH   HOH A . 
E 5 HOH   51 1051 42  HOH   HOH A . 
E 5 HOH   52 1052 52  HOH   HOH A . 
E 5 HOH   53 1053 10  HOH   HOH A . 
E 5 HOH   54 1054 35  HOH   HOH A . 
E 5 HOH   55 1055 50  HOH   HOH A . 
E 5 HOH   56 1056 57  HOH   HOH A . 
E 5 HOH   57 1057 44  HOH   HOH A . 
E 5 HOH   58 1058 23  HOH   HOH A . 
E 5 HOH   59 1059 66  HOH   HOH A . 
E 5 HOH   60 1060 46  HOH   HOH A . 
E 5 HOH   61 1061 38  HOH   HOH A . 
E 5 HOH   62 1062 56  HOH   HOH A . 
E 5 HOH   63 1063 51  HOH   HOH A . 
E 5 HOH   64 1064 48  HOH   HOH A . 
E 5 HOH   65 1065 36  HOH   HOH A . 
E 5 HOH   66 1066 47  HOH   HOH A . 
E 5 HOH   67 1067 55  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? Phenix1.16-3549 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .               2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .               3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .               4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XWW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.261 
_cell.length_a_esd                 ? 
_cell.length_b                     74.261 
_cell.length_b_esd                 ? 
_cell.length_c                     131.943 
_cell.length_c_esd                 ? 
_cell.volume                       630142.211 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         8XWW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            
;P 31 2"
;
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XWW 
_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             2.61 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.84 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M magnesium sulfate, 0.1 M sodium cacodylate, pH 6.5, 17% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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                         'RIGAKU HyPix-3000' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-07 
_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   1.54184 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        RIGAKU 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54184 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XWW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.46 
_reflns.d_resolution_low                               23.91 
_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                                     15861 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          25.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.072 
_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                                    2.46 
_reflns_shell.d_res_low                                     2.56 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1764 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.763 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.746 
_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                               55.02 
_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                                 8XWW 
_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                            2.46 
_refine.ls_d_res_low                             23.91 
_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                     15822 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2672 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2351 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_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                       2.46 
_refine_hist.d_res_low                        23.91 
_refine_hist.number_atoms_solvent             67 
_refine_hist.number_atoms_total               2448 
_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        2357 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_struct.entry_id                     8XWW 
_struct.title                        
;Crystal structure of the catalytic domain of human PDE5A complexed with 2-(3-chlorobenzyl)-4-oxo-3,4-dihydroquinazoline-7-carboxylic acid
;
_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        8XWW 
_struct_keywords.text            'Inhibitor, Complex, Hydrolase' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PDE5A_HUMAN 
_struct_ref.pdbx_db_accession          O76074 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNY
RKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHF
DQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLS
AITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGC
RKNRQKWQALAEQQEKMLINGESGQAKRN
;
_struct_ref.pdbx_align_begin           527 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XWW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 349 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O76074 
_struct_ref_seq.db_align_beg                  527 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  875 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       527 
_struct_ref_seq.pdbx_auth_seq_align_end       875 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 11  ? ALA A 20  ? THR A 537 ALA A 546 1 ? 10 
HELX_P HELX_P2  AA2 SER A 24  ? LYS A 29  ? SER A 550 LYS A 555 1 ? 6  
HELX_P HELX_P3  AA3 SER A 41  ? LEU A 56  ? SER A 567 LEU A 582 1 ? 16 
HELX_P HELX_P4  AA4 ASN A 57  ? PHE A 62  ? ASN A 583 PHE A 588 1 ? 6  
HELX_P HELX_P5  AA5 LYS A 65  ? ASN A 79  ? LYS A 591 ASN A 605 1 ? 15 
HELX_P HELX_P6  AA6 ASN A 88  ? ALA A 105 ? ASN A 614 ALA A 631 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 107 ? LEU A 112 ? LYS A 633 LEU A 638 5 ? 6  
HELX_P HELX_P8  AA8 THR A 113 ? HIS A 127 ? THR A 639 HIS A 653 1 ? 15 
HELX_P HELX_P9  AA9 SER A 153 ? SER A 169 ? SER A 679 SER A 695 1 ? 17 
HELX_P HELX_P10 AB1 SER A 179 ? THR A 197 ? SER A 705 THR A 723 1 ? 19 
HELX_P HELX_P11 AB2 ASP A 198 ? ARG A 214 ? ASP A 724 ARG A 740 1 ? 17 
HELX_P HELX_P12 AB3 ASP A 222 ? LEU A 239 ? ASP A 748 LEU A 765 1 ? 18 
HELX_P HELX_P13 AB4 SER A 240 ? LYS A 244 ? SER A 766 LYS A 770 5 ? 5  
HELX_P HELX_P14 AB5 PRO A 245 ? ASP A 262 ? PRO A 771 ASP A 788 1 ? 18 
HELX_P HELX_P15 AB6 LYS A 286 ? ILE A 298 ? LYS A 812 ILE A 824 1 ? 13 
HELX_P HELX_P16 AB7 ILE A 298 ? SER A 310 ? ILE A 824 SER A 836 1 ? 13 
HELX_P HELX_P17 AB8 CYS A 313 ? GLU A 332 ? CYS A 839 GLU A 858 1 ? 20 
# 
_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 HIS 91  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 617 A ZN  902  1_555 ? ? ? ? ? ? ? 2.261 ? ? 
metalc2  metalc ? ? A HIS 127 NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 653 A ZN  902  1_555 ? ? ? ? ? ? ? 2.186 ? ? 
metalc3  metalc ? ? A ASP 128 OD2 ? ? ? 1_555 C ZN  . ZN ? ? A ASP 654 A ZN  902  1_555 ? ? ? ? ? ? ? 2.136 ? ? 
metalc4  metalc ? ? A ASP 128 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASP 654 A MG  903  1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc5  metalc ? ? A ASP 128 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 654 A MG  903  1_555 ? ? ? ? ? ? ? 2.996 ? ? 
metalc6  metalc ? ? A ASP 238 OD1 ? ? ? 1_555 C ZN  . ZN ? ? A ASP 764 A ZN  902  1_555 ? ? ? ? ? ? ? 2.212 ? ? 
metalc7  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 E HOH . O  ? ? A ZN  902 A HOH 1005 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc8  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 E HOH . O  ? ? A ZN  902 A HOH 1026 1_555 ? ? ? ? ? ? ? 2.248 ? ? 
metalc9  metalc ? ? D MG  .   MG  ? ? ? 1_555 E HOH . O  ? ? A MG  903 A HOH 1020 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc10 metalc ? ? D MG  .   MG  ? ? ? 1_555 E HOH . O  ? ? A MG  903 A HOH 1026 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc11 metalc ? ? D MG  .   MG  ? ? ? 1_555 E HOH . O  ? ? A MG  903 A HOH 1029 1_555 ? ? ? ? ? ? ? 2.163 ? ? 
metalc12 metalc ? ? D MG  .   MG  ? ? ? 1_555 E HOH . O  ? ? A MG  903 A HOH 1039 1_555 ? ? ? ? ? ? ? 2.282 ? ? 
metalc13 metalc ? ? D MG  .   MG  ? ? ? 1_555 E HOH . O  ? ? A MG  903 A HOH 1040 1_555 ? ? ? ? ? ? ? 2.217 ? ? 
# 
_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  NE2 ? A HIS 91  ? A HIS 617  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 NE2 ? A HIS 127 ? A HIS 653  ? 1_555 88.8  ? 
2  NE2 ? A HIS 91  ? A HIS 617  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 94.5  ? 
3  NE2 ? A HIS 127 ? A HIS 653  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 86.3  ? 
4  NE2 ? A HIS 91  ? A HIS 617  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 OD1 ? A ASP 238 ? A ASP 764  ? 1_555 83.7  ? 
5  NE2 ? A HIS 127 ? A HIS 653  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 OD1 ? A ASP 238 ? A ASP 764  ? 1_555 87.8  ? 
6  OD2 ? A ASP 128 ? A ASP 654  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 OD1 ? A ASP 238 ? A ASP 764  ? 1_555 173.9 ? 
7  NE2 ? A HIS 91  ? A HIS 617  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1005 ? 1_555 87.9  ? 
8  NE2 ? A HIS 127 ? A HIS 653  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1005 ? 1_555 175.0 ? 
9  OD2 ? A ASP 128 ? A ASP 654  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1005 ? 1_555 90.2  ? 
10 OD1 ? A ASP 238 ? A ASP 764  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1005 ? 1_555 95.6  ? 
11 NE2 ? A HIS 91  ? A HIS 617  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1026 ? 1_555 166.2 ? 
12 NE2 ? A HIS 127 ? A HIS 653  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1026 ? 1_555 104.9 ? 
13 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1026 ? 1_555 87.5  ? 
14 OD1 ? A ASP 238 ? A ASP 764  ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1026 ? 1_555 95.6  ? 
15 O   ? E HOH .   ? A HOH 1005 ? 1_555 ZN ? C ZN . ? A ZN 902 ? 1_555 O   ? E HOH .   ? A HOH 1026 ? 1_555 78.5  ? 
16 OD1 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 47.2  ? 
17 OD1 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1020 ? 1_555 76.6  ? 
18 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1020 ? 1_555 104.9 ? 
19 OD1 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1026 ? 1_555 107.6 ? 
20 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1026 ? 1_555 71.0  ? 
21 O   ? E HOH .   ? A HOH 1020 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1026 ? 1_555 89.5  ? 
22 OD1 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1029 ? 1_555 144.5 ? 
23 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1029 ? 1_555 152.7 ? 
24 O   ? E HOH .   ? A HOH 1020 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1029 ? 1_555 69.3  ? 
25 O   ? E HOH .   ? A HOH 1026 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1029 ? 1_555 82.1  ? 
26 OD1 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1039 ? 1_555 83.0  ? 
27 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1039 ? 1_555 119.9 ? 
28 O   ? E HOH .   ? A HOH 1020 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1039 ? 1_555 89.8  ? 
29 O   ? E HOH .   ? A HOH 1026 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1039 ? 1_555 168.8 ? 
30 O   ? E HOH .   ? A HOH 1029 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1039 ? 1_555 87.2  ? 
31 OD1 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1040 ? 1_555 120.1 ? 
32 OD2 ? A ASP 128 ? A ASP 654  ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1040 ? 1_555 87.0  ? 
33 O   ? E HOH .   ? A HOH 1020 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1040 ? 1_555 163.1 ? 
34 O   ? E HOH .   ? A HOH 1026 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1040 ? 1_555 83.1  ? 
35 O   ? E HOH .   ? A HOH 1029 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1040 ? 1_555 94.6  ? 
36 O   ? E HOH .   ? A HOH 1039 ? 1_555 MG ? D MG . ? A MG 903 ? 1_555 O   ? E HOH .   ? A HOH 1040 ? 1_555 94.6  ? 
# 
_pdbx_entry_details.entry_id                   8XWW 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    1059 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    1065 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
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 LYS A 630 ? ? -84.96  -71.94 
2 1 SER A 679 ? ? 60.66   74.05  
3 1 PHE A 787 ? ? -109.99 -65.10 
4 1 LYS A 812 ? ? 63.34   -8.87  
5 1 ILE A 824 ? ? -121.57 -56.45 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+1/3   
3 -x+y,-x,z+2/3  
4 x-y,-y,-z+2/3  
5 -x,-x+y,-z+1/3 
6 y,x,-z         
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 527 ? A SER 1   
2  1 Y 1 A TYR 528 ? A TYR 2   
3  1 Y 1 A HIS 529 ? A HIS 3   
4  1 Y 1 A ALA 530 ? A ALA 4   
5  1 Y 1 A SER 531 ? A SER 5   
6  1 Y 1 A ALA 532 ? A ALA 6   
7  1 Y 1 A ALA 533 ? A ALA 7   
8  1 Y 1 A GLU 534 ? A GLU 8   
9  1 Y 1 A GLU 535 ? A GLU 9   
10 1 Y 1 A GLU 536 ? A GLU 10  
11 1 Y 1 A ARG 667 ? A ARG 141 
12 1 Y 1 A SER 668 ? A SER 142 
13 1 Y 1 A GLU 669 ? A GLU 143 
14 1 Y 1 A HIS 670 ? A HIS 144 
15 1 Y 1 A PRO 671 ? A PRO 145 
16 1 Y 1 A LEU 672 ? A LEU 146 
17 1 Y 1 A ALA 673 ? A ALA 147 
18 1 Y 1 A GLN 674 ? A GLN 148 
19 1 Y 1 A LEU 675 ? A LEU 149 
20 1 Y 1 A TYR 676 ? A TYR 150 
21 1 Y 1 A CYS 677 ? A CYS 151 
22 1 Y 1 A ASP 791 ? A ASP 265 
23 1 Y 1 A ARG 792 ? A ARG 266 
24 1 Y 1 A GLU 793 ? A GLU 267 
25 1 Y 1 A ARG 794 ? A ARG 268 
26 1 Y 1 A LYS 795 ? A LYS 269 
27 1 Y 1 A GLU 796 ? A GLU 270 
28 1 Y 1 A LEU 797 ? A LEU 271 
29 1 Y 1 A ASN 798 ? A ASN 272 
30 1 Y 1 A ILE 799 ? A ILE 273 
31 1 Y 1 A GLU 800 ? A GLU 274 
32 1 Y 1 A PRO 801 ? A PRO 275 
33 1 Y 1 A THR 802 ? A THR 276 
34 1 Y 1 A ASP 803 ? A ASP 277 
35 1 Y 1 A LEU 804 ? A LEU 278 
36 1 Y 1 A MET 805 ? A MET 279 
37 1 Y 1 A ASN 806 ? A ASN 280 
38 1 Y 1 A ARG 807 ? A ARG 281 
39 1 Y 1 A GLU 808 ? A GLU 282 
40 1 Y 1 A LYS 809 ? A LYS 283 
41 1 Y 1 A LYS 810 ? A LYS 284 
42 1 Y 1 A GLN 860 ? A GLN 334 
43 1 Y 1 A GLU 861 ? A GLU 335 
44 1 Y 1 A LYS 862 ? A LYS 336 
45 1 Y 1 A MET 863 ? A MET 337 
46 1 Y 1 A LEU 864 ? A LEU 338 
47 1 Y 1 A ILE 865 ? A ILE 339 
48 1 Y 1 A ASN 866 ? A ASN 340 
49 1 Y 1 A GLY 867 ? A GLY 341 
50 1 Y 1 A GLU 868 ? A GLU 342 
51 1 Y 1 A SER 869 ? A SER 343 
52 1 Y 1 A GLY 870 ? A GLY 344 
53 1 Y 1 A GLN 871 ? A GLN 345 
54 1 Y 1 A ALA 872 ? A ALA 346 
55 1 Y 1 A LYS 873 ? A LYS 347 
56 1 Y 1 A ARG 874 ? A ARG 348 
57 1 Y 1 A ASN 875 ? A ASN 349 
# 
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 
A1D5K O1   O  N N 1   
A1D5K C3   C  N N 2   
A1D5K C4   C  N N 3   
A1D5K C5   C  Y N 4   
A1D5K C6   C  Y N 5   
A1D5K C7   C  Y N 6   
A1D5K C8   C  N N 7   
A1D5K N    N  N N 8   
A1D5K C    C  Y N 9   
A1D5K O    O  N N 10  
A1D5K C1   C  Y N 11  
A1D5K C10  C  Y N 12  
A1D5K C11  C  Y N 13  
A1D5K C12  C  N N 14  
A1D5K C13  C  Y N 15  
A1D5K C14  C  Y N 16  
A1D5K C15  C  Y N 17  
A1D5K C2   C  Y N 18  
A1D5K C9   C  Y N 19  
A1D5K N1   N  N N 20  
A1D5K O2   O  N N 21  
A1D5K CL   CL N N 22  
A1D5K H1   H  N N 23  
A1D5K H2   H  N N 24  
A1D5K H3   H  N N 25  
A1D5K H4   H  N N 26  
A1D5K H    H  N N 27  
A1D5K H6   H  N N 28  
A1D5K H8   H  N N 29  
A1D5K H9   H  N N 30  
A1D5K H10  H  N N 31  
A1D5K H5   H  N N 32  
A1D5K H7   H  N N 33  
ALA   N    N  N N 34  
ALA   CA   C  N S 35  
ALA   C    C  N N 36  
ALA   O    O  N N 37  
ALA   CB   C  N N 38  
ALA   OXT  O  N N 39  
ALA   H    H  N N 40  
ALA   H2   H  N N 41  
ALA   HA   H  N N 42  
ALA   HB1  H  N N 43  
ALA   HB2  H  N N 44  
ALA   HB3  H  N N 45  
ALA   HXT  H  N N 46  
ARG   N    N  N N 47  
ARG   CA   C  N S 48  
ARG   C    C  N N 49  
ARG   O    O  N N 50  
ARG   CB   C  N N 51  
ARG   CG   C  N N 52  
ARG   CD   C  N N 53  
ARG   NE   N  N N 54  
ARG   CZ   C  N N 55  
ARG   NH1  N  N N 56  
ARG   NH2  N  N N 57  
ARG   OXT  O  N N 58  
ARG   H    H  N N 59  
ARG   H2   H  N N 60  
ARG   HA   H  N N 61  
ARG   HB2  H  N N 62  
ARG   HB3  H  N N 63  
ARG   HG2  H  N N 64  
ARG   HG3  H  N N 65  
ARG   HD2  H  N N 66  
ARG   HD3  H  N N 67  
ARG   HE   H  N N 68  
ARG   HH11 H  N N 69  
ARG   HH12 H  N N 70  
ARG   HH21 H  N N 71  
ARG   HH22 H  N N 72  
ARG   HXT  H  N N 73  
ASN   N    N  N N 74  
ASN   CA   C  N S 75  
ASN   C    C  N N 76  
ASN   O    O  N N 77  
ASN   CB   C  N N 78  
ASN   CG   C  N N 79  
ASN   OD1  O  N N 80  
ASN   ND2  N  N N 81  
ASN   OXT  O  N N 82  
ASN   H    H  N N 83  
ASN   H2   H  N N 84  
ASN   HA   H  N N 85  
ASN   HB2  H  N N 86  
ASN   HB3  H  N N 87  
ASN   HD21 H  N N 88  
ASN   HD22 H  N N 89  
ASN   HXT  H  N N 90  
ASP   N    N  N N 91  
ASP   CA   C  N S 92  
ASP   C    C  N N 93  
ASP   O    O  N N 94  
ASP   CB   C  N N 95  
ASP   CG   C  N N 96  
ASP   OD1  O  N N 97  
ASP   OD2  O  N N 98  
ASP   OXT  O  N N 99  
ASP   H    H  N N 100 
ASP   H2   H  N N 101 
ASP   HA   H  N N 102 
ASP   HB2  H  N N 103 
ASP   HB3  H  N N 104 
ASP   HD2  H  N N 105 
ASP   HXT  H  N N 106 
CYS   N    N  N N 107 
CYS   CA   C  N R 108 
CYS   C    C  N N 109 
CYS   O    O  N N 110 
CYS   CB   C  N N 111 
CYS   SG   S  N N 112 
CYS   OXT  O  N N 113 
CYS   H    H  N N 114 
CYS   H2   H  N N 115 
CYS   HA   H  N N 116 
CYS   HB2  H  N N 117 
CYS   HB3  H  N N 118 
CYS   HG   H  N N 119 
CYS   HXT  H  N N 120 
GLN   N    N  N N 121 
GLN   CA   C  N S 122 
GLN   C    C  N N 123 
GLN   O    O  N N 124 
GLN   CB   C  N N 125 
GLN   CG   C  N N 126 
GLN   CD   C  N N 127 
GLN   OE1  O  N N 128 
GLN   NE2  N  N N 129 
GLN   OXT  O  N N 130 
GLN   H    H  N N 131 
GLN   H2   H  N N 132 
GLN   HA   H  N N 133 
GLN   HB2  H  N N 134 
GLN   HB3  H  N N 135 
GLN   HG2  H  N N 136 
GLN   HG3  H  N N 137 
GLN   HE21 H  N N 138 
GLN   HE22 H  N N 139 
GLN   HXT  H  N N 140 
GLU   N    N  N N 141 
GLU   CA   C  N S 142 
GLU   C    C  N N 143 
GLU   O    O  N N 144 
GLU   CB   C  N N 145 
GLU   CG   C  N N 146 
GLU   CD   C  N N 147 
GLU   OE1  O  N N 148 
GLU   OE2  O  N N 149 
GLU   OXT  O  N N 150 
GLU   H    H  N N 151 
GLU   H2   H  N N 152 
GLU   HA   H  N N 153 
GLU   HB2  H  N N 154 
GLU   HB3  H  N N 155 
GLU   HG2  H  N N 156 
GLU   HG3  H  N N 157 
GLU   HE2  H  N N 158 
GLU   HXT  H  N N 159 
GLY   N    N  N N 160 
GLY   CA   C  N N 161 
GLY   C    C  N N 162 
GLY   O    O  N N 163 
GLY   OXT  O  N N 164 
GLY   H    H  N N 165 
GLY   H2   H  N N 166 
GLY   HA2  H  N N 167 
GLY   HA3  H  N N 168 
GLY   HXT  H  N N 169 
HIS   N    N  N N 170 
HIS   CA   C  N S 171 
HIS   C    C  N N 172 
HIS   O    O  N N 173 
HIS   CB   C  N N 174 
HIS   CG   C  Y N 175 
HIS   ND1  N  Y N 176 
HIS   CD2  C  Y N 177 
HIS   CE1  C  Y N 178 
HIS   NE2  N  Y N 179 
HIS   OXT  O  N N 180 
HIS   H    H  N N 181 
HIS   H2   H  N N 182 
HIS   HA   H  N N 183 
HIS   HB2  H  N N 184 
HIS   HB3  H  N N 185 
HIS   HD1  H  N N 186 
HIS   HD2  H  N N 187 
HIS   HE1  H  N N 188 
HIS   HE2  H  N N 189 
HIS   HXT  H  N N 190 
HOH   O    O  N N 191 
HOH   H1   H  N N 192 
HOH   H2   H  N N 193 
ILE   N    N  N N 194 
ILE   CA   C  N S 195 
ILE   C    C  N N 196 
ILE   O    O  N N 197 
ILE   CB   C  N S 198 
ILE   CG1  C  N N 199 
ILE   CG2  C  N N 200 
ILE   CD1  C  N N 201 
ILE   OXT  O  N N 202 
ILE   H    H  N N 203 
ILE   H2   H  N N 204 
ILE   HA   H  N N 205 
ILE   HB   H  N N 206 
ILE   HG12 H  N N 207 
ILE   HG13 H  N N 208 
ILE   HG21 H  N N 209 
ILE   HG22 H  N N 210 
ILE   HG23 H  N N 211 
ILE   HD11 H  N N 212 
ILE   HD12 H  N N 213 
ILE   HD13 H  N N 214 
ILE   HXT  H  N N 215 
LEU   N    N  N N 216 
LEU   CA   C  N S 217 
LEU   C    C  N N 218 
LEU   O    O  N N 219 
LEU   CB   C  N N 220 
LEU   CG   C  N N 221 
LEU   CD1  C  N N 222 
LEU   CD2  C  N N 223 
LEU   OXT  O  N N 224 
LEU   H    H  N N 225 
LEU   H2   H  N N 226 
LEU   HA   H  N N 227 
LEU   HB2  H  N N 228 
LEU   HB3  H  N N 229 
LEU   HG   H  N N 230 
LEU   HD11 H  N N 231 
LEU   HD12 H  N N 232 
LEU   HD13 H  N N 233 
LEU   HD21 H  N N 234 
LEU   HD22 H  N N 235 
LEU   HD23 H  N N 236 
LEU   HXT  H  N N 237 
LYS   N    N  N N 238 
LYS   CA   C  N S 239 
LYS   C    C  N N 240 
LYS   O    O  N N 241 
LYS   CB   C  N N 242 
LYS   CG   C  N N 243 
LYS   CD   C  N N 244 
LYS   CE   C  N N 245 
LYS   NZ   N  N N 246 
LYS   OXT  O  N N 247 
LYS   H    H  N N 248 
LYS   H2   H  N N 249 
LYS   HA   H  N N 250 
LYS   HB2  H  N N 251 
LYS   HB3  H  N N 252 
LYS   HG2  H  N N 253 
LYS   HG3  H  N N 254 
LYS   HD2  H  N N 255 
LYS   HD3  H  N N 256 
LYS   HE2  H  N N 257 
LYS   HE3  H  N N 258 
LYS   HZ1  H  N N 259 
LYS   HZ2  H  N N 260 
LYS   HZ3  H  N N 261 
LYS   HXT  H  N N 262 
MET   N    N  N N 263 
MET   CA   C  N S 264 
MET   C    C  N N 265 
MET   O    O  N N 266 
MET   CB   C  N N 267 
MET   CG   C  N N 268 
MET   SD   S  N N 269 
MET   CE   C  N N 270 
MET   OXT  O  N N 271 
MET   H    H  N N 272 
MET   H2   H  N N 273 
MET   HA   H  N N 274 
MET   HB2  H  N N 275 
MET   HB3  H  N N 276 
MET   HG2  H  N N 277 
MET   HG3  H  N N 278 
MET   HE1  H  N N 279 
MET   HE2  H  N N 280 
MET   HE3  H  N N 281 
MET   HXT  H  N N 282 
MG    MG   MG N N 283 
PHE   N    N  N N 284 
PHE   CA   C  N S 285 
PHE   C    C  N N 286 
PHE   O    O  N N 287 
PHE   CB   C  N N 288 
PHE   CG   C  Y N 289 
PHE   CD1  C  Y N 290 
PHE   CD2  C  Y N 291 
PHE   CE1  C  Y N 292 
PHE   CE2  C  Y N 293 
PHE   CZ   C  Y N 294 
PHE   OXT  O  N N 295 
PHE   H    H  N N 296 
PHE   H2   H  N N 297 
PHE   HA   H  N N 298 
PHE   HB2  H  N N 299 
PHE   HB3  H  N N 300 
PHE   HD1  H  N N 301 
PHE   HD2  H  N N 302 
PHE   HE1  H  N N 303 
PHE   HE2  H  N N 304 
PHE   HZ   H  N N 305 
PHE   HXT  H  N N 306 
PRO   N    N  N N 307 
PRO   CA   C  N S 308 
PRO   C    C  N N 309 
PRO   O    O  N N 310 
PRO   CB   C  N N 311 
PRO   CG   C  N N 312 
PRO   CD   C  N N 313 
PRO   OXT  O  N N 314 
PRO   H    H  N N 315 
PRO   HA   H  N N 316 
PRO   HB2  H  N N 317 
PRO   HB3  H  N N 318 
PRO   HG2  H  N N 319 
PRO   HG3  H  N N 320 
PRO   HD2  H  N N 321 
PRO   HD3  H  N N 322 
PRO   HXT  H  N N 323 
SER   N    N  N N 324 
SER   CA   C  N S 325 
SER   C    C  N N 326 
SER   O    O  N N 327 
SER   CB   C  N N 328 
SER   OG   O  N N 329 
SER   OXT  O  N N 330 
SER   H    H  N N 331 
SER   H2   H  N N 332 
SER   HA   H  N N 333 
SER   HB2  H  N N 334 
SER   HB3  H  N N 335 
SER   HG   H  N N 336 
SER   HXT  H  N N 337 
THR   N    N  N N 338 
THR   CA   C  N S 339 
THR   C    C  N N 340 
THR   O    O  N N 341 
THR   CB   C  N R 342 
THR   OG1  O  N N 343 
THR   CG2  C  N N 344 
THR   OXT  O  N N 345 
THR   H    H  N N 346 
THR   H2   H  N N 347 
THR   HA   H  N N 348 
THR   HB   H  N N 349 
THR   HG1  H  N N 350 
THR   HG21 H  N N 351 
THR   HG22 H  N N 352 
THR   HG23 H  N N 353 
THR   HXT  H  N N 354 
TRP   N    N  N N 355 
TRP   CA   C  N S 356 
TRP   C    C  N N 357 
TRP   O    O  N N 358 
TRP   CB   C  N N 359 
TRP   CG   C  Y N 360 
TRP   CD1  C  Y N 361 
TRP   CD2  C  Y N 362 
TRP   NE1  N  Y N 363 
TRP   CE2  C  Y N 364 
TRP   CE3  C  Y N 365 
TRP   CZ2  C  Y N 366 
TRP   CZ3  C  Y N 367 
TRP   CH2  C  Y N 368 
TRP   OXT  O  N N 369 
TRP   H    H  N N 370 
TRP   H2   H  N N 371 
TRP   HA   H  N N 372 
TRP   HB2  H  N N 373 
TRP   HB3  H  N N 374 
TRP   HD1  H  N N 375 
TRP   HE1  H  N N 376 
TRP   HE3  H  N N 377 
TRP   HZ2  H  N N 378 
TRP   HZ3  H  N N 379 
TRP   HH2  H  N N 380 
TRP   HXT  H  N N 381 
TYR   N    N  N N 382 
TYR   CA   C  N S 383 
TYR   C    C  N N 384 
TYR   O    O  N N 385 
TYR   CB   C  N N 386 
TYR   CG   C  Y N 387 
TYR   CD1  C  Y N 388 
TYR   CD2  C  Y N 389 
TYR   CE1  C  Y N 390 
TYR   CE2  C  Y N 391 
TYR   CZ   C  Y N 392 
TYR   OH   O  N N 393 
TYR   OXT  O  N N 394 
TYR   H    H  N N 395 
TYR   H2   H  N N 396 
TYR   HA   H  N N 397 
TYR   HB2  H  N N 398 
TYR   HB3  H  N N 399 
TYR   HD1  H  N N 400 
TYR   HD2  H  N N 401 
TYR   HE1  H  N N 402 
TYR   HE2  H  N N 403 
TYR   HH   H  N N 404 
TYR   HXT  H  N N 405 
VAL   N    N  N N 406 
VAL   CA   C  N S 407 
VAL   C    C  N N 408 
VAL   O    O  N N 409 
VAL   CB   C  N N 410 
VAL   CG1  C  N N 411 
VAL   CG2  C  N N 412 
VAL   OXT  O  N N 413 
VAL   H    H  N N 414 
VAL   H2   H  N N 415 
VAL   HA   H  N N 416 
VAL   HB   H  N N 417 
VAL   HG11 H  N N 418 
VAL   HG12 H  N N 419 
VAL   HG13 H  N N 420 
VAL   HG21 H  N N 421 
VAL   HG22 H  N N 422 
VAL   HG23 H  N N 423 
VAL   HXT  H  N N 424 
ZN    ZN   ZN N N 425 
# 
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 
A1D5K CL  C    sing N N 1   
A1D5K C   C1   doub Y N 2   
A1D5K C1  C2   sing Y N 3   
A1D5K C2  C3   sing N N 4   
A1D5K C3  C4   sing N N 5   
A1D5K C4  N    doub N N 6   
A1D5K N   C5   sing N N 7   
A1D5K C5  C6   sing Y N 8   
A1D5K C6  C7   doub Y N 9   
A1D5K C8  C7   sing N N 10  
A1D5K O   C8   sing N N 11  
A1D5K O1  C8   doub N N 12  
A1D5K C7  C9   sing Y N 13  
A1D5K C9  C10  doub Y N 14  
A1D5K C5  C11  doub Y N 15  
A1D5K C10 C11  sing Y N 16  
A1D5K C11 C12  sing N N 17  
A1D5K N1  C12  sing N N 18  
A1D5K C4  N1   sing N N 19  
A1D5K C12 O2   doub N N 20  
A1D5K C13 C2   doub Y N 21  
A1D5K C14 C13  sing Y N 22  
A1D5K C15 C14  doub Y N 23  
A1D5K C   C15  sing Y N 24  
A1D5K C3  H1   sing N N 25  
A1D5K C3  H2   sing N N 26  
A1D5K C6  H3   sing N N 27  
A1D5K O   H4   sing N N 28  
A1D5K C1  H    sing N N 29  
A1D5K C10 H6   sing N N 30  
A1D5K C13 H8   sing N N 31  
A1D5K C14 H9   sing N N 32  
A1D5K C15 H10  sing N N 33  
A1D5K C9  H5   sing N N 34  
A1D5K N1  H7   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
GLN   N   CA   sing N N 118 
GLN   N   H    sing N N 119 
GLN   N   H2   sing N N 120 
GLN   CA  C    sing N N 121 
GLN   CA  CB   sing N N 122 
GLN   CA  HA   sing N N 123 
GLN   C   O    doub N N 124 
GLN   C   OXT  sing N N 125 
GLN   CB  CG   sing N N 126 
GLN   CB  HB2  sing N N 127 
GLN   CB  HB3  sing N N 128 
GLN   CG  CD   sing N N 129 
GLN   CG  HG2  sing N N 130 
GLN   CG  HG3  sing N N 131 
GLN   CD  OE1  doub N N 132 
GLN   CD  NE2  sing N N 133 
GLN   NE2 HE21 sing N N 134 
GLN   NE2 HE22 sing N N 135 
GLN   OXT HXT  sing N N 136 
GLU   N   CA   sing N N 137 
GLU   N   H    sing N N 138 
GLU   N   H2   sing N N 139 
GLU   CA  C    sing N N 140 
GLU   CA  CB   sing N N 141 
GLU   CA  HA   sing N N 142 
GLU   C   O    doub N N 143 
GLU   C   OXT  sing N N 144 
GLU   CB  CG   sing N N 145 
GLU   CB  HB2  sing N N 146 
GLU   CB  HB3  sing N N 147 
GLU   CG  CD   sing N N 148 
GLU   CG  HG2  sing N N 149 
GLU   CG  HG3  sing N N 150 
GLU   CD  OE1  doub N N 151 
GLU   CD  OE2  sing N N 152 
GLU   OE2 HE2  sing N N 153 
GLU   OXT HXT  sing N N 154 
GLY   N   CA   sing N N 155 
GLY   N   H    sing N N 156 
GLY   N   H2   sing N N 157 
GLY   CA  C    sing N N 158 
GLY   CA  HA2  sing N N 159 
GLY   CA  HA3  sing N N 160 
GLY   C   O    doub N N 161 
GLY   C   OXT  sing N N 162 
GLY   OXT HXT  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
MET   N   CA   sing N N 253 
MET   N   H    sing N N 254 
MET   N   H2   sing N N 255 
MET   CA  C    sing N N 256 
MET   CA  CB   sing N N 257 
MET   CA  HA   sing N N 258 
MET   C   O    doub N N 259 
MET   C   OXT  sing N N 260 
MET   CB  CG   sing N N 261 
MET   CB  HB2  sing N N 262 
MET   CB  HB3  sing N N 263 
MET   CG  SD   sing N N 264 
MET   CG  HG2  sing N N 265 
MET   CG  HG3  sing N N 266 
MET   SD  CE   sing N N 267 
MET   CE  HE1  sing N N 268 
MET   CE  HE2  sing N N 269 
MET   CE  HE3  sing N N 270 
MET   OXT HXT  sing N N 271 
PHE   N   CA   sing N N 272 
PHE   N   H    sing N N 273 
PHE   N   H2   sing N N 274 
PHE   CA  C    sing N N 275 
PHE   CA  CB   sing N N 276 
PHE   CA  HA   sing N N 277 
PHE   C   O    doub N N 278 
PHE   C   OXT  sing N N 279 
PHE   CB  CG   sing N N 280 
PHE   CB  HB2  sing N N 281 
PHE   CB  HB3  sing N N 282 
PHE   CG  CD1  doub Y N 283 
PHE   CG  CD2  sing Y N 284 
PHE   CD1 CE1  sing Y N 285 
PHE   CD1 HD1  sing N N 286 
PHE   CD2 CE2  doub Y N 287 
PHE   CD2 HD2  sing N N 288 
PHE   CE1 CZ   doub Y N 289 
PHE   CE1 HE1  sing N N 290 
PHE   CE2 CZ   sing Y N 291 
PHE   CE2 HE2  sing N N 292 
PHE   CZ  HZ   sing N N 293 
PHE   OXT HXT  sing N N 294 
PRO   N   CA   sing N N 295 
PRO   N   CD   sing N N 296 
PRO   N   H    sing N N 297 
PRO   CA  C    sing N N 298 
PRO   CA  CB   sing N N 299 
PRO   CA  HA   sing N N 300 
PRO   C   O    doub N N 301 
PRO   C   OXT  sing N N 302 
PRO   CB  CG   sing N N 303 
PRO   CB  HB2  sing N N 304 
PRO   CB  HB3  sing N N 305 
PRO   CG  CD   sing N N 306 
PRO   CG  HG2  sing N N 307 
PRO   CG  HG3  sing N N 308 
PRO   CD  HD2  sing N N 309 
PRO   CD  HD3  sing N N 310 
PRO   OXT HXT  sing N N 311 
SER   N   CA   sing N N 312 
SER   N   H    sing N N 313 
SER   N   H2   sing N N 314 
SER   CA  C    sing N N 315 
SER   CA  CB   sing N N 316 
SER   CA  HA   sing N N 317 
SER   C   O    doub N N 318 
SER   C   OXT  sing N N 319 
SER   CB  OG   sing N N 320 
SER   CB  HB2  sing N N 321 
SER   CB  HB3  sing N N 322 
SER   OG  HG   sing N N 323 
SER   OXT HXT  sing N N 324 
THR   N   CA   sing N N 325 
THR   N   H    sing N N 326 
THR   N   H2   sing N N 327 
THR   CA  C    sing N N 328 
THR   CA  CB   sing N N 329 
THR   CA  HA   sing N N 330 
THR   C   O    doub N N 331 
THR   C   OXT  sing N N 332 
THR   CB  OG1  sing N N 333 
THR   CB  CG2  sing N N 334 
THR   CB  HB   sing N N 335 
THR   OG1 HG1  sing N N 336 
THR   CG2 HG21 sing N N 337 
THR   CG2 HG22 sing N N 338 
THR   CG2 HG23 sing N N 339 
THR   OXT HXT  sing N N 340 
TRP   N   CA   sing N N 341 
TRP   N   H    sing N N 342 
TRP   N   H2   sing N N 343 
TRP   CA  C    sing N N 344 
TRP   CA  CB   sing N N 345 
TRP   CA  HA   sing N N 346 
TRP   C   O    doub N N 347 
TRP   C   OXT  sing N N 348 
TRP   CB  CG   sing N N 349 
TRP   CB  HB2  sing N N 350 
TRP   CB  HB3  sing N N 351 
TRP   CG  CD1  doub Y N 352 
TRP   CG  CD2  sing Y N 353 
TRP   CD1 NE1  sing Y N 354 
TRP   CD1 HD1  sing N N 355 
TRP   CD2 CE2  doub Y N 356 
TRP   CD2 CE3  sing Y N 357 
TRP   NE1 CE2  sing Y N 358 
TRP   NE1 HE1  sing N N 359 
TRP   CE2 CZ2  sing Y N 360 
TRP   CE3 CZ3  doub Y N 361 
TRP   CE3 HE3  sing N N 362 
TRP   CZ2 CH2  doub Y N 363 
TRP   CZ2 HZ2  sing N N 364 
TRP   CZ3 CH2  sing Y N 365 
TRP   CZ3 HZ3  sing N N 366 
TRP   CH2 HH2  sing N N 367 
TRP   OXT HXT  sing N N 368 
TYR   N   CA   sing N N 369 
TYR   N   H    sing N N 370 
TYR   N   H2   sing N N 371 
TYR   CA  C    sing N N 372 
TYR   CA  CB   sing N N 373 
TYR   CA  HA   sing N N 374 
TYR   C   O    doub N N 375 
TYR   C   OXT  sing N N 376 
TYR   CB  CG   sing N N 377 
TYR   CB  HB2  sing N N 378 
TYR   CB  HB3  sing N N 379 
TYR   CG  CD1  doub Y N 380 
TYR   CG  CD2  sing Y N 381 
TYR   CD1 CE1  sing Y N 382 
TYR   CD1 HD1  sing N N 383 
TYR   CD2 CE2  doub Y N 384 
TYR   CD2 HD2  sing N N 385 
TYR   CE1 CZ   doub Y N 386 
TYR   CE1 HE1  sing N N 387 
TYR   CE2 CZ   sing Y N 388 
TYR   CE2 HE2  sing N N 389 
TYR   CZ  OH   sing N N 390 
TYR   OH  HH   sing N N 391 
TYR   OXT HXT  sing N N 392 
VAL   N   CA   sing N N 393 
VAL   N   H    sing N N 394 
VAL   N   H2   sing N N 395 
VAL   CA  C    sing N N 396 
VAL   CA  CB   sing N N 397 
VAL   CA  HA   sing N N 398 
VAL   C   O    doub N N 399 
VAL   C   OXT  sing N N 400 
VAL   CB  CG1  sing N N 401 
VAL   CB  CG2  sing N N 402 
VAL   CB  HB   sing N N 403 
VAL   CG1 HG11 sing N N 404 
VAL   CG1 HG12 sing N N 405 
VAL   CG1 HG13 sing N N 406 
VAL   CG2 HG21 sing N N 407 
VAL   CG2 HG22 sing N N 408 
VAL   CG2 HG23 sing N N 409 
VAL   OXT HXT  sing N N 410 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 21977127 1 
'National Natural Science Foundation of China (NSFC)' China 22077143 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7FAQ 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.crystal_system   trigonal 
_space_group.name_H-M_alt     'P 31 2 1' 
_space_group.IT_number        152 
_space_group.name_Hall        
;P 31 2"
;
_space_group.id               1 
# 
_atom_sites.entry_id                    8XWW 
_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]   0.013466 
_atom_sites.fract_transf_matrix[1][2]   0.007775 
_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]   0.015549 
_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]   0.007579 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
MG 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR   A 1 11  ? -16.99700 6.05000  12.60200  1.000 74.41000  ? 537  THR   A N   1 
ATOM   2    C  CA  . THR   A 1 11  ? -17.54300 6.23900  13.94000  1.000 79.68000  ? 537  THR   A CA  1 
ATOM   3    C  C   . THR   A 1 11  ? -17.13800 7.59900  14.50100  1.000 79.47000  ? 537  THR   A C   1 
ATOM   4    O  O   . THR   A 1 11  ? -17.79200 8.13400  15.39700  1.000 73.04000  ? 537  THR   A O   1 
ATOM   5    C  CB  . THR   A 1 11  ? -17.08200 5.12600  14.90200  1.000 82.86000  ? 537  THR   A CB  1 
ATOM   6    O  OG1 . THR   A 1 11  ? -17.66200 5.33700  16.19500  1.000 83.36000  ? 537  THR   A OG1 1 
ATOM   7    C  CG2 . THR   A 1 11  ? -15.56500 5.11000  15.02100  1.000 74.80000  ? 537  THR   A CG2 1 
ATOM   8    N  N   . ARG   A 1 12  ? -16.04900 8.15400  13.96800  1.000 73.20000  ? 538  ARG   A N   1 
ATOM   9    C  CA  . ARG   A 1 12  ? -15.63200 9.49800  14.34100  1.000 76.21000  ? 538  ARG   A CA  1 
ATOM   10   C  C   . ARG   A 1 12  ? -16.44000 10.56900 13.62200  1.000 78.00000  ? 538  ARG   A C   1 
ATOM   11   O  O   . ARG   A 1 12  ? -16.54300 11.69300 14.12600  1.000 74.07000  ? 538  ARG   A O   1 
ATOM   12   C  CB  . ARG   A 1 12  ? -14.13800 9.69200  14.06000  1.000 78.45000  ? 538  ARG   A CB  1 
ATOM   13   C  CG  . ARG   A 1 12  ? -13.73600 9.55700  12.59600  1.000 86.58000  ? 538  ARG   A CG  1 
ATOM   14   C  CD  . ARG   A 1 12  ? -13.42200 8.11400  12.22200  1.000 80.55000  ? 538  ARG   A CD  1 
ATOM   15   N  NE  . ARG   A 1 12  ? -13.35300 7.92600  10.77600  1.000 87.62000  ? 538  ARG   A NE  1 
ATOM   16   C  CZ  . ARG   A 1 12  ? -14.41500 7.83000  9.98300   1.000 85.99000  ? 538  ARG   A CZ  1 
ATOM   17   N  NH1 . ARG   A 1 12  ? -14.25500 7.65800  8.67700   1.000 100.38000 ? 538  ARG   A NH1 1 
ATOM   18   N  NH2 . ARG   A 1 12  ? -15.63800 7.90500  10.49100  1.000 77.81000  ? 538  ARG   A NH2 1 
ATOM   19   N  N   . GLU   A 1 13  ? -17.00900 10.24600 12.45800  1.000 78.41000  ? 539  GLU   A N   1 
ATOM   20   C  CA  . GLU   A 1 13  ? -17.92500 11.16300 11.79200  1.000 74.53000  ? 539  GLU   A CA  1 
ATOM   21   C  C   . GLU   A 1 13  ? -19.30200 11.15000 12.44100  1.000 62.66000  ? 539  GLU   A C   1 
ATOM   22   O  O   . GLU   A 1 13  ? -19.94700 12.20000 12.53700  1.000 66.03000  ? 539  GLU   A O   1 
ATOM   23   C  CB  . GLU   A 1 13  ? -18.04100 10.81200 10.30700  1.000 64.16000  ? 539  GLU   A CB  1 
ATOM   24   C  CG  . GLU   A 1 13  ? -18.95800 11.73700 9.52600   1.000 62.64000  ? 539  GLU   A CG  1 
ATOM   25   C  CD  . GLU   A 1 13  ? -18.93600 11.46100 8.03700   1.000 68.76000  ? 539  GLU   A CD  1 
ATOM   26   O  OE1 . GLU   A 1 13  ? -18.24600 10.50800 7.61800   1.000 76.25000  ? 539  GLU   A OE1 1 
ATOM   27   O  OE2 . GLU   A 1 13  ? -19.61000 12.19700 7.28600   1.000 61.42000  ? 539  GLU   A OE2 1 
ATOM   28   N  N   . LEU   A 1 14  ? -19.76600 9.98000  12.88700  1.000 60.19000  ? 540  LEU   A N   1 
ATOM   29   C  CA  . LEU   A 1 14  ? -21.01300 9.92300  13.64100  1.000 65.80000  ? 540  LEU   A CA  1 
ATOM   30   C  C   . LEU   A 1 14  ? -20.90600 10.68500 14.95400  1.000 60.50000  ? 540  LEU   A C   1 
ATOM   31   O  O   . LEU   A 1 14  ? -21.89100 11.28300 15.40000  1.000 62.53000  ? 540  LEU   A O   1 
ATOM   32   C  CB  . LEU   A 1 14  ? -21.41300 8.46700  13.89600  1.000 59.10000  ? 540  LEU   A CB  1 
ATOM   33   C  CG  . LEU   A 1 14  ? -22.60800 8.14700  14.80600  1.000 64.23000  ? 540  LEU   A CG  1 
ATOM   34   C  CD1 . LEU   A 1 14  ? -23.81900 9.02400  14.50600  1.000 50.58000  ? 540  LEU   A CD1 1 
ATOM   35   C  CD2 . LEU   A 1 14  ? -22.98200 6.67600  14.69400  1.000 65.77000  ? 540  LEU   A CD2 1 
ATOM   36   N  N   . GLN   A 1 15  ? -19.72800 10.69400 15.58200  1.000 70.57000  ? 541  GLN   A N   1 
ATOM   37   C  CA  . GLN   A 1 15  ? -19.61900 11.36000 16.87600  1.000 68.86000  ? 541  GLN   A CA  1 
ATOM   38   C  C   . GLN   A 1 15  ? -19.74400 12.87200 16.73800  1.000 66.75000  ? 541  GLN   A C   1 
ATOM   39   O  O   . GLN   A 1 15  ? -20.41100 13.52000 17.55300  1.000 65.11000  ? 541  GLN   A O   1 
ATOM   40   C  CB  . GLN   A 1 15  ? -18.30900 10.98300 17.57200  1.000 68.62000  ? 541  GLN   A CB  1 
ATOM   41   C  CG  . GLN   A 1 15  ? -18.07000 11.61200 18.97000  1.000 92.28000  ? 541  GLN   A CG  1 
ATOM   42   C  CD  . GLN   A 1 15  ? -19.30300 11.71500 19.88700  1.000 102.68000 ? 541  GLN   A CD  1 
ATOM   43   O  OE1 . GLN   A 1 15  ? -20.33800 11.08400 19.66600  1.000 94.69000  ? 541  GLN   A OE1 1 
ATOM   44   N  NE2 . GLN   A 1 15  ? -19.17500 12.52400 20.93300  1.000 95.13000  ? 541  GLN   A NE2 1 
ATOM   45   N  N   . SER   A 1 16  ? -19.12000 13.45800 15.71300  1.000 62.34000  ? 542  SER   A N   1 
ATOM   46   C  CA  . SER   A 1 16  ? -19.23400 14.90100 15.53200  1.000 70.85000  ? 542  SER   A CA  1 
ATOM   47   C  C   . SER   A 1 16  ? -20.61300 15.29500 15.01800  1.000 59.67000  ? 542  SER   A C   1 
ATOM   48   O  O   . SER   A 1 16  ? -21.08300 16.40300 15.30200  1.000 60.50000  ? 542  SER   A O   1 
ATOM   49   C  CB  . SER   A 1 16  ? -18.14600 15.40100 14.58400  1.000 68.16000  ? 542  SER   A CB  1 
ATOM   50   O  OG  . SER   A 1 16  ? -16.93700 14.69500 14.79100  1.000 72.42000  ? 542  SER   A OG  1 
ATOM   51   N  N   . LEU   A 1 17  ? -21.28000 14.40800 14.27500  1.000 67.36000  ? 543  LEU   A N   1 
ATOM   52   C  CA  . LEU   A 1 17  ? -22.61100 14.72600 13.76600  1.000 57.74000  ? 543  LEU   A CA  1 
ATOM   53   C  C   . LEU   A 1 17  ? -23.66000 14.63400 14.86800  1.000 48.89000  ? 543  LEU   A C   1 
ATOM   54   O  O   . LEU   A 1 17  ? -24.52500 15.50900 14.99100  1.000 47.17000  ? 543  LEU   A O   1 
ATOM   55   C  CB  . LEU   A 1 17  ? -22.97100 13.79500 12.60900  1.000 56.67000  ? 543  LEU   A CB  1 
ATOM   56   C  CG  . LEU   A 1 17  ? -24.42400 13.92600 12.14400  1.000 48.94000  ? 543  LEU   A CG  1 
ATOM   57   C  CD1 . LEU   A 1 17  ? -24.64500 15.26900 11.46600  1.000 40.51000  ? 543  LEU   A CD1 1 
ATOM   58   C  CD2 . LEU   A 1 17  ? -24.82100 12.78400 11.22700  1.000 51.64000  ? 543  LEU   A CD2 1 
ATOM   59   N  N   . ALA   A 1 18  ? -23.60300 13.57300 15.67600  1.000 55.54000  ? 544  ALA   A N   1 
ATOM   60   C  CA  . ALA   A 1 18  ? -24.60500 13.37100 16.71600  1.000 57.20000  ? 544  ALA   A CA  1 
ATOM   61   C  C   . ALA   A 1 18  ? -24.50700 14.40200 17.83200  1.000 51.36000  ? 544  ALA   A C   1 
ATOM   62   O  O   . ALA   A 1 18  ? -25.50800 14.65700 18.51000  1.000 59.66000  ? 544  ALA   A O   1 
ATOM   63   C  CB  . ALA   A 1 18  ? -24.48000 11.96200 17.29900  1.000 54.94000  ? 544  ALA   A CB  1 
ATOM   64   N  N   . ALA   A 1 19  ? -23.33500 15.00100 18.03600  1.000 52.25000  ? 545  ALA   A N   1 
ATOM   65   C  CA  . ALA   A 1 19  ? -23.14200 15.96700 19.10800  1.000 55.32000  ? 545  ALA   A CA  1 
ATOM   66   C  C   . ALA   A 1 19  ? -23.34000 17.41000 18.66400  1.000 58.54000  ? 545  ALA   A C   1 
ATOM   67   O  O   . ALA   A 1 19  ? -23.42000 18.29800 19.52000  1.000 72.27000  ? 545  ALA   A O   1 
ATOM   68   C  CB  . ALA   A 1 19  ? -21.74200 15.81100 19.71200  1.000 57.49000  ? 545  ALA   A CB  1 
ATOM   69   N  N   . ALA   A 1 20  ? -23.42600 17.66600 17.36300  1.000 63.18000  ? 546  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 20  ? -23.54600 19.02800 16.86800  1.000 53.75000  ? 546  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 20  ? -24.95900 19.56400 17.08000  1.000 51.64000  ? 546  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 20  ? -25.91400 18.81600 17.30600  1.000 62.89000  ? 546  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 20  ? -23.17800 19.09600 15.38600  1.000 54.96000  ? 546  ALA   A CB  1 
ATOM   74   N  N   . VAL   A 1 21  ? -25.07800 20.88400 17.00800  1.000 57.26000  ? 547  VAL   A N   1 
ATOM   75   C  CA  . VAL   A 1 21  ? -26.36600 21.56200 17.08000  1.000 57.06000  ? 547  VAL   A CA  1 
ATOM   76   C  C   . VAL   A 1 21  ? -26.90100 21.73200 15.66500  1.000 63.96000  ? 547  VAL   A C   1 
ATOM   77   O  O   . VAL   A 1 21  ? -26.14500 22.01700 14.72900  1.000 64.65000  ? 547  VAL   A O   1 
ATOM   78   C  CB  . VAL   A 1 21  ? -26.23500 22.91700 17.80500  1.000 61.22000  ? 547  VAL   A CB  1 
ATOM   79   C  CG1 . VAL   A 1 21  ? -25.15900 23.77600 17.15400  1.000 61.29000  ? 547  VAL   A CG1 1 
ATOM   80   C  CG2 . VAL   A 1 21  ? -27.57200 23.64900 17.83700  1.000 52.77000  ? 547  VAL   A CG2 1 
ATOM   81   N  N   . VAL   A 1 22  ? -28.20600 21.53700 15.50300  1.000 67.05000  ? 548  VAL   A N   1 
ATOM   82   C  CA  . VAL   A 1 22  ? -28.85600 21.62400 14.19500  1.000 57.22000  ? 548  VAL   A CA  1 
ATOM   83   C  C   . VAL   A 1 22  ? -29.39300 23.03800 14.03700  1.000 52.55000  ? 548  VAL   A C   1 
ATOM   84   O  O   . VAL   A 1 22  ? -30.34600 23.41300 14.74500  1.000 65.46000  ? 548  VAL   A O   1 
ATOM   85   C  CB  . VAL   A 1 22  ? -29.97700 20.58500 14.05800  1.000 54.23000  ? 548  VAL   A CB  1 
ATOM   86   C  CG1 . VAL   A 1 22  ? -30.58300 20.64200 12.66300  1.000 41.46000  ? 548  VAL   A CG1 1 
ATOM   87   C  CG2 . VAL   A 1 22  ? -29.44700 19.19300 14.36100  1.000 47.81000  ? 548  VAL   A CG2 1 
ATOM   88   N  N   . PRO   A 1 23  ? -28.83100 23.85600 13.14500  1.000 52.71000  ? 549  PRO   A N   1 
ATOM   89   C  CA  . PRO   A 1 23  ? -29.35200 25.21200 12.94300  1.000 47.37000  ? 549  PRO   A CA  1 
ATOM   90   C  C   . PRO   A 1 23  ? -30.77000 25.18600 12.39400  1.000 49.66000  ? 549  PRO   A C   1 
ATOM   91   O  O   . PRO   A 1 23  ? -31.27000 24.16900 11.91000  1.000 59.60000  ? 549  PRO   A O   1 
ATOM   92   C  CB  . PRO   A 1 23  ? -28.37100 25.82800 11.93900  1.000 46.27000  ? 549  PRO   A CB  1 
ATOM   93   C  CG  . PRO   A 1 23  ? -27.13200 24.99100 12.04900  1.000 51.22000  ? 549  PRO   A CG  1 
ATOM   94   C  CD  . PRO   A 1 23  ? -27.61500 23.60700 12.35200  1.000 48.32000  ? 549  PRO   A CD  1 
ATOM   95   N  N   . SER   A 1 24  ? -31.42200 26.34400 12.47200  1.000 51.36000  ? 550  SER   A N   1 
ATOM   96   C  CA  . SER   A 1 24  ? -32.79800 26.47000 12.02300  1.000 45.47000  ? 550  SER   A CA  1 
ATOM   97   C  C   . SER   A 1 24  ? -32.89900 26.23500 10.51500  1.000 53.13000  ? 550  SER   A C   1 
ATOM   98   O  O   . SER   A 1 24  ? -31.90300 26.21300 9.78800   1.000 59.41000  ? 550  SER   A O   1 
ATOM   99   C  CB  . SER   A 1 24  ? -33.34900 27.85000 12.38100  1.000 47.73000  ? 550  SER   A CB  1 
ATOM   100  O  OG  . SER   A 1 24  ? -34.30500 28.28200 11.42800  1.000 63.67000  ? 550  SER   A OG  1 
ATOM   101  N  N   . ALA   A 1 25  ? -34.13600 26.04700 10.05000  1.000 59.83000  ? 551  ALA   A N   1 
ATOM   102  C  CA  . ALA   A 1 25  ? -34.36400 25.88100 8.61800   1.000 62.71000  ? 551  ALA   A CA  1 
ATOM   103  C  C   . ALA   A 1 25  ? -34.05500 27.16500 7.85900   1.000 69.49000  ? 551  ALA   A C   1 
ATOM   104  O  O   . ALA   A 1 25  ? -33.54300 27.12100 6.73400   1.000 61.19000  ? 551  ALA   A O   1 
ATOM   105  C  CB  . ALA   A 1 25  ? -35.80300 25.43800 8.36200   1.000 46.08000  ? 551  ALA   A CB  1 
ATOM   106  N  N   . GLN   A 1 26  ? -34.35700 28.31900 8.46000   1.000 74.99000  ? 552  GLN   A N   1 
ATOM   107  C  CA  . GLN   A 1 26  ? -34.04300 29.59000 7.81700   1.000 66.95000  ? 552  GLN   A CA  1 
ATOM   108  C  C   . GLN   A 1 26  ? -32.54200 29.84400 7.78400   1.000 55.26000  ? 552  GLN   A C   1 
ATOM   109  O  O   . GLN   A 1 26  ? -32.04000 30.46300 6.83900   1.000 59.37000  ? 552  GLN   A O   1 
ATOM   110  C  CB  . GLN   A 1 26  ? -34.76200 30.73200 8.53500   1.000 53.93000  ? 552  GLN   A CB  1 
ATOM   111  C  CG  . GLN   A 1 26  ? -35.95000 31.29500 7.77100   1.000 76.56000  ? 552  GLN   A CG  1 
ATOM   112  C  CD  . GLN   A 1 26  ? -36.92800 30.22000 7.33400   1.000 91.07000  ? 552  GLN   A CD  1 
ATOM   113  O  OE1 . GLN   A 1 26  ? -37.28500 29.33400 8.11200   1.000 95.57000  ? 552  GLN   A OE1 1 
ATOM   114  N  NE2 . GLN   A 1 26  ? -37.36700 30.29300 6.08300   1.000 89.22000  ? 552  GLN   A NE2 1 
ATOM   115  N  N   . THR   A 1 27  ? -31.81200 29.37800 8.80000   1.000 50.83000  ? 553  THR   A N   1 
ATOM   116  C  CA  . THR   A 1 27  ? -30.36200 29.53400 8.80100   1.000 54.20000  ? 553  THR   A CA  1 
ATOM   117  C  C   . THR   A 1 27  ? -29.71600 28.68600 7.71200   1.000 66.22000  ? 553  THR   A C   1 
ATOM   118  O  O   . THR   A 1 27  ? -28.72200 29.09800 7.10200   1.000 53.92000  ? 553  THR   A O   1 
ATOM   119  C  CB  . THR   A 1 27  ? -29.79700 29.16700 10.17500  1.000 57.30000  ? 553  THR   A CB  1 
ATOM   120  O  OG1 . THR   A 1 27  ? -30.47400 29.92000 11.19000  1.000 69.15000  ? 553  THR   A OG1 1 
ATOM   121  C  CG2 . THR   A 1 27  ? -28.30500 29.46600 10.24300  1.000 50.50000  ? 553  THR   A CG2 1 
ATOM   122  N  N   . LEU   A 1 28  ? -30.27200 27.50500 7.44600   1.000 66.72000  ? 554  LEU   A N   1 
ATOM   123  C  CA  . LEU   A 1 28  ? -29.72300 26.58900 6.45500   1.000 54.27000  ? 554  LEU   A CA  1 
ATOM   124  C  C   . LEU   A 1 28  ? -30.25700 26.83300 5.04900   1.000 51.47000  ? 554  LEU   A C   1 
ATOM   125  O  O   . LEU   A 1 28  ? -29.78000 26.19200 4.10600   1.000 50.10000  ? 554  LEU   A O   1 
ATOM   126  C  CB  . LEU   A 1 28  ? -30.00600 25.14000 6.86800   1.000 52.02000  ? 554  LEU   A CB  1 
ATOM   127  C  CG  . LEU   A 1 28  ? -29.43200 24.71400 8.22200   1.000 57.57000  ? 554  LEU   A CG  1 
ATOM   128  C  CD1 . LEU   A 1 28  ? -29.91200 23.32100 8.60200   1.000 52.17000  ? 554  LEU   A CD1 1 
ATOM   129  C  CD2 . LEU   A 1 28  ? -27.91100 24.77700 8.21000   1.000 43.74000  ? 554  LEU   A CD2 1 
ATOM   130  N  N   . LYS   A 1 29  ? -31.23000 27.73500 4.89000   1.000 51.59000  ? 555  LYS   A N   1 
ATOM   131  C  CA  . LYS   A 1 29  ? -31.77300 28.11900 3.58400   1.000 45.21000  ? 555  LYS   A CA  1 
ATOM   132  C  C   . LYS   A 1 29  ? -32.40200 26.94000 2.84400   1.000 51.86000  ? 555  LYS   A C   1 
ATOM   133  O  O   . LYS   A 1 29  ? -32.47900 26.94200 1.61300   1.000 47.55000  ? 555  LYS   A O   1 
ATOM   134  C  CB  . LYS   A 1 29  ? -30.70700 28.77700 2.69800   1.000 55.52000  ? 555  LYS   A CB  1 
ATOM   135  C  CG  . LYS   A 1 29  ? -29.78800 29.75900 3.40600   1.000 51.27000  ? 555  LYS   A CG  1 
ATOM   136  C  CD  . LYS   A 1 29  ? -28.53600 30.01400 2.57700   1.000 53.20000  ? 555  LYS   A CD  1 
ATOM   137  C  CE  . LYS   A 1 29  ? -27.38500 30.51500 3.43500   1.000 59.17000  ? 555  LYS   A CE  1 
ATOM   138  N  NZ  . LYS   A 1 29  ? -26.06400 30.19900 2.82200   1.000 62.89000  ? 555  LYS   A NZ  1 
ATOM   139  N  N   . ILE   A 1 30  ? -32.86600 25.92300 3.57800   1.000 45.24000  ? 556  ILE   A N   1 
ATOM   140  C  CA  . ILE   A 1 30  ? -33.42500 24.73300 2.93600   1.000 42.90000  ? 556  ILE   A CA  1 
ATOM   141  C  C   . ILE   A 1 30  ? -34.87500 24.90700 2.52000   1.000 44.20000  ? 556  ILE   A C   1 
ATOM   142  O  O   . ILE   A 1 30  ? -35.44500 23.99200 1.91000   1.000 46.73000  ? 556  ILE   A O   1 
ATOM   143  C  CB  . ILE   A 1 30  ? -33.31100 23.49600 3.84800   1.000 43.01000  ? 556  ILE   A CB  1 
ATOM   144  C  CG1 . ILE   A 1 30  ? -34.02800 23.74100 5.17600   1.000 45.69000  ? 556  ILE   A CG1 1 
ATOM   145  C  CG2 . ILE   A 1 30  ? -31.85000 23.13500 4.07600   1.000 34.98000  ? 556  ILE   A CG2 1 
ATOM   146  C  CD1 . ILE   A 1 30  ? -34.16400 22.50200 6.02100   1.000 40.20000  ? 556  ILE   A CD1 1 
ATOM   147  N  N   . THR   A 1 31  ? -35.49400 26.04700 2.82600   1.000 45.13000  ? 557  THR   A N   1 
ATOM   148  C  CA  . THR   A 1 31  ? -36.85300 26.32400 2.38000   1.000 44.89000  ? 557  THR   A CA  1 
ATOM   149  C  C   . THR   A 1 31  ? -36.89600 27.01800 1.02400   1.000 47.50000  ? 557  THR   A C   1 
ATOM   150  O  O   . THR   A 1 31  ? -37.90700 26.91400 0.31900   1.000 49.11000  ? 557  THR   A O   1 
ATOM   151  C  CB  . THR   A 1 31  ? -37.58600 27.17800 3.42400   1.000 59.29000  ? 557  THR   A CB  1 
ATOM   152  O  OG1 . THR   A 1 31  ? -37.41200 26.59500 4.72200   1.000 66.49000  ? 557  THR   A OG1 1 
ATOM   153  C  CG2 . THR   A 1 31  ? -39.07900 27.25700 3.12000   1.000 50.73000  ? 557  THR   A CG2 1 
ATOM   154  N  N   . ASP   A 1 32  ? -35.82200 27.70000 0.63500   1.000 50.99000  ? 558  ASP   A N   1 
ATOM   155  C  CA  . ASP   A 1 32  ? -35.78500 28.36400 -0.66000  1.000 49.55000  ? 558  ASP   A CA  1 
ATOM   156  C  C   . ASP   A 1 32  ? -35.73400 27.34000 -1.78600  1.000 49.75000  ? 558  ASP   A C   1 
ATOM   157  O  O   . ASP   A 1 32  ? -35.00000 26.35000 -1.71600  1.000 53.27000  ? 558  ASP   A O   1 
ATOM   158  C  CB  . ASP   A 1 32  ? -34.57200 29.29100 -0.75100  1.000 54.26000  ? 558  ASP   A CB  1 
ATOM   159  C  CG  . ASP   A 1 32  ? -34.31600 30.04800 0.53500   1.000 65.34000  ? 558  ASP   A CG  1 
ATOM   160  O  OD1 . ASP   A 1 32  ? -35.29000 30.35300 1.25400   1.000 74.42000  ? 558  ASP   A OD1 1 
ATOM   161  O  OD2 . ASP   A 1 32  ? -33.13600 30.33900 0.82700   1.000 60.25000  ? 558  ASP   A OD2 1 
ATOM   162  N  N   . PHE   A 1 33  ? -36.52300 27.58400 -2.83600  1.000 47.26000  ? 559  PHE   A N   1 
ATOM   163  C  CA  . PHE   A 1 33  ? -36.42500 26.76800 -4.03900  1.000 40.09000  ? 559  PHE   A CA  1 
ATOM   164  C  C   . PHE   A 1 33  ? -35.08000 26.93500 -4.73200  1.000 42.93000  ? 559  PHE   A C   1 
ATOM   165  O  O   . PHE   A 1 33  ? -34.67400 26.05300 -5.49700  1.000 59.44000  ? 559  PHE   A O   1 
ATOM   166  C  CB  . PHE   A 1 33  ? -37.55200 27.11800 -5.01300  1.000 35.40000  ? 559  PHE   A CB  1 
ATOM   167  C  CG  . PHE   A 1 33  ? -38.88500 26.53200 -4.64000  1.000 44.61000  ? 559  PHE   A CG  1 
ATOM   168  C  CD1 . PHE   A 1 33  ? -39.08500 25.16100 -4.66000  1.000 54.96000  ? 559  PHE   A CD1 1 
ATOM   169  C  CD2 . PHE   A 1 33  ? -39.94200 27.35300 -4.28100  1.000 48.71000  ? 559  PHE   A CD2 1 
ATOM   170  C  CE1 . PHE   A 1 33  ? -40.31300 24.61900 -4.32200  1.000 49.11000  ? 559  PHE   A CE1 1 
ATOM   171  C  CE2 . PHE   A 1 33  ? -41.17200 26.81800 -3.94200  1.000 49.86000  ? 559  PHE   A CE2 1 
ATOM   172  C  CZ  . PHE   A 1 33  ? -41.35700 25.44900 -3.96300  1.000 57.57000  ? 559  PHE   A CZ  1 
ATOM   173  N  N   . SER   A 1 34  ? -34.38400 28.04300 -4.48100  1.000 48.51000  ? 560  SER   A N   1 
ATOM   174  C  CA  . SER   A 1 34  ? -33.08900 28.32500 -5.08000  1.000 42.92000  ? 560  SER   A CA  1 
ATOM   175  C  C   . SER   A 1 34  ? -31.92600 27.83500 -4.22600  1.000 41.33000  ? 560  SER   A C   1 
ATOM   176  O  O   . SER   A 1 34  ? -30.79600 28.30000 -4.41100  1.000 52.58000  ? 560  SER   A O   1 
ATOM   177  C  CB  . SER   A 1 34  ? -32.94800 29.82700 -5.33700  1.000 46.46000  ? 560  SER   A CB  1 
ATOM   178  O  OG  . SER   A 1 34  ? -32.63500 30.51700 -4.13900  1.000 51.64000  ? 560  SER   A OG  1 
ATOM   179  N  N   . PHE   A 1 35  ? -32.18000 26.91500 -3.29700  1.000 43.23000  ? 561  PHE   A N   1 
ATOM   180  C  CA  . PHE   A 1 35  ? -31.12500 26.41700 -2.42400  1.000 36.73000  ? 561  PHE   A CA  1 
ATOM   181  C  C   . PHE   A 1 35  ? -30.01800 25.76200 -3.23900  1.000 41.30000  ? 561  PHE   A C   1 
ATOM   182  O  O   . PHE   A 1 35  ? -30.27600 25.07000 -4.22800  1.000 46.34000  ? 561  PHE   A O   1 
ATOM   183  C  CB  . PHE   A 1 35  ? -31.70300 25.42000 -1.41500  1.000 45.44000  ? 561  PHE   A CB  1 
ATOM   184  C  CG  . PHE   A 1 35  ? -30.66000 24.65300 -0.63700  1.000 37.48000  ? 561  PHE   A CG  1 
ATOM   185  C  CD1 . PHE   A 1 35  ? -30.16700 25.14800 0.55900   1.000 38.62000  ? 561  PHE   A CD1 1 
ATOM   186  C  CD2 . PHE   A 1 35  ? -30.19000 23.42800 -1.09200  1.000 30.42000  ? 561  PHE   A CD2 1 
ATOM   187  C  CE1 . PHE   A 1 35  ? -29.21600 24.44500 1.28100   1.000 31.41000  ? 561  PHE   A CE1 1 
ATOM   188  C  CE2 . PHE   A 1 35  ? -29.23700 22.72300 -0.37600  1.000 41.89000  ? 561  PHE   A CE2 1 
ATOM   189  C  CZ  . PHE   A 1 35  ? -28.75100 23.23200 0.81300   1.000 38.28000  ? 561  PHE   A CZ  1 
ATOM   190  N  N   . SER   A 1 36  ? -28.77600 25.98700 -2.81800  1.000 37.04000  ? 562  SER   A N   1 
ATOM   191  C  CA  . SER   A 1 36  ? -27.61800 25.34000 -3.41400  1.000 42.08000  ? 562  SER   A CA  1 
ATOM   192  C  C   . SER   A 1 36  ? -26.72900 24.79000 -2.30900  1.000 43.19000  ? 562  SER   A C   1 
ATOM   193  O  O   . SER   A 1 36  ? -26.59800 25.40000 -1.24300  1.000 40.64000  ? 562  SER   A O   1 
ATOM   194  C  CB  . SER   A 1 36  ? -26.82400 26.30300 -4.29300  1.000 46.17000  ? 562  SER   A CB  1 
ATOM   195  O  OG  . SER   A 1 36  ? -25.56600 25.74600 -4.62300  1.000 43.39000  ? 562  SER   A OG  1 
ATOM   196  N  N   . ASP   A 1 37  ? -26.11800 23.63600 -2.57100  1.000 47.09000  ? 563  ASP   A N   1 
ATOM   197  C  CA  . ASP   A 1 37  ? -25.30500 22.92700 -1.59000  1.000 47.32000  ? 563  ASP   A CA  1 
ATOM   198  C  C   . ASP   A 1 37  ? -23.81000 23.10800 -1.81400  1.000 48.37000  ? 563  ASP   A C   1 
ATOM   199  O  O   . ASP   A 1 37  ? -23.01100 22.43000 -1.15800  1.000 38.32000  ? 563  ASP   A O   1 
ATOM   200  C  CB  . ASP   A 1 37  ? -25.63500 21.43500 -1.62100  1.000 36.13000  ? 563  ASP   A CB  1 
ATOM   201  C  CG  . ASP   A 1 37  ? -25.01400 20.73800 -2.81600  1.000 38.83000  ? 563  ASP   A CG  1 
ATOM   202  O  OD1 . ASP   A 1 37  ? -25.28000 21.18300 -3.95200  1.000 45.42000  ? 563  ASP   A OD1 1 
ATOM   203  O  OD2 . ASP   A 1 37  ? -24.25900 19.76200 -2.63000  1.000 45.46000  ? 563  ASP   A OD2 1 
ATOM   204  N  N   . PHE   A 1 38  ? -23.41600 24.00100 -2.72200  1.000 46.82000  ? 564  PHE   A N   1 
ATOM   205  C  CA  . PHE   A 1 38  ? -22.03300 24.02000 -3.19200  1.000 46.43000  ? 564  PHE   A CA  1 
ATOM   206  C  C   . PHE   A 1 38  ? -21.05600 24.32800 -2.06200  1.000 58.27000  ? 564  PHE   A C   1 
ATOM   207  O  O   . PHE   A 1 38  ? -20.05400 23.62600 -1.88400  1.000 63.99000  ? 564  PHE   A O   1 
ATOM   208  C  CB  . PHE   A 1 38  ? -21.88000 25.03800 -4.31700  1.000 55.92000  ? 564  PHE   A CB  1 
ATOM   209  C  CG  . PHE   A 1 38  ? -22.39400 24.55400 -5.64000  1.000 53.99000  ? 564  PHE   A CG  1 
ATOM   210  C  CD1 . PHE   A 1 38  ? -22.70300 23.21000 -5.83800  1.000 59.56000  ? 564  PHE   A CD1 1 
ATOM   211  C  CD2 . PHE   A 1 38  ? -22.56600 25.43700 -6.68700  1.000 58.61000  ? 564  PHE   A CD2 1 
ATOM   212  C  CE1 . PHE   A 1 38  ? -23.16900 22.76800 -7.05200  1.000 54.81000  ? 564  PHE   A CE1 1 
ATOM   213  C  CE2 . PHE   A 1 38  ? -23.02700 24.99900 -7.90400  1.000 41.54000  ? 564  PHE   A CE2 1 
ATOM   214  C  CZ  . PHE   A 1 38  ? -23.33000 23.66100 -8.08500  1.000 56.08000  ? 564  PHE   A CZ  1 
ATOM   215  N  N   . GLU   A 1 39  ? -21.33100 25.37300 -1.28100  1.000 48.34000  ? 565  GLU   A N   1 
ATOM   216  C  CA  . GLU   A 1 39  ? -20.41300 25.80800 -0.23200  1.000 52.07000  ? 565  GLU   A CA  1 
ATOM   217  C  C   . GLU   A 1 39  ? -20.47000 24.94100 1.01800   1.000 54.77000  ? 565  GLU   A C   1 
ATOM   218  O  O   . GLU   A 1 39  ? -19.80500 25.27300 2.00600   1.000 55.02000  ? 565  GLU   A O   1 
ATOM   219  C  CB  . GLU   A 1 39  ? -20.72000 27.25600 0.14400   1.000 45.88000  ? 565  GLU   A CB  1 
ATOM   220  C  CG  . GLU   A 1 39  ? -22.06000 27.44000 0.84200   1.000 43.04000  ? 565  GLU   A CG  1 
ATOM   221  C  CD  . GLU   A 1 39  ? -23.21600 27.57200 -0.13400  1.000 51.13000  ? 565  GLU   A CD  1 
ATOM   222  O  OE1 . GLU   A 1 39  ? -23.05200 27.19800 -1.31500  1.000 50.43000  ? 565  GLU   A OE1 1 
ATOM   223  O  OE2 . GLU   A 1 39  ? -24.29400 28.04600 0.28000   1.000 56.40000  ? 565  GLU   A OE2 1 
ATOM   224  N  N   . LEU   A 1 40  ? -21.22500 23.84500 1.00400   1.000 49.09000  ? 566  LEU   A N   1 
ATOM   225  C  CA  . LEU   A 1 40  ? -21.49800 23.07100 2.20500   1.000 43.26000  ? 566  LEU   A CA  1 
ATOM   226  C  C   . LEU   A 1 40  ? -20.58000 21.86000 2.29600   1.000 41.61000  ? 566  LEU   A C   1 
ATOM   227  O  O   . LEU   A 1 40  ? -20.22500 21.25400 1.28000   1.000 50.11000  ? 566  LEU   A O   1 
ATOM   228  C  CB  . LEU   A 1 40  ? -22.95700 22.61800 2.23400   1.000 43.25000  ? 566  LEU   A CB  1 
ATOM   229  C  CG  . LEU   A 1 40  ? -24.01100 23.72400 2.20100   1.000 48.29000  ? 566  LEU   A CG  1 
ATOM   230  C  CD1 . LEU   A 1 40  ? -25.40100 23.13400 2.37600   1.000 40.71000  ? 566  LEU   A CD1 1 
ATOM   231  C  CD2 . LEU   A 1 40  ? -23.72500 24.76900 3.26900   1.000 40.51000  ? 566  LEU   A CD2 1 
ATOM   232  N  N   . SER   A 1 41  ? -20.20200 21.51700 3.52400   1.000 46.39000  ? 567  SER   A N   1 
ATOM   233  C  CA  . SER   A 1 41  ? -19.46800 20.29300 3.78600   1.000 42.45000  ? 567  SER   A CA  1 
ATOM   234  C  C   . SER   A 1 41  ? -20.40500 19.09200 3.66800   1.000 43.60000  ? 567  SER   A C   1 
ATOM   235  O  O   . SER   A 1 41  ? -21.61300 19.22500 3.45000   1.000 45.42000  ? 567  SER   A O   1 
ATOM   236  C  CB  . SER   A 1 41  ? -18.83000 20.34700 5.17100   1.000 40.35000  ? 567  SER   A CB  1 
ATOM   237  O  OG  . SER   A 1 41  ? -19.79800 20.10100 6.17900   1.000 53.82000  ? 567  SER   A OG  1 
ATOM   238  N  N   . ASP   A 1 42  ? -19.83500 17.89500 3.80600   1.000 38.24000  ? 568  ASP   A N   1 
ATOM   239  C  CA  . ASP   A 1 42  ? -20.66900 16.70300 3.91600   1.000 43.87000  ? 568  ASP   A CA  1 
ATOM   240  C  C   . ASP   A 1 42  ? -21.43600 16.69900 5.23100   1.000 44.81000  ? 568  ASP   A C   1 
ATOM   241  O  O   . ASP   A 1 42  ? -22.60600 16.30100 5.27400   1.000 48.66000  ? 568  ASP   A O   1 
ATOM   242  C  CB  . ASP   A 1 42  ? -19.81100 15.44600 3.78600   1.000 42.03000  ? 568  ASP   A CB  1 
ATOM   243  C  CG  . ASP   A 1 42  ? -19.47600 15.11500 2.34700   1.000 50.17000  ? 568  ASP   A CG  1 
ATOM   244  O  OD1 . ASP   A 1 42  ? -20.12800 15.67200 1.43800   1.000 48.35000  ? 568  ASP   A OD1 1 
ATOM   245  O  OD2 . ASP   A 1 42  ? -18.56300 14.29300 2.12400   1.000 57.23000  ? 568  ASP   A OD2 1 
ATOM   246  N  N   . LEU   A 1 43  ? -20.79600 17.15100 6.31300   1.000 46.29000  ? 569  LEU   A N   1 
ATOM   247  C  CA  . LEU   A 1 43  ? -21.46900 17.21600 7.60600   1.000 43.51000  ? 569  LEU   A CA  1 
ATOM   248  C  C   . LEU   A 1 43  ? -22.56200 18.27700 7.61900   1.000 33.84000  ? 569  LEU   A C   1 
ATOM   249  O  O   . LEU   A 1 43  ? -23.58800 18.09800 8.28500   1.000 45.28000  ? 569  LEU   A O   1 
ATOM   250  C  CB  . LEU   A 1 43  ? -20.45000 17.48800 8.71300   1.000 51.65000  ? 569  LEU   A CB  1 
ATOM   251  C  CG  . LEU   A 1 43  ? -20.98000 17.53800 10.14800  1.000 64.61000  ? 569  LEU   A CG  1 
ATOM   252  C  CD1 . LEU   A 1 43  ? -20.26000 16.52300 11.02100  1.000 61.35000  ? 569  LEU   A CD1 1 
ATOM   253  C  CD2 . LEU   A 1 43  ? -20.84100 18.93900 10.72300  1.000 59.40000  ? 569  LEU   A CD2 1 
ATOM   254  N  N   . GLU   A 1 44  ? -22.36600 19.38000 6.89400   1.000 43.74000  ? 570  GLU   A N   1 
ATOM   255  C  CA  . GLU   A 1 44  ? -23.38400 20.42400 6.85200   1.000 36.38000  ? 570  GLU   A CA  1 
ATOM   256  C  C   . GLU   A 1 44  ? -24.64200 19.94100 6.13900   1.000 43.64000  ? 570  GLU   A C   1 
ATOM   257  O  O   . GLU   A 1 44  ? -25.75900 20.29500 6.53200   1.000 44.54000  ? 570  GLU   A O   1 
ATOM   258  C  CB  . GLU   A 1 44  ? -22.82500 21.67400 6.17500   1.000 41.27000  ? 570  GLU   A CB  1 
ATOM   259  C  CG  . GLU   A 1 44  ? -21.86600 22.47100 7.04500   1.000 46.24000  ? 570  GLU   A CG  1 
ATOM   260  C  CD  . GLU   A 1 44  ? -21.42100 23.76400 6.39100   1.000 49.44000  ? 570  GLU   A CD  1 
ATOM   261  O  OE1 . GLU   A 1 44  ? -20.59800 23.70400 5.45300   1.000 43.19000  ? 570  GLU   A OE1 1 
ATOM   262  O  OE2 . GLU   A 1 44  ? -21.89400 24.84000 6.81400   1.000 50.78000  ? 570  GLU   A OE2 1 
ATOM   263  N  N   . THR   A 1 45  ? -24.48200 19.13400 5.08600   1.000 34.58000  ? 571  THR   A N   1 
ATOM   264  C  CA  . THR   A 1 45  ? -25.64900 18.56400 4.42000   1.000 41.64000  ? 571  THR   A CA  1 
ATOM   265  C  C   . THR   A 1 45  ? -26.36100 17.55600 5.31200   1.000 36.68000  ? 571  THR   A C   1 
ATOM   266  O  O   . THR   A 1 45  ? -27.58800 17.42700 5.24300   1.000 36.68000  ? 571  THR   A O   1 
ATOM   267  C  CB  . THR   A 1 45  ? -25.24300 17.90800 3.09800   1.000 32.41000  ? 571  THR   A CB  1 
ATOM   268  O  OG1 . THR   A 1 45  ? -24.34800 16.81900 3.35500   1.000 36.51000  ? 571  THR   A OG1 1 
ATOM   269  C  CG2 . THR   A 1 45  ? -24.56100 18.91700 2.18700   1.000 31.61000  ? 571  THR   A CG2 1 
ATOM   270  N  N   . ALA   A 1 46  ? -25.61300 16.83900 6.15400   1.000 41.03000  ? 572  ALA   A N   1 
ATOM   271  C  CA  . ALA   A 1 46  ? -26.23800 15.90600 7.08600   1.000 39.85000  ? 572  ALA   A CA  1 
ATOM   272  C  C   . ALA   A 1 46  ? -27.07200 16.64200 8.12600   1.000 38.09000  ? 572  ALA   A C   1 
ATOM   273  O  O   . ALA   A 1 46  ? -28.13400 16.15800 8.53500   1.000 43.55000  ? 572  ALA   A O   1 
ATOM   274  C  CB  . ALA   A 1 46  ? -25.17200 15.04400 7.76100   1.000 39.97000  ? 572  ALA   A CB  1 
ATOM   275  N  N   . LEU   A 1 47  ? -26.60900 17.81500 8.56600   1.000 45.53000  ? 573  LEU   A N   1 
ATOM   276  C  CA  . LEU   A 1 47  ? -27.38200 18.60200 9.52100   1.000 38.27000  ? 573  LEU   A CA  1 
ATOM   277  C  C   . LEU   A 1 47  ? -28.61600 19.20400 8.86400   1.000 36.76000  ? 573  LEU   A C   1 
ATOM   278  O  O   . LEU   A 1 47  ? -29.67200 19.31400 9.49800   1.000 47.65000  ? 573  LEU   A O   1 
ATOM   279  C  CB  . LEU   A 1 47  ? -26.50600 19.69500 10.13200  1.000 44.23000  ? 573  LEU   A CB  1 
ATOM   280  C  CG  . LEU   A 1 47  ? -25.29400 19.20900 10.93000  1.000 50.63000  ? 573  LEU   A CG  1 
ATOM   281  C  CD1 . LEU   A 1 47  ? -24.27000 20.32200 11.08600  1.000 40.39000  ? 573  LEU   A CD1 1 
ATOM   282  C  CD2 . LEU   A 1 47  ? -25.72600 18.67600 12.28800  1.000 49.07000  ? 573  LEU   A CD2 1 
ATOM   283  N  N   . CYS   A 1 48  ? -28.50200 19.60300 7.59400   1.000 52.14000  ? 574  CYS   A N   1 
ATOM   284  C  CA  . CYS   A 1 48  ? -29.67400 20.06400 6.85700   1.000 38.37000  ? 574  CYS   A CA  1 
ATOM   285  C  C   . CYS   A 1 48  ? -30.70200 18.95000 6.71700   1.000 39.67000  ? 574  CYS   A C   1 
ATOM   286  O  O   . CYS   A 1 48  ? -31.91200 19.20100 6.76700   1.000 40.35000  ? 574  CYS   A O   1 
ATOM   287  C  CB  . CYS   A 1 48  ? -29.26300 20.58400 5.48000   1.000 49.97000  ? 574  CYS   A CB  1 
ATOM   288  S  SG  . CYS   A 1 48  ? -28.21800 22.05600 5.49900   1.000 47.97000  ? 574  CYS   A SG  1 
ATOM   289  N  N   . THR   A 1 49  ? -30.23800 17.71100 6.54400   1.000 40.76000  ? 575  THR   A N   1 
ATOM   290  C  CA  . THR   A 1 49  ? -31.15600 16.58300 6.43800   1.000 42.08000  ? 575  THR   A CA  1 
ATOM   291  C  C   . THR   A 1 49  ? -31.85100 16.31100 7.76800   1.000 41.26000  ? 575  THR   A C   1 
ATOM   292  O  O   . THR   A 1 49  ? -33.03300 15.94700 7.79300   1.000 38.60000  ? 575  THR   A O   1 
ATOM   293  C  CB  . THR   A 1 49  ? -30.40500 15.34200 5.95500   1.000 39.82000  ? 575  THR   A CB  1 
ATOM   294  O  OG1 . THR   A 1 49  ? -29.64300 15.67000 4.78500   1.000 37.34000  ? 575  THR   A OG1 1 
ATOM   295  C  CG2 . THR   A 1 49  ? -31.37800 14.22700 5.61600   1.000 35.01000  ? 575  THR   A CG2 1 
ATOM   296  N  N   . ILE   A 1 50  ? -31.13600 16.48100 8.88300   1.000 36.52000  ? 576  ILE   A N   1 
ATOM   297  C  CA  . ILE   A 1 50  ? -31.76600 16.34800 10.19400  1.000 34.43000  ? 576  ILE   A CA  1 
ATOM   298  C  C   . ILE   A 1 50  ? -32.84700 17.40500 10.36900  1.000 37.30000  ? 576  ILE   A C   1 
ATOM   299  O  O   . ILE   A 1 50  ? -33.93500 17.12500 10.88800  1.000 40.94000  ? 576  ILE   A O   1 
ATOM   300  C  CB  . ILE   A 1 50  ? -30.70900 16.43200 11.31200  1.000 37.86000  ? 576  ILE   A CB  1 
ATOM   301  C  CG1 . ILE   A 1 50  ? -29.81400 15.19300 11.30700  1.000 39.44000  ? 576  ILE   A CG1 1 
ATOM   302  C  CG2 . ILE   A 1 50  ? -31.37700 16.58300 12.66900  1.000 34.57000  ? 576  ILE   A CG2 1 
ATOM   303  C  CD1 . ILE   A 1 50  ? -28.65300 15.27400 12.27400  1.000 42.18000  ? 576  ILE   A CD1 1 
ATOM   304  N  N   . ARG   A 1 51  ? -32.56900 18.63500 9.92900   1.000 40.09000  ? 577  ARG   A N   1 
ATOM   305  C  CA  . ARG   A 1 51  ? -33.54900 19.71000 10.04900  1.000 40.68000  ? 577  ARG   A CA  1 
ATOM   306  C  C   . ARG   A 1 51  ? -34.79700 19.41500 9.22600   1.000 40.43000  ? 577  ARG   A C   1 
ATOM   307  O  O   . ARG   A 1 51  ? -35.91500 19.75300 9.63500   1.000 43.39000  ? 577  ARG   A O   1 
ATOM   308  C  CB  . ARG   A 1 51  ? -32.91700 21.03700 9.62200   1.000 47.30000  ? 577  ARG   A CB  1 
ATOM   309  C  CG  . ARG   A 1 51  ? -33.87500 22.21800 9.58400   1.000 41.63000  ? 577  ARG   A CG  1 
ATOM   310  C  CD  . ARG   A 1 51  ? -34.60100 22.39500 10.90500  1.000 35.19000  ? 577  ARG   A CD  1 
ATOM   311  N  NE  . ARG   A 1 51  ? -33.68800 22.71700 11.99500  1.000 45.75000  ? 577  ARG   A NE  1 
ATOM   312  C  CZ  . ARG   A 1 51  ? -34.00500 22.62700 13.28200  1.000 47.17000  ? 577  ARG   A CZ  1 
ATOM   313  N  NH1 . ARG   A 1 51  ? -35.21500 22.22100 13.64000  1.000 46.41000  ? 577  ARG   A NH1 1 
ATOM   314  N  NH2 . ARG   A 1 51  ? -33.11200 22.94000 14.21000  1.000 47.81000  ? 577  ARG   A NH2 1 
ATOM   315  N  N   . MET   A 1 52  ? -34.62900 18.78100 8.06400   1.000 42.07000  ? 578  MET   A N   1 
ATOM   316  C  CA  . MET   A 1 52  ? -35.78400 18.43800 7.24100   1.000 42.82000  ? 578  MET   A CA  1 
ATOM   317  C  C   . MET   A 1 52  ? -36.65300 17.38600 7.91900   1.000 41.60000  ? 578  MET   A C   1 
ATOM   318  O  O   . MET   A 1 52  ? -37.88600 17.47300 7.88100   1.000 45.06000  ? 578  MET   A O   1 
ATOM   319  C  CB  . MET   A 1 52  ? -35.32200 17.96400 5.86500   1.000 37.64000  ? 578  MET   A CB  1 
ATOM   320  C  CG  . MET   A 1 52  ? -34.66600 19.05900 5.04100   1.000 52.73000  ? 578  MET   A CG  1 
ATOM   321  S  SD  . MET   A 1 52  ? -33.31900 18.46800 4.00400   1.000 56.78000  ? 578  MET   A SD  1 
ATOM   322  C  CE  . MET   A 1 52  ? -34.19700 17.30200 2.98500   1.000 31.28000  ? 578  MET   A CE  1 
ATOM   323  N  N   . PHE   A 1 53  ? -36.03100 16.38400 8.54600   1.000 40.70000  ? 579  PHE   A N   1 
ATOM   324  C  CA  . PHE   A 1 53  ? -36.79400 15.42800 9.34000   1.000 38.76000  ? 579  PHE   A CA  1 
ATOM   325  C  C   . PHE   A 1 53  ? -37.42800 16.09800 10.55200  1.000 41.21000  ? 579  PHE   A C   1 
ATOM   326  O  O   . PHE   A 1 53  ? -38.53100 15.72200 10.96500  1.000 41.76000  ? 579  PHE   A O   1 
ATOM   327  C  CB  . PHE   A 1 53  ? -35.89400 14.27700 9.79300   1.000 39.88000  ? 579  PHE   A CB  1 
ATOM   328  C  CG  . PHE   A 1 53  ? -35.72800 13.19100 8.76800   1.000 45.66000  ? 579  PHE   A CG  1 
ATOM   329  C  CD1 . PHE   A 1 53  ? -36.61100 12.12300 8.72200   1.000 43.51000  ? 579  PHE   A CD1 1 
ATOM   330  C  CD2 . PHE   A 1 53  ? -34.68300 13.23000 7.86000   1.000 33.23000  ? 579  PHE   A CD2 1 
ATOM   331  C  CE1 . PHE   A 1 53  ? -36.45800 11.11800 7.78300   1.000 46.96000  ? 579  PHE   A CE1 1 
ATOM   332  C  CE2 . PHE   A 1 53  ? -34.52400 12.22800 6.91900   1.000 38.89000  ? 579  PHE   A CE2 1 
ATOM   333  C  CZ  . PHE   A 1 53  ? -35.41400 11.17200 6.88100   1.000 44.57000  ? 579  PHE   A CZ  1 
ATOM   334  N  N   . THR   A 1 54  ? -36.75200 17.09500 11.12600  1.000 45.07000  ? 580  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 54  ? -37.23200 17.73300 12.34600  1.000 44.61000  ? 580  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 54  ? -38.40400 18.66800 12.06800  1.000 46.70000  ? 580  THR   A C   1 
ATOM   337  O  O   . THR   A 1 54  ? -39.44900 18.57400 12.72100  1.000 50.60000  ? 580  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 54  ? -36.09000 18.49600 13.02100  1.000 50.77000  ? 580  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 54  ? -34.89000 17.71800 12.95100  1.000 48.58000  ? 580  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 54  ? -36.41800 18.77500 14.47700  1.000 47.05000  ? 580  THR   A CG2 1 
ATOM   341  N  N   . ASP   A 1 55  ? -38.25000 19.57400 11.09900  1.000 55.84000  ? 581  ASP   A N   1 
ATOM   342  C  CA  . ASP   A 1 55  ? -39.28900 20.56400 10.83600  1.000 45.65000  ? 581  ASP   A CA  1 
ATOM   343  C  C   . ASP   A 1 55  ? -40.52100 19.96000 10.17700  1.000 43.64000  ? 581  ASP   A C   1 
ATOM   344  O  O   . ASP   A 1 55  ? -41.57400 20.60500 10.15700  1.000 53.06000  ? 581  ASP   A O   1 
ATOM   345  C  CB  . ASP   A 1 55  ? -38.73200 21.69300 9.97000   1.000 44.45000  ? 581  ASP   A CB  1 
ATOM   346  C  CG  . ASP   A 1 55  ? -38.03600 22.76000 10.78900  1.000 50.93000  ? 581  ASP   A CG  1 
ATOM   347  O  OD1 . ASP   A 1 55  ? -37.66500 22.47400 11.94800  1.000 42.73000  ? 581  ASP   A OD1 1 
ATOM   348  O  OD2 . ASP   A 1 55  ? -37.86200 23.88600 10.27800  1.000 63.14000  ? 581  ASP   A OD2 1 
ATOM   349  N  N   . LEU   A 1 56  ? -40.41600 18.75000 9.63500   1.000 46.23000  ? 582  LEU   A N   1 
ATOM   350  C  CA  . LEU   A 1 56  ? -41.57300 18.02400 9.13100   1.000 53.00000  ? 582  LEU   A CA  1 
ATOM   351  C  C   . LEU   A 1 56  ? -42.24900 17.19100 10.21300  1.000 51.56000  ? 582  LEU   A C   1 
ATOM   352  O  O   . LEU   A 1 56  ? -43.16400 16.42100 9.90500   1.000 49.41000  ? 582  LEU   A O   1 
ATOM   353  C  CB  . LEU   A 1 56  ? -41.16900 17.13000 7.95600   1.000 41.93000  ? 582  LEU   A CB  1 
ATOM   354  C  CG  . LEU   A 1 56  ? -40.87800 17.85100 6.63700   1.000 42.99000  ? 582  LEU   A CG  1 
ATOM   355  C  CD1 . LEU   A 1 56  ? -40.27300 16.89500 5.62000   1.000 40.55000  ? 582  LEU   A CD1 1 
ATOM   356  C  CD2 . LEU   A 1 56  ? -42.13900 18.49900 6.08700   1.000 46.13000  ? 582  LEU   A CD2 1 
ATOM   357  N  N   . ASN   A 1 57  ? -41.80900 17.32800 11.46600  1.000 53.74000  ? 583  ASN   A N   1 
ATOM   358  C  CA  . ASN   A 1 57  ? -42.36100 16.61800 12.61900  1.000 53.50000  ? 583  ASN   A CA  1 
ATOM   359  C  C   . ASN   A 1 57  ? -42.23300 15.10300 12.49100  1.000 55.48000  ? 583  ASN   A C   1 
ATOM   360  O  O   . ASN   A 1 57  ? -42.91300 14.35800 13.20400  1.000 52.31000  ? 583  ASN   A O   1 
ATOM   361  C  CB  . ASN   A 1 57  ? -43.82400 17.00800 12.86300  1.000 47.94000  ? 583  ASN   A CB  1 
ATOM   362  C  CG  . ASN   A 1 57  ? -44.04200 18.50800 12.81500  1.000 62.92000  ? 583  ASN   A CG  1 
ATOM   363  O  OD1 . ASN   A 1 57  ? -44.85000 19.00400 12.03000  1.000 68.08000  ? 583  ASN   A OD1 1 
ATOM   364  N  ND2 . ASN   A 1 57  ? -43.31900 19.23800 13.65600  1.000 65.72000  ? 583  ASN   A ND2 1 
ATOM   365  N  N   . LEU   A 1 58  ? -41.36200 14.62900 11.59600  1.000 50.77000  ? 584  LEU   A N   1 
ATOM   366  C  CA  . LEU   A 1 58  ? -41.17500 13.19100 11.44000  1.000 48.77000  ? 584  LEU   A CA  1 
ATOM   367  C  C   . LEU   A 1 58  ? -40.44600 12.59700 12.63900  1.000 44.35000  ? 584  LEU   A C   1 
ATOM   368  O  O   . LEU   A 1 58  ? -40.72200 11.45900 13.03900  1.000 50.92000  ? 584  LEU   A O   1 
ATOM   369  C  CB  . LEU   A 1 58  ? -40.41300 12.89800 10.14800  1.000 45.82000  ? 584  LEU   A CB  1 
ATOM   370  C  CG  . LEU   A 1 58  ? -41.02800 13.46500 8.86700   1.000 44.00000  ? 584  LEU   A CG  1 
ATOM   371  C  CD1 . LEU   A 1 58  ? -40.19600 13.07600 7.65400   1.000 40.91000  ? 584  LEU   A CD1 1 
ATOM   372  C  CD2 . LEU   A 1 58  ? -42.46700 12.99800 8.71100   1.000 37.94000  ? 584  LEU   A CD2 1 
ATOM   373  N  N   . VAL   A 1 59  ? -39.51000 13.34900 13.22100  1.000 49.15000  ? 585  VAL   A N   1 
ATOM   374  C  CA  . VAL   A 1 59  ? -38.81700 12.87800 14.41500  1.000 47.06000  ? 585  VAL   A CA  1 
ATOM   375  C  C   . VAL   A 1 59  ? -39.78700 12.77100 15.58500  1.000 50.55000  ? 585  VAL   A C   1 
ATOM   376  O  O   . VAL   A 1 59  ? -39.72400 11.82500 16.37900  1.000 51.29000  ? 585  VAL   A O   1 
ATOM   377  C  CB  . VAL   A 1 59  ? -37.63300 13.80700 14.74300  1.000 38.73000  ? 585  VAL   A CB  1 
ATOM   378  C  CG1 . VAL   A 1 59  ? -36.92400 13.34700 16.01000  1.000 41.48000  ? 585  VAL   A CG1 1 
ATOM   379  C  CG2 . VAL   A 1 59  ? -36.66400 13.86600 13.57400  1.000 39.55000  ? 585  VAL   A CG2 1 
ATOM   380  N  N   . GLN   A 1 60  ? -40.70600 13.73000 15.70200  1.000 53.90000  ? 586  GLN   A N   1 
ATOM   381  C  CA  . GLN   A 1 60  ? -41.64200 13.74200 16.82000  1.000 55.69000  ? 586  GLN   A CA  1 
ATOM   382  C  C   . GLN   A 1 60  ? -42.74500 12.70500 16.64200  1.000 55.97000  ? 586  GLN   A C   1 
ATOM   383  O  O   . GLN   A 1 60  ? -43.00500 11.90300 17.54500  1.000 53.38000  ? 586  GLN   A O   1 
ATOM   384  C  CB  . GLN   A 1 60  ? -42.24500 15.14000 16.97700  1.000 56.79000  ? 586  GLN   A CB  1 
ATOM   385  C  CG  . GLN   A 1 60  ? -43.40500 15.20700 17.95500  1.000 57.09000  ? 586  GLN   A CG  1 
ATOM   386  C  CD  . GLN   A 1 60  ? -42.99100 14.84500 19.36600  1.000 67.83000  ? 586  GLN   A CD  1 
ATOM   387  O  OE1 . GLN   A 1 60  ? -41.94200 15.27400 19.84600  1.000 71.59000  ? 586  GLN   A OE1 1 
ATOM   388  N  NE2 . GLN   A 1 60  ? -43.81500 14.05000 20.03900  1.000 65.96000  ? 586  GLN   A NE2 1 
ATOM   389  N  N   . ASN   A 1 61  ? -43.40200 12.70300 15.47900  1.000 53.56000  ? 587  ASN   A N   1 
ATOM   390  C  CA  . ASN   A 1 61  ? -44.57800 11.86400 15.28400  1.000 56.48000  ? 587  ASN   A CA  1 
ATOM   391  C  C   . ASN   A 1 61  ? -44.24000 10.38300 15.17100  1.000 52.44000  ? 587  ASN   A C   1 
ATOM   392  O  O   . ASN   A 1 61  ? -45.13900 9.54600  15.30900  1.000 61.00000  ? 587  ASN   A O   1 
ATOM   393  C  CB  . ASN   A 1 61  ? -45.34300 12.31500 14.03900  1.000 48.50000  ? 587  ASN   A CB  1 
ATOM   394  C  CG  . ASN   A 1 61  ? -45.98300 13.67800 14.21300  1.000 54.72000  ? 587  ASN   A CG  1 
ATOM   395  O  OD1 . ASN   A 1 61  ? -46.20900 14.13100 15.33500  1.000 62.97000  ? 587  ASN   A OD1 1 
ATOM   396  N  ND2 . ASN   A 1 61  ? -46.28000 14.34000 13.10000  1.000 59.79000  ? 587  ASN   A ND2 1 
ATOM   397  N  N   . PHE   A 1 62  ? -42.97700 10.03500 14.92700  1.000 46.69000  ? 588  PHE   A N   1 
ATOM   398  C  CA  . PHE   A 1 62  ? -42.58200 8.63900  14.77600  1.000 50.19000  ? 588  PHE   A CA  1 
ATOM   399  C  C   . PHE   A 1 62  ? -41.48000 8.22900  15.74400  1.000 50.32000  ? 588  PHE   A C   1 
ATOM   400  O  O   . PHE   A 1 62  ? -40.93200 7.12800  15.61100  1.000 47.40000  ? 588  PHE   A O   1 
ATOM   401  C  CB  . PHE   A 1 62  ? -42.15800 8.36500  13.33000  1.000 45.96000  ? 588  PHE   A CB  1 
ATOM   402  C  CG  . PHE   A 1 62  ? -43.24500 8.63000  12.32700  1.000 56.06000  ? 588  PHE   A CG  1 
ATOM   403  C  CD1 . PHE   A 1 62  ? -44.32200 7.76700  12.21100  1.000 52.03000  ? 588  PHE   A CD1 1 
ATOM   404  C  CD2 . PHE   A 1 62  ? -43.19900 9.74800  11.51000  1.000 52.93000  ? 588  PHE   A CD2 1 
ATOM   405  C  CE1 . PHE   A 1 62  ? -45.32900 8.00800  11.29400  1.000 48.22000  ? 588  PHE   A CE1 1 
ATOM   406  C  CE2 . PHE   A 1 62  ? -44.20300 9.99500  10.59100  1.000 53.27000  ? 588  PHE   A CE2 1 
ATOM   407  C  CZ  . PHE   A 1 62  ? -45.26900 9.12300  10.48300  1.000 53.87000  ? 588  PHE   A CZ  1 
ATOM   408  N  N   . GLN   A 1 63  ? -41.14000 9.08800  16.70700  1.000 52.52000  ? 589  GLN   A N   1 
ATOM   409  C  CA  . GLN   A 1 63  ? -40.26600 8.73400  17.82800  1.000 53.21000  ? 589  GLN   A CA  1 
ATOM   410  C  C   . GLN   A 1 63  ? -38.90800 8.21800  17.35300  1.000 55.27000  ? 589  GLN   A C   1 
ATOM   411  O  O   . GLN   A 1 63  ? -38.45100 7.14400  17.75100  1.000 60.14000  ? 589  GLN   A O   1 
ATOM   412  C  CB  . GLN   A 1 63  ? -40.94800 7.71600  18.74500  1.000 58.45000  ? 589  GLN   A CB  1 
ATOM   413  C  CG  . GLN   A 1 63  ? -41.82800 8.33800  19.81700  1.000 69.47000  ? 589  GLN   A CG  1 
ATOM   414  C  CD  . GLN   A 1 63  ? -41.11300 8.47400  21.14800  1.000 81.13000  ? 589  GLN   A CD  1 
ATOM   415  O  OE1 . GLN   A 1 63  ? -40.11100 7.80500  21.39800  1.000 84.96000  ? 589  GLN   A OE1 1 
ATOM   416  N  NE2 . GLN   A 1 63  ? -41.62700 9.34500  22.00900  1.000 74.41000  ? 589  GLN   A NE2 1 
ATOM   417  N  N   . MET   A 1 64  ? -38.25700 8.99800  16.49400  1.000 51.51000  ? 590  MET   A N   1 
ATOM   418  C  CA  . MET   A 1 64  ? -36.91300 8.66400  16.04600  1.000 48.57000  ? 590  MET   A CA  1 
ATOM   419  C  C   . MET   A 1 64  ? -35.89500 9.11200  17.08700  1.000 46.89000  ? 590  MET   A C   1 
ATOM   420  O  O   . MET   A 1 64  ? -35.88800 10.27500 17.50100  1.000 55.15000  ? 590  MET   A O   1 
ATOM   421  C  CB  . MET   A 1 64  ? -36.60800 9.32400  14.70200  1.000 43.26000  ? 590  MET   A CB  1 
ATOM   422  C  CG  . MET   A 1 64  ? -37.57800 8.98300  13.58800  1.000 45.60000  ? 590  MET   A CG  1 
ATOM   423  S  SD  . MET   A 1 64  ? -37.08300 9.75300  12.03400  1.000 39.58000  ? 590  MET   A SD  1 
ATOM   424  C  CE  . MET   A 1 64  ? -38.50200 9.38500  11.00900  1.000 45.33000  ? 590  MET   A CE  1 
ATOM   425  N  N   . LYS   A 1 65  ? -35.03800 8.18900  17.51100  1.000 49.22000  ? 591  LYS   A N   1 
ATOM   426  C  CA  . LYS   A 1 65  ? -33.94900 8.53700  18.41000  1.000 55.35000  ? 591  LYS   A CA  1 
ATOM   427  C  C   . LYS   A 1 65  ? -32.81600 9.18100  17.62100  1.000 58.91000  ? 591  LYS   A C   1 
ATOM   428  O  O   . LYS   A 1 65  ? -32.51900 8.78100  16.49200  1.000 59.02000  ? 591  LYS   A O   1 
ATOM   429  C  CB  . LYS   A 1 65  ? -33.45300 7.30200  19.16200  1.000 53.64000  ? 591  LYS   A CB  1 
ATOM   430  C  CG  . LYS   A 1 65  ? -34.22300 7.02300  20.44900  1.000 63.91000  ? 591  LYS   A CG  1 
ATOM   431  C  CD  . LYS   A 1 65  ? -35.05800 5.75500  20.34300  1.000 77.06000  ? 591  LYS   A CD  1 
ATOM   432  C  CE  . LYS   A 1 65  ? -36.05000 5.64200  21.49100  1.000 77.00000  ? 591  LYS   A CE  1 
ATOM   433  N  NZ  . LYS   A 1 65  ? -37.11100 4.64100  21.19500  1.000 75.91000  ? 591  LYS   A NZ  1 
ATOM   434  N  N   . HIS   A 1 66  ? -32.18200 10.18400 18.23500  1.000 61.29000  ? 592  HIS   A N   1 
ATOM   435  C  CA  . HIS   A 1 66  ? -31.28100 11.07100 17.50300  1.000 42.28000  ? 592  HIS   A CA  1 
ATOM   436  C  C   . HIS   A 1 66  ? -30.11400 10.30900 16.88500  1.000 50.06000  ? 592  HIS   A C   1 
ATOM   437  O  O   . HIS   A 1 66  ? -29.77800 10.51100 15.71300  1.000 49.57000  ? 592  HIS   A O   1 
ATOM   438  C  CB  . HIS   A 1 66  ? -30.77400 12.17500 18.43200  1.000 58.90000  ? 592  HIS   A CB  1 
ATOM   439  C  CG  . HIS   A 1 66  ? -30.09400 13.30200 17.72000  1.000 53.55000  ? 592  HIS   A CG  1 
ATOM   440  N  ND1 . HIS   A 1 66  ? -30.78400 14.24200 16.98500  1.000 62.40000  ? 592  HIS   A ND1 1 
ATOM   441  C  CD2 . HIS   A 1 66  ? -28.78700 13.64400 17.63600  1.000 51.86000  ? 592  HIS   A CD2 1 
ATOM   442  C  CE1 . HIS   A 1 66  ? -29.93000 15.11300 16.47600  1.000 63.85000  ? 592  HIS   A CE1 1 
ATOM   443  N  NE2 . HIS   A 1 66  ? -28.71200 14.77300 16.85600  1.000 57.36000  ? 592  HIS   A NE2 1 
ATOM   444  N  N   . GLU   A 1 67  ? -29.48100 9.42600  17.66000  1.000 53.91000  ? 593  GLU   A N   1 
ATOM   445  C  CA  . GLU   A 1 67  ? -28.30800 8.71300  17.16400  1.000 53.38000  ? 593  GLU   A CA  1 
ATOM   446  C  C   . GLU   A 1 67  ? -28.65200 7.71100  16.07000  1.000 42.82000  ? 593  GLU   A C   1 
ATOM   447  O  O   . GLU   A 1 67  ? -27.77100 7.34800  15.28300  1.000 52.27000  ? 593  GLU   A O   1 
ATOM   448  C  CB  . GLU   A 1 67  ? -27.59500 8.00100  18.31600  1.000 62.73000  ? 593  GLU   A CB  1 
ATOM   449  C  CG  . GLU   A 1 67  ? -28.42700 6.92900  18.99900  1.000 64.25000  ? 593  GLU   A CG  1 
ATOM   450  C  CD  . GLU   A 1 67  ? -29.25100 7.47300  20.15100  1.000 72.09000  ? 593  GLU   A CD  1 
ATOM   451  O  OE1 . GLU   A 1 67  ? -29.71700 6.66500  20.98100  1.000 84.47000  ? 593  GLU   A OE1 1 
ATOM   452  O  OE2 . GLU   A 1 67  ? -29.43300 8.70600  20.22600  1.000 74.45000  ? 593  GLU   A OE2 1 
ATOM   453  N  N   . VAL   A 1 68  ? -29.90200 7.25400  16.00300  1.000 49.22000  ? 594  VAL   A N   1 
ATOM   454  C  CA  . VAL   A 1 68  ? -30.29900 6.34400  14.93300  1.000 45.88000  ? 594  VAL   A CA  1 
ATOM   455  C  C   . VAL   A 1 68  ? -30.50100 7.10600  13.62900  1.000 39.86000  ? 594  VAL   A C   1 
ATOM   456  O  O   . VAL   A 1 68  ? -30.09300 6.64300  12.55700  1.000 36.73000  ? 594  VAL   A O   1 
ATOM   457  C  CB  . VAL   A 1 68  ? -31.56100 5.56300  15.34000  1.000 48.47000  ? 594  VAL   A CB  1 
ATOM   458  C  CG1 . VAL   A 1 68  ? -32.04400 4.69000  14.19100  1.000 36.60000  ? 594  VAL   A CG1 1 
ATOM   459  C  CG2 . VAL   A 1 68  ? -31.28400 4.72100  16.57500  1.000 41.47000  ? 594  VAL   A CG2 1 
ATOM   460  N  N   . LEU   A 1 69  ? -31.12600 8.28500  13.69800  1.000 33.71000  ? 595  LEU   A N   1 
ATOM   461  C  CA  . LEU   A 1 69  ? -31.28400 9.10900  12.50400  1.000 38.49000  ? 595  LEU   A CA  1 
ATOM   462  C  C   . LEU   A 1 69  ? -29.93300 9.57900  11.97900  1.000 44.96000  ? 595  LEU   A C   1 
ATOM   463  O  O   . LEU   A 1 69  ? -29.70400 9.59800  10.76400  1.000 41.94000  ? 595  LEU   A O   1 
ATOM   464  C  CB  . LEU   A 1 69  ? -32.18900 10.30400 12.80300  1.000 34.77000  ? 595  LEU   A CB  1 
ATOM   465  C  CG  . LEU   A 1 69  ? -32.40500 11.28900 11.65200  1.000 38.90000  ? 595  LEU   A CG  1 
ATOM   466  C  CD1 . LEU   A 1 69  ? -32.99400 10.57900 10.44100  1.000 42.04000  ? 595  LEU   A CD1 1 
ATOM   467  C  CD2 . LEU   A 1 69  ? -33.29500 12.44200 12.08600  1.000 35.75000  ? 595  LEU   A CD2 1 
ATOM   468  N  N   . CYS   A 1 70  ? -29.02700 9.96400  12.88200  1.000 43.51000  ? 596  CYS   A N   1 
ATOM   469  C  CA  . CYS   A 1 70  ? -27.68500 10.35500 12.46300  1.000 41.79000  ? 596  CYS   A CA  1 
ATOM   470  C  C   . CYS   A 1 70  ? -26.97100 9.20400  11.76800  1.000 46.09000  ? 596  CYS   A C   1 
ATOM   471  O  O   . CYS   A 1 70  ? -26.32600 9.39800  10.73100  1.000 47.56000  ? 596  CYS   A O   1 
ATOM   472  C  CB  . CYS   A 1 70  ? -26.87700 10.83800 13.66800  1.000 41.37000  ? 596  CYS   A CB  1 
ATOM   473  S  SG  . CYS   A 1 70  ? -27.46400 12.38000 14.40400  1.000 49.40000  ? 596  CYS   A SG  1 
ATOM   474  N  N   . ARG   A 1 71  ? -27.08300 7.99300  12.31800  1.000 47.47000  ? 597  ARG   A N   1 
ATOM   475  C  CA  . ARG   A 1 71  ? -26.42800 6.84000  11.71000  1.000 45.59000  ? 597  ARG   A CA  1 
ATOM   476  C  C   . ARG   A 1 71  ? -27.06600 6.48300  10.37200  1.000 46.85000  ? 597  ARG   A C   1 
ATOM   477  O  O   . ARG   A 1 71  ? -26.36500 6.09800  9.42800   1.000 37.32000  ? 597  ARG   A O   1 
ATOM   478  C  CB  . ARG   A 1 71  ? -26.47500 5.65000  12.66800  1.000 46.73000  ? 597  ARG   A CB  1 
ATOM   479  C  CG  . ARG   A 1 71  ? -25.44000 4.57500  12.37800  1.000 52.18000  ? 597  ARG   A CG  1 
ATOM   480  C  CD  . ARG   A 1 71  ? -25.58900 3.39000  13.32200  1.000 60.50000  ? 597  ARG   A CD  1 
ATOM   481  N  NE  . ARG   A 1 71  ? -24.94800 3.62500  14.61300  1.000 55.69000  ? 597  ARG   A NE  1 
ATOM   482  C  CZ  . ARG   A 1 71  ? -25.59500 3.98100  15.71800  1.000 66.03000  ? 597  ARG   A CZ  1 
ATOM   483  N  NH1 . ARG   A 1 71  ? -26.91000 4.14800  15.69800  1.000 50.21000  ? 597  ARG   A NH1 1 
ATOM   484  N  NH2 . ARG   A 1 71  ? -24.92500 4.17100  16.84700  1.000 63.24000  ? 597  ARG   A NH2 1 
ATOM   485  N  N   . TRP   A 1 72  ? -28.39200 6.60600  10.26900  1.000 44.74000  ? 598  TRP   A N   1 
ATOM   486  C  CA  . TRP   A 1 72  ? -29.06800 6.29700  9.01100   1.000 48.06000  ? 598  TRP   A CA  1 
ATOM   487  C  C   . TRP   A 1 72  ? -28.69800 7.30200  7.92900   1.000 43.77000  ? 598  TRP   A C   1 
ATOM   488  O  O   . TRP   A 1 72  ? -28.35100 6.91800  6.80500   1.000 41.11000  ? 598  TRP   A O   1 
ATOM   489  C  CB  . TRP   A 1 72  ? -30.58200 6.27000  9.21100   1.000 40.46000  ? 598  TRP   A CB  1 
ATOM   490  C  CG  . TRP   A 1 72  ? -31.33900 6.07600  7.92800   1.000 43.86000  ? 598  TRP   A CG  1 
ATOM   491  C  CD1 . TRP   A 1 72  ? -31.65000 4.88800  7.33100   1.000 36.93000  ? 598  TRP   A CD1 1 
ATOM   492  C  CD2 . TRP   A 1 72  ? -31.87300 7.10200  7.07800   1.000 43.39000  ? 598  TRP   A CD2 1 
ATOM   493  N  NE1 . TRP   A 1 72  ? -32.34600 5.10900  6.16700   1.000 43.23000  ? 598  TRP   A NE1 1 
ATOM   494  C  CE2 . TRP   A 1 72  ? -32.49600 6.46000  5.98900   1.000 47.99000  ? 598  TRP   A CE2 1 
ATOM   495  C  CE3 . TRP   A 1 72  ? -31.88500 8.49900  7.13400   1.000 37.56000  ? 598  TRP   A CE3 1 
ATOM   496  C  CZ2 . TRP   A 1 72  ? -33.12500 7.16600  4.96500   1.000 34.13000  ? 598  TRP   A CZ2 1 
ATOM   497  C  CZ3 . TRP   A 1 72  ? -32.51000 9.19900  6.11500   1.000 38.36000  ? 598  TRP   A CZ3 1 
ATOM   498  C  CH2 . TRP   A 1 72  ? -33.12100 8.53200  5.04600   1.000 41.75000  ? 598  TRP   A CH2 1 
ATOM   499  N  N   . ILE   A 1 73  ? -28.78700 8.59800  8.24600   1.000 41.27000  ? 599  ILE   A N   1 
ATOM   500  C  CA  . ILE   A 1 73  ? -28.36100 9.63200  7.30500   1.000 38.93000  ? 599  ILE   A CA  1 
ATOM   501  C  C   . ILE   A 1 73  ? -26.93400 9.37300  6.85500   1.000 43.24000  ? 599  ILE   A C   1 
ATOM   502  O  O   . ILE   A 1 73  ? -26.60300 9.49800  5.66800   1.000 43.02000  ? 599  ILE   A O   1 
ATOM   503  C  CB  . ILE   A 1 73  ? -28.50000 11.02800 7.94000   1.000 37.90000  ? 599  ILE   A CB  1 
ATOM   504  C  CG1 . ILE   A 1 73  ? -29.97100 11.40800 8.08500   1.000 36.21000  ? 599  ILE   A CG1 1 
ATOM   505  C  CG2 . ILE   A 1 73  ? -27.75600 12.06900 7.11300   1.000 31.39000  ? 599  ILE   A CG2 1 
ATOM   506  C  CD1 . ILE   A 1 73  ? -30.17900 12.72900 8.77200   1.000 34.26000  ? 599  ILE   A CD1 1 
ATOM   507  N  N   . LEU   A 1 74  ? -26.06800 8.99000  7.79200   1.000 37.80000  ? 600  LEU   A N   1 
ATOM   508  C  CA  . LEU   A 1 74  ? -24.68600 8.73400  7.41900   1.000 36.76000  ? 600  LEU   A CA  1 
ATOM   509  C  C   . LEU   A 1 74  ? -24.56800 7.48500  6.55600   1.000 37.83000  ? 600  LEU   A C   1 
ATOM   510  O  O   . LEU   A 1 74  ? -23.87000 7.50100  5.53800   1.000 45.20000  ? 600  LEU   A O   1 
ATOM   511  C  CB  . LEU   A 1 74  ? -23.79900 8.64400  8.65900   1.000 42.63000  ? 600  LEU   A CB  1 
ATOM   512  C  CG  . LEU   A 1 74  ? -23.55300 10.00200 9.33300   1.000 51.15000  ? 600  LEU   A CG  1 
ATOM   513  C  CD1 . LEU   A 1 74  ? -22.48200 9.90600  10.39900  1.000 55.33000  ? 600  LEU   A CD1 1 
ATOM   514  C  CD2 . LEU   A 1 74  ? -23.20800 11.10100 8.33600   1.000 46.52000  ? 600  LEU   A CD2 1 
ATOM   515  N  N   . SER   A 1 75  ? -25.27100 6.40800  6.91800   1.000 46.81000  ? 601  SER   A N   1 
ATOM   516  C  CA  . SER   A 1 75  ? -25.23200 5.19400  6.10600   1.000 40.81000  ? 601  SER   A CA  1 
ATOM   517  C  C   . SER   A 1 75  ? -25.67700 5.46600  4.67300   1.000 39.92000  ? 601  SER   A C   1 
ATOM   518  O  O   . SER   A 1 75  ? -25.16100 4.85600  3.73000   1.000 42.88000  ? 601  SER   A O   1 
ATOM   519  C  CB  . SER   A 1 75  ? -26.10400 4.10700  6.73700   1.000 45.25000  ? 601  SER   A CB  1 
ATOM   520  O  OG  . SER   A 1 75  ? -25.53600 3.62600  7.94300   1.000 45.51000  ? 601  SER   A OG  1 
ATOM   521  N  N   . VAL   A 1 76  ? -26.62200 6.38900  4.48900   1.000 38.52000  ? 602  VAL   A N   1 
ATOM   522  C  CA  . VAL   A 1 76  ? -27.13400 6.67200  3.15200   1.000 34.11000  ? 602  VAL   A CA  1 
ATOM   523  C  C   . VAL   A 1 76  ? -26.08600 7.40400  2.31800   1.000 36.91000  ? 602  VAL   A C   1 
ATOM   524  O  O   . VAL   A 1 76  ? -25.85200 7.06500  1.15300   1.000 46.61000  ? 602  VAL   A O   1 
ATOM   525  C  CB  . VAL   A 1 76  ? -28.44900 7.46600  3.23800   1.000 38.29000  ? 602  VAL   A CB  1 
ATOM   526  C  CG1 . VAL   A 1 76  ? -28.82000 8.03000  1.87500   1.000 34.70000  ? 602  VAL   A CG1 1 
ATOM   527  C  CG2 . VAL   A 1 76  ? -29.56700 6.58000  3.76900   1.000 34.53000  ? 602  VAL   A CG2 1 
ATOM   528  N  N   . LYS   A 1 77  ? -25.43400 8.41500  2.90000   1.000 37.89000  ? 603  LYS   A N   1 
ATOM   529  C  CA  . LYS   A 1 77  ? -24.45900 9.19000  2.13500   1.000 43.23000  ? 603  LYS   A CA  1 
ATOM   530  C  C   . LYS   A 1 77  ? -23.21100 8.37300  1.79900   1.000 44.29000  ? 603  LYS   A C   1 
ATOM   531  O  O   . LYS   A 1 77  ? -22.57000 8.62700  0.77200   1.000 48.41000  ? 603  LYS   A O   1 
ATOM   532  C  CB  . LYS   A 1 77  ? -24.09500 10.47200 2.89300   1.000 49.50000  ? 603  LYS   A CB  1 
ATOM   533  C  CG  . LYS   A 1 77  ? -22.79200 11.14900 2.44600   1.000 36.57000  ? 603  LYS   A CG  1 
ATOM   534  C  CD  . LYS   A 1 77  ? -22.46600 12.44600 3.20900   1.000 41.20000  ? 603  LYS   A CD  1 
ATOM   535  C  CE  . LYS   A 1 77  ? -21.56400 12.24500 4.42800   1.000 52.43000  ? 603  LYS   A CE  1 
ATOM   536  N  NZ  . LYS   A 1 77  ? -20.19600 11.79200 4.07000   1.000 57.06000  ? 603  LYS   A NZ  1 
ATOM   537  N  N   . LYS   A 1 78  ? -22.85700 7.38200  2.62500   1.000 44.27000  ? 604  LYS   A N   1 
ATOM   538  C  CA  . LYS   A 1 78  ? -21.70300 6.54700  2.30100   1.000 41.34000  ? 604  LYS   A CA  1 
ATOM   539  C  C   . LYS   A 1 78  ? -21.99700 5.54900  1.18900   1.000 45.15000  ? 604  LYS   A C   1 
ATOM   540  O  O   . LYS   A 1 78  ? -21.06300 5.10300  0.51500   1.000 46.21000  ? 604  LYS   A O   1 
ATOM   541  C  CB  . LYS   A 1 78  ? -21.19000 5.77300  3.52300   1.000 49.12000  ? 604  LYS   A CB  1 
ATOM   542  C  CG  . LYS   A 1 78  ? -21.18400 6.50500  4.86000   1.000 74.64000  ? 604  LYS   A CG  1 
ATOM   543  C  CD  . LYS   A 1 78  ? -20.75100 7.96000  4.76100   1.000 64.45000  ? 604  LYS   A CD  1 
ATOM   544  C  CE  . LYS   A 1 78  ? -20.39300 8.52100  6.12800   1.000 62.25000  ? 604  LYS   A CE  1 
ATOM   545  N  NZ  . LYS   A 1 78  ? -19.57000 7.58200  6.93500   1.000 61.13000  ? 604  LYS   A NZ  1 
ATOM   546  N  N   . ASN   A 1 79  ? -23.26100 5.18300  0.98700   1.000 45.01000  ? 605  ASN   A N   1 
ATOM   547  C  CA  . ASN   A 1 79  ? -23.64000 4.26500  -0.07700  1.000 43.78000  ? 605  ASN   A CA  1 
ATOM   548  C  C   . ASN   A 1 79  ? -23.86200 4.97300  -1.40800  1.000 45.61000  ? 605  ASN   A C   1 
ATOM   549  O  O   . ASN   A 1 79  ? -24.37900 4.35900  -2.34700  1.000 45.27000  ? 605  ASN   A O   1 
ATOM   550  C  CB  . ASN   A 1 79  ? -24.88900 3.47600  0.32400   1.000 50.83000  ? 605  ASN   A CB  1 
ATOM   551  C  CG  . ASN   A 1 79  ? -24.55500 2.21800  1.10900   1.000 55.71000  ? 605  ASN   A CG  1 
ATOM   552  O  OD1 . ASN   A 1 79  ? -24.43900 1.13000  0.54300   1.000 59.77000  ? 605  ASN   A OD1 1 
ATOM   553  N  ND2 . ASN   A 1 79  ? -24.39300 2.36400  2.41900   1.000 52.75000  ? 605  ASN   A ND2 1 
ATOM   554  N  N   . TYR   A 1 80  ? -23.50400 6.25000  -1.49600  1.000 52.56000  ? 606  TYR   A N   1 
ATOM   555  C  CA  . TYR   A 1 80  ? -23.36500 6.95700  -2.75900  1.000 37.64000  ? 606  TYR   A CA  1 
ATOM   556  C  C   . TYR   A 1 80  ? -21.88500 7.05500  -3.10500  1.000 46.84000  ? 606  TYR   A C   1 
ATOM   557  O  O   . TYR   A 1 80  ? -21.02900 7.14000  -2.22100  1.000 49.52000  ? 606  TYR   A O   1 
ATOM   558  C  CB  . TYR   A 1 80  ? -23.98300 8.35500  -2.68900  1.000 35.39000  ? 606  TYR   A CB  1 
ATOM   559  C  CG  . TYR   A 1 80  ? -25.49200 8.36500  -2.77900  1.000 33.80000  ? 606  TYR   A CG  1 
ATOM   560  C  CD1 . TYR   A 1 80  ? -26.13300 8.27000  -4.00600  1.000 27.73000  ? 606  TYR   A CD1 1 
ATOM   561  C  CD2 . TYR   A 1 80  ? -26.27500 8.47300  -1.63800  1.000 30.57000  ? 606  TYR   A CD2 1 
ATOM   562  C  CE1 . TYR   A 1 80  ? -27.51100 8.28200  -4.09200  1.000 28.49000  ? 606  TYR   A CE1 1 
ATOM   563  C  CE2 . TYR   A 1 80  ? -27.65400 8.48500  -1.71500  1.000 35.82000  ? 606  TYR   A CE2 1 
ATOM   564  C  CZ  . TYR   A 1 80  ? -28.26600 8.38500  -2.94500  1.000 32.18000  ? 606  TYR   A CZ  1 
ATOM   565  O  OH  . TYR   A 1 80  ? -29.64000 8.39600  -3.02900  1.000 32.30000  ? 606  TYR   A OH  1 
ATOM   566  N  N   . ARG   A 1 81  ? -21.58800 7.04100  -4.40000  1.000 51.03000  ? 607  ARG   A N   1 
ATOM   567  C  CA  . ARG   A 1 81  ? -20.21500 6.94200  -4.87700  1.000 48.96000  ? 607  ARG   A CA  1 
ATOM   568  C  C   . ARG   A 1 81  ? -19.69200 8.32200  -5.25800  1.000 43.67000  ? 607  ARG   A C   1 
ATOM   569  O  O   . ARG   A 1 81  ? -20.25200 8.98500  -6.13900  1.000 54.60000  ? 607  ARG   A O   1 
ATOM   570  C  CB  . ARG   A 1 81  ? -20.12500 5.96900  -6.05200  1.000 59.68000  ? 607  ARG   A CB  1 
ATOM   571  C  CG  . ARG   A 1 81  ? -20.64300 4.58700  -5.69300  1.000 57.89000  ? 607  ARG   A CG  1 
ATOM   572  C  CD  . ARG   A 1 81  ? -20.46200 3.58700  -6.81500  1.000 59.98000  ? 607  ARG   A CD  1 
ATOM   573  N  NE  . ARG   A 1 81  ? -21.05700 2.30000  -6.47000  1.000 65.79000  ? 607  ARG   A NE  1 
ATOM   574  C  CZ  . ARG   A 1 81  ? -20.38000 1.26800  -5.97600  1.000 80.54000  ? 607  ARG   A CZ  1 
ATOM   575  N  NH1 . ARG   A 1 81  ? -19.07400 1.36500  -5.76900  1.000 78.44000  ? 607  ARG   A NH1 1 
ATOM   576  N  NH2 . ARG   A 1 81  ? -21.01100 0.13600  -5.69200  1.000 70.09000  ? 607  ARG   A NH2 1 
ATOM   577  N  N   . LYS   A 1 82  ? -18.62000 8.74600  -4.58300  1.000 60.73000  ? 608  LYS   A N   1 
ATOM   578  C  CA  . LYS   A 1 82  ? -18.02100 10.05100 -4.84600  1.000 62.22000  ? 608  LYS   A CA  1 
ATOM   579  C  C   . LYS   A 1 82  ? -17.47000 10.14200 -6.26000  1.000 62.33000  ? 608  LYS   A C   1 
ATOM   580  O  O   . LYS   A 1 82  ? -17.46800 11.22400 -6.85900  1.000 62.89000  ? 608  LYS   A O   1 
ATOM   581  C  CB  . LYS   A 1 82  ? -16.90500 10.32100 -3.83700  1.000 65.14000  ? 608  LYS   A CB  1 
ATOM   582  C  CG  . LYS   A 1 82  ? -16.74000 11.77700 -3.43900  1.000 77.25000  ? 608  LYS   A CG  1 
ATOM   583  C  CD  . LYS   A 1 82  ? -17.08000 11.97300 -1.97300  1.000 79.26000  ? 608  LYS   A CD  1 
ATOM   584  C  CE  . LYS   A 1 82  ? -16.67000 13.35100 -1.48400  1.000 77.77000  ? 608  LYS   A CE  1 
ATOM   585  N  NZ  . LYS   A 1 82  ? -16.72500 13.44400 0.00100   1.000 72.95000  ? 608  LYS   A NZ  1 
ATOM   586  N  N   . ASN   A 1 83  ? -16.99100 9.02400  -6.80400  1.000 68.26000  ? 609  ASN   A N   1 
ATOM   587  C  CA  . ASN   A 1 83  ? -16.35600 8.99500  -8.11400  1.000 67.63000  ? 609  ASN   A CA  1 
ATOM   588  C  C   . ASN   A 1 83  ? -17.34300 9.13800  -9.26600  1.000 65.21000  ? 609  ASN   A C   1 
ATOM   589  O  O   . ASN   A 1 83  ? -16.92300 9.08800  -10.42800 1.000 67.99000  ? 609  ASN   A O   1 
ATOM   590  C  CB  . ASN   A 1 83  ? -15.55700 7.69900  -8.26900  1.000 69.43000  ? 609  ASN   A CB  1 
ATOM   591  C  CG  . ASN   A 1 83  ? -16.30800 6.48800  -7.75000  1.000 70.84000  ? 609  ASN   A CG  1 
ATOM   592  O  OD1 . ASN   A 1 83  ? -16.10300 6.05300  -6.61600  1.000 84.08000  ? 609  ASN   A OD1 1 
ATOM   593  N  ND2 . ASN   A 1 83  ? -17.18600 5.93700  -8.58000  1.000 50.15000  ? 609  ASN   A ND2 1 
ATOM   594  N  N   . VAL   A 1 84  ? -18.63100 9.30100  -8.98100  1.000 66.16000  ? 610  VAL   A N   1 
ATOM   595  C  CA  . VAL   A 1 84  ? -19.64200 9.55700  -10.00000 1.000 59.25000  ? 610  VAL   A CA  1 
ATOM   596  C  C   . VAL   A 1 84  ? -19.94700 11.04800 -9.99200  1.000 56.63000  ? 610  VAL   A C   1 
ATOM   597  O  O   . VAL   A 1 84  ? -20.16000 11.64000 -8.92600  1.000 42.16000  ? 610  VAL   A O   1 
ATOM   598  C  CB  . VAL   A 1 84  ? -20.90800 8.72100  -9.75000  1.000 50.45000  ? 610  VAL   A CB  1 
ATOM   599  C  CG1 . VAL   A 1 84  ? -21.95500 9.01400  -10.80900 1.000 49.57000  ? 610  VAL   A CG1 1 
ATOM   600  C  CG2 . VAL   A 1 84  ? -20.56400 7.23800  -9.73500  1.000 48.80000  ? 610  VAL   A CG2 1 
ATOM   601  N  N   . ALA   A 1 85  ? -19.96700 11.65600 -11.18100 1.000 53.18000  ? 611  ALA   A N   1 
ATOM   602  C  CA  . ALA   A 1 85  ? -19.99200 13.11400 -11.27300 1.000 43.81000  ? 611  ALA   A CA  1 
ATOM   603  C  C   . ALA   A 1 85  ? -21.29300 13.69300 -10.72900 1.000 46.47000  ? 611  ALA   A C   1 
ATOM   604  O  O   . ALA   A 1 85  ? -21.27500 14.59900 -9.88800  1.000 46.35000  ? 611  ALA   A O   1 
ATOM   605  C  CB  . ALA   A 1 85  ? -19.77200 13.55000 -12.72200 1.000 50.89000  ? 611  ALA   A CB  1 
ATOM   606  N  N   . TYR   A 1 86  ? -22.43400 13.19100 -11.19700 1.000 40.02000  ? 612  TYR   A N   1 
ATOM   607  C  CA  . TYR   A 1 86  ? -23.72800 13.75400 -10.83000 1.000 46.00000  ? 612  TYR   A CA  1 
ATOM   608  C  C   . TYR   A 1 86  ? -24.52800 12.86900 -9.88600  1.000 41.78000  ? 612  TYR   A C   1 
ATOM   609  O  O   . TYR   A 1 86  ? -24.95400 13.32900 -8.82300  1.000 38.67000  ? 612  TYR   A O   1 
ATOM   610  C  CB  . TYR   A 1 86  ? -24.55700 14.04100 -12.09000 1.000 37.98000  ? 612  TYR   A CB  1 
ATOM   611  C  CG  . TYR   A 1 86  ? -25.91400 14.62800 -11.78300 1.000 32.18000  ? 612  TYR   A CG  1 
ATOM   612  C  CD1 . TYR   A 1 86  ? -26.03200 15.88800 -11.21100 1.000 31.79000  ? 612  TYR   A CD1 1 
ATOM   613  C  CD2 . TYR   A 1 86  ? -27.07800 13.92100 -12.05600 1.000 33.89000  ? 612  TYR   A CD2 1 
ATOM   614  C  CE1 . TYR   A 1 86  ? -27.26900 16.42900 -10.92300 1.000 35.53000  ? 612  TYR   A CE1 1 
ATOM   615  C  CE2 . TYR   A 1 86  ? -28.32100 14.45500 -11.77200 1.000 39.39000  ? 612  TYR   A CE2 1 
ATOM   616  C  CZ  . TYR   A 1 86  ? -28.41000 15.71000 -11.20600 1.000 42.88000  ? 612  TYR   A CZ  1 
ATOM   617  O  OH  . TYR   A 1 86  ? -29.64300 16.24800 -10.92000 1.000 46.04000  ? 612  TYR   A OH  1 
ATOM   618  N  N   . HIS   A 1 87  ? -24.75500 11.60600 -10.25000 1.000 45.57000  ? 613  HIS   A N   1 
ATOM   619  C  CA  . HIS   A 1 87  ? -25.58900 10.70600 -9.45200  1.000 39.06000  ? 613  HIS   A CA  1 
ATOM   620  C  C   . HIS   A 1 87  ? -24.81800 10.28600 -8.20400  1.000 41.67000  ? 613  HIS   A C   1 
ATOM   621  O  O   . HIS   A 1 87  ? -24.30300 9.17100  -8.09000  1.000 44.10000  ? 613  HIS   A O   1 
ATOM   622  C  CB  . HIS   A 1 87  ? -26.01900 9.50100  -10.28000 1.000 36.98000  ? 613  HIS   A CB  1 
ATOM   623  C  CG  . HIS   A 1 87  ? -26.99900 9.83100  -11.36200 1.000 36.52000  ? 613  HIS   A CG  1 
ATOM   624  N  ND1 . HIS   A 1 87  ? -26.63900 9.92300  -12.69000 1.000 36.80000  ? 613  HIS   A ND1 1 
ATOM   625  C  CD2 . HIS   A 1 87  ? -28.32700 10.09300 -11.31400 1.000 37.89000  ? 613  HIS   A CD2 1 
ATOM   626  C  CE1 . HIS   A 1 87  ? -27.70300 10.22700 -13.41200 1.000 43.57000  ? 613  HIS   A CE1 1 
ATOM   627  N  NE2 . HIS   A 1 87  ? -28.74000 10.33600 -12.60100 1.000 39.60000  ? 613  HIS   A NE2 1 
ATOM   628  N  N   . ASN   A 1 88  ? -24.74700 11.20400 -7.24300  1.000 39.18000  ? 614  ASN   A N   1 
ATOM   629  C  CA  . ASN   A 1 88  ? -24.03300 10.97500 -5.99400  1.000 30.50000  ? 614  ASN   A CA  1 
ATOM   630  C  C   . ASN   A 1 88  ? -24.89100 11.50000 -4.84700  1.000 30.65000  ? 614  ASN   A C   1 
ATOM   631  O  O   . ASN   A 1 88  ? -26.07700 11.80100 -5.01800  1.000 30.81000  ? 614  ASN   A O   1 
ATOM   632  C  CB  . ASN   A 1 88  ? -22.64500 11.63000 -6.03300  1.000 40.32000  ? 614  ASN   A CB  1 
ATOM   633  C  CG  . ASN   A 1 88  ? -22.69500 13.07400 -6.49000  1.000 41.89000  ? 614  ASN   A CG  1 
ATOM   634  O  OD1 . ASN   A 1 88  ? -23.32900 13.91800 -5.85500  1.000 38.01000  ? 614  ASN   A OD1 1 
ATOM   635  N  ND2 . ASN   A 1 88  ? -22.02100 13.36800 -7.59600  1.000 40.57000  ? 614  ASN   A ND2 1 
ATOM   636  N  N   . TRP   A 1 89  ? -24.27800 11.61900 -3.66600  1.000 28.83000  ? 615  TRP   A N   1 
ATOM   637  C  CA  . TRP   A 1 89  ? -25.02700 12.01300 -2.47600  1.000 25.68000  ? 615  TRP   A CA  1 
ATOM   638  C  C   . TRP   A 1 89  ? -25.56800 13.43200 -2.59900  1.000 34.95000  ? 615  TRP   A C   1 
ATOM   639  O  O   . TRP   A 1 89  ? -26.68200 13.72100 -2.14300  1.000 35.20000  ? 615  TRP   A O   1 
ATOM   640  C  CB  . TRP   A 1 89  ? -24.14500 11.88700 -1.23400  1.000 28.19000  ? 615  TRP   A CB  1 
ATOM   641  C  CG  . TRP   A 1 89  ? -24.59800 12.75700 -0.10200  1.000 36.88000  ? 615  TRP   A CG  1 
ATOM   642  C  CD1 . TRP   A 1 89  ? -23.97900 13.87900 0.37200   1.000 26.79000  ? 615  TRP   A CD1 1 
ATOM   643  C  CD2 . TRP   A 1 89  ? -25.77600 12.58200 0.69400   1.000 31.38000  ? 615  TRP   A CD2 1 
ATOM   644  N  NE1 . TRP   A 1 89  ? -24.69700 14.41000 1.41600   1.000 36.01000  ? 615  TRP   A NE1 1 
ATOM   645  C  CE2 . TRP   A 1 89  ? -25.80500 13.63200 1.63400   1.000 37.51000  ? 615  TRP   A CE2 1 
ATOM   646  C  CE3 . TRP   A 1 89  ? -26.80700 11.63800 0.70600   1.000 39.51000  ? 615  TRP   A CE3 1 
ATOM   647  C  CZ2 . TRP   A 1 89  ? -26.82500 13.76400 2.57400   1.000 40.72000  ? 615  TRP   A CZ2 1 
ATOM   648  C  CZ3 . TRP   A 1 89  ? -27.81900 11.77100 1.64000   1.000 32.75000  ? 615  TRP   A CZ3 1 
ATOM   649  C  CH2 . TRP   A 1 89  ? -27.82000 12.82600 2.56000   1.000 33.33000  ? 615  TRP   A CH2 1 
ATOM   650  N  N   . ARG   A 1 90  ? -24.79300 14.33500 -3.20600  1.000 37.45000  ? 616  ARG   A N   1 
ATOM   651  C  CA  . ARG   A 1 90  ? -25.23700 15.72000 -3.33100  1.000 36.60000  ? 616  ARG   A CA  1 
ATOM   652  C  C   . ARG   A 1 90  ? -26.48700 15.83400 -4.19300  1.000 34.02000  ? 616  ARG   A C   1 
ATOM   653  O  O   . ARG   A 1 90  ? -27.32600 16.71100 -3.95600  1.000 34.28000  ? 616  ARG   A O   1 
ATOM   654  C  CB  . ARG   A 1 90  ? -24.11200 16.58400 -3.90200  1.000 37.18000  ? 616  ARG   A CB  1 
ATOM   655  C  CG  . ARG   A 1 90  ? -22.89700 16.69700 -2.99300  1.000 30.89000  ? 616  ARG   A CG  1 
ATOM   656  C  CD  . ARG   A 1 90  ? -23.30700 16.98100 -1.55500  1.000 34.92000  ? 616  ARG   A CD  1 
ATOM   657  N  NE  . ARG   A 1 90  ? -22.15300 17.18100 -0.68400  1.000 44.17000  ? 616  ARG   A NE  1 
ATOM   658  C  CZ  . ARG   A 1 90  ? -21.71700 18.37000 -0.28100  1.000 45.65000  ? 616  ARG   A CZ  1 
ATOM   659  N  NH1 . ARG   A 1 90  ? -22.33900 19.47400 -0.67000  1.000 44.74000  ? 616  ARG   A NH1 1 
ATOM   660  N  NH2 . ARG   A 1 90  ? -20.65700 18.45600 0.51100   1.000 33.57000  ? 616  ARG   A NH2 1 
ATOM   661  N  N   . HIS   A 1 91  ? -26.63400 14.96100 -5.19200  1.000 33.42000  ? 617  HIS   A N   1 
ATOM   662  C  CA  . HIS   A 1 91  ? -27.86300 14.94800 -5.97700  1.000 31.68000  ? 617  HIS   A CA  1 
ATOM   663  C  C   . HIS   A 1 91  ? -29.03900 14.45500 -5.14300  1.000 30.82000  ? 617  HIS   A C   1 
ATOM   664  O  O   . HIS   A 1 91  ? -30.13600 15.02300 -5.20900  1.000 33.68000  ? 617  HIS   A O   1 
ATOM   665  C  CB  . HIS   A 1 91  ? -27.68900 14.07900 -7.22100  1.000 29.90000  ? 617  HIS   A CB  1 
ATOM   666  C  CG  . HIS   A 1 91  ? -28.98200 13.67000 -7.85500  1.000 31.92000  ? 617  HIS   A CG  1 
ATOM   667  N  ND1 . HIS   A 1 91  ? -29.92900 14.58300 -8.26500  1.000 36.02000  ? 617  HIS   A ND1 1 
ATOM   668  C  CD2 . HIS   A 1 91  ? -29.48800 12.44800 -8.14300  1.000 25.80000  ? 617  HIS   A CD2 1 
ATOM   669  C  CE1 . HIS   A 1 91  ? -30.96200 13.94100 -8.78100  1.000 31.48000  ? 617  HIS   A CE1 1 
ATOM   670  N  NE2 . HIS   A 1 91  ? -30.71900 12.64400 -8.71900  1.000 37.69000  ? 617  HIS   A NE2 1 
ATOM   671  N  N   . ALA   A 1 92  ? -28.83000 13.39900 -4.35400  1.000 32.87000  ? 618  ALA   A N   1 
ATOM   672  C  CA  . ALA   A 1 92  ? -29.89500 12.89400 -3.49500  1.000 32.34000  ? 618  ALA   A CA  1 
ATOM   673  C  C   . ALA   A 1 92  ? -30.24800 13.89700 -2.40600  1.000 30.88000  ? 618  ALA   A C   1 
ATOM   674  O  O   . ALA   A 1 92  ? -31.42300 14.05500 -2.05600  1.000 32.59000  ? 618  ALA   A O   1 
ATOM   675  C  CB  . ALA   A 1 92  ? -29.48200 11.56000 -2.87800  1.000 31.43000  ? 618  ALA   A CB  1 
ATOM   676  N  N   . PHE   A 1 93  ? -29.24100 14.57900 -1.85600  1.000 34.73000  ? 619  PHE   A N   1 
ATOM   677  C  CA  . PHE   A 1 93  ? -29.50200 15.59400 -0.84200  1.000 33.24000  ? 619  PHE   A CA  1 
ATOM   678  C  C   . PHE   A 1 93  ? -30.29800 16.75700 -1.42100  1.000 29.73000  ? 619  PHE   A C   1 
ATOM   679  O  O   . PHE   A 1 93  ? -31.21200 17.27700 -0.77000  1.000 35.37000  ? 619  PHE   A O   1 
ATOM   680  C  CB  . PHE   A 1 93  ? -28.18300 16.08400 -0.24400  1.000 36.21000  ? 619  PHE   A CB  1 
ATOM   681  C  CG  . PHE   A 1 93  ? -28.31500 17.33600 0.57400   1.000 40.00000  ? 619  PHE   A CG  1 
ATOM   682  C  CD1 . PHE   A 1 93  ? -28.94200 17.30900 1.80900   1.000 38.62000  ? 619  PHE   A CD1 1 
ATOM   683  C  CD2 . PHE   A 1 93  ? -27.80600 18.53900 0.11200   1.000 37.36000  ? 619  PHE   A CD2 1 
ATOM   684  C  CE1 . PHE   A 1 93  ? -29.06400 18.45900 2.56500   1.000 34.12000  ? 619  PHE   A CE1 1 
ATOM   685  C  CE2 . PHE   A 1 93  ? -27.92600 19.69300 0.86400   1.000 42.52000  ? 619  PHE   A CE2 1 
ATOM   686  C  CZ  . PHE   A 1 93  ? -28.55500 19.65200 2.09200   1.000 40.09000  ? 619  PHE   A CZ  1 
ATOM   687  N  N   . ASN   A 1 94  ? -29.97200 17.17200 -2.64700  1.000 35.29000  ? 620  ASN   A N   1 
ATOM   688  C  CA  . ASN   A 1 94  ? -30.70800 18.26300 -3.27800  1.000 32.83000  ? 620  ASN   A CA  1 
ATOM   689  C  C   . ASN   A 1 94  ? -32.12300 17.83600 -3.64900  1.000 32.86000  ? 620  ASN   A C   1 
ATOM   690  O  O   . ASN   A 1 94  ? -33.05800 18.64200 -3.58000  1.000 33.86000  ? 620  ASN   A O   1 
ATOM   691  C  CB  . ASN   A 1 94  ? -29.95600 18.75900 -4.51100  1.000 38.24000  ? 620  ASN   A CB  1 
ATOM   692  C  CG  . ASN   A 1 94  ? -28.90500 19.79700 -4.17300  1.000 40.29000  ? 620  ASN   A CG  1 
ATOM   693  O  OD1 . ASN   A 1 94  ? -29.22700 20.94400 -3.86300  1.000 41.33000  ? 620  ASN   A OD1 1 
ATOM   694  N  ND2 . ASN   A 1 94  ? -27.64000 19.39900 -4.23400  1.000 31.53000  ? 620  ASN   A ND2 1 
ATOM   695  N  N   . THR   A 1 95  ? -32.29800 16.57500 -4.05300  1.000 34.01000  ? 621  THR   A N   1 
ATOM   696  C  CA  . THR   A 1 95  ? -33.63400 16.08000 -4.37100  1.000 35.14000  ? 621  THR   A CA  1 
ATOM   697  C  C   . THR   A 1 95  ? -34.53800 16.11900 -3.14600  1.000 30.33000  ? 621  THR   A C   1 
ATOM   698  O  O   . THR   A 1 95  ? -35.70500 16.51800 -3.23700  1.000 28.62000  ? 621  THR   A O   1 
ATOM   699  C  CB  . THR   A 1 95  ? -33.55200 14.65800 -4.92800  1.000 34.23000  ? 621  THR   A CB  1 
ATOM   700  O  OG1 . THR   A 1 95  ? -32.75000 14.65100 -6.11600  1.000 27.10000  ? 621  THR   A OG1 1 
ATOM   701  C  CG2 . THR   A 1 95  ? -34.94000 14.13200 -5.25900  1.000 27.96000  ? 621  THR   A CG2 1 
ATOM   702  N  N   . ALA   A 1 96  ? -34.01400 15.71500 -1.98800  1.000 28.72000  ? 622  ALA   A N   1 
ATOM   703  C  CA  . ALA   A 1 96  ? -34.80600 15.76700 -0.76600  1.000 36.09000  ? 622  ALA   A CA  1 
ATOM   704  C  C   . ALA   A 1 96  ? -35.04400 17.20000 -0.31100  1.000 36.43000  ? 622  ALA   A C   1 
ATOM   705  O  O   . ALA   A 1 96  ? -36.09200 17.49700 0.27400   1.000 36.76000  ? 622  ALA   A O   1 
ATOM   706  C  CB  . ALA   A 1 96  ? -34.11900 14.96200 0.33500   1.000 30.98000  ? 622  ALA   A CB  1 
ATOM   707  N  N   . GLN   A 1 97  ? -34.08900 18.09800 -0.56800  1.000 35.13000  ? 623  GLN   A N   1 
ATOM   708  C  CA  . GLN   A 1 97  ? -34.26100 19.49100 -0.17100  1.000 28.72000  ? 623  GLN   A CA  1 
ATOM   709  C  C   . GLN   A 1 97  ? -35.41400 20.13900 -0.92700  1.000 30.93000  ? 623  GLN   A C   1 
ATOM   710  O  O   . GLN   A 1 97  ? -36.22500 20.86100 -0.33700  1.000 34.73000  ? 623  GLN   A O   1 
ATOM   711  C  CB  . GLN   A 1 97  ? -32.96200 20.26500 -0.40100  1.000 37.27000  ? 623  GLN   A CB  1 
ATOM   712  C  CG  . GLN   A 1 97  ? -33.05000 21.74400 -0.05700  1.000 38.04000  ? 623  GLN   A CG  1 
ATOM   713  C  CD  . GLN   A 1 97  ? -33.52400 22.59200 -1.22400  1.000 38.90000  ? 623  GLN   A CD  1 
ATOM   714  O  OE1 . GLN   A 1 97  ? -33.03700 22.45500 -2.34700  1.000 39.25000  ? 623  GLN   A OE1 1 
ATOM   715  N  NE2 . GLN   A 1 97  ? -34.48500 23.47000 -0.96200  1.000 32.06000  ? 623  GLN   A NE2 1 
ATOM   716  N  N   . CYS   A 1 98  ? -35.49700 19.90100 -2.23800  1.000 34.43000  ? 624  CYS   A N   1 
ATOM   717  C  CA  . CYS   A 1 98  ? -36.60500 20.45000 -3.01000  1.000 38.16000  ? 624  CYS   A CA  1 
ATOM   718  C  C   . CYS   A 1 98  ? -37.93000 19.82100 -2.60100  1.000 42.12000  ? 624  CYS   A C   1 
ATOM   719  O  O   . CYS   A 1 98  ? -38.96800 20.49100 -2.63500  1.000 44.68000  ? 624  CYS   A O   1 
ATOM   720  C  CB  . CYS   A 1 98  ? -36.35000 20.26000 -4.50400  1.000 34.88000  ? 624  CYS   A CB  1 
ATOM   721  S  SG  . CYS   A 1 98  ? -37.69100 20.82600 -5.57400  1.000 45.90000  ? 624  CYS   A SG  1 
ATOM   722  N  N   . MET   A 1 99  ? -37.91300 18.54600 -2.20500  1.000 41.59000  ? 625  MET   A N   1 
ATOM   723  C  CA  . MET   A 1 99  ? -39.10400 17.94100 -1.61800  1.000 42.73000  ? 625  MET   A CA  1 
ATOM   724  C  C   . MET   A 1 99  ? -39.50800 18.67000 -0.34400  1.000 36.83000  ? 625  MET   A C   1 
ATOM   725  O  O   . MET   A 1 99  ? -40.69500 18.93100 -0.11600  1.000 45.00000  ? 625  MET   A O   1 
ATOM   726  C  CB  . MET   A 1 99  ? -38.85900 16.45700 -1.33500  1.000 40.63000  ? 625  MET   A CB  1 
ATOM   727  C  CG  . MET   A 1 99  ? -40.05600 15.71900 -0.75300  1.000 30.38000  ? 625  MET   A CG  1 
ATOM   728  S  SD  . MET   A 1 99  ? -41.37800 15.48600 -1.95800  1.000 42.59000  ? 625  MET   A SD  1 
ATOM   729  C  CE  . MET   A 1 99  ? -40.60600 14.32900 -3.08400  1.000 26.89000  ? 625  MET   A CE  1 
ATOM   730  N  N   . PHE   A 1 100 ? -38.52800 19.01600 0.49500   1.000 43.84000  ? 626  PHE   A N   1 
ATOM   731  C  CA  . PHE   A 1 100 ? -38.81100 19.81400 1.68300   1.000 44.83000  ? 626  PHE   A CA  1 
ATOM   732  C  C   . PHE   A 1 100 ? -39.33200 21.19600 1.30600   1.000 48.09000  ? 626  PHE   A C   1 
ATOM   733  O  O   . PHE   A 1 100 ? -40.28300 21.69800 1.91600   1.000 48.84000  ? 626  PHE   A O   1 
ATOM   734  C  CB  . PHE   A 1 100 ? -37.55300 19.93000 2.54500   1.000 41.70000  ? 626  PHE   A CB  1 
ATOM   735  C  CG  . PHE   A 1 100 ? -37.74800 20.71800 3.80900   1.000 51.80000  ? 626  PHE   A CG  1 
ATOM   736  C  CD1 . PHE   A 1 100 ? -38.21000 20.10100 4.95900   1.000 43.91000  ? 626  PHE   A CD1 1 
ATOM   737  C  CD2 . PHE   A 1 100 ? -37.46100 22.07400 3.85000   1.000 48.96000  ? 626  PHE   A CD2 1 
ATOM   738  C  CE1 . PHE   A 1 100 ? -38.39000 20.82000 6.12500   1.000 49.95000  ? 626  PHE   A CE1 1 
ATOM   739  C  CE2 . PHE   A 1 100 ? -37.63900 22.79900 5.01300   1.000 46.46000  ? 626  PHE   A CE2 1 
ATOM   740  C  CZ  . PHE   A 1 100 ? -38.10300 22.17100 6.15200   1.000 54.03000  ? 626  PHE   A CZ  1 
ATOM   741  N  N   . ALA   A 1 101 ? -38.71800 21.82500 0.30000   1.000 45.05000  ? 627  ALA   A N   1 
ATOM   742  C  CA  . ALA   A 1 101 ? -39.16200 23.14900 -0.12500  1.000 52.77000  ? 627  ALA   A CA  1 
ATOM   743  C  C   . ALA   A 1 101 ? -40.54700 23.09100 -0.75700  1.000 48.61000  ? 627  ALA   A C   1 
ATOM   744  O  O   . ALA   A 1 101 ? -41.36500 23.99600 -0.55400  1.000 49.31000  ? 627  ALA   A O   1 
ATOM   745  C  CB  . ALA   A 1 101 ? -38.15100 23.75400 -1.09800  1.000 39.58000  ? 627  ALA   A CB  1 
ATOM   746  N  N   . ALA   A 1 102 ? -40.83000 22.03600 -1.52500  1.000 48.66000  ? 628  ALA   A N   1 
ATOM   747  C  CA  . ALA   A 1 102 ? -42.15100 21.90000 -2.12900  1.000 45.96000  ? 628  ALA   A CA  1 
ATOM   748  C  C   . ALA   A 1 102 ? -43.22400 21.63500 -1.08200  1.000 46.95000  ? 628  ALA   A C   1 
ATOM   749  O  O   . ALA   A 1 102 ? -44.38400 22.01200 -1.27800  1.000 53.45000  ? 628  ALA   A O   1 
ATOM   750  C  CB  . ALA   A 1 102 ? -42.14300 20.78500 -3.17500  1.000 42.28000  ? 628  ALA   A CB  1 
ATOM   751  N  N   . LEU   A 1 103 ? -42.86300 20.99300 0.03000   1.000 47.32000  ? 629  LEU   A N   1 
ATOM   752  C  CA  . LEU   A 1 103 ? -43.83200 20.76500 1.09600   1.000 51.15000  ? 629  LEU   A CA  1 
ATOM   753  C  C   . LEU   A 1 103 ? -44.06900 22.02800 1.91300   1.000 50.72000  ? 629  LEU   A C   1 
ATOM   754  O  O   . LEU   A 1 103 ? -45.21200 22.33400 2.27000   1.000 55.18000  ? 629  LEU   A O   1 
ATOM   755  C  CB  . LEU   A 1 103 ? -43.36300 19.62500 2.00100   1.000 50.03000  ? 629  LEU   A CB  1 
ATOM   756  C  CG  . LEU   A 1 103 ? -43.37700 18.21600 1.40500   1.000 45.69000  ? 629  LEU   A CG  1 
ATOM   757  C  CD1 . LEU   A 1 103 ? -42.71200 17.22900 2.35100   1.000 48.53000  ? 629  LEU   A CD1 1 
ATOM   758  C  CD2 . LEU   A 1 103 ? -44.79300 17.77500 1.07200   1.000 55.61000  ? 629  LEU   A CD2 1 
ATOM   759  N  N   . LYS   A 1 104 ? -43.00600 22.77600 2.21300   1.000 54.75000  ? 630  LYS   A N   1 
ATOM   760  C  CA  . LYS   A 1 104 ? -43.14200 23.98900 3.01900   1.000 49.17000  ? 630  LYS   A CA  1 
ATOM   761  C  C   . LYS   A 1 104 ? -43.51900 25.18700 2.15100   1.000 51.41000  ? 630  LYS   A C   1 
ATOM   762  O  O   . LYS   A 1 104 ? -44.65400 25.67200 2.19900   1.000 58.32000  ? 630  LYS   A O   1 
ATOM   763  C  CB  . LYS   A 1 104 ? -41.84300 24.25600 3.78600   1.000 43.51000  ? 630  LYS   A CB  1 
ATOM   764  C  CG  . LYS   A 1 104 ? -41.52200 23.21600 4.84700   1.000 52.99000  ? 630  LYS   A CG  1 
ATOM   765  C  CD  . LYS   A 1 104 ? -42.57500 23.19500 5.94200   1.000 42.74000  ? 630  LYS   A CD  1 
ATOM   766  C  CE  . LYS   A 1 104 ? -42.17000 22.27100 7.07900   1.000 60.33000  ? 630  LYS   A CE  1 
ATOM   767  N  NZ  . LYS   A 1 104 ? -43.22100 22.18900 8.13100   1.000 67.06000  ? 630  LYS   A NZ  1 
ATOM   768  N  N   . ALA   A 1 105 ? -42.57000 25.67600 1.34700   1.000 55.44000  ? 631  ALA   A N   1 
ATOM   769  C  CA  . ALA   A 1 105 ? -42.82200 26.86000 0.53200   1.000 59.64000  ? 631  ALA   A CA  1 
ATOM   770  C  C   . ALA   A 1 105 ? -43.91200 26.61500 -0.50300  1.000 58.54000  ? 631  ALA   A C   1 
ATOM   771  O  O   . ALA   A 1 105 ? -44.66200 27.53700 -0.84300  1.000 63.58000  ? 631  ALA   A O   1 
ATOM   772  C  CB  . ALA   A 1 105 ? -41.53100 27.31200 -0.15100  1.000 49.52000  ? 631  ALA   A CB  1 
ATOM   773  N  N   . GLY   A 1 106 ? -44.01600 25.39100 -1.01300  1.000 58.29000  ? 632  GLY   A N   1 
ATOM   774  C  CA  . GLY   A 1 106 ? -45.06200 25.05000 -1.95100  1.000 53.26000  ? 632  GLY   A CA  1 
ATOM   775  C  C   . GLY   A 1 106 ? -46.38100 24.65500 -1.33200  1.000 56.28000  ? 632  GLY   A C   1 
ATOM   776  O  O   . GLY   A 1 106 ? -47.34500 24.40500 -2.06100  1.000 61.36000  ? 632  GLY   A O   1 
ATOM   777  N  N   . LYS   A 1 107 ? -46.44700 24.58400 -0.00200  1.000 53.15000  ? 633  LYS   A N   1 
ATOM   778  C  CA  . LYS   A 1 107 ? -47.66600 24.26800 0.74400   1.000 63.08000  ? 633  LYS   A CA  1 
ATOM   779  C  C   . LYS   A 1 107 ? -48.26200 22.91700 0.35800   1.000 64.11000  ? 633  LYS   A C   1 
ATOM   780  O  O   . LYS   A 1 107 ? -49.45100 22.67300 0.59000   1.000 75.41000  ? 633  LYS   A O   1 
ATOM   781  C  CB  . LYS   A 1 107 ? -48.71700 25.37300 0.58400   1.000 62.07000  ? 633  LYS   A CB  1 
ATOM   782  C  CG  . LYS   A 1 107 ? -48.57300 26.51200 1.58100   1.000 73.42000  ? 633  LYS   A CG  1 
ATOM   783  C  CD  . LYS   A 1 107 ? -48.66900 27.86500 0.89600   1.000 68.79000  ? 633  LYS   A CD  1 
ATOM   784  C  CE  . LYS   A 1 107 ? -47.81900 28.90400 1.60900   1.000 78.07000  ? 633  LYS   A CE  1 
ATOM   785  N  NZ  . LYS   A 1 107 ? -46.39400 28.84400 1.17600   1.000 78.01000  ? 633  LYS   A NZ  1 
ATOM   786  N  N   . ILE   A 1 108 ? -47.45800 22.02700 -0.22800  1.000 67.98000  ? 634  ILE   A N   1 
ATOM   787  C  CA  . ILE   A 1 108 ? -47.93200 20.68700 -0.55100  1.000 61.37000  ? 634  ILE   A CA  1 
ATOM   788  C  C   . ILE   A 1 108 ? -48.10400 19.84600 0.71000   1.000 63.52000  ? 634  ILE   A C   1 
ATOM   789  O  O   . ILE   A 1 108 ? -48.84100 18.85200 0.69700   1.000 60.11000  ? 634  ILE   A O   1 
ATOM   790  C  CB  . ILE   A 1 108 ? -46.96500 20.03200 -1.56000  1.000 53.02000  ? 634  ILE   A CB  1 
ATOM   791  C  CG1 . ILE   A 1 108 ? -46.93500 20.83700 -2.86100  1.000 57.62000  ? 634  ILE   A CG1 1 
ATOM   792  C  CG2 . ILE   A 1 108 ? -47.35100 18.58700 -1.86300  1.000 61.01000  ? 634  ILE   A CG2 1 
ATOM   793  C  CD1 . ILE   A 1 108 ? -46.14700 20.18000 -3.97500  1.000 58.65000  ? 634  ILE   A CD1 1 
ATOM   794  N  N   . GLN   A 1 109 ? -47.47400 20.25500 1.81600   1.000 57.73000  ? 635  GLN   A N   1 
ATOM   795  C  CA  . GLN   A 1 109 ? -47.49300 19.46000 3.04300   1.000 60.24000  ? 635  GLN   A CA  1 
ATOM   796  C  C   . GLN   A 1 109 ? -48.91400 19.17700 3.51700   1.000 73.08000  ? 635  GLN   A C   1 
ATOM   797  O  O   . GLN   A 1 109 ? -49.19600 18.09000 4.03600   1.000 67.72000  ? 635  GLN   A O   1 
ATOM   798  C  CB  . GLN   A 1 109 ? -46.70100 20.18200 4.13400   1.000 52.93000  ? 635  GLN   A CB  1 
ATOM   799  C  CG  . GLN   A 1 109 ? -46.69400 19.47900 5.47900   1.000 52.35000  ? 635  GLN   A CG  1 
ATOM   800  C  CD  . GLN   A 1 109 ? -45.92100 20.25000 6.53100   1.000 71.64000  ? 635  GLN   A CD  1 
ATOM   801  O  OE1 . GLN   A 1 109 ? -45.66100 21.44300 6.37700   1.000 68.75000  ? 635  GLN   A OE1 1 
ATOM   802  N  NE2 . GLN   A 1 109 ? -45.54800 19.56800 7.60800   1.000 74.37000  ? 635  GLN   A NE2 1 
ATOM   803  N  N   . ASN   A 1 110 ? -49.82500 20.13700 3.34300   1.000 79.57000  ? 636  ASN   A N   1 
ATOM   804  C  CA  . ASN   A 1 110 ? -51.18400 19.96800 3.84200   1.000 66.27000  ? 636  ASN   A CA  1 
ATOM   805  C  C   . ASN   A 1 110 ? -52.01400 19.02900 2.97500   1.000 68.65000  ? 636  ASN   A C   1 
ATOM   806  O  O   . ASN   A 1 110 ? -53.05800 18.55200 3.42900   1.000 74.97000  ? 636  ASN   A O   1 
ATOM   807  C  CB  . ASN   A 1 110 ? -51.87300 21.32800 3.95600   1.000 64.01000  ? 636  ASN   A CB  1 
ATOM   808  C  CG  . ASN   A 1 110 ? -51.24800 22.20700 5.02200   1.000 87.56000  ? 636  ASN   A CG  1 
ATOM   809  O  OD1 . ASN   A 1 110 ? -50.75400 21.71600 6.03800   1.000 74.72000  ? 636  ASN   A OD1 1 
ATOM   810  N  ND2 . ASN   A 1 110 ? -51.26300 23.51400 4.79400   1.000 84.32000  ? 636  ASN   A ND2 1 
ATOM   811  N  N   . LYS   A 1 111 ? -51.57600 18.75000 1.74800   1.000 61.86000  ? 637  LYS   A N   1 
ATOM   812  C  CA  . LYS   A 1 111 ? -52.30300 17.83900 0.87200   1.000 60.71000  ? 637  LYS   A CA  1 
ATOM   813  C  C   . LYS   A 1 111 ? -51.97300 16.37300 1.12300   1.000 66.80000  ? 637  LYS   A C   1 
ATOM   814  O  O   . LYS   A 1 111 ? -52.61900 15.50100 0.53200   1.000 73.35000  ? 637  LYS   A O   1 
ATOM   815  C  CB  . LYS   A 1 111 ? -52.01200 18.16700 -0.59600  1.000 64.27000  ? 637  LYS   A CB  1 
ATOM   816  C  CG  . LYS   A 1 111 ? -52.37700 19.57800 -1.01800  1.000 71.89000  ? 637  LYS   A CG  1 
ATOM   817  C  CD  . LYS   A 1 111 ? -51.66500 19.95300 -2.31000  1.000 66.75000  ? 637  LYS   A CD  1 
ATOM   818  C  CE  . LYS   A 1 111 ? -52.09300 21.32400 -2.80400  1.000 63.44000  ? 637  LYS   A CE  1 
ATOM   819  N  NZ  . LYS   A 1 111 ? -53.48700 21.31400 -3.32600  1.000 73.62000  ? 637  LYS   A NZ  1 
ATOM   820  N  N   . LEU   A 1 112 ? -50.99300 16.07700 1.97300   1.000 64.94000  ? 638  LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 112 ? -50.51700 14.71900 2.17000   1.000 59.56000  ? 638  LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 112 ? -50.61100 14.32400 3.63800   1.000 54.96000  ? 638  LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 112 ? -50.76200 15.16800 4.52600   1.000 60.39000  ? 638  LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 112 ? -49.06900 14.56700 1.68500   1.000 55.80000  ? 638  LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 112 ? -48.79300 15.02800 0.25200   1.000 50.68000  ? 638  LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 112 ? -47.30000 15.05200 -0.02800  1.000 50.77000  ? 638  LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 112 ? -49.51400 14.13700 -0.74400  1.000 56.10000  ? 638  LEU   A CD2 1 
ATOM   828  N  N   . THR   A 1 113 ? -50.52000 13.02100 3.87900   1.000 47.52000  ? 639  THR   A N   1 
ATOM   829  C  CA  . THR   A 1 113 ? -50.49500 12.48200 5.22800   1.000 55.09000  ? 639  THR   A CA  1 
ATOM   830  C  C   . THR   A 1 113 ? -49.05900 12.41200 5.74100   1.000 58.64000  ? 639  THR   A C   1 
ATOM   831  O  O   . THR   A 1 113 ? -48.09200 12.54300 4.98600   1.000 57.90000  ? 639  THR   A O   1 
ATOM   832  C  CB  . THR   A 1 113 ? -51.14100 11.09600 5.27000   1.000 51.36000  ? 639  THR   A CB  1 
ATOM   833  O  OG1 . THR   A 1 113 ? -50.20400 10.11500 4.80500   1.000 58.33000  ? 639  THR   A OG1 1 
ATOM   834  C  CG2 . THR   A 1 113 ? -52.38500 11.05900 4.39300   1.000 51.49000  ? 639  THR   A CG2 1 
ATOM   835  N  N   . ASP   A 1 114 ? -48.92800 12.20400 7.05400   1.000 54.46000  ? 640  ASP   A N   1 
ATOM   836  C  CA  . ASP   A 1 114 ? -47.60300 12.10800 7.65800   1.000 49.01000  ? 640  ASP   A CA  1 
ATOM   837  C  C   . ASP   A 1 114 ? -46.81900 10.93400 7.08600   1.000 48.34000  ? 640  ASP   A C   1 
ATOM   838  O  O   . ASP   A 1 114 ? -45.61500 11.05000 6.82400   1.000 54.49000  ? 640  ASP   A O   1 
ATOM   839  C  CB  . ASP   A 1 114 ? -47.72400 11.97900 9.17600   1.000 54.88000  ? 640  ASP   A CB  1 
ATOM   840  C  CG  . ASP   A 1 114 ? -48.14700 13.27500 9.83900   1.000 64.06000  ? 640  ASP   A CG  1 
ATOM   841  O  OD1 . ASP   A 1 114 ? -48.17300 14.31600 9.15100   1.000 66.01000  ? 640  ASP   A OD1 1 
ATOM   842  O  OD2 . ASP   A 1 114 ? -48.45200 13.25100 11.05100  1.000 66.21000  ? 640  ASP   A OD2 1 
ATOM   843  N  N   . LEU   A 1 115 ? -47.48500 9.79500  6.88000   1.000 48.52000  ? 641  LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 115 ? -46.80300 8.62800  6.33300   1.000 43.90000  ? 641  LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 115 ? -46.35800 8.86000  4.89500   1.000 40.76000  ? 641  LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 115 ? -45.30400 8.35900  4.48700   1.000 40.37000  ? 641  LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 115 ? -47.71100 7.40200  6.42100   1.000 44.49000  ? 641  LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 115 ? -48.06900 6.94800  7.83900   1.000 45.12000  ? 641  LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 115 ? -49.24900 5.98900  7.82100   1.000 48.83000  ? 641  LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 115 ? -46.86500 6.31200  8.51700   1.000 43.28000  ? 641  LEU   A CD2 1 
ATOM   851  N  N   . GLU   A 1 116 ? -47.14000 9.61100  4.11600   1.000 47.38000  ? 642  GLU   A N   1 
ATOM   852  C  CA  . GLU   A 1 116 ? -46.72100 9.94700  2.75900   1.000 44.66000  ? 642  GLU   A CA  1 
ATOM   853  C  C   . GLU   A 1 116 ? -45.52500 10.89100 2.77200   1.000 44.86000  ? 642  GLU   A C   1 
ATOM   854  O  O   . GLU   A 1 116 ? -44.58300 10.71900 1.99000   1.000 38.15000  ? 642  GLU   A O   1 
ATOM   855  C  CB  . GLU   A 1 116 ? -47.88600 10.56600 1.98800   1.000 53.13000  ? 642  GLU   A CB  1 
ATOM   856  C  CG  . GLU   A 1 116 ? -49.01700 9.59600  1.68400   1.000 58.26000  ? 642  GLU   A CG  1 
ATOM   857  C  CD  . GLU   A 1 116 ? -50.28200 10.30000 1.23200   1.000 57.94000  ? 642  GLU   A CD  1 
ATOM   858  O  OE1 . GLU   A 1 116 ? -50.51000 11.45000 1.66400   1.000 59.84000  ? 642  GLU   A OE1 1 
ATOM   859  O  OE2 . GLU   A 1 116 ? -51.04700 9.70500  0.44600   1.000 61.49000  ? 642  GLU   A OE2 1 
ATOM   860  N  N   . ILE   A 1 117 ? -45.54700 11.89400 3.65400   1.000 44.40000  ? 643  ILE   A N   1 
ATOM   861  C  CA  . ILE   A 1 117 ? -44.41400 12.80700 3.78000   1.000 38.46000  ? 643  ILE   A CA  1 
ATOM   862  C  C   . ILE   A 1 117 ? -43.17900 12.05800 4.26200   1.000 41.05000  ? 643  ILE   A C   1 
ATOM   863  O  O   . ILE   A 1 117 ? -42.06900 12.26700 3.75800   1.000 41.59000  ? 643  ILE   A O   1 
ATOM   864  C  CB  . ILE   A 1 117 ? -44.77200 13.97200 4.72200   1.000 49.36000  ? 643  ILE   A CB  1 
ATOM   865  C  CG1 . ILE   A 1 117 ? -45.88800 14.82500 4.11700   1.000 55.37000  ? 643  ILE   A CG1 1 
ATOM   866  C  CG2 . ILE   A 1 117 ? -43.54300 14.81900 5.02300   1.000 39.01000  ? 643  ILE   A CG2 1 
ATOM   867  C  CD1 . ILE   A 1 117 ? -46.49500 15.80800 5.09300   1.000 60.35000  ? 643  ILE   A CD1 1 
ATOM   868  N  N   . LEU   A 1 118 ? -43.35500 11.17400 5.24800   1.000 41.45000  ? 644  LEU   A N   1 
ATOM   869  C  CA  . LEU   A 1 118 ? -42.23700 10.38300 5.75100   1.000 39.89000  ? 644  LEU   A CA  1 
ATOM   870  C  C   . LEU   A 1 118 ? -41.61700 9.53600  4.64600   1.000 37.05000  ? 644  LEU   A C   1 
ATOM   871  O  O   . LEU   A 1 118 ? -40.38900 9.41800  4.55700   1.000 38.34000  ? 644  LEU   A O   1 
ATOM   872  C  CB  . LEU   A 1 118 ? -42.70700 9.49900  6.90500   1.000 38.04000  ? 644  LEU   A CB  1 
ATOM   873  C  CG  . LEU   A 1 118 ? -41.75700 8.39900  7.37800   1.000 34.27000  ? 644  LEU   A CG  1 
ATOM   874  C  CD1 . LEU   A 1 118 ? -40.52300 9.00400  8.02100   1.000 37.61000  ? 644  LEU   A CD1 1 
ATOM   875  C  CD2 . LEU   A 1 118 ? -42.46700 7.46100  8.34200   1.000 46.81000  ? 644  LEU   A CD2 1 
ATOM   876  N  N   . ALA   A 1 119 ? -42.45100 8.94900  3.78700   1.000 40.18000  ? 645  ALA   A N   1 
ATOM   877  C  CA  . ALA   A 1 119 ? -41.93600 8.09900  2.72000   1.000 41.41000  ? 645  ALA   A CA  1 
ATOM   878  C  C   . ALA   A 1 119 ? -41.29100 8.92200  1.61300   1.000 35.53000  ? 645  ALA   A C   1 
ATOM   879  O  O   . ALA   A 1 119 ? -40.28600 8.50300  1.02600   1.000 35.43000  ? 645  ALA   A O   1 
ATOM   880  C  CB  . ALA   A 1 119 ? -43.05900 7.22800  2.16000   1.000 34.84000  ? 645  ALA   A CB  1 
ATOM   881  N  N   . LEU   A 1 120 ? -41.85300 10.09700 1.31200   1.000 37.06000  ? 646  LEU   A N   1 
ATOM   882  C  CA  . LEU   A 1 120 ? -41.31500 10.92200 0.23400   1.000 37.98000  ? 646  LEU   A CA  1 
ATOM   883  C  C   . LEU   A 1 120 ? -39.91300 11.42100 0.56100   1.000 34.96000  ? 646  LEU   A C   1 
ATOM   884  O  O   . LEU   A 1 120 ? -39.04100 11.46400 -0.31500  1.000 33.35000  ? 646  LEU   A O   1 
ATOM   885  C  CB  . LEU   A 1 120 ? -42.24800 12.10000 -0.04400  1.000 35.95000  ? 646  LEU   A CB  1 
ATOM   886  C  CG  . LEU   A 1 120 ? -43.48600 11.82100 -0.89500  1.000 42.76000  ? 646  LEU   A CG  1 
ATOM   887  C  CD1 . LEU   A 1 120 ? -44.37600 13.05100 -0.94400  1.000 30.27000  ? 646  LEU   A CD1 1 
ATOM   888  C  CD2 . LEU   A 1 120 ? -43.09100 11.38400 -2.29700  1.000 34.83000  ? 646  LEU   A CD2 1 
ATOM   889  N  N   . LEU   A 1 121 ? -39.67800 11.80700 1.81800   1.000 32.98000  ? 647  LEU   A N   1 
ATOM   890  C  CA  . LEU   A 1 121 ? -38.35900 12.29500 2.20400   1.000 42.67000  ? 647  LEU   A CA  1 
ATOM   891  C  C   . LEU   A 1 121 ? -37.33000 11.17100 2.19400   1.000 34.63000  ? 647  LEU   A C   1 
ATOM   892  O  O   . LEU   A 1 121 ? -36.19800 11.36200 1.73500   1.000 39.13000  ? 647  LEU   A O   1 
ATOM   893  C  CB  . LEU   A 1 121 ? -38.42400 12.95200 3.58200   1.000 31.87000  ? 647  LEU   A CB  1 
ATOM   894  C  CG  . LEU   A 1 121 ? -37.14200 13.64700 4.04100   1.000 40.55000  ? 647  LEU   A CG  1 
ATOM   895  C  CD1 . LEU   A 1 121 ? -36.81000 14.80200 3.11500   1.000 34.29000  ? 647  LEU   A CD1 1 
ATOM   896  C  CD2 . LEU   A 1 121 ? -37.27400 14.12700 5.47700   1.000 37.37000  ? 647  LEU   A CD2 1 
ATOM   897  N  N   . ILE   A 1 122 ? -37.70600 9.99300  2.69700   1.000 35.34000  ? 648  ILE   A N   1 
ATOM   898  C  CA  . ILE   A 1 122 ? -36.79200 8.85500  2.69100   1.000 29.50000  ? 648  ILE   A CA  1 
ATOM   899  C  C   . ILE   A 1 122 ? -36.49200 8.41900  1.26200   1.000 28.59000  ? 648  ILE   A C   1 
ATOM   900  O  O   . ILE   A 1 122 ? -35.34800 8.09000  0.92600   1.000 32.37000  ? 648  ILE   A O   1 
ATOM   901  C  CB  . ILE   A 1 122 ? -37.37700 7.69900  3.52300   1.000 35.14000  ? 648  ILE   A CB  1 
ATOM   902  C  CG1 . ILE   A 1 122 ? -37.48200 8.09800  4.99500   1.000 33.08000  ? 648  ILE   A CG1 1 
ATOM   903  C  CG2 . ILE   A 1 122 ? -36.53100 6.44400  3.37200   1.000 29.24000  ? 648  ILE   A CG2 1 
ATOM   904  C  CD1 . ILE   A 1 122 ? -38.19300 7.07200  5.85200   1.000 34.78000  ? 648  ILE   A CD1 1 
ATOM   905  N  N   . ALA   A 1 123 ? -37.50900 8.41700  0.39800   1.000 32.53000  ? 649  ALA   A N   1 
ATOM   906  C  CA  . ALA   A 1 123 ? -37.30200 7.99000  -0.98200  1.000 34.32000  ? 649  ALA   A CA  1 
ATOM   907  C  C   . ALA   A 1 123 ? -36.42200 8.97400  -1.74100  1.000 29.72000  ? 649  ALA   A C   1 
ATOM   908  O  O   . ALA   A 1 123 ? -35.56100 8.56300  -2.52800  1.000 35.39000  ? 649  ALA   A O   1 
ATOM   909  C  CB  . ALA   A 1 123 ? -38.64600 7.81900  -1.68700  1.000 36.90000  ? 649  ALA   A CB  1 
ATOM   910  N  N   . ALA   A 1 124 ? -36.62000 10.27500 -1.51800  1.000 32.09000  ? 650  ALA   A N   1 
ATOM   911  C  CA  . ALA   A 1 124 ? -35.81500 11.27500 -2.21200  1.000 31.73000  ? 650  ALA   A CA  1 
ATOM   912  C  C   . ALA   A 1 124 ? -34.33800 11.13500 -1.86600  1.000 26.69000  ? 650  ALA   A C   1 
ATOM   913  O  O   . ALA   A 1 124 ? -33.47200 11.28400 -2.73600  1.000 28.21000  ? 650  ALA   A O   1 
ATOM   914  C  CB  . ALA   A 1 124 ? -36.31700 12.67800 -1.87300  1.000 31.13000  ? 650  ALA   A CB  1 
ATOM   915  N  N   . LEU   A 1 125 ? -34.03000 10.84400 -0.60100  1.000 28.51000  ? 651  LEU   A N   1 
ATOM   916  C  CA  . LEU   A 1 125 ? -32.64400 10.65100 -0.19400  1.000 27.42000  ? 651  LEU   A CA  1 
ATOM   917  C  C   . LEU   A 1 125 ? -32.06400 9.33900  -0.70300  1.000 31.55000  ? 651  LEU   A C   1 
ATOM   918  O  O   . LEU   A 1 125 ? -30.83900 9.22000  -0.81300  1.000 31.48000  ? 651  LEU   A O   1 
ATOM   919  C  CB  . LEU   A 1 125 ? -32.52900 10.69900 1.33100   1.000 37.24000  ? 651  LEU   A CB  1 
ATOM   920  C  CG  . LEU   A 1 125 ? -32.74700 12.04800 2.01800   1.000 38.52000  ? 651  LEU   A CG  1 
ATOM   921  C  CD1 . LEU   A 1 125 ? -33.17300 11.84600 3.46300   1.000 41.24000  ? 651  LEU   A CD1 1 
ATOM   922  C  CD2 . LEU   A 1 125 ? -31.49100 12.90100 1.93900   1.000 42.50000  ? 651  LEU   A CD2 1 
ATOM   923  N  N   . SER   A 1 126 ? -32.90700 8.35900  -1.02000  1.000 37.08000  ? 652  SER   A N   1 
ATOM   924  C  CA  . SER   A 1 126 ? -32.44900 7.01300  -1.33300  1.000 32.92000  ? 652  SER   A CA  1 
ATOM   925  C  C   . SER   A 1 126 ? -32.68800 6.60500  -2.78000  1.000 37.56000  ? 652  SER   A C   1 
ATOM   926  O  O   . SER   A 1 126 ? -32.31000 5.49100  -3.16100  1.000 45.15000  ? 652  SER   A O   1 
ATOM   927  C  CB  . SER   A 1 126 ? -33.13600 6.00600  -0.40500  1.000 29.76000  ? 652  SER   A CB  1 
ATOM   928  O  OG  . SER   A 1 126 ? -33.32300 6.54400  0.89300   1.000 33.93000  ? 652  SER   A OG  1 
ATOM   929  N  N   . HIS   A 1 127 ? -33.28700 7.47100  -3.60000  1.000 31.67000  ? 653  HIS   A N   1 
ATOM   930  C  CA  . HIS   A 1 127 ? -33.77400 7.06400  -4.91500  1.000 28.13000  ? 653  HIS   A CA  1 
ATOM   931  C  C   . HIS   A 1 127 ? -32.66500 6.70000  -5.89700  1.000 30.00000  ? 653  HIS   A C   1 
ATOM   932  O  O   . HIS   A 1 127 ? -32.97200 6.16700  -6.96800  1.000 38.29000  ? 653  HIS   A O   1 
ATOM   933  C  CB  . HIS   A 1 127 ? -34.64300 8.17000  -5.51800  1.000 29.08000  ? 653  HIS   A CB  1 
ATOM   934  C  CG  . HIS   A 1 127 ? -33.86000 9.31600  -6.07800  1.000 36.30000  ? 653  HIS   A CG  1 
ATOM   935  N  ND1 . HIS   A 1 127 ? -33.40700 10.35900 -5.29900  1.000 32.30000  ? 653  HIS   A ND1 1 
ATOM   936  C  CD2 . HIS   A 1 127 ? -33.44800 9.58300  -7.34000  1.000 32.49000  ? 653  HIS   A CD2 1 
ATOM   937  C  CE1 . HIS   A 1 127 ? -32.75000 11.21900 -6.05700  1.000 39.93000  ? 653  HIS   A CE1 1 
ATOM   938  N  NE2 . HIS   A 1 127 ? -32.76000 10.77200 -7.30000  1.000 36.97000  ? 653  HIS   A NE2 1 
ATOM   939  N  N   . ASP   A 1 128 ? -31.39800 6.96400  -5.57400  1.000 27.76000  ? 654  ASP   A N   1 
ATOM   940  C  CA  . ASP   A 1 128 ? -30.30300 6.68400  -6.49600  1.000 28.63000  ? 654  ASP   A CA  1 
ATOM   941  C  C   . ASP   A 1 128 ? -29.13300 6.00800  -5.79200  1.000 35.42000  ? 654  ASP   A C   1 
ATOM   942  O  O   . ASP   A 1 128 ? -27.98700 6.12800  -6.23400  1.000 35.69000  ? 654  ASP   A O   1 
ATOM   943  C  CB  . ASP   A 1 128 ? -29.83300 7.96300  -7.19000  1.000 31.00000  ? 654  ASP   A CB  1 
ATOM   944  C  CG  . ASP   A 1 128 ? -30.58500 8.23800  -8.47600  1.000 40.74000  ? 654  ASP   A CG  1 
ATOM   945  O  OD1 . ASP   A 1 128 ? -31.09500 7.27400  -9.08600  1.000 43.46000  ? 654  ASP   A OD1 1 
ATOM   946  O  OD2 . ASP   A 1 128 ? -30.66000 9.41800  -8.88000  1.000 38.11000  ? 654  ASP   A OD2 1 
ATOM   947  N  N   . LEU   A 1 129 ? -29.40500 5.29300  -4.70100  1.000 37.06000  ? 655  LEU   A N   1 
ATOM   948  C  CA  . LEU   A 1 129 ? -28.34100 4.67000  -3.92300  1.000 31.20000  ? 655  LEU   A CA  1 
ATOM   949  C  C   . LEU   A 1 129 ? -27.53600 3.69800  -4.77800  1.000 41.63000  ? 655  LEU   A C   1 
ATOM   950  O  O   . LEU   A 1 129 ? -28.08500 2.98500  -5.62200  1.000 44.27000  ? 655  LEU   A O   1 
ATOM   951  C  CB  . LEU   A 1 129 ? -28.92700 3.94000  -2.71400  1.000 37.76000  ? 655  LEU   A CB  1 
ATOM   952  C  CG  . LEU   A 1 129 ? -29.21800 4.77300  -1.46500  1.000 37.78000  ? 655  LEU   A CG  1 
ATOM   953  C  CD1 . LEU   A 1 129 ? -30.14700 4.01800  -0.53600  1.000 35.76000  ? 655  LEU   A CD1 1 
ATOM   954  C  CD2 . LEU   A 1 129 ? -27.93100 5.13500  -0.74900  1.000 27.71000  ? 655  LEU   A CD2 1 
ATOM   955  N  N   . ASP   A 1 130 ? -26.22000 3.68800  -4.55500  1.000 47.48000  ? 656  ASP   A N   1 
ATOM   956  C  CA  . ASP   A 1 130 ? -25.29200 2.78500  -5.24000  1.000 44.44000  ? 656  ASP   A CA  1 
ATOM   957  C  C   . ASP   A 1 130 ? -25.29600 2.99700  -6.75300  1.000 44.27000  ? 656  ASP   A C   1 
ATOM   958  O  O   . ASP   A 1 130 ? -25.12900 2.05000  -7.52500  1.000 45.66000  ? 656  ASP   A O   1 
ATOM   959  C  CB  . ASP   A 1 130 ? -25.58900 1.32100  -4.89900  1.000 47.36000  ? 656  ASP   A CB  1 
ATOM   960  C  CG  . ASP   A 1 130 ? -24.39100 0.41600  -5.11500  1.000 52.78000  ? 656  ASP   A CG  1 
ATOM   961  O  OD1 . ASP   A 1 130 ? -23.28400 0.77100  -4.65600  1.000 55.39000  ? 656  ASP   A OD1 1 
ATOM   962  O  OD2 . ASP   A 1 130 ? -24.55700 -0.65000 -5.74400  1.000 54.98000  ? 656  ASP   A OD2 1 
ATOM   963  N  N   . HIS   A 1 131 ? -25.48500 4.24000  -7.19000  1.000 57.39000  ? 657  HIS   A N   1 
ATOM   964  C  CA  . HIS   A 1 131 ? -25.39100 4.57100  -8.60500  1.000 42.71000  ? 657  HIS   A CA  1 
ATOM   965  C  C   . HIS   A 1 131 ? -23.92800 4.66700  -9.01900  1.000 45.02000  ? 657  HIS   A C   1 
ATOM   966  O  O   . HIS   A 1 131 ? -23.10400 5.25300  -8.31000  1.000 50.16000  ? 657  HIS   A O   1 
ATOM   967  C  CB  . HIS   A 1 131 ? -26.11100 5.88900  -8.89200  1.000 45.86000  ? 657  HIS   A CB  1 
ATOM   968  C  CG  . HIS   A 1 131 ? -26.58000 6.03000  -10.30800 1.000 38.16000  ? 657  HIS   A CG  1 
ATOM   969  N  ND1 . HIS   A 1 131 ? -25.72100 5.98600  -11.38500 1.000 38.21000  ? 657  HIS   A ND1 1 
ATOM   970  C  CD2 . HIS   A 1 131 ? -27.81700 6.22400  -10.82200 1.000 32.35000  ? 657  HIS   A CD2 1 
ATOM   971  C  CE1 . HIS   A 1 131 ? -26.40900 6.14200  -12.50100 1.000 38.35000  ? 657  HIS   A CE1 1 
ATOM   972  N  NE2 . HIS   A 1 131 ? -27.68400 6.28800  -12.18800 1.000 39.53000  ? 657  HIS   A NE2 1 
ATOM   973  N  N   . ARG   A 1 132 ? -23.60400 4.08400  -10.17500 1.000 47.99000  ? 658  ARG   A N   1 
ATOM   974  C  CA  . ARG   A 1 132 ? -22.22600 4.02100  -10.65200 1.000 61.29000  ? 658  ARG   A CA  1 
ATOM   975  C  C   . ARG   A 1 132 ? -22.01600 4.80800  -11.94100 1.000 51.37000  ? 658  ARG   A C   1 
ATOM   976  O  O   . ARG   A 1 132 ? -20.99700 4.62600  -12.61200 1.000 59.03000  ? 658  ARG   A O   1 
ATOM   977  C  CB  . ARG   A 1 132 ? -21.79500 2.56800  -10.85200 1.000 65.22000  ? 658  ARG   A CB  1 
ATOM   978  C  CG  . ARG   A 1 132 ? -22.07100 1.66900  -9.66400  1.000 64.32000  ? 658  ARG   A CG  1 
ATOM   979  C  CD  . ARG   A 1 132 ? -20.86400 0.80500  -9.34900  1.000 77.02000  ? 658  ARG   A CD  1 
ATOM   980  N  NE  . ARG   A 1 132 ? -21.24900 -0.45700 -8.72600  1.000 89.85000  ? 658  ARG   A NE  1 
ATOM   981  C  CZ  . ARG   A 1 132 ? -20.93200 -1.65200 -9.21100  1.000 95.57000  ? 658  ARG   A CZ  1 
ATOM   982  N  NH1 . ARG   A 1 132 ? -21.32500 -2.75100 -8.58100  1.000 96.86000  ? 658  ARG   A NH1 1 
ATOM   983  N  NH2 . ARG   A 1 132 ? -20.21900 -1.74900 -10.32400 1.000 94.35000  ? 658  ARG   A NH2 1 
ATOM   984  N  N   . GLY   A 1 133 ? -22.94400 5.67700  -12.29700 1.000 52.88000  ? 659  GLY   A N   1 
ATOM   985  C  CA  . GLY   A 1 133 ? -22.82200 6.41200  -13.53800 1.000 59.11000  ? 659  GLY   A CA  1 
ATOM   986  C  C   . GLY   A 1 133 ? -23.65500 5.79500  -14.64500 1.000 63.97000  ? 659  GLY   A C   1 
ATOM   987  O  O   . GLY   A 1 133 ? -23.85700 4.57700  -14.70900 1.000 71.79000  ? 659  GLY   A O   1 
ATOM   988  N  N   . VAL   A 1 134 ? -24.15000 6.65300  -15.54100 1.000 64.65000  ? 660  VAL   A N   1 
ATOM   989  C  CA  . VAL   A 1 134 ? -25.03800 6.19700  -16.60400 1.000 75.58000  ? 660  VAL   A CA  1 
ATOM   990  C  C   . VAL   A 1 134 ? -24.32000 5.31500  -17.61500 1.000 81.98000  ? 660  VAL   A C   1 
ATOM   991  O  O   . VAL   A 1 134 ? -24.96200 4.49500  -18.28300 1.000 67.52000  ? 660  VAL   A O   1 
ATOM   992  C  CB  . VAL   A 1 134 ? -25.68800 7.40300  -17.30600 1.000 69.57000  ? 660  VAL   A CB  1 
ATOM   993  C  CG1 . VAL   A 1 134 ? -26.67600 8.08200  -16.37400 1.000 52.94000  ? 660  VAL   A CG1 1 
ATOM   994  C  CG2 . VAL   A 1 134 ? -24.62200 8.38500  -17.77100 1.000 65.98000  ? 660  VAL   A CG2 1 
ATOM   995  N  N   . ASN   A 1 135 ? -23.00300 5.45700  -17.75100 1.000 81.48000  ? 661  ASN   A N   1 
ATOM   996  C  CA  . ASN   A 1 135 ? -22.22600 4.66400  -18.69100 1.000 87.74000  ? 661  ASN   A CA  1 
ATOM   997  C  C   . ASN   A 1 135 ? -21.51200 3.49800  -18.02000 1.000 89.31000  ? 661  ASN   A C   1 
ATOM   998  O  O   . ASN   A 1 135 ? -20.62400 2.89300  -18.62800 1.000 85.32000  ? 661  ASN   A O   1 
ATOM   999  C  CB  . ASN   A 1 135 ? -21.22000 5.55500  -19.42000 1.000 81.26000  ? 661  ASN   A CB  1 
ATOM   1000 C  CG  . ASN   A 1 135 ? -21.89500 6.63000  -20.25000 1.000 80.28000  ? 661  ASN   A CG  1 
ATOM   1001 O  OD1 . ASN   A 1 135 ? -22.97000 6.41400  -20.81000 1.000 75.77000  ? 661  ASN   A OD1 1 
ATOM   1002 N  ND2 . ASN   A 1 135 ? -21.27000 7.79900  -20.32700 1.000 89.53000  ? 661  ASN   A ND2 1 
ATOM   1003 N  N   . ASN   A 1 136 ? -21.87100 3.18000  -16.78000 1.000 90.18000  ? 662  ASN   A N   1 
ATOM   1004 C  CA  . ASN   A 1 136 ? -21.30800 2.06300  -16.02800 1.000 87.08000  ? 662  ASN   A CA  1 
ATOM   1005 C  C   . ASN   A 1 136 ? -22.42400 1.17200  -15.50100 1.000 88.00000  ? 662  ASN   A C   1 
ATOM   1006 O  O   . ASN   A 1 136 ? -22.39500 0.72300  -14.35200 1.000 84.42000  ? 662  ASN   A O   1 
ATOM   1007 C  CB  . ASN   A 1 136 ? -20.43300 2.55600  -14.87500 1.000 79.83000  ? 662  ASN   A CB  1 
ATOM   1008 C  CG  . ASN   A 1 136 ? -19.05000 3.01700  -15.32400 1.000 96.79000  ? 662  ASN   A CG  1 
ATOM   1009 O  OD1 . ASN   A 1 136 ? -18.09400 2.97700  -14.54700 1.000 101.32000 ? 662  ASN   A OD1 1 
ATOM   1010 N  ND2 . ASN   A 1 136 ? -18.93900 3.46400  -16.56600 1.000 98.50000  ? 662  ASN   A ND2 1 
ATOM   1011 N  N   . SER   A 1 137 ? -23.43100 0.90800  -16.33300 1.000 88.64000  ? 663  SER   A N   1 
ATOM   1012 C  CA  . SER   A 1 137 ? -24.61600 0.16800  -15.92000 1.000 99.16000  ? 663  SER   A CA  1 
ATOM   1013 C  C   . SER   A 1 137 ? -24.58200 -1.29700 -16.34200 1.000 107.36000 ? 663  SER   A C   1 
ATOM   1014 O  O   . SER   A 1 137 ? -25.58400 -2.00100 -16.17400 1.000 111.21000 ? 663  SER   A O   1 
ATOM   1015 C  CB  . SER   A 1 137 ? -25.87500 0.83900  -16.47600 1.000 90.73000  ? 663  SER   A CB  1 
ATOM   1016 O  OG  . SER   A 1 137 ? -26.96800 -0.06400 -16.51000 1.000 103.58000 ? 663  SER   A OG  1 
ATOM   1017 N  N   . TYR   A 1 138 ? -23.45600 -1.77500 -16.88100 1.000 99.92000  ? 664  TYR   A N   1 
ATOM   1018 C  CA  . TYR   A 1 138 ? -23.39300 -3.15900 -17.34000 1.000 109.37000 ? 664  TYR   A CA  1 
ATOM   1019 C  C   . TYR   A 1 138 ? -23.46600 -4.14700 -16.18300 1.000 115.94000 ? 664  TYR   A C   1 
ATOM   1020 O  O   . TYR   A 1 138 ? -24.00400 -5.24800 -16.34700 1.000 121.19000 ? 664  TYR   A O   1 
ATOM   1021 C  CB  . TYR   A 1 138 ? -22.11700 -3.39600 -18.15000 1.000 109.39000 ? 664  TYR   A CB  1 
ATOM   1022 C  CG  . TYR   A 1 138 ? -21.89000 -4.85100 -18.50100 1.000 115.13000 ? 664  TYR   A CG  1 
ATOM   1023 C  CD1 . TYR   A 1 138 ? -22.53600 -5.43200 -19.58400 1.000 113.03000 ? 664  TYR   A CD1 1 
ATOM   1024 C  CD2 . TYR   A 1 138 ? -21.03400 -5.64500 -17.74500 1.000 113.58000 ? 664  TYR   A CD2 1 
ATOM   1025 C  CE1 . TYR   A 1 138 ? -22.33600 -6.76200 -19.90600 1.000 110.37000 ? 664  TYR   A CE1 1 
ATOM   1026 C  CE2 . TYR   A 1 138 ? -20.82900 -6.97600 -18.06000 1.000 116.10000 ? 664  TYR   A CE2 1 
ATOM   1027 C  CZ  . TYR   A 1 138 ? -21.48200 -7.52900 -19.14200 1.000 114.95000 ? 664  TYR   A CZ  1 
ATOM   1028 O  OH  . TYR   A 1 138 ? -21.27800 -8.85200 -19.45800 1.000 106.07000 ? 664  TYR   A OH  1 
ATOM   1029 N  N   . ILE   A 1 139 ? -22.93200 -3.77900 -15.01400 1.000 105.62000 ? 665  ILE   A N   1 
ATOM   1030 C  CA  . ILE   A 1 139 ? -22.95800 -4.66700 -13.85700 1.000 103.24000 ? 665  ILE   A CA  1 
ATOM   1031 C  C   . ILE   A 1 139 ? -24.38000 -4.95800 -13.40700 1.000 108.99000 ? 665  ILE   A C   1 
ATOM   1032 O  O   . ILE   A 1 139 ? -24.60600 -5.91900 -12.66300 1.000 114.70000 ? 665  ILE   A O   1 
ATOM   1033 C  CB  . ILE   A 1 139 ? -22.11600 -4.06200 -12.70700 1.000 106.02000 ? 665  ILE   A CB  1 
ATOM   1034 C  CG1 . ILE   A 1 139 ? -22.74700 -2.77000 -12.16800 1.000 105.49000 ? 665  ILE   A CG1 1 
ATOM   1035 C  CG2 . ILE   A 1 139 ? -20.68700 -3.81900 -13.16600 1.000 99.05000  ? 665  ILE   A CG2 1 
ATOM   1036 C  CD1 . ILE   A 1 139 ? -23.66000 -2.96000 -10.96000 1.000 101.99000 ? 665  ILE   A CD1 1 
ATOM   1037 N  N   . GLN   A 1 140 ? -25.34200 -4.14000 -13.83200 1.000 106.30000 ? 666  GLN   A N   1 
ATOM   1038 C  CA  . GLN   A 1 140 ? -26.75200 -4.29900 -13.48100 1.000 105.27000 ? 666  GLN   A CA  1 
ATOM   1039 C  C   . GLN   A 1 140 ? -26.95900 -4.22200 -11.97100 1.000 108.05000 ? 666  GLN   A C   1 
ATOM   1040 O  O   . GLN   A 1 140 ? -27.00500 -3.13200 -11.39800 1.000 91.16000  ? 666  GLN   A O   1 
ATOM   1041 C  CB  . GLN   A 1 140 ? -27.30200 -5.61900 -14.03000 1.000 109.93000 ? 666  GLN   A CB  1 
ATOM   1042 C  CG  . GLN   A 1 140 ? -27.17000 -5.76100 -15.53900 1.000 111.41000 ? 666  GLN   A CG  1 
ATOM   1043 C  CD  . GLN   A 1 140 ? -26.46900 -7.04300 -15.94600 1.000 111.01000 ? 666  GLN   A CD  1 
ATOM   1044 O  OE1 . GLN   A 1 140 ? -26.09800 -7.85700 -15.10000 1.000 105.38000 ? 666  GLN   A OE1 1 
ATOM   1045 N  NE2 . GLN   A 1 140 ? -26.28200 -7.22800 -17.24800 1.000 105.55000 ? 666  GLN   A NE2 1 
ATOM   1046 N  N   . HIS   A 1 152 ? -37.70000 -2.37800 -17.42400 1.000 78.18000  ? 678  HIS   A N   1 
ATOM   1047 C  CA  . HIS   A 1 152 ? -38.57300 -2.59500 -16.27600 1.000 85.10000  ? 678  HIS   A CA  1 
ATOM   1048 C  C   . HIS   A 1 152 ? -37.97600 -1.99000 -15.00600 1.000 91.52000  ? 678  HIS   A C   1 
ATOM   1049 O  O   . HIS   A 1 152 ? -38.29300 -2.42100 -13.89600 1.000 90.95000  ? 678  HIS   A O   1 
ATOM   1050 C  CB  . HIS   A 1 152 ? -38.84200 -4.09000 -16.08100 1.000 86.77000  ? 678  HIS   A CB  1 
ATOM   1051 C  CG  . HIS   A 1 152 ? -37.65100 -4.86500 -15.60500 1.000 94.79000  ? 678  HIS   A CG  1 
ATOM   1052 N  ND1 . HIS   A 1 152 ? -37.32700 -4.98600 -14.27100 1.000 89.87000  ? 678  HIS   A ND1 1 
ATOM   1053 C  CD2 . HIS   A 1 152 ? -36.71100 -5.56100 -16.28600 1.000 98.86000  ? 678  HIS   A CD2 1 
ATOM   1054 C  CE1 . HIS   A 1 152 ? -36.23800 -5.72400 -14.15100 1.000 90.12000  ? 678  HIS   A CE1 1 
ATOM   1055 N  NE2 . HIS   A 1 152 ? -35.84400 -6.08600 -15.35900 1.000 101.98000 ? 678  HIS   A NE2 1 
ATOM   1056 N  N   . SER   A 1 153 ? -37.10900 -0.99200 -15.18900 1.000 77.27000  ? 679  SER   A N   1 
ATOM   1057 C  CA  . SER   A 1 153 ? -36.48600 -0.24300 -14.09600 1.000 58.86000  ? 679  SER   A CA  1 
ATOM   1058 C  C   . SER   A 1 153 ? -35.65700 -1.16800 -13.19800 1.000 56.70000  ? 679  SER   A C   1 
ATOM   1059 O  O   . SER   A 1 153 ? -36.03200 -1.50300 -12.07300 1.000 61.82000  ? 679  SER   A O   1 
ATOM   1060 C  CB  . SER   A 1 153 ? -37.54100 0.51500  -13.28100 1.000 49.27000  ? 679  SER   A CB  1 
ATOM   1061 O  OG  . SER   A 1 153 ? -38.59300 0.98100  -14.11000 1.000 60.75000  ? 679  SER   A OG  1 
ATOM   1062 N  N   . ILE   A 1 154 ? -34.50300 -1.56800 -13.73400 1.000 59.74000  ? 680  ILE   A N   1 
ATOM   1063 C  CA  . ILE   A 1 154 ? -33.58300 -2.40500 -12.97000 1.000 57.61000  ? 680  ILE   A CA  1 
ATOM   1064 C  C   . ILE   A 1 154 ? -32.82100 -1.57200 -11.94800 1.000 51.30000  ? 680  ILE   A C   1 
ATOM   1065 O  O   . ILE   A 1 154 ? -32.67700 -1.96800 -10.78500 1.000 64.76000  ? 680  ILE   A O   1 
ATOM   1066 C  CB  . ILE   A 1 154 ? -32.62100 -3.15300 -13.91200 1.000 63.25000  ? 680  ILE   A CB  1 
ATOM   1067 C  CG1 . ILE   A 1 154 ? -33.39800 -4.06500 -14.85700 1.000 71.23000  ? 680  ILE   A CG1 1 
ATOM   1068 C  CG2 . ILE   A 1 154 ? -31.61100 -3.96000 -13.10900 1.000 62.87000  ? 680  ILE   A CG2 1 
ATOM   1069 C  CD1 . ILE   A 1 154 ? -32.53300 -4.78900 -15.86200 1.000 79.43000  ? 680  ILE   A CD1 1 
ATOM   1070 N  N   . MET   A 1 155 ? -32.32100 -0.40600 -12.36800 1.000 55.46000  ? 681  MET   A N   1 
ATOM   1071 C  CA  . MET   A 1 155 ? -31.56800 0.44700  -11.45400 1.000 48.79000  ? 681  MET   A CA  1 
ATOM   1072 C  C   . MET   A 1 155 ? -32.43300 0.90600  -10.28800 1.000 37.70000  ? 681  MET   A C   1 
ATOM   1073 O  O   . MET   A 1 155 ? -31.98900 0.89600  -9.13400  1.000 43.94000  ? 681  MET   A O   1 
ATOM   1074 C  CB  . MET   A 1 155 ? -31.00100 1.65300  -12.20500 1.000 49.53000  ? 681  MET   A CB  1 
ATOM   1075 C  CG  . MET   A 1 155 ? -30.03600 1.29800  -13.32400 1.000 46.18000  ? 681  MET   A CG  1 
ATOM   1076 S  SD  . MET   A 1 155 ? -28.75600 0.13700  -12.81000 1.000 87.74000  ? 681  MET   A SD  1 
ATOM   1077 C  CE  . MET   A 1 155 ? -27.97200 1.04500  -11.48000 1.000 59.09000  ? 681  MET   A CE  1 
ATOM   1078 N  N   . GLU   A 1 156 ? -33.67700 1.30200  -10.56900 1.000 36.52000  ? 682  GLU   A N   1 
ATOM   1079 C  CA  . GLU   A 1 156 ? -34.56200 1.77800  -9.51100  1.000 39.04000  ? 682  GLU   A CA  1 
ATOM   1080 C  C   . GLU   A 1 156 ? -34.87000 0.67300  -8.50900  1.000 47.33000  ? 682  GLU   A C   1 
ATOM   1081 O  O   . GLU   A 1 156 ? -34.97800 0.92900  -7.30300  1.000 43.65000  ? 682  GLU   A O   1 
ATOM   1082 C  CB  . GLU   A 1 156 ? -35.85100 2.33300  -10.11700 1.000 45.33000  ? 682  GLU   A CB  1 
ATOM   1083 C  CG  . GLU   A 1 156 ? -35.68100 3.66500  -10.83500 1.000 45.02000  ? 682  GLU   A CG  1 
ATOM   1084 C  CD  . GLU   A 1 156 ? -35.00200 3.52300  -12.18500 1.000 49.33000  ? 682  GLU   A CD  1 
ATOM   1085 O  OE1 . GLU   A 1 156 ? -34.96000 2.39300  -12.71500 1.000 56.52000  ? 682  GLU   A OE1 1 
ATOM   1086 O  OE2 . GLU   A 1 156 ? -34.50900 4.53900  -12.71600 1.000 50.12000  ? 682  GLU   A OE2 1 
ATOM   1087 N  N   . HIS   A 1 157 ? -35.01900 -0.56500 -8.98700  1.000 46.64000  ? 683  HIS   A N   1 
ATOM   1088 C  CA  . HIS   A 1 157 ? -35.20100 -1.68700 -8.07200  1.000 42.70000  ? 683  HIS   A CA  1 
ATOM   1089 C  C   . HIS   A 1 157 ? -33.95400 -1.91000 -7.22700  1.000 36.32000  ? 683  HIS   A C   1 
ATOM   1090 O  O   . HIS   A 1 157 ? -34.05100 -2.25900 -6.04500  1.000 40.28000  ? 683  HIS   A O   1 
ATOM   1091 C  CB  . HIS   A 1 157 ? -35.55700 -2.95200 -8.85200  1.000 47.29000  ? 683  HIS   A CB  1 
ATOM   1092 C  CG  . HIS   A 1 157 ? -37.02300 -3.10800 -9.11300  1.000 33.93000  ? 683  HIS   A CG  1 
ATOM   1093 N  ND1 . HIS   A 1 157 ? -37.58900 -2.87400 -10.34700 1.000 44.78000  ? 683  HIS   A ND1 1 
ATOM   1094 C  CD2 . HIS   A 1 157 ? -38.04000 -3.47200 -8.29600  1.000 40.69000  ? 683  HIS   A CD2 1 
ATOM   1095 C  CE1 . HIS   A 1 157 ? -38.89100 -3.08800 -10.28000 1.000 45.83000  ? 683  HIS   A CE1 1 
ATOM   1096 N  NE2 . HIS   A 1 157 ? -39.19000 -3.45200 -9.04600  1.000 39.57000  ? 683  HIS   A NE2 1 
ATOM   1097 N  N   . HIS   A 1 158 ? -32.77300 -1.71200 -7.81700  1.000 33.92000  ? 684  HIS   A N   1 
ATOM   1098 C  CA  . HIS   A 1 158 ? -31.53700 -1.81300 -7.04900  1.000 33.38000  ? 684  HIS   A CA  1 
ATOM   1099 C  C   . HIS   A 1 158 ? -31.42200 -0.67700 -6.04100  1.000 46.54000  ? 684  HIS   A C   1 
ATOM   1100 O  O   . HIS   A 1 158 ? -30.89300 -0.86800 -4.94000  1.000 46.03000  ? 684  HIS   A O   1 
ATOM   1101 C  CB  . HIS   A 1 158 ? -30.33400 -1.81900 -7.99200  1.000 32.95000  ? 684  HIS   A CB  1 
ATOM   1102 C  CG  . HIS   A 1 158 ? -29.01300 -1.82600 -7.28700  1.000 43.41000  ? 684  HIS   A CG  1 
ATOM   1103 N  ND1 . HIS   A 1 158 ? -28.58900 -2.88100 -6.50800  1.000 43.47000  ? 684  HIS   A ND1 1 
ATOM   1104 C  CD2 . HIS   A 1 158 ? -28.02100 -0.90500 -7.24300  1.000 38.15000  ? 684  HIS   A CD2 1 
ATOM   1105 C  CE1 . HIS   A 1 158 ? -27.39200 -2.61100 -6.01700  1.000 45.11000  ? 684  HIS   A CE1 1 
ATOM   1106 N  NE2 . HIS   A 1 158 ? -27.02600 -1.41700 -6.44800  1.000 47.73000  ? 684  HIS   A NE2 1 
ATOM   1107 N  N   . HIS   A 1 159 ? -31.91400 0.51200  -6.39900  1.000 38.31000  ? 685  HIS   A N   1 
ATOM   1108 C  CA  . HIS   A 1 159 ? -31.86600 1.64200  -5.47700  1.000 44.45000  ? 685  HIS   A CA  1 
ATOM   1109 C  C   . HIS   A 1 159 ? -32.74100 1.39600  -4.25500  1.000 39.18000  ? 685  HIS   A C   1 
ATOM   1110 O  O   . HIS   A 1 159 ? -32.35200 1.72700  -3.12900  1.000 37.02000  ? 685  HIS   A O   1 
ATOM   1111 C  CB  . HIS   A 1 159 ? -32.29200 2.92400  -6.19200  1.000 39.47000  ? 685  HIS   A CB  1 
ATOM   1112 C  CG  . HIS   A 1 159 ? -31.39400 3.31200  -7.32500  1.000 37.84000  ? 685  HIS   A CG  1 
ATOM   1113 N  ND1 . HIS   A 1 159 ? -30.02300 3.18300  -7.26400  1.000 34.18000  ? 685  HIS   A ND1 1 
ATOM   1114 C  CD2 . HIS   A 1 159 ? -31.67000 3.82600  -8.54700  1.000 31.08000  ? 685  HIS   A CD2 1 
ATOM   1115 C  CE1 . HIS   A 1 159 ? -29.49300 3.60000  -8.40000  1.000 32.10000  ? 685  HIS   A CE1 1 
ATOM   1116 N  NE2 . HIS   A 1 159 ? -30.47100 3.99400  -9.19600  1.000 34.01000  ? 685  HIS   A NE2 1 
ATOM   1117 N  N   . PHE   A 1 160 ? -33.92700 0.81700  -4.45400  1.000 34.34000  ? 686  PHE   A N   1 
ATOM   1118 C  CA  . PHE   A 1 160 ? -34.79300 0.52600  -3.31800  1.000 36.49000  ? 686  PHE   A CA  1 
ATOM   1119 C  C   . PHE   A 1 160 ? -34.23300 -0.61200 -2.47300  1.000 41.53000  ? 686  PHE   A C   1 
ATOM   1120 O  O   . PHE   A 1 160 ? -34.36900 -0.60200 -1.24400  1.000 46.81000  ? 686  PHE   A O   1 
ATOM   1121 C  CB  . PHE   A 1 160 ? -36.20500 0.19000  -3.79400  1.000 34.17000  ? 686  PHE   A CB  1 
ATOM   1122 C  CG  . PHE   A 1 160 ? -37.11100 -0.27100 -2.69300  1.000 47.93000  ? 686  PHE   A CG  1 
ATOM   1123 C  CD1 . PHE   A 1 160 ? -37.72600 0.64600  -1.85700  1.000 45.95000  ? 686  PHE   A CD1 1 
ATOM   1124 C  CD2 . PHE   A 1 160 ? -37.33500 -1.62000 -2.48100  1.000 50.59000  ? 686  PHE   A CD2 1 
ATOM   1125 C  CE1 . PHE   A 1 160 ? -38.55600 0.22500  -0.83600  1.000 54.43000  ? 686  PHE   A CE1 1 
ATOM   1126 C  CE2 . PHE   A 1 160 ? -38.15800 -2.04500 -1.46300  1.000 47.97000  ? 686  PHE   A CE2 1 
ATOM   1127 C  CZ  . PHE   A 1 160 ? -38.77300 -1.12300 -0.64000  1.000 56.23000  ? 686  PHE   A CZ  1 
ATOM   1128 N  N   . ASP   A 1 161 ? -33.61600 -1.60900 -3.11500  1.000 41.39000  ? 687  ASP   A N   1 
ATOM   1129 C  CA  . ASP   A 1 161 ? -32.97200 -2.68300 -2.36500  1.000 41.77000  ? 687  ASP   A CA  1 
ATOM   1130 C  C   . ASP   A 1 161 ? -31.90800 -2.13100 -1.42600  1.000 41.17000  ? 687  ASP   A C   1 
ATOM   1131 O  O   . ASP   A 1 161 ? -31.78700 -2.57700 -0.27900  1.000 49.06000  ? 687  ASP   A O   1 
ATOM   1132 C  CB  . ASP   A 1 161 ? -32.36000 -3.70300 -3.32600  1.000 45.79000  ? 687  ASP   A CB  1 
ATOM   1133 C  CG  . ASP   A 1 161 ? -33.38100 -4.68500 -3.86600  1.000 61.20000  ? 687  ASP   A CG  1 
ATOM   1134 O  OD1 . ASP   A 1 161 ? -34.30500 -5.06000 -3.11400  1.000 76.73000  ? 687  ASP   A OD1 1 
ATOM   1135 O  OD2 . ASP   A 1 161 ? -33.25800 -5.08200 -5.04400  1.000 65.34000  ? 687  ASP   A OD2 1 
ATOM   1136 N  N   . GLN   A 1 162 ? -31.12800 -1.15600 -1.89600  1.000 46.44000  ? 688  GLN   A N   1 
ATOM   1137 C  CA  . GLN   A 1 162 ? -30.15100 -0.50600 -1.03000  1.000 45.89000  ? 688  GLN   A CA  1 
ATOM   1138 C  C   . GLN   A 1 162 ? -30.83900 0.31500  0.05300   1.000 42.43000  ? 688  GLN   A C   1 
ATOM   1139 O  O   . GLN   A 1 162 ? -30.36600 0.36800  1.19400   1.000 45.18000  ? 688  GLN   A O   1 
ATOM   1140 C  CB  . GLN   A 1 162 ? -29.22100 0.37500  -1.86200  1.000 46.36000  ? 688  GLN   A CB  1 
ATOM   1141 C  CG  . GLN   A 1 162 ? -28.38200 -0.39000 -2.86900  1.000 44.30000  ? 688  GLN   A CG  1 
ATOM   1142 C  CD  . GLN   A 1 162 ? -27.23900 -1.14200 -2.22000  1.000 55.47000  ? 688  GLN   A CD  1 
ATOM   1143 O  OE1 . GLN   A 1 162 ? -26.54400 -0.61100 -1.35500  1.000 60.44000  ? 688  GLN   A OE1 1 
ATOM   1144 N  NE2 . GLN   A 1 162 ? -27.03800 -2.38700 -2.63700  1.000 54.97000  ? 688  GLN   A NE2 1 
ATOM   1145 N  N   . CYS   A 1 163 ? -31.95800 0.95900  -0.28600  1.000 41.25000  ? 689  CYS   A N   1 
ATOM   1146 C  CA  . CYS   A 1 163 ? -32.68900 1.74700  0.70100   1.000 35.16000  ? 689  CYS   A CA  1 
ATOM   1147 C  C   . CYS   A 1 163 ? -33.27100 0.86300  1.79500   1.000 40.81000  ? 689  CYS   A C   1 
ATOM   1148 O  O   . CYS   A 1 163 ? -33.18900 1.19900  2.98200   1.000 45.01000  ? 689  CYS   A O   1 
ATOM   1149 C  CB  . CYS   A 1 163 ? -33.79100 2.54800  0.01000   1.000 28.21000  ? 689  CYS   A CB  1 
ATOM   1150 S  SG  . CYS   A 1 163 ? -34.97800 3.32900  1.12500   1.000 40.23000  ? 689  CYS   A SG  1 
ATOM   1151 N  N   . LEU   A 1 164 ? -33.86200 -0.27300 1.41700   1.000 39.42000  ? 690  LEU   A N   1 
ATOM   1152 C  CA  . LEU   A 1 164 ? -34.41700 -1.18100 2.41500   1.000 38.77000  ? 690  LEU   A CA  1 
ATOM   1153 C  C   . LEU   A 1 164 ? -33.31800 -1.81600 3.25600   1.000 37.73000  ? 690  LEU   A C   1 
ATOM   1154 O  O   . LEU   A 1 164 ? -33.50700 -2.05900 4.45400   1.000 43.44000  ? 690  LEU   A O   1 
ATOM   1155 C  CB  . LEU   A 1 164 ? -35.25700 -2.25900 1.73200   1.000 47.74000  ? 690  LEU   A CB  1 
ATOM   1156 C  CG  . LEU   A 1 164 ? -36.04100 -3.18000 2.66700   1.000 40.14000  ? 690  LEU   A CG  1 
ATOM   1157 C  CD1 . LEU   A 1 164 ? -37.18800 -2.42400 3.31300   1.000 40.70000  ? 690  LEU   A CD1 1 
ATOM   1158 C  CD2 . LEU   A 1 164 ? -36.54900 -4.39100 1.91000   1.000 38.53000  ? 690  LEU   A CD2 1 
ATOM   1159 N  N   . MET   A 1 165 ? -32.16600 -2.09900 2.64400   1.000 43.69000  ? 691  MET   A N   1 
ATOM   1160 C  CA  . MET   A 1 165 ? -31.05600 -2.68600 3.38700   1.000 46.42000  ? 691  MET   A CA  1 
ATOM   1161 C  C   . MET   A 1 165 ? -30.54800 -1.73400 4.46300   1.000 49.10000  ? 691  MET   A C   1 
ATOM   1162 O  O   . MET   A 1 165 ? -30.23300 -2.15900 5.58000   1.000 54.02000  ? 691  MET   A O   1 
ATOM   1163 C  CB  . MET   A 1 165 ? -29.92800 -3.06300 2.42700   1.000 50.53000  ? 691  MET   A CB  1 
ATOM   1164 C  CG  . MET   A 1 165 ? -28.73500 -3.72000 3.09900   1.000 65.92000  ? 691  MET   A CG  1 
ATOM   1165 S  SD  . MET   A 1 165 ? -27.16100 -3.00500 2.58600   1.000 88.14000  ? 691  MET   A SD  1 
ATOM   1166 C  CE  . MET   A 1 165 ? -27.00300 -1.65800 3.75600   1.000 56.49000  ? 691  MET   A CE  1 
ATOM   1167 N  N   . ILE   A 1 166 ? -30.46200 -0.44200 4.14300   1.000 44.18000  ? 692  ILE   A N   1 
ATOM   1168 C  CA  . ILE   A 1 166 ? -30.02200 0.53700  5.13200   1.000 40.49000  ? 692  ILE   A CA  1 
ATOM   1169 C  C   . ILE   A 1 166 ? -31.08700 0.72800  6.20400   1.000 39.43000  ? 692  ILE   A C   1 
ATOM   1170 O  O   . ILE   A 1 166 ? -30.77300 0.88500  7.39000   1.000 49.78000  ? 692  ILE   A O   1 
ATOM   1171 C  CB  . ILE   A 1 166 ? -29.66200 1.86500  4.44000   1.000 41.13000  ? 692  ILE   A CB  1 
ATOM   1172 C  CG1 . ILE   A 1 166 ? -28.50500 1.65900  3.46100   1.000 42.04000  ? 692  ILE   A CG1 1 
ATOM   1173 C  CG2 . ILE   A 1 166 ? -29.30200 2.92600  5.46700   1.000 34.54000  ? 692  ILE   A CG2 1 
ATOM   1174 C  CD1 . ILE   A 1 166 ? -28.12300 2.90700  2.69400   1.000 44.98000  ? 692  ILE   A CD1 1 
ATOM   1175 N  N   . LEU   A 1 167 ? -32.36400 0.71000  5.80900   1.000 36.44000  ? 693  LEU   A N   1 
ATOM   1176 C  CA  . LEU   A 1 167 ? -33.44400 0.87300  6.77700   1.000 44.44000  ? 693  LEU   A CA  1 
ATOM   1177 C  C   . LEU   A 1 167 ? -33.48200 -0.27500 7.77700   1.000 42.83000  ? 693  LEU   A C   1 
ATOM   1178 O  O   . LEU   A 1 167 ? -33.95700 -0.09900 8.90500   1.000 44.32000  ? 693  LEU   A O   1 
ATOM   1179 C  CB  . LEU   A 1 167 ? -34.78600 0.98300  6.05300   1.000 41.06000  ? 693  LEU   A CB  1 
ATOM   1180 C  CG  . LEU   A 1 167 ? -35.15100 2.34100  5.45200   1.000 39.76000  ? 693  LEU   A CG  1 
ATOM   1181 C  CD1 . LEU   A 1 167 ? -36.39200 2.22200  4.58000   1.000 32.45000  ? 693  LEU   A CD1 1 
ATOM   1182 C  CD2 . LEU   A 1 167 ? -35.35900 3.37500  6.54600   1.000 34.05000  ? 693  LEU   A CD2 1 
ATOM   1183 N  N   . ASN   A 1 168 ? -32.99400 -1.45200 7.38500   1.000 38.19000  ? 694  ASN   A N   1 
ATOM   1184 C  CA  . ASN   A 1 168 ? -32.97200 -2.61600 8.25800   1.000 47.97000  ? 694  ASN   A CA  1 
ATOM   1185 C  C   . ASN   A 1 168 ? -31.62800 -2.83100 8.93900   1.000 46.41000  ? 694  ASN   A C   1 
ATOM   1186 O  O   . ASN   A 1 168 ? -31.51500 -3.73600 9.77300   1.000 54.02000  ? 694  ASN   A O   1 
ATOM   1187 C  CB  . ASN   A 1 168 ? -33.34500 -3.87800 7.46900   1.000 39.81000  ? 694  ASN   A CB  1 
ATOM   1188 C  CG  . ASN   A 1 168 ? -34.79100 -3.87300 7.01700   1.000 42.49000  ? 694  ASN   A CG  1 
ATOM   1189 O  OD1 . ASN   A 1 168 ? -35.62800 -3.17000 7.58400   1.000 49.61000  ? 694  ASN   A OD1 1 
ATOM   1190 N  ND2 . ASN   A 1 168 ? -35.09200 -4.65800 5.99000   1.000 51.57000  ? 694  ASN   A ND2 1 
ATOM   1191 N  N   . SER   A 1 169 ? -30.61700 -2.03400 8.60600   1.000 50.84000  ? 695  SER   A N   1 
ATOM   1192 C  CA  . SER   A 1 169 ? -29.31500 -2.19100 9.23400   1.000 48.76000  ? 695  SER   A CA  1 
ATOM   1193 C  C   . SER   A 1 169 ? -29.42200 -1.89800 10.72900  1.000 51.21000  ? 695  SER   A C   1 
ATOM   1194 O  O   . SER   A 1 169 ? -30.17700 -1.00600 11.13400  1.000 48.23000  ? 695  SER   A O   1 
ATOM   1195 C  CB  . SER   A 1 169 ? -28.29000 -1.25900 8.58700   1.000 47.75000  ? 695  SER   A CB  1 
ATOM   1196 O  OG  . SER   A 1 169 ? -27.75300 -1.83400 7.40800   1.000 45.84000  ? 695  SER   A OG  1 
ATOM   1197 N  N   . PRO   A 1 170 ? -28.70100 -2.63200 11.57400  1.000 48.38000  ? 696  PRO   A N   1 
ATOM   1198 C  CA  . PRO   A 1 170 ? -28.75400 -2.36200 13.01600  1.000 40.73000  ? 696  PRO   A CA  1 
ATOM   1199 C  C   . PRO   A 1 170 ? -28.22400 -0.97100 13.33300  1.000 48.23000  ? 696  PRO   A C   1 
ATOM   1200 O  O   . PRO   A 1 170 ? -27.18500 -0.54900 12.81800  1.000 51.06000  ? 696  PRO   A O   1 
ATOM   1201 C  CB  . PRO   A 1 170 ? -27.87100 -3.46200 13.61600  1.000 43.26000  ? 696  PRO   A CB  1 
ATOM   1202 C  CG  . PRO   A 1 170 ? -27.00400 -3.92200 12.48500  1.000 43.96000  ? 696  PRO   A CG  1 
ATOM   1203 C  CD  . PRO   A 1 170 ? -27.83400 -3.77800 11.25200  1.000 42.45000  ? 696  PRO   A CD  1 
ATOM   1204 N  N   . GLY   A 1 171 ? -28.95500 -0.25500 14.18700  1.000 45.51000  ? 697  GLY   A N   1 
ATOM   1205 C  CA  . GLY   A 1 171 ? -28.62400 1.11100  14.52700  1.000 41.87000  ? 697  GLY   A CA  1 
ATOM   1206 C  C   . GLY   A 1 171 ? -29.12800 2.15500  13.55600  1.000 52.69000  ? 697  GLY   A C   1 
ATOM   1207 O  O   . GLY   A 1 171 ? -28.96400 3.35300  13.82200  1.000 52.67000  ? 697  GLY   A O   1 
ATOM   1208 N  N   . ASN   A 1 172 ? -29.73900 1.74800  12.44200  1.000 53.98000  ? 698  ASN   A N   1 
ATOM   1209 C  CA  . ASN   A 1 172 ? -30.21600 2.67500  11.42200  1.000 42.16000  ? 698  ASN   A CA  1 
ATOM   1210 C  C   . ASN   A 1 172 ? -31.72200 2.58700  11.21100  1.000 45.23000  ? 698  ASN   A C   1 
ATOM   1211 O  O   . ASN   A 1 172 ? -32.22400 3.09400  10.20100  1.000 45.58000  ? 698  ASN   A O   1 
ATOM   1212 C  CB  . ASN   A 1 172 ? -29.49500 2.42300  10.09300  1.000 39.35000  ? 698  ASN   A CB  1 
ATOM   1213 C  CG  . ASN   A 1 172 ? -27.98400 2.47000  10.22500  1.000 43.77000  ? 698  ASN   A CG  1 
ATOM   1214 O  OD1 . ASN   A 1 172 ? -27.35000 3.46000  9.86200   1.000 48.27000  ? 698  ASN   A OD1 1 
ATOM   1215 N  ND2 . ASN   A 1 172 ? -27.39800 1.39400  10.73600  1.000 53.30000  ? 698  ASN   A ND2 1 
ATOM   1216 N  N   . GLN   A 1 173 ? -32.45600 1.96200  12.13200  1.000 44.28000  ? 699  GLN   A N   1 
ATOM   1217 C  CA  . GLN   A 1 173 ? -33.88800 1.71500  11.95700  1.000 42.06000  ? 699  GLN   A CA  1 
ATOM   1218 C  C   . GLN   A 1 173 ? -34.67400 2.94100  12.41100  1.000 37.98000  ? 699  GLN   A C   1 
ATOM   1219 O  O   . GLN   A 1 173 ? -35.22100 3.00300  13.51500  1.000 47.61000  ? 699  GLN   A O   1 
ATOM   1220 C  CB  . GLN   A 1 173 ? -34.31400 0.47100  12.72500  1.000 38.86000  ? 699  GLN   A CB  1 
ATOM   1221 C  CG  . GLN   A 1 173 ? -33.73200 -0.82700 12.19500  1.000 44.91000  ? 699  GLN   A CG  1 
ATOM   1222 C  CD  . GLN   A 1 173 ? -34.36900 -2.04400 12.83500  1.000 59.33000  ? 699  GLN   A CD  1 
ATOM   1223 O  OE1 . GLN   A 1 173 ? -33.67900 -2.92400 13.34800  1.000 58.76000  ? 699  GLN   A OE1 1 
ATOM   1224 N  NE2 . GLN   A 1 173 ? -35.69700 -2.09700 12.81200  1.000 64.29000  ? 699  GLN   A NE2 1 
ATOM   1225 N  N   . ILE   A 1 174 ? -34.74400 3.93800  11.52400  1.000 41.14000  ? 700  ILE   A N   1 
ATOM   1226 C  CA  . ILE   A 1 174 ? -35.51100 5.14300  11.82100  1.000 41.63000  ? 700  ILE   A CA  1 
ATOM   1227 C  C   . ILE   A 1 174 ? -37.01200 4.91300  11.75900  1.000 34.76000  ? 700  ILE   A C   1 
ATOM   1228 O  O   . ILE   A 1 174 ? -37.78000 5.79800  12.15200  1.000 47.40000  ? 700  ILE   A O   1 
ATOM   1229 C  CB  . ILE   A 1 174 ? -35.12800 6.29300  10.86800  1.000 43.31000  ? 700  ILE   A CB  1 
ATOM   1230 C  CG1 . ILE   A 1 174 ? -35.42900 5.91600  9.41600   1.000 43.78000  ? 700  ILE   A CG1 1 
ATOM   1231 C  CG2 . ILE   A 1 174 ? -33.66400 6.65900  11.03700  1.000 30.80000  ? 700  ILE   A CG2 1 
ATOM   1232 C  CD1 . ILE   A 1 174 ? -35.31100 7.07600  8.44900   1.000 37.28000  ? 700  ILE   A CD1 1 
ATOM   1233 N  N   . LEU   A 1 175 ? -37.45100 3.75000  11.28000  1.000 48.72000  ? 701  LEU   A N   1 
ATOM   1234 C  CA  . LEU   A 1 175 ? -38.86500 3.40900  11.21300  1.000 44.12000  ? 701  LEU   A CA  1 
ATOM   1235 C  C   . LEU   A 1 175 ? -39.28300 2.42700  12.30100  1.000 49.09000  ? 701  LEU   A C   1 
ATOM   1236 O  O   . LEU   A 1 175 ? -40.37800 1.86000  12.22200  1.000 40.49000  ? 701  LEU   A O   1 
ATOM   1237 C  CB  . LEU   A 1 175 ? -39.20500 2.83300  9.83700   1.000 41.97000  ? 701  LEU   A CB  1 
ATOM   1238 C  CG  . LEU   A 1 175 ? -38.94800 3.73200  8.62700   1.000 49.92000  ? 701  LEU   A CG  1 
ATOM   1239 C  CD1 . LEU   A 1 175 ? -39.28400 3.00000  7.33800   1.000 40.10000  ? 701  LEU   A CD1 1 
ATOM   1240 C  CD2 . LEU   A 1 175 ? -39.74500 5.02000  8.73900   1.000 35.53000  ? 701  LEU   A CD2 1 
ATOM   1241 N  N   . SER   A 1 176 ? -38.43900 2.21600  13.31500  1.000 49.17000  ? 702  SER   A N   1 
ATOM   1242 C  CA  . SER   A 1 176 ? -38.76100 1.25300  14.36200  1.000 53.37000  ? 702  SER   A CA  1 
ATOM   1243 C  C   . SER   A 1 176 ? -39.96500 1.69000  15.18600  1.000 51.01000  ? 702  SER   A C   1 
ATOM   1244 O  O   . SER   A 1 176 ? -40.67000 0.84300  15.74600  1.000 60.44000  ? 702  SER   A O   1 
ATOM   1245 C  CB  . SER   A 1 176 ? -37.54800 1.04000  15.26900  1.000 46.86000  ? 702  SER   A CB  1 
ATOM   1246 O  OG  . SER   A 1 176 ? -37.43500 2.08300  16.22100  1.000 50.72000  ? 702  SER   A OG  1 
ATOM   1247 N  N   . GLY   A 1 177 ? -40.21800 2.99400  15.27200  1.000 54.44000  ? 703  GLY   A N   1 
ATOM   1248 C  CA  . GLY   A 1 177 ? -41.33900 3.51200  16.02700  1.000 42.48000  ? 703  GLY   A CA  1 
ATOM   1249 C  C   . GLY   A 1 177 ? -42.68600 3.40700  15.35200  1.000 48.80000  ? 703  GLY   A C   1 
ATOM   1250 O  O   . GLY   A 1 177 ? -43.69300 3.82300  15.93100  1.000 54.21000  ? 703  GLY   A O   1 
ATOM   1251 N  N   . LEU   A 1 178 ? -42.73700 2.86600  14.14000  1.000 45.12000  ? 704  LEU   A N   1 
ATOM   1252 C  CA  . LEU   A 1 178 ? -43.98700 2.69600  13.41800  1.000 50.08000  ? 704  LEU   A CA  1 
ATOM   1253 C  C   . LEU   A 1 178 ? -44.59300 1.33300  13.72300  1.000 48.39000  ? 704  LEU   A C   1 
ATOM   1254 O  O   . LEU   A 1 178 ? -43.88200 0.35300  13.96000  1.000 50.25000  ? 704  LEU   A O   1 
ATOM   1255 C  CB  . LEU   A 1 178 ? -43.76900 2.83100  11.90900  1.000 49.91000  ? 704  LEU   A CB  1 
ATOM   1256 C  CG  . LEU   A 1 178 ? -43.66200 4.22700  11.29000  1.000 50.06000  ? 704  LEU   A CG  1 
ATOM   1257 C  CD1 . LEU   A 1 178 ? -42.31800 4.86500  11.60400  1.000 46.65000  ? 704  LEU   A CD1 1 
ATOM   1258 C  CD2 . LEU   A 1 178 ? -43.88100 4.15300  9.78600   1.000 43.93000  ? 704  LEU   A CD2 1 
ATOM   1259 N  N   . SER   A 1 179 ? -45.92200 1.27900  13.71700  1.000 54.19000  ? 705  SER   A N   1 
ATOM   1260 C  CA  . SER   A 1 179 ? -46.60200 -0.00100 13.80500  1.000 56.38000  ? 705  SER   A CA  1 
ATOM   1261 C  C   . SER   A 1 179 ? -46.35800 -0.80700 12.53300  1.000 53.83000  ? 705  SER   A C   1 
ATOM   1262 O  O   . SER   A 1 179 ? -45.94000 -0.27400 11.50100  1.000 60.20000  ? 705  SER   A O   1 
ATOM   1263 C  CB  . SER   A 1 179 ? -48.10200 0.19600  14.02500  1.000 50.24000  ? 705  SER   A CB  1 
ATOM   1264 O  OG  . SER   A 1 179 ? -48.74200 0.61000  12.83000  1.000 48.23000  ? 705  SER   A OG  1 
ATOM   1265 N  N   . ILE   A 1 180 ? -46.62000 -2.11300 12.61600  1.000 56.99000  ? 706  ILE   A N   1 
ATOM   1266 C  CA  . ILE   A 1 180 ? -46.44500 -2.96800 11.44500  1.000 54.81000  ? 706  ILE   A CA  1 
ATOM   1267 C  C   . ILE   A 1 180 ? -47.40100 -2.55400 10.33400  1.000 47.84000  ? 706  ILE   A C   1 
ATOM   1268 O  O   . ILE   A 1 180 ? -47.11200 -2.75100 9.14700   1.000 60.36000  ? 706  ILE   A O   1 
ATOM   1269 C  CB  . ILE   A 1 180 ? -46.61600 -4.45200 11.83300  1.000 52.87000  ? 706  ILE   A CB  1 
ATOM   1270 C  CG1 . ILE   A 1 180 ? -46.27900 -5.36400 10.65000  1.000 50.67000  ? 706  ILE   A CG1 1 
ATOM   1271 C  CG2 . ILE   A 1 180 ? -48.02200 -4.72000 12.34600  1.000 56.57000  ? 706  ILE   A CG2 1 
ATOM   1272 C  CD1 . ILE   A 1 180 ? -44.89600 -5.13700 10.07700  1.000 61.02000  ? 706  ILE   A CD1 1 
ATOM   1273 N  N   . GLU   A 1 181 ? -48.53900 -1.95700 10.69100  1.000 52.46000  ? 707  GLU   A N   1 
ATOM   1274 C  CA  . GLU   A 1 181 ? -49.44800 -1.42700 9.68100   1.000 54.48000  ? 707  GLU   A CA  1 
ATOM   1275 C  C   . GLU   A 1 181 ? -48.85200 -0.20000 9.00000   1.000 61.97000  ? 707  GLU   A C   1 
ATOM   1276 O  O   . GLU   A 1 181 ? -48.84100 -0.10400 7.76800   1.000 61.47000  ? 707  GLU   A O   1 
ATOM   1277 C  CB  . GLU   A 1 181 ? -50.79800 -1.09100 10.31400  1.000 64.82000  ? 707  GLU   A CB  1 
ATOM   1278 C  CG  . GLU   A 1 181 ? -51.40600 -2.22700 11.12200  1.000 73.32000  ? 707  GLU   A CG  1 
ATOM   1279 C  CD  . GLU   A 1 181 ? -51.25300 -2.02800 12.61900  1.000 79.15000  ? 707  GLU   A CD  1 
ATOM   1280 O  OE1 . GLU   A 1 181 ? -52.04600 -1.25900 13.20200  1.000 81.80000  ? 707  GLU   A OE1 1 
ATOM   1281 O  OE2 . GLU   A 1 181 ? -50.34200 -2.64100 13.21200  1.000 79.04000  ? 707  GLU   A OE2 1 
ATOM   1282 N  N   . GLU   A 1 182 ? -48.34900 0.75300  9.79100   1.000 60.89000  ? 708  GLU   A N   1 
ATOM   1283 C  CA  . GLU   A 1 182 ? -47.71800 1.93500  9.21400   1.000 51.64000  ? 708  GLU   A CA  1 
ATOM   1284 C  C   . GLU   A 1 182 ? -46.42300 1.58500  8.49300   1.000 52.10000  ? 708  GLU   A C   1 
ATOM   1285 O  O   . GLU   A 1 182 ? -46.08400 2.22000  7.48800   1.000 49.98000  ? 708  GLU   A O   1 
ATOM   1286 C  CB  . GLU   A 1 182 ? -47.43400 2.97200  10.30000  1.000 50.57000  ? 708  GLU   A CB  1 
ATOM   1287 C  CG  . GLU   A 1 182 ? -48.63400 3.36200  11.14200  1.000 50.16000  ? 708  GLU   A CG  1 
ATOM   1288 C  CD  . GLU   A 1 182 ? -48.23800 4.13100  12.38700  1.000 55.32000  ? 708  GLU   A CD  1 
ATOM   1289 O  OE1 . GLU   A 1 182 ? -48.81000 5.21500  12.62800  1.000 55.89000  ? 708  GLU   A OE1 1 
ATOM   1290 O  OE2 . GLU   A 1 182 ? -47.34900 3.65200  13.12400  1.000 53.08000  ? 708  GLU   A OE2 1 
ATOM   1291 N  N   . TYR   A 1 183 ? -45.69400 0.58300  8.98900   1.000 49.28000  ? 709  TYR   A N   1 
ATOM   1292 C  CA  . TYR   A 1 183 ? -44.38700 0.26200  8.42600   1.000 43.02000  ? 709  TYR   A CA  1 
ATOM   1293 C  C   . TYR   A 1 183 ? -44.49800 -0.21100 6.97900   1.000 50.73000  ? 709  TYR   A C   1 
ATOM   1294 O  O   . TYR   A 1 183 ? -43.65300 0.13300  6.14100   1.000 53.20000  ? 709  TYR   A O   1 
ATOM   1295 C  CB  . TYR   A 1 183 ? -43.69700 -0.80000 9.28400   1.000 42.84000  ? 709  TYR   A CB  1 
ATOM   1296 C  CG  . TYR   A 1 183 ? -42.38500 -1.30100 8.72200   1.000 48.47000  ? 709  TYR   A CG  1 
ATOM   1297 C  CD1 . TYR   A 1 183 ? -41.26300 -0.48300 8.68800   1.000 47.18000  ? 709  TYR   A CD1 1 
ATOM   1298 C  CD2 . TYR   A 1 183 ? -42.26700 -2.59600 8.23700   1.000 43.82000  ? 709  TYR   A CD2 1 
ATOM   1299 C  CE1 . TYR   A 1 183 ? -40.06200 -0.94000 8.18100   1.000 45.94000  ? 709  TYR   A CE1 1 
ATOM   1300 C  CE2 . TYR   A 1 183 ? -41.07000 -3.06300 7.72900   1.000 44.93000  ? 709  TYR   A CE2 1 
ATOM   1301 C  CZ  . TYR   A 1 183 ? -39.97100 -2.23100 7.70300   1.000 50.32000  ? 709  TYR   A CZ  1 
ATOM   1302 O  OH  . TYR   A 1 183 ? -38.77800 -2.69400 7.19600   1.000 59.24000  ? 709  TYR   A OH  1 
ATOM   1303 N  N   . LYS   A 1 184 ? -45.53000 -1.00600 6.66200   1.000 55.19000  ? 710  LYS   A N   1 
ATOM   1304 C  CA  . LYS   A 1 184 ? -45.66400 -1.52200 5.29800   1.000 54.92000  ? 710  LYS   A CA  1 
ATOM   1305 C  C   . LYS   A 1 184 ? -46.28400 -0.48900 4.36200   1.000 54.34000  ? 710  LYS   A C   1 
ATOM   1306 O  O   . LYS   A 1 184 ? -45.89800 -0.40000 3.19000   1.000 55.53000  ? 710  LYS   A O   1 
ATOM   1307 C  CB  . LYS   A 1 184 ? -46.50500 -2.80100 5.27700   1.000 62.17000  ? 710  LYS   A CB  1 
ATOM   1308 C  CG  . LYS   A 1 184 ? -46.09300 -3.91700 6.20200   1.000 69.58000  ? 710  LYS   A CG  1 
ATOM   1309 C  CD  . LYS   A 1 184 ? -46.90700 -5.13800 5.84400   1.000 69.34000  ? 710  LYS   A CD  1 
ATOM   1310 C  CE  . LYS   A 1 184 ? -48.15100 -5.23200 6.72700   1.000 65.58000  ? 710  LYS   A CE  1 
ATOM   1311 N  NZ  . LYS   A 1 184 ? -49.07000 -6.33900 6.32200   1.000 79.28000  ? 710  LYS   A NZ  1 
ATOM   1312 N  N   . THR   A 1 185 ? -47.25600 0.28600  4.85400   1.000 47.63000  ? 711  THR   A N   1 
ATOM   1313 C  CA  . THR   A 1 185 ? -47.76800 1.39600  4.05900   1.000 52.66000  ? 711  THR   A CA  1 
ATOM   1314 C  C   . THR   A 1 185 ? -46.63800 2.34200  3.66900   1.000 52.36000  ? 711  THR   A C   1 
ATOM   1315 O  O   . THR   A 1 185 ? -46.55400 2.78900  2.51800   1.000 54.09000  ? 711  THR   A O   1 
ATOM   1316 C  CB  . THR   A 1 185 ? -48.85800 2.14200  4.83200   1.000 58.66000  ? 711  THR   A CB  1 
ATOM   1317 O  OG1 . THR   A 1 185 ? -49.94700 1.25400  5.11200   1.000 57.14000  ? 711  THR   A OG1 1 
ATOM   1318 C  CG2 . THR   A 1 185 ? -49.37900 3.32500  4.02900   1.000 42.22000  ? 711  THR   A CG2 1 
ATOM   1319 N  N   . THR   A 1 186 ? -45.73500 2.62100  4.60900   1.000 48.41000  ? 712  THR   A N   1 
ATOM   1320 C  CA  . THR   A 1 186 ? -44.57800 3.45600  4.31000   1.000 39.13000  ? 712  THR   A CA  1 
ATOM   1321 C  C   . THR   A 1 186 ? -43.64000 2.77400  3.32000   1.000 45.20000  ? 712  THR   A C   1 
ATOM   1322 O  O   . THR   A 1 186 ? -43.14100 3.41700  2.38900   1.000 47.08000  ? 712  THR   A O   1 
ATOM   1323 C  CB  . THR   A 1 186 ? -43.83500 3.79900  5.60100   1.000 41.12000  ? 712  THR   A CB  1 
ATOM   1324 O  OG1 . THR   A 1 186 ? -44.74400 4.40400  6.52900   1.000 40.49000  ? 712  THR   A OG1 1 
ATOM   1325 C  CG2 . THR   A 1 186 ? -42.69300 4.76300  5.32100   1.000 42.67000  ? 712  THR   A CG2 1 
ATOM   1326 N  N   . LEU   A 1 187 ? -43.39400 1.47200  3.49800   1.000 48.67000  ? 713  LEU   A N   1 
ATOM   1327 C  CA  . LEU   A 1 187 ? -42.45600 0.77200  2.62400   1.000 39.09000  ? 713  LEU   A CA  1 
ATOM   1328 C  C   . LEU   A 1 187 ? -42.95400 0.73400  1.18400   1.000 37.78000  ? 713  LEU   A C   1 
ATOM   1329 O  O   . LEU   A 1 187 ? -42.16100 0.85800  0.24300   1.000 45.49000  ? 713  LEU   A O   1 
ATOM   1330 C  CB  . LEU   A 1 187 ? -42.21000 -0.64700 3.13700   1.000 44.56000  ? 713  LEU   A CB  1 
ATOM   1331 C  CG  . LEU   A 1 187 ? -41.12200 -0.83300 4.19500   1.000 58.21000  ? 713  LEU   A CG  1 
ATOM   1332 C  CD1 . LEU   A 1 187 ? -40.72700 -2.29900 4.28800   1.000 52.30000  ? 713  LEU   A CD1 1 
ATOM   1333 C  CD2 . LEU   A 1 187 ? -39.90900 0.03600  3.89300   1.000 54.39000  ? 713  LEU   A CD2 1 
ATOM   1334 N  N   . LYS   A 1 188 ? -44.26400 0.56300  0.99000   1.000 50.41000  ? 714  LYS   A N   1 
ATOM   1335 C  CA  . LYS   A 1 188 ? -44.79300 0.48300  -0.36800  1.000 59.61000  ? 714  LYS   A CA  1 
ATOM   1336 C  C   . LYS   A 1 188 ? -44.82700 1.85000  -1.04300  1.000 44.78000  ? 714  LYS   A C   1 
ATOM   1337 O  O   . LYS   A 1 188 ? -44.66300 1.93700  -2.26500  1.000 43.55000  ? 714  LYS   A O   1 
ATOM   1338 C  CB  . LYS   A 1 188 ? -46.18300 -0.16000 -0.35900  1.000 59.22000  ? 714  LYS   A CB  1 
ATOM   1339 C  CG  . LYS   A 1 188 ? -47.31400 0.73800  0.11500   1.000 62.91000  ? 714  LYS   A CG  1 
ATOM   1340 C  CD  . LYS   A 1 188 ? -48.65500 0.23300  -0.39300  1.000 65.57000  ? 714  LYS   A CD  1 
ATOM   1341 C  CE  . LYS   A 1 188 ? -48.65000 0.10900  -1.90900  1.000 65.09000  ? 714  LYS   A CE  1 
ATOM   1342 N  NZ  . LYS   A 1 188 ? -49.90700 -0.49500 -2.43100  1.000 81.27000  ? 714  LYS   A NZ  1 
ATOM   1343 N  N   . ILE   A 1 189 ? -45.02900 2.92400  -0.27400  1.000 46.56000  ? 715  ILE   A N   1 
ATOM   1344 C  CA  . ILE   A 1 189 ? -44.93800 4.26100  -0.85100  1.000 40.79000  ? 715  ILE   A CA  1 
ATOM   1345 C  C   . ILE   A 1 189 ? -43.49200 4.59000  -1.20100  1.000 35.95000  ? 715  ILE   A C   1 
ATOM   1346 O  O   . ILE   A 1 189 ? -43.21400 5.19600  -2.24300  1.000 39.77000  ? 715  ILE   A O   1 
ATOM   1347 C  CB  . ILE   A 1 189 ? -45.54200 5.30700  0.10500   1.000 51.87000  ? 715  ILE   A CB  1 
ATOM   1348 C  CG1 . ILE   A 1 189 ? -47.00300 4.97800  0.41700   1.000 39.88000  ? 715  ILE   A CG1 1 
ATOM   1349 C  CG2 . ILE   A 1 189 ? -45.45300 6.69800  -0.50000  1.000 48.20000  ? 715  ILE   A CG2 1 
ATOM   1350 C  CD1 . ILE   A 1 189 ? -47.59400 5.82900  1.52600   1.000 33.20000  ? 715  ILE   A CD1 1 
ATOM   1351 N  N   . ILE   A 1 190 ? -42.54800 4.19200  -0.34200  1.000 39.30000  ? 716  ILE   A N   1 
ATOM   1352 C  CA  . ILE   A 1 190 ? -41.13200 4.41100  -0.62900  1.000 41.18000  ? 716  ILE   A CA  1 
ATOM   1353 C  C   . ILE   A 1 190 ? -40.73800 3.71900  -1.92700  1.000 49.36000  ? 716  ILE   A C   1 
ATOM   1354 O  O   . ILE   A 1 190 ? -40.04000 4.29600  -2.77200  1.000 43.50000  ? 716  ILE   A O   1 
ATOM   1355 C  CB  . ILE   A 1 190 ? -40.26400 3.92900  0.54900   1.000 34.19000  ? 716  ILE   A CB  1 
ATOM   1356 C  CG1 . ILE   A 1 190 ? -40.38900 4.87700  1.74100   1.000 34.06000  ? 716  ILE   A CG1 1 
ATOM   1357 C  CG2 . ILE   A 1 190 ? -38.80900 3.80800  0.12800   1.000 34.03000  ? 716  ILE   A CG2 1 
ATOM   1358 C  CD1 . ILE   A 1 190 ? -39.67600 4.38900  2.98500   1.000 27.89000  ? 716  ILE   A CD1 1 
ATOM   1359 N  N   . LYS   A 1 191 ? -41.18500 2.47400  -2.11100  1.000 44.64000  ? 717  LYS   A N   1 
ATOM   1360 C  CA  . LYS   A 1 191 ? -40.81700 1.72000  -3.30500  1.000 41.74000  ? 717  LYS   A CA  1 
ATOM   1361 C  C   . LYS   A 1 191 ? -41.39800 2.35400  -4.56200  1.000 42.15000  ? 717  LYS   A C   1 
ATOM   1362 O  O   . LYS   A 1 191 ? -40.69700 2.49900  -5.57000  1.000 43.03000  ? 717  LYS   A O   1 
ATOM   1363 C  CB  . LYS   A 1 191 ? -41.27900 0.26900  -3.16900  1.000 42.21000  ? 717  LYS   A CB  1 
ATOM   1364 C  CG  . LYS   A 1 191 ? -40.91800 -0.61400 -4.35200  1.000 47.49000  ? 717  LYS   A CG  1 
ATOM   1365 C  CD  . LYS   A 1 191 ? -40.76100 -2.06300 -3.92200  1.000 48.86000  ? 717  LYS   A CD  1 
ATOM   1366 C  CE  . LYS   A 1 191 ? -40.92800 -3.01200 -5.09600  1.000 46.13000  ? 717  LYS   A CE  1 
ATOM   1367 N  NZ  . LYS   A 1 191 ? -40.54000 -4.40600 -4.74600  1.000 47.24000  ? 717  LYS   A NZ  1 
ATOM   1368 N  N   . GLN   A 1 192 ? -42.67400 2.74300  -4.52200  1.000 42.32000  ? 718  GLN   A N   1 
ATOM   1369 C  CA  . GLN   A 1 192 ? -43.29300 3.35600  -5.69200  1.000 39.38000  ? 718  GLN   A CA  1 
ATOM   1370 C  C   . GLN   A 1 192 ? -42.67500 4.71400  -6.00000  1.000 47.67000  ? 718  GLN   A C   1 
ATOM   1371 O  O   . GLN   A 1 192 ? -42.53200 5.08600  -7.17100  1.000 42.58000  ? 718  GLN   A O   1 
ATOM   1372 C  CB  . GLN   A 1 192 ? -44.80100 3.48100  -5.48000  1.000 38.34000  ? 718  GLN   A CB  1 
ATOM   1373 C  CG  . GLN   A 1 192 ? -45.52500 2.14200  -5.42700  1.000 64.38000  ? 718  GLN   A CG  1 
ATOM   1374 C  CD  . GLN   A 1 192 ? -46.91700 2.25600  -4.83900  1.000 75.60000  ? 718  GLN   A CD  1 
ATOM   1375 O  OE1 . GLN   A 1 192 ? -47.29400 3.29700  -4.30200  1.000 58.76000  ? 718  GLN   A OE1 1 
ATOM   1376 N  NE2 . GLN   A 1 192 ? -47.69300 1.18300  -4.94300  1.000 83.08000  ? 718  GLN   A NE2 1 
ATOM   1377 N  N   . ALA   A 1 193 ? -42.29300 5.46600  -4.96400  1.000 48.90000  ? 719  ALA   A N   1 
ATOM   1378 C  CA  . ALA   A 1 193 ? -41.67300 6.76800  -5.18600  1.000 36.25000  ? 719  ALA   A CA  1 
ATOM   1379 C  C   . ALA   A 1 193 ? -40.30100 6.62600  -5.83600  1.000 33.85000  ? 719  ALA   A C   1 
ATOM   1380 O  O   . ALA   A 1 193 ? -39.94000 7.41800  -6.71400  1.000 38.25000  ? 719  ALA   A O   1 
ATOM   1381 C  CB  . ALA   A 1 193 ? -41.56700 7.53300  -3.86800  1.000 34.28000  ? 719  ALA   A CB  1 
ATOM   1382 N  N   . ILE   A 1 194 ? -39.52400 5.62500  -5.41800  1.000 37.23000  ? 720  ILE   A N   1 
ATOM   1383 C  CA  . ILE   A 1 194 ? -38.20800 5.41200  -6.01300  1.000 35.18000  ? 720  ILE   A CA  1 
ATOM   1384 C  C   . ILE   A 1 194 ? -38.34300 4.90500  -7.44400  1.000 38.63000  ? 720  ILE   A C   1 
ATOM   1385 O  O   . ILE   A 1 194 ? -37.62100 5.34800  -8.34500  1.000 37.05000  ? 720  ILE   A O   1 
ATOM   1386 C  CB  . ILE   A 1 194 ? -37.37700 4.45100  -5.14300  1.000 29.31000  ? 720  ILE   A CB  1 
ATOM   1387 C  CG1 . ILE   A 1 194 ? -37.00600 5.12200  -3.81800  1.000 33.82000  ? 720  ILE   A CG1 1 
ATOM   1388 C  CG2 . ILE   A 1 194 ? -36.12500 3.99900  -5.88200  1.000 25.53000  ? 720  ILE   A CG2 1 
ATOM   1389 C  CD1 . ILE   A 1 194 ? -36.04600 4.31600  -2.96900  1.000 32.23000  ? 720  ILE   A CD1 1 
ATOM   1390 N  N   . LEU   A 1 195 ? -39.27300 3.97300  -7.67800  1.000 40.64000  ? 721  LEU   A N   1 
ATOM   1391 C  CA  . LEU   A 1 195 ? -39.49200 3.47000  -9.03100  1.000 50.07000  ? 721  LEU   A CA  1 
ATOM   1392 C  C   . LEU   A 1 195 ? -39.97300 4.57000  -9.96600  1.000 39.33000  ? 721  LEU   A C   1 
ATOM   1393 O  O   . LEU   A 1 195 ? -39.68600 4.53200  -11.16800 1.000 41.56000  ? 721  LEU   A O   1 
ATOM   1394 C  CB  . LEU   A 1 195 ? -40.50000 2.32000  -9.01100  1.000 51.33000  ? 721  LEU   A CB  1 
ATOM   1395 C  CG  . LEU   A 1 195 ? -40.07100 1.01300  -8.34300  1.000 45.14000  ? 721  LEU   A CG  1 
ATOM   1396 C  CD1 . LEU   A 1 195 ? -41.18000 -0.02300 -8.44200  1.000 37.72000  ? 721  LEU   A CD1 1 
ATOM   1397 C  CD2 . LEU   A 1 195 ? -38.78300 0.48600  -8.95500  1.000 36.62000  ? 721  LEU   A CD2 1 
ATOM   1398 N  N   . ALA   A 1 196 ? -40.70000 5.55600  -9.43600  1.000 41.58000  ? 722  ALA   A N   1 
ATOM   1399 C  CA  . ALA   A 1 196 ? -41.19600 6.65100  -10.26000 1.000 32.59000  ? 722  ALA   A CA  1 
ATOM   1400 C  C   . ALA   A 1 196 ? -40.07300 7.49900  -10.83900 1.000 43.38000  ? 722  ALA   A C   1 
ATOM   1401 O  O   . ALA   A 1 196 ? -40.28300 8.17500  -11.85300 1.000 43.39000  ? 722  ALA   A O   1 
ATOM   1402 C  CB  . ALA   A 1 196 ? -42.14200 7.53200  -9.44500  1.000 31.04000  ? 722  ALA   A CB  1 
ATOM   1403 N  N   . THR   A 1 197 ? -38.88800 7.48200  -10.22600 1.000 33.40000  ? 723  THR   A N   1 
ATOM   1404 C  CA  . THR   A 1 197 ? -37.76400 8.25500  -10.74000 1.000 41.39000  ? 723  THR   A CA  1 
ATOM   1405 C  C   . THR   A 1 197 ? -37.20000 7.68900  -12.03600 1.000 45.33000  ? 723  THR   A C   1 
ATOM   1406 O  O   . THR   A 1 197 ? -36.29500 8.30100  -12.61500 1.000 44.43000  ? 723  THR   A O   1 
ATOM   1407 C  CB  . THR   A 1 197 ? -36.65800 8.34900  -9.68700  1.000 39.92000  ? 723  THR   A CB  1 
ATOM   1408 O  OG1 . THR   A 1 197 ? -36.21500 7.03400  -9.33300  1.000 38.60000  ? 723  THR   A OG1 1 
ATOM   1409 C  CG2 . THR   A 1 197 ? -37.17200 9.06100  -8.44400  1.000 30.52000  ? 723  THR   A CG2 1 
ATOM   1410 N  N   . ASP   A 1 198 ? -37.69600 6.54300  -12.49800 1.000 47.73000  ? 724  ASP   A N   1 
ATOM   1411 C  CA  . ASP   A 1 198 ? -37.39000 6.06900  -13.84200 1.000 47.70000  ? 724  ASP   A CA  1 
ATOM   1412 C  C   . ASP   A 1 198 ? -38.15400 6.92900  -14.83900 1.000 49.29000  ? 724  ASP   A C   1 
ATOM   1413 O  O   . ASP   A 1 198 ? -39.38900 6.91700  -14.85900 1.000 48.19000  ? 724  ASP   A O   1 
ATOM   1414 C  CB  . ASP   A 1 198 ? -37.76300 4.59600  -13.98600 1.000 57.08000  ? 724  ASP   A CB  1 
ATOM   1415 C  CG  . ASP   A 1 198 ? -37.29400 3.99700  -15.30200 1.000 60.88000  ? 724  ASP   A CG  1 
ATOM   1416 O  OD1 . ASP   A 1 198 ? -36.63300 4.70800  -16.08900 1.000 54.73000  ? 724  ASP   A OD1 1 
ATOM   1417 O  OD2 . ASP   A 1 198 ? -37.58700 2.80900  -15.55200 1.000 55.41000  ? 724  ASP   A OD2 1 
ATOM   1418 N  N   . LEU   A 1 199 ? -37.42100 7.68600  -15.66200 1.000 47.73000  ? 725  LEU   A N   1 
ATOM   1419 C  CA  . LEU   A 1 199 ? -38.06900 8.57800  -16.61900 1.000 56.08000  ? 725  LEU   A CA  1 
ATOM   1420 C  C   . LEU   A 1 199 ? -38.96100 7.81300  -17.58600 1.000 42.91000  ? 725  LEU   A C   1 
ATOM   1421 O  O   . LEU   A 1 199 ? -39.92900 8.37500  -18.11200 1.000 49.98000  ? 725  LEU   A O   1 
ATOM   1422 C  CB  . LEU   A 1 199 ? -37.01700 9.38100  -17.38500 1.000 48.66000  ? 725  LEU   A CB  1 
ATOM   1423 C  CG  . LEU   A 1 199 ? -36.41400 10.56800 -16.63300 1.000 53.51000  ? 725  LEU   A CG  1 
ATOM   1424 C  CD1 . LEU   A 1 199 ? -35.25400 11.16500 -17.41300 1.000 61.09000  ? 725  LEU   A CD1 1 
ATOM   1425 C  CD2 . LEU   A 1 199 ? -37.47600 11.62000 -16.35200 1.000 42.16000  ? 725  LEU   A CD2 1 
ATOM   1426 N  N   . ALA   A 1 200 ? -38.65500 6.53700  -17.83100 1.000 53.06000  ? 726  ALA   A N   1 
ATOM   1427 C  CA  . ALA   A 1 200 ? -39.53700 5.70400  -18.64200 1.000 54.70000  ? 726  ALA   A CA  1 
ATOM   1428 C  C   . ALA   A 1 200 ? -40.92900 5.63300  -18.02900 1.000 53.51000  ? 726  ALA   A C   1 
ATOM   1429 O  O   . ALA   A 1 200 ? -41.93600 5.81600  -18.72300 1.000 55.61000  ? 726  ALA   A O   1 
ATOM   1430 C  CB  . ALA   A 1 200 ? -38.94100 4.30500  -18.79800 1.000 48.06000  ? 726  ALA   A CB  1 
ATOM   1431 N  N   . LEU   A 1 201 ? -41.00500 5.38000  -16.72000 1.000 49.86000  ? 727  LEU   A N   1 
ATOM   1432 C  CA  . LEU   A 1 201 ? -42.30000 5.34700  -16.04800 1.000 49.06000  ? 727  LEU   A CA  1 
ATOM   1433 C  C   . LEU   A 1 201 ? -42.96600 6.71600  -16.06500 1.000 48.97000  ? 727  LEU   A C   1 
ATOM   1434 O  O   . LEU   A 1 201 ? -44.19200 6.81400  -16.19900 1.000 54.41000  ? 727  LEU   A O   1 
ATOM   1435 C  CB  . LEU   A 1 201 ? -42.13700 4.85000  -14.61200 1.000 47.65000  ? 727  LEU   A CB  1 
ATOM   1436 C  CG  . LEU   A 1 201 ? -41.74700 3.38300  -14.43200 1.000 57.59000  ? 727  LEU   A CG  1 
ATOM   1437 C  CD1 . LEU   A 1 201 ? -41.90300 2.96400  -12.97800 1.000 53.75000  ? 727  LEU   A CD1 1 
ATOM   1438 C  CD2 . LEU   A 1 201 ? -42.57500 2.49200  -15.34400 1.000 65.71000  ? 727  LEU   A CD2 1 
ATOM   1439 N  N   . TYR   A 1 202 ? -42.17800 7.78500  -15.92700 1.000 57.35000  ? 728  TYR   A N   1 
ATOM   1440 C  CA  . TYR   A 1 202 ? -42.74400 9.12800  -15.99200 1.000 52.18000  ? 728  TYR   A CA  1 
ATOM   1441 C  C   . TYR   A 1 202 ? -43.34000 9.40500  -17.36600 1.000 52.07000  ? 728  TYR   A C   1 
ATOM   1442 O  O   . TYR   A 1 202 ? -44.41500 10.00500 -17.47500 1.000 51.68000  ? 728  TYR   A O   1 
ATOM   1443 C  CB  . TYR   A 1 202 ? -41.67700 10.17000 -15.65200 1.000 49.60000  ? 728  TYR   A CB  1 
ATOM   1444 C  CG  . TYR   A 1 202 ? -42.02000 11.57000 -16.11400 1.000 44.07000  ? 728  TYR   A CG  1 
ATOM   1445 C  CD1 . TYR   A 1 202 ? -42.96700 12.33100 -15.44200 1.000 39.69000  ? 728  TYR   A CD1 1 
ATOM   1446 C  CD2 . TYR   A 1 202 ? -41.39900 12.12800 -17.22400 1.000 45.65000  ? 728  TYR   A CD2 1 
ATOM   1447 C  CE1 . TYR   A 1 202 ? -43.28600 13.61000 -15.86100 1.000 51.09000  ? 728  TYR   A CE1 1 
ATOM   1448 C  CE2 . TYR   A 1 202 ? -41.71100 13.40500 -17.65200 1.000 41.53000  ? 728  TYR   A CE2 1 
ATOM   1449 C  CZ  . TYR   A 1 202 ? -42.65500 14.14100 -16.96600 1.000 46.35000  ? 728  TYR   A CZ  1 
ATOM   1450 O  OH  . TYR   A 1 202 ? -42.96900 15.41300 -17.38800 1.000 62.50000  ? 728  TYR   A OH  1 
ATOM   1451 N  N   . ILE   A 1 203 ? -42.66000 8.96400  -18.42600 1.000 49.64000  ? 729  ILE   A N   1 
ATOM   1452 C  CA  . ILE   A 1 203 ? -43.14100 9.21600  -19.78200 1.000 53.34000  ? 729  ILE   A CA  1 
ATOM   1453 C  C   . ILE   A 1 203 ? -44.46100 8.49300  -20.02700 1.000 61.32000  ? 729  ILE   A C   1 
ATOM   1454 O  O   . ILE   A 1 203 ? -45.37800 9.04000  -20.65200 1.000 65.25000  ? 729  ILE   A O   1 
ATOM   1455 C  CB  . ILE   A 1 203 ? -42.06600 8.81000  -20.80800 1.000 54.87000  ? 729  ILE   A CB  1 
ATOM   1456 C  CG1 . ILE   A 1 203 ? -40.94000 9.84600  -20.83500 1.000 46.89000  ? 729  ILE   A CG1 1 
ATOM   1457 C  CG2 . ILE   A 1 203 ? -42.67100 8.64200  -22.19400 1.000 54.51000  ? 729  ILE   A CG2 1 
ATOM   1458 C  CD1 . ILE   A 1 203 ? -39.72800 9.41400  -21.63000 1.000 52.34000  ? 729  ILE   A CD1 1 
ATOM   1459 N  N   . LYS   A 1 204 ? -44.58700 7.26300  -19.52500 1.000 66.44000  ? 730  LYS   A N   1 
ATOM   1460 C  CA  . LYS   A 1 204 ? -45.79200 6.47500  -19.75700 1.000 52.68000  ? 730  LYS   A CA  1 
ATOM   1461 C  C   . LYS   A 1 204 ? -46.97000 6.91400  -18.89800 1.000 52.07000  ? 730  LYS   A C   1 
ATOM   1462 O  O   . LYS   A 1 204 ? -48.11500 6.59100  -19.23500 1.000 80.66000  ? 730  LYS   A O   1 
ATOM   1463 C  CB  . LYS   A 1 204 ? -45.51500 4.99100  -19.50800 1.000 61.44000  ? 730  LYS   A CB  1 
ATOM   1464 C  CG  . LYS   A 1 204 ? -44.27300 4.45100  -20.19800 1.000 60.86000  ? 730  LYS   A CG  1 
ATOM   1465 C  CD  . LYS   A 1 204 ? -44.21600 2.92700  -20.14700 1.000 72.46000  ? 730  LYS   A CD  1 
ATOM   1466 C  CE  . LYS   A 1 204 ? -44.95400 2.36900  -18.93600 1.000 74.40000  ? 730  LYS   A CE  1 
ATOM   1467 N  NZ  . LYS   A 1 204 ? -44.49700 0.99800  -18.58100 1.000 81.47000  ? 730  LYS   A NZ  1 
ATOM   1468 N  N   . ARG   A 1 205 ? -46.72600 7.63400  -17.80300 1.000 58.74000  ? 731  ARG   A N   1 
ATOM   1469 C  CA  . ARG   A 1 205 ? -47.79000 8.03000  -16.89100 1.000 52.68000  ? 731  ARG   A CA  1 
ATOM   1470 C  C   . ARG   A 1 205 ? -48.07500 9.52500  -16.89000 1.000 60.70000  ? 731  ARG   A C   1 
ATOM   1471 O  O   . ARG   A 1 205 ? -49.11400 9.93500  -16.35900 1.000 59.43000  ? 731  ARG   A O   1 
ATOM   1472 C  CB  . ARG   A 1 205 ? -47.45900 7.58100  -15.46000 1.000 61.30000  ? 731  ARG   A CB  1 
ATOM   1473 C  CG  . ARG   A 1 205 ? -47.21500 6.08800  -15.31400 1.000 62.04000  ? 731  ARG   A CG  1 
ATOM   1474 C  CD  . ARG   A 1 205 ? -47.10400 5.69000  -13.85100 1.000 67.81000  ? 731  ARG   A CD  1 
ATOM   1475 N  NE  . ARG   A 1 205 ? -48.37500 5.84400  -13.14800 1.000 77.96000  ? 731  ARG   A NE  1 
ATOM   1476 C  CZ  . ARG   A 1 205 ? -48.49600 5.90700  -11.82600 1.000 82.57000  ? 731  ARG   A CZ  1 
ATOM   1477 N  NH1 . ARG   A 1 205 ? -47.41900 5.83100  -11.05500 1.000 71.43000  ? 731  ARG   A NH1 1 
ATOM   1478 N  NH2 . ARG   A 1 205 ? -49.69300 6.04700  -11.27400 1.000 71.03000  ? 731  ARG   A NH2 1 
ATOM   1479 N  N   . ARG   A 1 206 ? -47.19300 10.34800 -17.46300 1.000 65.61000  ? 732  ARG   A N   1 
ATOM   1480 C  CA  . ARG   A 1 206 ? -47.42300 11.79000 -17.45400 1.000 71.92000  ? 732  ARG   A CA  1 
ATOM   1481 C  C   . ARG   A 1 206 ? -48.59400 12.18200 -18.34500 1.000 73.17000  ? 732  ARG   A C   1 
ATOM   1482 O  O   . ARG   A 1 206 ? -49.25800 13.19000 -18.08000 1.000 68.47000  ? 732  ARG   A O   1 
ATOM   1483 C  CB  . ARG   A 1 206 ? -46.16200 12.53500 -17.89000 1.000 65.87000  ? 732  ARG   A CB  1 
ATOM   1484 C  CG  . ARG   A 1 206 ? -45.76800 12.29500 -19.33800 1.000 56.67000  ? 732  ARG   A CG  1 
ATOM   1485 C  CD  . ARG   A 1 206 ? -44.67600 13.25100 -19.77500 1.000 63.89000  ? 732  ARG   A CD  1 
ATOM   1486 N  NE  . ARG   A 1 206 ? -44.36000 13.10400 -21.19200 1.000 60.71000  ? 732  ARG   A NE  1 
ATOM   1487 C  CZ  . ARG   A 1 206 ? -43.47200 13.85200 -21.83800 1.000 69.89000  ? 732  ARG   A CZ  1 
ATOM   1488 N  NH1 . ARG   A 1 206 ? -42.80800 14.80100 -21.19100 1.000 62.84000  ? 732  ARG   A NH1 1 
ATOM   1489 N  NH2 . ARG   A 1 206 ? -43.24600 13.65200 -23.12900 1.000 68.65000  ? 732  ARG   A NH2 1 
ATOM   1490 N  N   . GLY   A 1 207 ? -48.85600 11.40900 -19.40300 1.000 71.88000  ? 733  GLY   A N   1 
ATOM   1491 C  CA  . GLY   A 1 207 ? -49.99000 11.70900 -20.26100 1.000 71.55000  ? 733  GLY   A CA  1 
ATOM   1492 C  C   . GLY   A 1 207 ? -51.30600 11.67700 -19.51000 1.000 76.76000  ? 733  GLY   A C   1 
ATOM   1493 O  O   . GLY   A 1 207 ? -52.15300 12.55800 -19.67900 1.000 80.19000  ? 733  GLY   A O   1 
ATOM   1494 N  N   . GLU   A 1 208 ? -51.49400 10.66300 -18.66400 1.000 74.60000  ? 734  GLU   A N   1 
ATOM   1495 C  CA  . GLU   A 1 208 ? -52.67600 10.63400 -17.81300 1.000 73.44000  ? 734  GLU   A CA  1 
ATOM   1496 C  C   . GLU   A 1 208 ? -52.69300 11.82900 -16.86700 1.000 75.21000  ? 734  GLU   A C   1 
ATOM   1497 O  O   . GLU   A 1 208 ? -53.71800 12.50500 -16.73200 1.000 71.04000  ? 734  GLU   A O   1 
ATOM   1498 C  CB  . GLU   A 1 208 ? -52.72900 9.31800  -17.03600 1.000 76.07000  ? 734  GLU   A CB  1 
ATOM   1499 C  CG  . GLU   A 1 208 ? -53.88900 9.20900  -16.06300 1.000 77.91000  ? 734  GLU   A CG  1 
ATOM   1500 C  CD  . GLU   A 1 208 ? -53.81000 7.97100  -15.18800 1.000 80.35000  ? 734  GLU   A CD  1 
ATOM   1501 O  OE1 . GLU   A 1 208 ? -52.96400 7.09300  -15.46300 1.000 82.98000  ? 734  GLU   A OE1 1 
ATOM   1502 O  OE2 . GLU   A 1 208 ? -54.59200 7.87900  -14.21900 1.000 75.38000  ? 734  GLU   A OE2 1 
ATOM   1503 N  N   . PHE   A 1 209 ? -51.55500 12.12300 -16.23000 1.000 82.05000  ? 735  PHE   A N   1 
ATOM   1504 C  CA  . PHE   A 1 209 ? -51.49400 13.21700 -15.26200 1.000 75.25000  ? 735  PHE   A CA  1 
ATOM   1505 C  C   . PHE   A 1 209 ? -51.91700 14.54300 -15.88600 1.000 77.51000  ? 735  PHE   A C   1 
ATOM   1506 O  O   . PHE   A 1 209 ? -52.66600 15.31400 -15.27400 1.000 72.46000  ? 735  PHE   A O   1 
ATOM   1507 C  CB  . PHE   A 1 209 ? -50.08300 13.32400 -14.67800 1.000 67.86000  ? 735  PHE   A CB  1 
ATOM   1508 C  CG  . PHE   A 1 209 ? -49.95200 14.35300 -13.59000 1.000 63.66000  ? 735  PHE   A CG  1 
ATOM   1509 C  CD1 . PHE   A 1 209 ? -50.80400 14.33600 -12.49600 1.000 52.88000  ? 735  PHE   A CD1 1 
ATOM   1510 C  CD2 . PHE   A 1 209 ? -48.97700 15.33400 -13.65700 1.000 62.40000  ? 735  PHE   A CD2 1 
ATOM   1511 C  CE1 . PHE   A 1 209 ? -50.68600 15.28000 -11.49300 1.000 58.35000  ? 735  PHE   A CE1 1 
ATOM   1512 C  CE2 . PHE   A 1 209 ? -48.85400 16.27900 -12.65700 1.000 56.03000  ? 735  PHE   A CE2 1 
ATOM   1513 C  CZ  . PHE   A 1 209 ? -49.71000 16.25200 -11.57400 1.000 55.99000  ? 735  PHE   A CZ  1 
ATOM   1514 N  N   . PHE   A 1 210 ? -51.45400 14.82300 -17.10700 1.000 80.68000  ? 736  PHE   A N   1 
ATOM   1515 C  CA  . PHE   A 1 210 ? -51.81100 16.07800 -17.76400 1.000 80.65000  ? 736  PHE   A CA  1 
ATOM   1516 C  C   . PHE   A 1 210 ? -53.27000 16.08200 -18.20300 1.000 91.43000  ? 736  PHE   A C   1 
ATOM   1517 O  O   . PHE   A 1 210 ? -53.96400 17.09500 -18.05600 1.000 89.02000  ? 736  PHE   A O   1 
ATOM   1518 C  CB  . PHE   A 1 210 ? -50.90400 16.32700 -18.96900 1.000 74.71000  ? 736  PHE   A CB  1 
ATOM   1519 C  CG  . PHE   A 1 210 ? -49.44600 16.40400 -18.63000 1.000 76.76000  ? 736  PHE   A CG  1 
ATOM   1520 C  CD1 . PHE   A 1 210 ? -49.02700 16.92500 -17.41700 1.000 71.13000  ? 736  PHE   A CD1 1 
ATOM   1521 C  CD2 . PHE   A 1 210 ? -48.49100 15.95400 -19.52800 1.000 66.03000  ? 736  PHE   A CD2 1 
ATOM   1522 C  CE1 . PHE   A 1 210 ? -47.68600 16.99500 -17.10600 1.000 62.36000  ? 736  PHE   A CE1 1 
ATOM   1523 C  CE2 . PHE   A 1 210 ? -47.14800 16.02100 -19.22200 1.000 63.50000  ? 736  PHE   A CE2 1 
ATOM   1524 C  CZ  . PHE   A 1 210 ? -46.74500 16.54100 -18.00900 1.000 68.10000  ? 736  PHE   A CZ  1 
ATOM   1525 N  N   . GLU   A 1 211 ? -53.75400 14.96100 -18.74900 1.000 93.61000  ? 737  GLU   A N   1 
ATOM   1526 C  CA  . GLU   A 1 211 ? -55.10200 14.91300 -19.30600 1.000 98.62000  ? 737  GLU   A CA  1 
ATOM   1527 C  C   . GLU   A 1 211 ? -56.18900 15.10200 -18.25400 1.000 94.34000  ? 737  GLU   A C   1 
ATOM   1528 O  O   . GLU   A 1 211 ? -57.31300 15.46200 -18.61800 1.000 99.11000  ? 737  GLU   A O   1 
ATOM   1529 C  CB  . GLU   A 1 211 ? -55.33000 13.59100 -20.04300 1.000 98.77000  ? 737  GLU   A CB  1 
ATOM   1530 C  CG  . GLU   A 1 211 ? -56.46600 13.61200 -21.06200 1.000 108.17000 ? 737  GLU   A CG  1 
ATOM   1531 C  CD  . GLU   A 1 211 ? -57.38300 12.41500 -20.93700 1.000 110.79000 ? 737  GLU   A CD  1 
ATOM   1532 O  OE1 . GLU   A 1 211 ? -58.43300 12.40300 -21.60900 1.000 107.86000 ? 737  GLU   A OE1 1 
ATOM   1533 O  OE2 . GLU   A 1 211 ? -57.06000 11.49400 -20.15400 1.000 113.99000 ? 737  GLU   A OE2 1 
ATOM   1534 N  N   . LEU   A 1 212 ? -55.89700 14.85700 -16.96800 1.000 83.33000  ? 738  LEU   A N   1 
ATOM   1535 C  CA  . LEU   A 1 212 ? -56.87600 15.15700 -15.92400 1.000 90.65000  ? 738  LEU   A CA  1 
ATOM   1536 C  C   . LEU   A 1 212 ? -56.71800 16.57800 -15.40000 1.000 97.31000  ? 738  LEU   A C   1 
ATOM   1537 O  O   . LEU   A 1 212 ? -57.69100 17.16600 -14.91900 1.000 97.63000  ? 738  LEU   A O   1 
ATOM   1538 C  CB  . LEU   A 1 212 ? -56.78400 14.12700 -14.77900 1.000 93.56000  ? 738  LEU   A CB  1 
ATOM   1539 C  CG  . LEU   A 1 212 ? -57.34000 12.76000 -15.19800 1.000 101.57000 ? 738  LEU   A CG  1 
ATOM   1540 C  CD1 . LEU   A 1 212 ? -56.26000 11.68200 -15.26300 1.000 98.48000  ? 738  LEU   A CD1 1 
ATOM   1541 C  CD2 . LEU   A 1 212 ? -58.55600 12.29400 -14.35700 1.000 102.79000 ? 738  LEU   A CD2 1 
ATOM   1542 N  N   . ILE   A 1 213 ? -55.51200 17.14100 -15.48900 1.000 104.05000 ? 739  ILE   A N   1 
ATOM   1543 C  CA  . ILE   A 1 213 ? -55.33200 18.56400 -15.21400 1.000 101.68000 ? 739  ILE   A CA  1 
ATOM   1544 C  C   . ILE   A 1 213 ? -56.11900 19.40200 -16.21300 1.000 100.41000 ? 739  ILE   A C   1 
ATOM   1545 O  O   . ILE   A 1 213 ? -56.73900 20.41400 -15.85500 1.000 100.21000 ? 739  ILE   A O   1 
ATOM   1546 C  CB  . ILE   A 1 213 ? -53.83200 18.91500 -15.23100 1.000 99.74000  ? 739  ILE   A CB  1 
ATOM   1547 C  CG1 . ILE   A 1 213 ? -53.18500 18.58200 -13.88200 1.000 92.11000  ? 739  ILE   A CG1 1 
ATOM   1548 C  CG2 . ILE   A 1 213 ? -53.60000 20.37000 -15.58400 1.000 94.97000  ? 739  ILE   A CG2 1 
ATOM   1549 C  CD1 . ILE   A 1 213 ? -53.53400 19.56400 -12.78400 1.000 82.70000  ? 739  ILE   A CD1 1 
ATOM   1550 N  N   . ARG   A 1 214 ? -56.11800 18.98600 -17.48200 1.000 102.75000 ? 740  ARG   A N   1 
ATOM   1551 C  CA  . ARG   A 1 214 ? -56.78300 19.76000 -18.52200 1.000 106.18000 ? 740  ARG   A CA  1 
ATOM   1552 C  C   . ARG   A 1 214 ? -58.30100 19.76600 -18.37200 1.000 113.92000 ? 740  ARG   A C   1 
ATOM   1553 O  O   . ARG   A 1 214 ? -58.96600 20.59300 -19.00400 1.000 120.00000 ? 740  ARG   A O   1 
ATOM   1554 C  CB  . ARG   A 1 214 ? -56.39600 19.23200 -19.91100 1.000 103.72000 ? 740  ARG   A CB  1 
ATOM   1555 C  CG  . ARG   A 1 214 ? -57.11700 17.96100 -20.33600 1.000 107.54000 ? 740  ARG   A CG  1 
ATOM   1556 C  CD  . ARG   A 1 214 ? -56.70700 17.49900 -21.73400 1.000 107.31000 ? 740  ARG   A CD  1 
ATOM   1557 N  NE  . ARG   A 1 214 ? -55.36100 16.93400 -21.76400 1.000 108.58000 ? 740  ARG   A NE  1 
ATOM   1558 C  CZ  . ARG   A 1 214 ? -54.91600 16.10400 -22.70200 1.000 108.15000 ? 740  ARG   A CZ  1 
ATOM   1559 N  NH1 . ARG   A 1 214 ? -55.71500 15.72800 -23.69200 1.000 106.75000 ? 740  ARG   A NH1 1 
ATOM   1560 N  NH2 . ARG   A 1 214 ? -53.67500 15.63900 -22.64600 1.000 103.93000 ? 740  ARG   A NH2 1 
ATOM   1561 N  N   . LYS   A 1 215 ? -58.86600 18.88300 -17.54900 1.000 112.51000 ? 741  LYS   A N   1 
ATOM   1562 C  CA  . LYS   A 1 215 ? -60.31300 18.79600 -17.38500 1.000 109.40000 ? 741  LYS   A CA  1 
ATOM   1563 C  C   . LYS   A 1 215 ? -60.77300 19.18900 -15.99000 1.000 108.71000 ? 741  LYS   A C   1 
ATOM   1564 O  O   . LYS   A 1 215 ? -61.96400 19.05500 -15.68000 1.000 106.06000 ? 741  LYS   A O   1 
ATOM   1565 C  CB  . LYS   A 1 215 ? -60.80200 17.38400 -17.71100 1.000 102.33000 ? 741  LYS   A CB  1 
ATOM   1566 C  CG  . LYS   A 1 215 ? -60.24700 16.84200 -19.00700 1.000 100.01000 ? 741  LYS   A CG  1 
ATOM   1567 C  CD  . LYS   A 1 215 ? -60.95500 15.57300 -19.43500 1.000 100.76000 ? 741  LYS   A CD  1 
ATOM   1568 C  CE  . LYS   A 1 215 ? -60.00000 14.67300 -20.18600 1.000 97.17000  ? 741  LYS   A CE  1 
ATOM   1569 N  NZ  . LYS   A 1 215 ? -60.64800 13.43700 -20.70400 1.000 95.16000  ? 741  LYS   A NZ  1 
ATOM   1570 N  N   . ASN   A 1 216 ? -59.86000 19.66000 -15.14100 1.000 113.29000 ? 742  ASN   A N   1 
ATOM   1571 C  CA  . ASN   A 1 216 ? -60.15600 20.02200 -13.75900 1.000 111.66000 ? 742  ASN   A CA  1 
ATOM   1572 C  C   . ASN   A 1 216 ? -60.79500 18.86700 -12.98600 1.000 109.71000 ? 742  ASN   A C   1 
ATOM   1573 O  O   . ASN   A 1 216 ? -61.43100 19.06800 -11.95100 1.000 105.65000 ? 742  ASN   A O   1 
ATOM   1574 C  CB  . ASN   A 1 216 ? -61.02800 21.28100 -13.70700 1.000 111.55000 ? 742  ASN   A CB  1 
ATOM   1575 C  CG  . ASN   A 1 216 ? -60.26600 22.52800 -14.14700 1.000 111.72000 ? 742  ASN   A CG  1 
ATOM   1576 O  OD1 . ASN   A 1 216 ? -59.97000 22.70600 -15.33100 1.000 118.58000 ? 742  ASN   A OD1 1 
ATOM   1577 N  ND2 . ASN   A 1 216 ? -59.93200 23.38800 -13.19000 1.000 111.07000 ? 742  ASN   A ND2 1 
ATOM   1578 N  N   . GLN   A 1 217 ? -60.61100 17.65200 -13.48200 1.000 110.24000 ? 743  GLN   A N   1 
ATOM   1579 C  CA  . GLN   A 1 217 ? -61.04400 16.42200 -12.83700 1.000 110.00000 ? 743  GLN   A CA  1 
ATOM   1580 C  C   . GLN   A 1 217 ? -60.11100 15.98500 -11.71600 1.000 111.13000 ? 743  GLN   A C   1 
ATOM   1581 O  O   . GLN   A 1 217 ? -60.40300 14.99900 -11.03300 1.000 105.18000 ? 743  GLN   A O   1 
ATOM   1582 C  CB  . GLN   A 1 217 ? -61.13400 15.30700 -13.86800 1.000 103.76000 ? 743  GLN   A CB  1 
ATOM   1583 C  CG  . GLN   A 1 217 ? -62.50200 15.07100 -14.48300 1.000 105.84000 ? 743  GLN   A CG  1 
ATOM   1584 C  CD  . GLN   A 1 217 ? -62.38100 14.44300 -15.85700 1.000 98.92000  ? 743  GLN   A CD  1 
ATOM   1585 O  OE1 . GLN   A 1 217 ? -61.39600 13.76500 -16.13400 1.000 94.83000  ? 743  GLN   A OE1 1 
ATOM   1586 N  NE2 . GLN   A 1 217 ? -63.37500 14.65100 -16.71500 1.000 98.43000  ? 743  GLN   A NE2 1 
ATOM   1587 N  N   . PHE   A 1 218 ? -59.00700 16.69400 -11.51300 1.000 112.80000 ? 744  PHE   A N   1 
ATOM   1588 C  CA  . PHE   A 1 218 ? -57.94800 16.23200 -10.62500 1.000 104.52000 ? 744  PHE   A CA  1 
ATOM   1589 C  C   . PHE   A 1 218 ? -58.42400 16.19400 -9.17600  1.000 99.40000  ? 744  PHE   A C   1 
ATOM   1590 O  O   . PHE   A 1 218 ? -58.81500 17.22400 -8.61700  1.000 96.14000  ? 744  PHE   A O   1 
ATOM   1591 C  CB  . PHE   A 1 218 ? -56.73200 17.14400 -10.77100 1.000 107.76000 ? 744  PHE   A CB  1 
ATOM   1592 C  CG  . PHE   A 1 218 ? -55.48300 16.58400 -10.16600 1.000 100.43000 ? 744  PHE   A CG  1 
ATOM   1593 C  CD1 . PHE   A 1 218 ? -55.03400 15.32500 -10.52900 1.000 88.40000  ? 744  PHE   A CD1 1 
ATOM   1594 C  CD2 . PHE   A 1 218 ? -54.75700 17.31000 -9.23900  1.000 92.68000  ? 744  PHE   A CD2 1 
ATOM   1595 C  CE1 . PHE   A 1 218 ? -53.89000 14.80000 -9.97600  1.000 84.43000  ? 744  PHE   A CE1 1 
ATOM   1596 C  CE2 . PHE   A 1 218 ? -53.61000 16.78800 -8.68300  1.000 86.52000  ? 744  PHE   A CE2 1 
ATOM   1597 C  CZ  . PHE   A 1 218 ? -53.17600 15.53100 -9.05400  1.000 83.24000  ? 744  PHE   A CZ  1 
ATOM   1598 N  N   . ASN   A 1 219 ? -58.35400 15.01100 -8.56100  1.000 97.55000  ? 745  ASN   A N   1 
ATOM   1599 C  CA  . ASN   A 1 219 ? -58.93500 14.76500 -7.24300  1.000 95.85000  ? 745  ASN   A CA  1 
ATOM   1600 C  C   . ASN   A 1 219 ? -58.00700 13.87400 -6.42900  1.000 99.98000  ? 745  ASN   A C   1 
ATOM   1601 O  O   . ASN   A 1 219 ? -57.88300 12.68100 -6.71900  1.000 96.89000  ? 745  ASN   A O   1 
ATOM   1602 C  CB  . ASN   A 1 219 ? -60.31000 14.10400 -7.37000  1.000 91.14000  ? 745  ASN   A CB  1 
ATOM   1603 C  CG  . ASN   A 1 219 ? -60.69400 13.33100 -6.12900  1.000 98.93000  ? 745  ASN   A CG  1 
ATOM   1604 O  OD1 . ASN   A 1 219 ? -60.90400 13.91300 -5.07200  1.000 94.72000  ? 745  ASN   A OD1 1 
ATOM   1605 N  ND2 . ASN   A 1 219 ? -60.76300 12.01200 -6.24500  1.000 95.76000  ? 745  ASN   A ND2 1 
ATOM   1606 N  N   . LEU   A 1 220 ? -57.38300 14.43300 -5.39400  1.000 94.88000  ? 746  LEU   A N   1 
ATOM   1607 C  CA  . LEU   A 1 220 ? -56.38800 13.68300 -4.64000  1.000 86.03000  ? 746  LEU   A CA  1 
ATOM   1608 C  C   . LEU   A 1 220 ? -56.98700 12.70600 -3.63500  1.000 88.63000  ? 746  LEU   A C   1 
ATOM   1609 O  O   . LEU   A 1 220 ? -56.23900 11.90900 -3.05800  1.000 92.73000  ? 746  LEU   A O   1 
ATOM   1610 C  CB  . LEU   A 1 220 ? -55.43600 14.64300 -3.92300  1.000 77.93000  ? 746  LEU   A CB  1 
ATOM   1611 C  CG  . LEU   A 1 220 ? -54.50200 15.37200 -4.89000  1.000 69.50000  ? 746  LEU   A CG  1 
ATOM   1612 C  CD1 . LEU   A 1 220 ? -53.51700 16.24000 -4.13600  1.000 55.59000  ? 746  LEU   A CD1 1 
ATOM   1613 C  CD2 . LEU   A 1 220 ? -53.77200 14.37900 -5.78600  1.000 73.50000  ? 746  LEU   A CD2 1 
ATOM   1614 N  N   . GLU   A 1 221 ? -58.30500 12.73800 -3.41300  1.000 89.55000  ? 747  GLU   A N   1 
ATOM   1615 C  CA  . GLU   A 1 221 ? -58.93400 11.74200 -2.55100  1.000 86.25000  ? 747  GLU   A CA  1 
ATOM   1616 C  C   . GLU   A 1 221 ? -58.95900 10.36000 -3.19300  1.000 79.81000  ? 747  GLU   A C   1 
ATOM   1617 O  O   . GLU   A 1 221 ? -59.08900 9.35800  -2.48000  1.000 78.99000  ? 747  GLU   A O   1 
ATOM   1618 C  CB  . GLU   A 1 221 ? -60.35600 12.17900 -2.18600  1.000 91.76000  ? 747  GLU   A CB  1 
ATOM   1619 C  CG  . GLU   A 1 221 ? -60.43000 13.18300 -1.04100  1.000 95.35000  ? 747  GLU   A CG  1 
ATOM   1620 C  CD  . GLU   A 1 221 ? -60.49400 14.62400 -1.51200  1.000 96.74000  ? 747  GLU   A CD  1 
ATOM   1621 O  OE1 . GLU   A 1 221 ? -60.76500 15.50700 -0.67300  1.000 92.44000  ? 747  GLU   A OE1 1 
ATOM   1622 O  OE2 . GLU   A 1 221 ? -60.26400 14.88000 -2.70900  1.000 101.80000 ? 747  GLU   A OE2 1 
ATOM   1623 N  N   . ASP   A 1 222 ? -58.85600 10.29000 -4.51000  1.000 85.59000  ? 748  ASP   A N   1 
ATOM   1624 C  CA  . ASP   A 1 222 ? -58.73700 9.02100  -5.21700  1.000 80.38000  ? 748  ASP   A CA  1 
ATOM   1625 C  C   . ASP   A 1 222 ? -57.36000 8.42500  -4.95100  1.000 83.32000  ? 748  ASP   A C   1 
ATOM   1626 O  O   . ASP   A 1 222 ? -56.35000 9.10700  -5.17000  1.000 86.90000  ? 748  ASP   A O   1 
ATOM   1627 C  CB  . ASP   A 1 222 ? -58.95800 9.24900  -6.71300  1.000 64.61000  ? 748  ASP   A CB  1 
ATOM   1628 C  CG  . ASP   A 1 222 ? -59.06400 7.95600  -7.50900  1.000 80.90000  ? 748  ASP   A CG  1 
ATOM   1629 O  OD1 . ASP   A 1 222 ? -58.35300 6.98100  -7.19000  1.000 84.74000  ? 748  ASP   A OD1 1 
ATOM   1630 O  OD2 . ASP   A 1 222 ? -59.84300 7.92300  -8.48500  1.000 87.74000  ? 748  ASP   A OD2 1 
ATOM   1631 N  N   . PRO   A 1 223 ? -57.26700 7.17900  -4.47800  1.000 78.25000  ? 749  PRO   A N   1 
ATOM   1632 C  CA  . PRO   A 1 223 ? -55.94300 6.59300  -4.20000  1.000 81.15000  ? 749  PRO   A CA  1 
ATOM   1633 C  C   . PRO   A 1 223 ? -55.07300 6.42600  -5.43300  1.000 84.19000  ? 749  PRO   A C   1 
ATOM   1634 O  O   . PRO   A 1 223 ? -53.84600 6.56900  -5.34100  1.000 84.00000  ? 749  PRO   A O   1 
ATOM   1635 C  CB  . PRO   A 1 223 ? -56.29000 5.23600  -3.56900  1.000 84.73000  ? 749  PRO   A CB  1 
ATOM   1636 C  CG  . PRO   A 1 223 ? -57.68300 5.40500  -3.04100  1.000 81.66000  ? 749  PRO   A CG  1 
ATOM   1637 C  CD  . PRO   A 1 223 ? -58.36700 6.32600  -4.00200  1.000 81.30000  ? 749  PRO   A CD  1 
ATOM   1638 N  N   . HIS   A 1 224 ? -55.66800 6.10500  -6.58300  1.000 82.12000  ? 750  HIS   A N   1 
ATOM   1639 C  CA  . HIS   A 1 224 ? -54.89800 6.04200  -7.82100  1.000 81.21000  ? 750  HIS   A CA  1 
ATOM   1640 C  C   . HIS   A 1 224 ? -54.37300 7.41900  -8.20900  1.000 78.39000  ? 750  HIS   A C   1 
ATOM   1641 O  O   . HIS   A 1 224 ? -53.26500 7.54500  -8.73700  1.000 73.50000  ? 750  HIS   A O   1 
ATOM   1642 C  CB  . HIS   A 1 224 ? -55.76200 5.45700  -8.93800  1.000 72.03000  ? 750  HIS   A CB  1 
ATOM   1643 C  CG  . HIS   A 1 224 ? -55.12700 5.51500  -10.29300 1.000 71.59000  ? 750  HIS   A CG  1 
ATOM   1644 N  ND1 . HIS   A 1 224 ? -54.20000 4.58800  -10.72000 1.000 67.97000  ? 750  HIS   A ND1 1 
ATOM   1645 C  CD2 . HIS   A 1 224 ? -55.29400 6.38000  -11.32200 1.000 74.10000  ? 750  HIS   A CD2 1 
ATOM   1646 C  CE1 . HIS   A 1 224 ? -53.82100 4.88200  -11.95100 1.000 68.74000  ? 750  HIS   A CE1 1 
ATOM   1647 N  NE2 . HIS   A 1 224 ? -54.46900 5.96500  -12.33900 1.000 71.70000  ? 750  HIS   A NE2 1 
ATOM   1648 N  N   . GLN   A 1 225 ? -55.15600 8.46000  -7.94700  1.000 78.48000  ? 751  GLN   A N   1 
ATOM   1649 C  CA  . GLN   A 1 225 ? -54.73700 9.82600  -8.22700  1.000 79.63000  ? 751  GLN   A CA  1 
ATOM   1650 C  C   . GLN   A 1 225 ? -53.56500 10.24800 -7.34700  1.000 78.77000  ? 751  GLN   A C   1 
ATOM   1651 O  O   . GLN   A 1 225 ? -52.61800 10.89000 -7.81800  1.000 65.74000  ? 751  GLN   A O   1 
ATOM   1652 C  CB  . GLN   A 1 225 ? -55.91200 10.75300 -7.99800  1.000 85.41000  ? 751  GLN   A CB  1 
ATOM   1653 C  CG  . GLN   A 1 225 ? -56.96000 10.72800 -9.10400  1.000 95.49000  ? 751  GLN   A CG  1 
ATOM   1654 C  CD  . GLN   A 1 225 ? -56.92800 11.99000 -9.93500  1.000 97.76000  ? 751  GLN   A CD  1 
ATOM   1655 O  OE1 . GLN   A 1 225 ? -56.83300 13.07200 -9.37500  1.000 100.21000 ? 751  GLN   A OE1 1 
ATOM   1656 N  NE2 . GLN   A 1 225 ? -57.02800 11.87100 -11.26200 1.000 89.08000  ? 751  GLN   A NE2 1 
ATOM   1657 N  N   . LYS   A 1 226 ? -53.63200 9.91400  -6.05800  1.000 75.66000  ? 752  LYS   A N   1 
ATOM   1658 C  CA  . LYS   A 1 226 ? -52.61100 10.34100 -5.11100  1.000 67.38000  ? 752  LYS   A CA  1 
ATOM   1659 C  C   . LYS   A 1 226 ? -51.27500 9.69500  -5.43300  1.000 68.68000  ? 752  LYS   A C   1 
ATOM   1660 O  O   . LYS   A 1 226 ? -50.23400 10.35800 -5.41400  1.000 66.79000  ? 752  LYS   A O   1 
ATOM   1661 C  CB  . LYS   A 1 226 ? -53.05900 10.00400 -3.68800  1.000 67.58000  ? 752  LYS   A CB  1 
ATOM   1662 C  CG  . LYS   A 1 226 ? -51.99800 10.25400 -2.63000  1.000 67.94000  ? 752  LYS   A CG  1 
ATOM   1663 C  CD  . LYS   A 1 226 ? -51.78400 11.74000 -2.41900  1.000 72.16000  ? 752  LYS   A CD  1 
ATOM   1664 C  CE  . LYS   A 1 226 ? -52.94900 12.33800 -1.65400  1.000 60.34000  ? 752  LYS   A CE  1 
ATOM   1665 N  NZ  . LYS   A 1 226 ? -53.06700 11.76400 -0.28600  1.000 65.84000  ? 752  LYS   A NZ  1 
ATOM   1666 N  N   . GLU   A 1 227 ? -51.29100 8.39800  -5.75500  1.000 63.15000  ? 753  GLU   A N   1 
ATOM   1667 C  CA  . GLU   A 1 227 ? -50.06400 7.70700  -6.13900  1.000 62.46000  ? 753  GLU   A CA  1 
ATOM   1668 C  C   . GLU   A 1 227 ? -49.46100 8.30900  -7.40300  1.000 65.27000  ? 753  GLU   A C   1 
ATOM   1669 O  O   . GLU   A 1 227 ? -48.23600 8.42300  -7.52300  1.000 68.92000  ? 753  GLU   A O   1 
ATOM   1670 C  CB  . GLU   A 1 227 ? -50.35300 6.21900  -6.33100  1.000 63.04000  ? 753  GLU   A CB  1 
ATOM   1671 C  CG  . GLU   A 1 227 ? -49.17100 5.41300  -6.81900  1.000 63.87000  ? 753  GLU   A CG  1 
ATOM   1672 C  CD  . GLU   A 1 227 ? -49.53600 3.97600  -7.11600  1.000 81.76000  ? 753  GLU   A CD  1 
ATOM   1673 O  OE1 . GLU   A 1 227 ? -48.83200 3.34800  -7.93300  1.000 80.21000  ? 753  GLU   A OE1 1 
ATOM   1674 O  OE2 . GLU   A 1 227 ? -50.52200 3.47400  -6.53500  1.000 84.56000  ? 753  GLU   A OE2 1 
ATOM   1675 N  N   . LEU   A 1 228 ? -50.30800 8.69700  -8.36000  1.000 65.77000  ? 754  LEU   A N   1 
ATOM   1676 C  CA  . LEU   A 1 228 ? -49.81000 9.33800  -9.57200  1.000 64.36000  ? 754  LEU   A CA  1 
ATOM   1677 C  C   . LEU   A 1 228 ? -49.18100 10.69100 -9.26200  1.000 58.21000  ? 754  LEU   A C   1 
ATOM   1678 O  O   . LEU   A 1 228 ? -48.15900 11.05600 -9.85400  1.000 54.27000  ? 754  LEU   A O   1 
ATOM   1679 C  CB  . LEU   A 1 228 ? -50.94300 9.49000  -10.58600 1.000 63.20000  ? 754  LEU   A CB  1 
ATOM   1680 C  CG  . LEU   A 1 228 ? -50.58300 10.13100 -11.92800 1.000 66.03000  ? 754  LEU   A CG  1 
ATOM   1681 C  CD1 . LEU   A 1 228 ? -49.79200 9.16400  -12.79700 1.000 67.82000  ? 754  LEU   A CD1 1 
ATOM   1682 C  CD2 . LEU   A 1 228 ? -51.83500 10.60400 -12.65000 1.000 65.81000  ? 754  LEU   A CD2 1 
ATOM   1683 N  N   . PHE   A 1 229 ? -49.77200 11.44500 -8.33200  1.000 48.22000  ? 755  PHE   A N   1 
ATOM   1684 C  CA  . PHE   A 1 229 ? -49.21200 12.74200 -7.96600  1.000 53.26000  ? 755  PHE   A CA  1 
ATOM   1685 C  C   . PHE   A 1 229 ? -47.88400 12.58500 -7.23500  1.000 60.46000  ? 755  PHE   A C   1 
ATOM   1686 O  O   . PHE   A 1 229 ? -46.94200 13.34800 -7.47900  1.000 60.18000  ? 755  PHE   A O   1 
ATOM   1687 C  CB  . PHE   A 1 229 ? -50.20700 13.52300 -7.10800  1.000 47.74000  ? 755  PHE   A CB  1 
ATOM   1688 C  CG  . PHE   A 1 229 ? -49.64700 14.79300 -6.53500  1.000 50.78000  ? 755  PHE   A CG  1 
ATOM   1689 C  CD1 . PHE   A 1 229 ? -49.43000 15.89600 -7.34400  1.000 61.22000  ? 755  PHE   A CD1 1 
ATOM   1690 C  CD2 . PHE   A 1 229 ? -49.33900 14.88500 -5.18800  1.000 52.50000  ? 755  PHE   A CD2 1 
ATOM   1691 C  CE1 . PHE   A 1 229 ? -48.91600 17.06800 -6.82000  1.000 44.00000  ? 755  PHE   A CE1 1 
ATOM   1692 C  CE2 . PHE   A 1 229 ? -48.82400 16.05400 -4.65800  1.000 51.08000  ? 755  PHE   A CE2 1 
ATOM   1693 C  CZ  . PHE   A 1 229 ? -48.61300 17.14600 -5.47500  1.000 54.44000  ? 755  PHE   A CZ  1 
ATOM   1694 N  N   . LEU   A 1 230 ? -47.79100 11.60400 -6.33200  1.000 60.34000  ? 756  LEU   A N   1 
ATOM   1695 C  CA  . LEU   A 1 230 ? -46.52600 11.34300 -5.65200  1.000 51.18000  ? 756  LEU   A CA  1 
ATOM   1696 C  C   . LEU   A 1 230 ? -45.44400 10.93900 -6.64600  1.000 47.75000  ? 756  LEU   A C   1 
ATOM   1697 O  O   . LEU   A 1 230 ? -44.27000 11.28500 -6.47300  1.000 48.63000  ? 756  LEU   A O   1 
ATOM   1698 C  CB  . LEU   A 1 230 ? -46.71000 10.25500 -4.59300  1.000 53.56000  ? 756  LEU   A CB  1 
ATOM   1699 C  CG  . LEU   A 1 230 ? -47.70400 10.52400 -3.46200  1.000 51.47000  ? 756  LEU   A CG  1 
ATOM   1700 C  CD1 . LEU   A 1 230 ? -47.73800 9.35200  -2.49100  1.000 52.42000  ? 756  LEU   A CD1 1 
ATOM   1701 C  CD2 . LEU   A 1 230 ? -47.36600 11.81600 -2.73700  1.000 48.45000  ? 756  LEU   A CD2 1 
ATOM   1702 N  N   . ALA   A 1 231 ? -45.82400 10.20500 -7.69400  1.000 49.27000  ? 757  ALA   A N   1 
ATOM   1703 C  CA  . ALA   A 1 231 ? -44.86100 9.82100  -8.72000  1.000 51.18000  ? 757  ALA   A CA  1 
ATOM   1704 C  C   . ALA   A 1 231 ? -44.34900 11.03700 -9.48000  1.000 52.74000  ? 757  ALA   A C   1 
ATOM   1705 O  O   . ALA   A 1 231 ? -43.14200 11.16200 -9.72500  1.000 46.01000  ? 757  ALA   A O   1 
ATOM   1706 C  CB  . ALA   A 1 231 ? -45.49400 8.81300  -9.67900  1.000 53.21000  ? 757  ALA   A CB  1 
ATOM   1707 N  N   . MET   A 1 232 ? -45.25000 11.94600 -9.86000  1.000 52.98000  ? 758  MET   A N   1 
ATOM   1708 C  CA  . MET   A 1 232 ? -44.83000 13.14900 -10.56900 1.000 48.12000  ? 758  MET   A CA  1 
ATOM   1709 C  C   . MET   A 1 232 ? -44.06500 14.09900 -9.65800  1.000 46.02000  ? 758  MET   A C   1 
ATOM   1710 O  O   . MET   A 1 232 ? -43.16600 14.81100 -10.12200 1.000 39.77000  ? 758  MET   A O   1 
ATOM   1711 C  CB  . MET   A 1 232 ? -46.04600 13.85500 -11.16900 1.000 54.06000  ? 758  MET   A CB  1 
ATOM   1712 C  CG  . MET   A 1 232 ? -46.85900 12.99100 -12.11900 1.000 45.56000  ? 758  MET   A CG  1 
ATOM   1713 S  SD  . MET   A 1 232 ? -45.98100 12.62700 -13.65000 1.000 57.99000  ? 758  MET   A SD  1 
ATOM   1714 C  CE  . MET   A 1 232 ? -46.37000 10.89200 -13.86100 1.000 52.82000  ? 758  MET   A CE  1 
ATOM   1715 N  N   . LEU   A 1 233 ? -44.40200 14.12400 -8.36600  1.000 44.52000  ? 759  LEU   A N   1 
ATOM   1716 C  CA  . LEU   A 1 233 ? -43.70200 15.00100 -7.43300  1.000 42.27000  ? 759  LEU   A CA  1 
ATOM   1717 C  C   . LEU   A 1 233 ? -42.24700 14.58100 -7.26400  1.000 43.78000  ? 759  LEU   A C   1 
ATOM   1718 O  O   . LEU   A 1 233 ? -41.35900 15.43300 -7.14200  1.000 46.72000  ? 759  LEU   A O   1 
ATOM   1719 C  CB  . LEU   A 1 233 ? -44.42200 15.00900 -6.08400  1.000 47.49000  ? 759  LEU   A CB  1 
ATOM   1720 C  CG  . LEU   A 1 233 ? -43.82300 15.88800 -4.98400  1.000 44.82000  ? 759  LEU   A CG  1 
ATOM   1721 C  CD1 . LEU   A 1 233 ? -43.69800 17.32700 -5.45600  1.000 49.88000  ? 759  LEU   A CD1 1 
ATOM   1722 C  CD2 . LEU   A 1 233 ? -44.66100 15.80600 -3.71700  1.000 37.49000  ? 759  LEU   A CD2 1 
ATOM   1723 N  N   . MET   A 1 234 ? -41.98100 13.27300 -7.25800  1.000 42.87000  ? 760  MET   A N   1 
ATOM   1724 C  CA  . MET   A 1 234 ? -40.60600 12.80600 -7.11600  1.000 35.70000  ? 760  MET   A CA  1 
ATOM   1725 C  C   . MET   A 1 234 ? -39.78500 13.12500 -8.35900  1.000 35.35000  ? 760  MET   A C   1 
ATOM   1726 O  O   . MET   A 1 234 ? -38.60200 13.46600 -8.25500  1.000 46.60000  ? 760  MET   A O   1 
ATOM   1727 C  CB  . MET   A 1 234 ? -40.58400 11.30500 -6.82500  1.000 40.20000  ? 760  MET   A CB  1 
ATOM   1728 C  CG  . MET   A 1 234 ? -40.92300 10.93700 -5.38600  1.000 32.00000  ? 760  MET   A CG  1 
ATOM   1729 S  SD  . MET   A 1 234 ? -39.53200 11.11200 -4.25400  1.000 37.65000  ? 760  MET   A SD  1 
ATOM   1730 C  CE  . MET   A 1 234 ? -38.45700 9.79600  -4.81900  1.000 30.21000  ? 760  MET   A CE  1 
ATOM   1731 N  N   . THR   A 1 235 ? -40.39200 13.02000 -9.54400  1.000 45.38000  ? 761  THR   A N   1 
ATOM   1732 C  CA  . THR   A 1 235 ? -39.69400 13.40600 -10.76600 1.000 42.89000  ? 761  THR   A CA  1 
ATOM   1733 C  C   . THR   A 1 235 ? -39.39600 14.90100 -10.77800 1.000 35.32000  ? 761  THR   A C   1 
ATOM   1734 O  O   . THR   A 1 235 ? -38.34700 15.33100 -11.27200 1.000 45.28000  ? 761  THR   A O   1 
ATOM   1735 C  CB  . THR   A 1 235 ? -40.52300 13.01200 -11.99200 1.000 44.97000  ? 761  THR   A CB  1 
ATOM   1736 O  OG1 . THR   A 1 235 ? -40.74800 11.59700 -11.98400 1.000 41.83000  ? 761  THR   A OG1 1 
ATOM   1737 C  CG2 . THR   A 1 235 ? -39.80500 13.39500 -13.28000 1.000 35.36000  ? 761  THR   A CG2 1 
ATOM   1738 N  N   . ALA   A 1 236 ? -40.30400 15.70700 -10.22100 1.000 43.30000  ? 762  ALA   A N   1 
ATOM   1739 C  CA  . ALA   A 1 236 ? -40.11600 17.15400 -10.21200 1.000 43.81000  ? 762  ALA   A CA  1 
ATOM   1740 C  C   . ALA   A 1 236 ? -38.87600 17.54700 -9.41700  1.000 40.69000  ? 762  ALA   A C   1 
ATOM   1741 O  O   . ALA   A 1 236 ? -38.08200 18.38400 -9.86300  1.000 43.53000  ? 762  ALA   A O   1 
ATOM   1742 C  CB  . ALA   A 1 236 ? -41.36100 17.83400 -9.64200  1.000 30.96000  ? 762  ALA   A CB  1 
ATOM   1743 N  N   . CYS   A 1 237 ? -38.69600 16.95200 -8.23400  1.000 39.82000  ? 763  CYS   A N   1 
ATOM   1744 C  CA  . CYS   A 1 237 ? -37.52000 17.23000 -7.41600  1.000 42.29000  ? 763  CYS   A CA  1 
ATOM   1745 C  C   . CYS   A 1 237 ? -36.28900 16.49500 -7.92100  1.000 39.85000  ? 763  CYS   A C   1 
ATOM   1746 O  O   . CYS   A 1 237 ? -35.16800 16.97900 -7.73600  1.000 36.58000  ? 763  CYS   A O   1 
ATOM   1747 C  CB  . CYS   A 1 237 ? -37.78500 16.84700 -5.95500  1.000 33.25000  ? 763  CYS   A CB  1 
ATOM   1748 S  SG  . CYS   A 1 237 ? -39.25500 17.59300 -5.24200  1.000 44.09000  ? 763  CYS   A SG  1 
ATOM   1749 N  N   . ASP   A 1 238 ? -36.47400 15.32900 -8.54300  1.000 40.17000  ? 764  ASP   A N   1 
ATOM   1750 C  CA  . ASP   A 1 238 ? -35.34200 14.60300 -9.11100  1.000 37.06000  ? 764  ASP   A CA  1 
ATOM   1751 C  C   . ASP   A 1 238 ? -34.62300 15.43900 -10.16400 1.000 39.37000  ? 764  ASP   A C   1 
ATOM   1752 O  O   . ASP   A 1 238 ? -33.38700 15.44700 -10.23100 1.000 39.70000  ? 764  ASP   A O   1 
ATOM   1753 C  CB  . ASP   A 1 238 ? -35.81900 13.28000 -9.71500  1.000 34.28000  ? 764  ASP   A CB  1 
ATOM   1754 C  CG  . ASP   A 1 238 ? -34.67700 12.38400 -10.14900 1.000 39.12000  ? 764  ASP   A CG  1 
ATOM   1755 O  OD1 . ASP   A 1 238 ? -33.55700 12.56200 -9.63700  1.000 43.63000  ? 764  ASP   A OD1 1 
ATOM   1756 O  OD2 . ASP   A 1 238 ? -34.89900 11.50400 -11.00800 1.000 46.08000  ? 764  ASP   A OD2 1 
ATOM   1757 N  N   . LEU   A 1 239 ? -35.38200 16.15500 -10.99200 1.000 37.20000  ? 765  LEU   A N   1 
ATOM   1758 C  CA  . LEU   A 1 239 ? -34.82900 17.00100 -12.03900 1.000 47.55000  ? 765  LEU   A CA  1 
ATOM   1759 C  C   . LEU   A 1 239 ? -34.81600 18.47500 -11.64900 1.000 40.19000  ? 765  LEU   A C   1 
ATOM   1760 O  O   . LEU   A 1 239 ? -34.66800 19.33600 -12.52100 1.000 42.72000  ? 765  LEU   A O   1 
ATOM   1761 C  CB  . LEU   A 1 239 ? -35.61400 16.80800 -13.33800 1.000 38.79000  ? 765  LEU   A CB  1 
ATOM   1762 C  CG  . LEU   A 1 239 ? -36.05400 15.38200 -13.67800 1.000 36.12000  ? 765  LEU   A CG  1 
ATOM   1763 C  CD1 . LEU   A 1 239 ? -37.05600 15.39300 -14.82000 1.000 41.26000  ? 765  LEU   A CD1 1 
ATOM   1764 C  CD2 . LEU   A 1 239 ? -34.85500 14.51300 -14.02500 1.000 28.62000  ? 765  LEU   A CD2 1 
ATOM   1765 N  N   . SER   A 1 240 ? -34.95800 18.78200 -10.35600 1.000 34.98000  ? 766  SER   A N   1 
ATOM   1766 C  CA  . SER   A 1 240 ? -35.09600 20.16500 -9.91000  1.000 35.64000  ? 766  SER   A CA  1 
ATOM   1767 C  C   . SER   A 1 240 ? -33.85300 21.01000 -10.16400 1.000 37.30000  ? 766  SER   A C   1 
ATOM   1768 O  O   . SER   A 1 240 ? -33.93200 22.23900 -10.05400 1.000 34.81000  ? 766  SER   A O   1 
ATOM   1769 C  CB  . SER   A 1 240 ? -35.44400 20.20200 -8.42100  1.000 34.87000  ? 766  SER   A CB  1 
ATOM   1770 O  OG  . SER   A 1 240 ? -34.52200 19.43800 -7.66500  1.000 41.68000  ? 766  SER   A OG  1 
ATOM   1771 N  N   . ALA   A 1 241 ? -32.71500 20.39500 -10.49300 1.000 30.94000  ? 767  ALA   A N   1 
ATOM   1772 C  CA  . ALA   A 1 241 ? -31.52800 21.17300 -10.82700 1.000 36.98000  ? 767  ALA   A CA  1 
ATOM   1773 C  C   . ALA   A 1 241 ? -31.73100 22.01400 -12.07800 1.000 42.14000  ? 767  ALA   A C   1 
ATOM   1774 O  O   . ALA   A 1 241 ? -31.03400 23.01900 -12.26000 1.000 33.22000  ? 767  ALA   A O   1 
ATOM   1775 C  CB  . ALA   A 1 241 ? -30.32500 20.24700 -11.00700 1.000 26.99000  ? 767  ALA   A CB  1 
ATOM   1776 N  N   . ILE   A 1 242 ? -32.67400 21.62800 -12.94100 1.000 34.31000  ? 768  ILE   A N   1 
ATOM   1777 C  CA  . ILE   A 1 242 ? -32.98600 22.40400 -14.13400 1.000 38.09000  ? 768  ILE   A CA  1 
ATOM   1778 C  C   . ILE   A 1 242 ? -33.70500 23.70600 -13.81300 1.000 39.81000  ? 768  ILE   A C   1 
ATOM   1779 O  O   . ILE   A 1 242 ? -33.81200 24.57600 -14.68500 1.000 37.16000  ? 768  ILE   A O   1 
ATOM   1780 C  CB  . ILE   A 1 242 ? -33.82600 21.54700 -15.10600 1.000 32.78000  ? 768  ILE   A CB  1 
ATOM   1781 C  CG1 . ILE   A 1 242 ? -33.64100 22.02500 -16.54500 1.000 32.77000  ? 768  ILE   A CG1 1 
ATOM   1782 C  CG2 . ILE   A 1 242 ? -35.29600 21.57100 -14.71600 1.000 26.25000  ? 768  ILE   A CG2 1 
ATOM   1783 C  CD1 . ILE   A 1 242 ? -32.24200 21.84200 -17.07600 1.000 33.77000  ? 768  ILE   A CD1 1 
ATOM   1784 N  N   . THR   A 1 243 ? -34.18700 23.86700 -12.58200 1.000 36.52000  ? 769  THR   A N   1 
ATOM   1785 C  CA  . THR   A 1 243 ? -34.91700 25.05600 -12.16500 1.000 36.90000  ? 769  THR   A CA  1 
ATOM   1786 C  C   . THR   A 1 243 ? -34.06800 26.02400 -11.35100 1.000 44.27000  ? 769  THR   A C   1 
ATOM   1787 O  O   . THR   A 1 243 ? -34.55100 27.10400 -10.99800 1.000 39.97000  ? 769  THR   A O   1 
ATOM   1788 C  CB  . THR   A 1 243 ? -36.15000 24.65600 -11.34900 1.000 34.71000  ? 769  THR   A CB  1 
ATOM   1789 O  OG1 . THR   A 1 243 ? -35.73900 24.21000 -10.05100 1.000 37.48000  ? 769  THR   A OG1 1 
ATOM   1790 C  CG2 . THR   A 1 243 ? -36.90500 23.53400 -12.04100 1.000 31.92000  ? 769  THR   A CG2 1 
ATOM   1791 N  N   . LYS   A 1 244 ? -32.82300 25.66500 -11.04700 1.000 39.93000  ? 770  LYS   A N   1 
ATOM   1792 C  CA  . LYS   A 1 244 ? -31.98300 26.48500 -10.19300 1.000 42.71000  ? 770  LYS   A CA  1 
ATOM   1793 C  C   . LYS   A 1 244 ? -31.58800 27.77900 -10.90100 1.000 45.80000  ? 770  LYS   A C   1 
ATOM   1794 O  O   . LYS   A 1 244 ? -31.71100 27.89200 -12.12300 1.000 50.18000  ? 770  LYS   A O   1 
ATOM   1795 C  CB  . LYS   A 1 244 ? -30.73300 25.70600 -9.78700  1.000 39.43000  ? 770  LYS   A CB  1 
ATOM   1796 C  CG  . LYS   A 1 244 ? -31.01500 24.51000 -8.89900  1.000 37.71000  ? 770  LYS   A CG  1 
ATOM   1797 C  CD  . LYS   A 1 244 ? -31.71700 24.93000 -7.61900  1.000 40.69000  ? 770  LYS   A CD  1 
ATOM   1798 C  CE  . LYS   A 1 244 ? -31.90500 23.74900 -6.68100  1.000 33.66000  ? 770  LYS   A CE  1 
ATOM   1799 N  NZ  . LYS   A 1 244 ? -32.50000 24.15800 -5.37900  1.000 42.09000  ? 770  LYS   A NZ  1 
ATOM   1800 N  N   . PRO   A 1 245 ? -31.12500 28.78900 -10.14100 1.000 44.83000  ? 771  PRO   A N   1 
ATOM   1801 C  CA  . PRO   A 1 245 ? -30.58300 30.00000 -10.77400 1.000 38.13000  ? 771  PRO   A CA  1 
ATOM   1802 C  C   . PRO   A 1 245 ? -29.48300 29.69300 -11.77800 1.000 41.85000  ? 771  PRO   A C   1 
ATOM   1803 O  O   . PRO   A 1 245 ? -28.82200 28.65300 -11.69000 1.000 45.41000  ? 771  PRO   A O   1 
ATOM   1804 C  CB  . PRO   A 1 245 ? -30.05300 30.80600 -9.58300  1.000 30.18000  ? 771  PRO   A CB  1 
ATOM   1805 C  CG  . PRO   A 1 245 ? -30.93200 30.39800 -8.45200  1.000 43.32000  ? 771  PRO   A CG  1 
ATOM   1806 C  CD  . PRO   A 1 245 ? -31.25100 28.94200 -8.68000  1.000 41.76000  ? 771  PRO   A CD  1 
ATOM   1807 N  N   . TRP   A 1 246 ? -29.28100 30.60600 -12.72900 1.000 46.97000  ? 772  TRP   A N   1 
ATOM   1808 C  CA  . TRP   A 1 246 ? -28.41100 30.32800 -13.87100 1.000 46.84000  ? 772  TRP   A CA  1 
ATOM   1809 C  C   . TRP   A 1 246 ? -26.99000 29.93200 -13.48200 1.000 44.29000  ? 772  TRP   A C   1 
ATOM   1810 O  O   . TRP   A 1 246 ? -26.47900 28.94700 -14.04300 1.000 43.40000  ? 772  TRP   A O   1 
ATOM   1811 C  CB  . TRP   A 1 246 ? -28.41600 31.53300 -14.81800 1.000 49.92000  ? 772  TRP   A CB  1 
ATOM   1812 C  CG  . TRP   A 1 246 ? -27.48100 31.39600 -15.98000 1.000 45.47000  ? 772  TRP   A CG  1 
ATOM   1813 C  CD1 . TRP   A 1 246 ? -26.49100 32.26400 -16.33900 1.000 43.74000  ? 772  TRP   A CD1 1 
ATOM   1814 C  CD2 . TRP   A 1 246 ? -27.45000 30.33200 -16.94000 1.000 49.11000  ? 772  TRP   A CD2 1 
ATOM   1815 N  NE1 . TRP   A 1 246 ? -25.84400 31.80600 -17.46100 1.000 49.10000  ? 772  TRP   A NE1 1 
ATOM   1816 C  CE2 . TRP   A 1 246 ? -26.41400 30.62200 -17.85000 1.000 54.36000  ? 772  TRP   A CE2 1 
ATOM   1817 C  CE3 . TRP   A 1 246 ? -28.19700 29.16300 -17.12000 1.000 44.36000  ? 772  TRP   A CE3 1 
ATOM   1818 C  CZ2 . TRP   A 1 246 ? -26.10500 29.78600 -18.92100 1.000 54.14000  ? 772  TRP   A CZ2 1 
ATOM   1819 C  CZ3 . TRP   A 1 246 ? -27.88900 28.33500 -18.18300 1.000 43.48000  ? 772  TRP   A CZ3 1 
ATOM   1820 C  CH2 . TRP   A 1 246 ? -26.85300 28.65000 -19.07000 1.000 47.99000  ? 772  TRP   A CH2 1 
ATOM   1821 N  N   . PRO   A 1 247 ? -26.29500 30.62600 -12.57100 1.000 49.14000  ? 773  PRO   A N   1 
ATOM   1822 C  CA  . PRO   A 1 247 ? -24.94100 30.17000 -12.21400 1.000 51.66000  ? 773  PRO   A CA  1 
ATOM   1823 C  C   . PRO   A 1 247 ? -24.91700 28.79200 -11.57600 1.000 39.56000  ? 773  PRO   A C   1 
ATOM   1824 O  O   . PRO   A 1 247 ? -23.92000 28.07200 -11.71700 1.000 44.74000  ? 773  PRO   A O   1 
ATOM   1825 C  CB  . PRO   A 1 247 ? -24.44900 31.25200 -11.24000 1.000 44.93000  ? 773  PRO   A CB  1 
ATOM   1826 C  CG  . PRO   A 1 247 ? -25.28300 32.44400 -11.54300 1.000 47.21000  ? 773  PRO   A CG  1 
ATOM   1827 C  CD  . PRO   A 1 247 ? -26.62700 31.89500 -11.89800 1.000 39.42000  ? 773  PRO   A CD  1 
ATOM   1828 N  N   . ILE   A 1 248 ? -25.98400 28.40000 -10.88100 1.000 41.63000  ? 774  ILE   A N   1 
ATOM   1829 C  CA  . ILE   A 1 248 ? -26.02900 27.07800 -10.26600 1.000 38.77000  ? 774  ILE   A CA  1 
ATOM   1830 C  C   . ILE   A 1 248 ? -26.32800 26.00800 -11.30800 1.000 38.40000  ? 774  ILE   A C   1 
ATOM   1831 O  O   . ILE   A 1 248 ? -25.65600 24.97200 -11.36500 1.000 40.82000  ? 774  ILE   A O   1 
ATOM   1832 C  CB  . ILE   A 1 248 ? -27.05800 27.05500 -9.12100  1.000 46.75000  ? 774  ILE   A CB  1 
ATOM   1833 C  CG1 . ILE   A 1 248 ? -26.84700 28.24900 -8.18800  1.000 42.97000  ? 774  ILE   A CG1 1 
ATOM   1834 C  CG2 . ILE   A 1 248 ? -26.96600 25.74800 -8.34900  1.000 35.65000  ? 774  ILE   A CG2 1 
ATOM   1835 C  CD1 . ILE   A 1 248 ? -25.50100 28.25400 -7.49800  1.000 32.28000  ? 774  ILE   A CD1 1 
ATOM   1836 N  N   . GLN   A 1 249 ? -27.34000 26.24300 -12.14900 1.000 38.78000  ? 775  GLN   A N   1 
ATOM   1837 C  CA  . GLN   A 1 249 ? -27.69100 25.26800 -13.17800 1.000 43.73000  ? 775  GLN   A CA  1 
ATOM   1838 C  C   . GLN   A 1 249 ? -26.54800 25.07400 -14.16700 1.000 41.80000  ? 775  GLN   A C   1 
ATOM   1839 O  O   . GLN   A 1 249 ? -26.32500 23.96100 -14.66000 1.000 44.34000  ? 775  GLN   A O   1 
ATOM   1840 C  CB  . GLN   A 1 249 ? -28.96900 25.70800 -13.89800 1.000 40.88000  ? 775  GLN   A CB  1 
ATOM   1841 C  CG  . GLN   A 1 249 ? -29.07200 25.28300 -15.36100 1.000 34.58000  ? 775  GLN   A CG  1 
ATOM   1842 C  CD  . GLN   A 1 249 ? -29.21200 23.78000 -15.53900 1.000 39.70000  ? 775  GLN   A CD  1 
ATOM   1843 O  OE1 . GLN   A 1 249 ? -28.86000 23.23300 -16.58400 1.000 36.51000  ? 775  GLN   A OE1 1 
ATOM   1844 N  NE2 . GLN   A 1 249 ? -29.72800 23.10500 -14.51700 1.000 40.90000  ? 775  GLN   A NE2 1 
ATOM   1845 N  N   . GLN   A 1 250 ? -25.80700 26.14500 -14.46200 1.000 41.30000  ? 776  GLN   A N   1 
ATOM   1846 C  CA  . GLN   A 1 250 ? -24.65700 26.03200 -15.35400 1.000 46.72000  ? 776  GLN   A CA  1 
ATOM   1847 C  C   . GLN   A 1 250 ? -23.63600 25.03800 -14.81700 1.000 38.65000  ? 776  GLN   A C   1 
ATOM   1848 O  O   . GLN   A 1 250 ? -23.06100 24.25200 -15.57900 1.000 40.69000  ? 776  GLN   A O   1 
ATOM   1849 C  CB  . GLN   A 1 250 ? -24.01500 27.40500 -15.55000 1.000 47.43000  ? 776  GLN   A CB  1 
ATOM   1850 C  CG  . GLN   A 1 250 ? -23.66200 27.73900 -16.98800 1.000 54.76000  ? 776  GLN   A CG  1 
ATOM   1851 C  CD  . GLN   A 1 250 ? -23.08200 29.13300 -17.13000 1.000 64.48000  ? 776  GLN   A CD  1 
ATOM   1852 O  OE1 . GLN   A 1 250 ? -23.39400 30.03000 -16.34600 1.000 52.87000  ? 776  GLN   A OE1 1 
ATOM   1853 N  NE2 . GLN   A 1 250 ? -22.23100 29.32100 -18.13200 1.000 61.63000  ? 776  GLN   A NE2 1 
ATOM   1854 N  N   . ARG   A 1 251 ? -23.40100 25.05300 -13.50300 1.000 40.33000  ? 777  ARG   A N   1 
ATOM   1855 C  CA  . ARG   A 1 251 ? -22.41700 24.14900 -12.91600 1.000 40.81000  ? 777  ARG   A CA  1 
ATOM   1856 C  C   . ARG   A 1 251 ? -22.94800 22.72300 -12.83700 1.000 39.52000  ? 777  ARG   A C   1 
ATOM   1857 O  O   . ARG   A 1 251 ? -22.20100 21.76400 -13.06400 1.000 35.39000  ? 777  ARG   A O   1 
ATOM   1858 C  CB  . ARG   A 1 251 ? -22.01100 24.64700 -11.53000 1.000 48.54000  ? 777  ARG   A CB  1 
ATOM   1859 C  CG  . ARG   A 1 251 ? -21.30300 25.99100 -11.53300 1.000 37.65000  ? 777  ARG   A CG  1 
ATOM   1860 C  CD  . ARG   A 1 251 ? -19.92500 25.89100 -12.16500 1.000 43.71000  ? 777  ARG   A CD  1 
ATOM   1861 N  NE  . ARG   A 1 251 ? -19.13200 27.09400 -11.93000 1.000 59.49000  ? 777  ARG   A NE  1 
ATOM   1862 C  CZ  . ARG   A 1 251 ? -17.87900 27.25700 -12.34000 1.000 49.77000  ? 777  ARG   A CZ  1 
ATOM   1863 N  NH1 . ARG   A 1 251 ? -17.26800 26.29100 -13.01200 1.000 50.85000  ? 777  ARG   A NH1 1 
ATOM   1864 N  NH2 . ARG   A 1 251 ? -17.23600 28.38600 -12.08000 1.000 58.58000  ? 777  ARG   A NH2 1 
ATOM   1865 N  N   . ILE   A 1 252 ? -24.23300 22.56200 -12.51100 1.000 43.77000  ? 778  ILE   A N   1 
ATOM   1866 C  CA  . ILE   A 1 252 ? -24.80400 21.22300 -12.40200 1.000 44.69000  ? 778  ILE   A CA  1 
ATOM   1867 C  C   . ILE   A 1 252 ? -24.86700 20.55500 -13.76900 1.000 44.28000  ? 778  ILE   A C   1 
ATOM   1868 O  O   . ILE   A 1 252 ? -24.60300 19.35300 -13.90000 1.000 46.29000  ? 778  ILE   A O   1 
ATOM   1869 C  CB  . ILE   A 1 252 ? -26.18900 21.28300 -11.73400 1.000 40.59000  ? 778  ILE   A CB  1 
ATOM   1870 C  CG1 . ILE   A 1 252 ? -26.08300 21.91900 -10.34600 1.000 39.58000  ? 778  ILE   A CG1 1 
ATOM   1871 C  CG2 . ILE   A 1 252 ? -26.78800 19.89200 -11.63100 1.000 41.21000  ? 778  ILE   A CG2 1 
ATOM   1872 C  CD1 . ILE   A 1 252 ? -27.41800 22.30300 -9.74900  1.000 50.85000  ? 778  ILE   A CD1 1 
ATOM   1873 N  N   . ALA   A 1 253 ? -25.21600 21.31900 -14.80900 1.000 44.23000  ? 779  ALA   A N   1 
ATOM   1874 C  CA  . ALA   A 1 253 ? -25.19200 20.77600 -16.16300 1.000 41.04000  ? 779  ALA   A CA  1 
ATOM   1875 C  C   . ALA   A 1 253 ? -23.79400 20.31700 -16.55000 1.000 41.08000  ? 779  ALA   A C   1 
ATOM   1876 O  O   . ALA   A 1 253 ? -23.64300 19.35700 -17.31400 1.000 46.61000  ? 779  ALA   A O   1 
ATOM   1877 C  CB  . ALA   A 1 253 ? -25.70800 21.81500 -17.15800 1.000 36.14000  ? 779  ALA   A CB  1 
ATOM   1878 N  N   . GLU   A 1 254 ? -22.76200 20.98800 -16.03200 1.000 40.80000  ? 780  GLU   A N   1 
ATOM   1879 C  CA  . GLU   A 1 254 ? -21.39400 20.52900 -16.24600 1.000 46.10000  ? 780  GLU   A CA  1 
ATOM   1880 C  C   . GLU   A 1 254 ? -21.15400 19.18600 -15.56700 1.000 48.23000  ? 780  GLU   A C   1 
ATOM   1881 O  O   . GLU   A 1 254 ? -20.45800 18.32300 -16.11400 1.000 46.54000  ? 780  GLU   A O   1 
ATOM   1882 C  CB  . GLU   A 1 254 ? -20.40900 21.57900 -15.73400 1.000 44.14000  ? 780  GLU   A CB  1 
ATOM   1883 C  CG  . GLU   A 1 254 ? -18.98100 21.39600 -16.21500 1.000 59.74000  ? 780  GLU   A CG  1 
ATOM   1884 C  CD  . GLU   A 1 254 ? -18.03400 22.41700 -15.61100 1.000 68.50000  ? 780  GLU   A CD  1 
ATOM   1885 O  OE1 . GLU   A 1 254 ? -16.84400 22.08900 -15.42100 1.000 72.46000  ? 780  GLU   A OE1 1 
ATOM   1886 O  OE2 . GLU   A 1 254 ? -18.48200 23.54700 -15.32500 1.000 53.34000  ? 780  GLU   A OE2 1 
ATOM   1887 N  N   . LEU   A 1 255 ? -21.72300 18.99200 -14.37400 1.000 46.20000  ? 781  LEU   A N   1 
ATOM   1888 C  CA  . LEU   A 1 255 ? -21.60100 17.70600 -13.69500 1.000 44.68000  ? 781  LEU   A CA  1 
ATOM   1889 C  C   . LEU   A 1 255 ? -22.32900 16.60900 -14.46000 1.000 47.09000  ? 781  LEU   A C   1 
ATOM   1890 O  O   . LEU   A 1 255 ? -21.82600 15.48500 -14.57500 1.000 46.52000  ? 781  LEU   A O   1 
ATOM   1891 C  CB  . LEU   A 1 255 ? -22.14200 17.81000 -12.26900 1.000 36.53000  ? 781  LEU   A CB  1 
ATOM   1892 C  CG  . LEU   A 1 255 ? -21.32200 18.62900 -11.27200 1.000 45.20000  ? 781  LEU   A CG  1 
ATOM   1893 C  CD1 . LEU   A 1 255 ? -22.00300 18.64700 -9.91200  1.000 35.31000  ? 781  LEU   A CD1 1 
ATOM   1894 C  CD2 . LEU   A 1 255 ? -19.90900 18.08000 -11.16100 1.000 31.81000  ? 781  LEU   A CD2 1 
ATOM   1895 N  N   . VAL   A 1 256 ? -23.51800 16.91600 -14.98500 1.000 43.20000  ? 782  VAL   A N   1 
ATOM   1896 C  CA  . VAL   A 1 256 ? -24.26100 15.93500 -15.77200 1.000 44.57000  ? 782  VAL   A CA  1 
ATOM   1897 C  C   . VAL   A 1 256 ? -23.47400 15.55600 -17.02000 1.000 48.93000  ? 782  VAL   A C   1 
ATOM   1898 O  O   . VAL   A 1 256 ? -23.28400 14.37200 -17.32000 1.000 64.20000  ? 782  VAL   A O   1 
ATOM   1899 C  CB  . VAL   A 1 256 ? -25.65700 16.47900 -16.12700 1.000 41.27000  ? 782  VAL   A CB  1 
ATOM   1900 C  CG1 . VAL   A 1 256 ? -26.40000 15.49500 -17.01700 1.000 44.80000  ? 782  VAL   A CG1 1 
ATOM   1901 C  CG2 . VAL   A 1 256 ? -26.45100 16.76800 -14.86300 1.000 38.01000  ? 782  VAL   A CG2 1 
ATOM   1902 N  N   . ALA   A 1 257 ? -22.99000 16.55800 -17.75700 1.000 52.08000  ? 783  ALA   A N   1 
ATOM   1903 C  CA  . ALA   A 1 257 ? -22.23900 16.28300 -18.97800 1.000 55.00000  ? 783  ALA   A CA  1 
ATOM   1904 C  C   . ALA   A 1 257 ? -20.95900 15.50700 -18.69300 1.000 49.16000  ? 783  ALA   A C   1 
ATOM   1905 O  O   . ALA   A 1 257 ? -20.50000 14.73800 -19.54500 1.000 61.82000  ? 783  ALA   A O   1 
ATOM   1906 C  CB  . ALA   A 1 257 ? -21.91700 17.59000 -19.70300 1.000 43.05000  ? 783  ALA   A CB  1 
ATOM   1907 N  N   . THR   A 1 258 ? -20.37300 15.68800 -17.50700 1.000 49.96000  ? 784  THR   A N   1 
ATOM   1908 C  CA  . THR   A 1 258 ? -19.15400 14.96000 -17.16800 1.000 54.96000  ? 784  THR   A CA  1 
ATOM   1909 C  C   . THR   A 1 258 ? -19.42400 13.47000 -17.00500 1.000 60.72000  ? 784  THR   A C   1 
ATOM   1910 O  O   . THR   A 1 258 ? -18.59700 12.63600 -17.39200 1.000 70.35000  ? 784  THR   A O   1 
ATOM   1911 C  CB  . THR   A 1 258 ? -18.53800 15.53100 -15.89000 1.000 57.06000  ? 784  THR   A CB  1 
ATOM   1912 O  OG1 . THR   A 1 258 ? -18.56600 16.96300 -15.94000 1.000 52.39000  ? 784  THR   A OG1 1 
ATOM   1913 C  CG2 . THR   A 1 258 ? -17.09800 15.06300 -15.73600 1.000 58.68000  ? 784  THR   A CG2 1 
ATOM   1914 N  N   . GLU   A 1 259 ? -20.57800 13.11600 -16.43800 1.000 57.59000  ? 785  GLU   A N   1 
ATOM   1915 C  CA  . GLU   A 1 259 ? -20.89800 11.71300 -16.20200 1.000 57.20000  ? 785  GLU   A CA  1 
ATOM   1916 C  C   . GLU   A 1 259 ? -21.30800 11.00500 -17.48800 1.000 66.33000  ? 785  GLU   A C   1 
ATOM   1917 O  O   . GLU   A 1 259 ? -20.97300 9.83200  -17.68800 1.000 68.98000  ? 785  GLU   A O   1 
ATOM   1918 C  CB  . GLU   A 1 259 ? -22.00700 11.60500 -15.15400 1.000 55.20000  ? 785  GLU   A CB  1 
ATOM   1919 C  CG  . GLU   A 1 259 ? -22.40100 10.18400 -14.79100 1.000 57.88000  ? 785  GLU   A CG  1 
ATOM   1920 C  CD  . GLU   A 1 259 ? -23.49200 10.14200 -13.73800 1.000 55.80000  ? 785  GLU   A CD  1 
ATOM   1921 O  OE1 . GLU   A 1 259 ? -23.48400 11.00600 -12.83600 1.000 48.09000  ? 785  GLU   A OE1 1 
ATOM   1922 O  OE2 . GLU   A 1 259 ? -24.36000 9.24700  -13.81300 1.000 56.47000  ? 785  GLU   A OE2 1 
ATOM   1923 N  N   . PHE   A 1 260 ? -22.02600 11.70000 -18.37000 1.000 63.89000  ? 786  PHE   A N   1 
ATOM   1924 C  CA  . PHE   A 1 260 ? -22.51000 11.10100 -19.60700 1.000 71.37000  ? 786  PHE   A CA  1 
ATOM   1925 C  C   . PHE   A 1 260 ? -21.45700 11.08500 -20.70800 1.000 74.73000  ? 786  PHE   A C   1 
ATOM   1926 O  O   . PHE   A 1 260 ? -21.64000 10.37700 -21.70500 1.000 80.91000  ? 786  PHE   A O   1 
ATOM   1927 C  CB  . PHE   A 1 260 ? -23.75800 11.84400 -20.10200 1.000 69.04000  ? 786  PHE   A CB  1 
ATOM   1928 C  CG  . PHE   A 1 260 ? -24.98200 11.64500 -19.23700 1.000 80.41000  ? 786  PHE   A CG  1 
ATOM   1929 C  CD1 . PHE   A 1 260 ? -24.98200 12.02000 -17.90200 1.000 69.61000  ? 786  PHE   A CD1 1 
ATOM   1930 C  CD2 . PHE   A 1 260 ? -26.13800 11.09700 -19.76700 1.000 82.18000  ? 786  PHE   A CD2 1 
ATOM   1931 C  CE1 . PHE   A 1 260 ? -26.10100 11.84700 -17.11200 1.000 60.61000  ? 786  PHE   A CE1 1 
ATOM   1932 C  CE2 . PHE   A 1 260 ? -27.26400 10.92100 -18.98000 1.000 78.77000  ? 786  PHE   A CE2 1 
ATOM   1933 C  CZ  . PHE   A 1 260 ? -27.24500 11.29800 -17.65100 1.000 60.34000  ? 786  PHE   A CZ  1 
ATOM   1934 N  N   . PHE   A 1 261 ? -20.36900 11.84000 -20.55500 1.000 75.79000  ? 787  PHE   A N   1 
ATOM   1935 C  CA  . PHE   A 1 261 ? -19.29500 11.88300 -21.54300 1.000 77.59000  ? 787  PHE   A CA  1 
ATOM   1936 C  C   . PHE   A 1 261 ? -18.03800 11.20500 -21.00900 1.000 82.84000  ? 787  PHE   A C   1 
ATOM   1937 O  O   . PHE   A 1 261 ? -17.62100 10.17200 -21.53800 1.000 89.31000  ? 787  PHE   A O   1 
ATOM   1938 C  CB  . PHE   A 1 261 ? -18.98700 13.32700 -21.95000 1.000 80.22000  ? 787  PHE   A CB  1 
ATOM   1939 C  CG  . PHE   A 1 261 ? -20.08600 14.00100 -22.71900 1.000 68.99000  ? 787  PHE   A CG  1 
ATOM   1940 C  CD1 . PHE   A 1 261 ? -21.07100 13.26400 -23.35300 1.000 75.48000  ? 787  PHE   A CD1 1 
ATOM   1941 C  CD2 . PHE   A 1 261 ? -20.12400 15.38300 -22.81300 1.000 75.73000  ? 787  PHE   A CD2 1 
ATOM   1942 C  CE1 . PHE   A 1 261 ? -22.07700 13.89400 -24.06100 1.000 73.95000  ? 787  PHE   A CE1 1 
ATOM   1943 C  CE2 . PHE   A 1 261 ? -21.12500 16.01700 -23.51800 1.000 77.39000  ? 787  PHE   A CE2 1 
ATOM   1944 C  CZ  . PHE   A 1 261 ? -22.10200 15.27200 -24.14300 1.000 70.63000  ? 787  PHE   A CZ  1 
ATOM   1945 N  N   . ASP   A 1 262 ? -17.42300 11.75900 -19.96200 1.000 81.51000  ? 788  ASP   A N   1 
ATOM   1946 C  CA  . ASP   A 1 262 ? -16.07800 11.38900 -19.53100 1.000 89.13000  ? 788  ASP   A CA  1 
ATOM   1947 C  C   . ASP   A 1 262 ? -16.00800 10.05700 -18.79500 1.000 89.66000  ? 788  ASP   A C   1 
ATOM   1948 O  O   . ASP   A 1 262 ? -14.90300 9.67500  -18.38800 1.000 100.52000 ? 788  ASP   A O   1 
ATOM   1949 C  CB  . ASP   A 1 262 ? -15.50100 12.48700 -18.63500 1.000 84.97000  ? 788  ASP   A CB  1 
ATOM   1950 C  CG  . ASP   A 1 262 ? -15.00400 13.68300 -19.42100 1.000 95.71000  ? 788  ASP   A CG  1 
ATOM   1951 O  OD1 . ASP   A 1 262 ? -14.53100 13.49600 -20.56300 1.000 101.31000 ? 788  ASP   A OD1 1 
ATOM   1952 O  OD2 . ASP   A 1 262 ? -15.08000 14.81100 -18.89100 1.000 94.18000  ? 788  ASP   A OD2 1 
ATOM   1953 N  N   . GLN   A 1 263 ? -17.13000 9.35600  -18.60400 1.000 77.42000  ? 789  GLN   A N   1 
ATOM   1954 C  CA  . GLN   A 1 263 ? -17.14500 8.09300  -17.86000 1.000 90.82000  ? 789  GLN   A CA  1 
ATOM   1955 C  C   . GLN   A 1 263 ? -16.64700 8.30600  -16.42600 1.000 98.55000  ? 789  GLN   A C   1 
ATOM   1956 O  O   . GLN   A 1 263 ? -15.97300 7.45500  -15.84400 1.000 106.64000 ? 789  GLN   A O   1 
ATOM   1957 C  CB  . GLN   A 1 263 ? -16.32300 7.02400  -18.59500 1.000 100.21000 ? 789  GLN   A CB  1 
ATOM   1958 C  CG  . GLN   A 1 263 ? -16.34700 5.60600  -18.02800 1.000 102.15000 ? 789  GLN   A CG  1 
ATOM   1959 C  CD  . GLN   A 1 263 ? -14.95100 5.13300  -17.69100 1.000 104.98000 ? 789  GLN   A CD  1 
ATOM   1960 O  OE1 . GLN   A 1 263 ? -13.97400 5.63300  -18.24400 1.000 99.29000  ? 789  GLN   A OE1 1 
ATOM   1961 N  NE2 . GLN   A 1 263 ? -14.84300 4.19700  -16.75400 1.000 102.84000 ? 789  GLN   A NE2 1 
ATOM   1962 N  N   . GLY   A 1 264 ? -16.97700 9.46200  -15.85100 1.000 93.75000  ? 790  GLY   A N   1 
ATOM   1963 C  CA  . GLY   A 1 264 ? -16.52200 9.81700  -14.51400 1.000 79.20000  ? 790  GLY   A CA  1 
ATOM   1964 C  C   . GLY   A 1 264 ? -17.41200 10.81400 -13.79400 1.000 75.63000  ? 790  GLY   A C   1 
ATOM   1965 O  O   . GLY   A 1 264 ? -18.57200 10.52900 -13.49500 1.000 66.59000  ? 790  GLY   A O   1 
ATOM   1966 N  N   . ASN   A 1 285 ? -19.89500 22.24500 -24.68500 1.000 75.63000  ? 811  ASN   A N   1 
ATOM   1967 C  CA  . ASN   A 1 285 ? -19.76800 21.07700 -25.54800 1.000 95.96000  ? 811  ASN   A CA  1 
ATOM   1968 C  C   . ASN   A 1 285 ? -21.11400 20.37400 -25.70500 1.000 94.49000  ? 811  ASN   A C   1 
ATOM   1969 O  O   . ASN   A 1 285 ? -21.46400 19.50900 -24.90200 1.000 93.37000  ? 811  ASN   A O   1 
ATOM   1970 C  CB  . ASN   A 1 285 ? -18.72200 20.10900 -24.98900 1.000 86.35000  ? 811  ASN   A CB  1 
ATOM   1971 C  CG  . ASN   A 1 285 ? -18.43200 18.95600 -25.93000 1.000 94.64000  ? 811  ASN   A CG  1 
ATOM   1972 O  OD1 . ASN   A 1 285 ? -19.16900 17.97100 -25.97300 1.000 92.24000  ? 811  ASN   A OD1 1 
ATOM   1973 N  ND2 . ASN   A 1 285 ? -17.35200 19.07600 -26.69400 1.000 84.24000  ? 811  ASN   A ND2 1 
ATOM   1974 N  N   . LYS   A 1 286 ? -21.86500 20.76400 -26.74000 1.000 83.90000  ? 812  LYS   A N   1 
ATOM   1975 C  CA  . LYS   A 1 286 ? -23.18100 20.20900 -27.06200 1.000 76.56000  ? 812  LYS   A CA  1 
ATOM   1976 C  C   . LYS   A 1 286 ? -24.21900 20.46900 -25.97100 1.000 70.23000  ? 812  LYS   A C   1 
ATOM   1977 O  O   . LYS   A 1 286 ? -25.41100 20.22700 -26.18100 1.000 65.57000  ? 812  LYS   A O   1 
ATOM   1978 C  CB  . LYS   A 1 286 ? -23.09800 18.69900 -27.33000 1.000 71.80000  ? 812  LYS   A CB  1 
ATOM   1979 C  CG  . LYS   A 1 286 ? -21.85600 18.22800 -28.07400 1.000 81.86000  ? 812  LYS   A CG  1 
ATOM   1980 C  CD  . LYS   A 1 286 ? -22.01000 16.78500 -28.52600 1.000 82.31000  ? 812  LYS   A CD  1 
ATOM   1981 C  CE  . LYS   A 1 286 ? -20.66000 16.12500 -28.75600 1.000 90.79000  ? 812  LYS   A CE  1 
ATOM   1982 N  NZ  . LYS   A 1 286 ? -20.76900 14.63900 -28.81500 1.000 79.16000  ? 812  LYS   A NZ  1 
ATOM   1983 N  N   . ILE   A 1 287 ? -23.78100 20.98300 -24.81800 1.000 59.29000  ? 813  ILE   A N   1 
ATOM   1984 C  CA  . ILE   A 1 287 ? -24.66400 21.03700 -23.65000 1.000 56.91000  ? 813  ILE   A CA  1 
ATOM   1985 C  C   . ILE   A 1 287 ? -25.87100 21.95400 -23.85500 1.000 53.63000  ? 813  ILE   A C   1 
ATOM   1986 O  O   . ILE   A 1 287 ? -26.98700 21.53200 -23.50300 1.000 52.71000  ? 813  ILE   A O   1 
ATOM   1987 C  CB  . ILE   A 1 287 ? -23.84300 21.42200 -22.39300 1.000 53.48000  ? 813  ILE   A CB  1 
ATOM   1988 C  CG1 . ILE   A 1 287 ? -22.83300 20.32200 -22.07200 1.000 56.92000  ? 813  ILE   A CG1 1 
ATOM   1989 C  CG2 . ILE   A 1 287 ? -24.76500 21.66100 -21.21000 1.000 47.55000  ? 813  ILE   A CG2 1 
ATOM   1990 C  CD1 . ILE   A 1 287 ? -21.50200 20.84500 -21.58200 1.000 66.05000  ? 813  ILE   A CD1 1 
ATOM   1991 N  N   . PRO   A 1 288 ? -25.73400 23.17400 -24.38200 1.000 56.96000  ? 814  PRO   A N   1 
ATOM   1992 C  CA  . PRO   A 1 288 ? -26.93000 24.03500 -24.50000 1.000 55.92000  ? 814  PRO   A CA  1 
ATOM   1993 C  C   . PRO   A 1 288 ? -28.05800 23.40300 -25.29400 1.000 45.22000  ? 814  PRO   A C   1 
ATOM   1994 O  O   . PRO   A 1 288 ? -29.21800 23.44700 -24.86100 1.000 57.62000  ? 814  PRO   A O   1 
ATOM   1995 C  CB  . PRO   A 1 288 ? -26.38100 25.29600 -25.18300 1.000 47.36000  ? 814  PRO   A CB  1 
ATOM   1996 C  CG  . PRO   A 1 288 ? -24.95300 25.32900 -24.80400 1.000 48.25000  ? 814  PRO   A CG  1 
ATOM   1997 C  CD  . PRO   A 1 288 ? -24.51700 23.89500 -24.80100 1.000 50.15000  ? 814  PRO   A CD  1 
ATOM   1998 N  N   . SER   A 1 289 ? -27.74800 22.81000 -26.44900 1.000 53.21000  ? 815  SER   A N   1 
ATOM   1999 C  CA  . SER   A 1 289 ? -28.78000 22.16100 -27.25100 1.000 57.00000  ? 815  SER   A CA  1 
ATOM   2000 C  C   . SER   A 1 289 ? -29.45900 21.03900 -26.47500 1.000 57.15000  ? 815  SER   A C   1 
ATOM   2001 O  O   . SER   A 1 289 ? -30.68300 20.87700 -26.54600 1.000 51.10000  ? 815  SER   A O   1 
ATOM   2002 C  CB  . SER   A 1 289 ? -28.17600 21.62300 -28.54800 1.000 56.77000  ? 815  SER   A CB  1 
ATOM   2003 O  OG  . SER   A 1 289 ? -29.14400 21.58200 -29.58400 1.000 84.13000  ? 815  SER   A OG  1 
ATOM   2004 N  N   . MET   A 1 290 ? -28.68300 20.26300 -25.71700 1.000 51.45000  ? 816  MET   A N   1 
ATOM   2005 C  CA  . MET   A 1 290 ? -29.23700 19.12400 -24.99700 1.000 50.70000  ? 816  MET   A CA  1 
ATOM   2006 C  C   . MET   A 1 290 ? -30.05300 19.54700 -23.78300 1.000 45.46000  ? 816  MET   A C   1 
ATOM   2007 O  O   . MET   A 1 290 ? -30.96900 18.82400 -23.37700 1.000 52.00000  ? 816  MET   A O   1 
ATOM   2008 C  CB  . MET   A 1 290 ? -28.11000 18.18000 -24.58200 1.000 49.40000  ? 816  MET   A CB  1 
ATOM   2009 C  CG  . MET   A 1 290 ? -27.32600 17.63300 -25.76300 1.000 56.57000  ? 816  MET   A CG  1 
ATOM   2010 S  SD  . MET   A 1 290 ? -26.36800 16.16500 -25.36000 1.000 73.05000  ? 816  MET   A SD  1 
ATOM   2011 C  CE  . MET   A 1 290 ? -25.19400 16.84700 -24.19600 1.000 64.68000  ? 816  MET   A CE  1 
ATOM   2012 N  N   . GLN   A 1 291 ? -29.74700 20.70500 -23.19500 1.000 44.33000  ? 817  GLN   A N   1 
ATOM   2013 C  CA  . GLN   A 1 291 ? -30.54800 21.18400 -22.07300 1.000 45.10000  ? 817  GLN   A CA  1 
ATOM   2014 C  C   . GLN   A 1 291 ? -31.89100 21.72200 -22.54700 1.000 49.78000  ? 817  GLN   A C   1 
ATOM   2015 O  O   . GLN   A 1 291 ? -32.91300 21.53000 -21.87800 1.000 48.79000  ? 817  GLN   A O   1 
ATOM   2016 C  CB  . GLN   A 1 291 ? -29.78200 22.25200 -21.29400 1.000 56.51000  ? 817  GLN   A CB  1 
ATOM   2017 C  CG  . GLN   A 1 291 ? -28.58300 21.71900 -20.52400 1.000 45.65000  ? 817  GLN   A CG  1 
ATOM   2018 C  CD  . GLN   A 1 291 ? -28.96000 20.63500 -19.53200 1.000 50.19000  ? 817  GLN   A CD  1 
ATOM   2019 O  OE1 . GLN   A 1 291 ? -28.97300 19.45100 -19.86500 1.000 61.83000  ? 817  GLN   A OE1 1 
ATOM   2020 N  NE2 . GLN   A 1 291 ? -29.26600 21.03600 -18.30400 1.000 44.45000  ? 817  GLN   A NE2 1 
ATOM   2021 N  N   . VAL   A 1 292 ? -31.91100 22.39100 -23.70200 1.000 47.25000  ? 818  VAL   A N   1 
ATOM   2022 C  CA  . VAL   A 1 292 ? -33.16600 22.90800 -24.23900 1.000 43.18000  ? 818  VAL   A CA  1 
ATOM   2023 C  C   . VAL   A 1 292 ? -34.09600 21.76200 -24.62000 1.000 39.31000  ? 818  VAL   A C   1 
ATOM   2024 O  O   . VAL   A 1 292 ? -35.30200 21.80700 -24.34700 1.000 36.71000  ? 818  VAL   A O   1 
ATOM   2025 C  CB  . VAL   A 1 292 ? -32.89100 23.83800 -25.43500 1.000 49.17000  ? 818  VAL   A CB  1 
ATOM   2026 C  CG1 . VAL   A 1 292 ? -34.19400 24.24600 -26.10400 1.000 32.60000  ? 818  VAL   A CG1 1 
ATOM   2027 C  CG2 . VAL   A 1 292 ? -32.11100 25.06300 -24.98500 1.000 45.95000  ? 818  VAL   A CG2 1 
ATOM   2028 N  N   . GLY   A 1 293 ? -33.55400 20.71700 -25.24900 1.000 40.10000  ? 819  GLY   A N   1 
ATOM   2029 C  CA  . GLY   A 1 293 ? -34.37500 19.57000 -25.60000 1.000 42.95000  ? 819  GLY   A CA  1 
ATOM   2030 C  C   . GLY   A 1 293 ? -34.90100 18.83400 -24.38200 1.000 44.75000  ? 819  GLY   A C   1 
ATOM   2031 O  O   . GLY   A 1 293 ? -36.05700 18.40100 -24.35800 1.000 48.04000  ? 819  GLY   A O   1 
ATOM   2032 N  N   . PHE   A 1 294 ? -34.06100 18.68200 -23.35500 1.000 51.70000  ? 820  PHE   A N   1 
ATOM   2033 C  CA  . PHE   A 1 294 ? -34.50900 18.06200 -22.11300 1.000 38.76000  ? 820  PHE   A CA  1 
ATOM   2034 C  C   . PHE   A 1 294 ? -35.57800 18.90100 -21.42400 1.000 42.25000  ? 820  PHE   A C   1 
ATOM   2035 O  O   . PHE   A 1 294 ? -36.49700 18.35100 -20.80700 1.000 50.26000  ? 820  PHE   A O   1 
ATOM   2036 C  CB  . PHE   A 1 294 ? -33.31500 17.84300 -21.18200 1.000 50.62000  ? 820  PHE   A CB  1 
ATOM   2037 C  CG  . PHE   A 1 294 ? -33.65700 17.12200 -19.90800 1.000 53.08000  ? 820  PHE   A CG  1 
ATOM   2038 C  CD1 . PHE   A 1 294 ? -34.00200 15.78100 -19.92600 1.000 54.82000  ? 820  PHE   A CD1 1 
ATOM   2039 C  CD2 . PHE   A 1 294 ? -33.62300 17.78400 -18.69100 1.000 49.89000  ? 820  PHE   A CD2 1 
ATOM   2040 C  CE1 . PHE   A 1 294 ? -34.31400 15.11400 -18.75600 1.000 54.98000  ? 820  PHE   A CE1 1 
ATOM   2041 C  CE2 . PHE   A 1 294 ? -33.93200 17.12100 -17.51600 1.000 56.16000  ? 820  PHE   A CE2 1 
ATOM   2042 C  CZ  . PHE   A 1 294 ? -34.28000 15.78500 -17.54900 1.000 50.64000  ? 820  PHE   A CZ  1 
ATOM   2043 N  N   . ILE   A 1 295 ? -35.47800 20.22900 -21.52300 1.000 48.68000  ? 821  ILE   A N   1 
ATOM   2044 C  CA  . ILE   A 1 295 ? -36.48800 21.09900 -20.92900 1.000 43.88000  ? 821  ILE   A CA  1 
ATOM   2045 C  C   . ILE   A 1 295 ? -37.79200 21.01600 -21.71300 1.000 49.32000  ? 821  ILE   A C   1 
ATOM   2046 O  O   . ILE   A 1 295 ? -38.88300 20.98300 -21.13000 1.000 45.12000  ? 821  ILE   A O   1 
ATOM   2047 C  CB  . ILE   A 1 295 ? -35.96000 22.54400 -20.84900 1.000 48.82000  ? 821  ILE   A CB  1 
ATOM   2048 C  CG1 . ILE   A 1 295 ? -34.88800 22.66100 -19.76700 1.000 48.86000  ? 821  ILE   A CG1 1 
ATOM   2049 C  CG2 . ILE   A 1 295 ? -37.08300 23.52200 -20.56500 1.000 38.26000  ? 821  ILE   A CG2 1 
ATOM   2050 C  CD1 . ILE   A 1 295 ? -34.25000 24.03200 -19.68700 1.000 38.75000  ? 821  ILE   A CD1 1 
ATOM   2051 N  N   . ASP   A 1 296 ? -37.70200 20.96800 -23.04400 1.000 50.23000  ? 822  ASP   A N   1 
ATOM   2052 C  CA  . ASP   A 1 296 ? -38.90600 20.91600 -23.86700 1.000 53.98000  ? 822  ASP   A CA  1 
ATOM   2053 C  C   . ASP   A 1 296 ? -39.64000 19.59100 -23.70300 1.000 53.52000  ? 822  ASP   A C   1 
ATOM   2054 O  O   . ASP   A 1 296 ? -40.87200 19.56600 -23.58900 1.000 50.95000  ? 822  ASP   A O   1 
ATOM   2055 C  CB  . ASP   A 1 296 ? -38.54700 21.14300 -25.33600 1.000 59.08000  ? 822  ASP   A CB  1 
ATOM   2056 C  CG  . ASP   A 1 296 ? -38.26800 22.59900 -25.65200 1.000 53.02000  ? 822  ASP   A CG  1 
ATOM   2057 O  OD1 . ASP   A 1 296 ? -38.68900 23.47200 -24.86500 1.000 48.94000  ? 822  ASP   A OD1 1 
ATOM   2058 O  OD2 . ASP   A 1 296 ? -37.62700 22.86800 -26.69100 1.000 55.72000  ? 822  ASP   A OD2 1 
ATOM   2059 N  N   . ALA   A 1 297 ? -38.90400 18.47800 -23.67900 1.000 47.83000  ? 823  ALA   A N   1 
ATOM   2060 C  CA  . ALA   A 1 297 ? -39.53700 17.16700 -23.74700 1.000 50.12000  ? 823  ALA   A CA  1 
ATOM   2061 C  C   . ALA   A 1 297 ? -40.02100 16.66900 -22.39000 1.000 54.21000  ? 823  ALA   A C   1 
ATOM   2062 O  O   . ALA   A 1 297 ? -40.97300 15.88300 -22.33300 1.000 64.82000  ? 823  ALA   A O   1 
ATOM   2063 C  CB  . ALA   A 1 297 ? -38.57000 16.15200 -24.36000 1.000 38.77000  ? 823  ALA   A CB  1 
ATOM   2064 N  N   . ILE   A 1 298 ? -39.40300 17.11200 -21.29400 1.000 53.89000  ? 824  ILE   A N   1 
ATOM   2065 C  CA  . ILE   A 1 298 ? -39.59000 16.50400 -19.98100 1.000 40.02000  ? 824  ILE   A CA  1 
ATOM   2066 C  C   . ILE   A 1 298 ? -40.11400 17.50900 -18.95700 1.000 54.84000  ? 824  ILE   A C   1 
ATOM   2067 O  O   . ILE   A 1 298 ? -41.15700 17.28700 -18.33200 1.000 50.94000  ? 824  ILE   A O   1 
ATOM   2068 C  CB  . ILE   A 1 298 ? -38.28500 15.84500 -19.47500 1.000 43.50000  ? 824  ILE   A CB  1 
ATOM   2069 C  CG1 . ILE   A 1 298 ? -37.74700 14.85400 -20.50500 1.000 41.32000  ? 824  ILE   A CG1 1 
ATOM   2070 C  CG2 . ILE   A 1 298 ? -38.51400 15.14600 -18.14500 1.000 47.49000  ? 824  ILE   A CG2 1 
ATOM   2071 C  CD1 . ILE   A 1 298 ? -38.62800 13.64400 -20.70800 1.000 42.22000  ? 824  ILE   A CD1 1 
ATOM   2072 N  N   . CYS   A 1 299 ? -39.39700 18.61600 -18.76300 1.000 46.46000  ? 825  CYS   A N   1 
ATOM   2073 C  CA  . CYS   A 1 299 ? -39.55900 19.41300 -17.54800 1.000 45.73000  ? 825  CYS   A CA  1 
ATOM   2074 C  C   . CYS   A 1 299 ? -40.65800 20.46700 -17.63400 1.000 46.16000  ? 825  CYS   A C   1 
ATOM   2075 O  O   . CYS   A 1 299 ? -41.37100 20.68000 -16.64800 1.000 47.06000  ? 825  CYS   A O   1 
ATOM   2076 C  CB  . CYS   A 1 299 ? -38.23500 20.09300 -17.19100 1.000 42.19000  ? 825  CYS   A CB  1 
ATOM   2077 S  SG  . CYS   A 1 299 ? -36.80100 19.01500 -17.33800 1.000 45.02000  ? 825  CYS   A SG  1 
ATOM   2078 N  N   . LEU   A 1 300 ? -40.80600 21.13900 -18.78000 1.000 45.93000  ? 826  LEU   A N   1 
ATOM   2079 C  CA  . LEU   A 1 300 ? -41.70600 22.29000 -18.86100 1.000 45.96000  ? 826  LEU   A CA  1 
ATOM   2080 C  C   . LEU   A 1 300 ? -43.13100 21.92100 -18.46200 1.000 50.69000  ? 826  LEU   A C   1 
ATOM   2081 O  O   . LEU   A 1 300 ? -43.73200 22.56800 -17.59500 1.000 49.12000  ? 826  LEU   A O   1 
ATOM   2082 C  CB  . LEU   A 1 300 ? -41.68000 22.87900 -20.27100 1.000 55.70000  ? 826  LEU   A CB  1 
ATOM   2083 C  CG  . LEU   A 1 300 ? -40.60100 23.92700 -20.55100 1.000 56.36000  ? 826  LEU   A CG  1 
ATOM   2084 C  CD1 . LEU   A 1 300 ? -40.72400 24.46300 -21.96900 1.000 58.38000  ? 826  LEU   A CD1 1 
ATOM   2085 C  CD2 . LEU   A 1 300 ? -40.65900 25.06000 -19.53500 1.000 50.71000  ? 826  LEU   A CD2 1 
ATOM   2086 N  N   . GLN   A 1 301 ? -43.68900 20.88100 -19.08500 1.000 47.07000  ? 827  GLN   A N   1 
ATOM   2087 C  CA  . GLN   A 1 301 ? -45.05900 20.48500 -18.77200 1.000 64.45000  ? 827  GLN   A CA  1 
ATOM   2088 C  C   . GLN   A 1 301 ? -45.18000 19.98900 -17.33700 1.000 64.72000  ? 827  GLN   A C   1 
ATOM   2089 O  O   . GLN   A 1 301 ? -46.19300 20.23500 -16.67100 1.000 62.78000  ? 827  GLN   A O   1 
ATOM   2090 C  CB  . GLN   A 1 301 ? -45.53000 19.40800 -19.75000 1.000 65.27000  ? 827  GLN   A CB  1 
ATOM   2091 C  CG  . GLN   A 1 301 ? -45.09500 19.63500 -21.18700 1.000 68.27000  ? 827  GLN   A CG  1 
ATOM   2092 C  CD  . GLN   A 1 301 ? -44.09100 18.60300 -21.65900 1.000 78.11000  ? 827  GLN   A CD  1 
ATOM   2093 O  OE1 . GLN   A 1 301 ? -42.97200 18.52900 -21.14900 1.000 72.13000  ? 827  GLN   A OE1 1 
ATOM   2094 N  NE2 . GLN   A 1 301 ? -44.48700 17.79500 -22.63700 1.000 66.40000  ? 827  GLN   A NE2 1 
ATOM   2095 N  N   . LEU   A 1 302 ? -44.15500 19.28900 -16.84300 1.000 56.56000  ? 828  LEU   A N   1 
ATOM   2096 C  CA  . LEU   A 1 302 ? -44.20500 18.75200 -15.48600 1.000 45.93000  ? 828  LEU   A CA  1 
ATOM   2097 C  C   . LEU   A 1 302 ? -44.32100 19.86800 -14.45700 1.000 51.11000  ? 828  LEU   A C   1 
ATOM   2098 O  O   . LEU   A 1 302 ? -45.20400 19.84200 -13.59100 1.000 49.09000  ? 828  LEU   A O   1 
ATOM   2099 C  CB  . LEU   A 1 302 ? -42.96700 17.89700 -15.21500 1.000 55.35000  ? 828  LEU   A CB  1 
ATOM   2100 C  CG  . LEU   A 1 302 ? -42.74100 17.47000 -13.76300 1.000 49.30000  ? 828  LEU   A CG  1 
ATOM   2101 C  CD1 . LEU   A 1 302 ? -43.89200 16.60600 -13.26500 1.000 46.59000  ? 828  LEU   A CD1 1 
ATOM   2102 C  CD2 . LEU   A 1 302 ? -41.41800 16.73800 -13.62600 1.000 45.27000  ? 828  LEU   A CD2 1 
ATOM   2103 N  N   . TYR   A 1 303 ? -43.43400 20.86200 -14.53600 1.000 49.50000  ? 829  TYR   A N   1 
ATOM   2104 C  CA  . TYR   A 1 303 ? -43.50500 21.97600 -13.59800 1.000 46.50000  ? 829  TYR   A CA  1 
ATOM   2105 C  C   . TYR   A 1 303 ? -44.72400 22.85000 -13.86100 1.000 50.63000  ? 829  TYR   A C   1 
ATOM   2106 O  O   . TYR   A 1 303 ? -45.23200 23.49200 -12.93700 1.000 51.04000  ? 829  TYR   A O   1 
ATOM   2107 C  CB  . TYR   A 1 303 ? -42.21800 22.79700 -13.66000 1.000 48.32000  ? 829  TYR   A CB  1 
ATOM   2108 C  CG  . TYR   A 1 303 ? -41.00800 22.02300 -13.19000 1.000 37.37000  ? 829  TYR   A CG  1 
ATOM   2109 C  CD1 . TYR   A 1 303 ? -40.89800 21.60800 -11.86900 1.000 44.09000  ? 829  TYR   A CD1 1 
ATOM   2110 C  CD2 . TYR   A 1 303 ? -39.98700 21.69100 -14.06800 1.000 35.37000  ? 829  TYR   A CD2 1 
ATOM   2111 C  CE1 . TYR   A 1 303 ? -39.80000 20.89200 -11.43400 1.000 32.55000  ? 829  TYR   A CE1 1 
ATOM   2112 C  CE2 . TYR   A 1 303 ? -38.88500 20.97400 -13.64300 1.000 48.28000  ? 829  TYR   A CE2 1 
ATOM   2113 C  CZ  . TYR   A 1 303 ? -38.79700 20.57800 -12.32500 1.000 37.22000  ? 829  TYR   A CZ  1 
ATOM   2114 O  OH  . TYR   A 1 303 ? -37.70100 19.86500 -11.89700 1.000 30.68000  ? 829  TYR   A OH  1 
ATOM   2115 N  N   . GLU   A 1 304 ? -45.21100 22.88200 -15.10400 1.000 56.33000  ? 830  GLU   A N   1 
ATOM   2116 C  CA  . GLU   A 1 304 ? -46.47200 23.56300 -15.38000 1.000 63.47000  ? 830  GLU   A CA  1 
ATOM   2117 C  C   . GLU   A 1 304 ? -47.62800 22.87700 -14.66400 1.000 61.38000  ? 830  GLU   A C   1 
ATOM   2118 O  O   . GLU   A 1 304 ? -48.48500 23.54300 -14.06900 1.000 58.25000  ? 830  GLU   A O   1 
ATOM   2119 C  CB  . GLU   A 1 304 ? -46.73000 23.60900 -16.88600 1.000 65.92000  ? 830  GLU   A CB  1 
ATOM   2120 C  CG  . GLU   A 1 304 ? -46.16700 24.83600 -17.58100 1.000 66.34000  ? 830  GLU   A CG  1 
ATOM   2121 C  CD  . GLU   A 1 304 ? -46.34000 24.78300 -19.08600 1.000 73.27000  ? 830  GLU   A CD  1 
ATOM   2122 O  OE1 . GLU   A 1 304 ? -45.57000 25.46100 -19.79900 1.000 63.90000  ? 830  GLU   A OE1 1 
ATOM   2123 O  OE2 . GLU   A 1 304 ? -47.24600 24.06300 -19.55700 1.000 77.03000  ? 830  GLU   A OE2 1 
ATOM   2124 N  N   . ALA   A 1 305 ? -47.66700 21.54300 -14.70800 1.000 57.73000  ? 831  ALA   A N   1 
ATOM   2125 C  CA  . ALA   A 1 305 ? -48.72600 20.80800 -14.02800 1.000 49.30000  ? 831  ALA   A CA  1 
ATOM   2126 C  C   . ALA   A 1 305 ? -48.60100 20.91100 -12.51300 1.000 59.61000  ? 831  ALA   A C   1 
ATOM   2127 O  O   . ALA   A 1 305 ? -49.61600 20.89900 -11.80800 1.000 64.80000  ? 831  ALA   A O   1 
ATOM   2128 C  CB  . ALA   A 1 305 ? -48.71000 19.34300 -14.46400 1.000 48.74000  ? 831  ALA   A CB  1 
ATOM   2129 N  N   . LEU   A 1 306 ? -47.37400 21.01600 -11.99700 1.000 59.70000  ? 832  LEU   A N   1 
ATOM   2130 C  CA  . LEU   A 1 306 ? -47.18600 21.10500 -10.55300 1.000 51.29000  ? 832  LEU   A CA  1 
ATOM   2131 C  C   . LEU   A 1 306 ? -47.72000 22.42200 -10.00300 1.000 58.74000  ? 832  LEU   A C   1 
ATOM   2132 O  O   . LEU   A 1 306 ? -48.26400 22.46200 -8.89300  1.000 57.25000  ? 832  LEU   A O   1 
ATOM   2133 C  CB  . LEU   A 1 306 ? -45.70700 20.93700 -10.20600 1.000 49.17000  ? 832  LEU   A CB  1 
ATOM   2134 C  CG  . LEU   A 1 306 ? -45.34700 20.97300 -8.71900  1.000 52.12000  ? 832  LEU   A CG  1 
ATOM   2135 C  CD1 . LEU   A 1 306 ? -46.10100 19.89500 -7.95700  1.000 45.15000  ? 832  LEU   A CD1 1 
ATOM   2136 C  CD2 . LEU   A 1 306 ? -43.84500 20.82100 -8.52400  1.000 55.48000  ? 832  LEU   A CD2 1 
ATOM   2137 N  N   . THR   A 1 307 ? -47.57800 23.51000 -10.76300 1.000 63.45000  ? 833  THR   A N   1 
ATOM   2138 C  CA  . THR   A 1 307 ? -48.07900 24.80200 -10.30700 1.000 64.16000  ? 833  THR   A CA  1 
ATOM   2139 C  C   . THR   A 1 307 ? -49.59500 24.88900 -10.39600 1.000 65.72000  ? 833  THR   A C   1 
ATOM   2140 O  O   . THR   A 1 307 ? -50.21600 25.60700 -9.60500  1.000 61.14000  ? 833  THR   A O   1 
ATOM   2141 C  CB  . THR   A 1 307 ? -47.44300 25.93400 -11.11300 1.000 59.12000  ? 833  THR   A CB  1 
ATOM   2142 O  OG1 . THR   A 1 307 ? -47.88100 25.86000 -12.47500 1.000 73.88000  ? 833  THR   A OG1 1 
ATOM   2143 C  CG2 . THR   A 1 307 ? -45.93500 25.82200 -11.06800 1.000 53.32000  ? 833  THR   A CG2 1 
ATOM   2144 N  N   . HIS   A 1 308 ? -50.20600 24.18300 -11.35000 1.000 58.91000  ? 834  HIS   A N   1 
ATOM   2145 C  CA  . HIS   A 1 308 ? -51.66200 24.09700 -11.37200 1.000 67.54000  ? 834  HIS   A CA  1 
ATOM   2146 C  C   . HIS   A 1 308 ? -52.18500 23.43400 -10.10500 1.000 66.75000  ? 834  HIS   A C   1 
ATOM   2147 O  O   . HIS   A 1 308 ? -53.22100 23.83800 -9.56400  1.000 69.72000  ? 834  HIS   A O   1 
ATOM   2148 C  CB  . HIS   A 1 308 ? -52.12700 23.33300 -12.61300 1.000 68.94000  ? 834  HIS   A CB  1 
ATOM   2149 C  CG  . HIS   A 1 308 ? -51.91900 24.07700 -13.89600 1.000 82.09000  ? 834  HIS   A CG  1 
ATOM   2150 N  ND1 . HIS   A 1 308 ? -51.85700 23.44600 -15.11900 1.000 87.36000  ? 834  HIS   A ND1 1 
ATOM   2151 C  CD2 . HIS   A 1 308 ? -51.75900 25.39800 -14.14600 1.000 83.69000  ? 834  HIS   A CD2 1 
ATOM   2152 C  CE1 . HIS   A 1 308 ? -51.66800 24.34500 -16.06800 1.000 89.62000  ? 834  HIS   A CE1 1 
ATOM   2153 N  NE2 . HIS   A 1 308 ? -51.60500 25.53800 -15.50400 1.000 93.28000  ? 834  HIS   A NE2 1 
ATOM   2154 N  N   . VAL   A 1 309 ? -51.47300 22.42100 -9.60900  1.000 61.26000  ? 835  VAL   A N   1 
ATOM   2155 C  CA  . VAL   A 1 309 ? -51.89400 21.74000 -8.38800  1.000 57.26000  ? 835  VAL   A CA  1 
ATOM   2156 C  C   . VAL   A 1 309 ? -51.70000 22.64900 -7.18000  1.000 65.19000  ? 835  VAL   A C   1 
ATOM   2157 O  O   . VAL   A 1 309 ? -52.59000 22.77900 -6.33100  1.000 73.41000  ? 835  VAL   A O   1 
ATOM   2158 C  CB  . VAL   A 1 309 ? -51.13400 20.41000 -8.23100  1.000 60.98000  ? 835  VAL   A CB  1 
ATOM   2159 C  CG1 . VAL   A 1 309 ? -51.52700 19.72200 -6.93900  1.000 56.22000  ? 835  VAL   A CG1 1 
ATOM   2160 C  CG2 . VAL   A 1 309 ? -51.40200 19.49900 -9.42400  1.000 55.81000  ? 835  VAL   A CG2 1 
ATOM   2161 N  N   . SER   A 1 310 ? -50.53900 23.30100 -7.09300  1.000 65.44000  ? 836  SER   A N   1 
ATOM   2162 C  CA  . SER   A 1 310 ? -50.24500 24.24900 -6.01900  1.000 64.94000  ? 836  SER   A CA  1 
ATOM   2163 C  C   . SER   A 1 310 ? -49.51700 25.43700 -6.63100  1.000 65.98000  ? 836  SER   A C   1 
ATOM   2164 O  O   . SER   A 1 310 ? -48.37000 25.30100 -7.07100  1.000 68.75000  ? 836  SER   A O   1 
ATOM   2165 C  CB  . SER   A 1 310 ? -49.40000 23.60900 -4.91400  1.000 59.97000  ? 836  SER   A CB  1 
ATOM   2166 O  OG  . SER   A 1 310 ? -48.57500 24.56000 -4.25800  1.000 66.51000  ? 836  SER   A OG  1 
ATOM   2167 N  N   . GLU   A 1 311 ? -50.17400 26.60200 -6.63200  1.000 67.98000  ? 837  GLU   A N   1 
ATOM   2168 C  CA  . GLU   A 1 311 ? -49.64200 27.78100 -7.30800  1.000 73.01000  ? 837  GLU   A CA  1 
ATOM   2169 C  C   . GLU   A 1 311 ? -48.32100 28.26100 -6.71900  1.000 65.30000  ? 837  GLU   A C   1 
ATOM   2170 O  O   . GLU   A 1 311 ? -47.58300 28.98500 -7.39800  1.000 70.03000  ? 837  GLU   A O   1 
ATOM   2171 C  CB  . GLU   A 1 311 ? -50.66500 28.92100 -7.26100  1.000 79.50000  ? 837  GLU   A CB  1 
ATOM   2172 C  CG  . GLU   A 1 311 ? -50.79700 29.71000 -8.55800  1.000 91.92000  ? 837  GLU   A CG  1 
ATOM   2173 C  CD  . GLU   A 1 311 ? -51.55100 28.95000 -9.63100  1.000 83.07000  ? 837  GLU   A CD  1 
ATOM   2174 O  OE1 . GLU   A 1 311 ? -52.53000 28.24700 -9.29500  1.000 77.90000  ? 837  GLU   A OE1 1 
ATOM   2175 O  OE2 . GLU   A 1 311 ? -51.16000 29.05400 -10.81200 1.000 79.99000  ? 837  GLU   A OE2 1 
ATOM   2176 N  N   . ASP   A 1 312 ? -47.99700 27.87500 -5.48400  1.000 59.28000  ? 838  ASP   A N   1 
ATOM   2177 C  CA  . ASP   A 1 312 ? -46.80600 28.38100 -4.81200  1.000 65.98000  ? 838  ASP   A CA  1 
ATOM   2178 C  C   . ASP   A 1 312 ? -45.53300 27.64100 -5.20300  1.000 63.20000  ? 838  ASP   A C   1 
ATOM   2179 O  O   . ASP   A 1 312 ? -44.44900 28.03100 -4.75100  1.000 63.63000  ? 838  ASP   A O   1 
ATOM   2180 C  CB  . ASP   A 1 312 ? -47.00100 28.33000 -3.29500  1.000 71.79000  ? 838  ASP   A CB  1 
ATOM   2181 C  CG  . ASP   A 1 312 ? -48.28300 29.00800 -2.85400  1.000 83.51000  ? 838  ASP   A CG  1 
ATOM   2182 O  OD1 . ASP   A 1 312 ? -49.37400 28.45400 -3.11000  1.000 87.83000  ? 838  ASP   A OD1 1 
ATOM   2183 O  OD2 . ASP   A 1 312 ? -48.19700 30.10500 -2.26400  1.000 84.28000  ? 838  ASP   A OD2 1 
ATOM   2184 N  N   . CYS   A 1 313 ? -45.63100 26.58900 -6.01600  1.000 58.09000  ? 839  CYS   A N   1 
ATOM   2185 C  CA  . CYS   A 1 313 ? -44.46500 25.97500 -6.63500  1.000 52.52000  ? 839  CYS   A CA  1 
ATOM   2186 C  C   . CYS   A 1 313 ? -44.13700 26.60000 -7.98400  1.000 60.99000  ? 839  CYS   A C   1 
ATOM   2187 O  O   . CYS   A 1 313 ? -43.36800 26.01900 -8.75700  1.000 54.49000  ? 839  CYS   A O   1 
ATOM   2188 C  CB  . CYS   A 1 313 ? -44.67100 24.46300 -6.78700  1.000 56.48000  ? 839  CYS   A CB  1 
ATOM   2189 S  SG  . CYS   A 1 313 ? -45.15600 23.61900 -5.26800  1.000 59.00000  ? 839  CYS   A SG  1 
ATOM   2190 N  N   . PHE   A 1 314 ? -44.70700 27.76900 -8.27400  1.000 65.08000  ? 840  PHE   A N   1 
ATOM   2191 C  CA  . PHE   A 1 314 ? -44.35500 28.50200 -9.48800  1.000 54.30000  ? 840  PHE   A CA  1 
ATOM   2192 C  C   . PHE   A 1 314 ? -42.86400 28.80000 -9.62200  1.000 53.93000  ? 840  PHE   A C   1 
ATOM   2193 O  O   . PHE   A 1 314 ? -42.36300 28.76400 -10.76000 1.000 51.01000  ? 840  PHE   A O   1 
ATOM   2194 C  CB  . PHE   A 1 314 ? -45.18100 29.79500 -9.55000  1.000 66.33000  ? 840  PHE   A CB  1 
ATOM   2195 C  CG  . PHE   A 1 314 ? -44.69200 30.78300 -10.57000 1.000 59.02000  ? 840  PHE   A CG  1 
ATOM   2196 C  CD1 . PHE   A 1 314 ? -44.93900 30.58900 -11.91900 1.000 63.07000  ? 840  PHE   A CD1 1 
ATOM   2197 C  CD2 . PHE   A 1 314 ? -43.99000 31.91000 -10.17700 1.000 56.56000  ? 840  PHE   A CD2 1 
ATOM   2198 C  CE1 . PHE   A 1 314 ? -44.49000 31.50200 -12.86000 1.000 58.19000  ? 840  PHE   A CE1 1 
ATOM   2199 C  CE2 . PHE   A 1 314 ? -43.53800 32.82500 -11.11000 1.000 61.76000  ? 840  PHE   A CE2 1 
ATOM   2200 C  CZ  . PHE   A 1 314 ? -43.78900 32.62100 -12.45300 1.000 63.61000  ? 840  PHE   A CZ  1 
ATOM   2201 N  N   . PRO   A 1 315 ? -42.10200 29.11300 -8.54400  1.000 51.73000  ? 841  PRO   A N   1 
ATOM   2202 C  CA  . PRO   A 1 315 ? -40.65800 29.34600 -8.71000  1.000 44.41000  ? 841  PRO   A CA  1 
ATOM   2203 C  C   . PRO   A 1 315 ? -39.91200 28.21000 -9.39400  1.000 51.09000  ? 841  PRO   A C   1 
ATOM   2204 O  O   . PRO   A 1 315 ? -38.84400 28.43400 -9.97300  1.000 58.50000  ? 841  PRO   A O   1 
ATOM   2205 C  CB  . PRO   A 1 315 ? -40.17500 29.53400 -7.26800  1.000 44.72000  ? 841  PRO   A CB  1 
ATOM   2206 C  CG  . PRO   A 1 315 ? -41.33400 30.14000 -6.58300  1.000 53.66000  ? 841  PRO   A CG  1 
ATOM   2207 C  CD  . PRO   A 1 315 ? -42.55100 29.50300 -7.19200  1.000 53.71000  ? 841  PRO   A CD  1 
ATOM   2208 N  N   . LEU   A 1 316 ? -40.45100 26.99000 -9.33300  1.000 53.81000  ? 842  LEU   A N   1 
ATOM   2209 C  CA  . LEU   A 1 316 ? -39.83700 25.88100 -10.05600 1.000 49.73000  ? 842  LEU   A CA  1 
ATOM   2210 C  C   . LEU   A 1 316 ? -40.05300 26.02500 -11.55800 1.000 45.29000  ? 842  LEU   A C   1 
ATOM   2211 O  O   . LEU   A 1 316 ? -39.11100 25.89000 -12.34800 1.000 44.91000  ? 842  LEU   A O   1 
ATOM   2212 C  CB  . LEU   A 1 316 ? -40.39300 24.55000 -9.54900  1.000 42.76000  ? 842  LEU   A CB  1 
ATOM   2213 C  CG  . LEU   A 1 316 ? -39.98500 24.15500 -8.12800  1.000 41.36000  ? 842  LEU   A CG  1 
ATOM   2214 C  CD1 . LEU   A 1 316 ? -40.85900 23.02100 -7.61900  1.000 55.73000  ? 842  LEU   A CD1 1 
ATOM   2215 C  CD2 . LEU   A 1 316 ? -38.51300 23.76800 -8.08000  1.000 32.34000  ? 842  LEU   A CD2 1 
ATOM   2216 N  N   . LEU   A 1 317 ? -41.29100 26.30300 -11.97200 1.000 49.68000  ? 843  LEU   A N   1 
ATOM   2217 C  CA  . LEU   A 1 317 ? -41.56300 26.53700 -13.38600 1.000 44.36000  ? 843  LEU   A CA  1 
ATOM   2218 C  C   . LEU   A 1 317 ? -40.88100 27.80800 -13.87500 1.000 47.33000  ? 843  LEU   A C   1 
ATOM   2219 O  O   . LEU   A 1 317 ? -40.35200 27.84600 -14.99300 1.000 45.54000  ? 843  LEU   A O   1 
ATOM   2220 C  CB  . LEU   A 1 317 ? -43.07200 26.61200 -13.62100 1.000 50.58000  ? 843  LEU   A CB  1 
ATOM   2221 C  CG  . LEU   A 1 317 ? -43.53600 27.19300 -14.95800 1.000 53.58000  ? 843  LEU   A CG  1 
ATOM   2222 C  CD1 . LEU   A 1 317 ? -43.14400 26.27700 -16.10800 1.000 42.82000  ? 843  LEU   A CD1 1 
ATOM   2223 C  CD2 . LEU   A 1 317 ? -45.03800 27.44000 -14.94700 1.000 50.87000  ? 843  LEU   A CD2 1 
ATOM   2224 N  N   . ASP   A 1 318 ? -40.87800 28.85700 -13.04800 1.000 48.05000  ? 844  ASP   A N   1 
ATOM   2225 C  CA  . ASP   A 1 318 ? -40.23900 30.10900 -13.43900 1.000 45.33000  ? 844  ASP   A CA  1 
ATOM   2226 C  C   . ASP   A 1 318 ? -38.73600 29.93200 -13.61900 1.000 47.40000  ? 844  ASP   A C   1 
ATOM   2227 O  O   . ASP   A 1 318 ? -38.15700 30.42800 -14.59200 1.000 48.61000  ? 844  ASP   A O   1 
ATOM   2228 C  CB  . ASP   A 1 318 ? -40.53100 31.19000 -12.39800 1.000 51.88000  ? 844  ASP   A CB  1 
ATOM   2229 C  CG  . ASP   A 1 318 ? -40.07200 32.56700 -12.83900 1.000 54.21000  ? 844  ASP   A CG  1 
ATOM   2230 O  OD1 . ASP   A 1 318 ? -40.35900 32.95000 -13.99300 1.000 68.40000  ? 844  ASP   A OD1 1 
ATOM   2231 O  OD2 . ASP   A 1 318 ? -39.42600 33.26700 -12.03100 1.000 71.43000  ? 844  ASP   A OD2 1 
ATOM   2232 N  N   . GLY   A 1 319 ? -38.08800 29.22300 -12.69200 1.000 43.59000  ? 845  GLY   A N   1 
ATOM   2233 C  CA  . GLY   A 1 319 ? -36.65500 29.01100 -12.80100 1.000 43.22000  ? 845  GLY   A CA  1 
ATOM   2234 C  C   . GLY   A 1 319 ? -36.26500 28.15100 -13.98500 1.000 36.92000  ? 845  GLY   A C   1 
ATOM   2235 O  O   . GLY   A 1 319 ? -35.18900 28.33600 -14.56200 1.000 42.24000  ? 845  GLY   A O   1 
ATOM   2236 N  N   . CYS   A 1 320 ? -37.12600 27.20200 -14.36300 1.000 41.85000  ? 846  CYS   A N   1 
ATOM   2237 C  CA  . CYS   A 1 320 ? -36.83500 26.34600 -15.50900 1.000 43.53000  ? 846  CYS   A CA  1 
ATOM   2238 C  C   . CYS   A 1 320 ? -37.02000 27.09000 -16.82400 1.000 40.23000  ? 846  CYS   A C   1 
ATOM   2239 O  O   . CYS   A 1 320 ? -36.31200 26.81100 -17.79800 1.000 45.59000  ? 846  CYS   A O   1 
ATOM   2240 C  CB  . CYS   A 1 320 ? -37.72100 25.09700 -15.46800 1.000 42.00000  ? 846  CYS   A CB  1 
ATOM   2241 S  SG  . CYS   A 1 320 ? -37.58200 24.02300 -16.91700 1.000 44.20000  ? 846  CYS   A SG  1 
ATOM   2242 N  N   . ARG   A 1 321 ? -37.96400 28.03200 -16.87300 1.000 51.68000  ? 847  ARG   A N   1 
ATOM   2243 C  CA  . ARG   A 1 321 ? -38.12200 28.85700 -18.06600 1.000 52.56000  ? 847  ARG   A CA  1 
ATOM   2244 C  C   . ARG   A 1 321 ? -36.91800 29.76600 -18.26600 1.000 50.11000  ? 847  ARG   A C   1 
ATOM   2245 O  O   . ARG   A 1 321 ? -36.44200 29.94100 -19.39500 1.000 50.69000  ? 847  ARG   A O   1 
ATOM   2246 C  CB  . ARG   A 1 321 ? -39.40000 29.69000 -17.96600 1.000 39.42000  ? 847  ARG   A CB  1 
ATOM   2247 C  CG  . ARG   A 1 321 ? -40.68300 28.89500 -18.11300 1.000 45.43000  ? 847  ARG   A CG  1 
ATOM   2248 C  CD  . ARG   A 1 321 ? -41.89700 29.76700 -17.83600 1.000 42.98000  ? 847  ARG   A CD  1 
ATOM   2249 N  NE  . ARG   A 1 321 ? -43.14300 29.08600 -18.17300 1.000 67.94000  ? 847  ARG   A NE  1 
ATOM   2250 C  CZ  . ARG   A 1 321 ? -44.35200 29.55200 -17.87700 1.000 53.47000  ? 847  ARG   A CZ  1 
ATOM   2251 N  NH1 . ARG   A 1 321 ? -44.48100 30.70400 -17.23500 1.000 54.94000  ? 847  ARG   A NH1 1 
ATOM   2252 N  NH2 . ARG   A 1 321 ? -45.43200 28.86400 -18.22300 1.000 58.70000  ? 847  ARG   A NH2 1 
ATOM   2253 N  N   . LYS   A 1 322 ? -36.41600 30.35600 -17.17900 1.000 46.68000  ? 848  LYS   A N   1 
ATOM   2254 C  CA  . LYS   A 1 322 ? -35.25500 31.23300 -17.28000 1.000 46.33000  ? 848  LYS   A CA  1 
ATOM   2255 C  C   . LYS   A 1 322 ? -34.02600 30.47000 -17.75800 1.000 54.39000  ? 848  LYS   A C   1 
ATOM   2256 O  O   . LYS   A 1 322 ? -33.21000 31.00600 -18.51500 1.000 56.48000  ? 848  LYS   A O   1 
ATOM   2257 C  CB  . LYS   A 1 322 ? -34.98900 31.90100 -15.93100 1.000 37.86000  ? 848  LYS   A CB  1 
ATOM   2258 C  CG  . LYS   A 1 322 ? -36.04000 32.92600 -15.54100 1.000 39.15000  ? 848  LYS   A CG  1 
ATOM   2259 C  CD  . LYS   A 1 322 ? -35.77600 33.49100 -14.15900 1.000 48.83000  ? 848  LYS   A CD  1 
ATOM   2260 C  CE  . LYS   A 1 322 ? -36.81900 34.52800 -13.78600 1.000 51.49000  ? 848  LYS   A CE  1 
ATOM   2261 N  NZ  . LYS   A 1 322 ? -36.67400 34.96200 -12.37000 1.000 46.03000  ? 848  LYS   A NZ  1 
ATOM   2262 N  N   . ASN   A 1 323 ? -33.88200 29.21100 -17.33400 1.000 49.69000  ? 849  ASN   A N   1 
ATOM   2263 C  CA  . ASN   A 1 323 ? -32.75100 28.40600 -17.78400 1.000 45.50000  ? 849  ASN   A CA  1 
ATOM   2264 C  C   . ASN   A 1 323 ? -32.88300 28.02200 -19.25100 1.000 44.17000  ? 849  ASN   A C   1 
ATOM   2265 O  O   . ASN   A 1 323 ? -31.87400 27.93400 -19.96200 1.000 45.92000  ? 849  ASN   A O   1 
ATOM   2266 C  CB  . ASN   A 1 323 ? -32.61900 27.15600 -16.91300 1.000 51.78000  ? 849  ASN   A CB  1 
ATOM   2267 C  CG  . ASN   A 1 323 ? -31.98700 27.44900 -15.56200 1.000 54.92000  ? 849  ASN   A CG  1 
ATOM   2268 O  OD1 . ASN   A 1 323 ? -31.14900 28.34200 -15.43600 1.000 52.23000  ? 849  ASN   A OD1 1 
ATOM   2269 N  ND2 . ASN   A 1 323 ? -32.38400 26.69100 -14.54500 1.000 49.67000  ? 849  ASN   A ND2 1 
ATOM   2270 N  N   . ARG   A 1 324 ? -34.11000 27.78200 -19.72100 1.000 44.67000  ? 850  ARG   A N   1 
ATOM   2271 C  CA  . ARG   A 1 324 ? -34.31400 27.51100 -21.14200 1.000 56.90000  ? 850  ARG   A CA  1 
ATOM   2272 C  C   . ARG   A 1 324 ? -33.95900 28.72800 -21.98300 1.000 53.90000  ? 850  ARG   A C   1 
ATOM   2273 O  O   . ARG   A 1 324 ? -33.42000 28.59500 -23.08600 1.000 49.13000  ? 850  ARG   A O   1 
ATOM   2274 C  CB  . ARG   A 1 324 ? -35.76000 27.08300 -21.39500 1.000 46.97000  ? 850  ARG   A CB  1 
ATOM   2275 C  CG  . ARG   A 1 324 ? -36.01200 26.51000 -22.78000 1.000 42.69000  ? 850  ARG   A CG  1 
ATOM   2276 C  CD  . ARG   A 1 324 ? -37.43600 26.77400 -23.25000 1.000 56.00000  ? 850  ARG   A CD  1 
ATOM   2277 N  NE  . ARG   A 1 324 ? -37.68900 26.14800 -24.54400 1.000 54.95000  ? 850  ARG   A NE  1 
ATOM   2278 C  CZ  . ARG   A 1 324 ? -37.33700 26.67700 -25.71100 1.000 56.65000  ? 850  ARG   A CZ  1 
ATOM   2279 N  NH1 . ARG   A 1 324 ? -36.72200 27.85100 -25.75300 1.000 54.00000  ? 850  ARG   A NH1 1 
ATOM   2280 N  NH2 . ARG   A 1 324 ? -37.60100 26.03200 -26.83800 1.000 48.30000  ? 850  ARG   A NH2 1 
ATOM   2281 N  N   . GLN   A 1 325 ? -34.24700 29.92500 -21.47200 1.000 56.45000  ? 851  GLN   A N   1 
ATOM   2282 C  CA  . GLN   A 1 325 ? -33.88700 31.15000 -22.17200 1.000 58.94000  ? 851  GLN   A CA  1 
ATOM   2283 C  C   . GLN   A 1 325 ? -32.37400 31.29700 -22.30200 1.000 57.58000  ? 851  GLN   A C   1 
ATOM   2284 O  O   . GLN   A 1 325 ? -31.87600 31.67000 -23.37100 1.000 61.74000  ? 851  GLN   A O   1 
ATOM   2285 C  CB  . GLN   A 1 325 ? -34.47800 32.35200 -21.44800 1.000 63.07000  ? 851  GLN   A CB  1 
ATOM   2286 C  CG  . GLN   A 1 325 ? -34.20700 33.71100 -22.08400 1.000 71.86000  ? 851  GLN   A CG  1 
ATOM   2287 C  CD  . GLN   A 1 325 ? -33.01600 34.39700 -21.46000 1.000 82.60000  ? 851  GLN   A CD  1 
ATOM   2288 O  OE1 . GLN   A 1 325 ? -32.13200 34.89400 -22.15700 1.000 75.16000  ? 851  GLN   A OE1 1 
ATOM   2289 N  NE2 . GLN   A 1 325 ? -32.96500 34.39200 -20.13300 1.000 85.05000  ? 851  GLN   A NE2 1 
ATOM   2290 N  N   . LYS   A 1 326 ? -31.62200 31.00800 -21.23400 1.000 53.65000  ? 852  LYS   A N   1 
ATOM   2291 C  CA  . LYS   A 1 326 ? -30.17500 31.20200 -21.28900 1.000 50.10000  ? 852  LYS   A CA  1 
ATOM   2292 C  C   . LYS   A 1 326 ? -29.49800 30.10400 -22.09500 1.000 45.51000  ? 852  LYS   A C   1 
ATOM   2293 O  O   . LYS   A 1 326 ? -28.52900 30.37000 -22.81300 1.000 55.55000  ? 852  LYS   A O   1 
ATOM   2294 C  CB  . LYS   A 1 326 ? -29.59900 31.26300 -19.87800 1.000 44.29000  ? 852  LYS   A CB  1 
ATOM   2295 C  CG  . LYS   A 1 326 ? -30.32500 32.22600 -18.97000 1.000 47.02000  ? 852  LYS   A CG  1 
ATOM   2296 C  CD  . LYS   A 1 326 ? -29.37200 33.16300 -18.25700 1.000 61.29000  ? 852  LYS   A CD  1 
ATOM   2297 C  CE  . LYS   A 1 326 ? -29.13900 34.43600 -19.04600 1.000 63.73000  ? 852  LYS   A CE  1 
ATOM   2298 N  NZ  . LYS   A 1 326 ? -28.21100 35.35800 -18.33200 1.000 63.10000  ? 852  LYS   A NZ  1 
ATOM   2299 N  N   . TRP   A 1 327 ? -29.98900 28.86600 -21.98900 1.000 47.49000  ? 853  TRP   A N   1 
ATOM   2300 C  CA  . TRP   A 1 327 ? -29.41700 27.77100 -22.76700 1.000 45.65000  ? 853  TRP   A CA  1 
ATOM   2301 C  C   . TRP   A 1 327 ? -29.68900 27.94900 -24.25700 1.000 56.54000  ? 853  TRP   A C   1 
ATOM   2302 O  O   . TRP   A 1 327 ? -28.84200 27.61100 -25.09300 1.000 52.87000  ? 853  TRP   A O   1 
ATOM   2303 C  CB  . TRP   A 1 327 ? -29.97400 26.43400 -22.27900 1.000 48.97000  ? 853  TRP   A CB  1 
ATOM   2304 C  CG  . TRP   A 1 327 ? -29.33800 25.90200 -21.02200 1.000 50.37000  ? 853  TRP   A CG  1 
ATOM   2305 C  CD1 . TRP   A 1 327 ? -29.98100 25.50500 -19.88400 1.000 43.18000  ? 853  TRP   A CD1 1 
ATOM   2306 C  CD2 . TRP   A 1 327 ? -27.93900 25.70000 -20.78100 1.000 46.68000  ? 853  TRP   A CD2 1 
ATOM   2307 N  NE1 . TRP   A 1 327 ? -29.07100 25.07200 -18.95100 1.000 43.90000  ? 853  TRP   A NE1 1 
ATOM   2308 C  CE2 . TRP   A 1 327 ? -27.81000 25.18200 -19.47600 1.000 39.72000  ? 853  TRP   A CE2 1 
ATOM   2309 C  CE3 . TRP   A 1 327 ? -26.78200 25.91000 -21.53900 1.000 47.39000  ? 853  TRP   A CE3 1 
ATOM   2310 C  CZ2 . TRP   A 1 327 ? -26.57300 24.87000 -18.91500 1.000 46.40000  ? 853  TRP   A CZ2 1 
ATOM   2311 C  CZ3 . TRP   A 1 327 ? -25.55500 25.60000 -20.98100 1.000 48.85000  ? 853  TRP   A CZ3 1 
ATOM   2312 C  CH2 . TRP   A 1 327 ? -25.46000 25.08600 -19.68200 1.000 47.83000  ? 853  TRP   A CH2 1 
ATOM   2313 N  N   . GLN   A 1 328 ? -30.86700 28.47100 -24.60900 1.000 56.79000  ? 854  GLN   A N   1 
ATOM   2314 C  CA  . GLN   A 1 328 ? -31.19100 28.68800 -26.01500 1.000 58.47000  ? 854  GLN   A CA  1 
ATOM   2315 C  C   . GLN   A 1 328 ? -30.31000 29.77300 -26.62400 1.000 61.89000  ? 854  GLN   A C   1 
ATOM   2316 O  O   . GLN   A 1 328 ? -29.89800 29.66500 -27.78500 1.000 60.15000  ? 854  GLN   A O   1 
ATOM   2317 C  CB  . GLN   A 1 328 ? -32.67000 29.04700 -26.16000 1.000 63.30000  ? 854  GLN   A CB  1 
ATOM   2318 C  CG  . GLN   A 1 328 ? -33.06500 29.56900 -27.53500 1.000 64.80000  ? 854  GLN   A CG  1 
ATOM   2319 C  CD  . GLN   A 1 328 ? -33.02600 28.49500 -28.60600 1.000 64.55000  ? 854  GLN   A CD  1 
ATOM   2320 O  OE1 . GLN   A 1 328 ? -32.98100 27.30100 -28.30700 1.000 59.70000  ? 854  GLN   A OE1 1 
ATOM   2321 N  NE2 . GLN   A 1 328 ? -33.04500 28.91600 -29.86500 1.000 75.71000  ? 854  GLN   A NE2 1 
ATOM   2322 N  N   . ALA   A 1 329 ? -30.00700 30.82100 -25.85400 1.000 55.47000  ? 855  ALA   A N   1 
ATOM   2323 C  CA  . ALA   A 1 329 ? -29.15900 31.89400 -26.36600 1.000 50.35000  ? 855  ALA   A CA  1 
ATOM   2324 C  C   . ALA   A 1 329 ? -27.75600 31.38800 -26.67800 1.000 58.37000  ? 855  ALA   A C   1 
ATOM   2325 O  O   . ALA   A 1 329 ? -27.15500 31.78200 -27.68500 1.000 68.60000  ? 855  ALA   A O   1 
ATOM   2326 C  CB  . ALA   A 1 329 ? -29.10300 33.04500 -25.36300 1.000 46.40000  ? 855  ALA   A CB  1 
ATOM   2327 N  N   . LEU   A 1 330 ? -27.21700 30.51500 -25.82600 1.000 59.31000  ? 856  LEU   A N   1 
ATOM   2328 C  CA  . LEU   A 1 330 ? -25.90000 29.95100 -26.09900 1.000 60.03000  ? 856  LEU   A CA  1 
ATOM   2329 C  C   . LEU   A 1 330 ? -25.95600 28.91800 -27.21600 1.000 58.74000  ? 856  LEU   A C   1 
ATOM   2330 O  O   . LEU   A 1 330 ? -24.97300 28.74500 -27.94600 1.000 62.42000  ? 856  LEU   A O   1 
ATOM   2331 C  CB  . LEU   A 1 330 ? -25.31800 29.33300 -24.82900 1.000 60.56000  ? 856  LEU   A CB  1 
ATOM   2332 C  CG  . LEU   A 1 330 ? -24.48600 30.27200 -23.95400 1.000 68.41000  ? 856  LEU   A CG  1 
ATOM   2333 C  CD1 . LEU   A 1 330 ? -24.48500 29.79500 -22.51200 1.000 65.99000  ? 856  LEU   A CD1 1 
ATOM   2334 C  CD2 . LEU   A 1 330 ? -23.07000 30.38000 -24.49100 1.000 54.67000  ? 856  LEU   A CD2 1 
ATOM   2335 N  N   . ALA   A 1 331 ? -27.09000 28.22800 -27.36800 1.000 61.28000  ? 857  ALA   A N   1 
ATOM   2336 C  CA  . ALA   A 1 331 ? -27.23800 27.28400 -28.47100 1.000 65.00000  ? 857  ALA   A CA  1 
ATOM   2337 C  C   . ALA   A 1 331 ? -27.13500 27.98300 -29.81900 1.000 77.64000  ? 857  ALA   A C   1 
ATOM   2338 O  O   . ALA   A 1 331 ? -26.66900 27.38400 -30.79700 1.000 79.82000  ? 857  ALA   A O   1 
ATOM   2339 C  CB  . ALA   A 1 331 ? -28.56900 26.54200 -28.35400 1.000 58.07000  ? 857  ALA   A CB  1 
ATOM   2340 N  N   . GLU   A 1 332 ? -27.55800 29.24500 -29.89200 1.000 73.87000  ? 858  GLU   A N   1 
ATOM   2341 C  CA  . GLU   A 1 332 ? -27.41900 30.05900 -31.09200 1.000 75.18000  ? 858  GLU   A CA  1 
ATOM   2342 C  C   . GLU   A 1 332 ? -26.04900 30.72100 -31.20000 1.000 78.37000  ? 858  GLU   A C   1 
ATOM   2343 O  O   . GLU   A 1 332 ? -25.89000 31.65400 -31.99800 1.000 85.12000  ? 858  GLU   A O   1 
ATOM   2344 C  CB  . GLU   A 1 332 ? -28.51900 31.12400 -31.13400 1.000 63.99000  ? 858  GLU   A CB  1 
ATOM   2345 C  CG  . GLU   A 1 332 ? -29.92500 30.57200 -30.95700 1.000 64.61000  ? 858  GLU   A CG  1 
ATOM   2346 C  CD  . GLU   A 1 332 ? -30.95300 31.66100 -30.71900 1.000 70.91000  ? 858  GLU   A CD  1 
ATOM   2347 O  OE1 . GLU   A 1 332 ? -32.09400 31.52200 -31.20900 1.000 77.76000  ? 858  GLU   A OE1 1 
ATOM   2348 O  OE2 . GLU   A 1 332 ? -30.62100 32.65700 -30.04200 1.000 72.76000  ? 858  GLU   A OE2 1 
ATOM   2349 N  N   . GLN   A 1 333 ? -25.07600 30.26000 -30.41500 1.000 82.57000  ? 859  GLN   A N   1 
ATOM   2350 C  CA  . GLN   A 1 333 ? -23.71800 30.80100 -30.41600 1.000 74.93000  ? 859  GLN   A CA  1 
ATOM   2351 C  C   . GLN   A 1 333 ? -23.70800 32.29700 -30.11800 1.000 75.61000  ? 859  GLN   A C   1 
ATOM   2352 O  O   . GLN   A 1 333 ? -23.51500 32.70900 -28.97400 1.000 77.66000  ? 859  GLN   A O   1 
ATOM   2353 C  CB  . GLN   A 1 333 ? -23.02900 30.52300 -31.75500 1.000 70.95000  ? 859  GLN   A CB  1 
ATOM   2354 C  CG  . GLN   A 1 333 ? -23.03900 29.06000 -32.16500 1.000 84.69000  ? 859  GLN   A CG  1 
ATOM   2355 C  CD  . GLN   A 1 333 ? -22.77500 28.86800 -33.64500 1.000 102.67000 ? 859  GLN   A CD  1 
ATOM   2356 O  OE1 . GLN   A 1 333 ? -23.62000 28.35400 -34.37700 1.000 95.34000  ? 859  GLN   A OE1 1 
ATOM   2357 N  NE2 . GLN   A 1 333 ? -21.59500 29.28200 -34.09300 1.000 95.78000  ? 859  GLN   A NE2 1 
HETATM 2358 O  O1  . A1D5K B 2 .   ? -31.80700 13.06700 -12.43300 1.000 50.29000  ? 901  A1D5K A O1  1 
HETATM 2359 C  C3  . A1D5K B 2 .   ? -30.20000 15.90600 -20.15800 1.000 53.70000  ? 901  A1D5K A C3  1 
HETATM 2360 C  C4  . A1D5K B 2 .   ? -30.36800 16.06100 -18.68400 1.000 57.68000  ? 901  A1D5K A C4  1 
HETATM 2361 C  C5  . A1D5K B 2 .   ? -30.71600 15.17500 -16.57100 1.000 52.94000  ? 901  A1D5K A C5  1 
HETATM 2362 C  C6  . A1D5K B 2 .   ? -30.90700 14.04500 -15.76000 1.000 50.01000  ? 901  A1D5K A C6  1 
HETATM 2363 C  C7  . A1D5K B 2 .   ? -31.07100 14.19900 -14.38900 1.000 58.19000  ? 901  A1D5K A C7  1 
HETATM 2364 C  C8  . A1D5K B 2 .   ? -31.25600 12.99900 -13.52500 1.000 60.55000  ? 901  A1D5K A C8  1 
HETATM 2365 N  N   . A1D5K B 2 .   ? -30.55200 14.97900 -17.93400 1.000 51.45000  ? 901  A1D5K A N   1 
HETATM 2366 C  C   . A1D5K B 2 .   ? -26.51200 16.40600 -20.85400 1.000 57.98000  ? 901  A1D5K A C   1 
HETATM 2367 O  O   . A1D5K B 2 .   ? -30.78500 11.88900 -14.02400 1.000 53.54000  ? 901  A1D5K A O   1 
HETATM 2368 C  C1  . A1D5K B 2 .   ? -27.83100 16.66600 -20.53600 1.000 53.59000  ? 901  A1D5K A C1  1 
HETATM 2369 C  C10 . A1D5K B 2 .   ? -30.86600 16.59200 -14.61400 1.000 50.54000  ? 901  A1D5K A C10 1 
HETATM 2370 C  C11 . A1D5K B 2 .   ? -30.69600 16.44800 -15.97700 1.000 54.04000  ? 901  A1D5K A C11 1 
HETATM 2371 C  C12 . A1D5K B 2 .   ? -30.48700 17.61800 -16.84900 1.000 54.26000  ? 901  A1D5K A C12 1 
HETATM 2372 C  C13 . A1D5K B 2 .   ? -28.32500 14.34100 -20.79000 1.000 56.41000  ? 901  A1D5K A C13 1 
HETATM 2373 C  C14 . A1D5K B 2 .   ? -26.99800 14.09500 -21.11000 1.000 57.04000  ? 901  A1D5K A C14 1 
HETATM 2374 C  C15 . A1D5K B 2 .   ? -26.08300 15.12700 -21.14300 1.000 60.91000  ? 901  A1D5K A C15 1 
HETATM 2375 C  C2  . A1D5K B 2 .   ? -28.75300 15.63300 -20.50100 1.000 58.05000  ? 901  A1D5K A C2  1 
HETATM 2376 C  C9  . A1D5K B 2 .   ? -31.05300 15.47100 -13.82100 1.000 53.27000  ? 901  A1D5K A C9  1 
HETATM 2377 N  N1  . A1D5K B 2 .   ? -30.33300 17.33400 -18.18100 1.000 53.80000  ? 901  A1D5K A N1  1 
HETATM 2378 O  O2  . A1D5K B 2 .   ? -30.44600 18.77700 -16.43700 1.000 57.38000  ? 901  A1D5K A O2  1 
HETATM 2379 CL CL  . A1D5K B 2 .   ? -25.37100 17.71700 -20.88300 1.000 58.20000  ? 901  A1D5K A CL  1 
HETATM 2380 ZN ZN  . ZN    C 3 .   ? -32.06800 10.94900 -9.36600  1.000 48.29000  ? 902  ZN    A ZN  1 
HETATM 2381 MG MG  . MG    D 4 .   ? -32.13900 7.66300  -10.80500 1.000 38.97000  ? 903  MG    A MG  1 
HETATM 2382 O  O   . HOH   E 5 .   ? -32.55000 19.61600 -6.63400  1.000 40.93000  ? 1001 HOH   A O   1 
HETATM 2383 O  O   . HOH   E 5 .   ? -36.78000 -1.74200 9.02900   1.000 45.79000  ? 1002 HOH   A O   1 
HETATM 2384 O  O   . HOH   E 5 .   ? -23.93600 27.34300 -3.48900  1.000 61.59000  ? 1003 HOH   A O   1 
HETATM 2385 O  O   . HOH   E 5 .   ? -26.63900 16.36500 15.59700  1.000 44.41000  ? 1004 HOH   A O   1 
HETATM 2386 O  O   . HOH   E 5 .   ? -31.27200 11.11100 -11.19400 1.000 40.40000  ? 1005 HOH   A O   1 
HETATM 2387 O  O   . HOH   E 5 .   ? -32.50600 21.43000 -4.43400  1.000 45.55000  ? 1006 HOH   A O   1 
HETATM 2388 O  O   . HOH   E 5 .   ? -36.57700 29.79800 -24.33600 1.000 57.01000  ? 1007 HOH   A O   1 
HETATM 2389 O  O   . HOH   E 5 .   ? -33.05600 -5.48900 -7.43900  1.000 54.99000  ? 1008 HOH   A O   1 
HETATM 2390 O  O   . HOH   E 5 .   ? -27.13400 19.28500 -6.62400  1.000 53.04000  ? 1009 HOH   A O   1 
HETATM 2391 O  O   . HOH   E 5 .   ? -20.75200 9.14300  -0.84100  1.000 53.03000  ? 1010 HOH   A O   1 
HETATM 2392 O  O   . HOH   E 5 .   ? -39.19900 10.15800 -13.24700 1.000 45.11000  ? 1011 HOH   A O   1 
HETATM 2393 O  O   . HOH   E 5 .   ? -31.84800 17.40000 -10.52600 1.000 42.00000  ? 1012 HOH   A O   1 
HETATM 2394 O  O   . HOH   E 5 .   ? -36.64100 11.07500 -12.78900 1.000 39.26000  ? 1013 HOH   A O   1 
HETATM 2395 O  O   . HOH   E 5 .   ? -28.65100 29.64400 -4.58000  1.000 52.13000  ? 1014 HOH   A O   1 
HETATM 2396 O  O   . HOH   E 5 .   ? -39.28200 5.50300  14.43700  1.000 50.74000  ? 1015 HOH   A O   1 
HETATM 2397 O  O   . HOH   E 5 .   ? -23.57800 7.05900  -6.49900  1.000 41.94000  ? 1016 HOH   A O   1 
HETATM 2398 O  O   . HOH   E 5 .   ? -47.22100 6.43400  14.29200  1.000 56.72000  ? 1017 HOH   A O   1 
HETATM 2399 O  O   . HOH   E 5 .   ? -33.45200 34.12200 -17.56900 1.000 66.49000  ? 1018 HOH   A O   1 
HETATM 2400 O  O   . HOH   E 5 .   ? -28.75000 22.47300 -5.94400  1.000 51.44000  ? 1019 HOH   A O   1 
HETATM 2401 O  O   . HOH   E 5 .   ? -33.62900 6.52700  -9.53200  1.000 36.21000  ? 1020 HOH   A O   1 
HETATM 2402 O  O   . HOH   E 5 .   ? -31.65400 30.93300 -15.28000 1.000 59.95000  ? 1021 HOH   A O   1 
HETATM 2403 O  O   . HOH   E 5 .   ? -22.99400 10.02700 5.50900   1.000 78.09000  ? 1022 HOH   A O   1 
HETATM 2404 O  O   . HOH   E 5 .   ? -33.32500 29.87400 -13.36400 1.000 42.29000  ? 1023 HOH   A O   1 
HETATM 2405 O  O   . HOH   E 5 .   ? -37.90100 30.85600 0.78400   1.000 59.84000  ? 1024 HOH   A O   1 
HETATM 2406 O  O   . HOH   E 5 .   ? -29.09000 20.11200 -14.48800 1.000 44.10000  ? 1025 HOH   A O   1 
HETATM 2407 O  O   . HOH   E 5 .   ? -33.22400 9.39000  -10.50000 1.000 43.88000  ? 1026 HOH   A O   1 
HETATM 2408 O  O   . HOH   E 5 .   ? -33.53500 4.85300  -15.26800 1.000 51.77000  ? 1027 HOH   A O   1 
HETATM 2409 O  O   . HOH   E 5 .   ? -38.18300 -5.58500 -3.93600  1.000 46.46000  ? 1028 HOH   A O   1 
HETATM 2410 O  O   . HOH   E 5 .   ? -33.88400 7.12700  -11.96600 1.000 38.40000  ? 1029 HOH   A O   1 
HETATM 2411 O  O   . HOH   E 5 .   ? -22.22600 19.97200 -4.48900  1.000 46.51000  ? 1030 HOH   A O   1 
HETATM 2412 O  O   . HOH   E 5 .   ? -27.49900 -9.81000 -13.70600 1.000 68.95000  ? 1031 HOH   A O   1 
HETATM 2413 O  O   . HOH   E 5 .   ? -22.34300 3.00700  13.85700  1.000 70.17000  ? 1032 HOH   A O   1 
HETATM 2414 O  O   . HOH   E 5 .   ? -34.67200 7.11800  -15.68700 1.000 58.84000  ? 1033 HOH   A O   1 
HETATM 2415 O  O   . HOH   E 5 .   ? -32.56700 4.02200  3.57600   1.000 36.84000  ? 1034 HOH   A O   1 
HETATM 2416 O  O   . HOH   E 5 .   ? -28.51100 28.05300 -0.91200  1.000 50.83000  ? 1035 HOH   A O   1 
HETATM 2417 O  O   . HOH   E 5 .   ? -36.25200 1.38500  9.66900   1.000 40.25000  ? 1036 HOH   A O   1 
HETATM 2418 O  O   . HOH   E 5 .   ? -29.80000 -4.93600 6.07900   1.000 44.80000  ? 1037 HOH   A O   1 
HETATM 2419 O  O   . HOH   E 5 .   ? -29.72300 20.89600 17.85900  1.000 63.67000  ? 1038 HOH   A O   1 
HETATM 2420 O  O   . HOH   E 5 .   ? -31.22100 5.68600  -11.48000 1.000 46.11000  ? 1039 HOH   A O   1 
HETATM 2421 O  O   . HOH   E 5 .   ? -31.20600 8.85500  -12.42500 1.000 37.66000  ? 1040 HOH   A O   1 
HETATM 2422 O  O   . HOH   E 5 .   ? -26.18800 23.26700 -5.98700  1.000 45.82000  ? 1041 HOH   A O   1 
HETATM 2423 O  O   . HOH   E 5 .   ? -40.06000 -1.97100 16.11600  1.000 52.15000  ? 1042 HOH   A O   1 
HETATM 2424 O  O   . HOH   E 5 .   ? -39.71100 16.36800 14.93200  1.000 50.27000  ? 1043 HOH   A O   1 
HETATM 2425 O  O   . HOH   E 5 .   ? -24.39100 16.03400 -7.66800  1.000 45.41000  ? 1044 HOH   A O   1 
HETATM 2426 O  O   . HOH   E 5 .   ? -20.71600 23.37500 -27.63500 1.000 72.22000  ? 1045 HOH   A O   1 
HETATM 2427 O  O   . HOH   E 5 .   ? -26.83200 25.84200 3.62300   1.000 51.22000  ? 1046 HOH   A O   1 
HETATM 2428 O  O   . HOH   E 5 .   ? -32.01400 17.25500 -7.51800  1.000 38.49000  ? 1047 HOH   A O   1 
HETATM 2429 O  O   . HOH   E 5 .   ? -38.97000 14.83900 19.31200  1.000 51.64000  ? 1048 HOH   A O   1 
HETATM 2430 O  O   . HOH   E 5 .   ? -33.86900 32.54600 -25.54700 1.000 57.85000  ? 1049 HOH   A O   1 
HETATM 2431 O  O   . HOH   E 5 .   ? -51.00100 7.14000  4.80900   1.000 56.42000  ? 1050 HOH   A O   1 
HETATM 2432 O  O   . HOH   E 5 .   ? -33.60900 1.51700  -15.36500 1.000 46.94000  ? 1051 HOH   A O   1 
HETATM 2433 O  O   . HOH   E 5 .   ? -53.64500 16.33200 5.55600   1.000 61.61000  ? 1052 HOH   A O   1 
HETATM 2434 O  O   . HOH   E 5 .   ? -24.38400 19.49500 -6.43500  1.000 45.04000  ? 1053 HOH   A O   1 
HETATM 2435 O  O   . HOH   E 5 .   ? -45.73000 6.21700  16.07200  1.000 62.83000  ? 1054 HOH   A O   1 
HETATM 2436 O  O   . HOH   E 5 .   ? -36.54300 -4.42900 -5.27300  1.000 54.19000  ? 1055 HOH   A O   1 
HETATM 2437 O  O   . HOH   E 5 .   ? -29.93000 7.24200  -14.24800 1.000 48.88000  ? 1056 HOH   A O   1 
HETATM 2438 O  O   . HOH   E 5 .   ? -28.59600 17.82300 -8.30800  1.000 34.43000  ? 1057 HOH   A O   1 
HETATM 2439 O  O   . HOH   E 5 .   ? -33.88600 10.16600 -13.76200 1.000 47.62000  ? 1058 HOH   A O   1 
HETATM 2440 O  O   . HOH   E 5 .   ? -31.00100 20.83200 -7.61500  1.000 53.02000  ? 1059 HOH   A O   1 
HETATM 2441 O  O   . HOH   E 5 .   ? -26.04300 17.57400 -7.52900  1.000 31.81000  ? 1060 HOH   A O   1 
HETATM 2442 O  O   . HOH   E 5 .   ? -33.97800 30.91600 -10.79800 1.000 54.49000  ? 1061 HOH   A O   1 
HETATM 2443 O  O   . HOH   E 5 .   ? -31.13000 5.22900  -14.17800 1.000 43.62000  ? 1062 HOH   A O   1 
HETATM 2444 O  O   . HOH   E 5 .   ? -48.06600 5.88900  16.33900  1.000 58.79000  ? 1063 HOH   A O   1 
HETATM 2445 O  O   . HOH   E 5 .   ? -48.16900 18.87800 -22.09700 1.000 58.73000  ? 1064 HOH   A O   1 
HETATM 2446 O  O   . HOH   E 5 .   ? -29.01000 19.98800 -7.83200  1.000 38.82000  ? 1065 HOH   A O   1 
HETATM 2447 O  O   . HOH   E 5 .   ? -47.209   -9.906   6.275     1.000 46.89000  ? 1066 HOH   A O   1 
HETATM 2448 O  O   . HOH   E 5 .   ? -33.14900 8.79600  -15.49100 1.000 58.46000  ? 1067 HOH   A O   1 
# 
